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***  NSLS_100K_sub  ***

elNémo ID: 191029175041147104

Job options:

ID        	=	 191029175041147104
JOBID     	=	 NSLS_100K_sub
USERID    	=	 unknown
PRIVAT    	=	 0

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

DOPROJMODS	=	 0
DORMSD    	=	 0

NRBL      	=	 0
CUTOFF    	=	 0
CAONLY    	=	 0


Input data for this run:

HEADER NSLS_100K_sub

REMARK Date 2019-10-29 Time 12:25:44 EDT -0400 (1572366344.20 s)
REMARK PHENIX refinement
REMARK 
REMARK ****************** INPUT FILES AND LABELS ******************************
REMARK Reflections:
REMARK   file name      : /Users/jonathan/Projects/PEPCK_variableT/NSLS_20191024/100K_substrate/xia2/DataFiles/AUTOMATIC_DEFAULT_free.mtz
REMARK   labels         : ['IMEAN,SIGIMEAN']
REMARK R-free flags:
REMARK   file name      : /Users/jonathan/Projects/PEPCK_variableT/NSLS_20191024/100K_substrate/xia2/DataFiles/AUTOMATIC_DEFAULT_free.mtz
REMARK   label          : FreeR_flag
REMARK   test_flag_value: 0
REMARK Model file name(s): 
REMARK   /Users/jonathan/Projects/PEPCK_variableT/NSLS_20191024/100K_substrate/phenix/Refine_17/100K_sub_PEPCK_refine_17-coot-0.pdb
REMARK 
REMARK ******************** REFINEMENT SUMMARY: QUICK FACTS *******************
REMARK Start: r_work = 0.2045 r_free = 0.2373 bonds = 0.009 angles = 0.992
REMARK Final: r_work = 0.1900 r_free = 0.2281 bonds = 0.006 angles = 0.866
REMARK ************************************************************************
REMARK 
REMARK ****************** REFINEMENT STATISTICS STEP BY STEP ******************
REMARK leading digit, like 1_, means number of macro-cycle                     
REMARK 0    : statistics at the very beginning when nothing is done yet        
REMARK 1_bss: bulk solvent correction and/or (anisotropic) scaling             
REMARK 1_xyz: refinement of coordinates                                        
REMARK 1_adp: refinement of ADPs (Atomic Displacement Parameters)              
REMARK 1_occ: refinement of occupancies                                        
REMARK ------------------------------------------------------------------------
REMARK  stage r-work r-free bonds angles b_min b_max b_ave n_water shift
REMARK       0    : 0.3605 0.3478 0.009  0.992  12.1 102.7  29.1 267      0.000
REMARK       1_bss: 0.2045 0.2373 0.009  0.992  12.1 102.7  29.1 267      0.000
REMARK 1_settarget: 0.2045 0.2373 0.009  0.992  12.1 102.7  29.1 267      0.000
REMARK       1_nqh: 0.2045 0.2373 0.009  0.992  12.1 102.7  29.1 267      0.000
REMARK    1_weight: 0.2045 0.2373 0.009  0.992  12.1 102.7  29.1 267      0.000
REMARK    1_xyzrec: 0.2029 0.2428 0.007  0.906  12.1 102.7  29.1 267      0.051
REMARK       1_adp: 0.1937 0.2390 0.007  0.906  11.5 117.2  31.1 267      0.051
REMARK       1_occ: 0.1937 0.2389 0.007  0.906  11.5 117.2  31.1 267      0.051
REMARK       2_bss: 0.1929 0.2386 0.007  0.906  11.5 117.2  31.1 267      0.051
REMARK 2_settarget: 0.1929 0.2386 0.007  0.906  11.5 117.2  31.1 267      0.051
REMARK 2_updatecdl: 0.1929 0.2386 0.007  0.928  11.5 117.2  31.1 267      0.051
REMARK       2_nqh: 0.1929 0.2386 0.007  0.928  11.5 117.2  31.1 267      0.051
REMARK    2_weight: 0.1929 0.2386 0.007  0.928  11.5 117.2  31.1 267      0.051
REMARK    2_xyzrec: 0.1915 0.2374 0.007  0.869  11.5 117.2  31.1 267      0.062
REMARK       2_adp: 0.1902 0.2363 0.007  0.869  11.1 133.2  32.2 267      0.062
REMARK       2_occ: 0.1902 0.2363 0.007  0.869  11.1 133.2  32.2 267      0.062
REMARK       3_bss: 0.1894 0.2360 0.007  0.869  11.1 133.2  32.2 267      0.062
REMARK 3_settarget: 0.1894 0.2360 0.007  0.869  11.1 133.2  32.2 267      0.062
REMARK 3_updatecdl: 0.1894 0.2360 0.007  0.871  11.1 133.2  32.2 267      0.062
REMARK       3_nqh: 0.1894 0.2360 0.007  0.871  11.1 133.2  32.2 267      0.062
REMARK    3_weight: 0.1894 0.2360 0.007  0.871  11.1 133.2  32.2 267      0.062
REMARK    3_xyzrec: 0.1910 0.2321 0.006  0.867  11.1 133.2  32.2 267      0.041
REMARK       3_adp: 0.1925 0.2309 0.006  0.867  11.1 138.1  32.5 267      0.041
REMARK       3_occ: 0.1925 0.2309 0.006  0.867  11.1 138.1  32.5 267      0.041
REMARK       4_bss: 0.1916 0.2300 0.006  0.867  11.1 138.1  32.5 267      0.041
REMARK 4_settarget: 0.1916 0.2300 0.006  0.867  11.1 138.1  32.5 267      0.041
REMARK 4_updatecdl: 0.1916 0.2300 0.006  0.872  11.1 138.1  32.5 267      0.041
REMARK       4_nqh: 0.1916 0.2300 0.006  0.872  11.1 138.1  32.5 267      0.041
REMARK    4_weight: 0.1916 0.2300 0.006  0.872  11.1 138.1  32.5 267      0.041
REMARK    4_xyzrec: 0.1906 0.2292 0.006  0.868  11.1 138.1  32.5 267      0.040
REMARK       4_adp: 0.1906 0.2291 0.006  0.868  10.8 139.4  32.6 267      0.040
REMARK       4_occ: 0.1906 0.2291 0.006  0.868  10.8 139.4  32.6 267      0.040
REMARK       5_bss: 0.1899 0.2285 0.006  0.868  10.8 139.4  32.6 267      0.040
REMARK 5_settarget: 0.1899 0.2285 0.006  0.868  10.8 139.4  32.6 267      0.040
REMARK 5_updatecdl: 0.1899 0.2285 0.006  0.876  10.8 139.4  32.6 267      0.040
REMARK     5_setrh: 0.1899 0.2285 0.006  0.876  10.8 139.4  32.6 267      0.040
REMARK       5_nqh: 0.1899 0.2285 0.006  0.876  10.8 139.4  32.6 267      0.040
REMARK    5_weight: 0.1899 0.2285 0.006  0.876  10.8 139.4  32.6 267      0.040
REMARK    5_xyzrec: 0.1901 0.2290 0.006  0.866  10.8 139.4  32.6 267      0.043
REMARK       5_adp: 0.1904 0.2285 0.006  0.866  11.4 138.9  32.7 267      0.043
REMARK       5_occ: 0.1904 0.2285 0.006  0.866  11.4 138.9  32.7 267      0.043
REMARK         end: 0.1900 0.2281 0.006  0.866  11.4 138.9  32.7 267      0.043
REMARK ------------------------------------------------------------------------
REMARK MODEL CONTENT.
REMARK  ELEMENT        ATOM RECORD COUNT   OCCUPANCY SUM
REMARK        C                     3163         3124.00
REMARK       Mn                        3            3.00
REMARK        O                     1186         1178.00
REMARK        N                      852          841.00
REMARK        P                        3            3.00
REMARK        S                       33           32.00
REMARK    TOTAL                     5240         5181.00
REMARK -----------------------------------------------------------------------
REMARK r_free_flags.md5.hexdigest ee90244c591b4a6e9f53010d67a7d358
REMARK 
REMARK IF THIS FILE IS FOR PDB DEPOSITION: REMOVE ALL FROM THIS LINE UP.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : PHENIX (1.16_3549: ???)
REMARK   3   AUTHORS     : Adams,Afonine,Bunkoczi,Burnley,Chen,Dar,Davis,
REMARK   3               : Draizen,Echols,Gildea,Gros,Grosse-Kunstleve,Headd,
REMARK   3               : Hintze,Hung,Ioerger,Liebschner,McCoy,McKee,Moriarty,
REMARK   3               : Oeffner,Poon,Read,Richardson,Richardson,Sacchettini,
REMARK   3               : Sauter,Sobolev,Storoni,Terwilliger,Williams,Zwart
REMARK   3
REMARK   3  X-RAY DATA.
REMARK   3  
REMARK   3  REFINEMENT TARGET : ML
REMARK   3  
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.760   
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 55.651  
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.34  
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.53 
REMARK   3   NUMBER OF REFLECTIONS             : 56665     
REMARK   3   NUMBER OF REFLECTIONS (NON-ANOMALOUS) : 56665     
REMARK   3  
REMARK   3  FIT TO DATA USED IN REFINEMENT.
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.1919
REMARK   3   R VALUE            (WORKING SET) : 0.1900
REMARK   3   FREE R VALUE                     : 0.2281
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.96  
REMARK   3   FREE R VALUE TEST SET COUNT      : 2808      
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 55.6789 -  4.7757    1.00     2762   138  0.1516 0.1593   0.945  0.941
REMARK   3     2  4.7757 -  3.7909    1.00     2713   150  0.1392 0.1582   0.953  0.945
REMARK   3     3  3.7909 -  3.3118    1.00     2702   153  0.1657 0.2178   0.934  0.881
REMARK   3     4  3.3118 -  3.0090    1.00     2680   143  0.1881 0.2041   0.920  0.896
REMARK   3     5  3.0090 -  2.7933    1.00     2764   117  0.1916 0.2493   0.920  0.869
REMARK   3     6  2.7933 -  2.6286    1.00     2681   150  0.1900 0.2395   0.929  0.876
REMARK   3     7  2.6286 -  2.4970    1.00     2726   114  0.1915 0.2685   0.929  0.865
REMARK   3     8  2.4970 -  2.3883    1.00     2700   156  0.1773 0.2023   0.936  0.915
REMARK   3     9  2.3883 -  2.2963    1.00     2700   134  0.1883 0.2487   0.932  0.863
REMARK   3    10  2.2963 -  2.2171    1.00     2657   149  0.1995 0.2763   0.923  0.866
REMARK   3    11  2.2171 -  2.1478    1.00     2735   135  0.2001 0.2642   0.920  0.881
REMARK   3    12  2.1478 -  2.0864    1.00     2724   128  0.2260 0.2559   0.907  0.884
REMARK   3    13  2.0864 -  2.0315    1.00     2676   139  0.2193 0.2561   0.910  0.844
REMARK   3    14  2.0315 -  1.9819    1.00     2692   136  0.2307 0.2999   0.905  0.849
REMARK   3    15  1.9819 -  1.9368    1.00     2645   139  0.2413 0.2979   0.889  0.814
REMARK   3    16  1.9368 -  1.8956    1.00     2715   155  0.2598 0.3484   0.873  0.758
REMARK   3    17  1.8956 -  1.8577    1.00     2689   139  0.2773 0.3448   0.868  0.770
REMARK   3    18  1.8577 -  1.8226    1.00     2674   154  0.3099 0.3244   0.827  0.803
REMARK   3    19  1.8226 -  1.7901    0.99     2688   149  0.3370 0.3717   0.805  0.707
REMARK   3    20  1.7901 -  1.7597    0.95     2534   130  0.3617 0.3919   0.780  0.737
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)     : 0.25    
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 27.74   
REMARK   3  
REMARK   3  STRUCTURE FACTORS CALCULATION ALGORITHM : FFT
REMARK   3  
REMARK   3  
REMARK   3  GEOMETRY RESTRAINTS LIBRARY: GEOSTD + MONOMER LIBRARY + CDL V1.2
REMARK   3  DEVIATIONS FROM IDEAL VALUES.
REMARK   3    BOND      :  0.006   0.073   5108
REMARK   3    ANGLE     :  0.866   7.835   6936
REMARK   3    CHIRALITY :  0.054   0.242    724
REMARK   3    PLANARITY :  0.005   0.041    904
REMARK   3    DIHEDRAL  : 16.915 176.831   3065
REMARK   3    MIN NONBONDED DISTANCE : 1.895
REMARK   3  
REMARK   3  MOLPROBITY STATISTICS.
REMARK   3    ALL-ATOM CLASHSCORE : 4.76
REMARK   3    RAMACHANDRAN PLOT:
REMARK   3      OUTLIERS :  0.16 %
REMARK   3      ALLOWED  :  4.21 %
REMARK   3      FAVORED  : 95.63 %
REMARK   3    ROTAMER OUTLIERS :  1.90 %
REMARK   3    CBETA DEVIATIONS :  0.00 %
REMARK   3    PEPTIDE PLANE:
REMARK   3      CIS-PROLINE     : 2.33 %
REMARK   3      CIS-GENERAL     : 0.17 %
REMARK   3      TWISTED PROLINE : 0.00 %
REMARK   3      TWISTED GENERAL : 0.00 %
REMARK   3  
REMARK   3                  min    max   mean    iso aniso
REMARK   3     Overall:   11.43 138.92  32.67   4.13  5240  4928
REMARK   3     Protein:   11.43 138.92  32.69   4.14  4928  4928
REMARK   3     Water:     14.63  86.06  33.64    N/A   267     0
REMARK   3     Other:     15.20  83.94  24.52    N/A    45     0
REMARK   3     Chain  A:  11.43 138.92  32.70    N/A  4930  4928
REMARK   3     Chain   :  15.20  30.83  23.26    N/A    42     0
REMARK   3     Chain  S:  14.63  86.06  33.64    N/A   267     0
REMARK   3     Chain  B:  23.36  23.36  23.36    N/A     1     0
REMARK   3     Histogram:
REMARK   3         Values      Number of atoms
REMARK   3      11.43 - 24.18      1640
REMARK   3      24.18 - 36.93      2319
REMARK   3      36.93 - 49.68       720
REMARK   3      49.68 - 62.43       294
REMARK   3      62.43 - 75.18       124
REMARK   3      75.18 - 87.93        50
REMARK   3      87.93 - 100.68       29
REMARK   3     100.68 - 113.43       38
REMARK   3     113.43 - 126.18       12
REMARK   3     126.18 - 138.92       14
REMARK   3  
REMARK   3  
REMARK   3  TLS DETAILS.
REMARK   3   NUMBER OF TLS GROUPS: 5     
REMARK   3   ORIGIN: CENTER OF MASS
REMARK   3   TLS GROUP : 1     
REMARK   3    SELECTION: chain 'A' and (resid    3  through  225 )
REMARK   3    ORIGIN FOR THE GROUP (A):   2.4491 -11.1857  -5.7409
REMARK   3    T TENSOR                                            
REMARK   3      T11:   0.1949 T22:   0.1566                       
REMARK   3      T33:   0.2059 T12:  -0.0080                       
REMARK   3      T13:   0.0407 T23:  -0.0217                       
REMARK   3    L TENSOR                                            
REMARK   3      L11:   0.1483 L22:   0.6760                       
REMARK   3      L33:   0.4841 L12:   0.1534                       
REMARK   3      L13:   0.0552 L23:   0.1966                       
REMARK   3    S TENSOR                                            
REMARK   3      S11:   0.0002 S12:   0.0656 S13:  -0.0549         
REMARK   3      S21:  -0.0792 S22:  -0.0333 S23:  -0.0116         
REMARK   3      S31:   0.0123 S32:   0.0128 S33:  -0.0000         
REMARK   3   TLS GROUP : 2     
REMARK   3    SELECTION: chain 'A' and (resid  226  through  352 )
REMARK   3    ORIGIN FOR THE GROUP (A):  -9.5797   1.6504   8.5021
REMARK   3    T TENSOR                                            
REMARK   3      T11:   0.2586 T22:   0.1910                       
REMARK   3      T33:   0.2171 T12:  -0.0350                       
REMARK   3      T13:   0.0858 T23:  -0.0232                       
REMARK   3    L TENSOR                                            
REMARK   3      L11:   0.1874 L22:   0.1526                       
REMARK   3      L33:   0.0929 L12:  -0.1758                       
REMARK   3      L13:   0.0348 L23:   0.0276                       
REMARK   3    S TENSOR                                            
REMARK   3      S11:  -0.0975 S12:   0.1125 S13:  -0.1660         
REMARK   3      S21:   0.2188 S22:  -0.0272 S23:   0.1393         
REMARK   3      S31:   0.1517 S32:  -0.0918 S33:  -0.0014         
REMARK   3   TLS GROUP : 3     
REMARK   3    SELECTION: chain 'A' and (resid  353  through  412 )
REMARK   3    ORIGIN FOR THE GROUP (A):  -2.4106 -18.7836  20.0485
REMARK   3    T TENSOR                                            
REMARK   3      T11:   0.6307 T22:   0.0340                       
REMARK   3      T33:   0.2934 T12:  -0.1269                       
REMARK   3      T13:   0.1484 T23:   0.0823                       
REMARK   3    L TENSOR                                            
REMARK   3      L11:   0.2555 L22:   0.1712                       
REMARK   3      L33:   0.0951 L12:   0.0882                       
REMARK   3      L13:  -0.1447 L23:  -0.0327                       
REMARK   3    S TENSOR                                            
REMARK   3      S11:  -0.0913 S12:  -0.0865 S13:  -0.4134         
REMARK   3      S21:   0.4617 S22:  -0.0446 S23:  -0.0192         
REMARK   3      S31:   0.1695 S32:   0.0427 S33:  -0.4526         
REMARK   3   TLS GROUP : 4     
REMARK   3    SELECTION: chain 'A' and (resid  413  through  474 )
REMARK   3    ORIGIN FOR THE GROUP (A):  -4.8976   8.9374  14.8192
REMARK   3    T TENSOR                                            
REMARK   3      T11:   0.2107 T22:   0.1483                       
REMARK   3      T33:   0.1782 T12:  -0.0218                       
REMARK   3      T13:   0.0439 T23:  -0.0038                       
REMARK   3    L TENSOR                                            
REMARK   3      L11:   0.0983 L22:   0.0725                       
REMARK   3      L33:   0.1182 L12:  -0.0289                       
REMARK   3      L13:  -0.0881 L23:   0.0700                       
REMARK   3    S TENSOR                                            
REMARK   3      S11:  -0.1086 S12:   0.0397 S13:  -0.1658         
REMARK   3      S21:   0.1295 S22:  -0.0680 S23:   0.0328         
REMARK   3      S31:   0.1229 S32:  -0.0250 S33:  -0.0042         
REMARK   3   TLS GROUP : 5     
REMARK   3    SELECTION: chain 'A' and (resid  475  through  622 )
REMARK   3    ORIGIN FOR THE GROUP (A):  -2.4520  16.8314  19.1910
REMARK   3    T TENSOR                                            
REMARK   3      T11:   0.2528 T22:   0.1424                       
REMARK   3      T33:   0.1578 T12:  -0.0190                       
REMARK   3      T13:   0.0295 T23:   0.0085                       
REMARK   3    L TENSOR                                            
REMARK   3      L11:   0.4963 L22:   0.1962                       
REMARK   3      L33:   0.1138 L12:  -0.1186                       
REMARK   3      L13:  -0.0212 L23:  -0.0348                       
REMARK   3    S TENSOR                                            
REMARK   3      S11:  -0.0664 S12:  -0.0445 S13:   0.0107         
REMARK   3      S21:   0.0765 S22:   0.0037 S23:   0.0076         
REMARK   3      S31:  -0.0526 S32:  -0.0125 S33:  -0.0000         
REMARK   3
HELIX    1   1 PHE A   11  ALA A   13  5                                   3
HELIX    2   2 PRO A   24  GLN A   39  1                                  16
HELIX    3   3 SER A   49  GLU A   63  1                                  15
HELIX    4   4 ILE A   88  SER A   90  5                                   3
HELIX    5   5 GLU A   98  VAL A  103  1                                   6
HELIX    6   6 SER A  118  ALA A  128  1                                  11
HELIX    7   7 SER A  163  THR A  174  1                                  12
HELIX    8   8 GLY A  177  GLY A  185  1                                   9
HELIX    9   9 ASN A  213  THR A  217  5                                   5
HELIX   10  10 TYR A  235  LEU A  240  1                                   6
HELIX   11  11 LEU A  248  GLY A  259  1                                  12
HELIX   12  12 GLY A  289  MET A  295  1                                   7
HELIX   13  13 ASN A  344  ILE A  351  1                                   8
HELIX   14  14 SER A  411  CYS A  413  5                                   3
HELIX   15  15 SER A  449  ALA A  459  1                                  11
HELIX   16  16 PRO A  479  MET A  482  5                                   4
HELIX   17  17 ASN A  489  MET A  500  1                                  12
HELIX   18  18 ALA A  501  ARG A  503  5                                   3
HELIX   19  19 GLY A  529  GLU A  532  5                                   4
HELIX   20  20 ASN A  533  GLU A  545  1                                  13
HELIX   21  21 ASN A  573  PHE A  578  1                                   6
HELIX   22  22 SER A  581  VAL A  600  1                                  20
HELIX   23  23 ASN A  601  LEU A  604  5                                   4
HELIX   24  24 PRO A  605  GLN A  621  1                                  17
SHEET    1   A 9 VAL A  15  GLN A  17  0
SHEET    2   A 9 TYR A  42  ILE A  45  1  O  ILE A  43   N  ILE A  16
SHEET    3   A 9 THR A 138  MET A 146  1  O  MET A 139   N  TYR A  42
SHEET    4   A 9 LYS A 155  THR A 161 -1  O  THR A 161   N  TYR A 140
SHEET    5   A 9 ILE A 190  SER A 195  1  O  CYS A 192   N  LEU A 160
SHEET    6   A 9 GLU A 227  PHE A 231  1  O  SER A 230   N  LEU A 193
SHEET    7   A 9 LEU A 218  LEU A 222 -1  N  LEU A 222   O  GLU A 227
SHEET    8   A 9 THR A  92  ILE A  95  1  N  ILE A  95   O  HIS A 221
SHEET    9   A 9 TRP A 116  MET A 117  1  O  MET A 117   N  ILE A  94
SHEET    1   B 4 VAL A  15  GLN A  17  0
SHEET    2   B 4 TYR A  42  ILE A  45  1  O  ILE A  43   N  ILE A  16
SHEET    3   B 4 THR A 138  MET A 146  1  O  MET A 139   N  TYR A  42
SHEET    4   B 4 ARG A 175  MET A 176 -1  O  ARG A 175   N  SER A 145
SHEET    1   C 5 ARG A  67  LEU A  69  0
SHEET    2   C 5 CYS A  75  ALA A  78 -1  O  CYS A  75   N  LEU A  69
SHEET    3   C 5 ILE A 356  THR A 358  1  O  PHE A 357   N  TRP A  76
SHEET    4   C 5 ARG A 405  PRO A 409 -1  O  ARG A 405   N  THR A 358
SHEET    5   C 5 GLY A 331  VAL A 335 -1  N  PHE A 332   O  THR A 408
SHEET    1   D 7 LEU A 261  GLU A 263  0
SHEET    2   D 7 ALA A 313  PHE A 317 -1  O  MET A 315   N  LEU A 261
SHEET    3   D 7 LEU A 323  ILE A 326 -1  O  ILE A 326   N  TRP A 314
SHEET    4   D 7 VAL A 426  GLY A 434 -1  O  ILE A 428   N  LEU A 323
SHEET    5   D 7 LYS A 277  ALA A 283  1  N  TYR A 279   O  GLU A 429
SHEET    6   D 7 LEU A 266  THR A 271 -1  N  ILE A 270   O  LYS A 278
SHEET    7   D 7 LYS A 304  GLY A 309 -1  O  GLU A 306   N  GLY A 269
SHEET    1   E 6 LEU A 261  GLU A 263  0
SHEET    2   E 6 ALA A 313  PHE A 317 -1  O  MET A 315   N  LEU A 261
SHEET    3   E 6 LEU A 323  ILE A 326 -1  O  ILE A 326   N  TRP A 314
SHEET    4   E 6 VAL A 426  GLY A 434 -1  O  ILE A 428   N  LEU A 323
SHEET    5   E 6 LYS A 510  VAL A 514  1  O  PHE A 512   N  PHE A 433
SHEET    6   E 6 VAL A 444  GLU A 446 -1  N  TYR A 445   O  HIS A 513
SHEET    1   F 4 VAL A 368  TYR A 369  0
SHEET    2   F 4 ALA A 361  THR A 363 -1  N  ALA A 361   O  TYR A 369
SHEET    3   F 4 ILE A 383  THR A 384 -1  O  THR A 384   N  GLU A 362
SHEET    4   F 4 GLU A 390  TRP A 391 -1  O  TRP A 391   N  ILE A 383
SHEET    1   G 2 ARG A 461  GLU A 463  0
SHEET    2   G 2 ILE A 475  HIS A 477 -1  O  MET A 476   N  SER A 462
SHEET    1   H 2 ALA A 550  THR A 553  0
SHEET    2   H 2 GLY A 556  PRO A 559 -1  O  VAL A 558   N  LYS A 551
CRYST1   44.392  118.614   59.865  90.00 111.62  90.00 P 1 21 1
SCALE1      0.022527  0.000000  0.008930        0.00000
SCALE2      0.000000  0.008431  0.000000        0.00000
SCALE3      0.000000  0.000000  0.017969        0.00000
HETATM    1  C14 GTP     1      -3.508  -3.347  20.009  1.00 30.83           C
HETATM    2  C15 GTP     1      -2.487  -2.711  21.077  1.00 28.62           C
HETATM    3  C17 GTP     1      -2.301  -3.445  22.304  1.00 26.24           C
HETATM    4  C19 GTP     1      -3.451  -3.036  23.274  1.00 24.19           C
HETATM    5  C21 GTP     1      -3.117  -1.386  22.949  1.00 23.34           C
HETATM    6  C23 GTP     1      -5.380  -0.499  22.134  1.00 19.80           C
HETATM    7  C25 GTP     1      -5.784   0.760  24.041  1.00 22.36           C
HETATM    8  C26 GTP     1      -6.373   1.526  24.837  1.00 26.52           C
HETATM    9  C29 GTP     1      -4.447   1.049  26.107  1.00 24.10           C
HETATM   10  C32 GTP     1      -4.630   0.156  24.210  1.00 23.72           C
HETATM   11  N22 GTP     1      -4.386  -0.577  23.105  1.00 21.58           N
HETATM   12  N24 GTP     1      -6.216   0.345  22.779  1.00 22.03           N
HETATM   13  N28 GTP     1      -5.554   1.711  26.091  1.00 21.78           N
HETATM   14  N30 GTP     1      -3.632   1.227  27.343  1.00 20.64           N
HETATM   15  N31 GTP     1      -3.820   0.232  25.269  1.00 24.48           N
HETATM   16  O02 GTP     1      -0.619  -2.828  12.823  1.00 22.52           O
HETATM   17  O03 GTP     1      -3.115  -3.245  12.464  1.00 27.97           O
HETATM   18  O04 GTP     1      -2.078  -1.005  11.925  1.00 24.53           O
HETATM   19  O05 GTP     1      -2.085  -1.688  14.269  1.00 23.11           O
HETATM   20  O07 GTP     1      -3.242   0.417  15.223  1.00 19.45           O
HETATM   21  O08 GTP     1      -4.657  -1.561  14.806  1.00 15.71           O
HETATM   22  O09 GTP     1      -2.823  -1.613  16.613  1.00 21.93           O
HETATM   23  O11 GTP     1      -3.979  -3.829  16.945  1.00 23.51           O
HETATM   24  O12 GTP     1      -1.525  -3.533  17.677  1.00 22.42           O
HETATM   25  O13 GTP     1      -3.452  -2.321  18.922  1.00 25.43           O
HETATM   26  O16 GTP     1      -2.796  -1.380  21.548  1.00 27.06           O
HETATM   27  O18 GTP     1      -1.018  -3.307  22.859  1.00 24.95           O
HETATM   28  O20 GTP     1      -3.157  -3.168  24.562  1.00 25.60           O
HETATM   29  O27 GTP     1      -7.444   2.195  24.906  1.00 21.71           O
HETATM   30  P01 GTP     1      -2.009  -2.228  12.724  1.00 22.79           P
HETATM   31  P06 GTP     1      -3.310  -1.135  15.206  1.00 22.68           P
HETATM   32  P10 GTP     1      -2.941  -2.979  17.501  1.00 28.26           P
HETATM   33  C01 LIG     1       0.570  -2.083   9.968  1.00 25.55           C
HETATM   34  C02 LIG     1      -0.274  -3.284   9.571  1.00 22.59           C
HETATM   35  C03 LIG     1       0.063  -4.615   9.376  1.00 19.17           C
HETATM   36  O01 LIG     1       1.809  -2.380  10.166  1.00 25.74           O
HETATM   37  O02 LIG     1       0.087  -0.952  10.099  1.00 15.20           O
HETATM   38  O03 LIG     1      -1.510  -2.972   9.411  1.00 19.52           O
HETATM   39  O04 LIG     1       1.731  -4.025   7.409  1.00 24.39           O
HETATM   40  O05 LIG     1      -0.395  -4.997   6.911  1.00 19.94           O
HETATM   41  O06 LIG     1       1.446  -6.250   7.780  1.00 24.28           O
HETATM   42  S01 LIG     1       0.777  -5.008   7.734  1.00 20.82           S
ATOM     43  N   PRO A   3       2.632 -13.735 -31.633  1.00 81.14           N
ANISOU   43  N   PRO A   3    11409   9886   9534   -227    516   -524       N
ATOM     44  CA  PRO A   3       3.893 -13.810 -32.379  1.00 74.51           C
ANISOU   44  CA  PRO A   3    10611   9045   8653   -252    605   -537       C
ATOM     45  C   PRO A   3       4.915 -14.696 -31.675  1.00 60.35           C
ANISOU   45  C   PRO A   3     8738   7267   6925   -240    681   -553       C
ATOM     46  O   PRO A   3       5.114 -14.565 -30.463  1.00 55.75           O
ANISOU   46  O   PRO A   3     8071   6700   6411   -220    681   -536       O
ATOM     47  CB  PRO A   3       4.362 -12.350 -32.429  1.00 80.76           C
ANISOU   47  CB  PRO A   3    11434   9840   9410   -272    612   -504       C
ATOM     48  CG  PRO A   3       3.720 -11.705 -31.249  1.00 83.98           C
ANISOU   48  CG  PRO A   3    11777  10259   9874   -247    552   -475       C
ATOM     49  CD  PRO A   3       2.395 -12.395 -31.069  1.00 85.90           C
ANISOU   49  CD  PRO A   3    12002  10495  10143   -223    476   -487       C
ATOM     50  N   GLN A   4       5.555 -15.585 -32.434  1.00 54.59           N
ANISOU   50  N   GLN A   4     8038   6531   6174   -250    744   -587       N
ATOM     51  CA  GLN A   4       6.440 -16.585 -31.851  1.00 46.94           C
ANISOU   51  CA  GLN A   4     6996   5571   5268   -232    809   -608       C
ATOM     52  C   GLN A   4       7.229 -17.333 -32.921  1.00 40.36           C
ANISOU   52  C   GLN A   4     6211   4728   4395   -249    885   -647       C
ATOM     53  O   GLN A   4       6.647 -17.863 -33.875  1.00 35.74           O
ANISOU   53  O   GLN A   4     5698   4124   3759   -259    867   -669       O
ATOM     54  CB  GLN A   4       5.621 -17.577 -31.020  1.00 53.45           C
ANISOU   54  CB  GLN A   4     7761   6392   6155   -201    761   -615       C
ATOM     55  CG  GLN A   4       6.309 -18.061 -29.775  1.00 50.80           C
ANISOU   55  CG  GLN A   4     7326   6069   5905   -174    793   -612       C
ATOM     56  CD  GLN A   4       5.395 -18.911 -28.910  1.00 52.02           C
ANISOU   56  CD  GLN A   4     7432   6218   6115   -149    740   -615       C
ATOM     57  OE1 GLN A   4       5.677 -19.136 -27.737  1.00 53.19           O
ANISOU   57  OE1 GLN A   4     7504   6374   6331   -128    744   -604       O
ATOM     58  NE2 GLN A   4       4.287 -19.376 -29.484  1.00 50.57           N
ANISOU   58  NE2 GLN A   4     7295   6019   5902   -153    688   -630       N
ATOM     59  N   LEU A   5       8.555 -17.386 -32.783  1.00 39.86           N
ANISOU   59  N   LEU A   5     6110   4678   4357   -251    971   -658       N
ATOM     60  CA  LEU A   5       9.350 -18.222 -33.676  1.00 43.12           C
ANISOU   60  CA  LEU A   5     6555   5082   4746   -261   1051   -700       C
ATOM     61  C   LEU A   5       9.481 -19.646 -33.162  1.00 42.48           C
ANISOU   61  C   LEU A   5     6413   4995   4733   -226   1066   -729       C
ATOM     62  O   LEU A   5       9.810 -20.550 -33.942  1.00 36.83           O
ANISOU   62  O   LEU A   5     5733   4266   3997   -228   1115   -769       O
ATOM     63  CB  LEU A   5      10.741 -17.613 -33.889  1.00 44.05           C
ANISOU   63  CB  LEU A   5     6663   5217   4858   -284   1142   -705       C
ATOM     64  CG  LEU A   5      10.767 -16.458 -34.894  1.00 40.49           C
ANISOU   64  CG  LEU A   5     6309   4762   4314   -332   1152   -691       C
ATOM     65  CD1 LEU A   5      12.099 -15.720 -34.851  1.00 36.85           C
ANISOU   65  CD1 LEU A   5     5822   4321   3859   -356   1236   -690       C
ATOM     66  CD2 LEU A   5      10.485 -16.993 -36.291  1.00 44.50           C
ANISOU   66  CD2 LEU A   5     6923   5246   4740   -356   1168   -724       C
ATOM     67  N   HIS A   6       9.220 -19.854 -31.870  1.00 45.73           N
ANISOU   67  N   HIS A   6     6740   5415   5222   -194   1026   -710       N
ATOM     68  CA  HIS A   6       9.246 -21.167 -31.242  1.00 47.03           C
ANISOU   68  CA  HIS A   6     6849   5570   5452   -159   1029   -732       C
ATOM     69  C   HIS A   6       8.023 -21.318 -30.345  1.00 49.96           C
ANISOU   69  C   HIS A   6     7189   5936   5856   -141    940   -709       C
ATOM     70  O   HIS A   6       6.899 -21.082 -30.798  1.00 51.12           O
ANISOU   70  O   HIS A   6     7390   6074   5958   -155    879   -702       O
ATOM     71  CB  HIS A   6      10.550 -21.352 -30.467  1.00 47.36           C
ANISOU   71  CB  HIS A   6     6804   5626   5563   -137   1091   -736       C
ATOM     72  CG  HIS A   6      11.770 -21.184 -31.315  1.00 50.61           C
ANISOU   72  CG  HIS A   6     7236   6046   5949   -156   1183   -763       C
ATOM     73  ND1 HIS A   6      12.250 -22.183 -32.135  1.00 50.16           N
ANISOU   73  ND1 HIS A   6     7207   5972   5878   -153   1243   -809       N
ATOM     74  CD2 HIS A   6      12.591 -20.121 -31.494  1.00 50.34           C
ANISOU   74  CD2 HIS A   6     7200   6032   5896   -182   1229   -751       C
ATOM     75  CE1 HIS A   6      13.321 -21.747 -32.773  1.00 50.33           C
ANISOU   75  CE1 HIS A   6     7239   6006   5877   -175   1324   -827       C
ATOM     76  NE2 HIS A   6      13.551 -20.500 -32.400  1.00 49.19           N
ANISOU   76  NE2 HIS A   6     7077   5885   5729   -194   1317   -792       N
ATOM     77  N   ASN A   7       8.218 -21.701 -29.071  1.00 57.84           N
ANISOU   77  N   ASN A   7     8103   6940   6933   -112    932   -698       N
ATOM     78  CA  ASN A   7       7.062 -21.950 -28.213  1.00 68.54           C
ANISOU   78  CA  ASN A   7     9432   8289   8321    -99    856   -681       C
ATOM     79  C   ASN A   7       7.286 -21.558 -26.753  1.00 64.75           C
ANISOU   79  C   ASN A   7     8868   7824   7908    -80    839   -649       C
ATOM     80  O   ASN A   7       6.602 -22.099 -25.874  1.00 55.86           O
ANISOU   80  O   ASN A   7     7708   6690   6825    -65    796   -643       O
ATOM     81  CB  ASN A   7       6.656 -23.436 -28.269  1.00 76.22           C
ANISOU   81  CB  ASN A   7    10410   9237   9313    -83    849   -712       C
ATOM     82  CG  ASN A   7       5.177 -23.651 -27.993  1.00 85.04           C
ANISOU   82  CG  ASN A   7    11537  10345  10429    -87    770   -705       C
ATOM     83  OD1 ASN A   7       4.342 -22.804 -28.314  1.00 88.66           O
ANISOU   83  OD1 ASN A   7    12028  10811  10849   -105    721   -688       O
ATOM     84  ND2 ASN A   7       4.847 -24.789 -27.389  1.00 89.01           N
ANISOU   84  ND2 ASN A   7    12013  10831  10977    -70    756   -718       N
ATOM     85  N   GLY A   8       8.198 -20.635 -26.464  1.00 67.81           N
ANISOU   85  N   GLY A   8     9227   8231   8305    -84    872   -630       N
ATOM     86  CA  GLY A   8       8.488 -20.231 -25.105  1.00 67.33           C
ANISOU   86  CA  GLY A   8     9092   8184   8306    -69    858   -601       C
ATOM     87  C   GLY A   8       7.816 -18.961 -24.627  1.00 63.28           C
ANISOU   87  C   GLY A   8     8578   7685   7780    -82    807   -562       C
ATOM     88  O   GLY A   8       8.121 -18.504 -23.518  1.00 69.19           O
ANISOU   88  O   GLY A   8     9269   8445   8574    -72    798   -537       O
ATOM     89  N   LEU A   9       6.911 -18.374 -25.413  1.00 54.80           N
ANISOU   89  N   LEU A   9     7566   6608   6647   -102    769   -558       N
ATOM     90  CA  LEU A   9       6.259 -17.121 -25.048  1.00 51.08           C
ANISOU   90  CA  LEU A   9     7098   6146   6162   -111    719   -524       C
ATOM     91  C   LEU A   9       4.762 -17.250 -24.815  1.00 43.81           C
ANISOU   91  C   LEU A   9     6186   5218   5244   -106    643   -521       C
ATOM     92  O   LEU A   9       4.220 -16.531 -23.975  1.00 46.77           O
ANISOU   92  O   LEU A   9     6529   5600   5640   -102    601   -495       O
ATOM     93  CB  LEU A   9       6.497 -16.062 -26.130  1.00 51.19           C
ANISOU   93  CB  LEU A   9     7180   6165   6106   -139    733   -518       C
ATOM     94  CG  LEU A   9       7.958 -15.772 -26.472  1.00 50.81           C
ANISOU   94  CG  LEU A   9     7129   6127   6049   -153    813   -523       C
ATOM     95  CD1 LEU A   9       8.030 -14.594 -27.428  1.00 52.24           C
ANISOU   95  CD1 LEU A   9     7383   6309   6156   -185    818   -511       C
ATOM     96  CD2 LEU A   9       8.772 -15.498 -25.211  1.00 46.54           C
ANISOU   96  CD2 LEU A   9     6505   5603   5575   -139    832   -503       C
ATOM     97  N   ASP A  10       4.084 -18.128 -25.551  1.00 36.85           N
ANISOU   97  N   ASP A  10     5342   4320   4338   -108    626   -548       N
ATOM     98  CA  ASP A  10       2.674 -18.433 -25.314  1.00 39.22           C
ANISOU   98  CA  ASP A  10     5642   4614   4648   -104    557   -551       C
ATOM     99  C   ASP A  10       2.578 -19.406 -24.138  1.00 31.14           C
ANISOU   99  C   ASP A  10     4553   3586   3693    -86    557   -555       C
ATOM    100  O   ASP A  10       2.917 -20.588 -24.274  1.00 24.45           O
ANISOU  100  O   ASP A  10     3705   2725   2860    -79    587   -580       O
ATOM    101  CB  ASP A  10       2.053 -19.036 -26.575  1.00 41.60           C
ANISOU  101  CB  ASP A  10     6011   4898   4897   -116    540   -580       C
ATOM    102  CG  ASP A  10       0.538 -19.097 -26.519  1.00 45.52           C
ANISOU  102  CG  ASP A  10     6512   5389   5394   -117    462   -584       C
ATOM    103  OD1 ASP A  10      -0.085 -19.199 -27.595  1.00 48.39           O
ANISOU  103  OD1 ASP A  10     6937   5742   5707   -130    432   -601       O
ATOM    104  OD2 ASP A  10      -0.034 -19.026 -25.411  1.00 43.99           O
ANISOU  104  OD2 ASP A  10     6260   5203   5252   -107    431   -571       O
ATOM    105  N   PHE A  11       2.109 -18.934 -22.985  1.00 27.99           N
ANISOU  105  N   PHE A  11     4104   3196   3335    -79    524   -532       N
ATOM    106  CA  PHE A  11       2.031 -19.797 -21.809  1.00 24.77           C
ANISOU  106  CA  PHE A  11     3641   2782   2988    -66    524   -533       C
ATOM    107  C   PHE A  11       0.698 -20.511 -21.667  1.00 23.16           C
ANISOU  107  C   PHE A  11     3437   2567   2796    -71    476   -550       C
ATOM    108  O   PHE A  11       0.430 -21.074 -20.597  1.00 25.37           O
ANISOU  108  O   PHE A  11     3674   2842   3124    -65    469   -547       O
ATOM    109  CB  PHE A  11       2.327 -18.997 -20.537  1.00 20.35           C
ANISOU  109  CB  PHE A  11     3028   2236   2469    -59    521   -501       C
ATOM    110  CG  PHE A  11       3.773 -19.078 -20.100  1.00 29.17           C
ANISOU  110  CG  PHE A  11     4115   3356   3611    -49    575   -492       C
ATOM    111  CD1 PHE A  11       4.144 -19.843 -19.002  1.00 30.91           C
ANISOU  111  CD1 PHE A  11     4289   3569   3886    -34    586   -490       C
ATOM    112  CD2 PHE A  11       4.761 -18.398 -20.797  1.00 33.05           C
ANISOU  112  CD2 PHE A  11     4626   3859   4072    -55    615   -488       C
ATOM    113  CE1 PHE A  11       5.476 -19.929 -18.607  1.00 27.42           C
ANISOU  113  CE1 PHE A  11     3816   3130   3471    -21    629   -484       C
ATOM    114  CE2 PHE A  11       6.089 -18.476 -20.407  1.00 33.98           C
ANISOU  114  CE2 PHE A  11     4709   3983   4220    -45    664   -484       C
ATOM    115  CZ  PHE A  11       6.445 -19.246 -19.308  1.00 31.30           C
ANISOU  115  CZ  PHE A  11     4319   3635   3938    -27    669   -482       C
ATOM    116  N   SER A  12      -0.129 -20.530 -22.716  1.00 20.32           N
ANISOU  116  N   SER A  12     3125   2203   2393    -83    443   -567       N
ATOM    117  CA  SER A  12      -1.465 -21.116 -22.596  1.00 26.71           C
ANISOU  117  CA  SER A  12     3930   3005   3215    -90    393   -585       C
ATOM    118  C   SER A  12      -1.421 -22.584 -22.180  1.00 24.86           C
ANISOU  118  C   SER A  12     3681   2752   3014    -88    414   -606       C
ATOM    119  O   SER A  12      -2.288 -23.047 -21.425  1.00 29.09           O
ANISOU  119  O   SER A  12     4185   3283   3585    -94    386   -611       O
ATOM    120  CB  SER A  12      -2.224 -20.967 -23.909  1.00 31.07           C
ANISOU  120  CB  SER A  12     4540   3552   3712   -103    355   -603       C
ATOM    121  OG  SER A  12      -2.307 -19.606 -24.277  1.00 38.64           O
ANISOU  121  OG  SER A  12     5519   4523   4638   -103    331   -582       O
ATOM    122  N   ALA A  13      -0.435 -23.343 -22.666  1.00 23.57           N
ANISOU  122  N   ALA A  13     3540   2575   2841    -82    463   -621       N
ATOM    123  CA  ALA A  13      -0.395 -24.764 -22.322  1.00 23.67           C
ANISOU  123  CA  ALA A  13     3546   2565   2884    -78    480   -642       C
ATOM    124  C   ALA A  13      -0.196 -25.002 -20.835  1.00 25.32           C
ANISOU  124  C   ALA A  13     3698   2770   3151    -68    486   -624       C
ATOM    125  O   ALA A  13      -0.380 -26.133 -20.374  1.00 24.68           O
ANISOU  125  O   ALA A  13     3612   2668   3098    -68    488   -638       O
ATOM    126  CB  ALA A  13       0.715 -25.483 -23.087  1.00 22.74           C
ANISOU  126  CB  ALA A  13     3461   2432   2748    -68    535   -662       C
ATOM    127  N   LYS A  14       0.167 -23.973 -20.075  1.00 24.23           N
ANISOU  127  N   LYS A  14     3523   2651   3030    -61    486   -593       N
ATOM    128  CA  LYS A  14       0.465 -24.127 -18.661  1.00 26.47           C
ANISOU  128  CA  LYS A  14     3760   2933   3366    -52    493   -573       C
ATOM    129  C   LYS A  14      -0.649 -23.598 -17.775  1.00 23.96           C
ANISOU  129  C   LYS A  14     3412   2624   3068    -65    450   -559       C
ATOM    130  O   LYS A  14      -0.483 -23.561 -16.553  1.00 26.66           O
ANISOU  130  O   LYS A  14     3717   2964   3447    -62    453   -541       O
ATOM    131  CB  LYS A  14       1.784 -23.435 -18.317  1.00 27.53           C
ANISOU  131  CB  LYS A  14     3871   3079   3511    -35    528   -550       C
ATOM    132  CG  LYS A  14       3.014 -24.243 -18.697  1.00 35.57           C
ANISOU  132  CG  LYS A  14     4897   4083   4535    -17    577   -565       C
ATOM    133  CD  LYS A  14       4.301 -23.568 -18.247  1.00 42.21           C
ANISOU  133  CD  LYS A  14     5704   4937   5395     -2    610   -544       C
ATOM    134  CE  LYS A  14       5.505 -24.493 -18.448  1.00 49.91           C
ANISOU  134  CE  LYS A  14     6675   5897   6390     20    657   -562       C
ATOM    135  NZ  LYS A  14       5.630 -24.973 -19.856  1.00 49.71           N
ANISOU  135  NZ  LYS A  14     6697   5864   6325     18    684   -595       N
ATOM    136  N   VAL A  15      -1.782 -23.219 -18.357  1.00 22.21           N
ANISOU  136  N   VAL A  15     3204   2411   2822    -80    411   -570       N
ATOM    137  CA  VAL A  15      -2.877 -22.629 -17.592  1.00 27.18           C
ANISOU  137  CA  VAL A  15     3802   3053   3473    -91    371   -562       C
ATOM    138  C   VAL A  15      -3.712 -23.759 -17.003  1.00 23.65           C
ANISOU  138  C   VAL A  15     3342   2589   3055   -107    360   -581       C
ATOM    139  O   VAL A  15      -4.243 -24.601 -17.735  1.00 26.85           O
ANISOU  139  O   VAL A  15     3774   2981   3445   -119    349   -610       O
ATOM    140  CB  VAL A  15      -3.734 -21.701 -18.466  1.00 27.12           C
ANISOU  140  CB  VAL A  15     3811   3061   3432    -97    329   -566       C
ATOM    141  CG1 VAL A  15      -4.928 -21.180 -17.662  1.00 22.91           C
ANISOU  141  CG1 VAL A  15     3237   2539   2927   -106    289   -564       C
ATOM    142  CG2 VAL A  15      -2.895 -20.529 -19.005  1.00 23.53           C
ANISOU  142  CG2 VAL A  15     3376   2620   2945    -85    341   -544       C
ATOM    143  N   ILE A  16      -3.818 -23.789 -15.675  1.00 19.77           N
ANISOU  143  N   ILE A  16     2814   2096   2603   -111    364   -567       N
ATOM    144  CA  ILE A  16      -4.586 -24.830 -15.000  1.00 26.20           C
ANISOU  144  CA  ILE A  16     3619   2892   3444   -132    358   -583       C
ATOM    145  C   ILE A  16      -5.936 -24.335 -14.510  1.00 29.93           C
ANISOU  145  C   ILE A  16     4059   3379   3933   -152    324   -590       C
ATOM    146  O   ILE A  16      -6.759 -25.156 -14.079  1.00 26.15           O
ANISOU  146  O   ILE A  16     3574   2889   3475   -176    318   -609       O
ATOM    147  CB  ILE A  16      -3.782 -25.432 -13.832  1.00 24.79           C
ANISOU  147  CB  ILE A  16     3430   2693   3296   -126    388   -567       C
ATOM    148  CG1 ILE A  16      -3.431 -24.327 -12.834  1.00 26.80           C
ANISOU  148  CG1 ILE A  16     3651   2964   3567   -118    391   -534       C
ATOM    149  CG2 ILE A  16      -2.529 -26.147 -14.396  1.00 24.20           C
ANISOU  149  CG2 ILE A  16     3384   2600   3211   -104    421   -569       C
ATOM    150  CD1 ILE A  16      -2.590 -24.771 -11.662  1.00 27.40           C
ANISOU  150  CD1 ILE A  16     3719   3021   3670   -112    414   -514       C
ATOM    151  N   GLN A  17      -6.187 -23.025 -14.543  1.00 22.38           N
ANISOU  151  N   GLN A  17     3085   2448   2972   -144    303   -576       N
ATOM    152  CA  GLN A  17      -7.536 -22.505 -14.354  1.00 28.24           C
ANISOU  152  CA  GLN A  17     3796   3205   3729   -159    266   -589       C
ATOM    153  C   GLN A  17      -7.671 -21.208 -15.128  1.00 27.84           C
ANISOU  153  C   GLN A  17     3750   3175   3652   -142    236   -581       C
ATOM    154  O   GLN A  17      -6.781 -20.361 -15.054  1.00 24.35           O
ANISOU  154  O   GLN A  17     3313   2740   3199   -124    251   -553       O
ATOM    155  CB  GLN A  17      -7.859 -22.252 -12.883  1.00 25.43           C
ANISOU  155  CB  GLN A  17     3398   2852   3410   -170    276   -577       C
ATOM    156  CG  GLN A  17      -9.278 -21.740 -12.694  1.00 29.71           C
ANISOU  156  CG  GLN A  17     3904   3411   3973   -185    242   -597       C
ATOM    157  CD  GLN A  17      -9.738 -21.805 -11.258  1.00 35.88           C
ANISOU  157  CD  GLN A  17     4650   4192   4793   -205    258   -595       C
ATOM    158  OE1 GLN A  17      -9.922 -22.885 -10.699  1.00 35.03           O
ANISOU  158  OE1 GLN A  17     4545   4066   4701   -230    278   -607       O
ATOM    159  NE2 GLN A  17      -9.935 -20.644 -10.653  1.00 29.76           N
ANISOU  159  NE2 GLN A  17     3844   3432   4030   -196    252   -581       N
ATOM    160  N   GLY A  18      -8.779 -21.056 -15.850  1.00 26.68           N
ANISOU  160  N   GLY A  18     3602   3037   3499   -149    192   -606       N
ATOM    161  CA  GLY A  18      -9.014 -19.867 -16.638  1.00 31.16           C
ANISOU  161  CA  GLY A  18     4180   3619   4040   -133    155   -600       C
ATOM    162  C   GLY A  18      -8.475 -19.993 -18.049  1.00 32.98           C
ANISOU  162  C   GLY A  18     4469   3843   4220   -126    150   -604       C
ATOM    163  O   GLY A  18      -8.205 -21.087 -18.562  1.00 29.42           O
ANISOU  163  O   GLY A  18     4046   3377   3754   -135    167   -620       O
ATOM    164  N   SER A  19      -8.306 -18.834 -18.682  1.00 27.67           N
ANISOU  164  N   SER A  19     3818   3179   3515   -110    128   -588       N
ATOM    165  CA  SER A  19      -7.834 -18.759 -20.059  1.00 30.19           C
ANISOU  165  CA  SER A  19     4199   3491   3778   -106    122   -590       C
ATOM    166  C   SER A  19      -7.137 -17.424 -20.288  1.00 34.94           C
ANISOU  166  C   SER A  19     4823   4101   4351    -90    124   -560       C
ATOM    167  O   SER A  19      -7.704 -16.365 -19.988  1.00 32.29           O
ANISOU  167  O   SER A  19     4468   3775   4026    -80     89   -549       O
ATOM    168  CB  SER A  19      -9.002 -18.924 -21.041  1.00 34.11           C
ANISOU  168  CB  SER A  19     4716   3987   4257   -113     62   -620       C
ATOM    169  OG  SER A  19      -8.597 -18.655 -22.370  1.00 40.44           O
ANISOU  169  OG  SER A  19     5586   4782   4999   -110     51   -619       O
ATOM    170  N   LEU A  20      -5.909 -17.481 -20.819  1.00 32.80           N
ANISOU  170  N   LEU A  20     4593   3823   4045    -88    168   -547       N
ATOM    171  CA  LEU A  20      -5.204 -16.260 -21.204  1.00 33.52           C
ANISOU  171  CA  LEU A  20     4715   3920   4101    -80    174   -521       C
ATOM    172  C   LEU A  20      -5.987 -15.474 -22.248  1.00 37.55           C
ANISOU  172  C   LEU A  20     5269   4429   4570    -77    113   -525       C
ATOM    173  O   LEU A  20      -5.946 -14.235 -22.257  1.00 32.69           O
ANISOU  173  O   LEU A  20     4665   3818   3940    -68     94   -503       O
ATOM    174  CB  LEU A  20      -3.813 -16.602 -21.737  1.00 35.28           C
ANISOU  174  CB  LEU A  20     4975   4137   4293    -83    234   -515       C
ATOM    175  CG  LEU A  20      -2.841 -17.205 -20.727  1.00 27.75           C
ANISOU  175  CG  LEU A  20     3980   3184   3380    -79    291   -506       C
ATOM    176  CD1 LEU A  20      -1.508 -17.455 -21.360  1.00 27.01           C
ANISOU  176  CD1 LEU A  20     3919   3086   3258    -80    347   -505       C
ATOM    177  CD2 LEU A  20      -2.688 -16.284 -19.524  1.00 26.74           C
ANISOU  177  CD2 LEU A  20     3806   3068   3286    -72    292   -477       C
ATOM    178  N   ASP A  21      -6.705 -16.179 -23.126  1.00 37.94           N
ANISOU  178  N   ASP A  21     5347   4470   4599    -85     80   -554       N
ATOM    179  CA  ASP A  21      -7.548 -15.529 -24.122  1.00 46.13           C
ANISOU  179  CA  ASP A  21     6427   5503   5598    -83     13   -561       C
ATOM    180  C   ASP A  21      -8.669 -14.720 -23.480  1.00 50.38           C
ANISOU  180  C   ASP A  21     6916   6050   6175    -68    -46   -560       C
ATOM    181  O   ASP A  21      -9.099 -13.705 -24.041  1.00 55.57           O
ANISOU  181  O   ASP A  21     7604   6705   6805    -57    -98   -552       O
ATOM    182  CB  ASP A  21      -8.132 -16.584 -25.066  1.00 53.32           C
ANISOU  182  CB  ASP A  21     7370   6402   6486    -96    -12   -596       C
ATOM    183  CG  ASP A  21      -7.063 -17.438 -25.719  1.00 57.98           C
ANISOU  183  CG  ASP A  21     8008   6981   7039   -109     48   -602       C
ATOM    184  OD1 ASP A  21      -6.110 -16.861 -26.283  1.00 60.34           O
ANISOU  184  OD1 ASP A  21     8358   7277   7293   -109     79   -584       O
ATOM    185  OD2 ASP A  21      -7.165 -18.684 -25.660  1.00 60.98           O
ANISOU  185  OD2 ASP A  21     8378   7355   7437   -119     67   -626       O
ATOM    186  N   SER A  22      -9.157 -15.149 -22.311  1.00 45.88           N
ANISOU  186  N   SER A  22     6273   5490   5668    -69    -37   -568       N
ATOM    187  CA  SER A  22     -10.234 -14.422 -21.642  1.00 42.88           C
ANISOU  187  CA  SER A  22     5841   5121   5331    -56    -86   -572       C
ATOM    188  C   SER A  22      -9.749 -13.105 -21.058  1.00 42.58           C
ANISOU  188  C   SER A  22     5796   5086   5294    -40    -77   -538       C
ATOM    189  O   SER A  22     -10.538 -12.164 -20.906  1.00 48.38           O
ANISOU  189  O   SER A  22     6514   5825   6045    -23   -127   -538       O
ATOM    190  CB  SER A  22     -10.839 -15.281 -20.533  1.00 41.62           C
ANISOU  190  CB  SER A  22     5610   4969   5235    -67    -70   -592       C
ATOM    191  OG  SER A  22     -11.246 -16.531 -21.042  1.00 48.66           O
ANISOU  191  OG  SER A  22     6509   5854   6124    -86    -75   -623       O
ATOM    192  N   LEU A  23      -8.469 -13.022 -20.722  1.00 37.45           N
ANISOU  192  N   LEU A  23     5160   4437   4633    -44    -15   -512       N
ATOM    193  CA  LEU A  23      -7.943 -11.847 -20.055  1.00 36.36           C
ANISOU  193  CA  LEU A  23     5013   4303   4500    -32     -2   -480       C
ATOM    194  C   LEU A  23      -7.978 -10.624 -20.977  1.00 36.06           C
ANISOU  194  C   LEU A  23     5033   4256   4412    -21    -44   -465       C
ATOM    195  O   LEU A  23      -7.826 -10.746 -22.196  1.00 37.01           O
ANISOU  195  O   LEU A  23     5217   4366   4479    -27    -59   -470       O
ATOM    196  CB  LEU A  23      -6.512 -12.112 -19.600  1.00 33.43           C
ANISOU  196  CB  LEU A  23     4645   3933   4125    -42     72   -459       C
ATOM    197  CG  LEU A  23      -6.327 -13.291 -18.644  1.00 27.28           C
ANISOU  197  CG  LEU A  23     3817   3157   3392    -51    114   -469       C
ATOM    198  CD1 LEU A  23      -4.866 -13.407 -18.263  1.00 26.95           C
ANISOU  198  CD1 LEU A  23     3779   3116   3346    -55    177   -446       C
ATOM    199  CD2 LEU A  23      -7.201 -13.134 -17.390  1.00 29.62           C
ANISOU  199  CD2 LEU A  23     4049   3462   3745    -48     98   -473       C
ATOM    200  N   PRO A  24      -8.171  -9.430 -20.418  1.00 33.07           N
ANISOU  200  N   PRO A  24     4640   3879   4047     -5    -65   -447       N
ATOM    201  CA  PRO A  24      -7.968  -8.212 -21.212  1.00 31.85           C
ANISOU  201  CA  PRO A  24     4549   3711   3840      4    -96   -426       C
ATOM    202  C   PRO A  24      -6.526  -8.142 -21.681  1.00 34.40           C
ANISOU  202  C   PRO A  24     4926   4031   4115    -14    -37   -403       C
ATOM    203  O   PRO A  24      -5.611  -8.540 -20.958  1.00 38.08           O
ANISOU  203  O   PRO A  24     5363   4506   4601    -24     26   -393       O
ATOM    204  CB  PRO A  24      -8.292  -7.083 -20.228  1.00 35.66           C
ANISOU  204  CB  PRO A  24     4995   4196   4358     23   -113   -410       C
ATOM    205  CG  PRO A  24      -9.043  -7.731 -19.106  1.00 36.74           C
ANISOU  205  CG  PRO A  24     5047   4347   4564     25   -108   -432       C
ATOM    206  CD  PRO A  24      -8.538  -9.134 -19.025  1.00 33.08           C
ANISOU  206  CD  PRO A  24     4571   3890   4107      3    -57   -444       C
ATOM    207  N   GLN A  25      -6.334  -7.637 -22.905  1.00 33.86           N
ANISOU  207  N   GLN A  25     4938   3946   3980    -18    -60   -396       N
ATOM    208  CA  GLN A  25      -5.023  -7.613 -23.551  1.00 42.76           C
ANISOU  208  CA  GLN A  25     6123   5070   5055    -40     -3   -380       C
ATOM    209  C   GLN A  25      -3.887  -7.279 -22.588  1.00 36.97           C
ANISOU  209  C   GLN A  25     5356   4347   4343    -47     63   -356       C
ATOM    210  O   GLN A  25      -2.934  -8.051 -22.440  1.00 40.21           O
ANISOU  210  O   GLN A  25     5752   4765   4760    -61    127   -358       O
ATOM    211  CB  GLN A  25      -5.030  -6.604 -24.708  1.00 55.38           C
ANISOU  211  CB  GLN A  25     7814   6648   6582    -43    -41   -367       C
ATOM    212  CG  GLN A  25      -3.660  -6.411 -25.372  1.00 64.90           C
ANISOU  212  CG  GLN A  25     9082   7848   7728    -70     23   -350       C
ATOM    213  CD  GLN A  25      -3.560  -5.135 -26.207  1.00 72.03           C
ANISOU  213  CD  GLN A  25    10075   8730   8565    -76     -8   -328       C
ATOM    214  OE1 GLN A  25      -3.952  -4.049 -25.766  1.00 71.74           O
ANISOU  214  OE1 GLN A  25    10035   8685   8538    -60    -49   -309       O
ATOM    215  NE2 GLN A  25      -3.028  -5.264 -27.419  1.00 72.89           N
ANISOU  215  NE2 GLN A  25    10267   8825   8602   -100     11   -330       N
ATOM    216  N   GLU A  26      -3.983  -6.125 -21.920  1.00 33.95           N
ANISOU  216  N   GLU A  26     4961   3963   3975    -36     45   -333       N
ATOM    217  CA  GLU A  26      -2.902  -5.678 -21.046  1.00 28.06           C
ANISOU  217  CA  GLU A  26     4190   3226   3246    -45    102   -308       C
ATOM    218  C   GLU A  26      -2.709  -6.608 -19.855  1.00 27.19           C
ANISOU  218  C   GLU A  26     4000   3132   3199    -44    140   -316       C
ATOM    219  O   GLU A  26      -1.592  -6.728 -19.335  1.00 25.63           O
ANISOU  219  O   GLU A  26     3783   2943   3011    -56    197   -303       O
ATOM    220  CB  GLU A  26      -3.175  -4.250 -20.562  1.00 31.28           C
ANISOU  220  CB  GLU A  26     4604   3626   3655    -33     68   -285       C
ATOM    221  CG  GLU A  26      -3.107  -3.204 -21.666  1.00 45.51           C
ANISOU  221  CG  GLU A  26     6495   5407   5389    -38     38   -270       C
ATOM    222  CD  GLU A  26      -1.797  -3.245 -22.440  1.00 49.31           C
ANISOU  222  CD  GLU A  26     7032   5887   5816    -70     98   -259       C
ATOM    223  OE1 GLU A  26      -1.845  -3.440 -23.674  1.00 51.94           O
ANISOU  223  OE1 GLU A  26     7434   6209   6094    -80     86   -268       O
ATOM    224  OE2 GLU A  26      -0.722  -3.091 -21.817  1.00 50.17           O
ANISOU  224  OE2 GLU A  26     7116   6007   5938    -85    157   -243       O
ATOM    225  N   VAL A  27      -3.779  -7.242 -19.383  1.00 29.27           N
ANISOU  225  N   VAL A  27     4217   3400   3505    -31    108   -338       N
ATOM    226  CA  VAL A  27      -3.627  -8.224 -18.319  1.00 29.58           C
ANISOU  226  CA  VAL A  27     4191   3450   3598    -34    144   -347       C
ATOM    227  C   VAL A  27      -2.854  -9.428 -18.839  1.00 26.28           C
ANISOU  227  C   VAL A  27     3784   3033   3167    -47    190   -359       C
ATOM    228  O   VAL A  27      -1.898  -9.892 -18.206  1.00 26.44           O
ANISOU  228  O   VAL A  27     3778   3059   3209    -54    242   -352       O
ATOM    229  CB  VAL A  27      -5.001  -8.626 -17.752  1.00 31.63           C
ANISOU  229  CB  VAL A  27     4402   3712   3903    -22    102   -370       C
ATOM    230  CG1 VAL A  27      -4.838  -9.652 -16.637  1.00 27.06           C
ANISOU  230  CG1 VAL A  27     3765   3142   3375    -30    141   -377       C
ATOM    231  CG2 VAL A  27      -5.742  -7.394 -17.240  1.00 27.14           C
ANISOU  231  CG2 VAL A  27     3820   3143   3351     -6     60   -360       C
ATOM    232  N   ARG A  28      -3.221  -9.913 -20.029  1.00 24.52           N
ANISOU  232  N   ARG A  28     3606   2803   2908    -51    170   -379       N
ATOM    233  CA  ARG A  28      -2.483 -11.029 -20.616  1.00 24.13           C
ANISOU  233  CA  ARG A  28     3574   2752   2843    -63    215   -394       C
ATOM    234  C   ARG A  28      -0.996 -10.711 -20.738  1.00 27.26           C
ANISOU  234  C   ARG A  28     3990   3151   3218    -74    276   -375       C
ATOM    235  O   ARG A  28      -0.152 -11.539 -20.381  1.00 26.93           O
ANISOU  235  O   ARG A  28     3921   3113   3199    -77    327   -380       O
ATOM    236  CB  ARG A  28      -3.062 -11.410 -21.979  1.00 24.73           C
ANISOU  236  CB  ARG A  28     3708   2816   2872    -67    183   -417       C
ATOM    237  CG  ARG A  28      -2.179 -12.441 -22.684  1.00 30.17           C
ANISOU  237  CG  ARG A  28     4425   3502   3538    -80    236   -432       C
ATOM    238  CD  ARG A  28      -2.837 -13.173 -23.833  1.00 35.00           C
ANISOU  238  CD  ARG A  28     5083   4101   4113    -86    208   -461       C
ATOM    239  NE  ARG A  28      -2.033 -14.352 -24.170  1.00 30.89           N
ANISOU  239  NE  ARG A  28     4570   3577   3588    -95    265   -479       N
ATOM    240  CZ  ARG A  28      -2.479 -15.411 -24.837  1.00 29.98           C
ANISOU  240  CZ  ARG A  28     4478   3452   3461   -101    255   -509       C
ATOM    241  NH1 ARG A  28      -3.732 -15.453 -25.269  1.00 33.39           N
ANISOU  241  NH1 ARG A  28     4925   3878   3883   -100    189   -524       N
ATOM    242  NH2 ARG A  28      -1.666 -16.434 -25.067  1.00 34.60           N
ANISOU  242  NH2 ARG A  28     5070   4032   4046   -106    311   -525       N
ATOM    243  N   LYS A  29      -0.648  -9.502 -21.197  1.00 25.83           N
ANISOU  243  N   LYS A  29     3852   2967   2996    -80    272   -354       N
ATOM    244  CA  LYS A  29       0.765  -9.188 -21.392  1.00 24.50           C
ANISOU  244  CA  LYS A  29     3702   2803   2805    -95    332   -339       C
ATOM    245  C   LYS A  29       1.512  -9.127 -20.068  1.00 20.06           C
ANISOU  245  C   LYS A  29     3074   2252   2294    -93    368   -323       C
ATOM    246  O   LYS A  29       2.690  -9.496 -19.993  1.00 26.93           O
ANISOU  246  O   LYS A  29     3930   3129   3172   -101    425   -322       O
ATOM    247  CB  LYS A  29       0.913  -7.863 -22.144  1.00 27.76           C
ANISOU  247  CB  LYS A  29     4180   3207   3160   -107    318   -320       C
ATOM    248  CG  LYS A  29       0.363  -7.901 -23.572  1.00 37.97           C
ANISOU  248  CG  LYS A  29     5551   4485   4390   -114    286   -334       C
ATOM    249  CD  LYS A  29      -0.013  -6.502 -24.083  1.00 40.47           C
ANISOU  249  CD  LYS A  29     5931   4787   4659   -116    240   -313       C
ATOM    250  CE  LYS A  29       1.167  -5.775 -24.709  1.00 52.84           C
ANISOU  250  CE  LYS A  29     7556   6350   6172   -144    289   -296       C
ATOM    251  NZ  LYS A  29       2.207  -5.388 -23.714  1.00 58.47           N
ANISOU  251  NZ  LYS A  29     8218   7078   6921   -152    343   -277       N
ATOM    252  N   PHE A  30       0.862  -8.601 -19.030  1.00 24.01           N
ANISOU  252  N   PHE A  30     3536   2756   2831    -81    334   -310       N
ATOM    253  CA  PHE A  30       1.454  -8.580 -17.696  1.00 24.34           C
ANISOU  253  CA  PHE A  30     3519   2806   2922    -79    361   -294       C
ATOM    254  C   PHE A  30       1.678  -9.996 -17.185  1.00 24.79           C
ANISOU  254  C   PHE A  30     3533   2866   3021    -74    387   -312       C
ATOM    255  O   PHE A  30       2.760 -10.325 -16.683  1.00 22.77           O
ANISOU  255  O   PHE A  30     3250   2616   2787    -77    431   -306       O
ATOM    256  CB  PHE A  30       0.538  -7.779 -16.749  1.00 25.06           C
ANISOU  256  CB  PHE A  30     3585   2897   3040    -68    317   -282       C
ATOM    257  CG  PHE A  30       0.981  -7.768 -15.307  1.00 22.29           C
ANISOU  257  CG  PHE A  30     3179   2553   2737    -67    337   -267       C
ATOM    258  CD1 PHE A  30       2.262  -7.369 -14.959  1.00 19.98           C
ANISOU  258  CD1 PHE A  30     2879   2267   2446    -79    378   -247       C
ATOM    259  CD2 PHE A  30       0.100  -8.140 -14.295  1.00 22.22           C
ANISOU  259  CD2 PHE A  30     3127   2544   2772    -58    315   -275       C
ATOM    260  CE1 PHE A  30       2.662  -7.353 -13.639  1.00 26.34           C
ANISOU  260  CE1 PHE A  30     3638   3077   3293    -78    391   -233       C
ATOM    261  CE2 PHE A  30       0.488  -8.113 -12.971  1.00 22.38           C
ANISOU  261  CE2 PHE A  30     3105   2568   2831    -60    332   -260       C
ATOM    262  CZ  PHE A  30       1.769  -7.726 -12.636  1.00 21.66           C
ANISOU  262  CZ  PHE A  30     3009   2482   2739    -69    367   -239       C
ATOM    263  N   VAL A  31       0.666 -10.855 -17.318  1.00 22.75           N
ANISOU  263  N   VAL A  31     3269   2602   2773    -67    359   -335       N
ATOM    264  CA  VAL A  31       0.801 -12.242 -16.862  1.00 24.42           C
ANISOU  264  CA  VAL A  31     3447   2811   3021    -63    381   -353       C
ATOM    265  C   VAL A  31       1.876 -12.960 -17.665  1.00 21.96           C
ANISOU  265  C   VAL A  31     3156   2497   2690    -68    429   -364       C
ATOM    266  O   VAL A  31       2.798 -13.572 -17.105  1.00 28.10           O
ANISOU  266  O   VAL A  31     3903   3275   3498    -64    468   -363       O
ATOM    267  CB  VAL A  31      -0.550 -12.977 -16.957  1.00 21.72           C
ANISOU  267  CB  VAL A  31     3100   2462   2690    -60    341   -377       C
ATOM    268  CG1 VAL A  31      -0.360 -14.495 -16.745  1.00 23.34           C
ANISOU  268  CG1 VAL A  31     3288   2659   2922    -60    367   -398       C
ATOM    269  CG2 VAL A  31      -1.542 -12.423 -15.944  1.00 22.21           C
ANISOU  269  CG2 VAL A  31     3127   2527   2784    -55    304   -370       C
ATOM    270  N   GLU A  32       1.793 -12.879 -18.993  1.00 23.66           N
ANISOU  270  N   GLU A  32     3427   2708   2855    -75    427   -377       N
ATOM    271  CA  GLU A  32       2.681 -13.693 -19.820  1.00 30.12           C
ANISOU  271  CA  GLU A  32     4267   3523   3654    -79    475   -395       C
ATOM    272  C   GLU A  32       4.123 -13.220 -19.732  1.00 30.86           C
ANISOU  272  C   GLU A  32     4352   3626   3748    -86    529   -381       C
ATOM    273  O   GLU A  32       5.050 -14.037 -19.728  1.00 27.73           O
ANISOU  273  O   GLU A  32     3936   3230   3370    -82    576   -394       O
ATOM    274  CB  GLU A  32       2.213 -13.691 -21.272  1.00 37.68           C
ANISOU  274  CB  GLU A  32     5293   4472   4553    -89    460   -413       C
ATOM    275  CG  GLU A  32       1.063 -14.627 -21.556  1.00 43.08           C
ANISOU  275  CG  GLU A  32     5984   5146   5240    -84    421   -439       C
ATOM    276  CD  GLU A  32       0.985 -14.994 -23.025  1.00 39.71           C
ANISOU  276  CD  GLU A  32     5624   4708   4755    -95    423   -461       C
ATOM    277  OE1 GLU A  32       0.979 -16.208 -23.339  1.00 37.28           O
ANISOU  277  OE1 GLU A  32     5321   4392   4453    -94    440   -488       O
ATOM    278  OE2 GLU A  32       0.945 -14.062 -23.860  1.00 32.86           O
ANISOU  278  OE2 GLU A  32     4812   3840   3836   -105    409   -452       O
ATOM    279  N   GLY A  33       4.341 -11.906 -19.675  1.00 26.43           N
ANISOU  279  N   GLY A  33     3804   3073   3167    -96    524   -356       N
ATOM    280  CA  GLY A  33       5.704 -11.417 -19.622  1.00 24.47           C
ANISOU  280  CA  GLY A  33     3546   2835   2918   -107    576   -344       C
ATOM    281  C   GLY A  33       6.393 -11.787 -18.327  1.00 22.39           C
ANISOU  281  C   GLY A  33     3213   2578   2717    -95    595   -335       C
ATOM    282  O   GLY A  33       7.594 -12.069 -18.308  1.00 24.50           O
ANISOU  282  O   GLY A  33     3457   2852   2999    -97    644   -339       O
ATOM    283  N   ASN A  34       5.651 -11.777 -17.221  1.00 17.96           N
ANISOU  283  N   ASN A  34     2618   2015   2192    -84    556   -323       N
ATOM    284  CA  ASN A  34       6.250 -12.190 -15.965  1.00 19.88           C
ANISOU  284  CA  ASN A  34     2803   2261   2490    -75    568   -314       C
ATOM    285  C   ASN A  34       6.320 -13.705 -15.831  1.00 20.51           C
ANISOU  285  C   ASN A  34     2862   2330   2601    -59    581   -338       C
ATOM    286  O   ASN A  34       7.194 -14.209 -15.119  1.00 23.94           O
ANISOU  286  O   ASN A  34     3257   2764   3075    -50    604   -336       O
ATOM    287  CB  ASN A  34       5.483 -11.577 -14.799  1.00 21.86           C
ANISOU  287  CB  ASN A  34     3031   2511   2764    -72    527   -293       C
ATOM    288  CG  ASN A  34       5.876 -10.143 -14.571  1.00 25.20           C
ANISOU  288  CG  ASN A  34     3459   2943   3172    -85    526   -266       C
ATOM    289  OD1 ASN A  34       7.018  -9.866 -14.199  1.00 26.31           O
ANISOU  289  OD1 ASN A  34     3577   3092   3327    -91    557   -254       O
ATOM    290  ND2 ASN A  34       4.950  -9.219 -14.807  1.00 28.35           N
ANISOU  290  ND2 ASN A  34     3889   3340   3543    -88    489   -258       N
ATOM    291  N   ALA A  35       5.454 -14.442 -16.526  1.00 25.97           N
ANISOU  291  N   ALA A  35     3582   3011   3274    -57    565   -361       N
ATOM    292  CA  ALA A  35       5.641 -15.892 -16.597  1.00 20.49           C
ANISOU  292  CA  ALA A  35     2879   2304   2603    -44    583   -386       C
ATOM    293  C   ALA A  35       6.899 -16.246 -17.382  1.00 24.90           C
ANISOU  293  C   ALA A  35     3444   2865   3153    -42    638   -401       C
ATOM    294  O   ALA A  35       7.636 -17.163 -17.002  1.00 26.86           O
ANISOU  294  O   ALA A  35     3662   3107   3438    -27    663   -412       O
ATOM    295  CB  ALA A  35       4.415 -16.558 -17.223  1.00 21.99           C
ANISOU  295  CB  ALA A  35     3101   2481   2772    -46    553   -408       C
ATOM    296  N   GLN A  36       7.169 -15.533 -18.480  1.00 27.34           N
ANISOU  296  N   GLN A  36     3793   3182   3412    -58    657   -404       N
ATOM    297  CA  GLN A  36       8.418 -15.754 -19.202  1.00 26.94           C
ANISOU  297  CA  GLN A  36     3746   3137   3354    -60    718   -420       C
ATOM    298  C   GLN A  36       9.617 -15.495 -18.301  1.00 27.38           C
ANISOU  298  C   GLN A  36     3744   3204   3456    -54    745   -406       C
ATOM    299  O   GLN A  36      10.605 -16.230 -18.338  1.00 26.03           O
ANISOU  299  O   GLN A  36     3545   3033   3313    -42    787   -424       O
ATOM    300  CB  GLN A  36       8.465 -14.860 -20.445  1.00 30.97           C
ANISOU  300  CB  GLN A  36     4315   3654   3799    -85    733   -421       C
ATOM    301  CG  GLN A  36       7.371 -15.186 -21.454  1.00 38.26           C
ANISOU  301  CG  GLN A  36     5300   4564   4674    -91    704   -438       C
ATOM    302  CD  GLN A  36       7.069 -14.042 -22.413  1.00 47.95           C
ANISOU  302  CD  GLN A  36     6591   5792   5834   -115    693   -428       C
ATOM    303  OE1 GLN A  36       7.797 -13.044 -22.474  1.00 48.42           O
ANISOU  303  OE1 GLN A  36     6656   5864   5878   -131    718   -411       O
ATOM    304  NE2 GLN A  36       5.982 -14.183 -23.169  1.00 42.94           N
ANISOU  304  NE2 GLN A  36     6009   5146   5159   -118    652   -439       N
ATOM    305  N   LEU A  37       9.525 -14.482 -17.445  1.00 26.41           N
ANISOU  305  N   LEU A  37     3601   3091   3343    -62    720   -375       N
ATOM    306  CA  LEU A  37      10.651 -14.131 -16.589  1.00 22.66           C
ANISOU  306  CA  LEU A  37     3074   2628   2909    -60    742   -360       C
ATOM    307  C   LEU A  37      10.778 -15.082 -15.403  1.00 22.66           C
ANISOU  307  C   LEU A  37     3024   2617   2969    -34    726   -359       C
ATOM    308  O   LEU A  37      11.876 -15.553 -15.091  1.00 25.32           O
ANISOU  308  O   LEU A  37     3319   2956   3345    -21    754   -367       O
ATOM    309  CB  LEU A  37      10.493 -12.692 -16.092  1.00 25.65           C
ANISOU  309  CB  LEU A  37     3454   3017   3273    -78    719   -327       C
ATOM    310  CG  LEU A  37      11.448 -12.273 -14.977  1.00 25.34           C
ANISOU  310  CG  LEU A  37     3361   2989   3279    -78    726   -307       C
ATOM    311  CD1 LEU A  37      12.827 -11.925 -15.524  1.00 31.88           C
ANISOU  311  CD1 LEU A  37     4173   3834   4106    -92    782   -315       C
ATOM    312  CD2 LEU A  37      10.855 -11.129 -14.195  1.00 27.25           C
ANISOU  312  CD2 LEU A  37     3607   3234   3514    -89    686   -275       C
ATOM    313  N   CYS A  38       9.671 -15.335 -14.699  1.00 24.17           N
ANISOU  313  N   CYS A  38     3219   2796   3169    -29    679   -350       N
ATOM    314  CA  CYS A  38       9.732 -16.102 -13.462  1.00 21.36           C
ANISOU  314  CA  CYS A  38     2825   2427   2865    -10    660   -344       C
ATOM    315  C   CYS A  38       9.712 -17.606 -13.690  1.00 20.09           C
ANISOU  315  C   CYS A  38     2666   2246   2722     10    668   -372       C
ATOM    316  O   CYS A  38      10.077 -18.353 -12.775  1.00 25.77           O
ANISOU  316  O   CYS A  38     3356   2951   3485     27    661   -370       O
ATOM    317  CB  CYS A  38       8.577 -15.721 -12.551  1.00 17.11           C
ANISOU  317  CB  CYS A  38     2290   1884   2328    -17    612   -323       C
ATOM    318  SG  CYS A  38       8.588 -13.949 -12.146  1.00 27.11           S
ANISOU  318  SG  CYS A  38     3554   3169   3576    -38    599   -290       S
ATOM    319  N   GLN A  39       9.262 -18.048 -14.868  1.00 24.78           N
ANISOU  319  N   GLN A  39     3299   2835   3281      7    681   -397       N
ATOM    320  C   GLN A  39       8.348 -20.310 -14.353  1.00 27.47           C
ANISOU  320  C   GLN A  39     3648   3131   3657     31    654   -424       C
ATOM    321  O   GLN A  39       8.790 -21.380 -13.906  1.00 25.04           O
ANISOU  321  O   GLN A  39     3325   2804   3386     51    659   -435       O
ATOM    322  CA AGLN A  39       9.219 -19.453 -15.271  0.62 25.02           C
ANISOU  322  CA AGLN A  39     3341   2844   3322     24    692   -427       C
ATOM    323  CB AGLN A  39      10.633 -20.036 -15.322  0.62 27.76           C
ANISOU  323  CB AGLN A  39     3655   3189   3703     45    735   -442       C
ATOM    324  CG AGLN A  39      11.520 -19.481 -16.420  0.62 31.17           C
ANISOU  324  CG AGLN A  39     4094   3640   4109     35    786   -456       C
ATOM    325  CD AGLN A  39      12.887 -20.143 -16.430  0.62 34.77           C
ANISOU  325  CD AGLN A  39     4509   4094   4608     59    830   -477       C
ATOM    326  OE1AGLN A  39      13.728 -19.869 -15.572  0.62 35.36           O
ANISOU  326  OE1AGLN A  39     4532   4176   4725     68    830   -462       O
ATOM    327  NE2AGLN A  39      13.106 -21.035 -17.390  0.62 37.37           N
ANISOU  327  NE2AGLN A  39     4860   4412   4928     69    865   -513       N
ATOM    328  CA BGLN A  39       9.222 -19.452 -15.269  0.38 25.55           C
ANISOU  328  CA BGLN A  39     3408   2911   3389     24    692   -427       C
ATOM    329  CB BGLN A  39      10.643 -20.021 -15.315  0.38 27.78           C
ANISOU  329  CB BGLN A  39     3658   3192   3706     45    735   -442       C
ATOM    330  CG BGLN A  39      11.595 -19.262 -16.228  0.38 30.60           C
ANISOU  330  CG BGLN A  39     4014   3571   4041     33    783   -449       C
ATOM    331  CD BGLN A  39      11.505 -19.710 -17.672  0.38 35.20           C
ANISOU  331  CD BGLN A  39     4642   4149   4581     28    817   -482       C
ATOM    332  OE1BGLN A  39      10.581 -20.429 -18.055  0.38 37.07           O
ANISOU  332  OE1BGLN A  39     4917   4370   4800     29    798   -497       O
ATOM    333  NE2BGLN A  39      12.477 -19.298 -18.481  0.38 37.27           N
ANISOU  333  NE2BGLN A  39     4905   4428   4829     19    870   -496       N
ATOM    334  N   PRO A  40       7.103 -19.917 -14.067  1.00 23.57           N
ANISOU  334  N   PRO A  40     3170   2638   3147     15    615   -413       N
ATOM    335  CA  PRO A  40       6.246 -20.802 -13.265  1.00 24.88           C
ANISOU  335  CA  PRO A  40     3335   2782   3335     16    585   -416       C
ATOM    336  C   PRO A  40       5.975 -22.087 -14.032  1.00 25.39           C
ANISOU  336  C   PRO A  40     3429   2826   3393     23    595   -448       C
ATOM    337  O   PRO A  40       6.039 -22.120 -15.263  1.00 24.11           O
ANISOU  337  O   PRO A  40     3295   2668   3197     20    614   -469       O
ATOM    338  CB  PRO A  40       4.963 -19.982 -13.075  1.00 23.02           C
ANISOU  338  CB  PRO A  40     3110   2558   3080     -5    549   -404       C
ATOM    339  CG  PRO A  40       4.906 -19.157 -14.315  1.00 23.89           C
ANISOU  339  CG  PRO A  40     3247   2686   3145    -13    557   -409       C
ATOM    340  CD  PRO A  40       6.344 -18.752 -14.560  1.00 26.32           C
ANISOU  340  CD  PRO A  40     3540   3004   3455     -5    597   -403       C
ATOM    341  N   GLU A  41       5.691 -23.161 -13.284  1.00 24.79           N
ANISOU  341  N   GLU A  41     3350   2723   3345     29    581   -454       N
ATOM    342  CA  GLU A  41       5.301 -24.422 -13.905  1.00 25.96           C
ANISOU  342  CA  GLU A  41     3530   2848   3488     32    586   -484       C
ATOM    343  C   GLU A  41       3.844 -24.391 -14.361  1.00 28.38           C
ANISOU  343  C   GLU A  41     3864   3155   3763      7    557   -496       C
ATOM    344  O   GLU A  41       3.498 -25.008 -15.377  1.00 26.77           O
ANISOU  344  O   GLU A  41     3693   2942   3535      4    563   -523       O
ATOM    345  CB  GLU A  41       5.535 -25.575 -12.922  1.00 29.32           C
ANISOU  345  CB  GLU A  41     3948   3240   3953     46    580   -485       C
ATOM    346  CG  GLU A  41       5.315 -26.977 -13.497  1.00 32.94           C
ANISOU  346  CG  GLU A  41     4440   3667   4409     53    587   -517       C
ATOM    347  CD  GLU A  41       6.441 -27.412 -14.410  1.00 50.29           C
ANISOU  347  CD  GLU A  41     6642   5860   6608     79    627   -539       C
ATOM    348  OE1 GLU A  41       6.292 -28.448 -15.092  1.00 56.60           O
ANISOU  348  OE1 GLU A  41     7473   6636   7398     84    638   -569       O
ATOM    349  OE2 GLU A  41       7.481 -26.720 -14.446  1.00 55.29           O
ANISOU  349  OE2 GLU A  41     7245   6513   7250     93    650   -529       O
ATOM    350  N   TYR A  42       2.990 -23.669 -13.635  1.00 23.88           N
ANISOU  350  N   TYR A  42     3280   2597   3196    -10    527   -477       N
ATOM    351  CA  TYR A  42       1.561 -23.590 -13.909  1.00 19.18           C
ANISOU  351  CA  TYR A  42     2699   2006   2582    -32    496   -488       C
ATOM    352  C   TYR A  42       1.123 -22.149 -13.745  1.00 22.57           C
ANISOU  352  C   TYR A  42     3114   2463   3000    -42    476   -468       C
ATOM    353  O   TYR A  42       1.736 -21.384 -13.006  1.00 24.22           O
ANISOU  353  O   TYR A  42     3298   2682   3224    -36    481   -442       O
ATOM    354  CB  TYR A  42       0.726 -24.433 -12.943  1.00 20.04           C
ANISOU  354  CB  TYR A  42     2804   2094   2717    -46    477   -493       C
ATOM    355  CG  TYR A  42       1.246 -25.838 -12.735  1.00 27.43           C
ANISOU  355  CG  TYR A  42     3754   2996   3672    -35    494   -506       C
ATOM    356  CD1 TYR A  42       0.888 -26.861 -13.592  1.00 41.69           C
ANISOU  356  CD1 TYR A  42     5592   4783   5463    -39    497   -537       C
ATOM    357  CD2 TYR A  42       2.092 -26.131 -11.675  1.00 30.90           C
ANISOU  357  CD2 TYR A  42     4176   3419   4144    -21    503   -487       C
ATOM    358  CE1 TYR A  42       1.354 -28.139 -13.401  1.00 37.85           C
ANISOU  358  CE1 TYR A  42     5123   4262   4995    -27    511   -549       C
ATOM    359  CE2 TYR A  42       2.567 -27.409 -11.476  1.00 36.07           C
ANISOU  359  CE2 TYR A  42     4849   4040   4818     -7    513   -499       C
ATOM    360  CZ  TYR A  42       2.192 -28.407 -12.342  1.00 35.20           C
ANISOU  360  CZ  TYR A  42     4771   3910   4693    -10    518   -530       C
ATOM    361  OH  TYR A  42       2.664 -29.687 -12.156  1.00 41.17           O
ANISOU  361  OH  TYR A  42     5548   4628   5468      5    528   -542       O
ATOM    362  N   ILE A  43       0.033 -21.797 -14.420  1.00 26.44           N
ANISOU  362  N   ILE A  43     3619   2963   3465    -56    449   -480       N
ATOM    363  CA  ILE A  43      -0.626 -20.514 -14.219  1.00 24.54           C
ANISOU  363  CA  ILE A  43     3364   2743   3217    -63    421   -465       C
ATOM    364  C   ILE A  43      -2.065 -20.781 -13.807  1.00 22.56           C
ANISOU  364  C   ILE A  43     3102   2489   2980    -80    388   -479       C
ATOM    365  O   ILE A  43      -2.794 -21.496 -14.501  1.00 22.88           O
ANISOU  365  O   ILE A  43     3162   2522   3009    -90    374   -506       O
ATOM    366  CB  ILE A  43      -0.571 -19.622 -15.471  1.00 23.70           C
ANISOU  366  CB  ILE A  43     3287   2653   3067    -61    415   -466       C
ATOM    367  CG1 ILE A  43       0.884 -19.353 -15.869  1.00 25.45           C
ANISOU  367  CG1 ILE A  43     3517   2877   3274    -49    455   -455       C
ATOM    368  CG2 ILE A  43      -1.321 -18.311 -15.185  1.00 17.47           C
ANISOU  368  CG2 ILE A  43     2484   1880   2273    -66    381   -450       C
ATOM    369  CD1 ILE A  43       1.044 -18.453 -17.105  1.00 28.10           C
ANISOU  369  CD1 ILE A  43     3890   3226   3562    -52    455   -454       C
ATOM    370  N   HIS A  44      -2.467 -20.208 -12.676  1.00 19.69           N
ANISOU  370  N   HIS A  44     2708   2133   2641    -87    377   -463       N
ATOM    371  CA  HIS A  44      -3.813 -20.351 -12.129  1.00 19.79           C
ANISOU  371  CA  HIS A  44     2702   2146   2673   -105    351   -477       C
ATOM    372  C   HIS A  44      -4.434 -18.957 -12.099  1.00 22.89           C
ANISOU  372  C   HIS A  44     3077   2560   3061   -103    324   -468       C
ATOM    373  O   HIS A  44      -4.014 -18.107 -11.310  1.00 23.57           O
ANISOU  373  O   HIS A  44     3146   2653   3157    -98    331   -442       O
ATOM    374  CB  HIS A  44      -3.756 -20.970 -10.733  1.00 21.05           C
ANISOU  374  CB  HIS A  44     2843   2290   2867   -117    367   -469       C
ATOM    375  CG  HIS A  44      -5.092 -21.155 -10.079  1.00 23.34           C
ANISOU  375  CG  HIS A  44     3111   2579   3177   -141    350   -486       C
ATOM    376  ND1 HIS A  44      -5.641 -22.398  -9.835  1.00 24.98           N
ANISOU  376  ND1 HIS A  44     3325   2766   3398   -162    354   -507       N
ATOM    377  CD2 HIS A  44      -5.967 -20.256  -9.575  1.00 20.48           C
ANISOU  377  CD2 HIS A  44     2721   2234   2828   -150    332   -485       C
ATOM    378  CE1 HIS A  44      -6.808 -22.252  -9.235  1.00 25.31           C
ANISOU  378  CE1 HIS A  44     3342   2815   3459   -186    342   -521       C
ATOM    379  NE2 HIS A  44      -7.026 -20.960  -9.059  1.00 19.96           N
ANISOU  379  NE2 HIS A  44     2641   2160   2783   -176    329   -509       N
ATOM    380  N   ILE A  45      -5.415 -18.710 -12.959  1.00 20.37           N
ANISOU  380  N   ILE A  45     2765   2250   2727   -106    291   -488       N
ATOM    381  CA  ILE A  45      -6.123 -17.433 -12.960  1.00 22.39           C
ANISOU  381  CA  ILE A  45     3005   2522   2981   -101    258   -483       C
ATOM    382  C   ILE A  45      -7.289 -17.552 -11.992  1.00 24.64           C
ANISOU  382  C   ILE A  45     3248   2809   3304   -117    245   -498       C
ATOM    383  O   ILE A  45      -8.198 -18.360 -12.207  1.00 24.76           O
ANISOU  383  O   ILE A  45     3257   2821   3330   -132    231   -528       O
ATOM    384  CB  ILE A  45      -6.614 -17.065 -14.366  1.00 24.08           C
ANISOU  384  CB  ILE A  45     3247   2742   3160    -94    222   -499       C
ATOM    385  CG1 ILE A  45      -5.425 -16.948 -15.328  1.00 25.68           C
ANISOU  385  CG1 ILE A  45     3495   2942   3322    -83    243   -485       C
ATOM    386  CG2 ILE A  45      -7.426 -15.776 -14.310  1.00 23.71           C
ANISOU  386  CG2 ILE A  45     3183   2708   3116    -85    182   -495       C
ATOM    387  CD1 ILE A  45      -5.843 -16.786 -16.779  1.00 29.45           C
ANISOU  387  CD1 ILE A  45     4013   3419   3757    -81    210   -501       C
ATOM    388  N   CYS A  46      -7.264 -16.760 -10.925  1.00 22.57           N
ANISOU  388  N   CYS A  46     2960   2553   3061   -115    252   -480       N
ATOM    389  CA  CYS A  46      -8.225 -16.959  -9.844  1.00 16.41           C
ANISOU  389  CA  CYS A  46     2143   1773   2318   -134    253   -494       C
ATOM    390  C   CYS A  46      -9.606 -16.462 -10.237  1.00 24.86           C
ANISOU  390  C   CYS A  46     3188   2858   3401   -134    213   -522       C
ATOM    391  O   CYS A  46      -9.746 -15.421 -10.886  1.00 26.10           O
ANISOU  391  O   CYS A  46     3350   3025   3543   -114    182   -517       O
ATOM    392  CB  CYS A  46      -7.776 -16.239  -8.582  1.00 17.89           C
ANISOU  392  CB  CYS A  46     2315   1962   2522   -134    274   -467       C
ATOM    393  SG  CYS A  46      -6.218 -16.762  -7.908  1.00 23.36           S
ANISOU  393  SG  CYS A  46     3028   2638   3209   -134    314   -436       S
ATOM    394  N   ASP A  47     -10.638 -17.187  -9.797  1.00 28.48           N
ANISOU  394  N   ASP A  47     3617   3314   3889   -158    212   -552       N
ATOM    395  CA  ASP A  47     -12.010 -16.772 -10.046  1.00 26.36           C
ANISOU  395  CA  ASP A  47     3313   3061   3642   -160    174   -583       C
ATOM    396  C   ASP A  47     -12.742 -16.285  -8.803  1.00 27.87           C
ANISOU  396  C   ASP A  47     3458   3260   3873   -171    186   -591       C
ATOM    397  O   ASP A  47     -13.851 -15.758  -8.935  1.00 32.41           O
ANISOU  397  O   ASP A  47     3995   3849   4471   -167    155   -618       O
ATOM    398  CB  ASP A  47     -12.805 -17.905 -10.721  1.00 24.46           C
ANISOU  398  CB  ASP A  47     3070   2817   3407   -180    158   -620       C
ATOM    399  CG  ASP A  47     -12.992 -19.140  -9.835  1.00 32.88           C
ANISOU  399  CG  ASP A  47     4127   3870   4495   -217    196   -634       C
ATOM    400  OD1 ASP A  47     -12.553 -19.165  -8.665  1.00 33.53           O
ANISOU  400  OD1 ASP A  47     4205   3944   4589   -227    233   -615       O
ATOM    401  OD2 ASP A  47     -13.603 -20.105 -10.333  1.00 36.26           O
ANISOU  401  OD2 ASP A  47     4556   4293   4927   -238    185   -663       O
ATOM    402  N   GLY A  48     -12.141 -16.398  -7.615  1.00 26.91           N
ANISOU  402  N   GLY A  48     3338   3129   3759   -184    228   -570       N
ATOM    403  CA  GLY A  48     -12.747 -15.902  -6.391  1.00 22.22           C
ANISOU  403  CA  GLY A  48     2707   2539   3196   -198    246   -576       C
ATOM    404  C   GLY A  48     -13.800 -16.806  -5.796  1.00 26.18           C
ANISOU  404  C   GLY A  48     3177   3040   3730   -236    262   -613       C
ATOM    405  O   GLY A  48     -14.407 -16.445  -4.772  1.00 26.51           O
ANISOU  405  O   GLY A  48     3187   3087   3800   -252    282   -624       O
ATOM    406  N   SER A  49     -14.021 -17.974  -6.386  1.00 24.08           N
ANISOU  406  N   SER A  49     2923   2767   3461   -254    259   -632       N
ATOM    407  CA  SER A  49     -15.121 -18.845  -6.001  1.00 28.21           C
ANISOU  407  CA  SER A  49     3415   3289   4013   -294    271   -672       C
ATOM    408  C   SER A  49     -14.840 -19.533  -4.670  1.00 28.45           C
ANISOU  408  C   SER A  49     3460   3300   4050   -331    322   -662       C
ATOM    409  O   SER A  49     -13.693 -19.673  -4.236  1.00 24.82           O
ANISOU  409  O   SER A  49     3040   2822   3567   -324    344   -625       O
ATOM    410  CB  SER A  49     -15.363 -19.901  -7.081  1.00 32.22           C
ANISOU  410  CB  SER A  49     3939   3791   4510   -304    250   -694       C
ATOM    411  OG  SER A  49     -14.275 -20.806  -7.162  1.00 36.02           O
ANISOU  411  OG  SER A  49     4474   4249   4963   -308    272   -670       O
ATOM    412  N   GLU A  50     -15.917 -19.978  -4.017  1.00 31.37           N
ANISOU  412  N   GLU A  50     3796   3673   4451   -371    342   -697       N
ATOM    413  C   GLU A  50     -15.095 -22.080  -3.033  1.00 30.51           C
ANISOU  413  C   GLU A  50     3760   3512   4319   -428    400   -680       C
ATOM    414  O   GLU A  50     -14.304 -22.554  -2.209  1.00 36.04           O
ANISOU  414  O   GLU A  50     4502   4187   5005   -440    429   -653       O
ATOM    415  CA AGLU A  50     -15.761 -20.733  -2.778  0.61 31.98           C
ANISOU  415  CA AGLU A  50     3894   3727   4529   -413    391   -691       C
ATOM    416  CB AGLU A  50     -17.119 -20.929  -2.099  0.61 32.58           C
ANISOU  416  CB AGLU A  50     3923   3812   4642   -457    414   -735       C
ATOM    417  CG AGLU A  50     -17.683 -19.679  -1.469  0.61 33.56           C
ANISOU  417  CG AGLU A  50     4001   3959   4793   -447    419   -744       C
ATOM    418  CD AGLU A  50     -18.895 -19.958  -0.601  0.61 36.01           C
ANISOU  418  CD AGLU A  50     4268   4275   5140   -498    456   -788       C
ATOM    419  OE1AGLU A  50     -19.657 -19.009  -0.328  0.61 38.64           O
ANISOU  419  OE1AGLU A  50     4547   4629   5504   -489    455   -811       O
ATOM    420  OE2AGLU A  50     -19.079 -21.122  -0.188  0.61 38.75           O
ANISOU  420  OE2AGLU A  50     4636   4603   5484   -547    487   -800       O
ATOM    421  CA BGLU A  50     -15.756 -20.727  -2.777  0.39 31.87           C
ANISOU  421  CA BGLU A  50     3880   3713   4515   -412    391   -691       C
ATOM    422  CB BGLU A  50     -17.112 -20.901  -2.087  0.39 32.71           C
ANISOU  422  CB BGLU A  50     3940   3830   4660   -457    414   -735       C
ATOM    423  CG BGLU A  50     -17.147 -20.407  -0.646  0.39 34.11           C
ANISOU  423  CG BGLU A  50     4113   4003   4846   -477    456   -726       C
ATOM    424  CD BGLU A  50     -17.411 -18.913  -0.533  0.39 35.12           C
ANISOU  424  CD BGLU A  50     4198   4154   4990   -443    442   -726       C
ATOM    425  OE1BGLU A  50     -18.197 -18.375  -1.341  0.39 37.66           O
ANISOU  425  OE1BGLU A  50     4473   4501   5336   -422    406   -755       O
ATOM    426  OE2BGLU A  50     -16.835 -18.273   0.371  0.39 34.47           O
ANISOU  426  OE2BGLU A  50     4134   4065   4898   -438    465   -698       O
ATOM    427  N   GLU A  51     -15.400 -22.718  -4.171  1.00 32.94           N
ANISOU  427  N   GLU A  51     4070   3822   4623   -426    374   -702       N
ATOM    428  CA  GLU A  51     -14.772 -24.002  -4.487  1.00 36.92           C
ANISOU  428  CA  GLU A  51     4626   4297   5105   -437    382   -695       C
ATOM    429  C   GLU A  51     -13.272 -23.839  -4.667  1.00 32.96           C
ANISOU  429  C   GLU A  51     4168   3781   4573   -398    381   -650       C
ATOM    430  O   GLU A  51     -12.478 -24.644  -4.166  1.00 31.33           O
ANISOU  430  O   GLU A  51     4005   3544   4353   -406    403   -630       O
ATOM    431  CB  GLU A  51     -15.376 -24.616  -5.754  1.00 46.39           C
ANISOU  431  CB  GLU A  51     5820   5502   6304   -441    351   -728       C
ATOM    432  CG  GLU A  51     -16.885 -24.508  -5.875  1.00 61.71           C
ANISOU  432  CG  GLU A  51     7703   7466   8279   -469    337   -775       C
ATOM    433  CD  GLU A  51     -17.320 -23.194  -6.494  1.00 71.41           C
ANISOU  433  CD  GLU A  51     8886   8728   9519   -431    296   -782       C
ATOM    434  OE1 GLU A  51     -17.831 -22.326  -5.753  1.00 67.94           O
ANISOU  434  OE1 GLU A  51     8403   8305   9105   -431    305   -788       O
ATOM    435  OE2 GLU A  51     -17.136 -23.026  -7.721  1.00 76.77           O
ANISOU  435  OE2 GLU A  51     9576   9413  10178   -401    255   -782       O
ATOM    436  N   GLU A  52     -12.867 -22.804  -5.406  1.00 30.47           N
ANISOU  436  N   GLU A  52     3843   3487   4247   -355    354   -636       N
ATOM    437  CA  GLU A  52     -11.450 -22.503  -5.555  1.00 27.93           C
ANISOU  437  CA  GLU A  52     3556   3157   3900   -319    357   -595       C
ATOM    438  C   GLU A  52     -10.792 -22.283  -4.203  1.00 26.65           C
ANISOU  438  C   GLU A  52     3404   2981   3740   -325    386   -565       C
ATOM    439  O   GLU A  52      -9.687 -22.782  -3.947  1.00 27.29           O
ANISOU  439  O   GLU A  52     3522   3040   3808   -316    399   -538       O
ATOM    440  CB  GLU A  52     -11.291 -21.269  -6.439  1.00 24.68           C
ANISOU  440  CB  GLU A  52     3129   2771   3477   -280    326   -587       C
ATOM    441  CG  GLU A  52      -9.937 -20.629  -6.380  1.00 27.47           C
ANISOU  441  CG  GLU A  52     3506   3122   3810   -249    333   -546       C
ATOM    442  CD  GLU A  52      -9.897 -19.359  -7.192  1.00 31.66           C
ANISOU  442  CD  GLU A  52     4026   3676   4328   -217    304   -539       C
ATOM    443  OE1 GLU A  52     -10.231 -18.286  -6.634  1.00 26.97           O
ANISOU  443  OE1 GLU A  52     3406   3096   3746   -211    299   -532       O
ATOM    444  OE2 GLU A  52      -9.563 -19.448  -8.396  1.00 26.32           O
ANISOU  444  OE2 GLU A  52     3371   3002   3628   -199    286   -541       O
ATOM    445  N   TYR A  53     -11.462 -21.530  -3.325  1.00 29.88           N
ANISOU  445  N   TYR A  53     3782   3403   4168   -340    395   -570       N
ATOM    446  CA  TYR A  53     -10.924 -21.254  -1.999  1.00 27.04           C
ANISOU  446  CA  TYR A  53     3435   3030   3809   -349    421   -542       C
ATOM    447  C   TYR A  53     -10.764 -22.538  -1.202  1.00 25.67           C
ANISOU  447  C   TYR A  53     3298   2821   3632   -385    448   -541       C
ATOM    448  O   TYR A  53      -9.715 -22.782  -0.591  1.00 29.36           O
ANISOU  448  O   TYR A  53     3802   3266   4087   -378    458   -509       O
ATOM    449  CB  TYR A  53     -11.852 -20.277  -1.277  1.00 24.67           C
ANISOU  449  CB  TYR A  53     3093   2749   3529   -362    429   -556       C
ATOM    450  CG  TYR A  53     -11.391 -19.779   0.068  1.00 26.81           C
ANISOU  450  CG  TYR A  53     3377   3009   3798   -372    454   -530       C
ATOM    451  CD1 TYR A  53     -10.137 -19.211   0.232  1.00 31.24           C
ANISOU  451  CD1 TYR A  53     3963   3567   4342   -343    449   -489       C
ATOM    452  CD2 TYR A  53     -12.250 -19.802   1.164  1.00 37.72           C
ANISOU  452  CD2 TYR A  53     4746   4389   5197   -412    484   -548       C
ATOM    453  CE1 TYR A  53      -9.729 -18.717   1.462  1.00 32.96           C
ANISOU  453  CE1 TYR A  53     4194   3775   4556   -352    468   -465       C
ATOM    454  CE2 TYR A  53     -11.852 -19.311   2.396  1.00 41.15           C
ANISOU  454  CE2 TYR A  53     5197   4812   5625   -423    507   -525       C
ATOM    455  CZ  TYR A  53     -10.591 -18.770   2.540  1.00 35.95           C
ANISOU  455  CZ  TYR A  53     4566   4148   4947   -392    496   -483       C
ATOM    456  OH  TYR A  53     -10.182 -18.283   3.761  1.00 31.81           O
ANISOU  456  OH  TYR A  53     4060   3611   4414   -404    515   -460       O
ATOM    457  N   GLY A  54     -11.797 -23.379  -1.206  1.00 27.41           N
ANISOU  457  N   GLY A  54     3512   3037   3866   -423    457   -576       N
ATOM    458  CA  GLY A  54     -11.736 -24.607  -0.429  1.00 33.27           C
ANISOU  458  CA  GLY A  54     4295   3742   4603   -462    483   -576       C
ATOM    459  C   GLY A  54     -10.663 -25.555  -0.929  1.00 30.96           C
ANISOU  459  C   GLY A  54     4051   3421   4291   -442    474   -557       C
ATOM    460  O   GLY A  54      -9.946 -26.174  -0.138  1.00 28.22           O
ANISOU  460  O   GLY A  54     3749   3040   3934   -450    488   -534       O
ATOM    461  N   ARG A  55     -10.522 -25.665  -2.246  1.00 36.48           N
ANISOU  461  N   ARG A  55     4745   4132   4985   -414    451   -567       N
ATOM    462  CA  ARG A  55      -9.482 -26.534  -2.781  1.00 40.31           C
ANISOU  462  CA  ARG A  55     5273   4590   5453   -391    446   -553       C
ATOM    463  C   ARG A  55      -8.099 -25.936  -2.560  1.00 36.70           C
ANISOU  463  C   ARG A  55     4828   4131   4987   -350    443   -512       C
ATOM    464  O   ARG A  55      -7.129 -26.674  -2.361  1.00 31.39           O
ANISOU  464  O   ARG A  55     4192   3427   4306   -338    448   -494       O
ATOM    465  CB  ARG A  55      -9.751 -26.804  -4.258  1.00 46.83           C
ANISOU  465  CB  ARG A  55     6093   5429   6273   -377    425   -578       C
ATOM    466  CG  ARG A  55     -11.074 -27.530  -4.491  1.00 54.60           C
ANISOU  466  CG  ARG A  55     7066   6413   7268   -420    424   -620       C
ATOM    467  CD  ARG A  55     -11.546 -27.424  -5.934  1.00 66.97           C
ANISOU  467  CD  ARG A  55     8615   8002   8830   -405    395   -646       C
ATOM    468  NE  ARG A  55     -10.563 -27.943  -6.883  1.00 78.88           N
ANISOU  468  NE  ARG A  55    10162   9494  10315   -374    388   -637       N
ATOM    469  CZ  ARG A  55      -9.734 -27.183  -7.593  1.00 87.00           C
ANISOU  469  CZ  ARG A  55    11190  10539  11327   -330    375   -618       C
ATOM    470  NH1 ARG A  55      -9.768 -25.862  -7.464  1.00 89.43           N
ANISOU  470  NH1 ARG A  55    11464  10876  11639   -312    366   -604       N
ATOM    471  NH2 ARG A  55      -8.870 -27.742  -8.432  1.00 88.02           N
ANISOU  471  NH2 ARG A  55    11354  10653  11437   -305    376   -615       N
ATOM    472  N   LEU A  56      -7.994 -24.604  -2.553  1.00 32.33           N
ANISOU  472  N   LEU A  56     4242   3609   4435   -329    436   -499       N
ATOM    473  CA  LEU A  56      -6.724 -23.968  -2.233  1.00 27.38           C
ANISOU  473  CA  LEU A  56     3623   2981   3801   -297    435   -461       C
ATOM    474  C   LEU A  56      -6.311 -24.260  -0.793  1.00 25.50           C
ANISOU  474  C   LEU A  56     3410   2714   3564   -316    450   -438       C
ATOM    475  O   LEU A  56      -5.151 -24.589  -0.519  1.00 25.04           O
ANISOU  475  O   LEU A  56     3378   2635   3501   -295    448   -413       O
ATOM    476  CB  LEU A  56      -6.836 -22.463  -2.462  1.00 36.95           C
ANISOU  476  CB  LEU A  56     4798   4228   5012   -278    424   -454       C
ATOM    477  CG  LEU A  56      -5.773 -21.807  -3.325  1.00 49.64           C
ANISOU  477  CG  LEU A  56     6404   5850   6605   -236    412   -434       C
ATOM    478  CD1 LEU A  56      -5.710 -20.345  -2.976  1.00 52.35           C
ANISOU  478  CD1 LEU A  56     6725   6218   6950   -225    407   -416       C
ATOM    479  CD2 LEU A  56      -4.439 -22.478  -3.101  1.00 59.42           C
ANISOU  479  CD2 LEU A  56     7672   7064   7840   -219    420   -411       C
ATOM    480  N   LEU A  57      -7.247 -24.093   0.149  1.00 26.65           N
ANISOU  480  N   LEU A  57     3548   2859   3717   -354    464   -448       N
ATOM    481  CA  LEU A  57      -6.989 -24.437   1.544  1.00 26.50           C
ANISOU  481  CA  LEU A  57     3564   2811   3696   -380    480   -429       C
ATOM    482  C   LEU A  57      -6.613 -25.907   1.685  1.00 30.36           C
ANISOU  482  C   LEU A  57     4103   3256   4179   -391    482   -428       C
ATOM    483  O   LEU A  57      -5.704 -26.258   2.449  1.00 23.45           O
ANISOU  483  O   LEU A  57     3264   2349   3295   -385    480   -400       O
ATOM    484  CB  LEU A  57      -8.223 -24.122   2.391  1.00 26.29           C
ANISOU  484  CB  LEU A  57     3521   2791   3677   -426    502   -449       C
ATOM    485  CG  LEU A  57      -8.570 -22.634   2.512  1.00 30.13           C
ANISOU  485  CG  LEU A  57     3963   3314   4171   -414    500   -448       C
ATOM    486  CD1 LEU A  57     -10.005 -22.467   2.984  1.00 34.75           C
ANISOU  486  CD1 LEU A  57     4521   3912   4772   -457    523   -482       C
ATOM    487  CD2 LEU A  57      -7.621 -21.944   3.458  1.00 29.76           C
ANISOU  487  CD2 LEU A  57     3934   3259   4114   -403    501   -410       C
ATOM    488  N   ALA A  58      -7.303 -26.782   0.958  1.00 27.88           N
ANISOU  488  N   ALA A  58     3791   2936   3866   -407    484   -459       N
ATOM    489  CA  ALA A  58      -6.953 -28.199   1.010  1.00 36.69           C
ANISOU  489  CA  ALA A  58     4959   4007   4975   -416    485   -460       C
ATOM    490  C   ALA A  58      -5.547 -28.425   0.476  1.00 32.89           C
ANISOU  490  C   ALA A  58     4494   3513   4491   -364    468   -437       C
ATOM    491  O   ALA A  58      -4.780 -29.218   1.035  1.00 37.95           O
ANISOU  491  O   ALA A  58     5179   4112   5128   -358    464   -419       O
ATOM    492  CB  ALA A  58      -7.968 -29.029   0.224  1.00 38.66           C
ANISOU  492  CB  ALA A  58     5206   4255   5228   -443    490   -499       C
ATOM    493  N   HIS A  59      -5.186 -27.720  -0.599  1.00 35.80           N
ANISOU  493  N   HIS A  59     4827   3915   4860   -326    457   -439       N
ATOM    494  CA  HIS A  59      -3.831 -27.810  -1.136  1.00 33.37           C
ANISOU  494  CA  HIS A  59     4526   3600   4551   -277    446   -421       C
ATOM    495  C   HIS A  59      -2.802 -27.424  -0.080  1.00 33.94           C
ANISOU  495  C   HIS A  59     4609   3659   4627   -262    441   -384       C
ATOM    496  O   HIS A  59      -1.816 -28.137   0.134  1.00 37.04           O
ANISOU  496  O   HIS A  59     5030   4020   5023   -240    434   -369       O
ATOM    497  CB  HIS A  59      -3.715 -26.916  -2.372  1.00 41.57           C
ANISOU  497  CB  HIS A  59     5526   4681   5586   -247    440   -428       C
ATOM    498  CG  HIS A  59      -2.317 -26.749  -2.879  1.00 51.58           C
ANISOU  498  CG  HIS A  59     6794   5951   6855   -201    436   -410       C
ATOM    499  ND1 HIS A  59      -1.481 -27.816  -3.128  1.00 50.99           N
ANISOU  499  ND1 HIS A  59     6747   5843   6782   -179    437   -411       N
ATOM    500  CD2 HIS A  59      -1.613 -25.637  -3.198  1.00 51.38           C
ANISOU  500  CD2 HIS A  59     6740   5955   6827   -173    433   -393       C
ATOM    501  CE1 HIS A  59      -0.321 -27.368  -3.574  1.00 49.72           C
ANISOU  501  CE1 HIS A  59     6571   5694   6625   -140    436   -397       C
ATOM    502  NE2 HIS A  59      -0.374 -26.050  -3.624  1.00 54.24           N
ANISOU  502  NE2 HIS A  59     7110   6304   7193   -138    435   -386       N
ATOM    503  N   MET A  60      -3.035 -26.307   0.617  1.00 30.28           N
ANISOU  503  N   MET A  60     4122   3218   4163   -273    443   -369       N
ATOM    504  CA  MET A  60      -2.085 -25.873   1.634  1.00 26.70           C
ANISOU  504  CA  MET A  60     3679   2754   3711   -262    436   -335       C
ATOM    505  C   MET A  60      -2.065 -26.825   2.818  1.00 22.84           C
ANISOU  505  C   MET A  60     3243   2217   3218   -289    435   -324       C
ATOM    506  O   MET A  60      -1.017 -27.031   3.441  1.00 27.10           O
ANISOU  506  O   MET A  60     3806   2732   3761   -269    420   -297       O
ATOM    507  CB  MET A  60      -2.428 -24.460   2.097  1.00 22.88           C
ANISOU  507  CB  MET A  60     3164   2304   3225   -271    439   -324       C
ATOM    508  CG  MET A  60      -2.134 -23.403   1.062  1.00 24.28           C
ANISOU  508  CG  MET A  60     3298   2522   3403   -239    434   -325       C
ATOM    509  SD  MET A  60      -2.563 -21.777   1.696  1.00 30.28           S
ANISOU  509  SD  MET A  60     4030   3315   4162   -250    436   -313       S
ATOM    510  CE  MET A  60      -4.261 -21.648   1.164  1.00 22.04           C
ANISOU  510  CE  MET A  60     2960   2293   3120   -277    446   -352       C
ATOM    511  N   GLN A  61      -3.218 -27.390   3.169  1.00 29.99           N
ANISOU  511  N   GLN A  61     4168   3109   4118   -335    451   -345       N
ATOM    512  CA  GLN A  61      -3.251 -28.337   4.276  1.00 36.56           C
ANISOU  512  CA  GLN A  61     5060   3892   4941   -366    453   -335       C
ATOM    513  C   GLN A  61      -2.473 -29.604   3.932  1.00 38.52           C
ANISOU  513  C   GLN A  61     5347   4097   5191   -342    437   -333       C
ATOM    514  O   GLN A  61      -1.799 -30.177   4.795  1.00 36.48           O
ANISOU  514  O   GLN A  61     5138   3796   4929   -339    423   -310       O
ATOM    515  CB  GLN A  61      -4.700 -28.658   4.644  1.00 32.71           C
ANISOU  515  CB  GLN A  61     4582   3400   4446   -426    479   -363       C
ATOM    516  CG  GLN A  61      -4.856 -29.451   5.918  1.00 36.21           C
ANISOU  516  CG  GLN A  61     5091   3794   4874   -470    487   -352       C
ATOM    517  CD  GLN A  61      -6.297 -29.853   6.165  1.00 36.79           C
ANISOU  517  CD  GLN A  61     5171   3865   4943   -533    519   -384       C
ATOM    518  OE1 GLN A  61      -7.091 -29.962   5.228  1.00 44.31           O
ANISOU  518  OE1 GLN A  61     6087   4843   5906   -540    528   -418       O
ATOM    519  NE2 GLN A  61      -6.645 -30.065   7.425  1.00 34.36           N
ANISOU  519  NE2 GLN A  61     4910   3528   4618   -582    537   -377       N
ATOM    520  N   GLU A  62      -2.541 -30.043   2.671  1.00 42.12           N
ANISOU  520  N   GLU A  62     5787   4563   5654   -321    438   -357       N
ATOM    521  CA  GLU A  62      -1.750 -31.195   2.237  1.00 45.19           C
ANISOU  521  CA  GLU A  62     6210   4913   6047   -291    425   -358       C
ATOM    522  C   GLU A  62      -0.253 -30.908   2.332  1.00 51.62           C
ANISOU  522  C   GLU A  62     7016   5724   6874   -238    404   -330       C
ATOM    523  O   GLU A  62       0.522 -31.755   2.790  1.00 55.67           O
ANISOU  523  O   GLU A  62     7570   6191   7392   -220    386   -317       O
ATOM    524  CB  GLU A  62      -2.118 -31.580   0.801  1.00 39.46           C
ANISOU  524  CB  GLU A  62     5465   4204   5323   -280    433   -391       C
ATOM    525  CG  GLU A  62      -3.560 -32.021   0.563  1.00 40.93           C
ANISOU  525  CG  GLU A  62     5657   4393   5501   -331    450   -423       C
ATOM    526  CD  GLU A  62      -3.870 -32.134  -0.928  1.00 42.22           C
ANISOU  526  CD  GLU A  62     5795   4580   5665   -316    452   -454       C
ATOM    527  OE1 GLU A  62      -2.936 -31.927  -1.727  1.00 46.25           O
ANISOU  527  OE1 GLU A  62     6291   5103   6181   -268    444   -449       O
ATOM    528  OE2 GLU A  62      -5.030 -32.414  -1.306  1.00 38.04           O
ANISOU  528  OE2 GLU A  62     5262   4060   5133   -353    461   -484       O
ATOM    529  N   GLU A  63       0.173 -29.720   1.897  1.00 50.82           N
ANISOU  529  N   GLU A  63     6861   5668   6779   -212    404   -322       N
ATOM    530  CA  GLU A  63       1.579 -29.329   1.915  1.00 48.09           C
ANISOU  530  CA  GLU A  63     6498   5326   6449   -164    387   -299       C
ATOM    531  C   GLU A  63       2.086 -28.956   3.301  1.00 51.92           C
ANISOU  531  C   GLU A  63     7001   5794   6934   -170    368   -266       C
ATOM    532  O   GLU A  63       3.279 -28.664   3.445  1.00 52.85           O
ANISOU  532  O   GLU A  63     7102   5912   7066   -133    350   -246       O
ATOM    533  CB  GLU A  63       1.806 -28.144   0.978  1.00 49.87           C
ANISOU  533  CB  GLU A  63     6665   5607   6677   -142    396   -303       C
ATOM    534  CG  GLU A  63       1.524 -28.435  -0.476  1.00 53.54           C
ANISOU  534  CG  GLU A  63     7115   6089   7140   -129    410   -334       C
ATOM    535  CD  GLU A  63       2.787 -28.689  -1.258  1.00 54.96           C
ANISOU  535  CD  GLU A  63     7281   6267   7334    -79    409   -335       C
ATOM    536  OE1 GLU A  63       2.680 -29.070  -2.440  1.00 52.46           O
ANISOU  536  OE1 GLU A  63     6962   5958   7014    -67    421   -361       O
ATOM    537  OE2 GLU A  63       3.886 -28.501  -0.692  1.00 57.18           O
ANISOU  537  OE2 GLU A  63     7555   6541   7631    -53    395   -312       O
ATOM    538  N   GLY A  64       1.223 -28.935   4.313  1.00 47.26           N
ANISOU  538  N   GLY A  64     6441   5190   6327   -218    374   -260       N
ATOM    539  CA  GLY A  64       1.633 -28.471   5.621  1.00 42.76           C
ANISOU  539  CA  GLY A  64     5891   4606   5751   -229    358   -229       C
ATOM    540  C   GLY A  64       1.814 -26.975   5.740  1.00 39.97           C
ANISOU  540  C   GLY A  64     5490   4298   5398   -224    360   -215       C
ATOM    541  O   GLY A  64       2.351 -26.511   6.749  1.00 43.89           O
ANISOU  541  O   GLY A  64     6000   4785   5891   -227    343   -187       O
ATOM    542  N   VAL A  65       1.368 -26.201   4.748  1.00 35.85           N
ANISOU  542  N   VAL A  65     4918   3824   4879   -219    379   -233       N
ATOM    543  CA  VAL A  65       1.527 -24.748   4.813  1.00 29.13           C
ANISOU  543  CA  VAL A  65     4026   3014   4027   -214    381   -220       C
ATOM    544  C   VAL A  65       0.579 -24.142   5.845  1.00 32.30           C
ANISOU  544  C   VAL A  65     4441   3418   4413   -259    393   -216       C
ATOM    545  O   VAL A  65       0.913 -23.144   6.495  1.00 31.83           O
ANISOU  545  O   VAL A  65     4372   3372   4350   -261    387   -195       O
ATOM    546  CB  VAL A  65       1.332 -24.138   3.412  1.00 30.99           C
ANISOU  546  CB  VAL A  65     4213   3294   4268   -193    394   -240       C
ATOM    547  CG1 VAL A  65       1.429 -22.629   3.451  1.00 33.45           C
ANISOU  547  CG1 VAL A  65     4488   3645   4576   -190    395   -227       C
ATOM    548  CG2 VAL A  65       2.384 -24.699   2.462  1.00 28.96           C
ANISOU  548  CG2 VAL A  65     3946   3033   4024   -149    386   -244       C
ATOM    549  N   ILE A  66      -0.605 -24.734   6.026  1.00 26.76           N
ANISOU  549  N   ILE A  66     3761   2704   3702   -299    412   -238       N
ATOM    550  CA  ILE A  66      -1.546 -24.315   7.055  1.00 27.37           C
ANISOU  550  CA  ILE A  66     3854   2780   3767   -347    431   -239       C
ATOM    551  C   ILE A  66      -2.064 -25.550   7.775  1.00 33.09           C
ANISOU  551  C   ILE A  66     4638   3457   4478   -387    439   -246       C
ATOM    552  O   ILE A  66      -1.937 -26.682   7.298  1.00 29.89           O
ANISOU  552  O   ILE A  66     4255   3026   4076   -379    433   -256       O
ATOM    553  CB  ILE A  66      -2.740 -23.513   6.499  1.00 28.91           C
ANISOU  553  CB  ILE A  66     4003   3017   3965   -363    454   -268       C
ATOM    554  CG1 ILE A  66      -3.535 -24.378   5.522  1.00 23.52           C
ANISOU  554  CG1 ILE A  66     3313   2337   3289   -370    465   -302       C
ATOM    555  CG2 ILE A  66      -2.290 -22.203   5.858  1.00 35.54           C
ANISOU  555  CG2 ILE A  66     4792   3899   4811   -328    446   -259       C
ATOM    556  CD1 ILE A  66      -4.693 -23.652   4.872  1.00 34.48           C
ANISOU  556  CD1 ILE A  66     4651   3765   4684   -381    480   -332       C
ATOM    557  N   ARG A  67      -2.665 -25.309   8.937  1.00 30.03           N
ANISOU  557  N   ARG A  67     4278   3057   4074   -432    455   -242       N
ATOM    558  CA  ARG A  67      -3.377 -26.327   9.699  1.00 36.96           C
ANISOU  558  CA  ARG A  67     5215   3893   4936   -483    473   -252       C
ATOM    559  C   ARG A  67      -4.799 -25.850   9.951  1.00 34.02           C
ANISOU  559  C   ARG A  67     4822   3545   4561   -533    514   -281       C
ATOM    560  O   ARG A  67      -5.023 -24.665  10.234  1.00 26.21           O
ANISOU  560  O   ARG A  67     3799   2587   3573   -535    524   -280       O
ATOM    561  CB  ARG A  67      -2.704 -26.607  11.045  1.00 44.02           C
ANISOU  561  CB  ARG A  67     6178   4740   5808   -499    455   -218       C
ATOM    562  CG  ARG A  67      -1.385 -27.342  10.987  1.00 49.70           C
ANISOU  562  CG  ARG A  67     6929   5424   6532   -456    412   -192       C
ATOM    563  CD  ARG A  67      -0.862 -27.547  12.402  1.00 52.61           C
ANISOU  563  CD  ARG A  67     7369   5745   6876   -476    391   -160       C
ATOM    564  NE  ARG A  67      -1.901 -28.058  13.301  1.00 56.22           N
ANISOU  564  NE  ARG A  67     7886   6170   7304   -544    422   -170       N
ATOM    565  CZ  ARG A  67      -2.122 -29.350  13.539  1.00 61.45           C
ANISOU  565  CZ  ARG A  67     8614   6782   7952   -570    421   -174       C
ATOM    566  NH1 ARG A  67      -1.382 -30.278  12.950  1.00 60.34           N
ANISOU  566  NH1 ARG A  67     8488   6614   7826   -529    389   -169       N
ATOM    567  NH2 ARG A  67      -3.087 -29.717  14.370  1.00 65.58           N
ANISOU  567  NH2 ARG A  67     9191   7279   8447   -637    455   -185       N
ATOM    568  N   LYS A  68      -5.756 -26.770   9.858  1.00 33.69           N
ANISOU  568  N   LYS A  68     4797   3487   4516   -574    537   -310       N
ATOM    569  CA  LYS A  68      -7.136 -26.446  10.185  1.00 35.41           C
ANISOU  569  CA  LYS A  68     4995   3724   4735   -626    579   -342       C
ATOM    570  C   LYS A  68      -7.316 -26.378  11.692  1.00 31.69           C
ANISOU  570  C   LYS A  68     4580   3223   4237   -676    601   -329       C
ATOM    571  O   LYS A  68      -6.802 -27.219  12.432  1.00 31.92           O
ANISOU  571  O   LYS A  68     4683   3200   4243   -693    590   -307       O
ATOM    572  CB  LYS A  68      -8.104 -27.474   9.599  1.00 33.36           C
ANISOU  572  CB  LYS A  68     4735   3457   4482   -658    599   -379       C
ATOM    573  CG  LYS A  68      -9.559 -27.101   9.823  1.00 28.48           C
ANISOU  573  CG  LYS A  68     4081   2866   3873   -710    642   -419       C
ATOM    574  CD  LYS A  68     -10.487 -27.656   8.753  1.00 43.49           C
ANISOU  574  CD  LYS A  68     5942   4786   5795   -720    650   -461       C
ATOM    575  CE  LYS A  68     -11.951 -27.378   9.098  1.00 54.14           C
ANISOU  575  CE  LYS A  68     7256   6159   7158   -776    694   -503       C
ATOM    576  NZ  LYS A  68     -12.768 -27.037   7.894  1.00 58.73           N
ANISOU  576  NZ  LYS A  68     7758   6786   7771   -760    689   -542       N
ATOM    577  N   LEU A  69      -8.053 -25.368  12.138  1.00 28.65           N
ANISOU  577  N   LEU A  69     4163   2869   3856   -699    631   -344       N
ATOM    578  CA  LEU A  69      -8.369 -25.171  13.551  1.00 24.18           C
ANISOU  578  CA  LEU A  69     3645   2279   3263   -752    660   -338       C
ATOM    579  C   LEU A  69      -9.750 -25.777  13.780  1.00 36.02           C
ANISOU  579  C   LEU A  69     5149   3773   4763   -819    711   -380       C
ATOM    580  O   LEU A  69     -10.774 -25.155  13.472  1.00 32.45           O
ANISOU  580  O   LEU A  69     4633   3363   4335   -831    741   -417       O
ATOM    581  CB  LEU A  69      -8.311 -23.689  13.912  1.00 26.28           C
ANISOU  581  CB  LEU A  69     3874   2579   3533   -737    665   -331       C
ATOM    582  CG  LEU A  69      -6.926 -23.063  13.725  1.00 28.18           C
ANISOU  582  CG  LEU A  69     4110   2824   3773   -677    617   -290       C
ATOM    583  CD1 LEU A  69      -7.029 -21.548  13.548  1.00 24.10           C
ANISOU  583  CD1 LEU A  69     3533   2354   3270   -652    620   -293       C
ATOM    584  CD2 LEU A  69      -6.016 -23.417  14.904  1.00 31.90           C
ANISOU  584  CD2 LEU A  69     4664   3245   4210   -690    597   -250       C
ATOM    585  N   LYS A  70      -9.761 -27.005  14.321  1.00 35.01           N
ANISOU  585  N   LYS A  70     5097   3593   4610   -861    718   -375       N
ATOM    586  CA  LYS A  70     -10.975 -27.819  14.395  1.00 39.11           C
ANISOU  586  CA  LYS A  70     5626   4103   5129   -926    764   -415       C
ATOM    587  C   LYS A  70     -12.042 -27.221  15.302  1.00 40.73           C
ANISOU  587  C   LYS A  70     5822   4323   5330   -987    822   -444       C
ATOM    588  O   LYS A  70     -13.230 -27.518  15.129  1.00 39.84           O
ANISOU  588  O   LYS A  70     5678   4225   5233  -1033    865   -489       O
ATOM    589  CB  LYS A  70     -10.632 -29.223  14.889  1.00 39.56           C
ANISOU  589  CB  LYS A  70     5781   4094   5154   -959    757   -398       C
ATOM    590  CG  LYS A  70      -9.664 -29.979  14.005  1.00 51.29           C
ANISOU  590  CG  LYS A  70     7280   5561   6648   -903    704   -377       C
ATOM    591  CD  LYS A  70     -10.325 -30.389  12.700  1.00 59.04           C
ANISOU  591  CD  LYS A  70     8201   6571   7660   -893    708   -415       C
ATOM    592  CE  LYS A  70      -9.487 -31.410  11.949  1.00 57.13           C
ANISOU  592  CE  LYS A  70     7991   6298   7419   -852    666   -399       C
ATOM    593  NZ  LYS A  70     -10.093 -31.751  10.631  1.00 58.84           N
ANISOU  593  NZ  LYS A  70     8149   6543   7662   -842    668   -435       N
ATOM    594  N   LYS A  71     -11.649 -26.414  16.288  1.00 42.44           N
ANISOU  594  N   LYS A  71     6067   4534   5526   -991    827   -420       N
ATOM    595  CA  LYS A  71     -12.624 -25.868  17.225  1.00 41.80           C
ANISOU  595  CA  LYS A  71     5984   4462   5437  -1050    888   -448       C
ATOM    596  C   LYS A  71     -13.570 -24.877  16.564  1.00 44.44           C
ANISOU  596  C   LYS A  71     6210   4860   5817  -1035    912   -491       C
ATOM    597  O   LYS A  71     -14.676 -24.658  17.071  1.00 38.03           O
ANISOU  597  O   LYS A  71     5378   4061   5013  -1089    970   -532       O
ATOM    598  CB  LYS A  71     -11.905 -25.203  18.400  1.00 42.24           C
ANISOU  598  CB  LYS A  71     6098   4495   5456  -1054    883   -411       C
ATOM    599  CG  LYS A  71     -12.809 -24.726  19.525  1.00 44.71           C
ANISOU  599  CG  LYS A  71     6426   4812   5750  -1115    946   -436       C
ATOM    600  CD  LYS A  71     -11.991 -24.301  20.732  1.00 46.30           C
ANISOU  600  CD  LYS A  71     6700   4990   5901  -1111    928   -392       C
ATOM    601  CE  LYS A  71     -12.812 -24.420  22.003  1.00 54.48           C
ANISOU  601  CE  LYS A  71     7777   6030   6892  -1164    978   -408       C
ATOM    602  NZ  LYS A  71     -11.960 -24.437  23.225  1.00 54.92           N
ANISOU  602  NZ  LYS A  71     7928   6053   6888  -1166    950   -362       N
ATOM    603  N   TYR A  72     -13.168 -24.278  15.448  1.00 44.64           N
ANISOU  603  N   TYR A  72     6167   4923   5873   -964    869   -486       N
ATOM    604  CA  TYR A  72     -13.930 -23.217  14.811  1.00 34.23           C
ANISOU  604  CA  TYR A  72     4750   3660   4595   -939    879   -521       C
ATOM    605  C   TYR A  72     -14.442 -23.681  13.450  1.00 34.65           C
ANISOU  605  C   TYR A  72     4741   3741   4684   -918    862   -550       C
ATOM    606  O   TYR A  72     -14.192 -24.807  13.006  1.00 36.81           O
ANISOU  606  O   TYR A  72     5047   3989   4950   -923    845   -544       O
ATOM    607  CB  TYR A  72     -13.079 -21.948  14.690  1.00 27.50           C
ANISOU  607  CB  TYR A  72     3874   2830   3745   -877    844   -490       C
ATOM    608  CG  TYR A  72     -12.375 -21.587  15.979  1.00 29.05           C
ANISOU  608  CG  TYR A  72     4142   2995   3903   -894    849   -454       C
ATOM    609  CD1 TYR A  72     -13.095 -21.341  17.143  1.00 28.95           C
ANISOU  609  CD1 TYR A  72     4154   2971   3873   -954    905   -473       C
ATOM    610  CD2 TYR A  72     -10.990 -21.511  16.037  1.00 32.41           C
ANISOU  610  CD2 TYR A  72     4608   3400   4307   -852    799   -402       C
ATOM    611  CE1 TYR A  72     -12.450 -21.027  18.327  1.00 30.94           C
ANISOU  611  CE1 TYR A  72     4478   3191   4085   -972    908   -441       C
ATOM    612  CE2 TYR A  72     -10.341 -21.194  17.209  1.00 29.73           C
ANISOU  612  CE2 TYR A  72     4334   3031   3931   -868    798   -370       C
ATOM    613  CZ  TYR A  72     -11.072 -20.958  18.355  1.00 30.38           C
ANISOU  613  CZ  TYR A  72     4448   3101   3993   -929    851   -388       C
ATOM    614  OH  TYR A  72     -10.414 -20.633  19.524  1.00 33.31           O
ANISOU  614  OH  TYR A  72     4891   3440   4324   -946    848   -355       O
ATOM    615  N   ASP A  73     -15.178 -22.789  12.802  1.00 36.14           N
ANISOU  615  N   ASP A  73     4842   3978   4911   -894    865   -584       N
ATOM    616  CA  ASP A  73     -15.824 -23.042  11.522  1.00 32.78           C
ANISOU  616  CA  ASP A  73     4349   3583   4522   -876    848   -618       C
ATOM    617  C   ASP A  73     -14.930 -22.468  10.429  1.00 32.51           C
ANISOU  617  C   ASP A  73     4288   3569   4494   -797    788   -589       C
ATOM    618  O   ASP A  73     -14.827 -21.244  10.288  1.00 29.92           O
ANISOU  618  O   ASP A  73     3920   3270   4179   -757    775   -585       O
ATOM    619  CB  ASP A  73     -17.216 -22.406  11.515  1.00 34.67           C
ANISOU  619  CB  ASP A  73     4511   3862   4802   -898    884   -674       C
ATOM    620  CG  ASP A  73     -17.877 -22.401  10.141  1.00 39.85           C
ANISOU  620  CG  ASP A  73     5087   4554   5497   -869    855   -708       C
ATOM    621  OD1 ASP A  73     -17.383 -23.066   9.211  1.00 40.68           O
ANISOU  621  OD1 ASP A  73     5205   4653   5597   -843    816   -694       O
ATOM    622  OD2 ASP A  73     -18.914 -21.719   9.997  1.00 42.90           O
ANISOU  622  OD2 ASP A  73     5400   4977   5923   -871    871   -752       O
ATOM    623  N   ASN A  74     -14.275 -23.353   9.670  1.00 28.03           N
ANISOU  623  N   ASN A  74     3748   2985   3918   -776    755   -571       N
ATOM    624  CA  ASN A  74     -13.464 -22.962   8.506  1.00 26.75           C
ANISOU  624  CA  ASN A  74     3561   2842   3761   -706    703   -550       C
ATOM    625  C   ASN A  74     -12.394 -21.925   8.873  1.00 28.75           C
ANISOU  625  C   ASN A  74     3827   3098   4000   -664    683   -508       C
ATOM    626  O   ASN A  74     -12.239 -20.895   8.214  1.00 31.27           O
ANISOU  626  O   ASN A  74     4100   3448   4332   -618    660   -504       O
ATOM    627  CB  ASN A  74     -14.362 -22.452   7.372  1.00 29.56           C
ANISOU  627  CB  ASN A  74     3837   3243   4153   -684    690   -589       C
ATOM    628  CG  ASN A  74     -13.620 -22.311   6.034  1.00 34.03           C
ANISOU  628  CG  ASN A  74     4388   3823   4719   -622    640   -572       C
ATOM    629  OD1 ASN A  74     -12.743 -23.108   5.698  1.00 30.99           O
ANISOU  629  OD1 ASN A  74     4046   3413   4315   -608    621   -547       O
ATOM    630  ND2 ASN A  74     -13.978 -21.285   5.272  1.00 34.46           N
ANISOU  630  ND2 ASN A  74     4383   3916   4795   -585    618   -585       N
ATOM    631  N   CYS A  75     -11.625 -22.222   9.920  1.00 26.33           N
ANISOU  631  N   CYS A  75     3588   2754   3664   -682    690   -474       N
ATOM    632  CA  CYS A  75     -10.517 -21.381  10.351  1.00 27.30           C
ANISOU  632  CA  CYS A  75     3730   2874   3771   -647    668   -432       C
ATOM    633  C   CYS A  75      -9.205 -22.145  10.236  1.00 30.29           C
ANISOU  633  C   CYS A  75     4160   3219   4129   -622    634   -392       C
ATOM    634  O   CYS A  75      -9.163 -23.371  10.409  1.00 27.74           O
ANISOU  634  O   CYS A  75     3883   2861   3795   -648    638   -392       O
ATOM    635  CB  CYS A  75     -10.708 -20.903  11.786  1.00 30.20           C
ANISOU  635  CB  CYS A  75     4129   3225   4119   -688    701   -426       C
ATOM    636  SG  CYS A  75     -12.057 -19.728  11.966  1.00 28.55           S
ANISOU  636  SG  CYS A  75     3854   3057   3938   -704    740   -470       S
ATOM    637  N   TRP A  76      -8.129 -21.409   9.947  1.00 24.91           N
ANISOU  637  N   TRP A  76     3469   2549   3446   -572    602   -360       N
ATOM    638  CA  TRP A  76      -6.851 -22.020   9.598  1.00 24.58           C
ANISOU  638  CA  TRP A  76     3458   2485   3396   -537    566   -328       C
ATOM    639  C   TRP A  76      -5.701 -21.271  10.258  1.00 26.46           C
ANISOU  639  C   TRP A  76     3715   2716   3621   -514    545   -287       C
ATOM    640  O   TRP A  76      -5.806 -20.080  10.579  1.00 31.85           O
ANISOU  640  O   TRP A  76     4375   3422   4304   -511    551   -284       O
ATOM    641  CB  TRP A  76      -6.656 -22.059   8.071  1.00 24.26           C
ANISOU  641  CB  TRP A  76     3372   2471   3373   -492    544   -338       C
ATOM    642  CG  TRP A  76      -7.802 -22.701   7.374  1.00 22.52           C
ANISOU  642  CG  TRP A  76     3129   2260   3166   -513    560   -380       C
ATOM    643  CD1 TRP A  76      -8.984 -22.114   7.022  1.00 25.64           C
ANISOU  643  CD1 TRP A  76     3473   2690   3580   -526    576   -415       C
ATOM    644  CD2 TRP A  76      -7.894 -24.067   6.960  1.00 23.27           C
ANISOU  644  CD2 TRP A  76     3252   2330   3261   -526    558   -392       C
ATOM    645  NE1 TRP A  76      -9.802 -23.027   6.403  1.00 26.96           N
ANISOU  645  NE1 TRP A  76     3631   2855   3757   -547    584   -448       N
ATOM    646  CE2 TRP A  76      -9.160 -24.237   6.359  1.00 23.43           C
ANISOU  646  CE2 TRP A  76     3234   2371   3297   -549    575   -434       C
ATOM    647  CE3 TRP A  76      -7.028 -25.163   7.034  1.00 30.38           C
ANISOU  647  CE3 TRP A  76     4205   3189   4149   -518    543   -372       C
ATOM    648  CZ2 TRP A  76      -9.581 -25.459   5.841  1.00 27.99           C
ANISOU  648  CZ2 TRP A  76     3827   2930   3876   -569    578   -457       C
ATOM    649  CZ3 TRP A  76      -7.442 -26.371   6.508  1.00 33.93           C
ANISOU  649  CZ3 TRP A  76     4672   3619   4600   -534    547   -394       C
ATOM    650  CH2 TRP A  76      -8.711 -26.509   5.922  1.00 30.60           C
ANISOU  650  CH2 TRP A  76     4214   3220   4192   -561    565   -436       C
ATOM    651  N   LEU A  77      -4.597 -21.985  10.449  1.00 24.34           N
ANISOU  651  N   LEU A  77     3490   2415   3343   -498    518   -258       N
ATOM    652  CA  LEU A  77      -3.404 -21.457  11.096  1.00 28.61           C
ANISOU  652  CA  LEU A  77     4053   2945   3873   -477    491   -219       C
ATOM    653  C   LEU A  77      -2.184 -21.678  10.211  1.00 29.64           C
ANISOU  653  C   LEU A  77     4166   3078   4016   -423    456   -201       C
ATOM    654  O   LEU A  77      -1.935 -22.798   9.760  1.00 29.18           O
ANISOU  654  O   LEU A  77     4126   2998   3964   -412    445   -205       O
ATOM    655  CB  LEU A  77      -3.185 -22.125  12.450  1.00 31.15           C
ANISOU  655  CB  LEU A  77     4450   3216   4169   -514    490   -200       C
ATOM    656  CG  LEU A  77      -1.978 -21.675  13.261  1.00 29.99           C
ANISOU  656  CG  LEU A  77     4333   3052   4009   -498    457   -159       C
ATOM    657  CD1 LEU A  77      -2.109 -20.190  13.572  1.00 25.24           C
ANISOU  657  CD1 LEU A  77     3701   2484   3406   -499    468   -156       C
ATOM    658  CD2 LEU A  77      -1.891 -22.501  14.544  1.00 28.99           C
ANISOU  658  CD2 LEU A  77     4291   2869   3853   -538    453   -143       C
ATOM    659  N   ALA A  78      -1.424 -20.615   9.969  1.00 23.29           N
ANISOU  659  N   ALA A  78     3329   2301   3218   -389    439   -183       N
ATOM    660  CA  ALA A  78      -0.110 -20.698   9.343  1.00 30.30           C
ANISOU  660  CA  ALA A  78     4203   3191   4119   -342    408   -164       C
ATOM    661  C   ALA A  78       0.959 -20.293  10.350  1.00 28.59           C
ANISOU  661  C   ALA A  78     4012   2957   3895   -337    381   -128       C
ATOM    662  O   ALA A  78       0.756 -19.376  11.151  1.00 30.24           O
ANISOU  662  O   ALA A  78     4227   3172   4090   -358    388   -119       O
ATOM    663  CB  ALA A  78      -0.026 -19.801   8.102  1.00 27.78           C
ANISOU  663  CB  ALA A  78     3823   2918   3813   -308    409   -174       C
ATOM    664  N   LEU A  79       2.092 -20.982  10.315  1.00 30.02           N
ANISOU  664  N   LEU A  79     4207   3115   4085   -308    350   -110       N
ATOM    665  CA  LEU A  79       3.260 -20.625  11.107  1.00 31.71           C
ANISOU  665  CA  LEU A  79     4435   3314   4298   -295    316    -77       C
ATOM    666  C   LEU A  79       4.384 -20.303  10.139  1.00 32.78           C
ANISOU  666  C   LEU A  79     4520   3476   4459   -246    299    -72       C
ATOM    667  O   LEU A  79       4.646 -21.073   9.209  1.00 33.83           O
ANISOU  667  O   LEU A  79     4636   3608   4609   -218    298    -86       O
ATOM    668  CB  LEU A  79       3.682 -21.748  12.052  1.00 31.19           C
ANISOU  668  CB  LEU A  79     4435   3193   4223   -305    289    -61       C
ATOM    669  CG  LEU A  79       2.601 -22.295  12.989  1.00 33.62           C
ANISOU  669  CG  LEU A  79     4805   3468   4502   -359    310    -68       C
ATOM    670  CD1 LEU A  79       3.183 -23.338  13.958  1.00 35.34           C
ANISOU  670  CD1 LEU A  79     5095   3625   4707   -366    275    -45       C
ATOM    671  CD2 LEU A  79       1.887 -21.171  13.746  1.00 26.70           C
ANISOU  671  CD2 LEU A  79     3931   2609   3605   -398    335    -67       C
ATOM    672  N   THR A  80       5.027 -19.168  10.340  1.00 25.31           N
ANISOU  672  N   THR A  80     3550   2553   3515   -238    288    -54       N
ATOM    673  CA  THR A  80       6.011 -18.681   9.392  1.00 25.58           C
ANISOU  673  CA  THR A  80     3531   2618   3572   -198    279    -52       C
ATOM    674  C   THR A  80       7.419 -19.013   9.859  1.00 27.91           C
ANISOU  674  C   THR A  80     3829   2891   3884   -173    239    -29       C
ATOM    675  O   THR A  80       7.651 -19.363  11.018  1.00 28.79           O
ANISOU  675  O   THR A  80     3986   2967   3986   -188    212    -10       O
ATOM    676  CB  THR A  80       5.895 -17.169   9.206  1.00 27.14           C
ANISOU  676  CB  THR A  80     3695   2854   3761   -205    293    -48       C
ATOM    677  OG1 THR A  80       6.428 -16.508  10.361  1.00 30.28           O
ANISOU  677  OG1 THR A  80     4113   3242   4150   -220    271    -22       O
ATOM    678  CG2 THR A  80       4.440 -16.753   9.002  1.00 21.88           C
ANISOU  678  CG2 THR A  80     3029   2204   3079   -231    326    -70       C
ATOM    679  N   ASP A  81       8.351 -18.919   8.917  1.00 29.99           N
ANISOU  679  N   ASP A  81     4044   3178   4174   -136    235    -33       N
ATOM    680  CA  ASP A  81       9.759 -18.788   9.239  1.00 29.85           C
ANISOU  680  CA  ASP A  81     4008   3156   4179   -111    200    -14       C
ATOM    681  C   ASP A  81       9.928 -17.614  10.203  1.00 32.66           C
ANISOU  681  C   ASP A  81     4371   3520   4519   -136    186     10       C
ATOM    682  O   ASP A  81       9.410 -16.524   9.932  1.00 31.14           O
ANISOU  682  O   ASP A  81     4161   3358   4311   -153    211      7       O
ATOM    683  CB  ASP A  81      10.545 -18.554   7.942  1.00 28.19           C
ANISOU  683  CB  ASP A  81     3736   2981   3996    -76    214    -28       C
ATOM    684  CG  ASP A  81      12.047 -18.739   8.098  1.00 30.22           C
ANISOU  684  CG  ASP A  81     3963   3231   4287    -44    180    -17       C
ATOM    685  OD1 ASP A  81      12.637 -18.169   9.034  1.00 34.43           O
ANISOU  685  OD1 ASP A  81     4501   3760   4822    -53    149      6       O
ATOM    686  OD2 ASP A  81      12.646 -19.437   7.254  1.00 30.01           O
ANISOU  686  OD2 ASP A  81     3908   3206   4289     -9    184    -34       O
ATOM    687  N   PRO A  82      10.591 -17.801  11.346  1.00 34.15           N
ANISOU  687  N   PRO A  82     4589   3677   4708   -140    144     33       N
ATOM    688  CA  PRO A  82      10.742 -16.682  12.290  1.00 30.88           C
ANISOU  688  CA  PRO A  82     4187   3269   4276   -167    130     55       C
ATOM    689  C   PRO A  82      11.547 -15.511  11.735  1.00 33.12           C
ANISOU  689  C   PRO A  82     4413   3595   4576   -155    133     59       C
ATOM    690  O   PRO A  82      11.505 -14.431  12.331  1.00 31.97           O
ANISOU  690  O   PRO A  82     4275   3460   4413   -180    131     73       O
ATOM    691  CB  PRO A  82      11.439 -17.322  13.500  1.00 32.18           C
ANISOU  691  CB  PRO A  82     4397   3388   4442   -167     77     78       C
ATOM    692  CG  PRO A  82      12.005 -18.603  12.999  1.00 40.21           C
ANISOU  692  CG  PRO A  82     5404   4383   5490   -128     58     69       C
ATOM    693  CD  PRO A  82      11.095 -19.066  11.904  1.00 37.36           C
ANISOU  693  CD  PRO A  82     5031   4037   5128   -124    106     40       C
ATOM    694  N   ARG A  83      12.263 -15.684  10.620  1.00 34.31           N
ANISOU  694  N   ARG A  83     4509   3768   4758   -121    141     46       N
ATOM    695  CA  ARG A  83      12.919 -14.571   9.939  1.00 34.98           C
ANISOU  695  CA  ARG A  83     4541   3896   4855   -115    153     45       C
ATOM    696  C   ARG A  83      11.953 -13.722   9.123  1.00 35.67           C
ANISOU  696  C   ARG A  83     4620   4015   4919   -130    199     32       C
ATOM    697  O   ARG A  83      12.360 -12.680   8.593  1.00 33.79           O
ANISOU  697  O   ARG A  83     4348   3809   4682   -132    212     33       O
ATOM    698  CB  ARG A  83      14.024 -15.095   9.022  1.00 33.54           C
ANISOU  698  CB  ARG A  83     4304   3725   4713    -75    151     32       C
ATOM    699  CG  ARG A  83      15.197 -15.712   9.749  1.00 35.14           C
ANISOU  699  CG  ARG A  83     4500   3902   4947    -54    101     45       C
ATOM    700  CD  ARG A  83      16.127 -16.419   8.779  1.00 35.11           C
ANISOU  700  CD  ARG A  83     4445   3909   4989    -11    105     24       C
ATOM    701  NE  ARG A  83      15.429 -17.388   7.935  1.00 33.28           N
ANISOU  701  NE  ARG A  83     4224   3667   4753      5    135      1       N
ATOM    702  CZ  ARG A  83      15.946 -17.928   6.832  1.00 37.18           C
ANISOU  702  CZ  ARG A  83     4677   4174   5276     38    156    -24       C
ATOM    703  NH1 ARG A  83      17.168 -17.594   6.435  1.00 39.61           N
ANISOU  703  NH1 ARG A  83     4925   4506   5621     59    154    -29       N
ATOM    704  NH2 ARG A  83      15.243 -18.796   6.116  1.00 36.12           N
ANISOU  704  NH2 ARG A  83     4560   4029   5135     49    181    -44       N
ATOM    705  N   ASP A  84      10.686 -14.133   9.015  1.00 31.13           N
ANISOU  705  N   ASP A  84     4074   3430   4323   -142    221     18       N
ATOM    706  CA  ASP A  84       9.707 -13.490   8.137  1.00 30.37           C
ANISOU  706  CA  ASP A  84     3968   3362   4210   -151    259      1       C
ATOM    707  C   ASP A  84       8.402 -13.375   8.930  1.00 29.10           C
ANISOU  707  C   ASP A  84     3850   3186   4021   -182    269     -0       C
ATOM    708  O   ASP A  84       7.457 -14.155   8.768  1.00 30.48           O
ANISOU  708  O   ASP A  84     4043   3348   4190   -188    284    -18       O
ATOM    709  CB  ASP A  84       9.538 -14.281   6.841  1.00 29.10           C
ANISOU  709  CB  ASP A  84     3785   3210   4060   -126    281    -24       C
ATOM    710  CG  ASP A  84       8.617 -13.605   5.860  1.00 31.60           C
ANISOU  710  CG  ASP A  84     4092   3555   4359   -132    312    -41       C
ATOM    711  OD1 ASP A  84       8.409 -12.379   5.995  1.00 30.31           O
ANISOU  711  OD1 ASP A  84     3926   3409   4181   -147    317    -32       O
ATOM    712  OD2 ASP A  84       8.102 -14.302   4.956  1.00 27.18           O
ANISOU  712  OD2 ASP A  84     3529   2997   3801   -120    329    -63       O
ATOM    713  N   VAL A  85       8.351 -12.381   9.817  1.00 28.57           N
ANISOU  713  N   VAL A  85     3799   3119   3937   -206    262     16       N
ATOM    714  CA  VAL A  85       7.271 -12.262  10.785  1.00 30.09           C
ANISOU  714  CA  VAL A  85     4035   3293   4105   -239    271     16       C
ATOM    715  C   VAL A  85       6.578 -10.910  10.741  1.00 30.91           C
ANISOU  715  C   VAL A  85     4134   3420   4192   -255    292     12       C
ATOM    716  O   VAL A  85       5.642 -10.688  11.506  1.00 34.81           O
ANISOU  716  O   VAL A  85     4657   3901   4667   -282    305      7       O
ATOM    717  CB  VAL A  85       7.777 -12.551  12.213  1.00 29.99           C
ANISOU  717  CB  VAL A  85     4065   3245   4084   -257    239     39       C
ATOM    718  CG1 VAL A  85       8.120 -14.044  12.373  1.00 28.37           C
ANISOU  718  CG1 VAL A  85     3880   3008   3892   -244    218     39       C
ATOM    719  CG2 VAL A  85       8.991 -11.708  12.519  1.00 32.56           C
ANISOU  719  CG2 VAL A  85     4374   3580   4416   -252    211     62       C
ATOM    720  N   ALA A  86       6.987 -10.002   9.859  1.00 24.82           N
ANISOU  720  N   ALA A  86     3327   2679   3426   -240    297     12       N
ATOM    721  CA  ALA A  86       6.415  -8.664   9.861  1.00 22.21           C
ANISOU  721  CA  ALA A  86     2996   2365   3078   -253    312     11       C
ATOM    722  C   ALA A  86       6.745  -7.954   8.557  1.00 21.85           C
ANISOU  722  C   ALA A  86     2914   2350   3038   -233    320      6       C
ATOM    723  O   ALA A  86       7.702  -8.297   7.859  1.00 23.62           O
ANISOU  723  O   ALA A  86     3113   2584   3277   -214    314      9       O
ATOM    724  CB  ALA A  86       6.933  -7.836  11.038  1.00 26.67           C
ANISOU  724  CB  ALA A  86     3584   2918   3630   -275    294     35       C
ATOM    725  N   ARG A  87       5.924  -6.958   8.239  1.00 31.64           N
ANISOU  725  N   ARG A  87     4154   3603   4263   -238    336     -3       N
ATOM    726  CA  ARG A  87       6.339  -5.930   7.293  1.00 28.98           C
ANISOU  726  CA  ARG A  87     3798   3291   3922   -227    339      1       C
ATOM    727  C   ARG A  87       7.729  -5.438   7.680  1.00 27.42           C
ANISOU  727  C   ARG A  87     3595   3095   3729   -233    322     26       C
ATOM    728  O   ARG A  87       8.009  -5.219   8.860  1.00 27.41           O
ANISOU  728  O   ARG A  87     3614   3078   3723   -252    307     42       O
ATOM    729  CB  ARG A  87       5.320  -4.790   7.328  1.00 23.99           C
ANISOU  729  CB  ARG A  87     3179   2664   3274   -235    349     -7       C
ATOM    730  CG  ARG A  87       5.551  -3.682   6.361  1.00 25.09           C
ANISOU  730  CG  ARG A  87     3309   2822   3403   -226    352     -4       C
ATOM    731  CD  ARG A  87       4.410  -2.674   6.399  1.00 24.90           C
ANISOU  731  CD  ARG A  87     3299   2797   3365   -228    358    -15       C
ATOM    732  NE  ARG A  87       4.054  -2.275   7.759  1.00 27.16           N
ANISOU  732  NE  ARG A  87     3609   3066   3646   -248    357    -10       N
ATOM    733  CZ  ARG A  87       4.756  -1.424   8.499  1.00 25.63           C
ANISOU  733  CZ  ARG A  87     3432   2866   3441   -265    349     11       C
ATOM    734  NH1 ARG A  87       5.860  -0.884   8.017  1.00 24.58           N
ANISOU  734  NH1 ARG A  87     3290   2743   3304   -264    340     29       N
ATOM    735  NH2 ARG A  87       4.361  -1.116   9.728  1.00 23.12           N
ANISOU  735  NH2 ARG A  87     3140   2530   3116   -285    350     13       N
ATOM    736  N   ILE A  88       8.621  -5.289   6.700  1.00 23.08           N
ANISOU  736  N   ILE A  88     3018   2565   3187   -220    325     28       N
ATOM    737  CA  ILE A  88      10.010  -4.947   6.995  1.00 26.70           C
ANISOU  737  CA  ILE A  88     3461   3028   3656   -226    310     47       C
ATOM    738  C   ILE A  88      10.363  -3.664   6.239  1.00 33.99           C
ANISOU  738  C   ILE A  88     4377   3973   4566   -233    322     52       C
ATOM    739  O   ILE A  88      10.574  -3.659   5.019  1.00 36.99           O
ANISOU  739  O   ILE A  88     4738   4371   4946   -221    339     42       O
ATOM    740  CB  ILE A  88      10.968  -6.110   6.705  1.00 30.19           C
ANISOU  740  CB  ILE A  88     3874   3470   4127   -208    303     44       C
ATOM    741  CG1 ILE A  88      12.410  -5.742   7.060  1.00 36.77           C
ANISOU  741  CG1 ILE A  88     4683   4309   4976   -214    285     62       C
ATOM    742  CG2 ILE A  88      10.810  -6.690   5.280  1.00 35.06           C
ANISOU  742  CG2 ILE A  88     4470   4103   4749   -185    327     22       C
ATOM    743  CD1 ILE A  88      13.307  -6.970   7.158  1.00 36.94           C
ANISOU  743  CD1 ILE A  88     4680   4323   5032   -194    268     59       C
ATOM    744  N   GLU A  89      10.419  -2.562   6.987  1.00 26.18           N
ANISOU  744  N   GLU A  89     3407   2978   3561   -254    313     68       N
ATOM    745  CA  GLU A  89      10.562  -1.229   6.403  1.00 29.32           C
ANISOU  745  CA  GLU A  89     3810   3389   3940   -265    323     73       C
ATOM    746  C   GLU A  89      11.929  -1.042   5.752  1.00 36.01           C
ANISOU  746  C   GLU A  89     4627   4256   4800   -268    327     80       C
ATOM    747  O   GLU A  89      12.043  -0.382   4.712  1.00 35.08           O
ANISOU  747  O   GLU A  89     4507   4153   4668   -270    345     76       O
ATOM    748  CB  GLU A  89      10.330  -0.185   7.495  1.00 27.03           C
ANISOU  748  CB  GLU A  89     3551   3085   3633   -288    311     88       C
ATOM    749  CG  GLU A  89      10.321   1.272   7.036  1.00 39.42           C
ANISOU  749  CG  GLU A  89     5138   4661   5179   -300    318     94       C
ATOM    750  CD  GLU A  89       9.856   2.234   8.141  1.00 53.00           C
ANISOU  750  CD  GLU A  89     6895   6363   6881   -319    309    103       C
ATOM    751  OE1 GLU A  89       9.860   3.466   7.914  1.00 59.40           O
ANISOU  751  OE1 GLU A  89     7724   7173   7672   -330    311    110       O
ATOM    752  OE2 GLU A  89       9.482   1.760   9.236  1.00 55.28           O
ANISOU  752  OE2 GLU A  89     7197   6634   7173   -325    299    104       O
ATOM    753  N   SER A  90      12.976  -1.617   6.347  1.00 34.62           N
ANISOU  753  N   SER A  90     4426   4078   4649   -271    310     88       N
ATOM    754  CA  SER A  90      14.328  -1.424   5.832  1.00 43.66           C
ANISOU  754  CA  SER A  90     5534   5243   5812   -276    315     92       C
ATOM    755  C   SER A  90      14.482  -1.967   4.417  1.00 49.02           C
ANISOU  755  C   SER A  90     6188   5940   6498   -257    344     72       C
ATOM    756  O   SER A  90      15.328  -1.485   3.657  1.00 55.58           O
ANISOU  756  O   SER A  90     6996   6790   7330   -267    363     71       O
ATOM    757  CB  SER A  90      15.342  -2.083   6.770  1.00 41.47           C
ANISOU  757  CB  SER A  90     5232   4959   5567   -276    285    101       C
ATOM    758  OG  SER A  90      15.035  -3.453   6.984  1.00 48.18           O
ANISOU  758  OG  SER A  90     6078   5794   6434   -251    275     92       O
ATOM    759  N   LYS A  91      13.687  -2.968   4.047  1.00 38.93           N
ANISOU  759  N   LYS A  91     4914   4655   5222   -233    350     56       N
ATOM    760  CA  LYS A  91      13.728  -3.547   2.713  1.00 34.58           C
ANISOU  760  CA  LYS A  91     4347   4119   4675   -215    377     36       C
ATOM    761  C   LYS A  91      12.660  -2.968   1.791  1.00 27.76           C
ANISOU  761  C   LYS A  91     3514   3259   3776   -214    395     28       C
ATOM    762  O   LYS A  91      12.406  -3.536   0.725  1.00 27.36           O
ANISOU  762  O   LYS A  91     3459   3214   3721   -198    414      9       O
ATOM    763  CB  LYS A  91      13.574  -5.066   2.796  1.00 33.04           C
ANISOU  763  CB  LYS A  91     4137   3912   4503   -188    372     22       C
ATOM    764  CG  LYS A  91      14.443  -5.738   3.841  1.00 36.22           C
ANISOU  764  CG  LYS A  91     4519   4304   4940   -184    344     32       C
ATOM    765  CD  LYS A  91      15.898  -5.799   3.427  1.00 44.47           C
ANISOU  765  CD  LYS A  91     5515   5366   6015   -181    351     28       C
ATOM    766  CE  LYS A  91      16.672  -6.764   4.321  1.00 47.13           C
ANISOU  766  CE  LYS A  91     5829   5688   6392   -165    318     32       C
ATOM    767  NZ  LYS A  91      18.062  -6.990   3.839  1.00 53.62           N
ANISOU  767  NZ  LYS A  91     6594   6528   7252   -155    326     21       N
ATOM    768  N   THR A  92      12.015  -1.875   2.186  1.00 25.12           N
ANISOU  768  N   THR A  92     3211   2917   3416   -229    387     39       N
ATOM    769  CA  THR A  92      10.932  -1.269   1.415  1.00 24.64           C
ANISOU  769  CA  THR A  92     3181   2856   3325   -225    395     31       C
ATOM    770  C   THR A  92      11.415   0.027   0.781  1.00 29.27           C
ANISOU  770  C   THR A  92     3783   3452   3886   -245    406     41       C
ATOM    771  O   THR A  92      11.956   0.892   1.477  1.00 27.72           O
ANISOU  771  O   THR A  92     3592   3253   3687   -267    398     59       O
ATOM    772  CB  THR A  92       9.713  -1.006   2.297  1.00 23.18           C
ANISOU  772  CB  THR A  92     3023   2654   3132   -225    377     32       C
ATOM    773  OG1 THR A  92       9.261  -2.257   2.842  1.00 22.49           O
ANISOU  773  OG1 THR A  92     2925   2556   3064   -212    371     22       O
ATOM    774  CG2 THR A  92       8.589  -0.384   1.486  1.00 19.13           C
ANISOU  774  CG2 THR A  92     2537   2140   2593   -216    380     21       C
ATOM    775  N   VAL A  93      11.209   0.155  -0.538  1.00 25.09           N
ANISOU  775  N   VAL A  93     3267   2932   3336   -239    424     30       N
ATOM    776  CA  VAL A  93      11.757   1.248  -1.335  1.00 21.74           C
ANISOU  776  CA  VAL A  93     2862   2515   2884   -260    440     38       C
ATOM    777  C   VAL A  93      10.705   1.744  -2.325  1.00 20.15           C
ANISOU  777  C   VAL A  93     2702   2306   2646   -250    438     30       C
ATOM    778  O   VAL A  93       9.785   1.021  -2.705  1.00 25.24           O
ANISOU  778  O   VAL A  93     3349   2948   3292   -226    432     14       O
ATOM    779  CB  VAL A  93      13.037   0.817  -2.106  1.00 23.09           C
ANISOU  779  CB  VAL A  93     3001   2705   3066   -269    470     31       C
ATOM    780  CG1 VAL A  93      14.171   0.452  -1.154  1.00 23.45           C
ANISOU  780  CG1 VAL A  93     3001   2757   3150   -277    466     38       C
ATOM    781  CG2 VAL A  93      12.740  -0.363  -3.034  1.00 19.32           C
ANISOU  781  CG2 VAL A  93     2514   2234   2594   -244    485      8       C
ATOM    782  N   ILE A  94      10.871   2.990  -2.775  1.00 19.70           N
ANISOU  782  N   ILE A  94     2681   2246   2557   -269    442     42       N
ATOM    783  CA  ILE A  94      10.061   3.544  -3.857  1.00 21.20           C
ANISOU  783  CA  ILE A  94     2917   2428   2709   -261    438     36       C
ATOM    784  C   ILE A  94      11.007   4.074  -4.925  1.00 22.46           C
ANISOU  784  C   ILE A  94     3097   2597   2841   -287    466     41       C
ATOM    785  O   ILE A  94      12.027   4.688  -4.603  1.00 22.26           O
ANISOU  785  O   ILE A  94     3065   2578   2817   -317    480     54       O
ATOM    786  CB  ILE A  94       9.112   4.650  -3.359  1.00 22.25           C
ANISOU  786  CB  ILE A  94     3088   2540   2825   -257    409     46       C
ATOM    787  CG1 ILE A  94       8.045   4.052  -2.418  1.00 20.82           C
ANISOU  787  CG1 ILE A  94     2888   2352   2672   -233    387     36       C
ATOM    788  CG2 ILE A  94       8.458   5.383  -4.522  1.00 19.93           C
ANISOU  788  CG2 ILE A  94     2847   2235   2490   -251    400     44       C
ATOM    789  CD1 ILE A  94       7.113   5.089  -1.855  1.00 24.48           C
ANISOU  789  CD1 ILE A  94     3383   2796   3125   -227    363     40       C
ATOM    790  N   ILE A  95      10.683   3.819  -6.191  1.00 17.47           N
ANISOU  790  N   ILE A  95     2489   1966   2182   -279    476     28       N
ATOM    791  CA  ILE A  95      11.565   4.149  -7.313  1.00 21.02           C
ANISOU  791  CA  ILE A  95     2960   2424   2602   -305    510     27       C
ATOM    792  C   ILE A  95      10.975   5.332  -8.067  1.00 20.74           C
ANISOU  792  C   ILE A  95     2997   2368   2513   -314    496     37       C
ATOM    793  O   ILE A  95       9.848   5.254  -8.577  1.00 23.56           O
ANISOU  793  O   ILE A  95     3385   2713   2852   -288    469     29       O
ATOM    794  CB  ILE A  95      11.764   2.956  -8.260  1.00 21.82           C
ANISOU  794  CB  ILE A  95     3044   2539   2707   -294    536      4       C
ATOM    795  CG1 ILE A  95      12.652   1.893  -7.617  1.00 30.84           C
ANISOU  795  CG1 ILE A  95     4117   3700   3900   -290    556     -4       C
ATOM    796  CG2 ILE A  95      12.395   3.420  -9.567  1.00 28.94           C
ANISOU  796  CG2 ILE A  95     3985   3444   3565   -322    572      2       C
ATOM    797  CD1 ILE A  95      11.912   0.898  -6.746  1.00 23.94           C
ANISOU  797  CD1 ILE A  95     3211   2821   3064   -258    528    -12       C
ATOM    798  N   THR A  96      11.742   6.423  -8.150  1.00 23.50           N
ANISOU  798  N   THR A  96     3375   2715   2839   -350    511     54       N
ATOM    799  CA  THR A  96      11.433   7.552  -9.018  1.00 22.37           C
ANISOU  799  CA  THR A  96     3308   2550   2640   -365    504     64       C
ATOM    800  C   THR A  96      12.732   8.031  -9.657  1.00 23.40           C
ANISOU  800  C   THR A  96     3454   2691   2745   -413    551     70       C
ATOM    801  O   THR A  96      13.824   7.799  -9.131  1.00 24.24           O
ANISOU  801  O   THR A  96     3508   2818   2883   -436    580     70       O
ATOM    802  CB  THR A  96      10.773   8.720  -8.261  1.00 23.53           C
ANISOU  802  CB  THR A  96     3490   2673   2778   -360    465     83       C
ATOM    803  OG1 THR A  96      11.602   9.091  -7.153  1.00 25.61           O
ANISOU  803  OG1 THR A  96     3721   2943   3068   -385    475     96       O
ATOM    804  CG2 THR A  96       9.384   8.326  -7.748  1.00 29.30           C
ANISOU  804  CG2 THR A  96     4210   3393   3531   -313    422     73       C
ATOM    805  N   GLN A  97      12.608   8.719 -10.794  1.00 28.05           N
ANISOU  805  N   GLN A  97     4116   3264   3277   -431    556     74       N
ATOM    806  CA  GLN A  97      13.802   9.266 -11.443  1.00 30.30           C
ANISOU  806  CA  GLN A  97     4424   3556   3533   -484    605     79       C
ATOM    807  C   GLN A  97      14.518  10.265 -10.537  1.00 31.45           C
ANISOU  807  C   GLN A  97     4563   3699   3687   -518    609     99       C
ATOM    808  O   GLN A  97      15.750  10.249 -10.440  1.00 33.81           O
ANISOU  808  O   GLN A  97     4825   4019   4002   -557    652     96       O
ATOM    809  CB  GLN A  97      13.434   9.913 -12.780  1.00 30.53           C
ANISOU  809  CB  GLN A  97     4548   3561   3491   -499    605     82       C
ATOM    810  CG  GLN A  97      14.608  10.616 -13.511  1.00 37.68           C
ANISOU  810  CG  GLN A  97     5492   4469   4356   -561    660     88       C
ATOM    811  CD  GLN A  97      15.802   9.695 -13.770  1.00 41.10           C
ANISOU  811  CD  GLN A  97     5859   4938   4817   -585    724     66       C
ATOM    812  OE1 GLN A  97      15.642   8.487 -13.975  1.00 41.12           O
ANISOU  812  OE1 GLN A  97     5818   4959   4848   -554    731     44       O
ATOM    813  NE2 GLN A  97      17.007  10.266 -13.753  1.00 38.58           N
ANISOU  813  NE2 GLN A  97     5531   4631   4496   -639    771     70       N
ATOM    814  N   GLU A  98      13.768  11.125  -9.851  1.00 27.95           N
ANISOU  814  N   GLU A  98     4152   3230   3237   -505    564    116       N
ATOM    815  CA  GLU A  98      14.323  12.114  -8.931  1.00 23.78           C
ANISOU  815  CA  GLU A  98     3625   2695   2715   -536    561    135       C
ATOM    816  C   GLU A  98      14.015  11.711  -7.495  1.00 22.47           C
ANISOU  816  C   GLU A  98     3398   2535   2604   -507    532    136       C
ATOM    817  O   GLU A  98      12.859  11.441  -7.171  1.00 21.08           O
ANISOU  817  O   GLU A  98     3225   2347   2438   -463    494    132       O
ATOM    818  CB  GLU A  98      13.728  13.493  -9.205  1.00 28.62           C
ANISOU  818  CB  GLU A  98     4330   3268   3275   -545    533    154       C
ATOM    819  CG  GLU A  98      14.018  14.020 -10.591  1.00 42.21           C
ANISOU  819  CG  GLU A  98     6127   4976   4934   -578    558    157       C
ATOM    820  CD  GLU A  98      15.225  14.928 -10.607  1.00 51.32           C
ANISOU  820  CD  GLU A  98     7301   6130   6066   -644    597    170       C
ATOM    821  OE1 GLU A  98      15.447  15.622  -9.590  1.00 48.52           O
ANISOU  821  OE1 GLU A  98     6939   5769   5729   -658    583    185       O
ATOM    822  OE2 GLU A  98      15.950  14.943 -11.627  1.00 54.54           O
ANISOU  822  OE2 GLU A  98     7735   6546   6441   -685    643    165       O
ATOM    823  N   GLN A  99      15.042  11.703  -6.635  1.00 19.33           N
ANISOU  823  N   GLN A  99     2949   2155   2240   -535    549    140       N
ATOM    824  CA  GLN A  99      14.839  11.320  -5.244  1.00 22.02           C
ANISOU  824  CA  GLN A  99     3238   2500   2628   -512    522    142       C
ATOM    825  C   GLN A  99      13.840  12.241  -4.551  1.00 19.76           C
ANISOU  825  C   GLN A  99     2999   2181   2326   -496    480    156       C
ATOM    826  O   GLN A  99      13.055  11.791  -3.705  1.00 21.84           O
ANISOU  826  O   GLN A  99     3239   2441   2618   -461    452    151       O
ATOM    827  CB  GLN A  99      16.165  11.333  -4.475  1.00 21.56           C
ANISOU  827  CB  GLN A  99     3126   2462   2603   -549    542    147       C
ATOM    828  CG  GLN A  99      15.964  11.028  -2.980  1.00 22.51           C
ANISOU  828  CG  GLN A  99     3206   2582   2765   -530    509    152       C
ATOM    829  CD  GLN A  99      17.260  10.815  -2.217  1.00 30.97           C
ANISOU  829  CD  GLN A  99     4216   3676   3876   -560    521    153       C
ATOM    830  OE1 GLN A  99      18.349  11.126  -2.706  1.00 35.21           O
ANISOU  830  OE1 GLN A  99     4741   4228   4409   -601    553    152       O
ATOM    831  NE2 GLN A  99      17.148  10.258  -1.018  1.00 27.29           N
ANISOU  831  NE2 GLN A  99     3711   3211   3447   -541    493    155       N
ATOM    832  N   ARG A 100      13.859  13.531  -4.896  1.00 20.70           N
ANISOU  832  N   ARG A 100     3186   2276   2401   -523    477    171       N
ATOM    833  CA  ARG A 100      13.015  14.503  -4.214  1.00 20.24           C
ANISOU  833  CA  ARG A 100     3175   2186   2331   -509    439    183       C
ATOM    834  C   ARG A 100      11.531  14.255  -4.453  1.00 23.04           C
ANISOU  834  C   ARG A 100     3550   2523   2682   -454    404    172       C
ATOM    835  O   ARG A 100      10.700  14.734  -3.673  1.00 27.17           O
ANISOU  835  O   ARG A 100     4087   3024   3211   -431    373    174       O
ATOM    836  CB  ARG A 100      13.396  15.919  -4.667  1.00 21.51           C
ANISOU  836  CB  ARG A 100     3410   2320   2442   -550    444    201       C
ATOM    837  CG  ARG A 100      12.787  17.049  -3.823  1.00 29.08           C
ANISOU  837  CG  ARG A 100     4416   3243   3390   -543    409    215       C
ATOM    838  CD  ARG A 100      13.102  18.433  -4.418  1.00 37.58           C
ANISOU  838  CD  ARG A 100     5577   4289   4412   -582    412    232       C
ATOM    839  NE  ARG A 100      12.391  19.506  -3.715  1.00 42.35           N
ANISOU  839  NE  ARG A 100     6233   4854   5004   -569    376    243       N
ATOM    840  CZ  ARG A 100      12.525  20.804  -3.984  1.00 48.03           C
ANISOU  840  CZ  ARG A 100     7033   5537   5679   -597    369    259       C
ATOM    841  NH1 ARG A 100      13.347  21.204  -4.945  1.00 46.81           N
ANISOU  841  NH1 ARG A 100     6919   5383   5485   -645    399    269       N
ATOM    842  NH2 ARG A 100      11.836  21.708  -3.291  1.00 39.87           N
ANISOU  842  NH2 ARG A 100     6042   4467   4639   -579    336    265       N
ATOM    843  N   ASP A 101      11.165  13.528  -5.511  1.00 22.73           N
ANISOU  843  N   ASP A 101     3511   2492   2633   -433    410    158       N
ATOM    844  CA  ASP A 101       9.752  13.230  -5.666  1.00 20.57           C
ANISOU  844  CA  ASP A 101     3248   2204   2362   -382    374    146       C
ATOM    845  C   ASP A 101       9.284  12.207  -4.638  1.00 24.23           C
ANISOU  845  C   ASP A 101     3643   2685   2879   -352    365    132       C
ATOM    846  O   ASP A 101       8.084  12.131  -4.360  1.00 29.22           O
ANISOU  846  O   ASP A 101     4277   3304   3522   -313    334    121       O
ATOM    847  CB  ASP A 101       9.457  12.732  -7.075  1.00 24.65           C
ANISOU  847  CB  ASP A 101     3789   2725   2853   -370    377    134       C
ATOM    848  CG  ASP A 101       9.710  13.793  -8.120  1.00 34.40           C
ANISOU  848  CG  ASP A 101     5108   3936   4028   -397    380    148       C
ATOM    849  OD1 ASP A 101      10.230  13.457  -9.195  1.00 39.19           O
ANISOU  849  OD1 ASP A 101     5731   4553   4608   -417    408    144       O
ATOM    850  OD2 ASP A 101       9.418  14.974  -7.839  1.00 39.99           O
ANISOU  850  OD2 ASP A 101     5868   4613   4714   -400    356    163       O
ATOM    851  N   THR A 102      10.206  11.438  -4.063  1.00 19.63           N
ANISOU  851  N   THR A 102     3001   2128   2328   -370    391    131       N
ATOM    852  CA  THR A 102       9.870  10.351  -3.142  1.00 18.37           C
ANISOU  852  CA  THR A 102     2781   1983   2215   -345    385    118       C
ATOM    853  C   THR A 102      10.043  10.722  -1.674  1.00 26.44           C
ANISOU  853  C   THR A 102     3787   2998   3259   -356    375    129       C
ATOM    854  O   THR A 102       9.231  10.303  -0.837  1.00 21.53           O
ANISOU  854  O   THR A 102     3146   2372   2662   -331    358    120       O
ATOM    855  CB  THR A 102      10.719   9.118  -3.470  1.00 20.81           C
ANISOU  855  CB  THR A 102     3036   2322   2548   -352    414    108       C
ATOM    856  OG1 THR A 102      10.236   8.537  -4.690  1.00 23.89           O
ANISOU  856  OG1 THR A 102     3439   2716   2922   -332    418     93       O
ATOM    857  CG2 THR A 102      10.667   8.058  -2.337  1.00 20.16           C
ANISOU  857  CG2 THR A 102     2895   2252   2514   -336    408    101       C
ATOM    858  N   VAL A 103      11.098  11.465  -1.343  1.00 22.40           N
ANISOU  858  N   VAL A 103     3284   2487   2740   -396    387    146       N
ATOM    859  CA  VAL A 103      11.308  12.005   0.004  1.00 17.84           C
ANISOU  859  CA  VAL A 103     2704   1899   2175   -412    374    158       C
ATOM    860  C   VAL A 103      11.827  13.418  -0.114  1.00 24.66           C
ANISOU  860  C   VAL A 103     3620   2746   3005   -448    376    176       C
ATOM    861  O   VAL A 103      12.479  13.779  -1.103  1.00 24.03           O
ANISOU  861  O   VAL A 103     3561   2670   2899   -473    396    181       O
ATOM    862  CB  VAL A 103      12.320  11.166   0.816  1.00 20.21           C
ANISOU  862  CB  VAL A 103     2943   2223   2512   -429    385    159       C
ATOM    863  CG1 VAL A 103      11.762   9.806   1.119  1.00 18.61           C
ANISOU  863  CG1 VAL A 103     2697   2031   2343   -395    380    143       C
ATOM    864  CG2 VAL A 103      13.665  11.058   0.064  1.00 22.90           C
ANISOU  864  CG2 VAL A 103     3262   2587   2852   -463    415    162       C
ATOM    865  N   PRO A 104      11.575  14.248   0.895  1.00 21.15           N
ANISOU  865  N   PRO A 104     3200   2279   2557   -454    358    185       N
ATOM    866  CA  PRO A 104      12.262  15.541   0.949  1.00 25.43           C
ANISOU  866  CA  PRO A 104     3788   2805   3070   -496    361    203       C
ATOM    867  C   PRO A 104      13.752  15.321   1.137  1.00 23.31           C
ANISOU  867  C   PRO A 104     3479   2562   2817   -542    383    211       C
ATOM    868  O   PRO A 104      14.184  14.365   1.785  1.00 23.58           O
ANISOU  868  O   PRO A 104     3453   2618   2888   -539    385    206       O
ATOM    869  CB  PRO A 104      11.645  16.237   2.176  1.00 21.57           C
ANISOU  869  CB  PRO A 104     3324   2288   2583   -489    336    207       C
ATOM    870  CG  PRO A 104      10.404  15.451   2.492  1.00 21.73           C
ANISOU  870  CG  PRO A 104     3322   2307   2626   -439    322    188       C
ATOM    871  CD  PRO A 104      10.682  14.043   2.053  1.00 21.72           C
ANISOU  871  CD  PRO A 104     3262   2339   2651   -428    337    178       C
ATOM    872  N   ILE A 105      14.544  16.203   0.544  1.00 22.78           N
ANISOU  872  N   ILE A 105     3446   2491   2720   -585    400    223       N
ATOM    873  CA  ILE A 105      15.991  16.092   0.710  1.00 27.38           C
ANISOU  873  CA  ILE A 105     3986   3099   3320   -632    423    228       C
ATOM    874  C   ILE A 105      16.332  16.676   2.076  1.00 26.79           C
ANISOU  874  C   ILE A 105     3911   3013   3256   -656    402    240       C
ATOM    875  O   ILE A 105      16.120  17.876   2.302  1.00 25.13           O
ANISOU  875  O   ILE A 105     3762   2773   3014   -674    391    252       O
ATOM    876  CB  ILE A 105      16.746  16.789  -0.432  1.00 31.95           C
ANISOU  876  CB  ILE A 105     4598   3678   3863   -675    454    233       C
ATOM    877  CG1 ILE A 105      16.396  16.129  -1.767  1.00 32.21           C
ANISOU  877  CG1 ILE A 105     4634   3722   3883   -652    474    220       C
ATOM    878  CG2 ILE A 105      18.248  16.739  -0.185  1.00 30.61           C
ANISOU  878  CG2 ILE A 105     4377   3536   3716   -727    478    235       C
ATOM    879  CD1 ILE A 105      16.665  14.629  -1.790  1.00 29.84           C
ANISOU  879  CD1 ILE A 105     4253   3457   3628   -628    487    202       C
ATOM    880  N   PRO A 106      16.833  15.876   3.018  1.00 23.84           N
ANISOU  880  N   PRO A 106     3476   2659   2923   -655    394    237       N
ATOM    881  CA  PRO A 106      16.997  16.373   4.390  1.00 26.21           C
ANISOU  881  CA  PRO A 106     3784   2944   3231   -674    368    248       C
ATOM    882  C   PRO A 106      18.129  17.384   4.491  1.00 27.90           C
ANISOU  882  C   PRO A 106     4012   3158   3431   -734    376    261       C
ATOM    883  O   PRO A 106      19.059  17.404   3.677  1.00 26.33           O
ANISOU  883  O   PRO A 106     3792   2980   3233   -766    404    259       O
ATOM    884  CB  PRO A 106      17.304  15.105   5.202  1.00 28.59           C
ANISOU  884  CB  PRO A 106     4017   3269   3579   -657    356    241       C
ATOM    885  CG  PRO A 106      16.995  13.948   4.279  1.00 26.14           C
ANISOU  885  CG  PRO A 106     3669   2979   3284   -620    373    225       C
ATOM    886  CD  PRO A 106      17.210  14.455   2.893  1.00 23.83           C
ANISOU  886  CD  PRO A 106     3402   2690   2963   -636    403    223       C
ATOM    887  N   LYS A 107      18.034  18.244   5.509  1.00 23.88           N
ANISOU  887  N   LYS A 107     3541   2623   2909   -753    353    273       N
ATOM    888  C   LYS A 107      20.376  18.749   6.062  1.00 27.34           C
ANISOU  888  C   LYS A 107     3928   3090   3372   -848    359    284       C
ATOM    889  O   LYS A 107      21.413  19.184   5.539  1.00 28.28           O
ANISOU  889  O   LYS A 107     4033   3223   3488   -896    381    286       O
ATOM    890  CA ALYS A 107      19.021  19.307   5.658  0.44 27.75           C
ANISOU  890  CA ALYS A 107     4053   3107   3383   -814    357    285       C
ATOM    891  CB ALYS A 107      18.545  20.339   6.680  0.44 27.99           C
ANISOU  891  CB ALYS A 107     4145   3099   3389   -823    331    296       C
ATOM    892  CG ALYS A 107      19.327  21.646   6.613  0.44 28.20           C
ANISOU  892  CG ALYS A 107     4217   3110   3387   -885    337    310       C
ATOM    893  CD ALYS A 107      18.888  22.610   7.710  0.44 30.61           C
ANISOU  893  CD ALYS A 107     4583   3376   3670   -894    310    319       C
ATOM    894  CE ALYS A 107      19.563  23.969   7.562  0.44 34.20           C
ANISOU  894  CE ALYS A 107     5094   3810   4091   -955    317    332       C
ATOM    895  NZ ALYS A 107      21.042  23.877   7.684  0.44 39.31           N
ANISOU  895  NZ ALYS A 107     5687   4489   4760  -1014    325    335       N
ATOM    896  CA BLYS A 107      19.020  19.307   5.663  0.56 27.97           C
ANISOU  896  CA BLYS A 107     4081   3136   3411   -814    357    285       C
ATOM    897  CB BLYS A 107      18.552  20.336   6.694  0.56 27.94           C
ANISOU  897  CB BLYS A 107     4139   3093   3384   -824    331    296       C
ATOM    898  CG BLYS A 107      19.554  21.482   6.869  0.56 28.67           C
ANISOU  898  CG BLYS A 107     4260   3177   3457   -890    333    310       C
ATOM    899  CD BLYS A 107      19.103  22.501   7.916  0.56 30.06           C
ANISOU  899  CD BLYS A 107     4500   3312   3608   -900    308    319       C
ATOM    900  CE BLYS A 107      18.072  23.465   7.345  0.56 35.75           C
ANISOU  900  CE BLYS A 107     5305   3992   4285   -880    310    322       C
ATOM    901  NZ BLYS A 107      17.979  24.745   8.124  0.56 36.88           N
ANISOU  901  NZ BLYS A 107     5520   4094   4398   -908    293    332       N
ATOM    902  N   SER A 108      20.389  17.773   6.965  1.00 30.73           N
ANISOU  902  N   SER A 108     4306   3531   3837   -824    335    279       N
ATOM    903  CA  SER A 108      21.648  17.288   7.503  1.00 29.60           C
ANISOU  903  CA  SER A 108     4095   3416   3735   -852    325    278       C
ATOM    904  C   SER A 108      21.712  15.769   7.571  1.00 29.72           C
ANISOU  904  C   SER A 108     4040   3457   3796   -811    320    266       C
ATOM    905  O   SER A 108      22.799  15.196   7.474  1.00 26.28           O
ANISOU  905  O   SER A 108     3535   3050   3398   -826    323    258       O
ATOM    906  CB  SER A 108      21.857  17.869   8.898  1.00 38.40           C
ANISOU  906  CB  SER A 108     5232   4510   4847   -879    288    291       C
ATOM    907  OG  SER A 108      20.786  17.490   9.756  1.00 33.49           O
ANISOU  907  OG  SER A 108     4637   3867   4221   -838    263    292       O
ATOM    908  N   GLY A 109      20.569  15.110   7.769  1.00 26.64           N
ANISOU  908  N   GLY A 109     3664   3054   3403   -761    310    261       N
ATOM    909  CA  GLY A 109      20.535  13.701   8.081  1.00 24.51           C
ANISOU  909  CA  GLY A 109     3339   2800   3173   -723    297    251       C
ATOM    910  C   GLY A 109      20.050  12.828   6.935  1.00 21.00           C
ANISOU  910  C   GLY A 109     2873   2370   2735   -684    325    236       C
ATOM    911  O   GLY A 109      19.844  13.272   5.801  1.00 24.66           O
ANISOU  911  O   GLY A 109     3360   2835   3174   -687    356    232       O
ATOM    912  N   GLN A 110      19.886  11.545   7.253  1.00 22.69           N
ANISOU  912  N   GLN A 110     3046   2593   2981   -647    313    227       N
ATOM    913  CA  GLN A 110      19.303  10.604   6.314  1.00 23.37           C
ANISOU  913  CA  GLN A 110     3115   2690   3075   -607    335    212       C
ATOM    914  C   GLN A 110      17.791  10.673   6.441  1.00 23.55           C
ANISOU  914  C   GLN A 110     3190   2688   3070   -574    329    211       C
ATOM    915  O   GLN A 110      17.258  10.786   7.546  1.00 25.18           O
ANISOU  915  O   GLN A 110     3422   2874   3273   -570    303    217       O
ATOM    916  CB  GLN A 110      19.807   9.185   6.602  1.00 25.55           C
ANISOU  916  CB  GLN A 110     3326   2984   3398   -583    323    202       C
ATOM    917  CG  GLN A 110      19.377   8.120   5.599  1.00 31.89           C
ANISOU  917  CG  GLN A 110     4106   3799   4212   -543    347    183       C
ATOM    918  CD  GLN A 110      20.281   8.068   4.367  1.00 37.25           C
ANISOU  918  CD  GLN A 110     4747   4505   4900   -557    385    171       C
ATOM    919  OE1 GLN A 110      20.917   9.058   4.000  1.00 40.85           O
ANISOU  919  OE1 GLN A 110     5213   4968   5341   -597    403    176       O
ATOM    920  NE2 GLN A 110      20.347   6.900   3.732  1.00 38.29           N
ANISOU  920  NE2 GLN A 110     4838   4652   5057   -526    401    153       N
ATOM    921  N   SER A 111      17.094  10.632   5.309  1.00 23.76           N
ANISOU  921  N   SER A 111     3234   2716   3079   -553    352    201       N
ATOM    922  CA  SER A 111      15.638  10.683   5.374  1.00 20.46           C
ANISOU  922  CA  SER A 111     2858   2276   2640   -520    345    196       C
ATOM    923  C   SER A 111      15.082   9.482   6.117  1.00 26.62           C
ANISOU  923  C   SER A 111     3613   3054   3447   -488    329    188       C
ATOM    924  O   SER A 111      15.444   8.335   5.837  1.00 25.06           O
ANISOU  924  O   SER A 111     3370   2876   3278   -472    334    178       O
ATOM    925  CB  SER A 111      15.025  10.740   3.982  1.00 22.43           C
ANISOU  925  CB  SER A 111     3127   2528   2868   -501    367    186       C
ATOM    926  OG  SER A 111      13.613  10.820   4.093  1.00 25.32           O
ANISOU  926  OG  SER A 111     3528   2873   3220   -468    356    179       O
ATOM    927  N   GLN A 112      14.183   9.748   7.059  1.00 23.83           N
ANISOU  927  N   GLN A 112     3294   2678   3083   -480    312    190       N
ATOM    928  CA  GLN A 112      13.388   8.695   7.673  1.00 24.82           C
ANISOU  928  CA  GLN A 112     3408   2798   3226   -452    303    179       C
ATOM    929  C   GLN A 112      11.930   8.761   7.223  1.00 26.25           C
ANISOU  929  C   GLN A 112     3615   2966   3391   -420    311    164       C
ATOM    930  O   GLN A 112      11.046   8.229   7.897  1.00 33.39           O
ANISOU  930  O   GLN A 112     4525   3860   4303   -403    305    155       O
ATOM    931  CB  GLN A 112      13.514   8.750   9.203  1.00 24.25           C
ANISOU  931  CB  GLN A 112     3348   2708   3157   -469    279    189       C
ATOM    932  CG  GLN A 112      12.998  10.003   9.895  1.00 31.42           C
ANISOU  932  CG  GLN A 112     4311   3591   4035   -486    273    196       C
ATOM    933  CD  GLN A 112      12.940   9.830  11.420  1.00 42.40           C
ANISOU  933  CD  GLN A 112     5718   4963   5427   -499    252    202       C
ATOM    934  OE1 GLN A 112      11.872   9.572  11.985  1.00 38.30           O
ANISOU  934  OE1 GLN A 112     5220   4428   4903   -483    255    191       O
ATOM    935  NE2 GLN A 112      14.094   9.954  12.085  1.00 42.43           N
ANISOU  935  NE2 GLN A 112     5713   4970   5438   -530    231    218       N
ATOM    936  N   LEU A 113      11.668   9.386   6.074  1.00 22.19           N
ANISOU  936  N   LEU A 113     3120   2454   2857   -414    324    161       N
ATOM    937  CA  LEU A 113      10.317   9.580   5.556  1.00 20.22           C
ANISOU  937  CA  LEU A 113     2897   2193   2594   -384    325    146       C
ATOM    938  C   LEU A 113      10.044   8.705   4.350  1.00 22.47           C
ANISOU  938  C   LEU A 113     3158   2495   2886   -358    337    132       C
ATOM    939  O   LEU A 113       9.025   8.882   3.666  1.00 21.68           O
ANISOU  939  O   LEU A 113     3077   2387   2773   -333    335    119       O
ATOM    940  CB  LEU A 113      10.094  11.050   5.200  1.00 21.40           C
ANISOU  940  CB  LEU A 113     3097   2324   2711   -393    323    154       C
ATOM    941  CG  LEU A 113      10.188  12.006   6.379  1.00 24.88           C
ANISOU  941  CG  LEU A 113     3570   2743   3141   -416    311    166       C
ATOM    942  CD1 LEU A 113       9.970  13.433   5.895  1.00 22.29           C
ANISOU  942  CD1 LEU A 113     3296   2393   2780   -423    308    172       C
ATOM    943  CD2 LEU A 113       9.142  11.620   7.378  1.00 26.82           C
ANISOU  943  CD2 LEU A 113     3817   2975   3399   -396    305    152       C
ATOM    944  N   GLY A 114      10.924   7.753   4.097  1.00 27.17           N
ANISOU  944  N   GLY A 114     3711   3111   3501   -362    346    131       N
ATOM    945  CA  GLY A 114      10.842   6.906   2.929  1.00 25.86           C
ANISOU  945  CA  GLY A 114     3524   2961   3340   -342    361    117       C
ATOM    946  C   GLY A 114      12.225   6.378   2.634  1.00 27.19           C
ANISOU  946  C   GLY A 114     3654   3152   3527   -359    375    121       C
ATOM    947  O   GLY A 114      13.200   6.696   3.321  1.00 25.57           O
ANISOU  947  O   GLY A 114     3435   2949   3330   -386    371    135       O
ATOM    948  N   ARG A 115      12.291   5.534   1.612  1.00 21.56           N
ANISOU  948  N   ARG A 115     2919   2453   2819   -343    392    107       N
ATOM    949  C   ARG A 115      13.566   4.970  -0.336  1.00 27.81           C
ANISOU  949  C   ARG A 115     3681   3277   3609   -352    437     94       C
ATOM    950  O   ARG A 115      12.904   4.150  -0.976  1.00 27.03           O
ANISOU  950  O   ARG A 115     3580   3181   3511   -325    442     77       O
ATOM    951  CA AARG A 115      13.559   4.941   1.187  0.37 25.32           C
ANISOU  951  CA AARG A 115     3354   2952   3316   -354    411    105       C
ATOM    952  CB AARG A 115      13.735   3.520   1.717  0.37 27.76           C
ANISOU  952  CB AARG A 115     3617   3266   3663   -334    404     95       C
ATOM    953  CG AARG A 115      13.718   3.389   3.237  0.37 32.19           C
ANISOU  953  CG AARG A 115     4174   3814   4243   -338    376    107       C
ATOM    954  CD AARG A 115      14.742   2.363   3.725  0.37 35.97           C
ANISOU  954  CD AARG A 115     4605   4303   4762   -335    369    106       C
ATOM    955  NE AARG A 115      16.025   2.994   4.028  0.37 37.87           N
ANISOU  955  NE AARG A 115     4824   4552   5012   -365    366    118       N
ATOM    956  CZ AARG A 115      17.136   2.332   4.334  0.37 31.90           C
ANISOU  956  CZ AARG A 115     4020   3807   4293   -366    359    117       C
ATOM    957  NH1AARG A 115      17.134   1.007   4.364  0.37 36.26           N
ANISOU  957  NH1AARG A 115     4543   4359   4873   -337    354    105       N
ATOM    958  NH2AARG A 115      18.251   2.995   4.601  0.37 23.95           N
ANISOU  958  NH2AARG A 115     2992   2811   3296   -396    355    126       N
ATOM    959  CA BARG A 115      13.561   4.950   1.187  0.63 24.85           C
ANISOU  959  CA BARG A 115     3294   2892   3256   -355    411    105       C
ATOM    960  CB BARG A 115      13.757   3.539   1.731  0.63 27.52           C
ANISOU  960  CB BARG A 115     3586   3235   3633   -335    404     96       C
ATOM    961  CG BARG A 115      15.044   3.387   2.528  0.63 32.51           C
ANISOU  961  CG BARG A 115     4181   3877   4296   -354    397    105       C
ATOM    962  CD BARG A 115      15.322   1.945   2.933  0.63 38.81           C
ANISOU  962  CD BARG A 115     4937   4678   5133   -331    387     96       C
ATOM    963  NE BARG A 115      15.808   1.150   1.808  0.63 48.65           N
ANISOU  963  NE BARG A 115     6151   5942   6393   -317    414     78       N
ATOM    964  CZ BARG A 115      16.784   0.254   1.903  0.63 47.13           C
ANISOU  964  CZ BARG A 115     5908   5759   6238   -308    415     70       C
ATOM    965  NH1BARG A 115      17.373   0.051   3.075  0.63 36.67           N
ANISOU  965  NH1BARG A 115     4563   4429   4942   -313    385     81       N
ATOM    966  NH2BARG A 115      17.171  -0.436   0.834  0.63 46.78           N
ANISOU  966  NH2BARG A 115     5838   5730   6205   -295    444     50       N
ATOM    967  N   TRP A 116      14.305   5.912  -0.900  1.00 23.22           N
ANISOU  967  N   TRP A 116     3117   2701   3006   -383    455    102       N
ATOM    968  CA  TRP A 116      14.404   6.028  -2.344  1.00 25.24           C
ANISOU  968  CA  TRP A 116     3392   2964   3234   -387    483     93       C
ATOM    969  C   TRP A 116      15.427   5.050  -2.903  1.00 27.12           C
ANISOU  969  C   TRP A 116     3579   3227   3498   -390    515     78       C
ATOM    970  O   TRP A 116      16.485   4.821  -2.309  1.00 27.81           O
ANISOU  970  O   TRP A 116     3620   3328   3619   -404    520     80       O
ATOM    971  CB  TRP A 116      14.798   7.451  -2.722  1.00 20.85           C
ANISOU  971  CB  TRP A 116     2881   2401   2640   -425    493    108       C
ATOM    972  CG  TRP A 116      14.956   7.663  -4.187  1.00 23.29           C
ANISOU  972  CG  TRP A 116     3222   2714   2914   -437    523    101       C
ATOM    973  CD1 TRP A 116      13.960   7.736  -5.116  1.00 21.33           C
ANISOU  973  CD1 TRP A 116     3021   2453   2631   -416    517     95       C
ATOM    974  CD2 TRP A 116      16.182   7.872  -4.890  1.00 24.45           C
ANISOU  974  CD2 TRP A 116     3357   2878   3053   -475    565     98       C
ATOM    975  NE1 TRP A 116      14.496   7.970  -6.362  1.00 24.55           N
ANISOU  975  NE1 TRP A 116     3456   2866   3005   -440    551     90       N
ATOM    976  CE2 TRP A 116      15.858   8.054  -6.248  1.00 22.53           C
ANISOU  976  CE2 TRP A 116     3164   2631   2767   -478    584     91       C
ATOM    977  CE3 TRP A 116      17.525   7.919  -4.505  1.00 29.29           C
ANISOU  977  CE3 TRP A 116     3923   3512   3695   -508    587     99       C
ATOM    978  CZ2 TRP A 116      16.825   8.277  -7.222  1.00 24.67           C
ANISOU  978  CZ2 TRP A 116     3441   2914   3017   -515    631     85       C
ATOM    979  CZ3 TRP A 116      18.487   8.145  -5.478  1.00 31.20           C
ANISOU  979  CZ3 TRP A 116     4164   3770   3922   -544    633     91       C
ATOM    980  CH2 TRP A 116      18.132   8.315  -6.818  1.00 31.12           C
ANISOU  980  CH2 TRP A 116     4206   3753   3864   -549    658     84       C
ATOM    981  N   MET A 117      15.113   4.484  -4.063  1.00 27.40           N
ANISOU  981  N   MET A 117     3624   3267   3518   -374    535     61       N
ATOM    982  CA  MET A 117      16.086   3.720  -4.833  1.00 29.23           C
ANISOU  982  CA  MET A 117     3818   3522   3767   -380    573     43       C
ATOM    983  C   MET A 117      16.002   4.148  -6.286  1.00 24.94           C
ANISOU  983  C   MET A 117     3322   2979   3177   -394    603     36       C
ATOM    984  O   MET A 117      14.905   4.294  -6.832  1.00 24.20           O
ANISOU  984  O   MET A 117     3278   2869   3049   -377    588     35       O
ATOM    985  CB  MET A 117      15.838   2.208  -4.708  1.00 29.32           C
ANISOU  985  CB  MET A 117     3788   3537   3814   -342    568     25       C
ATOM    986  CG  MET A 117      16.695   1.348  -5.608  1.00 28.58           C
ANISOU  986  CG  MET A 117     3659   3463   3737   -340    609      2       C
ATOM    987  SD  MET A 117      16.273  -0.394  -5.370  1.00 33.21           S
ANISOU  987  SD  MET A 117     4208   4048   4364   -293    596    -18       S
ATOM    988  CE  MET A 117      17.092  -0.734  -3.817  1.00 38.54           C
ANISOU  988  CE  MET A 117     4824   4725   5095   -290    570     -7       C
ATOM    989  N   SER A 118      17.155   4.347  -6.917  1.00 26.50           N
ANISOU  989  N   SER A 118     3505   3193   3371   -427    647     29       N
ATOM    990  CA  SER A 118      17.122   4.786  -8.302  1.00 30.12           C
ANISOU  990  CA  SER A 118     4016   3649   3778   -447    679     23       C
ATOM    991  C   SER A 118      16.637   3.657  -9.203  1.00 28.44           C
ANISOU  991  C   SER A 118     3804   3440   3562   -417    691     -0       C
ATOM    992  O   SER A 118      16.663   2.474  -8.836  1.00 28.57           O
ANISOU  992  O   SER A 118     3769   3465   3621   -386    687    -15       O
ATOM    993  CB  SER A 118      18.503   5.252  -8.762  1.00 32.80           C
ANISOU  993  CB  SER A 118     4339   4007   4115   -495    730     18       C
ATOM    994  OG  SER A 118      19.296   4.134  -9.098  1.00 31.96           O
ANISOU  994  OG  SER A 118     4172   3926   4048   -487    766     -8       O
ATOM    995  N   GLU A 119      16.171   4.042 -10.393  1.00 29.27           N
ANISOU  995  N   GLU A 119     3976   3535   3612   -426    703     -3       N
ATOM    996  CA  GLU A 119      15.727   3.064 -11.382  1.00 39.64           C
ANISOU  996  CA  GLU A 119     5300   4849   4913   -403    716    -26       C
ATOM    997  C   GLU A 119      16.856   2.116 -11.766  1.00 36.60           C
ANISOU  997  C   GLU A 119     4859   4489   4560   -409    768    -52       C
ATOM    998  O   GLU A 119      16.639   0.910 -11.944  1.00 33.38           O
ANISOU  998  O   GLU A 119     4423   4084   4174   -377    771    -72       O
ATOM    999  CB  GLU A 119      15.200   3.781 -12.627  1.00 49.80           C
ANISOU  999  CB  GLU A 119     6674   6119   6129   -419    720    -23       C
ATOM   1000  CG  GLU A 119      13.688   3.728 -12.814  1.00 58.30           C
ANISOU 1000  CG  GLU A 119     7797   7173   7182   -384    668    -20       C
ATOM   1001  CD  GLU A 119      13.029   5.078 -12.582  1.00 66.69           C
ANISOU 1001  CD  GLU A 119     8919   8211   8210   -391    629      5       C
ATOM   1002  OE1 GLU A 119      11.779   5.139 -12.543  1.00 64.98           O
ANISOU 1002  OE1 GLU A 119     8730   7976   7983   -360    581      7       O
ATOM   1003  OE2 GLU A 119      13.768   6.077 -12.440  1.00 72.64           O
ANISOU 1003  OE2 GLU A 119     9689   8963   8948   -429    647     21       O
ATOM   1004  N   GLU A 120      18.070   2.652 -11.902  1.00 46.44           N
ANISOU 1004  N   GLU A 120     6087   5750   5808   -450    811    -52       N
ATOM   1005  CA  GLU A 120      19.213   1.840 -12.298  1.00 43.88           C
ANISOU 1005  CA  GLU A 120     5704   5451   5518   -457    866    -80       C
ATOM   1006  C   GLU A 120      19.595   0.866 -11.193  1.00 42.10           C
ANISOU 1006  C   GLU A 120     5393   5237   5366   -424    847    -87       C
ATOM   1007  O   GLU A 120      19.957  -0.286 -11.465  1.00 40.52           O
ANISOU 1007  O   GLU A 120     5150   5048   5200   -401    869   -114       O
ATOM   1008  CB  GLU A 120      20.392   2.746 -12.668  1.00 49.86           C
ANISOU 1008  CB  GLU A 120     6460   6222   6261   -514    917    -81       C
ATOM   1009  CG  GLU A 120      20.070   3.814 -13.726  1.00 57.80           C
ANISOU 1009  CG  GLU A 120     7563   7212   7188   -553    935    -70       C
ATOM   1010  CD  GLU A 120      19.252   4.976 -13.177  1.00 64.33           C
ANISOU 1010  CD  GLU A 120     8447   8013   7982   -558    881    -36       C
ATOM   1011  OE1 GLU A 120      19.472   5.353 -12.008  1.00 61.24           O
ANISOU 1011  OE1 GLU A 120     8018   7625   7627   -559    854    -19       O
ATOM   1012  OE2 GLU A 120      18.378   5.499 -13.907  1.00 67.47           O
ANISOU 1012  OE2 GLU A 120     8930   8388   8319   -559    864    -26       O
ATOM   1013  N   ASP A 121      19.505   1.299  -9.937  1.00 34.01           N
ANISOU 1013  N   ASP A 121     4349   4208   4368   -421    804    -64       N
ATOM   1014  CA  ASP A 121      19.777   0.371  -8.849  1.00 30.75           C
ANISOU 1014  CA  ASP A 121     3865   3800   4020   -389    778    -68       C
ATOM   1015  C   ASP A 121      18.687  -0.688  -8.732  1.00 30.36           C
ANISOU 1015  C   ASP A 121     3824   3735   3976   -341    746    -75       C
ATOM   1016  O   ASP A 121      18.984  -1.840  -8.402  1.00 34.38           O
ANISOU 1016  O   ASP A 121     4282   4248   4531   -312    744    -91       O
ATOM   1017  CB  ASP A 121      19.943   1.134  -7.533  1.00 32.29           C
ANISOU 1017  CB  ASP A 121     4044   3990   4233   -401    739    -42       C
ATOM   1018  CG  ASP A 121      21.133   2.076  -7.561  1.00 43.79           C
ANISOU 1018  CG  ASP A 121     5483   5464   5693   -450    770    -38       C
ATOM   1019  OD1 ASP A 121      21.007   3.229  -7.091  1.00 49.62           O
ANISOU 1019  OD1 ASP A 121     6253   6193   6407   -478    751    -14       O
ATOM   1020  OD2 ASP A 121      22.189   1.661  -8.084  1.00 42.37           O
ANISOU 1020  OD2 ASP A 121     5254   5305   5538   -462    816    -62       O
ATOM   1021  N   PHE A 122      17.430  -0.330  -9.016  1.00 29.41           N
ANISOU 1021  N   PHE A 122     3768   3596   3811   -333    720    -64       N
ATOM   1022  CA  PHE A 122      16.371  -1.325  -8.900  1.00 32.84           C
ANISOU 1022  CA  PHE A 122     4207   4018   4253   -292    691    -72       C
ATOM   1023  C   PHE A 122      16.447  -2.355 -10.021  1.00 32.65           C
ANISOU 1023  C   PHE A 122     4182   3999   4225   -278    725   -102       C
ATOM   1024  O   PHE A 122      16.158  -3.536  -9.797  1.00 29.32           O
ANISOU 1024  O   PHE A 122     3735   3572   3832   -245    714   -116       O
ATOM   1025  CB  PHE A 122      14.988  -0.677  -8.879  1.00 33.31           C
ANISOU 1025  CB  PHE A 122     4327   4057   4272   -286    652    -57       C
ATOM   1026  CG  PHE A 122      13.877  -1.690  -8.863  1.00 30.88           C
ANISOU 1026  CG  PHE A 122     4024   3738   3972   -249    626    -69       C
ATOM   1027  CD1 PHE A 122      13.647  -2.458  -7.732  1.00 30.46           C
ANISOU 1027  CD1 PHE A 122     3931   3679   3962   -226    599    -67       C
ATOM   1028  CD2 PHE A 122      13.107  -1.915  -9.991  1.00 30.60           C
ANISOU 1028  CD2 PHE A 122     4032   3696   3900   -241    629    -83       C
ATOM   1029  CE1 PHE A 122      12.658  -3.418  -7.720  1.00 27.98           C
ANISOU 1029  CE1 PHE A 122     3621   3354   3655   -197    579    -80       C
ATOM   1030  CE2 PHE A 122      12.117  -2.878  -9.988  1.00 28.98           C
ANISOU 1030  CE2 PHE A 122     3827   3481   3702   -210    606    -96       C
ATOM   1031  CZ  PHE A 122      11.886  -3.619  -8.850  1.00 27.75           C
ANISOU 1031  CZ  PHE A 122     3631   3321   3591   -190    583    -95       C
ATOM   1032  N   GLU A 123      16.812  -1.939 -11.237  1.00 33.37           N
ANISOU 1032  N   GLU A 123     4307   4097   4276   -303    768   -112       N
ATOM   1033  CA  GLU A 123      16.902  -2.919 -12.320  1.00 33.69           C
ANISOU 1033  CA  GLU A 123     4351   4141   4309   -291    803   -142       C
ATOM   1034  C   GLU A 123      17.946  -3.984 -12.002  1.00 31.58           C
ANISOU 1034  C   GLU A 123     4008   3889   4103   -275    829   -165       C
ATOM   1035  O   GLU A 123      17.734  -5.175 -12.268  1.00 29.93           O
ANISOU 1035  O   GLU A 123     3785   3674   3911   -244    833   -187       O
ATOM   1036  CB  GLU A 123      17.194  -2.231 -13.659  1.00 46.68           C
ANISOU 1036  CB  GLU A 123     6051   5790   5897   -328    848   -150       C
ATOM   1037  CG  GLU A 123      18.601  -1.683 -13.830  1.00 58.60           C
ANISOU 1037  CG  GLU A 123     7530   7320   7416   -367    902   -155       C
ATOM   1038  CD  GLU A 123      18.799  -0.949 -15.147  1.00 61.08           C
ANISOU 1038  CD  GLU A 123     7911   7634   7664   -409    948   -160       C
ATOM   1039  OE1 GLU A 123      17.991  -1.165 -16.077  1.00 62.12           O
ANISOU 1039  OE1 GLU A 123     8104   7750   7747   -402    944   -168       O
ATOM   1040  OE2 GLU A 123      19.760  -0.151 -15.248  1.00 58.98           O
ANISOU 1040  OE2 GLU A 123     7637   7380   7393   -452    986   -158       O
ATOM   1041  N   LYS A 124      19.064  -3.583 -11.394  1.00 31.81           N
ANISOU 1041  N   LYS A 124     3986   3934   4168   -293    844   -160       N
ATOM   1042  CA  LYS A 124      20.053  -4.555 -10.943  1.00 36.69           C
ANISOU 1042  CA  LYS A 124     4526   4563   4852   -272    858   -180       C
ATOM   1043  C   LYS A 124      19.482  -5.439  -9.842  1.00 32.85           C
ANISOU 1043  C   LYS A 124     4015   4061   4405   -230    804   -172       C
ATOM   1044  O   LYS A 124      19.629  -6.665  -9.873  1.00 31.44           O
ANISOU 1044  O   LYS A 124     3806   3879   4261   -197    807   -194       O
ATOM   1045  CB  LYS A 124      21.310  -3.830 -10.463  1.00 32.53           C
ANISOU 1045  CB  LYS A 124     3949   4057   4356   -302    876   -175       C
ATOM   1046  CG  LYS A 124      21.840  -2.815 -11.483  1.00 42.35           C
ANISOU 1046  CG  LYS A 124     5223   5313   5554   -353    931   -179       C
ATOM   1047  CD  LYS A 124      23.304  -3.032 -11.833  1.00 49.98           C
ANISOU 1047  CD  LYS A 124     6123   6306   6561   -370    990   -209       C
ATOM   1048  CE  LYS A 124      24.239  -2.500 -10.755  1.00 52.69           C
ANISOU 1048  CE  LYS A 124     6403   6664   6953   -387    974   -196       C
ATOM   1049  NZ  LYS A 124      25.674  -2.618 -11.166  1.00 51.08           N
ANISOU 1049  NZ  LYS A 124     6129   6488   6790   -408   1034   -229       N
ATOM   1050  N   ALA A 125      18.813  -4.830  -8.861  1.00 25.87           N
ANISOU 1050  N   ALA A 125     3150   3166   3515   -233    754   -142       N
ATOM   1051  CA  ALA A 125      18.223  -5.617  -7.782  1.00 30.21           C
ANISOU 1051  CA  ALA A 125     3685   3699   4096   -199    706   -134       C
ATOM   1052  C   ALA A 125      17.153  -6.557  -8.320  1.00 25.32           C
ANISOU 1052  C   ALA A 125     3098   3063   3459   -172    699   -148       C
ATOM   1053  O   ALA A 125      17.010  -7.691  -7.850  1.00 29.81           O
ANISOU 1053  O   ALA A 125     3645   3621   4062   -141    681   -157       O
ATOM   1054  CB  ALA A 125      17.640  -4.690  -6.713  1.00 29.00           C
ANISOU 1054  CB  ALA A 125     3553   3535   3931   -212    661   -101       C
ATOM   1055  N   PHE A 126      16.394  -6.096  -9.313  1.00 25.59           N
ANISOU 1055  N   PHE A 126     3189   3096   3440   -184    710   -151       N
ATOM   1056  CA  PHE A 126      15.343  -6.914  -9.897  1.00 24.99           C
ANISOU 1056  CA  PHE A 126     3145   3005   3344   -162    701   -165       C
ATOM   1057  C   PHE A 126      15.941  -8.117 -10.616  1.00 30.90           C
ANISOU 1057  C   PHE A 126     3869   3757   4113   -143    737   -198       C
ATOM   1058  O   PHE A 126      15.508  -9.260 -10.408  1.00 29.94           O
ANISOU 1058  O   PHE A 126     3740   3622   4013   -114    722   -210       O
ATOM   1059  CB  PHE A 126      14.511  -6.048 -10.843  1.00 26.94           C
ANISOU 1059  CB  PHE A 126     3458   3250   3529   -181    702   -161       C
ATOM   1060  CG  PHE A 126      13.419  -6.784 -11.559  1.00 29.61           C
ANISOU 1060  CG  PHE A 126     3833   3575   3843   -162    690   -177       C
ATOM   1061  CD1 PHE A 126      12.217  -7.046 -10.931  1.00 23.41           C
ANISOU 1061  CD1 PHE A 126     3058   2775   3062   -144    644   -170       C
ATOM   1062  CD2 PHE A 126      13.582  -7.178 -12.879  1.00 33.22           C
ANISOU 1062  CD2 PHE A 126     4316   4035   4272   -165    727   -201       C
ATOM   1063  CE1 PHE A 126      11.200  -7.705 -11.592  1.00 27.32           C
ANISOU 1063  CE1 PHE A 126     3584   3260   3538   -130    632   -187       C
ATOM   1064  CE2 PHE A 126      12.571  -7.838 -13.546  1.00 36.29           C
ANISOU 1064  CE2 PHE A 126     4741   4412   4637   -150    712   -217       C
ATOM   1065  CZ  PHE A 126      11.376  -8.103 -12.902  1.00 32.32           C
ANISOU 1065  CZ  PHE A 126     4243   3895   4142   -132    663   -210       C
ATOM   1066  N   ASN A 127      16.975  -7.885 -11.429  1.00 26.51           N
ANISOU 1066  N   ASN A 127     3302   3219   3553   -161    789   -213       N
ATOM   1067  CA  ASN A 127      17.559  -8.969 -12.219  1.00 26.93           C
ANISOU 1067  CA  ASN A 127     3335   3275   3624   -145    830   -248       C
ATOM   1068  C   ASN A 127      18.294  -9.993 -11.369  1.00 27.39           C
ANISOU 1068  C   ASN A 127     3325   3330   3750   -113    822   -259       C
ATOM   1069  O   ASN A 127      18.518 -11.118 -11.834  1.00 29.51           O
ANISOU 1069  O   ASN A 127     3580   3593   4039    -88    843   -288       O
ATOM   1070  CB  ASN A 127      18.512  -8.403 -13.272  1.00 29.12           C
ANISOU 1070  CB  ASN A 127     3613   3571   3878   -176    893   -265       C
ATOM   1071  CG  ASN A 127      17.787  -7.686 -14.373  1.00 34.40           C
ANISOU 1071  CG  ASN A 127     4360   4237   4474   -203    905   -262       C
ATOM   1072  OD1 ASN A 127      16.648  -8.016 -14.697  1.00 39.72           O
ANISOU 1072  OD1 ASN A 127     5080   4894   5117   -189    877   -261       O
ATOM   1073  ND2 ASN A 127      18.438  -6.691 -14.956  1.00 35.86           N
ANISOU 1073  ND2 ASN A 127     4561   4435   4628   -243    945   -259       N
ATOM   1074  N   ALA A 128      18.689  -9.633 -10.153  1.00 28.47           N
ANISOU 1074  N   ALA A 128     3425   3470   3924   -113    791   -237       N
ATOM   1075  CA  ALA A 128      19.323 -10.566  -9.232  1.00 33.26           C
ANISOU 1075  CA  ALA A 128     3974   4069   4595    -81    770   -243       C
ATOM   1076  C   ALA A 128      18.320 -11.387  -8.427  1.00 35.55           C
ANISOU 1076  C   ALA A 128     4283   4332   4893    -54    719   -232       C
ATOM   1077  O   ALA A 128      18.733 -12.155  -7.554  1.00 38.03           O
ANISOU 1077  O   ALA A 128     4560   4633   5255    -28    693   -232       O
ATOM   1078  CB  ALA A 128      20.244  -9.814  -8.266  1.00 30.38           C
ANISOU 1078  CB  ALA A 128     3562   3717   4264    -97    756   -224       C
ATOM   1079  N   ARG A 129      17.020 -11.236  -8.684  1.00 29.19           N
ANISOU 1079  N   ARG A 129     3534   3515   4043    -60    703   -224       N
ATOM   1080  CA  ARG A 129      16.001 -11.859  -7.844  1.00 23.68           C
ANISOU 1080  CA  ARG A 129     2855   2794   3350    -42    656   -213       C
ATOM   1081  C   ARG A 129      14.982 -12.635  -8.661  1.00 29.78           C
ANISOU 1081  C   ARG A 129     3668   3553   4095    -31    661   -232       C
ATOM   1082  O   ARG A 129      14.746 -13.825  -8.419  1.00 30.36           O
ANISOU 1082  O   ARG A 129     3738   3607   4192     -6    648   -245       O
ATOM   1083  CB  ARG A 129      15.275 -10.798  -7.002  1.00 24.93           C
ANISOU 1083  CB  ARG A 129     3035   2950   3487    -64    621   -181       C
ATOM   1084  CG  ARG A 129      16.044 -10.337  -5.779  1.00 25.28           C
ANISOU 1084  CG  ARG A 129     3044   2996   3564    -70    598   -159       C
ATOM   1085  CD  ARG A 129      15.562  -8.976  -5.283  1.00 26.50           C
ANISOU 1085  CD  ARG A 129     3224   3156   3689    -98    579   -131       C
ATOM   1086  NE  ARG A 129      16.264  -8.578  -4.071  1.00 29.79           N
ANISOU 1086  NE  ARG A 129     3611   3573   4136   -106    555   -110       N
ATOM   1087  CZ  ARG A 129      17.460  -8.000  -4.052  1.00 33.82           C
ANISOU 1087  CZ  ARG A 129     4085   4101   4664   -120    570   -107       C
ATOM   1088  NH1 ARG A 129      18.086  -7.737  -5.187  1.00 38.60           N
ANISOU 1088  NH1 ARG A 129     4680   4726   5260   -131    616   -125       N
ATOM   1089  NH2 ARG A 129      18.024  -7.676  -2.898  1.00 36.66           N
ANISOU 1089  NH2 ARG A 129     4420   4459   5050   -127    541    -89       N
ATOM   1090  N   PHE A 130      14.378 -11.977  -9.632  1.00 21.85           N
ANISOU 1090  N   PHE A 130     2704   2557   3041    -50    676   -235       N
ATOM   1091  CA  PHE A 130      13.183 -12.555 -10.234  1.00 25.35           C
ANISOU 1091  CA  PHE A 130     3190   2986   3455    -43    666   -248       C
ATOM   1092  C   PHE A 130      13.407 -13.571 -11.354  1.00 24.22           C
ANISOU 1092  C   PHE A 130     3055   2839   3307    -29    700   -282       C
ATOM   1093  O   PHE A 130      12.590 -14.488 -11.476  1.00 24.80           O
ANISOU 1093  O   PHE A 130     3149   2895   3378    -15    685   -295       O
ATOM   1094  CB  PHE A 130      12.278 -11.433 -10.726  1.00 27.38           C
ANISOU 1094  CB  PHE A 130     3493   3249   3660    -66    654   -235       C
ATOM   1095  CG  PHE A 130      11.471 -10.814  -9.617  1.00 25.01           C
ANISOU 1095  CG  PHE A 130     3197   2943   3363    -72    611   -209       C
ATOM   1096  CD1 PHE A 130      11.957  -9.722  -8.914  1.00 23.08           C
ANISOU 1096  CD1 PHE A 130     2939   2708   3123    -88    604   -184       C
ATOM   1097  CD2 PHE A 130      10.260 -11.372  -9.242  1.00 22.07           C
ANISOU 1097  CD2 PHE A 130     2841   2555   2991    -62    579   -212       C
ATOM   1098  CE1 PHE A 130      11.226  -9.177  -7.880  1.00 28.18           C
ANISOU 1098  CE1 PHE A 130     3590   3346   3770    -93    568   -162       C
ATOM   1099  CE2 PHE A 130       9.527 -10.842  -8.205  1.00 25.08           C
ANISOU 1099  CE2 PHE A 130     3223   2930   3376    -68    545   -192       C
ATOM   1100  CZ  PHE A 130      10.008  -9.738  -7.523  1.00 30.68           C
ANISOU 1100  CZ  PHE A 130     3922   3648   4087    -83    540   -167       C
ATOM   1101  N   PRO A 131      14.441 -13.438 -12.222  1.00 24.70           N
ANISOU 1101  N   PRO A 131     3104   2915   3365    -35    749   -299       N
ATOM   1102  CA  PRO A 131      14.637 -14.454 -13.272  1.00 24.86           C
ANISOU 1102  CA  PRO A 131     3136   2930   3381    -21    785   -335       C
ATOM   1103  C   PRO A 131      14.597 -15.886 -12.746  1.00 24.90           C
ANISOU 1103  C   PRO A 131     3120   2912   3428     13    769   -349       C
ATOM   1104  O   PRO A 131      15.439 -16.289 -11.938  1.00 29.43           O
ANISOU 1104  O   PRO A 131     3645   3482   4054     33    765   -348       O
ATOM   1105  CB  PRO A 131      16.014 -14.097 -13.841  1.00 27.23           C
ANISOU 1105  CB  PRO A 131     3406   3251   3690    -31    840   -349       C
ATOM   1106  CG  PRO A 131      16.061 -12.586 -13.708  1.00 26.94           C
ANISOU 1106  CG  PRO A 131     3379   3231   3625    -66    836   -321       C
ATOM   1107  CD  PRO A 131      15.334 -12.272 -12.419  1.00 29.83           C
ANISOU 1107  CD  PRO A 131     3740   3587   4005    -61    777   -289       C
ATOM   1108  N   GLY A 132      13.591 -16.650 -13.174  1.00 28.04           N
ANISOU 1108  N   GLY A 132     3558   3292   3805     21    756   -363       N
ATOM   1109  CA  GLY A 132      13.458 -18.038 -12.768  1.00 20.75           C
ANISOU 1109  CA  GLY A 132     2625   2342   2916     50    742   -378       C
ATOM   1110  C   GLY A 132      12.962 -18.278 -11.355  1.00 26.84           C
ANISOU 1110  C   GLY A 132     3385   3097   3717     58    692   -354       C
ATOM   1111  O   GLY A 132      13.009 -19.425 -10.883  1.00 24.23           O
ANISOU 1111  O   GLY A 132     3047   2742   3418     82    679   -364       O
ATOM   1112  N   CYS A 133      12.460 -17.248 -10.671  1.00 27.17           N
ANISOU 1112  N   CYS A 133     3430   3149   3746     38    663   -324       N
ATOM   1113  CA  CYS A 133      12.195 -17.372  -9.238  1.00 25.45           C
ANISOU 1113  CA  CYS A 133     3197   2916   3555     42    622   -301       C
ATOM   1114  C   CYS A 133      11.005 -18.271  -8.917  1.00 27.24           C
ANISOU 1114  C   CYS A 133     3454   3117   3778     45    594   -306       C
ATOM   1115  O   CYS A 133      10.893 -18.732  -7.775  1.00 26.20           O
ANISOU 1115  O   CYS A 133     3315   2967   3674     51    566   -293       O
ATOM   1116  CB  CYS A 133      11.977 -15.986  -8.608  1.00 24.91           C
ANISOU 1116  CB  CYS A 133     3127   2864   3473     18    604   -270       C
ATOM   1117  SG  CYS A 133      10.514 -15.108  -9.175  1.00 24.93           S
ANISOU 1117  SG  CYS A 133     3176   2875   3422     -7    590   -264       S
ATOM   1118  N   MET A 134      10.104 -18.518  -9.870  1.00 22.13           N
ANISOU 1118  N   MET A 134     2843   2469   3098     38    600   -324       N
ATOM   1119  CA  MET A 134       8.942 -19.365  -9.625  1.00 21.31           C
ANISOU 1119  CA  MET A 134     2764   2342   2990     37    576   -333       C
ATOM   1120  C   MET A 134       9.074 -20.738 -10.278  1.00 22.52           C
ANISOU 1120  C   MET A 134     2931   2474   3150     55    592   -363       C
ATOM   1121  O   MET A 134       8.060 -21.402 -10.515  1.00 24.32           O
ANISOU 1121  O   MET A 134     3189   2687   3364     49    579   -377       O
ATOM   1122  CB  MET A 134       7.667 -18.687 -10.116  1.00 23.28           C
ANISOU 1122  CB  MET A 134     3043   2604   3200     14    561   -332       C
ATOM   1123  CG  MET A 134       7.323 -17.346  -9.397  1.00 16.60           C
ANISOU 1123  CG  MET A 134     2189   1774   2346     -3    540   -304       C
ATOM   1124  SD  MET A 134       5.760 -16.786 -10.078  1.00 23.37           S
ANISOU 1124  SD  MET A 134     3078   2639   3163    -21    518   -311       S
ATOM   1125  CE  MET A 134       5.602 -15.191  -9.244  1.00 22.64           C
ANISOU 1125  CE  MET A 134     2973   2562   3066    -35    500   -279       C
ATOM   1126  N   LYS A 135      10.291 -21.165 -10.594  1.00 24.96           N
ANISOU 1126  N   LYS A 135     3219   2781   3482     77    620   -376       N
ATOM   1127  CA  LYS A 135      10.463 -22.459 -11.238  1.00 24.25           C
ANISOU 1127  CA  LYS A 135     3144   2669   3400     98    638   -408       C
ATOM   1128  C   LYS A 135       9.848 -23.553 -10.373  1.00 24.16           C
ANISOU 1128  C   LYS A 135     3147   2623   3409    105    607   -407       C
ATOM   1129  O   LYS A 135      10.074 -23.606  -9.159  1.00 27.21           O
ANISOU 1129  O   LYS A 135     3517   2998   3826    110    582   -385       O
ATOM   1130  CB  LYS A 135      11.943 -22.747 -11.494  1.00 27.96           C
ANISOU 1130  CB  LYS A 135     3579   3142   3903    125    672   -422       C
ATOM   1131  CG  LYS A 135      12.172 -23.800 -12.584  1.00 34.65           C
ANISOU 1131  CG  LYS A 135     4446   3974   4747    143    705   -461       C
ATOM   1132  CD  LYS A 135      12.482 -23.148 -13.929  1.00 45.57           C
ANISOU 1132  CD  LYS A 135     5838   5384   6093    129    750   -479       C
ATOM   1133  CE  LYS A 135      11.992 -23.988 -15.109  1.00 55.34           C
ANISOU 1133  CE  LYS A 135     7122   6607   7299    130    771   -513       C
ATOM   1134  NZ  LYS A 135      10.562 -23.700 -15.459  1.00 58.96           N
ANISOU 1134  NZ  LYS A 135     7627   7066   7708    101    743   -507       N
ATOM   1135  N   GLY A 136       9.037 -24.403 -10.998  1.00 25.47           N
ANISOU 1135  N   GLY A 136     3350   2771   3556    101    607   -430       N
ATOM   1136  CA  GLY A 136       8.400 -25.509 -10.317  1.00 25.85           C
ANISOU 1136  CA  GLY A 136     3420   2784   3618    102    582   -433       C
ATOM   1137  C   GLY A 136       7.215 -25.138  -9.445  1.00 24.05           C
ANISOU 1137  C   GLY A 136     3202   2555   3380     73    549   -413       C
ATOM   1138  O   GLY A 136       6.665 -26.023  -8.780  1.00 26.66           O
ANISOU 1138  O   GLY A 136     3552   2855   3721     68    530   -414       O
ATOM   1139  N   ARG A 137       6.814 -23.868  -9.417  1.00 23.11           N
ANISOU 1139  N   ARG A 137     3073   2468   3242     53    543   -396       N
ATOM   1140  CA  ARG A 137       5.665 -23.405  -8.645  1.00 30.03           C
ANISOU 1140  CA  ARG A 137     3954   3346   4109     26    515   -380       C
ATOM   1141  C   ARG A 137       4.539 -22.926  -9.556  1.00 23.97           C
ANISOU 1141  C   ARG A 137     3203   2597   3306      5    511   -394       C
ATOM   1142  O   ARG A 137       4.697 -22.771 -10.770  1.00 27.97           O
ANISOU 1142  O   ARG A 137     3722   3117   3789     10    527   -410       O
ATOM   1143  CB  ARG A 137       6.055 -22.274  -7.693  1.00 22.04           C
ANISOU 1143  CB  ARG A 137     2915   2351   3107     21    505   -348       C
ATOM   1144  CG  ARG A 137       7.245 -22.572  -6.812  1.00 29.78           C
ANISOU 1144  CG  ARG A 137     3875   3316   4122     41    503   -333       C
ATOM   1145  CD  ARG A 137       7.330 -21.548  -5.683  1.00 25.69           C
ANISOU 1145  CD  ARG A 137     3340   2811   3612     28    485   -301       C
ATOM   1146  NE  ARG A 137       8.374 -21.865  -4.711  1.00 30.58           N
ANISOU 1146  NE  ARG A 137     3943   3413   4264     45    474   -284       N
ATOM   1147  CZ  ARG A 137       8.221 -22.694  -3.680  1.00 30.19           C
ANISOU 1147  CZ  ARG A 137     3911   3328   4230     45    451   -277       C
ATOM   1148  NH1 ARG A 137       7.060 -23.304  -3.465  1.00 28.55           N
ANISOU 1148  NH1 ARG A 137     3736   3102   4010     25    443   -285       N
ATOM   1149  NH2 ARG A 137       9.236 -22.916  -2.857  1.00 28.30           N
ANISOU 1149  NH2 ARG A 137     3659   3074   4021     64    436   -261       N
ATOM   1150  N   THR A 138       3.381 -22.690  -8.943  1.00 20.46           N
ANISOU 1150  N   THR A 138     2762   2154   2858    -18    487   -389       N
ATOM   1151  CA  THR A 138       2.232 -22.129  -9.642  1.00 20.18           C
ANISOU 1151  CA  THR A 138     2736   2136   2795    -36    474   -400       C
ATOM   1152  C   THR A 138       2.270 -20.612  -9.511  1.00 20.85           C
ANISOU 1152  C   THR A 138     2803   2249   2869    -40    468   -378       C
ATOM   1153  O   THR A 138       2.427 -20.091  -8.404  1.00 26.26           O
ANISOU 1153  O   THR A 138     3471   2937   3572    -44    461   -355       O
ATOM   1154  CB  THR A 138       0.920 -22.659  -9.055  1.00 22.31           C
ANISOU 1154  CB  THR A 138     3013   2393   3072    -60    454   -411       C
ATOM   1155  OG1 THR A 138       0.762 -24.048  -9.379  1.00 21.96           O
ANISOU 1155  OG1 THR A 138     2992   2321   3031    -60    460   -435       O
ATOM   1156  CG2 THR A 138      -0.275 -21.882  -9.600  1.00 23.41           C
ANISOU 1156  CG2 THR A 138     3149   2554   3190    -76    435   -421       C
ATOM   1157  N   MET A 139       2.146 -19.905 -10.634  1.00 19.07           N
ANISOU 1157  N   MET A 139     2589   2044   2614    -39    469   -385       N
ATOM   1158  CA  MET A 139       1.893 -18.464 -10.600  1.00 21.09           C
ANISOU 1158  CA  MET A 139     2837   2322   2855    -46    456   -367       C
ATOM   1159  C   MET A 139       0.384 -18.258 -10.524  1.00 25.99           C
ANISOU 1159  C   MET A 139     3459   2946   3471    -61    425   -378       C
ATOM   1160  O   MET A 139      -0.343 -18.587 -11.468  1.00 24.56           O
ANISOU 1160  O   MET A 139     3296   2765   3270    -65    413   -402       O
ATOM   1161  CB  MET A 139       2.470 -17.752 -11.819  1.00 22.43           C
ANISOU 1161  CB  MET A 139     3024   2508   2991    -40    469   -368       C
ATOM   1162  CG  MET A 139       1.889 -16.338 -11.978  1.00 22.06           C
ANISOU 1162  CG  MET A 139     2981   2480   2922    -48    447   -355       C
ATOM   1163  SD  MET A 139       2.470 -15.447 -13.443  1.00 27.11           S
ANISOU 1163  SD  MET A 139     3654   3134   3514    -47    460   -354       S
ATOM   1164  CE  MET A 139       4.149 -15.153 -12.957  1.00 18.69           C
ANISOU 1164  CE  MET A 139     2565   2074   2464    -42    500   -333       C
ATOM   1165  N   TYR A 140      -0.087 -17.729  -9.398  1.00 24.93           N
ANISOU 1165  N   TYR A 140     3303   2813   3354    -70    412   -364       N
ATOM   1166  CA  TYR A 140      -1.492 -17.381  -9.242  1.00 20.61           C
ANISOU 1166  CA  TYR A 140     2749   2273   2809    -84    385   -376       C
ATOM   1167  C   TYR A 140      -1.734 -15.961  -9.731  1.00 20.01           C
ANISOU 1167  C   TYR A 140     2674   2216   2712    -79    367   -366       C
ATOM   1168  O   TYR A 140      -0.942 -15.056  -9.455  1.00 21.14           O
ANISOU 1168  O   TYR A 140     2815   2368   2851    -73    376   -341       O
ATOM   1169  CB  TYR A 140      -1.914 -17.496  -7.778  1.00 20.74           C
ANISOU 1169  CB  TYR A 140     2745   2281   2854    -98    385   -368       C
ATOM   1170  CG  TYR A 140      -1.805 -18.902  -7.252  1.00 18.62           C
ANISOU 1170  CG  TYR A 140     2483   1988   2604   -107    398   -377       C
ATOM   1171  CD1 TYR A 140      -2.849 -19.793  -7.409  1.00 17.83           C
ANISOU 1171  CD1 TYR A 140     2388   1878   2509   -123    390   -404       C
ATOM   1172  CD2 TYR A 140      -0.662 -19.327  -6.585  1.00 16.01           C
ANISOU 1172  CD2 TYR A 140     2155   1642   2286    -98    414   -358       C
ATOM   1173  CE1 TYR A 140      -2.757 -21.100  -6.933  1.00 21.26           C
ANISOU 1173  CE1 TYR A 140     2835   2285   2957   -133    402   -412       C
ATOM   1174  CE2 TYR A 140      -0.556 -20.647  -6.111  1.00 20.83           C
ANISOU 1174  CE2 TYR A 140     2778   2224   2911   -104    422   -365       C
ATOM   1175  CZ  TYR A 140      -1.606 -21.514  -6.283  1.00 26.85           C
ANISOU 1175  CZ  TYR A 140     3552   2976   3676   -122    417   -392       C
ATOM   1176  OH  TYR A 140      -1.499 -22.813  -5.817  1.00 29.13           O
ANISOU 1176  OH  TYR A 140     3859   3232   3976   -129    424   -398       O
ATOM   1177  N   VAL A 141      -2.846 -15.764 -10.436  1.00 23.39           N
ANISOU 1177  N   VAL A 141     3108   2651   3128    -81    340   -386       N
ATOM   1178  CA  VAL A 141      -3.215 -14.449 -10.955  1.00 24.64           C
ANISOU 1178  CA  VAL A 141     3272   2823   3266    -74    314   -380       C
ATOM   1179  C   VAL A 141      -4.437 -13.979 -10.179  1.00 21.63           C
ANISOU 1179  C   VAL A 141     2863   2447   2910    -80    290   -388       C
ATOM   1180  O   VAL A 141      -5.536 -14.519 -10.345  1.00 24.81           O
ANISOU 1180  O   VAL A 141     3255   2849   3324    -87    271   -415       O
ATOM   1181  CB  VAL A 141      -3.488 -14.486 -12.467  1.00 22.41           C
ANISOU 1181  CB  VAL A 141     3023   2544   2949    -68    296   -397       C
ATOM   1182  CG1 VAL A 141      -3.828 -13.108 -12.970  1.00 26.50           C
ANISOU 1182  CG1 VAL A 141     3555   3071   3443    -60    266   -388       C
ATOM   1183  CG2 VAL A 141      -2.272 -15.010 -13.203  1.00 18.04           C
ANISOU 1183  CG2 VAL A 141     2498   1985   2372    -65    328   -394       C
ATOM   1184  N   ILE A 142      -4.251 -12.950  -9.358  1.00 25.25           N
ANISOU 1184  N   ILE A 142     3308   2910   3376    -77    291   -366       N
ATOM   1185  CA  ILE A 142      -5.282 -12.473  -8.440  1.00 27.92           C
ANISOU 1185  CA  ILE A 142     3616   3251   3741    -83    277   -373       C
ATOM   1186  C   ILE A 142      -5.848 -11.162  -8.967  1.00 23.31           C
ANISOU 1186  C   ILE A 142     3036   2676   3143    -67    243   -372       C
ATOM   1187  O   ILE A 142      -5.180 -10.126  -8.854  1.00 23.15           O
ANISOU 1187  O   ILE A 142     3029   2658   3109    -59    246   -347       O
ATOM   1188  CB  ILE A 142      -4.720 -12.259  -7.027  1.00 27.77           C
ANISOU 1188  CB  ILE A 142     3583   3227   3740    -92    303   -350       C
ATOM   1189  CG1 ILE A 142      -4.093 -13.530  -6.467  1.00 24.95           C
ANISOU 1189  CG1 ILE A 142     3228   2857   3395   -104    331   -348       C
ATOM   1190  CG2 ILE A 142      -5.805 -11.789  -6.104  1.00 28.13           C
ANISOU 1190  CG2 ILE A 142     3601   3276   3812   -100    294   -362       C
ATOM   1191  CD1 ILE A 142      -3.330 -13.249  -5.180  1.00 24.00           C
ANISOU 1191  CD1 ILE A 142     3103   2730   3287   -111    350   -321       C
ATOM   1192  N   PRO A 143      -7.039 -11.153  -9.566  1.00 23.81           N
ANISOU 1192  N   PRO A 143     3091   2744   3212    -63    208   -400       N
ATOM   1193  CA  PRO A 143      -7.646  -9.878  -9.954  1.00 23.42           C
ANISOU 1193  CA  PRO A 143     3044   2700   3155    -44    170   -400       C
ATOM   1194  C   PRO A 143      -8.444  -9.356  -8.781  1.00 22.93           C
ANISOU 1194  C   PRO A 143     2941   2640   3130    -46    169   -408       C
ATOM   1195  O   PRO A 143      -9.308 -10.069  -8.267  1.00 25.08           O
ANISOU 1195  O   PRO A 143     3179   2915   3434    -59    173   -435       O
ATOM   1196  CB  PRO A 143      -8.546 -10.250 -11.145  1.00 21.00           C
ANISOU 1196  CB  PRO A 143     2745   2394   2838    -38    129   -430       C
ATOM   1197  CG  PRO A 143      -8.489 -11.811 -11.242  1.00 22.19           C
ANISOU 1197  CG  PRO A 143     2892   2542   2996    -57    152   -448       C
ATOM   1198  CD  PRO A 143      -7.887 -12.292  -9.953  1.00 26.69           C
ANISOU 1198  CD  PRO A 143     3444   3108   3589    -73    198   -434       C
ATOM   1199  N   PHE A 144      -8.159  -8.151  -8.310  1.00 23.46           N
ANISOU 1199  N   PHE A 144     3014   2707   3194    -35    167   -386       N
ATOM   1200  CA  PHE A 144      -8.800  -7.713  -7.085  1.00 17.53           C
ANISOU 1200  CA  PHE A 144     2226   1956   2477    -39    175   -394       C
ATOM   1201  C   PHE A 144      -9.170  -6.244  -7.190  1.00 20.52           C
ANISOU 1201  C   PHE A 144     2609   2334   2852    -15    144   -388       C
ATOM   1202  O   PHE A 144      -8.497  -5.452  -7.861  1.00 20.87           O
ANISOU 1202  O   PHE A 144     2693   2374   2862     -2    130   -365       O
ATOM   1203  CB  PHE A 144      -7.905  -7.979  -5.862  1.00 20.20           C
ANISOU 1203  CB  PHE A 144     2564   2290   2822    -59    221   -370       C
ATOM   1204  CG  PHE A 144      -6.640  -7.182  -5.838  1.00 20.41           C
ANISOU 1204  CG  PHE A 144     2623   2313   2821    -54    232   -332       C
ATOM   1205  CD1 PHE A 144      -5.507  -7.631  -6.501  1.00 22.32           C
ANISOU 1205  CD1 PHE A 144     2892   2554   3035    -56    245   -314       C
ATOM   1206  CD2 PHE A 144      -6.574  -5.969  -5.149  1.00 18.01           C
ANISOU 1206  CD2 PHE A 144     2319   2006   2518    -48    231   -317       C
ATOM   1207  CE1 PHE A 144      -4.334  -6.905  -6.482  1.00 20.24           C
ANISOU 1207  CE1 PHE A 144     2653   2288   2749    -55    258   -282       C
ATOM   1208  CE2 PHE A 144      -5.396  -5.234  -5.129  1.00 25.46           C
ANISOU 1208  CE2 PHE A 144     3291   2945   3435    -47    241   -282       C
ATOM   1209  CZ  PHE A 144      -4.274  -5.708  -5.794  1.00 29.34           C
ANISOU 1209  CZ  PHE A 144     3806   3438   3902    -52    255   -266       C
ATOM   1210  N   SER A 145     -10.263  -5.901  -6.525  1.00 23.64           N
ANISOU 1210  N   SER A 145     2966   2732   3285    -10    135   -413       N
ATOM   1211  CA  SER A 145     -10.733  -4.530  -6.425  1.00 23.24           C
ANISOU 1211  CA  SER A 145     2913   2678   3240     15    107   -413       C
ATOM   1212  C   SER A 145     -10.484  -4.029  -5.007  1.00 25.48           C
ANISOU 1212  C   SER A 145     3185   2957   3540      3    143   -400       C
ATOM   1213  O   SER A 145     -10.791  -4.726  -4.032  1.00 24.81           O
ANISOU 1213  O   SER A 145     3069   2876   3482    -20    177   -415       O
ATOM   1214  CB  SER A 145     -12.223  -4.443  -6.780  1.00 25.53           C
ANISOU 1214  CB  SER A 145     3164   2974   3564     33     66   -455       C
ATOM   1215  OG  SER A 145     -12.733  -3.144  -6.558  1.00 32.48           O
ANISOU 1215  OG  SER A 145     4037   3848   4456     60     40   -459       O
ATOM   1216  N   MET A 146      -9.889  -2.844  -4.901  1.00 23.65           N
ANISOU 1216  N   MET A 146     2982   2716   3287     16    138   -373       N
ATOM   1217  CA  MET A 146      -9.749  -2.127  -3.638  1.00 25.01           C
ANISOU 1217  CA  MET A 146     3148   2882   3472     10    164   -363       C
ATOM   1218  C   MET A 146     -10.918  -1.159  -3.562  1.00 30.24           C
ANISOU 1218  C   MET A 146     3787   3541   4161     38    133   -389       C
ATOM   1219  O   MET A 146     -10.976  -0.188  -4.326  1.00 27.26           O
ANISOU 1219  O   MET A 146     3436   3156   3767     66     93   -382       O
ATOM   1220  CB  MET A 146      -8.412  -1.391  -3.560  1.00 26.96           C
ANISOU 1220  CB  MET A 146     3441   3120   3682      6    175   -319       C
ATOM   1221  CG  MET A 146      -7.200  -2.308  -3.693  1.00 24.96           C
ANISOU 1221  CG  MET A 146     3206   2870   3406    -17    203   -295       C
ATOM   1222  SD  MET A 146      -7.231  -3.612  -2.440  1.00 22.73           S
ANISOU 1222  SD  MET A 146     2893   2591   3152    -49    247   -306       S
ATOM   1223  CE  MET A 146      -7.184  -2.610  -0.940  1.00 26.67           C
ANISOU 1223  CE  MET A 146     3391   3081   3663    -58    267   -294       C
ATOM   1224  N   GLY A 147     -11.856  -1.433  -2.658  1.00 28.48           N
ANISOU 1224  N   GLY A 147     3517   3324   3980     29    152   -422       N
ATOM   1225  CA  GLY A 147     -13.100  -0.711  -2.624  1.00 28.99           C
ANISOU 1225  CA  GLY A 147     3546   3388   4080     57    124   -457       C
ATOM   1226  C   GLY A 147     -14.221  -1.546  -3.204  1.00 34.69           C
ANISOU 1226  C   GLY A 147     4222   4123   4834     61    102   -500       C
ATOM   1227  O   GLY A 147     -13.985  -2.528  -3.915  1.00 30.63           O
ANISOU 1227  O   GLY A 147     3717   3617   4306     48     98   -498       O
ATOM   1228  N   PRO A 148     -15.468  -1.177  -2.903  1.00 39.87           N
ANISOU 1228  N   PRO A 148     4828   4785   5538     78     90   -542       N
ATOM   1229  CA  PRO A 148     -16.607  -1.914  -3.467  1.00 39.10           C
ANISOU 1229  CA  PRO A 148     4679   4702   5476     81     64   -587       C
ATOM   1230  C   PRO A 148     -16.548  -1.909  -4.985  1.00 45.34           C
ANISOU 1230  C   PRO A 148     5497   5490   6240    106      2   -579       C
ATOM   1231  O   PRO A 148     -16.173  -0.910  -5.605  1.00 45.29           O
ANISOU 1231  O   PRO A 148     5533   5470   6205    137    -36   -556       O
ATOM   1232  CB  PRO A 148     -17.825  -1.138  -2.949  1.00 34.42           C
ANISOU 1232  CB  PRO A 148     4030   4110   4937    105     54   -630       C
ATOM   1233  CG  PRO A 148     -17.327  -0.376  -1.754  1.00 38.23           C
ANISOU 1233  CG  PRO A 148     4531   4582   5415     98     98   -611       C
ATOM   1234  CD  PRO A 148     -15.899  -0.030  -2.085  1.00 38.06           C
ANISOU 1234  CD  PRO A 148     4583   4546   5333     97     95   -553       C
ATOM   1235  N   LEU A 149     -16.915  -3.040  -5.581  1.00 46.43           N
ANISOU 1235  N   LEU A 149     5617   5640   6385     90     -7   -600       N
ATOM   1236  C   LEU A 149     -17.654  -2.105  -7.724  1.00 60.10           C
ANISOU 1236  C   LEU A 149     7373   7362   8100    156   -133   -611       C
ATOM   1237  O   LEU A 149     -18.868  -2.007  -7.527  1.00 69.86           O
ANISOU 1237  O   LEU A 149     8547   8608   9391    171   -154   -656       O
ATOM   1238  CA ALEU A 149     -16.829  -3.178  -7.027  1.00 54.67           C
ANISOU 1238  CA ALEU A 149     6692   6681   7398    108    -62   -593       C
ATOM   1239  CB ALEU A 149     -17.292  -4.568  -7.449  1.00 54.49           C
ANISOU 1239  CB ALEU A 149     6643   6673   7388     82    -61   -621       C
ATOM   1240  CG ALEU A 149     -16.199  -5.349  -8.174  1.00 56.16           C
ANISOU 1240  CG ALEU A 149     6912   6880   7546     64    -51   -589       C
ATOM   1241  CD1ALEU A 149     -16.782  -6.582  -8.839  1.00 55.09           C
ANISOU 1241  CD1ALEU A 149     6757   6755   7421     46    -65   -619       C
ATOM   1242  CD2ALEU A 149     -15.487  -4.446  -9.188  1.00 57.99           C
ANISOU 1242  CD2ALEU A 149     7209   7097   7727     92    -91   -554       C
ATOM   1243  CA BLEU A 149     -16.844  -3.191  -7.031  0.00 54.19           C
ANISOU 1243  CA BLEU A 149     6631   6621   7338    108    -62   -594       C
ATOM   1244  CB BLEU A 149     -17.354  -4.572  -7.440  0.00 55.25           C
ANISOU 1244  CB BLEU A 149     6737   6770   7487     83    -62   -623       C
ATOM   1245  CG BLEU A 149     -16.338  -5.713  -7.486  0.00 55.25           C
ANISOU 1245  CG BLEU A 149     6772   6769   7451     46    -19   -598       C
ATOM   1246  CD1BLEU A 149     -17.032  -7.025  -7.811  0.00 55.69           C
ANISOU 1246  CD1BLEU A 149     6795   6836   7527     21    -21   -633       C
ATOM   1247  CD2BLEU A 149     -15.259  -5.412  -8.511  0.00 55.86           C
ANISOU 1247  CD2BLEU A 149     6921   6835   7469     59    -41   -558       C
ATOM   1248  N   GLY A 150     -16.982  -1.295  -8.540  1.00 57.17           N
ANISOU 1248  N   GLY A 150     7066   6974   7681    180   -169   -576       N
ATOM   1249  CA  GLY A 150     -17.628  -0.225  -9.262  1.00 54.82           C
ANISOU 1249  CA  GLY A 150     6779   6663   7388    228   -242   -586       C
ATOM   1250  C   GLY A 150     -17.687   1.099  -8.534  1.00 55.77           C
ANISOU 1250  C   GLY A 150     6899   6768   7522    255   -242   -579       C
ATOM   1251  O   GLY A 150     -18.085   2.099  -9.145  1.00 60.64           O
ANISOU 1251  O   GLY A 150     7537   7368   8136    297   -305   -581       O
ATOM   1252  N   SER A 151     -17.317   1.139  -7.255  1.00 48.86           N
ANISOU 1252  N   SER A 151     6007   5897   6661    232   -176   -572       N
ATOM   1253  CA  SER A 151     -17.312   2.396  -6.517  1.00 50.30           C
ANISOU 1253  CA  SER A 151     6195   6063   6854    255   -171   -565       C
ATOM   1254  C   SER A 151     -16.454   3.430  -7.247  1.00 59.91           C
ANISOU 1254  C   SER A 151     7495   7255   8014    275   -206   -521       C
ATOM   1255  O   SER A 151     -15.397   3.085  -7.794  1.00 59.55           O
ANISOU 1255  O   SER A 151     7504   7207   7914    252   -194   -483       O
ATOM   1256  CB  SER A 151     -16.780   2.182  -5.094  1.00 48.52           C
ANISOU 1256  CB  SER A 151     5957   5844   6636    218    -92   -555       C
ATOM   1257  OG  SER A 151     -16.620   3.418  -4.398  1.00 46.66           O
ANISOU 1257  OG  SER A 151     5738   5590   6402    236    -84   -544       O
ATOM   1258  N   PRO A 152     -16.875   4.699  -7.286  1.00 67.95           N
ANISOU 1258  N   PRO A 152     8525   8251   9041    317   -248   -524       N
ATOM   1259  CA  PRO A 152     -16.051   5.723  -7.952  1.00 66.27           C
ANISOU 1259  CA  PRO A 152     8398   8011   8770    333   -279   -481       C
ATOM   1260  C   PRO A 152     -14.676   5.863  -7.337  1.00 57.06           C
ANISOU 1260  C   PRO A 152     7278   6842   7562    296   -217   -435       C
ATOM   1261  O   PRO A 152     -13.717   6.215  -8.037  1.00 54.26           O
ANISOU 1261  O   PRO A 152     6995   6473   7150    288   -227   -396       O
ATOM   1262  CB  PRO A 152     -16.873   7.009  -7.779  1.00 71.76           C
ANISOU 1262  CB  PRO A 152     9087   8683   9497    384   -325   -500       C
ATOM   1263  CG  PRO A 152     -18.261   6.550  -7.464  1.00 75.76           C
ANISOU 1263  CG  PRO A 152     9501   9208  10077    402   -339   -559       C
ATOM   1264  CD  PRO A 152     -18.106   5.266  -6.713  1.00 73.66           C
ANISOU 1264  CD  PRO A 152     9185   8972   9828    352   -267   -570       C
ATOM   1265  N   LEU A 153     -14.549   5.594  -6.043  1.00 46.23           N
ANISOU 1265  N   LEU A 153     5867   5481   6217    271   -155   -441       N
ATOM   1266  CA  LEU A 153     -13.260   5.621  -5.374  1.00 44.53           C
ANISOU 1266  CA  LEU A 153     5688   5265   5968    233    -99   -401       C
ATOM   1267  C   LEU A 153     -12.527   4.277  -5.440  1.00 36.31           C
ANISOU 1267  C   LEU A 153     4642   4245   4908    191    -57   -388       C
ATOM   1268  O   LEU A 153     -11.514   4.111  -4.759  1.00 38.25           O
ANISOU 1268  O   LEU A 153     4904   4493   5135    159     -8   -360       O
ATOM   1269  CB  LEU A 153     -13.446   6.078  -3.918  1.00 47.91           C
ANISOU 1269  CB  LEU A 153     6086   5690   6428    228    -56   -411       C
ATOM   1270  CG  LEU A 153     -14.007   7.513  -3.798  1.00 52.95           C
ANISOU 1270  CG  LEU A 153     6738   6302   7080    270    -92   -420       C
ATOM   1271  CD1 LEU A 153     -14.093   8.017  -2.352  1.00 48.89           C
ANISOU 1271  CD1 LEU A 153     6203   5782   6591    262    -46   -429       C
ATOM   1272  CD2 LEU A 153     -13.195   8.488  -4.654  1.00 54.91           C
ANISOU 1272  CD2 LEU A 153     7068   6524   7271    283   -129   -379       C
ATOM   1273  N   ALA A 154     -12.986   3.334  -6.260  1.00 31.39           N
ANISOU 1273  N   ALA A 154     4000   3636   4292    191    -79   -408       N
ATOM   1274  CA  ALA A 154     -12.405   1.994  -6.294  1.00 39.95           C
ANISOU 1274  CA  ALA A 154     5076   4738   5365    154    -40   -402       C
ATOM   1275  C   ALA A 154     -11.345   1.878  -7.385  1.00 37.04           C
ANISOU 1275  C   ALA A 154     4771   4365   4939    145    -49   -367       C
ATOM   1276  O   ALA A 154     -11.463   2.488  -8.451  1.00 42.52           O
ANISOU 1276  O   ALA A 154     5505   5046   5606    169    -99   -361       O
ATOM   1277  CB  ALA A 154     -13.480   0.927  -6.506  1.00 40.27           C
ANISOU 1277  CB  ALA A 154     5061   4796   5445    153    -51   -445       C
ATOM   1278  N   LYS A 155     -10.310   1.084  -7.104  1.00 29.42           N
ANISOU 1278  N   LYS A 155     3814   3409   3956    111     -0   -346       N
ATOM   1279  CA  LYS A 155      -9.199   0.826  -8.016  1.00 20.73           C
ANISOU 1279  CA  LYS A 155     2765   2307   2805     97      6   -316       C
ATOM   1280  C   LYS A 155      -8.932  -0.674  -8.070  1.00 26.72           C
ANISOU 1280  C   LYS A 155     3501   3082   3569     71     38   -325       C
ATOM   1281  O   LYS A 155      -9.099  -1.387  -7.078  1.00 26.99           O
ANISOU 1281  O   LYS A 155     3494   3126   3637     54     72   -337       O
ATOM   1282  CB  LYS A 155      -7.935   1.541  -7.554  1.00 23.25           C
ANISOU 1282  CB  LYS A 155     3121   2619   3095     81     38   -277       C
ATOM   1283  CG  LYS A 155      -8.068   3.071  -7.452  1.00 32.10           C
ANISOU 1283  CG  LYS A 155     4272   3718   4205    102     11   -264       C
ATOM   1284  CD  LYS A 155      -8.010   3.693  -8.821  1.00 39.72           C
ANISOU 1284  CD  LYS A 155     5297   4670   5127    119    -35   -253       C
ATOM   1285  CE  LYS A 155      -7.450   5.100  -8.783  1.00 53.73           C
ANISOU 1285  CE  LYS A 155     7123   6420   6870    123    -44   -224       C
ATOM   1286  NZ  LYS A 155      -6.852   5.452 -10.105  1.00 59.15           N
ANISOU 1286  NZ  LYS A 155     7881   7095   7498    120    -65   -202       N
ATOM   1287  N   ILE A 156      -8.492  -1.144  -9.230  1.00 27.52           N
ANISOU 1287  N   ILE A 156     3637   3185   3636     68     27   -319       N
ATOM   1288  CA  ILE A 156      -8.314  -2.567  -9.478  1.00 26.55           C
ANISOU 1288  CA  ILE A 156     3498   3073   3515     48     50   -330       C
ATOM   1289  C   ILE A 156      -6.833  -2.861  -9.648  1.00 24.43           C
ANISOU 1289  C   ILE A 156     3264   2806   3213     27     91   -300       C
ATOM   1290  O   ILE A 156      -6.094  -2.072 -10.250  1.00 23.16           O
ANISOU 1290  O   ILE A 156     3150   2637   3012     29     86   -275       O
ATOM   1291  CB  ILE A 156      -9.121  -3.012 -10.710  1.00 22.32           C
ANISOU 1291  CB  ILE A 156     2971   2538   2971     62      5   -356       C
ATOM   1292  CG1 ILE A 156     -10.615  -2.894 -10.412  1.00 26.40           C
ANISOU 1292  CG1 ILE A 156     3438   3058   3534     80    -32   -393       C
ATOM   1293  CG2 ILE A 156      -8.734  -4.448 -11.148  1.00 23.18           C
ANISOU 1293  CG2 ILE A 156     3080   2657   3073     40     30   -364       C
ATOM   1294  CD1 ILE A 156     -11.494  -3.057 -11.624  1.00 27.77           C
ANISOU 1294  CD1 ILE A 156     3620   3230   3700     98    -91   -418       C
ATOM   1295  N   GLY A 157      -6.402  -4.003  -9.108  1.00 27.07           N
ANISOU 1295  N   GLY A 157     3574   3149   3564      7    131   -302       N
ATOM   1296  CA  GLY A 157      -5.052  -4.471  -9.308  1.00 20.06           C
ANISOU 1296  CA  GLY A 157     2709   2262   2651    -10    168   -280       C
ATOM   1297  C   GLY A 157      -5.053  -5.921  -9.753  1.00 22.37           C
ANISOU 1297  C   GLY A 157     2992   2560   2948    -19    181   -299       C
ATOM   1298  O   GLY A 157      -6.053  -6.630  -9.654  1.00 24.14           O
ANISOU 1298  O   GLY A 157     3188   2786   3198    -19    168   -327       O
ATOM   1299  N   ILE A 158      -3.912  -6.336 -10.289  1.00 20.71           N
ANISOU 1299  N   ILE A 158     2807   2350   2713    -28    208   -285       N
ATOM   1300  CA  ILE A 158      -3.635  -7.737 -10.586  1.00 20.12           C
ANISOU 1300  CA  ILE A 158     2727   2277   2642    -38    230   -299       C
ATOM   1301  C   ILE A 158      -2.398  -8.101  -9.786  1.00 21.13           C
ANISOU 1301  C   ILE A 158     2844   2406   2780    -50    274   -278       C
ATOM   1302  O   ILE A 158      -1.342  -7.491  -9.980  1.00 22.46           O
ANISOU 1302  O   ILE A 158     3032   2575   2927    -52    291   -256       O
ATOM   1303  CB  ILE A 158      -3.388  -7.986 -12.083  1.00 19.88           C
ANISOU 1303  CB  ILE A 158     2738   2246   2571    -35    222   -306       C
ATOM   1304  CG1 ILE A 158      -4.541  -7.473 -12.953  1.00 23.06           C
ANISOU 1304  CG1 ILE A 158     3159   2645   2958    -21    169   -323       C
ATOM   1305  CG2 ILE A 158      -3.128  -9.485 -12.326  1.00 21.92           C
ANISOU 1305  CG2 ILE A 158     2990   2504   2837    -43    246   -323       C
ATOM   1306  CD1 ILE A 158      -5.845  -8.242 -12.814  1.00 23.78           C
ANISOU 1306  CD1 ILE A 158     3216   2738   3080    -19    143   -356       C
ATOM   1307  N   GLU A 159      -2.514  -9.080  -8.885  1.00 18.83           N
ANISOU 1307  N   GLU A 159     2522   2111   2521    -58    290   -287       N
ATOM   1308  CA  GLU A 159      -1.343  -9.566  -8.164  1.00 17.81           C
ANISOU 1308  CA  GLU A 159     2384   1980   2404    -66    325   -269       C
ATOM   1309  C   GLU A 159      -0.955 -10.934  -8.715  1.00 20.61           C
ANISOU 1309  C   GLU A 159     2743   2330   2759    -67    343   -284       C
ATOM   1310  O   GLU A 159      -1.785 -11.846  -8.775  1.00 20.80           O
ANISOU 1310  O   GLU A 159     2759   2349   2795    -70    334   -308       O
ATOM   1311  CB  GLU A 159      -1.557  -9.646  -6.649  1.00 19.41           C
ANISOU 1311  CB  GLU A 159     2559   2176   2638    -76    332   -263       C
ATOM   1312  CG  GLU A 159      -0.346 -10.326  -5.967  1.00 18.29           C
ANISOU 1312  CG  GLU A 159     2411   2028   2508    -83    361   -246       C
ATOM   1313  CD  GLU A 159      -0.142 -10.012  -4.489  1.00 22.02           C
ANISOU 1313  CD  GLU A 159     2870   2494   3000    -93    367   -228       C
ATOM   1314  OE1 GLU A 159      -0.933  -9.240  -3.893  1.00 20.52           O
ANISOU 1314  OE1 GLU A 159     2675   2306   2816    -97    355   -229       O
ATOM   1315  OE2 GLU A 159       0.836 -10.556  -3.918  1.00 19.98           O
ANISOU 1315  OE2 GLU A 159     2609   2230   2754    -97    383   -214       O
ATOM   1316  N   LEU A 160       0.296 -11.051  -9.144  1.00 18.68           N
ANISOU 1316  N   LEU A 160     2511   2087   2501    -66    368   -272       N
ATOM   1317  CA  LEU A 160       0.911 -12.320  -9.498  1.00 19.39           C
ANISOU 1317  CA  LEU A 160     2601   2170   2596    -64    391   -284       C
ATOM   1318  C   LEU A 160       1.664 -12.808  -8.279  1.00 24.07           C
ANISOU 1318  C   LEU A 160     3170   2756   3220    -66    409   -270       C
ATOM   1319  O   LEU A 160       2.409 -12.036  -7.670  1.00 23.60           O
ANISOU 1319  O   LEU A 160     3101   2700   3164    -68    416   -246       O
ATOM   1320  CB  LEU A 160       1.875 -12.142 -10.673  1.00 15.52           C
ANISOU 1320  CB  LEU A 160     2135   1687   2076    -60    411   -283       C
ATOM   1321  CG  LEU A 160       1.296 -11.364 -11.843  1.00 21.07           C
ANISOU 1321  CG  LEU A 160     2872   2395   2739    -60    391   -289       C
ATOM   1322  CD1 LEU A 160       2.320 -11.276 -12.985  1.00 18.16           C
ANISOU 1322  CD1 LEU A 160     2533   2031   2336    -62    419   -289       C
ATOM   1323  CD2 LEU A 160      -0.017 -11.991 -12.289  1.00 17.00           C
ANISOU 1323  CD2 LEU A 160     2363   1875   2222    -58    361   -316       C
ATOM   1324  N   THR A 161       1.474 -14.076  -7.922  1.00 19.06           N
ANISOU 1324  N   THR A 161     2529   2107   2607    -67    413   -284       N
ATOM   1325  CA  THR A 161       2.143 -14.580  -6.738  1.00 17.23           C
ANISOU 1325  CA  THR A 161     2281   1863   2402    -68    424   -270       C
ATOM   1326  C   THR A 161       2.321 -16.077  -6.881  1.00 18.89           C
ANISOU 1326  C   THR A 161     2496   2055   2626    -63    434   -288       C
ATOM   1327  O   THR A 161       1.534 -16.752  -7.545  1.00 21.52           O
ANISOU 1327  O   THR A 161     2841   2383   2951    -65    429   -312       O
ATOM   1328  CB  THR A 161       1.366 -14.266  -5.437  1.00 19.08           C
ANISOU 1328  CB  THR A 161     2505   2092   2653    -82    410   -262       C
ATOM   1329  OG1 THR A 161       2.081 -14.796  -4.315  1.00 21.21           O
ANISOU 1329  OG1 THR A 161     2768   2347   2945    -85    417   -246       O
ATOM   1330  CG2 THR A 161      -0.027 -14.872  -5.459  1.00 18.80           C
ANISOU 1330  CG2 THR A 161     2471   2050   2622    -93    398   -287       C
ATOM   1331  N   ASP A 162       3.381 -16.582  -6.267  1.00 15.73           N
ANISOU 1331  N   ASP A 162     2087   1644   2246    -55    446   -276       N
ATOM   1332  CA  ASP A 162       3.596 -18.009  -6.190  1.00 19.31           C
ANISOU 1332  CA  ASP A 162     2546   2074   2716    -48    453   -290       C
ATOM   1333  C   ASP A 162       3.242 -18.563  -4.817  1.00 20.39           C
ANISOU 1333  C   ASP A 162     2684   2188   2874    -60    441   -281       C
ATOM   1334  O   ASP A 162       3.600 -19.705  -4.510  1.00 22.24           O
ANISOU 1334  O   ASP A 162     2927   2398   3125    -53    444   -286       O
ATOM   1335  CB  ASP A 162       5.038 -18.344  -6.564  1.00 20.80           C
ANISOU 1335  CB  ASP A 162     2727   2262   2915    -27    473   -287       C
ATOM   1336  CG  ASP A 162       6.058 -17.601  -5.727  1.00 25.02           C
ANISOU 1336  CG  ASP A 162     3239   2803   3466    -24    473   -260       C
ATOM   1337  OD1 ASP A 162       5.672 -16.935  -4.742  1.00 23.91           O
ANISOU 1337  OD1 ASP A 162     3095   2663   3327    -38    457   -241       O
ATOM   1338  OD2 ASP A 162       7.265 -17.665  -6.073  1.00 27.86           O
ANISOU 1338  OD2 ASP A 162     3583   3167   3836     -8    490   -259       O
ATOM   1339  N   SER A 163       2.535 -17.786  -3.996  1.00 22.15           N
ANISOU 1339  N   SER A 163     2904   2418   3096    -78    429   -269       N
ATOM   1340  CA  SER A 163       2.154 -18.190  -2.645  1.00 24.04           C
ANISOU 1340  CA  SER A 163     3149   2636   3350    -95    422   -261       C
ATOM   1341  C   SER A 163       0.652 -18.402  -2.556  1.00 25.49           C
ANISOU 1341  C   SER A 163     3338   2817   3529   -117    417   -282       C
ATOM   1342  O   SER A 163      -0.110 -17.424  -2.619  1.00 23.68           O
ANISOU 1342  O   SER A 163     3098   2607   3292   -126    412   -284       O
ATOM   1343  CB  SER A 163       2.580 -17.142  -1.620  1.00 25.30           C
ANISOU 1343  CB  SER A 163     3299   2801   3512   -101    416   -233       C
ATOM   1344  OG  SER A 163       1.887 -17.335  -0.391  1.00 22.54           O
ANISOU 1344  OG  SER A 163     2961   2435   3168   -124    410   -229       O
ATOM   1345  N   PRO A 164       0.180 -19.634  -2.363  1.00 20.88           N
ANISOU 1345  N   PRO A 164     2771   2210   2953   -129    419   -298       N
ATOM   1346  CA  PRO A 164      -1.253 -19.831  -2.106  1.00 19.99           C
ANISOU 1346  CA  PRO A 164     2659   2095   2840   -156    418   -319       C
ATOM   1347  C   PRO A 164      -1.739 -19.133  -0.847  1.00 22.07           C
ANISOU 1347  C   PRO A 164     2918   2360   3109   -179    418   -306       C
ATOM   1348  O   PRO A 164      -2.912 -18.744  -0.776  1.00 19.47           O
ANISOU 1348  O   PRO A 164     2575   2042   2780   -197    418   -324       O
ATOM   1349  CB  PRO A 164      -1.374 -21.356  -1.985  1.00 20.15           C
ANISOU 1349  CB  PRO A 164     2704   2083   2867   -166    423   -333       C
ATOM   1350  CG  PRO A 164      -0.004 -21.817  -1.624  1.00 27.96           C
ANISOU 1350  CG  PRO A 164     3707   3053   3864   -145    423   -312       C
ATOM   1351  CD  PRO A 164       0.913 -20.911  -2.396  1.00 24.58           C
ANISOU 1351  CD  PRO A 164     3258   2651   3431   -117    423   -300       C
ATOM   1352  N   TYR A 165      -0.870 -18.970   0.153  1.00 20.36           N
ANISOU 1352  N   TYR A 165     2710   2129   2895   -178    418   -279       N
ATOM   1353  CA  TYR A 165      -1.267 -18.272   1.368  1.00 21.06           C
ANISOU 1353  CA  TYR A 165     2799   2217   2984   -200    420   -266       C
ATOM   1354  C   TYR A 165      -1.637 -16.826   1.059  1.00 23.19           C
ANISOU 1354  C   TYR A 165     3044   2517   3248   -195    417   -265       C
ATOM   1355  O   TYR A 165      -2.563 -16.264   1.660  1.00 20.10           O
ANISOU 1355  O   TYR A 165     2646   2132   2860   -214    422   -273       O
ATOM   1356  CB  TYR A 165      -0.132 -18.345   2.394  1.00 19.70           C
ANISOU 1356  CB  TYR A 165     2646   2024   2815   -198    415   -235       C
ATOM   1357  CG  TYR A 165      -0.263 -17.349   3.548  1.00 23.31           C
ANISOU 1357  CG  TYR A 165     3105   2483   3267   -216    415   -217       C
ATOM   1358  CD1 TYR A 165       0.232 -16.050   3.440  1.00 20.07           C
ANISOU 1358  CD1 TYR A 165     2677   2097   2853   -202    409   -201       C
ATOM   1359  CD2 TYR A 165      -0.866 -17.720   4.741  1.00 27.36           C
ANISOU 1359  CD2 TYR A 165     3643   2974   3777   -249    423   -218       C
ATOM   1360  CE1 TYR A 165       0.114 -15.141   4.487  1.00 24.91           C
ANISOU 1360  CE1 TYR A 165     3295   2709   3460   -219    410   -186       C
ATOM   1361  CE2 TYR A 165      -0.990 -16.820   5.794  1.00 28.32           C
ANISOU 1361  CE2 TYR A 165     3771   3096   3892   -268    426   -204       C
ATOM   1362  CZ  TYR A 165      -0.497 -15.532   5.659  1.00 23.35           C
ANISOU 1362  CZ  TYR A 165     3122   2489   3259   -251    419   -188       C
ATOM   1363  OH  TYR A 165      -0.624 -14.648   6.711  1.00 23.45           O
ANISOU 1363  OH  TYR A 165     3145   2501   3265   -270    422   -175       O
ATOM   1364  N   VAL A 166      -0.923 -16.213   0.111  1.00 20.92           N
ANISOU 1364  N   VAL A 166     2745   2249   2954   -168    410   -257       N
ATOM   1365  CA  VAL A 166      -1.259 -14.865  -0.334  1.00 20.71           C
ANISOU 1365  CA  VAL A 166     2701   2248   2918   -160    404   -256       C
ATOM   1366  C   VAL A 166      -2.614 -14.858  -1.035  1.00 22.64           C
ANISOU 1366  C   VAL A 166     2934   2505   3164   -165    398   -288       C
ATOM   1367  O   VAL A 166      -3.415 -13.941  -0.845  1.00 20.83           O
ANISOU 1367  O   VAL A 166     2690   2287   2935   -169    393   -295       O
ATOM   1368  CB  VAL A 166      -0.143 -14.314  -1.248  1.00 23.03           C
ANISOU 1368  CB  VAL A 166     2993   2557   3201   -135    401   -241       C
ATOM   1369  CG1 VAL A 166      -0.619 -13.095  -1.996  1.00 18.81           C
ANISOU 1369  CG1 VAL A 166     2450   2044   2652   -127    391   -245       C
ATOM   1370  CG2 VAL A 166       1.106 -13.974  -0.446  1.00 22.58           C
ANISOU 1370  CG2 VAL A 166     2938   2493   3148   -133    402   -211       C
ATOM   1371  N   VAL A 167      -2.902 -15.885  -1.847  1.00 21.74           N
ANISOU 1371  N   VAL A 167     2825   2387   3050   -163    398   -310       N
ATOM   1372  CA  VAL A 167      -4.178 -15.912  -2.566  1.00 19.13           C
ANISOU 1372  CA  VAL A 167     2481   2068   2722   -168    387   -341       C
ATOM   1373  C   VAL A 167      -5.340 -16.001  -1.587  1.00 21.15           C
ANISOU 1373  C   VAL A 167     2723   2319   2995   -196    394   -359       C
ATOM   1374  O   VAL A 167      -6.329 -15.271  -1.702  1.00 21.56           O
ANISOU 1374  O   VAL A 167     2752   2386   3053   -198    385   -376       O
ATOM   1375  CB  VAL A 167      -4.220 -17.076  -3.571  1.00 19.60           C
ANISOU 1375  CB  VAL A 167     2551   2120   2776   -165    386   -362       C
ATOM   1376  CG1 VAL A 167      -5.579 -17.084  -4.291  1.00 20.22           C
ANISOU 1376  CG1 VAL A 167     2614   2211   2858   -172    369   -396       C
ATOM   1377  CG2 VAL A 167      -3.082 -16.952  -4.571  1.00 18.19           C
ANISOU 1377  CG2 VAL A 167     2385   1946   2579   -138    385   -349       C
ATOM   1378  N   ALA A 168      -5.251 -16.929  -0.635  1.00 24.69           N
ANISOU 1378  N   ALA A 168     3186   2743   3450   -219    411   -356       N
ATOM   1379  CA  ALA A 168      -6.312 -17.087   0.356  1.00 20.45           C
ANISOU 1379  CA  ALA A 168     2642   2201   2928   -253    426   -374       C
ATOM   1380  C   ALA A 168      -6.498 -15.801   1.149  1.00 20.20           C
ANISOU 1380  C   ALA A 168     2597   2180   2898   -254    429   -363       C
ATOM   1381  O   ALA A 168      -7.625 -15.343   1.371  1.00 22.64           O
ANISOU 1381  O   ALA A 168     2881   2500   3221   -267    433   -387       O
ATOM   1382  CB  ALA A 168      -5.972 -18.255   1.282  1.00 25.82           C
ANISOU 1382  CB  ALA A 168     3354   2848   3607   -278    443   -366       C
ATOM   1383  N   SER A 169      -5.395 -15.191   1.553  1.00 19.78           N
ANISOU 1383  N   SER A 169     2559   2124   2834   -241    427   -329       N
ATOM   1384  CA  SER A 169      -5.467 -13.971   2.349  1.00 20.06           C
ANISOU 1384  CA  SER A 169     2588   2166   2870   -243    430   -317       C
ATOM   1385  C   SER A 169      -6.040 -12.804   1.546  1.00 24.01           C
ANISOU 1385  C   SER A 169     3060   2690   3371   -221    414   -328       C
ATOM   1386  O   SER A 169      -6.808 -11.993   2.081  1.00 21.38           O
ANISOU 1386  O   SER A 169     2712   2365   3048   -228    418   -340       O
ATOM   1387  CB  SER A 169      -4.074 -13.643   2.882  1.00 19.02           C
ANISOU 1387  CB  SER A 169     2478   2024   2724   -234    428   -277       C
ATOM   1388  OG  SER A 169      -3.640 -14.645   3.787  1.00 25.51           O
ANISOU 1388  OG  SER A 169     3327   2819   3546   -255    438   -267       O
ATOM   1389  N   MET A 170      -5.689 -12.710   0.257  1.00 19.31           N
ANISOU 1389  N   MET A 170     2463   2107   2766   -195    394   -327       N
ATOM   1390  CA  MET A 170      -6.197 -11.628  -0.589  1.00 18.75           C
ANISOU 1390  CA  MET A 170     2376   2056   2693   -173    372   -337       C
ATOM   1391  C   MET A 170      -7.687 -11.794  -0.852  1.00 20.69           C
ANISOU 1391  C   MET A 170     2593   2311   2959   -179    365   -377       C
ATOM   1392  O   MET A 170      -8.409 -10.801  -1.021  1.00 23.78           O
ANISOU 1392  O   MET A 170     2964   2714   3358   -166    349   -389       O
ATOM   1393  CB  MET A 170      -5.419 -11.581  -1.917  1.00 17.63           C
ANISOU 1393  CB  MET A 170     2247   1921   2529   -148    356   -326       C
ATOM   1394  CG  MET A 170      -3.999 -11.048  -1.789  1.00 18.63           C
ANISOU 1394  CG  MET A 170     2393   2046   2640   -138    361   -289       C
ATOM   1395  SD  MET A 170      -3.974  -9.259  -1.539  1.00 22.24           S
ANISOU 1395  SD  MET A 170     2850   2512   3087   -127    350   -272       S
ATOM   1396  CE  MET A 170      -4.544  -8.728  -3.147  1.00 18.60           C
ANISOU 1396  CE  MET A 170     2390   2065   2612   -103    320   -289       C
ATOM   1397  N   ARG A 171      -8.167 -13.037  -0.860  1.00 16.83           N
ANISOU 1397  N   ARG A 171     2100   1814   2480   -200    375   -399       N
ATOM   1398  CA  ARG A 171      -9.602 -13.273  -0.975  1.00 15.44           C
ANISOU 1398  CA  ARG A 171     1891   1647   2328   -213    371   -440       C
ATOM   1399  C   ARG A 171     -10.356 -12.667   0.200  1.00 18.80           C
ANISOU 1399  C   ARG A 171     2295   2073   2774   -230    390   -452       C
ATOM   1400  O   ARG A 171     -11.499 -12.224   0.046  1.00 22.24           O
ANISOU 1400  O   ARG A 171     2695   2524   3233   -228    380   -484       O
ATOM   1401  CB  ARG A 171      -9.900 -14.781  -1.032  1.00 19.09           C
ANISOU 1401  CB  ARG A 171     2360   2098   2797   -239    384   -460       C
ATOM   1402  CG  ARG A 171     -11.363 -15.064  -1.393  1.00 24.19           C
ANISOU 1402  CG  ARG A 171     2967   2755   3468   -253    375   -506       C
ATOM   1403  CD  ARG A 171     -11.715 -16.556  -1.338  1.00 26.90           C
ANISOU 1403  CD  ARG A 171     3319   3085   3817   -287    391   -526       C
ATOM   1404  NE  ARG A 171     -12.982 -16.833  -2.014  1.00 29.83           N
ANISOU 1404  NE  ARG A 171     3654   3471   4211   -295    374   -570       N
ATOM   1405  CZ  ARG A 171     -14.166 -16.886  -1.407  1.00 35.66           C
ANISOU 1405  CZ  ARG A 171     4353   4216   4979   -324    389   -605       C
ATOM   1406  NH1 ARG A 171     -14.256 -16.686  -0.097  1.00 29.39           N
ANISOU 1406  NH1 ARG A 171     3559   3415   4194   -349    426   -601       N
ATOM   1407  NH2 ARG A 171     -15.262 -17.144  -2.112  1.00 32.23           N
ANISOU 1407  NH2 ARG A 171     3882   3796   4567   -330    368   -646       N
ATOM   1408  N   ILE A 172      -9.741 -12.663   1.379  1.00 19.75           N
ANISOU 1408  N   ILE A 172     2438   2179   2888   -248    417   -429       N
ATOM   1409  CA  ILE A 172     -10.377 -12.067   2.550  1.00 18.29           C
ANISOU 1409  CA  ILE A 172     2240   1993   2717   -268    440   -439       C
ATOM   1410  C   ILE A 172     -10.186 -10.557   2.553  1.00 20.38           C
ANISOU 1410  C   ILE A 172     2498   2266   2977   -239    425   -425       C
ATOM   1411  O   ILE A 172     -11.123  -9.796   2.835  1.00 24.70           O
ANISOU 1411  O   ILE A 172     3016   2823   3545   -237    428   -449       O
ATOM   1412  CB  ILE A 172      -9.812 -12.693   3.839  1.00 20.05           C
ANISOU 1412  CB  ILE A 172     2497   2191   2928   -302    472   -420       C
ATOM   1413  CG1 ILE A 172     -10.188 -14.175   3.940  1.00 23.65           C
ANISOU 1413  CG1 ILE A 172     2963   2634   3390   -335    489   -438       C
ATOM   1414  CG2 ILE A 172     -10.296 -11.929   5.072  1.00 22.95           C
ANISOU 1414  CG2 ILE A 172     2860   2556   3303   -321    499   -426       C
ATOM   1415  CD1 ILE A 172      -9.403 -14.917   4.998  1.00 21.72           C
ANISOU 1415  CD1 ILE A 172     2765   2360   3127   -362    510   -412       C
ATOM   1416  N  AMET A 173      -8.964 -10.100   2.263  0.00 21.67           N
ANISOU 1416  N  AMET A 173     2691   2428   3117   -219    411   -387       N
ATOM   1417  CA AMET A 173      -8.619  -8.687   2.389  0.00 22.31           C
ANISOU 1417  CA AMET A 173     2776   2512   3188   -197    400   -368       C
ATOM   1418  C  AMET A 173      -9.204  -7.837   1.272  0.00 23.19           C
ANISOU 1418  C  AMET A 173     2867   2640   3305   -164    366   -383       C
ATOM   1419  O  AMET A 173      -9.497  -6.656   1.491  0.00 23.52           O
ANISOU 1419  O  AMET A 173     2902   2684   3351   -149    358   -384       O
ATOM   1420  CB AMET A 173      -7.097  -8.515   2.409  0.00 21.45           C
ANISOU 1420  CB AMET A 173     2701   2395   3052   -190    397   -324       C
ATOM   1421  CG AMET A 173      -6.418  -8.929   3.702  0.00 21.01           C
ANISOU 1421  CG AMET A 173     2671   2321   2990   -218    422   -303       C
ATOM   1422  SD AMET A 173      -6.928  -7.920   5.105  0.00 20.49           S
ANISOU 1422  SD AMET A 173     2607   2249   2929   -236    442   -306       S
ATOM   1423  CE AMET A 173      -8.056  -9.041   5.922  0.00 20.74           C
ANISOU 1423  CE AMET A 173     2629   2272   2980   -275    475   -341       C
ATOM   1424  N  BMET A 173      -8.986 -10.090   2.228  1.00 22.33           N
ANISOU 1424  N  BMET A 173     2772   2511   3200   -218    410   -388       N
ATOM   1425  CA BMET A 173      -8.664  -8.682   2.419  1.00 21.63           C
ANISOU 1425  CA BMET A 173     2689   2427   3104   -198    401   -369       C
ATOM   1426  C  BMET A 173      -9.041  -7.809   1.228  1.00 23.09           C
ANISOU 1426  C  BMET A 173     2858   2626   3288   -162    365   -378       C
ATOM   1427  O  BMET A 173      -9.004  -6.582   1.343  1.00 24.07           O
ANISOU 1427  O  BMET A 173     2985   2752   3409   -145    355   -369       O
ATOM   1428  CB BMET A 173      -7.167  -8.519   2.715  1.00 22.77           C
ANISOU 1428  CB BMET A 173     2869   2560   3221   -196    403   -325       C
ATOM   1429  CG BMET A 173      -6.699  -9.185   3.984  1.00 19.89           C
ANISOU 1429  CG BMET A 173     2527   2177   2853   -228    430   -310       C
ATOM   1430  SD BMET A 173      -7.596  -8.564   5.441  1.00 20.68           S
ANISOU 1430  SD BMET A 173     2622   2269   2965   -255    458   -327       S
ATOM   1431  CE BMET A 173      -7.355  -6.799   5.222  1.00 14.56           C
ANISOU 1431  CE BMET A 173     1845   1503   2182   -224    439   -312       C
ATOM   1432  N   THR A 174      -9.361  -8.399   0.079  1.00 24.31           N
ANISOU 1432  N   THR A 174     3003   2789   3444   -151    344   -395       N
ATOM   1433  CA  THR A 174      -9.785  -7.646  -1.088  1.00 22.04           C
ANISOU 1433  CA  THR A 174     2707   2513   3154   -119    305   -405       C
ATOM   1434  C   THR A 174     -11.036  -8.297  -1.652  1.00 19.52           C
ANISOU 1434  C   THR A 174     2353   2203   2860   -121    290   -448       C
ATOM   1435  O   THR A 174     -11.457  -9.364  -1.207  1.00 22.87           O
ANISOU 1435  O   THR A 174     2763   2626   3301   -149    313   -467       O
ATOM   1436  CB  THR A 174      -8.676  -7.593  -2.156  1.00 20.27           C
ANISOU 1436  CB  THR A 174     2517   2288   2896   -102    287   -376       C
ATOM   1437  OG1 THR A 174      -8.501  -8.904  -2.716  1.00 20.70           O
ANISOU 1437  OG1 THR A 174     2577   2342   2946   -112    292   -383       O
ATOM   1438  CG2 THR A 174      -7.366  -7.186  -1.525  1.00 18.26           C
ANISOU 1438  CG2 THR A 174     2291   2025   2620   -107    307   -336       C
ATOM   1439  N   ARG A 175     -11.645  -7.641  -2.633  1.00 21.99           N
ANISOU 1439  N   ARG A 175     2654   2524   3176    -92    249   -463       N
ATOM   1440  CA  ARG A 175     -12.670  -8.284  -3.442  1.00 25.46           C
ANISOU 1440  CA  ARG A 175     3065   2974   3635    -90    224   -501       C
ATOM   1441  C   ARG A 175     -11.982  -8.868  -4.669  1.00 23.60           C
ANISOU 1441  C   ARG A 175     2864   2737   3366    -82    204   -486       C
ATOM   1442  O   ARG A 175     -11.396  -8.133  -5.468  1.00 23.07           O
ANISOU 1442  O   ARG A 175     2828   2668   3269    -58    179   -464       O
ATOM   1443  CB  ARG A 175     -13.777  -7.306  -3.815  1.00 28.75           C
ANISOU 1443  CB  ARG A 175     3449   3399   4076    -61    184   -528       C
ATOM   1444  CG  ARG A 175     -14.588  -6.829  -2.604  1.00 27.30           C
ANISOU 1444  CG  ARG A 175     3225   3218   3932    -69    209   -552       C
ATOM   1445  CD  ARG A 175     -14.697  -5.323  -2.575  1.00 27.49           C
ANISOU 1445  CD  ARG A 175     3250   3237   3956    -34    184   -545       C
ATOM   1446  NE  ARG A 175     -15.624  -4.830  -1.557  1.00 25.26           N
ANISOU 1446  NE  ARG A 175     2923   2958   3716    -37    205   -576       N
ATOM   1447  CZ  ARG A 175     -15.279  -4.034  -0.545  1.00 27.77           C
ANISOU 1447  CZ  ARG A 175     3253   3266   4031    -39    233   -560       C
ATOM   1448  NH1 ARG A 175     -14.022  -3.628  -0.406  1.00 29.02           N
ANISOU 1448  NH1 ARG A 175     3464   3413   4148    -39    240   -513       N
ATOM   1449  NH2 ARG A 175     -16.196  -3.635   0.330  1.00 28.60           N
ANISOU 1449  NH2 ARG A 175     3318   3375   4176    -42    254   -594       N
ATOM   1450  N   MET A 176     -12.047 -10.190  -4.809  1.00 22.27           N
ANISOU 1450  N   MET A 176     2693   2567   3200   -106    218   -500       N
ATOM   1451  CA  MET A 176     -11.159 -10.932  -5.694  1.00 27.98           C
ANISOU 1451  CA  MET A 176     3455   3285   3892   -105    217   -483       C
ATOM   1452  C   MET A 176     -11.949 -11.879  -6.589  1.00 27.34           C
ANISOU 1452  C   MET A 176     3363   3209   3817   -112    195   -517       C
ATOM   1453  O   MET A 176     -12.877 -12.547  -6.122  1.00 24.47           O
ANISOU 1453  O   MET A 176     2965   2848   3486   -135    204   -549       O
ATOM   1454  CB  MET A 176     -10.156 -11.729  -4.841  1.00 33.04           C
ANISOU 1454  CB  MET A 176     4116   3914   4526   -128    261   -460       C
ATOM   1455  CG  MET A 176      -9.055 -12.365  -5.586  1.00 35.83           C
ANISOU 1455  CG  MET A 176     4505   4260   4849   -124    266   -440       C
ATOM   1456  SD  MET A 176      -9.412 -14.049  -6.089  1.00 25.37           S
ANISOU 1456  SD  MET A 176     3183   2928   3528   -144    271   -468       S
ATOM   1457  CE  MET A 176      -8.987 -14.990  -4.626  1.00 23.71           C
ANISOU 1457  CE  MET A 176     2977   2700   3334   -176    316   -457       C
ATOM   1458  N   GLY A 177     -11.586 -11.938  -7.884  1.00 26.50           N
ANISOU 1458  N   GLY A 177     3287   3102   3680    -95    167   -512       N
ATOM   1459  CA  GLY A 177     -12.058 -13.016  -8.730  1.00 31.38           C
ANISOU 1459  CA  GLY A 177     3907   3720   4296   -106    152   -539       C
ATOM   1460  C   GLY A 177     -12.579 -12.529 -10.069  1.00 29.57           C
ANISOU 1460  C   GLY A 177     3688   3496   4050    -82     96   -552       C
ATOM   1461  O   GLY A 177     -12.277 -11.417 -10.513  1.00 29.70           O
ANISOU 1461  O   GLY A 177     3725   3513   4045    -57     72   -533       O
ATOM   1462  N   THR A 178     -13.401 -13.373 -10.702  1.00 28.75           N
ANISOU 1462  N   THR A 178     3572   3395   3956    -94     74   -586       N
ATOM   1463  CA  THR A 178     -13.770 -13.150 -12.099  1.00 31.33           C
ANISOU 1463  CA  THR A 178     3921   3724   4258    -75     19   -598       C
ATOM   1464  C   THR A 178     -14.579 -11.866 -12.280  1.00 33.02           C
ANISOU 1464  C   THR A 178     4113   3946   4487    -46    -32   -607       C
ATOM   1465  O   THR A 178     -14.431 -11.177 -13.294  1.00 30.32           O
ANISOU 1465  O   THR A 178     3809   3600   4110    -22    -74   -596       O
ATOM   1466  CB  THR A 178     -14.551 -14.349 -12.641  1.00 30.16           C
ANISOU 1466  CB  THR A 178     3761   3577   4121    -97      3   -636       C
ATOM   1467  OG1 THR A 178     -13.753 -15.532 -12.538  1.00 26.88           O
ANISOU 1467  OG1 THR A 178     3374   3150   3690   -120     48   -627       O
ATOM   1468  CG2 THR A 178     -14.927 -14.132 -14.099  1.00 33.87           C
ANISOU 1468  CG2 THR A 178     4260   4047   4562    -79    -58   -648       C
ATOM   1469  N   SER A 179     -15.447 -11.528 -11.322  1.00 30.24           N
ANISOU 1469  N   SER A 179     3703   3603   4183    -48    -28   -627       N
ATOM   1470  CA  SER A 179     -16.244 -10.314 -11.476  1.00 33.92           C
ANISOU 1470  CA  SER A 179     4145   4074   4668    -16    -78   -638       C
ATOM   1471  C   SER A 179     -15.367  -9.065 -11.512  1.00 32.91           C
ANISOU 1471  C   SER A 179     4060   3937   4508     10    -81   -597       C
ATOM   1472  O   SER A 179     -15.753  -8.053 -12.107  1.00 35.30           O
ANISOU 1472  O   SER A 179     4373   4237   4804     42   -134   -598       O
ATOM   1473  CB  SER A 179     -17.286 -10.208 -10.358  1.00 45.01           C
ANISOU 1473  CB  SER A 179     5477   5490   6134    -25    -64   -671       C
ATOM   1474  OG  SER A 179     -16.682 -10.064  -9.087  1.00 48.20           O
ANISOU 1474  OG  SER A 179     5878   5892   6546    -40     -4   -649       O
ATOM   1475  N   VAL A 180     -14.176  -9.126 -10.909  1.00 28.82           N
ANISOU 1475  N   VAL A 180     3569   3413   3968     -2    -27   -562       N
ATOM   1476  CA  VAL A 180     -13.237  -8.013 -11.000  1.00 28.11           C
ANISOU 1476  CA  VAL A 180     3523   3314   3843     17    -27   -523       C
ATOM   1477  C   VAL A 180     -12.702  -7.873 -12.423  1.00 29.62           C
ANISOU 1477  C   VAL A 180     3776   3497   3980     29    -59   -507       C
ATOM   1478  O   VAL A 180     -12.600  -6.760 -12.953  1.00 36.30           O
ANISOU 1478  O   VAL A 180     4654   4335   4801     54    -94   -492       O
ATOM   1479  CB  VAL A 180     -12.102  -8.193  -9.974  1.00 28.21           C
ANISOU 1479  CB  VAL A 180     3545   3324   3850     -3     37   -492       C
ATOM   1480  CG1 VAL A 180     -11.046  -7.093 -10.134  1.00 34.56           C
ANISOU 1480  CG1 VAL A 180     4396   4120   4617     13     39   -451       C
ATOM   1481  CG2 VAL A 180     -12.668  -8.184  -8.571  1.00 28.66           C
ANISOU 1481  CG2 VAL A 180     3551   3386   3954    -15     66   -506       C
ATOM   1482  N   LEU A 181     -12.343  -8.992 -13.066  1.00 26.18           N
ANISOU 1482  N   LEU A 181     3362   3061   3523     11    -46   -512       N
ATOM   1483  CA  LEU A 181     -11.863  -8.922 -14.447  1.00 27.77           C
ANISOU 1483  CA  LEU A 181     3626   3254   3671     19    -72   -501       C
ATOM   1484  C   LEU A 181     -12.922  -8.337 -15.373  1.00 31.34           C
ANISOU 1484  C   LEU A 181     4085   3704   4119     42   -148   -522       C
ATOM   1485  O   LEU A 181     -12.616  -7.490 -16.224  1.00 37.64           O
ANISOU 1485  O   LEU A 181     4937   4491   4874     60   -180   -504       O
ATOM   1486  CB  LEU A 181     -11.441 -10.309 -14.945  1.00 28.39           C
ANISOU 1486  CB  LEU A 181     3723   3332   3733     -4    -46   -510       C
ATOM   1487  CG  LEU A 181     -10.133 -10.893 -14.421  1.00 29.49           C
ANISOU 1487  CG  LEU A 181     3876   3469   3861    -22     21   -486       C
ATOM   1488  CD1 LEU A 181      -9.948 -12.354 -14.887  1.00 27.42           C
ANISOU 1488  CD1 LEU A 181     3625   3202   3591    -41     41   -503       C
ATOM   1489  CD2 LEU A 181      -8.981 -10.026 -14.882  1.00 29.74           C
ANISOU 1489  CD2 LEU A 181     3958   3494   3847    -12     33   -451       C
ATOM   1490  N   GLU A 182     -14.172  -8.785 -15.232  1.00 35.50           N
ANISOU 1490  N   GLU A 182     4559   4240   4690     42   -178   -561       N
ATOM   1491  CA  GLU A 182     -15.237  -8.273 -16.089  1.00 39.15           C
ANISOU 1491  CA  GLU A 182     5020   4700   5156     67   -257   -585       C
ATOM   1492  C   GLU A 182     -15.447  -6.783 -15.869  1.00 39.58           C
ANISOU 1492  C   GLU A 182     5075   4747   5215    100   -290   -571       C
ATOM   1493  O   GLU A 182     -15.727  -6.039 -16.816  1.00 38.92           O
ANISOU 1493  O   GLU A 182     5032   4651   5105    126   -353   -569       O
ATOM   1494  CB  GLU A 182     -16.532  -9.041 -15.835  1.00 39.09           C
ANISOU 1494  CB  GLU A 182     4942   4706   5204     57   -277   -633       C
ATOM   1495  CG  GLU A 182     -16.405 -10.533 -16.086  1.00 48.79           C
ANISOU 1495  CG  GLU A 182     6174   5938   6427     22   -249   -648       C
ATOM   1496  CD  GLU A 182     -17.661 -11.302 -15.726  1.00 57.69           C
ANISOU 1496  CD  GLU A 182     7230   7079   7611      6   -262   -696       C
ATOM   1497  OE1 GLU A 182     -18.471 -10.787 -14.921  1.00 63.39           O
ANISOU 1497  OE1 GLU A 182     7890   7811   8386     15   -268   -715       O
ATOM   1498  OE2 GLU A 182     -17.835 -12.424 -16.250  1.00 54.43           O
ANISOU 1498  OE2 GLU A 182     6825   6666   7191    -18   -263   -716       O
ATOM   1499  N   ALA A 183     -15.317  -6.330 -14.622  1.00 40.45           N
ANISOU 1499  N   ALA A 183     5148   4863   5360    101   -249   -563       N
ATOM   1500  CA  ALA A 183     -15.463  -4.909 -14.337  1.00 36.53           C
ANISOU 1500  CA  ALA A 183     4654   4356   4869    132   -276   -550       C
ATOM   1501  C   ALA A 183     -14.288  -4.107 -14.875  1.00 38.48           C
ANISOU 1501  C   ALA A 183     4981   4586   5052    138   -271   -505       C
ATOM   1502  O   ALA A 183     -14.455  -2.946 -15.261  1.00 40.33           O
ANISOU 1502  O   ALA A 183     5247   4806   5272    167   -318   -494       O
ATOM   1503  CB  ALA A 183     -15.605  -4.690 -12.832  1.00 37.19           C
ANISOU 1503  CB  ALA A 183     4680   4449   5003    127   -228   -554       C
ATOM   1504  N   LEU A 184     -13.098  -4.705 -14.907  1.00 38.56           N
ANISOU 1504  N   LEU A 184     5025   4597   5027    110   -215   -479       N
ATOM   1505  CA  LEU A 184     -11.915  -3.983 -15.353  1.00 35.35           C
ANISOU 1505  CA  LEU A 184     4690   4177   4564    110   -201   -438       C
ATOM   1506  C   LEU A 184     -11.978  -3.689 -16.844  1.00 33.70           C
ANISOU 1506  C   LEU A 184     4549   3953   4301    121   -256   -435       C
ATOM   1507  O   LEU A 184     -11.722  -2.558 -17.273  1.00 36.80           O
ANISOU 1507  O   LEU A 184     4994   4328   4658    137   -284   -413       O
ATOM   1508  CB  LEU A 184     -10.660  -4.786 -15.018  1.00 30.28           C
ANISOU 1508  CB  LEU A 184     4058   3542   3905     78   -128   -418       C
ATOM   1509  CG  LEU A 184      -9.346  -4.201 -15.534  1.00 27.56           C
ANISOU 1509  CG  LEU A 184     3781   3187   3503     71   -104   -380       C
ATOM   1510  CD1 LEU A 184      -9.064  -2.836 -14.895  1.00 27.66           C
ANISOU 1510  CD1 LEU A 184     3802   3191   3516     83   -104   -354       C
ATOM   1511  CD2 LEU A 184      -8.195  -5.173 -15.300  1.00 31.32           C
ANISOU 1511  CD2 LEU A 184     4258   3671   3970     43    -36   -368       C
ATOM   1512  N   GLY A 185     -12.329  -4.690 -17.645  1.00 37.47           N
ANISOU 1512  N   GLY A 185     5032   4434   4768    111   -274   -458       N
ATOM   1513  CA  GLY A 185     -12.247  -4.546 -19.089  1.00 39.33           C
ANISOU 1513  CA  GLY A 185     5345   4656   4945    115   -319   -453       C
ATOM   1514  C   GLY A 185     -10.839  -4.169 -19.497  1.00 42.05           C
ANISOU 1514  C   GLY A 185     5761   4990   5228     99   -275   -415       C
ATOM   1515  O   GLY A 185      -9.852  -4.682 -18.965  1.00 41.90           O
ANISOU 1515  O   GLY A 185     5731   4980   5209     76   -204   -401       O
ATOM   1516  N   ASP A 186     -10.736  -3.230 -20.432  1.00 43.68           N
ANISOU 1516  N   ASP A 186     6041   5174   5380    110   -318   -398       N
ATOM   1517  CA  ASP A 186      -9.446  -2.694 -20.842  1.00 44.58           C
ANISOU 1517  CA  ASP A 186     6227   5277   5433     92   -278   -362       C
ATOM   1518  C   ASP A 186      -9.046  -1.443 -20.067  1.00 45.45           C
ANISOU 1518  C   ASP A 186     6338   5379   5550    102   -266   -334       C
ATOM   1519  O   ASP A 186      -8.258  -0.640 -20.576  1.00 42.14           O
ANISOU 1519  O   ASP A 186     5990   4944   5076     93   -258   -305       O
ATOM   1520  CB  ASP A 186      -9.445  -2.399 -22.343  1.00 46.40           C
ANISOU 1520  CB  ASP A 186     6552   5485   5592     91   -325   -357       C
ATOM   1521  CG  ASP A 186      -9.107  -3.617 -23.167  1.00 48.10           C
ANISOU 1521  CG  ASP A 186     6794   5707   5777     66   -299   -372       C
ATOM   1522  OD1 ASP A 186      -8.357  -4.480 -22.661  1.00 42.50           O
ANISOU 1522  OD1 ASP A 186     6049   5014   5085     44   -227   -373       O
ATOM   1523  OD2 ASP A 186      -9.591  -3.707 -24.313  1.00 55.41           O
ANISOU 1523  OD2 ASP A 186     7775   6617   6660     68   -354   -384       O
ATOM   1524  N   GLY A 187      -9.562  -1.259 -18.856  1.00 42.21           N
ANISOU 1524  N   GLY A 187     5855   4980   5203    117   -263   -342       N
ATOM   1525  CA  GLY A 187      -9.123  -0.155 -18.032  1.00 41.37           C
ANISOU 1525  CA  GLY A 187     5748   4867   5104    122   -245   -317       C
ATOM   1526  C   GLY A 187      -7.721  -0.375 -17.497  1.00 39.07           C
ANISOU 1526  C   GLY A 187     5459   4586   4801     91   -163   -291       C
ATOM   1527  O   GLY A 187      -7.105  -1.429 -17.671  1.00 33.22           O
ANISOU 1527  O   GLY A 187     4711   3858   4053     67   -118   -295       O
ATOM   1528  N   GLU A 188      -7.202   0.654 -16.834  1.00 41.20           N
ANISOU 1528  N   GLU A 188     5736   4847   5069     91   -146   -265       N
ATOM   1529  CA  GLU A 188      -5.892   0.531 -16.217  1.00 45.84           C
ANISOU 1529  CA  GLU A 188     6318   5446   5652     62    -73   -242       C
ATOM   1530  C   GLU A 188      -6.012  -0.180 -14.867  1.00 40.04           C
ANISOU 1530  C   GLU A 188     5502   4732   4980     58    -37   -254       C
ATOM   1531  O   GLU A 188      -7.066  -0.175 -14.219  1.00 34.37           O
ANISOU 1531  O   GLU A 188     4735   4016   4309     78    -64   -274       O
ATOM   1532  CB  GLU A 188      -5.232   1.909 -16.060  1.00 49.87           C
ANISOU 1532  CB  GLU A 188     6876   5940   6134     58    -69   -209       C
ATOM   1533  CG  GLU A 188      -3.831   1.927 -15.387  1.00 59.10           C
ANISOU 1533  CG  GLU A 188     8038   7120   7299     27      2   -184       C
ATOM   1534  CD  GLU A 188      -2.732   1.168 -16.157  1.00 63.57           C
ANISOU 1534  CD  GLU A 188     8630   7695   7829     -3     50   -179       C
ATOM   1535  OE1 GLU A 188      -2.870  -0.056 -16.411  1.00 58.43           O
ANISOU 1535  OE1 GLU A 188     7953   7057   7191     -6     62   -200       O
ATOM   1536  OE2 GLU A 188      -1.707   1.806 -16.490  1.00 62.96           O
ANISOU 1536  OE2 GLU A 188     8600   7612   7711    -26     79   -155       O
ATOM   1537  N   PHE A 189      -4.911  -0.813 -14.462  1.00 33.47           N
ANISOU 1537  N   PHE A 189     4656   3912   4149     32     25   -241       N
ATOM   1538  CA  PHE A 189      -4.831  -1.536 -13.201  1.00 28.52           C
ANISOU 1538  CA  PHE A 189     3964   3301   3573     24     63   -248       C
ATOM   1539  C   PHE A 189      -3.424  -1.388 -12.642  1.00 27.73           C
ANISOU 1539  C   PHE A 189     3867   3205   3465      1    118   -220       C
ATOM   1540  O   PHE A 189      -2.465  -1.141 -13.380  1.00 30.49           O
ANISOU 1540  O   PHE A 189     4261   3551   3771    -13    137   -203       O
ATOM   1541  CB  PHE A 189      -5.189  -3.018 -13.384  1.00 23.07           C
ANISOU 1541  CB  PHE A 189     3242   2622   2903     19     72   -275       C
ATOM   1542  CG  PHE A 189      -4.355  -3.728 -14.424  1.00 25.95           C
ANISOU 1542  CG  PHE A 189     3643   2988   3228      4     96   -273       C
ATOM   1543  CD1 PHE A 189      -4.706  -3.674 -15.764  1.00 30.04           C
ANISOU 1543  CD1 PHE A 189     4212   3498   3705      9     61   -282       C
ATOM   1544  CD2 PHE A 189      -3.221  -4.444 -14.059  1.00 26.18           C
ANISOU 1544  CD2 PHE A 189     3659   3026   3262    -16    153   -263       C
ATOM   1545  CE1 PHE A 189      -3.940  -4.324 -16.726  1.00 31.43           C
ANISOU 1545  CE1 PHE A 189     4426   3674   3842     -7     88   -283       C
ATOM   1546  CE2 PHE A 189      -2.456  -5.096 -15.012  1.00 31.05           C
ANISOU 1546  CE2 PHE A 189     4307   3644   3845    -28    179   -266       C
ATOM   1547  CZ  PHE A 189      -2.818  -5.036 -16.346  1.00 31.00           C
ANISOU 1547  CZ  PHE A 189     4354   3630   3796    -25    149   -276       C
ATOM   1548  N   ILE A 190      -3.306  -1.532 -11.325  1.00 19.09           N
ANISOU 1548  N   ILE A 190     2726   2118   2411     -4    143   -216       N
ATOM   1549  CA  ILE A 190      -1.993  -1.557 -10.687  1.00 17.95           C
ANISOU 1549  CA  ILE A 190     2576   1979   2266    -25    191   -193       C
ATOM   1550  C   ILE A 190      -1.402  -2.953 -10.855  1.00 25.80           C
ANISOU 1550  C   ILE A 190     3551   2985   3268    -37    226   -202       C
ATOM   1551  O   ILE A 190      -2.031  -3.954 -10.497  1.00 23.83           O
ANISOU 1551  O   ILE A 190     3266   2739   3049    -34    225   -224       O
ATOM   1552  CB  ILE A 190      -2.094  -1.164  -9.204  1.00 26.73           C
ANISOU 1552  CB  ILE A 190     3651   3090   3414    -27    201   -185       C
ATOM   1553  CG1 ILE A 190      -2.773   0.202  -9.058  1.00 26.36           C
ANISOU 1553  CG1 ILE A 190     3624   3030   3363    -11    165   -180       C
ATOM   1554  CG2 ILE A 190      -0.708  -1.155  -8.559  1.00 24.69           C
ANISOU 1554  CG2 ILE A 190     3388   2837   3155    -49    244   -160       C
ATOM   1555  CD1 ILE A 190      -2.091   1.318  -9.856  1.00 29.35           C
ANISOU 1555  CD1 ILE A 190     4061   3397   3692    -15    158   -156       C
ATOM   1556  N   LYS A 191      -0.191  -3.023 -11.409  1.00 26.73           N
ANISOU 1556  N   LYS A 191     3693   3106   3359    -53    258   -188       N
ATOM   1557  CA  LYS A 191       0.513  -4.280 -11.622  1.00 23.37           C
ANISOU 1557  CA  LYS A 191     3251   2688   2940    -62    294   -197       C
ATOM   1558  C   LYS A 191       1.258  -4.666 -10.352  1.00 27.71           C
ANISOU 1558  C   LYS A 191     3758   3243   3526    -70    325   -186       C
ATOM   1559  O   LYS A 191       2.144  -3.934  -9.905  1.00 25.21           O
ANISOU 1559  O   LYS A 191     3444   2929   3206    -82    343   -163       O
ATOM   1560  CB  LYS A 191       1.488  -4.145 -12.793  1.00 20.77           C
ANISOU 1560  CB  LYS A 191     2965   2360   2567    -74    318   -191       C
ATOM   1561  CG  LYS A 191       0.813  -3.865 -14.115  1.00 22.87           C
ANISOU 1561  CG  LYS A 191     3282   2617   2789    -68    286   -202       C
ATOM   1562  CD  LYS A 191       1.847  -3.441 -15.153  1.00 28.58           C
ANISOU 1562  CD  LYS A 191     4056   3339   3463    -87    315   -191       C
ATOM   1563  CE  LYS A 191       1.185  -3.064 -16.462  1.00 40.62           C
ANISOU 1563  CE  LYS A 191     5645   4851   4937    -83    279   -198       C
ATOM   1564  NZ  LYS A 191       2.184  -2.650 -17.483  1.00 45.02           N
ANISOU 1564  NZ  LYS A 191     6259   5405   5440   -107    311   -188       N
ATOM   1565  N   CYS A 192       0.915  -5.820  -9.782  1.00 23.85           N
ANISOU 1565  N   CYS A 192     3235   2756   3071    -67    330   -202       N
ATOM   1566  CA  CYS A 192       1.479  -6.278  -8.521  1.00 20.40           C
ANISOU 1566  CA  CYS A 192     2763   2320   2669    -74    352   -192       C
ATOM   1567  C   CYS A 192       2.149  -7.622  -8.753  1.00 21.86           C
ANISOU 1567  C   CYS A 192     2935   2505   2864    -75    379   -203       C
ATOM   1568  O   CYS A 192       1.484  -8.579  -9.148  1.00 21.43           O
ANISOU 1568  O   CYS A 192     2879   2448   2815    -69    372   -226       O
ATOM   1569  CB  CYS A 192       0.388  -6.406  -7.453  1.00 18.16           C
ANISOU 1569  CB  CYS A 192     2454   2030   2416    -71    334   -201       C
ATOM   1570  SG  CYS A 192      -0.514  -4.853  -7.168  1.00 23.35           S
ANISOU 1570  SG  CYS A 192     3122   2684   3066    -64    302   -195       S
ATOM   1571  N   LEU A 193       3.451  -7.695  -8.495  1.00 19.74           N
ANISOU 1571  N   LEU A 193     2657   2241   2602    -81    408   -189       N
ATOM   1572  CA  LEU A 193       4.229  -8.907  -8.715  1.00 23.62           C
ANISOU 1572  CA  LEU A 193     3135   2732   3108    -78    434   -199       C
ATOM   1573  C   LEU A 193       4.857  -9.329  -7.400  1.00 24.84           C
ANISOU 1573  C   LEU A 193     3257   2882   3299    -80    442   -187       C
ATOM   1574  O   LEU A 193       5.555  -8.536  -6.765  1.00 20.78           O
ANISOU 1574  O   LEU A 193     2734   2371   2789    -88    446   -165       O
ATOM   1575  CB  LEU A 193       5.324  -8.682  -9.774  1.00 24.28           C
ANISOU 1575  CB  LEU A 193     3235   2825   3167    -83    463   -198       C
ATOM   1576  CG  LEU A 193       6.364  -9.786  -9.996  1.00 20.47           C
ANISOU 1576  CG  LEU A 193     2734   2343   2701    -77    496   -209       C
ATOM   1577  CD1 LEU A 193       5.665 -11.038 -10.434  1.00 21.05           C
ANISOU 1577  CD1 LEU A 193     2813   2406   2778    -66    491   -236       C
ATOM   1578  CD2 LEU A 193       7.434  -9.372 -11.034  1.00 20.19           C
ANISOU 1578  CD2 LEU A 193     2712   2318   2639    -86    531   -210       C
ATOM   1579  N   HIS A 194       4.628 -10.579  -7.003  1.00 18.56           N
ANISOU 1579  N   HIS A 194     2449   2076   2528    -74    442   -200       N
ATOM   1580  CA  HIS A 194       5.154 -11.061  -5.739  1.00 24.09           C
ANISOU 1580  CA  HIS A 194     3127   2767   3261    -75    444   -188       C
ATOM   1581  C   HIS A 194       5.740 -12.455  -5.906  1.00 25.09           C
ANISOU 1581  C   HIS A 194     3243   2883   3406    -63    459   -202       C
ATOM   1582  O   HIS A 194       5.157 -13.293  -6.587  1.00 20.13           O
ANISOU 1582  O   HIS A 194     2627   2249   2773    -57    460   -225       O
ATOM   1583  CB  HIS A 194       4.068 -11.097  -4.657  1.00 20.58           C
ANISOU 1583  CB  HIS A 194     2680   2311   2828    -83    423   -187       C
ATOM   1584  CG  HIS A 194       4.517 -11.786  -3.415  1.00 21.07           C
ANISOU 1584  CG  HIS A 194     2730   2358   2918    -86    423   -177       C
ATOM   1585  ND1 HIS A 194       4.099 -13.052  -3.075  1.00 21.13           N
ANISOU 1585  ND1 HIS A 194     2740   2349   2942    -85    421   -191       N
ATOM   1586  CD2 HIS A 194       5.394 -11.404  -2.458  1.00 22.57           C
ANISOU 1586  CD2 HIS A 194     2910   2546   3121    -91    422   -154       C
ATOM   1587  CE1 HIS A 194       4.684 -13.413  -1.948  1.00 22.08           C
ANISOU 1587  CE1 HIS A 194     2854   2454   3082    -88    418   -176       C
ATOM   1588  NE2 HIS A 194       5.471 -12.428  -1.550  1.00 22.35           N
ANISOU 1588  NE2 HIS A 194     2879   2497   3114    -91    416   -154       N
ATOM   1589  N   SER A 195       6.880 -12.702  -5.266  1.00 20.22           N
ANISOU 1589  N   SER A 195     2607   2263   2814    -59    467   -190       N
ATOM   1590  CA  SER A 195       7.441 -14.042  -5.193  1.00 25.94           C
ANISOU 1590  CA  SER A 195     3321   2972   3562    -44    475   -202       C
ATOM   1591  C   SER A 195       8.091 -14.252  -3.834  1.00 22.13           C
ANISOU 1591  C   SER A 195     2821   2476   3110    -43    462   -182       C
ATOM   1592  O   SER A 195       8.732 -13.344  -3.297  1.00 29.89           O
ANISOU 1592  O   SER A 195     3791   3468   4096    -50    458   -161       O
ATOM   1593  CB  SER A 195       8.468 -14.286  -6.315  1.00 24.32           C
ANISOU 1593  CB  SER A 195     3108   2778   3356    -31    504   -215       C
ATOM   1594  OG  SER A 195       8.994 -15.603  -6.226  1.00 26.22           O
ANISOU 1594  OG  SER A 195     3338   3001   3624    -12    511   -229       O
ATOM   1595  N   VAL A 196       7.920 -15.456  -3.276  1.00 21.47           N
ANISOU 1595  N   VAL A 196     2743   2368   3047    -35    453   -189       N
ATOM   1596  CA  VAL A 196       8.590 -15.796  -2.026  1.00 20.20           C
ANISOU 1596  CA  VAL A 196     2574   2190   2913    -32    435   -172       C
ATOM   1597  C   VAL A 196      10.080 -16.024  -2.224  1.00 20.71           C
ANISOU 1597  C   VAL A 196     2608   2257   3003    -11    444   -171       C
ATOM   1598  O   VAL A 196      10.832 -16.074  -1.244  1.00 25.07           O
ANISOU 1598  O   VAL A 196     3147   2799   3579     -7    426   -154       O
ATOM   1599  CB  VAL A 196       7.932 -17.033  -1.369  1.00 20.97           C
ANISOU 1599  CB  VAL A 196     2693   2255   3020    -32    421   -179       C
ATOM   1600  CG1 VAL A 196       6.450 -16.757  -1.046  1.00 19.54           C
ANISOU 1600  CG1 VAL A 196     2534   2072   2819    -57    415   -182       C
ATOM   1601  CG2 VAL A 196       8.054 -18.245  -2.255  1.00 19.42           C
ANISOU 1601  CG2 VAL A 196     2500   2046   2831    -12    434   -204       C
ATOM   1602  N   GLY A 197      10.532 -16.151  -3.468  1.00 21.09           N
ANISOU 1602  N   GLY A 197     2646   2320   3048      1    471   -190       N
ATOM   1603  CA  GLY A 197      11.953 -16.152  -3.739  1.00 28.70           C
ANISOU 1603  CA  GLY A 197     3574   3294   4037     17    487   -193       C
ATOM   1604  C   GLY A 197      12.641 -17.478  -3.533  1.00 30.47           C
ANISOU 1604  C   GLY A 197     3785   3493   4297     47    482   -206       C
ATOM   1605  O   GLY A 197      13.843 -17.505  -3.239  1.00 31.29           O
ANISOU 1605  O   GLY A 197     3854   3600   4435     62    480   -202       O
ATOM   1606  N   CYS A 198      11.918 -18.582  -3.692  1.00 27.83           N
ANISOU 1606  N   CYS A 198     3478   3136   3961     55    478   -221       N
ATOM   1607  CA  CYS A 198      12.445 -19.925  -3.445  1.00 27.21           C
ANISOU 1607  CA  CYS A 198     3397   3026   3915     84    469   -234       C
ATOM   1608  C   CYS A 198      12.073 -20.842  -4.601  1.00 31.05           C
ANISOU 1608  C   CYS A 198     3901   3505   4392     97    494   -266       C
ATOM   1609  O   CYS A 198      11.248 -21.753  -4.441  1.00 29.41           O
ANISOU 1609  O   CYS A 198     3727   3271   4178     96    483   -274       O
ATOM   1610  CB  CYS A 198      11.906 -20.480  -2.126  1.00 26.33           C
ANISOU 1610  CB  CYS A 198     3313   2882   3811     78    431   -216       C
ATOM   1611  SG  CYS A 198      12.388 -19.502  -0.681  1.00 32.02           S
ANISOU 1611  SG  CYS A 198     4020   3605   4540     63    398   -179       S
ATOM   1612  N   PRO A 199      12.664 -20.631  -5.780  1.00 30.02           N
ANISOU 1612  N   PRO A 199     3752   3396   4257    105    531   -286       N
ATOM   1613  CA  PRO A 199      12.395 -21.530  -6.909  1.00 25.40           C
ANISOU 1613  CA  PRO A 199     3187   2803   3661    118    556   -318       C
ATOM   1614  C   PRO A 199      12.725 -22.967  -6.552  1.00 28.38           C
ANISOU 1614  C   PRO A 199     3570   3142   4073    148    544   -332       C
ATOM   1615  O   PRO A 199      13.560 -23.241  -5.688  1.00 28.69           O
ANISOU 1615  O   PRO A 199     3584   3166   4150    168    524   -321       O
ATOM   1616  CB  PRO A 199      13.324 -21.014  -8.016  1.00 26.10           C
ANISOU 1616  CB  PRO A 199     3250   2921   3748    123    600   -335       C
ATOM   1617  CG  PRO A 199      14.402 -20.270  -7.300  1.00 31.91           C
ANISOU 1617  CG  PRO A 199     3940   3672   4514    125    594   -316       C
ATOM   1618  CD  PRO A 199      13.699 -19.635  -6.114  1.00 32.92           C
ANISOU 1618  CD  PRO A 199     4081   3797   4632    103    553   -282       C
ATOM   1619  N   LEU A 200      12.054 -23.884  -7.224  1.00 29.76           N
ANISOU 1619  N   LEU A 200     3778   3298   4231    151    554   -356       N
ATOM   1620  CA  LEU A 200      12.381 -25.286  -6.959  1.00 29.44           C
ANISOU 1620  CA  LEU A 200     3747   3216   4221    182    544   -371       C
ATOM   1621  C   LEU A 200      13.354 -25.816  -8.006  1.00 32.62           C
ANISOU 1621  C   LEU A 200     4130   3622   4644    213    582   -404       C
ATOM   1622  O   LEU A 200      13.285 -25.412  -9.175  1.00 28.47           O
ANISOU 1622  O   LEU A 200     3606   3121   4090    203    619   -422       O
ATOM   1623  CB  LEU A 200      11.118 -26.150  -6.960  1.00 29.88           C
ANISOU 1623  CB  LEU A 200     3855   3244   4255    167    531   -379       C
ATOM   1624  CG  LEU A 200      10.061 -25.686  -5.957  1.00 35.84           C
ANISOU 1624  CG  LEU A 200     4630   3997   4991    132    500   -352       C
ATOM   1625  CD1 LEU A 200       8.737 -26.382  -6.214  1.00 36.98           C
ANISOU 1625  CD1 LEU A 200     4818   4123   5109    111    496   -367       C
ATOM   1626  CD2 LEU A 200      10.535 -25.935  -4.528  1.00 34.71           C
ANISOU 1626  CD2 LEU A 200     4483   3828   4878    141    465   -327       C
ATOM   1627  N   PRO A 201      14.281 -26.720  -7.630  1.00 29.85           N
ANISOU 1627  N   PRO A 201     3760   3242   4338    252    573   -414       N
ATOM   1628  CA  PRO A 201      14.469 -27.280  -6.284  1.00 34.86           C
ANISOU 1628  CA  PRO A 201     4398   3841   5005    268    525   -393       C
ATOM   1629  C   PRO A 201      15.061 -26.285  -5.279  1.00 34.33           C
ANISOU 1629  C   PRO A 201     4294   3792   4956    261    500   -360       C
ATOM   1630  O   PRO A 201      15.860 -25.423  -5.656  1.00 34.19           O
ANISOU 1630  O   PRO A 201     4231   3812   4949    262    523   -362       O
ATOM   1631  CB  PRO A 201      15.440 -28.442  -6.528  1.00 37.95           C
ANISOU 1631  CB  PRO A 201     4776   4202   5441    318    531   -421       C
ATOM   1632  CG  PRO A 201      16.236 -28.002  -7.688  1.00 35.95           C
ANISOU 1632  CG  PRO A 201     4482   3985   5194    328    583   -448       C
ATOM   1633  CD  PRO A 201      15.269 -27.260  -8.581  1.00 38.15           C
ANISOU 1633  CD  PRO A 201     4786   4293   5414    286    612   -450       C
ATOM   1634  N   LEU A 202      14.665 -26.421  -4.013  1.00 36.91           N
ANISOU 1634  N   LEU A 202     4645   4094   5285    252    454   -332       N
ATOM   1635  CA  LEU A 202      15.083 -25.473  -2.986  1.00 33.57           C
ANISOU 1635  CA  LEU A 202     4197   3685   4872    240    426   -299       C
ATOM   1636  C   LEU A 202      16.595 -25.500  -2.807  1.00 35.20           C
ANISOU 1636  C   LEU A 202     4347   3895   5133    278    418   -304       C
ATOM   1637  O   LEU A 202      17.209 -26.565  -2.738  1.00 42.02           O
ANISOU 1637  O   LEU A 202     5207   4726   6034    318    405   -320       O
ATOM   1638  CB  LEU A 202      14.399 -25.792  -1.652  1.00 26.78           C
ANISOU 1638  CB  LEU A 202     3381   2790   4003    223    379   -271       C
ATOM   1639  CG  LEU A 202      12.878 -25.646  -1.569  1.00 28.09           C
ANISOU 1639  CG  LEU A 202     3596   2954   4122    181    383   -264       C
ATOM   1640  CD1 LEU A 202      12.352 -26.098  -0.215  1.00 26.20           C
ANISOU 1640  CD1 LEU A 202     3402   2676   3878    165    342   -240       C
ATOM   1641  CD2 LEU A 202      12.475 -24.203  -1.838  1.00 30.05           C
ANISOU 1641  CD2 LEU A 202     3825   3250   4341    148    402   -253       C
ATOM   1642  N   LYS A 203      17.192 -24.315  -2.721  1.00 35.38           N
ANISOU 1642  N   LYS A 203     4326   3957   5161    265    425   -291       N
ATOM   1643  CA  LYS A 203      18.624 -24.200  -2.480  1.00 39.51           C
ANISOU 1643  CA  LYS A 203     4788   4487   5736    295    416   -295       C
ATOM   1644  C   LYS A 203      18.963 -24.086  -0.999  1.00 43.09           C
ANISOU 1644  C   LYS A 203     5240   4919   6211    297    355   -262       C
ATOM   1645  O   LYS A 203      20.046 -24.516  -0.584  1.00 43.03           O
ANISOU 1645  O   LYS A 203     5195   4897   6256    334    327   -267       O
ATOM   1646  CB  LYS A 203      19.189 -22.994  -3.238  1.00 38.45           C
ANISOU 1646  CB  LYS A 203     4605   4406   5599    276    460   -302       C
ATOM   1647  CG  LYS A 203      19.320 -23.219  -4.741  1.00 43.68           C
ANISOU 1647  CG  LYS A 203     5257   5087   6253    284    521   -340       C
ATOM   1648  CD  LYS A 203      20.182 -24.445  -5.030  1.00 46.63           C
ANISOU 1648  CD  LYS A 203     5604   5435   6678    336    526   -374       C
ATOM   1649  CE  LYS A 203      20.334 -24.704  -6.526  1.00 51.62           C
ANISOU 1649  CE  LYS A 203     6230   6083   7301    343    592   -415       C
ATOM   1650  NZ  LYS A 203      20.910 -26.057  -6.799  1.00 53.19           N
ANISOU 1650  NZ  LYS A 203     6418   6249   7544    394    596   -449       N
ATOM   1651  N   LYS A 204      18.063 -23.539  -0.196  1.00 45.40           N
ANISOU 1651  N   LYS A 204     5574   5209   6466    259    331   -231       N
ATOM   1652  CA  LYS A 204      18.257 -23.354   1.232  1.00 47.27           C
ANISOU 1652  CA  LYS A 204     5823   5425   6712    253    275   -198       C
ATOM   1653  C   LYS A 204      17.083 -23.970   1.978  1.00 47.37           C
ANISOU 1653  C   LYS A 204     5910   5398   6691    234    249   -182       C
ATOM   1654  O   LYS A 204      15.993 -24.124   1.414  1.00 42.22           O
ANISOU 1654  O   LYS A 204     5293   4747   6002    213    278   -191       O
ATOM   1655  CB  LYS A 204      18.397 -21.861   1.566  1.00 49.26           C
ANISOU 1655  CB  LYS A 204     6051   5717   6950    218    277   -175       C
ATOM   1656  CG  LYS A 204      17.316 -20.999   0.958  1.00 54.67           C
ANISOU 1656  CG  LYS A 204     6758   6431   7582    178    316   -173       C
ATOM   1657  CD  LYS A 204      17.708 -19.530   0.937  1.00 57.30           C
ANISOU 1657  CD  LYS A 204     7058   6807   7908    151    329   -159       C
ATOM   1658  CE  LYS A 204      16.507 -18.655   0.606  1.00 52.30           C
ANISOU 1658  CE  LYS A 204     6458   6194   7220    111    353   -151       C
ATOM   1659  NZ  LYS A 204      15.424 -18.846   1.603  1.00 38.59           N
ANISOU 1659  NZ  LYS A 204     4776   4429   5457     91    324   -131       N
ATOM   1660  N   PRO A 205      17.273 -24.349   3.246  1.00 53.05           N
ANISOU 1660  N   PRO A 205     6657   6079   7421    239    194   -158       N
ATOM   1661  CA  PRO A 205      16.245 -25.135   3.942  1.00 49.94           C
ANISOU 1661  CA  PRO A 205     6338   5639   6997    222    172   -146       C
ATOM   1662  C   PRO A 205      14.937 -24.371   4.107  1.00 44.41           C
ANISOU 1662  C   PRO A 205     5673   4957   6244    168    194   -133       C
ATOM   1663  O   PRO A 205      14.877 -23.142   4.028  1.00 42.59           O
ANISOU 1663  O   PRO A 205     5417   4767   5999    144    210   -124       O
ATOM   1664  CB  PRO A 205      16.886 -25.441   5.303  1.00 51.48           C
ANISOU 1664  CB  PRO A 205     6552   5795   7212    234    107   -120       C
ATOM   1665  CG  PRO A 205      18.355 -25.294   5.079  1.00 53.82           C
ANISOU 1665  CG  PRO A 205     6778   6108   7565    276     93   -130       C
ATOM   1666  CD  PRO A 205      18.483 -24.184   4.072  1.00 55.94           C
ANISOU 1666  CD  PRO A 205     6988   6437   7828    261    147   -143       C
ATOM   1667  N   LEU A 206      13.873 -25.137   4.338  1.00 45.00           N
ANISOU 1667  N   LEU A 206     5807   4999   6291    150    194   -135       N
ATOM   1668  CA  LEU A 206      12.510 -24.627   4.413  1.00 44.12           C
ANISOU 1668  CA  LEU A 206     5729   4901   6135    102    217   -130       C
ATOM   1669  C   LEU A 206      12.042 -24.762   5.855  1.00 45.28           C
ANISOU 1669  C   LEU A 206     5932   5011   6261     73    183   -104       C
ATOM   1670  O   LEU A 206      11.875 -25.879   6.356  1.00 41.18           O
ANISOU 1670  O   LEU A 206     5462   4442   5741     77    160   -102       O
ATOM   1671  CB  LEU A 206      11.598 -25.396   3.457  1.00 37.45           C
ANISOU 1671  CB  LEU A 206     4905   4050   5274     98    251   -159       C
ATOM   1672  CG  LEU A 206      10.132 -24.966   3.384  1.00 34.82           C
ANISOU 1672  CG  LEU A 206     4597   3732   4900     52    276   -161       C
ATOM   1673  CD1 LEU A 206      10.000 -23.631   2.657  1.00 29.19           C
ANISOU 1673  CD1 LEU A 206     3842   3075   4176     41    304   -164       C
ATOM   1674  CD2 LEU A 206       9.274 -26.044   2.721  1.00 35.48           C
ANISOU 1674  CD2 LEU A 206     4713   3795   4972     48    294   -188       C
ATOM   1675  N   VAL A 207      11.832 -23.631   6.523  1.00 42.18           N
ANISOU 1675  N   VAL A 207     5538   4640   5850     42    179    -82       N
ATOM   1676  CA  VAL A 207      11.468 -23.614   7.935  1.00 43.04           C
ANISOU 1676  CA  VAL A 207     5701   4716   5936     10    149    -56       C
ATOM   1677  C   VAL A 207       9.958 -23.462   8.055  1.00 46.38           C
ANISOU 1677  C   VAL A 207     6161   5142   6319    -36    181    -62       C
ATOM   1678  O   VAL A 207       9.368 -22.564   7.441  1.00 44.75           O
ANISOU 1678  O   VAL A 207     5925   4977   6099    -52    215    -72       O
ATOM   1679  CB  VAL A 207      12.196 -22.485   8.683  1.00 38.25           C
ANISOU 1679  CB  VAL A 207     5072   4128   5333      4    125    -31       C
ATOM   1680  CG1 VAL A 207      11.827 -22.508  10.166  1.00 32.62           C
ANISOU 1680  CG1 VAL A 207     4424   3378   4593    -30     93     -5       C
ATOM   1681  CG2 VAL A 207      13.702 -22.609   8.487  1.00 34.55           C
ANISOU 1681  CG2 VAL A 207     4555   3661   4910     50     95    -30       C
ATOM   1682  N   ASN A 208       9.332 -24.353   8.833  1.00 45.68           N
ANISOU 1682  N   ASN A 208     6137   5007   6212    -59    169    -58       N
ATOM   1683  CA  ASN A 208       7.898 -24.292   9.141  1.00 47.22           C
ANISOU 1683  CA  ASN A 208     6370   5200   6371   -108    198    -65       C
ATOM   1684  C   ASN A 208       7.034 -24.263   7.884  1.00 36.26           C
ANISOU 1684  C   ASN A 208     4952   3845   4981   -111    242    -96       C
ATOM   1685  O   ASN A 208       5.976 -23.622   7.868  1.00 37.31           O
ANISOU 1685  O   ASN A 208     5083   4001   5093   -146    270   -104       O
ATOM   1686  CB  ASN A 208       7.566 -23.088  10.033  1.00 51.90           C
ANISOU 1686  CB  ASN A 208     6969   5811   6942   -144    200    -46       C
ATOM   1687  CG  ASN A 208       7.966 -23.304  11.478  1.00 60.85           C
ANISOU 1687  CG  ASN A 208     8158   6900   8061   -160    160    -17       C
ATOM   1688  OD1 ASN A 208       8.816 -24.140  11.777  1.00 67.11           O
ANISOU 1688  OD1 ASN A 208     8972   7656   8871   -133    121     -7       O
ATOM   1689  ND2 ASN A 208       7.350 -22.553  12.383  1.00 65.14           N
ANISOU 1689  ND2 ASN A 208     8729   7446   8576   -203    169     -5       N
ATOM   1690  N   ASN A 209       7.486 -24.956   6.832  1.00 35.07           N
ANISOU 1690  N   ASN A 209     4779   3695   4853    -75    246   -114       N
ATOM   1691  CA  ASN A 209       6.799 -24.992   5.538  1.00 33.60           C
ANISOU 1691  CA  ASN A 209     4566   3536   4663    -73    282   -144       C
ATOM   1692  C   ASN A 209       6.451 -23.590   5.047  1.00 31.20           C
ANISOU 1692  C   ASN A 209     4219   3286   4350    -84    305   -146       C
ATOM   1693  O   ASN A 209       5.388 -23.364   4.463  1.00 30.78           O
ANISOU 1693  O   ASN A 209     4160   3254   4282   -105    331   -165       O
ATOM   1694  CB  ASN A 209       5.543 -25.856   5.601  1.00 36.72           C
ANISOU 1694  CB  ASN A 209     5006   3907   5038   -107    298   -162       C
ATOM   1695  CG  ASN A 209       5.860 -27.315   5.768  1.00 40.92           C
ANISOU 1695  CG  ASN A 209     5583   4386   5579    -92    280   -165       C
ATOM   1696  OD1 ASN A 209       6.344 -27.960   4.842  1.00 42.55           O
ANISOU 1696  OD1 ASN A 209     5775   4588   5804    -57    282   -183       O
ATOM   1697  ND2 ASN A 209       5.583 -27.850   6.950  1.00 46.09           N
ANISOU 1697  ND2 ASN A 209     6297   4997   6219   -120    262   -150       N
ATOM   1698  N   TRP A 210       7.357 -22.640   5.286  1.00 27.35           N
ANISOU 1698  N   TRP A 210     3700   2819   3872    -71    292   -127       N
ATOM   1699  CA  TRP A 210       7.120 -21.226   4.987  1.00 26.11           C
ANISOU 1699  CA  TRP A 210     3509   2708   3704    -83    309   -124       C
ATOM   1700  C   TRP A 210       8.230 -20.736   4.064  1.00 23.50           C
ANISOU 1700  C   TRP A 210     3129   2406   3392    -49    313   -126       C
ATOM   1701  O   TRP A 210       9.335 -20.414   4.516  1.00 28.40           O
ANISOU 1701  O   TRP A 210     3732   3027   4031    -34    293   -107       O
ATOM   1702  CB  TRP A 210       7.059 -20.398   6.260  1.00 23.78           C
ANISOU 1702  CB  TRP A 210     3230   2409   3395   -110    294    -98       C
ATOM   1703  CG  TRP A 210       6.821 -18.942   6.006  1.00 23.25           C
ANISOU 1703  CG  TRP A 210     3133   2384   3317   -121    310    -94       C
ATOM   1704  CD1 TRP A 210       7.769 -17.975   5.832  1.00 27.18           C
ANISOU 1704  CD1 TRP A 210     3596   2907   3824   -107    303    -81       C
ATOM   1705  CD2 TRP A 210       5.556 -18.296   5.865  1.00 30.62           C
ANISOU 1705  CD2 TRP A 210     4068   3336   4230   -148    333   -106       C
ATOM   1706  NE1 TRP A 210       7.171 -16.752   5.619  1.00 23.96           N
ANISOU 1706  NE1 TRP A 210     3175   2530   3399   -124    320    -81       N
ATOM   1707  CE2 TRP A 210       5.810 -16.922   5.630  1.00 24.44           C
ANISOU 1707  CE2 TRP A 210     3256   2587   3443   -146    337    -97       C
ATOM   1708  CE3 TRP A 210       4.231 -18.739   5.926  1.00 26.35           C
ANISOU 1708  CE3 TRP A 210     3549   2786   3676   -174    350   -125       C
ATOM   1709  CZ2 TRP A 210       4.786 -15.992   5.458  1.00 29.86           C
ANISOU 1709  CZ2 TRP A 210     3936   3296   4113   -165    355   -106       C
ATOM   1710  CZ3 TRP A 210       3.213 -17.814   5.756  1.00 24.49           C
ANISOU 1710  CZ3 TRP A 210     3300   2576   3427   -193    368   -136       C
ATOM   1711  CH2 TRP A 210       3.496 -16.453   5.526  1.00 30.34           C
ANISOU 1711  CH2 TRP A 210     4015   3349   4165   -186    369   -126       C
ATOM   1712  N   ALA A 211       7.945 -20.702   2.769  1.00 24.66           N
ANISOU 1712  N   ALA A 211     3255   2578   3537    -39    340   -149       N
ATOM   1713  CA  ALA A 211       8.955 -20.288   1.803  1.00 25.06           C
ANISOU 1713  CA  ALA A 211     3264   2657   3602    -11    352   -154       C
ATOM   1714  C   ALA A 211       9.181 -18.787   1.913  1.00 26.71           C
ANISOU 1714  C   ALA A 211     3448   2899   3802    -24    355   -138       C
ATOM   1715  O   ALA A 211       8.232 -17.999   1.889  1.00 27.65           O
ANISOU 1715  O   ALA A 211     3575   3035   3897    -48    364   -137       O
ATOM   1716  CB  ALA A 211       8.524 -20.661   0.393  1.00 24.18           C
ANISOU 1716  CB  ALA A 211     3146   2558   3482     -2    380   -184       C
ATOM   1717  N   CYS A 212      10.441 -18.401   2.069  1.00 25.77           N
ANISOU 1717  N   CYS A 212     3299   2789   3704     -8    345   -125       N
ATOM   1718  CA  CYS A 212      10.813 -16.999   2.162  1.00 28.07           C
ANISOU 1718  CA  CYS A 212     3568   3111   3988    -21    348   -109       C
ATOM   1719  C   CYS A 212      12.301 -16.911   1.879  1.00 28.83           C
ANISOU 1719  C   CYS A 212     3622   3219   4115      3    347   -108       C
ATOM   1720  O   CYS A 212      13.025 -17.909   1.942  1.00 25.55           O
ANISOU 1720  O   CYS A 212     3196   2783   3729     30    335   -115       O
ATOM   1721  CB  CYS A 212      10.473 -16.414   3.535  1.00 27.80           C
ANISOU 1721  CB  CYS A 212     3556   3064   3942    -47    324    -84       C
ATOM   1722  SG  CYS A 212      11.432 -17.133   4.883  1.00 29.31           S
ANISOU 1722  SG  CYS A 212     3759   3219   4159    -37    280    -63       S
ATOM   1723  N   ASN A 213      12.746 -15.710   1.538  1.00 26.92           N
ANISOU 1723  N   ASN A 213     3354   3008   3866     -7    360   -101       N
ATOM   1724  CA  ASN A 213      14.149 -15.464   1.206  1.00 28.43           C
ANISOU 1724  CA  ASN A 213     3498   3216   4086      9    365   -102       C
ATOM   1725  C   ASN A 213      14.520 -14.159   1.885  1.00 35.52           C
ANISOU 1725  C   ASN A 213     4387   4131   4978    -15    352    -78       C
ATOM   1726  O   ASN A 213      14.487 -13.088   1.271  1.00 30.47           O
ANISOU 1726  O   ASN A 213     3739   3520   4319    -32    376    -77       O
ATOM   1727  CB  ASN A 213      14.364 -15.414  -0.312  1.00 27.17           C
ANISOU 1727  CB  ASN A 213     3319   3083   3923     19    408   -128       C
ATOM   1728  CG  ASN A 213      15.839 -15.329  -0.703  1.00 31.70           C
ANISOU 1728  CG  ASN A 213     3840   3674   4531     35    421   -136       C
ATOM   1729  OD1 ASN A 213      16.669 -14.826   0.052  1.00 34.25           O
ANISOU 1729  OD1 ASN A 213     4137   4001   4876     31    400   -120       O
ATOM   1730  ND2 ASN A 213      16.165 -15.820  -1.897  1.00 33.43           N
ANISOU 1730  ND2 ASN A 213     4043   3902   4757     53    457   -164       N
ATOM   1731  N   PRO A 214      14.886 -14.214   3.168  1.00 33.29           N
ANISOU 1731  N   PRO A 214     4109   3829   4710    -18    314    -57       N
ATOM   1732  CA  PRO A 214      15.072 -12.971   3.930  1.00 33.29           C
ANISOU 1732  CA  PRO A 214     4111   3841   4699    -46    299    -32       C
ATOM   1733  C   PRO A 214      16.244 -12.131   3.453  1.00 38.86           C
ANISOU 1733  C   PRO A 214     4768   4577   5421    -48    311    -32       C
ATOM   1734  O   PRO A 214      16.168 -10.896   3.521  1.00 37.80           O
ANISOU 1734  O   PRO A 214     4636   4460   5264    -75    318    -19       O
ATOM   1735  CB  PRO A 214      15.283 -13.473   5.369  1.00 28.24           C
ANISOU 1735  CB  PRO A 214     3491   3167   4071    -45    251    -13       C
ATOM   1736  CG  PRO A 214      14.814 -14.898   5.371  1.00 31.14           C
ANISOU 1736  CG  PRO A 214     3883   3503   4445    -25    245    -26       C
ATOM   1737  CD  PRO A 214      15.136 -15.407   3.993  1.00 30.16           C
ANISOU 1737  CD  PRO A 214     3725   3395   4338      2    278    -54       C
ATOM   1738  N   GLU A 215      17.320 -12.760   2.967  1.00 37.94           N
ANISOU 1738  N   GLU A 215     4607   4466   5344    -21    317    -48       N
ATOM   1739  CA  GLU A 215      18.492 -12.011   2.521  1.00 39.20           C
ANISOU 1739  CA  GLU A 215     4715   4656   5524    -26    333    -52       C
ATOM   1740  C   GLU A 215      18.189 -11.140   1.308  1.00 41.16           C
ANISOU 1740  C   GLU A 215     4965   4935   5741    -45    382    -63       C
ATOM   1741  O   GLU A 215      18.777 -10.063   1.156  1.00 48.12           O
ANISOU 1741  O   GLU A 215     5826   5839   6618    -68    395    -56       O
ATOM   1742  CB  GLU A 215      19.637 -12.971   2.193  1.00 42.60           C
ANISOU 1742  CB  GLU A 215     5094   5085   6007     10    333    -74       C
ATOM   1743  CG  GLU A 215      20.290 -13.627   3.397  1.00 46.67           C
ANISOU 1743  CG  GLU A 215     5598   5573   6561     29    276    -62       C
ATOM   1744  CD  GLU A 215      19.666 -14.964   3.766  1.00 53.22           C
ANISOU 1744  CD  GLU A 215     6466   6362   7392     56    252    -65       C
ATOM   1745  OE1 GLU A 215      18.597 -15.310   3.211  1.00 55.23           O
ANISOU 1745  OE1 GLU A 215     6758   6610   7615     53    278    -74       O
ATOM   1746  OE2 GLU A 215      20.253 -15.671   4.615  1.00 51.35           O
ANISOU 1746  OE2 GLU A 215     6224   6098   7190     78    206    -58       O
ATOM   1747  N   LEU A 216      17.301 -11.592   0.424  1.00 37.82           N
ANISOU 1747  N   LEU A 216     4568   4509   5293    -38    409    -79       N
ATOM   1748  CA  LEU A 216      16.961 -10.865  -0.792  1.00 28.70           C
ANISOU 1748  CA  LEU A 216     3422   3378   4104    -53    451    -90       C
ATOM   1749  C   LEU A 216      15.606 -10.178  -0.702  1.00 28.75           C
ANISOU 1749  C   LEU A 216     3479   3380   4064    -74    447    -77       C
ATOM   1750  O   LEU A 216      15.058  -9.772  -1.733  1.00 28.69           O
ANISOU 1750  O   LEU A 216     3492   3386   4025    -82    474    -87       O
ATOM   1751  CB  LEU A 216      16.988 -11.808  -1.998  1.00 31.06           C
ANISOU 1751  CB  LEU A 216     3715   3680   4408    -30    485   -121       C
ATOM   1752  CG  LEU A 216      18.290 -12.573  -2.242  1.00 36.70           C
ANISOU 1752  CG  LEU A 216     4375   4397   5171     -4    497   -141       C
ATOM   1753  CD1 LEU A 216      18.247 -13.320  -3.569  1.00 36.07           C
ANISOU 1753  CD1 LEU A 216     4296   4321   5087     13    540   -174       C
ATOM   1754  CD2 LEU A 216      19.483 -11.639  -2.181  1.00 44.24           C
ANISOU 1754  CD2 LEU A 216     5285   5378   6146    -22    508   -136       C
ATOM   1755  N   THR A 217      15.052 -10.037   0.501  1.00 27.32           N
ANISOU 1755  N   THR A 217     3321   3180   3878    -83    412    -57       N
ATOM   1756  CA  THR A 217      13.737  -9.432   0.637  1.00 25.81           C
ANISOU 1756  CA  THR A 217     3173   2985   3649   -100    408    -49       C
ATOM   1757  C   THR A 217      13.806  -7.967   0.220  1.00 32.86           C
ANISOU 1757  C   THR A 217     4071   3899   4515   -124    423    -39       C
ATOM   1758  O   THR A 217      14.730  -7.245   0.604  1.00 24.35           O
ANISOU 1758  O   THR A 217     2973   2831   3446   -139    419    -25       O
ATOM   1759  CB  THR A 217      13.222  -9.574   2.068  1.00 26.79           C
ANISOU 1759  CB  THR A 217     3320   3085   3775   -108    373    -31       C
ATOM   1760  OG1 THR A 217      12.905 -10.950   2.317  1.00 32.23           O
ANISOU 1760  OG1 THR A 217     4016   3750   4479    -88    363    -42       O
ATOM   1761  CG2 THR A 217      11.963  -8.729   2.288  1.00 26.35           C
ANISOU 1761  CG2 THR A 217     3300   3028   3684   -127    373    -25       C
ATOM   1762  N   LEU A 218      12.841  -7.554  -0.599  1.00 29.60           N
ANISOU 1762  N   LEU A 218     3687   3492   4069   -129    438    -47       N
ATOM   1763  CA  LEU A 218      12.824  -6.230  -1.214  1.00 28.57           C
ANISOU 1763  CA  LEU A 218     3571   3378   3908   -149    453    -40       C
ATOM   1764  C   LEU A 218      11.398  -5.955  -1.659  1.00 23.77           C
ANISOU 1764  C   LEU A 218     3001   2764   3267   -148    451    -47       C
ATOM   1765  O   LEU A 218      10.862  -6.688  -2.496  1.00 22.84           O
ANISOU 1765  O   LEU A 218     2891   2646   3143   -133    461    -66       O
ATOM   1766  CB  LEU A 218      13.794  -6.164  -2.402  1.00 30.61           C
ANISOU 1766  CB  LEU A 218     3808   3655   4165   -150    488    -53       C
ATOM   1767  CG  LEU A 218      13.932  -4.797  -3.087  1.00 28.89           C
ANISOU 1767  CG  LEU A 218     3611   3453   3913   -175    506    -45       C
ATOM   1768  CD1 LEU A 218      14.499  -3.775  -2.125  1.00 23.42           C
ANISOU 1768  CD1 LEU A 218     2912   2761   3225   -199    491    -21       C
ATOM   1769  CD2 LEU A 218      14.791  -4.881  -4.333  1.00 32.22           C
ANISOU 1769  CD2 LEU A 218     4019   3893   4331   -180    547    -62       C
ATOM   1770  N   ILE A 219      10.776  -4.924  -1.097  1.00 23.21           N
ANISOU 1770  N   ILE A 219     2954   2689   3177   -162    435    -32       N
ATOM   1771  CA  ILE A 219       9.409  -4.548  -1.446  1.00 20.53           C
ANISOU 1771  CA  ILE A 219     2645   2343   2811   -159    428    -39       C
ATOM   1772  C   ILE A 219       9.487  -3.196  -2.143  1.00 25.17           C
ANISOU 1772  C   ILE A 219     3256   2940   3367   -173    435    -31       C
ATOM   1773  O   ILE A 219       9.754  -2.174  -1.498  1.00 22.98           O
ANISOU 1773  O   ILE A 219     2987   2660   3084   -190    427    -12       O
ATOM   1774  CB  ILE A 219       8.495  -4.505  -0.215  1.00 18.65           C
ANISOU 1774  CB  ILE A 219     2418   2089   2579   -162    406    -33       C
ATOM   1775  CG1 ILE A 219       8.553  -5.852   0.517  1.00 18.14           C
ANISOU 1775  CG1 ILE A 219     2338   2012   2543   -153    400    -39       C
ATOM   1776  CG2 ILE A 219       7.062  -4.250  -0.633  1.00 17.55           C
ANISOU 1776  CG2 ILE A 219     2301   1946   2421   -155    400    -47       C
ATOM   1777  CD1 ILE A 219       9.614  -5.920   1.603  1.00 23.82           C
ANISOU 1777  CD1 ILE A 219     3042   2726   3283   -162    389    -20       C
ATOM   1778  N   ALA A 220       9.248  -3.185  -3.456  1.00 20.76           N
ANISOU 1778  N   ALA A 220     2713   2388   2785   -167    449    -44       N
ATOM   1779  CA  ALA A 220       9.523  -2.021  -4.289  1.00 20.10           C
ANISOU 1779  CA  ALA A 220     2657   2311   2668   -182    459    -36       C
ATOM   1780  C   ALA A 220       8.243  -1.456  -4.891  1.00 21.42           C
ANISOU 1780  C   ALA A 220     2864   2470   2804   -173    441    -42       C
ATOM   1781  O   ALA A 220       7.300  -2.190  -5.192  1.00 21.15           O
ANISOU 1781  O   ALA A 220     2831   2431   2773   -155    431    -60       O
ATOM   1782  CB  ALA A 220      10.505  -2.371  -5.420  1.00 20.61           C
ANISOU 1782  CB  ALA A 220     2714   2390   2726   -187    492    -46       C
ATOM   1783  N   HIS A 221       8.231  -0.134  -5.079  1.00 18.94           N
ANISOU 1783  N   HIS A 221     2582   2151   2462   -187    435    -28       N
ATOM   1784  CA  HIS A 221       7.105   0.578  -5.660  1.00 17.38           C
ANISOU 1784  CA  HIS A 221     2425   1943   2235   -177    413    -31       C
ATOM   1785  C   HIS A 221       7.624   1.479  -6.764  1.00 23.39           C
ANISOU 1785  C   HIS A 221     3228   2705   2955   -194    425    -23       C
ATOM   1786  O   HIS A 221       8.604   2.201  -6.558  1.00 24.13           O
ANISOU 1786  O   HIS A 221     3325   2802   3041   -219    441     -6       O
ATOM   1787  CB  HIS A 221       6.382   1.426  -4.606  1.00 17.61           C
ANISOU 1787  CB  HIS A 221     2462   1958   2270   -175    387    -21       C
ATOM   1788  CG  HIS A 221       6.042   0.657  -3.363  1.00 17.03           C
ANISOU 1788  CG  HIS A 221     2354   1883   2234   -168    381    -26       C
ATOM   1789  ND1 HIS A 221       6.995   0.284  -2.438  1.00 20.11           N
ANISOU 1789  ND1 HIS A 221     2715   2277   2647   -182    393    -15       N
ATOM   1790  CD2 HIS A 221       4.866   0.163  -2.916  1.00 21.01           C
ANISOU 1790  CD2 HIS A 221     2848   2380   2754   -151    365    -42       C
ATOM   1791  CE1 HIS A 221       6.413  -0.395  -1.463  1.00 21.94           C
ANISOU 1791  CE1 HIS A 221     2930   2503   2905   -174    384    -21       C
ATOM   1792  NE2 HIS A 221       5.122  -0.485  -1.731  1.00 17.09           N
ANISOU 1792  NE2 HIS A 221     2325   1883   2287   -158    370    -39       N
ATOM   1793  N   LEU A 222       6.962   1.442  -7.923  1.00 27.38           N
ANISOU 1793  N   LEU A 222     3768   3206   3431   -183    416    -36       N
ATOM   1794  CA  LEU A 222       7.331   2.255  -9.082  1.00 28.54           C
ANISOU 1794  CA  LEU A 222     3965   3348   3529   -199    425    -29       C
ATOM   1795  C   LEU A 222       6.078   2.997  -9.529  1.00 23.88           C
ANISOU 1795  C   LEU A 222     3423   2739   2911   -182    383    -30       C
ATOM   1796  O   LEU A 222       5.405   2.593 -10.485  1.00 22.15           O
ANISOU 1796  O   LEU A 222     3226   2516   2673   -167    369    -46       O
ATOM   1797  CB  LEU A 222       7.921   1.392 -10.205  1.00 32.21           C
ANISOU 1797  CB  LEU A 222     4432   3825   3981   -205    458    -45       C
ATOM   1798  CG  LEU A 222       9.120   0.489  -9.881  1.00 29.02           C
ANISOU 1798  CG  LEU A 222     3975   3440   3610   -215    498    -50       C
ATOM   1799  CD1 LEU A 222       8.709  -0.851  -9.245  1.00 24.30           C
ANISOU 1799  CD1 LEU A 222     3329   2846   3056   -190    490    -66       C
ATOM   1800  CD2 LEU A 222       9.954   0.233 -11.127  1.00 37.68           C
ANISOU 1800  CD2 LEU A 222     5090   4548   4681   -232    540    -61       C
ATOM   1801  N   PRO A 223       5.729   4.095  -8.851  1.00 21.87           N
ANISOU 1801  N   PRO A 223     3185   2470   2655   -181    360    -15       N
ATOM   1802  CA  PRO A 223       4.439   4.740  -9.139  1.00 22.20           C
ANISOU 1802  CA  PRO A 223     3263   2492   2681   -157    315    -20       C
ATOM   1803  C   PRO A 223       4.289   5.198 -10.582  1.00 25.02           C
ANISOU 1803  C   PRO A 223     3685   2837   2986   -158    302    -20       C
ATOM   1804  O   PRO A 223       3.173   5.162 -11.112  1.00 29.04           O
ANISOU 1804  O   PRO A 223     4213   3334   3486   -132    263    -33       O
ATOM   1805  CB  PRO A 223       4.398   5.928  -8.157  1.00 25.51           C
ANISOU 1805  CB  PRO A 223     3692   2896   3105   -162    301     -2       C
ATOM   1806  CG  PRO A 223       5.797   6.107  -7.662  1.00 24.25           C
ANISOU 1806  CG  PRO A 223     3519   2748   2948   -197    340     17       C
ATOM   1807  CD  PRO A 223       6.456   4.746  -7.752  1.00 21.30           C
ANISOU 1807  CD  PRO A 223     3097   2398   2598   -201    372      5       C
ATOM   1808  N   ASP A 224       5.370   5.627 -11.239  1.00 25.11           N
ANISOU 1808  N   ASP A 224     3731   2849   2961   -191    334     -6       N
ATOM   1809  CA  ASP A 224       5.240   6.077 -12.621  1.00 32.23           C
ANISOU 1809  CA  ASP A 224     4705   3736   3806   -197    323     -5       C
ATOM   1810  C   ASP A 224       4.795   4.939 -13.527  1.00 38.59           C
ANISOU 1810  C   ASP A 224     5507   4549   4606   -182    320    -28       C
ATOM   1811  O   ASP A 224       3.980   5.144 -14.435  1.00 39.32           O
ANISOU 1811  O   ASP A 224     5650   4625   4666   -166    283    -35       O
ATOM   1812  CB  ASP A 224       6.557   6.670 -13.118  1.00 35.59           C
ANISOU 1812  CB  ASP A 224     5166   4162   4193   -242    367     12       C
ATOM   1813  CG  ASP A 224       6.972   7.904 -12.340  1.00 47.94           C
ANISOU 1813  CG  ASP A 224     6746   5715   5756   -261    366     36       C
ATOM   1814  OD1 ASP A 224       8.147   7.982 -11.918  1.00 55.22           O
ANISOU 1814  OD1 ASP A 224     7642   6652   6688   -294    409     45       O
ATOM   1815  OD2 ASP A 224       6.117   8.791 -12.135  1.00 49.04           O
ANISOU 1815  OD2 ASP A 224     6920   5829   5885   -242    321     44       O
ATOM   1816  N   ARG A 225       5.310   3.727 -13.285  1.00 28.06           N
ANISOU 1816  N   ARG A 225     4117   3239   3305   -184    356    -42       N
ATOM   1817  CA  ARG A 225       4.916   2.545 -14.041  1.00 25.26           C
ANISOU 1817  CA  ARG A 225     3754   2892   2950   -170    356    -67       C
ATOM   1818  C   ARG A 225       3.656   1.888 -13.494  1.00 31.85           C
ANISOU 1818  C   ARG A 225     4550   3727   3824   -135    317    -84       C
ATOM   1819  O   ARG A 225       3.195   0.901 -14.084  1.00 30.57           O
ANISOU 1819  O   ARG A 225     4382   3569   3664   -123    311   -106       O
ATOM   1820  CB  ARG A 225       6.058   1.519 -14.055  1.00 31.23           C
ANISOU 1820  CB  ARG A 225     4470   3671   3726   -188    413    -76       C
ATOM   1821  CG  ARG A 225       7.280   1.927 -14.886  1.00 40.02           C
ANISOU 1821  CG  ARG A 225     5620   4788   4798   -225    461    -68       C
ATOM   1822  CD  ARG A 225       8.480   1.012 -14.643  1.00 47.13           C
ANISOU 1822  CD  ARG A 225     6464   5712   5731   -238    517    -78       C
ATOM   1823  NE  ARG A 225       8.221  -0.376 -15.026  1.00 61.75           N
ANISOU 1823  NE  ARG A 225     8291   7572   7600   -219    525   -104       N
ATOM   1824  CZ  ARG A 225       9.132  -1.349 -14.987  1.00 69.37           C
ANISOU 1824  CZ  ARG A 225     9211   8553   8593   -223    569   -119       C
ATOM   1825  NH1 ARG A 225      10.369  -1.086 -14.585  1.00 70.75           N
ANISOU 1825  NH1 ARG A 225     9356   8742   8785   -245    610   -111       N
ATOM   1826  NH2 ARG A 225       8.810  -2.588 -15.352  1.00 67.02           N
ANISOU 1826  NH2 ARG A 225     8899   8259   8308   -204    573   -143       N
ATOM   1827  N   ARG A 226       3.109   2.402 -12.385  1.00 23.53           N
ANISOU 1827  N   ARG A 226     2327   3845   2767    -51    -31   -348       N
ATOM   1828  CA  ARG A 226       1.965   1.794 -11.691  1.00 20.61           C
ANISOU 1828  CA  ARG A 226     1989   3416   2428    -92     31   -393       C
ATOM   1829  C   ARG A 226       2.242   0.333 -11.326  1.00 26.48           C
ANISOU 1829  C   ARG A 226     2785   4089   3187   -103     69   -422       C
ATOM   1830  O   ARG A 226       1.379  -0.539 -11.471  1.00 23.76           O
ANISOU 1830  O   ARG A 226     2430   3726   2873   -133    115   -484       O
ATOM   1831  CB  ARG A 226       0.679   1.906 -12.514  1.00 27.83           C
ANISOU 1831  CB  ARG A 226     2826   4387   3362   -115     49   -454       C
ATOM   1832  CG  ARG A 226      -0.132   3.178 -12.262  1.00 42.85           C
ANISOU 1832  CG  ARG A 226     4704   6314   5261   -123     42   -436       C
ATOM   1833  CD  ARG A 226       0.334   4.337 -13.124  1.00 50.07           C
ANISOU 1833  CD  ARG A 226     5558   7318   6149    -91    -18   -401       C
ATOM   1834  NE  ARG A 226      -0.601   5.459 -13.081  1.00 55.60           N
ANISOU 1834  NE  ARG A 226     6223   8053   6849   -101    -22   -397       N
ATOM   1835  CZ  ARG A 226      -0.343   6.643 -12.527  1.00 59.13           C
ANISOU 1835  CZ  ARG A 226     6688   8500   7279    -87    -52   -337       C
ATOM   1836  NH1 ARG A 226       0.835   6.884 -11.964  1.00 59.45           N
ANISOU 1836  NH1 ARG A 226     6780   8509   7300    -62    -82   -274       N
ATOM   1837  NH2 ARG A 226      -1.265   7.595 -12.545  1.00 59.21           N
ANISOU 1837  NH2 ARG A 226     6663   8542   7291    -98    -53   -340       N
ATOM   1838  N   GLU A 227       3.447   0.061 -10.834  1.00 21.45           N
ANISOU 1838  N   GLU A 227     2206   3411   2532    -80     51   -377       N
ATOM   1839  CA  GLU A 227       3.859  -1.297 -10.518  1.00 23.60           C
ANISOU 1839  CA  GLU A 227     2531   3619   2816    -85     81   -399       C
ATOM   1840  C   GLU A 227       4.299  -1.417  -9.066  1.00 25.23           C
ANISOU 1840  C   GLU A 227     2837   3731   3017    -85    100   -354       C
ATOM   1841  O   GLU A 227       4.911  -0.506  -8.511  1.00 25.22           O
ANISOU 1841  O   GLU A 227     2864   3725   2993    -63     67   -293       O
ATOM   1842  CB  GLU A 227       5.004  -1.759 -11.434  1.00 19.97           C
ANISOU 1842  CB  GLU A 227     2048   3202   2340    -53     42   -396       C
ATOM   1843  CG  GLU A 227       4.568  -2.167 -12.819  1.00 29.76           C
ANISOU 1843  CG  GLU A 227     3202   4515   3590    -56     38   -457       C
ATOM   1844  CD  GLU A 227       5.739  -2.353 -13.747  1.00 34.25           C
ANISOU 1844  CD  GLU A 227     3741   5137   4134    -18     -9   -444       C
ATOM   1845  OE1 GLU A 227       5.569  -2.148 -14.968  1.00 40.67           O
ANISOU 1845  OE1 GLU A 227     4474   6035   4942     -7    -32   -471       O
ATOM   1846  OE2 GLU A 227       6.837  -2.675 -13.248  1.00 37.75           O
ANISOU 1846  OE2 GLU A 227     4241   5539   4562      2    -22   -405       O
ATOM   1847  N   ILE A 228       3.981  -2.559  -8.463  1.00 19.50           N
ANISOU 1847  N   ILE A 228     2163   2930   2314   -108    153   -386       N
ATOM   1848  CA  ILE A 228       4.515  -2.970  -7.173  1.00 19.53           C
ANISOU 1848  CA  ILE A 228     2266   2842   2313   -104    174   -350       C
ATOM   1849  C   ILE A 228       5.221  -4.299  -7.397  1.00 16.96           C
ANISOU 1849  C   ILE A 228     1967   2485   1993    -98    185   -373       C
ATOM   1850  O   ILE A 228       4.672  -5.186  -8.057  1.00 18.71           O
ANISOU 1850  O   ILE A 228     2153   2716   2240   -119    212   -434       O
ATOM   1851  CB  ILE A 228       3.400  -3.122  -6.120  1.00 16.03           C
ANISOU 1851  CB  ILE A 228     1867   2329   1893   -139    235   -364       C
ATOM   1852  CG1 ILE A 228       2.696  -1.782  -5.878  1.00 20.21           C
ANISOU 1852  CG1 ILE A 228     2372   2891   2417   -143    224   -342       C
ATOM   1853  CG2 ILE A 228       3.964  -3.679  -4.811  1.00 16.27           C
ANISOU 1853  CG2 ILE A 228     2001   2262   1918   -132    261   -331       C
ATOM   1854  CD1 ILE A 228       1.272  -1.957  -5.361  1.00 19.78           C
ANISOU 1854  CD1 ILE A 228     2322   2801   2392   -184    285   -379       C
ATOM   1855  N   ILE A 229       6.432  -4.435  -6.864  1.00 18.58           N
ANISOU 1855  N   ILE A 229     2232   2653   2174    -69    161   -326       N
ATOM   1856  CA  ILE A 229       7.255  -5.616  -7.119  1.00 18.48           C
ANISOU 1856  CA  ILE A 229     2244   2616   2162    -57    163   -342       C
ATOM   1857  C   ILE A 229       7.873  -6.016  -5.787  1.00 22.68           C
ANISOU 1857  C   ILE A 229     2880   3054   2685    -48    181   -303       C
ATOM   1858  O   ILE A 229       8.676  -5.267  -5.225  1.00 23.27           O
ANISOU 1858  O   ILE A 229     2990   3120   2733    -20    145   -243       O
ATOM   1859  CB  ILE A 229       8.339  -5.345  -8.182  1.00 23.25           C
ANISOU 1859  CB  ILE A 229     2798   3297   2741    -21    100   -325       C
ATOM   1860  CG1 ILE A 229       7.690  -4.905  -9.495  1.00 23.18           C
ANISOU 1860  CG1 ILE A 229     2686   3383   2739    -27     83   -362       C
ATOM   1861  CG2 ILE A 229       9.153  -6.591  -8.474  1.00 18.56           C
ANISOU 1861  CG2 ILE A 229     2227   2679   2147     -8    102   -345       C
ATOM   1862  CD1 ILE A 229       8.696  -4.501 -10.592  1.00 16.27           C
ANISOU 1862  CD1 ILE A 229     1754   2591   1836     11     20   -342       C
ATOM   1863  N   SER A 230       7.470  -7.171  -5.256  1.00 25.22           N
ANISOU 1863  N   SER A 230     3250   3302   3030    -72    238   -336       N
ATOM   1864  CA  SER A 230       7.858  -7.573  -3.913  1.00 23.02           C
ANISOU 1864  CA  SER A 230     3072   2928   2745    -66    265   -303       C
ATOM   1865  C   SER A 230       8.458  -8.969  -3.959  1.00 21.60           C
ANISOU 1865  C   SER A 230     2932   2703   2574    -63    284   -326       C
ATOM   1866  O   SER A 230       7.889  -9.864  -4.582  1.00 21.20           O
ANISOU 1866  O   SER A 230     2847   2656   2551    -87    314   -385       O
ATOM   1867  CB  SER A 230       6.655  -7.545  -2.964  1.00 23.08           C
ANISOU 1867  CB  SER A 230     3115   2880   2777   -100    324   -313       C
ATOM   1868  OG  SER A 230       7.035  -8.032  -1.700  1.00 23.84           O
ANISOU 1868  OG  SER A 230     3308   2883   2865    -93    353   -283       O
ATOM   1869  N   PHE A 231       9.601  -9.155  -3.301  1.00 22.12           N
ANISOU 1869  N   PHE A 231     3067   2724   2615    -32    265   -282       N
ATOM   1870  CA  PHE A 231      10.364 -10.391  -3.419  1.00 19.47           C
ANISOU 1870  CA  PHE A 231     2765   2352   2279    -22    272   -299       C
ATOM   1871  C   PHE A 231      10.826 -10.829  -2.041  1.00 24.00           C
ANISOU 1871  C   PHE A 231     3446   2828   2844    -12    298   -264       C
ATOM   1872  O   PHE A 231      11.308 -10.004  -1.260  1.00 27.62           O
ANISOU 1872  O   PHE A 231     3947   3271   3277     11    274   -208       O
ATOM   1873  CB  PHE A 231      11.575 -10.190  -4.347  1.00 21.52           C
ANISOU 1873  CB  PHE A 231     2985   2678   2512     15    206   -282       C
ATOM   1874  CG  PHE A 231      12.355 -11.451  -4.631  1.00 22.92           C
ANISOU 1874  CG  PHE A 231     3188   2830   2690     27    209   -303       C
ATOM   1875  CD1 PHE A 231      12.057 -12.226  -5.736  1.00 25.17           C
ANISOU 1875  CD1 PHE A 231     3414   3155   2996     14    216   -363       C
ATOM   1876  CD2 PHE A 231      13.400 -11.837  -3.810  1.00 19.10           C
ANISOU 1876  CD2 PHE A 231     2786   2286   2186     54    201   -265       C
ATOM   1877  CE1 PHE A 231      12.765 -13.391  -6.005  1.00 21.54           C
ANISOU 1877  CE1 PHE A 231     2978   2672   2536     26    217   -384       C
ATOM   1878  CE2 PHE A 231      14.119 -12.998  -4.073  1.00 21.33           C
ANISOU 1878  CE2 PHE A 231     3092   2544   2467     66    203   -285       C
ATOM   1879  CZ  PHE A 231      13.810 -13.767  -5.175  1.00 22.05           C
ANISOU 1879  CZ  PHE A 231     3124   2675   2579     52    211   -344       C
ATOM   1880  N   GLY A 232      10.647 -12.121  -1.728  1.00 24.87           N
ANISOU 1880  N   GLY A 232     3601   2872   2975    -28    348   -296       N
ATOM   1881  CA  GLY A 232      11.354 -12.750  -0.639  1.00 21.11           C
ANISOU 1881  CA  GLY A 232     3224   2309   2486    -11    366   -266       C
ATOM   1882  C   GLY A 232      10.586 -12.875   0.664  1.00 30.44           C
ANISOU 1882  C   GLY A 232     4478   3408   3681    -30    426   -255       C
ATOM   1883  O   GLY A 232      10.973 -13.694   1.506  1.00 26.69           O
ANISOU 1883  O   GLY A 232     4084   2853   3204    -23    456   -245       O
ATOM   1884  N   SER A 233       9.530 -12.088   0.873  1.00 24.13           N
ANISOU 1884  N   SER A 233     3652   2623   2894    -54    445   -257       N
ATOM   1885  CA  SER A 233       8.736 -12.198   2.094  1.00 26.09           C
ANISOU 1885  CA  SER A 233     3964   2794   3153    -72    505   -247       C
ATOM   1886  C   SER A 233       7.323 -12.650   1.767  1.00 27.14           C
ANISOU 1886  C   SER A 233     4054   2926   3332   -121    563   -304       C
ATOM   1887  O   SER A 233       6.713 -12.177   0.804  1.00 27.31           O
ANISOU 1887  O   SER A 233     3989   3021   3367   -138    547   -335       O
ATOM   1888  CB  SER A 233       8.673 -10.876   2.876  1.00 26.48           C
ANISOU 1888  CB  SER A 233     4035   2849   3178    -56    484   -195       C
ATOM   1889  OG  SER A 233       7.725 -10.982   3.942  1.00 25.96           O
ANISOU 1889  OG  SER A 233     4021   2717   3127    -78    547   -193       O
ATOM   1890  N   GLY A 234       6.803 -13.569   2.572  1.00 29.01           N
ANISOU 1890  N   GLY A 234     4350   3079   3592   -142    630   -317       N
ATOM   1891  CA  GLY A 234       5.427 -13.978   2.428  1.00 20.50           C
ANISOU 1891  CA  GLY A 234     3239   1991   2560   -189    689   -366       C
ATOM   1892  C   GLY A 234       4.462 -13.325   3.391  1.00 27.08           C
ANISOU 1892  C   GLY A 234     4098   2794   3398   -205    729   -346       C
ATOM   1893  O   GLY A 234       3.284 -13.701   3.403  1.00 34.03           O
ANISOU 1893  O   GLY A 234     4956   3655   4317   -245    785   -385       O
ATOM   1894  N   TYR A 235       4.905 -12.346   4.178  1.00 26.73           N
ANISOU 1894  N   TYR A 235     4096   2744   3316   -175    701   -288       N
ATOM   1895  CA  TYR A 235       4.168 -11.881   5.346  1.00 27.89           C
ANISOU 1895  CA  TYR A 235     4292   2843   3462   -183    743   -262       C
ATOM   1896  C   TYR A 235       3.426 -10.576   5.075  1.00 27.14           C
ANISOU 1896  C   TYR A 235     4134   2814   3363   -192    721   -258       C
ATOM   1897  O   TYR A 235       4.017  -9.616   4.570  1.00 25.51           O
ANISOU 1897  O   TYR A 235     3890   2674   3130   -167    655   -235       O
ATOM   1898  CB  TYR A 235       5.114 -11.685   6.533  1.00 32.83           C
ANISOU 1898  CB  TYR A 235     5015   3412   4048   -141    730   -200       C
ATOM   1899  CG  TYR A 235       4.385 -11.704   7.854  1.00 33.77           C
ANISOU 1899  CG  TYR A 235     5204   3456   4170   -149    792   -179       C
ATOM   1900  CD1 TYR A 235       3.841 -10.544   8.389  1.00 28.85           C
ANISOU 1900  CD1 TYR A 235     4579   2850   3533   -145    786   -152       C
ATOM   1901  CD2 TYR A 235       4.213 -12.898   8.551  1.00 31.08           C
ANISOU 1901  CD2 TYR A 235     4930   3030   3849   -161    857   -188       C
ATOM   1902  CE1 TYR A 235       3.152 -10.566   9.600  1.00 33.15           C
ANISOU 1902  CE1 TYR A 235     5187   3328   4080   -151    844   -133       C
ATOM   1903  CE2 TYR A 235       3.532 -12.935   9.761  1.00 30.72           C
ANISOU 1903  CE2 TYR A 235     4949   2917   3806   -167    917   -168       C
ATOM   1904  CZ  TYR A 235       3.004 -11.765  10.281  1.00 32.36           C
ANISOU 1904  CZ  TYR A 235     5153   3144   3998   -161    910   -140       C
ATOM   1905  OH  TYR A 235       2.322 -11.803  11.482  1.00 32.03           O
ANISOU 1905  OH  TYR A 235     5175   3036   3957   -165    970   -120       O
ATOM   1906  N   GLY A 236       2.133 -10.560   5.417  1.00 22.37           N
ANISOU 1906  N   GLY A 236     3520   2191   2788   -227    778   -280       N
ATOM   1907  CA  GLY A 236       1.328  -9.362   5.619  1.00 21.82           C
ANISOU 1907  CA  GLY A 236     3420   2157   2714   -234    773   -267       C
ATOM   1908  C   GLY A 236       1.535  -8.239   4.630  1.00 23.05           C
ANISOU 1908  C   GLY A 236     3494   2410   2852   -222    703   -265       C
ATOM   1909  O   GLY A 236       1.343  -8.414   3.423  1.00 24.24           O
ANISOU 1909  O   GLY A 236     3566   2622   3022   -239    686   -309       O
ATOM   1910  N   GLY A 237       1.943  -7.079   5.137  1.00 22.52           N
ANISOU 1910  N   GLY A 237     3448   2360   2750   -192    660   -213       N
ATOM   1911  CA  GLY A 237       2.175  -5.929   4.284  1.00 19.72           C
ANISOU 1911  CA  GLY A 237     3020   2095   2377   -178    593   -204       C
ATOM   1912  C   GLY A 237       3.254  -6.123   3.231  1.00 21.74           C
ANISOU 1912  C   GLY A 237     3237   2401   2621   -158    536   -209       C
ATOM   1913  O   GLY A 237       3.348  -5.299   2.309  1.00 24.70           O
ANISOU 1913  O   GLY A 237     3538   2858   2988   -151    485   -211       O
ATOM   1914  N   ASN A 238       4.081  -7.165   3.349  1.00 19.01           N
ANISOU 1914  N   ASN A 238     2938   2010   2273   -146    543   -209       N
ATOM   1915  CA  ASN A 238       5.092  -7.408   2.318  1.00 26.36           C
ANISOU 1915  CA  ASN A 238     3831   2991   3194   -126    491   -216       C
ATOM   1916  C   ASN A 238       4.537  -8.161   1.115  1.00 26.24           C
ANISOU 1916  C   ASN A 238     3741   3016   3212   -157    508   -282       C
ATOM   1917  O   ASN A 238       5.082  -8.034   0.013  1.00 23.69           O
ANISOU 1917  O   ASN A 238     3357   2763   2882   -144    459   -293       O
ATOM   1918  CB  ASN A 238       6.277  -8.210   2.868  1.00 24.10           C
ANISOU 1918  CB  ASN A 238     3623   2644   2890    -98    486   -190       C
ATOM   1919  CG  ASN A 238       6.986  -7.520   4.004  1.00 21.79           C
ANISOU 1919  CG  ASN A 238     3405   2312   2562    -62    463   -126       C
ATOM   1920  OD1 ASN A 238       7.056  -6.282   4.071  1.00 22.13           O
ANISOU 1920  OD1 ASN A 238     3427   2395   2585    -46    420    -93       O
ATOM   1921  ND2 ASN A 238       7.514  -8.320   4.928  1.00 23.07           N
ANISOU 1921  ND2 ASN A 238     3657   2393   2716    -47    489   -109       N
ATOM   1922  N   SER A 239       3.483  -8.957   1.297  1.00 21.53           N
ANISOU 1922  N   SER A 239     3147   2379   2653   -195    575   -325       N
ATOM   1923  CA  SER A 239       3.021  -9.872   0.258  1.00 18.70           C
ANISOU 1923  CA  SER A 239     2730   2046   2331   -223    594   -391       C
ATOM   1924  C   SER A 239       1.580  -9.641  -0.175  1.00 19.31           C
ANISOU 1924  C   SER A 239     2739   2155   2442   -264    627   -437       C
ATOM   1925  O   SER A 239       1.244  -9.934  -1.318  1.00 21.23           O
ANISOU 1925  O   SER A 239     2907   2453   2707   -279    619   -488       O
ATOM   1926  CB  SER A 239       3.158 -11.326   0.743  1.00 19.56           C
ANISOU 1926  CB  SER A 239     2901   2070   2461   -235    646   -410       C
ATOM   1927  OG  SER A 239       2.346 -11.534   1.898  1.00 23.04           O
ANISOU 1927  OG  SER A 239     3401   2435   2919   -256    712   -402       O
ATOM   1928  N   LEU A 240       0.719  -9.139   0.709  1.00 18.08           N
ANISOU 1928  N   LEU A 240     2609   1968   2293   -280    664   -423       N
ATOM   1929  CA  LEU A 240      -0.666  -8.828   0.353  1.00 20.43           C
ANISOU 1929  CA  LEU A 240     2844   2298   2623   -317    694   -464       C
ATOM   1930  C   LEU A 240      -0.634  -7.440  -0.274  1.00 23.53           C
ANISOU 1930  C   LEU A 240     3171   2780   2989   -300    634   -447       C
ATOM   1931  O   LEU A 240      -0.806  -6.432   0.398  1.00 21.36           O
ANISOU 1931  O   LEU A 240     2917   2505   2694   -291    624   -406       O
ATOM   1932  CB  LEU A 240      -1.563  -8.891   1.587  1.00 21.35           C
ANISOU 1932  CB  LEU A 240     3017   2341   2755   -339    760   -453       C
ATOM   1933  CG  LEU A 240      -1.442 -10.154   2.458  1.00 20.74           C
ANISOU 1933  CG  LEU A 240     3021   2164   2695   -348    820   -454       C
ATOM   1934  CD1 LEU A 240      -2.366 -10.125   3.680  1.00 20.98           C
ANISOU 1934  CD1 LEU A 240     3106   2128   2740   -367    886   -439       C
ATOM   1935  CD2 LEU A 240      -1.693 -11.423   1.655  1.00 20.72           C
ANISOU 1935  CD2 LEU A 240     2983   2155   2735   -376    848   -517       C
ATOM   1936  N   LEU A 241      -0.370  -7.385  -1.585  1.00 19.38           N
ANISOU 1936  N   LEU A 241     2568   2332   2463   -295    590   -476       N
ATOM   1937  CA  LEU A 241       0.107  -6.135  -2.170  1.00 20.47           C
ANISOU 1937  CA  LEU A 241     2658   2551   2568   -267    521   -445       C
ATOM   1938  C   LEU A 241      -0.974  -5.059  -2.276  1.00 19.67           C
ANISOU 1938  C   LEU A 241     2504   2496   2472   -284    522   -452       C
ATOM   1939  O   LEU A 241      -0.640  -3.874  -2.420  1.00 22.06           O
ANISOU 1939  O   LEU A 241     2785   2851   2745   -260    471   -414       O
ATOM   1940  CB  LEU A 241       0.745  -6.424  -3.538  1.00 18.82           C
ANISOU 1940  CB  LEU A 241     2384   2412   2356   -253    476   -473       C
ATOM   1941  CG  LEU A 241       1.997  -7.282  -3.353  1.00 20.44           C
ANISOU 1941  CG  LEU A 241     2646   2575   2546   -228    464   -453       C
ATOM   1942  CD1 LEU A 241       2.761  -7.508  -4.669  1.00 16.99           C
ANISOU 1942  CD1 LEU A 241     2149   2208   2100   -208    414   -473       C
ATOM   1943  CD2 LEU A 241       2.916  -6.696  -2.292  1.00 18.92           C
ANISOU 1943  CD2 LEU A 241     2531   2342   2317   -195    440   -381       C
ATOM   1944  N   GLY A 242      -2.251  -5.427  -2.164  1.00 22.66           N
ANISOU 1944  N   GLY A 242     2865   2856   2888   -323    580   -497       N
ATOM   1945  CA  GLY A 242      -3.310  -4.442  -2.193  1.00 22.39           C
ANISOU 1945  CA  GLY A 242     2786   2862   2860   -340    584   -504       C
ATOM   1946  C   GLY A 242      -3.353  -3.543  -0.972  1.00 19.50           C
ANISOU 1946  C   GLY A 242     2480   2459   2470   -327    587   -447       C
ATOM   1947  O   GLY A 242      -3.881  -2.431  -1.059  1.00 29.48           O
ANISOU 1947  O   GLY A 242     3706   3770   3725   -327    567   -437       O
ATOM   1948  N   LYS A 243      -2.755  -3.971   0.140  1.00 21.17           N
ANISOU 1948  N   LYS A 243     2784   2591   2670   -314    607   -408       N
ATOM   1949  CA  LYS A 243      -2.958  -3.329   1.436  1.00 26.25           C
ANISOU 1949  CA  LYS A 243     3492   3184   3295   -305    624   -361       C
ATOM   1950  C   LYS A 243      -2.077  -2.092   1.627  1.00 29.91           C
ANISOU 1950  C   LYS A 243     3968   3681   3715   -264    556   -301       C
ATOM   1951  O   LYS A 243      -2.510  -0.963   1.362  1.00 29.67           O
ANISOU 1951  O   LYS A 243     3891   3707   3676   -262    527   -293       O
ATOM   1952  CB  LYS A 243      -2.716  -4.350   2.560  1.00 21.89           C
ANISOU 1952  CB  LYS A 243     3036   2531   2749   -307    677   -347       C
ATOM   1953  CG  LYS A 243      -3.073  -3.823   3.960  1.00 25.27           C
ANISOU 1953  CG  LYS A 243     3535   2903   3164   -300    706   -305       C
ATOM   1954  CD  LYS A 243      -3.069  -4.920   5.034  1.00 18.25           C
ANISOU 1954  CD  LYS A 243     2735   1913   2286   -307    770   -298       C
ATOM   1955  CE  LYS A 243      -3.375  -4.323   6.413  1.00 25.01           C
ANISOU 1955  CE  LYS A 243     3661   2718   3123   -294    794   -253       C
ATOM   1956  NZ  LYS A 243      -4.729  -3.674   6.514  1.00 29.70           N
ANISOU 1956  NZ  LYS A 243     4216   3335   3735   -322    825   -271       N
ATOM   1957  N   LYS A 244      -0.845  -2.276   2.101  1.00 20.51           N
ANISOU 1957  N   LYS A 244     2840   2454   2498   -231    529   -258       N
ATOM   1958  CA  LYS A 244       0.026  -1.120   2.282  1.00 15.96           C
ANISOU 1958  CA  LYS A 244     2275   1907   1884   -191    463   -201       C
ATOM   1959  C   LYS A 244       0.631  -0.655   0.958  1.00 21.34           C
ANISOU 1959  C   LYS A 244     2876   2677   2554   -177    398   -205       C
ATOM   1960  O   LYS A 244       0.679   0.545   0.682  1.00 16.45           O
ANISOU 1960  O   LYS A 244     2218   2114   1918   -162    351   -181       O
ATOM   1961  CB  LYS A 244       1.142  -1.457   3.271  1.00 23.81           C
ANISOU 1961  CB  LYS A 244     3362   2831   2852   -159    455   -153       C
ATOM   1962  CG  LYS A 244       0.627  -2.009   4.576  1.00 20.50           C
ANISOU 1962  CG  LYS A 244     3026   2321   2441   -170    521   -147       C
ATOM   1963  CD  LYS A 244      -0.204  -0.939   5.303  1.00 16.16           C
ANISOU 1963  CD  LYS A 244     2484   1772   1884   -172    529   -126       C
ATOM   1964  CE  LYS A 244      -0.676  -1.482   6.640  1.00 17.20           C
ANISOU 1964  CE  LYS A 244     2700   1813   2020   -178    595   -116       C
ATOM   1965  NZ  LYS A 244      -1.201  -0.373   7.503  1.00 16.91           N
ANISOU 1965  NZ  LYS A 244     2687   1772   1967   -168    593    -83       N
ATOM   1966  N   CYS A 245       1.089  -1.589   0.123  1.00 18.36           N
ANISOU 1966  N   CYS A 245     2474   2314   2188   -180    396   -237       N
ATOM   1967  CA  CYS A 245       1.816  -1.195  -1.082  1.00 15.50           C
ANISOU 1967  CA  CYS A 245     2045   2033   1813   -159    333   -235       C
ATOM   1968  C   CYS A 245       0.925  -0.411  -2.040  1.00 19.88           C
ANISOU 1968  C   CYS A 245     2506   2672   2377   -176    318   -264       C
ATOM   1969  O   CYS A 245       1.303   0.660  -2.535  1.00 19.34           O
ANISOU 1969  O   CYS A 245     2394   2667   2287   -154    262   -236       O
ATOM   1970  CB  CYS A 245       2.387  -2.451  -1.766  1.00 15.72           C
ANISOU 1970  CB  CYS A 245     2065   2056   1851   -160    339   -268       C
ATOM   1971  SG  CYS A 245       3.619  -3.246  -0.750  1.00 20.99           S
ANISOU 1971  SG  CYS A 245     2839   2636   2501   -134    343   -228       S
ATOM   1972  N   PHE A 246      -0.249  -0.956  -2.342  1.00 21.54           N
ANISOU 1972  N   PHE A 246     2681   2883   2621   -214    368   -322       N
ATOM   1973  CA  PHE A 246      -1.212  -0.314  -3.232  1.00 21.65           C
ANISOU 1973  CA  PHE A 246     2605   2973   2646   -231    361   -357       C
ATOM   1974  C   PHE A 246      -2.000   0.771  -2.487  1.00 25.23           C
ANISOU 1974  C   PHE A 246     3068   3422   3095   -238    368   -333       C
ATOM   1975  O   PHE A 246      -1.884   1.969  -2.791  1.00 23.54           O
ANISOU 1975  O   PHE A 246     2818   3266   2860   -220    320   -305       O
ATOM   1976  CB  PHE A 246      -2.085  -1.446  -3.799  1.00 23.57           C
ANISOU 1976  CB  PHE A 246     2814   3211   2930   -268    412   -430       C
ATOM   1977  CG  PHE A 246      -3.179  -1.055  -4.770  1.00 27.67           C
ANISOU 1977  CG  PHE A 246     3240   3803   3469   -291    414   -481       C
ATOM   1978  CD1 PHE A 246      -3.704   0.219  -4.862  1.00 26.04           C
ANISOU 1978  CD1 PHE A 246     2995   3649   3251   -288    390   -464       C
ATOM   1979  CD2 PHE A 246      -3.730  -2.050  -5.575  1.00 30.14           C
ANISOU 1979  CD2 PHE A 246     3508   4129   3816   -316    443   -548       C
ATOM   1980  CE1 PHE A 246      -4.745   0.493  -5.745  1.00 23.57           C
ANISOU 1980  CE1 PHE A 246     2599   3399   2957   -309    395   -515       C
ATOM   1981  CE2 PHE A 246      -4.755  -1.776  -6.464  1.00 26.93           C
ANISOU 1981  CE2 PHE A 246     3017   3787   3429   -337    446   -600       C
ATOM   1982  CZ  PHE A 246      -5.263  -0.500  -6.546  1.00 27.60           C
ANISOU 1982  CZ  PHE A 246     3064   3923   3500   -333    422   -582       C
ATOM   1983  N   ALA A 247      -2.771   0.373  -1.474  1.00 22.16           N
ANISOU 1983  N   ALA A 247     2732   2964   2723   -261    429   -342       N
ATOM   1984  CA  ALA A 247      -3.790   1.257  -0.922  1.00 24.94           C
ANISOU 1984  CA  ALA A 247     3079   3318   3078   -275    446   -335       C
ATOM   1985  C   ALA A 247      -3.220   2.399  -0.087  1.00 21.18           C
ANISOU 1985  C   ALA A 247     2649   2832   2566   -242    407   -268       C
ATOM   1986  O   ALA A 247      -3.946   3.358   0.175  1.00 20.84           O
ANISOU 1986  O   ALA A 247     2589   2809   2519   -247    404   -259       O
ATOM   1987  CB  ALA A 247      -4.797   0.440  -0.101  1.00 24.53           C
ANISOU 1987  CB  ALA A 247     3069   3195   3057   -309    526   -365       C
ATOM   1988  N   LEU A 248      -1.954   2.345   0.338  1.00 24.78           N
ANISOU 1988  N   LEU A 248     3161   3258   2997   -209    374   -221       N
ATOM   1989  CA  LEU A 248      -1.320   3.537   0.901  1.00 24.14           C
ANISOU 1989  CA  LEU A 248     3107   3181   2883   -175    322   -159       C
ATOM   1990  C   LEU A 248      -0.221   4.095   0.002  1.00 25.17           C
ANISOU 1990  C   LEU A 248     3195   3376   2993   -144    249   -133       C
ATOM   1991  O   LEU A 248      -0.258   5.278  -0.352  1.00 21.58           O
ANISOU 1991  O   LEU A 248     2696   2979   2526   -132    203   -112       O
ATOM   1992  CB  LEU A 248      -0.766   3.279   2.313  1.00 14.93           C
ANISOU 1992  CB  LEU A 248     2047   1926   1702   -156    339   -116       C
ATOM   1993  CG  LEU A 248      -1.822   3.014   3.398  1.00 19.24           C
ANISOU 1993  CG  LEU A 248     2642   2407   2261   -179    408   -126       C
ATOM   1994  CD1 LEU A 248      -1.147   2.854   4.758  1.00 17.04           C
ANISOU 1994  CD1 LEU A 248     2467   2045   1960   -152    416    -79       C
ATOM   1995  CD2 LEU A 248      -2.881   4.125   3.437  1.00 19.43           C
ANISOU 1995  CD2 LEU A 248     2626   2471   2287   -190    406   -129       C
ATOM   1996  N   ARG A 249       0.778   3.299  -0.374  1.00 23.88           N
ANISOU 1996  N   ARG A 249     3044   3205   2826   -130    234   -132       N
ATOM   1997  CA  ARG A 249       1.927   3.892  -1.057  1.00 24.45           C
ANISOU 1997  CA  ARG A 249     3085   3331   2875    -97    164    -97       C
ATOM   1998  C   ARG A 249       1.568   4.339  -2.468  1.00 22.01           C
ANISOU 1998  C   ARG A 249     2673   3118   2572   -104    136   -127       C
ATOM   1999  O   ARG A 249       1.674   5.526  -2.807  1.00 21.64           O
ANISOU 1999  O   ARG A 249     2584   3126   2510    -88     88    -98       O
ATOM   2000  CB  ARG A 249       3.102   2.914  -1.054  1.00 21.29           C
ANISOU 2000  CB  ARG A 249     2727   2895   2468    -78    156    -88       C
ATOM   2001  CG  ARG A 249       3.563   2.627   0.347  1.00 19.72           C
ANISOU 2001  CG  ARG A 249     2631   2606   2258    -64    175    -52       C
ATOM   2002  CD  ARG A 249       5.037   2.264   0.455  1.00 16.81           C
ANISOU 2002  CD  ARG A 249     2304   2214   1869    -30    138    -17       C
ATOM   2003  NE  ARG A 249       5.279   1.812   1.812  1.00 21.71           N
ANISOU 2003  NE  ARG A 249     3024   2742   2482    -21    169      7       N
ATOM   2004  CZ  ARG A 249       5.078   0.565   2.221  1.00 25.11           C
ANISOU 2004  CZ  ARG A 249     3503   3112   2927    -38    225    -21       C
ATOM   2005  NH1 ARG A 249       4.694  -0.366   1.349  1.00 23.83           N
ANISOU 2005  NH1 ARG A 249     3296   2969   2788    -64    254    -74       N
ATOM   2006  NH2 ARG A 249       5.290   0.239   3.491  1.00 24.55           N
ANISOU 2006  NH2 ARG A 249     3523   2957   2846    -27    252      4       N
ATOM   2007  N   ILE A 250       1.129   3.410  -3.311  1.00 25.93           N
ANISOU 2007  N   ILE A 250     3125   3636   3090   -127    165   -184       N
ATOM   2008  CA  ILE A 250       0.737   3.810  -4.658  1.00 27.26           C
ANISOU 2008  CA  ILE A 250     3197   3898   3264   -132    140   -215       C
ATOM   2009  C   ILE A 250      -0.451   4.760  -4.604  1.00 27.72           C
ANISOU 2009  C   ILE A 250     3217   3986   3329   -150    149   -226       C
ATOM   2010  O   ILE A 250      -0.481   5.787  -5.296  1.00 23.44           O
ANISOU 2010  O   ILE A 250     2613   3517   2775   -137    105   -213       O
ATOM   2011  CB  ILE A 250       0.427   2.573  -5.516  1.00 24.94           C
ANISOU 2011  CB  ILE A 250     2866   3616   2995   -153    172   -280       C
ATOM   2012  CG1 ILE A 250       1.703   1.753  -5.747  1.00 19.16           C
ANISOU 2012  CG1 ILE A 250     2161   2868   2252   -130    152   -268       C
ATOM   2013  CG2 ILE A 250      -0.237   3.010  -6.817  1.00 26.37           C
ANISOU 2013  CG2 ILE A 250     2947   3891   3183   -161    155   -319       C
ATOM   2014  CD1 ILE A 250       2.821   2.521  -6.503  1.00 18.22           C
ANISOU 2014  CD1 ILE A 250     2003   2815   2104    -91     80   -226       C
ATOM   2015  N   ALA A 251      -1.447   4.435  -3.776  1.00 24.01           N
ANISOU 2015  N   ALA A 251     2783   3462   2878   -178    207   -248       N
ATOM   2016  CA  ALA A 251      -2.678   5.208  -3.750  1.00 23.29           C
ANISOU 2016  CA  ALA A 251     2654   3399   2797   -199    222   -266       C
ATOM   2017  C   ALA A 251      -2.447   6.624  -3.240  1.00 21.69           C
ANISOU 2017  C   ALA A 251     2463   3210   2569   -175    178   -208       C
ATOM   2018  O   ALA A 251      -3.125   7.554  -3.691  1.00 22.21           O
ANISOU 2018  O   ALA A 251     2471   3333   2633   -180    161   -215       O
ATOM   2019  CB  ALA A 251      -3.733   4.505  -2.881  1.00 21.71           C
ANISOU 2019  CB  ALA A 251     2495   3130   2622   -234    296   -298       C
ATOM   2020  N   SER A 252      -1.528   6.817  -2.285  1.00 24.47           N
ANISOU 2020  N   SER A 252     2889   3508   2900   -149    159   -153       N
ATOM   2021  CA  SER A 252      -1.332   8.181  -1.804  1.00 13.63           C
ANISOU 2021  CA  SER A 252     1525   2148   1506   -126    115   -100       C
ATOM   2022  C   SER A 252      -0.750   9.055  -2.901  1.00 22.75           C
ANISOU 2022  C   SER A 252     2609   3388   2646   -104     48    -81       C
ATOM   2023  O   SER A 252      -1.080  10.243  -2.979  1.00 19.00           O
ANISOU 2023  O   SER A 252     2102   2954   2163    -97     18    -61       O
ATOM   2024  CB  SER A 252      -0.443   8.235  -0.564  1.00 18.84           C
ANISOU 2024  CB  SER A 252     2278   2734   2147   -100    104    -46       C
ATOM   2025  OG  SER A 252       0.870   7.773  -0.796  1.00 19.22           O
ANISOU 2025  OG  SER A 252     2345   2774   2182    -75     73    -22       O
ATOM   2026  N   ARG A 253       0.096   8.491  -3.769  1.00 19.26           N
ANISOU 2026  N   ARG A 253     2140   2976   2202    -92     26    -86       N
ATOM   2027  CA  ARG A 253       0.598   9.313  -4.865  1.00 23.66           C
ANISOU 2027  CA  ARG A 253     2626   3619   2747    -70    -34    -68       C
ATOM   2028  C   ARG A 253      -0.486   9.560  -5.905  1.00 20.53           C
ANISOU 2028  C   ARG A 253     2141   3296   2364    -92    -25   -117       C
ATOM   2029  O   ARG A 253      -0.617  10.679  -6.414  1.00 29.51           O
ANISOU 2029  O   ARG A 253     3226   4495   3492    -80    -65    -99       O
ATOM   2030  CB  ARG A 253       1.827   8.693  -5.518  1.00 24.47           C
ANISOU 2030  CB  ARG A 253     2722   3736   2842    -49    -63    -58       C
ATOM   2031  CG  ARG A 253       2.260   9.582  -6.674  1.00 32.77           C
ANISOU 2031  CG  ARG A 253     3694   4878   3880    -27   -121    -39       C
ATOM   2032  CD  ARG A 253       3.626   9.304  -7.166  1.00 39.86           C
ANISOU 2032  CD  ARG A 253     4590   5791   4764      3   -161    -10       C
ATOM   2033  NE  ARG A 253       3.641   9.419  -8.614  1.00 42.16           N
ANISOU 2033  NE  ARG A 253     4792   6173   5054      9   -186    -32       N
ATOM   2034  CZ  ARG A 253       4.748   9.529  -9.328  1.00 39.02           C
ANISOU 2034  CZ  ARG A 253     4367   5816   4642     39   -231     -2       C
ATOM   2035  NH1 ARG A 253       5.922   9.558  -8.714  1.00 41.82           N
ANISOU 2035  NH1 ARG A 253     4776   6129   4984     63   -258     49       N
ATOM   2036  NH2 ARG A 253       4.676   9.619 -10.647  1.00 45.58           N
ANISOU 2036  NH2 ARG A 253     5116   6731   5470     45   -249    -24       N
ATOM   2037  N   LEU A 254      -1.294   8.540  -6.213  1.00 24.21           N
ANISOU 2037  N   LEU A 254     2591   3754   2853   -122     27   -180       N
ATOM   2038  CA  LEU A 254      -2.451   8.755  -7.079  1.00 25.57           C
ANISOU 2038  CA  LEU A 254     2685   3990   3040   -144     41   -231       C
ATOM   2039  C   LEU A 254      -3.388   9.798  -6.489  1.00 30.09           C
ANISOU 2039  C   LEU A 254     3257   4563   3612   -154     47   -221       C
ATOM   2040  O   LEU A 254      -3.912  10.653  -7.213  1.00 28.31           O
ANISOU 2040  O   LEU A 254     2964   4408   3383   -153     23   -229       O
ATOM   2041  CB  LEU A 254      -3.216   7.453  -7.293  1.00 35.93           C
ANISOU 2041  CB  LEU A 254     3991   5280   4382   -177    101   -301       C
ATOM   2042  CG  LEU A 254      -2.497   6.272  -7.949  1.00 37.50           C
ANISOU 2042  CG  LEU A 254     4185   5479   4586   -172    104   -325       C
ATOM   2043  CD1 LEU A 254      -3.508   5.165  -8.205  1.00 39.17           C
ANISOU 2043  CD1 LEU A 254     4377   5673   4830   -209    163   -399       C
ATOM   2044  CD2 LEU A 254      -1.812   6.704  -9.225  1.00 32.74           C
ANISOU 2044  CD2 LEU A 254     3512   4963   3966   -145     47   -317       C
ATOM   2045  N   ALA A 255      -3.619   9.730  -5.172  1.00 22.37           N
ANISOU 2045  N   ALA A 255     2355   3508   2636   -163     79   -203       N
ATOM   2046  CA  ALA A 255      -4.509  10.680  -4.511  1.00 23.05           C
ANISOU 2046  CA  ALA A 255     2448   3589   2722   -171     87   -192       C
ATOM   2047  C   ALA A 255      -4.027  12.114  -4.702  1.00 21.19           C
ANISOU 2047  C   ALA A 255     2186   3402   2462   -141     21   -140       C
ATOM   2048  O   ALA A 255      -4.814  13.005  -5.034  1.00 22.89           O
ANISOU 2048  O   ALA A 255     2352   3667   2678   -147     10   -149       O
ATOM   2049  CB  ALA A 255      -4.612  10.335  -3.026  1.00 19.60           C
ANISOU 2049  CB  ALA A 255     2104   3058   2286   -177    127   -174       C
ATOM   2050  N   LYS A 256      -2.732  12.353  -4.478  1.00 26.83           N
ANISOU 2050  N   LYS A 256     2935   4102   3158   -109    -24    -86       N
ATOM   2051  CA  LYS A 256      -2.170  13.689  -4.655  1.00 27.06           C
ANISOU 2051  CA  LYS A 256     2941   4174   3167    -80    -89    -33       C
ATOM   2052  C   LYS A 256      -2.385  14.197  -6.073  1.00 25.46           C
ANISOU 2052  C   LYS A 256     2641   4069   2964    -77   -120    -52       C
ATOM   2053  O   LYS A 256      -2.720  15.371  -6.274  1.00 31.13           O
ANISOU 2053  O   LYS A 256     3322   4832   3675    -70   -152    -33       O
ATOM   2054  CB  LYS A 256      -0.679  13.676  -4.316  1.00 32.83           C
ANISOU 2054  CB  LYS A 256     3719   4874   3882    -47   -131     22       C
ATOM   2055  CG  LYS A 256       0.037  15.009  -4.578  1.00 36.34           C
ANISOU 2055  CG  LYS A 256     4136   5363   4310    -16   -201     79       C
ATOM   2056  CD  LYS A 256       1.415  14.782  -5.179  1.00 43.38           C
ANISOU 2056  CD  LYS A 256     5017   6273   5191     11   -244    109       C
ATOM   2057  CE  LYS A 256       1.973  16.066  -5.802  1.00 53.56           C
ANISOU 2057  CE  LYS A 256     6255   7627   6470     38   -311    155       C
ATOM   2058  NZ  LYS A 256       3.103  15.803  -6.745  1.00 52.31           N
ANISOU 2058  NZ  LYS A 256     6061   7509   6304     60   -346    172       N
ATOM   2059  N   GLU A 257      -2.192  13.329  -7.068  1.00 28.50           N
ANISOU 2059  N   GLU A 257     2985   4488   3356    -82   -112    -88       N
ATOM   2060  CA  GLU A 257      -2.370  13.729  -8.459  1.00 35.52           C
ANISOU 2060  CA  GLU A 257     3782   5472   4243    -76   -140   -108       C
ATOM   2061  C   GLU A 257      -3.827  14.009  -8.780  1.00 34.62           C
ANISOU 2061  C   GLU A 257     3618   5394   4142   -103   -111   -158       C
ATOM   2062  O   GLU A 257      -4.116  14.831  -9.655  1.00 39.30           O
ANISOU 2062  O   GLU A 257     4140   6062   4729    -94   -141   -160       O
ATOM   2063  CB  GLU A 257      -1.851  12.641  -9.402  1.00 38.13           C
ANISOU 2063  CB  GLU A 257     4084   5826   4578    -74   -135   -140       C
ATOM   2064  CG  GLU A 257      -0.405  12.255  -9.183  1.00 41.02           C
ANISOU 2064  CG  GLU A 257     4495   6160   4931    -48   -161    -96       C
ATOM   2065  CD  GLU A 257       0.072  11.214 -10.175  1.00 50.84           C
ANISOU 2065  CD  GLU A 257     5706   7433   6178    -44   -158   -129       C
ATOM   2066  OE1 GLU A 257       1.083  11.477 -10.858  1.00 57.23           O
ANISOU 2066  OE1 GLU A 257     6488   8286   6971    -14   -204    -97       O
ATOM   2067  OE2 GLU A 257      -0.563  10.140 -10.281  1.00 52.87           O
ANISOU 2067  OE2 GLU A 257     5964   7670   6453    -70   -109   -188       O
ATOM   2068  N   GLU A 258      -4.749  13.347  -8.082  1.00 27.42           N
ANISOU 2068  N   GLU A 258     2741   4429   3250   -134    -52   -197       N
ATOM   2069  CA  GLU A 258      -6.154  13.332  -8.455  1.00 27.57           C
ANISOU 2069  CA  GLU A 258     2710   4478   3287   -163    -16   -256       C
ATOM   2070  C   GLU A 258      -7.053  14.071  -7.474  1.00 30.75           C
ANISOU 2070  C   GLU A 258     3141   4850   3691   -177      3   -247       C
ATOM   2071  O   GLU A 258      -8.262  14.159  -7.718  1.00 27.18           O
ANISOU 2071  O   GLU A 258     2649   4424   3254   -201     32   -293       O
ATOM   2072  CB  GLU A 258      -6.640  11.882  -8.607  1.00 34.11           C
ANISOU 2072  CB  GLU A 258     3542   5278   4141   -193     42   -320       C
ATOM   2073  CG  GLU A 258      -5.928  11.124  -9.729  1.00 38.29           C
ANISOU 2073  CG  GLU A 258     4031   5847   4670   -181     25   -341       C
ATOM   2074  CD  GLU A 258      -6.152   9.628  -9.662  1.00 47.00           C
ANISOU 2074  CD  GLU A 258     5157   6904   5799   -206     78   -393       C
ATOM   2075  OE1 GLU A 258      -7.122   9.201  -9.008  1.00 48.91           O
ANISOU 2075  OE1 GLU A 258     5422   7098   6063   -238    132   -426       O
ATOM   2076  OE2 GLU A 258      -5.352   8.876 -10.262  1.00 52.47           O
ANISOU 2076  OE2 GLU A 258     5842   7605   6489   -194     67   -400       O
ATOM   2077  N   GLY A 259      -6.508  14.597  -6.379  1.00 25.02           N
ANISOU 2077  N   GLY A 259     2484   4072   2952   -161    -13   -190       N
ATOM   2078  CA  GLY A 259      -7.283  15.429  -5.477  1.00 23.10           C
ANISOU 2078  CA  GLY A 259     2266   3806   2706   -167     -3   -176       C
ATOM   2079  C   GLY A 259      -7.936  14.717  -4.309  1.00 30.25           C
ANISOU 2079  C   GLY A 259     3238   4629   3626   -192     60   -194       C
ATOM   2080  O   GLY A 259      -8.863  15.273  -3.707  1.00 28.90           O
ANISOU 2080  O   GLY A 259     3075   4447   3457   -204     80   -199       O
ATOM   2081  N   TRP A 260      -7.486  13.512  -3.956  1.00 21.01           N
ANISOU 2081  N   TRP A 260     2117   3402   2466   -199     94   -204       N
ATOM   2082  CA  TRP A 260      -8.063  12.839  -2.796  1.00 21.02           C
ANISOU 2082  CA  TRP A 260     2186   3321   2479   -221    155   -217       C
ATOM   2083  C   TRP A 260      -6.985  12.433  -1.803  1.00 17.23           C
ANISOU 2083  C   TRP A 260     1794   2765   1985   -200    152   -170       C
ATOM   2084  O   TRP A 260      -5.854  12.925  -1.879  1.00 20.12           O
ANISOU 2084  O   TRP A 260     2172   3142   2331   -168     97   -122       O
ATOM   2085  CB  TRP A 260      -8.907  11.636  -3.221  1.00 22.49           C
ANISOU 2085  CB  TRP A 260     2347   3502   2698   -257    216   -286       C
ATOM   2086  CG  TRP A 260      -8.285  10.668  -4.201  1.00 25.14           C
ANISOU 2086  CG  TRP A 260     2651   3859   3041   -258    211   -314       C
ATOM   2087  CD1 TRP A 260      -8.084  10.865  -5.535  1.00 26.54           C
ANISOU 2087  CD1 TRP A 260     2750   4117   3215   -249    174   -332       C
ATOM   2088  CD2 TRP A 260      -7.864   9.325  -3.924  1.00 23.56           C
ANISOU 2088  CD2 TRP A 260     2497   3599   2855   -267    249   -329       C
ATOM   2089  NE1 TRP A 260      -7.539   9.732  -6.107  1.00 25.93           N
ANISOU 2089  NE1 TRP A 260     2667   4035   3148   -251    183   -358       N
ATOM   2090  CE2 TRP A 260      -7.391   8.775  -5.138  1.00 28.65           C
ANISOU 2090  CE2 TRP A 260     3088   4294   3505   -263    228   -357       C
ATOM   2091  CE3 TRP A 260      -7.832   8.538  -2.765  1.00 25.55           C
ANISOU 2091  CE3 TRP A 260     2832   3760   3115   -277    297   -321       C
ATOM   2092  CZ2 TRP A 260      -6.880   7.474  -5.226  1.00 27.66           C
ANISOU 2092  CZ2 TRP A 260     2989   4130   3392   -269    253   -378       C
ATOM   2093  CZ3 TRP A 260      -7.326   7.231  -2.856  1.00 25.26           C
ANISOU 2093  CZ3 TRP A 260     2821   3684   3091   -284    323   -341       C
ATOM   2094  CH2 TRP A 260      -6.863   6.718  -4.076  1.00 23.30           C
ANISOU 2094  CH2 TRP A 260     2518   3487   2849   -280    300   -370       C
ATOM   2095  N   LEU A 261      -7.331  11.566  -0.850  1.00 21.69           N
ANISOU 2095  N   LEU A 261     2424   3254   2563   -217    211   -183       N
ATOM   2096  CA  LEU A 261      -6.451  11.204   0.253  1.00 18.56           C
ANISOU 2096  CA  LEU A 261     2119   2780   2153   -198    215   -140       C
ATOM   2097  C   LEU A 261      -6.499   9.698   0.481  1.00 19.45           C
ANISOU 2097  C   LEU A 261     2269   2834   2286   -219    275   -173       C
ATOM   2098  O   LEU A 261      -7.570   9.092   0.427  1.00 26.85           O
ANISOU 2098  O   LEU A 261     3190   3763   3250   -254    331   -223       O
ATOM   2099  CB  LEU A 261      -6.870  11.921   1.550  1.00 17.47           C
ANISOU 2099  CB  LEU A 261     2041   2595   2003   -190    225   -107       C
ATOM   2100  CG  LEU A 261      -6.820  13.457   1.506  1.00 14.57           C
ANISOU 2100  CG  LEU A 261     1647   2275   1615   -167    166    -70       C
ATOM   2101  CD1 LEU A 261      -7.602  14.041   2.701  1.00 18.67           C
ANISOU 2101  CD1 LEU A 261     2212   2752   2128   -168    191    -55       C
ATOM   2102  CD2 LEU A 261      -5.368  13.911   1.531  1.00 17.88           C
ANISOU 2102  CD2 LEU A 261     2090   2694   2012   -128    100    -13       C
ATOM   2103  N   ALA A 262      -5.337   9.108   0.753  1.00 19.33           N
ANISOU 2103  N   ALA A 262     2306   2779   2261   -199    261   -145       N
ATOM   2104  CA  ALA A 262      -5.212   7.697   1.101  1.00 16.55           C
ANISOU 2104  CA  ALA A 262     2002   2362   1925   -214    314   -168       C
ATOM   2105  C   ALA A 262      -4.414   7.626   2.389  1.00 19.24           C
ANISOU 2105  C   ALA A 262     2441   2625   2245   -188    313   -116       C
ATOM   2106  O   ALA A 262      -3.245   8.016   2.406  1.00 19.17           O
ANISOU 2106  O   ALA A 262     2451   2620   2212   -154    259    -72       O
ATOM   2107  CB  ALA A 262      -4.521   6.891  -0.012  1.00 18.40           C
ANISOU 2107  CB  ALA A 262     2195   2628   2166   -214    298   -193       C
ATOM   2108  N   GLU A 263      -5.035   7.128   3.468  1.00 18.65           N
ANISOU 2108  N   GLU A 263     2429   2480   2179   -202    374   -121       N
ATOM   2109  CA  GLU A 263      -4.488   7.338   4.803  1.00 21.12           C
ANISOU 2109  CA  GLU A 263     2833   2723   2468   -174    372    -70       C
ATOM   2110  C   GLU A 263      -4.534   6.065   5.636  1.00 16.67           C
ANISOU 2110  C   GLU A 263     2344   2075   1917   -185    438    -80       C
ATOM   2111  O   GLU A 263      -5.378   5.193   5.432  1.00 22.38           O
ANISOU 2111  O   GLU A 263     3049   2785   2669   -221    497   -127       O
ATOM   2112  CB  GLU A 263      -5.252   8.452   5.549  1.00 16.03           C
ANISOU 2112  CB  GLU A 263     2200   2079   1813   -170    371    -50       C
ATOM   2113  CG  GLU A 263      -5.276   9.814   4.794  1.00 19.93           C
ANISOU 2113  CG  GLU A 263     2622   2656   2295   -158    306    -37       C
ATOM   2114  CD  GLU A 263      -3.902  10.440   4.654  1.00 21.43           C
ANISOU 2114  CD  GLU A 263     2822   2862   2459   -118    231     13       C
ATOM   2115  OE1 GLU A 263      -3.737  11.308   3.762  1.00 19.18           O
ANISOU 2115  OE1 GLU A 263     2469   2649   2169   -110    177     19       O
ATOM   2116  OE2 GLU A 263      -2.986  10.084   5.432  1.00 21.16           O
ANISOU 2116  OE2 GLU A 263     2862   2769   2411    -93    225     47       O
ATOM   2117  N   HIS A 264      -3.599   5.982   6.587  1.00 18.37           N
ANISOU 2117  N   HIS A 264     2642   2231   2108   -153    425    -33       N
ATOM   2118  CA  HIS A 264      -3.535   4.911   7.580  1.00 20.87           C
ANISOU 2118  CA  HIS A 264     3042   2460   2428   -155    483    -31       C
ATOM   2119  C   HIS A 264      -4.550   5.200   8.694  1.00 20.31           C
ANISOU 2119  C   HIS A 264     3014   2346   2358   -163    532    -25       C
ATOM   2120  O   HIS A 264      -4.196   5.476   9.838  1.00 17.79           O
ANISOU 2120  O   HIS A 264     2771   1974   2014   -134    531     17       O
ATOM   2121  CB  HIS A 264      -2.116   4.821   8.131  1.00 16.98           C
ANISOU 2121  CB  HIS A 264     2618   1927   1907   -113    444     17       C
ATOM   2122  CG  HIS A 264      -1.822   3.568   8.895  1.00 15.55           C
ANISOU 2122  CG  HIS A 264     2515   1662   1729   -113    496     17       C
ATOM   2123  ND1 HIS A 264      -0.729   3.448   9.732  1.00 17.57           N
ANISOU 2123  ND1 HIS A 264     2852   1865   1959    -74    475     61       N
ATOM   2124  CD2 HIS A 264      -2.457   2.371   8.930  1.00 18.28           C
ANISOU 2124  CD2 HIS A 264     2872   1970   2105   -146    567    -22       C
ATOM   2125  CE1 HIS A 264      -0.709   2.231  10.254  1.00 22.05           C
ANISOU 2125  CE1 HIS A 264     3477   2364   2536    -83    532     50       C
ATOM   2126  NE2 HIS A 264      -1.743   1.556   9.779  1.00 18.49           N
ANISOU 2126  NE2 HIS A 264     2985   1921   2120   -127    589      0       N
ATOM   2127  N   MET A 265      -5.837   5.154   8.331  1.00 15.81           N
ANISOU 2127  N   MET A 265     2391   1801   1814   -201    575    -68       N
ATOM   2128  CA  MET A 265      -6.923   5.514   9.243  1.00 18.40           C
ANISOU 2128  CA  MET A 265     2745   2101   2144   -211    622    -67       C
ATOM   2129  C   MET A 265      -8.020   4.456   9.302  1.00 19.14           C
ANISOU 2129  C   MET A 265     2834   2163   2277   -255    707   -114       C
ATOM   2130  O   MET A 265      -8.471   3.947   8.270  1.00 22.28           O
ANISOU 2130  O   MET A 265     3162   2598   2704   -288    721   -164       O
ATOM   2131  CB  MET A 265      -7.581   6.833   8.836  1.00 18.75           C
ANISOU 2131  CB  MET A 265     2725   2215   2183   -213    586    -68       C
ATOM   2132  CG  MET A 265      -6.675   8.003   8.915  1.00 20.98           C
ANISOU 2132  CG  MET A 265     3014   2525   2431   -171    506    -19       C
ATOM   2133  SD  MET A 265      -7.398   9.528   8.266  1.00 22.06           S
ANISOU 2133  SD  MET A 265     3068   2750   2564   -174    460    -24       S
ATOM   2134  CE  MET A 265      -6.015  10.611   8.581  1.00 17.93           C
ANISOU 2134  CE  MET A 265     2577   2233   2002   -120    370     42       C
ATOM   2135  N   LEU A 266      -8.484   4.169  10.517  1.00 17.73           N
ANISOU 2135  N   LEU A 266     2726   1915   2096   -254    763    -99       N
ATOM   2136  CA  LEU A 266      -9.768   3.512  10.672  1.00 17.92           C
ANISOU 2136  CA  LEU A 266     2737   1915   2156   -296    843   -140       C
ATOM   2137  C   LEU A 266     -10.888   4.495  10.327  1.00 23.59           C
ANISOU 2137  C   LEU A 266     3387   2693   2881   -314    839   -160       C
ATOM   2138  O   LEU A 266     -10.703   5.718  10.319  1.00 22.10           O
ANISOU 2138  O   LEU A 266     3184   2547   2665   -289    782   -133       O
ATOM   2139  CB  LEU A 266      -9.939   2.995  12.109  1.00 22.40           C
ANISOU 2139  CB  LEU A 266     3402   2393   2717   -286    905   -113       C
ATOM   2140  CG  LEU A 266     -10.029   4.119  13.182  1.00 24.97           C
ANISOU 2140  CG  LEU A 266     3776   2707   3006   -252    887    -66       C
ATOM   2141  CD1 LEU A 266     -11.466   4.587  13.450  1.00 28.08           C
ANISOU 2141  CD1 LEU A 266     4141   3114   3415   -277    932    -85       C
ATOM   2142  CD2 LEU A 266      -9.371   3.722  14.495  1.00 17.59           C
ANISOU 2142  CD2 LEU A 266     2949   1688   2044   -217    908    -20       C
ATOM   2143  N   ILE A 267     -12.060   3.943  10.034  1.00 22.07           N
ANISOU 2143  N   ILE A 267     3153   2503   2728   -357    900   -210       N
ATOM   2144  CA  ILE A 267     -13.284   4.710   9.851  1.00 21.48           C
ANISOU 2144  CA  ILE A 267     3022   2474   2666   -378    912   -233       C
ATOM   2145  C   ILE A 267     -14.342   4.055  10.727  1.00 20.75           C
ANISOU 2145  C   ILE A 267     2966   2321   2599   -405   1001   -247       C
ATOM   2146  O   ILE A 267     -14.544   2.838  10.655  1.00 22.70           O
ANISOU 2146  O   ILE A 267     3219   2526   2879   -433   1057   -277       O
ATOM   2147  CB  ILE A 267     -13.764   4.735   8.387  1.00 24.45           C
ANISOU 2147  CB  ILE A 267     3291   2928   3070   -409    893   -289       C
ATOM   2148  CG1 ILE A 267     -12.686   5.251   7.435  1.00 20.39           C
ANISOU 2148  CG1 ILE A 267     2739   2474   2534   -384    809   -276       C
ATOM   2149  CG2 ILE A 267     -15.033   5.573   8.255  1.00 27.49           C
ANISOU 2149  CG2 ILE A 267     3620   3359   3465   -429    905   -312       C
ATOM   2150  CD1 ILE A 267     -12.964   4.878   5.981  1.00 21.36           C
ANISOU 2150  CD1 ILE A 267     2768   2661   2687   -413    799   -334       C
ATOM   2151  N   LEU A 268     -15.005   4.840  11.564  1.00 22.32           N
ANISOU 2151  N   LEU A 268     3187   2511   2782   -396   1016   -226       N
ATOM   2152  CA  LEU A 268     -16.074   4.295  12.389  1.00 22.11           C
ANISOU 2152  CA  LEU A 268     3190   2432   2779   -420   1102   -238       C
ATOM   2153  C   LEU A 268     -17.272   5.226  12.332  1.00 29.20           C
ANISOU 2153  C   LEU A 268     4035   3376   3682   -435   1109   -255       C
ATOM   2154  O   LEU A 268     -17.137   6.420  12.049  1.00 24.38           O
ANISOU 2154  O   LEU A 268     3395   2823   3044   -414   1046   -240       O
ATOM   2155  CB  LEU A 268     -15.635   4.084  13.860  1.00 24.85           C
ANISOU 2155  CB  LEU A 268     3648   2696   3098   -388   1131   -185       C
ATOM   2156  CG  LEU A 268     -15.265   5.302  14.720  1.00 22.86           C
ANISOU 2156  CG  LEU A 268     3444   2445   2795   -340   1086   -130       C
ATOM   2157  CD1 LEU A 268     -16.488   6.033  15.288  1.00 22.48           C
ANISOU 2157  CD1 LEU A 268     3387   2408   2747   -347   1118   -132       C
ATOM   2158  CD2 LEU A 268     -14.330   4.884  15.846  1.00 20.75           C
ANISOU 2158  CD2 LEU A 268     3283   2102   2498   -301   1094    -80       C
ATOM   2159  N   GLY A 269     -18.452   4.660  12.614  1.00 25.07           N
ANISOU 2159  N   GLY A 269     3503   2827   3196   -472   1187   -286       N
ATOM   2160  CA  GLY A 269     -19.642   5.475  12.787  1.00 24.37           C
ANISOU 2160  CA  GLY A 269     3378   2770   3111   -484   1204   -299       C
ATOM   2161  C   GLY A 269     -20.129   5.395  14.214  1.00 24.84           C
ANISOU 2161  C   GLY A 269     3515   2763   3161   -474   1266   -266       C
ATOM   2162  O   GLY A 269     -20.226   4.301  14.768  1.00 26.56           O
ANISOU 2162  O   GLY A 269     3779   2911   3399   -488   1333   -267       O
ATOM   2163  N   ILE A 270     -20.454   6.520  14.841  1.00 20.96           N
ANISOU 2163  N   ILE A 270     3039   2287   2636   -448   1247   -238       N
ATOM   2164  CA  ILE A 270     -20.864   6.515  16.237  1.00 19.62           C
ANISOU 2164  CA  ILE A 270     2947   2056   2452   -432   1302   -203       C
ATOM   2165  C   ILE A 270     -22.230   7.188  16.358  1.00 22.16           C
ANISOU 2165  C   ILE A 270     3225   2411   2785   -451   1331   -224       C
ATOM   2166  O   ILE A 270     -22.467   8.244  15.758  1.00 22.82           O
ANISOU 2166  O   ILE A 270     3250   2565   2857   -447   1277   -234       O
ATOM   2167  CB  ILE A 270     -19.816   7.200  17.136  1.00 25.22           C
ANISOU 2167  CB  ILE A 270     3738   2741   3104   -373   1251   -139       C
ATOM   2168  CG1 ILE A 270     -20.289   7.206  18.586  1.00 24.61           C
ANISOU 2168  CG1 ILE A 270     3740   2602   3009   -353   1309   -105       C
ATOM   2169  CG2 ILE A 270     -19.496   8.635  16.641  1.00 22.54           C
ANISOU 2169  CG2 ILE A 270     3357   2475   2732   -347   1160   -127       C
ATOM   2170  CD1 ILE A 270     -19.158   7.419  19.573  1.00 30.57           C
ANISOU 2170  CD1 ILE A 270     4590   3309   3714   -296   1276    -45       C
ATOM   2171  N   THR A 271     -23.135   6.558  17.106  1.00 20.81           N
ANISOU 2171  N   THR A 271     3080   2189   2637   -472   1418   -230       N
ATOM   2172  CA  THR A 271     -24.492   7.062  17.283  1.00 22.87           C
ANISOU 2172  CA  THR A 271     3302   2474   2913   -492   1456   -251       C
ATOM   2173  C   THR A 271     -24.705   7.366  18.753  1.00 25.81           C
ANISOU 2173  C   THR A 271     3760   2795   3253   -459   1493   -203       C
ATOM   2174  O   THR A 271     -24.356   6.554  19.612  1.00 24.82           O
ANISOU 2174  O   THR A 271     3711   2595   3124   -448   1541   -175       O
ATOM   2175  CB  THR A 271     -25.545   6.063  16.796  1.00 25.21           C
ANISOU 2175  CB  THR A 271     3544   2762   3273   -551   1532   -307       C
ATOM   2176  OG1 THR A 271     -25.326   5.787  15.411  1.00 27.29           O
ANISOU 2176  OG1 THR A 271     3729   3076   3564   -578   1495   -354       O
ATOM   2177  CG2 THR A 271     -26.945   6.641  16.976  1.00 24.53           C
ANISOU 2177  CG2 THR A 271     3415   2704   3201   -571   1569   -329       C
ATOM   2178  N   ASN A 272     -25.259   8.530  19.040  1.00 23.44           N
ANISOU 2178  N   ASN A 272     3446   2533   2927   -442   1470   -193       N
ATOM   2179  CA  ASN A 272     -25.420   8.987  20.402  1.00 22.85           C
ANISOU 2179  CA  ASN A 272     3449   2418   2815   -404   1493   -146       C
ATOM   2180  C   ASN A 272     -26.823   8.661  20.906  1.00 27.13           C
ANISOU 2180  C   ASN A 272     3980   2940   3387   -434   1583   -165       C
ATOM   2181  O   ASN A 272     -27.670   8.155  20.161  1.00 25.12           O
ANISOU 2181  O   ASN A 272     3653   2706   3183   -486   1623   -217       O
ATOM   2182  CB  ASN A 272     -25.081  10.495  20.479  1.00 23.16           C
ANISOU 2182  CB  ASN A 272     3486   2509   2805   -361   1408   -118       C
ATOM   2183  CG  ASN A 272     -26.192  11.411  19.962  1.00 27.17           C
ANISOU 2183  CG  ASN A 272     3915   3087   3323   -381   1397   -151       C
ATOM   2184  OD1 ASN A 272     -27.157  10.983  19.328  1.00 24.90           O
ANISOU 2184  OD1 ASN A 272     3559   2821   3081   -429   1442   -200       O
ATOM   2185  ND2 ASN A 272     -26.030  12.708  20.224  1.00 32.62           N
ANISOU 2185  ND2 ASN A 272     4612   3812   3970   -342   1334   -124       N
ATOM   2186  N   PRO A 273     -27.087   8.878  22.197  1.00 23.69           N
ANISOU 2186  N   PRO A 273     3617   2460   2923   -403   1621   -125       N
ATOM   2187  CA  PRO A 273     -28.423   8.569  22.740  1.00 30.67           C
ANISOU 2187  CA  PRO A 273     4494   3323   3835   -430   1711   -140       C
ATOM   2188  C   PRO A 273     -29.556   9.407  22.155  1.00 30.51           C
ANISOU 2188  C   PRO A 273     4387   3374   3830   -455   1702   -178       C
ATOM   2189  O   PRO A 273     -30.723   9.047  22.349  1.00 31.11           O
ANISOU 2189  O   PRO A 273     4438   3441   3941   -488   1777   -202       O
ATOM   2190  CB  PRO A 273     -28.258   8.844  24.241  1.00 35.56           C
ANISOU 2190  CB  PRO A 273     5215   3890   4408   -378   1734    -81       C
ATOM   2191  CG  PRO A 273     -26.804   8.590  24.498  1.00 31.51           C
ANISOU 2191  CG  PRO A 273     4771   3339   3861   -339   1689    -43       C
ATOM   2192  CD  PRO A 273     -26.112   9.130  23.275  1.00 27.33           C
ANISOU 2192  CD  PRO A 273     4179   2876   3330   -344   1596    -64       C
ATOM   2193  N   GLU A 274     -29.261  10.506  21.457  1.00 27.48           N
ANISOU 2193  N   GLU A 274     3957   3061   3423   -441   1615   -185       N
ATOM   2194  CA  GLU A 274     -30.285  11.328  20.826  1.00 31.34           C
ANISOU 2194  CA  GLU A 274     4362   3622   3925   -463   1601   -223       C
ATOM   2195  C   GLU A 274     -30.589  10.893  19.396  1.00 38.32           C
ANISOU 2195  C   GLU A 274     5147   4553   4859   -515   1594   -285       C
ATOM   2196  O   GLU A 274     -31.277  11.623  18.674  1.00 31.85           O
ANISOU 2196  O   GLU A 274     4251   3802   4049   -531   1567   -319       O
ATOM   2197  CB  GLU A 274     -29.860  12.802  20.830  1.00 31.63           C
ANISOU 2197  CB  GLU A 274     4398   3710   3909   -418   1510   -197       C
ATOM   2198  CG  GLU A 274     -29.465  13.362  22.188  1.00 31.76           C
ANISOU 2198  CG  GLU A 274     4509   3685   3871   -361   1502   -137       C
ATOM   2199  CD  GLU A 274     -30.637  13.497  23.142  1.00 34.76           C
ANISOU 2199  CD  GLU A 274     4910   4046   4251   -360   1573   -131       C
ATOM   2200  OE1 GLU A 274     -30.397  13.573  24.364  1.00 37.76           O
ANISOU 2200  OE1 GLU A 274     5377   4376   4595   -318   1592    -84       O
ATOM   2201  OE2 GLU A 274     -31.798  13.522  22.680  1.00 33.88           O
ANISOU 2201  OE2 GLU A 274     4729   3970   4175   -401   1610   -174       O
ATOM   2202  N   GLY A 275     -30.072   9.740  18.967  1.00 36.16           N
ANISOU 2202  N   GLY A 275     4875   4246   4617   -538   1615   -300       N
ATOM   2203  CA  GLY A 275     -30.282   9.255  17.616  1.00 35.20           C
ANISOU 2203  CA  GLY A 275     4665   4167   4543   -584   1606   -359       C
ATOM   2204  C   GLY A 275     -29.535   9.999  16.532  1.00 32.55           C
ANISOU 2204  C   GLY A 275     4279   3901   4188   -571   1509   -368       C
ATOM   2205  O   GLY A 275     -29.965   9.976  15.375  1.00 29.77           O
ANISOU 2205  O   GLY A 275     3839   3605   3868   -605   1493   -421       O
ATOM   2206  N   LYS A 276     -28.429  10.660  16.862  1.00 24.21           N
ANISOU 2206  N   LYS A 276     3274   2844   3080   -522   1442   -319       N
ATOM   2207  CA  LYS A 276     -27.578  11.299  15.863  1.00 26.04           C
ANISOU 2207  CA  LYS A 276     3464   3136   3292   -507   1349   -322       C
ATOM   2208  C   LYS A 276     -26.347  10.436  15.617  1.00 23.09           C
ANISOU 2208  C   LYS A 276     3124   2727   2920   -501   1332   -309       C
ATOM   2209  O   LYS A 276     -25.770   9.891  16.562  1.00 26.28           O
ANISOU 2209  O   LYS A 276     3614   3062   3309   -479   1359   -270       O
ATOM   2210  CB  LYS A 276     -27.136  12.690  16.319  1.00 29.66           C
ANISOU 2210  CB  LYS A 276     3952   3622   3695   -457   1279   -277       C
ATOM   2211  CG  LYS A 276     -28.274  13.607  16.757  1.00 37.76           C
ANISOU 2211  CG  LYS A 276     4959   4676   4712   -455   1294   -281       C
ATOM   2212  CD  LYS A 276     -29.245  13.855  15.619  1.00 41.44           C
ANISOU 2212  CD  LYS A 276     5319   5213   5212   -496   1291   -340       C
ATOM   2213  CE  LYS A 276     -30.033  15.118  15.849  1.00 43.37           C
ANISOU 2213  CE  LYS A 276     5539   5504   5434   -481   1270   -338       C
ATOM   2214  NZ  LYS A 276     -30.251  15.316  17.292  1.00 44.77           N
ANISOU 2214  NZ  LYS A 276     5800   5628   5585   -452   1308   -294       N
ATOM   2215  N   LYS A 277     -25.922  10.339  14.350  1.00 21.38           N
ANISOU 2215  N   LYS A 277     2843   2561   2719   -516   1285   -341       N
ATOM   2216  CA  LYS A 277     -24.801   9.489  13.978  1.00 22.78           C
ANISOU 2216  CA  LYS A 277     3042   2712   2901   -513   1268   -335       C
ATOM   2217  C   LYS A 277     -23.753  10.291  13.221  1.00 27.55           C
ANISOU 2217  C   LYS A 277     3623   3372   3474   -484   1170   -319       C
ATOM   2218  O   LYS A 277     -24.086  11.081  12.332  1.00 24.70           O
ANISOU 2218  O   LYS A 277     3186   3085   3113   -490   1125   -344       O
ATOM   2219  CB  LYS A 277     -25.260   8.304  13.112  1.00 25.03           C
ANISOU 2219  CB  LYS A 277     3271   2996   3244   -564   1314   -394       C
ATOM   2220  CG  LYS A 277     -24.135   7.397  12.687  1.00 21.83           C
ANISOU 2220  CG  LYS A 277     2885   2565   2844   -562   1298   -392       C
ATOM   2221  CD  LYS A 277     -24.685   6.126  12.038  1.00 27.89           C
ANISOU 2221  CD  LYS A 277     3607   3318   3671   -612   1356   -449       C
ATOM   2222  CE  LYS A 277     -23.561   5.230  11.565  1.00 25.26           C
ANISOU 2222  CE  LYS A 277     3292   2963   3343   -609   1336   -449       C
ATOM   2223  NZ  LYS A 277     -24.063   3.942  10.994  1.00 26.54           N
ANISOU 2223  NZ  LYS A 277     3416   3104   3565   -656   1393   -504       N
ATOM   2224  N   LYS A 278     -22.481  10.085  13.576  1.00 21.21           N
ANISOU 2224  N   LYS A 278     2883   2531   2643   -451   1138   -277       N
ATOM   2225  CA  LYS A 278     -21.379  10.760  12.907  1.00 28.18           C
ANISOU 2225  CA  LYS A 278     3749   3460   3498   -422   1047   -257       C
ATOM   2226  C   LYS A 278     -20.288   9.748  12.586  1.00 26.48           C
ANISOU 2226  C   LYS A 278     3558   3213   3289   -421   1040   -253       C
ATOM   2227  O   LYS A 278     -20.159   8.710  13.246  1.00 25.10           O
ANISOU 2227  O   LYS A 278     3443   2967   3127   -426   1097   -246       O
ATOM   2228  CB  LYS A 278     -20.812  11.912  13.755  1.00 27.17           C
ANISOU 2228  CB  LYS A 278     3677   3328   3318   -371    994   -198       C
ATOM   2229  CG  LYS A 278     -21.779  13.085  13.907  1.00 26.04           C
ANISOU 2229  CG  LYS A 278     3501   3229   3164   -368    984   -202       C
ATOM   2230  CD  LYS A 278     -21.260  14.128  14.889  1.00 29.23           C
ANISOU 2230  CD  LYS A 278     3969   3618   3519   -316    939   -144       C
ATOM   2231  CE  LYS A 278     -22.295  15.228  15.099  1.00 26.62           C
ANISOU 2231  CE  LYS A 278     3608   3327   3178   -314    934   -150       C
ATOM   2232  NZ  LYS A 278     -22.772  15.713  13.778  1.00 22.60           N
ANISOU 2232  NZ  LYS A 278     2996   2901   2689   -340    901   -192       N
ATOM   2233  N   TYR A 279     -19.522  10.044  11.546  1.00 21.65           N
ANISOU 2233  N   TYR A 279     2900   2655   2671   -413    972   -258       N
ATOM   2234  CA  TYR A 279     -18.399   9.210  11.156  1.00 17.59           C
ANISOU 2234  CA  TYR A 279     2404   2119   2159   -407    955   -253       C
ATOM   2235  C   TYR A 279     -17.084   9.901  11.488  1.00 22.31           C
ANISOU 2235  C   TYR A 279     3051   2713   2711   -357    882   -196       C
ATOM   2236  O   TYR A 279     -16.910  11.106  11.233  1.00 21.26           O
ANISOU 2236  O   TYR A 279     2890   2634   2554   -335    818   -178       O
ATOM   2237  CB  TYR A 279     -18.474   8.852   9.669  1.00 25.65           C
ANISOU 2237  CB  TYR A 279     3334   3202   3211   -437    936   -306       C
ATOM   2238  CG  TYR A 279     -19.556   7.823   9.346  1.00 27.34           C
ANISOU 2238  CG  TYR A 279     3509   3402   3476   -487   1012   -364       C
ATOM   2239  CD1 TYR A 279     -20.848   8.220   9.006  1.00 21.49           C
ANISOU 2239  CD1 TYR A 279     2703   2703   2758   -516   1036   -405       C
ATOM   2240  CD2 TYR A 279     -19.283   6.455   9.387  1.00 19.62           C
ANISOU 2240  CD2 TYR A 279     2559   2369   2526   -506   1059   -380       C
ATOM   2241  CE1 TYR A 279     -21.839   7.283   8.711  1.00 25.48           C
ANISOU 2241  CE1 TYR A 279     3171   3196   3313   -562   1104   -460       C
ATOM   2242  CE2 TYR A 279     -20.263   5.513   9.087  1.00 23.74           C
ANISOU 2242  CE2 TYR A 279     3044   2877   3098   -552   1127   -435       C
ATOM   2243  CZ  TYR A 279     -21.535   5.930   8.749  1.00 25.53           C
ANISOU 2243  CZ  TYR A 279     3206   3147   3349   -581   1149   -475       C
ATOM   2244  OH  TYR A 279     -22.503   4.994   8.448  1.00 26.85           O
ANISOU 2244  OH  TYR A 279     3333   3299   3569   -627   1215   -530       O
ATOM   2245  N   LEU A 280     -16.162   9.129  12.063  1.00 23.12           N
ANISOU 2245  N   LEU A 280     3227   2753   2805   -339    892   -168       N
ATOM   2246  CA  LEU A 280     -14.851   9.604  12.480  1.00 20.40           C
ANISOU 2246  CA  LEU A 280     2937   2393   2420   -292    830   -114       C
ATOM   2247  C   LEU A 280     -13.771   8.768  11.806  1.00 22.83           C
ANISOU 2247  C   LEU A 280     3244   2696   2735   -291    808   -119       C
ATOM   2248  O   LEU A 280     -13.929   7.556  11.633  1.00 21.29           O
ANISOU 2248  O   LEU A 280     3051   2468   2570   -319    862   -148       O
ATOM   2249  CB  LEU A 280     -14.689   9.515  14.006  1.00 21.06           C
ANISOU 2249  CB  LEU A 280     3124   2398   2479   -262    862    -70       C
ATOM   2250  CG  LEU A 280     -15.762  10.189  14.866  1.00 22.33           C
ANISOU 2250  CG  LEU A 280     3301   2552   2631   -260    895    -63       C
ATOM   2251  CD1 LEU A 280     -15.472   9.987  16.346  1.00 21.05           C
ANISOU 2251  CD1 LEU A 280     3246   2311   2443   -227    925    -18       C
ATOM   2252  CD2 LEU A 280     -15.808  11.688  14.531  1.00 19.83           C
ANISOU 2252  CD2 LEU A 280     2940   2303   2291   -240    822    -50       C
ATOM   2253  N   ALA A 281     -12.675   9.411  11.417  1.00 22.94           N
ANISOU 2253  N   ALA A 281     3252   2742   2723   -259    730    -89       N
ATOM   2254  CA  ALA A 281     -11.488   8.694  10.973  1.00 21.89           C
ANISOU 2254  CA  ALA A 281     3132   2596   2588   -249    704    -82       C
ATOM   2255  C   ALA A 281     -10.392   8.874  12.016  1.00 22.46           C
ANISOU 2255  C   ALA A 281     3296   2614   2624   -202    676    -24       C
ATOM   2256  O   ALA A 281     -10.335   9.907  12.689  1.00 19.87           O
ANISOU 2256  O   ALA A 281     2996   2287   2268   -172    644     12       O
ATOM   2257  CB  ALA A 281     -11.019   9.203   9.608  1.00 22.27           C
ANISOU 2257  CB  ALA A 281     3097   2726   2637   -249    636    -95       C
ATOM   2258  N   ALA A 282      -9.526   7.872  12.172  1.00 18.24           N
ANISOU 2258  N   ALA A 282     2809   2031   2090   -194    687    -15       N
ATOM   2259  CA  ALA A 282      -8.468   7.998  13.169  1.00 20.73           C
ANISOU 2259  CA  ALA A 282     3213   2293   2371   -149    661     38       C
ATOM   2260  C   ALA A 282      -7.168   7.383  12.673  1.00 23.46           C
ANISOU 2260  C   ALA A 282     3568   2632   2712   -135    625     47       C
ATOM   2261  O   ALA A 282      -7.138   6.212  12.272  1.00 22.33           O
ANISOU 2261  O   ALA A 282     3420   2470   2593   -159    665     17       O
ATOM   2262  CB  ALA A 282      -8.886   7.373  14.511  1.00 18.92           C
ANISOU 2262  CB  ALA A 282     3070   1980   2137   -144    732     51       C
ATOM   2263  N   ALA A 283      -6.085   8.163  12.736  1.00 18.75           N
ANISOU 2263  N   ALA A 283     2988   2051   2087    -94    551     89       N
ATOM   2264  CA  ALA A 283      -4.762   7.707  12.318  1.00 20.22           C
ANISOU 2264  CA  ALA A 283     3185   2232   2264    -75    509    103       C
ATOM   2265  C   ALA A 283      -3.898   7.498  13.553  1.00 19.13           C
ANISOU 2265  C   ALA A 283     3151   2019   2099    -34    507    148       C
ATOM   2266  O   ALA A 283      -3.458   8.462  14.181  1.00 20.30           O
ANISOU 2266  O   ALA A 283     3332   2163   2219      3    460    189       O
ATOM   2267  CB  ALA A 283      -4.102   8.698  11.356  1.00 20.04           C
ANISOU 2267  CB  ALA A 283     3098   2285   2233    -60    425    116       C
ATOM   2268  N   PHE A 284      -3.653   6.237  13.899  1.00 15.72           N
ANISOU 2268  N   PHE A 284     2770   1528   1675    -40    557    140       N
ATOM   2269  CA  PHE A 284      -2.674   5.859  14.901  1.00 15.77           C
ANISOU 2269  CA  PHE A 284     2871   1465   1655     -1    552    179       C
ATOM   2270  C   PHE A 284      -1.626   4.984  14.236  1.00 17.89           C
ANISOU 2270  C   PHE A 284     3137   1731   1930      0    534    172       C
ATOM   2271  O   PHE A 284      -1.958   4.245  13.308  1.00 21.93           O
ANISOU 2271  O   PHE A 284     3595   2268   2471    -37    560    131       O
ATOM   2272  CB  PHE A 284      -3.291   5.037  16.048  1.00 16.24           C
ANISOU 2272  CB  PHE A 284     3008   1446   1717     -6    635    179       C
ATOM   2273  CG  PHE A 284      -4.520   5.641  16.671  1.00 19.75           C
ANISOU 2273  CG  PHE A 284     3454   1889   2162    -15    672    176       C
ATOM   2274  CD1 PHE A 284      -4.647   7.022  16.838  1.00 20.09           C
ANISOU 2274  CD1 PHE A 284     3479   1970   2185      7    620    199       C
ATOM   2275  CD2 PHE A 284      -5.544   4.814  17.122  1.00 26.65           C
ANISOU 2275  CD2 PHE A 284     4348   2720   3057    -45    760    152       C
ATOM   2276  CE1 PHE A 284      -5.784   7.564  17.413  1.00 22.75           C
ANISOU 2276  CE1 PHE A 284     3817   2307   2521     -1    654    196       C
ATOM   2277  CE2 PHE A 284      -6.675   5.343  17.716  1.00 25.46           C
ANISOU 2277  CE2 PHE A 284     4199   2567   2906    -53    797    151       C
ATOM   2278  CZ  PHE A 284      -6.800   6.727  17.862  1.00 21.49           C
ANISOU 2278  CZ  PHE A 284     3678   2106   2382    -30    743    172       C
ATOM   2279  N   PRO A 285      -0.390   4.969  14.733  1.00 20.34           N
ANISOU 2279  N   PRO A 285     3507   2008   2214     42    493    211       N
ATOM   2280  CA  PRO A 285       0.626   4.071  14.167  1.00 20.65           C
ANISOU 2280  CA  PRO A 285     3549   2041   2258     45    479    205       C
ATOM   2281  C   PRO A 285       0.282   2.611  14.439  1.00 20.35           C
ANISOU 2281  C   PRO A 285     3550   1942   2238     21    559    178       C
ATOM   2282  O   PRO A 285      -0.574   2.279  15.251  1.00 20.60           O
ANISOU 2282  O   PRO A 285     3624   1928   2277      9    624    173       O
ATOM   2283  CB  PRO A 285       1.917   4.466  14.896  1.00 24.75           C
ANISOU 2283  CB  PRO A 285     4135   2527   2741     99    423    256       C
ATOM   2284  CG  PRO A 285       1.627   5.805  15.532  1.00 26.01           C
ANISOU 2284  CG  PRO A 285     4302   2698   2881    122    390    286       C
ATOM   2285  CD  PRO A 285       0.154   5.794  15.822  1.00 25.91           C
ANISOU 2285  CD  PRO A 285     4279   2681   2884     90    456    260       C
ATOM   2286  N   SER A 286       0.982   1.724  13.741  1.00 22.72           N
ANISOU 2286  N   SER A 286     3838   2245   2550     14    553    162       N
ATOM   2287  CA  SER A 286       0.813   0.304  14.040  1.00 22.39           C
ANISOU 2287  CA  SER A 286     3841   2140   2526     -4    624    140       C
ATOM   2288  C   SER A 286       1.087   0.042  15.517  1.00 22.96           C
ANISOU 2288  C   SER A 286     4023   2128   2573     29    653    177       C
ATOM   2289  O   SER A 286       1.894   0.725  16.152  1.00 28.50           O
ANISOU 2289  O   SER A 286     4771   2817   3241     74    604    220       O
ATOM   2290  CB  SER A 286       1.747  -0.537  13.166  1.00 30.13           C
ANISOU 2290  CB  SER A 286     4802   3132   3514     -6    602    124       C
ATOM   2291  OG  SER A 286       1.864   0.033  11.867  1.00 41.30           O
ANISOU 2291  OG  SER A 286     6122   4633   4938    -18    549    106       O
ATOM   2292  N   ALA A 287       0.377  -0.948  16.072  1.00 27.42           N
ANISOU 2292  N   ALA A 287     4629   2634   3156      7    735    160       N
ATOM   2293  CA  ALA A 287       0.466  -1.349  17.476  1.00 28.83           C
ANISOU 2293  CA  ALA A 287     4912   2728   3314     34    778    191       C
ATOM   2294  C   ALA A 287      -0.051  -0.293  18.447  1.00 26.17           C
ANISOU 2294  C   ALA A 287     4607   2384   2954     57    775    221       C
ATOM   2295  O   ALA A 287       0.294  -0.330  19.637  1.00 28.12           O
ANISOU 2295  O   ALA A 287     4943   2571   3172     95    787    257       O
ATOM   2296  CB  ALA A 287       1.895  -1.739  17.873  1.00 25.37           C
ANISOU 2296  CB  ALA A 287     4542   2250   2847     78    742    222       C
ATOM   2297  N   CYS A 288      -0.876   0.653  17.984  1.00 25.48           N
ANISOU 2297  N   CYS A 288     4449   2357   2876     37    761    208       N
ATOM   2298  CA  CYS A 288      -1.337   1.750  18.830  1.00 17.77           C
ANISOU 2298  CA  CYS A 288     3497   1380   1875     60    750    236       C
ATOM   2299  C   CYS A 288      -2.859   1.851  18.937  1.00 29.77           C
ANISOU 2299  C   CYS A 288     4986   2908   3419     23    814    210       C
ATOM   2300  O   CYS A 288      -3.369   2.875  19.428  1.00 23.65           O
ANISOU 2300  O   CYS A 288     4211   2148   2627     37    801    227       O
ATOM   2301  CB  CYS A 288      -0.753   3.077  18.314  1.00 21.43           C
ANISOU 2301  CB  CYS A 288     3912   1910   2320     84    657    255       C
ATOM   2302  SG  CYS A 288       1.032   3.164  18.553  1.00 26.43           S
ANISOU 2302  SG  CYS A 288     4600   2523   2920    138    582    297       S
ATOM   2303  N   GLY A 289      -3.596   0.843  18.472  1.00 31.80           N
ANISOU 2303  N   GLY A 289     5212   3156   3714    -24    879    169       N
ATOM   2304  CA  GLY A 289      -4.982   0.652  18.863  1.00 26.38           C
ANISOU 2304  CA  GLY A 289     4521   2452   3050    -56    956    148       C
ATOM   2305  C   GLY A 289      -6.059   1.036  17.867  1.00 25.94           C
ANISOU 2305  C   GLY A 289     4363   2464   3027   -102    962    105       C
ATOM   2306  O   GLY A 289      -7.210   1.242  18.284  1.00 23.89           O
ANISOU 2306  O   GLY A 289     4098   2200   2780   -121   1012     95       O
ATOM   2307  N   LYS A 290      -5.738   1.143  16.577  1.00 20.21           N
ANISOU 2307  N   LYS A 290     3559   1803   2317   -120    915     78       N
ATOM   2308  CA  LYS A 290      -6.776   1.451  15.593  1.00 20.37           C
ANISOU 2308  CA  LYS A 290     3482   1889   2370   -164    922     33       C
ATOM   2309  C   LYS A 290      -7.884   0.407  15.612  1.00 23.15           C
ANISOU 2309  C   LYS A 290     3824   2208   2765   -210   1013     -8       C
ATOM   2310  O   LYS A 290      -9.075   0.743  15.624  1.00 25.47           O
ANISOU 2310  O   LYS A 290     4081   2520   3078   -237   1049    -29       O
ATOM   2311  CB  LYS A 290      -6.177   1.551  14.190  1.00 19.36           C
ANISOU 2311  CB  LYS A 290     3275   1830   2251   -173    861     10       C
ATOM   2312  CG  LYS A 290      -5.452   2.871  13.919  1.00 16.96           C
ANISOU 2312  CG  LYS A 290     2948   1582   1914   -138    771     41       C
ATOM   2313  CD  LYS A 290      -5.018   3.021  12.450  1.00 17.69           C
ANISOU 2313  CD  LYS A 290     2953   1751   2019   -150    716     16       C
ATOM   2314  CE  LYS A 290      -4.250   1.803  11.959  1.00 17.08           C
ANISOU 2314  CE  LYS A 290     2884   1651   1954   -156    724     -0       C
ATOM   2315  NZ  LYS A 290      -2.959   1.623  12.706  1.00 17.26           N
ANISOU 2315  NZ  LYS A 290     2990   1622   1945   -112    695     46       N
ATOM   2316  N   THR A 291      -7.514  -0.878  15.582  1.00 21.76           N
ANISOU 2316  N   THR A 291     3678   1982   2607   -222   1051    -21       N
ATOM   2317  CA  THR A 291      -8.543  -1.902  15.473  1.00 21.94           C
ANISOU 2317  CA  THR A 291     3683   1975   2677   -269   1134    -63       C
ATOM   2318  C   THR A 291      -9.405  -1.953  16.733  1.00 20.93           C
ANISOU 2318  C   THR A 291     3615   1789   2548   -269   1205    -44       C
ATOM   2319  O   THR A 291     -10.619  -2.165  16.643  1.00 24.57           O
ANISOU 2319  O   THR A 291     4039   2252   3045   -309   1263    -76       O
ATOM   2320  CB  THR A 291      -7.892  -3.242  15.148  1.00 23.70           C
ANISOU 2320  CB  THR A 291     3926   2159   2920   -279   1154    -80       C
ATOM   2321  OG1 THR A 291      -7.254  -3.106  13.883  1.00 24.81           O
ANISOU 2321  OG1 THR A 291     3999   2365   3063   -282   1089   -102       O
ATOM   2322  CG2 THR A 291      -8.927  -4.371  15.039  1.00 20.81           C
ANISOU 2322  CG2 THR A 291     3542   1758   2607   -329   1240   -124       C
ATOM   2323  N   ASN A 292      -8.813  -1.710  17.908  1.00 23.00           N
ANISOU 2323  N   ASN A 292     3968   2001   2769   -223   1200      8       N
ATOM   2324  CA  ASN A 292      -9.619  -1.648  19.134  1.00 22.29           C
ANISOU 2324  CA  ASN A 292     3936   1860   2672   -217   1264     30       C
ATOM   2325  C   ASN A 292     -10.660  -0.540  19.056  1.00 27.88           C
ANISOU 2325  C   ASN A 292     4590   2621   3381   -229   1258     21       C
ATOM   2326  O   ASN A 292     -11.810  -0.713  19.484  1.00 22.07           O
ANISOU 2326  O   ASN A 292     3851   1865   2668   -254   1327      8       O
ATOM   2327  CB  ASN A 292      -8.735  -1.404  20.358  1.00 23.69           C
ANISOU 2327  CB  ASN A 292     4216   1985   2800   -158   1246     89       C
ATOM   2328  CG  ASN A 292      -7.693  -2.471  20.558  1.00 32.64           C
ANISOU 2328  CG  ASN A 292     5412   3062   3928   -142   1252    101       C
ATOM   2329  OD1 ASN A 292      -6.545  -2.298  20.161  1.00 30.14           O
ANISOU 2329  OD1 ASN A 292     5098   2764   3590   -116   1184    114       O
ATOM   2330  ND2 ASN A 292      -8.078  -3.577  21.207  1.00 29.41           N
ANISOU 2330  ND2 ASN A 292     5055   2580   3538   -155   1335    100       N
ATOM   2331  N   LEU A 293     -10.257   0.631  18.560  1.00 28.75           N
ANISOU 2331  N   LEU A 293     4658   2797   3466   -209   1176     31       N
ATOM   2332  CA  LEU A 293     -11.180   1.755  18.490  1.00 19.12           C
ANISOU 2332  CA  LEU A 293     3389   1630   2244   -216   1165     25       C
ATOM   2333  C   LEU A 293     -12.221   1.544  17.396  1.00 25.61           C
ANISOU 2333  C   LEU A 293     4113   2503   3115   -273   1191    -34       C
ATOM   2334  O   LEU A 293     -13.406   1.827  17.601  1.00 20.18           O
ANISOU 2334  O   LEU A 293     3400   1825   2444   -295   1234    -50       O
ATOM   2335  CB  LEU A 293     -10.395   3.051  18.257  1.00 18.52           C
ANISOU 2335  CB  LEU A 293     3299   1609   2130   -178   1068     53       C
ATOM   2336  CG  LEU A 293     -11.222   4.312  18.096  1.00 25.31           C
ANISOU 2336  CG  LEU A 293     4105   2529   2984   -181   1043     48       C
ATOM   2337  CD1 LEU A 293     -12.114   4.455  19.299  1.00 21.89           C
ANISOU 2337  CD1 LEU A 293     3724   2052   2542   -175   1103     65       C
ATOM   2338  CD2 LEU A 293     -10.324   5.534  17.953  1.00 24.57           C
ANISOU 2338  CD2 LEU A 293     4005   2478   2851   -140    947     81       C
ATOM   2339  N   ALA A 294     -11.802   1.001  16.241  1.00 22.03           N
ANISOU 2339  N   ALA A 294     3605   2081   2686   -295   1167    -68       N
ATOM   2340  CA  ALA A 294     -12.705   0.873  15.100  1.00 19.24           C
ANISOU 2340  CA  ALA A 294     3152   1783   2376   -344   1180   -126       C
ATOM   2341  C   ALA A 294     -13.889  -0.038  15.398  1.00 26.38           C
ANISOU 2341  C   ALA A 294     4055   2644   3325   -387   1276   -158       C
ATOM   2342  O   ALA A 294     -14.982   0.165  14.850  1.00 23.90           O
ANISOU 2342  O   ALA A 294     3669   2371   3042   -424   1298   -199       O
ATOM   2343  CB  ALA A 294     -11.938   0.343  13.877  1.00 19.07           C
ANISOU 2343  CB  ALA A 294     3081   1795   2369   -355   1139   -154       C
ATOM   2344  N   MET A 295     -13.702  -1.049  16.239  1.00 24.04           N
ANISOU 2344  N   MET A 295     3835   2266   3034   -384   1334   -142       N
ATOM   2345  CA  MET A 295     -14.800  -1.938  16.601  1.00 21.51           C
ANISOU 2345  CA  MET A 295     3518   1898   2758   -423   1429   -168       C
ATOM   2346  C   MET A 295     -15.087  -1.867  18.093  1.00 27.87           C
ANISOU 2346  C   MET A 295     4412   2637   3540   -399   1481   -122       C
ATOM   2347  O   MET A 295     -15.414  -2.871  18.737  1.00 24.72           O
ANISOU 2347  O   MET A 295     4060   2168   3164   -413   1557   -121       O
ATOM   2348  CB  MET A 295     -14.539  -3.375  16.147  1.00 26.30           C
ANISOU 2348  CB  MET A 295     4124   2464   3404   -451   1466   -198       C
ATOM   2349  CG  MET A 295     -13.092  -3.801  16.113  1.00 28.85           C
ANISOU 2349  CG  MET A 295     4497   2765   3701   -418   1422   -173       C
ATOM   2350  SD  MET A 295     -12.813  -5.425  15.343  1.00 29.61           S
ANISOU 2350  SD  MET A 295     4576   2828   3846   -454   1455   -218       S
ATOM   2351  CE  MET A 295     -12.763  -5.049  13.592  1.00 32.72           C
ANISOU 2351  CE  MET A 295     4850   3323   4258   -477   1386   -271       C
ATOM   2352  N   MET A 296     -15.027  -0.655  18.642  1.00 23.62           N
ANISOU 2352  N   MET A 296     3894   2123   2958   -363   1440    -86       N
ATOM   2353  CA  MET A 296     -15.216  -0.471  20.075  1.00 22.79           C
ANISOU 2353  CA  MET A 296     3875   1960   2823   -331   1481    -41       C
ATOM   2354  C   MET A 296     -16.582  -0.975  20.528  1.00 27.21           C
ANISOU 2354  C   MET A 296     4429   2488   3422   -368   1576    -60       C
ATOM   2355  O   MET A 296     -17.576  -0.870  19.804  1.00 30.44           O
ANISOU 2355  O   MET A 296     4756   2941   3869   -412   1594   -105       O
ATOM   2356  CB  MET A 296     -15.063   1.019  20.431  1.00 21.42           C
ANISOU 2356  CB  MET A 296     3707   1830   2602   -290   1416     -7       C
ATOM   2357  CG  MET A 296     -15.145   1.303  21.914  1.00 29.80           C
ANISOU 2357  CG  MET A 296     4861   2837   3627   -250   1447     42       C
ATOM   2358  SD  MET A 296     -15.140   3.087  22.170  1.00 34.90           S
ANISOU 2358  SD  MET A 296     5495   3540   4223   -209   1371     71       S
ATOM   2359  CE  MET A 296     -16.752   3.428  21.562  1.00 43.08           C
ANISOU 2359  CE  MET A 296     6437   4630   5300   -262   1410     22       C
ATOM   2360  N   ASN A 297     -16.623  -1.543  21.738  1.00 22.95           N
ANISOU 2360  N   ASN A 297     3978   1870   2872   -350   1639    -26       N
ATOM   2361  CA  ASN A 297     -17.874  -1.769  22.444  1.00 29.84           C
ANISOU 2361  CA  ASN A 297     4860   2710   3769   -372   1727    -29       C
ATOM   2362  C   ASN A 297     -17.988  -0.660  23.483  1.00 28.34           C
ANISOU 2362  C   ASN A 297     4719   2521   3526   -326   1711     17       C
ATOM   2363  O   ASN A 297     -17.327  -0.733  24.528  1.00 28.64           O
ANISOU 2363  O   ASN A 297     4851   2506   3524   -279   1715     65       O
ATOM   2364  CB  ASN A 297     -17.884  -3.149  23.112  1.00 29.17           C
ANISOU 2364  CB  ASN A 297     4839   2535   3707   -382   1811    -20       C
ATOM   2365  CG  ASN A 297     -19.202  -3.466  23.778  1.00 35.40           C
ANISOU 2365  CG  ASN A 297     5633   3289   4527   -409   1907    -25       C
ATOM   2366  OD1 ASN A 297     -20.256  -3.047  23.307  1.00 37.31           O
ANISOU 2366  OD1 ASN A 297     5801   3578   4798   -444   1920    -59       O
ATOM   2367  ND2 ASN A 297     -19.153  -4.221  24.878  1.00 33.76           N
ANISOU 2367  ND2 ASN A 297     5512   3000   4314   -393   1975     10       N
ATOM   2368  N   PRO A 298     -18.763   0.397  23.239  1.00 32.68           N
ANISOU 2368  N   PRO A 298     5212   3132   4072   -333   1689      4       N
ATOM   2369  CA  PRO A 298     -18.758   1.544  24.165  1.00 28.97           C
ANISOU 2369  CA  PRO A 298     4788   2669   3550   -284   1661     47       C
ATOM   2370  C   PRO A 298     -19.336   1.177  25.521  1.00 29.73           C
ANISOU 2370  C   PRO A 298     4962   2696   3637   -268   1744     79       C
ATOM   2371  O   PRO A 298     -20.320   0.443  25.616  1.00 28.44           O
ANISOU 2371  O   PRO A 298     4782   2506   3517   -308   1828     57       O
ATOM   2372  CB  PRO A 298     -19.636   2.584  23.458  1.00 26.49           C
ANISOU 2372  CB  PRO A 298     4383   2436   3246   -307   1631     16       C
ATOM   2373  CG  PRO A 298     -20.500   1.795  22.537  1.00 36.67           C
ANISOU 2373  CG  PRO A 298     5594   3740   4600   -372   1681    -42       C
ATOM   2374  CD  PRO A 298     -19.662   0.611  22.093  1.00 30.71           C
ANISOU 2374  CD  PRO A 298     4854   2949   3867   -384   1686    -52       C
ATOM   2375  N   THR A 299     -18.721   1.716  26.578  1.00 32.16           N
ANISOU 2375  N   THR A 299     5354   2977   3889   -208   1720    131       N
ATOM   2376  CA  THR A 299     -19.243   1.499  27.920  1.00 30.84           C
ANISOU 2376  CA  THR A 299     5264   2749   3706   -185   1794    166       C
ATOM   2377  C   THR A 299     -20.405   2.424  28.241  1.00 29.35           C
ANISOU 2377  C   THR A 299     5044   2596   3512   -188   1811    163       C
ATOM   2378  O   THR A 299     -21.229   2.078  29.086  1.00 27.93           O
ANISOU 2378  O   THR A 299     4885   2381   3345   -182   1868    164       O
ATOM   2379  CB  THR A 299     -18.143   1.677  28.975  1.00 28.87           C
ANISOU 2379  CB  THR A 299     5109   2461   3400   -111   1748    214       C
ATOM   2380  OG1 THR A 299     -17.544   2.977  28.847  1.00 27.55           O
ANISOU 2380  OG1 THR A 299     4942   2339   3185    -76   1665    237       O
ATOM   2381  CG2 THR A 299     -17.072   0.605  28.823  1.00 30.35           C
ANISOU 2381  CG2 THR A 299     5331   2607   3595   -105   1740    214       C
ATOM   2382  N   LEU A 300     -20.497   3.575  27.581  1.00 26.95           N
ANISOU 2382  N   LEU A 300     4676   2367   3196   -187   1739    147       N
ATOM   2383  CA  LEU A 300     -21.557   4.527  27.890  1.00 26.76           C
ANISOU 2383  CA  LEU A 300     4624   2379   3164   -186   1749    145       C
ATOM   2384  C   LEU A 300     -22.891   4.030  27.347  1.00 28.23           C
ANISOU 2384  C   LEU A 300     4736   2581   3410   -251   1821     98       C
ATOM   2385  O   LEU A 300     -22.986   3.709  26.156  1.00 27.24           O
ANISOU 2385  O   LEU A 300     4531   2491   3327   -297   1807     52       O
ATOM   2386  CB  LEU A 300     -21.229   5.894  27.284  1.00 28.07           C
ANISOU 2386  CB  LEU A 300     4741   2621   3302   -167   1648    141       C
ATOM   2387  CG  LEU A 300     -20.029   6.618  27.885  1.00 31.88           C
ANISOU 2387  CG  LEU A 300     5293   3096   3725   -100   1571    189       C
ATOM   2388  CD1 LEU A 300     -19.931   8.002  27.289  1.00 30.01           C
ANISOU 2388  CD1 LEU A 300     4999   2936   3468    -88   1480    182       C
ATOM   2389  CD2 LEU A 300     -20.169   6.699  29.395  1.00 38.79           C
ANISOU 2389  CD2 LEU A 300     6264   3913   4560    -52   1614    235       C
ATOM   2390  N   PRO A 301     -23.944   3.965  28.169  1.00 32.01           N
ANISOU 2390  N   PRO A 301     5231   3034   3896   -252   1890    104       N
ATOM   2391  CA  PRO A 301     -25.224   3.445  27.667  1.00 32.26           C
ANISOU 2391  CA  PRO A 301     5187   3079   3993   -311   1947     55       C
ATOM   2392  C   PRO A 301     -25.844   4.400  26.659  1.00 31.64           C
ANISOU 2392  C   PRO A 301     5013   3084   3923   -344   1917     19       C
ATOM   2393  O   PRO A 301     -25.727   5.621  26.778  1.00 27.31           O
ANISOU 2393  O   PRO A 301     4463   2581   3332   -310   1856     35       O
ATOM   2394  CB  PRO A 301     -26.086   3.310  28.934  1.00 32.86           C
ANISOU 2394  CB  PRO A 301     5305   3111   4069   -287   1998     75       C
ATOM   2395  CG  PRO A 301     -25.489   4.234  29.915  1.00 37.38           C
ANISOU 2395  CG  PRO A 301     5952   3679   4573   -219   1955    126       C
ATOM   2396  CD  PRO A 301     -24.012   4.356  29.586  1.00 37.66           C
ANISOU 2396  CD  PRO A 301     6024   3714   4571   -193   1893    148       C
ATOM   2397  N   GLY A 302     -26.498   3.827  25.650  1.00 32.18           N
ANISOU 2397  N   GLY A 302     4998   3177   4053   -404   1943    -36       N
ATOM   2398  CA  GLY A 302     -27.131   4.604  24.608  1.00 32.34           C
ANISOU 2398  CA  GLY A 302     4919   3279   4091   -435   1906    -80       C
ATOM   2399  C   GLY A 302     -26.234   4.976  23.448  1.00 32.16           C
ANISOU 2399  C   GLY A 302     4846   3312   4060   -435   1811   -100       C
ATOM   2400  O   GLY A 302     -26.716   5.598  22.492  1.00 33.97           O
ANISOU 2400  O   GLY A 302     4989   3613   4306   -459   1774   -139       O
ATOM   2401  N   TRP A 303     -24.947   4.636  23.508  1.00 29.51           N
ANISOU 2401  N   TRP A 303     4564   2948   3702   -406   1772    -73       N
ATOM   2402  CA  TRP A 303     -23.987   4.925  22.446  1.00 26.13           C
ANISOU 2402  CA  TRP A 303     4095   2568   3266   -403   1684    -87       C
ATOM   2403  C   TRP A 303     -23.720   3.673  21.636  1.00 26.44           C
ANISOU 2403  C   TRP A 303     4105   2588   3353   -443   1708   -122       C
ATOM   2404  O   TRP A 303     -23.658   2.573  22.189  1.00 25.81           O
ANISOU 2404  O   TRP A 303     4077   2437   3291   -451   1774   -113       O
ATOM   2405  CB  TRP A 303     -22.682   5.444  23.040  1.00 21.53           C
ANISOU 2405  CB  TRP A 303     3588   1968   2623   -341   1618    -33       C
ATOM   2406  CG  TRP A 303     -22.836   6.851  23.577  1.00 22.48           C
ANISOU 2406  CG  TRP A 303     3721   2123   2697   -300   1571     -5       C
ATOM   2407  CD1 TRP A 303     -23.341   7.222  24.786  1.00 27.94           C
ANISOU 2407  CD1 TRP A 303     4471   2784   3361   -271   1609     28       C
ATOM   2408  CD2 TRP A 303     -22.483   8.053  22.892  1.00 27.07           C
ANISOU 2408  CD2 TRP A 303     4253   2777   3254   -284   1478     -8       C
ATOM   2409  NE1 TRP A 303     -23.324   8.607  24.902  1.00 22.42           N
ANISOU 2409  NE1 TRP A 303     3763   2134   2623   -237   1542     45       N
ATOM   2410  CE2 TRP A 303     -22.794   9.131  23.748  1.00 24.68           C
ANISOU 2410  CE2 TRP A 303     3982   2483   2911   -246   1461     24       C
ATOM   2411  CE3 TRP A 303     -21.926   8.322  21.638  1.00 26.57           C
ANISOU 2411  CE3 TRP A 303     4122   2774   3201   -298   1407    -33       C
ATOM   2412  CZ2 TRP A 303     -22.570  10.461  23.384  1.00 24.90           C
ANISOU 2412  CZ2 TRP A 303     3976   2575   2910   -222   1376     30       C
ATOM   2413  CZ3 TRP A 303     -21.701   9.643  21.276  1.00 26.86           C
ANISOU 2413  CZ3 TRP A 303     4124   2874   3208   -274   1324    -25       C
ATOM   2414  CH2 TRP A 303     -22.030  10.699  22.157  1.00 25.80           C
ANISOU 2414  CH2 TRP A 303     4024   2745   3036   -237   1309      6       C
ATOM   2415  N   LYS A 304     -23.535   3.840  20.326  1.00 23.92           N
ANISOU 2415  N   LYS A 304     3705   2332   3053   -467   1653   -163       N
ATOM   2416  CA  LYS A 304     -23.268   2.706  19.454  1.00 22.94           C
ANISOU 2416  CA  LYS A 304     3546   2198   2974   -504   1668   -201       C
ATOM   2417  C   LYS A 304     -22.120   3.057  18.527  1.00 27.77           C
ANISOU 2417  C   LYS A 304     4131   2855   3564   -487   1575   -202       C
ATOM   2418  O   LYS A 304     -22.069   4.163  17.986  1.00 25.27           O
ANISOU 2418  O   LYS A 304     3768   2609   3226   -475   1507   -206       O
ATOM   2419  CB  LYS A 304     -24.517   2.342  18.638  1.00 26.22           C
ANISOU 2419  CB  LYS A 304     3869   2643   3449   -564   1714   -264       C
ATOM   2420  CG  LYS A 304     -24.329   1.220  17.627  1.00 31.31           C
ANISOU 2420  CG  LYS A 304     4468   3285   4144   -605   1725   -311       C
ATOM   2421  CD  LYS A 304     -24.543  -0.142  18.244  1.00 49.20           C
ANISOU 2421  CD  LYS A 304     6782   5465   6447   -626   1815   -310       C
ATOM   2422  CE  LYS A 304     -24.584  -1.228  17.165  1.00 58.69           C
ANISOU 2422  CE  LYS A 304     7925   6669   7707   -673   1830   -366       C
ATOM   2423  NZ  LYS A 304     -25.760  -1.086  16.250  1.00 59.18           N
ANISOU 2423  NZ  LYS A 304     7883   6786   7817   -721   1843   -429       N
ATOM   2424  N   VAL A 305     -21.196   2.123  18.343  1.00 30.47           N
ANISOU 2424  N   VAL A 305     4503   3160   3912   -485   1573   -199       N
ATOM   2425  CA  VAL A 305     -20.107   2.296  17.390  1.00 27.38           C
ANISOU 2425  CA  VAL A 305     4083   2811   3507   -473   1491   -204       C
ATOM   2426  C   VAL A 305     -20.218   1.201  16.350  1.00 30.26           C
ANISOU 2426  C   VAL A 305     4391   3180   3925   -519   1513   -258       C
ATOM   2427  O   VAL A 305     -20.431   0.031  16.691  1.00 25.96           O
ANISOU 2427  O   VAL A 305     3877   2572   3414   -541   1584   -267       O
ATOM   2428  CB  VAL A 305     -18.736   2.278  18.082  1.00 31.43           C
ANISOU 2428  CB  VAL A 305     4686   3282   3973   -421   1453   -149       C
ATOM   2429  CG1 VAL A 305     -17.593   2.113  17.049  1.00 26.63           C
ANISOU 2429  CG1 VAL A 305     4050   2708   3362   -415   1383   -159       C
ATOM   2430  CG2 VAL A 305     -18.571   3.565  18.826  1.00 30.03           C
ANISOU 2430  CG2 VAL A 305     4545   3121   3743   -375   1409   -104       C
ATOM   2431  N   GLU A 306     -20.117   1.585  15.087  1.00 27.76           N
ANISOU 2431  N   GLU A 306     3991   2938   3618   -532   1455   -294       N
ATOM   2432  CA  GLU A 306     -20.098   0.629  13.996  1.00 27.64           C
ANISOU 2432  CA  GLU A 306     3917   2935   3648   -570   1463   -346       C
ATOM   2433  C   GLU A 306     -18.820   0.826  13.197  1.00 24.51           C
ANISOU 2433  C   GLU A 306     3509   2577   3226   -545   1380   -338       C
ATOM   2434  O   GLU A 306     -18.298   1.930  13.108  1.00 22.66           O
ANISOU 2434  O   GLU A 306     3271   2389   2950   -511   1310   -310       O
ATOM   2435  CB  GLU A 306     -21.334   0.788  13.114  1.00 31.32           C
ANISOU 2435  CB  GLU A 306     4285   3458   4158   -615   1480   -406       C
ATOM   2436  CG  GLU A 306     -22.625   0.488  13.879  1.00 33.74           C
ANISOU 2436  CG  GLU A 306     4600   3724   4496   -644   1569   -417       C
ATOM   2437  CD  GLU A 306     -23.855   0.983  13.161  1.00 36.70           C
ANISOU 2437  CD  GLU A 306     4880   4161   4902   -679   1576   -468       C
ATOM   2438  OE1 GLU A 306     -24.092   2.208  13.152  1.00 37.98           O
ANISOU 2438  OE1 GLU A 306     5020   4377   5033   -660   1533   -455       O
ATOM   2439  OE2 GLU A 306     -24.589   0.146  12.604  1.00 40.72           O
ANISOU 2439  OE2 GLU A 306     5337   4665   5467   -725   1623   -521       O
ATOM   2440  N   CYS A 307     -18.306  -0.260  12.637  1.00 23.05           N
ANISOU 2440  N   CYS A 307     3318   2372   3067   -561   1388   -362       N
ATOM   2441  CA  CYS A 307     -17.002  -0.248  11.985  1.00 27.87           C
ANISOU 2441  CA  CYS A 307     3928   3007   3653   -535   1316   -351       C
ATOM   2442  C   CYS A 307     -17.172  -0.184  10.470  1.00 28.20           C
ANISOU 2442  C   CYS A 307     3866   3127   3720   -560   1277   -406       C
ATOM   2443  O   CYS A 307     -17.826  -1.051   9.881  1.00 24.82           O
ANISOU 2443  O   CYS A 307     3391   2696   3342   -602   1320   -459       O
ATOM   2444  CB  CYS A 307     -16.206  -1.492  12.386  1.00 28.34           C
ANISOU 2444  CB  CYS A 307     4056   2992   3720   -530   1346   -338       C
ATOM   2445  SG  CYS A 307     -14.566  -1.604  11.634  1.00 28.78           S
ANISOU 2445  SG  CYS A 307     4117   3073   3747   -498   1264   -324       S
ATOM   2446  N   VAL A 308     -16.596   0.844   9.845  1.00 23.33           N
ANISOU 2446  N   VAL A 308     3213   2580   3070   -534   1195   -393       N
ATOM   2447  CA  VAL A 308     -16.454   0.868   8.380  1.00 24.04           C
ANISOU 2447  CA  VAL A 308     3214   2744   3175   -548   1148   -437       C
ATOM   2448  C   VAL A 308     -15.146   0.221   7.943  1.00 27.77           C
ANISOU 2448  C   VAL A 308     3707   3206   3637   -529   1111   -428       C
ATOM   2449  O   VAL A 308     -15.120  -0.584   7.011  1.00 28.27           O
ANISOU 2449  O   VAL A 308     3724   3286   3732   -552   1115   -474       O
ATOM   2450  CB  VAL A 308     -16.546   2.309   7.835  1.00 21.99           C
ANISOU 2450  CB  VAL A 308     2898   2570   2888   -530   1080   -430       C
ATOM   2451  CG1 VAL A 308     -16.138   2.339   6.349  1.00 21.79           C
ANISOU 2451  CG1 VAL A 308     2790   2619   2868   -534   1023   -466       C
ATOM   2452  CG2 VAL A 308     -17.935   2.903   8.046  1.00 25.34           C
ANISOU 2452  CG2 VAL A 308     3286   3015   3328   -554   1115   -451       C
ATOM   2453  N   GLY A 309     -14.038   0.587   8.588  1.00 23.87           N
ANISOU 2453  N   GLY A 309     3283   2689   3098   -486   1072   -370       N
ATOM   2454  CA  GLY A 309     -12.747  -0.025   8.311  1.00 22.59           C
ANISOU 2454  CA  GLY A 309     3150   2511   2923   -465   1039   -355       C
ATOM   2455  C   GLY A 309     -11.847   0.166   9.509  1.00 25.94           C
ANISOU 2455  C   GLY A 309     3673   2876   3306   -422   1028   -290       C
ATOM   2456  O   GLY A 309     -12.117   1.001  10.380  1.00 22.25           O
ANISOU 2456  O   GLY A 309     3242   2399   2814   -404   1029   -255       O
ATOM   2457  N   ASP A 310     -10.774  -0.616   9.569  1.00 24.35           N
ANISOU 2457  N   ASP A 310     3519   2637   3097   -406   1019   -275       N
ATOM   2458  CA  ASP A 310      -9.914  -0.528  10.739  1.00 25.52           C
ANISOU 2458  CA  ASP A 310     3765   2725   3206   -365   1012   -216       C
ATOM   2459  C   ASP A 310      -8.481  -0.114  10.451  1.00 22.09           C
ANISOU 2459  C   ASP A 310     3345   2314   2734   -323    932   -181       C
ATOM   2460  O   ASP A 310      -7.673  -0.069  11.391  1.00 24.99           O
ANISOU 2460  O   ASP A 310     3794   2631   3070   -286    922   -133       O
ATOM   2461  CB  ASP A 310      -9.921  -1.853  11.513  1.00 21.76           C
ANISOU 2461  CB  ASP A 310     3361   2158   2749   -375   1085   -216       C
ATOM   2462  CG  ASP A 310      -9.038  -2.908  10.892  1.00 26.54           C
ANISOU 2462  CG  ASP A 310     3968   2749   3366   -377   1075   -233       C
ATOM   2463  OD1 ASP A 310      -8.850  -2.910   9.653  1.00 26.50           O
ANISOU 2463  OD1 ASP A 310     3888   2808   3374   -389   1035   -267       O
ATOM   2464  OD2 ASP A 310      -8.533  -3.738  11.666  1.00 26.35           O
ANISOU 2464  OD2 ASP A 310     4022   2651   3337   -365   1108   -211       O
ATOM   2465  N   ASP A 311      -8.137   0.218   9.208  1.00 21.77           N
ANISOU 2465  N   ASP A 311     3228   2348   2695   -325    875   -202       N
ATOM   2466  CA  ASP A 311      -6.717   0.385   8.895  1.00 20.35           C
ANISOU 2466  CA  ASP A 311     3063   2185   2486   -289    807   -171       C
ATOM   2467  C   ASP A 311      -6.410   1.382   7.781  1.00 22.04           C
ANISOU 2467  C   ASP A 311     3196   2491   2688   -279    731   -174       C
ATOM   2468  O   ASP A 311      -5.403   2.086   7.861  1.00 25.53           O
ANISOU 2468  O   ASP A 311     3656   2949   3095   -241    668   -131       O
ATOM   2469  CB  ASP A 311      -6.105  -0.973   8.519  1.00 19.02           C
ANISOU 2469  CB  ASP A 311     2909   1982   2335   -297    826   -193       C
ATOM   2470  CG  ASP A 311      -4.586  -0.929   8.391  1.00 21.61           C
ANISOU 2470  CG  ASP A 311     3267   2313   2631   -257    763   -157       C
ATOM   2471  OD1 ASP A 311      -3.879  -0.714   9.395  1.00 18.62           O
ANISOU 2471  OD1 ASP A 311     2967   1886   2221   -222    751   -107       O
ATOM   2472  OD2 ASP A 311      -4.087  -1.165   7.274  1.00 21.57           O
ANISOU 2472  OD2 ASP A 311     3206   2356   2632   -260    727   -180       O
ATOM   2473  N   ILE A 312      -7.215   1.416   6.719  1.00 17.29           N
ANISOU 2473  N   ILE A 312     2505   1950   2113   -312    735   -224       N
ATOM   2474  CA  ILE A 312      -6.931   2.255   5.559  1.00 18.44           C
ANISOU 2474  CA  ILE A 312     2570   2186   2249   -303    667   -231       C
ATOM   2475  C   ILE A 312      -8.208   2.964   5.140  1.00 21.70           C
ANISOU 2475  C   ILE A 312     2913   2653   2679   -329    677   -262       C
ATOM   2476  O   ILE A 312      -9.279   2.351   5.080  1.00 20.85           O
ANISOU 2476  O   ILE A 312     2784   2532   2607   -367    738   -308       O
ATOM   2477  CB  ILE A 312      -6.368   1.438   4.372  1.00 24.63           C
ANISOU 2477  CB  ILE A 312     3307   3002   3049   -311    649   -265       C
ATOM   2478  CG1 ILE A 312      -5.122   0.656   4.803  1.00 21.05           C
ANISOU 2478  CG1 ILE A 312     2925   2492   2580   -286    642   -236       C
ATOM   2479  CG2 ILE A 312      -6.041   2.380   3.175  1.00 22.02           C
ANISOU 2479  CG2 ILE A 312     2893   2768   2705   -298    576   -267       C
ATOM   2480  CD1 ILE A 312      -4.626  -0.344   3.778  1.00 27.84           C
ANISOU 2480  CD1 ILE A 312     3749   3370   3458   -295    636   -273       C
ATOM   2481  N   ALA A 313      -8.089   4.253   4.834  1.00 18.96           N
ANISOU 2481  N   ALA A 313     2529   2367   2308   -309    618   -239       N
ATOM   2482  CA  ALA A 313      -9.201   5.066   4.375  1.00 19.71           C
ANISOU 2482  CA  ALA A 313     2554   2521   2414   -329    618   -266       C
ATOM   2483  C   ALA A 313      -8.811   5.791   3.095  1.00 18.51           C
ANISOU 2483  C   ALA A 313     2321   2460   2253   -318    549   -272       C
ATOM   2484  O   ALA A 313      -7.709   6.323   2.987  1.00 21.01           O
ANISOU 2484  O   ALA A 313     2649   2795   2541   -283    488   -230       O
ATOM   2485  CB  ALA A 313      -9.614   6.113   5.434  1.00 16.03           C
ANISOU 2485  CB  ALA A 313     2127   2037   1926   -314    617   -227       C
ATOM   2486  N   TRP A 314      -9.725   5.820   2.136  1.00 19.57           N
ANISOU 2486  N   TRP A 314     2372   2653   2411   -346    559   -324       N
ATOM   2487  CA  TRP A 314      -9.587   6.646   0.945  1.00 23.90           C
ANISOU 2487  CA  TRP A 314     2837   3293   2950   -336    498   -332       C
ATOM   2488  C   TRP A 314     -10.655   7.720   1.031  1.00 21.73           C
ANISOU 2488  C   TRP A 314     2526   3056   2675   -345    498   -337       C
ATOM   2489  O   TRP A 314     -11.841   7.402   1.160  1.00 24.82           O
ANISOU 2489  O   TRP A 314     2900   3438   3093   -378    553   -379       O
ATOM   2490  CB  TRP A 314      -9.760   5.820  -0.329  1.00 22.08           C
ANISOU 2490  CB  TRP A 314     2537   3106   2747   -358    506   -391       C
ATOM   2491  CG  TRP A 314      -8.609   4.895  -0.656  1.00 21.16           C
ANISOU 2491  CG  TRP A 314     2443   2970   2627   -345    492   -386       C
ATOM   2492  CD1 TRP A 314      -7.439   4.738   0.037  1.00 21.60           C
ANISOU 2492  CD1 TRP A 314     2573   2976   2660   -316    473   -335       C
ATOM   2493  CD2 TRP A 314      -8.534   4.006  -1.775  1.00 18.26           C
ANISOU 2493  CD2 TRP A 314     2022   2634   2281   -358    494   -436       C
ATOM   2494  NE1 TRP A 314      -6.638   3.790  -0.594  1.00 17.44           N
ANISOU 2494  NE1 TRP A 314     2040   2448   2137   -311    464   -350       N
ATOM   2495  CE2 TRP A 314      -7.291   3.343  -1.710  1.00 17.69           C
ANISOU 2495  CE2 TRP A 314     1994   2530   2196   -337    477   -412       C
ATOM   2496  CE3 TRP A 314      -9.395   3.714  -2.834  1.00 21.38           C
ANISOU 2496  CE3 TRP A 314     2336   3083   2706   -385    508   -501       C
ATOM   2497  CZ2 TRP A 314      -6.896   2.394  -2.660  1.00 22.43           C
ANISOU 2497  CZ2 TRP A 314     2561   3149   2811   -341    474   -450       C
ATOM   2498  CZ3 TRP A 314      -8.995   2.770  -3.783  1.00 19.65           C
ANISOU 2498  CZ3 TRP A 314     2082   2883   2501   -389    504   -539       C
ATOM   2499  CH2 TRP A 314      -7.756   2.134  -3.691  1.00 21.21           C
ANISOU 2499  CH2 TRP A 314     2327   3048   2685   -367    487   -513       C
ATOM   2500  N   MET A 315     -10.246   8.985   0.968  1.00 21.03           N
ANISOU 2500  N   MET A 315     2424   3010   2556   -316    437   -296       N
ATOM   2501  CA  MET A 315     -11.166  10.068   1.277  1.00 23.39           C
ANISOU 2501  CA  MET A 315     2704   3334   2849   -320    435   -291       C
ATOM   2502  C   MET A 315     -11.063  11.165   0.230  1.00 23.77           C
ANISOU 2502  C   MET A 315     2674   3473   2883   -305    370   -288       C
ATOM   2503  O   MET A 315      -9.967  11.495  -0.230  1.00 24.38           O
ANISOU 2503  O   MET A 315     2745   3579   2941   -277    313   -255       O
ATOM   2504  CB  MET A 315     -10.883  10.654   2.658  1.00 26.37           C
ANISOU 2504  CB  MET A 315     3164   3653   3201   -295    432   -235       C
ATOM   2505  CG  MET A 315     -10.827   9.624   3.779  1.00 32.55           C
ANISOU 2505  CG  MET A 315     4033   4343   3992   -302    491   -228       C
ATOM   2506  SD  MET A 315     -10.654  10.366   5.416  1.00 27.53           S
ANISOU 2506  SD  MET A 315     3492   3644   3326   -272    490   -167       S
ATOM   2507  CE  MET A 315      -9.220  11.413   5.181  1.00 31.20           C
ANISOU 2507  CE  MET A 315     3960   4143   3754   -224    393   -108       C
ATOM   2508  N   LYS A 316     -12.211  11.741  -0.119  1.00 27.78           N
ANISOU 2508  N   LYS A 316     3126   4028   3403   -324    381   -320       N
ATOM   2509  CA  LYS A 316     -12.277  12.779  -1.136  1.00 34.66           C
ANISOU 2509  CA  LYS A 316     3919   4987   4262   -312    325   -321       C
ATOM   2510  C   LYS A 316     -13.411  13.735  -0.803  1.00 35.52           C
ANISOU 2510  C   LYS A 316     4009   5117   4371   -322    334   -327       C
ATOM   2511  O   LYS A 316     -14.524  13.290  -0.513  1.00 29.77           O
ANISOU 2511  O   LYS A 316     3276   4368   3666   -353    393   -368       O
ATOM   2512  CB  LYS A 316     -12.498  12.159  -2.521  1.00 39.30           C
ANISOU 2512  CB  LYS A 316     4427   5634   4871   -330    327   -378       C
ATOM   2513  CG  LYS A 316     -12.593  13.159  -3.663  1.00 44.71           C
ANISOU 2513  CG  LYS A 316     5028   6415   5545   -317    272   -383       C
ATOM   2514  CD  LYS A 316     -13.015  12.462  -4.956  1.00 52.04           C
ANISOU 2514  CD  LYS A 316     5878   7397   6496   -337    284   -448       C
ATOM   2515  CE  LYS A 316     -14.435  11.912  -4.846  1.00 57.88           C
ANISOU 2515  CE  LYS A 316     6598   8124   7270   -378    349   -510       C
ATOM   2516  NZ  LYS A 316     -14.819  11.057  -6.006  1.00 62.91           N
ANISOU 2516  NZ  LYS A 316     7168   8802   7934   -397    365   -577       N
ATOM   2517  N   PHE A 317     -13.133  15.038  -0.844  1.00 33.01           N
ANISOU 2517  N   PHE A 317     3677   4839   4027   -295    276   -287       N
ATOM   2518  CA  PHE A 317     -14.212  16.017  -0.783  1.00 34.01           C
ANISOU 2518  CA  PHE A 317     3769   5002   4153   -302    276   -298       C
ATOM   2519  C   PHE A 317     -15.069  15.898  -2.041  1.00 39.07           C
ANISOU 2519  C   PHE A 317     4315   5715   4814   -326    284   -360       C
ATOM   2520  O   PHE A 317     -14.545  15.905  -3.157  1.00 45.79           O
ANISOU 2520  O   PHE A 317     5112   6623   5662   -316    246   -368       O
ATOM   2521  CB  PHE A 317     -13.647  17.434  -0.639  1.00 31.87           C
ANISOU 2521  CB  PHE A 317     3500   4759   3851   -266    207   -241       C
ATOM   2522  CG  PHE A 317     -13.110  17.732   0.737  1.00 33.67           C
ANISOU 2522  CG  PHE A 317     3819   4916   4059   -244    202   -185       C
ATOM   2523  CD1 PHE A 317     -11.747  17.683   0.994  1.00 34.92           C
ANISOU 2523  CD1 PHE A 317     4023   5044   4199   -214    163   -136       C
ATOM   2524  CD2 PHE A 317     -13.976  18.029   1.786  1.00 32.86           C
ANISOU 2524  CD2 PHE A 317     3755   4774   3955   -251    238   -184       C
ATOM   2525  CE1 PHE A 317     -11.260  17.942   2.274  1.00 39.66           C
ANISOU 2525  CE1 PHE A 317     4707   5579   4782   -191    158    -88       C
ATOM   2526  CE2 PHE A 317     -13.501  18.291   3.065  1.00 30.15           C
ANISOU 2526  CE2 PHE A 317     3496   4366   3593   -228    234   -135       C
ATOM   2527  CZ  PHE A 317     -12.140  18.250   3.312  1.00 34.00           C
ANISOU 2527  CZ  PHE A 317     4030   4825   4064   -197    193    -88       C
ATOM   2528  N   ASP A 318     -16.381  15.738  -1.866  1.00 36.60           N
ANISOU 2528  N   ASP A 318     3984   5400   4523   -357    336   -405       N
ATOM   2529  CA  ASP A 318     -17.279  15.678  -3.010  1.00 32.57           C
ANISOU 2529  CA  ASP A 318     3384   4958   4033   -379    344   -466       C
ATOM   2530  C   ASP A 318     -17.721  17.099  -3.379  1.00 32.88           C
ANISOU 2530  C   ASP A 318     3373   5066   4053   -364    298   -455       C
ATOM   2531  O   ASP A 318     -17.301  18.084  -2.767  1.00 31.27           O
ANISOU 2531  O   ASP A 318     3204   4854   3823   -338    261   -400       O
ATOM   2532  CB  ASP A 318     -18.453  14.731  -2.728  1.00 30.34           C
ANISOU 2532  CB  ASP A 318     3099   4641   3787   -420    421   -524       C
ATOM   2533  CG  ASP A 318     -19.454  15.289  -1.718  1.00 35.27           C
ANISOU 2533  CG  ASP A 318     3752   5238   4412   -431    454   -519       C
ATOM   2534  OD1 ASP A 318     -20.507  14.648  -1.501  1.00 35.37           O
ANISOU 2534  OD1 ASP A 318     3756   5227   4456   -465    517   -566       O
ATOM   2535  OD2 ASP A 318     -19.209  16.366  -1.145  1.00 34.21           O
ANISOU 2535  OD2 ASP A 318     3646   5105   4249   -405    419   -470       O
ATOM   2536  N   ALA A 319     -18.578  17.216  -4.395  1.00 36.79           N
ANISOU 2536  N   ALA A 319     3787   5629   4563   -380    301   -508       N
ATOM   2537  CA  ALA A 319     -18.968  18.540  -4.877  1.00 36.89           C
ANISOU 2537  CA  ALA A 319     3750   5708   4558   -364    254   -498       C
ATOM   2538  C   ALA A 319     -19.775  19.327  -3.850  1.00 40.38           C
ANISOU 2538  C   ALA A 319     4219   6129   4993   -368    272   -484       C
ATOM   2539  O   ALA A 319     -19.834  20.559  -3.940  1.00 45.53           O
ANISOU 2539  O   ALA A 319     4854   6822   5625   -347    226   -456       O
ATOM   2540  CB  ALA A 319     -19.763  18.412  -6.176  1.00 38.68           C
ANISOU 2540  CB  ALA A 319     3957   5945   4793   -357    237   -538       C
ATOM   2541  N   GLN A 320     -20.398  18.652  -2.882  1.00 29.87           N
ANISOU 2541  N   GLN A 320     2937   4732   3681   -392    335   -500       N
ATOM   2542  CA  GLN A 320     -21.101  19.327  -1.796  1.00 26.23           C
ANISOU 2542  CA  GLN A 320     2515   4240   3212   -393    354   -481       C
ATOM   2543  C   GLN A 320     -20.173  19.778  -0.680  1.00 26.88           C
ANISOU 2543  C   GLN A 320     2681   4266   3267   -363    329   -410       C
ATOM   2544  O   GLN A 320     -20.643  20.407   0.275  1.00 35.17           O
ANISOU 2544  O   GLN A 320     3769   5289   4305   -357    339   -389       O
ATOM   2545  CB  GLN A 320     -22.176  18.408  -1.205  1.00 31.36           C
ANISOU 2545  CB  GLN A 320     3181   4841   3894   -431    436   -527       C
ATOM   2546  CG  GLN A 320     -22.942  17.601  -2.236  1.00 40.02           C
ANISOU 2546  CG  GLN A 320     4204   5975   5025   -464    469   -601       C
ATOM   2547  CD  GLN A 320     -23.699  18.475  -3.211  1.00 46.02           C
ANISOU 2547  CD  GLN A 320     4923   6785   5779   -447    417   -615       C
ATOM   2548  OE1 GLN A 320     -24.276  19.492  -2.830  1.00 45.90           O
ANISOU 2548  OE1 GLN A 320     4909   6782   5749   -438    404   -600       O
ATOM   2549  NE2 GLN A 320     -23.696  18.085  -4.483  1.00 50.22           N
ANISOU 2549  NE2 GLN A 320     5431   7335   6317   -438    386   -641       N
ATOM   2550  N   GLY A 321     -18.882  19.458  -0.759  1.00 32.13           N
ANISOU 2550  N   GLY A 321     3377   4911   3920   -342    298   -374       N
ATOM   2551  CA  GLY A 321     -17.928  19.835   0.263  1.00 33.15           C
ANISOU 2551  CA  GLY A 321     3586   4987   4024   -312    272   -308       C
ATOM   2552  C   GLY A 321     -17.784  18.856   1.411  1.00 32.17           C
ANISOU 2552  C   GLY A 321     3545   4771   3906   -320    327   -299       C
ATOM   2553  O   GLY A 321     -17.024  19.133   2.349  1.00 32.75           O
ANISOU 2553  O   GLY A 321     3690   4795   3959   -293    308   -246       O
ATOM   2554  N   ASN A 322     -18.487  17.727   1.376  1.00 28.19           N
ANISOU 2554  N   ASN A 322     3035   4243   3433   -355    394   -350       N
ATOM   2555  CA  ASN A 322     -18.341  16.719   2.415  1.00 30.15           C
ANISOU 2555  CA  ASN A 322     3361   4403   3690   -363    449   -342       C
ATOM   2556  C   ASN A 322     -17.114  15.861   2.138  1.00 25.04           C
ANISOU 2556  C   ASN A 322     2740   3732   3043   -354    436   -328       C
ATOM   2557  O   ASN A 322     -16.833  15.510   0.987  1.00 25.86           O
ANISOU 2557  O   ASN A 322     2786   3883   3157   -360    416   -355       O
ATOM   2558  CB  ASN A 322     -19.600  15.853   2.487  1.00 25.79           C
ANISOU 2558  CB  ASN A 322     2792   3833   3174   -406    528   -400       C
ATOM   2559  CG  ASN A 322     -20.855  16.679   2.705  1.00 26.90           C
ANISOU 2559  CG  ASN A 322     2903   4002   3317   -417    543   -418       C
ATOM   2560  OD1 ASN A 322     -21.709  16.787   1.819  1.00 30.52           O
ANISOU 2560  OD1 ASN A 322     3284   4519   3794   -439    548   -468       O
ATOM   2561  ND2 ASN A 322     -20.970  17.272   3.885  1.00 26.19           N
ANISOU 2561  ND2 ASN A 322     2874   3871   3206   -399    548   -378       N
ATOM   2562  N   LEU A 323     -16.361  15.550   3.193  1.00 27.03           N
ANISOU 2562  N   LEU A 323     3078   3911   3280   -335    443   -284       N
ATOM   2563  CA  LEU A 323     -15.217  14.648   3.071  1.00 25.94           C
ANISOU 2563  CA  LEU A 323     2974   3741   3143   -326    437   -270       C
ATOM   2564  C   LEU A 323     -15.743  13.219   3.134  1.00 26.00           C
ANISOU 2564  C   LEU A 323     2990   3704   3183   -362    512   -317       C
ATOM   2565  O   LEU A 323     -16.059  12.704   4.210  1.00 28.43           O
ANISOU 2565  O   LEU A 323     3363   3942   3497   -370    566   -310       O
ATOM   2566  CB  LEU A 323     -14.187  14.916   4.163  1.00 23.44           C
ANISOU 2566  CB  LEU A 323     2744   3365   2796   -290    412   -206       C
ATOM   2567  CG  LEU A 323     -12.920  14.045   4.123  1.00 25.15           C
ANISOU 2567  CG  LEU A 323     3001   3545   3009   -276    401   -186       C
ATOM   2568  CD1 LEU A 323     -12.108  14.192   2.819  1.00 23.79           C
ANISOU 2568  CD1 LEU A 323     2767   3439   2834   -266    342   -189       C
ATOM   2569  CD2 LEU A 323     -12.051  14.352   5.339  1.00 23.18           C
ANISOU 2569  CD2 LEU A 323     2843   3234   2731   -240    381   -125       C
ATOM   2570  N   ARG A 324     -15.854  12.582   1.971  1.00 23.78           N
ANISOU 2570  N   ARG A 324     2645   3465   2927   -383    516   -365       N
ATOM   2571  CA  ARG A 324     -16.420  11.243   1.860  1.00 33.42           C
ANISOU 2571  CA  ARG A 324     3861   4652   4186   -420    583   -417       C
ATOM   2572  C   ARG A 324     -15.313  10.194   1.889  1.00 33.67           C
ANISOU 2572  C   ARG A 324     3938   4639   4218   -412    586   -404       C
ATOM   2573  O   ARG A 324     -14.337  10.290   1.139  1.00 26.28           O
ANISOU 2573  O   ARG A 324     2980   3738   3268   -391    532   -391       O
ATOM   2574  CB  ARG A 324     -17.230  11.121   0.568  1.00 38.04           C
ANISOU 2574  CB  ARG A 324     4347   5308   4797   -447    586   -481       C
ATOM   2575  CG  ARG A 324     -18.463  12.013   0.520  1.00 38.91           C
ANISOU 2575  CG  ARG A 324     4411   5462   4912   -460    594   -503       C
ATOM   2576  CD  ARG A 324     -19.698  11.204   0.845  1.00 40.33           C
ANISOU 2576  CD  ARG A 324     4586   5606   5131   -501    673   -553       C
ATOM   2577  NE  ARG A 324     -20.813  12.025   1.299  1.00 38.81           N
ANISOU 2577  NE  ARG A 324     4380   5428   4938   -510    691   -559       N
ATOM   2578  CZ  ARG A 324     -21.906  11.519   1.855  1.00 41.87           C
ANISOU 2578  CZ  ARG A 324     4775   5777   5355   -542    761   -590       C
ATOM   2579  NH1 ARG A 324     -21.999  10.202   2.016  1.00 38.37           N
ANISOU 2579  NH1 ARG A 324     4353   5280   4945   -568    819   -617       N
ATOM   2580  NH2 ARG A 324     -22.891  12.318   2.262  1.00 45.78           N
ANISOU 2580  NH2 ARG A 324     5258   6289   5848   -547    774   -593       N
ATOM   2581  N   ALA A 325     -15.473   9.182   2.739  1.00 28.72           N
ANISOU 2581  N   ALA A 325     3371   3932   3608   -428    649   -409       N
ATOM   2582  CA  ALA A 325     -14.450   8.165   2.931  1.00 23.77           C
ANISOU 2582  CA  ALA A 325     2797   3252   2981   -419    656   -394       C
ATOM   2583  C   ALA A 325     -14.989   6.784   2.594  1.00 20.52           C
ANISOU 2583  C   ALA A 325     2368   2814   2613   -458    718   -451       C
ATOM   2584  O   ALA A 325     -16.148   6.476   2.875  1.00 23.30           O
ANISOU 2584  O   ALA A 325     2710   3148   2994   -490    777   -486       O
ATOM   2585  CB  ALA A 325     -13.941   8.157   4.370  1.00 20.20           C
ANISOU 2585  CB  ALA A 325     2447   2720   2506   -396    671   -339       C
ATOM   2586  N   ILE A 326     -14.137   5.945   2.005  1.00 23.40           N
ANISOU 2586  N   ILE A 326     2732   3176   2984   -454    705   -461       N
ATOM   2587  CA  ILE A 326     -14.441   4.522   1.879  1.00 20.76           C
ANISOU 2587  CA  ILE A 326     2401   2798   2689   -486    764   -506       C
ATOM   2588  C   ILE A 326     -13.311   3.722   2.499  1.00 21.10           C
ANISOU 2588  C   ILE A 326     2524   2772   2720   -467    769   -471       C
ATOM   2589  O   ILE A 326     -12.161   4.165   2.572  1.00 21.06           O
ANISOU 2589  O   ILE A 326     2549   2773   2680   -431    715   -424       O
ATOM   2590  CB  ILE A 326     -14.668   4.042   0.429  1.00 23.47           C
ANISOU 2590  CB  ILE A 326     2654   3203   3059   -506    753   -569       C
ATOM   2591  CG1 ILE A 326     -13.399   4.228  -0.410  1.00 20.74           C
ANISOU 2591  CG1 ILE A 326     2291   2904   2687   -474    682   -549       C
ATOM   2592  CG2 ILE A 326     -15.872   4.725  -0.188  1.00 30.39           C
ANISOU 2592  CG2 ILE A 326     3451   4145   3951   -526    754   -610       C
ATOM   2593  CD1 ILE A 326     -13.291   3.231  -1.534  1.00 24.05           C
ANISOU 2593  CD1 ILE A 326     2657   3348   3133   -489    685   -603       C
ATOM   2594  N   ASN A 327     -13.660   2.528   2.960  1.00 24.29           N
ANISOU 2594  N   ASN A 327     2964   3109   3156   -493    837   -495       N
ATOM   2595  CA  ASN A 327     -12.681   1.522   3.311  1.00 23.93           C
ANISOU 2595  CA  ASN A 327     2982   3001   3108   -482    847   -477       C
ATOM   2596  C   ASN A 327     -12.365   0.717   2.057  1.00 23.63           C
ANISOU 2596  C   ASN A 327     2886   2999   3092   -494    832   -525       C
ATOM   2597  O   ASN A 327     -13.270   0.076   1.507  1.00 25.13           O
ANISOU 2597  O   ASN A 327     3025   3198   3325   -531    872   -584       O
ATOM   2598  CB  ASN A 327     -13.228   0.612   4.401  1.00 22.37           C
ANISOU 2598  CB  ASN A 327     2851   2714   2936   -504    929   -479       C
ATOM   2599  CG  ASN A 327     -12.331  -0.583   4.690  1.00 21.75           C
ANISOU 2599  CG  ASN A 327     2833   2569   2861   -498    948   -470       C
ATOM   2600  OD1 ASN A 327     -11.142  -0.598   4.342  1.00 23.79           O
ANISOU 2600  OD1 ASN A 327     3104   2842   3094   -469    895   -447       O
ATOM   2601  ND2 ASN A 327     -12.896  -1.589   5.357  1.00 21.53           N
ANISOU 2601  ND2 ASN A 327     2846   2469   2866   -524   1023   -486       N
ATOM   2602  N   PRO A 328     -11.133   0.759   1.545  1.00 20.02           N
ANISOU 2602  N   PRO A 328     2431   2567   2610   -464    774   -502       N
ATOM   2603  CA  PRO A 328     -10.818  -0.004   0.333  1.00 17.68           C
ANISOU 2603  CA  PRO A 328     2079   2307   2332   -472    759   -547       C
ATOM   2604  C   PRO A 328     -10.576  -1.482   0.579  1.00 21.77           C
ANISOU 2604  C   PRO A 328     2641   2754   2877   -488    807   -568       C
ATOM   2605  O   PRO A 328     -10.456  -2.240  -0.400  1.00 24.00           O
ANISOU 2605  O   PRO A 328     2877   3061   3182   -499    802   -613       O
ATOM   2606  CB  PRO A 328      -9.542   0.682  -0.181  1.00 23.20           C
ANISOU 2606  CB  PRO A 328     2770   3056   2989   -430    679   -506       C
ATOM   2607  CG  PRO A 328      -8.857   1.113   1.076  1.00 23.91           C
ANISOU 2607  CG  PRO A 328     2951   3090   3046   -401    671   -438       C
ATOM   2608  CD  PRO A 328      -9.993   1.582   1.987  1.00 18.85           C
ANISOU 2608  CD  PRO A 328     2329   2420   2413   -419    717   -435       C
ATOM   2609  N   GLU A 329     -10.473  -1.908   1.839  1.00 20.08           N
ANISOU 2609  N   GLU A 329     2514   2453   2661   -487    852   -535       N
ATOM   2610  CA  GLU A 329     -10.249  -3.307   2.165  1.00 25.14           C
ANISOU 2610  CA  GLU A 329     3203   3021   3327   -501    901   -551       C
ATOM   2611  C   GLU A 329     -11.577  -4.039   2.305  1.00 23.71           C
ANISOU 2611  C   GLU A 329     3003   2806   3199   -548    977   -602       C
ATOM   2612  O   GLU A 329     -12.654  -3.439   2.368  1.00 25.33           O
ANISOU 2612  O   GLU A 329     3172   3035   3418   -568    997   -619       O
ATOM   2613  CB  GLU A 329      -9.434  -3.456   3.452  1.00 25.01           C
ANISOU 2613  CB  GLU A 329     3294   2927   3283   -474    911   -489       C
ATOM   2614  CG  GLU A 329      -8.062  -2.804   3.408  1.00 19.50           C
ANISOU 2614  CG  GLU A 329     2620   2253   2535   -426    838   -437       C
ATOM   2615  CD  GLU A 329      -7.179  -3.221   4.573  1.00 22.35           C
ANISOU 2615  CD  GLU A 329     3087   2532   2873   -400    850   -386       C
ATOM   2616  OE1 GLU A 329      -7.459  -2.822   5.728  1.00 25.83           O
ANISOU 2616  OE1 GLU A 329     3587   2927   3300   -392    876   -350       O
ATOM   2617  OE2 GLU A 329      -6.217  -3.978   4.343  1.00 26.70           O
ANISOU 2617  OE2 GLU A 329     3662   3064   3419   -386    836   -383       O
ATOM   2618  N   ASN A 330     -11.478  -5.368   2.326  1.00 25.98           N
ANISOU 2618  N   ASN A 330     3315   3038   3519   -566   1020   -629       N
ATOM   2619  CA  ASN A 330     -12.613  -6.267   2.417  1.00 24.48           C
ANISOU 2619  CA  ASN A 330     3109   2808   3385   -612   1094   -680       C
ATOM   2620  C   ASN A 330     -12.592  -7.072   3.709  1.00 24.92           C
ANISOU 2620  C   ASN A 330     3258   2758   3450   -618   1160   -652       C
ATOM   2621  O   ASN A 330     -13.515  -7.857   3.954  1.00 25.33           O
ANISOU 2621  O   ASN A 330     3308   2766   3551   -656   1228   -687       O
ATOM   2622  CB  ASN A 330     -12.614  -7.212   1.201  1.00 23.62           C
ANISOU 2622  CB  ASN A 330     2936   2725   3313   -632   1089   -745       C
ATOM   2623  CG  ASN A 330     -13.960  -7.854   0.946  1.00 30.01           C
ANISOU 2623  CG  ASN A 330     3696   3522   4184   -682   1150   -810       C
ATOM   2624  OD1 ASN A 330     -15.004  -7.262   1.194  1.00 23.77           O
ANISOU 2624  OD1 ASN A 330     2880   2746   3407   -701   1175   -819       O
ATOM   2625  ND2 ASN A 330     -13.938  -9.082   0.438  1.00 27.77           N
ANISOU 2625  ND2 ASN A 330     3398   3213   3941   -703   1174   -857       N
ATOM   2626  N   GLY A 331     -11.570  -6.892   4.543  1.00 23.99           N
ANISOU 2626  N   GLY A 331     3223   2602   3289   -580   1141   -590       N
ATOM   2627  CA  GLY A 331     -11.406  -7.663   5.759  1.00 25.58           C
ANISOU 2627  CA  GLY A 331     3519   2706   3495   -579   1198   -559       C
ATOM   2628  C   GLY A 331     -10.532  -6.899   6.730  1.00 26.58           C
ANISOU 2628  C   GLY A 331     3722   2811   3564   -533   1167   -486       C
ATOM   2629  O   GLY A 331     -10.127  -5.762   6.474  1.00 28.93           O
ANISOU 2629  O   GLY A 331     3998   3169   3823   -506   1103   -460       O
ATOM   2630  N   PHE A 332     -10.259  -7.534   7.867  1.00 27.63           N
ANISOU 2630  N   PHE A 332     3948   2858   3693   -524   1213   -452       N
ATOM   2631  CA  PHE A 332      -9.404  -6.975   8.907  1.00 25.82           C
ANISOU 2631  CA  PHE A 332     3803   2597   3412   -479   1189   -383       C
ATOM   2632  C   PHE A 332      -8.201  -7.879   9.111  1.00 24.57           C
ANISOU 2632  C   PHE A 332     3708   2386   3239   -456   1182   -364       C
ATOM   2633  O   PHE A 332      -8.360  -9.085   9.328  1.00 26.94           O
ANISOU 2633  O   PHE A 332     4038   2625   3573   -477   1239   -384       O
ATOM   2634  CB  PHE A 332     -10.142  -6.837  10.244  1.00 24.24           C
ANISOU 2634  CB  PHE A 332     3666   2335   3210   -481   1252   -354       C
ATOM   2635  CG  PHE A 332     -11.487  -6.195  10.142  1.00 25.87           C
ANISOU 2635  CG  PHE A 332     3814   2577   3439   -511   1278   -379       C
ATOM   2636  CD1 PHE A 332     -11.614  -4.878   9.724  1.00 24.97           C
ANISOU 2636  CD1 PHE A 332     3649   2540   3299   -498   1221   -372       C
ATOM   2637  CD2 PHE A 332     -12.620  -6.886  10.524  1.00 24.99           C
ANISOU 2637  CD2 PHE A 332     3703   2420   3373   -550   1361   -407       C
ATOM   2638  CE1 PHE A 332     -12.851  -4.283   9.642  1.00 28.42           C
ANISOU 2638  CE1 PHE A 332     4033   3009   3755   -524   1244   -396       C
ATOM   2639  CE2 PHE A 332     -13.878  -6.285  10.465  1.00 29.64           C
ANISOU 2639  CE2 PHE A 332     4239   3041   3982   -577   1386   -430       C
ATOM   2640  CZ  PHE A 332     -13.990  -4.980  10.024  1.00 30.96           C
ANISOU 2640  CZ  PHE A 332     4355   3286   4122   -563   1327   -425       C
ATOM   2641  N   PHE A 333      -7.009  -7.293   9.069  1.00 21.86           N
ANISOU 2641  N   PHE A 333     3387   2068   2850   -412   1112   -324       N
ATOM   2642  CA  PHE A 333      -5.744  -8.007   9.252  1.00 21.35           C
ANISOU 2642  CA  PHE A 333     3383   1962   2766   -384   1094   -301       C
ATOM   2643  C   PHE A 333      -5.150  -7.496  10.562  1.00 29.46           C
ANISOU 2643  C   PHE A 333     4504   2941   3748   -342   1087   -235       C
ATOM   2644  O   PHE A 333      -4.224  -6.670  10.587  1.00 21.36           O
ANISOU 2644  O   PHE A 333     3491   1945   2679   -302   1020   -196       O
ATOM   2645  CB  PHE A 333      -4.806  -7.769   8.025  1.00 19.35           C
ANISOU 2645  CB  PHE A 333     3073   1783   2498   -367   1015   -313       C
ATOM   2646  CG  PHE A 333      -3.535  -8.569   8.048  1.00 20.65           C
ANISOU 2646  CG  PHE A 333     3287   1911   2646   -342    995   -297       C
ATOM   2647  CD1 PHE A 333      -3.562  -9.951   7.884  1.00 20.96           C
ANISOU 2647  CD1 PHE A 333     3341   1903   2721   -364   1041   -331       C
ATOM   2648  CD2 PHE A 333      -2.305  -7.941   8.192  1.00 25.59           C
ANISOU 2648  CD2 PHE A 333     3944   2553   3225   -295    928   -249       C
ATOM   2649  CE1 PHE A 333      -2.378 -10.689   7.879  1.00 26.65           C
ANISOU 2649  CE1 PHE A 333     4107   2593   3426   -339   1021   -317       C
ATOM   2650  CE2 PHE A 333      -1.126  -8.665   8.194  1.00 21.16           C
ANISOU 2650  CE2 PHE A 333     3428   1962   2649   -271    909   -235       C
ATOM   2651  CZ  PHE A 333      -1.164 -10.052   8.033  1.00 26.80           C
ANISOU 2651  CZ  PHE A 333     4158   2630   3396   -292    955   -270       C
ATOM   2652  N   GLY A 334      -5.716  -7.985  11.662  1.00 28.69           N
ANISOU 2652  N   GLY A 334     4473   2769   3661   -350   1159   -222       N
ATOM   2653  CA  GLY A 334      -5.530  -7.382  12.968  1.00 25.48           C
ANISOU 2653  CA  GLY A 334     4146   2319   3215   -315   1164   -165       C
ATOM   2654  C   GLY A 334      -4.512  -8.134  13.804  1.00 27.35           C
ANISOU 2654  C   GLY A 334     4481   2480   3429   -282   1174   -129       C
ATOM   2655  O   GLY A 334      -4.340  -9.342  13.669  1.00 26.81           O
ANISOU 2655  O   GLY A 334     4432   2369   3387   -297   1210   -150       O
ATOM   2656  N   VAL A 335      -3.825  -7.385  14.667  1.00 23.64           N
ANISOU 2656  N   VAL A 335     4074   1996   2911   -235   1139    -74       N
ATOM   2657  CA  VAL A 335      -2.898  -7.987  15.614  1.00 23.29           C
ANISOU 2657  CA  VAL A 335     4131   1879   2841   -198   1149    -35       C
ATOM   2658  C   VAL A 335      -3.686  -8.892  16.552  1.00 20.49           C
ANISOU 2658  C   VAL A 335     3835   1442   2509   -217   1244    -36       C
ATOM   2659  O   VAL A 335      -4.729  -8.493  17.083  1.00 22.85           O
ANISOU 2659  O   VAL A 335     4132   1733   2816   -231   1287    -34       O
ATOM   2660  CB  VAL A 335      -2.149  -6.886  16.383  1.00 26.10           C
ANISOU 2660  CB  VAL A 335     4537   2237   3141   -145   1092     21       C
ATOM   2661  CG1 VAL A 335      -1.276  -7.464  17.479  1.00 27.96           C
ANISOU 2661  CG1 VAL A 335     4882   2394   3348   -104   1106     62       C
ATOM   2662  CG2 VAL A 335      -1.313  -6.061  15.422  1.00 23.57           C
ANISOU 2662  CG2 VAL A 335     4158   1995   2801   -127   1000     23       C
ATOM   2663  N   ALA A 336      -3.213 -10.138  16.724  1.00 24.27           N
ANISOU 2663  N   ALA A 336     4362   1859   3000   -218   1278    -41       N
ATOM   2664  CA  ALA A 336      -3.925 -11.060  17.601  1.00 25.93           C
ANISOU 2664  CA  ALA A 336     4629   1989   3235   -236   1371    -40       C
ATOM   2665  C   ALA A 336      -3.592 -10.839  19.078  1.00 23.72           C
ANISOU 2665  C   ALA A 336     4455   1645   2911   -190   1389     18       C
ATOM   2666  O   ALA A 336      -4.524 -10.693  19.869  1.00 26.64           O
ANISOU 2666  O   ALA A 336     4849   1985   3287   -198   1447     29       O
ATOM   2667  CB  ALA A 336      -3.658 -12.513  17.196  1.00 26.22           C
ANISOU 2667  CB  ALA A 336     4674   1982   3306   -258   1406    -71       C
ATOM   2668  N   PRO A 337      -2.317 -10.829  19.505  1.00 29.00           N
ANISOU 2668  N   PRO A 337     5190   2292   3537   -140   1344     56       N
ATOM   2669  CA  PRO A 337      -2.031 -10.666  20.943  1.00 27.94           C
ANISOU 2669  CA  PRO A 337     5137   2123   3357    -91   1351    103       C
ATOM   2670  C   PRO A 337      -2.668  -9.412  21.524  1.00 30.47           C
ANISOU 2670  C   PRO A 337     5456   2465   3655    -77   1344    127       C
ATOM   2671  O   PRO A 337      -2.688  -8.350  20.895  1.00 30.37           O
ANISOU 2671  O   PRO A 337     5399   2502   3638    -80   1294    127       O
ATOM   2672  CB  PRO A 337      -0.499 -10.579  20.999  1.00 26.30           C
ANISOU 2672  CB  PRO A 337     4956   1933   3103    -39   1271    128       C
ATOM   2673  CG  PRO A 337      -0.035 -11.245  19.761  1.00 29.39           C
ANISOU 2673  CG  PRO A 337     5320   2319   3528    -68   1262     96       C
ATOM   2674  CD  PRO A 337      -1.069 -10.925  18.725  1.00 30.13           C
ANISOU 2674  CD  PRO A 337     5317   2467   3665   -121   1272     52       C
ATOM   2675  N   GLY A 338      -3.171  -9.541  22.759  1.00 26.92           N
ANISOU 2675  N   GLY A 338     5042   1999   3187    -56   1383    143       N
ATOM   2676  CA  GLY A 338      -3.911  -8.488  23.406  1.00 27.69           C
ANISOU 2676  CA  GLY A 338     5141   2112   3267    -44   1387    161       C
ATOM   2677  C   GLY A 338      -5.376  -8.437  23.040  1.00 31.94           C
ANISOU 2677  C   GLY A 338     5640   2642   3855   -101   1458    136       C
ATOM   2678  O   GLY A 338      -6.126  -7.669  23.656  1.00 37.19           O
ANISOU 2678  O   GLY A 338     6307   3316   4507    -93   1473    150       O
ATOM   2679  N   THR A 339      -5.815  -9.220  22.058  1.00 23.69           N
ANISOU 2679  N   THR A 339     4553   1581   2866   -158   1500     96       N
ATOM   2680  CA  THR A 339      -7.234  -9.293  21.734  1.00 26.38           C
ANISOU 2680  CA  THR A 339     4836   1931   3256   -213   1563     61       C
ATOM   2681  C   THR A 339      -7.906 -10.231  22.725  1.00 28.77           C
ANISOU 2681  C   THR A 339     5180   2178   3572   -216   1646     64       C
ATOM   2682  O   THR A 339      -7.525 -11.402  22.829  1.00 26.55           O
ANISOU 2682  O   THR A 339     4919   1866   3301   -215   1668     54       O
ATOM   2683  CB  THR A 339      -7.477  -9.801  20.317  1.00 28.23           C
ANISOU 2683  CB  THR A 339     4976   2210   3540   -264   1554      2       C
ATOM   2684  OG1 THR A 339      -6.820  -8.952  19.370  1.00 29.04           O
ANISOU 2684  OG1 THR A 339     5019   2393   3623   -252   1461     -6       O
ATOM   2685  CG2 THR A 339      -8.971  -9.817  20.035  1.00 26.38           C
ANISOU 2685  CG2 THR A 339     4676   1992   3355   -317   1613    -36       C
ATOM   2686  N   SER A 340      -8.905  -9.714  23.435  1.00 32.69           N
ANISOU 2686  N   SER A 340     5679   2677   4067   -216   1684     73       N
ATOM   2687  CA  SER A 340      -9.655 -10.488  24.414  1.00 40.58           C
ANISOU 2687  CA  SER A 340     6704   3638   5076   -214   1758     74       C
ATOM   2688  C   SER A 340     -11.090  -9.990  24.414  1.00 39.89           C
ANISOU 2688  C   SER A 340     6576   3559   5021   -252   1810     59       C
ATOM   2689  O   SER A 340     -11.428  -8.995  23.765  1.00 39.54           O
ANISOU 2689  O   SER A 340     6487   3553   4982   -274   1786     53       O
ATOM   2690  CB  SER A 340      -9.047 -10.361  25.814  1.00 36.40           C
ANISOU 2690  CB  SER A 340     6248   3099   4484   -143   1737    116       C
ATOM   2691  OG  SER A 340      -9.112  -9.014  26.271  1.00 33.39           O
ANISOU 2691  OG  SER A 340     5875   2748   4063   -110   1696    142       O
ATOM   2692  N   VAL A 341     -11.936 -10.678  25.180  1.00 35.83           N
ANISOU 2692  N   VAL A 341     6077   3012   4527   -258   1883     54       N
ATOM   2693  CA  VAL A 341     -13.297 -10.198  25.363  1.00 31.98           C
ANISOU 2693  CA  VAL A 341     5555   2531   4064   -286   1933     44       C
ATOM   2694  C   VAL A 341     -13.307  -8.823  26.024  1.00 32.74           C
ANISOU 2694  C   VAL A 341     5675   2657   4109   -243   1892     79       C
ATOM   2695  O   VAL A 341     -14.247  -8.047  25.824  1.00 39.41           O
ANISOU 2695  O   VAL A 341     6477   3528   4968   -269   1907     71       O
ATOM   2696  CB  VAL A 341     -14.103 -11.248  26.157  1.00 36.55           C
ANISOU 2696  CB  VAL A 341     6153   3064   4671   -292   2016     36       C
ATOM   2697  CG1 VAL A 341     -15.512 -10.750  26.452  1.00 34.08           C
ANISOU 2697  CG1 VAL A 341     5807   2757   4383   -315   2066     27       C
ATOM   2698  CG2 VAL A 341     -14.141 -12.571  25.374  1.00 34.06           C
ANISOU 2698  CG2 VAL A 341     5805   2723   4413   -339   2052     -4       C
ATOM   2699  N   LYS A 342     -12.251  -8.476  26.771  1.00 35.36           N
ANISOU 2699  N   LYS A 342     6067   2989   4378   -178   1837    117       N
ATOM   2700  CA  LYS A 342     -12.196  -7.177  27.441  1.00 36.38           C
ANISOU 2700  CA  LYS A 342     6219   3145   4457   -133   1793    149       C
ATOM   2701  C   LYS A 342     -11.732  -6.064  26.509  1.00 44.44           C
ANISOU 2701  C   LYS A 342     7204   4215   5465   -140   1720    153       C
ATOM   2702  O   LYS A 342     -12.246  -4.942  26.580  1.00 39.42           O
ANISOU 2702  O   LYS A 342     6551   3611   4816   -137   1704    164       O
ATOM   2703  CB  LYS A 342     -11.260  -7.232  28.651  1.00 44.35           C
ANISOU 2703  CB  LYS A 342     7302   4141   5407    -60   1759    184       C
ATOM   2704  CG  LYS A 342     -11.735  -8.079  29.815  1.00 45.03           C
ANISOU 2704  CG  LYS A 342     7432   4184   5492    -42   1827    189       C
ATOM   2705  CD  LYS A 342     -10.706  -8.066  30.946  1.00 46.77           C
ANISOU 2705  CD  LYS A 342     7719   4400   5651     29   1787    220       C
ATOM   2706  CE  LYS A 342     -11.287  -8.650  32.232  1.00 49.16           C
ANISOU 2706  CE  LYS A 342     8067   4666   5946     54   1853    230       C
ATOM   2707  NZ  LYS A 342     -11.967  -9.947  31.974  1.00 51.29           N
ANISOU 2707  NZ  LYS A 342     8322   4896   6271      7   1936    206       N
ATOM   2708  N   THR A 343     -10.744  -6.340  25.654  1.00 41.22           N
ANISOU 2708  N   THR A 343     6786   3815   5060   -146   1674    146       N
ATOM   2709  CA  THR A 343     -10.148  -5.289  24.839  1.00 37.34           C
ANISOU 2709  CA  THR A 343     6268   3369   4551   -144   1599    155       C
ATOM   2710  C   THR A 343     -10.781  -5.168  23.460  1.00 35.90           C
ANISOU 2710  C   THR A 343     5978   3247   4415   -203   1591    104       C
ATOM   2711  O   THR A 343     -10.669  -4.103  22.837  1.00 32.44           O
ANISOU 2711  O   THR A 343     5482   2881   3962   -197   1520     97       O
ATOM   2712  CB  THR A 343      -8.635  -5.512  24.688  1.00 34.87           C
ANISOU 2712  CB  THR A 343     5986   3056   4207   -105   1529    169       C
ATOM   2713  OG1 THR A 343      -8.377  -6.722  23.957  1.00 34.10           O
ANISOU 2713  OG1 THR A 343     5873   2934   4149   -140   1556    140       O
ATOM   2714  CG2 THR A 343      -7.979  -5.590  26.066  1.00 35.56           C
ANISOU 2714  CG2 THR A 343     6140   3129   4241    -36   1507    199       C
ATOM   2715  N   ASN A 344     -11.460  -6.214  22.979  1.00 30.59           N
ANISOU 2715  N   ASN A 344     5269   2555   3798   -255   1655     64       N
ATOM   2716  CA  ASN A 344     -12.077  -6.145  21.660  1.00 27.84           C
ANISOU 2716  CA  ASN A 344     4811   2273   3495   -306   1641      7       C
ATOM   2717  C   ASN A 344     -13.067  -7.291  21.481  1.00 31.44           C
ANISOU 2717  C   ASN A 344     5241   2691   4014   -361   1731    -31       C
ATOM   2718  O   ASN A 344     -12.840  -8.194  20.659  1.00 28.26           O
ANISOU 2718  O   ASN A 344     4805   2286   3648   -391   1735    -68       O
ATOM   2719  CB  ASN A 344     -10.991  -6.164  20.571  1.00 29.37           C
ANISOU 2719  CB  ASN A 344     4964   2511   3683   -301   1561    -10       C
ATOM   2720  CG  ASN A 344     -11.519  -5.768  19.216  1.00 31.26           C
ANISOU 2720  CG  ASN A 344     5089   2832   3954   -342   1528    -61       C
ATOM   2721  OD1 ASN A 344     -12.734  -5.729  18.999  1.00 31.55           O
ANISOU 2721  OD1 ASN A 344     5073   2886   4028   -382   1573    -93       O
ATOM   2722  ND2 ASN A 344     -10.605  -5.485  18.277  1.00 27.42           N
ANISOU 2722  ND2 ASN A 344     4564   2399   3455   -331   1449    -70       N
ATOM   2723  N   PRO A 345     -14.177  -7.291  22.230  1.00 33.59           N
ANISOU 2723  N   PRO A 345     5527   2934   4301   -376   1804    -26       N
ATOM   2724  CA  PRO A 345     -15.116  -8.421  22.135  1.00 30.14           C
ANISOU 2724  CA  PRO A 345     5071   2455   3928   -428   1894    -60       C
ATOM   2725  C   PRO A 345     -15.741  -8.563  20.761  1.00 34.83           C
ANISOU 2725  C   PRO A 345     5552   3107   4576   -484   1884   -126       C
ATOM   2726  O   PRO A 345     -16.094  -9.680  20.368  1.00 32.22           O
ANISOU 2726  O   PRO A 345     5198   2743   4299   -525   1935   -161       O
ATOM   2727  CB  PRO A 345     -16.166  -8.086  23.205  1.00 30.86           C
ANISOU 2727  CB  PRO A 345     5193   2517   4016   -426   1961    -35       C
ATOM   2728  CG  PRO A 345     -16.149  -6.574  23.243  1.00 32.46           C
ANISOU 2728  CG  PRO A 345     5376   2787   4172   -395   1893    -18       C
ATOM   2729  CD  PRO A 345     -14.700  -6.210  23.081  1.00 31.70           C
ANISOU 2729  CD  PRO A 345     5312   2707   4027   -349   1806      7       C
ATOM   2730  N   ASN A 346     -15.877  -7.468  20.004  1.00 31.48           N
ANISOU 2730  N   ASN A 346     5055   2767   4138   -485   1817   -144       N
ATOM   2731  CA  ASN A 346     -16.432  -7.586  18.660  1.00 34.69           C
ANISOU 2731  CA  ASN A 346     5354   3233   4593   -534   1804   -207       C
ATOM   2732  C   ASN A 346     -15.475  -8.296  17.705  1.00 33.27           C
ANISOU 2732  C   ASN A 346     5154   3063   4426   -538   1761   -233       C
ATOM   2733  O   ASN A 346     -15.930  -9.002  16.801  1.00 32.18           O
ANISOU 2733  O   ASN A 346     4950   2937   4341   -583   1781   -287       O
ATOM   2734  CB  ASN A 346     -16.811  -6.211  18.118  1.00 35.16           C
ANISOU 2734  CB  ASN A 346     5344   3381   4633   -530   1744   -218       C
ATOM   2735  CG  ASN A 346     -18.054  -5.660  18.783  1.00 37.67           C
ANISOU 2735  CG  ASN A 346     5656   3698   4958   -542   1795   -213       C
ATOM   2736  OD1 ASN A 346     -18.068  -4.533  19.286  1.00 30.24           O
ANISOU 2736  OD1 ASN A 346     4733   2784   3974   -509   1763   -180       O
ATOM   2737  ND2 ASN A 346     -19.109  -6.465  18.801  1.00 30.06           N
ANISOU 2737  ND2 ASN A 346     4668   2701   4051   -588   1877   -245       N
ATOM   2738  N   ALA A 347     -14.162  -8.152  17.895  1.00 26.50           N
ANISOU 2738  N   ALA A 347     4351   2198   3520   -492   1704   -196       N
ATOM   2739  CA  ALA A 347     -13.229  -8.958  17.116  1.00 33.05           C
ANISOU 2739  CA  ALA A 347     5171   3026   4360   -495   1673   -216       C
ATOM   2740  C   ALA A 347     -13.321 -10.433  17.500  1.00 33.97           C
ANISOU 2740  C   ALA A 347     5334   3058   4516   -516   1750   -224       C
ATOM   2741  O   ALA A 347     -13.250 -11.311  16.630  1.00 28.76           O
ANISOU 2741  O   ALA A 347     4632   2399   3897   -547   1755   -269       O
ATOM   2742  CB  ALA A 347     -11.802  -8.447  17.294  1.00 33.36           C
ANISOU 2742  CB  ALA A 347     5262   3076   4339   -439   1596   -172       C
ATOM   2743  N   ILE A 348     -13.469 -10.729  18.796  1.00 31.17           N
ANISOU 2743  N   ILE A 348     5067   2629   4149   -499   1811   -182       N
ATOM   2744  CA  ILE A 348     -13.627 -12.123  19.223  1.00 26.85           C
ANISOU 2744  CA  ILE A 348     4564   1996   3640   -520   1891   -187       C
ATOM   2745  C   ILE A 348     -14.771 -12.780  18.466  1.00 32.07           C
ANISOU 2745  C   ILE A 348     5145   2665   4376   -584   1943   -249       C
ATOM   2746  O   ILE A 348     -14.651 -13.914  17.980  1.00 32.96           O
ANISOU 2746  O   ILE A 348     5245   2745   4531   -612   1968   -282       O
ATOM   2747  CB  ILE A 348     -13.845 -12.206  20.747  1.00 31.87           C
ANISOU 2747  CB  ILE A 348     5298   2558   4253   -494   1956   -133       C
ATOM   2748  CG1 ILE A 348     -12.658 -11.609  21.506  1.00 37.18           C
ANISOU 2748  CG1 ILE A 348     6054   3221   4853   -427   1902    -74       C
ATOM   2749  CG2 ILE A 348     -14.067 -13.659  21.169  1.00 31.14           C
ANISOU 2749  CG2 ILE A 348     5234   2402   4197   -505   2024   -145       C
ATOM   2750  CD1 ILE A 348     -11.385 -12.414  21.416  1.00 35.99           C
ANISOU 2750  CD1 ILE A 348     5946   3043   4684   -400   1869    -66       C
ATOM   2751  N   LYS A 349     -15.897 -12.073  18.337  1.00 31.33           N
ANISOU 2751  N   LYS A 349     4992   2613   4300   -609   1959   -268       N
ATOM   2752  CA  LYS A 349     -17.032 -12.652  17.626  1.00 38.57           C
ANISOU 2752  CA  LYS A 349     5828   3537   5288   -670   2008   -329       C
ATOM   2753  C   LYS A 349     -16.732 -12.843  16.143  1.00 41.73           C
ANISOU 2753  C   LYS A 349     6142   3998   5714   -692   1950   -386       C
ATOM   2754  O   LYS A 349     -17.224 -13.796  15.531  1.00 48.60           O
ANISOU 2754  O   LYS A 349     6967   4853   6646   -737   1987   -436       O
ATOM   2755  CB  LYS A 349     -18.276 -11.783  17.807  1.00 34.68           C
ANISOU 2755  CB  LYS A 349     5290   3081   4805   -688   2032   -336       C
ATOM   2756  CG  LYS A 349     -18.637 -11.461  19.256  1.00 44.78           C
ANISOU 2756  CG  LYS A 349     6648   4309   6056   -663   2086   -280       C
ATOM   2757  CD  LYS A 349     -19.812 -10.495  19.285  1.00 48.38           C
ANISOU 2757  CD  LYS A 349     7050   4813   6518   -680   2098   -291       C
ATOM   2758  CE  LYS A 349     -20.241 -10.158  20.697  1.00 60.34           C
ANISOU 2758  CE  LYS A 349     8639   6282   8005   -653   2151   -238       C
ATOM   2759  NZ  LYS A 349     -21.272  -9.079  20.705  1.00 59.60           N
ANISOU 2759  NZ  LYS A 349     8494   6244   7909   -663   2151   -247       N
ATOM   2760  N   THR A 350     -15.926 -11.952  15.543  1.00 37.99           N
ANISOU 2760  N   THR A 350     5645   3595   5194   -662   1859   -379       N
ATOM   2761  CA  THR A 350     -15.721 -11.998  14.095  1.00 39.53           C
ANISOU 2761  CA  THR A 350     5751   3859   5410   -681   1802   -433       C
ATOM   2762  C   THR A 350     -14.863 -13.184  13.670  1.00 29.36           C
ANISOU 2762  C   THR A 350     4482   2533   4139   -683   1798   -450       C
ATOM   2763  O   THR A 350     -15.087 -13.760  12.598  1.00 29.57           O
ANISOU 2763  O   THR A 350     4438   2586   4211   -716   1792   -508       O
ATOM   2764  CB  THR A 350     -15.054 -10.712  13.603  1.00 39.82           C
ANISOU 2764  CB  THR A 350     5760   3978   5392   -645   1707   -417       C
ATOM   2765  OG1 THR A 350     -13.768 -10.588  14.219  1.00 52.54           O
ANISOU 2765  OG1 THR A 350     7454   5563   6947   -594   1668   -361       O
ATOM   2766  CG2 THR A 350     -15.870  -9.512  13.962  1.00 28.38           C
ANISOU 2766  CG2 THR A 350     4289   2569   3925   -642   1705   -403       C
ATOM   2767  N   ILE A 351     -13.850 -13.532  14.468  1.00 27.71           N
ANISOU 2767  N   ILE A 351     4367   2268   3893   -644   1796   -400       N
ATOM   2768  CA  ILE A 351     -12.712 -14.316  13.993  1.00 24.27           C
ANISOU 2768  CA  ILE A 351     3951   1818   3453   -630   1762   -406       C
ATOM   2769  C   ILE A 351     -12.905 -15.809  14.212  1.00 32.13           C
ANISOU 2769  C   ILE A 351     4977   2731   4499   -659   1836   -426       C
ATOM   2770  O   ILE A 351     -11.944 -16.574  14.090  1.00 31.22           O
ANISOU 2770  O   ILE A 351     4899   2584   4377   -644   1820   -422       O
ATOM   2771  CB  ILE A 351     -11.407 -13.869  14.664  1.00 33.24           C
ANISOU 2771  CB  ILE A 351     5170   2942   4519   -570   1713   -344       C
ATOM   2772  CG1 ILE A 351     -11.518 -14.098  16.181  1.00 24.18           C
ANISOU 2772  CG1 ILE A 351     4124   1708   3354   -551   1777   -291       C
ATOM   2773  CG2 ILE A 351     -11.066 -12.396  14.310  1.00 33.63           C
ANISOU 2773  CG2 ILE A 351     5184   3076   4519   -541   1629   -326       C
ATOM   2774  CD1 ILE A 351     -10.241 -13.795  16.959  1.00 25.34           C
ANISOU 2774  CD1 ILE A 351     4362   1831   3436   -490   1736   -229       C
ATOM   2775  N   GLN A 352     -14.107 -16.240  14.566  1.00 34.47           N
ANISOU 2775  N   GLN A 352     5261   2988   4846   -699   1916   -444       N
ATOM   2776  CA  GLN A 352     -14.351 -17.655  14.801  1.00 36.00           C
ANISOU 2776  CA  GLN A 352     5484   3101   5094   -729   1989   -462       C
ATOM   2777  C   GLN A 352     -14.956 -18.351  13.595  1.00 36.97           C
ANISOU 2777  C   GLN A 352     5513   3248   5285   -780   1997   -538       C
ATOM   2778  O   GLN A 352     -15.438 -19.485  13.720  1.00 41.09           O
ANISOU 2778  O   GLN A 352     6042   3706   5866   -815   2064   -562       O
ATOM   2779  CB  GLN A 352     -15.238 -17.827  16.027  1.00 38.99           C
ANISOU 2779  CB  GLN A 352     5915   3411   5489   -740   2080   -431       C
ATOM   2780  CG  GLN A 352     -14.587 -17.286  17.277  1.00 42.38           C
ANISOU 2780  CG  GLN A 352     6445   3807   5851   -685   2076   -356       C
ATOM   2781  CD  GLN A 352     -15.364 -17.608  18.524  1.00 47.71           C
ANISOU 2781  CD  GLN A 352     7160   4443   6523   -671   2143   -328       C
ATOM   2782  OE1 GLN A 352     -15.817 -18.741  18.720  1.00 43.72           O
ANISOU 2782  OE1 GLN A 352     6653   3901   6058   -687   2196   -346       O
ATOM   2783  NE2 GLN A 352     -15.515 -16.617  19.388  1.00 49.15           N
ANISOU 2783  NE2 GLN A 352     7380   4637   6659   -638   2139   -283       N
ATOM   2784  N   LYS A 353     -14.925 -17.709  12.432  1.00 32.46           N
ANISOU 2784  N   LYS A 353     5618   2885   3831   -798   1660   -376       N
ATOM   2785  CA  LYS A 353     -15.490 -18.268  11.212  1.00 32.56           C
ANISOU 2785  CA  LYS A 353     5548   2922   3901   -804   1716   -433       C
ATOM   2786  C   LYS A 353     -14.737 -17.702  10.012  1.00 33.00           C
ANISOU 2786  C   LYS A 353     5531   3041   3967   -803   1668   -453       C
ATOM   2787  O   LYS A 353     -14.510 -16.493   9.940  1.00 35.67           O
ANISOU 2787  O   LYS A 353     5878   3427   4248   -800   1621   -460       O
ATOM   2788  CB  LYS A 353     -16.991 -17.953  11.129  1.00 41.14           C
ANISOU 2788  CB  LYS A 353     6640   4027   4964   -806   1789   -495       C
ATOM   2789  CG  LYS A 353     -17.672 -18.357   9.835  1.00 50.08           C
ANISOU 2789  CG  LYS A 353     7670   5197   6161   -810   1816   -545       C
ATOM   2790  CD  LYS A 353     -19.171 -18.567  10.046  1.00 58.14           C
ANISOU 2790  CD  LYS A 353     8679   6211   7202   -811   1849   -562       C
ATOM   2791  CE  LYS A 353     -19.841 -17.346  10.637  1.00 62.15           C
ANISOU 2791  CE  LYS A 353     9210   6746   7658   -806   1797   -550       C
ATOM   2792  NZ  LYS A 353     -19.883 -16.227   9.661  1.00 65.08           N
ANISOU 2792  NZ  LYS A 353     9495   7200   8033   -799   1708   -558       N
ATOM   2793  N   ASN A 354     -14.315 -18.588   9.099  1.00 32.77           N
ANISOU 2793  N   ASN A 354     5431   3009   4012   -806   1678   -462       N
ATOM   2794  CA  ASN A 354     -13.702 -18.199   7.821  1.00 33.22           C
ANISOU 2794  CA  ASN A 354     5408   3126   4089   -806   1643   -490       C
ATOM   2795  C   ASN A 354     -12.501 -17.270   8.007  1.00 26.40           C
ANISOU 2795  C   ASN A 354     4562   2285   3184   -800   1549   -448       C
ATOM   2796  O   ASN A 354     -12.285 -16.338   7.227  1.00 26.60           O
ANISOU 2796  O   ASN A 354     4547   2375   3183   -799   1519   -475       O
ATOM   2797  CB  ASN A 354     -14.736 -17.560   6.892  1.00 37.53           C
ANISOU 2797  CB  ASN A 354     5899   3740   4622   -806   1675   -558       C
ATOM   2798  CG  ASN A 354     -15.923 -18.465   6.634  1.00 44.93           C
ANISOU 2798  CG  ASN A 354     6797   4659   5615   -810   1733   -586       C
ATOM   2799  OD1 ASN A 354     -15.769 -19.675   6.447  1.00 42.57           O
ANISOU 2799  OD1 ASN A 354     6490   4316   5367   -815   1801   -601       O
ATOM   2800  ND2 ASN A 354     -17.120 -17.886   6.636  1.00 48.37           N
ANISOU 2800  ND2 ASN A 354     7209   5126   6043   -806   1707   -593       N
ATOM   2801  N   THR A 355     -11.679 -17.559   9.014  1.00 29.92           N
ANISOU 2801  N   THR A 355     5066   2675   3627   -796   1502   -381       N
ATOM   2802  CA  THR A 355     -10.578 -16.685   9.403  1.00 29.97           C
ANISOU 2802  CA  THR A 355     5103   2694   3591   -790   1413   -338       C
ATOM   2803  C   THR A 355      -9.252 -17.433   9.363  1.00 33.70           C
ANISOU 2803  C   THR A 355     5559   3124   4122   -785   1358   -288       C
ATOM   2804  O   THR A 355      -9.159 -18.578   9.812  1.00 35.06           O
ANISOU 2804  O   THR A 355     5747   3231   4345   -785   1378   -259       O
ATOM   2805  CB  THR A 355     -10.825 -16.119  10.809  1.00 29.13           C
ANISOU 2805  CB  THR A 355     5094   2562   3412   -786   1401   -305       C
ATOM   2806  OG1 THR A 355     -11.980 -15.273  10.772  1.00 26.49           O
ANISOU 2806  OG1 THR A 355     4773   2270   3023   -789   1443   -356       O
ATOM   2807  CG2 THR A 355      -9.624 -15.337  11.303  1.00 25.90           C
ANISOU 2807  CG2 THR A 355     4720   2159   2961   -779   1309   -257       C
ATOM   2808  N   ILE A 356      -8.227 -16.778   8.821  1.00 28.13           N
ANISOU 2808  N   ILE A 356     4822   2456   3411   -781   1287   -280       N
ATOM   2809  CA  ILE A 356      -6.872 -17.312   8.783  1.00 27.06           C
ANISOU 2809  CA  ILE A 356     4672   2283   3326   -774   1222   -233       C
ATOM   2810  C   ILE A 356      -6.038 -16.617   9.847  1.00 25.81           C
ANISOU 2810  C   ILE A 356     4584   2108   3113   -766   1147   -175       C
ATOM   2811  O   ILE A 356      -5.972 -15.382   9.888  1.00 28.45           O
ANISOU 2811  O   ILE A 356     4935   2495   3378   -764   1114   -185       O
ATOM   2812  CB  ILE A 356      -6.242 -17.121   7.393  1.00 28.62           C
ANISOU 2812  CB  ILE A 356     4781   2530   3562   -774   1193   -265       C
ATOM   2813  CG1 ILE A 356      -7.068 -17.851   6.339  1.00 33.72           C
ANISOU 2813  CG1 ILE A 356     5356   3195   4263   -782   1270   -325       C
ATOM   2814  CG2 ILE A 356      -4.783 -17.598   7.392  1.00 26.51           C
ANISOU 2814  CG2 ILE A 356     4502   2222   3347   -766   1119   -218       C
ATOM   2815  CD1 ILE A 356      -6.524 -17.700   4.932  1.00 32.30           C
ANISOU 2815  CD1 ILE A 356     5086   3067   4121   -782   1249   -362       C
ATOM   2816  N   PHE A 357      -5.387 -17.407  10.692  1.00 26.06           N
ANISOU 2816  N   PHE A 357     4657   2069   3175   -759   1121   -116       N
ATOM   2817  CA  PHE A 357      -4.494 -16.922  11.733  1.00 28.24           C
ANISOU 2817  CA  PHE A 357     4998   2324   3409   -749   1050    -56       C
ATOM   2818  C   PHE A 357      -3.054 -17.199  11.326  1.00 29.40           C
ANISOU 2818  C   PHE A 357     5107   2453   3610   -740    976    -23       C
ATOM   2819  O   PHE A 357      -2.763 -18.229  10.708  1.00 32.49           O
ANISOU 2819  O   PHE A 357     5448   2812   4085   -740    987    -25       O
ATOM   2820  CB  PHE A 357      -4.790 -17.605  13.075  1.00 26.85           C
ANISOU 2820  CB  PHE A 357     4899   2079   3224   -746   1074     -8       C
ATOM   2821  CG  PHE A 357      -6.156 -17.309  13.621  1.00 27.08           C
ANISOU 2821  CG  PHE A 357     4973   2118   3197   -753   1142    -37       C
ATOM   2822  CD1 PHE A 357      -6.355 -16.239  14.489  1.00 27.32           C
ANISOU 2822  CD1 PHE A 357     5071   2171   3138   -752   1122    -30       C
ATOM   2823  CD2 PHE A 357      -7.245 -18.096  13.273  1.00 31.14           C
ANISOU 2823  CD2 PHE A 357     5464   2620   3749   -762   1227    -75       C
ATOM   2824  CE1 PHE A 357      -7.620 -15.974  15.012  1.00 25.38           C
ANISOU 2824  CE1 PHE A 357     4869   1930   2844   -758   1184    -59       C
ATOM   2825  CE2 PHE A 357      -8.511 -17.837  13.784  1.00 30.51           C
ANISOU 2825  CE2 PHE A 357     5425   2547   3621   -767   1290   -103       C
ATOM   2826  CZ  PHE A 357      -8.699 -16.768  14.656  1.00 30.11           C
ANISOU 2826  CZ  PHE A 357     5442   2514   3483   -765   1267    -95       C
ATOM   2827  N   THR A 358      -2.151 -16.285  11.679  1.00 24.14           N
ANISOU 2827  N   THR A 358     4467   1807   2897   -731    902      6       N
ATOM   2828  CA  THR A 358      -0.732 -16.457  11.391  1.00 22.94           C
ANISOU 2828  CA  THR A 358     4286   1638   2793   -720    826     41       C
ATOM   2829  C   THR A 358       0.074 -16.245  12.664  1.00 26.97           C
ANISOU 2829  C   THR A 358     4868   2113   3265   -708    769    109       C
ATOM   2830  O   THR A 358       0.028 -15.162  13.257  1.00 28.74           O
ANISOU 2830  O   THR A 358     5143   2373   3404   -707    745    112       O
ATOM   2831  CB  THR A 358      -0.269 -15.483  10.301  1.00 26.88           C
ANISOU 2831  CB  THR A 358     4727   2209   3280   -721    786      2       C
ATOM   2832  OG1 THR A 358      -1.084 -15.657   9.137  1.00 27.09           O
ANISOU 2832  OG1 THR A 358     4685   2274   3335   -732    844    -62       O
ATOM   2833  CG2 THR A 358       1.172 -15.767   9.944  1.00 27.12           C
ANISOU 2833  CG2 THR A 358     4720   2215   3369   -709    713     34       C
ATOM   2834  N   ASN A 359       0.815 -17.273  13.070  1.00 28.18           N
ANISOU 2834  N   ASN A 359     5027   2198   3483   -698    747    163       N
ATOM   2835  CA  ASN A 359       1.793 -17.217  14.156  1.00 27.26           C
ANISOU 2835  CA  ASN A 359     4965   2045   3345   -683    687    234       C
ATOM   2836  C   ASN A 359       1.162 -17.059  15.541  1.00 26.65           C
ANISOU 2836  C   ASN A 359     4979   1951   3197   -683    711    265       C
ATOM   2837  O   ASN A 359       1.820 -16.575  16.465  1.00 34.28           O
ANISOU 2837  O   ASN A 359     6000   2914   4112   -673    661    311       O
ATOM   2838  CB  ASN A 359       2.832 -16.104  13.909  1.00 30.55           C
ANISOU 2838  CB  ASN A 359     5372   2510   3724   -674    609    237       C
ATOM   2839  CG  ASN A 359       3.836 -16.476  12.815  1.00 29.12           C
ANISOU 2839  CG  ASN A 359     5111   2325   3628   -667    568    231       C
ATOM   2840  OD1 ASN A 359       4.016 -17.653  12.497  1.00 31.79           O
ANISOU 2840  OD1 ASN A 359     5413   2610   4057   -666    582    243       O
ATOM   2841  ND2 ASN A 359       4.488 -15.474  12.239  1.00 28.30           N
ANISOU 2841  ND2 ASN A 359     4980   2275   3496   -664    516    210       N
ATOM   2842  N   VAL A 360      -0.100 -17.444  15.725  1.00 29.33           N
ANISOU 2842  N   VAL A 360     5337   2281   3528   -695    788    238       N
ATOM   2843  CA  VAL A 360      -0.648 -17.541  17.078  1.00 25.00           C
ANISOU 2843  CA  VAL A 360     4872   1701   2927   -694    813    273       C
ATOM   2844  C   VAL A 360      -0.437 -18.969  17.558  1.00 35.18           C
ANISOU 2844  C   VAL A 360     6168   2910   4288   -687    830    327       C
ATOM   2845  O   VAL A 360      -0.073 -19.849  16.770  1.00 35.55           O
ANISOU 2845  O   VAL A 360     6154   2929   4423   -686    832    324       O
ATOM   2846  CB  VAL A 360      -2.139 -17.150  17.149  1.00 26.11           C
ANISOU 2846  CB  VAL A 360     5035   1869   3015   -708    887    219       C
ATOM   2847  CG1 VAL A 360      -2.347 -15.725  16.627  1.00 25.47           C
ANISOU 2847  CG1 VAL A 360     4945   1867   2866   -714    870    165       C
ATOM   2848  CG2 VAL A 360      -3.013 -18.147  16.388  1.00 26.21           C
ANISOU 2848  CG2 VAL A 360     4999   1864   3098   -718    963    181       C
ATOM   2849  N   ALA A 361      -0.660 -19.206  18.848  1.00 31.79           N
ANISOU 2849  N   ALA A 361     5814   2443   3823   -683    841    374       N
ATOM   2850  CA  ALA A 361      -0.582 -20.544  19.413  1.00 30.14           C
ANISOU 2850  CA  ALA A 361     5619   2158   3674   -677    862    427       C
ATOM   2851  C   ALA A 361      -1.867 -21.316  19.147  1.00 31.66           C
ANISOU 2851  C   ALA A 361     5801   2331   3898   -690    953    387       C
ATOM   2852  O   ALA A 361      -2.936 -20.737  18.923  1.00 29.41           O
ANISOU 2852  O   ALA A 361     5521   2087   3567   -702   1003    329       O
ATOM   2853  CB  ALA A 361      -0.321 -20.473  20.914  1.00 29.23           C
ANISOU 2853  CB  ALA A 361     5587   2014   3503   -667    839    495       C
ATOM   2854  N   GLU A 362      -1.755 -22.649  19.202  1.00 30.12           N
ANISOU 2854  N   GLU A 362     5592   2070   3781   -687    976    418       N
ATOM   2855  CA  GLU A 362      -2.861 -23.561  18.950  1.00 38.17           C
ANISOU 2855  CA  GLU A 362     6598   3062   4841   -698   1063    384       C
ATOM   2856  C   GLU A 362      -3.116 -24.407  20.191  1.00 40.74           C
ANISOU 2856  C   GLU A 362     6989   3322   5168   -693   1090    443       C
ATOM   2857  O   GLU A 362      -2.178 -24.957  20.780  1.00 39.41           O
ANISOU 2857  O   GLU A 362     6838   3106   5029   -680   1044    514       O
ATOM   2858  CB  GLU A 362      -2.563 -24.474  17.748  1.00 32.61           C
ANISOU 2858  CB  GLU A 362     5813   2340   4238   -700   1074    357       C
ATOM   2859  CG  GLU A 362      -3.709 -25.401  17.386  1.00 33.79           C
ANISOU 2859  CG  GLU A 362     5943   2467   4428   -712   1167    314       C
ATOM   2860  CD  GLU A 362      -3.348 -26.382  16.276  1.00 41.05           C
ANISOU 2860  CD  GLU A 362     6787   3364   5447   -714   1178    290       C
ATOM   2861  OE1 GLU A 362      -2.307 -26.180  15.611  1.00 39.11           O
ANISOU 2861  OE1 GLU A 362     6496   3131   5233   -708   1114    293       O
ATOM   2862  OE2 GLU A 362      -4.104 -27.361  16.071  1.00 45.67           O
ANISOU 2862  OE2 GLU A 362     7357   3918   6078   -720   1252    265       O
ATOM   2863  N   THR A 363      -4.381 -24.511  20.584  1.00 38.94           N
ANISOU 2863  N   THR A 363     6795   3092   4908   -702   1165    416       N
ATOM   2864  CA  THR A 363      -4.762 -25.339  21.714  1.00 37.72           C
ANISOU 2864  CA  THR A 363     6702   2877   4755   -699   1201    465       C
ATOM   2865  C   THR A 363      -5.005 -26.769  21.239  1.00 44.66           C
ANISOU 2865  C   THR A 363     7541   3700   5728   -701   1254    460       C
ATOM   2866  O   THR A 363      -5.346 -27.007  20.075  1.00 41.15           O
ANISOU 2866  O   THR A 363     7030   3275   5330   -710   1288    399       O
ATOM   2867  CB  THR A 363      -6.013 -24.794  22.406  1.00 32.42           C
ANISOU 2867  CB  THR A 363     6088   2225   4006   -707   1258    437       C
ATOM   2868  OG1 THR A 363      -7.123 -24.814  21.501  1.00 39.37           O
ANISOU 2868  OG1 THR A 363     6925   3133   4900   -720   1331    357       O
ATOM   2869  CG2 THR A 363      -5.793 -23.374  22.867  1.00 33.29           C
ANISOU 2869  CG2 THR A 363     6239   2389   4022   -705   1208    436       C
ATOM   2870  N   SER A 364      -4.830 -27.725  22.158  1.00 42.01           N
ANISOU 2870  N   SER A 364     7247   3297   5419   -693   1261    525       N
ATOM   2871  CA  SER A 364      -4.936 -29.133  21.797  1.00 43.51           C
ANISOU 2871  CA  SER A 364     7404   3427   5700   -694   1305    528       C
ATOM   2872  C   SER A 364      -6.324 -29.519  21.305  1.00 46.68           C
ANISOU 2872  C   SER A 364     7786   3835   6114   -708   1406    457       C
ATOM   2873  O   SER A 364      -6.485 -30.620  20.769  1.00 37.95           O
ANISOU 2873  O   SER A 364     6641   2692   5086   -710   1450    442       O
ATOM   2874  CB  SER A 364      -4.552 -30.013  22.986  1.00 37.38           C
ANISOU 2874  CB  SER A 364     6684   2580   4941   -682   1295    614       C
ATOM   2875  OG  SER A 364      -5.321 -29.688  24.132  1.00 46.44           O
ANISOU 2875  OG  SER A 364     7906   3725   6013   -684   1327    632       O
ATOM   2876  N   ASP A 365      -7.325 -28.652  21.462  1.00 43.13           N
ANISOU 2876  N   ASP A 365     7362   3433   5592   -716   1443    413       N
ATOM   2877  CA  ASP A 365      -8.664 -28.924  20.961  1.00 39.18           C
ANISOU 2877  CA  ASP A 365     6840   2945   5101   -729   1538    343       C
ATOM   2878  C   ASP A 365      -8.983 -28.148  19.686  1.00 39.47           C
ANISOU 2878  C   ASP A 365     6811   3054   5131   -739   1546    262       C
ATOM   2879  O   ASP A 365     -10.157 -28.007  19.327  1.00 38.43           O
ANISOU 2879  O   ASP A 365     6667   2950   4985   -749   1618    200       O
ATOM   2880  CB  ASP A 365      -9.704 -28.639  22.043  1.00 41.49           C
ANISOU 2880  CB  ASP A 365     7208   3233   5325   -732   1586    347       C
ATOM   2881  CG  ASP A 365      -9.736 -27.183  22.471  1.00 42.52           C
ANISOU 2881  CG  ASP A 365     7378   3419   5358   -732   1545    340       C
ATOM   2882  OD1 ASP A 365      -8.859 -26.389  22.049  1.00 43.02           O
ANISOU 2882  OD1 ASP A 365     7418   3523   5405   -729   1473    342       O
ATOM   2883  OD2 ASP A 365     -10.665 -26.839  23.227  1.00 41.01           O
ANISOU 2883  OD2 ASP A 365     7243   3231   5109   -736   1587    331       O
ATOM   2884  N   GLY A 366      -7.966 -27.634  19.000  1.00 40.26           N
ANISOU 2884  N   GLY A 366     6868   3186   5242   -736   1475    262       N
ATOM   2885  CA  GLY A 366      -8.182 -26.955  17.743  1.00 37.70           C
ANISOU 2885  CA  GLY A 366     6477   2930   4916   -744   1480    189       C
ATOM   2886  C   GLY A 366      -8.537 -25.488  17.838  1.00 39.89           C
ANISOU 2886  C   GLY A 366     6778   3277   5104   -748   1460    161       C
ATOM   2887  O   GLY A 366      -9.108 -24.951  16.883  1.00 34.37           O
ANISOU 2887  O   GLY A 366     6029   2634   4395   -757   1488     93       O
ATOM   2888  N   GLY A 367      -8.231 -24.824  18.956  1.00 40.92           N
ANISOU 2888  N   GLY A 367     6979   3403   5165   -741   1416    210       N
ATOM   2889  CA  GLY A 367      -8.475 -23.407  19.109  1.00 36.95           C
ANISOU 2889  CA  GLY A 367     6503   2962   4574   -743   1392    185       C
ATOM   2890  C   GLY A 367      -7.207 -22.583  18.981  1.00 32.17           C
ANISOU 2890  C   GLY A 367     5889   2386   3946   -735   1297    212       C
ATOM   2891  O   GLY A 367      -6.129 -23.082  18.649  1.00 30.31           O
ANISOU 2891  O   GLY A 367     5621   2128   3769   -728   1247    246       O
ATOM   2892  N   VAL A 368      -7.353 -21.283  19.242  1.00 28.31           N
ANISOU 2892  N   VAL A 368     5432   1950   3374   -736   1271    194       N
ATOM   2893  CA  VAL A 368      -6.265 -20.321  19.107  1.00 32.18           C
ANISOU 2893  CA  VAL A 368     5917   2479   3832   -730   1185    210       C
ATOM   2894  C   VAL A 368      -5.934 -19.746  20.479  1.00 36.72           C
ANISOU 2894  C   VAL A 368     6577   3042   4332   -723   1144    262       C
ATOM   2895  O   VAL A 368      -6.798 -19.648  21.356  1.00 33.86           O
ANISOU 2895  O   VAL A 368     6276   2667   3922   -726   1186    261       O
ATOM   2896  CB  VAL A 368      -6.612 -19.188  18.110  1.00 34.07           C
ANISOU 2896  CB  VAL A 368     6112   2796   4035   -738   1184    140       C
ATOM   2897  CG1 VAL A 368      -6.693 -19.725  16.687  1.00 27.62           C
ANISOU 2897  CG1 VAL A 368     5203   1995   3294   -744   1211     94       C
ATOM   2898  CG2 VAL A 368      -7.921 -18.513  18.496  1.00 31.11           C
ANISOU 2898  CG2 VAL A 368     5779   2449   3593   -746   1240     95       C
ATOM   2899  N   TYR A 369      -4.668 -19.372  20.666  1.00 36.87           N
ANISOU 2899  N   TYR A 369     6601   3065   4342   -712   1061    306       N
ATOM   2900  CA  TYR A 369      -4.259 -18.756  21.922  1.00 40.26           C
ANISOU 2900  CA  TYR A 369     7109   3491   4698   -705   1017    353       C
ATOM   2901  C   TYR A 369      -3.162 -17.730  21.675  1.00 30.02           C
ANISOU 2901  C   TYR A 369     5800   2240   3367   -699    933    358       C
ATOM   2902  O   TYR A 369      -2.395 -17.833  20.712  1.00 34.54           O
ANISOU 2902  O   TYR A 369     6307   2825   3992   -695    898    353       O
ATOM   2903  CB  TYR A 369      -3.769 -19.802  22.923  1.00 36.13           C
ANISOU 2903  CB  TYR A 369     6625   2897   4205   -695   1008    433       C
ATOM   2904  CG  TYR A 369      -4.035 -19.455  24.374  1.00 35.41           C
ANISOU 2904  CG  TYR A 369     6626   2792   4037   -693   1007    468       C
ATOM   2905  CD1 TYR A 369      -2.995 -19.128  25.234  1.00 41.74           C
ANISOU 2905  CD1 TYR A 369     7470   3588   4802   -681    937    529       C
ATOM   2906  CD2 TYR A 369      -5.325 -19.474  24.883  1.00 37.88           C
ANISOU 2906  CD2 TYR A 369     6981   3096   4314   -702   1078    439       C
ATOM   2907  CE1 TYR A 369      -3.232 -18.833  26.564  1.00 43.04           C
ANISOU 2907  CE1 TYR A 369     7718   3741   4896   -681    937    560       C
ATOM   2908  CE2 TYR A 369      -5.572 -19.191  26.214  1.00 40.78           C
ANISOU 2908  CE2 TYR A 369     7433   3448   4614   -702   1079    471       C
ATOM   2909  CZ  TYR A 369      -4.522 -18.862  27.046  1.00 46.69           C
ANISOU 2909  CZ  TYR A 369     8223   4193   5326   -691   1008    530       C
ATOM   2910  OH  TYR A 369      -4.769 -18.566  28.368  1.00 51.12           O
ANISOU 2910  OH  TYR A 369     8866   4739   5817   -692   1008    559       O
ATOM   2911  N   TRP A 370      -3.093 -16.740  22.565  1.00 32.67           N
ANISOU 2911  N   TRP A 370     6200   2598   3615   -698    902    367       N
ATOM   2912  CA  TRP A 370      -2.073 -15.700  22.494  1.00 38.86           C
ANISOU 2912  CA  TRP A 370     6985   3425   4356   -692    822    372       C
ATOM   2913  C   TRP A 370      -2.059 -14.934  23.806  1.00 38.88           C
ANISOU 2913  C   TRP A 370     7074   3431   4268   -691    796    393       C
ATOM   2914  O   TRP A 370      -3.070 -14.886  24.516  1.00 34.60           O
ANISOU 2914  O   TRP A 370     6584   2876   3687   -699    847    380       O
ATOM   2915  CB  TRP A 370      -2.321 -14.725  21.328  1.00 34.11           C
ANISOU 2915  CB  TRP A 370     6331   2891   3739   -701    819    298       C
ATOM   2916  CG  TRP A 370      -3.726 -14.182  21.265  1.00 24.71           C
ANISOU 2916  CG  TRP A 370     5157   1728   2504   -714    884    234       C
ATOM   2917  CD1 TRP A 370      -4.300 -13.294  22.121  1.00 24.47           C
ANISOU 2917  CD1 TRP A 370     5195   1712   2392   -720    890    217       C
ATOM   2918  CD2 TRP A 370      -4.730 -14.507  20.293  1.00 29.99           C
ANISOU 2918  CD2 TRP A 370     5772   2410   3212   -724    953    178       C
ATOM   2919  NE1 TRP A 370      -5.600 -13.036  21.741  1.00 27.17           N
ANISOU 2919  NE1 TRP A 370     5528   2075   2721   -731    957    154       N
ATOM   2920  CE2 TRP A 370      -5.885 -13.764  20.617  1.00 26.49           C
ANISOU 2920  CE2 TRP A 370     5368   1991   2707   -733    997    130       C
ATOM   2921  CE3 TRP A 370      -4.767 -15.358  19.183  1.00 30.05           C
ANISOU 2921  CE3 TRP A 370     5702   2412   3303   -725    982    162       C
ATOM   2922  CZ2 TRP A 370      -7.061 -13.839  19.864  1.00 28.03           C
ANISOU 2922  CZ2 TRP A 370     5525   2206   2919   -742   1069     69       C
ATOM   2923  CZ3 TRP A 370      -5.939 -15.431  18.432  1.00 26.77           C
ANISOU 2923  CZ3 TRP A 370     5250   2020   2903   -736   1053     99       C
ATOM   2924  CH2 TRP A 370      -7.066 -14.678  18.778  1.00 27.82           C
ANISOU 2924  CH2 TRP A 370     5422   2178   2971   -744   1096     55       C
ATOM   2925  N   GLU A 371      -0.901 -14.345  24.115  1.00 31.29           N
ANISOU 2925  N   GLU A 371     6128   2487   3276   -682    718    425       N
ATOM   2926  CA  GLU A 371      -0.791 -13.420  25.239  1.00 38.62           C
ANISOU 2926  CA  GLU A 371     7133   3429   4115   -684    685    435       C
ATOM   2927  C   GLU A 371      -1.932 -12.416  25.209  1.00 37.58           C
ANISOU 2927  C   GLU A 371     7024   3333   3921   -700    723    363       C
ATOM   2928  O   GLU A 371      -2.320 -11.928  24.145  1.00 35.72           O
ANISOU 2928  O   GLU A 371     6738   3139   3694   -707    738    302       O
ATOM   2929  CB  GLU A 371       0.544 -12.671  25.193  1.00 29.43           C
ANISOU 2929  CB  GLU A 371     5962   2296   2925   -676    595    453       C
ATOM   2930  CG  GLU A 371       1.766 -13.487  25.608  1.00 37.19           C
ANISOU 2930  CG  GLU A 371     6942   3239   3947   -658    547    535       C
ATOM   2931  CD  GLU A 371       2.030 -14.698  24.723  1.00 41.11           C
ANISOU 2931  CD  GLU A 371     7367   3702   4549   -649    566    555       C
ATOM   2932  OE1 GLU A 371       2.515 -15.705  25.270  1.00 40.48           O
ANISOU 2932  OE1 GLU A 371     7298   3571   4513   -637    560    623       O
ATOM   2933  OE2 GLU A 371       1.764 -14.654  23.495  1.00 38.57           O
ANISOU 2933  OE2 GLU A 371     6981   3406   4270   -655    586    504       O
ATOM   2934  N   GLY A 372      -2.481 -12.123  26.386  1.00 38.39           N
ANISOU 2934  N   GLY A 372     7204   3419   3963   -705    740    369       N
ATOM   2935  CA  GLY A 372      -3.535 -11.137  26.503  1.00 30.23           C
ANISOU 2935  CA  GLY A 372     6200   2412   2872   -720    773    304       C
ATOM   2936  C   GLY A 372      -4.912 -11.616  26.102  1.00 35.75           C
ANISOU 2936  C   GLY A 372     6883   3102   3599   -727    862    262       C
ATOM   2937  O   GLY A 372      -5.854 -10.820  26.118  1.00 36.61           O
ANISOU 2937  O   GLY A 372     7011   3232   3667   -738    894    204       O
ATOM   2938  N   ILE A 373      -5.074 -12.893  25.750  1.00 28.62           N
ANISOU 2938  N   ILE A 373     5944   2163   2767   -722    904    287       N
ATOM   2939  CA  ILE A 373      -6.406 -13.366  25.396  1.00 26.36           C
ANISOU 2939  CA  ILE A 373     5644   1867   2507   -730    991    245       C
ATOM   2940  C   ILE A 373      -7.333 -13.381  26.617  1.00 32.07           C
ANISOU 2940  C   ILE A 373     6446   2557   3184   -736   1036    249       C
ATOM   2941  O   ILE A 373      -8.561 -13.309  26.464  1.00 31.74           O
ANISOU 2941  O   ILE A 373     6407   2517   3137   -744   1104    199       O
ATOM   2942  CB  ILE A 373      -6.278 -14.750  24.724  1.00 26.62           C
ANISOU 2942  CB  ILE A 373     5618   1866   2632   -725   1021    270       C
ATOM   2943  CG1 ILE A 373      -7.523 -15.093  23.907  1.00 36.06           C
ANISOU 2943  CG1 ILE A 373     6771   3069   3863   -734   1103    210       C
ATOM   2944  CG2 ILE A 373      -5.999 -15.817  25.760  1.00 28.80           C
ANISOU 2944  CG2 ILE A 373     5938   2077   2929   -717   1025    344       C
ATOM   2945  CD1 ILE A 373      -7.396 -16.418  23.159  1.00 41.44           C
ANISOU 2945  CD1 ILE A 373     7389   3717   4638   -731   1132    225       C
ATOM   2946  N   ASP A 374      -6.775 -13.463  27.829  1.00 35.41           N
ANISOU 2946  N   ASP A 374     6934   2949   3572   -731   1002    308       N
ATOM   2947  CA  ASP A 374      -7.548 -13.330  29.073  1.00 42.62           C
ANISOU 2947  CA  ASP A 374     7928   3834   4432   -737   1036    313       C
ATOM   2948  C   ASP A 374      -8.701 -14.327  29.128  1.00 45.92           C
ANISOU 2948  C   ASP A 374     8348   4212   4888   -740   1124    306       C
ATOM   2949  O   ASP A 374      -9.825 -13.997  29.513  1.00 45.28           O
ANISOU 2949  O   ASP A 374     8304   4127   4774   -748   1178    266       O
ATOM   2950  CB  ASP A 374      -8.069 -11.904  29.246  1.00 54.08           C
ANISOU 2950  CB  ASP A 374     9412   5323   5814   -748   1029    252       C
ATOM   2951  CG  ASP A 374      -7.577 -11.264  30.515  1.00 62.80           C
ANISOU 2951  CG  ASP A 374    10593   6417   6850   -750    980    284       C
ATOM   2952  OD1 ASP A 374      -6.884 -10.228  30.427  1.00 69.15           O
ANISOU 2952  OD1 ASP A 374    11399   7258   7619   -753    917    269       O
ATOM   2953  OD2 ASP A 374      -7.863 -11.813  31.601  1.00 61.75           O
ANISOU 2953  OD2 ASP A 374    10519   6241   6701   -750   1006    325       O
ATOM   2954  N   GLU A 375      -8.419 -15.560  28.723  1.00 44.08           N
ANISOU 2954  N   GLU A 375     8073   3948   4729   -733   1141    342       N
ATOM   2955  CA  GLU A 375      -9.427 -16.608  28.643  1.00 47.20           C
ANISOU 2955  CA  GLU A 375     8460   4305   5171   -735   1224    334       C
ATOM   2956  C   GLU A 375      -8.807 -17.868  29.221  1.00 50.22           C
ANISOU 2956  C   GLU A 375     8854   4629   5598   -726   1217    415       C
ATOM   2957  O   GLU A 375      -7.756 -18.318  28.722  1.00 53.94           O
ANISOU 2957  O   GLU A 375     9280   5096   6120   -717   1170    451       O
ATOM   2958  CB  GLU A 375      -9.883 -16.851  27.204  1.00 54.53           C
ANISOU 2958  CB  GLU A 375     9304   5258   6159   -739   1263    278       C
ATOM   2959  CG  GLU A 375     -11.112 -16.082  26.816  1.00 59.73           C
ANISOU 2959  CG  GLU A 375     9959   5951   6785   -749   1315    198       C
ATOM   2960  CD  GLU A 375     -11.891 -16.761  25.716  1.00 62.35           C
ANISOU 2960  CD  GLU A 375    10223   6286   7182   -754   1382    153       C
ATOM   2961  OE1 GLU A 375     -12.004 -18.003  25.755  1.00 60.53           O
ANISOU 2961  OE1 GLU A 375     9980   6009   7010   -751   1421    182       O
ATOM   2962  OE2 GLU A 375     -12.390 -16.056  24.816  1.00 60.94           O
ANISOU 2962  OE2 GLU A 375    10001   6155   6997   -759   1397     87       O
ATOM   2963  N   PRO A 376      -9.393 -18.454  30.261  1.00 40.97           N
ANISOU 2963  N   PRO A 376     7742   3411   4415   -726   1260    445       N
ATOM   2964  CA  PRO A 376      -8.836 -19.691  30.818  1.00 41.53           C
ANISOU 2964  CA  PRO A 376     7824   3424   4532   -717   1255    523       C
ATOM   2965  C   PRO A 376      -9.042 -20.869  29.880  1.00 44.25           C
ANISOU 2965  C   PRO A 376     8101   3741   4971   -716   1300    516       C
ATOM   2966  O   PRO A 376     -10.058 -20.968  29.188  1.00 46.97           O
ANISOU 2966  O   PRO A 376     8413   4095   5337   -724   1365    454       O
ATOM   2967  CB  PRO A 376      -9.622 -19.884  32.122  1.00 42.96           C
ANISOU 2967  CB  PRO A 376     8087   3568   4668   -720   1299    544       C
ATOM   2968  CG  PRO A 376     -10.210 -18.559  32.432  1.00 48.26           C
ANISOU 2968  CG  PRO A 376     8799   4279   5257   -730   1300    490       C
ATOM   2969  CD  PRO A 376     -10.430 -17.862  31.122  1.00 41.30           C
ANISOU 2969  CD  PRO A 376     7852   3451   4389   -735   1301    416       C
ATOM   2970  N   LEU A 377      -8.066 -21.771  29.869  1.00 43.75           N
ANISOU 2970  N   LEU A 377     8014   3641   4966   -705   1265    580       N
ATOM   2971  CA  LEU A 377      -8.196 -23.041  29.168  1.00 42.97           C
ANISOU 2971  CA  LEU A 377     7860   3503   4962   -704   1307    583       C
ATOM   2972  C   LEU A 377      -8.638 -24.126  30.139  1.00 45.59           C
ANISOU 2972  C   LEU A 377     8240   3768   5312   -701   1354    633       C
ATOM   2973  O   LEU A 377      -8.146 -24.194  31.268  1.00 46.50           O
ANISOU 2973  O   LEU A 377     8415   3860   5394   -694   1321    699       O
ATOM   2974  CB  LEU A 377      -6.878 -23.447  28.508  1.00 40.52           C
ANISOU 2974  CB  LEU A 377     7493   3187   4717   -693   1243    621       C
ATOM   2975  CG  LEU A 377      -6.505 -22.518  27.353  1.00 42.40           C
ANISOU 2975  CG  LEU A 377     7672   3489   4951   -696   1205    566       C
ATOM   2976  CD1 LEU A 377      -5.057 -22.711  26.995  1.00 40.44           C
ANISOU 2976  CD1 LEU A 377     7383   3235   4747   -684   1127    614       C
ATOM   2977  CD2 LEU A 377      -7.402 -22.806  26.162  1.00 44.00           C
ANISOU 2977  CD2 LEU A 377     7810   3705   5202   -707   1271    492       C
ATOM   2978  N   ALA A 378      -9.563 -24.972  29.690  1.00 48.18           N
ANISOU 2978  N   ALA A 378     8543   4070   5694   -707   1433    599       N
ATOM   2979  CA  ALA A 378     -10.045 -26.065  30.519  1.00 49.26           C
ANISOU 2979  CA  ALA A 378     8720   4142   5854   -706   1485    641       C
ATOM   2980  C   ALA A 378      -8.877 -26.940  30.967  1.00 48.64           C
ANISOU 2980  C   ALA A 378     8644   4015   5822   -692   1433    730       C
ATOM   2981  O   ALA A 378      -7.882 -27.078  30.246  1.00 41.83           O
ANISOU 2981  O   ALA A 378     7726   3158   5008   -686   1380    745       O
ATOM   2982  CB  ALA A 378     -11.063 -26.916  29.757  1.00 47.36           C
ANISOU 2982  CB  ALA A 378     8436   3882   5677   -713   1572    589       C
ATOM   2983  N   PRO A 379      -8.961 -27.528  32.161  1.00 49.96           N
ANISOU 2983  N   PRO A 379     8874   4133   5975   -688   1446    792       N
ATOM   2984  CA  PRO A 379      -7.969 -28.533  32.550  1.00 51.19           C
ANISOU 2984  CA  PRO A 379     9028   4235   6186   -675   1408    878       C
ATOM   2985  C   PRO A 379      -7.881 -29.602  31.473  1.00 41.17           C
ANISOU 2985  C   PRO A 379     7685   2935   5023   -674   1435    861       C
ATOM   2986  O   PRO A 379      -8.896 -30.099  30.983  1.00 49.02           O
ANISOU 2986  O   PRO A 379     8658   3917   6050   -683   1514    808       O
ATOM   2987  CB  PRO A 379      -8.514 -29.087  33.873  1.00 55.17           C
ANISOU 2987  CB  PRO A 379     9609   4692   6663   -674   1448    927       C
ATOM   2988  CG  PRO A 379      -9.929 -28.582  33.974  1.00 54.09           C
ANISOU 2988  CG  PRO A 379     9502   4576   6475   -687   1521    856       C
ATOM   2989  CD  PRO A 379      -9.972 -27.307  33.207  1.00 46.72           C
ANISOU 2989  CD  PRO A 379     8538   3713   5499   -694   1497    787       C
ATOM   2990  N   GLY A 380      -6.663 -29.911  31.060  1.00 38.88           N
ANISOU 2990  N   GLY A 380     7353   2634   4786   -664   1370    902       N
ATOM   2991  CA  GLY A 380      -6.506 -30.839  29.961  1.00 40.90           C
ANISOU 2991  CA  GLY A 380     7535   2863   5141   -665   1390    880       C
ATOM   2992  C   GLY A 380      -6.006 -30.197  28.687  1.00 48.89           C
ANISOU 2992  C   GLY A 380     8476   3927   6173   -667   1351    828       C
ATOM   2993  O   GLY A 380      -5.192 -30.786  27.972  1.00 55.97           O
ANISOU 2993  O   GLY A 380     9316   4803   7145   -661   1320    841       O
ATOM   2994  N   VAL A 381      -6.473 -28.986  28.385  1.00 47.57           N
ANISOU 2994  N   VAL A 381     8310   3826   5939   -676   1352    767       N
ATOM   2995  CA  VAL A 381      -6.127 -28.353  27.115  1.00 48.20           C
ANISOU 2995  CA  VAL A 381     8320   3958   6036   -680   1323    710       C
ATOM   2996  C   VAL A 381      -4.661 -27.929  27.132  1.00 51.07           C
ANISOU 2996  C   VAL A 381     8671   4334   6398   -667   1224    762       C
ATOM   2997  O   VAL A 381      -4.203 -27.257  28.064  1.00 50.07           O
ANISOU 2997  O   VAL A 381     8599   4222   6205   -660   1176    807       O
ATOM   2998  CB  VAL A 381      -7.057 -27.162  26.841  1.00 46.62           C
ANISOU 2998  CB  VAL A 381     8127   3824   5761   -692   1352    635       C
ATOM   2999  CG1 VAL A 381      -6.703 -26.509  25.516  1.00 38.50           C
ANISOU 2999  CG1 VAL A 381     7027   2852   4750   -696   1323    577       C
ATOM   3000  CG2 VAL A 381      -8.511 -27.615  26.846  1.00 46.33           C
ANISOU 3000  CG2 VAL A 381     8102   3773   5728   -703   1452    586       C
ATOM   3001  N   THR A 382      -3.916 -28.319  26.098  1.00 43.20           N
ANISOU 3001  N   THR A 382     7604   3334   5478   -664   1194    754       N
ATOM   3002  CA  THR A 382      -2.494 -28.021  26.013  1.00 40.27           C
ANISOU 3002  CA  THR A 382     7212   2970   5120   -650   1102    801       C
ATOM   3003  C   THR A 382      -2.228 -27.059  24.858  1.00 39.52           C
ANISOU 3003  C   THR A 382     7059   2940   5016   -655   1071    738       C
ATOM   3004  O   THR A 382      -3.064 -26.886  23.967  1.00 42.85           O
ANISOU 3004  O   THR A 382     7444   3392   5445   -669   1122    661       O
ATOM   3005  CB  THR A 382      -1.670 -29.306  25.853  1.00 40.53           C
ANISOU 3005  CB  THR A 382     7212   2936   5252   -640   1082    854       C
ATOM   3006  OG1 THR A 382      -1.906 -29.896  24.564  1.00 42.04           O
ANISOU 3006  OG1 THR A 382     7331   3121   5521   -648   1118    794       O
ATOM   3007  CG2 THR A 382      -2.057 -30.299  26.932  1.00 43.89           C
ANISOU 3007  CG2 THR A 382     7693   3297   5688   -636   1122    911       C
ATOM   3008  N   ILE A 383      -1.046 -26.439  24.877  1.00 34.35           N
ANISOU 3008  N   ILE A 383     6397   2308   4347   -644    988    772       N
ATOM   3009  CA  ILE A 383      -0.717 -25.317  23.993  1.00 37.83           C
ANISOU 3009  CA  ILE A 383     6796   2816   4761   -647    949    720       C
ATOM   3010  C   ILE A 383       0.500 -25.654  23.142  1.00 44.60           C
ANISOU 3010  C   ILE A 383     7586   3663   5697   -637    891    736       C
ATOM   3011  O   ILE A 383       1.573 -25.963  23.677  1.00 52.61           O
ANISOU 3011  O   ILE A 383     8610   4645   6732   -621    833    809       O
ATOM   3012  CB  ILE A 383      -0.447 -24.025  24.780  1.00 37.94           C
ANISOU 3012  CB  ILE A 383     6865   2878   4671   -643    903    735       C
ATOM   3013  CG1 ILE A 383      -1.718 -23.535  25.454  1.00 46.39           C
ANISOU 3013  CG1 ILE A 383     7997   3967   5661   -655    961    702       C
ATOM   3014  CG2 ILE A 383       0.091 -22.940  23.836  1.00 40.95           C
ANISOU 3014  CG2 ILE A 383     7200   3325   5033   -644    854    689       C
ATOM   3015  CD1 ILE A 383      -2.715 -23.026  24.466  1.00 52.46           C
ANISOU 3015  CD1 ILE A 383     8729   4782   6421   -671   1012    610       C
ATOM   3016  N   THR A 384       0.347 -25.544  21.823  1.00 43.40           N
ANISOU 3016  N   THR A 384     7364   3540   5585   -646    903    668       N
ATOM   3017  CA  THR A 384       1.473 -25.495  20.899  1.00 41.77           C
ANISOU 3017  CA  THR A 384     7092   3343   5436   -639    842    667       C
ATOM   3018  C   THR A 384       1.735 -24.039  20.530  1.00 41.95           C
ANISOU 3018  C   THR A 384     7106   3442   5389   -640    799    630       C
ATOM   3019  O   THR A 384       0.824 -23.339  20.078  1.00 40.30           O
ANISOU 3019  O   THR A 384     6893   3285   5135   -654    839    563       O
ATOM   3020  CB  THR A 384       1.193 -26.319  19.640  1.00 46.48           C
ANISOU 3020  CB  THR A 384     7615   3923   6120   -648    881    612       C
ATOM   3021  OG1 THR A 384       0.914 -27.680  20.003  1.00 49.25           O
ANISOU 3021  OG1 THR A 384     7979   4203   6532   -648    925    642       O
ATOM   3022  CG2 THR A 384       2.391 -26.287  18.707  1.00 46.09           C
ANISOU 3022  CG2 THR A 384     7500   3880   6131   -640    815    611       C
ATOM   3023  N   SER A 385       2.974 -23.587  20.728  1.00 38.79           N
ANISOU 3023  N   SER A 385     6705   3051   4983   -624    721    675       N
ATOM   3024  CA  SER A 385       3.336 -22.207  20.437  1.00 42.92           C
ANISOU 3024  CA  SER A 385     7225   3645   5439   -623    676    645       C
ATOM   3025  C   SER A 385       3.455 -21.984  18.929  1.00 38.35           C
ANISOU 3025  C   SER A 385     6563   3102   4907   -631    671    579       C
ATOM   3026  O   SER A 385       3.349 -22.905  18.113  1.00 35.10           O
ANISOU 3026  O   SER A 385     6096   2660   4581   -636    697    557       O
ATOM   3027  CB  SER A 385       4.653 -21.834  21.121  1.00 41.85           C
ANISOU 3027  CB  SER A 385     7113   3508   5280   -603    597    714       C
ATOM   3028  OG  SER A 385       5.767 -22.382  20.428  1.00 41.40           O
ANISOU 3028  OG  SER A 385     6992   3425   5313   -590    552    736       O
ATOM   3029  N   TRP A 386       3.687 -20.725  18.559  1.00 35.67           N
ANISOU 3029  N   TRP A 386     6215   2829   4507   -632    636    544       N
ATOM   3030  CA  TRP A 386       3.890 -20.405  17.156  1.00 36.06           C
ANISOU 3030  CA  TRP A 386     6188   2919   4596   -638    624    484       C
ATOM   3031  C   TRP A 386       5.226 -20.916  16.626  1.00 40.29           C
ANISOU 3031  C   TRP A 386     6669   3425   5217   -623    565    516       C
ATOM   3032  O   TRP A 386       5.428 -20.925  15.405  1.00 36.03           O
ANISOU 3032  O   TRP A 386     6058   2904   4729   -628    558    468       O
ATOM   3033  CB  TRP A 386       3.787 -18.895  16.959  1.00 40.63           C
ANISOU 3033  CB  TRP A 386     6777   3577   5084   -643    601    442       C
ATOM   3034  CG  TRP A 386       5.008 -18.181  17.396  1.00 39.37           C
ANISOU 3034  CG  TRP A 386     6638   3434   4887   -626    522    483       C
ATOM   3035  CD1 TRP A 386       5.381 -17.890  18.677  1.00 38.41           C
ANISOU 3035  CD1 TRP A 386     6590   3303   4702   -616    492    540       C
ATOM   3036  CD2 TRP A 386       6.040 -17.677  16.549  1.00 35.90           C
ANISOU 3036  CD2 TRP A 386     6144   3025   4469   -618    463    471       C
ATOM   3037  NE1 TRP A 386       6.585 -17.230  18.679  1.00 38.43           N
ANISOU 3037  NE1 TRP A 386     6588   3330   4683   -601    418    562       N
ATOM   3038  CE2 TRP A 386       7.011 -17.086  17.382  1.00 38.65           C
ANISOU 3038  CE2 TRP A 386     6539   3383   4764   -602    400    521       C
ATOM   3039  CE3 TRP A 386       6.238 -17.665  15.162  1.00 37.20           C
ANISOU 3039  CE3 TRP A 386     6227   3214   4695   -623    458    420       C
ATOM   3040  CZ2 TRP A 386       8.161 -16.488  16.876  1.00 34.77           C
ANISOU 3040  CZ2 TRP A 386     6014   2921   4275   -590    335    521       C
ATOM   3041  CZ3 TRP A 386       7.383 -17.072  14.659  1.00 33.52           C
ANISOU 3041  CZ3 TRP A 386     5727   2776   4235   -611    392    421       C
ATOM   3042  CH2 TRP A 386       8.330 -16.494  15.514  1.00 37.74           C
ANISOU 3042  CH2 TRP A 386     6309   3316   4713   -595    332    471       C
ATOM   3043  N   LYS A 387       6.135 -21.342  17.505  1.00 44.35           N
ANISOU 3043  N   LYS A 387     7213   3893   5746   -604    524    594       N
ATOM   3044  CA  LYS A 387       7.388 -21.972  17.100  1.00 44.43           C
ANISOU 3044  CA  LYS A 387     7173   3863   5845   -588    472    631       C
ATOM   3045  C   LYS A 387       7.243 -23.475  16.855  1.00 50.79           C
ANISOU 3045  C   LYS A 387     7948   4595   6753   -590    504    645       C
ATOM   3046  O   LYS A 387       8.259 -24.171  16.714  1.00 51.15           O
ANISOU 3046  O   LYS A 387     7962   4595   6878   -576    463    687       O
ATOM   3047  CB  LYS A 387       8.465 -21.732  18.162  1.00 48.84           C
ANISOU 3047  CB  LYS A 387     7776   4410   6372   -564    414    712       C
ATOM   3048  CG  LYS A 387       8.572 -20.299  18.653  1.00 50.79           C
ANISOU 3048  CG  LYS A 387     8072   4725   6501   -562    383    703       C
ATOM   3049  CD  LYS A 387      10.020 -19.830  18.661  1.00 58.32           C
ANISOU 3049  CD  LYS A 387     9013   5693   7452   -539    308    739       C
ATOM   3050  CE  LYS A 387      10.504 -19.517  17.251  1.00 62.88           C
ANISOU 3050  CE  LYS A 387     9510   6301   8081   -541    286    684       C
ATOM   3051  NZ  LYS A 387      11.944 -19.141  17.219  1.00 63.94           N
ANISOU 3051  NZ  LYS A 387     9630   6446   8219   -516    217    718       N
ATOM   3052  N   ASN A 388       6.013 -23.984  16.802  1.00 43.65           N
ANISOU 3052  N   ASN A 388     7057   3680   5849   -608    576    609       N
ATOM   3053  CA  ASN A 388       5.753 -25.420  16.700  1.00 47.83           C
ANISOU 3053  CA  ASN A 388     7572   4140   6461   -612    614    619       C
ATOM   3054  C   ASN A 388       6.459 -26.164  17.829  1.00 54.27           C
ANISOU 3054  C   ASN A 388     8429   4889   7301   -594    585    714       C
ATOM   3055  O   ASN A 388       7.215 -27.113  17.613  1.00 60.64           O
ANISOU 3055  O   ASN A 388     9206   5640   8194   -585    558    747       O
ATOM   3056  CB  ASN A 388       6.165 -25.964  15.331  1.00 49.46           C
ANISOU 3056  CB  ASN A 388     7698   4338   6757   -617    604    573       C
ATOM   3057  CG  ASN A 388       5.216 -27.026  14.820  1.00 57.74           C
ANISOU 3057  CG  ASN A 388     8729   5358   7853   -632    681    527       C
ATOM   3058  OD1 ASN A 388       4.020 -26.996  15.114  1.00 58.39           O
ANISOU 3058  OD1 ASN A 388     8841   5453   7891   -645    751    500       O
ATOM   3059  ND2 ASN A 388       5.744 -27.976  14.054  1.00 62.02           N
ANISOU 3059  ND2 ASN A 388     9222   5860   8483   -631    672    516       N
ATOM   3060  N   LYS A 389       6.217 -25.700  19.051  1.00 59.05           N
ANISOU 3060  N   LYS A 389     9107   5504   7827   -589    588    759       N
ATOM   3061  CA  LYS A 389       6.827 -26.249  20.250  1.00 65.34           C
ANISOU 3061  CA  LYS A 389     9950   6248   8629   -571    561    852       C
ATOM   3062  C   LYS A 389       5.754 -26.426  21.310  1.00 65.64           C
ANISOU 3062  C   LYS A 389    10061   6272   8607   -579    619    868       C
ATOM   3063  O   LYS A 389       4.847 -25.597  21.427  1.00 60.38           O
ANISOU 3063  O   LYS A 389     9425   5656   7860   -592    653    821       O
ATOM   3064  CB  LYS A 389       7.930 -25.332  20.802  1.00 71.94           C
ANISOU 3064  CB  LYS A 389    10805   7117   9414   -550    490    902       C
ATOM   3065  CG  LYS A 389       9.298 -25.462  20.147  1.00 76.90           C
ANISOU 3065  CG  LYS A 389    11370   7733  10116   -532    426    923       C
ATOM   3066  CD  LYS A 389      10.256 -24.417  20.722  1.00 78.64           C
ANISOU 3066  CD  LYS A 389    11616   7997  10265   -511    367    962       C
ATOM   3067  CE  LYS A 389      11.713 -24.859  20.645  1.00 80.16           C
ANISOU 3067  CE  LYS A 389    11770   8157  10531   -484    310   1023       C
ATOM   3068  NZ  LYS A 389      12.185 -25.067  19.247  1.00 81.38           N
ANISOU 3068  NZ  LYS A 389    11837   8307  10777   -485    294    975       N
ATOM   3069  N   GLU A 390       5.858 -27.508  22.077  1.00 66.41           N
ANISOU 3069  N   GLU A 390    10186   6301   8744   -572    628    933       N
ATOM   3070  CA  GLU A 390       5.056 -27.627  23.283  1.00 69.06           C
ANISOU 3070  CA  GLU A 390    10598   6623   9019   -575    671    965       C
ATOM   3071  C   GLU A 390       5.376 -26.457  24.199  1.00 69.34           C
ANISOU 3071  C   GLU A 390    10689   6707   8951   -566    631    995       C
ATOM   3072  O   GLU A 390       6.539 -26.230  24.544  1.00 71.58           O
ANISOU 3072  O   GLU A 390    10971   6992   9233   -546    565   1052       O
ATOM   3073  CB  GLU A 390       5.339 -28.951  23.986  1.00 71.84           C
ANISOU 3073  CB  GLU A 390    10970   6895   9433   -565    675   1041       C
ATOM   3074  CG  GLU A 390       4.442 -29.207  25.185  1.00 80.03           C
ANISOU 3074  CG  GLU A 390    12082   7910  10415   -570    725   1071       C
ATOM   3075  CD  GLU A 390       3.187 -29.975  24.819  1.00 84.48           C
ANISOU 3075  CD  GLU A 390    12643   8448  11009   -588    812   1017       C
ATOM   3076  OE1 GLU A 390       3.072 -31.151  25.226  1.00 85.48           O
ANISOU 3076  OE1 GLU A 390    12784   8508  11188   -585    840   1057       O
ATOM   3077  OE2 GLU A 390       2.323 -29.407  24.115  1.00 84.91           O
ANISOU 3077  OE2 GLU A 390    12679   8548  11034   -604    855    934       O
ATOM   3078  N   TRP A 391       4.351 -25.702  24.579  1.00 68.45           N
ANISOU 3078  N   TRP A 391    10624   6636   8750   -579    671    954       N
ATOM   3079  CA  TRP A 391       4.540 -24.465  25.321  1.00 73.31           C
ANISOU 3079  CA  TRP A 391    11292   7305   9257   -575    636    963       C
ATOM   3080  C   TRP A 391       3.626 -24.456  26.534  1.00 78.09           C
ANISOU 3080  C   TRP A 391    11979   7900   9791   -582    680    981       C
ATOM   3081  O   TRP A 391       2.431 -24.745  26.416  1.00 75.28           O
ANISOU 3081  O   TRP A 391    11632   7535   9434   -598    750    937       O
ATOM   3082  CB  TRP A 391       4.255 -23.248  24.431  1.00 68.82           C
ANISOU 3082  CB  TRP A 391    10697   6810   8641   -587    632    880       C
ATOM   3083  CG  TRP A 391       4.446 -21.915  25.109  1.00 67.06           C
ANISOU 3083  CG  TRP A 391    10529   6646   8307   -585    593    879       C
ATOM   3084  CD1 TRP A 391       5.569 -21.138  25.088  1.00 62.57           C
ANISOU 3084  CD1 TRP A 391     9954   6113   7708   -572    521    896       C
ATOM   3085  CD2 TRP A 391       3.480 -21.201  25.892  1.00 66.78           C
ANISOU 3085  CD2 TRP A 391    10562   6637   8173   -597    626    854       C
ATOM   3086  NE1 TRP A 391       5.364 -19.990  25.812  1.00 62.28           N
ANISOU 3086  NE1 TRP A 391     9979   6125   7560   -576    504    882       N
ATOM   3087  CE2 TRP A 391       4.089 -20.003  26.315  1.00 65.28           C
ANISOU 3087  CE2 TRP A 391    10406   6499   7898   -592    567    856       C
ATOM   3088  CE3 TRP A 391       2.160 -21.458  26.277  1.00 66.13           C
ANISOU 3088  CE3 TRP A 391    10517   6541   8069   -612    699    828       C
ATOM   3089  CZ2 TRP A 391       3.425 -19.066  27.107  1.00 64.18           C
ANISOU 3089  CZ2 TRP A 391    10335   6394   7655   -603    578    832       C
ATOM   3090  CZ3 TRP A 391       1.501 -20.525  27.060  1.00 66.59           C
ANISOU 3090  CZ3 TRP A 391    10642   6633   8024   -621    712    806       C
ATOM   3091  CH2 TRP A 391       2.133 -19.343  27.463  1.00 62.81           C
ANISOU 3091  CH2 TRP A 391    10196   6204   7467   -617    650    808       C
ATOM   3092  N   ARG A 392       4.186 -24.120  27.692  1.00 87.58           N
ANISOU 3092  N   ARG A 392    13239   9105  10932   -570    639   1045       N
ATOM   3093  CA  ARG A 392       3.386 -23.909  28.884  1.00103.16           C
ANISOU 3093  CA  ARG A 392    15294  11078  12825   -577    672   1058       C
ATOM   3094  C   ARG A 392       3.612 -22.499  29.422  1.00105.91           C
ANISOU 3094  C   ARG A 392    15690  11489  13062   -577    629   1045       C
ATOM   3095  O   ARG A 392       4.693 -21.926  29.235  1.00106.13           O
ANISOU 3095  O   ARG A 392    15699  11547  13079   -565    562   1060       O
ATOM   3096  CB  ARG A 392       3.709 -24.948  29.969  1.00115.58           C
ANISOU 3096  CB  ARG A 392    16905  12588  14423   -564    670   1151       C
ATOM   3097  CG  ARG A 392       5.159 -25.415  30.016  1.00123.83           C
ANISOU 3097  CG  ARG A 392    17918  13607  15523   -541    602   1228       C
ATOM   3098  CD  ARG A 392       5.961 -24.632  31.041  1.00128.52           C
ANISOU 3098  CD  ARG A 392    18565  14234  16033   -527    542   1279       C
ATOM   3099  NE  ARG A 392       7.238 -25.268  31.355  1.00130.85           N
ANISOU 3099  NE  ARG A 392    18842  14496  16380   -502    488   1368       N
ATOM   3100  CZ  ARG A 392       7.421 -26.127  32.353  1.00130.46           C
ANISOU 3100  CZ  ARG A 392    18827  14397  16346   -492    490   1451       C
ATOM   3101  NH1 ARG A 392       6.407 -26.460  33.139  1.00130.26           N
ANISOU 3101  NH1 ARG A 392    18858  14347  16287   -505    544   1456       N
ATOM   3102  NH2 ARG A 392       8.620 -26.654  32.566  1.00130.56           N
ANISOU 3102  NH2 ARG A 392    18816  14383  16407   -468    440   1530       N
ATOM   3103  N   PRO A 393       2.606 -21.905  30.074  1.00105.91           N
ANISOU 3103  N   PRO A 393    15752  11510  12980   -592    667   1012       N
ATOM   3104  CA  PRO A 393       2.762 -20.523  30.567  1.00107.47           C
ANISOU 3104  CA  PRO A 393    15995  11766  13071   -595    627    990       C
ATOM   3105  C   PRO A 393       3.945 -20.332  31.496  1.00113.46           C
ANISOU 3105  C   PRO A 393    16790  12527  13794   -578    556   1065       C
ATOM   3106  O   PRO A 393       4.450 -19.207  31.606  1.00110.58           O
ANISOU 3106  O   PRO A 393    16441  12212  13360   -578    505   1046       O
ATOM   3107  CB  PRO A 393       1.431 -20.251  31.286  1.00104.67           C
ANISOU 3107  CB  PRO A 393    15705  11412  12652   -612    689    958       C
ATOM   3108  CG  PRO A 393       0.818 -21.608  31.514  1.00104.90           C
ANISOU 3108  CG  PRO A 393    15736  11376  12746   -612    750    990       C
ATOM   3109  CD  PRO A 393       1.267 -22.445  30.362  1.00104.49           C
ANISOU 3109  CD  PRO A 393    15600  11300  12801   -606    749    989       C
ATOM   3110  N   GLN A 394       4.418 -21.392  32.149  1.00124.56           N
ANISOU 3110  N   GLN A 394    18206  13878  15244   -564    551   1148       N
ATOM   3111  CA  GLN A 394       5.591 -21.302  33.008  1.00132.18           C
ANISOU 3111  CA  GLN A 394    19199  14845  16180   -545    484   1224       C
ATOM   3112  C   GLN A 394       6.886 -21.109  32.224  1.00134.11           C
ANISOU 3112  C   GLN A 394    19381  15109  16464   -528    418   1235       C
ATOM   3113  O   GLN A 394       7.959 -21.073  32.836  1.00138.92           O
ANISOU 3113  O   GLN A 394    20007  15721  17057   -510    361   1299       O
ATOM   3114  CB  GLN A 394       5.687 -22.549  33.895  1.00136.29           C
ANISOU 3114  CB  GLN A 394    19743  15299  16742   -534    501   1313       C
ATOM   3115  CG  GLN A 394       4.579 -22.673  34.949  1.00137.05           C
ANISOU 3115  CG  GLN A 394    19915  15377  16783   -548    555   1317       C
ATOM   3116  CD  GLN A 394       3.260 -23.179  34.383  1.00135.34           C
ANISOU 3116  CD  GLN A 394    19683  15135  16606   -565    638   1260       C
ATOM   3117  OE1 GLN A 394       3.211 -23.723  33.281  1.00135.27           O
ANISOU 3117  OE1 GLN A 394    19606  15110  16681   -566    657   1232       O
ATOM   3118  NE2 GLN A 394       2.184 -23.000  35.141  1.00133.96           N
ANISOU 3118  NE2 GLN A 394    19571  14957  16371   -580    688   1240       N
ATOM   3119  N   ASP A 395       6.817 -20.991  30.898  1.00128.21           N
ANISOU 3119  N   ASP A 395    18567  14378  15770   -533    426   1174       N
ATOM   3120  CA  ASP A 395       7.952 -20.524  30.114  1.00122.33           C
ANISOU 3120  CA  ASP A 395    17769  13665  15046   -520    364   1167       C
ATOM   3121  C   ASP A 395       8.096 -19.017  30.292  1.00118.49           C
ANISOU 3121  C   ASP A 395    17317  13249  14453   -528    322   1121       C
ATOM   3122  O   ASP A 395       7.549 -18.442  31.240  1.00117.95           O
ANISOU 3122  O   ASP A 395    17320  13197  14299   -540    331   1115       O
ATOM   3123  CB  ASP A 395       7.771 -20.875  28.634  1.00118.82           C
ANISOU 3123  CB  ASP A 395    17240  13214  14690   -525    388   1114       C
ATOM   3124  CG  ASP A 395       8.091 -22.326  28.328  1.00117.25           C
ANISOU 3124  CG  ASP A 395    16993  12945  14610   -513    404   1165       C
ATOM   3125  OD1 ASP A 395       9.267 -22.626  28.031  1.00116.80           O
ANISOU 3125  OD1 ASP A 395    16894  12876  14609   -492    356   1207       O
ATOM   3126  OD2 ASP A 395       7.171 -23.168  28.392  1.00115.64           O
ANISOU 3126  OD2 ASP A 395    16794  12698  14446   -524    466   1162       O
ATOM   3127  N   GLU A 396       8.825 -18.368  29.392  1.00114.16           N
ANISOU 3127  N   GLU A 396    16721  12741  13912   -523    277   1087       N
ATOM   3128  CA  GLU A 396       8.859 -16.909  29.354  1.00108.48           C
ANISOU 3128  CA  GLU A 396    16027  12090  13101   -535    241   1028       C
ATOM   3129  C   GLU A 396       8.714 -16.333  27.952  1.00101.82           C
ANISOU 3129  C   GLU A 396    15121  11285  12281   -545    243    949       C
ATOM   3130  O   GLU A 396       8.185 -15.225  27.816  1.00103.29           O
ANISOU 3130  O   GLU A 396    15326  11520  12398   -562    243    884       O
ATOM   3131  CB  GLU A 396      10.156 -16.384  29.985  1.00109.81           C
ANISOU 3131  CB  GLU A 396    16220  12283  13222   -519    160   1073       C
ATOM   3132  CG  GLU A 396      10.002 -15.095  30.793  1.00110.40           C
ANISOU 3132  CG  GLU A 396    16362  12404  13180   -535    131   1042       C
ATOM   3133  CD  GLU A 396       9.871 -13.852  29.926  1.00109.49           C
ANISOU 3133  CD  GLU A 396    16225  12349  13028   -551    112    954       C
ATOM   3134  OE1 GLU A 396       8.877 -13.113  30.087  1.00108.84           O
ANISOU 3134  OE1 GLU A 396    16177  12288  12889   -573    143    896       O
ATOM   3135  OE2 GLU A 396      10.763 -13.614  29.083  1.00108.81           O
ANISOU 3135  OE2 GLU A 396    16086  12286  12972   -540     66    943       O
ATOM   3136  N   GLU A 397       9.153 -17.038  26.912  1.00 94.66           N
ANISOU 3136  N   GLU A 397    14138  10358  11471   -534    244    953       N
ATOM   3137  CA  GLU A 397       8.884 -16.630  25.544  1.00 83.16           C
ANISOU 3137  CA  GLU A 397    12618   8933  10045   -545    256    878       C
ATOM   3138  C   GLU A 397       7.380 -16.679  25.274  1.00 71.19           C
ANISOU 3138  C   GLU A 397    11108   7417   8526   -567    333    820       C
ATOM   3139  O   GLU A 397       6.663 -17.497  25.859  1.00 75.96           O
ANISOU 3139  O   GLU A 397    11739   7976   9148   -571    384    847       O
ATOM   3140  CB  GLU A 397       9.618 -17.547  24.572  1.00 84.88           C
ANISOU 3140  CB  GLU A 397    12755   9117  10377   -529    248    898       C
ATOM   3141  CG  GLU A 397       9.320 -19.018  24.816  1.00 89.44           C
ANISOU 3141  CG  GLU A 397    13323   9620  11042   -524    294    949       C
ATOM   3142  CD  GLU A 397       9.972 -19.924  23.798  1.00 95.16           C
ANISOU 3142  CD  GLU A 397    13964  10306  11887   -512    289    960       C
ATOM   3143  OE1 GLU A 397      10.745 -19.417  22.959  1.00 96.50           O
ANISOU 3143  OE1 GLU A 397    14085  10507  12072   -505    247    934       O
ATOM   3144  OE2 GLU A 397       9.707 -21.145  23.838  1.00 98.34           O
ANISOU 3144  OE2 GLU A 397    14349  10645  12370   -511    326    992       O
ATOM   3145  N   PRO A 398       6.872 -15.822  24.396  1.00 57.09           N
ANISOU 3145  N   PRO A 398     9296   5682   6716   -583    343    742       N
ATOM   3146  CA  PRO A 398       5.428 -15.797  24.152  1.00 49.20           C
ANISOU 3146  CA  PRO A 398     8301   4687   5705   -603    417    685       C
ATOM   3147  C   PRO A 398       4.982 -16.961  23.284  1.00 48.54           C
ANISOU 3147  C   PRO A 398     8155   4563   5726   -605    471    677       C
ATOM   3148  O   PRO A 398       5.706 -17.425  22.398  1.00 50.58           O
ANISOU 3148  O   PRO A 398     8346   4810   6063   -597    449    682       O
ATOM   3149  CB  PRO A 398       5.217 -14.456  23.439  1.00 51.74           C
ANISOU 3149  CB  PRO A 398     8609   5080   5971   -616    401    609       C
ATOM   3150  CG  PRO A 398       6.508 -14.214  22.729  1.00 54.22           C
ANISOU 3150  CG  PRO A 398     8871   5414   6315   -602    333    618       C
ATOM   3151  CD  PRO A 398       7.584 -14.787  23.622  1.00 59.75           C
ANISOU 3151  CD  PRO A 398     9598   6076   7028   -582    288    702       C
ATOM   3152  N   CYS A 399       3.766 -17.447  23.562  1.00 48.01           N
ANISOU 3152  N   CYS A 399     8111   4471   5660   -618    543    660       N
ATOM   3153  CA  CYS A 399       3.220 -18.551  22.775  1.00 47.80           C
ANISOU 3153  CA  CYS A 399     8029   4407   5726   -623    599    644       C
ATOM   3154  C   CYS A 399       2.803 -18.102  21.379  1.00 45.12           C
ANISOU 3154  C   CYS A 399     7622   4112   5407   -636    618    564       C
ATOM   3155  O   CYS A 399       2.702 -18.935  20.471  1.00 40.10           O
ANISOU 3155  O   CYS A 399     6924   3453   4859   -639    645    547       O
ATOM   3156  CB  CYS A 399       2.039 -19.206  23.506  1.00 45.23           C
ANISOU 3156  CB  CYS A 399     7750   4042   5392   -633    672    649       C
ATOM   3157  SG  CYS A 399       0.515 -18.226  23.669  1.00 41.71           S
ANISOU 3157  SG  CYS A 399     7348   3645   4856   -653    731    574       S
ATOM   3158  N   ALA A 400       2.570 -16.809  21.195  1.00 37.31           N
ANISOU 3158  N   ALA A 400     6646   3189   4342   -644    603    515       N
ATOM   3159  CA  ALA A 400       2.292 -16.217  19.898  1.00 36.36           C
ANISOU 3159  CA  ALA A 400     6464   3121   4231   -654    611    443       C
ATOM   3160  C   ALA A 400       3.325 -15.138  19.626  1.00 38.96           C
ANISOU 3160  C   ALA A 400     6783   3500   4520   -647    535    438       C
ATOM   3161  O   ALA A 400       3.758 -14.443  20.550  1.00 40.32           O
ANISOU 3161  O   ALA A 400     7015   3686   4619   -642    492    464       O
ATOM   3162  CB  ALA A 400       0.887 -15.611  19.853  1.00 32.34           C
ANISOU 3162  CB  ALA A 400     5976   2648   3664   -671    673    379       C
ATOM   3163  N   HIS A 401       3.720 -14.997  18.364  1.00 32.50           N
ANISOU 3163  N   HIS A 401     5890   2711   3749   -648    518    403       N
ATOM   3164  CA  HIS A 401       4.608 -13.901  18.009  1.00 27.53           C
ANISOU 3164  CA  HIS A 401     5248   2133   3077   -642    449    389       C
ATOM   3165  C   HIS A 401       3.906 -12.572  18.282  1.00 31.85           C
ANISOU 3165  C   HIS A 401     5841   2741   3522   -655    454    341       C
ATOM   3166  O   HIS A 401       2.692 -12.462  18.075  1.00 34.08           O
ANISOU 3166  O   HIS A 401     6124   3038   3788   -669    516    295       O
ATOM   3167  CB  HIS A 401       5.021 -13.973  16.540  1.00 32.51           C
ANISOU 3167  CB  HIS A 401     5788   2787   3778   -643    438    353       C
ATOM   3168  CG  HIS A 401       6.079 -12.981  16.168  1.00 35.15           C
ANISOU 3168  CG  HIS A 401     6107   3170   4080   -635    364    346       C
ATOM   3169  ND1 HIS A 401       5.787 -11.706  15.726  1.00 28.19           N
ANISOU 3169  ND1 HIS A 401     5224   2359   3128   -645    352    291       N
ATOM   3170  CD2 HIS A 401       7.430 -13.068  16.199  1.00 35.49           C
ANISOU 3170  CD2 HIS A 401     6137   3200   4149   -618    298    388       C
ATOM   3171  CE1 HIS A 401       6.913 -11.059  15.486  1.00 32.69           C
ANISOU 3171  CE1 HIS A 401     5780   2957   3681   -636    281    298       C
ATOM   3172  NE2 HIS A 401       7.923 -11.861  15.770  1.00 33.45           N
ANISOU 3172  NE2 HIS A 401     5871   3005   3834   -619    247    356       N
ATOM   3173  N   PRO A 402       4.629 -11.554  18.752  1.00 30.96           N
ANISOU 3173  N   PRO A 402     5764   2660   3338   -651    390    349       N
ATOM   3174  CA  PRO A 402       3.975 -10.267  19.064  1.00 28.23           C
ANISOU 3174  CA  PRO A 402     5463   2365   2897   -664    391    300       C
ATOM   3175  C   PRO A 402       3.276  -9.623  17.880  1.00 29.59           C
ANISOU 3175  C   PRO A 402     5583   2593   3065   -677    420    227       C
ATOM   3176  O   PRO A 402       2.375  -8.801  18.089  1.00 34.28           O
ANISOU 3176  O   PRO A 402     6209   3218   3597   -689    446    183       O
ATOM   3177  CB  PRO A 402       5.131  -9.392  19.562  1.00 31.19           C
ANISOU 3177  CB  PRO A 402     5870   2763   3217   -657    306    320       C
ATOM   3178  CG  PRO A 402       6.155 -10.337  20.041  1.00 32.43           C
ANISOU 3178  CG  PRO A 402     6029   2870   3422   -639    273    394       C
ATOM   3179  CD  PRO A 402       6.031 -11.589  19.202  1.00 34.97           C
ANISOU 3179  CD  PRO A 402     6285   3154   3849   -634    315    405       C
ATOM   3180  N   ASN A 403       3.670  -9.942  16.648  1.00 28.75           N
ANISOU 3180  N   ASN A 403     5397   2501   3026   -674    415    213       N
ATOM   3181  CA  ASN A 403       3.007  -9.406  15.467  1.00 30.78           C
ANISOU 3181  CA  ASN A 403     5597   2813   3284   -685    445    148       C
ATOM   3182  C   ASN A 403       2.129 -10.448  14.778  1.00 29.03           C
ANISOU 3182  C   ASN A 403     5325   2568   3137   -691    520    129       C
ATOM   3183  O   ASN A 403       1.758 -10.271  13.611  1.00 27.75           O
ANISOU 3183  O   ASN A 403     5097   2447   2998   -698    544     82       O
ATOM   3184  CB  ASN A 403       4.032  -8.838  14.483  1.00 29.84           C
ANISOU 3184  CB  ASN A 403     5422   2739   3178   -679    384    136       C
ATOM   3185  CG  ASN A 403       3.380  -8.065  13.350  1.00 31.88           C
ANISOU 3185  CG  ASN A 403     5629   3065   3420   -690    409     71       C
ATOM   3186  OD1 ASN A 403       2.497  -7.240  13.583  1.00 29.90           O
ANISOU 3186  OD1 ASN A 403     5410   2848   3101   -700    435     33       O
ATOM   3187  ND2 ASN A 403       3.775  -8.371  12.109  1.00 29.44           N
ANISOU 3187  ND2 ASN A 403     5235   2772   3177   -687    404     56       N
ATOM   3188  N   SER A 404       1.785 -11.532  15.472  1.00 26.76           N
ANISOU 3188  N   SER A 404     5065   2217   2885   -689    559    165       N
ATOM   3189  CA  SER A 404       0.848 -12.490  14.898  1.00 24.70           C
ANISOU 3189  CA  SER A 404     4763   1935   2688   -697    634    141       C
ATOM   3190  C   SER A 404      -0.491 -11.812  14.613  1.00 27.67           C
ANISOU 3190  C   SER A 404     5142   2358   3013   -711    693     78       C
ATOM   3191  O   SER A 404      -0.866 -10.823  15.258  1.00 30.97           O
ANISOU 3191  O   SER A 404     5617   2804   3348   -715    686     64       O
ATOM   3192  CB  SER A 404       0.658 -13.693  15.832  1.00 26.80           C
ANISOU 3192  CB  SER A 404     5069   2125   2991   -693    665    191       C
ATOM   3193  OG  SER A 404       0.254 -13.303  17.127  1.00 30.61           O
ANISOU 3193  OG  SER A 404     5637   2596   3398   -694    671    211       O
ATOM   3194  N   ARG A 405      -1.207 -12.344  13.623  1.00 24.31           N
ANISOU 3194  N   ARG A 405     4653   1942   2641   -719    750     37       N
ATOM   3195  CA  ARG A 405      -2.346 -11.657  13.028  1.00 27.94           C
ANISOU 3195  CA  ARG A 405     5094   2459   3064   -731    802    -27       C
ATOM   3196  C   ARG A 405      -3.521 -12.598  12.838  1.00 28.06           C
ANISOU 3196  C   ARG A 405     5091   2448   3121   -739    889    -52       C
ATOM   3197  O   ARG A 405      -3.344 -13.810  12.685  1.00 25.33           O
ANISOU 3197  O   ARG A 405     4719   2052   2852   -738    908    -32       O
ATOM   3198  CB  ARG A 405      -1.983 -11.067  11.655  1.00 23.50           C
ANISOU 3198  CB  ARG A 405     4452   1961   2516   -732    778    -66       C
ATOM   3199  CG  ARG A 405      -0.884 -10.060  11.705  1.00 21.56           C
ANISOU 3199  CG  ARG A 405     4217   1749   2226   -725    696    -50       C
ATOM   3200  CD  ARG A 405      -1.463  -8.678  11.719  1.00 25.71           C
ANISOU 3200  CD  ARG A 405     4767   2339   2663   -730    697    -90       C
ATOM   3201  NE  ARG A 405      -0.476  -7.698  12.142  1.00 28.45           N
ANISOU 3201  NE  ARG A 405     5149   2708   2953   -724    617    -71       N
ATOM   3202  CZ  ARG A 405      -0.709  -6.395  12.185  1.00 25.74           C
ANISOU 3202  CZ  ARG A 405     4830   2419   2533   -728    599   -104       C
ATOM   3203  NH1 ARG A 405      -1.901  -5.921  11.827  1.00 20.84           N
ANISOU 3203  NH1 ARG A 405     4199   1835   1884   -737    656   -156       N
ATOM   3204  NH2 ARG A 405       0.248  -5.572  12.594  1.00 22.34           N
ANISOU 3204  NH2 ARG A 405     4431   2002   2054   -723    524    -88       N
ATOM   3205  N   PHE A 406      -4.724 -12.025  12.805  1.00 27.93           N
ANISOU 3205  N   PHE A 406     5088   2467   3056   -747    943   -101       N
ATOM   3206  CA  PHE A 406      -5.871 -12.710  12.224  1.00 27.04           C
ANISOU 3206  CA  PHE A 406     4937   2353   2984   -756   1027   -143       C
ATOM   3207  C   PHE A 406      -6.242 -12.035  10.910  1.00 23.45           C
ANISOU 3207  C   PHE A 406     4410   1974   2527   -761   1043   -203       C
ATOM   3208  O   PHE A 406      -5.995 -10.845  10.715  1.00 24.45           O
ANISOU 3208  O   PHE A 406     4538   2155   2598   -759   1003   -218       O
ATOM   3209  CB  PHE A 406      -7.089 -12.762  13.170  1.00 26.35           C
ANISOU 3209  CB  PHE A 406     4915   2241   2857   -760   1089   -153       C
ATOM   3210  CG  PHE A 406      -7.525 -11.432  13.713  1.00 26.05           C
ANISOU 3210  CG  PHE A 406     4930   2240   2728   -761   1077   -176       C
ATOM   3211  CD1 PHE A 406      -8.242 -10.534  12.930  1.00 27.01           C
ANISOU 3211  CD1 PHE A 406     5018   2425   2819   -766   1100   -238       C
ATOM   3212  CD2 PHE A 406      -7.233 -11.087  15.016  1.00 25.01           C
ANISOU 3212  CD2 PHE A 406     4883   2077   2543   -757   1043   -138       C
ATOM   3213  CE1 PHE A 406      -8.652  -9.313  13.447  1.00 25.75           C
ANISOU 3213  CE1 PHE A 406     4909   2293   2581   -767   1087   -262       C
ATOM   3214  CE2 PHE A 406      -7.643  -9.881  15.542  1.00 26.92           C
ANISOU 3214  CE2 PHE A 406     5176   2347   2707   -759   1031   -164       C
ATOM   3215  CZ  PHE A 406      -8.349  -8.985  14.756  1.00 26.22           C
ANISOU 3215  CZ  PHE A 406     5054   2317   2592   -764   1052   -228       C
ATOM   3216  N   CYS A 407      -6.801 -12.813   9.990  1.00 24.81           N
ANISOU 3216  N   CYS A 407     4516   2150   2761   -767   1100   -237       N
ATOM   3217  CA  CYS A 407      -7.243 -12.306   8.692  1.00 26.38           C
ANISOU 3217  CA  CYS A 407     4640   2420   2964   -771   1124   -295       C
ATOM   3218  C   CYS A 407      -8.711 -12.702   8.562  1.00 27.07           C
ANISOU 3218  C   CYS A 407     4721   2507   3057   -778   1216   -343       C
ATOM   3219  O   CYS A 407      -9.019 -13.868   8.297  1.00 25.85           O
ANISOU 3219  O   CYS A 407     4537   2317   2969   -781   1264   -349       O
ATOM   3220  CB  CYS A 407      -6.388 -12.883   7.560  1.00 28.08           C
ANISOU 3220  CB  CYS A 407     4772   2644   3254   -770   1099   -297       C
ATOM   3221  SG  CYS A 407      -6.745 -12.238   5.919  1.00 24.97           S
ANISOU 3221  SG  CYS A 407     4281   2343   2865   -773   1121   -362       S
ATOM   3222  N   THR A 408      -9.621 -11.745   8.744  1.00 25.35           N
ANISOU 3222  N   THR A 408     4531   2327   2774   -779   1241   -379       N
ATOM   3223  CA  THR A 408     -11.022 -12.119   8.879  1.00 26.22           C
ANISOU 3223  CA  THR A 408     4652   2425   2887   -784   1324   -419       C
ATOM   3224  C   THR A 408     -11.901 -11.270   7.967  1.00 30.35           C
ANISOU 3224  C   THR A 408     5065   3023   3444   -772   1278   -436       C
ATOM   3225  O   THR A 408     -11.592 -10.098   7.707  1.00 30.97           O
ANISOU 3225  O   THR A 408     5108   3156   3503   -761   1201   -424       O
ATOM   3226  CB  THR A 408     -11.476 -11.979  10.344  1.00 28.16           C
ANISOU 3226  CB  THR A 408     4996   2622   3083   -783   1332   -395       C
ATOM   3227  OG1 THR A 408     -12.747 -12.617  10.519  1.00 26.53           O
ANISOU 3227  OG1 THR A 408     4790   2388   2901   -786   1407   -420       O
ATOM   3228  CG2 THR A 408     -11.576 -10.496  10.749  1.00 18.10           C
ANISOU 3228  CG2 THR A 408     3728   1390   1758   -774   1257   -383       C
ATOM   3229  N   PRO A 409     -12.991 -11.840   7.444  1.00 28.10           N
ANISOU 3229  N   PRO A 409     4724   2741   3210   -772   1321   -464       N
ATOM   3230  CA  PRO A 409     -13.868 -11.068   6.551  1.00 25.91           C
ANISOU 3230  CA  PRO A 409     4349   2532   2962   -759   1275   -480       C
ATOM   3231  C   PRO A 409     -14.566  -9.952   7.315  1.00 29.13           C
ANISOU 3231  C   PRO A 409     4783   2955   3332   -748   1234   -465       C
ATOM   3232  O   PRO A 409     -15.083 -10.175   8.410  1.00 24.53           O
ANISOU 3232  O   PRO A 409     4275   2322   2722   -755   1273   -460       O
ATOM   3233  CB  PRO A 409     -14.872 -12.114   6.047  1.00 31.92           C
ANISOU 3233  CB  PRO A 409     5070   3279   3781   -764   1337   -512       C
ATOM   3234  CG  PRO A 409     -14.202 -13.438   6.263  1.00 28.39           C
ANISOU 3234  CG  PRO A 409     4667   2769   3351   -779   1410   -516       C
ATOM   3235  CD  PRO A 409     -13.398 -13.253   7.520  1.00 25.66           C
ANISOU 3235  CD  PRO A 409     4433   2377   2941   -783   1412   -484       C
ATOM   3236  N   ALA A 410     -14.572  -8.747   6.730  1.00 24.22           N
ANISOU 3236  N   ALA A 410     4097   2397   2707   -731   1159   -460       N
ATOM   3237  CA  ALA A 410     -15.242  -7.618   7.371  1.00 28.09           C
ANISOU 3237  CA  ALA A 410     4602   2902   3169   -719   1120   -450       C
ATOM   3238  C   ALA A 410     -16.749  -7.837   7.466  1.00 31.73           C
ANISOU 3238  C   ALA A 410     5051   3352   3654   -719   1156   -471       C
ATOM   3239  O   ALA A 410     -17.373  -7.434   8.456  1.00 31.30           O
ANISOU 3239  O   ALA A 410     5048   3271   3572   -720   1163   -465       O
ATOM   3240  CB  ALA A 410     -14.944  -6.322   6.614  1.00 22.19           C
ANISOU 3240  CB  ALA A 410     3782   2225   2424   -698   1036   -441       C
ATOM   3241  N   SER A 411     -17.336  -8.505   6.466  1.00 34.12           N
ANISOU 3241  N   SER A 411     5289   3669   4006   -719   1181   -497       N
ATOM   3242  CA  SER A 411     -18.786  -8.686   6.404  1.00 38.20           C
ANISOU 3242  CA  SER A 411     5788   4180   4548   -719   1208   -519       C
ATOM   3243  C   SER A 411     -19.343  -9.393   7.636  1.00 39.25           C
ANISOU 3243  C   SER A 411     6005   4244   4665   -734   1279   -518       C
ATOM   3244  O   SER A 411     -20.524  -9.218   7.967  1.00 41.33           O
ANISOU 3244  O   SER A 411     6273   4497   4933   -733   1293   -528       O
ATOM   3245  CB  SER A 411     -19.146  -9.482   5.151  1.00 36.29           C
ANISOU 3245  CB  SER A 411     5471   3957   4359   -719   1227   -547       C
ATOM   3246  OG  SER A 411     -18.705 -10.821   5.299  1.00 35.76           O
ANISOU 3246  OG  SER A 411     5434   3844   4310   -736   1295   -554       O
ATOM   3247  N   GLN A 412     -18.518 -10.192   8.320  1.00 32.27           N
ANISOU 3247  N   GLN A 412     5191   3309   3761   -748   1323   -506       N
ATOM   3248  CA  GLN A 412     -18.956 -10.955   9.484  1.00 37.47           C
ANISOU 3248  CA  GLN A 412     5936   3897   4402   -760   1395   -503       C
ATOM   3249  C   GLN A 412     -18.939 -10.152  10.778  1.00 36.16           C
ANISOU 3249  C   GLN A 412     5853   3709   4179   -758   1376   -480       C
ATOM   3250  O   GLN A 412     -19.521 -10.601  11.770  1.00 35.84           O
ANISOU 3250  O   GLN A 412     5882   3614   4121   -766   1430   -478       O
ATOM   3251  CB  GLN A 412     -18.075 -12.192   9.675  1.00 34.95           C
ANISOU 3251  CB  GLN A 412     5665   3526   4087   -772   1454   -499       C
ATOM   3252  CG  GLN A 412     -18.060 -13.136   8.489  1.00 36.77           C
ANISOU 3252  CG  GLN A 412     5821   3769   4381   -776   1483   -525       C
ATOM   3253  CD  GLN A 412     -17.088 -14.294   8.656  1.00 35.13           C
ANISOU 3253  CD  GLN A 412     5657   3509   4182   -787   1541   -521       C
ATOM   3254  OE1 GLN A 412     -17.082 -15.225   7.850  1.00 42.42           O
ANISOU 3254  OE1 GLN A 412     6529   4428   5160   -791   1578   -544       O
ATOM   3255  NE2 GLN A 412     -16.266 -14.244   9.699  1.00 28.83           N
ANISOU 3255  NE2 GLN A 412     4956   2667   3330   -790   1548   -494       N
ATOM   3256  N   CYS A 413     -18.252  -9.020  10.811  1.00 32.61           N
ANISOU 3256  N   CYS A 413     4337   3338   4716   -710   1645   -911       N
ATOM   3257  CA  CYS A 413     -18.216  -8.192  12.004  1.00 30.98           C
ANISOU 3257  CA  CYS A 413     4174   3122   4475   -689   1635   -880       C
ATOM   3258  C   CYS A 413     -19.637  -7.890  12.467  1.00 35.28           C
ANISOU 3258  C   CYS A 413     4706   3682   5015   -722   1631   -911       C
ATOM   3259  O   CYS A 413     -20.438  -7.368  11.678  1.00 32.41           O
ANISOU 3259  O   CYS A 413     4289   3376   4650   -744   1590   -956       O
ATOM   3260  CB  CYS A 413     -17.463  -6.893  11.724  1.00 25.90           C
ANISOU 3260  CB  CYS A 413     3521   2526   3793   -656   1574   -866       C
ATOM   3261  SG  CYS A 413     -17.184  -5.874  13.198  1.00 35.02           S
ANISOU 3261  SG  CYS A 413     4732   3671   4904   -625   1536   -802       S
ATOM   3262  N   PRO A 414     -19.999  -8.224  13.713  1.00 37.13           N
ANISOU 3262  N   PRO A 414     4988   3868   5250   -725   1673   -889       N
ATOM   3263  CA  PRO A 414     -21.378  -7.996  14.152  1.00 35.69           C
ANISOU 3263  CA  PRO A 414     4793   3701   5066   -758   1673   -918       C
ATOM   3264  C   PRO A 414     -21.746  -6.535  14.227  1.00 35.67           C
ANISOU 3264  C   PRO A 414     4774   3755   5025   -749   1609   -929       C
ATOM   3265  O   PRO A 414     -22.940  -6.224  14.282  1.00 29.25           O
ANISOU 3265  O   PRO A 414     3933   2969   4211   -777   1596   -962       O
ATOM   3266  CB  PRO A 414     -21.422  -8.656  15.539  1.00 37.10           C
ANISOU 3266  CB  PRO A 414     5036   3812   5250   -756   1733   -882       C
ATOM   3267  CG  PRO A 414     -20.012  -8.594  16.019  1.00 35.98           C
ANISOU 3267  CG  PRO A 414     4945   3633   5090   -709   1740   -826       C
ATOM   3268  CD  PRO A 414     -19.175  -8.810  14.786  1.00 34.08           C
ANISOU 3268  CD  PRO A 414     4671   3413   4864   -699   1723   -834       C
ATOM   3269  N   ILE A 415     -20.770  -5.632  14.222  1.00 36.08           N
ANISOU 3269  N   ILE A 415     4839   3823   5045   -712   1568   -903       N
ATOM   3270  CA  ILE A 415     -21.035  -4.203  14.233  1.00 32.51           C
ANISOU 3270  CA  ILE A 415     4371   3426   4554   -703   1504   -913       C
ATOM   3271  C   ILE A 415     -20.566  -3.541  12.939  1.00 32.93           C
ANISOU 3271  C   ILE A 415     4374   3540   4598   -693   1448   -933       C
ATOM   3272  O   ILE A 415     -20.357  -2.334  12.919  1.00 26.10           O
ANISOU 3272  O   ILE A 415     3504   2714   3698   -674   1393   -930       O
ATOM   3273  CB  ILE A 415     -20.400  -3.520  15.456  1.00 27.69           C
ANISOU 3273  CB  ILE A 415     3825   2787   3910   -670   1497   -866       C
ATOM   3274  CG1 ILE A 415     -18.877  -3.692  15.429  1.00 36.13           C
ANISOU 3274  CG1 ILE A 415     4916   3840   4973   -632   1470   -791       C
ATOM   3275  CG2 ILE A 415     -20.987  -4.066  16.748  1.00 27.25           C
ANISOU 3275  CG2 ILE A 415     3817   2677   3860   -682   1548   -849       C
ATOM   3276  CD1 ILE A 415     -18.157  -2.823  16.423  1.00 38.96           C
ANISOU 3276  CD1 ILE A 415     5312   4198   5292   -598   1410   -711       C
ATOM   3277  N   ILE A 416     -20.379  -4.319  11.866  1.00 28.91           N
ANISOU 3277  N   ILE A 416     3829   3037   4119   -704   1460   -953       N
ATOM   3278  CA  ILE A 416     -20.006  -3.730  10.584  1.00 30.14           C
ANISOU 3278  CA  ILE A 416     3933   3251   4266   -696   1407   -974       C
ATOM   3279  C   ILE A 416     -21.059  -2.705  10.189  1.00 34.78           C
ANISOU 3279  C   ILE A 416     4476   3904   4835   -713   1353  -1012       C
ATOM   3280  O   ILE A 416     -22.265  -2.890  10.421  1.00 29.38           O
ANISOU 3280  O   ILE A 416     3777   3224   4163   -742   1365  -1038       O
ATOM   3281  CB  ILE A 416     -19.819  -4.811   9.502  1.00 32.84           C
ANISOU 3281  CB  ILE A 416     4243   3588   4647   -712   1432   -994       C
ATOM   3282  CG1 ILE A 416     -18.966  -4.278   8.344  1.00 32.01           C
ANISOU 3282  CG1 ILE A 416     4103   3530   4530   -691   1385   -998       C
ATOM   3283  CG2 ILE A 416     -21.149  -5.308   8.963  1.00 33.84           C
ANISOU 3283  CG2 ILE A 416     4325   3732   4799   -755   1440  -1043       C
ATOM   3284  CD1 ILE A 416     -17.509  -4.084   8.698  1.00 22.56           C
ANISOU 3284  CD1 ILE A 416     2946   2310   3317   -650   1388   -948       C
ATOM   3285  N   ASP A 417     -20.593  -1.581   9.631  1.00 34.73           N
ANISOU 3285  N   ASP A 417     4447   3950   4798   -691   1292  -1013       N
ATOM   3286  CA  ASP A 417     -21.477  -0.453   9.400  1.00 30.36           C
ANISOU 3286  CA  ASP A 417     3858   3457   4220   -699   1236  -1041       C
ATOM   3287  C   ASP A 417     -22.356  -0.714   8.178  1.00 31.14           C
ANISOU 3287  C   ASP A 417     3891   3600   4342   -728   1222  -1089       C
ATOM   3288  O   ASP A 417     -21.872  -1.224   7.164  1.00 31.53           O
ANISOU 3288  O   ASP A 417     3914   3658   4409   -728   1224  -1099       O
ATOM   3289  CB  ASP A 417     -20.663   0.821   9.201  1.00 33.79           C
ANISOU 3289  CB  ASP A 417     4293   3931   4614   -668   1176  -1025       C
ATOM   3290  CG  ASP A 417     -21.508   2.061   9.291  1.00 31.00           C
ANISOU 3290  CG  ASP A 417     3918   3629   4230   -671   1121  -1043       C
ATOM   3291  OD1 ASP A 417     -21.706   2.556  10.420  1.00 31.54           O
ANISOU 3291  OD1 ASP A 417     4027   3679   4278   -666   1120  -1024       O
ATOM   3292  OD2 ASP A 417     -22.008   2.512   8.240  1.00 28.92           O
ANISOU 3292  OD2 ASP A 417     3598   3424   3965   -680   1080  -1075       O
ATOM   3293  N   PRO A 418     -23.647  -0.379   8.247  1.00 28.31           N
ANISOU 3293  N   PRO A 418     3505   3269   3981   -751   1209  -1117       N
ATOM   3294  CA  PRO A 418     -24.532  -0.644   7.101  1.00 30.76           C
ANISOU 3294  CA  PRO A 418     3754   3621   4314   -778   1197  -1163       C
ATOM   3295  C   PRO A 418     -24.118   0.078   5.834  1.00 35.43           C
ANISOU 3295  C   PRO A 418     4299   4272   4889   -763   1140  -1176       C
ATOM   3296  O   PRO A 418     -24.564  -0.316   4.748  1.00 30.61           O
ANISOU 3296  O   PRO A 418     3642   3689   4300   -782   1134  -1210       O
ATOM   3297  CB  PRO A 418     -25.905  -0.167   7.597  1.00 30.56           C
ANISOU 3297  CB  PRO A 418     3713   3615   4281   -797   1188  -1183       C
ATOM   3298  CG  PRO A 418     -25.600   0.749   8.759  1.00 34.23           C
ANISOU 3298  CG  PRO A 418     4224   4071   4711   -773   1171  -1149       C
ATOM   3299  CD  PRO A 418     -24.382   0.174   9.398  1.00 33.82           C
ANISOU 3299  CD  PRO A 418     4229   3959   4661   -754   1208  -1109       C
ATOM   3300  N   ALA A 419     -23.270   1.107   5.933  1.00 31.25           N
ANISOU 3300  N   ALA A 419     3784   3764   4324   -731   1097  -1152       N
ATOM   3301  CA  ALA A 419     -22.757   1.831   4.778  1.00 28.89           C
ANISOU 3301  CA  ALA A 419     3447   3521   4008   -714   1042  -1160       C
ATOM   3302  C   ALA A 419     -21.313   1.468   4.431  1.00 34.15           C
ANISOU 3302  C   ALA A 419     4131   4168   4678   -692   1051  -1136       C
ATOM   3303  O   ALA A 419     -20.686   2.186   3.641  1.00 36.45           O
ANISOU 3303  O   ALA A 419     4399   4502   4948   -672   1004  -1136       O
ATOM   3304  CB  ALA A 419     -22.854   3.341   5.018  1.00 30.74           C
ANISOU 3304  CB  ALA A 419     3678   3802   4199   -694    981  -1152       C
ATOM   3305  N   TRP A 420     -20.767   0.380   4.996  1.00 31.94           N
ANISOU 3305  N   TRP A 420     3890   3823   4421   -693   1110  -1115       N
ATOM   3306  CA  TRP A 420     -19.336   0.101   4.837  1.00 32.30           C
ANISOU 3306  CA  TRP A 420     3959   3847   4468   -666   1121  -1084       C
ATOM   3307  C   TRP A 420     -18.971  -0.277   3.409  1.00 31.14           C
ANISOU 3307  C   TRP A 420     3766   3729   4338   -669   1108  -1105       C
ATOM   3308  O   TRP A 420     -17.784  -0.236   3.050  1.00 28.44           O
ANISOU 3308  O   TRP A 420     3428   3387   3990   -645   1102  -1083       O
ATOM   3309  CB  TRP A 420     -18.874  -1.001   5.807  1.00 31.49           C
ANISOU 3309  CB  TRP A 420     3911   3667   4388   -665   1190  -1053       C
ATOM   3310  CG  TRP A 420     -19.096  -2.417   5.340  1.00 26.67           C
ANISOU 3310  CG  TRP A 420     3289   3023   3822   -690   1240  -1069       C
ATOM   3311  CD1 TRP A 420     -20.261  -3.129   5.397  1.00 29.06           C
ANISOU 3311  CD1 TRP A 420     3579   3312   4152   -726   1269  -1099       C
ATOM   3312  CD2 TRP A 420     -18.114  -3.303   4.769  1.00 33.94           C
ANISOU 3312  CD2 TRP A 420     4212   3918   4767   -681   1267  -1056       C
ATOM   3313  NE1 TRP A 420     -20.069  -4.395   4.878  1.00 26.77           N
ANISOU 3313  NE1 TRP A 420     3284   2989   3900   -741   1311  -1107       N
ATOM   3314  CE2 TRP A 420     -18.759  -4.526   4.497  1.00 33.96           C
ANISOU 3314  CE2 TRP A 420     4204   3891   4809   -713   1311  -1081       C
ATOM   3315  CE3 TRP A 420     -16.754  -3.175   4.457  1.00 30.90           C
ANISOU 3315  CE3 TRP A 420     3835   3534   4373   -649   1259  -1025       C
ATOM   3316  CZ2 TRP A 420     -18.094  -5.612   3.913  1.00 37.47           C
ANISOU 3316  CZ2 TRP A 420     4647   4305   5284   -715   1344  -1077       C
ATOM   3317  CZ3 TRP A 420     -16.096  -4.257   3.881  1.00 29.82           C
ANISOU 3317  CZ3 TRP A 420     3695   3368   4268   -649   1294  -1019       C
ATOM   3318  CH2 TRP A 420     -16.768  -5.455   3.619  1.00 33.57           C
ANISOU 3318  CH2 TRP A 420     4161   3812   4781   -682   1334  -1045       C
ATOM   3319  N   GLU A 421     -19.958  -0.617   2.581  1.00 32.87           N
ANISOU 3319  N   GLU A 421     3939   3974   4577   -699   1103  -1146       N
ATOM   3320  CA  GLU A 421     -19.725  -0.899   1.171  1.00 35.14           C
ANISOU 3320  CA  GLU A 421     4181   4293   4878   -703   1085  -1170       C
ATOM   3321  C   GLU A 421     -20.397   0.109   0.259  1.00 38.25           C
ANISOU 3321  C   GLU A 421     4523   4760   5252   -707   1023  -1200       C
ATOM   3322  O   GLU A 421     -20.519  -0.154  -0.941  1.00 41.69           O
ANISOU 3322  O   GLU A 421     4916   5224   5700   -718   1008  -1228       O
ATOM   3323  CB  GLU A 421     -20.203  -2.307   0.807  1.00 34.89           C
ANISOU 3323  CB  GLU A 421     4141   4226   4891   -735   1134  -1194       C
ATOM   3324  CG  GLU A 421     -19.535  -3.379   1.598  1.00 29.90           C
ANISOU 3324  CG  GLU A 421     3558   3521   4281   -732   1197  -1163       C
ATOM   3325  CD  GLU A 421     -19.709  -4.745   0.980  1.00 32.25           C
ANISOU 3325  CD  GLU A 421     3844   3788   4621   -758   1238  -1185       C
ATOM   3326  OE1 GLU A 421     -18.903  -5.103   0.097  1.00 36.97           O
ANISOU 3326  OE1 GLU A 421     4427   4390   5229   -749   1234  -1184       O
ATOM   3327  OE2 GLU A 421     -20.662  -5.441   1.367  1.00 35.91           O
ANISOU 3327  OE2 GLU A 421     4311   4224   5107   -789   1275  -1204       O
ATOM   3328  N   SER A 422     -20.839   1.248   0.786  1.00 32.15           N
ANISOU 3328  N   SER A 422     3751   4017   4446   -697    986  -1196       N
ATOM   3329  CA  SER A 422     -21.523   2.222  -0.051  1.00 33.25           C
ANISOU 3329  CA  SER A 422     3841   4226   4566   -699    928  -1222       C
ATOM   3330  C   SER A 422     -20.523   2.872  -0.999  1.00 35.38           C
ANISOU 3330  C   SER A 422     4091   4537   4816   -673    882  -1214       C
ATOM   3331  O   SER A 422     -19.504   3.399  -0.545  1.00 35.53           O
ANISOU 3331  O   SER A 422     4139   4549   4811   -645    869  -1182       O
ATOM   3332  CB  SER A 422     -22.206   3.284   0.802  1.00 34.57           C
ANISOU 3332  CB  SER A 422     4019   4413   4705   -693    901  -1215       C
ATOM   3333  OG  SER A 422     -22.718   4.310  -0.028  1.00 41.00           O
ANISOU 3333  OG  SER A 422     4785   5295   5497   -687    843  -1233       O
ATOM   3334  N   PRO A 423     -20.776   2.867  -2.310  1.00 38.81           N
ANISOU 3334  N   PRO A 423     4473   5014   5257   -681    856  -1242       N
ATOM   3335  CA  PRO A 423     -19.804   3.458  -3.245  1.00 38.67           C
ANISOU 3335  CA  PRO A 423     4437   5036   5221   -657    813  -1235       C
ATOM   3336  C   PRO A 423     -19.619   4.947  -3.049  1.00 38.97           C
ANISOU 3336  C   PRO A 423     4474   5120   5214   -630    755  -1218       C
ATOM   3337  O   PRO A 423     -18.564   5.484  -3.412  1.00 40.43           O
ANISOU 3337  O   PRO A 423     4661   5325   5378   -605    725  -1200       O
ATOM   3338  CB  PRO A 423     -20.405   3.144  -4.625  1.00 45.95           C
ANISOU 3338  CB  PRO A 423     5303   5994   6160   -676    798  -1273       C
ATOM   3339  CG  PRO A 423     -21.487   2.115  -4.373  1.00 45.13           C
ANISOU 3339  CG  PRO A 423     5198   5858   6091   -712    844  -1299       C
ATOM   3340  CD  PRO A 423     -21.985   2.382  -2.995  1.00 40.69           C
ANISOU 3340  CD  PRO A 423     4671   5270   5521   -713    862  -1283       C
ATOM   3341  N   GLU A 424     -20.608   5.635  -2.475  1.00 34.62           N
ANISOU 3341  N   GLU A 424     3920   4585   4648   -635    739  -1223       N
ATOM   3342  CA  GLU A 424     -20.487   7.064  -2.231  1.00 37.22           C
ANISOU 3342  CA  GLU A 424     4252   4955   4934   -610    682  -1206       C
ATOM   3343  C   GLU A 424     -19.587   7.379  -1.040  1.00 36.60           C
ANISOU 3343  C   GLU A 424     4233   4839   4833   -591    686  -1170       C
ATOM   3344  O   GLU A 424     -19.049   8.491  -0.958  1.00 38.64           O
ANISOU 3344  O   GLU A 424     4500   5127   5055   -568    635  -1152       O
ATOM   3345  CB  GLU A 424     -21.876   7.672  -2.026  1.00 43.25           C
ANISOU 3345  CB  GLU A 424     4994   5748   5691   -620    665  -1220       C
ATOM   3346  CG  GLU A 424     -21.886   9.197  -1.971  1.00 63.76           C
ANISOU 3346  CG  GLU A 424     7587   8394   8245   -594    601  -1203       C
ATOM   3347  CD  GLU A 424     -23.258   9.762  -1.648  1.00 74.08           C
ANISOU 3347  CD  GLU A 424     8876   9725   9547   -600    590  -1213       C
ATOM   3348  OE1 GLU A 424     -24.251   9.017  -1.797  1.00 86.81           O
ANISOU 3348  OE1 GLU A 424    10465  11330  11189   -627    625  -1241       O
ATOM   3349  OE2 GLU A 424     -23.347  10.943  -1.239  1.00 64.79           O
ANISOU 3349  OE2 GLU A 424     7709   8573   8337   -580    547  -1193       O
ATOM   3350  N   GLY A 425     -19.387   6.428  -0.137  1.00 29.79           N
ANISOU 3350  N   GLY A 425     3412   3914   3993   -600    745  -1159       N
ATOM   3351  CA  GLY A 425     -18.580   6.667   1.040  1.00 28.65           C
ANISOU 3351  CA  GLY A 425     3324   3730   3830   -582    746  -1111       C
ATOM   3352  C   GLY A 425     -19.405   7.269   2.158  1.00 30.47           C
ANISOU 3352  C   GLY A 425     3581   3954   4043   -588    741  -1110       C
ATOM   3353  O   GLY A 425     -20.600   7.534   2.023  1.00 31.71           O
ANISOU 3353  O   GLY A 425     3709   4137   4201   -604    734  -1140       O
ATOM   3354  N   VAL A 426     -18.744   7.488   3.291  1.00 26.02           N
ANISOU 3354  N   VAL A 426     3066   3353   3466   -569    726  -1038       N
ATOM   3355  CA  VAL A 426     -19.400   8.044   4.468  1.00 27.17           C
ANISOU 3355  CA  VAL A 426     3243   3487   3594   -572    721  -1028       C
ATOM   3356  C   VAL A 426     -18.753   9.386   4.792  1.00 27.43           C
ANISOU 3356  C   VAL A 426     3289   3546   3586   -543    641   -967       C
ATOM   3357  O   VAL A 426     -17.533   9.549   4.627  1.00 26.35           O
ANISOU 3357  O   VAL A 426     3162   3408   3442   -518    606   -910       O
ATOM   3358  CB  VAL A 426     -19.336   7.070   5.654  1.00 27.77           C
ANISOU 3358  CB  VAL A 426     3369   3490   3691   -580    782  -1001       C
ATOM   3359  CG1 VAL A 426     -20.101   5.800   5.325  1.00 29.59           C
ANISOU 3359  CG1 VAL A 426     3585   3696   3962   -612    863  -1068       C
ATOM   3360  CG2 VAL A 426     -17.892   6.743   6.017  1.00 26.54           C
ANISOU 3360  CG2 VAL A 426     3250   3299   3537   -553    772   -923       C
ATOM   3361  N   PRO A 427     -19.532  10.372   5.242  1.00 28.47           N
ANISOU 3361  N   PRO A 427     3421   3704   3692   -545    610   -979       N
ATOM   3362  CA  PRO A 427     -19.024  11.741   5.419  1.00 25.07           C
ANISOU 3362  CA  PRO A 427     2997   3307   3222   -518    532   -930       C
ATOM   3363  C   PRO A 427     -18.287  11.887   6.744  1.00 20.83           C
ANISOU 3363  C   PRO A 427     2516   2726   2672   -500    521   -853       C
ATOM   3364  O   PRO A 427     -18.860  11.680   7.817  1.00 26.20           O
ANISOU 3364  O   PRO A 427     3228   3371   3354   -511    552   -852       O
ATOM   3365  CB  PRO A 427     -20.299  12.591   5.386  1.00 27.57           C
ANISOU 3365  CB  PRO A 427     3290   3664   3520   -531    514   -982       C
ATOM   3366  CG  PRO A 427     -21.346  11.650   5.938  1.00 23.12           C
ANISOU 3366  CG  PRO A 427     2737   3065   2984   -562    587  -1030       C
ATOM   3367  CD  PRO A 427     -20.989  10.285   5.455  1.00 28.34           C
ANISOU 3367  CD  PRO A 427     3392   3693   3682   -573    646  -1046       C
ATOM   3368  N   ILE A 428     -17.014  12.246   6.666  1.00 23.21           N
ANISOU 3368  N   ILE A 428     2830   3030   2961   -473    477   -790       N
ATOM   3369  CA  ILE A 428     -16.151  12.308   7.837  1.00 23.20           C
ANISOU 3369  CA  ILE A 428     2879   2987   2948   -453    465   -714       C
ATOM   3370  C   ILE A 428     -16.333  13.670   8.498  1.00 28.64           C
ANISOU 3370  C   ILE A 428     3582   3701   3599   -441    407   -687       C
ATOM   3371  O   ILE A 428     -16.160  14.714   7.859  1.00 28.13           O
ANISOU 3371  O   ILE A 428     3492   3686   3510   -429    348   -685       O
ATOM   3372  CB  ILE A 428     -14.683  12.062   7.453  1.00 17.62           C
ANISOU 3372  CB  ILE A 428     2178   2272   2244   -429    445   -659       C
ATOM   3373  CG1 ILE A 428     -14.501  10.650   6.887  1.00 25.31           C
ANISOU 3373  CG1 ILE A 428     3143   3216   3258   -442    507   -684       C
ATOM   3374  CG2 ILE A 428     -13.757  12.292   8.647  1.00 21.15           C
ANISOU 3374  CG2 ILE A 428     2676   2685   2675   -406    423   -579       C
ATOM   3375  CD1 ILE A 428     -15.024   9.517   7.803  1.00 24.44           C
ANISOU 3375  CD1 ILE A 428     3065   3045   3174   -460    582   -695       C
ATOM   3376  N   GLU A 429     -16.700  13.668   9.777  1.00 22.54           N
ANISOU 3376  N   GLU A 429     2849   2894   2820   -445    425   -668       N
ATOM   3377  CA  GLU A 429     -16.878  14.916  10.506  1.00 15.92           C
ANISOU 3377  CA  GLU A 429     2027   2075   1946   -434    373   -641       C
ATOM   3378  C   GLU A 429     -15.786  15.160  11.529  1.00 21.44           C
ANISOU 3378  C   GLU A 429     2773   2744   2628   -410    346   -559       C
ATOM   3379  O   GLU A 429     -15.711  16.267  12.082  1.00 25.57           O
ANISOU 3379  O   GLU A 429     3310   3286   3120   -397    296   -529       O
ATOM   3380  CB  GLU A 429     -18.245  14.939  11.202  1.00 24.24           C
ANISOU 3380  CB  GLU A 429     3089   3121   3001   -458    405   -686       C
ATOM   3381  CG  GLU A 429     -19.385  14.797  10.231  1.00 23.90           C
ANISOU 3381  CG  GLU A 429     2998   3111   2971   -482    427   -769       C
ATOM   3382  CD  GLU A 429     -20.731  14.939  10.899  1.00 27.86           C
ANISOU 3382  CD  GLU A 429     3505   3610   3472   -504    453   -813       C
ATOM   3383  OE1 GLU A 429     -20.944  15.938  11.630  1.00 24.18           O
ANISOU 3383  OE1 GLU A 429     3056   3154   2976   -496    415   -790       O
ATOM   3384  OE2 GLU A 429     -21.569  14.045  10.694  1.00 28.18           O
ANISOU 3384  OE2 GLU A 429     3532   3635   3539   -530    514   -870       O
ATOM   3385  N   GLY A 430     -14.947  14.162  11.792  1.00 20.95           N
ANISOU 3385  N   GLY A 430     2735   2638   2586   -402    380   -524       N
ATOM   3386  CA  GLY A 430     -13.824  14.344  12.682  1.00 22.22           C
ANISOU 3386  CA  GLY A 430     2938   2773   2732   -376    354   -446       C
ATOM   3387  C   GLY A 430     -12.667  13.450  12.307  1.00 21.24           C
ANISOU 3387  C   GLY A 430     2818   2624   2628   -363    370   -413       C
ATOM   3388  O   GLY A 430     -12.864  12.303  11.883  1.00 21.54           O
ANISOU 3388  O   GLY A 430     2848   2638   2699   -377    428   -446       O
ATOM   3389  N   ILE A 431     -11.452  13.959  12.471  1.00 16.29           N
ANISOU 3389  N   ILE A 431     2206   2002   1982   -335    321   -349       N
ATOM   3390  CA  ILE A 431     -10.244  13.190  12.207  1.00 18.28           C
ANISOU 3390  CA  ILE A 431     2465   2231   2250   -318    331   -311       C
ATOM   3391  C   ILE A 431      -9.418  13.183  13.478  1.00 20.09           C
ANISOU 3391  C   ILE A 431     2744   2422   2465   -296    322   -239       C
ATOM   3392  O   ILE A 431      -9.193  14.236  14.081  1.00 21.47           O
ANISOU 3392  O   ILE A 431     2934   2614   2608   -283    270   -203       O
ATOM   3393  CB  ILE A 431      -9.447  13.775  11.028  1.00 16.82           C
ANISOU 3393  CB  ILE A 431     2244   2091   2057   -304    279   -303       C
ATOM   3394  CG1 ILE A 431     -10.259  13.649   9.743  1.00 21.55           C
ANISOU 3394  CG1 ILE A 431     2792   2725   2672   -325    293   -376       C
ATOM   3395  CG2 ILE A 431      -8.084  13.084  10.899  1.00 16.90           C
ANISOU 3395  CG2 ILE A 431     2265   2076   2079   -283    283   -254       C
ATOM   3396  CD1 ILE A 431      -9.583  14.352   8.528  1.00 24.60           C
ANISOU 3396  CD1 ILE A 431     3140   3162   3047   -312    238   -373       C
ATOM   3397  N   ILE A 432      -9.000  11.998  13.909  1.00 17.73           N
ANISOU 3397  N   ILE A 432     2474   2074   2190   -293    373   -218       N
ATOM   3398  CA  ILE A 432      -8.297  11.837  15.175  1.00 18.35           C
ANISOU 3398  CA  ILE A 432     2603   2112   2258   -273    374   -153       C
ATOM   3399  C   ILE A 432      -6.881  11.371  14.887  1.00 18.24           C
ANISOU 3399  C   ILE A 432     2594   2086   2251   -248    364   -104       C
ATOM   3400  O   ILE A 432      -6.679  10.424  14.114  1.00 23.66           O
ANISOU 3400  O   ILE A 432     3262   2759   2966   -253    401   -124       O
ATOM   3401  CB  ILE A 432      -9.013  10.830  16.096  1.00 16.76           C
ANISOU 3401  CB  ILE A 432     2437   1857   2075   -288    445   -166       C
ATOM   3402  CG1 ILE A 432     -10.501  11.154  16.234  1.00 14.62           C
ANISOU 3402  CG1 ILE A 432     2155   1598   1802   -317    464   -225       C
ATOM   3403  CG2 ILE A 432      -8.339  10.801  17.465  1.00 18.93           C
ANISOU 3403  CG2 ILE A 432     2764   2094   2333   -266    440    -97       C
ATOM   3404  CD1 ILE A 432     -11.297   9.986  16.889  1.00 18.03           C
ANISOU 3404  CD1 ILE A 432     2615   1977   2261   -337    545   -251       C
ATOM   3405  N   PHE A 433      -5.909  11.999  15.541  1.00 16.24           N
ANISOU 3405  N   PHE A 433     2365   1835   1972   -221    315    -39       N
ATOM   3406  CA  PHE A 433      -4.521  11.558  15.543  1.00 18.39           C
ANISOU 3406  CA  PHE A 433     2649   2090   2248   -194    306     16       C
ATOM   3407  C   PHE A 433      -4.144  11.114  16.950  1.00 19.19           C
ANISOU 3407  C   PHE A 433     2805   2143   2343   -179    327     69       C
ATOM   3408  O   PHE A 433      -4.748  11.539  17.934  1.00 17.38           O
ANISOU 3408  O   PHE A 433     2602   1906   2097   -183    325     74       O
ATOM   3409  CB  PHE A 433      -3.576  12.681  15.077  1.00 16.93           C
ANISOU 3409  CB  PHE A 433     2444   1950   2037   -174    229     50       C
ATOM   3410  CG  PHE A 433      -3.810  13.122  13.660  1.00 15.79           C
ANISOU 3410  CG  PHE A 433     2248   1853   1897   -185    206      4       C
ATOM   3411  CD1 PHE A 433      -3.639  12.236  12.602  1.00 21.41           C
ANISOU 3411  CD1 PHE A 433     2932   2561   2639   -192    239    -25       C
ATOM   3412  CD2 PHE A 433      -4.174  14.434  13.373  1.00 19.16           C
ANISOU 3412  CD2 PHE A 433     2653   2328   2297   -188    151    -10       C
ATOM   3413  CE1 PHE A 433      -3.847  12.653  11.282  1.00 20.31           C
ANISOU 3413  CE1 PHE A 433     2744   2468   2503   -202    217    -67       C
ATOM   3414  CE2 PHE A 433      -4.393  14.846  12.080  1.00 18.02           C
ANISOU 3414  CE2 PHE A 433     2461   2228   2156   -197    130    -51       C
ATOM   3415  CZ  PHE A 433      -4.210  13.968  11.021  1.00 19.15           C
ANISOU 3415  CZ  PHE A 433     2577   2369   2328   -204    161    -79       C
ATOM   3416  N   GLY A 434      -3.136  10.255  17.050  1.00 20.37           N
ANISOU 3416  N   GLY A 434     2972   2261   2507   -159    346    108       N
ATOM   3417  CA  GLY A 434      -2.669   9.824  18.358  1.00 21.76           C
ANISOU 3417  CA  GLY A 434     3200   2393   2676   -140    363    162       C
ATOM   3418  C   GLY A 434      -1.604   8.755  18.261  1.00 18.82           C
ANISOU 3418  C   GLY A 434     2841   1987   2324   -120    391    198       C
ATOM   3419  O   GLY A 434      -1.424   8.112  17.221  1.00 21.13           O
ANISOU 3419  O   GLY A 434     3104   2280   2643   -126    413    172       O
ATOM   3420  N   GLY A 435      -0.891   8.589  19.368  1.00 26.52           N
ANISOU 3420  N   GLY A 435     3858   2932   3285    -95    388    258       N
ATOM   3421  CA  GLY A 435       0.015   7.472  19.526  1.00 26.07           C
ANISOU 3421  CA  GLY A 435     3824   2834   3247    -75    422    294       C
ATOM   3422  C   GLY A 435       0.312   7.210  20.983  1.00 21.96           C
ANISOU 3422  C   GLY A 435     3358   2274   2712    -54    435    348       C
ATOM   3423  O   GLY A 435      -0.402   7.674  21.878  1.00 22.34           O
ANISOU 3423  O   GLY A 435     3430   2318   2741    -62    434    346       O
ATOM   3424  N  AARG A 436       1.395   6.477  21.226  0.07 23.13           N
ANISOU 3424  N  AARG A 436     3527   2394   2867    -27    447    396       N
ATOM   3425  CA AARG A 436       1.784   6.095  22.579  0.07 24.51           C
ANISOU 3425  CA AARG A 436     3755   2528   3028     -3    463    450       C
ATOM   3426  C  AARG A 436       2.722   7.154  23.151  0.07 24.87           C
ANISOU 3426  C  AARG A 436     3811   2604   3037     25    389    506       C
ATOM   3427  O  AARG A 436       3.890   7.240  22.754  0.07 25.05           O
ANISOU 3427  O  AARG A 436     3821   2642   3056     48    354    540       O
ATOM   3428  CB AARG A 436       2.444   4.718  22.577  0.07 24.39           C
ANISOU 3428  CB AARG A 436     3760   2466   3041     13    516    472       C
ATOM   3429  CG AARG A 436       1.593   3.622  21.961  0.07 23.95           C
ANISOU 3429  CG AARG A 436     3694   2380   3025    -15    591    416       C
ATOM   3430  CD AARG A 436       2.360   2.314  21.831  0.07 24.48           C
ANISOU 3430  CD AARG A 436     3776   2405   3120      3    639    440       C
ATOM   3431  NE AARG A 436       2.447   1.603  23.102  0.07 27.28           N
ANISOU 3431  NE AARG A 436     4187   2707   3471     21    680    480       N
ATOM   3432  CZ AARG A 436       1.611   0.639  23.474  0.07 29.57           C
ANISOU 3432  CZ AARG A 436     4502   2950   3784      4    755    455       C
ATOM   3433  NH1AARG A 436       0.625   0.265  22.670  0.07 29.88           N
ANISOU 3433  NH1AARG A 436     4514   2988   3851    -32    797    388       N
ATOM   3434  NH2AARG A 436       1.762   0.048  24.651  0.07 30.14           N
ANISOU 3434  NH2AARG A 436     4627   2975   3850     23    789    496       N
ATOM   3435  N  BARG A 436       1.401   6.485  21.219  0.93 21.84           N
ANISOU 3435  N  BARG A 436     3364   2231   2704    -27    446    396       N
ATOM   3436  CA BARG A 436       1.806   6.097  22.566  0.93 25.75           C
ANISOU 3436  CA BARG A 436     3912   2685   3185     -3    462    450       C
ATOM   3437  C  BARG A 436       2.729   7.162  23.146  0.93 26.16           C
ANISOU 3437  C  BARG A 436     3973   2766   3199     25    388    506       C
ATOM   3438  O  BARG A 436       3.899   7.252  22.758  0.93 24.87           O
ANISOU 3438  O  BARG A 436     3799   2619   3033     49    353    541       O
ATOM   3439  CB BARG A 436       2.499   4.734  22.551  0.93 24.51           C
ANISOU 3439  CB BARG A 436     3774   2483   3056     14    514    474       C
ATOM   3440  CG BARG A 436       1.585   3.552  22.307  0.93 23.29           C
ANISOU 3440  CG BARG A 436     3624   2287   2938    -11    597    426       C
ATOM   3441  CD BARG A 436       2.414   2.303  21.968  0.93 22.39           C
ANISOU 3441  CD BARG A 436     3518   2137   2854      6    639    446       C
ATOM   3442  NE BARG A 436       1.575   1.127  21.799  0.93 26.75           N
ANISOU 3442  NE BARG A 436     4076   2646   3441    -17    722    403       N
ATOM   3443  CZ BARG A 436       1.148   0.364  22.801  0.93 31.02           C
ANISOU 3443  CZ BARG A 436     4664   3135   3988    -16    779    414       C
ATOM   3444  NH1BARG A 436       1.478   0.656  24.054  0.93 30.07           N
ANISOU 3444  NH1BARG A 436     4586   3001   3838      7    761    467       N
ATOM   3445  NH2BARG A 436       0.383  -0.690  22.551  0.93 31.88           N
ANISOU 3445  NH2BARG A 436     4776   3207   4131    -40    855    371       N
ATOM   3446  N   ARG A 437       2.216   7.949  24.091  1.00 22.76           N
ANISOU 3446  N   ARG A 437     3564   2343   2740     22    365    515       N
ATOM   3447  CA  ARG A 437       3.014   8.968  24.776  1.00 21.69           C
ANISOU 3447  CA  ARG A 437     3441   2233   2566     48    298    567       C
ATOM   3448  C   ARG A 437       2.890   8.767  26.281  1.00 25.21           C
ANISOU 3448  C   ARG A 437     3941   2643   2994     61    317    605       C
ATOM   3449  O   ARG A 437       1.856   9.128  26.870  1.00 25.79           O
ANISOU 3449  O   ARG A 437     4028   2714   3057     42    328    582       O
ATOM   3450  CB  ARG A 437       2.591  10.390  24.405  1.00 18.18           C
ANISOU 3450  CB  ARG A 437     2966   1843   2100     32    238    544       C
ATOM   3451  CG  ARG A 437       2.885  10.804  22.962  1.00 26.03           C
ANISOU 3451  CG  ARG A 437     3907   2880   3104     25    205    516       C
ATOM   3452  CD  ARG A 437       4.331  10.553  22.586  1.00 27.40           C
ANISOU 3452  CD  ARG A 437     4073   3057   3280     54    181    559       C
ATOM   3453  NE  ARG A 437       5.323  11.363  23.297  1.00 21.77           N
ANISOU 3453  NE  ARG A 437     3377   2362   2534     82    122    618       N
ATOM   3454  CZ  ARG A 437       5.650  12.621  22.983  1.00 21.91           C
ANISOU 3454  CZ  ARG A 437     3370   2428   2528     84     54    623       C
ATOM   3455  NH1 ARG A 437       5.035  13.267  21.999  1.00 19.68           N
ANISOU 3455  NH1 ARG A 437     3047   2181   2248     60     36    575       N
ATOM   3456  NH2 ARG A 437       6.599  13.241  23.668  1.00 19.92           N
ANISOU 3456  NH2 ARG A 437     3133   2188   2247    110      5    677       N
ATOM   3457  N   PRO A 438       3.912   8.210  26.939  1.00 29.68           N
ANISOU 3457  N   PRO A 438     4538   3183   3555     94    321    662       N
ATOM   3458  CA  PRO A 438       3.797   7.959  28.385  1.00 30.55           C
ANISOU 3458  CA  PRO A 438     4702   3257   3647    108    342    699       C
ATOM   3459  C   PRO A 438       3.791   9.228  29.212  1.00 32.46           C
ANISOU 3459  C   PRO A 438     4955   3529   3848    114    283    722       C
ATOM   3460  O   PRO A 438       3.320   9.206  30.354  1.00 35.36           O
ANISOU 3460  O   PRO A 438     5362   3873   4200    116    301    737       O
ATOM   3461  CB  PRO A 438       5.027   7.091  28.693  1.00 35.29           C
ANISOU 3461  CB  PRO A 438     5327   3829   4253    145    355    754       C
ATOM   3462  CG  PRO A 438       6.018   7.456  27.613  1.00 31.90           C
ANISOU 3462  CG  PRO A 438     4855   3438   3828    155    307    760       C
ATOM   3463  CD  PRO A 438       5.187   7.714  26.388  1.00 29.06           C
ANISOU 3463  CD  PRO A 438     4449   3104   3488    120    311    694       C
ATOM   3464  N   ALA A 439       4.260  10.344  28.667  1.00 28.49           N
ANISOU 3464  N   ALA A 439     4420   3078   3329    116    215    725       N
ATOM   3465  CA  ALA A 439       4.411  11.554  29.451  1.00 29.72           C
ANISOU 3465  CA  ALA A 439     4585   3262   3444    125    156    752       C
ATOM   3466  C   ALA A 439       3.896  12.737  28.659  1.00 30.31           C
ANISOU 3466  C   ALA A 439     4618   3388   3512    102    110    712       C
ATOM   3467  O   ALA A 439       3.924  12.735  27.427  1.00 26.63           O
ANISOU 3467  O   ALA A 439     4110   2942   3064     90    105    680       O
ATOM   3468  CB  ALA A 439       5.872  11.806  29.840  1.00 30.38           C
ANISOU 3468  CB  ALA A 439     4636   3382   3527    151     97    788       C
ATOM   3469  N   GLY A 440       3.411  13.739  29.387  1.00 29.28           N
ANISOU 3469  N   GLY A 440     4498   3275   3351     96     77    714       N
ATOM   3470  CA  GLY A 440       3.269  15.074  28.848  1.00 24.66           C
ANISOU 3470  CA  GLY A 440     3879   2742   2749     84     17    695       C
ATOM   3471  C   GLY A 440       2.038  15.386  28.014  1.00 31.81           C
ANISOU 3471  C   GLY A 440     4752   3666   3668     48     30    629       C
ATOM   3472  O   GLY A 440       1.544  16.518  28.042  1.00 29.71           O
ANISOU 3472  O   GLY A 440     4473   3433   3381     36    -10    613       O
ATOM   3473  N   VAL A 441       1.547  14.413  27.257  1.00 24.16           N
ANISOU 3473  N   VAL A 441     3769   2676   2734     32     84    589       N
ATOM   3474  CA  VAL A 441       0.472  14.623  26.288  1.00 21.96           C
ANISOU 3474  CA  VAL A 441     3454   2419   2472     -1     96    523       C
ATOM   3475  C   VAL A 441      -0.851  14.253  26.946  1.00 25.18           C
ANISOU 3475  C   VAL A 441     3885   2798   2886    -24    148    489       C
ATOM   3476  O   VAL A 441      -1.015  13.096  27.380  1.00 22.06           O
ANISOU 3476  O   VAL A 441     3518   2356   2510    -23    209    492       O
ATOM   3477  CB  VAL A 441       0.704  13.800  25.012  1.00 22.22           C
ANISOU 3477  CB  VAL A 441     3454   2450   2539     -6    124    496       C
ATOM   3478  CG1 VAL A 441      -0.396  14.069  23.998  1.00 17.95           C
ANISOU 3478  CG1 VAL A 441     2874   1935   2013    -39    133    427       C
ATOM   3479  CG2 VAL A 441       2.073  14.124  24.419  1.00 19.12           C
ANISOU 3479  CG2 VAL A 441     3041   2083   2140     18     74    532       C
ATOM   3480  N   PRO A 442      -1.817  15.179  27.041  1.00 26.76           N
ANISOU 3480  N   PRO A 442     4075   3023   3071    -45    128    457       N
ATOM   3481  CA  PRO A 442      -3.087  14.864  27.706  1.00 27.40           C
ANISOU 3481  CA  PRO A 442     4178   3077   3156    -67    177    425       C
ATOM   3482  C   PRO A 442      -3.933  13.864  26.938  1.00 27.08           C
ANISOU 3482  C   PRO A 442     4119   3016   3153    -93    241    367       C
ATOM   3483  O   PRO A 442      -3.601  13.465  25.817  1.00 21.94           O
ANISOU 3483  O   PRO A 442     3436   2376   2525    -95    247    349       O
ATOM   3484  CB  PRO A 442      -3.793  16.229  27.800  1.00 22.73           C
ANISOU 3484  CB  PRO A 442     3572   2526   2539    -81    130    403       C
ATOM   3485  CG  PRO A 442      -2.800  17.241  27.346  1.00 25.51           C
ANISOU 3485  CG  PRO A 442     3901   2922   2870    -63     57    432       C
ATOM   3486  CD  PRO A 442      -1.781  16.558  26.531  1.00 23.91           C
ANISOU 3486  CD  PRO A 442     3682   2716   2688    -48     61    448       C
ATOM   3487  N   LEU A 443      -5.056  13.479  27.547  1.00 23.52           N
ANISOU 3487  N   LEU A 443     3690   2538   2710   -113    290    338       N
ATOM   3488  CA  LEU A 443      -5.908  12.431  27.000  1.00 23.84           C
ANISOU 3488  CA  LEU A 443     3718   2552   2786   -138    359    284       C
ATOM   3489  C   LEU A 443      -6.530  12.840  25.669  1.00 24.02           C
ANISOU 3489  C   LEU A 443     3687   2617   2822   -162    347    223       C
ATOM   3490  O   LEU A 443      -6.605  12.023  24.740  1.00 21.92           O
ANISOU 3490  O   LEU A 443     3397   2343   2587   -172    383    190       O
ATOM   3491  CB  LEU A 443      -6.996  12.073  28.016  1.00 23.39           C
ANISOU 3491  CB  LEU A 443     3696   2459   2730   -155    410    267       C
ATOM   3492  CG  LEU A 443      -8.101  11.095  27.606  1.00 23.66           C
ANISOU 3492  CG  LEU A 443     3723   2468   2800   -186    484    205       C
ATOM   3493  CD1 LEU A 443      -7.540   9.701  27.412  1.00 25.28           C
ANISOU 3493  CD1 LEU A 443     3940   2629   3035   -177    539    218       C
ATOM   3494  CD2 LEU A 443      -9.209  11.104  28.651  1.00 22.26           C
ANISOU 3494  CD2 LEU A 443     3576   2266   2615   -204    518    188       C
ATOM   3495  N   VAL A 444      -6.982  14.087  25.548  1.00 16.55           N
ANISOU 3495  N   VAL A 444     2721   1714   1853   -170    296    206       N
ATOM   3496  CA  VAL A 444      -7.565  14.531  24.288  1.00 17.14           C
ANISOU 3496  CA  VAL A 444     2744   1831   1937   -190    281    149       C
ATOM   3497  C   VAL A 444      -7.422  16.047  24.182  1.00 20.44           C
ANISOU 3497  C   VAL A 444     3144   2300   2322   -184    205    160       C
ATOM   3498  O   VAL A 444      -7.601  16.779  25.164  1.00 22.08           O
ANISOU 3498  O   VAL A 444     3377   2510   2502   -179    180    182       O
ATOM   3499  CB  VAL A 444      -9.039  14.070  24.170  1.00 19.85           C
ANISOU 3499  CB  VAL A 444     3079   2161   2301   -224    338     82       C
ATOM   3500  CG1 VAL A 444      -9.898  14.609  25.329  1.00 18.54           C
ANISOU 3500  CG1 VAL A 444     2942   1987   2114   -234    339     81       C
ATOM   3501  CG2 VAL A 444      -9.637  14.448  22.808  1.00 16.75           C
ANISOU 3501  CG2 VAL A 444     2631   1813   1920   -244    325     21       C
ATOM   3502  N   TYR A 445      -7.102  16.518  22.983  1.00 15.60           N
ANISOU 3502  N   TYR A 445     2488   1729   1712   -183    169    143       N
ATOM   3503  CA  TYR A 445      -7.234  17.943  22.714  1.00 18.05           C
ANISOU 3503  CA  TYR A 445     2776   2090   1994   -183    104    138       C
ATOM   3504  C   TYR A 445      -7.712  18.139  21.282  1.00 19.70           C
ANISOU 3504  C   TYR A 445     2932   2336   2217   -200     98     81       C
ATOM   3505  O   TYR A 445      -7.695  17.218  20.463  1.00 16.56           O
ANISOU 3505  O   TYR A 445     2515   1929   1849   -207    135     55       O
ATOM   3506  CB  TYR A 445      -5.933  18.719  23.010  1.00 19.21           C
ANISOU 3506  CB  TYR A 445     2932   2253   2113   -154     41    202       C
ATOM   3507  CG  TYR A 445      -4.708  18.370  22.185  1.00 23.52           C
ANISOU 3507  CG  TYR A 445     3460   2806   2671   -135     25    227       C
ATOM   3508  CD1 TYR A 445      -3.843  17.357  22.579  1.00 19.99           C
ANISOU 3508  CD1 TYR A 445     3039   2320   2236   -118     54    267       C
ATOM   3509  CD2 TYR A 445      -4.378  19.111  21.046  1.00 29.37           C
ANISOU 3509  CD2 TYR A 445     4160   3594   3407   -133    -21    214       C
ATOM   3510  CE1 TYR A 445      -2.695  17.059  21.839  1.00 20.44           C
ANISOU 3510  CE1 TYR A 445     3080   2384   2304   -100     38    291       C
ATOM   3511  CE2 TYR A 445      -3.235  18.821  20.300  1.00 24.88           C
ANISOU 3511  CE2 TYR A 445     3574   3031   2848   -117    -36    238       C
ATOM   3512  CZ  TYR A 445      -2.401  17.796  20.704  1.00 19.06           C
ANISOU 3512  CZ  TYR A 445     2863   2256   2125   -100     -7    276       C
ATOM   3513  OH  TYR A 445      -1.272  17.504  19.967  1.00 22.19           O
ANISOU 3513  OH  TYR A 445     3242   2659   2531    -83    -22    299       O
ATOM   3514  N   GLU A 446      -8.181  19.347  20.997  1.00 20.73           N
ANISOU 3514  N   GLU A 446     3040   2510   2326   -205     51     62       N
ATOM   3515  CA  GLU A 446      -8.770  19.675  19.708  1.00 21.23           C
ANISOU 3515  CA  GLU A 446     3055   2614   2398   -221     42      6       C
ATOM   3516  C   GLU A 446      -7.934  20.748  19.033  1.00 20.35           C
ANISOU 3516  C   GLU A 446     2919   2548   2266   -204    -28     30       C
ATOM   3517  O   GLU A 446      -7.490  21.693  19.687  1.00 20.13           O
ANISOU 3517  O   GLU A 446     2908   2531   2208   -189    -76     70       O
ATOM   3518  CB  GLU A 446     -10.208  20.160  19.884  1.00 17.50           C
ANISOU 3518  CB  GLU A 446     2575   2156   1920   -245     51    -45       C
ATOM   3519  CG  GLU A 446     -10.895  20.695  18.633  1.00 22.04           C
ANISOU 3519  CG  GLU A 446     3099   2777   2497   -259     34   -103       C
ATOM   3520  CD  GLU A 446     -12.222  21.339  18.980  1.00 30.35           C
ANISOU 3520  CD  GLU A 446     4149   3845   3538   -278     35   -145       C
ATOM   3521  OE1 GLU A 446     -12.849  20.872  19.944  1.00 25.36           O
ANISOU 3521  OE1 GLU A 446     3547   3178   2911   -289     76   -150       O
ATOM   3522  OE2 GLU A 446     -12.631  22.321  18.322  1.00 26.72           O
ANISOU 3522  OE2 GLU A 446     3657   3431   3063   -281     -5   -171       O
ATOM   3523  N   ALA A 447      -7.723  20.588  17.731  1.00 17.23           N
ANISOU 3523  N   ALA A 447     2484   2176   1885   -206    -32      4       N
ATOM   3524  CA  ALA A 447      -6.920  21.530  16.956  1.00 20.87           C
ANISOU 3524  CA  ALA A 447     2919   2680   2329   -190    -94     23       C
ATOM   3525  C   ALA A 447      -7.657  22.854  16.765  1.00 17.84           C
ANISOU 3525  C   ALA A 447     2517   2341   1921   -197   -138     -2       C
ATOM   3526  O   ALA A 447      -8.882  22.893  16.620  1.00 27.32           O
ANISOU 3526  O   ALA A 447     3705   3550   3127   -218   -116    -55       O
ATOM   3527  CB  ALA A 447      -6.570  20.924  15.595  1.00 15.91           C
ANISOU 3527  CB  ALA A 447     2255   2066   1726   -192    -82     -2       C
ATOM   3528  N   LEU A 448      -6.880  23.949  16.710  1.00 20.79           N
ANISOU 3528  N   LEU A 448     2888   2744   2269   -179   -200     35       N
ATOM   3529  CA  LEU A 448      -7.430  25.308  16.671  1.00 24.68           C
ANISOU 3529  CA  LEU A 448     3368   3275   2733   -182   -247     22       C
ATOM   3530  C   LEU A 448      -7.954  25.697  15.297  1.00 26.06           C
ANISOU 3530  C   LEU A 448     3496   3494   2913   -191   -259    -29       C
ATOM   3531  O   LEU A 448      -8.771  26.618  15.194  1.00 21.04           O
ANISOU 3531  O   LEU A 448     2847   2887   2259   -199   -282    -57       O
ATOM   3532  CB  LEU A 448      -6.364  26.321  17.098  1.00 20.59           C
ANISOU 3532  CB  LEU A 448     2864   2771   2186   -159   -307     80       C
ATOM   3533  CG  LEU A 448      -5.672  26.135  18.442  1.00 23.02           C
ANISOU 3533  CG  LEU A 448     3218   3044   2484   -146   -307    138       C
ATOM   3534  CD1 LEU A 448      -4.493  27.081  18.567  1.00 28.56           C
ANISOU 3534  CD1 LEU A 448     3925   3766   3161   -123   -368    191       C
ATOM   3535  CD2 LEU A 448      -6.649  26.362  19.602  1.00 20.97           C
ANISOU 3535  CD2 LEU A 448     2988   2768   2212   -157   -292    129       C
ATOM   3536  N   SER A 449      -7.507  25.009  14.253  1.00 21.71           N
ANISOU 3536  N   SER A 449     2919   2946   2382   -190   -244    -42       N
ATOM   3537  CA  SER A 449      -7.862  25.282  12.871  1.00 21.09           C
ANISOU 3537  CA  SER A 449     2794   2909   2309   -197   -256    -88       C
ATOM   3538  C   SER A 449      -7.444  24.071  12.054  1.00 18.91           C
ANISOU 3538  C   SER A 449     2502   2618   2065   -199   -217   -101       C
ATOM   3539  O   SER A 449      -6.774  23.163  12.553  1.00 22.75           O
ANISOU 3539  O   SER A 449     3012   3065   2566   -193   -189    -70       O
ATOM   3540  CB  SER A 449      -7.154  26.526  12.337  1.00 22.19           C
ANISOU 3540  CB  SER A 449     2918   3090   2423   -180   -323    -63       C
ATOM   3541  OG  SER A 449      -5.754  26.308  12.424  1.00 20.36           O
ANISOU 3541  OG  SER A 449     2699   2844   2192   -160   -339     -8       O
ATOM   3542  N   TRP A 450      -7.843  24.077  10.786  1.00 20.86           N
ANISOU 3542  N   TRP A 450     2707   2898   2321   -208   -216   -149       N
ATOM   3543  CA  TRP A 450      -7.345  23.076   9.845  1.00 22.02           C
ANISOU 3543  CA  TRP A 450     2832   3038   2496   -208   -188   -161       C
ATOM   3544  C   TRP A 450      -5.821  23.077   9.789  1.00 24.67           C
ANISOU 3544  C   TRP A 450     3178   3367   2828   -185   -217   -101       C
ATOM   3545  O   TRP A 450      -5.180  22.022   9.883  1.00 19.69           O
ANISOU 3545  O   TRP A 450     2559   2703   2220   -181   -184    -82       O
ATOM   3546  CB  TRP A 450      -7.927  23.346   8.464  1.00 18.63           C
ANISOU 3546  CB  TRP A 450     2356   2654   2070   -218   -196   -216       C
ATOM   3547  CG  TRP A 450      -7.598  22.289   7.473  1.00 18.24           C
ANISOU 3547  CG  TRP A 450     2281   2599   2050   -222   -162   -238       C
ATOM   3548  CD1 TRP A 450      -6.753  22.395   6.405  1.00 20.21           C
ANISOU 3548  CD1 TRP A 450     2505   2872   2301   -210   -187   -229       C
ATOM   3549  CD2 TRP A 450      -8.100  20.950   7.464  1.00 21.52           C
ANISOU 3549  CD2 TRP A 450     2698   2982   2499   -239    -96   -272       C
ATOM   3550  NE1 TRP A 450      -6.710  21.191   5.717  1.00 20.92           N
ANISOU 3550  NE1 TRP A 450     2578   2948   2424   -219   -140   -257       N
ATOM   3551  CE2 TRP A 450      -7.523  20.290   6.355  1.00 20.85           C
ANISOU 3551  CE2 TRP A 450     2585   2903   2434   -237    -84   -283       C
ATOM   3552  CE3 TRP A 450      -8.984  20.240   8.293  1.00 21.22           C
ANISOU 3552  CE3 TRP A 450     2681   2908   2475   -257    -44   -295       C
ATOM   3553  CZ2 TRP A 450      -7.804  18.952   6.047  1.00 23.10           C
ANISOU 3553  CZ2 TRP A 450     2863   3161   2754   -253    -21   -317       C
ATOM   3554  CZ3 TRP A 450      -9.269  18.919   7.981  1.00 20.22           C
ANISOU 3554  CZ3 TRP A 450     2547   2754   2382   -272     19   -328       C
ATOM   3555  CH2 TRP A 450      -8.677  18.288   6.871  1.00 22.60           C
ANISOU 3555  CH2 TRP A 450     2821   3063   2704   -270     29   -339       C
ATOM   3556  N   GLN A 451      -5.222  24.262   9.632  1.00 21.96           N
ANISOU 3556  N   GLN A 451     2829   3056   2458   -169   -278    -71       N
ATOM   3557  CA  GLN A 451      -3.773  24.347   9.494  1.00 20.26           C
ANISOU 3557  CA  GLN A 451     2620   2840   2239   -148   -308    -17       C
ATOM   3558  C   GLN A 451      -3.076  23.848  10.749  1.00 17.57           C
ANISOU 3558  C   GLN A 451     2322   2455   1899   -137   -295     36       C
ATOM   3559  O   GLN A 451      -2.077  23.121  10.672  1.00 19.93           O
ANISOU 3559  O   GLN A 451     2628   2733   2213   -125   -284     67       O
ATOM   3560  CB  GLN A 451      -3.352  25.794   9.182  1.00 21.79           C
ANISOU 3560  CB  GLN A 451     2802   3076   2402   -134   -375      3       C
ATOM   3561  CG  GLN A 451      -3.901  26.340   7.860  1.00 23.39           C
ANISOU 3561  CG  GLN A 451     2961   3325   2600   -141   -393    -45       C
ATOM   3562  CD  GLN A 451      -5.403  26.640   7.882  1.00 24.43           C
ANISOU 3562  CD  GLN A 451     3083   3472   2728   -160   -378    -99       C
ATOM   3563  OE1 GLN A 451      -5.975  27.006   8.922  1.00 23.42           O
ANISOU 3563  OE1 GLN A 451     2980   3331   2586   -164   -378    -94       O
ATOM   3564  NE2 GLN A 451      -6.051  26.480   6.726  1.00 23.37           N
ANISOU 3564  NE2 GLN A 451     2910   3365   2604   -171   -366   -153       N
ATOM   3565  N   HIS A 452      -3.592  24.223  11.920  1.00 16.62           N
ANISOU 3565  N   HIS A 452     2232   2319   1763   -140   -296     47       N
ATOM   3566  CA  HIS A 452      -3.034  23.692  13.149  1.00 12.12           C
ANISOU 3566  CA  HIS A 452     1705   1707   1194   -129   -280     95       C
ATOM   3567  C   HIS A 452      -3.212  22.180  13.201  1.00 14.03           C
ANISOU 3567  C   HIS A 452     1955   1907   1470   -138   -213     79       C
ATOM   3568  O   HIS A 452      -2.321  21.462  13.655  1.00 17.26           O
ANISOU 3568  O   HIS A 452     2386   2283   1887   -125   -199    119       O
ATOM   3569  CB  HIS A 452      -3.693  24.337  14.361  1.00 15.85           C
ANISOU 3569  CB  HIS A 452     2207   2171   1644   -133   -289    103       C
ATOM   3570  CG  HIS A 452      -3.172  23.830  15.665  1.00 19.02           C
ANISOU 3570  CG  HIS A 452     2653   2529   2043   -123   -273    152       C
ATOM   3571  ND1 HIS A 452      -4.000  23.475  16.708  1.00 18.15           N
ANISOU 3571  ND1 HIS A 452     2573   2389   1934   -134   -237    143       N
ATOM   3572  CD2 HIS A 452      -1.907  23.622  16.098  1.00 18.56           C
ANISOU 3572  CD2 HIS A 452     2615   2455   1982   -101   -288    208       C
ATOM   3573  CE1 HIS A 452      -3.264  23.080  17.731  1.00 19.76           C
ANISOU 3573  CE1 HIS A 452     2814   2560   2135   -119   -231    194       C
ATOM   3574  NE2 HIS A 452      -1.992  23.162  17.388  1.00 20.24           N
ANISOU 3574  NE2 HIS A 452     2869   2628   2192    -98   -262    234       N
ATOM   3575  N   GLY A 453      -4.346  21.687  12.705  1.00 17.40           N
ANISOU 3575  N   GLY A 453     2363   2335   1915   -161   -173     19       N
ATOM   3576  CA  GLY A 453      -4.606  20.258  12.759  1.00 16.00           C
ANISOU 3576  CA  GLY A 453     2193   2117   1770   -172   -106     -1       C
ATOM   3577  C   GLY A 453      -3.666  19.467  11.870  1.00 17.15           C
ANISOU 3577  C   GLY A 453     2321   2258   1938   -163    -94      8       C
ATOM   3578  O   GLY A 453      -3.236  18.373  12.232  1.00 21.42           O
ANISOU 3578  O   GLY A 453     2882   2758   2500   -159    -53     26       O
ATOM   3579  N   VAL A 454      -3.329  20.013  10.695  1.00 19.18           N
ANISOU 3579  N   VAL A 454     2541   2556   2191   -159   -129     -5       N
ATOM   3580  CA  VAL A 454      -2.310  19.393   9.852  1.00 18.23           C
ANISOU 3580  CA  VAL A 454     2404   2435   2089   -149   -126      9       C
ATOM   3581  C   VAL A 454      -0.962  19.399  10.569  1.00 18.95           C
ANISOU 3581  C   VAL A 454     2525   2505   2171   -123   -149     80       C
ATOM   3582  O   VAL A 454      -0.186  18.443  10.476  1.00 21.14           O
ANISOU 3582  O   VAL A 454     2809   2756   2469   -114   -124    100       O
ATOM   3583  CB  VAL A 454      -2.234  20.111   8.485  1.00 18.52           C
ANISOU 3583  CB  VAL A 454     2395   2523   2119   -149   -164    -17       C
ATOM   3584  CG1 VAL A 454      -1.169  19.498   7.608  1.00 14.79           C
ANISOU 3584  CG1 VAL A 454     1906   2049   1665   -138   -161     -3       C
ATOM   3585  CG2 VAL A 454      -3.580  20.063   7.759  1.00 16.69           C
ANISOU 3585  CG2 VAL A 454     2132   2312   1895   -173   -140    -89       C
ATOM   3586  N   PHE A 455      -0.655  20.479  11.290  1.00 15.35           N
ANISOU 3586  N   PHE A 455     2087   2063   1684   -111   -199    117       N
ATOM   3587  CA  PHE A 455       0.579  20.490  12.076  1.00 13.45           C
ANISOU 3587  CA  PHE A 455     1875   1802   1433    -87   -220    184       C
ATOM   3588  C   PHE A 455       0.552  19.396  13.149  1.00 17.57           C
ANISOU 3588  C   PHE A 455     2436   2271   1969    -85   -169    203       C
ATOM   3589  O   PHE A 455       1.575  18.752  13.412  1.00 19.35           O
ANISOU 3589  O   PHE A 455     2678   2471   2203    -68   -161    244       O
ATOM   3590  CB  PHE A 455       0.803  21.871  12.711  1.00 14.59           C
ANISOU 3590  CB  PHE A 455     2033   1971   1541    -76   -280    216       C
ATOM   3591  CG  PHE A 455       1.808  21.859  13.831  1.00 16.32           C
ANISOU 3591  CG  PHE A 455     2289   2165   1747    -54   -296    280       C
ATOM   3592  CD1 PHE A 455       3.161  21.998  13.569  1.00 16.07           C
ANISOU 3592  CD1 PHE A 455     2253   2142   1711    -33   -329    324       C
ATOM   3593  CD2 PHE A 455       1.387  21.693  15.152  1.00 11.43           C
ANISOU 3593  CD2 PHE A 455     1708   1515   1119    -55   -276    297       C
ATOM   3594  CE1 PHE A 455       4.095  21.952  14.603  1.00 15.73           C
ANISOU 3594  CE1 PHE A 455     2244   2078   1657    -12   -342    382       C
ATOM   3595  CE2 PHE A 455       2.303  21.646  16.187  1.00 16.81           C
ANISOU 3595  CE2 PHE A 455     2424   2174   1789    -34   -289    355       C
ATOM   3596  CZ  PHE A 455       3.656  21.770  15.920  1.00 13.92           C
ANISOU 3596  CZ  PHE A 455     2052   1817   1418    -12   -323    398       C
ATOM   3597  N   VAL A 456      -0.600  19.198  13.796  1.00 15.94           N
ANISOU 3597  N   VAL A 456     2246   2046   1764   -102   -135    174       N
ATOM   3598  CA  VAL A 456      -0.715  18.177  14.838  1.00 15.05           C
ANISOU 3598  CA  VAL A 456     2171   1881   1664   -102    -84    191       C
ATOM   3599  C   VAL A 456      -0.464  16.793  14.249  1.00 16.97           C
ANISOU 3599  C   VAL A 456     2407   2096   1944   -105    -31    177       C
ATOM   3600  O   VAL A 456       0.259  15.979  14.829  1.00 20.55           O
ANISOU 3600  O   VAL A 456     2889   2512   2408    -90     -7    215       O
ATOM   3601  CB  VAL A 456      -2.092  18.251  15.518  1.00 14.51           C
ANISOU 3601  CB  VAL A 456     2118   1803   1593   -123    -56    155       C
ATOM   3602  CG1 VAL A 456      -2.296  17.058  16.459  1.00 17.50           C
ANISOU 3602  CG1 VAL A 456     2534   2125   1989   -125      5    165       C
ATOM   3603  CG2 VAL A 456      -2.239  19.565  16.278  1.00 15.94           C
ANISOU 3603  CG2 VAL A 456     2313   2005   1737   -118   -108    177       C
ATOM   3604  N   GLY A 457      -1.055  16.509  13.091  1.00 16.66           N
ANISOU 3604  N   GLY A 457     2330   2075   1924   -123    -10    122       N
ATOM   3605  CA  GLY A 457      -0.727  15.271  12.400  1.00 21.54           C
ANISOU 3605  CA  GLY A 457     2936   2670   2576   -125     36    108       C
ATOM   3606  C   GLY A 457       0.753  15.161  12.096  1.00 22.71           C
ANISOU 3606  C   GLY A 457     3083   2820   2725   -100      9    157       C
ATOM   3607  O   GLY A 457       1.364  14.117  12.317  1.00 18.03           O
ANISOU 3607  O   GLY A 457     2508   2190   2152    -90     44    181       O
ATOM   3608  N   ALA A 458       1.359  16.257  11.611  1.00 17.39           N
ANISOU 3608  N   ALA A 458     2390   2189   2029    -88    -55    175       N
ATOM   3609  CA  ALA A 458       2.757  16.215  11.203  1.00 15.37           C
ANISOU 3609  CA  ALA A 458     2128   1939   1775    -66    -83    217       C
ATOM   3610  C   ALA A 458       3.677  16.027  12.396  1.00 18.80           C
ANISOU 3610  C   ALA A 458     2603   2341   2198    -42    -89    282       C
ATOM   3611  O   ALA A 458       4.777  15.480  12.253  1.00 19.29           O
ANISOU 3611  O   ALA A 458     2668   2389   2270    -23    -88    316       O
ATOM   3612  CB  ALA A 458       3.117  17.514  10.434  1.00 14.67           C
ANISOU 3612  CB  ALA A 458     2008   1903   1662    -60   -149    219       C
ATOM   3613  N   ALA A 459       3.243  16.463  13.579  1.00 17.17           N
ANISOU 3613  N   ALA A 459     2429   2124   1972    -41    -95    299       N
ATOM   3614  CA  ALA A 459       4.044  16.408  14.797  1.00 15.58           C
ANISOU 3614  CA  ALA A 459     2268   1896   1756    -18   -106    360       C
ATOM   3615  C   ALA A 459       3.890  15.107  15.572  1.00 15.97           C
ANISOU 3615  C   ALA A 459     2352   1891   1826    -17    -43    368       C
ATOM   3616  O   ALA A 459       4.535  14.958  16.616  1.00 22.80           O
ANISOU 3616  O   ALA A 459     3253   2731   2679      4    -47    419       O
ATOM   3617  CB  ALA A 459       3.676  17.572  15.732  1.00 14.80           C
ANISOU 3617  CB  ALA A 459     2188   1812   1622    -17   -146    375       C
ATOM   3618  N   MET A 460       3.084  14.164  15.091  1.00 19.76           N
ANISOU 3618  N   MET A 460     2822   2350   2335    -37     16    321       N
ATOM   3619  CA  MET A 460       2.849  12.921  15.835  1.00 19.89           C
ANISOU 3619  CA  MET A 460     2872   2313   2372    -38     80    326       C
ATOM   3620  C   MET A 460       4.146  12.224  16.216  1.00 22.06           C
ANISOU 3620  C   MET A 460     3170   2560   2653     -9     85    383       C
ATOM   3621  O   MET A 460       5.103  12.156  15.430  1.00 23.42           O
ANISOU 3621  O   MET A 460     3320   2747   2832      4     64    398       O
ATOM   3622  CB  MET A 460       1.982  11.964  15.021  1.00 15.42           C
ANISOU 3622  CB  MET A 460     2285   1733   1840    -63    140    266       C
ATOM   3623  CG  MET A 460       0.523  12.331  15.067  1.00 22.85           C
ANISOU 3623  CG  MET A 460     3219   2685   2778    -92    156    212       C
ATOM   3624  SD  MET A 460      -0.449  11.368  13.918  1.00 20.00           S
ANISOU 3624  SD  MET A 460     2824   2320   2457   -123    217    136       S
ATOM   3625  CE  MET A 460      -0.276   9.725  14.603  1.00 18.47           C
ANISOU 3625  CE  MET A 460     2669   2057   2294   -119    295    153       C
ATOM   3626  N   ARG A 461       4.167  11.708  17.441  1.00 19.81           N
ANISOU 3626  N   ARG A 461     2930   2233   2364      2    113    415       N
ATOM   3627  CA  ARG A 461       5.274  10.910  17.936  1.00 20.25           C
ANISOU 3627  CA  ARG A 461     3013   2256   2427     29    127    468       C
ATOM   3628  C   ARG A 461       4.702   9.774  18.762  1.00 21.26           C
ANISOU 3628  C   ARG A 461     3177   2328   2571     25    196    465       C
ATOM   3629  O   ARG A 461       3.608   9.881  19.332  1.00 21.74           O
ANISOU 3629  O   ARG A 461     3254   2379   2628      6    219    440       O
ATOM   3630  CB  ARG A 461       6.262  11.738  18.769  1.00 15.67           C
ANISOU 3630  CB  ARG A 461     2452   1689   1812     58     68    530       C
ATOM   3631  CG  ARG A 461       6.894  12.922  17.959  1.00 17.29           C
ANISOU 3631  CG  ARG A 461     2621   1950   2000     63     -3    534       C
ATOM   3632  CD  ARG A 461       7.675  13.843  18.873  1.00 20.19           C
ANISOU 3632  CD  ARG A 461     3009   2331   2332     86    -60    589       C
ATOM   3633  NE  ARG A 461       8.952  13.255  19.255  1.00 22.26           N
ANISOU 3633  NE  ARG A 461     3290   2573   2596    117    -61    643       N
ATOM   3634  CZ  ARG A 461       9.599  13.527  20.381  1.00 30.83           C
ANISOU 3634  CZ  ARG A 461     4408   3650   3657    141    -86    696       C
ATOM   3635  NH1 ARG A 461       9.084  14.383  21.263  1.00 28.99           N
ANISOU 3635  NH1 ARG A 461     4193   3426   3396    137   -110    702       N
ATOM   3636  NH2 ARG A 461      10.759  12.933  20.629  1.00 29.86           N
ANISOU 3636  NH2 ARG A 461     4298   3509   3537    170    -85    742       N
ATOM   3637  N   SER A 462       5.448   8.684  18.830  1.00 20.37           N
ANISOU 3637  N   SER A 462     3081   2180   2479     42    231    492       N
ATOM   3638  CA  SER A 462       4.909   7.514  19.506  1.00 21.64           C
ANISOU 3638  CA  SER A 462     3277   2286   2660     38    303    487       C
ATOM   3639  C   SER A 462       6.045   6.627  19.991  1.00 27.74           C
ANISOU 3639  C   SER A 462     4078   3022   3439     70    321    543       C
ATOM   3640  O   SER A 462       7.079   6.493  19.334  1.00 24.91           O
ANISOU 3640  O   SER A 462     3701   2676   3088     87    300    563       O
ATOM   3641  CB  SER A 462       3.973   6.726  18.584  1.00 23.06           C
ANISOU 3641  CB  SER A 462     3432   2455   2875      7    361    422       C
ATOM   3642  OG  SER A 462       3.403   5.639  19.283  1.00 22.88           O
ANISOU 3642  OG  SER A 462     3445   2378   2871      0    431    416       O
ATOM   3643  N   GLU A 463       5.819   6.001  21.144  1.00 28.42           N
ANISOU 3643  N   GLU A 463     4211   3064   3524     78    361    566       N
ATOM   3644  CA  GLU A 463       6.841   5.179  21.771  1.00 36.15           C
ANISOU 3644  CA  GLU A 463     5224   4006   4506    111    379    621       C
ATOM   3645  C   GLU A 463       7.248   4.014  20.874  1.00 38.10           C
ANISOU 3645  C   GLU A 463     5456   4230   4791    112    424    609       C
ATOM   3646  O   GLU A 463       6.416   3.404  20.195  1.00 38.54           O
ANISOU 3646  O   GLU A 463     5494   4273   4875     84    474    555       O
ATOM   3647  CB  GLU A 463       6.331   4.648  23.102  1.00 37.05           C
ANISOU 3647  CB  GLU A 463     5390   4073   4614    115    423    640       C
ATOM   3648  CG  GLU A 463       7.413   4.090  23.977  1.00 40.54           C
ANISOU 3648  CG  GLU A 463     5871   4484   5047    154    427    706       C
ATOM   3649  CD  GLU A 463       6.896   3.807  25.362  1.00 45.02           C
ANISOU 3649  CD  GLU A 463     6491   5014   5602    160    460    727       C
ATOM   3650  OE1 GLU A 463       6.033   2.910  25.495  1.00 39.87           O
ANISOU 3650  OE1 GLU A 463     5856   4321   4973    141    529    697       O
ATOM   3651  OE2 GLU A 463       7.333   4.506  26.301  1.00 45.24           O
ANISOU 3651  OE2 GLU A 463     6542   5053   5595    181    416    771       O
ATOM   3652  N   ALA A 464       8.543   3.705  20.896  1.00 32.96           N
ANISOU 3652  N   ALA A 464     4810   3573   4139    145    408    658       N
ATOM   3653  CA  ALA A 464       9.124   2.674  20.045  1.00 48.71           C
ANISOU 3653  CA  ALA A 464     6790   5550   6168    151    442    653       C
ATOM   3654  C   ALA A 464       8.660   1.299  20.498  1.00 65.88           C
ANISOU 3654  C   ALA A 464     8999   7663   8369    148    526    647       C
ATOM   3655  O   ALA A 464       8.987   0.862  21.607  1.00 69.29           O
ANISOU 3655  O   ALA A 464     9476   8059   8791    172    544    692       O
ATOM   3656  CB  ALA A 464      10.646   2.756  20.075  1.00 53.84           C
ANISOU 3656  CB  ALA A 464     7441   6210   6807    189    400    712       C
ATOM   3657  N   THR A 465       7.867   0.657  19.637  1.00 75.33           N
ANISOU 3657  N   THR A 465    10173   8849   9599    117    576    589       N
ATOM   3658  CA  THR A 465       7.533  -0.764  19.587  1.00 84.06           C
ANISOU 3658  CA  THR A 465    11296   9901  10741    110    659    571       C
ATOM   3659  C   THR A 465       6.268  -0.855  18.746  1.00 91.01           C
ANISOU 3659  C   THR A 465    12146  10791  11645     67    693    495       C
ATOM   3660  O   THR A 465       5.275  -0.171  19.019  1.00 90.65           O
ANISOU 3660  O   THR A 465    12098  10761  11584     44    683    465       O
ATOM   3661  CB  THR A 465       7.352  -1.417  20.968  1.00 83.04           C
ANISOU 3661  CB  THR A 465    11226   9719  10607    125    703    605       C
ATOM   3662  OG1 THR A 465       7.178  -2.833  20.809  1.00 81.44           O
ANISOU 3662  OG1 THR A 465    11039   9464  10441    121    783    591       O
ATOM   3663  CG2 THR A 465       6.169  -0.821  21.745  1.00 83.27           C
ANISOU 3663  CG2 THR A 465    11273   9750  10617    103    706    583       C
ATOM   3664  N   ALA A 466       6.309  -1.644  17.680  1.00 98.37           N
ANISOU 3664  N   ALA A 466    13050  11715  12611     55    729    461       N
ATOM   3665  CA  ALA A 466       5.219  -1.580  16.721  1.00104.20           C
ANISOU 3665  CA  ALA A 466    13750  12473  13368     14    749    387       C
ATOM   3666  C   ALA A 466       5.053  -2.878  15.945  1.00104.60           C
ANISOU 3666  C   ALA A 466    13789  12490  13463      0    820    351       C
ATOM   3667  O   ALA A 466       5.217  -3.974  16.493  1.00105.55           O
ANISOU 3667  O   ALA A 466    13946  12557  13602     11    878    371       O
ATOM   3668  CB  ALA A 466       5.437  -0.411  15.755  1.00105.82           C
ANISOU 3668  CB  ALA A 466    13907  12744  13558      9    678    370       C
ATOM   3669  N   ALA A 467       4.714  -2.749  14.664  1.00 99.22           N
ANISOU 3669  N   ALA A 467    13059  11842  12799    -25    815    297       N
ATOM   3670  CA  ALA A 467       4.451  -3.876  13.784  1.00 89.11           C
ANISOU 3670  CA  ALA A 467    11760  10538  11560    -43    879    253       C
ATOM   3671  C   ALA A 467       5.447  -3.913  12.628  1.00 85.78           C
ANISOU 3671  C   ALA A 467    11301  10143  11150    -32    851    257       C
ATOM   3672  O   ALA A 467       5.105  -4.285  11.503  1.00 69.10           O
ANISOU 3672  O   ALA A 467     9150   8042   9063    -55    874    205       O
ATOM   3673  CB  ALA A 467       3.010  -3.821  13.284  1.00 84.82           C
ANISOU 3673  CB  ALA A 467    11192  10007  11030    -86    910    176       C
ATOM   3674  N   ALA A 468       6.690  -3.515  12.905  1.00 94.83           N
ANISOU 3674  N   ALA A 468    12455  11300  12275      4    800    320       N
ATOM   3675  CA  ALA A 468       7.778  -3.557  11.938  1.00101.01           C
ANISOU 3675  CA  ALA A 468    13208  12104  13066     19    771    334       C
ATOM   3676  C   ALA A 468       9.030  -4.128  12.595  1.00105.01           C
ANISOU 3676  C   ALA A 468    13748  12577  13571     59    773    403       C
ATOM   3677  O   ALA A 468       8.959  -5.152  13.284  1.00106.16           O
ANISOU 3677  O   ALA A 468    13933  12669  13734     67    833    418       O
ATOM   3678  CB  ALA A 468       8.048  -2.162  11.372  1.00101.68           C
ANISOU 3678  CB  ALA A 468    13257  12256  13123     20    688    333       C
ATOM   3679  N   GLU A 469      10.178  -3.471  12.407  1.00104.57           N
ANISOU 3679  N   GLU A 469    13680  12554  13497     86    709    446       N
ATOM   3680  CA  GLU A 469      11.448  -3.927  12.963  1.00 99.88           C
ANISOU 3680  CA  GLU A 469    13114  11936  12900    126    703    512       C
ATOM   3681  C   GLU A 469      11.989  -2.978  14.033  1.00101.26           C
ANISOU 3681  C   GLU A 469    13315  12126  13033    154    643    569       C
ATOM   3682  O   GLU A 469      13.199  -2.927  14.271  1.00100.17           O
ANISOU 3682  O   GLU A 469    13185  11990  12884    188    611    623       O
ATOM   3683  CB  GLU A 469      12.481  -4.112  11.850  1.00 91.30           C
ANISOU 3683  CB  GLU A 469    11993  10869  11829    138    684    517       C
ATOM   3684  CG  GLU A 469      12.929  -2.813  11.186  1.00 82.26           C
ANISOU 3684  CG  GLU A 469    10808   9788  10659    138    603    518       C
ATOM   3685  CD  GLU A 469      12.170  -2.507   9.913  1.00 71.93           C
ANISOU 3685  CD  GLU A 469     9452   8515   9365    103    602    450       C
ATOM   3686  OE1 GLU A 469      12.825  -2.345   8.864  1.00 68.98           O
ANISOU 3686  OE1 GLU A 469     9040   8170   8997    105    575    444       O
ATOM   3687  OE2 GLU A 469      10.925  -2.438   9.958  1.00 68.80           O
ANISOU 3687  OE2 GLU A 469     9054   8118   8971     73    628    403       O
ATOM   3688  N   HIS A 470      11.107  -2.235  14.700  1.00104.61           N
ANISOU 3688  N   HIS A 470    13752  12562  13434    139    628    557       N
ATOM   3689  CA  HIS A 470      11.503  -1.191  15.636  1.00107.47           C
ANISOU 3689  CA  HIS A 470    14133  12946  13755    160    567    604       C
ATOM   3690  C   HIS A 470      11.315  -1.654  17.077  1.00105.46           C
ANISOU 3690  C   HIS A 470    13935  12645  13490    176    600    640       C
ATOM   3691  O   HIS A 470      10.314  -2.298  17.411  1.00105.39           O
ANISOU 3691  O   HIS A 470    13946  12601  13497    156    661    610       O
ATOM   3692  CB  HIS A 470      10.706   0.096  15.378  1.00110.66           C
ANISOU 3692  CB  HIS A 470    14511  13400  14136    135    520    569       C
ATOM   3693  CG  HIS A 470      10.931   0.683  14.016  1.00112.15           C
ANISOU 3693  CG  HIS A 470    14646  13638  14330    122    480    538       C
ATOM   3694  ND1 HIS A 470      11.797   1.731  13.789  1.00112.33           N
ANISOU 3694  ND1 HIS A 470    14648  13705  14326    139    406    567       N
ATOM   3695  CD2 HIS A 470      10.406   0.363  12.809  1.00112.29           C
ANISOU 3695  CD2 HIS A 470    14625  13667  14374     95    505    480       C
ATOM   3696  CE1 HIS A 470      11.795   2.034  12.503  1.00111.88           C
ANISOU 3696  CE1 HIS A 470    14545  13684  14280    123    387    530       C
ATOM   3697  NE2 HIS A 470      10.959   1.218  11.886  1.00112.34           N
ANISOU 3697  NE2 HIS A 470    14591  13724  14370     96    446    477       N
ATOM   3698  N   LYS A 471      12.283  -1.312  17.929  1.00101.56           N
ANISOU 3698  N   LYS A 471    13467  12153  12970    212    560    703       N
ATOM   3699  CA  LYS A 471      12.301  -1.748  19.319  1.00 95.53           C
ANISOU 3699  CA  LYS A 471    12758  11347  12193    233    587    746       C
ATOM   3700  C   LYS A 471      13.012  -0.699  20.165  1.00 99.19           C
ANISOU 3700  C   LYS A 471    13235  11839  12614    261    516    799       C
ATOM   3701  O   LYS A 471      13.694   0.190  19.648  1.00100.27           O
ANISOU 3701  O   LYS A 471    13341  12022  12735    268    452    809       O
ATOM   3702  CB  LYS A 471      12.990  -3.110  19.465  1.00 85.59           C
ANISOU 3702  CB  LYS A 471    11524  10038  10960    258    641    776       C
ATOM   3703  CG  LYS A 471      12.067  -4.303  19.312  1.00 76.02           C
ANISOU 3703  CG  LYS A 471    10324   8776   9783    235    728    734       C
ATOM   3704  CD  LYS A 471      11.099  -4.374  20.476  1.00 68.43           C
ANISOU 3704  CD  LYS A 471     9406   7783   8810    226    761    733       C
ATOM   3705  CE  LYS A 471      10.842  -5.808  20.874  1.00 66.56           C
ANISOU 3705  CE  LYS A 471     9206   7481   8602    229    848    735       C
ATOM   3706  NZ  LYS A 471      10.338  -5.908  22.271  1.00 69.41           N
ANISOU 3706  NZ  LYS A 471     9620   7807   8944    237    872    759       N
ATOM   3707  N   GLY A 472      12.846  -0.812  21.483  1.00100.04           N
ANISOU 3707  N   GLY A 472    13390  11917  12702    276    530    833       N
ATOM   3708  CA  GLY A 472      13.580   0.036  22.404  1.00 97.66           C
ANISOU 3708  CA  GLY A 472    13102  11643  12362    302    465    881       C
ATOM   3709  C   GLY A 472      12.741   0.799  23.411  1.00 93.50           C
ANISOU 3709  C   GLY A 472    12594  11126  11805    290    447    874       C
ATOM   3710  O   GLY A 472      11.712   0.305  23.884  1.00 96.33           O
ANISOU 3710  O   GLY A 472    12981  11446  12172    274    503    856       O
ATOM   3711  N   LYS A 473      13.191   2.006  23.752  1.00 83.03           N
ANISOU 3711  N   LYS A 473    11249   9851  10445    294    367    887       N
ATOM   3712  CA  LYS A 473      12.538   2.886  24.723  1.00 67.86           C
ANISOU 3712  CA  LYS A 473     9342   7948   8495    283    338    883       C
ATOM   3713  C   LYS A 473      12.677   4.337  24.267  1.00 57.74           C
ANISOU 3713  C   LYS A 473     8029   6720   7188    276    266    881       C
ATOM   3714  O   LYS A 473      13.078   5.226  25.020  1.00 50.91           O
ANISOU 3714  O   LYS A 473     7154   5893   6296    278    202    891       O
ATOM   3715  CB  LYS A 473      13.124   2.678  26.120  1.00 65.97           C
ANISOU 3715  CB  LYS A 473     9114   7712   8238    299    314    904       C
ATOM   3716  CG  LYS A 473      14.509   2.038  26.117  1.00 63.90           C
ANISOU 3716  CG  LYS A 473     8840   7455   7984    324    298    928       C
ATOM   3717  CD  LYS A 473      14.868   1.453  27.478  1.00 65.86           C
ANISOU 3717  CD  LYS A 473     9110   7690   8223    338    302    945       C
ATOM   3718  CE  LYS A 473      16.043   0.484  27.374  1.00 67.62           C
ANISOU 3718  CE  LYS A 473     9329   7902   8461    362    310    965       C
ATOM   3719  NZ  LYS A 473      16.312  -0.232  28.656  1.00 67.06           N
ANISOU 3719  NZ  LYS A 473     9283   7812   8383    378    324    981       N
ATOM   3720  N   VAL A 474      12.356   4.582  23.000  1.00 48.34           N
ANISOU 3720  N   VAL A 474     6817   5538   6011    263    274    860       N
ATOM   3721  CA  VAL A 474      12.544   5.885  22.381  1.00 41.81           C
ANISOU 3721  CA  VAL A 474     5952   4769   5165    255    204    849       C
ATOM   3722  C   VAL A 474      11.213   6.359  21.812  1.00 32.57           C
ANISOU 3722  C   VAL A 474     4757   3616   4001    214    213    785       C
ATOM   3723  O   VAL A 474      10.355   5.564  21.414  1.00 35.55           O
ANISOU 3723  O   VAL A 474     5132   3967   4407    191    272    742       O
ATOM   3724  CB  VAL A 474      13.638   5.849  21.285  1.00 49.95           C
ANISOU 3724  CB  VAL A 474     6946   5824   6209    267    176    856       C
ATOM   3725  CG1 VAL A 474      14.733   4.861  21.661  1.00 50.92           C
ANISOU 3725  CG1 VAL A 474     7084   5921   6343    297    192    894       C
ATOM   3726  CG2 VAL A 474      13.054   5.508  19.925  1.00 48.92           C
ANISOU 3726  CG2 VAL A 474     6775   5701   6111    237    204    797       C
ATOM   3727  N   ILE A 475      11.044   7.673  21.792  1.00 33.58           N
ANISOU 3727  N   ILE A 475     4846   3871   4043   -259    331    341       N
ATOM   3728  CA  ILE A 475       9.858   8.302  21.229  1.00 33.84           C
ANISOU 3728  CA  ILE A 475     4885   3899   4074   -260    333    314       C
ATOM   3729  C   ILE A 475      10.191   8.666  19.791  1.00 36.81           C
ANISOU 3729  C   ILE A 475     5249   4268   4468   -281    323    306       C
ATOM   3730  O   ILE A 475      10.973   9.589  19.546  1.00 40.95           O
ANISOU 3730  O   ILE A 475     5779   4791   4989   -291    291    307       O
ATOM   3731  CB  ILE A 475       9.450   9.538  22.035  1.00 37.09           C
ANISOU 3731  CB  ILE A 475     5323   4316   4455   -250    304    299       C
ATOM   3732  CG1 ILE A 475       9.299   9.166  23.509  1.00 37.36           C
ANISOU 3732  CG1 ILE A 475     5367   4362   4464   -227    311    310       C
ATOM   3733  CG2 ILE A 475       8.172  10.148  21.472  1.00 38.29           C
ANISOU 3733  CG2 ILE A 475     5480   4462   4607   -249    308    273       C
ATOM   3734  CD1 ILE A 475       8.259   8.105  23.756  1.00 40.69           C
ANISOU 3734  CD1 ILE A 475     5780   4786   4893   -214    355    315       C
ATOM   3735  N   MET A 476       9.609   7.945  18.836  1.00 24.68           N
ANISOU 3735  N   MET A 476     3695   2728   2954   -287    352    298       N
ATOM   3736  CA  MET A 476       9.935   8.188  17.439  1.00 29.28           C
ANISOU 3736  CA  MET A 476     4265   3309   3552   -304    346    291       C
ATOM   3737  C   MET A 476       8.839   8.993  16.739  1.00 29.81           C
ANISOU 3737  C   MET A 476     4337   3375   3613   -306    341    267       C
ATOM   3738  O   MET A 476       7.665   8.965  17.121  1.00 27.47           O
ANISOU 3738  O   MET A 476     4048   3079   3311   -295    353    253       O
ATOM   3739  CB  MET A 476      10.188   6.871  16.701  1.00 35.72           C
ANISOU 3739  CB  MET A 476     5055   4124   4395   -311    377    296       C
ATOM   3740  CG  MET A 476       9.017   5.944  16.608  1.00 48.50           C
ANISOU 3740  CG  MET A 476     6663   5738   6027   -304    412    283       C
ATOM   3741  SD  MET A 476       9.568   4.306  16.074  1.00 63.13           S
ANISOU 3741  SD  MET A 476     8486   7585   7916   -309    447    292       S
ATOM   3742  CE  MET A 476      10.533   4.732  14.624  1.00 65.45           C
ANISOU 3742  CE  MET A 476     8767   7887   8215   -327    430    287       C
ATOM   3743  N   HIS A 477       9.248   9.730  15.714  1.00 24.11           N
ANISOU 3743  N   HIS A 477     3611   2655   2895   -320    322    265       N
ATOM   3744  CA  HIS A 477       8.311  10.502  14.914  1.00 20.41           C
ANISOU 3744  CA  HIS A 477     3145   2189   2423   -322    316    246       C
ATOM   3745  C   HIS A 477       7.543   9.591  13.963  1.00 23.73           C
ANISOU 3745  C   HIS A 477     3544   2614   2857   -323    346    231       C
ATOM   3746  O   HIS A 477       8.122   8.699  13.336  1.00 26.30           O
ANISOU 3746  O   HIS A 477     3850   2943   3198   -331    362    236       O
ATOM   3747  CB  HIS A 477       9.070  11.578  14.134  1.00 17.39           C
ANISOU 3747  CB  HIS A 477     2761   1806   2039   -334    286    253       C
ATOM   3748  CG  HIS A 477       9.524  12.714  14.995  1.00 27.81           C
ANISOU 3748  CG  HIS A 477     4101   3117   3348   -333    252    259       C
ATOM   3749  ND1 HIS A 477       8.725  13.806  15.256  1.00 22.35           N
ANISOU 3749  ND1 HIS A 477     3426   2419   2645   -326    235    244       N
ATOM   3750  CD2 HIS A 477      10.668  12.906  15.697  1.00 27.13           C
ANISOU 3750  CD2 HIS A 477     4020   3027   3260   -336    232    275       C
ATOM   3751  CE1 HIS A 477       9.371  14.637  16.053  1.00 24.65           C
ANISOU 3751  CE1 HIS A 477     3733   2702   2931   -326    205    249       C
ATOM   3752  NE2 HIS A 477      10.545  14.109  16.349  1.00 26.67           N
ANISOU 3752  NE2 HIS A 477     3982   2959   3191   -331    202    267       N
ATOM   3753  N   ASP A 478       6.230   9.818  13.856  1.00 19.33           N
ANISOU 3753  N   ASP A 478     2990   2058   2296   -316    354    211       N
ATOM   3754  CA  ASP A 478       5.387   9.087  12.904  1.00 18.97           C
ANISOU 3754  CA  ASP A 478     2925   2019   2264   -318    379    192       C
ATOM   3755  C   ASP A 478       4.260   9.993  12.430  1.00 18.98           C
ANISOU 3755  C   ASP A 478     2932   2025   2256   -315    369    174       C
ATOM   3756  O   ASP A 478       3.090   9.794  12.770  1.00 18.94           O
ANISOU 3756  O   ASP A 478     2927   2017   2251   -306    383    159       O
ATOM   3757  CB  ASP A 478       4.841   7.801  13.537  1.00 19.83           C
ANISOU 3757  CB  ASP A 478     3025   2121   2388   -310    412    189       C
ATOM   3758  CG  ASP A 478       4.325   6.808  12.503  1.00 25.48           C
ANISOU 3758  CG  ASP A 478     3714   2841   3126   -316    438    170       C
ATOM   3759  OD1 ASP A 478       4.131   7.185  11.331  1.00 24.16           O
ANISOU 3759  OD1 ASP A 478     3538   2686   2957   -323    430    155       O
ATOM   3760  OD2 ASP A 478       4.112   5.634  12.864  1.00 23.11           O
ANISOU 3760  OD2 ASP A 478     3401   2533   2846   -312    466    169       O
ATOM   3761  N   PRO A 479       4.581  11.013  11.626  1.00 19.36           N
ANISOU 3761  N   PRO A 479     2981   2079   2295   -322    345    177       N
ATOM   3762  CA  PRO A 479       3.538  11.955  11.203  1.00 19.99           C
ANISOU 3762  CA  PRO A 479     3066   2163   2367   -318    333    164       C
ATOM   3763  C   PRO A 479       2.422  11.257  10.441  1.00 18.19           C
ANISOU 3763  C   PRO A 479     2820   1946   2147   -316    357    141       C
ATOM   3764  O   PRO A 479       2.667  10.436   9.546  1.00 16.69           O
ANISOU 3764  O   PRO A 479     2607   1767   1966   -323    371    135       O
ATOM   3765  CB  PRO A 479       4.289  12.960  10.310  1.00 20.04           C
ANISOU 3765  CB  PRO A 479     3071   2176   2369   -327    307    177       C
ATOM   3766  CG  PRO A 479       5.547  12.293   9.926  1.00 22.29           C
ANISOU 3766  CG  PRO A 479     3343   2466   2661   -338    312    192       C
ATOM   3767  CD  PRO A 479       5.892  11.320  11.023  1.00 17.49           C
ANISOU 3767  CD  PRO A 479     2739   1847   2060   -334    328    196       C
ATOM   3768  N   PHE A 480       1.190  11.602  10.819  1.00 16.85           N
ANISOU 3768  N   PHE A 480     2657   1773   1973   -305    359    126       N
ATOM   3769  CA  PHE A 480      -0.056  11.083  10.260  1.00 17.40           C
ANISOU 3769  CA  PHE A 480     2710   1851   2050   -301    379    103       C
ATOM   3770  C   PHE A 480      -0.150   9.561  10.339  1.00 17.63           C
ANISOU 3770  C   PHE A 480     2721   1878   2100   -303    410     94       C
ATOM   3771  O   PHE A 480      -0.983   8.962   9.656  1.00 18.38           O
ANISOU 3771  O   PHE A 480     2795   1981   2206   -304    427     72       O
ATOM   3772  CB  PHE A 480      -0.248  11.545   8.814  1.00 16.20           C
ANISOU 3772  CB  PHE A 480     2543   1718   1893   -307    368     95       C
ATOM   3773  CG  PHE A 480      -0.580  13.010   8.685  1.00 22.68           C
ANISOU 3773  CG  PHE A 480     3379   2540   2700   -302    341    101       C
ATOM   3774  CD1 PHE A 480       0.385  13.976   8.918  1.00 26.22           C
ANISOU 3774  CD1 PHE A 480     3842   2979   3140   -306    316    123       C
ATOM   3775  CD2 PHE A 480      -1.847  13.414   8.295  1.00 22.42           C
ANISOU 3775  CD2 PHE A 480     3340   2514   2663   -294    341     85       C
ATOM   3776  CE1 PHE A 480       0.086  15.323   8.773  1.00 25.36           C
ANISOU 3776  CE1 PHE A 480     3744   2867   3023   -302    292    129       C
ATOM   3777  CE2 PHE A 480      -2.153  14.756   8.157  1.00 28.18           C
ANISOU 3777  CE2 PHE A 480     4082   3243   3383   -289    317     92       C
ATOM   3778  CZ  PHE A 480      -1.191  15.704   8.392  1.00 21.83           C
ANISOU 3778  CZ  PHE A 480     3293   2427   2574   -293    293    114       C
ATOM   3779  N   ALA A 481       0.686   8.940  11.168  1.00 16.12           N
ANISOU 3779  N   ALA A 481     2535   1675   1915   -304    419    110       N
ATOM   3780  CA  ALA A 481       0.833   7.482  11.222  1.00 17.91           C
ANISOU 3780  CA  ALA A 481     2742   1896   2165   -307    449    106       C
ATOM   3781  C   ALA A 481       1.246   6.922   9.867  1.00 19.99           C
ANISOU 3781  C   ALA A 481     2982   2174   2440   -318    454     94       C
ATOM   3782  O   ALA A 481       1.003   5.756   9.556  1.00 17.85           O
ANISOU 3782  O   ALA A 481     2688   1900   2193   -320    479     79       O
ATOM   3783  CB  ALA A 481      -0.445   6.797  11.724  1.00 21.89           C
ANISOU 3783  CB  ALA A 481     3238   2393   2685   -298    475     92       C
ATOM   3784  N   MET A 482       1.858   7.756   9.042  1.00 16.29           N
ANISOU 3784  N   MET A 482     2515   1719   1955   -324    431    100       N
ATOM   3785  CA  MET A 482       2.151   7.388   7.668  1.00 16.42           C
ANISOU 3785  CA  MET A 482     2509   1755   1975   -332    434     87       C
ATOM   3786  C   MET A 482       3.637   7.277   7.392  1.00 14.34           C
ANISOU 3786  C   MET A 482     2243   1495   1711   -340    428    107       C
ATOM   3787  O   MET A 482       4.014   7.076   6.236  1.00 17.33           O
ANISOU 3787  O   MET A 482     2603   1892   2088   -346    429     99       O
ATOM   3788  CB  MET A 482       1.514   8.404   6.720  1.00 21.10           C
ANISOU 3788  CB  MET A 482     3100   2367   2549   -331    415     78       C
ATOM   3789  CG  MET A 482       0.011   8.206   6.574  1.00 23.98           C
ANISOU 3789  CG  MET A 482     3456   2736   2920   -325    426     50       C
ATOM   3790  SD  MET A 482      -0.368   6.862   5.444  1.00 21.58           S
ANISOU 3790  SD  MET A 482     3117   2447   2636   -330    450     15       S
ATOM   3791  CE  MET A 482       0.055   7.653   3.885  1.00 24.48           C
ANISOU 3791  CE  MET A 482     3474   2851   2976   -333    428     15       C
ATOM   3792  N   ARG A 483       4.490   7.395   8.417  1.00 17.45           N
ANISOU 3792  N   ARG A 483     2652   1872   2104   -340    421    133       N
ATOM   3793  CA  ARG A 483       5.937   7.355   8.193  1.00 18.32           C
ANISOU 3793  CA  ARG A 483     2760   1986   2215   -348    414    154       C
ATOM   3794  C   ARG A 483       6.381   6.181   7.328  1.00 19.83           C
ANISOU 3794  C   ARG A 483     2925   2187   2424   -353    436    142       C
ATOM   3795  O   ARG A 483       7.174   6.394   6.392  1.00 17.03           O
ANISOU 3795  O   ARG A 483     2559   1848   2062   -359    428    148       O
ATOM   3796  CB  ARG A 483       6.678   7.340   9.542  1.00 20.75           C
ANISOU 3796  CB  ARG A 483     3084   2274   2524   -346    409    179       C
ATOM   3797  CG  ARG A 483       8.191   7.557   9.391  1.00 25.93           C
ANISOU 3797  CG  ARG A 483     3739   2933   3179   -354    394    204       C
ATOM   3798  CD  ARG A 483       9.002   7.003  10.560  1.00 30.70           C
ANISOU 3798  CD  ARG A 483     4350   3522   3791   -351    399    224       C
ATOM   3799  NE  ARG A 483       8.825   5.569  10.723  1.00 35.64           N
ANISOU 3799  NE  ARG A 483     4960   4141   4440   -348    431    217       N
ATOM   3800  CZ  ARG A 483       8.212   5.002  11.765  1.00 44.01           C
ANISOU 3800  CZ  ARG A 483     6026   5188   5507   -338    447    217       C
ATOM   3801  NH1 ARG A 483       7.737   5.761  12.747  1.00 37.17           N
ANISOU 3801  NH1 ARG A 483     5183   4318   4624   -330    433    222       N
ATOM   3802  NH2 ARG A 483       8.083   3.677  11.835  1.00 39.02           N
ANISOU 3802  NH2 ARG A 483     5376   4547   4902   -336    478    212       N
ATOM   3803  N   PRO A 484       5.918   4.949   7.552  1.00 17.35           N
ANISOU 3803  N   PRO A 484     2597   1862   2134   -350    463    125       N
ATOM   3804  CA  PRO A 484       6.328   3.833   6.683  1.00 17.98           C
ANISOU 3804  CA  PRO A 484     2649   1948   2233   -355    484    109       C
ATOM   3805  C   PRO A 484       5.611   3.767   5.339  1.00 19.69           C
ANISOU 3805  C   PRO A 484     2847   2188   2445   -356    487     76       C
ATOM   3806  O   PRO A 484       5.924   2.875   4.536  1.00 23.86           O
ANISOU 3806  O   PRO A 484     3352   2726   2988   -359    503     57       O
ATOM   3807  CB  PRO A 484       5.984   2.591   7.525  1.00 18.55           C
ANISOU 3807  CB  PRO A 484     2715   1997   2338   -351    512    104       C
ATOM   3808  CG  PRO A 484       5.597   3.093   8.889  1.00 21.05           C
ANISOU 3808  CG  PRO A 484     3056   2297   2646   -344    506    124       C
ATOM   3809  CD  PRO A 484       5.107   4.485   8.695  1.00 18.53           C
ANISOU 3809  CD  PRO A 484     2754   1991   2296   -343    479    123       C
ATOM   3810  N   PHE A 485       4.679   4.678   5.060  1.00 19.14           N
ANISOU 3810  N   PHE A 485     2785   2131   2356   -353    472     67       N
ATOM   3811  CA  PHE A 485       3.732   4.504   3.970  1.00 21.59           C
ANISOU 3811  CA  PHE A 485     3077   2463   2664   -352    476     32       C
ATOM   3812  C   PHE A 485       3.638   5.663   2.979  1.00 24.21           C
ANISOU 3812  C   PHE A 485     3410   2824   2963   -351    453     35       C
ATOM   3813  O   PHE A 485       2.832   5.585   2.042  1.00 22.74           O
ANISOU 3813  O   PHE A 485     3208   2661   2771   -349    454      7       O
ATOM   3814  CB  PHE A 485       2.340   4.239   4.554  1.00 14.67           C
ANISOU 3814  CB  PHE A 485     2201   1571   1801   -347    487     13       C
ATOM   3815  CG  PHE A 485       2.308   3.101   5.552  1.00 23.62           C
ANISOU 3815  CG  PHE A 485     3331   2675   2969   -346    513     13       C
ATOM   3816  CD1 PHE A 485       2.641   1.806   5.159  1.00 18.24           C
ANISOU 3816  CD1 PHE A 485     2626   1989   2318   -350    536     -5       C
ATOM   3817  CD2 PHE A 485       1.934   3.327   6.880  1.00 20.75           C
ANISOU 3817  CD2 PHE A 485     2987   2289   2607   -340    515     32       C
ATOM   3818  CE1 PHE A 485       2.619   0.754   6.061  1.00 17.34           C
ANISOU 3818  CE1 PHE A 485     2505   1844   2237   -348    561     -0       C
ATOM   3819  CE2 PHE A 485       1.903   2.276   7.802  1.00 18.90           C
ANISOU 3819  CE2 PHE A 485     2748   2030   2404   -338    540     38       C
ATOM   3820  CZ  PHE A 485       2.235   0.986   7.397  1.00 16.81           C
ANISOU 3820  CZ  PHE A 485     2458   1758   2172   -342    563     23       C
ATOM   3821  N   PHE A 486       4.410   6.731   3.147  1.00 20.98           N
ANISOU 3821  N   PHE A 486     3018   2417   2535   -353    431     69       N
ATOM   3822  CA  PHE A 486       4.328   7.844   2.201  1.00 20.11           C
ANISOU 3822  CA  PHE A 486     2908   2334   2398   -352    410     76       C
ATOM   3823  C   PHE A 486       4.707   7.396   0.795  1.00 19.64           C
ANISOU 3823  C   PHE A 486     2823   2308   2330   -353    416     62       C
ATOM   3824  O   PHE A 486       5.806   6.882   0.578  1.00 27.02           O
ANISOU 3824  O   PHE A 486     3749   3247   3270   -357    424     70       O
ATOM   3825  CB  PHE A 486       5.240   8.987   2.635  1.00 19.58           C
ANISOU 3825  CB  PHE A 486     2861   2258   2320   -355    387    116       C
ATOM   3826  CG  PHE A 486       4.787   9.678   3.884  1.00 15.77           C
ANISOU 3826  CG  PHE A 486     2405   1749   1840   -352    375    127       C
ATOM   3827  CD1 PHE A 486       3.539  10.273   3.940  1.00 16.21           C
ANISOU 3827  CD1 PHE A 486     2467   1805   1887   -345    368    114       C
ATOM   3828  CD2 PHE A 486       5.613   9.747   4.990  1.00 15.09           C
ANISOU 3828  CD2 PHE A 486     2335   1638   1761   -355    369    150       C
ATOM   3829  CE1 PHE A 486       3.098  10.911   5.111  1.00 16.94           C
ANISOU 3829  CE1 PHE A 486     2583   1873   1980   -340    358    122       C
ATOM   3830  CE2 PHE A 486       5.168  10.393   6.173  1.00 13.80           C
ANISOU 3830  CE2 PHE A 486     2195   1452   1595   -350    358    156       C
ATOM   3831  CZ  PHE A 486       3.918  10.959   6.217  1.00 22.13           C
ANISOU 3831  CZ  PHE A 486     3258   2508   2644   -342    353    142       C
ATOM   3832  N   GLY A 487       3.803   7.609  -0.163  1.00 18.74           N
ANISOU 3832  N   GLY A 487     2697   2224   2201   -348    413     39       N
ATOM   3833  CA  GLY A 487       4.096   7.292  -1.551  1.00 22.47           C
ANISOU 3833  CA  GLY A 487     3145   2736   2658   -346    417     24       C
ATOM   3834  C   GLY A 487       4.912   8.337  -2.286  1.00 24.03           C
ANISOU 3834  C   GLY A 487     3343   2959   2828   -346    399     58       C
ATOM   3835  O   GLY A 487       5.309   8.111  -3.436  1.00 26.04           O
ANISOU 3835  O   GLY A 487     3577   3250   3066   -343    404     51       O
ATOM   3836  N   TYR A 488       5.188   9.459  -1.635  1.00 20.84           N
ANISOU 3836  N   TYR A 488     2961   2537   2421   -348    381     95       N
ATOM   3837  CA  TYR A 488       5.853  10.600  -2.255  1.00 22.22           C
ANISOU 3837  CA  TYR A 488     3138   2731   2576   -348    362    132       C
ATOM   3838  C   TYR A 488       6.303  11.543  -1.146  1.00 21.78           C
ANISOU 3838  C   TYR A 488     3107   2638   2529   -353    344    167       C
ATOM   3839  O   TYR A 488       6.012  11.329   0.038  1.00 18.60           O
ANISOU 3839  O   TYR A 488     2722   2202   2144   -355    346    161       O
ATOM   3840  CB  TYR A 488       4.933  11.310  -3.250  1.00 20.79           C
ANISOU 3840  CB  TYR A 488     2947   2584   2369   -339    352    127       C
ATOM   3841  CG  TYR A 488       3.701  11.948  -2.617  1.00 17.34           C
ANISOU 3841  CG  TYR A 488     2526   2128   1936   -335    340    121       C
ATOM   3842  CD1 TYR A 488       2.600  11.179  -2.269  1.00 20.10           C
ANISOU 3842  CD1 TYR A 488     2872   2469   2296   -332    352     82       C
ATOM   3843  CD2 TYR A 488       3.632  13.320  -2.419  1.00 22.74           C
ANISOU 3843  CD2 TYR A 488     3224   2802   2613   -333    318    154       C
ATOM   3844  CE1 TYR A 488       1.466  11.753  -1.699  1.00 22.44           C
ANISOU 3844  CE1 TYR A 488     3181   2749   2595   -326    344     76       C
ATOM   3845  CE2 TYR A 488       2.513  13.910  -1.868  1.00 26.84           C
ANISOU 3845  CE2 TYR A 488     3757   3305   3136   -327    309    147       C
ATOM   3846  CZ  TYR A 488       1.432  13.125  -1.506  1.00 24.57           C
ANISOU 3846  CZ  TYR A 488     3467   3011   2856   -324    322    108       C
ATOM   3847  OH  TYR A 488       0.319  13.721  -0.962  1.00 19.25           O
ANISOU 3847  OH  TYR A 488     2806   2322   2186   -317    314    102       O
ATOM   3848  N   ASN A 489       7.026  12.589  -1.557  1.00 17.69           N
ANISOU 3848  N   ASN A 489     2591   2129   2002   -356    328    205       N
ATOM   3849  CA  ASN A 489       7.591  13.637  -0.720  1.00 21.00           C
ANISOU 3849  CA  ASN A 489     3030   2517   2430   -361    307    240       C
ATOM   3850  C   ASN A 489       6.610  14.093   0.356  1.00 19.97           C
ANISOU 3850  C   ASN A 489     2922   2357   2309   -358    297    229       C
ATOM   3851  O   ASN A 489       5.511  14.567   0.048  1.00 21.05           O
ANISOU 3851  O   ASN A 489     3060   2503   2436   -350    292    218       O
ATOM   3852  CB  ASN A 489       7.978  14.805  -1.642  1.00 17.35           C
ANISOU 3852  CB  ASN A 489     2560   2077   1955   -361    291    275       C
ATOM   3853  CG  ASN A 489       8.686  15.928  -0.923  1.00 17.08           C
ANISOU 3853  CG  ASN A 489     2542   2010   1935   -368    268    312       C
ATOM   3854  OD1 ASN A 489       8.178  16.484   0.058  1.00 18.72           O
ANISOU 3854  OD1 ASN A 489     2771   2187   2154   -368    255    309       O
ATOM   3855  ND2 ASN A 489       9.869  16.302  -1.432  1.00 17.85           N
ANISOU 3855  ND2 ASN A 489     2629   2118   2035   -375    264    347       N
ATOM   3856  N   PHE A 490       6.990  13.895   1.629  1.00 16.41           N
ANISOU 3856  N   PHE A 490     2489   1871   1874   -363    296    231       N
ATOM   3857  CA  PHE A 490       6.106  14.230   2.741  1.00 18.16           C
ANISOU 3857  CA  PHE A 490     2732   2066   2102   -358    289    220       C
ATOM   3858  C   PHE A 490       5.809  15.729   2.796  1.00 18.57           C
ANISOU 3858  C   PHE A 490     2797   2108   2151   -355    263    239       C
ATOM   3859  O   PHE A 490       4.711  16.130   3.201  1.00 19.15           O
ANISOU 3859  O   PHE A 490     2881   2172   2222   -347    259    224       O
ATOM   3860  CB  PHE A 490       6.733  13.761   4.054  1.00 16.43           C
ANISOU 3860  CB  PHE A 490     2529   1818   1898   -362    291    223       C
ATOM   3861  CG  PHE A 490       6.023  14.262   5.297  1.00 16.43           C
ANISOU 3861  CG  PHE A 490     2552   1789   1900   -356    281    216       C
ATOM   3862  CD1 PHE A 490       4.667  14.037   5.482  1.00 19.83           C
ANISOU 3862  CD1 PHE A 490     2985   2221   2328   -347    292    190       C
ATOM   3863  CD2 PHE A 490       6.733  14.927   6.289  1.00 22.01           C
ANISOU 3863  CD2 PHE A 490     3277   2471   2613   -359    262    234       C
ATOM   3864  CE1 PHE A 490       4.017  14.476   6.640  1.00 21.01           C
ANISOU 3864  CE1 PHE A 490     3156   2347   2479   -339    285    184       C
ATOM   3865  CE2 PHE A 490       6.095  15.381   7.448  1.00 23.63           C
ANISOU 3865  CE2 PHE A 490     3505   2656   2819   -352    253    225       C
ATOM   3866  CZ  PHE A 490       4.733  15.151   7.621  1.00 20.10           C
ANISOU 3866  CZ  PHE A 490     3061   2210   2367   -341    266    201       C
ATOM   3867  N   GLY A 491       6.768  16.564   2.413  1.00 20.08           N
ANISOU 3867  N   GLY A 491     2986   2299   2343   -362    247    272       N
ATOM   3868  CA  GLY A 491       6.477  17.989   2.303  1.00 18.41           C
ANISOU 3868  CA  GLY A 491     2783   2080   2134   -359    223    292       C
ATOM   3869  C   GLY A 491       5.347  18.269   1.331  1.00 19.85           C
ANISOU 3869  C   GLY A 491     2954   2289   2301   -349    226    283       C
ATOM   3870  O   GLY A 491       4.468  19.093   1.603  1.00 20.33           O
ANISOU 3870  O   GLY A 491     3025   2336   2364   -342    214    280       O
ATOM   3871  N   LYS A 492       5.349  17.581   0.185  1.00 22.22           N
ANISOU 3871  N   LYS A 492     3231   2627   2586   -348    242    276       N
ATOM   3872  CA  LYS A 492       4.265  17.749  -0.781  1.00 18.65           C
ANISOU 3872  CA  LYS A 492     2765   2205   2115   -337    244    265       C
ATOM   3873  C   LYS A 492       2.956  17.173  -0.251  1.00 23.72           C
ANISOU 3873  C   LYS A 492     3413   2840   2758   -329    254    226       C
ATOM   3874  O   LYS A 492       1.875  17.677  -0.584  1.00 20.02           O
ANISOU 3874  O   LYS A 492     2943   2382   2283   -320    249    218       O
ATOM   3875  CB  LYS A 492       4.653  17.107  -2.116  1.00 18.76           C
ANISOU 3875  CB  LYS A 492     2752   2265   2111   -336    258    265       C
ATOM   3876  CG  LYS A 492       5.858  17.770  -2.791  1.00 24.02           C
ANISOU 3876  CG  LYS A 492     3410   2944   2775   -341    249    309       C
ATOM   3877  CD  LYS A 492       5.645  19.265  -2.911  1.00 26.63           C
ANISOU 3877  CD  LYS A 492     3745   3264   3109   -337    227    343       C
ATOM   3878  CE  LYS A 492       6.757  19.917  -3.715  1.00 40.55           C
ANISOU 3878  CE  LYS A 492     5495   5043   4871   -342    221    389       C
ATOM   3879  NZ  LYS A 492       6.527  21.377  -3.861  1.00 48.80           N
ANISOU 3879  NZ  LYS A 492     6543   6076   5925   -338    201    425       N
ATOM   3880  N   TYR A 493       3.039  16.122   0.570  1.00 20.36           N
ANISOU 3880  N   TYR A 493     2994   2399   2343   -333    270    202       N
ATOM   3881  CA  TYR A 493       1.865  15.574   1.233  1.00 16.65           C
ANISOU 3881  CA  TYR A 493     2530   1917   1879   -327    281    169       C
ATOM   3882  C   TYR A 493       1.243  16.593   2.189  1.00 19.58           C
ANISOU 3882  C   TYR A 493     2925   2259   2257   -321    265    175       C
ATOM   3883  O   TYR A 493       0.021  16.770   2.211  1.00 18.92           O
ANISOU 3883  O   TYR A 493     2841   2177   2170   -312    265    157       O
ATOM   3884  CB  TYR A 493       2.283  14.298   1.960  1.00 15.23           C
ANISOU 3884  CB  TYR A 493     2351   1723   1712   -333    301    152       C
ATOM   3885  CG  TYR A 493       1.323  13.677   2.945  1.00 18.68           C
ANISOU 3885  CG  TYR A 493     2797   2140   2160   -328    314    126       C
ATOM   3886  CD1 TYR A 493       1.230  14.144   4.250  1.00 20.33           C
ANISOU 3886  CD1 TYR A 493     3031   2318   2377   -325    306    133       C
ATOM   3887  CD2 TYR A 493       0.589  12.550   2.596  1.00 18.26           C
ANISOU 3887  CD2 TYR A 493     2726   2099   2112   -326    336     93       C
ATOM   3888  CE1 TYR A 493       0.379  13.534   5.165  1.00 19.64           C
ANISOU 3888  CE1 TYR A 493     2949   2214   2298   -319    322    112       C
ATOM   3889  CE2 TYR A 493      -0.260  11.933   3.512  1.00 21.16           C
ANISOU 3889  CE2 TYR A 493     3099   2448   2494   -322    351     73       C
ATOM   3890  CZ  TYR A 493      -0.349  12.424   4.785  1.00 22.52           C
ANISOU 3890  CZ  TYR A 493     3295   2591   2670   -318    344     84       C
ATOM   3891  OH  TYR A 493      -1.189  11.786   5.679  1.00 20.64           O
ANISOU 3891  OH  TYR A 493     3061   2337   2445   -312    362     66       O
ATOM   3892  N   LEU A 494       2.069  17.272   2.988  1.00 18.94           N
ANISOU 3892  N   LEU A 494     2861   2150   2184   -326    249    198       N
ATOM   3893  CA  LEU A 494       1.545  18.335   3.852  1.00 18.76           C
ANISOU 3893  CA  LEU A 494     2860   2099   2168   -320    232    202       C
ATOM   3894  C   LEU A 494       0.888  19.451   3.043  1.00 19.82           C
ANISOU 3894  C   LEU A 494     2988   2244   2297   -313    217    213       C
ATOM   3895  O   LEU A 494      -0.187  19.935   3.410  1.00 21.77           O
ANISOU 3895  O   LEU A 494     3244   2482   2546   -303    213    201       O
ATOM   3896  CB  LEU A 494       2.656  18.911   4.730  1.00 19.67           C
ANISOU 3896  CB  LEU A 494     2993   2185   2295   -328    215    223       C
ATOM   3897  CG  LEU A 494       3.211  17.984   5.806  1.00 20.75           C
ANISOU 3897  CG  LEU A 494     3139   2307   2437   -332    226    213       C
ATOM   3898  CD1 LEU A 494       4.409  18.639   6.478  1.00 24.67           C
ANISOU 3898  CD1 LEU A 494     3650   2781   2944   -340    205    236       C
ATOM   3899  CD2 LEU A 494       2.122  17.622   6.814  1.00 17.86           C
ANISOU 3899  CD2 LEU A 494     2787   1929   2071   -321    237    186       C
ATOM   3900  N   ALA A 495       1.523  19.895   1.945  1.00 19.75           N
ANISOU 3900  N   ALA A 495     2964   2256   2282   -317    209    240       N
ATOM   3901  CA  ALA A 495       0.894  20.931   1.131  1.00 20.27           C
ANISOU 3901  CA  ALA A 495     3023   2335   2344   -309    196    256       C
ATOM   3902  C   ALA A 495      -0.431  20.449   0.544  1.00 19.89           C
ANISOU 3902  C   ALA A 495     2961   2314   2281   -297    209    228       C
ATOM   3903  O   ALA A 495      -1.370  21.237   0.389  1.00 21.23           O
ANISOU 3903  O   ALA A 495     3132   2484   2450   -287    199    230       O
ATOM   3904  CB  ALA A 495       1.850  21.387   0.015  1.00 22.67           C
ANISOU 3904  CB  ALA A 495     3310   2661   2643   -314    189    293       C
ATOM   3905  N   HIS A 496      -0.521  19.159   0.214  1.00 16.43           N
ANISOU 3905  N   HIS A 496     2509   1899   1833   -300    229    203       N
ATOM   3906  CA  HIS A 496      -1.768  18.579  -0.273  1.00 18.13           C
ANISOU 3906  CA  HIS A 496     2711   2140   2039   -291    241    171       C
ATOM   3907  C   HIS A 496      -2.857  18.660   0.799  1.00 19.17           C
ANISOU 3907  C   HIS A 496     2858   2244   2182   -284    243    149       C
ATOM   3908  O   HIS A 496      -3.999  19.048   0.521  1.00 17.61           O
ANISOU 3908  O   HIS A 496     2655   2056   1981   -273    239    140       O
ATOM   3909  CB  HIS A 496      -1.491  17.123  -0.700  1.00 20.77           C
ANISOU 3909  CB  HIS A 496     3028   2497   2368   -296    263    146       C
ATOM   3910  CG  HIS A 496      -2.621  16.453  -1.422  1.00 21.68           C
ANISOU 3910  CG  HIS A 496     3121   2642   2473   -289    273    112       C
ATOM   3911  ND1 HIS A 496      -3.234  17.002  -2.530  1.00 20.62           N
ANISOU 3911  ND1 HIS A 496     2970   2544   2320   -279    264    116       N
ATOM   3912  CD2 HIS A 496      -3.228  15.258  -1.208  1.00 16.45           C
ANISOU 3912  CD2 HIS A 496     2450   1981   1819   -290    293     73       C
ATOM   3913  CE1 HIS A 496      -4.183  16.184  -2.957  1.00 21.25           C
ANISOU 3913  CE1 HIS A 496     3032   2646   2395   -275    275     79       C
ATOM   3914  NE2 HIS A 496      -4.196  15.115  -2.175  1.00 20.47           N
ANISOU 3914  NE2 HIS A 496     2938   2526   2315   -282    293     52       N
ATOM   3915  N   TRP A 497      -2.517  18.287   2.033  1.00 20.31           N
ANISOU 3915  N   TRP A 497     3021   2356   2340   -288    249    143       N
ATOM   3916  CA  TRP A 497      -3.490  18.344   3.121  1.00 19.80           C
ANISOU 3916  CA  TRP A 497     2971   2266   2284   -280    252    124       C
ATOM   3917  C   TRP A 497      -3.929  19.782   3.372  1.00 23.03           C
ANISOU 3917  C   TRP A 497     3394   2658   2696   -271    231    139       C
ATOM   3918  O   TRP A 497      -5.128  20.075   3.461  1.00 22.85           O
ANISOU 3918  O   TRP A 497     3371   2636   2674   -260    232    125       O
ATOM   3919  CB  TRP A 497      -2.892  17.730   4.384  1.00 14.96           C
ANISOU 3919  CB  TRP A 497     2375   1626   1682   -286    262    119       C
ATOM   3920  CG  TRP A 497      -3.229  16.284   4.553  1.00 18.72           C
ANISOU 3920  CG  TRP A 497     2840   2109   2163   -288    289     93       C
ATOM   3921  CD1 TRP A 497      -2.642  15.221   3.934  1.00 23.38           C
ANISOU 3921  CD1 TRP A 497     3413   2717   2754   -296    303     86       C
ATOM   3922  CD2 TRP A 497      -4.239  15.749   5.411  1.00 19.35           C
ANISOU 3922  CD2 TRP A 497     2924   2176   2251   -280    305     70       C
ATOM   3923  NE1 TRP A 497      -3.231  14.043   4.361  1.00 19.87           N
ANISOU 3923  NE1 TRP A 497     2961   2268   2321   -296    327     60       N
ATOM   3924  CE2 TRP A 497      -4.214  14.350   5.269  1.00 19.67           C
ANISOU 3924  CE2 TRP A 497     2948   2225   2300   -286    329     51       C
ATOM   3925  CE3 TRP A 497      -5.166  16.326   6.289  1.00 20.97           C
ANISOU 3925  CE3 TRP A 497     3144   2364   2459   -269    302     63       C
ATOM   3926  CZ2 TRP A 497      -5.089  13.514   5.972  1.00 23.86           C
ANISOU 3926  CZ2 TRP A 497     3476   2745   2844   -281    351     30       C
ATOM   3927  CZ3 TRP A 497      -6.025  15.498   6.990  1.00 24.17           C
ANISOU 3927  CZ3 TRP A 497     3547   2762   2873   -263    324     42       C
ATOM   3928  CH2 TRP A 497      -5.981  14.108   6.825  1.00 26.53           C
ANISOU 3928  CH2 TRP A 497     3829   3069   3183   -270    348     27       C
ATOM   3929  N   LEU A 498      -2.964  20.702   3.447  1.00 25.65           N
ANISOU 3929  N   LEU A 498     3737   2975   3033   -276    212    169       N
ATOM   3930  CA  LEU A 498      -3.292  22.108   3.653  1.00 22.67           C
ANISOU 3930  CA  LEU A 498     3371   2578   2665   -268    191    184       C
ATOM   3931  C   LEU A 498      -4.183  22.652   2.544  1.00 25.87           C
ANISOU 3931  C   LEU A 498     3759   3009   3062   -258    186    190       C
ATOM   3932  O   LEU A 498      -5.028  23.520   2.800  1.00 26.72           O
ANISOU 3932  O   LEU A 498     3873   3102   3176   -247    176    190       O
ATOM   3933  CB  LEU A 498      -2.007  22.936   3.749  1.00 22.83           C
ANISOU 3933  CB  LEU A 498     3400   2579   2695   -278    171    216       C
ATOM   3934  CG  LEU A 498      -1.187  22.688   5.015  1.00 21.73           C
ANISOU 3934  CG  LEU A 498     3281   2410   2564   -285    169    211       C
ATOM   3935  CD1 LEU A 498       0.224  23.207   4.843  1.00 22.01           C
ANISOU 3935  CD1 LEU A 498     3317   2436   2611   -298    153    242       C
ATOM   3936  CD2 LEU A 498      -1.877  23.360   6.201  1.00 19.63           C
ANISOU 3936  CD2 LEU A 498     3037   2113   2307   -274    160    195       C
ATOM   3937  N   SER A 499      -4.002  22.171   1.309  1.00 22.13           N
ANISOU 3937  N   SER A 499     3262   2573   2573   -261    192    196       N
ATOM   3938  CA  SER A 499      -4.753  22.701   0.176  1.00 21.73           C
ANISOU 3938  CA  SER A 499     3192   2553   2512   -251    186    206       C
ATOM   3939  C   SER A 499      -6.243  22.400   0.261  1.00 28.05           C
ANISOU 3939  C   SER A 499     3987   3362   3309   -239    194    175       C
ATOM   3940  O   SER A 499      -7.031  23.042  -0.441  1.00 25.54           O
ANISOU 3940  O   SER A 499     3657   3062   2986   -227    186    182       O
ATOM   3941  CB  SER A 499      -4.201  22.138  -1.143  1.00 31.13           C
ANISOU 3941  CB  SER A 499     4358   3788   3682   -255    192    215       C
ATOM   3942  OG  SER A 499      -4.611  20.794  -1.343  1.00 23.79           O
ANISOU 3942  OG  SER A 499     3416   2883   2743   -257    212    179       O
ATOM   3943  N   MET A 500      -6.644  21.425   1.082  1.00 24.61           N
ANISOU 3943  N   MET A 500     3557   2916   2878   -241    211    142       N
ATOM   3944  CA  MET A 500      -8.056  21.079   1.188  1.00 24.65           C
ANISOU 3944  CA  MET A 500     3555   2928   2884   -230    221    112       C
ATOM   3945  C   MET A 500      -8.885  22.236   1.740  1.00 26.69           C
ANISOU 3945  C   MET A 500     3826   3163   3152   -216    208    118       C
ATOM   3946  O   MET A 500     -10.066  22.370   1.403  1.00 27.24           O
ANISOU 3946  O   MET A 500     3883   3247   3219   -205    209    106       O
ATOM   3947  CB  MET A 500      -8.214  19.840   2.069  1.00 26.58           C
ANISOU 3947  CB  MET A 500     3803   3160   3135   -235    243     81       C
ATOM   3948  CG  MET A 500      -7.513  18.596   1.522  1.00 32.98           C
ANISOU 3948  CG  MET A 500     4597   3992   3940   -248    258     71       C
ATOM   3949  SD  MET A 500      -8.124  18.130  -0.109  1.00 39.94           S
ANISOU 3949  SD  MET A 500     5444   4927   4805   -244    260     55       S
ATOM   3950  CE  MET A 500      -6.830  17.020  -0.667  1.00 29.95           C
ANISOU 3950  CE  MET A 500     4167   3679   3532   -259    272     52       C
ATOM   3951  N   ALA A 501      -8.291  23.071   2.591  1.00 23.21           N
ANISOU 3951  N   ALA A 501     3408   2686   2723   -217    196    135       N
ATOM   3952  CA  ALA A 501      -8.985  24.250   3.112  1.00 26.10           C
ANISOU 3952  CA  ALA A 501     3788   3027   3102   -204    183    140       C
ATOM   3953  C   ALA A 501      -9.528  25.154   2.011  1.00 33.81           C
ANISOU 3953  C   ALA A 501     4748   4023   4076   -194    169    161       C
ATOM   3954  O   ALA A 501     -10.450  25.939   2.264  1.00 37.66           O
ANISOU 3954  O   ALA A 501     5238   4497   4573   -179    162    159       O
ATOM   3955  CB  ALA A 501      -8.039  25.047   4.008  1.00 28.97           C
ANISOU 3955  CB  ALA A 501     4176   3351   3479   -208    168    156       C
ATOM   3956  N   HIS A 502      -8.985  25.059   0.795  1.00 37.48           N
ANISOU 3956  N   HIS A 502     5193   4520   4527   -199    165    182       N
ATOM   3957  CA  HIS A 502      -9.376  25.909  -0.320  1.00 38.36           C
ANISOU 3957  CA  HIS A 502     5287   4655   4633   -189    152    208       C
ATOM   3958  C   HIS A 502     -10.390  25.258  -1.259  1.00 42.68           C
ANISOU 3958  C   HIS A 502     5808   5249   5161   -181    161    189       C
ATOM   3959  O   HIS A 502     -10.828  25.910  -2.212  1.00 49.16           O
ANISOU 3959  O   HIS A 502     6611   6095   5973   -170    150    210       O
ATOM   3960  CB  HIS A 502      -8.132  26.323  -1.114  1.00 37.50           C
ANISOU 3960  CB  HIS A 502     5171   4557   4520   -198    142    247       C
ATOM   3961  CG  HIS A 502      -7.016  26.839  -0.257  1.00 40.29           C
ANISOU 3961  CG  HIS A 502     5547   4868   4894   -209    133    264       C
ATOM   3962  ND1 HIS A 502      -7.157  27.930   0.574  1.00 42.05           N
ANISOU 3962  ND1 HIS A 502     5789   5047   5143   -203    119    272       N
ATOM   3963  CD2 HIS A 502      -5.735  26.422  -0.115  1.00 42.18           C
ANISOU 3963  CD2 HIS A 502     5791   5101   5133   -224    135    273       C
ATOM   3964  CE1 HIS A 502      -6.015  28.157   1.198  1.00 41.83           C
ANISOU 3964  CE1 HIS A 502     5776   4988   5129   -215    111    283       C
ATOM   3965  NE2 HIS A 502      -5.135  27.258   0.796  1.00 42.64           N
ANISOU 3965  NE2 HIS A 502     5871   5114   5217   -229    121    286       N
ATOM   3966  N   ARG A 503     -10.766  23.999  -1.028  1.00 44.39           N
ANISOU 3966  N   ARG A 503     6018   5477   5371   -186    179    151       N
ATOM   3967  CA  ARG A 503     -11.766  23.343  -1.861  1.00 49.73           C
ANISOU 3967  CA  ARG A 503     6668   6195   6031   -179    186    128       C
ATOM   3968  C   ARG A 503     -13.098  24.093  -1.795  1.00 57.61           C
ANISOU 3968  C   ARG A 503     7661   7190   7037   -161    179    125       C
ATOM   3969  O   ARG A 503     -13.394  24.765  -0.802  1.00 57.52           O
ANISOU 3969  O   ARG A 503     7671   7139   7045   -155    175    127       O
ATOM   3970  CB  ARG A 503     -11.968  21.896  -1.417  1.00 52.63           C
ANISOU 3970  CB  ARG A 503     7031   6564   6401   -188    208     86       C
ATOM   3971  CG  ARG A 503     -10.898  20.944  -1.899  1.00 55.97           C
ANISOU 3971  CG  ARG A 503     7447   7007   6813   -202    217     82       C
ATOM   3972  CD  ARG A 503     -11.156  20.512  -3.330  1.00 62.94           C
ANISOU 3972  CD  ARG A 503     8298   7944   7672   -199    215     74       C
ATOM   3973  NE  ARG A 503      -9.913  20.175  -4.017  1.00 65.98           N
ANISOU 3973  NE  ARG A 503     8677   8350   8041   -208    216     88       N
ATOM   3974  CZ  ARG A 503      -9.341  18.975  -3.998  1.00 64.44           C
ANISOU 3974  CZ  ARG A 503     8478   8161   7846   -220    232     64       C
ATOM   3975  NH1 ARG A 503      -9.902  17.979  -3.328  1.00 62.16           N
ANISOU 3975  NH1 ARG A 503     8188   7857   7574   -225    249     27       N
ATOM   3976  NH2 ARG A 503      -8.207  18.774  -4.653  1.00 67.37           N
ANISOU 3976  NH2 ARG A 503     8842   8551   8202   -227    232     80       N
ATOM   3977  N   PRO A 504     -13.921  23.995  -2.841  1.00 62.37           N
ANISOU 3977  N   PRO A 504     8237   7836   7624   -151    175    119       N
ATOM   3978  CA  PRO A 504     -15.205  24.715  -2.841  1.00 60.41           C
ANISOU 3978  CA  PRO A 504     7983   7588   7384   -134    168    119       C
ATOM   3979  C   PRO A 504     -16.192  24.094  -1.862  1.00 54.34           C
ANISOU 3979  C   PRO A 504     7218   6798   6631   -132    183     80       C
ATOM   3980  O   PRO A 504     -16.409  22.877  -1.857  1.00 47.00           O
ANISOU 3980  O   PRO A 504     6276   5882   5698   -140    199     46       O
ATOM   3981  CB  PRO A 504     -15.691  24.581  -4.291  1.00 66.54           C
ANISOU 3981  CB  PRO A 504     8726   8423   8135   -125    161    121       C
ATOM   3982  CG  PRO A 504     -14.469  24.217  -5.083  1.00 70.41           C
ANISOU 3982  CG  PRO A 504     9210   8940   8604   -136    160    136       C
ATOM   3983  CD  PRO A 504     -13.632  23.392  -4.152  1.00 68.19           C
ANISOU 3983  CD  PRO A 504     8948   8626   8334   -154    175    118       C
ATOM   3984  N   ALA A 505     -16.790  24.947  -1.029  1.00 49.98           N
ANISOU 3984  N   ALA A 505     6681   6211   6097   -120    179     85       N
ATOM   3985  CA  ALA A 505     -17.790  24.551  -0.042  1.00 44.04           C
ANISOU 3985  CA  ALA A 505     5934   5439   5361   -115    194     54       C
ATOM   3986  C   ALA A 505     -17.273  23.478   0.912  1.00 40.11           C
ANISOU 3986  C   ALA A 505     5451   4921   4869   -129    214     30       C
ATOM   3987  O   ALA A 505     -18.070  22.755   1.520  1.00 42.11           O
ANISOU 3987  O   ALA A 505     5699   5168   5132   -128    231      2       O
ATOM   3988  CB  ALA A 505     -19.083  24.080  -0.721  1.00 44.69           C
ANISOU 3988  CB  ALA A 505     5985   5556   5438   -106    198     30       C
ATOM   3989  N   ALA A 506     -15.951  23.362   1.053  1.00 38.63           N
ANISOU 3989  N   ALA A 506     5279   4722   4677   -143    212     45       N
ATOM   3990  CA  ALA A 506     -15.373  22.305   1.873  1.00 37.78           C
ANISOU 3990  CA  ALA A 506     5182   4598   4574   -156    231     27       C
ATOM   3991  C   ALA A 506     -15.865  22.414   3.307  1.00 38.01           C
ANISOU 3991  C   ALA A 506     5233   4591   4619   -149    242     14       C
ATOM   3992  O   ALA A 506     -15.804  23.483   3.921  1.00 34.29           O
ANISOU 3992  O   ALA A 506     4781   4092   4154   -140    230     29       O
ATOM   3993  CB  ALA A 506     -13.846  22.365   1.839  1.00 38.26           C
ANISOU 3993  CB  ALA A 506     5258   4651   4629   -170    225     49       C
ATOM   3994  N   LYS A 507     -16.382  21.302   3.825  1.00 33.49           N
ANISOU 3994  N   LYS A 507     4653   4018   4053   -152    265    -13       N
ATOM   3995  CA  LYS A 507     -16.781  21.186   5.227  1.00 27.84           C
ANISOU 3995  CA  LYS A 507     3955   3272   3349   -145    280    -25       C
ATOM   3996  C   LYS A 507     -15.667  20.398   5.901  1.00 27.62           C
ANISOU 3996  C   LYS A 507     3943   3230   3321   -159    291    -24       C
ATOM   3997  O   LYS A 507     -15.696  19.167   5.948  1.00 28.68           O
ANISOU 3997  O   LYS A 507     4065   3373   3461   -168    312    -41       O
ATOM   3998  CB  LYS A 507     -18.132  20.498   5.361  1.00 34.92           C
ANISOU 3998  CB  LYS A 507     4832   4178   4257   -138    299    -51       C
ATOM   3999  CG  LYS A 507     -19.216  21.057   4.454  1.00 40.16           C
ANISOU 3999  CG  LYS A 507     5474   4865   4922   -126    288    -54       C
ATOM   4000  CD  LYS A 507     -20.373  21.626   5.256  1.00 49.09           C
ANISOU 4000  CD  LYS A 507     6609   5979   6064   -108    293    -60       C
ATOM   4001  CE  LYS A 507     -21.512  22.080   4.349  1.00 49.55           C
ANISOU 4001  CE  LYS A 507     6641   6061   6123    -96    283    -64       C
ATOM   4002  NZ  LYS A 507     -22.034  20.973   3.492  1.00 43.19           N
ANISOU 4002  NZ  LYS A 507     5802   5289   5320   -105    292    -86       N
ATOM   4003  N   LEU A 508     -14.658  21.120   6.383  1.00 23.66           N
ANISOU 4003  N   LEU A 508     3466   2707   2815   -161    277     -4       N
ATOM   4004  CA  LEU A 508     -13.468  20.485   6.946  1.00 24.25           C
ANISOU 4004  CA  LEU A 508     3555   2770   2887   -174    284      1       C
ATOM   4005  C   LEU A 508     -13.809  19.831   8.280  1.00 27.65           C
ANISOU 4005  C   LEU A 508     3998   3184   3325   -169    306    -14       C
ATOM   4006  O   LEU A 508     -14.375  20.491   9.157  1.00 27.16           O
ANISOU 4006  O   LEU A 508     3951   3104   3265   -154    306    -17       O
ATOM   4007  CB  LEU A 508     -12.363  21.515   7.156  1.00 24.72           C
ANISOU 4007  CB  LEU A 508     3637   2811   2943   -177    261     25       C
ATOM   4008  CG  LEU A 508     -11.849  22.280   5.937  1.00 28.00           C
ANISOU 4008  CG  LEU A 508     4044   3241   3354   -181    239     48       C
ATOM   4009  CD1 LEU A 508     -10.995  23.442   6.417  1.00 30.75           C
ANISOU 4009  CD1 LEU A 508     4416   3562   3707   -181    217     69       C
ATOM   4010  CD2 LEU A 508     -11.057  21.374   5.015  1.00 23.31           C
ANISOU 4010  CD2 LEU A 508     3432   2673   2751   -197    244     51       C
ATOM   4011  N   PRO A 509     -13.466  18.562   8.485  1.00 23.39           N
ANISOU 4011  N   PRO A 509     3451   2648   2789   -179    327    -22       N
ATOM   4012  CA  PRO A 509     -13.736  17.941   9.789  1.00 24.08           C
ANISOU 4012  CA  PRO A 509     3549   2720   2882   -173    350    -30       C
ATOM   4013  C   PRO A 509     -12.886  18.544  10.897  1.00 26.93           C
ANISOU 4013  C   PRO A 509     3941   3058   3233   -169    340    -17       C
ATOM   4014  O   PRO A 509     -11.776  19.034  10.671  1.00 20.97           O
ANISOU 4014  O   PRO A 509     3197   2298   2471   -178    320     -2       O
ATOM   4015  CB  PRO A 509     -13.387  16.464   9.569  1.00 22.48           C
ANISOU 4015  CB  PRO A 509     3328   2525   2688   -187    372    -38       C
ATOM   4016  CG  PRO A 509     -12.526  16.420   8.347  1.00 24.27           C
ANISOU 4016  CG  PRO A 509     3544   2769   2910   -202    357    -31       C
ATOM   4017  CD  PRO A 509     -12.812  17.649   7.529  1.00 27.44           C
ANISOU 4017  CD  PRO A 509     3944   3180   3301   -196    332    -23       C
ATOM   4018  N   LYS A 510     -13.420  18.499  12.118  1.00 21.77           N
ANISOU 4018  N   LYS A 510     3300   2392   2579   -155    354    -24       N
ATOM   4019  CA  LYS A 510     -12.609  18.848  13.275  1.00 19.69           C
ANISOU 4019  CA  LYS A 510     3066   2112   2305   -151    348    -16       C
ATOM   4020  C   LYS A 510     -11.469  17.848  13.436  1.00 21.71           C
ANISOU 4020  C   LYS A 510     3322   2369   2559   -165    357     -6       C
ATOM   4021  O   LYS A 510     -11.608  16.658  13.137  1.00 26.61           O
ANISOU 4021  O   LYS A 510     3922   2999   3190   -174    379     -9       O
ATOM   4022  CB  LYS A 510     -13.464  18.887  14.546  1.00 25.07           C
ANISOU 4022  CB  LYS A 510     3758   2786   2982   -130    365    -25       C
ATOM   4023  CG  LYS A 510     -14.335  20.099  14.647  1.00 35.67           C
ANISOU 4023  CG  LYS A 510     5108   4121   4323   -113    352    -34       C
ATOM   4024  CD  LYS A 510     -14.981  20.208  16.011  1.00 37.28           C
ANISOU 4024  CD  LYS A 510     5327   4319   4519    -92    367    -43       C
ATOM   4025  CE  LYS A 510     -15.414  21.640  16.260  1.00 34.96           C
ANISOU 4025  CE  LYS A 510     5049   4012   4221    -75    346    -51       C
ATOM   4026  NZ  LYS A 510     -14.227  22.502  16.436  1.00 34.93           N
ANISOU 4026  NZ  LYS A 510     5067   3993   4211    -80    316    -44       N
ATOM   4027  N   ILE A 511     -10.326  18.336  13.914  1.00 22.94           N
ANISOU 4027  N   ILE A 511     3498   2513   2705   -169    339      7       N
ATOM   4028  CA  ILE A 511      -9.142  17.504  14.112  1.00 20.30           C
ANISOU 4028  CA  ILE A 511     3166   2179   2369   -182    344     18       C
ATOM   4029  C   ILE A 511      -8.846  17.419  15.603  1.00 25.30           C
ANISOU 4029  C   ILE A 511     3820   2803   2989   -170    350     21       C
ATOM   4030  O   ILE A 511      -8.850  18.439  16.306  1.00 19.66           O
ANISOU 4030  O   ILE A 511     3127   2078   2264   -158    332     17       O
ATOM   4031  CB  ILE A 511      -7.940  18.040  13.317  1.00 19.77           C
ANISOU 4031  CB  ILE A 511     3100   2111   2300   -197    317     33       C
ATOM   4032  CG1 ILE A 511      -8.144  17.744  11.833  1.00 16.92           C
ANISOU 4032  CG1 ILE A 511     2714   1767   1948   -208    319     32       C
ATOM   4033  CG2 ILE A 511      -6.626  17.439  13.811  1.00 16.65           C
ANISOU 4033  CG2 ILE A 511     2713   1713   1902   -207    318     46       C
ATOM   4034  CD1 ILE A 511      -7.096  18.398  10.919  1.00 16.96           C
ANISOU 4034  CD1 ILE A 511     2718   1775   1951   -221    293     49       C
ATOM   4035  N   PHE A 512      -8.641  16.195  16.089  1.00 19.98           N
ANISOU 4035  N   PHE A 512     3140   2134   2319   -173    375     26       N
ATOM   4036  CA  PHE A 512      -8.343  15.921  17.487  1.00 18.66           C
ANISOU 4036  CA  PHE A 512     2990   1963   2138   -161    385     32       C
ATOM   4037  C   PHE A 512      -7.058  15.120  17.597  1.00 21.09           C
ANISOU 4037  C   PHE A 512     3296   2270   2446   -174    387     49       C
ATOM   4038  O   PHE A 512      -6.651  14.422  16.660  1.00 20.80           O
ANISOU 4038  O   PHE A 512     3241   2238   2424   -190    393     53       O
ATOM   4039  CB  PHE A 512      -9.455  15.118  18.173  1.00 22.98           C
ANISOU 4039  CB  PHE A 512     3527   2514   2689   -147    420     27       C
ATOM   4040  CG  PHE A 512     -10.812  15.749  18.102  1.00 14.73           C
ANISOU 4040  CG  PHE A 512     2480   1471   1646   -133    423     11       C
ATOM   4041  CD1 PHE A 512     -11.695  15.395  17.105  1.00 21.53           C
ANISOU 4041  CD1 PHE A 512     3316   2337   2528   -139    434      2       C
ATOM   4042  CD2 PHE A 512     -11.216  16.680  19.055  1.00 14.88           C
ANISOU 4042  CD2 PHE A 512     2521   1487   1648   -112    414      4       C
ATOM   4043  CE1 PHE A 512     -12.958  15.943  17.045  1.00 15.50           C
ANISOU 4043  CE1 PHE A 512     2548   1575   1767   -126    437    -12       C
ATOM   4044  CE2 PHE A 512     -12.481  17.241  19.000  1.00 21.75           C
ANISOU 4044  CE2 PHE A 512     3387   2357   2520    -98    419    -11       C
ATOM   4045  CZ  PHE A 512     -13.355  16.877  17.996  1.00 15.33           C
ANISOU 4045  CZ  PHE A 512     2548   1548   1728   -105    430    -17       C
ATOM   4046  N   HIS A 513      -6.436  15.208  18.767  1.00 15.77           N
ANISOU 4046  N   HIS A 513     2642   1595   1755   -165    382     57       N
ATOM   4047  CA  HIS A 513      -5.323  14.349  19.147  1.00 20.54           C
ANISOU 4047  CA  HIS A 513     3246   2201   2358   -172    389     75       C
ATOM   4048  C   HIS A 513      -5.655  13.658  20.470  1.00 18.96           C
ANISOU 4048  C   HIS A 513     3050   2006   2146   -154    414     82       C
ATOM   4049  O   HIS A 513      -6.057  14.316  21.438  1.00 16.59           O
ANISOU 4049  O   HIS A 513     2770   1710   1826   -135    409     76       O
ATOM   4050  CB  HIS A 513      -4.035  15.154  19.278  1.00 17.38           C
ANISOU 4050  CB  HIS A 513     2863   1796   1946   -179    354     82       C
ATOM   4051  CG  HIS A 513      -2.793  14.318  19.338  1.00 19.63           C
ANISOU 4051  CG  HIS A 513     3143   2083   2235   -191    357    101       C
ATOM   4052  ND1 HIS A 513      -2.315  13.776  20.513  1.00 17.61           N
ANISOU 4052  ND1 HIS A 513     2896   1832   1965   -181    366    114       N
ATOM   4053  CD2 HIS A 513      -1.915  13.954  18.370  1.00 17.68           C
ANISOU 4053  CD2 HIS A 513     2882   1835   2002   -211    352    111       C
ATOM   4054  CE1 HIS A 513      -1.215  13.088  20.261  1.00 21.46           C
ANISOU 4054  CE1 HIS A 513     3374   2319   2461   -194    366    131       C
ATOM   4055  NE2 HIS A 513      -0.938  13.199  18.973  1.00 19.41           N
ANISOU 4055  NE2 HIS A 513     3100   2055   2218   -213    358    129       N
ATOM   4056  N   VAL A 514      -5.453  12.343  20.525  1.00 22.88           N
ANISOU 4056  N   VAL A 514     3530   2505   2657   -159    442     97       N
ATOM   4057  CA  VAL A 514      -5.704  11.585  21.745  1.00 22.30           C
ANISOU 4057  CA  VAL A 514     3459   2439   2576   -142    470    111       C
ATOM   4058  C   VAL A 514      -4.409  10.945  22.212  1.00 20.80           C
ANISOU 4058  C   VAL A 514     3271   2251   2381   -147    469    134       C
ATOM   4059  O   VAL A 514      -3.440  10.796  21.457  1.00 20.25           O
ANISOU 4059  O   VAL A 514     3195   2176   2323   -165    455    139       O
ATOM   4060  CB  VAL A 514      -6.790  10.508  21.577  1.00 18.41           C
ANISOU 4060  CB  VAL A 514     2941   1946   2109   -140    510    112       C
ATOM   4061  CG1 VAL A 514      -8.111  11.148  21.197  1.00 18.18           C
ANISOU 4061  CG1 VAL A 514     2908   1915   2083   -134    511     90       C
ATOM   4062  CG2 VAL A 514      -6.360   9.442  20.547  1.00 19.19           C
ANISOU 4062  CG2 VAL A 514     3013   2036   2240   -162    523    117       C
ATOM   4063  N   ASN A 515      -4.407  10.565  23.486  1.00 22.55           N
ANISOU 4063  N   ASN A 515     3502   2483   2586   -128    484    149       N
ATOM   4064  CA  ASN A 515      -3.322   9.796  24.087  1.00 15.07           C
ANISOU 4064  CA  ASN A 515     2553   1540   1634   -128    489    175       C
ATOM   4065  C   ASN A 515      -3.973   8.804  25.051  1.00 17.13           C
ANISOU 4065  C   ASN A 515     2806   1809   1895   -110    529    195       C
ATOM   4066  O   ASN A 515      -4.415   9.182  26.145  1.00 22.52           O
ANISOU 4066  O   ASN A 515     3503   2505   2548    -86    532    196       O
ATOM   4067  CB  ASN A 515      -2.317  10.696  24.797  1.00 16.80           C
ANISOU 4067  CB  ASN A 515     2798   1767   1820   -122    453    175       C
ATOM   4068  CG  ASN A 515      -1.131   9.929  25.342  1.00 21.97           C
ANISOU 4068  CG  ASN A 515     3450   2427   2469   -123    456    203       C
ATOM   4069  OD1 ASN A 515      -0.867   8.797  24.930  1.00 24.45           O
ANISOU 4069  OD1 ASN A 515     3744   2736   2811   -134    479    221       O
ATOM   4070  ND2 ASN A 515      -0.403  10.541  26.267  1.00 21.90           N
ANISOU 4070  ND2 ASN A 515     3462   2430   2429   -112    430    205       N
ATOM   4071  N   TRP A 516      -4.038   7.543  24.633  1.00 19.03           N
ANISOU 4071  N   TRP A 516     3020   2041   2171   -119    560    210       N
ATOM   4072  CA  TRP A 516      -4.535   6.495  25.505  1.00 20.64           C
ANISOU 4072  CA  TRP A 516     3211   2249   2382   -104    600    235       C
ATOM   4073  C   TRP A 516      -3.497   6.043  26.522  1.00 27.74           C
ANISOU 4073  C   TRP A 516     4118   3159   3262    -93    601    266       C
ATOM   4074  O   TRP A 516      -3.843   5.287  27.441  1.00 24.25           O
ANISOU 4074  O   TRP A 516     3669   2726   2818    -75    633    292       O
ATOM   4075  CB  TRP A 516      -4.966   5.262  24.695  1.00 21.69           C
ANISOU 4075  CB  TRP A 516     3311   2364   2566   -118    633    239       C
ATOM   4076  CG  TRP A 516      -6.034   5.402  23.607  1.00 23.27           C
ANISOU 4076  CG  TRP A 516     3496   2553   2793   -130    638    209       C
ATOM   4077  CD1 TRP A 516      -6.176   4.569  22.520  1.00 19.96           C
ANISOU 4077  CD1 TRP A 516     3048   2118   2417   -150    653    200       C
ATOM   4078  CD2 TRP A 516      -7.080   6.390  23.485  1.00 20.00           C
ANISOU 4078  CD2 TRP A 516     3091   2144   2364   -123    628    185       C
ATOM   4079  NE1 TRP A 516      -7.252   4.954  21.760  1.00 26.99           N
ANISOU 4079  NE1 TRP A 516     3930   3006   3319   -155    652    172       N
ATOM   4080  CE2 TRP A 516      -7.808   6.081  22.312  1.00 20.20           C
ANISOU 4080  CE2 TRP A 516     3093   2158   2425   -139    636    164       C
ATOM   4081  CE3 TRP A 516      -7.462   7.510  24.238  1.00 19.14           C
ANISOU 4081  CE3 TRP A 516     3007   2048   2217   -104    611    176       C
ATOM   4082  CZ2 TRP A 516      -8.902   6.831  21.893  1.00 20.56           C
ANISOU 4082  CZ2 TRP A 516     3138   2206   2469   -136    630    139       C
ATOM   4083  CZ3 TRP A 516      -8.547   8.262  23.813  1.00 20.33           C
ANISOU 4083  CZ3 TRP A 516     3158   2198   2367   -101    606    151       C
ATOM   4084  CH2 TRP A 516      -9.257   7.925  22.659  1.00 15.83           C
ANISOU 4084  CH2 TRP A 516     2563   1617   1833   -117    615    134       C
ATOM   4085  N   PHE A 517      -2.248   6.497  26.391  1.00 21.34           N
ANISOU 4085  N   PHE A 517     3321   2351   2437   -102    568    266       N
ATOM   4086  CA  PHE A 517      -1.101   5.787  26.948  1.00 22.18           C
ANISOU 4086  CA  PHE A 517     3425   2464   2540   -100    570    297       C
ATOM   4087  C   PHE A 517      -0.291   6.585  27.961  1.00 20.91           C
ANISOU 4087  C   PHE A 517     3289   2323   2331    -86    539    301       C
ATOM   4088  O   PHE A 517       0.829   6.170  28.288  1.00 23.55           O
ANISOU 4088  O   PHE A 517     3622   2662   2661    -87    532    324       O
ATOM   4089  CB  PHE A 517      -0.185   5.322  25.806  1.00 27.82           C
ANISOU 4089  CB  PHE A 517     4123   3161   3288   -127    563    297       C
ATOM   4090  CG  PHE A 517      -0.855   4.372  24.858  1.00 26.25           C
ANISOU 4090  CG  PHE A 517     3895   2942   3136   -140    594    293       C
ATOM   4091  CD1 PHE A 517      -0.856   2.998  25.114  1.00 26.42           C
ANISOU 4091  CD1 PHE A 517     3894   2956   3189   -138    632    320       C
ATOM   4092  CD2 PHE A 517      -1.517   4.843  23.736  1.00 22.08           C
ANISOU 4092  CD2 PHE A 517     3362   2404   2622   -155    586    261       C
ATOM   4093  CE1 PHE A 517      -1.495   2.115  24.254  1.00 28.64           C
ANISOU 4093  CE1 PHE A 517     4146   3217   3517   -151    660    312       C
ATOM   4094  CE2 PHE A 517      -2.155   3.964  22.861  1.00 22.53           C
ANISOU 4094  CE2 PHE A 517     3392   2447   2723   -167    613    252       C
ATOM   4095  CZ  PHE A 517      -2.148   2.591  23.127  1.00 24.53           C
ANISOU 4095  CZ  PHE A 517     3621   2689   3009   -165    650    276       C
ATOM   4096  N   ARG A 518      -0.817   7.697  28.481  1.00 23.59           N
ANISOU 4096  N   ARG A 518     3651   2675   2637    -71    520    280       N
ATOM   4097  CA  ARG A 518      -0.087   8.472  29.476  1.00 27.15           C
ANISOU 4097  CA  ARG A 518     4126   3146   3043    -56    489    278       C
ATOM   4098  C   ARG A 518       0.031   7.679  30.772  1.00 33.21           C
ANISOU 4098  C   ARG A 518     4892   3938   3787    -31    512    312       C
ATOM   4099  O   ARG A 518      -0.886   6.950  31.162  1.00 29.37           O
ANISOU 4099  O   ARG A 518     4395   3457   3309    -17    552    329       O
ATOM   4100  CB  ARG A 518      -0.771   9.819  29.728  1.00 26.33           C
ANISOU 4100  CB  ARG A 518     4045   3048   2912    -45    465    244       C
ATOM   4101  CG  ARG A 518       0.139  10.854  30.398  1.00 26.09           C
ANISOU 4101  CG  ARG A 518     4039   3031   2844    -38    421    230       C
ATOM   4102  CD  ARG A 518      -0.554  12.219  30.550  1.00 26.82           C
ANISOU 4102  CD  ARG A 518     4151   3123   2915    -28    397    192       C
ATOM   4103  NE  ARG A 518       0.359  13.222  31.082  1.00 24.99           N
ANISOU 4103  NE  ARG A 518     3940   2898   2655    -24    352    174       N
ATOM   4104  CZ  ARG A 518       0.090  14.526  31.156  1.00 27.62           C
ANISOU 4104  CZ  ARG A 518     4292   3227   2976    -20    322    139       C
ATOM   4105  NH1 ARG A 518      -1.072  15.002  30.727  1.00 25.27           N
ANISOU 4105  NH1 ARG A 518     3996   2918   2689    -17    332    118       N
ATOM   4106  NH2 ARG A 518       0.998  15.360  31.644  1.00 28.65           N
ANISOU 4106  NH2 ARG A 518     4438   3362   3086    -18    280    123       N
ATOM   4107  N   LYS A 519       1.182   7.805  31.427  1.00 28.94           N
ANISOU 4107  N   LYS A 519     4362   3414   3221    -25    488    324       N
ATOM   4108  CA  LYS A 519       1.487   7.027  32.616  1.00 31.41           C
ANISOU 4108  CA  LYS A 519     4672   3753   3510     -2    507    361       C
ATOM   4109  C   LYS A 519       1.879   7.957  33.755  1.00 39.88           C
ANISOU 4109  C   LYS A 519     5770   4856   4525     21    475    348       C
ATOM   4110  O   LYS A 519       2.449   9.029  33.534  1.00 37.28           O
ANISOU 4110  O   LYS A 519     5457   4523   4184     11    431    318       O
ATOM   4111  CB  LYS A 519       2.609   6.019  32.341  1.00 28.44           C
ANISOU 4111  CB  LYS A 519     4277   3368   3159    -16    513    394       C
ATOM   4112  CG  LYS A 519       2.167   4.795  31.547  1.00 28.91           C
ANISOU 4112  CG  LYS A 519     4308   3403   3274    -30    556    413       C
ATOM   4113  CD  LYS A 519       3.365   3.985  31.077  1.00 30.72           C
ANISOU 4113  CD  LYS A 519     4521   3619   3532    -47    555    437       C
ATOM   4114  CE  LYS A 519       2.959   2.579  30.646  1.00 35.75           C
ANISOU 4114  CE  LYS A 519     5127   4236   4220    -53    602    463       C
ATOM   4115  NZ  LYS A 519       4.061   1.899  29.912  1.00 35.49           N
ANISOU 4115  NZ  LYS A 519     5077   4184   4222    -73    600    476       N
ATOM   4116  N   ASP A 520       1.542   7.546  34.981  1.00 37.54           N
ANISOU 4116  N   ASP A 520     5477   4592   4196     52    497    372       N
ATOM   4117  CA  ASP A 520       1.993   8.262  36.163  1.00 42.38           C
ANISOU 4117  CA  ASP A 520     6112   5241   4750     77    468    363       C
ATOM   4118  C   ASP A 520       3.454   7.926  36.444  1.00 46.39           C
ANISOU 4118  C   ASP A 520     6616   5760   5250     72    445    385       C
ATOM   4119  O   ASP A 520       4.067   7.089  35.776  1.00 46.11           O
ANISOU 4119  O   ASP A 520     6562   5705   5254     52    456    411       O
ATOM   4120  CB  ASP A 520       1.115   7.931  37.370  1.00 47.63           C
ANISOU 4120  CB  ASP A 520     6779   5941   5378    114    500    382       C
ATOM   4121  CG  ASP A 520       1.002   6.428  37.633  1.00 51.35           C
ANISOU 4121  CG  ASP A 520     7224   6416   5869    122    550    438       C
ATOM   4122  OD1 ASP A 520      -0.119   5.956  37.926  1.00 51.27           O
ANISOU 4122  OD1 ASP A 520     7205   6412   5864    138    592    453       O
ATOM   4123  OD2 ASP A 520       2.024   5.716  37.544  1.00 49.47           O
ANISOU 4123  OD2 ASP A 520     6974   6175   5647    113    548    467       O
ATOM   4124  N   LYS A 521       4.009   8.559  37.479  1.00 52.15           N
ANISOU 4124  N   LYS A 521     7364   6523   5927     93    414    376       N
ATOM   4125  CA  LYS A 521       5.402   8.334  37.849  1.00 59.62           C
ANISOU 4125  CA  LYS A 521     8308   7484   6861     91    388    395       C
ATOM   4126  C   LYS A 521       5.690   6.897  38.273  1.00 62.77           C
ANISOU 4126  C   LYS A 521     8686   7897   7268    102    426    453       C
ATOM   4127  O   LYS A 521       6.860   6.557  38.486  1.00 66.22           O
ANISOU 4127  O   LYS A 521     9116   8344   7702    100    409    475       O
ATOM   4128  CB  LYS A 521       5.796   9.306  38.963  1.00 65.05           C
ANISOU 4128  CB  LYS A 521     9018   8209   7488    115    347    369       C
ATOM   4129  CG  LYS A 521       4.667   9.623  39.935  1.00 69.88           C
ANISOU 4129  CG  LYS A 521     9644   8852   8054    150    364    357       C
ATOM   4130  CD  LYS A 521       4.782  11.043  40.478  1.00 69.62           C
ANISOU 4130  CD  LYS A 521     9636   8836   7979    161    316    304       C
ATOM   4131  CE  LYS A 521       4.593  12.077  39.370  1.00 67.98           C
ANISOU 4131  CE  LYS A 521     9437   8584   7808    132    290    258       C
ATOM   4132  NZ  LYS A 521       4.735  13.480  39.859  1.00 64.78           N
ANISOU 4132  NZ  LYS A 521     9055   8189   7369    141    241    204       N
ATOM   4133  N   ASN A 522       4.672   6.044  38.383  1.00 61.57           N
ANISOU 4133  N   ASN A 522     8520   7744   7131    114    477    480       N
ATOM   4134  CA  ASN A 522       4.851   4.644  38.744  1.00 61.38           C
ANISOU 4134  CA  ASN A 522     8472   7727   7121    125    518    538       C
ATOM   4135  C   ASN A 522       4.759   3.707  37.548  1.00 56.79           C
ANISOU 4135  C   ASN A 522     7866   7101   6611     96    548    555       C
ATOM   4136  O   ASN A 522       4.722   2.485  37.736  1.00 50.18           O
ANISOU 4136  O   ASN A 522     7007   6262   5799    103    588    602       O
ATOM   4137  CB  ASN A 522       3.815   4.232  39.791  1.00 64.71           C
ANISOU 4137  CB  ASN A 522     8893   8181   7513    161    558    564       C
ATOM   4138  CG  ASN A 522       3.858   5.102  41.026  1.00 65.12           C
ANISOU 4138  CG  ASN A 522     8970   8283   7491    193    531    547       C
ATOM   4139  OD1 ASN A 522       4.927   5.538  41.456  1.00 63.38           O
ANISOU 4139  OD1 ASN A 522     8759   8084   7238    197    490    539       O
ATOM   4140  ND2 ASN A 522       2.691   5.361  41.605  1.00 65.39           N
ANISOU 4140  ND2 ASN A 522     9012   8337   7498    218    553    539       N
ATOM   4141  N   GLY A 523       4.707   4.242  36.328  1.00 52.39           N
ANISOU 4141  N   GLY A 523     7311   6508   6088     65    530    518       N
ATOM   4142  CA  GLY A 523       4.572   3.397  35.156  1.00 48.17           C
ANISOU 4142  CA  GLY A 523     6752   5933   5618     38    557    527       C
ATOM   4143  C   GLY A 523       3.195   2.805  34.955  1.00 42.15           C
ANISOU 4143  C   GLY A 523     5976   5157   4884     43    604    533       C
ATOM   4144  O   GLY A 523       3.043   1.863  34.172  1.00 43.78           O
ANISOU 4144  O   GLY A 523     6157   5333   5145     26    634    548       O
ATOM   4145  N   LYS A 524       2.182   3.332  35.643  1.00 38.36           N
ANISOU 4145  N   LYS A 524     5509   4697   4370     65    612    521       N
ATOM   4146  CA  LYS A 524       0.810   2.854  35.543  1.00 44.24           C
ANISOU 4146  CA  LYS A 524     6240   5431   5138     71    656    527       C
ATOM   4147  C   LYS A 524       0.011   3.748  34.599  1.00 34.00           C
ANISOU 4147  C   LYS A 524     4951   4112   3855     53    642    477       C
ATOM   4148  O   LYS A 524       0.108   4.977  34.672  1.00 32.62           O
ANISOU 4148  O   LYS A 524     4801   3947   3646     55    603    440       O
ATOM   4149  CB  LYS A 524       0.160   2.839  36.930  1.00 53.63           C
ANISOU 4149  CB  LYS A 524     7436   6660   6280    110    677    549       C
ATOM   4150  CG  LYS A 524      -1.320   2.495  36.948  1.00 67.42           C
ANISOU 4150  CG  LYS A 524     9171   8400   8047    119    721    554       C
ATOM   4151  CD  LYS A 524      -1.554   1.044  36.569  1.00 76.67           C
ANISOU 4151  CD  LYS A 524    10307   9545   9279    110    769    595       C
ATOM   4152  CE  LYS A 524      -3.017   0.665  36.739  1.00 80.65           C
ANISOU 4152  CE  LYS A 524    10796  10044   9802    122    814    604       C
ATOM   4153  NZ  LYS A 524      -3.272  -0.736  36.302  1.00 80.62           N
ANISOU 4153  NZ  LYS A 524    10756  10010   9867    110    860    640       N
ATOM   4154  N   PHE A 525      -0.787   3.130  33.721  1.00 28.76           N
ANISOU 4154  N   PHE A 525     4266   3418   3244     37    673    475       N
ATOM   4155  CA  PHE A 525      -1.640   3.909  32.820  1.00 29.84           C
ANISOU 4155  CA  PHE A 525     4408   3536   3394     22    662    431       C
ATOM   4156  C   PHE A 525      -2.615   4.772  33.612  1.00 33.79           C
ANISOU 4156  C   PHE A 525     4926   4060   3851     48    662    414       C
ATOM   4157  O   PHE A 525      -3.280   4.295  34.538  1.00 27.24           O
ANISOU 4157  O   PHE A 525     4092   3250   3008     73    695    440       O
ATOM   4158  CB  PHE A 525      -2.416   2.995  31.869  1.00 23.91           C
ANISOU 4158  CB  PHE A 525     3627   2753   2704      4    699    434       C
ATOM   4159  CG  PHE A 525      -1.575   2.394  30.766  1.00 27.19           C
ANISOU 4159  CG  PHE A 525     4025   3140   3164    -25    693    434       C
ATOM   4160  CD1 PHE A 525      -1.448   1.022  30.643  1.00 28.47           C
ANISOU 4160  CD1 PHE A 525     4159   3286   3372    -30    729    467       C
ATOM   4161  CD2 PHE A 525      -0.923   3.196  29.849  1.00 31.49           C
ANISOU 4161  CD2 PHE A 525     4581   3675   3708    -47    653    402       C
ATOM   4162  CE1 PHE A 525      -0.692   0.467  29.644  1.00 29.46           C
ANISOU 4162  CE1 PHE A 525     4269   3388   3538    -55    725    465       C
ATOM   4163  CE2 PHE A 525      -0.150   2.636  28.835  1.00 26.04           C
ANISOU 4163  CE2 PHE A 525     3875   2963   3057    -73    650    403       C
ATOM   4164  CZ  PHE A 525      -0.040   1.279  28.737  1.00 27.99           C
ANISOU 4164  CZ  PHE A 525     4094   3195   3346    -76    685    432       C
ATOM   4165  N   LEU A 526      -2.708   6.046  33.241  1.00 28.14           N
ANISOU 4165  N   LEU A 526     4232   3342   3117     41    624    370       N
ATOM   4166  CA  LEU A 526      -3.619   6.959  33.918  1.00 25.20           C
ANISOU 4166  CA  LEU A 526     3879   2990   2707     65    620    348       C
ATOM   4167  C   LEU A 526      -5.067   6.795  33.475  1.00 31.47           C
ANISOU 4167  C   LEU A 526     4658   3769   3529     65    653    339       C
ATOM   4168  O   LEU A 526      -5.970   7.221  34.205  1.00 34.75           O
ANISOU 4168  O   LEU A 526     5082   4205   3917     90    665    332       O
ATOM   4169  CB  LEU A 526      -3.181   8.409  33.681  1.00 28.64           C
ANISOU 4169  CB  LEU A 526     4341   3425   3117     58    568    304       C
ATOM   4170  CG  LEU A 526      -1.972   8.886  34.485  1.00 31.11           C
ANISOU 4170  CG  LEU A 526     4673   3761   3387     68    532    304       C
ATOM   4171  CD1 LEU A 526      -1.296  10.078  33.802  1.00 25.13           C
ANISOU 4171  CD1 LEU A 526     3932   2986   2629     48    480    266       C
ATOM   4172  CD2 LEU A 526      -2.419   9.265  35.883  1.00 35.84           C
ANISOU 4172  CD2 LEU A 526     5288   4398   3930    106    536    304       C
ATOM   4173  N   TRP A 527      -5.305   6.197  32.303  1.00 26.19           N
ANISOU 4173  N   TRP A 527     3966   3069   2914     38    667    337       N
ATOM   4174  CA  TRP A 527      -6.627   6.092  31.694  1.00 23.85           C
ANISOU 4174  CA  TRP A 527     3654   2756   2650     33    692    323       C
ATOM   4175  C   TRP A 527      -6.943   4.627  31.404  1.00 28.38           C
ANISOU 4175  C   TRP A 527     4194   3313   3275     24    737    355       C
ATOM   4176  O   TRP A 527      -6.096   3.918  30.822  1.00 28.94           O
ANISOU 4176  O   TRP A 527     4251   3367   3376      4    736    367       O
ATOM   4177  CB  TRP A 527      -6.662   6.895  30.394  1.00 27.74           C
ANISOU 4177  CB  TRP A 527     4151   3227   3163      7    660    282       C
ATOM   4178  CG  TRP A 527      -7.974   6.913  29.689  1.00 21.66           C
ANISOU 4178  CG  TRP A 527     3365   2442   2423      1    679    264       C
ATOM   4179  CD1 TRP A 527      -8.249   6.386  28.466  1.00 19.52           C
ANISOU 4179  CD1 TRP A 527     3070   2146   2201    -24    688    255       C
ATOM   4180  CD2 TRP A 527      -9.177   7.555  30.130  1.00 26.44           C
ANISOU 4180  CD2 TRP A 527     3977   3058   3011     21    688    248       C
ATOM   4181  NE1 TRP A 527      -9.555   6.640  28.122  1.00 22.19           N
ANISOU 4181  NE1 TRP A 527     3399   2479   2553    -21    701    236       N
ATOM   4182  CE2 TRP A 527     -10.150   7.352  29.130  1.00 26.14           C
ANISOU 4182  CE2 TRP A 527     3917   3000   3015      6    702    232       C
ATOM   4183  CE3 TRP A 527      -9.535   8.253  31.288  1.00 19.38           C
ANISOU 4183  CE3 TRP A 527     3103   2189   2069     52    686    245       C
ATOM   4184  CZ2 TRP A 527     -11.455   7.832  29.245  1.00 21.50           C
ANISOU 4184  CZ2 TRP A 527     3328   2417   2426     20    715    216       C
ATOM   4185  CZ3 TRP A 527     -10.833   8.737  31.400  1.00 26.60           C
ANISOU 4185  CZ3 TRP A 527     4018   3108   2982     66    699    228       C
ATOM   4186  CH2 TRP A 527     -11.776   8.522  30.383  1.00 23.01           C
ANISOU 4186  CH2 TRP A 527     3541   2632   2571     50    714    215       C
ATOM   4187  N   PRO A 528      -8.143   4.143  31.751  1.00 26.02           N
ANISOU 4187  N   PRO A 528     3878   3016   2992     38    777    367       N
ATOM   4188  CA  PRO A 528      -8.456   2.723  31.502  1.00 24.33           C
ANISOU 4188  CA  PRO A 528     3629   2782   2833     29    820    397       C
ATOM   4189  C   PRO A 528      -8.612   2.356  30.029  1.00 26.32           C
ANISOU 4189  C   PRO A 528     3859   2999   3142     -4    819    373       C
ATOM   4190  O   PRO A 528      -8.468   1.176  29.693  1.00 23.83           O
ANISOU 4190  O   PRO A 528     3516   2663   2874    -16    845    394       O
ATOM   4191  CB  PRO A 528      -9.770   2.507  32.271  1.00 28.31           C
ANISOU 4191  CB  PRO A 528     4122   3298   3335     54    860    413       C
ATOM   4192  CG  PRO A 528     -10.361   3.854  32.427  1.00 30.38           C
ANISOU 4192  CG  PRO A 528     4410   3577   3556     66    835    377       C
ATOM   4193  CD  PRO A 528      -9.199   4.812  32.532  1.00 27.68           C
ANISOU 4193  CD  PRO A 528     4100   3248   3169     65    786    358       C
ATOM   4194  N   GLY A 529      -8.919   3.306  29.145  1.00 29.88           N
ANISOU 4194  N   GLY A 529     4320   3444   3590    -17    789    330       N
ATOM   4195  CA  GLY A 529      -8.981   3.028  27.708  1.00 25.50           C
ANISOU 4195  CA  GLY A 529     3746   2862   3082    -48    783    306       C
ATOM   4196  C   GLY A 529     -10.017   1.988  27.286  1.00 28.55           C
ANISOU 4196  C   GLY A 529     4096   3228   3525    -55    824    310       C
ATOM   4197  O   GLY A 529     -10.963   1.665  28.008  1.00 27.24           O
ANISOU 4197  O   GLY A 529     3919   3067   3364    -37    857    327       O
ATOM   4198  N   PHE A 530      -9.796   1.451  26.079  1.00 20.28           N
ANISOU 4198  N   PHE A 530     3027   2156   2521    -82    821    293       N
ATOM   4199  CA  PHE A 530     -10.673   0.485  25.395  1.00 25.22           C
ANISOU 4199  CA  PHE A 530     3615   2759   3207    -95    852    286       C
ATOM   4200  C   PHE A 530     -12.094   1.052  25.358  1.00 28.93           C
ANISOU 4200  C   PHE A 530     4081   3233   3676    -87    858    265       C
ATOM   4201  O   PHE A 530     -12.292   2.167  24.854  1.00 22.97           O
ANISOU 4201  O   PHE A 530     3345   2489   2895    -90    826    234       O
ATOM   4202  CB  PHE A 530     -10.502  -0.895  26.051  1.00 26.24           C
ANISOU 4202  CB  PHE A 530     3720   2875   3373    -90    893    328       C
ATOM   4203  CG  PHE A 530      -9.072  -1.362  26.041  1.00 22.85           C
ANISOU 4203  CG  PHE A 530     3295   2442   2943    -97    883    347       C
ATOM   4204  CD1 PHE A 530      -8.276  -1.217  27.166  1.00 25.73           C
ANISOU 4204  CD1 PHE A 530     3682   2827   3267    -78    880    382       C
ATOM   4205  CD2 PHE A 530      -8.499  -1.846  24.880  1.00 22.69           C
ANISOU 4205  CD2 PHE A 530     3259   2401   2960   -123    874    327       C
ATOM   4206  CE1 PHE A 530      -6.942  -1.583  27.146  1.00 20.56           C
ANISOU 4206  CE1 PHE A 530     3032   2171   2611    -84    868    398       C
ATOM   4207  CE2 PHE A 530      -7.167  -2.213  24.847  1.00 27.28           C
ANISOU 4207  CE2 PHE A 530     3846   2980   3541   -129    863    343       C
ATOM   4208  CZ  PHE A 530      -6.389  -2.092  25.986  1.00 19.35           C
ANISOU 4208  CZ  PHE A 530     2861   1993   2497   -110    861    380       C
ATOM   4209  N   GLY A 531     -13.104   0.335  25.859  1.00 30.75           N
ANISOU 4209  N   GLY A 531     4288   3459   3938    -77    899    284       N
ATOM   4210  CA  GLY A 531     -14.463   0.828  25.742  1.00 26.35           C
ANISOU 4210  CA  GLY A 531     3723   2905   3384    -71    906    263       C
ATOM   4211  C   GLY A 531     -14.706   2.124  26.481  1.00 18.23           C
ANISOU 4211  C   GLY A 531     2728   1904   2294    -47    887    258       C
ATOM   4212  O   GLY A 531     -15.682   2.820  26.187  1.00 22.66           O
ANISOU 4212  O   GLY A 531     3290   2469   2851    -44    881    233       O
ATOM   4213  N   GLU A 532     -13.864   2.449  27.467  1.00 21.88           N
ANISOU 4213  N   GLU A 532     3219   2386   2710    -30    878    281       N
ATOM   4214  CA  GLU A 532     -14.024   3.724  28.158  1.00 21.26           C
ANISOU 4214  CA  GLU A 532     3174   2333   2573     -8    856    271       C
ATOM   4215  C   GLU A 532     -13.628   4.877  27.267  1.00 23.21           C
ANISOU 4215  C   GLU A 532     3441   2577   2799    -22    808    231       C
ATOM   4216  O   GLU A 532     -13.977   6.025  27.559  1.00 22.33           O
ANISOU 4216  O   GLU A 532     3353   2481   2651     -7    788    212       O
ATOM   4217  CB  GLU A 532     -13.193   3.773  29.440  1.00 23.65           C
ANISOU 4217  CB  GLU A 532     3499   2658   2829     15    857    302       C
ATOM   4218  CG  GLU A 532     -13.445   2.600  30.411  1.00 27.48           C
ANISOU 4218  CG  GLU A 532     3963   3148   3330     32    905    350       C
ATOM   4219  CD  GLU A 532     -14.829   2.602  31.045  1.00 30.18           C
ANISOU 4219  CD  GLU A 532     4293   3500   3674     54    940    359       C
ATOM   4220  OE1 GLU A 532     -15.623   3.527  30.782  1.00 29.70           O
ANISOU 4220  OE1 GLU A 532     4240   3443   3599     58    926    326       O
ATOM   4221  OE2 GLU A 532     -15.126   1.657  31.818  1.00 24.73           O
ANISOU 4221  OE2 GLU A 532     3583   2813   3000     68    982    401       O
ATOM   4222  N   ASN A 533     -12.909   4.597  26.187  1.00 24.70           N
ANISOU 4222  N   ASN A 533     3623   2750   3014    -49    790    218       N
ATOM   4223  CA  ASN A 533     -12.616   5.645  25.223  1.00 22.33           C
ANISOU 4223  CA  ASN A 533     3337   2447   2699    -63    748    184       C
ATOM   4224  C   ASN A 533     -13.882   6.242  24.632  1.00 18.72           C
ANISOU 4224  C   ASN A 533     2871   1988   2252    -63    746    155       C
ATOM   4225  O   ASN A 533     -13.833   7.351  24.087  1.00 20.90           O
ANISOU 4225  O   ASN A 533     3165   2269   2509    -66    712    129       O
ATOM   4226  CB  ASN A 533     -11.708   5.076  24.135  1.00 19.43           C
ANISOU 4226  CB  ASN A 533     2957   2065   2360    -91    736    178       C
ATOM   4227  CG  ASN A 533     -10.327   4.828  24.650  1.00 22.67           C
ANISOU 4227  CG  ASN A 533     3383   2480   2753    -90    727    202       C
ATOM   4228  OD1 ASN A 533      -9.943   5.400  25.668  1.00 22.97           O
ANISOU 4228  OD1 ASN A 533     3446   2534   2748    -72    716    214       O
ATOM   4229  ND2 ASN A 533      -9.555   4.001  23.950  1.00 22.35           N
ANISOU 4229  ND2 ASN A 533     3325   2425   2742   -110    729    207       N
ATOM   4230  N   SER A 534     -15.019   5.551  24.759  1.00 23.23           N
ANISOU 4230  N   SER A 534     3416   2555   2855    -58    782    161       N
ATOM   4231  CA  SER A 534     -16.297   6.128  24.360  1.00 20.06           C
ANISOU 4231  CA  SER A 534     3006   2155   2462    -54    782    136       C
ATOM   4232  C   SER A 534     -16.584   7.446  25.064  1.00 23.35           C
ANISOU 4232  C   SER A 534     3453   2589   2830    -30    764    127       C
ATOM   4233  O   SER A 534     -17.358   8.255  24.544  1.00 22.61           O
ANISOU 4233  O   SER A 534     3360   2496   2736    -29    750    102       O
ATOM   4234  CB  SER A 534     -17.431   5.151  24.647  1.00 21.70           C
ANISOU 4234  CB  SER A 534     3180   2355   2710    -48    828    150       C
ATOM   4235  OG  SER A 534     -17.561   4.932  26.038  1.00 23.38           O
ANISOU 4235  OG  SER A 534     3401   2582   2903    -23    855    182       O
ATOM   4236  N   ARG A 535     -16.005   7.672  26.246  1.00 18.72           N
ANISOU 4236  N   ARG A 535     2891   2017   2203    -10    765    147       N
ATOM   4237  CA  ARG A 535     -16.225   8.952  26.923  1.00 18.34           C
ANISOU 4237  CA  ARG A 535     2873   1986   2110     13    745    134       C
ATOM   4238  C   ARG A 535     -15.484  10.077  26.213  1.00 22.66           C
ANISOU 4238  C   ARG A 535     3443   2528   2638      1    696    107       C
ATOM   4239  O   ARG A 535     -15.911  11.238  26.272  1.00 22.25           O
ANISOU 4239  O   ARG A 535     3409   2481   2565     13    676     85       O
ATOM   4240  CB  ARG A 535     -15.780   8.870  28.383  1.00 20.63           C
ANISOU 4240  CB  ARG A 535     3182   2296   2360     39    757    159       C
ATOM   4241  CG  ARG A 535     -16.506   7.809  29.201  1.00 24.88           C
ANISOU 4241  CG  ARG A 535     3698   2842   2913     55    808    192       C
ATOM   4242  CD  ARG A 535     -15.655   7.343  30.360  1.00 25.76           C
ANISOU 4242  CD  ARG A 535     3821   2971   2994     71    819    226       C
ATOM   4243  NE  ARG A 535     -16.225   6.178  31.043  1.00 21.02           N
ANISOU 4243  NE  ARG A 535     3195   2375   2415     84    870    264       N
ATOM   4244  CZ  ARG A 535     -17.056   6.241  32.078  1.00 23.31           C
ANISOU 4244  CZ  ARG A 535     3486   2688   2685    114    899    280       C
ATOM   4245  NH1 ARG A 535     -17.426   7.417  32.575  1.00 26.85           N
ANISOU 4245  NH1 ARG A 535     3958   3155   3087    136    881    256       N
ATOM   4246  NH2 ARG A 535     -17.507   5.121  32.629  1.00 29.74           N
ANISOU 4246  NH2 ARG A 535     4273   3503   3524    123    946    319       N
ATOM   4247  N   VAL A 536     -14.365   9.753  25.572  1.00 25.35           N
ANISOU 4247  N   VAL A 536     3784   2859   2988    -22    678    111       N
ATOM   4248  CA  VAL A 536     -13.645  10.740  24.774  1.00 20.73           C
ANISOU 4248  CA  VAL A 536     3216   2269   2392    -36    634     90       C
ATOM   4249  C   VAL A 536     -14.397  11.027  23.481  1.00 23.32           C
ANISOU 4249  C   VAL A 536     3526   2587   2747    -51    625     66       C
ATOM   4250  O   VAL A 536     -14.524  12.192  23.052  1.00 21.11           O
ANISOU 4250  O   VAL A 536     3261   2306   2455    -50    596     45       O
ATOM   4251  CB  VAL A 536     -12.211  10.242  24.516  1.00 21.91           C
ANISOU 4251  CB  VAL A 536     3368   2413   2543    -54    621    104       C
ATOM   4252  CG1 VAL A 536     -11.496  11.113  23.477  1.00 21.72           C
ANISOU 4252  CG1 VAL A 536     3355   2382   2517    -73    579     85       C
ATOM   4253  CG2 VAL A 536     -11.431  10.198  25.825  1.00 18.80           C
ANISOU 4253  CG2 VAL A 536     2996   2033   2115    -36    621    124       C
ATOM   4254  N   LEU A 537     -14.893   9.975  22.827  1.00 22.03           N
ANISOU 4254  N   LEU A 537     3331   2416   2624    -65    651     68       N
ATOM   4255  CA  LEU A 537     -15.653  10.165  21.597  1.00 21.27           C
ANISOU 4255  CA  LEU A 537     3215   2314   2553    -78    643     45       C
ATOM   4256  C   LEU A 537     -16.910  10.988  21.852  1.00 21.31           C
ANISOU 4256  C   LEU A 537     3223   2325   2551    -59    645     31       C
ATOM   4257  O   LEU A 537     -17.306  11.812  21.018  1.00 23.59           O
ANISOU 4257  O   LEU A 537     3510   2613   2840    -63    622     10       O
ATOM   4258  CB  LEU A 537     -16.002   8.811  20.990  1.00 23.41           C
ANISOU 4258  CB  LEU A 537     3450   2577   2870    -94    672     48       C
ATOM   4259  CG  LEU A 537     -14.823   7.904  20.626  1.00 21.98           C
ANISOU 4259  CG  LEU A 537     3261   2387   2702   -113    672     59       C
ATOM   4260  CD1 LEU A 537     -15.349   6.607  20.050  1.00 25.32           C
ANISOU 4260  CD1 LEU A 537     3646   2799   3175   -127    701     56       C
ATOM   4261  CD2 LEU A 537     -13.881   8.549  19.637  1.00 17.13           C
ANISOU 4261  CD2 LEU A 537     2659   1774   2076   -130    634     46       C
ATOM   4262  N   GLU A 538     -17.546  10.794  23.008  1.00 21.33           N
ANISOU 4262  N   GLU A 538     3226   2334   2544    -37    673     43       N
ATOM   4263  CA  GLU A 538     -18.681  11.641  23.351  1.00 22.38           C
ANISOU 4263  CA  GLU A 538     3363   2473   2665    -16    675     30       C
ATOM   4264  C   GLU A 538     -18.282  13.111  23.351  1.00 22.24           C
ANISOU 4264  C   GLU A 538     3377   2457   2614     -8    635     13       C
ATOM   4265  O   GLU A 538     -18.999  13.958  22.809  1.00 21.92           O
ANISOU 4265  O   GLU A 538     3336   2415   2578     -5    621     -7       O
ATOM   4266  CB  GLU A 538     -19.252  11.242  24.711  1.00 16.93           C
ANISOU 4266  CB  GLU A 538     2674   1793   1964     10    711     49       C
ATOM   4267  CG  GLU A 538     -20.321  12.239  25.206  1.00 20.00           C
ANISOU 4267  CG  GLU A 538     3072   2192   2335     35    712     35       C
ATOM   4268  CD  GLU A 538     -20.998  11.808  26.506  1.00 28.08           C
ANISOU 4268  CD  GLU A 538     4092   3229   3348     63    752     54       C
ATOM   4269  OE1 GLU A 538     -20.298  11.456  27.475  1.00 23.93           O
ANISOU 4269  OE1 GLU A 538     3581   2715   2797     74    762     76       O
ATOM   4270  OE2 GLU A 538     -22.241  11.825  26.552  1.00 26.82           O
ANISOU 4270  OE2 GLU A 538     3915   3073   3204     74    773     50       O
ATOM   4271  N   TRP A 539     -17.131  13.432  23.943  1.00 19.25           N
ANISOU 4271  N   TRP A 539     3027   2082   2207     -5    617     21       N
ATOM   4272  CA  TRP A 539     -16.702  14.823  23.962  1.00 24.17           C
ANISOU 4272  CA  TRP A 539     3677   2702   2802      1    578      4       C
ATOM   4273  C   TRP A 539     -16.460  15.341  22.547  1.00 24.97           C
ANISOU 4273  C   TRP A 539     3773   2793   2922    -21    548    -10       C
ATOM   4274  O   TRP A 539     -16.851  16.466  22.220  1.00 21.70           O
ANISOU 4274  O   TRP A 539     3368   2375   2504    -15    525    -27       O
ATOM   4275  CB  TRP A 539     -15.455  14.980  24.834  1.00 21.56           C
ANISOU 4275  CB  TRP A 539     3374   2377   2441      6    563     14       C
ATOM   4276  CG  TRP A 539     -15.028  16.425  24.987  1.00 23.87           C
ANISOU 4276  CG  TRP A 539     3695   2665   2708     14    524     -6       C
ATOM   4277  CD1 TRP A 539     -15.609  17.378  25.782  1.00 25.22           C
ANISOU 4277  CD1 TRP A 539     3883   2841   2856     40    518    -22       C
ATOM   4278  CD2 TRP A 539     -13.946  17.069  24.308  1.00 20.96           C
ANISOU 4278  CD2 TRP A 539     3339   2286   2341     -5    485    -11       C
ATOM   4279  NE1 TRP A 539     -14.944  18.578  25.642  1.00 24.57           N
ANISOU 4279  NE1 TRP A 539     3824   2749   2763     38    478    -39       N
ATOM   4280  CE2 TRP A 539     -13.920  18.412  24.741  1.00 21.40           C
ANISOU 4280  CE2 TRP A 539     3418   2336   2376     10    457    -31       C
ATOM   4281  CE3 TRP A 539     -12.989  16.637  23.376  1.00 19.68           C
ANISOU 4281  CE3 TRP A 539     3167   2115   2194    -32    472     -1       C
ATOM   4282  CZ2 TRP A 539     -12.974  19.331  24.275  1.00 22.53           C
ANISOU 4282  CZ2 TRP A 539     3577   2466   2519     -2    416    -39       C
ATOM   4283  CZ3 TRP A 539     -12.048  17.546  22.916  1.00 21.75           C
ANISOU 4283  CZ3 TRP A 539     3444   2367   2452    -44    433     -7       C
ATOM   4284  CH2 TRP A 539     -12.046  18.882  23.371  1.00 23.01           C
ANISOU 4284  CH2 TRP A 539     3627   2520   2594    -29    406    -25       C
ATOM   4285  N   MET A 540     -15.841  14.523  21.686  1.00 21.65           N
ANISOU 4285  N   MET A 540     3336   2369   2523    -46    548     -2       N
ATOM   4286  CA  MET A 540     -15.616  14.931  20.301  1.00 23.53           C
ANISOU 4286  CA  MET A 540     3566   2600   2775    -66    522    -13       C
ATOM   4287  C   MET A 540     -16.929  15.148  19.565  1.00 19.67           C
ANISOU 4287  C   MET A 540     3056   2113   2306    -64    528    -28       C
ATOM   4288  O   MET A 540     -17.061  16.088  18.775  1.00 24.26           O
ANISOU 4288  O   MET A 540     3640   2693   2887    -67    501    -40       O
ATOM   4289  CB  MET A 540     -14.801  13.867  19.562  1.00 15.75           C
ANISOU 4289  CB  MET A 540     2563   1613   1808    -91    527     -3       C
ATOM   4290  CG  MET A 540     -13.423  13.637  20.115  1.00 15.53           C
ANISOU 4290  CG  MET A 540     2554   1584   1764    -96    519     14       C
ATOM   4291  SD  MET A 540     -12.752  12.187  19.259  1.00 22.16           S
ANISOU 4291  SD  MET A 540     3366   2421   2633   -121    534     24       S
ATOM   4292  CE  MET A 540     -11.097  12.205  19.926  1.00 18.71           C
ANISOU 4292  CE  MET A 540     2953   1982   2173   -125    518     43       C
ATOM   4293  N   PHE A 541     -17.894  14.255  19.788  1.00 15.45           N
ANISOU 4293  N   PHE A 541     2498   1583   1791    -59    562    -27       N
ATOM   4294  CA  PHE A 541     -19.203  14.366  19.156  1.00 17.06           C
ANISOU 4294  CA  PHE A 541     2679   1789   2015    -56    570    -42       C
ATOM   4295  C   PHE A 541     -19.862  15.691  19.526  1.00 23.22           C
ANISOU 4295  C   PHE A 541     3476   2570   2777    -35    555    -52       C
ATOM   4296  O   PHE A 541     -20.379  16.412  18.662  1.00 25.72           O
ANISOU 4296  O   PHE A 541     3786   2887   3101    -36    537    -66       O
ATOM   4297  CB  PHE A 541     -20.052  13.169  19.603  1.00 23.85           C
ANISOU 4297  CB  PHE A 541     3513   2651   2900    -53    612    -35       C
ATOM   4298  CG  PHE A 541     -21.276  12.915  18.772  1.00 23.27           C
ANISOU 4298  CG  PHE A 541     3405   2579   2856    -57    622    -50       C
ATOM   4299  CD1 PHE A 541     -22.363  13.784  18.807  1.00 25.47           C
ANISOU 4299  CD1 PHE A 541     3683   2861   3132    -40    618    -62       C
ATOM   4300  CD2 PHE A 541     -21.370  11.760  18.007  1.00 19.02           C
ANISOU 4300  CD2 PHE A 541     2836   2039   2353    -77    636    -54       C
ATOM   4301  CE1 PHE A 541     -23.508  13.529  18.062  1.00 23.93           C
ANISOU 4301  CE1 PHE A 541     3455   2670   2966    -44    627    -76       C
ATOM   4302  CE2 PHE A 541     -22.516  11.492  17.262  1.00 19.96           C
ANISOU 4302  CE2 PHE A 541     2921   2161   2501    -82    644    -70       C
ATOM   4303  CZ  PHE A 541     -23.585  12.376  17.291  1.00 26.88           C
ANISOU 4303  CZ  PHE A 541     3797   3044   3374    -65    639    -80       C
ATOM   4304  N   GLY A 542     -19.842  16.029  20.815  1.00 23.74           N
ANISOU 4304  N   GLY A 542     3564   2636   2819    -13    563    -48       N
ATOM   4305  CA  GLY A 542     -20.405  17.295  21.246  1.00 25.78           C
ANISOU 4305  CA  GLY A 542     3840   2893   3060      9    550    -61       C
ATOM   4306  C   GLY A 542     -19.677  18.489  20.659  1.00 24.29           C
ANISOU 4306  C   GLY A 542     3671   2696   2862      3    507    -69       C
ATOM   4307  O   GLY A 542     -20.298  19.500  20.322  1.00 28.80           O
ANISOU 4307  O   GLY A 542     4244   3262   3435     12    491    -82       O
ATOM   4308  N   ARG A 543     -18.347  18.400  20.549  1.00 25.30           N
ANISOU 4308  N   ARG A 543     3813   2820   2980    -13    489    -60       N
ATOM   4309  CA  ARG A 543     -17.587  19.513  19.990  1.00 24.47           C
ANISOU 4309  CA  ARG A 543     3724   2704   2869    -20    449    -65       C
ATOM   4310  C   ARG A 543     -17.906  19.711  18.516  1.00 27.79           C
ANISOU 4310  C   ARG A 543     4123   3124   3311    -35    435    -68       C
ATOM   4311  O   ARG A 543     -17.935  20.850  18.026  1.00 26.83           O
ANISOU 4311  O   ARG A 543     4010   2995   3191    -33    408    -73       O
ATOM   4312  CB  ARG A 543     -16.088  19.292  20.186  1.00 17.51           C
ANISOU 4312  CB  ARG A 543     2859   1819   1975    -34    434    -53       C
ATOM   4313  CG  ARG A 543     -15.616  19.369  21.634  1.00 24.06           C
ANISOU 4313  CG  ARG A 543     3713   2651   2778    -17    438    -52       C
ATOM   4314  CD  ARG A 543     -15.187  20.787  22.027  1.00 42.67           C
ANISOU 4314  CD  ARG A 543     6097   4996   5119     -6    404    -66       C
ATOM   4315  NE  ARG A 543     -16.206  21.774  21.715  1.00 50.55           N
ANISOU 4315  NE  ARG A 543     7093   5986   6126      7    396    -82       N
ATOM   4316  CZ  ARG A 543     -16.038  22.823  20.916  1.00 50.78           C
ANISOU 4316  CZ  ARG A 543     7126   6001   6168      0    365    -87       C
ATOM   4317  NH1 ARG A 543     -14.867  23.066  20.341  1.00 49.30           N
ANISOU 4317  NH1 ARG A 543     6944   5804   5984    -20    338    -78       N
ATOM   4318  NH2 ARG A 543     -17.056  23.642  20.706  1.00 50.42           N
ANISOU 4318  NH2 ARG A 543     7076   5949   6131     15    362   -100       N
ATOM   4319  N   ILE A 544     -18.129  18.616  17.788  1.00 26.02           N
ANISOU 4319  N   ILE A 544     3872   2909   3105    -51    453    -64       N
ATOM   4320  CA  ILE A 544     -18.536  18.736  16.393  1.00 29.49           C
ANISOU 4320  CA  ILE A 544     4289   3354   3562    -63    442    -69       C
ATOM   4321  C   ILE A 544     -19.888  19.432  16.300  1.00 28.25           C
ANISOU 4321  C   ILE A 544     4122   3198   3412    -46    443    -81       C
ATOM   4322  O   ILE A 544     -20.134  20.212  15.370  1.00 30.13           O
ANISOU 4322  O   ILE A 544     4354   3438   3655    -47    421    -84       O
ATOM   4323  CB  ILE A 544     -18.544  17.339  15.728  1.00 24.92           C
ANISOU 4323  CB  ILE A 544     3682   2786   3002    -82    462    -68       C
ATOM   4324  CG1 ILE A 544     -17.116  16.816  15.581  1.00 22.55           C
ANISOU 4324  CG1 ILE A 544     3389   2484   2696   -101    455    -55       C
ATOM   4325  CG2 ILE A 544     -19.235  17.371  14.378  1.00 19.83           C
ANISOU 4325  CG2 ILE A 544     3009   2152   2373    -91    454    -78       C
ATOM   4326  CD1 ILE A 544     -17.049  15.301  15.308  1.00 26.32           C
ANISOU 4326  CD1 ILE A 544     3842   2967   3193   -116    481    -54       C
ATOM   4327  N   GLU A 545     -20.769  19.191  17.271  1.00 23.40           N
ANISOU 4327  N   GLU A 545     3508   2586   2798    -27    469    -86       N
ATOM   4328  CA  GLU A 545     -22.091  19.810  17.292  1.00 27.35           C
ANISOU 4328  CA  GLU A 545     3998   3087   3306     -8    474    -97       C
ATOM   4329  C   GLU A 545     -22.072  21.264  17.732  1.00 30.15           C
ANISOU 4329  C   GLU A 545     4380   3430   3647     10    451   -103       C
ATOM   4330  O   GLU A 545     -23.090  21.941  17.573  1.00 28.66           O
ANISOU 4330  O   GLU A 545     4183   3241   3466     25    449   -112       O
ATOM   4331  CB  GLU A 545     -23.038  19.045  18.219  1.00 27.07           C
ANISOU 4331  CB  GLU A 545     3951   3057   3276      6    513    -98       C
ATOM   4332  CG  GLU A 545     -23.409  17.666  17.690  1.00 24.89           C
ANISOU 4332  CG  GLU A 545     3642   2790   3026    -11    538    -96       C
ATOM   4333  CD  GLU A 545     -24.664  17.138  18.339  1.00 33.31           C
ANISOU 4333  CD  GLU A 545     4689   3861   4107      5    573    -98       C
ATOM   4334  OE1 GLU A 545     -24.916  17.479  19.520  1.00 33.75           O
ANISOU 4334  OE1 GLU A 545     4763   3915   4146     28    587    -95       O
ATOM   4335  OE2 GLU A 545     -25.415  16.418  17.647  1.00 30.19           O
ANISOU 4335  OE2 GLU A 545     4260   3471   3739     -5    587   -104       O
ATOM   4336  N   GLY A 546     -20.963  21.747  18.284  1.00 28.71           N
ANISOU 4336  N   GLY A 546     4227   3238   3446     10    433    -99       N
ATOM   4337  CA  GLY A 546     -20.855  23.120  18.726  1.00 31.16           C
ANISOU 4337  CA  GLY A 546     4560   3532   3746     27    409   -108       C
ATOM   4338  C   GLY A 546     -21.033  23.335  20.209  1.00 34.28           C
ANISOU 4338  C   GLY A 546     4978   3926   4121     51    422   -118       C
ATOM   4339  O   GLY A 546     -21.216  24.483  20.628  1.00 34.46           O
ANISOU 4339  O   GLY A 546     5018   3937   4139     69    406   -131       O
ATOM   4340  N   GLU A 547     -20.982  22.275  21.012  1.00 26.13           N
ANISOU 4340  N   GLU A 547     3943   2906   3078     53    451   -111       N
ATOM   4341  CA  GLU A 547     -21.221  22.377  22.441  1.00 30.73           C
ANISOU 4341  CA  GLU A 547     4545   3494   3638     79    468   -119       C
ATOM   4342  C   GLU A 547     -20.089  23.113  23.140  1.00 34.44           C
ANISOU 4342  C   GLU A 547     5046   3954   4083     84    441   -125       C
ATOM   4343  O   GLU A 547     -18.919  23.008  22.771  1.00 30.68           O
ANISOU 4343  O   GLU A 547     4578   3473   3607     63    421   -116       O
ATOM   4344  CB  GLU A 547     -21.393  20.987  23.055  1.00 36.06           C
ANISOU 4344  CB  GLU A 547     5207   4185   4309     80    507   -104       C
ATOM   4345  CG  GLU A 547     -22.799  20.447  22.911  1.00 53.02           C
ANISOU 4345  CG  GLU A 547     7326   6343   6477     88    539   -104       C
ATOM   4346  CD  GLU A 547     -22.953  19.067  23.505  1.00 66.29           C
ANISOU 4346  CD  GLU A 547     8992   8036   8159     87    579    -87       C
ATOM   4347  OE1 GLU A 547     -23.653  18.230  22.895  1.00 70.85           O
ANISOU 4347  OE1 GLU A 547     9538   8616   8765     76    600    -81       O
ATOM   4348  OE2 GLU A 547     -22.365  18.822  24.579  1.00 71.19           O
ANISOU 4348  OE2 GLU A 547     9631   8664   8754     98    588    -78       O
ATOM   4349  N   ASP A 548     -20.455  23.867  24.175  1.00 34.68           N
ANISOU 4349  N   ASP A 548     5096   3985   4096    112    441   -142       N
ATOM   4350  CA  ASP A 548     -19.507  24.734  24.867  1.00 37.84           C
ANISOU 4350  CA  ASP A 548     5527   4376   4476    119    412   -156       C
ATOM   4351  C   ASP A 548     -18.797  23.941  25.965  1.00 37.09           C
ANISOU 4351  C   ASP A 548     5444   4298   4350    124    426   -148       C
ATOM   4352  O   ASP A 548     -18.925  24.200  27.163  1.00 43.36           O
ANISOU 4352  O   ASP A 548     6256   5103   5116    150    433   -162       O
ATOM   4353  CB  ASP A 548     -20.223  25.958  25.417  1.00 42.27           C
ANISOU 4353  CB  ASP A 548     6101   4927   5032    148    403   -183       C
ATOM   4354  CG  ASP A 548     -19.361  27.176  25.375  1.00 62.31           C
ANISOU 4354  CG  ASP A 548     8660   7441   7572    145    361   -198       C
ATOM   4355  OD1 ASP A 548     -19.813  28.227  24.875  1.00 71.00           O
ANISOU 4355  OD1 ASP A 548     9761   8523   8695    150    342   -211       O
ATOM   4356  OD2 ASP A 548     -18.205  27.064  25.819  1.00 69.55           O
ANISOU 4356  OD2 ASP A 548     9594   8359   8473    137    345   -197       O
ATOM   4357  N   SER A 549     -18.018  22.953  25.518  1.00 30.98           N
ANISOU 4357  N   SER A 549     4661   3528   3581     99    431   -126       N
ATOM   4358  CA  SER A 549     -17.381  21.990  26.402  1.00 30.87           C
ANISOU 4358  CA  SER A 549     4653   3533   3544    101    448   -111       C
ATOM   4359  C   SER A 549     -15.862  22.092  26.397  1.00 31.84           C
ANISOU 4359  C   SER A 549     4791   3649   3658     84    418   -106       C
ATOM   4360  O   SER A 549     -15.192  21.222  26.967  1.00 29.55           O
ANISOU 4360  O   SER A 549     4504   3373   3352     81    431    -90       O
ATOM   4361  CB  SER A 549     -17.796  20.575  25.994  1.00 28.16           C
ANISOU 4361  CB  SER A 549     4281   3199   3218     88    485    -87       C
ATOM   4362  OG  SER A 549     -17.578  20.407  24.603  1.00 24.86           O
ANISOU 4362  OG  SER A 549     3846   2769   2831     60    472    -81       O
ATOM   4363  N   ALA A 550     -15.298  23.112  25.757  1.00 27.38           N
ANISOU 4363  N   ALA A 550     4236   3063   3105     72    380   -118       N
ATOM   4364  CA  ALA A 550     -13.860  23.193  25.550  1.00 28.32           C
ANISOU 4364  CA  ALA A 550     4364   3173   3222     51    351   -110       C
ATOM   4365  C   ALA A 550     -13.283  24.412  26.244  1.00 30.71           C
ANISOU 4365  C   ALA A 550     4693   3464   3510     63    317   -134       C
ATOM   4366  O   ALA A 550     -13.936  25.456  26.356  1.00 23.72           O
ANISOU 4366  O   ALA A 550     3816   2567   2630     80    306   -157       O
ATOM   4367  CB  ALA A 550     -13.503  23.258  24.053  1.00 28.10           C
ANISOU 4367  CB  ALA A 550     4322   3130   3227     22    335    -98       C
ATOM   4368  N   LYS A 551     -12.045  24.279  26.700  1.00 27.68           N
ANISOU 4368  N   LYS A 551     4323   3083   3112     55    299   -130       N
ATOM   4369  CA  LYS A 551     -11.295  25.426  27.173  1.00 28.42           C
ANISOU 4369  CA  LYS A 551     4439   3162   3199     60    260   -153       C
ATOM   4370  C   LYS A 551      -9.973  25.495  26.424  1.00 30.12           C
ANISOU 4370  C   LYS A 551     4651   3361   3431     30    231   -138       C
ATOM   4371  O   LYS A 551      -9.401  24.469  26.015  1.00 24.59           O
ANISOU 4371  O   LYS A 551     3939   2671   2734     11    244   -112       O
ATOM   4372  CB  LYS A 551     -11.082  25.382  28.693  1.00 31.77           C
ANISOU 4372  CB  LYS A 551     4881   3607   3581     86    262   -169       C
ATOM   4373  CG  LYS A 551      -9.839  24.691  29.185  1.00 37.40           C
ANISOU 4373  CG  LYS A 551     5600   4335   4274     76    256   -153       C
ATOM   4374  CD  LYS A 551      -9.876  24.578  30.712  1.00 36.83           C
ANISOU 4374  CD  LYS A 551     5545   4292   4157    107    264   -168       C
ATOM   4375  CE  LYS A 551      -8.788  23.645  31.237  1.00 45.18           C
ANISOU 4375  CE  LYS A 551     6603   5370   5192    101    266   -145       C
ATOM   4376  NZ  LYS A 551      -9.055  23.169  32.627  1.00 51.04           N
ANISOU 4376  NZ  LYS A 551     7355   6150   5888    133    287   -147       N
ATOM   4377  N   LEU A 552      -9.511  26.724  26.220  1.00 22.49           N
ANISOU 4377  N   LEU A 552     3695   2369   2481     25    194   -155       N
ATOM   4378  CA  LEU A 552      -8.347  26.965  25.385  1.00 24.97           C
ANISOU 4378  CA  LEU A 552     4004   2664   2818     -3    166   -140       C
ATOM   4379  C   LEU A 552      -7.071  26.750  26.188  1.00 24.68           C
ANISOU 4379  C   LEU A 552     3981   2636   2762     -8    148   -141       C
ATOM   4380  O   LEU A 552      -6.973  27.191  27.336  1.00 29.30           O
ANISOU 4380  O   LEU A 552     4583   3226   3323     13    136   -166       O
ATOM   4381  CB  LEU A 552      -8.403  28.390  24.835  1.00 29.99           C
ANISOU 4381  CB  LEU A 552     4644   3268   3485     -6    134   -155       C
ATOM   4382  CG  LEU A 552      -7.251  28.839  23.942  1.00 23.95           C
ANISOU 4382  CG  LEU A 552     3873   2480   2748    -35    103   -138       C
ATOM   4383  CD1 LEU A 552      -7.168  27.965  22.696  1.00 25.79           C
ANISOU 4383  CD1 LEU A 552     4083   2722   2994    -58    121   -104       C
ATOM   4384  CD2 LEU A 552      -7.407  30.325  23.561  1.00 26.83           C
ANISOU 4384  CD2 LEU A 552     4241   2810   3145    -33     73   -153       C
ATOM   4385  N   THR A 553      -6.110  26.047  25.601  1.00 24.51           N
ANISOU 4385  N   THR A 553     3948   2616   2747    -33    146   -113       N
ATOM   4386  CA  THR A 553      -4.790  25.841  26.179  1.00 19.33           C
ANISOU 4386  CA  THR A 553     3300   1966   2078    -41    127   -109       C
ATOM   4387  C   THR A 553      -3.772  26.121  25.090  1.00 19.50           C
ANISOU 4387  C   THR A 553     3311   1966   2132    -71    103    -91       C
ATOM   4388  O   THR A 553      -4.134  26.290  23.923  1.00 24.19           O
ANISOU 4388  O   THR A 553     3891   2547   2752    -84    107    -78       O
ATOM   4389  CB  THR A 553      -4.610  24.407  26.711  1.00 21.26           C
ANISOU 4389  CB  THR A 553     3540   2241   2296    -37    158    -89       C
ATOM   4390  OG1 THR A 553      -4.372  23.521  25.614  1.00 19.25           O
ANISOU 4390  OG1 THR A 553     3265   1987   2062    -61    174    -58       O
ATOM   4391  CG2 THR A 553      -5.817  23.959  27.500  1.00 21.30           C
ANISOU 4391  CG2 THR A 553     3548   2268   2276     -9    191    -97       C
ATOM   4392  N   PRO A 554      -2.483  26.208  25.438  1.00 21.17           N
ANISOU 4392  N   PRO A 554     3528   2175   2341    -82     77    -88       N
ATOM   4393  CA  PRO A 554      -1.473  26.460  24.401  1.00 23.47           C
ANISOU 4393  CA  PRO A 554     3807   2447   2664   -111     56    -68       C
ATOM   4394  C   PRO A 554      -1.387  25.381  23.325  1.00 29.32           C
ANISOU 4394  C   PRO A 554     4527   3199   3414   -130     82    -34       C
ATOM   4395  O   PRO A 554      -0.910  25.688  22.228  1.00 24.23           O
ANISOU 4395  O   PRO A 554     3870   2539   2797   -151     70    -16       O
ATOM   4396  CB  PRO A 554      -0.163  26.562  25.197  1.00 25.89           C
ANISOU 4396  CB  PRO A 554     4122   2754   2960   -116     27    -72       C
ATOM   4397  CG  PRO A 554      -0.586  26.985  26.574  1.00 27.14           C
ANISOU 4397  CG  PRO A 554     4301   2922   3089    -88     20   -108       C
ATOM   4398  CD  PRO A 554      -1.913  26.310  26.800  1.00 21.83           C
ANISOU 4398  CD  PRO A 554     3628   2270   2394    -67     61   -108       C
ATOM   4399  N   ILE A 555      -1.836  24.144  23.581  1.00 23.02           N
ANISOU 4399  N   ILE A 555     3724   2427   2596   -123    117    -23       N
ATOM   4400  CA  ILE A 555      -1.747  23.076  22.582  1.00 21.59           C
ANISOU 4400  CA  ILE A 555     3522   2255   2426   -140    142      4       C
ATOM   4401  C   ILE A 555      -3.048  22.886  21.811  1.00 22.06           C
ANISOU 4401  C   ILE A 555     3569   2318   2496   -136    168      4       C
ATOM   4402  O   ILE A 555      -3.094  22.066  20.880  1.00 21.73           O
ANISOU 4402  O   ILE A 555     3509   2284   2465   -150    187     22       O
ATOM   4403  CB  ILE A 555      -1.326  21.734  23.220  1.00 17.87           C
ANISOU 4403  CB  ILE A 555     3048   1808   1935   -138    166     19       C
ATOM   4404  CG1 ILE A 555      -2.417  21.206  24.165  1.00 21.86           C
ANISOU 4404  CG1 ILE A 555     3559   2330   2415   -112    196      9       C
ATOM   4405  CG2 ILE A 555      -0.005  21.873  23.981  1.00 19.12           C
ANISOU 4405  CG2 ILE A 555     3216   1966   2082   -142    140     21       C
ATOM   4406  CD1 ILE A 555      -2.178  19.743  24.612  1.00 20.29           C
ANISOU 4406  CD1 ILE A 555     3352   2153   2203   -111    227     31       C
ATOM   4407  N   GLY A 556      -4.111  23.612  22.177  1.00 22.04           N
ANISOU 4407  N   GLY A 556     3576   2310   2489   -117    168    -18       N
ATOM   4408  CA  GLY A 556      -5.428  23.532  21.575  1.00 17.93           C
ANISOU 4408  CA  GLY A 556     3044   1792   1977   -110    190    -21       C
ATOM   4409  C   GLY A 556      -6.503  23.461  22.648  1.00 22.26           C
ANISOU 4409  C   GLY A 556     3603   2351   2504    -82    210    -41       C
ATOM   4410  O   GLY A 556      -6.255  23.706  23.832  1.00 24.58           O
ANISOU 4410  O   GLY A 556     3914   2648   2775    -67    202    -55       O
ATOM   4411  N   TYR A 557      -7.718  23.102  22.236  1.00 22.18           N
ANISOU 4411  N   TYR A 557     3580   2348   2500    -75    237    -42       N
ATOM   4412  CA  TYR A 557      -8.833  22.998  23.171  1.00 23.66           C
ANISOU 4412  CA  TYR A 557     3773   2547   2670    -49    259    -57       C
ATOM   4413  C   TYR A 557      -8.821  21.655  23.886  1.00 23.72           C
ANISOU 4413  C   TYR A 557     3777   2577   2660    -43    292    -44       C
ATOM   4414  O   TYR A 557      -8.595  20.615  23.269  1.00 23.34           O
ANISOU 4414  O   TYR A 557     3711   2535   2622    -60    310    -24       O
ATOM   4415  CB  TYR A 557     -10.169  23.165  22.445  1.00 24.05           C
ANISOU 4415  CB  TYR A 557     3808   2594   2735    -43    275    -62       C
ATOM   4416  CG  TYR A 557     -10.364  24.550  21.869  1.00 29.18           C
ANISOU 4416  CG  TYR A 557     4462   3222   3403    -43    246    -74       C
ATOM   4417  CD1 TYR A 557     -10.292  24.763  20.504  1.00 33.70           C
ANISOU 4417  CD1 TYR A 557     5019   3786   4001    -62    236    -61       C
ATOM   4418  CD2 TYR A 557     -10.607  25.644  22.696  1.00 33.97           C
ANISOU 4418  CD2 TYR A 557     5089   3816   4003    -23    228    -99       C
ATOM   4419  CE1 TYR A 557     -10.461  26.019  19.967  1.00 37.26           C
ANISOU 4419  CE1 TYR A 557     5471   4216   4469    -61    210    -67       C
ATOM   4420  CE2 TYR A 557     -10.779  26.912  22.166  1.00 33.92           C
ANISOU 4420  CE2 TYR A 557     5085   3787   4018    -22    202   -108       C
ATOM   4421  CZ  TYR A 557     -10.702  27.087  20.796  1.00 39.29           C
ANISOU 4421  CZ  TYR A 557     5747   4457   4723    -42    194    -90       C
ATOM   4422  OH  TYR A 557     -10.870  28.337  20.237  1.00 44.21           O
ANISOU 4422  OH  TYR A 557     6371   5057   5371    -41    169    -94       O
ATOM   4423  N   VAL A 558      -9.078  21.687  25.188  1.00 22.39           N
ANISOU 4423  N   VAL A 558     3624   2421   2463    -19    300    -55       N
ATOM   4424  CA  VAL A 558      -9.222  20.482  26.002  1.00 21.70           C
ANISOU 4424  CA  VAL A 558     3531   2356   2356     -8    334    -40       C
ATOM   4425  C   VAL A 558     -10.609  20.524  26.633  1.00 24.95           C
ANISOU 4425  C   VAL A 558     3943   2779   2757     19    361    -52       C
ATOM   4426  O   VAL A 558     -11.266  21.578  26.636  1.00 23.92           O
ANISOU 4426  O   VAL A 558     3821   2639   2628     32    348    -75       O
ATOM   4427  CB  VAL A 558      -8.120  20.383  27.083  1.00 20.21           C
ANISOU 4427  CB  VAL A 558     3360   2180   2139     -1    321    -37       C
ATOM   4428  CG1 VAL A 558      -6.739  20.331  26.464  1.00 21.08           C
ANISOU 4428  CG1 VAL A 558     3468   2279   2262    -28    295    -24       C
ATOM   4429  CG2 VAL A 558      -8.247  21.543  28.085  1.00 23.96           C
ANISOU 4429  CG2 VAL A 558     3860   2656   2589     23    298    -67       C
ATOM   4430  N   PRO A 559     -11.095  19.400  27.168  1.00 23.68           N
ANISOU 4430  N   PRO A 559     3771   2637   2588     29    400    -36       N
ATOM   4431  CA  PRO A 559     -12.396  19.429  27.851  1.00 21.95           C
ANISOU 4431  CA  PRO A 559     3552   2432   2358     57    427    -45       C
ATOM   4432  C   PRO A 559     -12.395  20.400  29.022  1.00 25.43           C
ANISOU 4432  C   PRO A 559     4018   2881   2763     85    411    -68       C
ATOM   4433  O   PRO A 559     -11.445  20.453  29.810  1.00 24.26           O
ANISOU 4433  O   PRO A 559     3887   2743   2589     90    395    -69       O
ATOM   4434  CB  PRO A 559     -12.583  17.982  28.325  1.00 22.14           C
ANISOU 4434  CB  PRO A 559     3560   2474   2379     61    469    -16       C
ATOM   4435  CG  PRO A 559     -11.815  17.188  27.357  1.00 21.97           C
ANISOU 4435  CG  PRO A 559     3522   2442   2383     30    468      3       C
ATOM   4436  CD  PRO A 559     -10.604  18.018  27.018  1.00 25.35           C
ANISOU 4436  CD  PRO A 559     3967   2858   2808     15    423     -6       C
ATOM   4437  N   LYS A 560     -13.468  21.184  29.119  1.00 27.31           N
ANISOU 4437  N   LYS A 560     4259   3115   3002    103    413    -91       N
ATOM   4438  CA  LYS A 560     -13.736  21.926  30.342  1.00 24.77           C
ANISOU 4438  CA  LYS A 560     3959   2807   2645    136    408   -115       C
ATOM   4439  C   LYS A 560     -13.707  20.987  31.533  1.00 34.33           C
ANISOU 4439  C   LYS A 560     5172   4052   3822    156    439    -97       C
ATOM   4440  O   LYS A 560     -13.975  19.791  31.410  1.00 33.56           O
ANISOU 4440  O   LYS A 560     5054   3964   3734    150    474    -67       O
ATOM   4441  CB  LYS A 560     -15.109  22.590  30.286  1.00 30.36           C
ANISOU 4441  CB  LYS A 560     4663   3510   3361    155    420   -135       C
ATOM   4442  CG  LYS A 560     -15.157  23.828  29.442  1.00 31.30           C
ANISOU 4442  CG  LYS A 560     4787   3599   3507    145    385   -158       C
ATOM   4443  CD  LYS A 560     -16.525  24.464  29.536  1.00 31.09           C
ANISOU 4443  CD  LYS A 560     4758   3570   3486    169    398   -177       C
ATOM   4444  CE  LYS A 560     -16.531  25.773  28.776  1.00 36.84           C
ANISOU 4444  CE  LYS A 560     5491   4267   4239    162    362   -199       C
ATOM   4445  NZ  LYS A 560     -17.845  26.472  28.852  1.00 36.24           N
ANISOU 4445  NZ  LYS A 560     5412   4186   4171    186    373   -219       N
ATOM   4446  N   GLU A 561     -13.397  21.537  32.701  1.00 38.09           N
ANISOU 4446  N   GLU A 561     5670   4545   4257    182    425   -116       N
ATOM   4447  CA  GLU A 561     -13.540  20.750  33.912  1.00 41.39           C
ANISOU 4447  CA  GLU A 561     6089   5000   4637    207    457   -100       C
ATOM   4448  C   GLU A 561     -14.988  20.289  34.019  1.00 36.97           C
ANISOU 4448  C   GLU A 561     5513   4451   4084    225    502    -90       C
ATOM   4449  O   GLU A 561     -15.918  21.076  33.812  1.00 36.31           O
ANISOU 4449  O   GLU A 561     5429   4356   4010    236    501   -114       O
ATOM   4450  CB  GLU A 561     -13.103  21.565  35.129  1.00 54.48           C
ANISOU 4450  CB  GLU A 561     7774   6678   6248    236    433   -129       C
ATOM   4451  CG  GLU A 561     -11.656  22.063  35.006  1.00 69.85           C
ANISOU 4451  CG  GLU A 561     9736   8612   8193    217    385   -140       C
ATOM   4452  CD  GLU A 561     -11.040  22.480  36.332  1.00 81.18           C
ANISOU 4452  CD  GLU A 561    11193  10075   9576    243    365   -162       C
ATOM   4453  OE1 GLU A 561     -11.707  22.318  37.377  1.00 84.68           O
ANISOU 4453  OE1 GLU A 561    11641  10552   9981    278    391   -165       O
ATOM   4454  OE2 GLU A 561      -9.884  22.965  36.326  1.00 83.30           O
ANISOU 4454  OE2 GLU A 561    11474  10334   9842    230    324   -175       O
ATOM   4455  N   ASP A 562     -15.168  18.987  34.242  1.00 35.88           N
ANISOU 4455  N   ASP A 562     5356   4330   3946    225    542    -52       N
ATOM   4456  CA  ASP A 562     -16.451  18.288  34.315  1.00 40.06           C
ANISOU 4456  CA  ASP A 562     5863   4868   4488    238    590    -34       C
ATOM   4457  C   ASP A 562     -17.132  18.092  32.961  1.00 37.29           C
ANISOU 4457  C   ASP A 562     5488   4489   4191    211    598    -31       C
ATOM   4458  O   ASP A 562     -18.236  17.548  32.925  1.00 36.38           O
ANISOU 4458  O   ASP A 562     5352   4379   4093    219    635    -18       O
ATOM   4459  CB  ASP A 562     -17.450  18.978  35.259  1.00 46.66           C
ANISOU 4459  CB  ASP A 562     6709   5726   5294    277    604    -55       C
ATOM   4460  CG  ASP A 562     -16.847  19.303  36.615  1.00 57.84           C
ANISOU 4460  CG  ASP A 562     8151   7175   6652    307    593    -65       C
ATOM   4461  OD1 ASP A 562     -16.770  20.506  36.963  1.00 63.35           O
ANISOU 4461  OD1 ASP A 562     8870   7872   7328    322    562   -106       O
ATOM   4462  OD2 ASP A 562     -16.441  18.358  37.325  1.00 55.82           O
ANISOU 4462  OD2 ASP A 562     7891   6946   6373    315    616    -33       O
ATOM   4463  N   ALA A 563     -16.518  18.501  31.844  1.00 32.71           N
ANISOU 4463  N   ALA A 563     4909   3881   3639    181    563    -42       N
ATOM   4464  CA  ALA A 563     -17.166  18.289  30.551  1.00 29.06           C
ANISOU 4464  CA  ALA A 563     4422   3396   3223    158    570    -39       C
ATOM   4465  C   ALA A 563     -17.130  16.823  30.127  1.00 29.74           C
ANISOU 4465  C   ALA A 563     4482   3483   3336    139    602     -6       C
ATOM   4466  O   ALA A 563     -18.013  16.369  29.390  1.00 27.65           O
ANISOU 4466  O   ALA A 563     4191   3210   3106    129    623     -1       O
ATOM   4467  CB  ALA A 563     -16.510  19.165  29.482  1.00 27.69           C
ANISOU 4467  CB  ALA A 563     4257   3196   3068    134    525    -58       C
ATOM   4468  N   LEU A 564     -16.129  16.074  30.579  1.00 22.82           N
ANISOU 4468  N   LEU A 564     3609   2616   2447    134    605     17       N
ATOM   4469  CA  LEU A 564     -15.999  14.661  30.241  1.00 30.50           C
ANISOU 4469  CA  LEU A 564     4556   3587   3447    116    635     50       C
ATOM   4470  C   LEU A 564     -16.848  13.821  31.189  1.00 30.50           C
ANISOU 4470  C   LEU A 564     4541   3607   3440    140    683     74       C
ATOM   4471  O   LEU A 564     -16.776  13.997  32.409  1.00 33.74           O
ANISOU 4471  O   LEU A 564     4968   4042   3809    169    691     79       O
ATOM   4472  CB  LEU A 564     -14.531  14.255  30.340  1.00 34.18           C
ANISOU 4472  CB  LEU A 564     5031   4053   3902    102    617     65       C
ATOM   4473  CG  LEU A 564     -13.883  13.403  29.258  1.00 41.23           C
ANISOU 4473  CG  LEU A 564     5905   4928   4834     68    616     80       C
ATOM   4474  CD1 LEU A 564     -14.264  13.921  27.905  1.00 35.55           C
ANISOU 4474  CD1 LEU A 564     5176   4187   4145     47    597     58       C
ATOM   4475  CD2 LEU A 564     -12.384  13.448  29.448  1.00 38.14           C
ANISOU 4475  CD2 LEU A 564     5530   4537   4423     59    588     87       C
ATOM   4476  N   ASN A 565     -17.665  12.923  30.634  1.00 24.34           N
ANISOU 4476  N   ASN A 565     3730   2818   2702    129    716     88       N
ATOM   4477  CA  ASN A 565     -18.425  11.974  31.450  1.00 31.34           C
ANISOU 4477  CA  ASN A 565     4597   3720   3592    148    766    118       C
ATOM   4478  C   ASN A 565     -17.447  11.015  32.111  1.00 32.64           C
ANISOU 4478  C   ASN A 565     4761   3895   3744    149    779    153       C
ATOM   4479  O   ASN A 565     -16.898  10.119  31.465  1.00 28.93           O
ANISOU 4479  O   ASN A 565     4275   3409   3309    123    784    170       O
ATOM   4480  CB  ASN A 565     -19.440  11.227  30.591  1.00 35.32           C
ANISOU 4480  CB  ASN A 565     5063   4206   4150    132    794    123       C
ATOM   4481  CG  ASN A 565     -20.416  10.392  31.407  1.00 41.46           C
ANISOU 4481  CG  ASN A 565     5819   4997   4937    152    846    152       C
ATOM   4482  OD1 ASN A 565     -20.148  10.030  32.550  1.00 34.83           O
ANISOU 4482  OD1 ASN A 565     4987   4181   4067    175    867    179       O
ATOM   4483  ND2 ASN A 565     -21.556  10.071  30.807  1.00 47.62           N
ANISOU 4483  ND2 ASN A 565     6569   5765   5760    145    868    148       N
ATOM   4484  N   LEU A 566     -17.207  11.211  33.406  1.00 28.25           N
ANISOU 4484  N   LEU A 566     4225   3369   3140    179    785    164       N
ATOM   4485  CA  LEU A 566     -16.343  10.329  34.179  1.00 24.77           C
ANISOU 4485  CA  LEU A 566     3784   2945   2682    185    800    202       C
ATOM   4486  C   LEU A 566     -17.117   9.591  35.270  1.00 35.16           C
ANISOU 4486  C   LEU A 566     5085   4286   3987    215    851    237       C
ATOM   4487  O   LEU A 566     -16.517   9.133  36.247  1.00 35.13           O
ANISOU 4487  O   LEU A 566     5088   4307   3952    232    862    267       O
ATOM   4488  CB  LEU A 566     -15.183  11.113  34.793  1.00 30.19           C
ANISOU 4488  CB  LEU A 566     4506   3649   3318    195    760    188       C
ATOM   4489  CG  LEU A 566     -14.230  11.794  33.811  1.00 34.45           C
ANISOU 4489  CG  LEU A 566     5059   4164   3867    166    710    160       C
ATOM   4490  CD1 LEU A 566     -13.167  12.581  34.548  1.00 38.11           C
ANISOU 4490  CD1 LEU A 566     5554   4645   4280    178    673    146       C
ATOM   4491  CD2 LEU A 566     -13.592  10.755  32.908  1.00 38.47           C
ANISOU 4491  CD2 LEU A 566     5547   4650   4420    133    716    182       C
ATOM   4492  N   LYS A 567     -18.436   9.462  35.122  1.00 35.15           N
ANISOU 4492  N   LYS A 567     5064   4281   4013    221    881    237       N
ATOM   4493  CA  LYS A 567     -19.219   8.728  36.112  1.00 39.23           C
ANISOU 4493  CA  LYS A 567     5562   4819   4523    249    933    274       C
ATOM   4494  C   LYS A 567     -18.796   7.264  36.139  1.00 37.66           C
ANISOU 4494  C   LYS A 567     5337   4613   4360    236    965    323       C
ATOM   4495  O   LYS A 567     -18.601   6.633  35.096  1.00 38.91           O
ANISOU 4495  O   LYS A 567     5474   4737   4571    203    963    323       O
ATOM   4496  CB  LYS A 567     -20.722   8.849  35.821  1.00 46.49           C
ANISOU 4496  CB  LYS A 567     6460   5732   5473    254    959    264       C
ATOM   4497  CG  LYS A 567     -21.218   8.098  34.574  1.00 61.51           C
ANISOU 4497  CG  LYS A 567     8327   7596   7448    219    972    265       C
ATOM   4498  CD  LYS A 567     -21.870   6.750  34.888  1.00 68.01           C
ANISOU 4498  CD  LYS A 567     9111   8417   8313    222   1028    311       C
ATOM   4499  CE  LYS A 567     -22.260   6.015  33.608  1.00 69.84           C
ANISOU 4499  CE  LYS A 567     9308   8610   8618    186   1034    305       C
ATOM   4500  NZ  LYS A 567     -23.011   4.757  33.895  1.00 70.43           N
ANISOU 4500  NZ  LYS A 567     9342   8677   8741    188   1089    346       N
ATOM   4501  N   GLY A 568     -18.633   6.733  37.348  1.00 34.74           N
ANISOU 4501  N   GLY A 568     4967   4274   3957    264    994    363       N
ATOM   4502  CA  GLY A 568     -18.278   5.346  37.541  1.00 45.91           C
ANISOU 4502  CA  GLY A 568     6356   5683   5404    258   1029    415       C
ATOM   4503  C   GLY A 568     -16.819   5.024  37.347  1.00 51.36           C
ANISOU 4503  C   GLY A 568     7058   6367   6090    240   1001    424       C
ATOM   4504  O   GLY A 568     -16.402   3.900  37.647  1.00 57.92           O
ANISOU 4504  O   GLY A 568     7870   7196   6941    239   1029    470       O
ATOM   4505  N   LEU A 569     -16.020   5.963  36.866  1.00 60.16           N
ANISOU 4505  N   LEU A 569     8200   7476   7181    227    949    384       N
ATOM   4506  CA  LEU A 569     -14.658   5.656  36.478  1.00 66.66           C
ANISOU 4506  CA  LEU A 569     9031   8288   8011    205    922    389       C
ATOM   4507  C   LEU A 569     -13.709   5.854  37.650  1.00 81.68           C
ANISOU 4507  C   LEU A 569    10957  10228   9850    231    909    407       C
ATOM   4508  O   LEU A 569     -13.731   6.904  38.300  1.00 89.07           O
ANISOU 4508  O   LEU A 569    11921  11192  10730    254    887    381       O
ATOM   4509  CB  LEU A 569     -14.242   6.531  35.299  1.00 55.76           C
ANISOU 4509  CB  LEU A 569     7665   6881   6641    175    873    340       C
ATOM   4510  CG  LEU A 569     -13.472   5.773  34.230  1.00 44.81           C
ANISOU 4510  CG  LEU A 569     6261   5461   5304    139    866    346       C
ATOM   4511  CD1 LEU A 569     -14.176   4.470  33.892  1.00 48.31           C
ANISOU 4511  CD1 LEU A 569     6665   5883   5809    128    913    375       C
ATOM   4512  CD2 LEU A 569     -13.318   6.641  33.002  1.00 35.92           C
ANISOU 4512  CD2 LEU A 569     5145   4311   4191    112    824    299       C
ATOM   4513  N   GLY A 570     -12.907   4.825  37.935  1.00 83.74           N
ANISOU 4513  N   GLY A 570    11206  10490  10120    228    925    450       N
ATOM   4514  CA  GLY A 570     -11.703   4.959  38.736  1.00 84.88           C
ANISOU 4514  CA  GLY A 570    11373  10665  10214    242    901    463       C
ATOM   4515  C   GLY A 570     -11.825   4.915  40.248  1.00 85.81           C
ANISOU 4515  C   GLY A 570    11499  10833  10272    286    923    494       C
ATOM   4516  O   GLY A 570     -12.153   3.874  40.825  1.00 90.81           O
ANISOU 4516  O   GLY A 570    12108  11477  10918    301    970    547       O
ATOM   4517  N   ASP A 571     -11.572   6.047  40.901  1.00 77.37           N
ANISOU 4517  N   ASP A 571    10462   9797   9138    308    889    462       N
ATOM   4518  CA  ASP A 571     -11.456   7.323  40.204  1.00 68.36           C
ANISOU 4518  CA  ASP A 571     9345   8639   7991    292    839    400       C
ATOM   4519  C   ASP A 571     -10.077   7.648  39.613  1.00 56.86           C
ANISOU 4519  C   ASP A 571     7903   7165   6536    265    790    381       C
ATOM   4520  O   ASP A 571      -9.030   7.305  40.166  1.00 51.76           O
ANISOU 4520  O   ASP A 571     7262   6538   5865    271    779    404       O
ATOM   4521  CB  ASP A 571     -11.899   8.449  41.132  1.00 69.11           C
ANISOU 4521  CB  ASP A 571     9466   8771   8021    327    826    369       C
ATOM   4522  CG  ASP A 571     -12.662   9.525  40.397  1.00 70.39           C
ANISOU 4522  CG  ASP A 571     9638   8909   8198    317    805    316       C
ATOM   4523  OD1 ASP A 571     -12.112  10.634  40.233  1.00 74.82           O
ANISOU 4523  OD1 ASP A 571    10225   9467   8736    312    756    271       O
ATOM   4524  OD2 ASP A 571     -13.796   9.244  39.949  1.00 67.28           O
ANISOU 4524  OD2 ASP A 571     9224   8498   7843    313    837    320       O
ATOM   4525  N   VAL A 572     -10.123   8.324  38.468  1.00 52.52           N
ANISOU 4525  N   VAL A 572     7358   6579   6017    236    760    339       N
ATOM   4526  CA  VAL A 572      -8.951   8.632  37.658  1.00 46.16           C
ANISOU 4526  CA  VAL A 572     6562   5750   5226    205    716    321       C
ATOM   4527  C   VAL A 572      -8.216   9.840  38.228  1.00 47.83           C
ANISOU 4527  C   VAL A 572     6806   5983   5383    218    667    286       C
ATOM   4528  O   VAL A 572      -8.822  10.752  38.805  1.00 40.37           O
ANISOU 4528  O   VAL A 572     5879   5058   4402    242    659    257       O
ATOM   4529  CB  VAL A 572      -9.395   8.867  36.199  1.00 44.25           C
ANISOU 4529  CB  VAL A 572     6309   5465   5039    171    708    293       C
ATOM   4530  CG1 VAL A 572      -8.305   9.524  35.383  1.00 45.23           C
ANISOU 4530  CG1 VAL A 572     6447   5568   5169    144    658    265       C
ATOM   4531  CG2 VAL A 572      -9.820   7.554  35.559  1.00 43.52           C
ANISOU 4531  CG2 VAL A 572     6182   5348   5004    153    749    325       C
ATOM   4532  N   ASN A 573      -6.888   9.847  38.069  1.00 50.86           N
ANISOU 4532  N   ASN A 573     7197   6363   5763    202    634    288       N
ATOM   4533  CA  ASN A 573      -6.065  11.010  38.408  1.00 50.82           C
ANISOU 4533  CA  ASN A 573     7221   6370   5718    206    582    251       C
ATOM   4534  C   ASN A 573      -6.220  12.048  37.301  1.00 54.43           C
ANISOU 4534  C   ASN A 573     7687   6791   6204    181    549    205       C
ATOM   4535  O   ASN A 573      -5.400  12.170  36.384  1.00 46.79           O
ANISOU 4535  O   ASN A 573     6718   5796   5266    150    521    198       O
ATOM   4536  CB  ASN A 573      -4.607  10.611  38.605  1.00 47.74           C
ANISOU 4536  CB  ASN A 573     6832   5988   5318    198    559    272       C
ATOM   4537  CG  ASN A 573      -3.756  11.758  39.127  1.00 48.44           C
ANISOU 4537  CG  ASN A 573     6948   6093   5363    205    506    236       C
ATOM   4538  OD1 ASN A 573      -4.244  12.873  39.320  1.00 53.03           O
ANISOU 4538  OD1 ASN A 573     7548   6678   5924    217    485    193       O
ATOM   4539  ND2 ASN A 573      -2.479  11.481  39.376  1.00 52.70           N
ANISOU 4539  ND2 ASN A 573     7489   6643   5891    200    484    252       N
ATOM   4540  N   VAL A 574      -7.300  12.825  37.409  1.00 53.53           N
ANISOU 4540  N   VAL A 574     7581   6679   6080    196    552    176       N
ATOM   4541  CA  VAL A 574      -7.619  13.830  36.400  1.00 51.37           C
ANISOU 4541  CA  VAL A 574     7314   6372   5834    176    525    135       C
ATOM   4542  C   VAL A 574      -6.532  14.895  36.311  1.00 51.13           C
ANISOU 4542  C   VAL A 574     7305   6333   5789    165    469    103       C
ATOM   4543  O   VAL A 574      -6.277  15.444  35.232  1.00 47.19           O
ANISOU 4543  O   VAL A 574     6805   5801   5323    138    443     83       O
ATOM   4544  CB  VAL A 574      -8.996  14.444  36.711  1.00 51.04           C
ANISOU 4544  CB  VAL A 574     7276   6337   5780    200    542    112       C
ATOM   4545  CG1 VAL A 574     -10.096  13.471  36.340  1.00 44.49           C
ANISOU 4545  CG1 VAL A 574     6420   5500   4985    198    593    139       C
ATOM   4546  CG2 VAL A 574      -9.091  14.794  38.193  1.00 52.75           C
ANISOU 4546  CG2 VAL A 574     7512   6597   5935    241    543    105       C
ATOM   4547  N   GLU A 575      -5.870  15.199  37.430  1.00 51.20           N
ANISOU 4547  N   GLU A 575     7331   6374   5749    188    449     97       N
ATOM   4548  CA  GLU A 575      -4.839  16.234  37.423  1.00 54.03           C
ANISOU 4548  CA  GLU A 575     7709   6725   6095    179    394     64       C
ATOM   4549  C   GLU A 575      -3.661  15.835  36.536  1.00 46.50           C
ANISOU 4549  C   GLU A 575     6745   5747   5177    143    375     82       C
ATOM   4550  O   GLU A 575      -3.188  16.626  35.713  1.00 42.47           O
ANISOU 4550  O   GLU A 575     6240   5207   4692    119    340     58       O
ATOM   4551  CB  GLU A 575      -4.376  16.506  38.855  1.00 61.62           C
ANISOU 4551  CB  GLU A 575     8688   7730   6996    212    379     55       C
ATOM   4552  CG  GLU A 575      -3.661  17.830  39.049  1.00 74.43           C
ANISOU 4552  CG  GLU A 575    10333   9347   8602    211    322      7       C
ATOM   4553  CD  GLU A 575      -4.550  19.023  38.749  1.00 85.91           C
ANISOU 4553  CD  GLU A 575    11797  10778  10065    215    309    -39       C
ATOM   4554  OE1 GLU A 575      -4.184  19.837  37.872  1.00 88.44           O
ANISOU 4554  OE1 GLU A 575    12121  11062  10421    189    275    -64       O
ATOM   4555  OE2 GLU A 575      -5.620  19.140  39.386  1.00 90.71           O
ANISOU 4555  OE2 GLU A 575    12410  11408  10649    245    335    -49       O
ATOM   4556  N   GLU A 576      -3.177  14.602  36.692  1.00 43.85           N
ANISOU 4556  N   GLU A 576     6394   5423   4844    140    400    126       N
ATOM   4557  CA  GLU A 576      -2.032  14.139  35.913  1.00 43.47           C
ANISOU 4557  CA  GLU A 576     6335   5355   4827    109    385    145       C
ATOM   4558  C   GLU A 576      -2.408  13.848  34.467  1.00 40.37           C
ANISOU 4558  C   GLU A 576     5924   4924   4490     77    399    149       C
ATOM   4559  O   GLU A 576      -1.600  14.077  33.559  1.00 36.10           O
ANISOU 4559  O   GLU A 576     5380   4359   3977     49    372    144       O
ATOM   4560  CB  GLU A 576      -1.438  12.890  36.556  1.00 46.73           C
ANISOU 4560  CB  GLU A 576     6736   5793   5227    118    409    191       C
ATOM   4561  CG  GLU A 576      -0.057  13.093  37.129  1.00 55.36           C
ANISOU 4561  CG  GLU A 576     7839   6903   6293    119    371    192       C
ATOM   4562  CD  GLU A 576       0.485  11.840  37.774  1.00 60.70           C
ANISOU 4562  CD  GLU A 576     8501   7604   6956    130    397    242       C
ATOM   4563  OE1 GLU A 576      -0.061  11.422  38.822  1.00 61.45           O
ANISOU 4563  OE1 GLU A 576     8597   7735   7016    162    425    260       O
ATOM   4564  OE2 GLU A 576       1.450  11.271  37.224  1.00 60.41           O
ANISOU 4564  OE2 GLU A 576     8452   7553   6948    107    391    264       O
ATOM   4565  N   LEU A 577      -3.623  13.349  34.238  1.00 34.52           N
ANISOU 4565  N   LEU A 577     5171   4180   3767     83    439    157       N
ATOM   4566  CA  LEU A 577      -4.026  12.917  32.905  1.00 34.35           C
ANISOU 4566  CA  LEU A 577     5129   4126   3797     55    455    162       C
ATOM   4567  C   LEU A 577      -4.239  14.102  31.965  1.00 25.16           C
ANISOU 4567  C   LEU A 577     3973   2936   2650     39    424    125       C
ATOM   4568  O   LEU A 577      -3.897  14.032  30.777  1.00 30.09           O
ANISOU 4568  O   LEU A 577     4585   3535   3311     10    415    125       O
ATOM   4569  CB  LEU A 577      -5.292  12.068  33.016  1.00 33.88           C
ANISOU 4569  CB  LEU A 577     5051   4071   3750     68    506    181       C
ATOM   4570  CG  LEU A 577      -5.890  11.507  31.730  1.00 33.13           C
ANISOU 4570  CG  LEU A 577     4932   3948   3708     43    527    184       C
ATOM   4571  CD1 LEU A 577      -4.889  10.607  30.973  1.00 28.19           C
ANISOU 4571  CD1 LEU A 577     4289   3306   3115     16    528    207       C
ATOM   4572  CD2 LEU A 577      -7.173  10.765  32.056  1.00 29.83           C
ANISOU 4572  CD2 LEU A 577     4497   3537   3300     59    576    200       C
ATOM   4573  N   PHE A 578      -4.789  15.202  32.470  1.00 30.31           N
ANISOU 4573  N   PHE A 578     4644   3594   3278     58    407     93       N
ATOM   4574  CA  PHE A 578      -5.088  16.359  31.638  1.00 33.24           C
ANISOU 4574  CA  PHE A 578     5022   3940   3668     45    379     60       C
ATOM   4575  C   PHE A 578      -4.092  17.492  31.819  1.00 30.57           C
ANISOU 4575  C   PHE A 578     4703   3595   3315     41    328     35       C
ATOM   4576  O   PHE A 578      -4.249  18.538  31.192  1.00 34.43           O
ANISOU 4576  O   PHE A 578     5198   4061   3820     31    302      8       O
ATOM   4577  CB  PHE A 578      -6.510  16.860  31.929  1.00 43.29           C
ANISOU 4577  CB  PHE A 578     6298   5217   4932     67    396     39       C
ATOM   4578  CG  PHE A 578      -7.572  15.793  31.794  1.00 45.34           C
ANISOU 4578  CG  PHE A 578     6537   5483   5209     72    446     62       C
ATOM   4579  CD1 PHE A 578      -8.044  15.113  32.908  1.00 49.23           C
ANISOU 4579  CD1 PHE A 578     7029   6004   5674    100    480     81       C
ATOM   4580  CD2 PHE A 578      -8.090  15.468  30.554  1.00 44.85           C
ANISOU 4580  CD2 PHE A 578     6454   5397   5189     50    459     66       C
ATOM   4581  CE1 PHE A 578      -9.015  14.131  32.785  1.00 51.58           C
ANISOU 4581  CE1 PHE A 578     7303   6303   5991    103    527    104       C
ATOM   4582  CE2 PHE A 578      -9.058  14.490  30.419  1.00 44.59           C
ANISOU 4582  CE2 PHE A 578     6400   5367   5176     53    503     84       C
ATOM   4583  CZ  PHE A 578      -9.523  13.819  31.535  1.00 48.53           C
ANISOU 4583  CZ  PHE A 578     6896   5890   5652     79    538    104       C
ATOM   4584  N   GLY A 579      -3.071  17.309  32.654  1.00 34.78           N
ANISOU 4584  N   GLY A 579     5245   4148   3821     48    313     43       N
ATOM   4585  CA  GLY A 579      -2.132  18.382  32.911  1.00 33.54           C
ANISOU 4585  CA  GLY A 579     5106   3986   3652     44    264     17       C
ATOM   4586  C   GLY A 579      -1.239  18.676  31.721  1.00 37.13           C
ANISOU 4586  C   GLY A 579     5553   4410   4146      9    236     19       C
ATOM   4587  O   GLY A 579      -0.902  17.803  30.924  1.00 42.15           O
ANISOU 4587  O   GLY A 579     6170   5037   4808    -12    253     48       O
ATOM   4588  N   ILE A 580      -0.852  19.941  31.610  1.00 30.62           N
ANISOU 4588  N   ILE A 580     4741   3567   3326      4    194    -11       N
ATOM   4589  CA  ILE A 580       0.001  20.432  30.532  1.00 32.65           C
ANISOU 4589  CA  ILE A 580     4992   3794   3620    -28    165    -11       C
ATOM   4590  C   ILE A 580       1.131  21.215  31.178  1.00 35.83           C
ANISOU 4590  C   ILE A 580     5408   4197   4009    -28    119    -29       C
ATOM   4591  O   ILE A 580       0.883  22.195  31.891  1.00 36.97           O
ANISOU 4591  O   ILE A 580     5570   4343   4136    -10     96    -64       O
ATOM   4592  CB  ILE A 580      -0.784  21.306  29.540  1.00 33.63           C
ANISOU 4592  CB  ILE A 580     5114   3889   3774    -38    159    -28       C
ATOM   4593  CG1 ILE A 580      -1.790  20.435  28.774  1.00 32.59           C
ANISOU 4593  CG1 ILE A 580     4965   3758   3660    -41    202     -9       C
ATOM   4594  CG2 ILE A 580       0.161  22.043  28.600  1.00 35.51           C
ANISOU 4594  CG2 ILE A 580     5348   4098   4046    -66    123    -29       C
ATOM   4595  CD1 ILE A 580      -2.883  21.218  28.065  1.00 32.18           C
ANISOU 4595  CD1 ILE A 580     4913   3687   3629    -41    203    -27       C
ATOM   4596  N   SER A 581       2.362  20.772  30.959  1.00 28.41           N
ANISOU 4596  N   SER A 581     4460   3257   3078    -47    106     -7       N
ATOM   4597  CA  SER A 581       3.528  21.344  31.619  1.00 32.37           C
ANISOU 4597  CA  SER A 581     4971   3763   3567    -48     64    -21       C
ATOM   4598  C   SER A 581       4.310  22.201  30.633  1.00 34.02           C
ANISOU 4598  C   SER A 581     5173   3936   3817    -78     28    -27       C
ATOM   4599  O   SER A 581       4.654  21.731  29.544  1.00 33.69           O
ANISOU 4599  O   SER A 581     5115   3880   3807   -102     39      1       O
ATOM   4600  CB  SER A 581       4.411  20.228  32.184  1.00 40.93           C
ANISOU 4600  CB  SER A 581     6047   4874   4631    -46     73     10       C
ATOM   4601  OG  SER A 581       5.764  20.626  32.260  1.00 45.19           O
ANISOU 4601  OG  SER A 581     6586   5408   5177    -61     33      7       O
ATOM   4602  N   LYS A 582       4.582  23.460  31.006  1.00 27.23           N
ANISOU 4602  N   LYS A 582     4325   3061   2959    -75    -13    -62       N
ATOM   4603  CA  LYS A 582       5.414  24.307  30.156  1.00 27.85           C
ANISOU 4603  CA  LYS A 582     4398   3105   3080   -103    -48    -65       C
ATOM   4604  C   LYS A 582       6.748  23.637  29.848  1.00 31.94           C
ANISOU 4604  C   LYS A 582     4900   3627   3609   -125    -56    -33       C
ATOM   4605  O   LYS A 582       7.234  23.680  28.709  1.00 29.58           O
ANISOU 4605  O   LYS A 582     4586   3305   3347   -152    -59    -12       O
ATOM   4606  CB  LYS A 582       5.644  25.663  30.824  1.00 28.94           C
ANISOU 4606  CB  LYS A 582     4550   3229   3219    -95    -93   -109       C
ATOM   4607  CG  LYS A 582       6.606  26.568  30.067  1.00 30.76           C
ANISOU 4607  CG  LYS A 582     4771   3421   3495   -124   -131   -110       C
ATOM   4608  CD  LYS A 582       6.552  27.996  30.590  1.00 33.89           C
ANISOU 4608  CD  LYS A 582     5181   3796   3902   -116   -172   -158       C
ATOM   4609  CE  LYS A 582       7.414  28.923  29.750  1.00 40.21           C
ANISOU 4609  CE  LYS A 582     5969   4553   4755   -145   -207   -155       C
ATOM   4610  NZ  LYS A 582       7.290  30.347  30.173  1.00 47.54           N
ANISOU 4610  NZ  LYS A 582     6908   5453   5703   -138   -245   -202       N
ATOM   4611  N   GLU A 583       7.341  22.987  30.850  1.00 30.66           N
ANISOU 4611  N   GLU A 583     4741   3495   3413   -112    -57    -27       N
ATOM   4612  CA  GLU A 583       8.670  22.415  30.684  1.00 34.76           C
ANISOU 4612  CA  GLU A 583     5246   4018   3941   -131    -68      1       C
ATOM   4613  C   GLU A 583       8.652  21.252  29.700  1.00 33.95           C
ANISOU 4613  C   GLU A 583     5126   3917   3858   -146    -29     43       C
ATOM   4614  O   GLU A 583       9.581  21.099  28.899  1.00 34.40           O
ANISOU 4614  O   GLU A 583     5167   3960   3943   -171    -38     65       O
ATOM   4615  CB  GLU A 583       9.225  21.983  32.043  1.00 42.60           C
ANISOU 4615  CB  GLU A 583     6247   5048   4891   -110    -78     -2       C
ATOM   4616  CG  GLU A 583       9.567  23.154  32.982  1.00 50.34           C
ANISOU 4616  CG  GLU A 583     7242   6028   5855    -98   -126    -47       C
ATOM   4617  CD  GLU A 583       8.339  23.926  33.460  1.00 55.94           C
ANISOU 4617  CD  GLU A 583     7970   6737   6548    -75   -124    -87       C
ATOM   4618  OE1 GLU A 583       7.332  23.280  33.826  1.00 51.18           O
ANISOU 4618  OE1 GLU A 583     7373   6157   5915    -52    -85    -80       O
ATOM   4619  OE2 GLU A 583       8.375  25.181  33.457  1.00 58.83           O
ANISOU 4619  OE2 GLU A 583     8343   7077   6932    -78   -159   -124       O
ATOM   4620  N   PHE A 584       7.598  20.432  29.727  1.00 33.54           N
ANISOU 4620  N   PHE A 584     5073   3879   3790   -131     14     54       N
ATOM   4621  CA  PHE A 584       7.502  19.340  28.761  1.00 30.85           C
ANISOU 4621  CA  PHE A 584     4714   3536   3470   -146     50     88       C
ATOM   4622  C   PHE A 584       7.303  19.876  27.351  1.00 29.18           C
ANISOU 4622  C   PHE A 584     4493   3295   3299   -169     48     88       C
ATOM   4623  O   PHE A 584       7.921  19.395  26.394  1.00 26.68           O
ANISOU 4623  O   PHE A 584     4158   2970   3007   -191     54    113       O
ATOM   4624  CB  PHE A 584       6.354  18.400  29.124  1.00 27.76           C
ANISOU 4624  CB  PHE A 584     4323   3165   3059   -125     96     97       C
ATOM   4625  CG  PHE A 584       6.111  17.322  28.089  1.00 27.04           C
ANISOU 4625  CG  PHE A 584     4212   3069   2993   -140    134    126       C
ATOM   4626  CD1 PHE A 584       6.769  16.103  28.169  1.00 28.00           C
ANISOU 4626  CD1 PHE A 584     4320   3204   3116   -143    154    158       C
ATOM   4627  CD2 PHE A 584       5.225  17.532  27.037  1.00 25.44           C
ANISOU 4627  CD2 PHE A 584     4004   2849   2815   -149    149    120       C
ATOM   4628  CE1 PHE A 584       6.559  15.119  27.214  1.00 26.45           C
ANISOU 4628  CE1 PHE A 584     4104   3001   2946   -156    187    180       C
ATOM   4629  CE2 PHE A 584       5.004  16.557  26.083  1.00 26.80           C
ANISOU 4629  CE2 PHE A 584     4156   3017   3010   -162    181    141       C
ATOM   4630  CZ  PHE A 584       5.674  15.341  26.168  1.00 21.05           C
ANISOU 4630  CZ  PHE A 584     3413   2299   2284   -166    201    170       C
ATOM   4631  N   TRP A 585       6.411  20.854  27.197  1.00 30.42           N
ANISOU 4631  N   TRP A 585     4661   3437   3462   -163     40     62       N
ATOM   4632  CA  TRP A 585       6.081  21.328  25.860  1.00 26.86           C
ANISOU 4632  CA  TRP A 585     4199   2960   3045   -182     41     65       C
ATOM   4633  C   TRP A 585       7.153  22.234  25.272  1.00 25.99           C
ANISOU 4633  C   TRP A 585     4084   2827   2965   -205      3     66       C
ATOM   4634  O   TRP A 585       7.252  22.323  24.045  1.00 26.08           O
ANISOU 4634  O   TRP A 585     4080   2823   3005   -224      7     83       O
ATOM   4635  CB  TRP A 585       4.705  22.006  25.876  1.00 26.89           C
ANISOU 4635  CB  TRP A 585     4214   2958   3046   -166     48     40       C
ATOM   4636  CG  TRP A 585       3.652  20.957  25.957  1.00 24.34           C
ANISOU 4636  CG  TRP A 585     3887   2653   2707   -152     93     48       C
ATOM   4637  CD1 TRP A 585       3.049  20.480  27.089  1.00 26.76           C
ANISOU 4637  CD1 TRP A 585     4205   2984   2981   -127    112     41       C
ATOM   4638  CD2 TRP A 585       3.147  20.176  24.873  1.00 26.92           C
ANISOU 4638  CD2 TRP A 585     4197   2980   3053   -164    125     68       C
ATOM   4639  NE1 TRP A 585       2.167  19.476  26.767  1.00 29.33           N
ANISOU 4639  NE1 TRP A 585     4518   3319   3307   -122    155     56       N
ATOM   4640  CE2 TRP A 585       2.215  19.265  25.412  1.00 25.42           C
ANISOU 4640  CE2 TRP A 585     4006   2809   2844   -145    162     71       C
ATOM   4641  CE3 TRP A 585       3.389  20.160  23.493  1.00 27.87           C
ANISOU 4641  CE3 TRP A 585     4299   3085   3204   -187    126     83       C
ATOM   4642  CZ2 TRP A 585       1.513  18.354  24.617  1.00 24.14           C
ANISOU 4642  CZ2 TRP A 585     3827   2649   2696   -151    199     85       C
ATOM   4643  CZ3 TRP A 585       2.688  19.264  22.708  1.00 28.59           C
ANISOU 4643  CZ3 TRP A 585     4375   3183   3304   -191    161     95       C
ATOM   4644  CH2 TRP A 585       1.765  18.366  23.275  1.00 23.86           C
ANISOU 4644  CH2 TRP A 585     3775   2600   2689   -174    196     95       C
ATOM   4645  N   GLU A 586       7.980  22.869  26.102  1.00 30.88           N
ANISOU 4645  N   GLU A 586     4712   3443   3577   -203    -34     51       N
ATOM   4646  CA  GLU A 586       9.150  23.563  25.569  1.00 30.45           C
ANISOU 4646  CA  GLU A 586     4648   3367   3555   -227    -68     58       C
ATOM   4647  C   GLU A 586      10.100  22.589  24.882  1.00 31.59           C
ANISOU 4647  C   GLU A 586     4772   3519   3712   -246    -55     96       C
ATOM   4648  O   GLU A 586      10.640  22.883  23.804  1.00 28.71           O
ANISOU 4648  O   GLU A 586     4392   3136   3380   -268    -62    113       O
ATOM   4649  CB  GLU A 586       9.878  24.306  26.685  1.00 28.76           C
ANISOU 4649  CB  GLU A 586     4445   3151   3330   -220   -110     32       C
ATOM   4650  CG  GLU A 586       9.172  25.546  27.156  1.00 35.04           C
ANISOU 4650  CG  GLU A 586     5257   3929   4126   -207   -132     -8       C
ATOM   4651  CD  GLU A 586       9.907  26.222  28.296  1.00 38.41           C
ANISOU 4651  CD  GLU A 586     5694   4357   4542   -199   -174    -39       C
ATOM   4652  OE1 GLU A 586      10.484  25.499  29.139  1.00 39.16           O
ANISOU 4652  OE1 GLU A 586     5791   4481   4606   -190   -175    -34       O
ATOM   4653  OE2 GLU A 586       9.919  27.471  28.340  1.00 43.29           O
ANISOU 4653  OE2 GLU A 586     6318   4946   5183   -202   -207    -68       O
ATOM   4654  N   LYS A 587      10.337  21.435  25.513  1.00 24.60           N
ANISOU 4654  N   LYS A 587     3885   2660   2800   -236    -35    110       N
ATOM   4655  CA  LYS A 587      11.158  20.395  24.902  1.00 24.74           C
ANISOU 4655  CA  LYS A 587     3883   2686   2830   -252    -18    145       C
ATOM   4656  C   LYS A 587      10.459  19.793  23.692  1.00 25.74           C
ANISOU 4656  C   LYS A 587     3997   2810   2972   -260     19    161       C
ATOM   4657  O   LYS A 587      11.097  19.540  22.661  1.00 25.80           O
ANISOU 4657  O   LYS A 587     3987   2811   3005   -280     23    183       O
ATOM   4658  CB  LYS A 587      11.477  19.309  25.934  1.00 28.48           C
ANISOU 4658  CB  LYS A 587     4360   3189   3274   -236     -3    156       C
ATOM   4659  CG  LYS A 587      12.133  18.047  25.358  1.00 36.86           C
ANISOU 4659  CG  LYS A 587     5399   4258   4346   -248     23    192       C
ATOM   4660  CD  LYS A 587      13.503  18.338  24.757  1.00 45.40           C
ANISOU 4660  CD  LYS A 587     6467   5329   5456   -272     -3    208       C
ATOM   4661  CE  LYS A 587      14.224  17.042  24.390  1.00 50.47           C
ANISOU 4661  CE  LYS A 587     7089   5982   6106   -280     22    242       C
ATOM   4662  NZ  LYS A 587      15.521  17.274  23.676  1.00 48.43           N
ANISOU 4662  NZ  LYS A 587     6813   5713   5876   -303      1    260       N
ATOM   4663  N   GLU A 588       9.147  19.567  23.797  1.00 26.28           N
ANISOU 4663  N   GLU A 588     4073   2885   3027   -244     45    149       N
ATOM   4664  CA  GLU A 588       8.410  18.940  22.704  1.00 25.63           C
ANISOU 4664  CA  GLU A 588     3978   2803   2958   -250     79    160       C
ATOM   4665  C   GLU A 588       8.492  19.773  21.435  1.00 25.12           C
ANISOU 4665  C   GLU A 588     3903   2717   2922   -269     66    163       C
ATOM   4666  O   GLU A 588       8.795  19.255  20.355  1.00 24.17           O
ANISOU 4666  O   GLU A 588     3765   2599   2820   -284     80    183       O
ATOM   4667  CB  GLU A 588       6.952  18.737  23.100  1.00 24.07           C
ANISOU 4667  CB  GLU A 588     3790   2612   2742   -229    105    144       C
ATOM   4668  CG  GLU A 588       6.183  17.873  22.114  1.00 25.30           C
ANISOU 4668  CG  GLU A 588     3930   2772   2911   -234    143    154       C
ATOM   4669  CD  GLU A 588       6.630  16.422  22.142  1.00 25.35           C
ANISOU 4669  CD  GLU A 588     3922   2793   2917   -236    172    177       C
ATOM   4670  OE1 GLU A 588       7.229  15.995  23.156  1.00 23.82           O
ANISOU 4670  OE1 GLU A 588     3733   2610   2706   -227    169    185       O
ATOM   4671  OE2 GLU A 588       6.382  15.711  21.143  1.00 24.39           O
ANISOU 4671  OE2 GLU A 588     3783   2672   2813   -246    196    187       O
ATOM   4672  N   VAL A 589       8.217  21.077  21.545  1.00 22.02           N
ANISOU 4672  N   VAL A 589     3524   2308   2537   -267     38    143       N
ATOM   4673  CA  VAL A 589       8.253  21.929  20.363  1.00 20.54           C
ANISOU 4673  CA  VAL A 589     3326   2101   2378   -283     25    149       C
ATOM   4674  C   VAL A 589       9.674  22.031  19.808  1.00 20.29           C
ANISOU 4674  C   VAL A 589     3279   2062   2369   -305      6    172       C
ATOM   4675  O   VAL A 589       9.860  22.133  18.592  1.00 20.05           O
ANISOU 4675  O   VAL A 589     3233   2027   2360   -320     11    191       O
ATOM   4676  CB  VAL A 589       7.631  23.303  20.700  1.00 30.52           C
ANISOU 4676  CB  VAL A 589     4605   3344   3647   -274     -0    122       C
ATOM   4677  CG1 VAL A 589       8.506  24.066  21.649  1.00 30.72           C
ANISOU 4677  CG1 VAL A 589     4641   3357   3673   -274    -39    108       C
ATOM   4678  CG2 VAL A 589       7.353  24.105  19.429  1.00 41.24           C
ANISOU 4678  CG2 VAL A 589     5952   4684   5034   -286     -6    131       C
ATOM   4679  N   GLU A 590      10.701  21.961  20.663  1.00 19.94           N
ANISOU 4679  N   GLU A 590     3238   2019   2319   -307    -14    174       N
ATOM   4680  CA  GLU A 590      12.063  21.951  20.135  1.00 23.50           C
ANISOU 4680  CA  GLU A 590     3672   2466   2792   -328    -29    198       C
ATOM   4681  C   GLU A 590      12.330  20.674  19.357  1.00 24.96           C
ANISOU 4681  C   GLU A 590     3838   2668   2977   -335      4    225       C
ATOM   4682  O   GLU A 590      12.974  20.704  18.301  1.00 24.23           O
ANISOU 4682  O   GLU A 590     3727   2571   2907   -353      5    247       O
ATOM   4683  CB  GLU A 590      13.085  22.110  21.262  1.00 30.69           C
ANISOU 4683  CB  GLU A 590     4589   3377   3697   -327    -59    192       C
ATOM   4684  CG  GLU A 590      13.208  23.534  21.793  1.00 48.49           C
ANISOU 4684  CG  GLU A 590     6854   5607   5963   -327   -101    168       C
ATOM   4685  CD  GLU A 590      13.396  24.579  20.685  1.00 61.83           C
ANISOU 4685  CD  GLU A 590     8532   7268   7692   -345   -117    178       C
ATOM   4686  OE1 GLU A 590      12.781  25.670  20.775  1.00 57.74           O
ANISOU 4686  OE1 GLU A 590     8024   6729   7185   -340   -134    156       O
ATOM   4687  OE2 GLU A 590      14.156  24.308  19.723  1.00 64.86           O
ANISOU 4687  OE2 GLU A 590     8895   7652   8096   -364   -111    209       O
ATOM   4688  N  AGLU A 591      11.849  19.527  19.852  0.85 22.98           N
ANISOU 4688  N  AGLU A 591     3591   2437   2704   -322     34    223       N
ATOM   4689  CA AGLU A 591      12.052  18.289  19.106  0.85 24.79           C
ANISOU 4689  CA AGLU A 591     3801   2680   2937   -328     67    245       C
ATOM   4690  C  AGLU A 591      11.285  18.302  17.792  0.85 24.91           C
ANISOU 4690  C  AGLU A 591     3805   2694   2964   -334     87    247       C
ATOM   4691  O  AGLU A 591      11.785  17.805  16.775  0.85 23.70           O
ANISOU 4691  O  AGLU A 591     3632   2547   2825   -347    100    265       O
ATOM   4692  CB AGLU A 591      11.640  17.071  19.943  0.85 25.71           C
ANISOU 4692  CB AGLU A 591     3922   2814   3032   -312     96    244       C
ATOM   4693  CG AGLU A 591      12.609  16.729  21.058  0.85 28.50           C
ANISOU 4693  CG AGLU A 591     4279   3175   3373   -307     82    252       C
ATOM   4694  CD AGLU A 591      14.054  16.622  20.582  0.85 27.68           C
ANISOU 4694  CD AGLU A 591     4158   3069   3290   -325     68    275       C
ATOM   4695  OE1AGLU A 591      14.935  17.232  21.222  0.85 24.41           O
ANISOU 4695  OE1AGLU A 591     3748   2651   2876   -329     34    275       O
ATOM   4696  OE2AGLU A 591      14.315  15.918  19.579  0.85 26.28           O
ANISOU 4696  OE2AGLU A 591     3962   2895   3129   -336     90    293       O
ATOM   4697  N  BGLU A 591      11.825  19.556  19.877  0.15 24.21           N
ANISOU 4697  N  BGLU A 591     3747   2592   2859   -321     34    222       N
ATOM   4698  CA BGLU A 591      11.953  18.264  19.223  0.15 24.79           C
ANISOU 4698  CA BGLU A 591     3803   2681   2935   -326     68    243       C
ATOM   4699  C  BGLU A 591      11.262  18.259  17.863  0.15 24.14           C
ANISOU 4699  C  BGLU A 591     3709   2597   2865   -333     87    246       C
ATOM   4700  O  BGLU A 591      11.807  17.746  16.879  0.15 24.01           O
ANISOU 4700  O  BGLU A 591     3673   2587   2863   -346    100    265       O
ATOM   4701  CB BGLU A 591      11.363  17.202  20.151  0.15 25.89           C
ANISOU 4701  CB BGLU A 591     3950   2836   3049   -307     95    237       C
ATOM   4702  CG BGLU A 591      12.141  15.933  20.219  0.15 27.48           C
ANISOU 4702  CG BGLU A 591     4137   3051   3253   -310    114    260       C
ATOM   4703  CD BGLU A 591      11.919  15.108  18.995  0.15 30.85           C
ANISOU 4703  CD BGLU A 591     4545   3482   3696   -319    146    271       C
ATOM   4704  OE1BGLU A 591      10.870  15.294  18.354  0.15 33.18           O
ANISOU 4704  OE1BGLU A 591     4840   3775   3993   -317    159    258       O
ATOM   4705  OE2BGLU A 591      12.794  14.289  18.656  0.15 35.48           O
ANISOU 4705  OE2BGLU A 591     5114   4073   4293   -328    157    291       O
ATOM   4706  N   ILE A 592      10.056  18.826  17.797  1.00 20.69           N
ANISOU 4706  N   ILE A 592     3283   2156   2423   -323     90    227       N
ATOM   4707  CA  ILE A 592       9.293  18.889  16.551  1.00 19.82           C
ANISOU 4707  CA  ILE A 592     3161   2048   2323   -328    106    228       C
ATOM   4708  C   ILE A 592       9.997  19.798  15.544  1.00 24.45           C
ANISOU 4708  C   ILE A 592     3736   2623   2931   -345     85    244       C
ATOM   4709  O   ILE A 592      10.082  19.483  14.349  1.00 24.11           O
ANISOU 4709  O   ILE A 592     3675   2590   2897   -354     99    259       O
ATOM   4710  CB  ILE A 592       7.860  19.379  16.835  1.00 18.64           C
ANISOU 4710  CB  ILE A 592     3026   1894   2162   -312    111    203       C
ATOM   4711  CG1 ILE A 592       7.088  18.385  17.712  1.00 20.97           C
ANISOU 4711  CG1 ILE A 592     3329   2202   2438   -295    138    191       C
ATOM   4712  CG2 ILE A 592       7.127  19.697  15.525  1.00 21.05           C
ANISOU 4712  CG2 ILE A 592     3319   2200   2478   -317    120    205       C
ATOM   4713  CD1 ILE A 592       5.797  18.980  18.341  1.00 22.17           C
ANISOU 4713  CD1 ILE A 592     3497   2349   2576   -276    138    166       C
ATOM   4714  N   ASP A 593      10.522  20.930  16.021  1.00 18.93           N
ANISOU 4714  N   ASP A 593     3046   1904   2241   -348     50    242       N
ATOM   4715  CA  ASP A 593      11.217  21.882  15.155  1.00 22.54           C
ANISOU 4715  CA  ASP A 593     3491   2348   2725   -365     28    260       C
ATOM   4716  C   ASP A 593      12.451  21.254  14.509  1.00 22.72           C
ANISOU 4716  C   ASP A 593     3493   2380   2758   -381     33    289       C
ATOM   4717  O   ASP A 593      12.633  21.318  13.287  1.00 23.89           O
ANISOU 4717  O   ASP A 593     3623   2535   2919   -391     41    309       O
ATOM   4718  CB  ASP A 593      11.602  23.101  15.986  1.00 20.28           C
ANISOU 4718  CB  ASP A 593     3218   2036   2451   -365    -11    249       C
ATOM   4719  CG  ASP A 593      12.376  24.143  15.185  1.00 36.51           C
ANISOU 4719  CG  ASP A 593     5260   4073   4540   -383    -35    271       C
ATOM   4720  OD1 ASP A 593      12.059  24.350  13.999  1.00 38.51           O
ANISOU 4720  OD1 ASP A 593     5501   4330   4804   -388    -24    287       O
ATOM   4721  OD2 ASP A 593      13.297  24.760  15.752  1.00 42.91           O
ANISOU 4721  OD2 ASP A 593     6072   4865   5366   -391    -66    271       O
ATOM   4722  N   LYS A 594      13.323  20.655  15.323  1.00 22.56           N
ANISOU 4722  N   LYS A 594     3474   2364   2733   -382     29    292       N
ATOM   4723  CA  LYS A 594      14.500  19.995  14.775  1.00 29.15           C
ANISOU 4723  CA  LYS A 594     4288   3208   3578   -395     36    319       C
ATOM   4724  C   LYS A 594      14.109  18.915  13.775  1.00 28.17           C
ANISOU 4724  C   LYS A 594     4148   3105   3448   -395     74    326       C
ATOM   4725  O   LYS A 594      14.757  18.754  12.734  1.00 24.79           O
ANISOU 4725  O   LYS A 594     3701   2687   3033   -407     81    348       O
ATOM   4726  CB  LYS A 594      15.333  19.400  15.907  1.00 22.93           C
ANISOU 4726  CB  LYS A 594     3505   2424   2783   -393     29    319       C
ATOM   4727  CG  LYS A 594      15.879  20.444  16.851  1.00 29.75           C
ANISOU 4727  CG  LYS A 594     4380   3269   3654   -395    -12    310       C
ATOM   4728  CD  LYS A 594      16.867  19.816  17.821  1.00 31.60           C
ANISOU 4728  CD  LYS A 594     4614   3512   3881   -394    -20    315       C
ATOM   4729  CE  LYS A 594      16.178  18.870  18.792  1.00 34.43           C
ANISOU 4729  CE  LYS A 594     4987   3887   4209   -374      1    300       C
ATOM   4730  NZ  LYS A 594      17.103  18.509  19.901  1.00 35.30           N
ANISOU 4730  NZ  LYS A 594     5100   4005   4310   -370    -15    304       N
ATOM   4731  N   TYR A 595      13.041  18.172  14.071  1.00 23.94           N
ANISOU 4731  N   TYR A 595     3622   2580   2895   -381     99    307       N
ATOM   4732  CA  TYR A 595      12.610  17.114  13.168  1.00 21.86           C
ANISOU 4732  CA  TYR A 595     3343   2335   2627   -380    134    308       C
ATOM   4733  C   TYR A 595      12.110  17.683  11.841  1.00 25.16           C
ANISOU 4733  C   TYR A 595     3750   2758   3051   -385    136    312       C
ATOM   4734  O   TYR A 595      12.566  17.267  10.771  1.00 23.87           O
ANISOU 4734  O   TYR A 595     3566   2610   2893   -393    150    327       O
ATOM   4735  CB  TYR A 595      11.542  16.258  13.847  1.00 21.50           C
ANISOU 4735  CB  TYR A 595     3308   2297   2566   -364    158    287       C
ATOM   4736  CG  TYR A 595      10.902  15.267  12.927  1.00 19.83           C
ANISOU 4736  CG  TYR A 595     3080   2100   2353   -363    192    282       C
ATOM   4737  CD1 TYR A 595      11.545  14.079  12.599  1.00 23.65           C
ANISOU 4737  CD1 TYR A 595     3547   2595   2844   -368    214    292       C
ATOM   4738  CD2 TYR A 595       9.630  15.495  12.412  1.00 23.81           C
ANISOU 4738  CD2 TYR A 595     3586   2609   2853   -356    202    265       C
ATOM   4739  CE1 TYR A 595      10.948  13.154  11.761  1.00 24.12           C
ANISOU 4739  CE1 TYR A 595     3591   2668   2907   -366    245    282       C
ATOM   4740  CE2 TYR A 595       9.025  14.578  11.576  1.00 29.23           C
ANISOU 4740  CE2 TYR A 595     4257   3311   3540   -355    231    256       C
ATOM   4741  CZ  TYR A 595       9.689  13.413  11.250  1.00 26.40           C
ANISOU 4741  CZ  TYR A 595     3881   2961   3189   -360    252    264       C
ATOM   4742  OH  TYR A 595       9.081  12.494  10.420  1.00 30.98           O
ANISOU 4742  OH  TYR A 595     4443   3555   3772   -359    280    250       O
ATOM   4743  N   LEU A 596      11.198  18.660  11.888  1.00 25.58           N
ANISOU 4743  N   LEU A 596     3816   2802   3102   -379    124    300       N
ATOM   4744  CA  LEU A 596      10.661  19.224  10.649  1.00 26.11           C
ANISOU 4744  CA  LEU A 596     3872   2876   3174   -381    126    305       C
ATOM   4745  C   LEU A 596      11.746  19.918   9.836  1.00 28.36           C
ANISOU 4745  C   LEU A 596     4142   3159   3476   -396    109    335       C
ATOM   4746  O   LEU A 596      11.784  19.796   8.604  1.00 28.15           O
ANISOU 4746  O   LEU A 596     4096   3150   3449   -400    121    349       O
ATOM   4747  CB  LEU A 596       9.522  20.202  10.952  1.00 23.37           C
ANISOU 4747  CB  LEU A 596     3541   2516   2824   -371    114    288       C
ATOM   4748  CG  LEU A 596       8.274  19.535  11.532  1.00 25.01           C
ANISOU 4748  CG  LEU A 596     3760   2730   3014   -355    135    260       C
ATOM   4749  CD1 LEU A 596       7.153  20.543  11.740  1.00 32.08           C
ANISOU 4749  CD1 LEU A 596     4668   3612   3908   -344    123    244       C
ATOM   4750  CD2 LEU A 596       7.833  18.389  10.612  1.00 24.85           C
ANISOU 4750  CD2 LEU A 596     3721   2734   2987   -355    167    257       C
ATOM   4751  N   GLU A 597      12.645  20.640  10.506  1.00 23.20           N
ANISOU 4751  N   GLU A 597     3494   2484   2837   -403     81    345       N
ATOM   4752  CA  GLU A 597      13.685  21.356   9.777  1.00 22.12           C
ANISOU 4752  CA  GLU A 597     3340   2342   2722   -418     65    376       C
ATOM   4753  C   GLU A 597      14.630  20.397   9.063  1.00 21.72           C
ANISOU 4753  C   GLU A 597     3268   2313   2671   -426     84    396       C
ATOM   4754  O   GLU A 597      15.014  20.640   7.913  1.00 27.38           O
ANISOU 4754  O   GLU A 597     3966   3042   3395   -433     88    421       O
ATOM   4755  CB  GLU A 597      14.477  22.259  10.716  1.00 26.08           C
ANISOU 4755  CB  GLU A 597     3851   2814   3242   -425     30    379       C
ATOM   4756  CG  GLU A 597      15.716  22.839  10.045  1.00 32.26           C
ANISOU 4756  CG  GLU A 597     4615   3592   4053   -442     15    414       C
ATOM   4757  CD  GLU A 597      16.688  23.453  11.027  1.00 41.37           C
ANISOU 4757  CD  GLU A 597     5773   4719   5227   -451    -18    415       C
ATOM   4758  OE1 GLU A 597      16.877  22.876  12.125  1.00 37.14           O
ANISOU 4758  OE1 GLU A 597     5250   4183   4679   -446    -22    396       O
ATOM   4759  OE2 GLU A 597      17.256  24.518  10.699  1.00 40.01           O
ANISOU 4759  OE2 GLU A 597     5591   4526   5084   -463    -41    435       O
ATOM   4760  N   ASP A 598      15.037  19.312   9.725  1.00 22.74           N
ANISOU 4760  N   ASP A 598     3400   2449   2793   -425     96    389       N
ATOM   4761  CA  ASP A 598      15.914  18.360   9.049  1.00 26.35           C
ANISOU 4761  CA  ASP A 598     3834   2925   3251   -431    116    406       C
ATOM   4762  C   ASP A 598      15.144  17.554   8.013  1.00 27.80           C
ANISOU 4762  C   ASP A 598     4007   3135   3420   -425    148    397       C
ATOM   4763  O   ASP A 598      15.533  17.505   6.839  1.00 25.13           O
ANISOU 4763  O   ASP A 598     3648   2815   3084   -430    158    415       O
ATOM   4764  CB  ASP A 598      16.596  17.422  10.051  1.00 29.59           C
ANISOU 4764  CB  ASP A 598     4249   3333   3661   -430    120    403       C
ATOM   4765  CG  ASP A 598      17.430  16.332   9.359  1.00 31.51           C
ANISOU 4765  CG  ASP A 598     4470   3597   3908   -435    144    418       C
ATOM   4766  OD1 ASP A 598      17.462  15.177   9.846  1.00 32.08           O
ANISOU 4766  OD1 ASP A 598     4541   3674   3973   -429    163    409       O
ATOM   4767  OD2 ASP A 598      18.018  16.632   8.301  1.00 28.42           O
ANISOU 4767  OD2 ASP A 598     4059   3215   3525   -444    144    440       O
ATOM   4768  N   GLN A 599      14.032  16.936   8.420  1.00 21.61           N
ANISOU 4768  N   GLN A 599     3235   2355   2622   -413    164    369       N
ATOM   4769  CA  GLN A 599      13.442  15.901   7.585  1.00 23.94           C
ANISOU 4769  CA  GLN A 599     3516   2674   2906   -407    196    356       C
ATOM   4770  C   GLN A 599      12.593  16.462   6.459  1.00 21.88           C
ANISOU 4770  C   GLN A 599     3248   2428   2637   -404    199    353       C
ATOM   4771  O   GLN A 599      12.484  15.830   5.401  1.00 23.21           O
ANISOU 4771  O   GLN A 599     3398   2622   2798   -403    219    351       O
ATOM   4772  CB  GLN A 599      12.618  14.951   8.449  1.00 19.03           C
ANISOU 4772  CB  GLN A 599     2906   2048   2277   -397    214    329       C
ATOM   4773  CG  GLN A 599      13.484  14.120   9.353  1.00 22.26           C
ANISOU 4773  CG  GLN A 599     3316   2450   2692   -398    219    335       C
ATOM   4774  CD  GLN A 599      14.259  13.099   8.574  1.00 18.10           C
ANISOU 4774  CD  GLN A 599     2766   1940   2173   -403    241    344       C
ATOM   4775  OE1 GLN A 599      13.683  12.345   7.797  1.00 25.70           O
ANISOU 4775  OE1 GLN A 599     3715   2917   3131   -399    266    329       O
ATOM   4776  NE2 GLN A 599      15.574  13.087   8.747  1.00 24.86           N
ANISOU 4776  NE2 GLN A 599     3615   2793   3039   -411    231    367       N
ATOM   4777  N   VAL A 600      12.013  17.643   6.628  1.00 19.31           N
ANISOU 4777  N   VAL A 600     2936   2089   2314   -402    178    354       N
ATOM   4778  CA  VAL A 600      11.177  18.172   5.554  1.00 18.39           C
ANISOU 4778  CA  VAL A 600     2810   1988   2188   -397    180    354       C
ATOM   4779  C   VAL A 600      11.905  19.306   4.837  1.00 23.73           C
ANISOU 4779  C   VAL A 600     3477   2664   2877   -406    161    388       C
ATOM   4780  O   VAL A 600      11.761  19.465   3.621  1.00 20.10           O
ANISOU 4780  O   VAL A 600     3000   2228   2409   -405    169    401       O
ATOM   4781  CB  VAL A 600       9.806  18.613   6.091  1.00 22.03           C
ANISOU 4781  CB  VAL A 600     3290   2438   2643   -386    176    330       C
ATOM   4782  CG1 VAL A 600       8.816  18.739   4.948  1.00 20.58           C
ANISOU 4782  CG1 VAL A 600     3094   2278   2447   -379    186    324       C
ATOM   4783  CG2 VAL A 600       9.290  17.567   7.110  1.00 21.35           C
ANISOU 4783  CG2 VAL A 600     3216   2347   2551   -379    193    302       C
ATOM   4784  N   ASN A 601      12.701  20.080   5.581  1.00 22.39           N
ANISOU 4784  N   ASN A 601     3316   2466   2725   -414    136    404       N
ATOM   4785  CA  ASN A 601      13.668  21.019   4.998  1.00 22.85           C
ANISOU 4785  CA  ASN A 601     3361   2519   2803   -425    119    441       C
ATOM   4786  C   ASN A 601      13.034  21.971   3.981  1.00 21.79           C
ANISOU 4786  C   ASN A 601     3217   2393   2668   -421    114    457       C
ATOM   4787  O   ASN A 601      12.078  22.674   4.310  1.00 25.02           O
ANISOU 4787  O   ASN A 601     3641   2787   3078   -414    103    444       O
ATOM   4788  CB  ASN A 601      14.832  20.238   4.373  1.00 24.39           C
ANISOU 4788  CB  ASN A 601     3533   2735   2998   -433    133    461       C
ATOM   4789  CG  ASN A 601      16.031  21.128   4.063  1.00 31.14           C
ANISOU 4789  CG  ASN A 601     4376   3580   3878   -446    115    501       C
ATOM   4790  OD1 ASN A 601      16.084  22.285   4.497  1.00 23.53           O
ANISOU 4790  OD1 ASN A 601     3420   2587   2935   -451     88    511       O
ATOM   4791  ND2 ASN A 601      16.991  20.599   3.307  1.00 22.89           N
ANISOU 4791  ND2 ASN A 601     3307   2556   2833   -452    129    523       N
ATOM   4792  N   ALA A 602      13.527  21.988   2.740  1.00 23.36           N
ANISOU 4792  N   ALA A 602     3393   2619   2864   -424    124    485       N
ATOM   4793  CA  ALA A 602      13.050  22.974   1.770  1.00 23.46           C
ANISOU 4793  CA  ALA A 602     3395   2641   2878   -420    119    508       C
ATOM   4794  C   ALA A 602      11.616  22.720   1.323  1.00 22.00           C
ANISOU 4794  C   ALA A 602     3214   2478   2668   -405    132    483       C
ATOM   4795  O   ALA A 602      11.015  23.590   0.694  1.00 21.38           O
ANISOU 4795  O   ALA A 602     3130   2404   2590   -399    126    498       O
ATOM   4796  CB  ALA A 602      13.972  22.996   0.542  1.00 27.33           C
ANISOU 4796  CB  ALA A 602     3857   3159   3367   -425    128    548       C
ATOM   4797  N   ASP A 603      11.041  21.567   1.642  1.00 17.14           N
ANISOU 4797  N   ASP A 603     2605   1875   2034   -399    151    446       N
ATOM   4798  CA  ASP A 603       9.681  21.241   1.228  1.00 19.55           C
ANISOU 4798  CA  ASP A 603     2911   2201   2318   -385    164    420       C
ATOM   4799  C   ASP A 603       8.662  21.422   2.359  1.00 23.56           C
ANISOU 4799  C   ASP A 603     3443   2681   2829   -379    156    390       C
ATOM   4800  O   ASP A 603       7.490  21.059   2.199  1.00 21.62           O
ANISOU 4800  O   ASP A 603     3199   2449   2568   -368    168    364       O
ATOM   4801  CB  ASP A 603       9.646  19.802   0.691  1.00 20.64           C
ANISOU 4801  CB  ASP A 603     3035   2373   2434   -383    192    398       C
ATOM   4802  CG  ASP A 603      10.329  19.679  -0.672  1.00 28.17           C
ANISOU 4802  CG  ASP A 603     3962   3365   3377   -384    203    424       C
ATOM   4803  OD1 ASP A 603      10.112  20.574  -1.510  1.00 28.39           O
ANISOU 4803  OD1 ASP A 603     3980   3408   3400   -379    195    449       O
ATOM   4804  OD2 ASP A 603      11.090  18.712  -0.895  1.00 28.05           O
ANISOU 4804  OD2 ASP A 603     3935   3366   3358   -388    219    421       O
ATOM   4805  N   LEU A 604       9.074  21.988   3.477  1.00 25.50           N
ANISOU 4805  N   LEU A 604     3706   2889   3093   -384    137    391       N
ATOM   4806  CA  LEU A 604       8.146  22.268   4.575  1.00 25.53           C
ANISOU 4806  CA  LEU A 604     3733   2867   3099   -376    129    364       C
ATOM   4807  C   LEU A 604       7.219  23.418   4.201  1.00 25.59           C
ANISOU 4807  C   LEU A 604     3744   2869   3111   -367    116    369       C
ATOM   4808  O   LEU A 604       7.702  24.533   3.938  1.00 22.40           O
ANISOU 4808  O   LEU A 604     3336   2449   2727   -372     96    398       O
ATOM   4809  CB  LEU A 604       8.927  22.608   5.830  1.00 23.76           C
ANISOU 4809  CB  LEU A 604     3526   2609   2892   -383    109    364       C
ATOM   4810  CG  LEU A 604       8.092  22.706   7.100  1.00 22.51           C
ANISOU 4810  CG  LEU A 604     3393   2429   2731   -372    103    332       C
ATOM   4811  CD1 LEU A 604       7.505  21.344   7.420  1.00 23.25           C
ANISOU 4811  CD1 LEU A 604     3488   2540   2805   -365    130    305       C
ATOM   4812  CD2 LEU A 604       8.967  23.212   8.233  1.00 20.84           C
ANISOU 4812  CD2 LEU A 604     3195   2186   2536   -379     79    334       C
ATOM   4813  N   PRO A 605       5.903  23.205   4.136  1.00 24.96           N
ANISOU 4813  N   PRO A 605     3668   2800   3018   -354    127    344       N
ATOM   4814  CA  PRO A 605       5.005  24.303   3.763  1.00 22.75           C
ANISOU 4814  CA  PRO A 605     3388   2514   2743   -345    115    351       C
ATOM   4815  C   PRO A 605       5.088  25.431   4.778  1.00 22.10           C
ANISOU 4815  C   PRO A 605     3326   2388   2685   -345     89    351       C
ATOM   4816  O   PRO A 605       5.283  25.202   5.970  1.00 19.16           O
ANISOU 4816  O   PRO A 605     2972   1994   2315   -346     84    331       O
ATOM   4817  CB  PRO A 605       3.621  23.641   3.756  1.00 21.61           C
ANISOU 4817  CB  PRO A 605     3246   2388   2579   -331    132    318       C
ATOM   4818  CG  PRO A 605       3.908  22.199   3.521  1.00 23.39           C
ANISOU 4818  CG  PRO A 605     3461   2639   2788   -336    156    304       C
ATOM   4819  CD  PRO A 605       5.182  21.926   4.261  1.00 25.48           C
ANISOU 4819  CD  PRO A 605     3733   2886   3064   -348    151    312       C
ATOM   4820  N   TYR A 606       5.006  26.669   4.283  1.00 20.70           N
ANISOU 4820  N   TYR A 606     3143   2198   2525   -343     72    376       N
ATOM   4821  CA  TYR A 606       5.079  27.821   5.173  1.00 21.90           C
ANISOU 4821  CA  TYR A 606     3311   2305   2705   -343     46    375       C
ATOM   4822  C   TYR A 606       4.053  27.738   6.311  1.00 26.24           C
ANISOU 4822  C   TYR A 606     3884   2839   3248   -330     46    334       C
ATOM   4823  O   TYR A 606       4.340  28.120   7.455  1.00 22.65           O
ANISOU 4823  O   TYR A 606     3448   2353   2806   -331     30    318       O
ATOM   4824  CB  TYR A 606       4.887  29.092   4.349  1.00 19.45           C
ANISOU 4824  CB  TYR A 606     2989   1986   2416   -341     32    408       C
ATOM   4825  CG  TYR A 606       4.725  30.330   5.184  1.00 29.32           C
ANISOU 4825  CG  TYR A 606     4254   3189   3698   -338      6    402       C
ATOM   4826  CD1 TYR A 606       5.831  31.003   5.680  1.00 47.88           C
ANISOU 4826  CD1 TYR A 606     6606   5504   6080   -351    -16    415       C
ATOM   4827  CD2 TYR A 606       3.462  30.824   5.483  1.00 38.76           C
ANISOU 4827  CD2 TYR A 606     5460   4372   4893   -321      4    381       C
ATOM   4828  CE1 TYR A 606       5.684  32.142   6.443  1.00 59.23           C
ANISOU 4828  CE1 TYR A 606     8057   6897   7550   -348    -41    405       C
ATOM   4829  CE2 TYR A 606       3.304  31.963   6.246  1.00 50.57           C
ANISOU 4829  CE2 TYR A 606     6970   5825   6420   -317    -19    372       C
ATOM   4830  CZ  TYR A 606       4.418  32.612   6.722  1.00 59.07           C
ANISOU 4830  CZ  TYR A 606     8049   6867   7529   -331    -42    383       C
ATOM   4831  OH  TYR A 606       4.262  33.742   7.477  1.00 64.24           O
ANISOU 4831  OH  TYR A 606     8716   7477   8216   -327    -66    370       O
ATOM   4832  N   GLU A 607       2.848  27.251   6.017  1.00 20.29           N
ANISOU 4832  N   GLU A 607     3128   2108   2472   -317     64    316       N
ATOM   4833  CA  GLU A 607       1.810  27.196   7.039  1.00 26.96           C
ANISOU 4833  CA  GLU A 607     3992   2939   3311   -304     67    279       C
ATOM   4834  C   GLU A 607       2.181  26.263   8.183  1.00 25.48           C
ANISOU 4834  C   GLU A 607     3820   2748   3112   -306     75    255       C
ATOM   4835  O   GLU A 607       1.760  26.491   9.326  1.00 18.37           O
ANISOU 4835  O   GLU A 607     2940   1828   2213   -297     69    230       O
ATOM   4836  CB  GLU A 607       0.484  26.780   6.409  1.00 23.15           C
ANISOU 4836  CB  GLU A 607     3501   2484   2810   -291     86    267       C
ATOM   4837  CG  GLU A 607      -0.201  27.936   5.715  1.00 31.86           C
ANISOU 4837  CG  GLU A 607     4597   3582   3927   -281     74    283       C
ATOM   4838  CD  GLU A 607      -1.180  27.501   4.658  1.00 49.23           C
ANISOU 4838  CD  GLU A 607     6778   5820   6107   -273     91    283       C
ATOM   4839  OE1 GLU A 607      -2.380  27.821   4.798  1.00 48.99           O
ANISOU 4839  OE1 GLU A 607     6751   5786   6076   -258     93    267       O
ATOM   4840  OE2 GLU A 607      -0.742  26.851   3.682  1.00 60.41           O
ANISOU 4840  OE2 GLU A 607     8175   7269   7509   -280    102    298       O
ATOM   4841  N   ILE A 608       2.967  25.219   7.911  1.00 20.50           N
ANISOU 4841  N   ILE A 608     3180   2138   2471   -317     89    262       N
ATOM   4842  CA  ILE A 608       3.376  24.320   8.992  1.00 24.95           C
ANISOU 4842  CA  ILE A 608     3756   2699   3025   -318     97    244       C
ATOM   4843  C   ILE A 608       4.437  24.994   9.847  1.00 24.65           C
ANISOU 4843  C   ILE A 608     3730   2632   3003   -326     71    250       C
ATOM   4844  O   ILE A 608       4.368  24.980  11.084  1.00 28.15           O
ANISOU 4844  O   ILE A 608     4192   3060   3442   -319     65    228       O
ATOM   4845  CB  ILE A 608       3.873  22.972   8.434  1.00 19.67           C
ANISOU 4845  CB  ILE A 608     3072   2059   2344   -326    121    249       C
ATOM   4846  CG1 ILE A 608       2.786  22.338   7.575  1.00 19.89           C
ANISOU 4846  CG1 ILE A 608     3086   2115   2357   -319    144    238       C
ATOM   4847  CG2 ILE A 608       4.251  22.047   9.578  1.00 23.34           C
ANISOU 4847  CG2 ILE A 608     3548   2520   2801   -326    130    233       C
ATOM   4848  CD1 ILE A 608       1.544  21.943   8.386  1.00 20.69           C
ANISOU 4848  CD1 ILE A 608     3199   2214   2450   -304    157    206       C
ATOM   4849  N   GLU A 609       5.423  25.614   9.194  1.00 19.38           N
ANISOU 4849  N   GLU A 609     3052   1958   2355   -339     55    280       N
ATOM   4850  CA  GLU A 609       6.392  26.437   9.905  1.00 21.94           C
ANISOU 4850  CA  GLU A 609     3384   2251   2702   -348     26    286       C
ATOM   4851  C   GLU A 609       5.701  27.484  10.775  1.00 22.63           C
ANISOU 4851  C   GLU A 609     3490   2308   2800   -336      6    264       C
ATOM   4852  O   GLU A 609       6.140  27.761  11.895  1.00 23.36           O
ANISOU 4852  O   GLU A 609     3599   2380   2898   -336    -12    247       O
ATOM   4853  CB  GLU A 609       7.313  27.117   8.890  1.00 28.18           C
ANISOU 4853  CB  GLU A 609     4154   3037   3515   -362     14    325       C
ATOM   4854  CG  GLU A 609       8.444  27.913   9.472  1.00 43.62           C
ANISOU 4854  CG  GLU A 609     6113   4961   5500   -374    -16    335       C
ATOM   4855  CD  GLU A 609       9.558  28.081   8.459  1.00 64.65           C
ANISOU 4855  CD  GLU A 609     8752   7629   8181   -391    -19    377       C
ATOM   4856  OE1 GLU A 609      10.631  27.468   8.647  1.00 74.57           O
ANISOU 4856  OE1 GLU A 609    10004   8893   9438   -402    -18    386       O
ATOM   4857  OE2 GLU A 609       9.342  28.794   7.454  1.00 66.24           O
ANISOU 4857  OE2 GLU A 609     8940   7832   8397   -391    -20    404       O
ATOM   4858  N   ARG A 610       4.613  28.069  10.273  1.00 17.72           N
ANISOU 4858  N   ARG A 610     2868   1686   2181   -325      9    262       N
ATOM   4859  CA  ARG A 610       3.907  29.095  11.036  1.00 17.62           C
ANISOU 4859  CA  ARG A 610     2871   1642   2180   -312     -9    240       C
ATOM   4860  C   ARG A 610       3.213  28.501  12.260  1.00 22.38           C
ANISOU 4860  C   ARG A 610     3495   2249   2759   -297      1    201       C
ATOM   4861  O   ARG A 610       3.260  29.087  13.347  1.00 26.04           O
ANISOU 4861  O   ARG A 610     3977   2689   3229   -291    -17    179       O
ATOM   4862  CB  ARG A 610       2.903  29.815  10.131  1.00 26.42           C
ANISOU 4862  CB  ARG A 610     3977   2758   3305   -303     -6    250       C
ATOM   4863  CG  ARG A 610       2.005  30.835  10.850  1.00 24.68           C
ANISOU 4863  CG  ARG A 610     3773   2508   3098   -287    -21    226       C
ATOM   4864  CD  ARG A 610       1.128  31.586   9.852  1.00 28.89           C
ANISOU 4864  CD  ARG A 610     4292   3040   3644   -279    -20    243       C
ATOM   4865  NE  ARG A 610       0.074  30.765   9.243  1.00 26.80           N
ANISOU 4865  NE  ARG A 610     4020   2812   3351   -269      8    239       N
ATOM   4866  CZ  ARG A 610      -0.586  31.116   8.142  1.00 29.13           C
ANISOU 4866  CZ  ARG A 610     4299   3121   3650   -264     13    259       C
ATOM   4867  NH1 ARG A 610      -0.282  32.254   7.529  1.00 35.95           N
ANISOU 4867  NH1 ARG A 610     5152   3964   4543   -267     -5    289       N
ATOM   4868  NH2 ARG A 610      -1.537  30.340   7.640  1.00 28.29           N
ANISOU 4868  NH2 ARG A 610     4183   3047   3517   -255     36    250       N
ATOM   4869  N   GLU A 611       2.574  27.335  12.109  1.00 22.58           N
ANISOU 4869  N   GLU A 611     3518   2305   2758   -291     31    193       N
ATOM   4870  CA  GLU A 611       1.972  26.674  13.270  1.00 25.97           C
ANISOU 4870  CA  GLU A 611     3963   2739   3163   -277     44    162       C
ATOM   4871  C   GLU A 611       3.032  26.287  14.287  1.00 23.86           C
ANISOU 4871  C   GLU A 611     3707   2468   2890   -283     35    157       C
ATOM   4872  O   GLU A 611       2.783  26.309  15.498  1.00 20.61           O
ANISOU 4872  O   GLU A 611     3314   2051   2467   -270     31    132       O
ATOM   4873  CB  GLU A 611       1.184  25.429  12.849  1.00 20.92           C
ANISOU 4873  CB  GLU A 611     3314   2131   2502   -272     79    158       C
ATOM   4874  CG  GLU A 611      -0.065  25.702  12.016  1.00 20.09           C
ANISOU 4874  CG  GLU A 611     3200   2036   2399   -263     90    156       C
ATOM   4875  CD  GLU A 611      -1.046  26.662  12.687  1.00 27.65           C
ANISOU 4875  CD  GLU A 611     4172   2973   3361   -245     79    135       C
ATOM   4876  OE1 GLU A 611      -1.258  26.559  13.914  1.00 26.88           O
ANISOU 4876  OE1 GLU A 611     4093   2867   3252   -234     80    111       O
ATOM   4877  OE2 GLU A 611      -1.610  27.520  11.972  1.00 25.91           O
ANISOU 4877  OE2 GLU A 611     3945   2746   3155   -241     71    143       O
ATOM   4878  N   LEU A 612       4.211  25.890  13.812  1.00 25.16           N
ANISOU 4878  N   LEU A 612     3859   2639   3062   -301     33    181       N
ATOM   4879  CA  LEU A 612       5.313  25.616  14.722  1.00 20.14           C
ANISOU 4879  CA  LEU A 612     3231   1998   2423   -307     20    179       C
ATOM   4880  C   LEU A 612       5.669  26.857  15.528  1.00 24.87           C
ANISOU 4880  C   LEU A 612     3844   2566   3040   -305    -15    166       C
ATOM   4881  O   LEU A 612       5.795  26.805  16.760  1.00 28.91           O
ANISOU 4881  O   LEU A 612     4372   3073   3537   -296    -25    143       O
ATOM   4882  CB  LEU A 612       6.517  25.129  13.929  1.00 22.83           C
ANISOU 4882  CB  LEU A 612     3553   2349   2774   -327     22    210       C
ATOM   4883  CG  LEU A 612       7.752  24.891  14.782  1.00 30.39           C
ANISOU 4883  CG  LEU A 612     4515   3301   3732   -334      6    212       C
ATOM   4884  CD1 LEU A 612       7.495  23.698  15.693  1.00 30.21           C
ANISOU 4884  CD1 LEU A 612     4502   3297   3680   -323     28    196       C
ATOM   4885  CD2 LEU A 612       8.939  24.635  13.862  1.00 33.57           C
ANISOU 4885  CD2 LEU A 612     4896   3709   4149   -354      6    245       C
ATOM   4886  N   ARG A 613       5.835  27.988  14.838  1.00 23.26           N
ANISOU 4886  N   ARG A 613     3632   2339   2865   -313    -36    180       N
ATOM   4887  CA  ARG A 613       6.101  29.246  15.529  1.00 24.06           C
ANISOU 4887  CA  ARG A 613     3745   2406   2991   -312    -70    165       C
ATOM   4888  C   ARG A 613       4.976  29.591  16.494  1.00 23.08           C
ANISOU 4888  C   ARG A 613     3642   2275   2852   -289    -71    127       C
ATOM   4889  O   ARG A 613       5.232  30.001  17.631  1.00 25.43           O
ANISOU 4889  O   ARG A 613     3955   2558   3147   -282    -92    100       O
ATOM   4890  CB  ARG A 613       6.302  30.364  14.507  1.00 19.92           C
ANISOU 4890  CB  ARG A 613     3206   1859   2505   -323    -87    190       C
ATOM   4891  CG  ARG A 613       7.466  30.120  13.553  1.00 25.64           C
ANISOU 4891  CG  ARG A 613     3908   2590   3245   -344    -87    230       C
ATOM   4892  CD  ARG A 613       7.348  31.025  12.328  1.00 37.46           C
ANISOU 4892  CD  ARG A 613     5387   4075   4772   -351    -91    261       C
ATOM   4893  NE  ARG A 613       8.619  31.202  11.637  1.00 52.35           N
ANISOU 4893  NE  ARG A 613     7253   5956   6683   -371   -101    299       N
ATOM   4894  CZ  ARG A 613       9.282  32.354  11.581  1.00 64.60           C
ANISOU 4894  CZ  ARG A 613     8797   7472   8277   -382   -129    313       C
ATOM   4895  NH1 ARG A 613       8.790  33.438  12.171  1.00 65.89           N
ANISOU 4895  NH1 ARG A 613     8972   7600   8464   -374   -152    291       N
ATOM   4896  NH2 ARG A 613      10.434  32.423  10.929  1.00 66.68           N
ANISOU 4896  NH2 ARG A 613     9039   7734   8562   -401   -135    350       N
ATOM   4897  N   ALA A 614       3.720  29.417  16.063  1.00 20.89           N
ANISOU 4897  N   ALA A 614     3363   2009   2563   -276    -48    122       N
ATOM   4898  CA  ALA A 614       2.593  29.795  16.917  1.00 20.41           C
ANISOU 4898  CA  ALA A 614     3322   1943   2491   -253    -46     88       C
ATOM   4899  C   ALA A 614       2.554  28.968  18.196  1.00 26.83           C
ANISOU 4899  C   ALA A 614     4151   2774   3270   -241    -36     63       C
ATOM   4900  O   ALA A 614       2.306  29.503  19.284  1.00 24.06           O
ANISOU 4900  O   ALA A 614     3819   2412   2913   -226    -51     32       O
ATOM   4901  CB  ALA A 614       1.277  29.650  16.148  1.00 19.83           C
ANISOU 4901  CB  ALA A 614     3240   1881   2411   -243    -21     91       C
ATOM   4902  N   LEU A 615       2.788  27.654  18.089  1.00 19.61           N
ANISOU 4902  N   LEU A 615     3230   1889   2333   -246    -11     76       N
ATOM   4903  CA  LEU A 615       2.814  26.830  19.291  1.00 18.92           C
ANISOU 4903  CA  LEU A 615     3156   1819   2214   -234     -0     59       C
ATOM   4904  C   LEU A 615       3.972  27.213  20.200  1.00 19.24           C
ANISOU 4904  C   LEU A 615     3206   1849   2257   -238    -31     51       C
ATOM   4905  O   LEU A 615       3.810  27.278  21.425  1.00 22.69           O
ANISOU 4905  O   LEU A 615     3660   2289   2672   -221    -38     24       O
ATOM   4906  CB  LEU A 615       2.908  25.351  18.917  1.00 16.49           C
ANISOU 4906  CB  LEU A 615     2836   1540   1890   -239     33     79       C
ATOM   4907  CG  LEU A 615       3.065  24.361  20.068  1.00 18.63           C
ANISOU 4907  CG  LEU A 615     3117   1832   2131   -228     47     71       C
ATOM   4908  CD1 LEU A 615       1.868  24.400  21.015  1.00 22.45           C
ANISOU 4908  CD1 LEU A 615     3617   2322   2593   -203     60     44       C
ATOM   4909  CD2 LEU A 615       3.271  22.947  19.486  1.00 19.15           C
ANISOU 4909  CD2 LEU A 615     3165   1919   2191   -238     78     94       C
ATOM   4910  N   LYS A 616       5.151  27.464  19.618  1.00 22.98           N
ANISOU 4910  N   LYS A 616     3667   2310   2753   -260    -51     73       N
ATOM   4911  CA  LYS A 616       6.282  27.958  20.402  1.00 25.84           C
ANISOU 4911  CA  LYS A 616     4036   2659   3124   -266    -84     64       C
ATOM   4912  C   LYS A 616       5.888  29.195  21.198  1.00 24.49           C
ANISOU 4912  C   LYS A 616     3881   2463   2961   -253   -112     28       C
ATOM   4913  O   LYS A 616       6.178  29.309  22.395  1.00 21.46           O
ANISOU 4913  O   LYS A 616     3511   2081   2560   -242   -130      2       O
ATOM   4914  CB  LYS A 616       7.454  28.294  19.480  1.00 31.04           C
ANISOU 4914  CB  LYS A 616     4675   3302   3817   -292   -102     95       C
ATOM   4915  CG  LYS A 616       8.641  27.372  19.582  1.00 44.22           C
ANISOU 4915  CG  LYS A 616     6335   4988   5478   -305   -100    114       C
ATOM   4916  CD  LYS A 616       9.671  27.745  18.533  1.00 49.77           C
ANISOU 4916  CD  LYS A 616     7017   5677   6217   -330   -113    147       C
ATOM   4917  CE  LYS A 616      10.619  26.598  18.235  1.00 51.91           C
ANISOU 4917  CE  LYS A 616     7273   5971   6479   -342    -98    174       C
ATOM   4918  NZ  LYS A 616      11.584  26.978  17.169  1.00 52.84           N
ANISOU 4918  NZ  LYS A 616     7369   6077   6630   -365   -108    208       N
ATOM   4919  N   GLN A 617       5.214  30.132  20.536  1.00 26.43           N
ANISOU 4919  N   GLN A 617     4124   2685   3234   -252   -117     27       N
ATOM   4920  CA  GLN A 617       4.865  31.387  21.187  1.00 20.15           C
ANISOU 4920  CA  GLN A 617     3342   1861   2454   -240   -145     -7       C
ATOM   4921  C   GLN A 617       3.856  31.170  22.310  1.00 24.32           C
ANISOU 4921  C   GLN A 617     3891   2406   2945   -211   -133    -43       C
ATOM   4922  O   GLN A 617       3.991  31.754  23.396  1.00 29.55           O
ANISOU 4922  O   GLN A 617     4568   3058   3600   -199   -157    -79       O
ATOM   4923  CB  GLN A 617       4.320  32.365  20.149  1.00 22.43           C
ANISOU 4923  CB  GLN A 617     3620   2122   2781   -244   -149      6       C
ATOM   4924  CG  GLN A 617       3.965  33.741  20.721  1.00 25.73           C
ANISOU 4924  CG  GLN A 617     4049   2503   3224   -233   -178    -28       C
ATOM   4925  CD  GLN A 617       5.188  34.548  21.114  1.00 32.51           C
ANISOU 4925  CD  GLN A 617     4906   3331   4114   -247   -219    -37       C
ATOM   4926  OE1 GLN A 617       6.321  34.178  20.812  1.00 35.68           O
ANISOU 4926  OE1 GLN A 617     5296   3737   4525   -268   -226    -12       O
ATOM   4927  NE2 GLN A 617       4.963  35.653  21.797  1.00 32.65           N
ANISOU 4927  NE2 GLN A 617     4935   3318   4153   -236   -246    -74       N
ATOM   4928  N   ARG A 618       2.834  30.346  22.070  1.00 20.76           N
ANISOU 4928  N   ARG A 618     3439   1979   2469   -200    -95    -37       N
ATOM   4929  CA  ARG A 618       1.840  30.118  23.117  1.00 23.16           C
ANISOU 4929  CA  ARG A 618     3761   2300   2738   -172    -80    -68       C
ATOM   4930  C   ARG A 618       2.453  29.421  24.326  1.00 26.22           C
ANISOU 4930  C   ARG A 618     4159   2713   3090   -163    -82    -80       C
ATOM   4931  O   ARG A 618       2.095  29.735  25.468  1.00 28.25           O
ANISOU 4931  O   ARG A 618     4434   2975   3324   -141    -90   -114       O
ATOM   4932  CB  ARG A 618       0.660  29.317  22.574  1.00 24.27           C
ANISOU 4932  CB  ARG A 618     3894   2462   2863   -163    -39    -55       C
ATOM   4933  CG  ARG A 618      -0.112  30.033  21.498  1.00 21.46           C
ANISOU 4933  CG  ARG A 618     3529   2088   2538   -166    -37    -47       C
ATOM   4934  CD  ARG A 618      -1.356  29.266  21.112  1.00 21.37           C
ANISOU 4934  CD  ARG A 618     3512   2099   2510   -154      1    -41       C
ATOM   4935  NE  ARG A 618      -1.037  27.904  20.661  1.00 25.75           N
ANISOU 4935  NE  ARG A 618     4054   2681   3050   -167     28    -15       N
ATOM   4936  CZ  ARG A 618      -0.991  27.533  19.386  1.00 26.51           C
ANISOU 4936  CZ  ARG A 618     4130   2782   3160   -183     39     13       C
ATOM   4937  NH1 ARG A 618      -1.237  28.425  18.438  1.00 23.10           N
ANISOU 4937  NH1 ARG A 618     3689   2332   2756   -189     27     22       N
ATOM   4938  NH2 ARG A 618      -0.701  26.274  19.057  1.00 25.75           N
ANISOU 4938  NH2 ARG A 618     4023   2710   3052   -193     63     31       N
ATOM   4939  N   ILE A 619       3.385  28.486  24.105  1.00 26.60           N
ANISOU 4939  N   ILE A 619     4198   2778   3132   -179    -75    -52       N
ATOM   4940  CA  ILE A 619       4.068  27.842  25.226  1.00 28.96           C
ANISOU 4940  CA  ILE A 619     4505   3100   3399   -172    -80    -59       C
ATOM   4941  C   ILE A 619       4.938  28.846  25.976  1.00 29.87           C
ANISOU 4941  C   ILE A 619     4629   3197   3523   -173   -125    -86       C
ATOM   4942  O   ILE A 619       5.005  28.829  27.210  1.00 29.83           O
ANISOU 4942  O   ILE A 619     4639   3208   3487   -154   -135   -113       O
ATOM   4943  CB  ILE A 619       4.893  26.633  24.742  1.00 30.27           C
ANISOU 4943  CB  ILE A 619     4656   3285   3562   -190    -62    -22       C
ATOM   4944  CG1 ILE A 619       3.976  25.518  24.241  1.00 22.33           C
ANISOU 4944  CG1 ILE A 619     3642   2301   2542   -185    -16     -3       C
ATOM   4945  CG2 ILE A 619       5.761  26.058  25.870  1.00 28.13           C
ANISOU 4945  CG2 ILE A 619     4391   3036   3261   -183    -71    -25       C
ATOM   4946  CD1 ILE A 619       4.719  24.508  23.363  1.00 29.21           C
ANISOU 4946  CD1 ILE A 619     4494   3181   3423   -206      0     34       C
ATOM   4947  N   SER A 620       5.624  29.728  25.252  1.00 30.70           N
ANISOU 4947  N   SER A 620     4724   3268   3672   -195   -153    -79       N
ATOM   4948  CA  SER A 620       6.457  30.723  25.917  1.00 30.46           C
ANISOU 4948  CA  SER A 620     4700   3216   3658   -198   -198   -106       C
ATOM   4949  C   SER A 620       5.651  31.648  26.820  1.00 32.35           C
ANISOU 4949  C   SER A 620     4957   3445   3889   -173   -213   -155       C
ATOM   4950  O   SER A 620       6.226  32.267  27.720  1.00 38.10           O
ANISOU 4950  O   SER A 620     5695   4166   4617   -168   -248   -188       O
ATOM   4951  CB  SER A 620       7.221  31.557  24.880  1.00 36.35           C
ANISOU 4951  CB  SER A 620     5427   3923   4459   -226   -223    -86       C
ATOM   4952  OG  SER A 620       6.361  32.504  24.274  1.00 37.22           O
ANISOU 4952  OG  SER A 620     5537   4005   4600   -223   -224    -93       O
ATOM   4953  N   GLN A 621       4.339  31.759  26.606  1.00 30.65           N
ANISOU 4953  N   GLN A 621     4748   3229   3668   -157   -189   -162       N
ATOM   4954  CA  GLN A 621       3.512  32.677  27.377  1.00 38.14           C
ANISOU 4954  CA  GLN A 621     5713   4166   4612   -132   -201   -208       C
ATOM   4955  C   GLN A 621       2.875  32.047  28.609  1.00 42.58           C
ANISOU 4955  C   GLN A 621     6293   4768   5118   -101   -182   -233       C
ATOM   4956  O   GLN A 621       2.292  32.775  29.419  1.00 42.77           O
ANISOU 4956  O   GLN A 621     6333   4788   5131    -77   -194   -276       O
ATOM   4957  CB  GLN A 621       2.409  33.267  26.493  1.00 44.16           C
ANISOU 4957  CB  GLN A 621     6471   4905   5403   -129   -186   -203       C
ATOM   4958  CG  GLN A 621       2.928  34.174  25.386  1.00 49.21           C
ANISOU 4958  CG  GLN A 621     7094   5502   6101   -154   -209   -183       C
ATOM   4959  CD  GLN A 621       3.789  35.308  25.913  1.00 47.37           C
ANISOU 4959  CD  GLN A 621     6864   5234   5899   -161   -256   -213       C
ATOM   4960  OE1 GLN A 621       4.959  35.436  25.545  1.00 49.16           O
ANISOU 4960  OE1 GLN A 621     7079   5447   6154   -185   -278   -194       O
ATOM   4961  NE2 GLN A 621       3.214  36.142  26.773  1.00 40.04           N
ANISOU 4961  NE2 GLN A 621     5952   4293   4970   -138   -272   -261       N
ATOM   4962  N   MET A 622       2.950  30.732  28.780  1.00 38.90           N
ANISOU 4962  N   MET A 622     5824   4340   4615    -99   -152   -207       N
ATOM   4963  CA  MET A 622       2.344  30.129  29.966  1.00 41.96           C
ANISOU 4963  CA  MET A 622     6228   4767   4949    -68   -133   -226       C
ATOM   4964  C   MET A 622       3.277  30.232  31.181  1.00 48.01           C
ANISOU 4964  C   MET A 622     7004   5551   5688    -59   -163   -252       C
ATOM   4965  O   MET A 622       4.443  30.626  31.076  1.00 48.54           O
ANISOU 4965  O   MET A 622     7066   5601   5778    -79   -198   -252       O
ATOM   4966  CB  MET A 622       1.951  28.668  29.694  1.00 44.08           C
ANISOU 4966  CB  MET A 622     6487   5068   5192    -67    -86   -187       C
ATOM   4967  CG  MET A 622       3.083  27.763  29.329  1.00 39.53           C
ANISOU 4967  CG  MET A 622     5898   4502   4619    -90    -84   -150       C
ATOM   4968  SD  MET A 622       2.506  26.198  28.639  1.00 34.29           S
ANISOU 4968  SD  MET A 622     5220   3864   3946    -94    -29   -105       S
ATOM   4969  CE  MET A 622       1.411  25.632  29.943  1.00 36.02           C
ANISOU 4969  CE  MET A 622     5453   4120   4112    -55      2   -122       C
ATOM   4970  OXT MET A 622       2.882  29.952  32.315  1.00 46.38           O
ANISOU 4970  OXT MET A 622     6811   5377   5434    -30   -155   -274       O
TER
HETATM 4971 MN    MN A 700      -1.801  -0.692   9.715  1.00 19.23          Mn
HETATM 4972 MN    MN A 701      -3.548  27.943   2.763  1.00 83.94          Mn
HETATM 4973  O   HOH S   1     -18.579  17.949  23.820  1.00 24.68           O
HETATM 4974  O   HOH S   2     -15.149  -4.668  20.394  1.00 24.28           O
HETATM 4975  O   HOH S   3     -13.731 -10.996   3.263  1.00 21.83           O
HETATM 4976  O   HOH S   4      -3.561   8.526  28.586  1.00 21.45           O
HETATM 4977  O   HOH S   5       5.757  11.026  26.156  1.00 23.01           O
HETATM 4978  O   HOH S   6       6.558  13.943  14.066  1.00 20.88           O
HETATM 4979  O   HOH S   7      -1.748  11.988  -0.721  1.00 22.26           O
HETATM 4980  O   HOH S   8       0.852  -4.322   1.163  1.00 17.79           O
HETATM 4981  O   HOH S   9      -0.540  28.250   9.864  1.00 29.80           O
HETATM 4982  O   HOH S  10       0.711  15.855  20.986  1.00 19.12           O
HETATM 4983  O   HOH S  11      -0.049  26.037  16.134  1.00 26.77           O
HETATM 4984  O   HOH S  12      14.924  19.945   1.197  1.00 31.17           O
HETATM 4985  O   HOH S  13     -16.125  -9.139   3.782  1.00 19.56           O
HETATM 4986  O   HOH S  14      -0.747 -13.494  28.845  1.00 41.96           O
HETATM 4987  O   HOH S  15       1.421  11.917  18.711  1.00 20.71           O
HETATM 4988  O   HOH S  16      11.758   9.138  14.672  1.00 28.85           O
HETATM 4989  O   HOH S  17      -9.062  -0.857   6.479  1.00 25.48           O
HETATM 4990  O   HOH S  18      -3.407   6.168  30.058  1.00 23.66           O
HETATM 4991  O   HOH S  19      -3.948  14.082  22.963  1.00 18.21           O
HETATM 4992  O   HOH S  20       4.607   3.380  18.869  1.00 23.32           O
HETATM 4993  O   HOH S  21     -23.229   3.976  15.073  1.00 24.89           O
HETATM 4994  O   HOH S  22     -16.264   2.084   2.776  1.00 28.64           O
HETATM 4995  O   HOH S  23     -15.567  -1.383   1.544  1.00 26.93           O
HETATM 4996  O   HOH S  24      -1.290  31.195  18.569  1.00 27.92           O
HETATM 4997  O   HOH S  25       4.457  15.622  19.300  1.00 21.66           O
HETATM 4998  O   HOH S  26       4.610  -2.817   2.919  1.00 20.14           O
HETATM 4999  O   HOH S  27       7.293  -3.610   3.520  1.00 22.49           O
HETATM 5000  O   HOH S  28       0.513  19.432  19.109  1.00 25.44           O
HETATM 5001  O   HOH S  29       3.079  13.516  20.743  1.00 23.08           O
HETATM 5002  O   HOH S  30       8.315   5.259 -10.659  1.00 35.43           O
HETATM 5003  O   HOH S  31       2.214  17.377  19.167  1.00 22.07           O
HETATM 5004  O   HOH S  32     -25.853  16.791  15.219  1.00 29.41           O
HETATM 5005  O   HOH S  33     -18.133  21.550  32.331  1.00 49.32           O
HETATM 5006  O   HOH S  34      -7.863   2.082  20.746  1.00 20.67           O
HETATM 5007  O   HOH S  35     -15.872  26.436  32.307  1.00 56.25           O
HETATM 5008  O   HOH S  36      -3.487   5.659  19.786  1.00 20.01           O
HETATM 5009  O   HOH S  39       5.980 -24.414   0.628  1.00 36.19           O
HETATM 5010  O   HOH S  41       7.899  10.594  -9.864  1.00 41.10           O
HETATM 5011  O   HOH S  43      -0.756  10.289  21.805  1.00 17.89           O
HETATM 5012  O   HOH S  44     -14.136  -1.903  23.041  1.00 28.21           O
HETATM 5013  O   HOH S  45       1.550  13.888  19.687  1.00 38.34           O
HETATM 5014  O   HOH S  46     -25.578  19.470  14.659  1.00 27.52           O
HETATM 5015  O   HOH S  47       0.958  15.559  17.278  1.00 21.24           O
HETATM 5016  O   HOH S  48       6.464   4.074  14.324  1.00 51.92           O
HETATM 5017  O   HOH S  49       8.378  -9.645  -0.279  1.00 29.39           O
HETATM 5018  O   HOH S  50     -10.628   2.112   7.481  1.00 23.46           O
HETATM 5019  O   HOH S  51     -13.008 -11.864  -2.449  1.00 24.15           O
HETATM 5020  O   HOH S  52      -3.367 -13.844   6.365  1.00 22.17           O
HETATM 5021  O   HOH S  53       8.318  11.250   1.890  1.00 21.36           O
HETATM 5022  O   HOH S  54      -2.910   8.650   7.895  1.00 14.63           O
HETATM 5023  O   HOH S  55      -3.178   7.242  21.927  1.00 21.33           O
HETATM 5024  O   HOH S  56     -20.917  11.793   9.641  1.00 18.84           O
HETATM 5025  O   HOH S  57     -10.368   2.372  21.935  1.00 25.71           O
HETATM 5026  O   HOH S  58      11.929 -21.072   5.347  1.00 30.72           O
HETATM 5027  O   HOH S  59     -10.737  -2.985   7.227  1.00 25.95           O
HETATM 5028  O   HOH S  61     -24.584  14.535  -3.130  1.00 38.28           O
HETATM 5029  O   HOH S  63      -7.079  -4.379   8.228  1.00 21.47           O
HETATM 5030  O   HOH S  64      -4.176  -4.280   9.539  1.00 23.72           O
HETATM 5031  O   HOH S  65       0.665 -22.750  16.645  1.00 27.44           O
HETATM 5032  O   HOH S  66      -3.320 -14.360   9.177  1.00 18.50           O
HETATM 5033  O   HOH S  68     -17.791  12.344  27.885  1.00 23.85           O
HETATM 5034  O   HOH S  70      -6.455  -4.479 -21.530  1.00 32.29           O
HETATM 5035  O   HOH S  71      13.650  18.589  -0.870  1.00 23.64           O
HETATM 5036  O   HOH S  72      -7.170  -4.043 -18.915  1.00 34.72           O
HETATM 5037  O   HOH S  73     -16.160 -22.965  -9.839  1.00 60.04           O
HETATM 5038  O   HOH S  75     -10.439 -30.417  28.876  1.00 31.04           O
HETATM 5039  O   HOH S  76      -2.376  28.249  15.803  1.00 38.12           O
HETATM 5040  O   HOH S  77      17.714  12.398  -7.527  1.00 30.84           O
HETATM 5041  O   HOH S  78       4.034   5.796  -4.809  1.00 24.81           O
HETATM 5042  O   HOH S  79      13.394  13.497   4.224  1.00 24.91           O
HETATM 5043  O   HOH S  80      20.824  10.774   9.636  1.00 26.80           O
HETATM 5044  O   HOH S  81     -15.971  25.464  24.886  1.00 30.29           O
HETATM 5045  O   HOH S  82     -17.029   4.262 -10.720  1.00 54.50           O
HETATM 5046  O   HOH S  83     -11.411  -4.632  -1.350  1.00 22.28           O
HETATM 5047  O   HOH S  84     -24.810   9.272   0.866  1.00 38.92           O
HETATM 5048  O   HOH S  85     -11.478   5.035  -9.335  1.00 46.40           O
HETATM 5049  O   HOH S  87     -11.896 -24.951  11.366  1.00 35.01           O
HETATM 5050  O   HOH S  88      -4.395  31.891  20.928  1.00 51.09           O
HETATM 5051  O   HOH S  90      -7.536  16.373  27.858  1.00 36.03           O
HETATM 5052  O   HOH S  91      -6.882  20.841  32.569  1.00 45.46           O
HETATM 5053  O   HOH S  92      -9.166  20.192  33.323  1.00 55.97           O
HETATM 5054  O   HOH S  93     -21.592  14.707  29.950  1.00 40.99           O
HETATM 5055  O   HOH S  94      -6.572   2.736  34.811  1.00 54.59           O
HETATM 5056  O   HOH S  95       0.527  -1.536  25.762  1.00 33.53           O
HETATM 5057  O   HOH S  96       9.282 -12.173  20.916  1.00 59.75           O
HETATM 5058  O   HOH S  97      12.611 -11.837  11.832  1.00 46.74           O
HETATM 5059  O   HOH S  98      -7.090  -5.424  29.817  1.00 50.00           O
HETATM 5060  O   HOH S  99       8.142   1.120   4.720  1.00 21.27           O
HETATM 5061  O   HOH S 100      -2.842  10.573   1.268  1.00 20.58           O
HETATM 5062  O   HOH S 101       6.595   4.635   2.054  1.00 19.85           O
HETATM 5063  O   HOH S 102       7.391  -1.143   5.313  1.00 26.86           O
HETATM 5064  O   HOH S 103       9.557 -19.136  -5.300  1.00 25.34           O
HETATM 5065  O   HOH S 104      -0.588  21.859  19.546  1.00 22.95           O
HETATM 5066  O   HOH S 105      -6.328  -5.165   1.796  1.00 20.19           O
HETATM 5067  O   HOH S 106       7.571   6.461   3.956  1.00 26.83           O
HETATM 5068  O   HOH S 107      10.438   2.300   3.022  1.00 27.44           O
HETATM 5069  O   HOH S 108      10.138   5.312   5.983  1.00 63.55           O
HETATM 5070  O   HOH S 109       5.384   0.632  11.806  1.00 38.23           O
HETATM 5071  O   HOH S 110       2.674   3.863  11.247  1.00 24.04           O
HETATM 5072  O   HOH S 111      11.000  11.654 -10.632  1.00 33.79           O
HETATM 5073  O   HOH S 112      16.049  14.781  -6.375  1.00 27.65           O
HETATM 5074  O   HOH S 113     -11.335 -18.217  -4.331  1.00 25.82           O
HETATM 5075  O   HOH S 114       2.775  19.536  -6.305  1.00 49.72           O
HETATM 5076  O   HOH S 115      -2.192  18.801  -4.145  1.00 38.88           O
HETATM 5077  O   HOH S 116      -0.986  23.898   0.213  1.00 25.38           O
HETATM 5078  O   HOH S 117       3.888  24.080   0.131  1.00 33.36           O
HETATM 5079  O   HOH S 118       5.946  21.558   0.147  1.00 43.68           O
HETATM 5080  O   HOH S 119       8.674  28.901   4.337  1.00 39.46           O
HETATM 5081  O   HOH S 120      12.481  24.702   9.576  1.00 39.37           O
HETATM 5082  O   HOH S 121      14.083  25.667  17.863  1.00 86.06           O
HETATM 5083  O   HOH S 122       1.249 -12.626   7.119  1.00 23.73           O
HETATM 5084  O   HOH S 123       5.324 -18.098   2.430  1.00 29.26           O
HETATM 5085  O   HOH S 124       7.104   8.881  -5.246  1.00 22.28           O
HETATM 5086  O   HOH S 125       3.144 -21.928  -5.878  1.00 24.10           O
HETATM 5087  O   HOH S 126       1.025 -23.630  -5.091  1.00 25.39           O
HETATM 5088  O   HOH S 127      -4.359  -6.634   0.137  1.00 27.07           O
HETATM 5089  O   HOH S 128      -0.661 -30.196  -2.761  1.00 60.26           O
HETATM 5090  O   HOH S 129       9.744  10.236  10.597  1.00 31.77           O
HETATM 5091  O   HOH S 130      17.252  -7.284  -0.060  1.00 40.33           O
HETATM 5092  O   HOH S 131       2.519 -25.142  -7.304  1.00 52.44           O
HETATM 5093  O   HOH S 132       4.730 -26.399  -5.940  1.00 47.41           O
HETATM 5094  O   HOH S 133      -1.575 -24.757  -7.954  1.00 25.62           O
HETATM 5095  O   HOH S 134     -11.201  24.128  17.097  1.00 26.29           O
HETATM 5096  O   HOH S 135     -10.219  21.194  14.436  1.00 22.47           O
HETATM 5097  O   HOH S 136      16.330   7.045 -10.944  1.00 42.51           O
HETATM 5098  O   HOH S 137      24.480  18.275  10.951  1.00 21.36           O
HETATM 5099  O   HOH S 138     -17.004  18.610  11.671  1.00 23.14           O
HETATM 5100  O   HOH S 139      17.135  20.192  12.474  1.00 24.10           O
HETATM 5101  O   HOH S 140      11.658 -13.174   4.387  1.00 29.90           O
HETATM 5102  O   HOH S 141      24.899  18.954   8.336  1.00 25.89           O
HETATM 5103  O   HOH S 142     -10.333 -18.145 -13.862  1.00 23.15           O
HETATM 5104  O   HOH S 143     -27.308  15.294  19.574  1.00 27.26           O
HETATM 5105  O   HOH S 144     -18.277  14.988  27.075  1.00 24.05           O
HETATM 5106  O   HOH S 145     -10.559  15.681  -1.658  1.00 27.69           O
HETATM 5107  O   HOH S 146      16.846  14.224  11.902  1.00 27.33           O
HETATM 5108  O   HOH S 147      -7.784  -6.408  18.471  1.00 23.79           O
HETATM 5109  O   HOH S 148      10.022   5.544   0.045  1.00 19.99           O
HETATM 5110  O   HOH S 149       3.681 -22.294   6.655  1.00 31.12           O
HETATM 5111  O   HOH S 150       3.363  -6.639   9.737  1.00 22.62           O
HETATM 5112  O   HOH S 151       7.282   0.467   9.831  1.00 27.71           O
HETATM 5113  O   HOH S 152      -9.629  26.027   9.676  1.00 21.94           O
HETATM 5114  O   HOH S 153      -6.223  -6.553  16.151  1.00 22.61           O
HETATM 5115  O   HOH S 154      -5.624   3.514  28.270  1.00 24.81           O
HETATM 5116  O   HOH S 155       4.224 -12.664  13.378  1.00 26.99           O
HETATM 5117  O   HOH S 156       8.822  16.723  25.209  1.00 26.56           O
HETATM 5118  O   HOH S 157       9.803 -10.165   6.825  1.00 33.98           O
HETATM 5119  O   HOH S 158      15.964 -20.430   3.919  1.00 33.45           O
HETATM 5120  O   HOH S 159     -10.670 -13.271  25.740  1.00 29.96           O
HETATM 5121  O   HOH S 160       3.513  13.786  32.111  1.00 31.30           O
HETATM 5122  O   HOH S 161     -25.948  10.785   2.657  1.00 29.58           O
HETATM 5123  O   HOH S 162      16.901  21.099  -0.283  1.00 27.76           O
HETATM 5124  O   HOH S 163       1.991  -5.987  17.800  1.00 31.48           O
HETATM 5125  O   HOH S 164     -16.847  16.570   5.814  1.00 28.53           O
HETATM 5126  O   HOH S 165      15.481 -17.717  -9.619  1.00 30.82           O
HETATM 5127  O   HOH S 166      -0.774  -6.625  20.941  1.00 28.67           O
HETATM 5128  O   HOH S 167     -18.724   3.650   2.199  1.00 26.38           O
HETATM 5129  O   HOH S 168     -13.734 -13.086   1.896  1.00 30.89           O
HETATM 5130  O   HOH S 169       8.405   7.894   0.375  1.00 28.05           O
HETATM 5131  O   HOH S 170      15.200 -21.006 -11.061  1.00 28.38           O
HETATM 5132  O   HOH S 171       5.460 -21.891   2.016  1.00 35.29           O
HETATM 5133  O   HOH S 172     -11.203 -15.420 -13.360  1.00 30.80           O
HETATM 5134  O   HOH S 173     -12.051   0.186  22.236  1.00 32.09           O
HETATM 5135  O   HOH S 174       4.277 -23.764  -4.796  1.00 35.14           O
HETATM 5136  O   HOH S 175       8.291 -24.798  -0.808  1.00 40.51           O
HETATM 5137  O   HOH S 176       3.272 -16.359   1.569  1.00 33.25           O
HETATM 5138  O   HOH S 177       4.854 -20.350  -1.760  1.00 40.49           O
HETATM 5139  O   HOH S 178       8.767 -24.204 -13.871  1.00 28.54           O
HETATM 5140  O   HOH S 179      12.058 -27.190 -11.105  1.00 46.76           O
HETATM 5141  O   HOH S 180      15.300 -23.500 -10.034  1.00 36.89           O
HETATM 5142  O   HOH S 181      16.771 -23.794  -7.533  1.00 34.20           O
HETATM 5143  O   HOH S 182      17.342 -20.141  -9.597  1.00 32.10           O
HETATM 5144  O   HOH S 183      14.950 -16.506  -7.245  1.00 38.37           O
HETATM 5145  O   HOH S 184      17.066 -19.990  -5.093  1.00 32.49           O
HETATM 5146  O   HOH S 185      15.244 -22.038  -3.898  1.00 30.10           O
HETATM 5147  O   HOH S 186      15.134 -22.005  -0.951  1.00 36.54           O
HETATM 5148  O   HOH S 187      13.756 -22.495   0.954  1.00 35.01           O
HETATM 5149  O   HOH S 188      19.212 -15.959   0.126  1.00 41.17           O
HETATM 5150  O   HOH S 189      21.628  -7.816 -11.254  1.00 36.27           O
HETATM 5151  O   HOH S 190      14.999  -6.406 -16.040  1.00 50.25           O
HETATM 5152  O   HOH S 191       4.809  -5.678 -17.047  1.00 46.34           O
HETATM 5153  O   HOH S 192      -5.461  -1.336  11.886  1.00 24.90           O
HETATM 5154  O   HOH S 194     -19.744  16.828   6.320  1.00 28.62           O
HETATM 5155  O   HOH S 195       8.869   3.226   1.092  1.00 25.61           O
HETATM 5156  O   HOH S 196      12.311 -11.139   6.061  1.00 30.44           O
HETATM 5157  O   HOH S 197      14.529  -9.744   5.392  1.00 34.96           O
HETATM 5158  O   HOH S 198      10.260 -10.278   9.452  1.00 29.92           O
HETATM 5159  O   HOH S 199      -0.031  -4.734  19.332  1.00 30.17           O
HETATM 5160  O   HOH S 200       2.511  -9.963  22.623  1.00 28.15           O
HETATM 5161  O   HOH S 201     -10.939  26.885   5.435  1.00 34.44           O
HETATM 5162  O   HOH S 202     -12.980  26.121   1.196  1.00 35.82           O
HETATM 5163  O   HOH S 203      -9.360  26.781   7.065  1.00 29.08           O
HETATM 5164  O   HOH S 204      -4.564  25.620   4.433  1.00 34.18           O
HETATM 5165  O   HOH S 205     -10.400  21.609  11.191  1.00 32.44           O
HETATM 5166  O   HOH S 206     -14.244  21.908  11.962  1.00 49.58           O
HETATM 5167  O   HOH S 207     -21.235  20.148  12.238  1.00 26.25           O
HETATM 5168  O   HOH S 208     -25.269  21.865  16.064  1.00 31.35           O
HETATM 5169  O   HOH S 209     -22.961  18.671  13.946  1.00 34.73           O
HETATM 5170  O   HOH S 210     -14.701  26.346  18.875  1.00 40.61           O
HETATM 5171  O   HOH S 211     -14.987  26.855  21.286  1.00 45.68           O
HETATM 5172  O   HOH S 212      16.103 -27.836   1.565  1.00 44.97           O
HETATM 5173  O   HOH S 213       2.742  18.291  29.795  1.00 37.46           O
HETATM 5174  O   HOH S 214     -27.491  11.602  12.190  1.00 24.21           O
HETATM 5175  O   HOH S 215     -23.641  18.775   1.947  1.00 28.46           O
HETATM 5176  O   HOH S 216      20.142  15.501  10.885  1.00 34.67           O
HETATM 5177  O   HOH S 217       3.236  -4.702  10.537  1.00 42.54           O
HETATM 5178  O   HOH S 218     -12.888 -15.417   1.888  1.00 34.06           O
HETATM 5179  O   HOH S 219      19.074  19.855  10.340  1.00 32.29           O
HETATM 5180  O   HOH S 220      19.504  22.201   2.794  1.00 30.44           O
HETATM 5181  O   HOH S 221       2.076  11.769  33.072  1.00 35.46           O
HETATM 5182  O   HOH S 222     -23.865  -2.752  12.662  1.00 32.28           O
HETATM 5183  O   HOH S 223       2.869  -5.797  15.723  1.00 37.29           O
HETATM 5184  O   HOH S 224       1.208 -22.728 -24.799  1.00 29.07           O
HETATM 5185  O   HOH S 225     -25.035  20.069  -0.251  1.00 34.40           O
HETATM 5186  O   HOH S 226     -25.407   5.659   8.211  1.00 36.75           O
HETATM 5187  O   HOH S 227     -25.095  13.891  13.429  1.00 34.64           O
HETATM 5188  O   HOH S 228      14.588 -27.981   3.215  1.00 44.39           O
HETATM 5189  O   HOH S 229     -24.051  -7.719  10.542  1.00 41.94           O
HETATM 5190  O   HOH S 230      19.381  12.123  -5.345  1.00 33.06           O
HETATM 5191  O   HOH S 231      -5.707  -4.505  11.499  1.00 24.77           O
HETATM 5192  O   HOH S 232      -4.978  -4.863  14.755  1.00 20.64           O
HETATM 5193  O   HOH S 233      -5.639  -5.106  22.236  1.00 35.10           O
HETATM 5194  O   HOH S 234      -4.358  -6.473  20.300  1.00 44.40           O
HETATM 5195  O   HOH S 235     -12.626  -2.962  20.819  1.00 39.07           O
HETATM 5196  O   HOH S 236     -20.459  -0.780  19.252  1.00 38.24           O
HETATM 5197  O   HOH S 237     -17.277 -20.903  14.760  1.00 37.84           O
HETATM 5198  O   HOH S 238     -11.560 -26.627   3.155  1.00 49.69           O
HETATM 5199  O   HOH S 239      -9.872 -23.823  -8.307  1.00 48.33           O
HETATM 5200  O   HOH S 240      -7.898 -23.941  -6.134  1.00 32.81           O
HETATM 5201  O   HOH S 241     -18.536 -19.060  -4.873  1.00 35.17           O
HETATM 5202  O   HOH S 242     -13.849 -13.802  -3.791  1.00 31.90           O
HETATM 5203  O   HOH S 243     -17.370 -13.242  -4.859  1.00 58.39           O
HETATM 5204  O   HOH S 244     -16.555 -13.477  -9.705  1.00 42.73           O
HETATM 5205  O   HOH S 245     -15.475 -18.510   2.804  1.00 56.92           O
HETATM 5206  O   HOH S 246     -17.227  -7.512   0.174  1.00 38.96           O
HETATM 5207  O   HOH S 247     -23.031  -4.182   2.721  1.00 34.25           O
HETATM 5208  O   HOH S 248     -26.243  -2.494   4.243  1.00 37.00           O
HETATM 5209  O   HOH S 249     -15.032 -26.210   9.503  1.00 43.94           O
HETATM 5210  O   HOH S 250      -0.816 -29.133  16.961  1.00 49.41           O
HETATM 5211  O   HOH S 251       1.600 -26.444  14.314  1.00 45.90           O
HETATM 5212  O   HOH S 252       0.099 -30.706  11.117  1.00 47.77           O
HETATM 5213  O   HOH S 253      -5.134 -29.514   9.290  1.00 36.60           O
HETATM 5214  O   HOH S 254       1.817 -20.456   0.847  1.00 35.54           O
HETATM 5215  O   HOH S 255      -1.583 -29.215   7.161  1.00 41.80           O
HETATM 5216  O   HOH S 256     -19.513 -17.249  14.478  1.00 57.81           O
HETATM 5217  O   HOH S 257     -21.625 -13.540   9.532  1.00 43.47           O
HETATM 5218  O   HOH S 258     -17.738  -9.074   2.120  1.00 39.93           O
HETATM 5219  O   HOH S 259     -12.411 -20.072 -13.880  1.00 50.87           O
HETATM 5220  O   HOH S 260     -11.607 -11.314 -18.700  1.00 43.83           O
HETATM 5221  O   HOH S 261     -10.334 -10.791 -24.960  1.00 51.37           O
HETATM 5222  O   HOH S 262      -5.392 -13.274 -25.676  1.00 43.45           O
HETATM 5223  O   HOH S 263       1.454 -11.565 -23.976  1.00 39.05           O
HETATM 5224  O   HOH S 264       4.442 -29.495 -15.961  1.00 40.43           O
HETATM 5225  O   HOH S 265       4.613 -30.475 -13.821  1.00 48.12           O
HETATM 5226  O   HOH S 266       8.797 -28.817 -12.024  1.00 45.35           O
HETATM 5227  O   HOH S 267      10.449 -27.491 -13.377  1.00 52.09           O
HETATM 5228  O   HOH S 268       8.201 -26.051 -17.333  1.00 50.72           O
HETATM 5229  O   HOH S 269       7.432 -28.172 -19.396  1.00 49.26           O
HETATM 5230  O   HOH S 270       8.810 -25.097 -20.545  1.00 52.55           O
HETATM 5231  O   HOH S 271       6.105 -22.511 -21.836  1.00 40.18           O
HETATM 5232  O   HOH S 272       7.639 -24.485 -30.925  1.00 50.62           O
HETATM 5233  O   HOH S 273       4.180  34.871   9.068  1.00 38.77           O
HETATM 5234  O   HOH S 274      16.217  16.170  13.540  1.00 28.23           O
HETATM 5235  O   HOH S 275     -22.281  14.730   0.476  1.00 42.24           O
HETATM 5236  O   HOH S 276     -17.947  10.173  -2.777  1.00 43.15           O
HETATM 5237  O   HOH S 277      10.888  25.453  23.006  1.00 35.11           O
HETATM 5238  O   HOH S 278       8.569  32.239  21.101  1.00 38.42           O
HETATM 5239  O   HOH S 279      -2.613  30.021  24.574  1.00 39.02           O
HETATM 5240 MN    MN B   1      -5.128  -3.129  13.225  1.00 23.36          Mn
END



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