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***  orm2_NMA  ***

elNémo ID: 200511113810142238

Job options:

ID        	=	 200511113810142238
JOBID     	=	 orm2_NMA
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 orm2_NMA

REMARK Date 2020-04-23 Time 14:12:53 BST +0100 (1587647573.92 s)                
REMARK PHENIX refinement                                                        
REMARK                                                                          
REMARK ****************** INPUT FILES AND LABELS ****************************** 
REMARK Reflections:                                                             
REMARK   file name      : /home/chxcw/Documents/orm2/80863927_AUTOMATIC_DEFAULT_
REMARK   labels         : ['IMEAN,SIGIMEAN']                                    
REMARK R-free flags:                                                            
REMARK   file name      : /home/chxcw/Documents/orm2/80863927_AUTOMATIC_DEFAULT_
REMARK   label          : FreeR_flag                                            
REMARK   test_flag_value: 0                                                     
REMARK Model file name(s):                                                      
REMARK   /home/chxcw/Documents/orm2/Refine_18/orm2_refine_18-coot-0.pdb         
REMARK                                                                          
REMARK ******************** REFINEMENT SUMMARY: QUICK FACTS ******************* 
REMARK Start: r_work = 0.1542 r_free = 0.1807 bonds = 0.009 angles = 1.326      
REMARK Final: r_work = 0.1532 r_free = 0.1822 bonds = 0.007 angles = 1.288      
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 s: bulk solvent correction and/or (anisotropic) scaling              
REMARK   1 z: refinement of coordinates                                         
REMARK   1 p: refinement of ADPs (Atomic Displacement Parameters)               
REMARK   1 t: ordered solvent update (add / remove)                             
REMARK   1 c: refinement of occupancies                                         
REMARK ------------------------------------------------------------------------ 
REMARK  stage r-work r-free bonds angles b_min b_max b_ave n_water shift        
REMARK       0    : 0.3470 0.2505 0.009  1.326   9.5  88.2  30.6 226      0.000 
REMARK       1_bss: 0.1542 0.1807 0.009  1.326   9.5  88.2  30.6 226      0.000 
REMARK   1 ttarget: 0.1542 0.1807 0.009  1.326   9.5  88.2  30.6 226      0.000 
REMARK       1_nqh: 0.1542 0.1807 0.009  1.326   9.5  88.2  30.6 226      0.000 
REMARK    1_weight: 0.1542 0.1807 0.009  1.326   9.5  88.2  30.6 226      0.000 
REMARK    1_xyzrec: 0.1534 0.1846 0.007  1.259   9.5  88.2  30.6 226      0.058 
REMARK       1_adp: 0.1532 0.1863 0.007  1.259   9.9 110.4  31.9 226      0.058 
REMARK       1_occ: 0.1532 0.1864 0.007  1.259   9.9 110.4  31.9 226      0.058 
REMARK       2_bss: 0.1530 0.1864 0.007  1.259   9.8 110.3  31.8 226      0.058 
REMARK   2 ttarget: 0.1530 0.1864 0.007  1.259   9.8 110.3  31.8 226      0.058 
REMARK   2 datecdl: 0.1530 0.1864 0.007  1.261   9.8 110.3  31.8 226      0.058 
REMARK       2_nqh: 0.1530 0.1864 0.007  1.261   9.8 110.3  31.8 226      0.058 
REMARK       2_sol: 0.1569 0.1843 0.007  1.261   9.8 110.3  31.8 229       n/a  
REMARK       2_ion: 0.1569 0.1843 0.007  1.261   9.8 110.3  31.8 229       n/a  
REMARK   2 realsrl: 0.1656 0.1926 0.007  1.293   9.8 110.3  31.8 229       n/a  
REMARK    2_weight: 0.1656 0.1926 0.007  1.293   9.8 110.3  31.8 229       n/a  
REMARK    2_xyzrec: 0.1573 0.1870 0.006  1.268   9.8 110.3  31.8 229       n/a  
REMARK   2 ealsrl2: 0.1573 0.1870 0.006  1.268   9.8 110.3  31.8 229       n/a  
REMARK       2_adp: 0.1540 0.1849 0.006  1.268  10.2 104.2  31.4 229       n/a  
REMARK       2_occ: 0.1540 0.1850 0.006  1.268  10.2 104.2  31.4 229       n/a  
REMARK       3_bss: 0.1540 0.1843 0.006  1.268  10.1 104.1  31.3 229       n/a  
REMARK   3 ttarget: 0.1540 0.1843 0.006  1.268  10.1 104.1  31.3 229       n/a  
REMARK   3 datecdl: 0.1540 0.1843 0.006  1.272  10.1 104.1  31.3 229       n/a  
REMARK     3_setrh: 0.1540 0.1843 0.006  1.272  10.1 104.1  31.3 229       n/a  
REMARK       3_nqh: 0.1539 0.1844 0.006  1.272  10.1 104.1  31.3 229       n/a  
REMARK       3_sol: 0.1557 0.1842 0.006  1.272  10.1 104.1  31.3 242       n/a  
REMARK       3_ion: 0.1557 0.1842 0.006  1.272  10.1 104.1  31.3 242       n/a  
REMARK   3 realsrl: 0.1640 0.1887 0.006  1.294  10.1 104.1  31.3 242       n/a  
REMARK    3_weight: 0.1640 0.1887 0.006  1.294  10.1 104.1  31.3 242       n/a  
REMARK    3_xyzrec: 0.1533 0.1830 0.007  1.288  10.1 104.1  31.3 242       n/a  
REMARK   3 ealsrl2: 0.1533 0.1830 0.007  1.288  10.1 104.1  31.3 242       n/a  
REMARK       3_adp: 0.1523 0.1830 0.007  1.288   9.7 101.6  30.9 242       n/a  
REMARK       3_occ: 0.1523 0.1830 0.007  1.288   9.7 101.6  30.9 242       n/a  
REMARK         end: 0.1532 0.1822 0.007  1.288   9.8 101.7  30.8 229       n/a  
REMARK ------------------------------------------------------------------------ 
REMARK MODEL CONTENT.                                                           
REMARK  ELEMENT        ATOM RECORD COUNT   OCCUPANCY SUM                        
REMARK        C                      951          946.00                        
REMARK        S                        6            6.00                        
REMARK        O                      511          508.00                        
REMARK        N                      245          244.00                        
REMARK    TOTAL                     1713         1704.00                        
REMARK -----------------------------------------------------------------------  
REMARK r_free_flags.md5.hexdigest a68738849c317950446f346787c80574              
REMARK                                                                          
REMARK IF THIS FILE IS FOR PDB DEPOSITION: REMOVE ALL FROM THIS LINE UP.        
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (1.17.1_3660: ???)                            
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) : 1.82                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 44.13                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.44                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.72                          
REMARK   3   NUMBER OF REFLECTIONS             : 21514                          
REMARK   3   NUMBER OF REFLECTIONS (NON-ANOMALOUS) : 21514                      
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.1546                          
REMARK   3   R VALUE            (WORKING SET) : 0.1532                          
REMARK   3   FREE R VALUE                     : 0.1822                          
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.58                            
REMARK   3   FREE R VALUE TEST SET COUNT      : 986                             
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE  CCWOR 
REMARK   3     1   44.13 -    3.48    1.00     3009   142  0.1329 0.1527   0.95 
REMARK   3     2    3.48 -    2.76    1.00     2968   131  0.1568 0.1828   0.94 
REMARK   3     3    2.76 -    2.41    1.00     2951   127  0.1682 0.1897   0.92 
REMARK   3     4    2.41 -    2.19    1.00     2923   133  0.1592 0.2000   0.93 
REMARK   3     5    2.19 -    2.04    1.00     2935   143  0.1667 0.2024   0.92 
REMARK   3     6    2.04 -    1.92    1.00     2890   135  0.1662 0.2194   0.92 
REMARK   3     7    1.92 -    1.82    0.98     2852   175  0.1820 0.2293   0.91 
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)     : 0.16             
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 17.47            
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      :  0.007   0.050   1529                                 
REMARK   3    ANGLE     :  1.288  21.266   2084                                 
REMARK   3    CHIRALITY :  0.069   0.486    214                                 
REMARK   3    PLANARITY :  0.005   0.040    265                                 
REMARK   3    DIHEDRAL  :  5.989  16.885    195                                 
REMARK   3    MIN NONBONDED DISTANCE : 1.690                                    
REMARK   3                                                                      
REMARK   3  MOLPROBITY STATISTICS.                                              
REMARK   3    ALL-ATOM CLASHSCORE : 2.77                                        
REMARK   3    RAMACHANDRAN PLOT:                                                
REMARK   3      OUTLIERS :  0.00 %                                              
REMARK   3      ALLOWED  :  0.58 %                                              
REMARK   3      FAVORED  : 99.42 %                                              
REMARK   3    ROTAMER OUTLIERS :  0.00 %                                        
REMARK   3    CBETA DEVIATIONS :  0.00 %                                        
REMARK   3    PEPTIDE PLANE:                                                    
REMARK   3      CIS-PROLINE     : 0.00 %                                        
REMARK   3      CIS-GENERAL     : 0.00 %                                        
REMARK   3      TWISTED PROLINE : 0.00 %                                        
REMARK   3      TWISTED GENERAL : 0.00 %                                        
REMARK   3                                                                      
REMARK   3                  min    max   mean    iso aniso                
REMARK   3     Overall:    9.76 101.70  30.79   4.68  1713  1448                
REMARK   3     Protein:    9.76 101.70  29.35   4.72  1448  1448                
REMARK   3     Water:     16.12  66.71  41.94    N/A   229     0                
REMARK   3     Other:     11.38  26.15  17.84    N/A    36     0                
REMARK   3     Chain  S:  16.12  66.71  41.94    N/A   229     0                
REMARK   3     Chain  B:   9.76 101.70  29.07    N/A  1484  1448                
REMARK   3     Histogram:                                                       
REMARK   3         Values      Number of atoms                                  
REMARK   3       9.76 - 18.96       343                                         
REMARK   3      18.96 - 28.15       566                                         
REMARK   3      28.15 - 37.35       342                                         
REMARK   3      37.35 - 46.54       210                                         
REMARK   3      46.54 - 55.73       149                                         
REMARK   3      55.73 - 64.93        57                                         
REMARK   3      64.93 - 74.12        22                                         
REMARK   3      74.12 - 83.32        16                                         
REMARK   3      83.32 - 92.51         5                                         
REMARK   3      92.51 - 101.70        3                                         
REMARK   3                                                                      
REMARK   3                                                                      
REMARK   3  TLS DETAILS.                                                        
REMARK   3   NUMBER OF TLS GROUPS: 10                                           
REMARK   3   ORIGIN: CENTER OF MASS                                             
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: chain 'B' and (resid 1 through 36 )                    
REMARK   3    ORIGIN FOR THE GROUP (A): -16.3815  29.9620  -4.6735              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2247 T22:   0.2157                                     
REMARK   3      T33:   0.1753 T12:  -0.0676                                     
REMARK   3      T13:   0.0008 T23:  -0.0006                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.1679 L22:   0.7864                                     
REMARK   3      L33:   1.4811 L12:   1.2049                                     
REMARK   3      L13:  -0.4258 L23:   0.6094                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.3178 S12:   0.5455 S13:  -0.2102                       
REMARK   3      S21:  -0.0997 S22:   0.2718 S23:   0.0244                       
REMARK   3      S31:   0.4086 S32:  -0.0789 S33:   0.0628                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: chain 'B' and (resid 37 through 59 )                   
REMARK   3    ORIGIN FOR THE GROUP (A):  -4.2977  32.1750  -2.8381              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0886 T22:   0.2465                                     
REMARK   3      T33:   0.1869 T12:  -0.0036                                     
REMARK   3      T13:   0.0275 T23:  -0.0173                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.3677 L22:   2.8517                                     
REMARK   3      L33:   3.0752 L12:   0.6627                                     
REMARK   3      L13:  -1.0204 L23:  -0.1939                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2617 S12:   0.1152 S13:  -0.2052                       
REMARK   3      S21:  -0.0501 S22:   0.0472 S23:  -0.2370                       
REMARK   3      S31:   0.1605 S32:   0.2185 S33:  -0.0065                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: chain 'B' and (resid 60 through 84 )                   
REMARK   3    ORIGIN FOR THE GROUP (A):   0.6906  30.3267  -6.1331              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1500 T22:   0.3028                                     
REMARK   3      T33:   0.1923 T12:   0.0168                                     
REMARK   3      T13:   0.0385 T23:  -0.0373                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.8286 L22:   4.2168                                     
REMARK   3      L33:   2.5893 L12:   2.1358                                     
REMARK   3      L13:  -1.0560 L23:  -0.0899                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.3501 S12:   0.1597 S13:  -0.4280                       
REMARK   3      S21:  -0.0427 S22:   0.1534 S23:  -0.2716                       
REMARK   3      S31:   0.2363 S32:   0.4260 S33:   0.1731                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: chain 'B' and (resid 85 through 96 )                   
REMARK   3    ORIGIN FOR THE GROUP (A):  -7.5743  21.4788  -1.9856              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2677 T22:   0.1668                                     
REMARK   3      T33:   0.3645 T12:   0.0312                                     
REMARK   3      T13:   0.1103 T23:  -0.0128                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.1693 L22:   5.8771                                     
REMARK   3      L33:   7.9522 L12:   2.5196                                     
REMARK   3      L13:   0.0363 L23:   1.6050                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.3844 S12:   0.1401 S13:  -1.5590                       
REMARK   3      S21:   0.2506 S22:   0.2465 S23:  -0.6688                       
REMARK   3      S31:   0.7076 S32:   0.5671 S33:  -0.1590                       
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION: chain 'B' and (resid 97 through 116 )                  
REMARK   3    ORIGIN FOR THE GROUP (A): -14.7084  30.4049  -4.4205              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1235 T22:   0.1615                                     
REMARK   3      T33:   0.1231 T12:  -0.0440                                     
REMARK   3      T13:   0.0208 T23:  -0.0207                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.2236 L22:   4.5172                                     
REMARK   3      L33:   7.4351 L12:  -1.6061                                     
REMARK   3      L13:   1.1037 L23:  -3.0311                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1540 S12:   0.1770 S13:  -0.1009                       
REMARK   3      S21:   0.0057 S22:  -0.0212 S23:  -0.0628                       
REMARK   3      S31:   0.2151 S32:   0.0608 S33:   0.1467                       
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    SELECTION: chain 'B' and (resid 117 through 124 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -16.8587  27.6812  10.1498              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1836 T22:   0.1984                                     
REMARK   3      T33:   0.1527 T12:   0.0359                                     
REMARK   3      T13:   0.0247 T23:   0.0521                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.3671 L22:   6.7269                                     
REMARK   3      L33:   7.7610 L12:   0.8775                                     
REMARK   3      L13:   1.7106 L23:   1.9777                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1524 S12:  -0.6236 S13:  -0.3188                       
REMARK   3      S21:   0.1469 S22:  -0.1144 S23:  -0.1885                       
REMARK   3      S31:   0.7177 S32:   0.2239 S33:   0.2803                       
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    SELECTION: chain 'B' and (resid 125 through 136 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -12.2722  40.3807  -7.1418              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1149 T22:   0.2617                                     
REMARK   3      T33:   0.1919 T12:  -0.0499                                     
REMARK   3      T13:  -0.0432 T23:   0.0790                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.0933 L22:   4.0728                                     
REMARK   3      L33:   4.8796 L12:  -0.6180                                     
REMARK   3      L13:  -0.4152 L23:  -1.2227                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1484 S12:   0.5889 S13:   0.5446                       
REMARK   3      S21:  -0.1003 S22:  -0.0287 S23:  -0.2261                       
REMARK   3      S31:  -0.3513 S32:   0.2285 S33:   0.0937                       
REMARK   3   TLS GROUP : 8                                                      
REMARK   3    SELECTION: chain 'B' and (resid 137 through 150 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -21.4939  40.9287  -1.3863              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1335 T22:   0.2054                                     
REMARK   3      T33:   0.2058 T12:  -0.0010                                     
REMARK   3      T13:  -0.0276 T23:   0.0025                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.0261 L22:   5.4390                                     
REMARK   3      L33:   8.2873 L12:   2.4878                                     
REMARK   3      L13:  -4.1448 L23:  -4.9662                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1434 S12:   0.4146 S13:   0.3861                       
REMARK   3      S21:   0.0127 S22:   0.2620 S23:   0.2818                       
REMARK   3      S31:  -0.1558 S32:  -0.7042 S33:  -0.0884                       
REMARK   3   TLS GROUP : 9                                                      
REMARK   3    SELECTION: chain 'B' and (resid 151 through 164 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -11.4109  44.2640   2.4175              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1477 T22:   0.1624                                     
REMARK   3      T33:   0.3381 T12:  -0.0258                                     
REMARK   3      T13:  -0.0232 T23:  -0.0281                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   7.6450 L22:   2.4369                                     
REMARK   3      L33:   7.5623 L12:   2.9680                                     
REMARK   3      L13:  -6.4526 L23:  -3.2384                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2920 S12:  -0.4142 S13:   0.6980                       
REMARK   3      S21:   0.3424 S22:  -0.1189 S23:  -0.2078                       
REMARK   3      S31:  -0.5628 S32:   0.3961 S33:  -0.1408                       
REMARK   3   TLS GROUP : 10                                                     
REMARK   3    SELECTION: chain 'B' and (resid 165 through 173 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):   6.0901  41.8463 -12.4739              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1917 T22:   0.5128                                     
REMARK   3      T33:   0.4457 T12:  -0.1076                                     
REMARK   3      T13:  -0.0073 T23:   0.1707                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   6.2904 L22:   6.7345                                     
REMARK   3      L33:   5.3346 L12:   0.1534                                     
REMARK   3      L13:  -2.7098 L23:  -0.2758                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.3937 S12:   1.0761 S13:   0.5538                       
REMARK   3      S21:  -0.7870 S22:  -0.1897 S23:  -0.5886                       
REMARK   3      S31:  -0.2770 S32:  -0.4658 S33:  -0.0432                       
REMARK   3                                                                      
CRYST1   88.270   88.270   53.840  90.00  90.00 120.00 P 61                     
SCALE1      0.011329  0.006541  0.000000        0.00000                         
SCALE2      0.000000  0.013081  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.018574        0.00000                         
ATOM      1  N   GLY B   1     -26.709  17.324  11.654  1.00 37.40           N  
ANISOU    1  N   GLY B   1     5967   3498   4747  -1329    713   1322       N  
ATOM      2  CA  GLY B   1     -27.236  17.632  10.334  1.00 41.29           C  
ANISOU    2  CA  GLY B   1     6443   3967   5278  -1385    730   1070       C  
ATOM      3  C   GLY B   1     -26.370  18.595   9.544  1.00 44.63           C  
ANISOU    3  C   GLY B   1     6843   4423   5691  -1270    678    966       C  
ATOM      4  O   GLY B   1     -25.337  19.058  10.047  1.00 37.22           O  
ANISOU    4  O   GLY B   1     5906   3521   4714  -1141    627   1079       O  
ATOM      5  N   PRO B   2     -26.783  18.893   8.310  1.00 28.34           N  
ANISOU    5  N   PRO B   2     4752   2363   3654  -1319    690    759       N  
ATOM      6  CA  PRO B   2     -26.026  19.839   7.480  1.00 26.47           C  
ANISOU    6  CA  PRO B   2     4484   2168   3405  -1230    643    664       C  
ATOM      7  C   PRO B   2     -25.810  21.168   8.188  1.00 26.31           C  
ANISOU    7  C   PRO B   2     4388   2353   3255  -1189    579    711       C  
ATOM      8  O   PRO B   2     -26.683  21.663   8.905  1.00 26.76           O  
ANISOU    8  O   PRO B   2     4369   2584   3215  -1281    574    707       O  
ATOM      9  CB  PRO B   2     -26.912  20.007   6.241  1.00 25.96           C  
ANISOU    9  CB  PRO B   2     4364   2158   3343  -1344    662    456       C  
ATOM     10  CG  PRO B   2     -27.676  18.725   6.152  1.00 27.92           C  
ANISOU   10  CG  PRO B   2     4661   2286   3664  -1448    738    428       C  
ATOM     11  CD  PRO B   2     -27.903  18.272   7.581  1.00 29.16           C  
ANISOU   11  CD  PRO B   2     4850   2432   3799  -1461    748    613       C  
ATOM     12  N   GLN B   3     -24.636  21.765   7.959  1.00 24.48           N  
ANISOU   12  N   GLN B   3     4136   2131   3034  -1028    521    720       N  
ATOM     13  CA  GLN B   3     -24.212  22.949   8.692  1.00 24.74           C  
ANISOU   13  CA  GLN B   3     4053   2373   2975   -932    446    746       C  
ATOM     14  C   GLN B   3     -23.924  24.169   7.825  1.00 28.30           C  
ANISOU   14  C   GLN B   3     4385   2932   3436   -859    383    609       C  
ATOM     15  O   GLN B   3     -23.857  25.281   8.367  1.00 23.46           O  
ANISOU   15  O   GLN B   3     3649   2493   2770   -816    334    589       O  
ATOM     16  CB  GLN B   3     -22.948  22.633   9.512  1.00 30.63           C  
ANISOU   16  CB  GLN B   3     4845   3080   3714   -780    420    911       C  
ATOM     17  CG  GLN B   3     -23.114  21.507  10.514  1.00 39.72           C  
ANISOU   17  CG  GLN B   3     6100   4141   4852   -837    464   1108       C  
ATOM     18  CD  GLN B   3     -24.077  21.867  11.617  1.00 43.80           C  
ANISOU   18  CD  GLN B   3     6550   4871   5222   -977    474   1147       C  
ATOM     19  OE1 GLN B   3     -24.084  22.997  12.100  1.00 46.48           O  
ANISOU   19  OE1 GLN B   3     6752   5448   5462   -958    431   1079       O  
ATOM     20  NE2 GLN B   3     -24.907  20.909  12.019  1.00 52.95           N  
ANISOU   20  NE2 GLN B   3     7765   5964   6391  -1102    534   1222       N  
ATOM     21  N   ILE B   4     -23.753  24.008   6.516  1.00 24.26           N  
ANISOU   21  N   ILE B   4     3895   2331   2991   -857    386    513       N  
ATOM     22  CA  ILE B   4     -23.391  25.133   5.650  1.00 19.65           C  
ANISOU   22  CA  ILE B   4     3203   1851   2412   -794    320    421       C  
ATOM     23  C   ILE B   4     -24.639  25.939   5.315  1.00 22.09           C  
ANISOU   23  C   ILE B   4     3393   2301   2701   -910    295    340       C  
ATOM     24  O   ILE B   4     -25.558  25.415   4.667  1.00 22.66           O  
ANISOU   24  O   ILE B   4     3485   2350   2776  -1045    331    279       O  
ATOM     25  CB  ILE B   4     -22.696  24.653   4.367  1.00 21.64           C  
ANISOU   25  CB  ILE B   4     3508   1995   2720   -764    333    351       C  
ATOM     26  CG1 ILE B   4     -21.433  23.855   4.699  1.00 26.71           C  
ANISOU   26  CG1 ILE B   4     4249   2484   3417   -631    357    421       C  
ATOM     27  CG2 ILE B   4     -22.385  25.837   3.445  1.00 23.03           C  
ANISOU   27  CG2 ILE B   4     3566   2303   2881   -727    262    283       C  
ATOM     28  CD1 ILE B   4     -20.771  23.234   3.481  1.00 33.99           C  
ANISOU   28  CD1 ILE B   4     5215   3288   4413   -615    392    316       C  
ATOM     29  N   PRO B   5     -24.732  27.202   5.724  1.00 22.21           N  
ANISOU   29  N   PRO B   5     3269   2459   2711   -865    238    328       N  
ATOM     30  CA  PRO B   5     -25.937  27.970   5.409  1.00 22.08           C  
ANISOU   30  CA  PRO B   5     3121   2557   2714   -959    209    258       C  
ATOM     31  C   PRO B   5     -25.928  28.336   3.933  1.00 20.80           C  
ANISOU   31  C   PRO B   5     2911   2410   2582   -970    160    217       C  
ATOM     32  O   PRO B   5     -24.904  28.756   3.393  1.00 25.11           O  
ANISOU   32  O   PRO B   5     3451   2945   3144   -871    121    234       O  
ATOM     33  CB  PRO B   5     -25.822  29.204   6.311  1.00 24.03           C  
ANISOU   33  CB  PRO B   5     3225   2920   2986   -887    171    247       C  
ATOM     34  CG  PRO B   5     -24.375  29.375   6.516  1.00 24.27           C  
ANISOU   34  CG  PRO B   5     3292   2917   3012   -741    153    294       C  
ATOM     35  CD  PRO B   5     -23.724  28.017   6.418  1.00 26.50           C  
ANISOU   35  CD  PRO B   5     3753   3063   3252   -725    198    361       C  
ATOM     36  N   LEU B   6     -27.055  28.104   3.271  1.00 21.02           N  
ANISOU   36  N   LEU B   6     2906   2482   2600  -1105    164    168       N  
ATOM     37  CA  LEU B   6     -27.230  28.494   1.880  1.00 22.85           C  
ANISOU   37  CA  LEU B   6     3064   2786   2832  -1145    108    144       C  
ATOM     38  C   LEU B   6     -28.067  29.752   1.809  1.00 22.88           C  
ANISOU   38  C   LEU B   6     2878   2917   2897  -1150     27    154       C  
ATOM     39  O   LEU B   6     -29.065  29.887   2.515  1.00 25.69           O  
ANISOU   39  O   LEU B   6     3168   3316   3279  -1205     41    122       O  
ATOM     40  CB  LEU B   6     -27.926  27.401   1.069  1.00 29.16           C  
ANISOU   40  CB  LEU B   6     3926   3579   3575  -1302    163     73       C  
ATOM     41  CG  LEU B   6     -27.165  26.115   0.805  1.00 31.58           C  
ANISOU   41  CG  LEU B   6     4397   3738   3863  -1314    249     34       C  
ATOM     42  CD1 LEU B   6     -27.606  25.510  -0.531  1.00 30.93           C  
ANISOU   42  CD1 LEU B   6     4308   3713   3732  -1463    275    -71       C  
ATOM     43  CD2 LEU B   6     -25.704  26.386   0.815  1.00 24.91           C  
ANISOU   43  CD2 LEU B   6     3591   2832   3042  -1156    225     79       C  
ATOM     44  N   CYS B   7     -27.667  30.661   0.938  1.00 20.23           N  
ANISOU   44  N   CYS B   7     2447   2641   2598  -1097    -57    202       N  
ATOM     45  CA  CYS B   7     -28.395  31.892   0.703  1.00 27.70           C  
ANISOU   45  CA  CYS B   7     3199   3681   3644  -1088   -146    241       C  
ATOM     46  C   CYS B   7     -28.182  32.263  -0.756  1.00 29.26           C  
ANISOU   46  C   CYS B   7     3339   3968   3813  -1114   -226    314       C  
ATOM     47  O   CYS B   7     -27.413  31.609  -1.467  1.00 27.49           O  
ANISOU   47  O   CYS B   7     3220   3740   3487  -1139   -201    304       O  
ATOM     48  CB  CYS B   7     -27.939  33.008   1.660  1.00 31.40           C  
ANISOU   48  CB  CYS B   7     3577   4110   4242   -956   -166    255       C  
ATOM     49  SG  CYS B   7     -27.617  32.521   3.418  1.00 36.88           S  
ANISOU   49  SG  CYS B   7     4362   4742   4909   -916    -66    183       S  
ATOM     50  N   ALA B   8     -28.815  33.362  -1.176  1.00 26.16           N  
ANISOU   50  N   ALA B   8     2762   3657   3521  -1107   -325    393       N  
ATOM     51  CA  ALA B   8     -28.903  33.732  -2.592  1.00 35.75           C  
ANISOU   51  CA  ALA B   8     3894   5001   4688  -1154   -415    493       C  
ATOM     52  C   ALA B   8     -27.565  33.641  -3.342  1.00 38.12           C  
ANISOU   52  C   ALA B   8     4273   5309   4901  -1141   -419    538       C  
ATOM     53  O   ALA B   8     -27.505  33.118  -4.462  1.00 51.82           O  
ANISOU   53  O   ALA B   8     6027   7170   6491  -1251   -429    539       O  
ATOM     54  CB  ALA B   8     -29.483  35.143  -2.709  1.00 39.55           C  
ANISOU   54  CB  ALA B   8     4202   5493   5331  -1045   -505    592       C  
ATOM     55  N   ASN B   9     -26.491  34.167  -2.762  1.00 20.88           N  
ANISOU   55  N   ASN B   9     2124   3012   2796  -1011   -407    555       N  
ATOM     56  CA  ASN B   9     -25.177  34.188  -3.413  1.00 19.48           C  
ANISOU   56  CA  ASN B   9     2010   2844   2547   -981   -407    585       C  
ATOM     57  C   ASN B   9     -24.155  33.331  -2.661  1.00 16.02           C  
ANISOU   57  C   ASN B   9     1743   2282   2064   -912   -304    473       C  
ATOM     58  O   ASN B   9     -22.945  33.587  -2.710  1.00 18.17           O  
ANISOU   58  O   ASN B   9     2050   2519   2333   -832   -298    483       O  
ATOM     59  CB  ASN B   9     -24.654  35.620  -3.557  1.00 22.14           C  
ANISOU   59  CB  ASN B   9     2223   3170   3019   -892   -490    719       C  
ATOM     60  CG  ASN B   9     -24.771  36.159  -4.990  1.00 38.11           C  
ANISOU   60  CG  ASN B   9     4137   5355   4988   -979   -592    873       C  
ATOM     61  OD1 ASN B   9     -24.865  35.392  -5.954  1.00 32.21           O  
ANISOU   61  OD1 ASN B   9     3430   4753   4057  -1103   -587    850       O  
ATOM     62  ND2 ASN B   9     -24.748  37.488  -5.128  1.00 30.98           N  
ANISOU   62  ND2 ASN B   9     3135   4409   4226   -880   -658   1007       N  
ATOM     63  N   LEU B  10     -24.618  32.307  -1.955  1.00 16.06           N  
ANISOU   63  N   LEU B  10     1848   2218   2036   -941   -224    377       N  
ATOM     64  CA  LEU B  10     -23.704  31.348  -1.328  1.00 16.19           C  
ANISOU   64  CA  LEU B  10     2024   2114   2013   -882   -134    302       C  
ATOM     65  C   LEU B  10     -24.293  29.964  -1.596  1.00 19.70           C  
ANISOU   65  C   LEU B  10     2571   2537   2379  -1004    -58    213       C  
ATOM     66  O   LEU B  10     -25.110  29.470  -0.817  1.00 20.26           O  
ANISOU   66  O   LEU B  10     2675   2556   2466  -1043    -14    186       O  
ATOM     67  CB  LEU B  10     -23.519  31.619   0.168  1.00 18.60           C  
ANISOU   67  CB  LEU B  10     2341   2329   2395   -772   -107    302       C  
ATOM     68  CG  LEU B  10     -22.142  31.148   0.672  1.00 17.34           C  
ANISOU   68  CG  LEU B  10     2294   2081   2213   -660    -58    283       C  
ATOM     69  CD1 LEU B  10     -21.830  31.713   2.063  1.00 20.69           C  
ANISOU   69  CD1 LEU B  10     2685   2482   2694   -554    -52    295       C  
ATOM     70  CD2 LEU B  10     -22.055  29.625   0.689  1.00 22.06           C  
ANISOU   70  CD2 LEU B  10     3046   2584   2751   -702     24    231       C  
ATOM     71  N   VAL B  11     -23.877  29.356  -2.710  1.00 17.19           N  
ANISOU   71  N   VAL B  11     2291   2264   1978  -1078    -36    154       N  
ATOM     72  CA  VAL B  11     -24.451  28.093  -3.173  1.00 19.81           C  
ANISOU   72  CA  VAL B  11     2693   2584   2248  -1218     44     39       C  
ATOM     73  C   VAL B  11     -23.336  27.200  -3.706  1.00 20.21           C  
ANISOU   73  C   VAL B  11     2842   2564   2274  -1210    119    -65       C  
ATOM     74  O   VAL B  11     -22.859  27.427  -4.827  1.00 23.09           O  
ANISOU   74  O   VAL B  11     3149   3064   2563  -1262     94    -99       O  
ATOM     75  CB  VAL B  11     -25.503  28.320  -4.273  1.00 29.43           C  
ANISOU   75  CB  VAL B  11     3790   4007   3382  -1382     -7     32       C  
ATOM     76  CG1 VAL B  11     -26.111  26.989  -4.707  1.00 26.21           C  
ANISOU   76  CG1 VAL B  11     3447   3594   2916  -1544     92   -121       C  
ATOM     77  CG2 VAL B  11     -26.597  29.278  -3.813  1.00 34.44           C  
ANISOU   77  CG2 VAL B  11     4300   4711   4074  -1375    -90    135       C  
ATOM     78  N   PRO B  12     -22.895  26.186  -2.964  1.00 21.49           N  
ANISOU   78  N   PRO B  12     3137   2525   2502  -1151    209   -116       N  
ATOM     79  CA  PRO B  12     -21.925  25.236  -3.525  1.00 22.37           C  
ANISOU   79  CA  PRO B  12     3324   2548   2630  -1146    290   -241       C  
ATOM     80  C   PRO B  12     -22.517  24.470  -4.696  1.00 23.82           C  
ANISOU   80  C   PRO B  12     3483   2817   2750  -1344    352   -403       C  
ATOM     81  O   PRO B  12     -23.682  24.068  -4.678  1.00 24.93           O  
ANISOU   81  O   PRO B  12     3620   2975   2876  -1473    380   -435       O  
ATOM     82  CB  PRO B  12     -21.614  24.301  -2.350  1.00 25.15           C  
ANISOU   82  CB  PRO B  12     3810   2649   3098  -1047    364   -221       C  
ATOM     83  CG  PRO B  12     -22.032  25.070  -1.120  1.00 26.79           C  
ANISOU   83  CG  PRO B  12     4001   2864   3314   -967    302    -67       C  
ATOM     84  CD  PRO B  12     -23.221  25.869  -1.564  1.00 22.38           C  
ANISOU   84  CD  PRO B  12     3326   2489   2688  -1085    240    -52       C  
ATOM     85  N   VAL B  13     -21.682  24.245  -5.709  1.00 22.46           N  
ANISOU   85  N   VAL B  13     3286   2713   2536  -1378    382   -526       N  
ATOM     86  CA  VAL B  13     -22.096  23.523  -6.914  1.00 27.13           C  
ANISOU   86  CA  VAL B  13     3830   3426   3050  -1582    452   -721       C  
ATOM     87  C   VAL B  13     -20.940  22.650  -7.389  1.00 27.72           C  
ANISOU   87  C   VAL B  13     3947   3396   3189  -1562    556   -911       C  
ATOM     88  O   VAL B  13     -19.772  22.949  -7.148  1.00 25.69           O  
ANISOU   88  O   VAL B  13     3709   3076   2977  -1406    535   -873       O  
ATOM     89  CB  VAL B  13     -22.516  24.492  -8.041  1.00 36.77           C  
ANISOU   89  CB  VAL B  13     4894   4990   4086  -1714    354   -680       C  
ATOM     90  CG1 VAL B  13     -23.910  25.052  -7.758  1.00 50.01           C  
ANISOU   90  CG1 VAL B  13     6508   6766   5726  -1776    276   -551       C  
ATOM     91  CG2 VAL B  13     -21.504  25.620  -8.187  1.00 37.76           C  
ANISOU   91  CG2 VAL B  13     4966   5208   4173  -1595    258   -552       C  
ATOM     92  N   PRO B  14     -21.265  21.529  -8.044  1.00 34.76           N  
ANISOU   92  N   PRO B  14     4843   4260   4103  -1721    678  -1139       N  
ATOM     93  CA  PRO B  14     -20.194  20.637  -8.499  1.00 33.08           C  
ANISOU   93  CA  PRO B  14     4651   3926   3993  -1704    792  -1357       C  
ATOM     94  C   PRO B  14     -19.347  21.312  -9.556  1.00 32.31           C  
ANISOU   94  C   PRO B  14     4437   4097   3744  -1740    750  -1425       C  
ATOM     95  O   PRO B  14     -19.822  22.136 -10.344  1.00 31.14           O  
ANISOU   95  O   PRO B  14     4175   4269   3390  -1874    667  -1373       O  
ATOM     96  CB  PRO B  14     -20.950  19.434  -9.083  1.00 35.28           C  
ANISOU   96  CB  PRO B  14     4911   4181   4313  -1866    925  -1566       C  
ATOM     97  CG  PRO B  14     -22.242  19.444  -8.411  1.00 39.57           C  
ANISOU   97  CG  PRO B  14     5496   4687   4850  -1909    899  -1435       C  
ATOM     98  CD  PRO B  14     -22.581  20.911  -8.243  1.00 38.52           C  
ANISOU   98  CD  PRO B  14     5310   4768   4558  -1911    736  -1228       C  
ATOM     99  N   ILE B  15     -18.077  20.942  -9.563  1.00 32.33           N  
ANISOU   99  N   ILE B  15     4461   3969   3853  -1623    807  -1532       N  
ATOM    100  CA  ILE B  15     -17.139  21.408 -10.569  1.00 30.55           C  
ANISOU  100  CA  ILE B  15     4127   3984   3498  -1669    794  -1641       C  
ATOM    101  C   ILE B  15     -17.215  20.456 -11.756  1.00 40.28           C  
ANISOU  101  C   ILE B  15     5254   5341   4709  -1825    924  -1899       C  
ATOM    102  O   ILE B  15     -17.042  19.241 -11.607  1.00 38.56           O  
ANISOU  102  O   ILE B  15     5071   4883   4698  -1778   1049  -2051       O  
ATOM    103  CB  ILE B  15     -15.720  21.488  -9.999  1.00 33.41           C  
ANISOU  103  CB  ILE B  15     4533   4173   3990  -1437    792  -1614       C  
ATOM    104  CG1 ILE B  15     -15.676  22.521  -8.868  1.00 25.93           C  
ANISOU  104  CG1 ILE B  15     3641   3165   3046  -1247    659  -1298       C  
ATOM    105  CG2 ILE B  15     -14.724  21.854 -11.086  1.00 32.17           C  
ANISOU  105  CG2 ILE B  15     4256   4267   3701  -1507    801  -1766       C  
ATOM    106  CD1 ILE B  15     -14.468  22.393  -7.977  1.00 27.98           C  
ANISOU  106  CD1 ILE B  15     3964   3202   3464  -1003    662  -1252       C  
ATOM    107  N   THR B  16     -17.501  21.007 -12.922  1.00 31.88           N  
ANISOU  107  N   THR B  16     4044   4657   3412  -1985    891  -1898       N  
ATOM    108  CA  THR B  16     -17.545  20.282 -14.179  1.00 38.62           C  
ANISOU  108  CA  THR B  16     4758   5711   4206  -2134   1013  -2104       C  
ATOM    109  C   THR B  16     -16.400  20.748 -15.067  1.00 39.53           C  
ANISOU  109  C   THR B  16     4751   6056   4211  -2153   1011  -2160       C  
ATOM    110  O   THR B  16     -15.624  21.641 -14.711  1.00 33.30           O  
ANISOU  110  O   THR B  16     3992   5272   3387  -2050    912  -2033       O  
ATOM    111  CB  THR B  16     -18.879  20.513 -14.880  1.00 45.86           C  
ANISOU  111  CB  THR B  16     5587   6916   4920  -2316    993  -2041       C  
ATOM    112  OG1 THR B  16     -18.982  21.904 -15.217  1.00 43.08           O  
ANISOU  112  OG1 THR B  16     5173   6849   4346  -2348    840  -1807       O  
ATOM    113  CG2 THR B  16     -20.035  20.114 -13.974  1.00 39.25           C  
ANISOU  113  CG2 THR B  16     4861   5866   4185  -2300    988  -1977       C  
ATOM    114  N   ASN B  17     -16.308  20.146 -16.252  1.00 37.31           N  
ANISOU  114  N   ASN B  17     4321   5984   3871  -2301   1131  -2356       N  
ATOM    115  CA  ASN B  17     -15.347  20.643 -17.228  1.00 46.90           C  
ANISOU  115  CA  ASN B  17     5393   7476   4949  -2363   1135  -2395       C  
ATOM    116  C   ASN B  17     -15.684  22.063 -17.663  1.00 36.99           C  
ANISOU  116  C   ASN B  17     4085   6546   3423  -2439    992  -2123       C  
ATOM    117  O   ASN B  17     -14.779  22.849 -17.957  1.00 37.26           O  
ANISOU  117  O   ASN B  17     4068   6713   3375  -2417    938  -2042       O  
ATOM    118  CB  ASN B  17     -15.277  19.703 -18.431  1.00 44.35           C  
ANISOU  118  CB  ASN B  17     4899   7338   4614  -2534   1303  -2665       C  
ATOM    119  CG  ASN B  17     -14.477  18.456 -18.134  1.00 55.08           C  
ANISOU  119  CG  ASN B  17     6271   8385   6270  -2434   1435  -2927       C  
ATOM    120  OD1 ASN B  17     -13.780  18.384 -17.118  1.00 52.35           O  
ANISOU  120  OD1 ASN B  17     6055   7715   6120  -2225   1393  -2888       O  
ATOM    121  ND2 ASN B  17     -14.557  17.469 -19.021  1.00 59.73           N  
ANISOU  121  ND2 ASN B  17     6715   9074   6905  -2580   1596  -3189       N  
ATOM    122  N   ALA B  18     -16.972  22.418 -17.689  1.00 40.93           N  
ANISOU  122  N   ALA B  18     4592   7163   3798  -2519    929  -1965       N  
ATOM    123  CA  ALA B  18     -17.340  23.803 -17.962  1.00 38.94           C  
ANISOU  123  CA  ALA B  18     4299   7161   3336  -2554    776  -1659       C  
ATOM    124  C   ALA B  18     -16.841  24.731 -16.858  1.00 40.15           C  
ANISOU  124  C   ALA B  18     4569   7115   3573  -2373    632  -1458       C  
ATOM    125  O   ALA B  18     -16.408  25.856 -17.133  1.00 39.52           O  
ANISOU  125  O   ALA B  18     4440   7196   3381  -2366    533  -1257       O  
ATOM    126  CB  ALA B  18     -18.853  23.927 -18.113  1.00 37.38           C  
ANISOU  126  CB  ALA B  18     4087   7092   3024  -2646    734  -1534       C  
ATOM    127  N   THR B  19     -16.904  24.281 -15.601  1.00 31.63           N  
ANISOU  127  N   THR B  19     3638   5686   2693  -2233    626  -1503       N  
ATOM    128  CA  THR B  19     -16.359  25.084 -14.508  1.00 29.34           C  
ANISOU  128  CA  THR B  19     3449   5213   2485  -2068    510  -1346       C  
ATOM    129  C   THR B  19     -14.862  25.283 -14.679  1.00 32.20           C  
ANISOU  129  C   THR B  19     3789   5581   2863  -1991    534  -1424       C  
ATOM    130  O   THR B  19     -14.340  26.385 -14.480  1.00 30.59           O  
ANISOU  130  O   THR B  19     3578   5443   2602  -1930    426  -1243       O  
ATOM    131  CB  THR B  19     -16.633  24.424 -13.160  1.00 31.49           C  
ANISOU  131  CB  THR B  19     3884   5110   2971  -1948    533  -1403       C  
ATOM    132  OG1 THR B  19     -18.016  24.083 -13.059  1.00 37.06           O  
ANISOU  132  OG1 THR B  19     4600   5809   3674  -2033    536  -1364       O  
ATOM    133  CG2 THR B  19     -16.261  25.378 -12.019  1.00 34.83           C  
ANISOU  133  CG2 THR B  19     4384   5363   3487  -1727    422  -1147       C  
ATOM    134  N   LEU B  20     -14.148  24.213 -15.027  1.00 32.64           N  
ANISOU  134  N   LEU B  20     3824   5558   3020  -1985    679  -1691       N  
ATOM    135  CA  LEU B  20     -12.701  24.320 -15.149  1.00 32.25           C  
ANISOU  135  CA  LEU B  20     3743   5500   3011  -1896    708  -1782       C  
ATOM    136  C   LEU B  20     -12.319  25.271 -16.277  1.00 37.71           C  
ANISOU  136  C   LEU B  20     4284   6557   3487  -2026    665  -1670       C  
ATOM    137  O   LEU B  20     -11.342  26.018 -16.162  1.00 32.42           O  
ANISOU  137  O   LEU B  20     3603   5917   2796  -1950    614  -1597       O  
ATOM    138  CB  LEU B  20     -12.093  22.932 -15.350  1.00 36.37           C  
ANISOU  138  CB  LEU B  20     4243   5859   3718  -1865    868  -2083       C  
ATOM    139  CG  LEU B  20     -12.260  22.024 -14.124  1.00 32.35           C  
ANISOU  139  CG  LEU B  20     3893   4931   3468  -1698    912  -2149       C  
ATOM    140  CD1 LEU B  20     -11.790  20.619 -14.446  1.00 34.72           C  
ANISOU  140  CD1 LEU B  20     4145   5071   3974  -1681   1066  -2415       C  
ATOM    141  CD2 LEU B  20     -11.533  22.588 -12.889  1.00 30.29           C  
ANISOU  141  CD2 LEU B  20     3758   4449   3301  -1473    835  -2029       C  
ATOM    142  N   ASP B  21     -13.097  25.285 -17.363  1.00 38.10           N  
ANISOU  142  N   ASP B  21     4214   6889   3373  -2223    691  -1642       N  
ATOM    143  CA  ASP B  21     -12.854  26.254 -18.428  1.00 38.07           C  
ANISOU  143  CA  ASP B  21     4072   7232   3161  -2358    651  -1485       C  
ATOM    144  C   ASP B  21     -13.109  27.682 -17.956  1.00 39.93           C  
ANISOU  144  C   ASP B  21     4353   7488   3332  -2295    481  -1138       C  
ATOM    145  O   ASP B  21     -12.347  28.596 -18.292  1.00 39.61           O  
ANISOU  145  O   ASP B  21     4255   7573   3221  -2304    434  -1006       O  
ATOM    146  CB  ASP B  21     -13.724  25.938 -19.646  1.00 42.62           C  
ANISOU  146  CB  ASP B  21     4513   8112   3567  -2580    723  -1516       C  
ATOM    147  CG  ASP B  21     -13.210  24.753 -20.442  1.00 50.26           C  
ANISOU  147  CG  ASP B  21     5368   9157   4573  -2685    903  -1854       C  
ATOM    148  OD1 ASP B  21     -12.000  24.448 -20.360  1.00 52.05           O  
ANISOU  148  OD1 ASP B  21     5578   9284   4915  -2612    956  -2021       O  
ATOM    149  OD2 ASP B  21     -14.014  24.136 -21.166  1.00 50.70           O  
ANISOU  149  OD2 ASP B  21     5337   9381   4547  -2843    992  -1959       O  
ATOM    150  N   ARG B  22     -14.177  27.893 -17.179  1.00 34.15           N  
ANISOU  150  N   ARG B  22     3711   6624   2640  -2237    390   -988       N  
ATOM    151  CA  ARG B  22     -14.528  29.237 -16.722  1.00 33.10           C  
ANISOU  151  CA  ARG B  22     3598   6493   2486  -2175    228   -656       C  
ATOM    152  C   ARG B  22     -13.460  29.827 -15.798  1.00 37.33           C  
ANISOU  152  C   ARG B  22     4204   6848   3133  -2009    169   -615       C  
ATOM    153  O   ARG B  22     -13.234  31.043 -15.810  1.00 36.01           O  
ANISOU  153  O   ARG B  22     3999   6745   2937  -1986     69   -369       O  
ATOM    154  CB  ARG B  22     -15.891  29.197 -16.021  1.00 36.82           C  
ANISOU  154  CB  ARG B  22     4133   6845   3014  -2142    155   -547       C  
ATOM    155  CG  ARG B  22     -16.380  30.498 -15.374  1.00 29.12           C  
ANISOU  155  CG  ARG B  22     3166   5812   2089  -2050    -11   -219       C  
ATOM    156  CD  ARG B  22     -17.737  30.275 -14.693  1.00 31.82           C  
ANISOU  156  CD  ARG B  22     3549   6032   2508  -2025    -60   -163       C  
ATOM    157  NE  ARG B  22     -18.218  31.422 -13.919  1.00 29.88           N  
ANISOU  157  NE  ARG B  22     3296   5680   2378  -1912   -203    114       N  
ATOM    158  CZ  ARG B  22     -19.504  31.726 -13.749  1.00 38.14           C  
ANISOU  158  CZ  ARG B  22     4314   6722   3455  -1907   -272    263       C  
ATOM    159  NH1 ARG B  22     -20.448  30.979 -14.306  1.00 42.75           N  
ANISOU  159  NH1 ARG B  22     4882   7424   3938  -2018   -220    170       N  
ATOM    160  NH2 ARG B  22     -19.851  32.781 -13.025  1.00 33.13           N  
ANISOU  160  NH2 ARG B  22     3655   5963   2967  -1786   -384    491       N  
ATOM    161  N   ILE B  23     -12.797  28.997 -14.982  1.00 34.62           N  
ANISOU  161  N   ILE B  23     3960   6268   2926  -1886    237   -845       N  
ATOM    162  CA  ILE B  23     -11.793  29.519 -14.057  1.00 25.26           C  
ANISOU  162  CA  ILE B  23     2844   4928   1826  -1719    192   -820       C  
ATOM    163  C   ILE B  23     -10.385  29.468 -14.630  1.00 31.04           C  
ANISOU  163  C   ILE B  23     3513   5746   2534  -1709    271   -961       C  
ATOM    164  O   ILE B  23      -9.430  29.834 -13.935  1.00 27.74           O  
ANISOU  164  O   ILE B  23     3141   5220   2181  -1565    255   -970       O  
ATOM    165  CB  ILE B  23     -11.819  28.780 -12.705  1.00 25.12           C  
ANISOU  165  CB  ILE B  23     2966   4524   2053  -1486    243   -880       C  
ATOM    166  CG1 ILE B  23     -11.313  27.346 -12.862  1.00 26.87           C  
ANISOU  166  CG1 ILE B  23     3220   4639   2351  -1484    390  -1210       C  
ATOM    167  CG2 ILE B  23     -13.210  28.823 -12.110  1.00 29.21           C  
ANISOU  167  CG2 ILE B  23     3533   4930   2634  -1472    187   -721       C  
ATOM    168  CD1 ILE B  23     -11.292  26.584 -11.565  1.00 30.47           C  
ANISOU  168  CD1 ILE B  23     3807   4718   3050  -1261    434  -1231       C  
ATOM    169  N   THR B  24     -10.224  29.025 -15.872  1.00 28.33           N  
ANISOU  169  N   THR B  24     3053   5609   2103  -1863    361  -1078       N  
ATOM    170  CA  THR B  24      -8.913  29.023 -16.503  1.00 34.90           C  
ANISOU  170  CA  THR B  24     3794   6551   2914  -1881    432  -1207       C  
ATOM    171  C   THR B  24      -8.458  30.456 -16.750  1.00 37.46           C  
ANISOU  171  C   THR B  24     4062   7032   3139  -1913    339   -956       C  
ATOM    172  O   THR B  24      -9.207  31.258 -17.312  1.00 53.10           O  
ANISOU  172  O   THR B  24     5985   9185   5006  -2037    268   -712       O  
ATOM    173  CB  THR B  24      -8.977  28.246 -17.818  1.00 32.63           C  
ANISOU  173  CB  THR B  24     3370   6483   2546  -2073    550  -1384       C  
ATOM    174  OG1 THR B  24      -9.254  26.866 -17.540  1.00 32.91           O  
ANISOU  174  OG1 THR B  24     3453   6332   2721  -2031    651  -1640       O  
ATOM    175  CG2 THR B  24      -7.665  28.363 -18.580  1.00 34.14           C  
ANISOU  175  CG2 THR B  24     3436   6835   2700  -2128    614  -1498       C  
ATOM    176  N   GLY B  25      -7.236  30.793 -16.313  1.00 33.65           N  
ANISOU  176  N   GLY B  25     3592   6476   2716  -1795    342  -1005       N  
ATOM    177  CA  GLY B  25      -6.703  32.105 -16.618  1.00 30.05           C  
ANISOU  177  CA  GLY B  25     3073   6165   2181  -1843    275   -792       C  
ATOM    178  C   GLY B  25      -6.221  32.828 -15.376  1.00 29.05           C  
ANISOU  178  C   GLY B  25     3038   5849   2150  -1652    201   -699       C  
ATOM    179  O   GLY B  25      -5.930  32.212 -14.344  1.00 24.98           O  
ANISOU  179  O   GLY B  25     2622   5115   1755  -1471    228   -851       O  
ATOM    180  N   LYS B  26      -6.159  34.154 -15.491  1.00 25.55           N  
ANISOU  180  N   LYS B  26     2552   5494   1662  -1700    114   -438       N  
ATOM    181  CA  LYS B  26      -5.573  35.036 -14.486  1.00 25.30           C  
ANISOU  181  CA  LYS B  26     2567   5336   1708  -1556     52   -341       C  
ATOM    182  C   LYS B  26      -6.669  35.640 -13.614  1.00 24.74           C  
ANISOU  182  C   LYS B  26     2552   5085   1762  -1463    -56    -97       C  
ATOM    183  O   LYS B  26      -7.688  36.113 -14.136  1.00 25.23           O  
ANISOU  183  O   LYS B  26     2569   5253   1765  -1592   -140    117       O  
ATOM    184  CB  LYS B  26      -4.781  36.150 -15.175  1.00 24.87           C  
ANISOU  184  CB  LYS B  26     2412   5453   1585  -1669     39   -202       C  
ATOM    185  CG  LYS B  26      -4.009  37.053 -14.240  1.00 23.61           C  
ANISOU  185  CG  LYS B  26     2277   5191   1502  -1543     -4   -140       C  
ATOM    186  CD  LYS B  26      -3.201  38.067 -15.054  1.00 25.87           C  
ANISOU  186  CD  LYS B  26     2459   5661   1709  -1691     -1    -22       C  
ATOM    187  CE  LYS B  26      -2.071  38.650 -14.223  1.00 29.25           C  
ANISOU  187  CE  LYS B  26     2896   5997   2219  -1560     16    -83       C  
ATOM    188  NZ  LYS B  26      -1.063  39.316 -15.099  1.00 31.30           N  
ANISOU  188  NZ  LYS B  26     3077   6447   2371  -1702     28    -75       N  
ATOM    189  N   TRP B  27      -6.460  35.608 -12.289  1.00 21.11           N  
ANISOU  189  N   TRP B  27     2172   4341   1506  -1225    -42   -126       N  
ATOM    190  CA  TRP B  27      -7.375  36.153 -11.295  1.00 22.27           C  
ANISOU  190  CA  TRP B  27     2359   4273   1829  -1100   -111     64       C  
ATOM    191  C   TRP B  27      -6.633  37.065 -10.328  1.00 24.31           C  
ANISOU  191  C   TRP B  27     2614   4386   2238   -945   -119    120       C  
ATOM    192  O   TRP B  27      -5.437  36.891 -10.079  1.00 19.83           O  
ANISOU  192  O   TRP B  27     2048   3818   1667   -867    -57    -39       O  
ATOM    193  CB  TRP B  27      -8.058  35.028 -10.503  1.00 19.56           C  
ANISOU  193  CB  TRP B  27     2117   3739   1576   -979    -74    -52       C  
ATOM    194  CG  TRP B  27      -8.921  34.201 -11.402  1.00 20.92           C  
ANISOU  194  CG  TRP B  27     2285   4041   1621  -1143    -62   -110       C  
ATOM    195  CD1 TRP B  27      -8.556  33.089 -12.109  1.00 24.18           C  
ANISOU  195  CD1 TRP B  27     2700   4562   1926  -1231     26   -354       C  
ATOM    196  CD2 TRP B  27     -10.293  34.458 -11.732  1.00 23.23           C  
ANISOU  196  CD2 TRP B  27     2550   4391   1886  -1251   -138     64       C  
ATOM    197  NE1 TRP B  27      -9.634  32.625 -12.851  1.00 26.74           N  
ANISOU  197  NE1 TRP B  27     3002   5016   2144  -1400     17   -353       N  
ATOM    198  CE2 TRP B  27     -10.703  33.458 -12.639  1.00 26.89           C  
ANISOU  198  CE2 TRP B  27     3001   5016   2200  -1413    -90    -88       C  
ATOM    199  CE3 TRP B  27     -11.211  35.442 -11.350  1.00 25.85           C  
ANISOU  199  CE3 TRP B  27     2849   4656   2318  -1227   -238    318       C  
ATOM    200  CZ2 TRP B  27     -11.999  33.411 -13.163  1.00 35.56           C  
ANISOU  200  CZ2 TRP B  27     4059   6231   3222  -1554   -146     18       C  
ATOM    201  CZ3 TRP B  27     -12.502  35.389 -11.870  1.00 23.18           C  
ANISOU  201  CZ3 TRP B  27     2469   4417   1921  -1352   -299    432       C  
ATOM    202  CH2 TRP B  27     -12.876  34.387 -12.769  1.00 31.30           C  
ANISOU  202  CH2 TRP B  27     3489   5629   2776  -1515   -255    287       C  
ATOM    203  N   PHE B  28      -7.367  38.014  -9.751  1.00 17.99           N  
ANISOU  203  N   PHE B  28     1792   3461   1581   -899   -189    325       N  
ATOM    204  CA  PHE B  28      -6.834  38.962  -8.784  1.00 18.28           C  
ANISOU  204  CA  PHE B  28     1806   3357   1784   -769   -192    368       C  
ATOM    205  C   PHE B  28      -7.591  38.844  -7.470  1.00 19.04           C  
ANISOU  205  C   PHE B  28     1950   3237   2046   -609   -200    371       C  
ATOM    206  O   PHE B  28      -8.826  38.801  -7.464  1.00 17.13           O  
ANISOU  206  O   PHE B  28     1713   2949   1845   -640   -248    478       O  
ATOM    207  CB  PHE B  28      -6.949  40.382  -9.313  1.00 17.88           C  
ANISOU  207  CB  PHE B  28     1654   3352   1789   -879   -258    604       C  
ATOM    208  CG  PHE B  28      -6.179  40.599 -10.569  1.00 20.42           C  
ANISOU  208  CG  PHE B  28     1918   3909   1931  -1056   -253    629       C  
ATOM    209  CD1 PHE B  28      -6.715  40.241 -11.801  1.00 23.08           C  
ANISOU  209  CD1 PHE B  28     2227   4463   2080  -1246   -289    705       C  
ATOM    210  CD2 PHE B  28      -4.894  41.128 -10.519  1.00 26.47           C  
ANISOU  210  CD2 PHE B  28     2649   4713   2698  -1049   -205    560       C  
ATOM    211  CE1 PHE B  28      -5.985  40.435 -12.976  1.00 27.69           C  
ANISOU  211  CE1 PHE B  28     2743   5309   2467  -1437   -279    722       C  
ATOM    212  CE2 PHE B  28      -4.165  41.321 -11.679  1.00 23.39           C  
ANISOU  212  CE2 PHE B  28     2199   4562   2126  -1231   -192    576       C  
ATOM    213  CZ  PHE B  28      -4.704  40.976 -12.906  1.00 27.74           C  
ANISOU  213  CZ  PHE B  28     2720   5341   2480  -1429   -229    658       C  
ATOM    214  N   TYR B  29      -6.849  38.809  -6.367  1.00 15.08           N  
ANISOU  214  N   TYR B  29     1471   2632   1626   -450   -153    251       N  
ATOM    215  CA  TYR B  29      -7.445  38.787  -5.037  1.00 14.48           C  
ANISOU  215  CA  TYR B  29     1423   2392   1689   -313   -155    246       C  
ATOM    216  C   TYR B  29      -7.935  40.188  -4.681  1.00 15.64           C  
ANISOU  216  C   TYR B  29     1475   2461   2009   -324   -198    390       C  
ATOM    217  O   TYR B  29      -7.177  41.165  -4.771  1.00 18.91           O  
ANISOU  217  O   TYR B  29     1813   2892   2482   -341   -191    413       O  
ATOM    218  CB  TYR B  29      -6.422  38.264  -4.022  1.00 14.50           C  
ANISOU  218  CB  TYR B  29     1461   2357   1693   -154    -96     79       C  
ATOM    219  CG  TYR B  29      -6.791  38.530  -2.588  1.00 15.55           C  
ANISOU  219  CG  TYR B  29     1585   2375   1949    -32    -95     77       C  
ATOM    220  CD1 TYR B  29      -8.030  38.149  -2.084  1.00 17.64           C  
ANISOU  220  CD1 TYR B  29     1892   2552   2260    -22   -115    131       C  
ATOM    221  CD2 TYR B  29      -5.890  39.138  -1.730  1.00 16.47           C  
ANISOU  221  CD2 TYR B  29     1640   2497   2120     57    -66      3       C  
ATOM    222  CE1 TYR B  29      -8.370  38.394  -0.773  1.00 13.70           C  
ANISOU  222  CE1 TYR B  29     1369   1983   1852     67   -108    114       C  
ATOM    223  CE2 TYR B  29      -6.218  39.397  -0.410  1.00 18.92           C  
ANISOU  223  CE2 TYR B  29     1921   2746   2520    146    -59    -20       C  
ATOM    224  CZ  TYR B  29      -7.462  39.036   0.060  1.00 19.59           C  
ANISOU  224  CZ  TYR B  29     2045   2754   2644    147    -79     37       C  
ATOM    225  OH  TYR B  29      -7.796  39.311   1.367  1.00 17.23           O  
ANISOU  225  OH  TYR B  29     1702   2427   2417    213    -65     -1       O  
ATOM    226  N   ILE B  30      -9.213  40.293  -4.309  1.00 13.84           N  
ANISOU  226  N   ILE B  30     1239   2141   1879   -320   -238    478       N  
ATOM    227  CA  ILE B  30      -9.878  41.578  -4.096  1.00 14.61           C  
ANISOU  227  CA  ILE B  30     1228   2146   2178   -337   -283    616       C  
ATOM    228  C   ILE B  30     -10.098  41.858  -2.614  1.00 19.96           C  
ANISOU  228  C   ILE B  30     1876   2697   3009   -213   -248    520       C  
ATOM    229  O   ILE B  30      -9.774  42.941  -2.127  1.00 18.77           O  
ANISOU  229  O   ILE B  30     1627   2480   3025   -187   -231    512       O  
ATOM    230  CB  ILE B  30     -11.222  41.644  -4.861  1.00 16.86           C  
ANISOU  230  CB  ILE B  30     1484   2441   2479   -438   -361    792       C  
ATOM    231  CG1 ILE B  30     -11.022  41.430  -6.362  1.00 15.79           C  
ANISOU  231  CG1 ILE B  30     1353   2484   2164   -589   -399    892       C  
ATOM    232  CG2 ILE B  30     -11.960  42.959  -4.546  1.00 17.67           C  
ANISOU  232  CG2 ILE B  30     1457   2413   2844   -429   -409    932       C  
ATOM    233  CD1 ILE B  30     -10.057  42.443  -7.029  1.00 17.32           C  
ANISOU  233  CD1 ILE B  30     1470   2739   2373   -662   -408    988       C  
ATOM    234  N   ALA B  31     -10.684  40.906  -1.888  1.00 17.23           N  
ANISOU  234  N   ALA B  31     1606   2326   2613   -153   -231    443       N  
ATOM    235  CA  ALA B  31     -11.121  41.163  -0.514  1.00 14.23           C  
ANISOU  235  CA  ALA B  31     1184   1866   2358    -68   -203    366       C  
ATOM    236  C   ALA B  31     -11.452  39.838   0.159  1.00 16.29           C  
ANISOU  236  C   ALA B  31     1558   2138   2494    -15   -178    290       C  
ATOM    237  O   ALA B  31     -11.722  38.843  -0.514  1.00 13.85           O  
ANISOU  237  O   ALA B  31     1346   1855   2061    -56   -189    316       O  
ATOM    238  CB  ALA B  31     -12.345  42.090  -0.484  1.00 14.64           C  
ANISOU  238  CB  ALA B  31     1125   1825   2612   -110   -246    466       C  
ATOM    239  N   SER B  32     -11.448  39.830   1.495  1.00 14.28           N  
ANISOU  239  N   SER B  32     1280   1869   2275     64   -139    195       N  
ATOM    240  CA  SER B  32     -11.851  38.611   2.196  1.00 14.21           C  
ANISOU  240  CA  SER B  32     1374   1866   2160    103   -120    161       C  
ATOM    241  C   SER B  32     -12.255  38.959   3.623  1.00 17.94           C  
ANISOU  241  C   SER B  32     1771   2346   2697    142    -90     90       C  
ATOM    242  O   SER B  32     -11.965  40.046   4.125  1.00 16.12           O  
ANISOU  242  O   SER B  32     1414   2128   2583    155    -71     24       O  
ATOM    243  CB  SER B  32     -10.734  37.563   2.227  1.00 13.52           C  
ANISOU  243  CB  SER B  32     1388   1822   1927    177    -93    110       C  
ATOM    244  OG  SER B  32      -9.607  38.034   2.968  1.00 19.84           O  
ANISOU  244  OG  SER B  32     2124   2687   2727    259    -66     26       O  
ATOM    245  N   ALA B  33     -12.912  38.004   4.278  1.00 14.42           N  
ANISOU  245  N   ALA B  33     1401   1905   2174    147    -79     92       N  
ATOM    246  CA  ALA B  33     -13.204  38.108   5.704  1.00 13.45           C  
ANISOU  246  CA  ALA B  33     1216   1840   2053    170    -44     20       C  
ATOM    247  C   ALA B  33     -13.419  36.706   6.244  1.00 14.99           C  
ANISOU  247  C   ALA B  33     1541   2051   2103    188    -33     61       C  
ATOM    248  O   ALA B  33     -14.009  35.870   5.562  1.00 13.50           O  
ANISOU  248  O   ALA B  33     1460   1789   1881    146    -47    131       O  
ATOM    249  CB  ALA B  33     -14.445  38.974   5.960  1.00 16.25           C  
ANISOU  249  CB  ALA B  33     1449   2161   2563    100    -45     -5       C  
ATOM    250  N   PHE B  34     -12.961  36.455   7.471  1.00 12.74           N  
ANISOU  250  N   PHE B  34     1236   1870   1735    240     -7     23       N  
ATOM    251  CA  PHE B  34     -13.082  35.132   8.073  1.00 12.66           C  
ANISOU  251  CA  PHE B  34     1342   1871   1596    261     -1     99       C  
ATOM    252  C   PHE B  34     -13.369  35.275   9.554  1.00 17.25           C  
ANISOU  252  C   PHE B  34     1840   2601   2114    242     25     63       C  
ATOM    253  O   PHE B  34     -13.027  36.278  10.183  1.00 18.46           O  
ANISOU  253  O   PHE B  34     1845   2873   2294    244     45    -49       O  
ATOM    254  CB  PHE B  34     -11.816  34.274   7.920  1.00 12.94           C  
ANISOU  254  CB  PHE B  34     1467   1901   1550    370    -10    143       C  
ATOM    255  CG  PHE B  34     -11.269  34.258   6.529  1.00 17.14           C  
ANISOU  255  CG  PHE B  34     2047   2340   2127    384    -24    134       C  
ATOM    256  CD1 PHE B  34     -10.396  35.243   6.113  1.00 19.62           C  
ANISOU  256  CD1 PHE B  34     2270   2703   2481    410    -28     62       C  
ATOM    257  CD2 PHE B  34     -11.645  33.267   5.640  1.00 13.03           C  
ANISOU  257  CD2 PHE B  34     1651   1697   1604    354    -24    184       C  
ATOM    258  CE1 PHE B  34      -9.897  35.241   4.815  1.00 20.50           C  
ANISOU  258  CE1 PHE B  34     2416   2761   2611    400    -38     56       C  
ATOM    259  CE2 PHE B  34     -11.156  33.261   4.342  1.00 17.57           C  
ANISOU  259  CE2 PHE B  34     2250   2227   2197    342    -30    155       C  
ATOM    260  CZ  PHE B  34     -10.283  34.263   3.936  1.00 15.04           C  
ANISOU  260  CZ  PHE B  34     1839   1976   1898    363    -39     98       C  
ATOM    261  N   ARG B  35     -13.986  34.242  10.107  1.00 13.90           N  
ANISOU  261  N   ARG B  35     1504   2179   1600    210     31    152       N  
ATOM    262  CA  ARG B  35     -13.991  34.085  11.561  1.00 14.86           C  
ANISOU  262  CA  ARG B  35     1565   2483   1598    195     50    157       C  
ATOM    263  C   ARG B  35     -12.760  33.342  12.063  1.00 20.61           C  
ANISOU  263  C   ARG B  35     2340   3287   2205    306     28    251       C  
ATOM    264  O   ARG B  35     -12.519  33.312  13.272  1.00 24.25           O  
ANISOU  264  O   ARG B  35     2725   3951   2539    302     32    265       O  
ATOM    265  CB  ARG B  35     -15.267  33.369  11.998  1.00 15.45           C  
ANISOU  265  CB  ARG B  35     1699   2545   1626     89     68    225       C  
ATOM    266  CG  ARG B  35     -16.489  34.264  11.819  1.00 21.67           C  
ANISOU  266  CG  ARG B  35     2384   3321   2529    -19     91    106       C  
ATOM    267  CD  ARG B  35     -17.775  33.533  12.073  1.00 19.91           C  
ANISOU  267  CD  ARG B  35     2223   3075   2266   -131    111    161       C  
ATOM    268  NE  ARG B  35     -18.903  34.464  12.046  1.00 22.15           N  
ANISOU  268  NE  ARG B  35     2371   3377   2666   -224    132     27       N  
ATOM    269  CZ  ARG B  35     -20.103  34.194  12.539  1.00 27.18           C  
ANISOU  269  CZ  ARG B  35     2989   4063   3274   -342    163      9       C  
ATOM    270  NH1 ARG B  35     -20.354  33.005  13.096  1.00 19.59           N  
ANISOU  270  NH1 ARG B  35     2147   3134   2162   -395    179    133       N  
ATOM    271  NH2 ARG B  35     -21.058  35.114  12.475  1.00 25.10           N  
ANISOU  271  NH2 ARG B  35     2579   3811   3148   -408    179   -128       N  
ATOM    272  N   ASN B  36     -11.967  32.763  11.162  1.00 19.34           N  
ANISOU  272  N   ASN B  36     2282   2987   2079    403      3    308       N  
ATOM    273  CA  ASN B  36     -10.794  31.975  11.539  1.00 20.56           C  
ANISOU  273  CA  ASN B  36     2476   3182   2154    529    -25    405       C  
ATOM    274  C   ASN B  36      -9.606  32.895  11.809  1.00 23.15           C  
ANISOU  274  C   ASN B  36     2666   3678   2453    601    -32    296       C  
ATOM    275  O   ASN B  36      -9.195  33.651  10.928  1.00 20.78           O  
ANISOU  275  O   ASN B  36     2329   3322   2243    613    -25    184       O  
ATOM    276  CB  ASN B  36     -10.452  30.987  10.426  1.00 19.79           C  
ANISOU  276  CB  ASN B  36     2525   2860   2136    596    -35    470       C  
ATOM    277  CG  ASN B  36      -9.179  30.217  10.698  1.00 24.35           C  
ANISOU  277  CG  ASN B  36     3123   3449   2680    747    -65    556       C  
ATOM    278  OD1 ASN B  36      -8.143  30.489  10.096  1.00 22.01           O  
ANISOU  278  OD1 ASN B  36     2794   3150   2419    834    -74    477       O  
ATOM    279  ND2 ASN B  36      -9.257  29.231  11.584  1.00 26.16           N  
ANISOU  279  ND2 ASN B  36     3402   3687   2849    778    -82    728       N  
ATOM    280  N   GLU B  37      -9.034  32.811  13.016  1.00 24.99           N  
ANISOU  280  N   GLU B  37     2948   4728   1819    196    201      6       N  
ATOM    281  CA  GLU B  37      -7.982  33.756  13.390  1.00 24.49           C  
ANISOU  281  CA  GLU B  37     2867   4801   1636    154     23   -103       C  
ATOM    282  C   GLU B  37      -6.732  33.592  12.523  1.00 23.55           C  
ANISOU  282  C   GLU B  37     2644   4635   1669    180   -122    -16       C  
ATOM    283  O   GLU B  37      -6.102  34.587  12.142  1.00 25.31           O  
ANISOU  283  O   GLU B  37     2816   4852   1950    121   -232   -160       O  
ATOM    284  CB  GLU B  37      -7.628  33.601  14.871  1.00 40.59           C  
ANISOU  284  CB  GLU B  37     4974   7112   3337    139    -32    -41       C  
ATOM    285  CG  GLU B  37      -6.753  34.736  15.386  1.00 56.75           C  
ANISOU  285  CG  GLU B  37     7009   9324   5230     50   -206   -228       C  
ATOM    286  CD  GLU B  37      -6.292  34.537  16.819  1.00 75.22           C  
ANISOU  286  CD  GLU B  37     9403  11985   7191     21   -297   -159       C  
ATOM    287  OE1 GLU B  37      -5.547  35.402  17.332  1.00 79.96           O  
ANISOU  287  OE1 GLU B  37     9994  12667   7721    -75   -437   -314       O  
ATOM    288  OE2 GLU B  37      -6.680  33.521  17.435  1.00 80.10           O  
ANISOU  288  OE2 GLU B  37    10078  12666   7688     82   -212     63       O  
ATOM    289  N   GLU B  38      -6.363  32.348  12.193  1.00 23.40           N  
ANISOU  289  N   GLU B  38     2591   4566   1735    267   -104    215       N  
ATOM    290  CA  GLU B  38      -5.142  32.110  11.422  1.00 22.93           C  
ANISOU  290  CA  GLU B  38     2417   4475   1820    311   -214    300       C  
ATOM    291  C   GLU B  38      -5.226  32.747  10.039  1.00 22.75           C  
ANISOU  291  C   GLU B  38     2342   4276   2025    265   -193    153       C  
ATOM    292  O   GLU B  38      -4.278  33.400   9.578  1.00 21.05           O  
ANISOU  292  O   GLU B  38     2040   4088   1871    228   -307     95       O  
ATOM    293  CB  GLU B  38      -4.875  30.606  11.293  1.00 31.94           C  
ANISOU  293  CB  GLU B  38     3543   5545   3049    432   -151    561       C  
ATOM    294  CG  GLU B  38      -4.291  29.959  12.549  1.00 44.44           C  
ANISOU  294  CG  GLU B  38     5134   7327   4423    506   -232    788       C  
ATOM    295  CD  GLU B  38      -5.354  29.479  13.538  1.00 59.98           C  
ANISOU  295  CD  GLU B  38     7239   9339   6212    500   -105    873       C  
ATOM    296  OE1 GLU B  38      -5.029  28.604  14.373  1.00 62.36           O  
ANISOU  296  OE1 GLU B  38     7565   9744   6387    584   -123   1135       O  
ATOM    297  OE2 GLU B  38      -6.511  29.962  13.482  1.00 47.42           O  
ANISOU  297  OE2 GLU B  38     5722   7684   4612    416     18    698       O  
ATOM    298  N   TYR B  39      -6.342  32.536   9.341  1.00 19.40           N  
ANISOU  298  N   TYR B  39     1959   3687   1726    258    -50    107       N  
ATOM    299  CA  TYR B  39      -6.495  33.157   8.029  1.00 20.82           C  
ANISOU  299  CA  TYR B  39     2094   3733   2085    214    -42     -9       C  
ATOM    300  C   TYR B  39      -6.515  34.676   8.148  1.00 19.94           C  
ANISOU  300  C   TYR B  39     1985   3645   1946    136   -117   -188       C  
ATOM    301  O   TYR B  39      -5.937  35.376   7.311  1.00 20.50           O  
ANISOU  301  O   TYR B  39     2000   3665   2126     93   -180   -241       O  
ATOM    302  CB  TYR B  39      -7.773  32.673   7.339  1.00 17.66           C  
ANISOU  302  CB  TYR B  39     1722   3195   1794    209    102    -26       C  
ATOM    303  CG  TYR B  39      -7.701  31.302   6.689  1.00 20.73           C  
ANISOU  303  CG  TYR B  39     2100   3482   2294    250    189     94       C  
ATOM    304  CD1 TYR B  39      -6.610  30.463   6.883  1.00 25.68           C  
ANISOU  304  CD1 TYR B  39     2702   4126   2930    326    164    240       C  
ATOM    305  CD2 TYR B  39      -8.732  30.854   5.872  1.00 20.40           C  
ANISOU  305  CD2 TYR B  39     2064   3324   2361    210    300     52       C  
ATOM    306  CE1 TYR B  39      -6.552  29.216   6.292  1.00 27.36           C  
ANISOU  306  CE1 TYR B  39     2916   4203   3277    371    271    329       C  
ATOM    307  CE2 TYR B  39      -8.691  29.605   5.275  1.00 19.64           C  
ANISOU  307  CE2 TYR B  39     1973   3113   2375    224    396    120       C  
ATOM    308  CZ  TYR B  39      -7.600  28.783   5.498  1.00 21.93           C  
ANISOU  308  CZ  TYR B  39     2259   3383   2691    309    395    253       C  
ATOM    309  OH  TYR B  39      -7.528  27.539   4.905  1.00 23.39           O  
ANISOU  309  OH  TYR B  39     2457   3413   3016    333    515    304       O  
ATOM    310  N   ASN B  40      -7.191  35.206   9.174  1.00 19.51           N  
ANISOU  310  N   ASN B  40     2003   3656   1756    113    -90   -288       N  
ATOM    311  CA  ASN B  40      -7.235  36.655   9.337  1.00 21.37           C  
ANISOU  311  CA  ASN B  40     2255   3874   1992     43   -135   -484       C  
ATOM    312  C   ASN B  40      -5.839  37.219   9.522  1.00 24.10           C  
ANISOU  312  C   ASN B  40     2551   4310   2294    -23   -294   -516       C  
ATOM    313  O   ASN B  40      -5.488  38.240   8.920  1.00 26.18           O  
ANISOU  313  O   ASN B  40     2785   4481   2681    -92   -341   -618       O  
ATOM    314  CB  ASN B  40      -8.116  37.043  10.522  1.00 23.43           C  
ANISOU  314  CB  ASN B  40     2604   4204   2095     33    -56   -610       C  
ATOM    315  CG  ASN B  40      -9.580  37.064  10.163  1.00 27.43           C  
ANISOU  315  CG  ASN B  40     3120   4589   2713     74    100   -651       C  
ATOM    316  OD1 ASN B  40      -9.940  37.399   9.038  1.00 30.12           O  
ANISOU  316  OD1 ASN B  40     3408   4783   3254     85    110   -657       O  
ATOM    317  ND2 ASN B  40     -10.433  36.719  11.116  1.00 29.15           N  
ANISOU  317  ND2 ASN B  40     3391   4890   2793     93    219   -668       N  
ATOM    318  N   LYS B  41      -5.026  36.555  10.342  1.00 24.46           N  
ANISOU  318  N   LYS B  41     2575   4543   2175     -7   -379   -411       N  
ATOM    319  CA  LYS B  41      -3.671  37.045  10.586  1.00 23.26           C  
ANISOU  319  CA  LYS B  41     2341   4523   1975    -81   -548   -438       C  
ATOM    320  C   LYS B  41      -2.820  36.987   9.320  1.00 27.15           C  
ANISOU  320  C   LYS B  41     2711   4924   2681    -80   -585   -360       C  
ATOM    321  O   LYS B  41      -2.009  37.885   9.086  1.00 30.04           O  
ANISOU  321  O   LYS B  41     3009   5299   3105   -184   -678   -453       O  
ATOM    322  CB  LYS B  41      -3.023  36.256  11.724  1.00 31.18           C  
ANISOU  322  CB  LYS B  41     3322   5778   2747    -43   -648   -301       C  
ATOM    323  CG  LYS B  41      -1.561  36.621  11.984  1.00 48.95           C  
ANISOU  323  CG  LYS B  41     5440   8212   4945   -116   -848   -301       C  
ATOM    324  CD  LYS B  41      -0.895  35.645  12.948  1.00 58.53           C  
ANISOU  324  CD  LYS B  41     6609   9653   5976    -37   -946    -87       C  
ATOM    325  CE  LYS B  41       0.616  35.875  13.034  1.00 64.92           C  
ANISOU  325  CE  LYS B  41     7282  10528   6855    -85  -1092    -49       C  
ATOM    326  NZ  LYS B  41       0.985  37.322  13.097  1.00 69.17           N  
ANISOU  326  NZ  LYS B  41     7830  11032   7420   -271  -1154   -304       N  
ATOM    327  N   SER B  42      -2.974  35.950   8.497  1.00 22.89           N  
ANISOU  327  N   SER B  42     2143   4295   2258     20   -498   -206       N  
ATOM    328  CA  SER B  42      -2.205  35.883   7.255  1.00 31.35           C  
ANISOU  328  CA  SER B  42     3107   5293   3513     18   -502   -153       C  
ATOM    329  C   SER B  42      -2.652  36.942   6.255  1.00 29.22           C  
ANISOU  329  C   SER B  42     2862   4862   3377    -65   -459   -273       C  
ATOM    330  O   SER B  42      -1.832  37.713   5.744  1.00 23.51           O  
ANISOU  330  O   SER B  42     2065   4132   2738   -152   -519   -311       O  
ATOM    331  CB  SER B  42      -2.303  34.492   6.620  1.00 25.84           C  
ANISOU  331  CB  SER B  42     2390   4526   2900    138   -397      5       C  
ATOM    332  OG  SER B  42      -2.110  33.471   7.576  1.00 49.14           O  
ANISOU  332  OG  SER B  42     5343   7580   5747    236   -411    150       O  
ATOM    333  N   VAL B  43      -3.947  36.977   5.931  1.00 22.66           N  
ANISOU  333  N   VAL B  43     2123   3907   2580    -40   -354   -311       N  
ATOM    334  CA  VAL B  43      -4.358  37.826   4.817  1.00 20.36           C  
ANISOU  334  CA  VAL B  43     1837   3471   2427    -90   -321   -362       C  
ATOM    335  C   VAL B  43      -4.294  39.305   5.179  1.00 20.77           C  
ANISOU  335  C   VAL B  43     1919   3468   2505   -183   -376   -503       C  
ATOM    336  O   VAL B  43      -4.240  40.142   4.278  1.00 22.37           O  
ANISOU  336  O   VAL B  43     2110   3551   2838   -238   -373   -511       O  
ATOM    337  CB  VAL B  43      -5.761  37.448   4.283  1.00 21.15           C  
ANISOU  337  CB  VAL B  43     1991   3476   2569    -35   -213   -350       C  
ATOM    338  CG1 VAL B  43      -5.845  35.950   4.032  1.00 24.40           C  
ANISOU  338  CG1 VAL B  43     2390   3915   2965     32   -144   -243       C  
ATOM    339  CG2 VAL B  43      -6.822  37.875   5.234  1.00 31.62           C  
ANISOU  339  CG2 VAL B  43     3391   4787   3837    -17   -175   -448       C  
ATOM    340  N   GLN B  44      -4.255  39.669   6.467  1.00 22.75           N  
ANISOU  340  N   GLN B  44     2215   3798   2632   -214   -420   -616       N  
ATOM    341  CA  GLN B  44      -4.247  41.094   6.783  1.00 24.12           C  
ANISOU  341  CA  GLN B  44     2432   3879   2853   -314   -447   -790       C  
ATOM    342  C   GLN B  44      -2.980  41.773   6.275  1.00 25.38           C  
ANISOU  342  C   GLN B  44     2508   4025   3111   -439   -537   -793       C  
ATOM    343  O   GLN B  44      -2.976  42.989   6.061  1.00 30.31           O  
ANISOU  343  O   GLN B  44     3165   4493   3859   -531   -533   -898       O  
ATOM    344  CB  GLN B  44      -4.409  41.325   8.294  1.00 31.01           C  
ANISOU  344  CB  GLN B  44     3378   4867   3540   -344   -469   -948       C  
ATOM    345  CG  GLN B  44      -3.406  40.596   9.155  1.00 50.42           C  
ANISOU  345  CG  GLN B  44     5779   7579   5800   -366   -586   -893       C  
ATOM    346  CD  GLN B  44      -3.382  41.106  10.585  1.00 73.59           C  
ANISOU  346  CD  GLN B  44     8785  10656   8520   -448   -636  -1081       C  
ATOM    347  OE1 GLN B  44      -4.325  41.753  11.038  1.00 77.81           O  
ANISOU  347  OE1 GLN B  44     9430  11097   9036   -453   -538  -1252       O  
ATOM    348  NE2 GLN B  44      -2.310  40.798  11.307  1.00 73.47           N  
ANISOU  348  NE2 GLN B  44     8698  10884   8332   -507   -786  -1052       N  
ATOM    349  N   GLU B  45      -1.911  41.012   6.041  1.00 25.01           N  
ANISOU  349  N   GLU B  45     2345   4123   3036   -441   -601   -671       N  
ATOM    350  CA  GLU B  45      -0.659  41.578   5.552  1.00 23.08           C  
ANISOU  350  CA  GLU B  45     1985   3894   2889   -566   -673   -664       C  
ATOM    351  C   GLU B  45      -0.557  41.601   4.028  1.00 24.59           C  
ANISOU  351  C   GLU B  45     2134   3969   3242   -562   -596   -539       C  
ATOM    352  O   GLU B  45       0.410  42.149   3.490  1.00 24.90           O  
ANISOU  352  O   GLU B  45     2079   4002   3378   -678   -624   -521       O  
ATOM    353  CB  GLU B  45       0.528  40.807   6.137  1.00 24.62           C  
ANISOU  353  CB  GLU B  45     2040   4336   2980   -565   -784   -596       C  
ATOM    354  CG  GLU B  45       0.473  40.658   7.654  1.00 29.49           C  
ANISOU  354  CG  GLU B  45     2709   5110   3386   -561   -868   -674       C  
ATOM    355  CD  GLU B  45       0.458  42.000   8.391  1.00 44.85           C  
ANISOU  355  CD  GLU B  45     4738   6998   5304   -720   -912   -900       C  
ATOM    356  OE1 GLU B  45       0.994  42.992   7.856  1.00 40.23           O  
ANISOU  356  OE1 GLU B  45     4126   6281   4878   -851   -919   -961       O  
ATOM    357  OE2 GLU B  45      -0.096  42.062   9.513  1.00 48.05           O  
ANISOU  357  OE2 GLU B  45     5246   7481   5529   -717   -923  -1018       O  
ATOM    358  N   ILE B  46      -1.527  41.051   3.312  1.00 21.56           N  
ANISOU  358  N   ILE B  46     1810   3507   2875   -452   -500   -457       N  
ATOM    359  CA  ILE B  46      -1.423  40.958   1.859  1.00 20.78           C  
ANISOU  359  CA  ILE B  46     1674   3348   2872   -454   -433   -339       C  
ATOM    360  C   ILE B  46      -1.799  42.303   1.244  1.00 23.92           C  
ANISOU  360  C   ILE B  46     2131   3563   3395   -537   -415   -355       C  
ATOM    361  O   ILE B  46      -2.888  42.827   1.495  1.00 28.43           O  
ANISOU  361  O   ILE B  46     2800   4010   3994   -495   -393   -410       O  
ATOM    362  CB  ILE B  46      -2.318  39.834   1.319  1.00 19.91           C  
ANISOU  362  CB  ILE B  46     1602   3246   2717   -329   -350   -264       C  
ATOM    363  CG1 ILE B  46      -1.862  38.483   1.887  1.00 17.23           C  
ANISOU  363  CG1 ILE B  46     1210   3042   2295   -242   -348   -223       C  
ATOM    364  CG2 ILE B  46      -2.325  39.846  -0.208  1.00 21.00           C  
ANISOU  364  CG2 ILE B  46     1721   3346   2914   -353   -284   -170       C  
ATOM    365  CD1 ILE B  46      -2.836  37.328   1.605  1.00 17.74           C  
ANISOU  365  CD1 ILE B  46     1331   3084   2326   -137   -256   -181       C  
ATOM    366  N   GLN B  47      -0.906  42.857   0.422  1.00 20.05           N  
ANISOU  366  N   GLN B  47     1573   3050   2996   -648   -410   -289       N  
ATOM    367  CA  GLN B  47      -1.215  44.114  -0.254  1.00 20.61           C  
ANISOU  367  CA  GLN B  47     1704   2925   3201   -724   -382   -253       C  
ATOM    368  C   GLN B  47      -1.875  43.884  -1.604  1.00 20.39           C  
ANISOU  368  C   GLN B  47     1703   2873   3171   -664   -315    -93       C  
ATOM    369  O   GLN B  47      -2.799  44.618  -1.982  1.00 22.11           O  
ANISOU  369  O   GLN B  47     1999   2939   3461   -632   -300    -44       O  
ATOM    370  CB  GLN B  47       0.063  44.943  -0.431  1.00 21.64           C  
ANISOU  370  CB  GLN B  47     1754   3032   3435   -906   -402   -252       C  
ATOM    371  CG  GLN B  47       0.660  45.456   0.885  1.00 25.83           C  
ANISOU  371  CG  GLN B  47     2263   3576   3976  -1012   -490   -439       C  
ATOM    372  CD  GLN B  47       2.070  45.994   0.716  1.00 37.90           C  
ANISOU  372  CD  GLN B  47     3659   5148   5595  -1209   -520   -439       C  
ATOM    373  OE1 GLN B  47       2.977  45.260   0.332  1.00 31.88           O  
ANISOU  373  OE1 GLN B  47     2746   4572   4794  -1215   -520   -354       O  
ATOM    374  NE2 GLN B  47       2.266  47.273   1.022  1.00 35.45           N  
ANISOU  374  NE2 GLN B  47     3392   4655   5423  -1374   -534   -546       N  
ATOM    375  N   ALA B  48      -1.406  42.881  -2.339  1.00 22.72           N  
ANISOU  375  N   ALA B  48     1928   3323   3381   -644   -273    -15       N  
ATOM    376  CA  ALA B  48      -1.976  42.514  -3.625  1.00 23.02           C  
ANISOU  376  CA  ALA B  48     1990   3392   3364   -607   -213    108       C  
ATOM    377  C   ALA B  48      -1.685  41.037  -3.864  1.00 22.92           C  
ANISOU  377  C   ALA B  48     1922   3546   3240   -545   -161     92       C  
ATOM    378  O   ALA B  48      -0.780  40.462  -3.257  1.00 21.47           O  
ANISOU  378  O   ALA B  48     1657   3445   3056   -538   -163     41       O  
ATOM    379  CB  ALA B  48      -1.402  43.385  -4.752  1.00 21.72           C  
ANISOU  379  CB  ALA B  48     1810   3189   3253   -727   -176    247       C  
ATOM    380  N   THR B  49      -2.474  40.419  -4.739  1.00 17.83           N  
ANISOU  380  N   THR B  49     1317   2947   2511   -499   -114    135       N  
ATOM    381  CA  THR B  49      -2.170  39.061  -5.181  1.00 18.67           C  
ANISOU  381  CA  THR B  49     1385   3176   2533   -460    -32    106       C  
ATOM    382  C   THR B  49      -2.890  38.797  -6.491  1.00 15.97           C  
ANISOU  382  C   THR B  49     1088   2894   2085   -482     15    154       C  
ATOM    383  O   THR B  49      -4.087  39.062  -6.601  1.00 18.89           O  
ANISOU  383  O   THR B  49     1516   3229   2431   -457    -38    176       O  
ATOM    384  CB  THR B  49      -2.597  37.993  -4.160  1.00 20.84           C  
ANISOU  384  CB  THR B  49     1673   3450   2795   -352    -35     15       C  
ATOM    385  OG1 THR B  49      -1.754  38.064  -3.008  1.00 18.40           O  
ANISOU  385  OG1 THR B  49     1306   3146   2537   -335    -84    -17       O  
ATOM    386  CG2 THR B  49      -2.467  36.587  -4.779  1.00 18.56           C  
ANISOU  386  CG2 THR B  49     1368   3232   2450   -312     74    -17       C  
ATOM    387  N   PHE B  50      -2.169  38.258  -7.468  1.00 18.40           N  
ANISOU  387  N   PHE B  50     1358   3311   2321   -529    116    163       N  
ATOM    388  CA  PHE B  50      -2.825  37.666  -8.623  1.00 20.01           C  
ANISOU  388  CA  PHE B  50     1610   3616   2379   -555    170    155       C  
ATOM    389  C   PHE B  50      -2.258  36.276  -8.857  1.00 22.09           C  
ANISOU  389  C   PHE B  50     1842   3944   2607   -527    305     34       C  
ATOM    390  O   PHE B  50      -1.193  35.923  -8.349  1.00 18.17           O  
ANISOU  390  O   PHE B  50     1266   3433   2203   -485    363      6       O  
ATOM    391  CB  PHE B  50      -2.695  38.542  -9.882  1.00 18.40           C  
ANISOU  391  CB  PHE B  50     1421   3495   2077   -663    179    293       C  
ATOM    392  CG  PHE B  50      -1.274  38.833 -10.310  1.00 21.33           C  
ANISOU  392  CG  PHE B  50     1721   3919   2465   -741    279    341       C  
ATOM    393  CD1 PHE B  50      -0.608  38.000 -11.202  1.00 20.52           C  
ANISOU  393  CD1 PHE B  50     1585   3959   2251   -778    432    280       C  
ATOM    394  CD2 PHE B  50      -0.626  39.970  -9.863  1.00 20.03           C  
ANISOU  394  CD2 PHE B  50     1517   3660   2435   -791    236    435       C  
ATOM    395  CE1 PHE B  50       0.687  38.284 -11.602  1.00 21.84           C  
ANISOU  395  CE1 PHE B  50     1666   4186   2445   -847    541    325       C  
ATOM    396  CE2 PHE B  50       0.673  40.266 -10.273  1.00 22.94           C  
ANISOU  396  CE2 PHE B  50     1795   4089   2833   -886    333    484       C  
ATOM    397  CZ  PHE B  50       1.328  39.421 -11.137  1.00 23.01           C  
ANISOU  397  CZ  PHE B  50     1759   4250   2733   -903    486    435       C  
ATOM    398  N   PHE B  51      -2.996  35.471  -9.614  1.00 18.12           N  
ANISOU  398  N   PHE B  51     1394   3508   1982   -549    356    -44       N  
ATOM    399  CA  PHE B  51      -2.577  34.099  -9.831  1.00 21.05           C  
ANISOU  399  CA  PHE B  51     1757   3893   2347   -519    507   -188       C  
ATOM    400  C   PHE B  51      -3.167  33.595 -11.134  1.00 21.83           C  
ANISOU  400  C   PHE B  51     1919   4118   2256   -617    573   -275       C  
ATOM    401  O   PHE B  51      -4.100  34.186 -11.678  1.00 19.25           O  
ANISOU  401  O   PHE B  51     1635   3875   1805   -689    467   -211       O  
ATOM    402  CB  PHE B  51      -2.982  33.182  -8.674  1.00 16.88           C  
ANISOU  402  CB  PHE B  51     1241   3232   1940   -410    502   -264       C  
ATOM    403  CG  PHE B  51      -4.471  33.069  -8.456  1.00 20.92           C  
ANISOU  403  CG  PHE B  51     1822   3715   2413   -425    416   -292       C  
ATOM    404  CD1 PHE B  51      -5.216  32.119  -9.140  1.00 17.88           C  
ANISOU  404  CD1 PHE B  51     1486   3361   1945   -484    483   -419       C  
ATOM    405  CD2 PHE B  51      -5.118  33.895  -7.543  1.00 17.69           C  
ANISOU  405  CD2 PHE B  51     1414   3247   2060   -387    280   -210       C  
ATOM    406  CE1 PHE B  51      -6.590  32.000  -8.929  1.00 20.15           C  
ANISOU  406  CE1 PHE B  51     1803   3640   2212   -512    402   -446       C  
ATOM    407  CE2 PHE B  51      -6.491  33.775  -7.319  1.00 18.07           C  
ANISOU  407  CE2 PHE B  51     1494   3280   2092   -391    219   -236       C  
ATOM    408  CZ  PHE B  51      -7.227  32.830  -8.015  1.00 18.65           C  
ANISOU  408  CZ  PHE B  51     1595   3403   2090   -457    273   -344       C  
ATOM    409  N   TYR B  52      -2.613  32.484 -11.610  1.00 21.82           N  
ANISOU  409  N   TYR B  52     1918   4134   2239   -617    750   -425       N  
ATOM    410  CA  TYR B  52      -3.051  31.820 -12.835  1.00 23.78           C  
ANISOU  410  CA  TYR B  52     2248   4483   2305   -717    827   -565       C  
ATOM    411  C   TYR B  52      -3.489  30.395 -12.528  1.00 24.48           C  
ANISOU  411  C   TYR B  52     2388   4432   2481   -678    913   -756       C  
ATOM    412  O   TYR B  52      -2.765  29.657 -11.850  1.00 23.49           O  
ANISOU  412  O   TYR B  52     2242   4137   2546   -552   1006   -786       O  
ATOM    413  CB  TYR B  52      -1.927  31.761 -13.868  1.00 23.55           C  
ANISOU  413  CB  TYR B  52     2224   4515   2207   -744    953   -585       C  
ATOM    414  CG  TYR B  52      -1.416  33.088 -14.369  1.00 28.31           C  
ANISOU  414  CG  TYR B  52     2790   5246   2719   -809    903   -397       C  
ATOM    415  CD1 TYR B  52      -0.440  33.796 -13.664  1.00 26.24           C  
ANISOU  415  CD1 TYR B  52     2435   4912   2624   -746    893   -264       C  
ATOM    416  CD2 TYR B  52      -1.869  33.612 -15.572  1.00 29.71           C  
ANISOU  416  CD2 TYR B  52     3025   5615   2647   -943    865   -343       C  
ATOM    417  CE1 TYR B  52       0.049  35.005 -14.140  1.00 26.24           C  
ANISOU  417  CE1 TYR B  52     2408   4996   2568   -826    864    -92       C  
ATOM    418  CE2 TYR B  52      -1.389  34.821 -16.056  1.00 31.45           C  
ANISOU  418  CE2 TYR B  52     3224   5927   2797  -1003    833   -139       C  
ATOM    419  CZ  TYR B  52      -0.431  35.513 -15.335  1.00 29.14           C  
ANISOU  419  CZ  TYR B  52     2846   5529   2698   -949    843    -19       C  
ATOM    420  OH  TYR B  52       0.046  36.713 -15.816  1.00 29.74           O  
ANISOU  420  OH  TYR B  52     2906   5662   2730  -1027    825    182       O  
ATOM    421  N   PHE B  53      -4.644  29.998 -13.068  1.00 25.66           N  
ANISOU  421  N   PHE B  53     2598   4658   2492   -794    882   -872       N  
ATOM    422  CA  PHE B  53      -5.140  28.623 -13.016  1.00 27.28           C  
ANISOU  422  CA  PHE B  53     2867   4731   2769   -811    977  -1077       C  
ATOM    423  C   PHE B  53      -4.960  27.978 -14.384  1.00 29.58           C  
ANISOU  423  C   PHE B  53     3226   5097   2916   -928   1076  -1249       C  
ATOM    424  O   PHE B  53      -5.394  28.546 -15.387  1.00 28.83           O  
ANISOU  424  O   PHE B  53     3143   5228   2584  -1063    992  -1236       O  
ATOM    425  CB  PHE B  53      -6.638  28.577 -12.671  1.00 22.57           C  
ANISOU  425  CB  PHE B  53     2274   4173   2130   -892    867  -1113       C  
ATOM    426  CG  PHE B  53      -6.963  28.655 -11.197  1.00 24.01           C  
ANISOU  426  CG  PHE B  53     2425   4170   2527   -761    789   -992       C  
ATOM    427  CD1 PHE B  53      -6.017  28.392 -10.222  1.00 22.64           C  
ANISOU  427  CD1 PHE B  53     2229   3824   2549   -603    867   -928       C  
ATOM    428  CD2 PHE B  53      -8.255  28.967 -10.803  1.00 23.40           C  
ANISOU  428  CD2 PHE B  53     2332   4118   2441   -799    639   -945       C  
ATOM    429  CE1 PHE B  53      -6.353  28.462  -8.868  1.00 18.45           C  
ANISOU  429  CE1 PHE B  53     1682   3161   2165   -499    791   -817       C  
ATOM    430  CE2 PHE B  53      -8.607  29.035  -9.454  1.00 23.32           C  
ANISOU  430  CE2 PHE B  53     2301   3961   2601   -690    589   -849       C  
ATOM    431  CZ  PHE B  53      -7.651  28.780  -8.488  1.00 23.80           C  
ANISOU  431  CZ  PHE B  53     2362   3863   2819   -547    665   -787       C  
ATOM    432  N   THR B  54      -4.375  26.780 -14.421  1.00 27.07           N  
ANISOU  432  N   THR B  54     2949   4593   2742   -875   1248  -1398       N  
ATOM    433  CA  THR B  54      -4.356  25.952 -15.630  1.00 29.87           C  
ANISOU  433  CA  THR B  54     3374   4983   2992   -997   1362  -1607       C  
ATOM    434  C   THR B  54      -4.841  24.547 -15.286  1.00 35.21           C  
ANISOU  434  C   THR B  54     4108   5428   3841  -1014   1474  -1796       C  
ATOM    435  O   THR B  54      -4.061  23.717 -14.785  1.00 32.84           O  
ANISOU  435  O   THR B  54     3818   4893   3769   -873   1625  -1823       O  
ATOM    436  CB  THR B  54      -2.966  25.905 -16.255  1.00 38.01           C  
ANISOU  436  CB  THR B  54     4395   6021   4027   -925   1507  -1609       C  
ATOM    437  OG1 THR B  54      -2.511  27.241 -16.484  1.00 46.01           O  
ANISOU  437  OG1 THR B  54     5350   7223   4907   -921   1414  -1411       O  
ATOM    438  CG2 THR B  54      -3.017  25.162 -17.589  1.00 45.02           C  
ANISOU  438  CG2 THR B  54     5357   6983   4767  -1070   1621  -1832       C  
ATOM    439  N   PRO B  55      -6.112  24.247 -15.530  1.00 31.54           N  
ANISOU  439  N   PRO B  55     3670   5023   3289  -1183   1404  -1913       N  
ATOM    440  CA  PRO B  55      -6.644  22.932 -15.164  1.00 33.92           C  
ANISOU  440  CA  PRO B  55     4024   5089   3776  -1225   1519  -2082       C  
ATOM    441  C   PRO B  55      -6.128  21.810 -16.054  1.00 40.32           C  
ANISOU  441  C   PRO B  55     4902   5795   4621  -1282   1715  -2297       C  
ATOM    442  O   PRO B  55      -5.820  21.995 -17.236  1.00 42.58           O  
ANISOU  442  O   PRO B  55     5203   6270   4706  -1375   1733  -2379       O  
ATOM    443  CB  PRO B  55      -8.158  23.108 -15.328  1.00 39.23           C  
ANISOU  443  CB  PRO B  55     4673   5923   4310  -1415   1370  -2131       C  
ATOM    444  CG  PRO B  55      -8.383  24.586 -15.247  1.00 38.41           C  
ANISOU  444  CG  PRO B  55     4497   6069   4027  -1389   1165  -1924       C  
ATOM    445  CD  PRO B  55      -7.176  25.196 -15.883  1.00 32.31           C  
ANISOU  445  CD  PRO B  55     3727   5394   3156  -1317   1198  -1840       C  
ATOM    446  N   ASN B  56      -6.033  20.628 -15.451  1.00 40.27           N  
ANISOU  446  N   ASN B  56     4941   5479   4880  -1220   1874  -2381       N  
ATOM    447  CA  ASN B  56      -5.785  19.370 -16.147  1.00 40.32           C  
ANISOU  447  CA  ASN B  56     5018   5330   4971  -1289   2079  -2611       C  
ATOM    448  C   ASN B  56      -7.010  18.510 -15.849  1.00 42.48           C  
ANISOU  448  C   ASN B  56     5326   5470   5344  -1442   2102  -2735       C  
ATOM    449  O   ASN B  56      -7.126  17.927 -14.765  1.00 41.48           O  
ANISOU  449  O   ASN B  56     5214   5070   5475  -1343   2170  -2666       O  
ATOM    450  CB  ASN B  56      -4.474  18.730 -15.681  1.00 44.34           C  
ANISOU  450  CB  ASN B  56     5535   5571   5740  -1056   2265  -2563       C  
ATOM    451  CG  ASN B  56      -4.189  17.388 -16.351  1.00 53.88           C  
ANISOU  451  CG  ASN B  56     6818   6585   7069  -1108   2499  -2804       C  
ATOM    452  OD1 ASN B  56      -5.070  16.757 -16.938  1.00 49.07           O  
ANISOU  452  OD1 ASN B  56     6264   5980   6400  -1323   2538  -3012       O  
ATOM    453  ND2 ASN B  56      -2.925  16.977 -16.309  1.00 57.71           N  
ANISOU  453  ND2 ASN B  56     7291   6920   7718   -912   2658  -2778       N  
ATOM    454  N   LYS B  57      -7.927  18.441 -16.815  1.00 44.93           N  
ANISOU  454  N   LYS B  57     5640   5988   5441  -1684   2045  -2902       N  
ATOM    455  CA  LYS B  57      -9.231  17.832 -16.572  1.00 43.98           C  
ANISOU  455  CA  LYS B  57     5520   5819   5372  -1850   2028  -2998       C  
ATOM    456  C   LYS B  57      -9.122  16.334 -16.316  1.00 53.13           C  
ANISOU  456  C   LYS B  57     6758   6615   6813  -1854   2271  -3153       C  
ATOM    457  O   LYS B  57      -9.782  15.808 -15.412  1.00 47.64           O  
ANISOU  457  O   LYS B  57     6069   5720   6313  -1858   2304  -3116       O  
ATOM    458  CB  LYS B  57     -10.160  18.120 -17.749  1.00 46.29           C  
ANISOU  458  CB  LYS B  57     5778   6455   5354  -2092   1900  -3125       C  
ATOM    459  CG  LYS B  57     -10.391  19.606 -17.960  1.00 43.50           C  
ANISOU  459  CG  LYS B  57     5342   6449   4739  -2080   1652  -2930       C  
ATOM    460  CD  LYS B  57     -11.191  19.892 -19.215  1.00 52.90           C  
ANISOU  460  CD  LYS B  57     6496   7992   5612  -2291   1523  -3017       C  
ATOM    461  CE  LYS B  57     -11.375  21.393 -19.397  1.00 52.49           C  
ANISOU  461  CE  LYS B  57     6361   8256   5326  -2249   1282  -2775       C  
ATOM    462  NZ  LYS B  57     -11.792  21.748 -20.783  1.00 53.82           N  
ANISOU  462  NZ  LYS B  57     6508   8776   5164  -2416   1173  -2818       N  
ATOM    463  N   THR B  58      -8.299  15.628 -17.096  1.00 49.70           N  
ANISOU  463  N   THR B  58     6387   6085   6412  -1851   2453  -3322       N  
ATOM    464  CA  THR B  58      -8.188  14.185 -16.915  1.00 52.82           C  
ANISOU  464  CA  THR B  58     6860   6122   7087  -1854   2697  -3472       C  
ATOM    465  C   THR B  58      -7.578  13.819 -15.567  1.00 55.21           C  
ANISOU  465  C   THR B  58     7173   6076   7728  -1599   2792  -3262       C  
ATOM    466  O   THR B  58      -7.881  12.751 -15.025  1.00 58.66           O  
ANISOU  466  O   THR B  58     7661   6207   8420  -1604   2943  -3298       O  
ATOM    467  CB  THR B  58      -7.375  13.567 -18.060  1.00 63.81           C  
ANISOU  467  CB  THR B  58     8313   7492   8438  -1889   2881  -3703       C  
ATOM    468  OG1 THR B  58      -5.976  13.808 -17.851  1.00 65.04           O  
ANISOU  468  OG1 THR B  58     8460   7557   8695  -1632   2955  -3572       O  
ATOM    469  CG2 THR B  58      -7.799  14.155 -19.396  1.00 57.96           C  
ANISOU  469  CG2 THR B  58     7556   7154   7312  -2109   2762  -3856       C  
ATOM    470  N   GLU B  59      -6.737  14.685 -14.998  1.00 48.31           N  
ANISOU  470  N   GLU B  59     6250   5250   6858  -1377   2703  -3029       N  
ATOM    471  CA  GLU B  59      -6.056  14.373 -13.750  1.00 47.26           C  
ANISOU  471  CA  GLU B  59     6112   4824   7020  -1116   2777  -2807       C  
ATOM    472  C   GLU B  59      -6.752  14.952 -12.526  1.00 52.71           C  
ANISOU  472  C   GLU B  59     6766   5517   7746  -1070   2627  -2588       C  
ATOM    473  O   GLU B  59      -6.331  14.657 -11.402  1.00 43.28           O  
ANISOU  473  O   GLU B  59     5571   4089   6786   -866   2680  -2384       O  
ATOM    474  CB  GLU B  59      -4.610  14.881 -13.793  1.00 47.28           C  
ANISOU  474  CB  GLU B  59     6065   4873   7027   -879   2784  -2678       C  
ATOM    475  CG  GLU B  59      -3.773  14.295 -14.931  1.00 57.97           C  
ANISOU  475  CG  GLU B  59     7450   6208   8369   -888   2963  -2885       C  
ATOM    476  CD  GLU B  59      -3.547  12.807 -14.794  1.00 79.55           C  
ANISOU  476  CD  GLU B  59    10250   8566  11410   -840   3215  -2990       C  
ATOM    477  OE1 GLU B  59      -4.117  12.035 -15.597  1.00 90.19           O  
ANISOU  477  OE1 GLU B  59    11671   9865  12731  -1049   3334  -3260       O  
ATOM    478  OE2 GLU B  59      -2.791  12.407 -13.885  1.00 87.67           O  
ANISOU  478  OE2 GLU B  59    11251   9353  12705   -591   3292  -2796       O  
ATOM    479  N   ASP B  60      -7.801  15.754 -12.724  1.00 40.35           N  
ANISOU  479  N   ASP B  60     4960   4088   6285  -1202   2284  -2547       N  
ATOM    480  CA  ASP B  60      -8.516  16.421 -11.632  1.00 37.37           C  
ANISOU  480  CA  ASP B  60     4600   3690   5908  -1088   2138  -2316       C  
ATOM    481  C   ASP B  60      -7.567  17.288 -10.811  1.00 34.61           C  
ANISOU  481  C   ASP B  60     4256   3369   5526   -811   2036  -2065       C  
ATOM    482  O   ASP B  60      -7.616  17.302  -9.582  1.00 34.09           O  
ANISOU  482  O   ASP B  60     4209   3135   5608   -605   2032  -1824       O  
ATOM    483  CB  ASP B  60      -9.243  15.416 -10.735  1.00 41.46           C  
ANISOU  483  CB  ASP B  60     5133   3884   6737  -1036   2274  -2230       C  
ATOM    484  CG  ASP B  60     -10.536  14.902 -11.351  1.00 53.01           C  
ANISOU  484  CG  ASP B  60     6573   5391   8179  -1315   2304  -2439       C  
ATOM    485  OD1 ASP B  60     -10.930  15.393 -12.432  1.00 54.14           O  
ANISOU  485  OD1 ASP B  60     6691   5839   8040  -1543   2182  -2622       O  
ATOM    486  OD2 ASP B  60     -11.162  14.005 -10.745  1.00 51.86           O  
ANISOU  486  OD2 ASP B  60     6431   4990   8284  -1304   2436  -2396       O  
ATOM    487  N   THR B  61      -6.682  18.006 -11.496  1.00 37.17           N  
ANISOU  487  N   THR B  61     4558   3926   5638   -816   1961  -2110       N  
ATOM    488  CA  THR B  61      -5.764  18.929 -10.851  1.00 38.12           C  
ANISOU  488  CA  THR B  61     4659   4135   5690   -583   1853  -1892       C  
ATOM    489  C   THR B  61      -5.859  20.288 -11.533  1.00 32.95           C  
ANISOU  489  C   THR B  61     3991   3851   4680   -721   1664  -1921       C  
ATOM    490  O   THR B  61      -6.391  20.417 -12.638  1.00 37.05           O  
ANISOU  490  O   THR B  61     4516   4567   4994   -992   1619  -2103       O  
ATOM    491  CB  THR B  61      -4.307  18.412 -10.882  1.00 37.89           C  
ANISOU  491  CB  THR B  61     4585   3993   5820   -409   1969  -1869       C  
ATOM    492  OG1 THR B  61      -3.897  18.163 -12.236  1.00 40.80           O  
ANISOU  492  OG1 THR B  61     4937   4477   6089   -608   2057  -2130       O  
ATOM    493  CG2 THR B  61      -4.176  17.124 -10.086  1.00 37.49           C  
ANISOU  493  CG2 THR B  61     4532   3569   6143   -248   2133  -1775       C  
ATOM    494  N   ILE B  62      -5.349  21.311 -10.851  1.00 30.27           N  
ANISOU  494  N   ILE B  62     3622   3621   4259   -545   1545  -1716       N  
ATOM    495  CA  ILE B  62      -5.196  22.649 -11.413  1.00 27.82           C  
ANISOU  495  CA  ILE B  62     3284   3643   3643   -645   1366  -1679       C  
ATOM    496  C   ILE B  62      -3.790  23.124 -11.087  1.00 29.97           C  
ANISOU  496  C   ILE B  62     3501   3962   3923   -451   1369  -1555       C  
ATOM    497  O   ILE B  62      -3.387  23.112  -9.919  1.00 27.55           O  
ANISOU  497  O   ILE B  62     3168   3525   3776   -214   1361  -1362       O  
ATOM    498  CB  ILE B  62      -6.228  23.650 -10.855  1.00 29.80           C  
ANISOU  498  CB  ILE B  62     3519   3989   3813   -656   1111  -1447       C  
ATOM    499  CG1 ILE B  62      -7.666  23.207 -11.135  1.00 30.06           C  
ANISOU  499  CG1 ILE B  62     3561   3987   3876   -845   1081  -1541       C  
ATOM    500  CG2 ILE B  62      -5.990  25.043 -11.446  1.00 27.86           C  
ANISOU  500  CG2 ILE B  62     3237   4037   3313   -744    898  -1336       C  
ATOM    501  CD1 ILE B  62      -8.702  24.045 -10.358  1.00 23.37           C  
ANISOU  501  CD1 ILE B  62     2660   3158   3061   -801    888  -1313       C  
ATOM    502  N   PHE B  63      -3.039  23.530 -12.110  1.00 30.62           N  
ANISOU  502  N   PHE B  63     3563   4241   3829   -570   1357  -1634       N  
ATOM    503  CA  PHE B  63      -1.738  24.136 -11.871  1.00 28.37           C  
ANISOU  503  CA  PHE B  63     3204   4036   3540   -422   1338  -1516       C  
ATOM    504  C   PHE B  63      -1.908  25.608 -11.501  1.00 26.24           C  
ANISOU  504  C   PHE B  63     2910   3977   3085   -430   1124  -1322       C  
ATOM    505  O   PHE B  63      -2.633  26.351 -12.172  1.00 25.57           O  
ANISOU  505  O   PHE B  63     2859   4069   2787   -629    972  -1295       O  
ATOM    506  CB  PHE B  63      -0.824  24.003 -13.087  1.00 28.54           C  
ANISOU  506  CB  PHE B  63     3206   4166   3471   -553   1430  -1667       C  
ATOM    507  CG  PHE B  63       0.497  24.668 -12.890  1.00 34.75           C  
ANISOU  507  CG  PHE B  63     3896   5046   4261   -426   1419  -1558       C  
ATOM    508  CD1 PHE B  63       1.339  24.246 -11.876  1.00 33.29           C  
ANISOU  508  CD1 PHE B  63     3618   4691   4338   -150   1478  -1451       C  
ATOM    509  CD2 PHE B  63       0.888  25.732 -13.685  1.00 40.15           C  
ANISOU  509  CD2 PHE B  63     4568   5996   4692   -593   1337  -1537       C  
ATOM    510  CE1 PHE B  63       2.560  24.861 -11.663  1.00 31.73           C  
ANISOU  510  CE1 PHE B  63     3297   4601   4157    -46   1458  -1355       C  
ATOM    511  CE2 PHE B  63       2.107  26.353 -13.479  1.00 42.61           C  
ANISOU  511  CE2 PHE B  63     4776   6387   5028   -494   1336  -1444       C  
ATOM    512  CZ  PHE B  63       2.945  25.916 -12.466  1.00 36.75           C  
ANISOU  512  CZ  PHE B  63     3921   5487   4554   -222   1397  -1366       C  
ATOM    513  N   LEU B  64      -1.213  26.031 -10.451  1.00 25.64           N  
ANISOU  513  N   LEU B  64     2773   3857   3111   -218   1058  -1131       N  
ATOM    514  CA  LEU B  64      -1.387  27.354  -9.865  1.00 21.35           C  
ANISOU  514  CA  LEU B  64     2221   3424   2467   -202    830   -916       C  
ATOM    515  C   LEU B  64      -0.047  28.072  -9.801  1.00 20.80           C  
ANISOU  515  C   LEU B  64     2056   3482   2364   -145    804   -850       C  
ATOM    516  O   LEU B  64       0.913  27.533  -9.244  1.00 26.83           O  
ANISOU  516  O   LEU B  64     2739   4174   3281     26    891   -838       O  
ATOM    517  CB  LEU B  64      -1.976  27.239  -8.459  1.00 20.37           C  
ANISOU  517  CB  LEU B  64     2125   3141   2472    -42    766   -765       C  
ATOM    518  CG  LEU B  64      -1.883  28.488  -7.584  1.00 24.77           C  
ANISOU  518  CG  LEU B  64     2663   3775   2972     10    589   -588       C  
ATOM    519  CD1 LEU B  64      -2.824  29.555  -8.137  1.00 20.55           C  
ANISOU  519  CD1 LEU B  64     2147   3328   2335   -150    448   -558       C  
ATOM    520  CD2 LEU B  64      -2.231  28.129  -6.142  1.00 24.11           C  
ANISOU  520  CD2 LEU B  64     2617   3559   2984    159    587   -475       C  
ATOM    521  N   ARG B  65       0.016  29.282 -10.358  1.00 23.56           N  
ANISOU  521  N   ARG B  65     2399   4011   2540   -290    675   -785       N  
ATOM    522  CA  ARG B  65       1.150  30.193 -10.177  1.00 20.37           C  
ANISOU  522  CA  ARG B  65     1904   3724   2113   -266    620   -697       C  
ATOM    523  C   ARG B  65       0.644  31.438  -9.468  1.00 21.87           C  
ANISOU  523  C   ARG B  65     2116   3913   2282   -270    415   -524       C  
ATOM    524  O   ARG B  65      -0.283  32.087  -9.960  1.00 21.70           O  
ANISOU  524  O   ARG B  65     2147   3914   2183   -401    310   -467       O  
ATOM    525  CB  ARG B  65       1.789  30.575 -11.522  1.00 27.05           C  
ANISOU  525  CB  ARG B  65     2721   4767   2791   -464    692   -776       C  
ATOM    526  CG  ARG B  65       2.499  29.436 -12.207  1.00 38.11           C  
ANISOU  526  CG  ARG B  65     4076   6173   4233   -467    950   -999       C  
ATOM    527  CD  ARG B  65       3.249  29.910 -13.450  1.00 50.71           C  
ANISOU  527  CD  ARG B  65     5667   7933   5668   -664    994  -1043       C  
ATOM    528  NE  ARG B  65       2.379  30.682 -14.328  1.00 51.62           N  
ANISOU  528  NE  ARG B  65     5883   8216   5514   -917    866   -975       N  
ATOM    529  CZ  ARG B  65       2.779  31.718 -15.055  1.00 58.17           C  
ANISOU  529  CZ  ARG B  65     6709   9226   6168  -1098    797   -866       C  
ATOM    530  NH1 ARG B  65       4.050  32.104 -15.017  1.00 59.62           N  
ANISOU  530  NH1 ARG B  65     6792   9447   6413  -1063    866   -855       N  
ATOM    531  NH2 ARG B  65       1.909  32.364 -15.824  1.00 48.40           N  
ANISOU  531  NH2 ARG B  65     5557   8125   4709  -1317    649   -745       N  
ATOM    532  N   GLU B  66       1.252  31.775  -8.325  1.00 22.73           N  
ANISOU  532  N   GLU B  66     2171   3994   2471   -136    357   -446       N  
ATOM    533  CA  GLU B  66       0.780  32.846  -7.450  1.00 17.50           C  
ANISOU  533  CA  GLU B  66     1535   3297   1817   -134    208   -343       C  
ATOM    534  C   GLU B  66       1.826  33.946  -7.353  1.00 19.40           C  
ANISOU  534  C   GLU B  66     1691   3644   2037   -189    136   -298       C  
ATOM    535  O   GLU B  66       3.013  33.662  -7.196  1.00 19.61           O  
ANISOU  535  O   GLU B  66     1615   3753   2084   -134    177   -318       O  
ATOM    536  CB  GLU B  66       0.518  32.335  -6.030  1.00 17.65           C  
ANISOU  536  CB  GLU B  66     1586   3218   1904     22    202   -313       C  
ATOM    537  CG  GLU B  66      -0.698  31.483  -5.862  1.00 27.13           C  
ANISOU  537  CG  GLU B  66     2875   4283   3151     60    263   -333       C  
ATOM    538  CD  GLU B  66      -0.737  30.886  -4.475  1.00 29.19           C  
ANISOU  538  CD  GLU B  66     3168   4474   3447    199    280   -273       C  
ATOM    539  OE1 GLU B  66       0.244  30.193  -4.108  1.00 24.76           O  
ANISOU  539  OE1 GLU B  66     2552   3936   2921    311    308   -230       O  
ATOM    540  OE2 GLU B  66      -1.728  31.127  -3.752  1.00 21.56           O  
ANISOU  540  OE2 GLU B  66     2272   3440   2480    192    267   -254       O  
ATOM    541  N   TYR B  67       1.373  35.192  -7.418  1.00 17.83           N  
ANISOU  541  N   TYR B  67     1515   3421   1837   -295     33   -233       N  
ATOM    542  CA  TYR B  67       2.232  36.368  -7.309  1.00 17.87           C  
ANISOU  542  CA  TYR B  67     1452   3485   1854   -380    -32   -196       C  
ATOM    543  C   TYR B  67       1.660  37.267  -6.226  1.00 17.74           C  
ANISOU  543  C   TYR B  67     1472   3348   1921   -367   -115   -190       C  
ATOM    544  O   TYR B  67       0.656  37.942  -6.454  1.00 18.77           O  
ANISOU  544  O   TYR B  67     1647   3356   2128   -419   -156   -141       O  
ATOM    545  CB  TYR B  67       2.302  37.115  -8.637  1.00 18.46           C  
ANISOU  545  CB  TYR B  67     1518   3619   1876   -562    -45   -118       C  
ATOM    546  CG  TYR B  67       2.946  36.314  -9.743  1.00 19.83           C  
ANISOU  546  CG  TYR B  67     1660   3946   1930   -621     77   -170       C  
ATOM    547  CD1 TYR B  67       4.301  36.448 -10.024  1.00 19.89           C  
ANISOU  547  CD1 TYR B  67     1553   4086   1919   -673    152   -202       C  
ATOM    548  CD2 TYR B  67       2.203  35.427 -10.504  1.00 20.64           C  
ANISOU  548  CD2 TYR B  67     1834   4062   1946   -645    138   -217       C  
ATOM    549  CE1 TYR B  67       4.903  35.712 -11.053  1.00 22.58           C  
ANISOU  549  CE1 TYR B  67     1853   4564   2164   -737    317   -291       C  
ATOM    550  CE2 TYR B  67       2.795  34.679 -11.518  1.00 20.07           C  
ANISOU  550  CE2 TYR B  67     1741   4129   1757   -725    292   -324       C  
ATOM    551  CZ  TYR B  67       4.131  34.832 -11.791  1.00 23.64           C  
ANISOU  551  CZ  TYR B  67     2081   4703   2198   -766    394   -365       C  
ATOM    552  OH  TYR B  67       4.694  34.086 -12.803  1.00 27.88           O  
ANISOU  552  OH  TYR B  67     2589   5370   2632   -853    593   -509       O  
ATOM    553  N   GLN B  68       2.296  37.302  -5.059  1.00 17.94           N  
ANISOU  553  N   GLN B  68     1466   3413   1939   -311   -139   -243       N  
ATOM    554  CA  GLN B  68       1.732  38.004  -3.911  1.00 17.88           C  
ANISOU  554  CA  GLN B  68     1512   3310   1971   -316   -176   -298       C  
ATOM    555  C   GLN B  68       2.661  39.119  -3.459  1.00 20.76           C  
ANISOU  555  C   GLN B  68     1811   3725   2354   -430   -237   -351       C  
ATOM    556  O   GLN B  68       3.863  38.901  -3.310  1.00 23.16           O  
ANISOU  556  O   GLN B  68     2016   4191   2593   -438   -272   -355       O  
ATOM    557  CB  GLN B  68       1.478  37.025  -2.764  1.00 17.55           C  
ANISOU  557  CB  GLN B  68     1525   3296   1848   -190   -152   -329       C  
ATOM    558  CG  GLN B  68       1.057  37.684  -1.463  1.00 18.18           C  
ANISOU  558  CG  GLN B  68     1666   3338   1903   -228   -161   -424       C  
ATOM    559  CD  GLN B  68       0.471  36.678  -0.508  1.00 21.27           C  
ANISOU  559  CD  GLN B  68     2143   3743   2195   -129   -111   -415       C  
ATOM    560  OE1 GLN B  68       1.083  36.340   0.503  1.00 22.01           O  
ANISOU  560  OE1 GLN B  68     2242   3980   2139   -114   -159   -406       O  
ATOM    561  NE2 GLN B  68      -0.724  36.181  -0.830  1.00 21.19           N  
ANISOU  561  NE2 GLN B  68     2194   3596   2263    -75    -25   -397       N  
ATOM    562  N   THR B  69       2.102  40.310  -3.240  1.00 18.48           N  
ANISOU  562  N   THR B  69     1554   3278   2188   -522   -242   -399       N  
ATOM    563  CA  THR B  69       2.860  41.439  -2.709  1.00 19.93           C  
ANISOU  563  CA  THR B  69     1689   3464   2418   -659   -279   -494       C  
ATOM    564  C   THR B  69       2.516  41.606  -1.236  1.00 22.68           C  
ANISOU  564  C   THR B  69     2105   3803   2711   -664   -262   -667       C  
ATOM    565  O   THR B  69       1.343  41.734  -0.880  1.00 21.59           O  
ANISOU  565  O   THR B  69     2048   3501   2653   -624   -185   -723       O  
ATOM    566  CB  THR B  69       2.554  42.736  -3.463  1.00 23.39           C  
ANISOU  566  CB  THR B  69     2114   3695   3076   -780   -271   -443       C  
ATOM    567  OG1 THR B  69       2.875  42.585  -4.849  1.00 24.51           O  
ANISOU  567  OG1 THR B  69     2212   3894   3207   -814   -287   -265       O  
ATOM    568  CG2 THR B  69       3.382  43.902  -2.873  1.00 24.71           C  
ANISOU  568  CG2 THR B  69     2231   3834   3325   -946   -287   -575       C  
ATOM    569  N   ARG B  70       3.535  41.588  -0.384  1.00 22.23           N  
ANISOU  569  N   ARG B  70     2001   3942   2505   -727   -330   -752       N  
ATOM    570  CA  ARG B  70       3.362  41.946   1.011  1.00 23.35           C  
ANISOU  570  CA  ARG B  70     2212   4123   2536   -807   -322   -943       C  
ATOM    571  C   ARG B  70       4.692  42.488   1.492  1.00 28.16           C  
ANISOU  571  C   ARG B  70     2719   4925   3056   -970   -433  -1034       C  
ATOM    572  O   ARG B  70       5.734  42.258   0.869  1.00 26.09           O  
ANISOU  572  O   ARG B  70     2319   4795   2799   -968   -516   -919       O  
ATOM    573  CB  ARG B  70       2.896  40.759   1.865  1.00 28.38           C  
ANISOU  573  CB  ARG B  70     2937   4888   2959   -685   -313   -907       C  
ATOM    574  CG  ARG B  70       3.602  39.467   1.559  1.00 30.95           C  
ANISOU  574  CG  ARG B  70     3189   5393   3179   -543   -399   -707       C  
ATOM    575  CD  ARG B  70       3.239  38.362   2.534  1.00 29.54           C  
ANISOU  575  CD  ARG B  70     3096   5326   2803   -443   -402   -639       C  
ATOM    576  NE  ARG B  70       4.392  37.498   2.725  1.00 31.31           N  
ANISOU  576  NE  ARG B  70     3201   5773   2922   -368   -541   -480       N  
ATOM    577  CZ  ARG B  70       4.674  36.459   1.948  1.00 28.54           C  
ANISOU  577  CZ  ARG B  70     2772   5398   2674   -199   -530   -313       C  
ATOM    578  NH1 ARG B  70       3.870  36.140   0.947  1.00 27.85           N  
ANISOU  578  NH1 ARG B  70     2737   5110   2735   -122   -399   -299       N  
ATOM    579  NH2 ARG B  70       5.765  35.736   2.176  1.00 28.49           N  
ANISOU  579  NH2 ARG B  70     2620   5568   2637   -117   -650   -168       N  
ATOM    580  N   GLN B  71       4.646  43.252   2.582  1.00 28.23           N  
ANISOU  580  N   GLN B  71     2784   4949   2994  -1133   -418  -1268       N  
ATOM    581  CA  GLN B  71       5.848  43.922   3.080  1.00 35.01           C  
ANISOU  581  CA  GLN B  71     3571   5934   3796  -1293   -505  -1349       C  
ATOM    582  C   GLN B  71       6.569  44.648   1.943  1.00 36.23           C  
ANISOU  582  C   GLN B  71     3604   5973   4189  -1357   -514  -1276       C  
ATOM    583  O   GLN B  71       7.800  44.743   1.921  1.00 36.02           O  
ANISOU  583  O   GLN B  71     3472   6082   4133  -1403   -602  -1218       O  
ATOM    584  CB  GLN B  71       6.777  42.924   3.781  1.00 38.90           C  
ANISOU  584  CB  GLN B  71     4016   6733   4032  -1217   -651  -1205       C  
ATOM    585  CG  GLN B  71       6.223  42.317   5.086  1.00 31.69           C  
ANISOU  585  CG  GLN B  71     3236   5958   2846  -1200   -652  -1241       C  
ATOM    586  CD  GLN B  71       5.491  40.980   4.901  1.00 44.54           C  
ANISOU  586  CD  GLN B  71     4909   7621   4392   -997   -641  -1063       C  
ATOM    587  OE1 GLN B  71       5.986  40.063   4.233  1.00 33.43           O  
ANISOU  587  OE1 GLN B  71     3393   6280   3028   -839   -716   -845       O  
ATOM    588  NE2 GLN B  71       4.316  40.859   5.526  1.00 35.92           N  
ANISOU  588  NE2 GLN B  71     3978   6473   3197  -1004   -520  -1169       N  
ATOM    589  N   ASN B  72       5.792  45.112   0.959  1.00 35.33           N  
ANISOU  589  N   ASN B  72     3495   5607   4321  -1362   -422  -1250       N  
ATOM    590  CA  ASN B  72       6.282  45.867  -0.196  1.00 42.40           C  
ANISOU  590  CA  ASN B  72     4303   6361   5446  -1443   -408  -1137       C  
ATOM    591  C   ASN B  72       7.266  45.079  -1.062  1.00 42.01           C  
ANISOU  591  C   ASN B  72     4138   6513   5312  -1358   -471   -920       C  
ATOM    592  O   ASN B  72       8.136  45.667  -1.714  1.00 37.83           O  
ANISOU  592  O   ASN B  72     3523   5964   4888  -1457   -470   -854       O  
ATOM    593  CB  ASN B  72       6.891  47.200   0.246  1.00 46.89           C  
ANISOU  593  CB  ASN B  72     4866   6804   6144  -1639   -387  -1295       C  
ATOM    594  CG  ASN B  72       5.848  48.142   0.804  1.00 63.89           C  
ANISOU  594  CG  ASN B  72     7130   8654   8492  -1712   -257  -1507       C  
ATOM    595  OD1 ASN B  72       5.547  48.119   1.998  1.00 63.85           O  
ANISOU  595  OD1 ASN B  72     7214   8707   8338  -1731   -219  -1721       O  
ATOM    596  ND2 ASN B  72       5.250  48.943  -0.072  1.00 68.68           N  
ANISOU  596  ND2 ASN B  72     7730   8923   9442  -1738   -173  -1425       N  
ATOM    597  N   GLN B  73       7.111  43.754  -1.117  1.00 30.48           N  
ANISOU  597  N   GLN B  73     2673   5216   3692  -1176   -498   -815       N  
ATOM    598  CA  GLN B  73       7.954  42.882  -1.930  1.00 28.06           C  
ANISOU  598  CA  GLN B  73     2258   5058   3343  -1071   -506   -648       C  
ATOM    599  C   GLN B  73       7.091  41.903  -2.707  1.00 27.15           C  
ANISOU  599  C   GLN B  73     2187   4924   3205   -922   -447   -535       C  
ATOM    600  O   GLN B  73       5.987  41.566  -2.279  1.00 27.77           O  
ANISOU  600  O   GLN B  73     2405   4895   3253   -822   -421   -552       O  
ATOM    601  CB  GLN B  73       8.943  42.098  -1.064  1.00 29.44           C  
ANISOU  601  CB  GLN B  73     2352   5454   3380   -986   -600   -639       C  
ATOM    602  CG  GLN B  73       9.821  42.988  -0.220  1.00 34.73           C  
ANISOU  602  CG  GLN B  73     2977   6178   4042  -1144   -679   -752       C  
ATOM    603  CD  GLN B  73      10.449  42.258   0.947  1.00 36.68           C  
ANISOU  603  CD  GLN B  73     3177   6642   4117  -1079   -809   -734       C  
ATOM    604  OE1 GLN B  73      11.385  41.469   0.775  1.00 40.58           O  
ANISOU  604  OE1 GLN B  73     3522   7274   4624   -976   -866   -607       O  
ATOM    605  NE2 GLN B  73       9.942  42.520   2.147  1.00 37.02           N  
ANISOU  605  NE2 GLN B  73     3341   6716   4009  -1148   -851   -857       N  
ATOM    606  N   CYS B  74       7.616  41.419  -3.839  1.00 24.86           N  
ANISOU  606  N   CYS B  74     1817   4700   2930   -890   -391   -420       N  
ATOM    607  CA  CYS B  74       6.933  40.401  -4.640  1.00 21.82           C  
ANISOU  607  CA  CYS B  74     1495   4291   2505   -754   -313   -331       C  
ATOM    608  C   CYS B  74       7.397  39.013  -4.222  1.00 21.79           C  
ANISOU  608  C   CYS B  74     1417   4432   2431   -574   -314   -324       C  
ATOM    609  O   CYS B  74       8.608  38.765  -4.146  1.00 23.17           O  
ANISOU  609  O   CYS B  74     1425   4752   2625   -563   -333   -319       O  
ATOM    610  CB  CYS B  74       7.192  40.596  -6.144  1.00 22.10           C  
ANISOU  610  CB  CYS B  74     1496   4339   2563   -855   -225   -240       C  
ATOM    611  SG  CYS B  74       6.308  39.366  -7.146  1.00 26.04           S  
ANISOU  611  SG  CYS B  74     2096   4824   2974   -738   -125   -183       S  
ATOM    612  N   PHE B  75       6.439  38.109  -3.975  1.00 20.57           N  
ANISOU  612  N   PHE B  75     1384   4197   2234   -425   -285   -304       N  
ATOM    613  CA  PHE B  75       6.712  36.717  -3.626  1.00 23.59           C  
ANISOU  613  CA  PHE B  75     1717   4648   2599   -239   -268   -262       C  
ATOM    614  C   PHE B  75       5.953  35.779  -4.550  1.00 24.19           C  
ANISOU  614  C   PHE B  75     1877   4618   2697   -154   -134   -247       C  
ATOM    615  O   PHE B  75       4.809  36.054  -4.922  1.00 22.19           O  
ANISOU  615  O   PHE B  75     1766   4240   2426   -201   -108   -254       O  
ATOM    616  CB  PHE B  75       6.322  36.395  -2.177  1.00 20.95           C  
ANISOU  616  CB  PHE B  75     1456   4327   2178   -158   -360   -248       C  
ATOM    617  CG  PHE B  75       7.102  37.172  -1.168  1.00 22.55           C  
ANISOU  617  CG  PHE B  75     1577   4682   2308   -265   -505   -289       C  
ATOM    618  CD1 PHE B  75       8.387  36.773  -0.801  1.00 24.44           C  
ANISOU  618  CD1 PHE B  75     1616   5117   2555   -223   -607   -223       C  
ATOM    619  CD2 PHE B  75       6.563  38.306  -0.584  1.00 24.72           C  
ANISOU  619  CD2 PHE B  75     1962   4901   2532   -417   -534   -407       C  
ATOM    620  CE1 PHE B  75       9.100  37.491   0.124  1.00 29.50           C  
ANISOU  620  CE1 PHE B  75     2238   5843   3126   -340   -727   -258       C  
ATOM    621  CE2 PHE B  75       7.280  39.037   0.338  1.00 24.92           C  
ANISOU  621  CE2 PHE B  75     1930   5062   2477   -553   -650   -489       C  
ATOM    622  CZ  PHE B  75       8.547  38.632   0.698  1.00 31.08           C  
ANISOU  622  CZ  PHE B  75     2574   5993   3241   -514   -743   -403       C  
ATOM    623  N   TYR B  76       6.564  34.646  -4.865  1.00 20.49           N  
ANISOU  623  N   TYR B  76     1307   4190   2290    -30    -50   -234       N  
ATOM    624  CA  TYR B  76       6.035  33.768  -5.897  1.00 20.10           C  
ANISOU  624  CA  TYR B  76     1318   4055   2264      5    107   -277       C  
ATOM    625  C   TYR B  76       5.918  32.339  -5.383  1.00 20.57           C  
ANISOU  625  C   TYR B  76     1374   4025   2415    207    166   -249       C  
ATOM    626  O   TYR B  76       6.690  31.897  -4.527  1.00 22.32           O  
ANISOU  626  O   TYR B  76     1473   4295   2713    338    102   -166       O  
ATOM    627  CB  TYR B  76       6.931  33.842  -7.149  1.00 21.29           C  
ANISOU  627  CB  TYR B  76     1345   4308   2434    -92    236   -341       C  
ATOM    628  CG  TYR B  76       6.724  32.760  -8.181  1.00 25.40           C  
ANISOU  628  CG  TYR B  76     1890   4784   2976    -68    436   -442       C  
ATOM    629  CD1 TYR B  76       7.483  31.594  -8.150  1.00 26.53           C  
ANISOU  629  CD1 TYR B  76     1891   4900   3288     94    572   -496       C  
ATOM    630  CD2 TYR B  76       5.801  32.919  -9.207  1.00 25.68           C  
ANISOU  630  CD2 TYR B  76     2076   4806   2876   -220    489   -488       C  
ATOM    631  CE1 TYR B  76       7.316  30.608  -9.090  1.00 28.66           C  
ANISOU  631  CE1 TYR B  76     2184   5105   3601     97    794   -643       C  
ATOM    632  CE2 TYR B  76       5.624  31.927 -10.167  1.00 27.34           C  
ANISOU  632  CE2 TYR B  76     2316   5002   3069   -244    680   -626       C  
ATOM    633  CZ  TYR B  76       6.390  30.777 -10.097  1.00 30.40           C  
ANISOU  633  CZ  TYR B  76     2577   5339   3636    -89    851   -728       C  
ATOM    634  OH  TYR B  76       6.238  29.786 -11.027  1.00 31.75           O  
ANISOU  634  OH  TYR B  76     2817   5422   3824   -122   1044   -888       O  
ATOM    635  N   ASN B  77       4.930  31.620  -5.909  1.00 19.88           N  
ANISOU  635  N   ASN B  77     1415   3806   2332    221    276   -300       N  
ATOM    636  CA  ASN B  77       4.788  30.201  -5.636  1.00 22.75           C  
ANISOU  636  CA  ASN B  77     1781   4034   2827    392    378   -288       C  
ATOM    637  C   ASN B  77       4.122  29.532  -6.826  1.00 30.32           C  
ANISOU  637  C   ASN B  77     2822   4898   3799    325    556   -434       C  
ATOM    638  O   ASN B  77       3.321  30.148  -7.537  1.00 26.29           O  
ANISOU  638  O   ASN B  77     2418   4420   3151    157    538   -488       O  
ATOM    639  CB  ASN B  77       3.963  29.936  -4.368  1.00 31.61           C  
ANISOU  639  CB  ASN B  77     3021   5068   3923    477    285   -170       C  
ATOM    640  CG  ASN B  77       3.723  28.450  -4.126  1.00 46.66           C  
ANISOU  640  CG  ASN B  77     4946   6794   5989    638    402   -125       C  
ATOM    641  OD1 ASN B  77       4.641  27.704  -3.794  1.00 42.91           O  
ANISOU  641  OD1 ASN B  77     4332   6294   5676    795    420    -35       O  
ATOM    642  ND2 ASN B  77       2.479  28.018  -4.304  1.00 56.53           N  
ANISOU  642  ND2 ASN B  77     6348   7900   7229    597    481   -177       N  
ATOM    643  N   SER B  78       4.471  28.269  -7.045  1.00 26.90           N  
ANISOU  643  N   SER B  78     2328   4346   3548    447    725   -497       N  
ATOM    644  CA  SER B  78       3.748  27.424  -7.981  1.00 30.71           C  
ANISOU  644  CA  SER B  78     2905   4709   4056    379    909   -670       C  
ATOM    645  C   SER B  78       3.449  26.098  -7.301  1.00 39.58           C  
ANISOU  645  C   SER B  78     4048   5587   5404    562    999   -626       C  
ATOM    646  O   SER B  78       4.256  25.603  -6.508  1.00 43.41           O  
ANISOU  646  O   SER B  78     4407   6007   6079    760    985   -488       O  
ATOM    647  CB  SER B  78       4.535  27.208  -9.277  1.00 36.06           C  
ANISOU  647  CB  SER B  78     3489   5465   4747    284   1114   -876       C  
ATOM    648  OG  SER B  78       5.694  26.430  -9.049  1.00 38.65           O  
ANISOU  648  OG  SER B  78     3647   5700   5338    470   1228   -867       O  
ATOM    649  N   SER B  79       2.277  25.538  -7.589  1.00 30.52           N  
ANISOU  649  N   SER B  79     3046   4306   4245    486   1074   -717       N  
ATOM    650  CA  SER B  79       1.852  24.294  -6.957  1.00 34.43           C  
ANISOU  650  CA  SER B  79     3582   4537   4962    627   1172   -665       C  
ATOM    651  C   SER B  79       0.646  23.762  -7.720  1.00 34.36           C  
ANISOU  651  C   SER B  79     3708   4420   4926    462   1292   -860       C  
ATOM    652  O   SER B  79       0.160  24.386  -8.667  1.00 28.33           O  
ANISOU  652  O   SER B  79     2998   3817   3951    250   1261  -1000       O  
ATOM    653  CB  SER B  79       1.522  24.504  -5.482  1.00 38.35           C  
ANISOU  653  CB  SER B  79     4126   5017   5430    740    995   -394       C  
ATOM    654  OG  SER B  79       0.531  25.493  -5.350  1.00 35.70           O  
ANISOU  654  OG  SER B  79     3904   4798   4862    592    860   -386       O  
ATOM    655  N   TYR B  80       0.166  22.596  -7.293  1.00 35.58           N  
ANISOU  655  N   TYR B  80     3911   4307   5302    549   1415   -847       N  
ATOM    656  CA  TYR B  80      -0.981  21.940  -7.901  1.00 32.67           C  
ANISOU  656  CA  TYR B  80     3662   3813   4937    380   1510  -1021       C  
ATOM    657  C   TYR B  80      -2.113  21.863  -6.889  1.00 32.49           C  
ANISOU  657  C   TYR B  80     3730   3684   4930    403   1446   -860       C  
ATOM    658  O   TYR B  80      -1.895  21.502  -5.728  1.00 40.40           O  
ANISOU  658  O   TYR B  80     4729   4563   6060    584   1423   -623       O  
ATOM    659  CB  TYR B  80      -0.615  20.540  -8.406  1.00 35.84           C  
ANISOU  659  CB  TYR B  80     4060   3971   5585    393   1691  -1147       C  
ATOM    660  CG  TYR B  80       0.200  20.585  -9.676  1.00 43.09           C  
ANISOU  660  CG  TYR B  80     4930   5014   6429    276   1763  -1358       C  
ATOM    661  CD1 TYR B  80      -0.421  20.658 -10.919  1.00 46.27           C  
ANISOU  661  CD1 TYR B  80     5409   5534   6639     -4   1796  -1600       C  
ATOM    662  CD2 TYR B  80       1.592  20.595  -9.636  1.00 50.69           C  
ANISOU  662  CD2 TYR B  80     5758   6000   7503    429   1796  -1307       C  
ATOM    663  CE1 TYR B  80       0.320  20.721 -12.089  1.00 51.13           C  
ANISOU  663  CE1 TYR B  80     5990   6279   7156   -138   1877  -1785       C  
ATOM    664  CE2 TYR B  80       2.342  20.655 -10.805  1.00 51.73           C  
ANISOU  664  CE2 TYR B  80     5846   6245   7565    308   1892  -1505       C  
ATOM    665  CZ  TYR B  80       1.697  20.720 -12.025  1.00 50.61           C  
ANISOU  665  CZ  TYR B  80     5805   6212   7212     20   1938  -1742       C  
ATOM    666  OH  TYR B  80       2.425  20.781 -13.190  1.00 49.14           O  
ANISOU  666  OH  TYR B  80     5586   6152   6934   -126   2046  -1934       O  
ATOM    667  N   LEU B  81      -3.307  22.229  -7.325  1.00 29.46           N  
ANISOU  667  N   LEU B  81     3420   3376   4396    203   1388   -958       N  
ATOM    668  CA  LEU B  81      -4.515  21.962  -6.561  1.00 25.36           C  
ANISOU  668  CA  LEU B  81     2976   2733   3927    181   1373   -859       C  
ATOM    669  C   LEU B  81      -5.088  20.619  -6.982  1.00 30.50           C  
ANISOU  669  C   LEU B  81     3670   3123   4797    102   1587  -1036       C  
ATOM    670  O   LEU B  81      -4.983  20.220  -8.143  1.00 32.83           O  
ANISOU  670  O   LEU B  81     3958   3428   5089    -44   1676  -1289       O  
ATOM    671  CB  LEU B  81      -5.570  23.042  -6.781  1.00 22.55           C  
ANISOU  671  CB  LEU B  81     2632   2571   3365     16   1201   -865       C  
ATOM    672  CG  LEU B  81      -5.149  24.516  -6.762  1.00 28.44           C  
ANISOU  672  CG  LEU B  81     3334   3567   3906     21   1002   -767       C  
ATOM    673  CD1 LEU B  81      -6.383  25.394  -6.777  1.00 26.79           C  
ANISOU  673  CD1 LEU B  81     3119   3447   3613   -103    864   -737       C  
ATOM    674  CD2 LEU B  81      -4.284  24.797  -5.557  1.00 28.69           C  
ANISOU  674  CD2 LEU B  81     3354   3602   3943    216    955   -565       C  
ATOM    675  N   ASN B  82      -5.692  19.923  -6.024  1.00 30.10           N  
ANISOU  675  N   ASN B  82     3671   2851   4915    168   1657   -890       N  
ATOM    676  CA  ASN B  82      -6.529  18.769  -6.312  1.00 28.55           C  
ANISOU  676  CA  ASN B  82     3522   2395   4932     48   1846  -1046       C  
ATOM    677  C   ASN B  82      -7.973  19.233  -6.398  1.00 28.17           C  
ANISOU  677  C   ASN B  82     3489   2460   4755   -156   1751  -1093       C  
ATOM    678  O   ASN B  82      -8.376  20.152  -5.684  1.00 29.61           O  
ANISOU  678  O   ASN B  82     3664   2795   4792   -123   1597   -911       O  
ATOM    679  CB  ASN B  82      -6.378  17.701  -5.231  1.00 36.64           C  
ANISOU  679  CB  ASN B  82     4585   3098   6239    219   1982   -818       C  
ATOM    680  CG  ASN B  82      -5.101  16.909  -5.380  1.00 45.62           C  
ANISOU  680  CG  ASN B  82     5664   4098   7571    366   2051   -773       C  
ATOM    681  OD1 ASN B  82      -4.851  16.314  -6.425  1.00 46.53           O  
ANISOU  681  OD1 ASN B  82     5747   4171   7761    250   2142  -1012       O  
ATOM    682  ND2 ASN B  82      -4.281  16.899  -4.336  1.00 40.52           N  
ANISOU  682  ND2 ASN B  82     4989   3394   7013    617   2011   -465       N  
ATOM    683  N   VAL B  83      -8.736  18.623  -7.297  1.00 30.77           N  
ANISOU  683  N   VAL B  83     3821   2720   5149   -379   1845  -1358       N  
ATOM    684  CA  VAL B  83     -10.107  19.033  -7.576  1.00 31.98           C  
ANISOU  684  CA  VAL B  83     3939   3004   5206   -597   1733  -1425       C  
ATOM    685  C   VAL B  83     -11.032  17.919  -7.115  1.00 33.17           C  
ANISOU  685  C   VAL B  83     4119   2863   5619   -675   1915  -1452       C  
ATOM    686  O   VAL B  83     -10.880  16.766  -7.538  1.00 37.98           O  
ANISOU  686  O   VAL B  83     4751   3273   6407   -737   2090  -1598       O  
ATOM    687  CB  VAL B  83     -10.321  19.324  -9.068  1.00 32.42           C  
ANISOU  687  CB  VAL B  83     3953   3291   5072   -851   1643  -1702       C  
ATOM    688  CG1 VAL B  83     -11.773  19.695  -9.330  1.00 31.68           C  
ANISOU  688  CG1 VAL B  83     3782   3332   4924  -1068   1495  -1730       C  
ATOM    689  CG2 VAL B  83      -9.385  20.418  -9.538  1.00 29.66           C  
ANISOU  689  CG2 VAL B  83     3581   3218   4468   -791   1484  -1649       C  
ATOM    690  N   GLN B  84     -11.995  18.257  -6.255  1.00 29.72           N  
ANISOU  690  N   GLN B  84     3658   2439   5196   -682   1864  -1279       N  
ATOM    691  CA  GLN B  84     -13.033  17.313  -5.834  1.00 31.68           C  
ANISOU  691  CA  GLN B  84     3915   2442   5679   -800   2034  -1297       C  
ATOM    692  C   GLN B  84     -14.308  17.720  -6.566  1.00 37.47           C  
ANISOU  692  C   GLN B  84     4523   3359   6353  -1063   1908  -1471       C  
ATOM    693  O   GLN B  84     -15.073  18.560  -6.097  1.00 35.85           O  
ANISOU  693  O   GLN B  84     4228   3304   6089  -1066   1788  -1342       O  
ATOM    694  CB  GLN B  84     -13.211  17.310  -4.316  1.00 31.35           C  
ANISOU  694  CB  GLN B  84     3923   2291   5697   -644   2103   -979       C  
ATOM    695  CG  GLN B  84     -11.974  16.858  -3.541  1.00 38.85           C  
ANISOU  695  CG  GLN B  84     4978   3081   6703   -393   2184   -749       C  
ATOM    696  CD  GLN B  84     -10.930  17.958  -3.403  1.00 35.24           C  
ANISOU  696  CD  GLN B  84     4508   2886   5994   -217   1990   -634       C  
ATOM    697  OE1 GLN B  84     -11.261  19.112  -3.123  1.00 30.78           O  
ANISOU  697  OE1 GLN B  84     3902   2571   5221   -224   1834   -578       O  
ATOM    698  NE2 GLN B  84      -9.667  17.607  -3.618  1.00 33.85           N  
ANISOU  698  NE2 GLN B  84     4350   2637   5876    -63   2013   -614       N  
ATOM    699  N   ARG B  85     -14.526  17.113  -7.736  1.00 33.19           N  
ANISOU  699  N   ARG B  85     4288   3101   5222  -1235   1883  -1591       N  
ATOM    700  CA  ARG B  85     -15.567  17.577  -8.651  1.00 35.74           C  
ANISOU  700  CA  ARG B  85     4542   3761   5279  -1456   1792  -1746       C  
ATOM    701  C   ARG B  85     -16.945  17.552  -8.003  1.00 33.82           C  
ANISOU  701  C   ARG B  85     4275   3559   5016  -1565   1745  -1696       C  
ATOM    702  O   ARG B  85     -17.667  18.556  -8.020  1.00 35.25           O  
ANISOU  702  O   ARG B  85     4365   4028   5001  -1600   1571  -1669       O  
ATOM    703  CB  ARG B  85     -15.575  16.720  -9.916  1.00 37.99           C  
ANISOU  703  CB  ARG B  85     4819   4057   5557  -1645   1906  -2012       C  
ATOM    704  CG  ARG B  85     -14.454  17.012 -10.892  1.00 37.32           C  
ANISOU  704  CG  ARG B  85     4704   4085   5391  -1633   1927  -2110       C  
ATOM    705  CD  ARG B  85     -14.542  16.065 -12.077  1.00 44.19           C  
ANISOU  705  CD  ARG B  85     5588   4938   6263  -1848   2078  -2396       C  
ATOM    706  NE  ARG B  85     -13.459  16.256 -13.035  1.00 38.94           N  
ANISOU  706  NE  ARG B  85     4889   4377   5531  -1879   2141  -2524       N  
ATOM    707  CZ  ARG B  85     -13.555  16.995 -14.137  1.00 41.72           C  
ANISOU  707  CZ  ARG B  85     5235   5064   5554  -2054   2049  -2576       C  
ATOM    708  NH1 ARG B  85     -14.686  17.620 -14.423  1.00 41.16           N  
ANISOU  708  NH1 ARG B  85     5187   5243   5209  -2166   1848  -2503       N  
ATOM    709  NH2 ARG B  85     -12.517  17.109 -14.957  1.00 40.54           N  
ANISOU  709  NH2 ARG B  85     5059   4989   5354  -2119   2145  -2700       N  
ATOM    710  N   GLU B  86     -17.336  16.404  -7.444  1.00 33.21           N  
ANISOU  710  N   GLU B  86     4268   3203   5149  -1640   1888  -1680       N  
ATOM    711  CA  GLU B  86     -18.689  16.277  -6.911  1.00 34.49           C  
ANISOU  711  CA  GLU B  86     4369   3448   5288  -1819   1869  -1651       C  
ATOM    712  C   GLU B  86     -18.903  17.186  -5.709  1.00 37.23           C  
ANISOU  712  C   GLU B  86     4679   3872   5596  -1686   1785  -1395       C  
ATOM    713  O   GLU B  86     -19.975  17.792  -5.565  1.00 34.16           O  
ANISOU  713  O   GLU B  86     4115   3771   5092  -1784   1690  -1406       O  
ATOM    714  CB  GLU B  86     -18.968  14.823  -6.541  1.00 38.59           C  
ANISOU  714  CB  GLU B  86     5020   3626   6017  -1968   2050  -1656       C  
ATOM    715  CG  GLU B  86     -19.114  13.926  -7.740  1.00 53.64           C  
ANISOU  715  CG  GLU B  86     6947   5496   7939  -2178   2140  -1948       C  
ATOM    716  CD  GLU B  86     -19.507  12.525  -7.356  1.00 59.14           C  
ANISOU  716  CD  GLU B  86     7807   5831   8834  -2369   2306  -1958       C  
ATOM    717  OE1 GLU B  86     -18.725  11.871  -6.635  1.00 59.02           O  
ANISOU  717  OE1 GLU B  86     7989   5400   9035  -2211   2389  -1783       O  
ATOM    718  OE2 GLU B  86     -20.600  12.082  -7.768  1.00 67.57           O  
ANISOU  718  OE2 GLU B  86     8812   7026   9835  -2686   2331  -2128       O  
ATOM    719  N   ASN B  87     -17.906  17.283  -4.825  1.00 31.35           N  
ANISOU  719  N   ASN B  87     4070   2896   4946  -1457   1816  -1158       N  
ATOM    720  CA  ASN B  87     -18.021  18.174  -3.677  1.00 32.08           C  
ANISOU  720  CA  ASN B  87     4155   3077   4956  -1331   1748   -897       C  
ATOM    721  C   ASN B  87     -17.984  19.642  -4.072  1.00 31.19           C  
ANISOU  721  C   ASN B  87     3924   3285   4642  -1249   1580   -932       C  
ATOM    722  O   ASN B  87     -18.419  20.488  -3.287  1.00 31.62           O  
ANISOU  722  O   ASN B  87     3915   3513   4588  -1171   1528   -771       O  
ATOM    723  CB  ASN B  87     -16.898  17.908  -2.670  1.00 40.75           C  
ANISOU  723  CB  ASN B  87     5443   3876   6163  -1108   1780   -611       C  
ATOM    724  CG  ASN B  87     -17.154  16.692  -1.810  1.00 60.80           C  
ANISOU  724  CG  ASN B  87     8137   6126   8836  -1185   1885   -445       C  
ATOM    725  OD1 ASN B  87     -16.263  15.869  -1.603  1.00 70.84           O  
ANISOU  725  OD1 ASN B  87     9564   7071  10281  -1060   1903   -339       O  
ATOM    726  ND2 ASN B  87     -18.364  16.584  -1.279  1.00 65.95           N  
ANISOU  726  ND2 ASN B  87     8742   6907   9408  -1392   1939   -413       N  
ATOM    727  N   GLY B  88     -17.471  19.968  -5.256  1.00 28.71           N  
ANISOU  727  N   GLY B  88     3593   3072   4242  -1263   1503  -1128       N  
ATOM    728  CA  GLY B  88     -17.338  21.365  -5.617  1.00 26.40           C  
ANISOU  728  CA  GLY B  88     3249   3051   3730  -1215   1326  -1127       C  
ATOM    729  C   GLY B  88     -16.273  22.080  -4.822  1.00 26.33           C  
ANISOU  729  C   GLY B  88     3379   2968   3657   -949   1280   -874       C  
ATOM    730  O   GLY B  88     -16.425  23.271  -4.517  1.00 22.88           O  
ANISOU  730  O   GLY B  88     2953   2737   3004   -793   1109   -747       O  
ATOM    731  N   THR B  89     -15.200  21.377  -4.459  1.00 23.16           N  
ANISOU  731  N   THR B  89     3085   2273   3442   -866   1403   -803       N  
ATOM    732  CA  THR B  89     -14.096  21.948  -3.702  1.00 22.03           C  
ANISOU  732  CA  THR B  89     3036   2095   3238   -623   1325   -570       C  
ATOM    733  C   THR B  89     -12.781  21.750  -4.444  1.00 21.05           C  
ANISOU  733  C   THR B  89     2907   1903   3186   -578   1352   -715       C  
ATOM    734  O   THR B  89     -12.657  20.905  -5.339  1.00 25.13           O  
ANISOU  734  O   THR B  89     3364   2337   3845   -691   1466   -944       O  
ATOM    735  CB  THR B  89     -13.958  21.321  -2.305  1.00 25.61           C  
ANISOU  735  CB  THR B  89     3583   2302   3848   -511   1403   -282       C  
ATOM    736  OG1 THR B  89     -13.728  19.909  -2.431  1.00 26.21           O  
ANISOU  736  OG1 THR B  89     3688   2048   4225   -543   1547   -344       O  
ATOM    737  CG2 THR B  89     -15.212  21.563  -1.460  1.00 22.72           C  
ANISOU  737  CG2 THR B  89     3208   2051   3372   -587   1437   -155       C  
ATOM    738  N   VAL B  90     -11.794  22.547  -4.038  1.00 22.33           N  
ANISOU  738  N   VAL B  90     3095   2166   3222   -422   1236   -567       N  
ATOM    739  CA  VAL B  90     -10.402  22.373  -4.426  1.00 22.89           C  
ANISOU  739  CA  VAL B  90     3090   2214   3393   -345   1278   -668       C  
ATOM    740  C   VAL B  90      -9.578  22.334  -3.148  1.00 25.29           C  
ANISOU  740  C   VAL B  90     3390   2422   3797   -106   1191   -372       C  
ATOM    741  O   VAL B  90      -9.988  22.841  -2.101  1.00 25.34           O  
ANISOU  741  O   VAL B  90     3507   2468   3654    -53   1076   -104       O  
ATOM    742  CB  VAL B  90      -9.904  23.495  -5.363  1.00 20.79           C  
ANISOU  742  CB  VAL B  90     2823   2260   2816   -483   1173   -792       C  
ATOM    743  CG1 VAL B  90     -10.545  23.343  -6.732  1.00 26.80           C  
ANISOU  743  CG1 VAL B  90     3560   3124   3500   -714   1139   -971       C  
ATOM    744  CG2 VAL B  90     -10.215  24.885  -4.757  1.00 18.10           C  
ANISOU  744  CG2 VAL B  90     2631   2097   2150   -462    980   -577       C  
ATOM    745  N   SER B  91      -8.414  21.700  -3.229  1.00 26.41           N  
ANISOU  745  N   SER B  91     3391   2451   4191     47   1243   -436       N  
ATOM    746  CA  SER B  91      -7.587  21.529  -2.048  1.00 24.68           C  
ANISOU  746  CA  SER B  91     3137   2147   4093    299   1107   -143       C  
ATOM    747  C   SER B  91      -6.122  21.681  -2.428  1.00 29.09           C  
ANISOU  747  C   SER B  91     3433   2872   4748    411   1085   -285       C  
ATOM    748  O   SER B  91      -5.732  21.457  -3.576  1.00 28.32           O  
ANISOU  748  O   SER B  91     3185   2830   4745    334   1263   -636       O  
ATOM    749  CB  SER B  91      -7.825  20.168  -1.376  1.00 32.23           C  
ANISOU  749  CB  SER B  91     4182   2669   5395    466   1161     22       C  
ATOM    750  OG  SER B  91      -7.516  19.098  -2.255  1.00 33.10           O  
ANISOU  750  OG  SER B  91     4191   2544   5840    515   1335   -264       O  
ATOM    751  N   ARG B  92      -5.316  22.071  -1.446  1.00 25.31           N  
ANISOU  751  N   ARG B  92     2883   2512   4221    563    875    -30       N  
ATOM    752  CA  ARG B  92      -3.889  22.241  -1.648  1.00 27.83           C  
ANISOU  752  CA  ARG B  92     2876   3056   4644    666    827   -148       C  
ATOM    753  C   ARG B  92      -3.175  21.994  -0.330  1.00 31.72           C  
ANISOU  753  C   ARG B  92     3286   3514   5252    946    558    200       C  
ATOM    754  O   ARG B  92      -3.763  22.099   0.750  1.00 29.80           O  
ANISOU  754  O   ARG B  92     3306   3173   4844    959    399    542       O  
ATOM    755  CB  ARG B  92      -3.560  23.643  -2.178  1.00 24.91           C  
ANISOU  755  CB  ARG B  92     2486   3106   3875    358    806   -280       C  
ATOM    756  CG  ARG B  92      -4.004  24.765  -1.250  1.00 22.57           C  
ANISOU  756  CG  ARG B  92     2455   2934   3186    233    590      6       C  
ATOM    757  CD  ARG B  92      -3.790  26.143  -1.881  1.00 22.87           C  
ANISOU  757  CD  ARG B  92     2575   3278   2837    -96    581   -130       C  
ATOM    758  NE  ARG B  92      -2.376  26.439  -2.129  1.00 25.69           N  
ANISOU  758  NE  ARG B  92     2617   3934   3209   -181    572   -268       N  
ATOM    759  CZ  ARG B  92      -1.914  27.640  -2.476  1.00 29.11           C  
ANISOU  759  CZ  ARG B  92     3117   4645   3301   -513    544   -344       C  
ATOM    760  NH1 ARG B  92      -2.751  28.666  -2.615  1.00 24.27           N  
ANISOU  760  NH1 ARG B  92     2913   3988   2321   -731    494   -277       N  
ATOM    761  NH2 ARG B  92      -0.612  27.823  -2.678  1.00 28.39           N  
ANISOU  761  NH2 ARG B  92     2677   4865   3243   -630    565   -493       N  
ATOM    762  N   TYR B  93      -1.894  21.667  -0.433  1.00 31.07           N  
ANISOU  762  N   TYR B  93     2818   3545   5442   1165    506     97       N  
ATOM    763  CA  TYR B  93      -1.020  21.568   0.722  1.00 39.60           C  
ANISOU  763  CA  TYR B  93     3739   4704   6605   1427    179    410       C  
ATOM    764  C   TYR B  93      -0.157  22.819   0.732  1.00 43.74           C  
ANISOU  764  C   TYR B  93     4037   5762   6821   1196     55    333       C  
ATOM    765  O   TYR B  93       0.553  23.096  -0.241  1.00 42.93           O  
ANISOU  765  O   TYR B  93     3610   5927   6774   1076    229    -24       O  
ATOM    766  CB  TYR B  93      -0.171  20.299   0.668  1.00 41.89           C  
ANISOU  766  CB  TYR B  93     3702   4750   7464   1888    159    356       C  
ATOM    767  CG  TYR B  93       0.452  19.904   1.991  1.00 49.61           C  
ANISOU  767  CG  TYR B  93     4637   5675   8537   2221   -250    780       C  
ATOM    768  CD1 TYR B  93      -0.316  19.356   3.011  1.00 53.39           C  
ANISOU  768  CD1 TYR B  93     5611   5814   8861   2242   -408   1152       C  
ATOM    769  CD2 TYR B  93       1.815  20.068   2.215  1.00 60.77           C  
ANISOU  769  CD2 TYR B  93     5592   7460  10038   2403   -480    730       C  
ATOM    770  CE1 TYR B  93       0.258  18.991   4.223  1.00 61.85           C  
ANISOU  770  CE1 TYR B  93     6769   6887   9844   2441   -789   1464       C  
ATOM    771  CE2 TYR B  93       2.397  19.705   3.418  1.00 67.33           C  
ANISOU  771  CE2 TYR B  93     6468   8300  10814   2647   -889   1056       C  
ATOM    772  CZ  TYR B  93       1.614  19.168   4.419  1.00 68.55           C  
ANISOU  772  CZ  TYR B  93     7170   8082  10792   2667  -1044   1425       C  
ATOM    773  OH  TYR B  93       2.193  18.808   5.617  1.00 74.65           O  
ANISOU  773  OH  TYR B  93     8038   8872  11453   2878  -1437   1720       O  
ATOM    774  N  AGLU B  94      -0.237  23.586   1.815  0.65 41.68           N  
ANISOU  774  N  AGLU B  94     3974   5658   6205   1080   -216    645       N  
ATOM    775  CA AGLU B  94       0.480  24.850   1.903  0.65 46.49           C  
ANISOU  775  CA AGLU B  94     4460   6733   6472    782   -339    580       C  
ATOM    776  C  AGLU B  94       0.765  25.150   3.364  0.65 49.96           C  
ANISOU  776  C  AGLU B  94     4996   7294   6693    827   -720    956       C  
ATOM    777  O  AGLU B  94      -0.129  25.039   4.208  0.65 53.46           O  
ANISOU  777  O  AGLU B  94     5847   7506   6960    852   -798   1242       O  
ATOM    778  CB AGLU B  94      -0.332  25.984   1.265  0.65 43.52           C  
ANISOU  778  CB AGLU B  94     4430   6419   5686    364   -155    427       C  
ATOM    779  CG AGLU B  94       0.495  27.176   0.818  0.65 49.02           C  
ANISOU  779  CG AGLU B  94     4991   7531   6105     -8   -158    231       C  
ATOM    780  CD AGLU B  94       0.689  28.199   1.924  0.65 53.37           C  
ANISOU  780  CD AGLU B  94     5740   8270   6268   -204   -437    450       C  
ATOM    781  OE1AGLU B  94       1.618  29.027   1.817  0.65 59.29           O  
ANISOU  781  OE1AGLU B  94     6312   9377   6837   -499   -503    328       O  
ATOM    782  OE2AGLU B  94      -0.087  28.174   2.903  0.65 50.00           O  
ANISOU  782  OE2AGLU B  94     5653   7646   5698   -103   -569    721       O  
ATOM    783  N  BGLU B  94      -0.222  23.571   1.827  0.35 42.43           N  
ANISOU  783  N  BGLU B  94     4064   5751   6305   1087   -220    649       N  
ATOM    784  CA BGLU B  94       0.447  24.860   1.920  0.35 46.42           C  
ANISOU  784  CA BGLU B  94     4465   6718   6454    778   -340    587       C  
ATOM    785  C  BGLU B  94       0.763  25.144   3.379  0.35 50.14           C  
ANISOU  785  C  BGLU B  94     5021   7315   6715    829   -723    961       C  
ATOM    786  O  BGLU B  94      -0.115  25.015   4.238  0.35 53.14           O  
ANISOU  786  O  BGLU B  94     5803   7462   6924    861   -806   1251       O  
ATOM    787  CB BGLU B  94      -0.435  25.967   1.330  0.35 43.54           C  
ANISOU  787  CB BGLU B  94     4470   6394   5679    371   -160    451       C  
ATOM    788  CG BGLU B  94      -0.142  27.357   1.857  0.35 48.58           C  
ANISOU  788  CG BGLU B  94     5261   7335   5863     42   -334    519       C  
ATOM    789  CD BGLU B  94       0.952  28.047   1.075  0.35 54.37           C  
ANISOU  789  CD BGLU B  94     5681   8452   6525   -247   -269    239       C  
ATOM    790  OE1BGLU B  94       1.244  27.601  -0.056  0.35 54.69           O  
ANISOU  790  OE1BGLU B  94     5460   8525   6793   -244    -20    -50       O  
ATOM    791  OE2BGLU B  94       1.518  29.034   1.589  0.35 58.49           O  
ANISOU  791  OE2BGLU B  94     6232   9252   6742   -520   -445    285       O  
ATOM    792  N   GLY B  95       2.007  25.520   3.657  1.00 52.12           N  
ANISOU  792  N   GLY B  95     4881   7968   6955    801   -948    936       N  
ATOM    793  CA  GLY B  95       2.388  25.823   5.027  1.00 51.18           C  
ANISOU  793  CA  GLY B  95     4827   8031   6587    804  -1354   1274       C  
ATOM    794  C   GLY B  95       2.322  24.619   5.938  1.00 55.62           C  
ANISOU  794  C   GLY B  95     5434   8304   7398   1247  -1603   1652       C  
ATOM    795  O   GLY B  95       1.956  24.749   7.113  1.00 58.15           O  
ANISOU  795  O   GLY B  95     6190   8512   7393   1161  -1771   1878       O  
ATOM    796  N   GLY B  96       2.652  23.441   5.414  1.00 55.42           N  
ANISOU  796  N   GLY B  96     5100   8039   7918   1661  -1532   1583       N  
ATOM    797  CA  GLY B  96       2.657  22.232   6.211  1.00 55.92           C  
ANISOU  797  CA  GLY B  96     5383   7693   8171   2015  -1708   1784       C  
ATOM    798  C   GLY B  96       1.296  21.677   6.557  1.00 54.24           C  
ANISOU  798  C   GLY B  96     5781   6990   7838   1970  -1541   1967       C  
ATOM    799  O   GLY B  96       1.206  20.813   7.433  1.00 57.32           O  
ANISOU  799  O   GLY B  96     6466   7101   8210   2147  -1698   2168       O  
ATOM    800  N   ARG B  97       0.231  22.138   5.902  1.00 49.87           N  
ANISOU  800  N   ARG B  97     5050   7878   6020   1891   -193   1816       N  
ATOM    801  CA  ARG B  97      -1.107  21.647   6.201  1.00 47.97           C  
ANISOU  801  CA  ARG B  97     5241   7278   5708   1955    -97   1644       C  
ATOM    802  C   ARG B  97      -1.961  21.686   4.943  1.00 44.55           C  
ANISOU  802  C   ARG B  97     4942   6659   5325   1918    121   1470       C  
ATOM    803  O   ARG B  97      -1.646  22.379   3.973  1.00 40.13           O  
ANISOU  803  O   ARG B  97     4126   6280   4842   1810    136   1489       O  
ATOM    804  CB  ARG B  97      -1.776  22.467   7.309  1.00 46.37           C  
ANISOU  804  CB  ARG B  97     5178   7007   5433   1686   -373   1569       C  
ATOM    805  CG  ARG B  97      -1.782  23.961   7.053  1.00 52.90           C  
ANISOU  805  CG  ARG B  97     5821   7953   6326   1292   -610   1502       C  
ATOM    806  CD  ARG B  97      -2.920  24.628   7.800  1.00 54.92           C  
ANISOU  806  CD  ARG B  97     6415   7971   6482   1052   -726   1276       C  
ATOM    807  NE  ARG B  97      -4.192  24.458   7.108  1.00 58.27           N  
ANISOU  807  NE  ARG B  97     7075   8128   6935   1002   -461   1064       N  
ATOM    808  CZ  ARG B  97      -5.379  24.499   7.704  1.00 56.01           C  
ANISOU  808  CZ  ARG B  97     7101   7626   6553    936   -409    912       C  
ATOM    809  NH1 ARG B  97      -5.459  24.695   9.015  1.00 61.13           N  
ANISOU  809  NH1 ARG B  97     7916   8275   7035    953   -577    928       N  
ATOM    810  NH2 ARG B  97      -6.486  24.335   6.990  1.00 45.71           N  
ANISOU  810  NH2 ARG B  97     5932   6136   5301    866   -192    766       N  
ATOM    811  N   GLU B  98      -3.060  20.937   4.978  1.00 39.86           N  
ANISOU  811  N   GLU B  98     4768   5687   4690   1935    283   1286       N  
ATOM    812  CA  GLU B  98      -4.006  20.924   3.874  1.00 38.19           C  
ANISOU  812  CA  GLU B  98     4743   5252   4515   1805    449   1067       C  
ATOM    813  C   GLU B  98      -5.006  22.057   4.047  1.00 31.98           C  
ANISOU  813  C   GLU B  98     3974   4417   3761   1398    314    906       C  
ATOM    814  O   GLU B  98      -5.378  22.404   5.171  1.00 32.34           O  
ANISOU  814  O   GLU B  98     4096   4436   3756   1274    171    903       O  
ATOM    815  CB  GLU B  98      -4.748  19.587   3.789  1.00 43.89           C  
ANISOU  815  CB  GLU B  98     5904   5581   5193   1955    641    971       C  
ATOM    816  CG  GLU B  98      -5.508  19.406   2.475  1.00 53.83           C  
ANISOU  816  CG  GLU B  98     7355   6629   6470   1865    781    766       C  
ATOM    817  CD  GLU B  98      -6.393  18.169   2.447  1.00 65.76           C  
ANISOU  817  CD  GLU B  98     9338   7695   7953   1886    889    663       C  
ATOM    818  OE1 GLU B  98      -7.124  17.927   3.432  1.00 67.69           O  
ANISOU  818  OE1 GLU B  98     9731   7777   8210   1725    842    689       O  
ATOM    819  OE2 GLU B  98      -6.366  17.446   1.427  1.00 67.64           O  
ANISOU  819  OE2 GLU B  98     9818   7739   8143   2057   1013    566       O  
ATOM    820  N   HIS B  99      -5.414  22.644   2.926  1.00 25.10           N  
ANISOU  820  N   HIS B  99     3047   3546   2943   1237    367    782       N  
ATOM    821  CA  HIS B  99      -6.502  23.610   2.872  1.00 24.76           C  
ANISOU  821  CA  HIS B  99     3061   3423   2924    913    289    621       C  
ATOM    822  C   HIS B  99      -7.536  23.104   1.880  1.00 27.87           C  
ANISOU  822  C   HIS B  99     3665   3595   3330    861    459    454       C  
ATOM    823  O   HIS B  99      -7.182  22.532   0.845  1.00 26.58           O  
ANISOU  823  O   HIS B  99     3531   3413   3156   1020    591    437       O  
ATOM    824  CB  HIS B  99      -6.012  25.005   2.438  1.00 20.89           C  
ANISOU  824  CB  HIS B  99     2288   3160   2490    721    131    657       C  
ATOM    825  CG  HIS B  99      -4.922  25.556   3.307  1.00 27.92           C  
ANISOU  825  CG  HIS B  99     2956   4272   3380    700   -106    838       C  
ATOM    826  ND1 HIS B  99      -5.170  26.402   4.368  1.00 25.20           N  
ANISOU  826  ND1 HIS B  99     2695   3896   2983    514   -351    798       N  
ATOM    827  CD2 HIS B  99      -3.580  25.368   3.282  1.00 30.00           C  
ANISOU  827  CD2 HIS B  99     2921   4804   3675    847   -156   1071       C  
ATOM    828  CE1 HIS B  99      -4.027  26.720   4.951  1.00 34.28           C  
ANISOU  828  CE1 HIS B  99     3631   5258   4135    498   -584    981       C  
ATOM    829  NE2 HIS B  99      -3.048  26.103   4.314  1.00 31.72           N  
ANISOU  829  NE2 HIS B  99     3029   5145   3878    688   -469   1171       N  
ATOM    830  N   VAL B 100      -8.810  23.321   2.189  1.00 22.54           N  
ANISOU  830  N   VAL B 100     3137   2770   2656    652    446    342       N  
ATOM    831  CA  VAL B 100      -9.903  22.998   1.279  1.00 20.39           C  
ANISOU  831  CA  VAL B 100     3014   2325   2407    521    540    203       C  
ATOM    832  C   VAL B 100     -10.768  24.240   1.125  1.00 20.75           C  
ANISOU  832  C   VAL B 100     2954   2455   2476    286    461    126       C  
ATOM    833  O   VAL B 100     -10.999  24.963   2.100  1.00 19.16           O  
ANISOU  833  O   VAL B 100     2716   2317   2246    230    373    156       O  
ATOM    834  CB  VAL B 100     -10.753  21.815   1.792  1.00 23.98           C  
ANISOU  834  CB  VAL B 100     3740   2514   2859    495    618    207       C  
ATOM    835  CG1 VAL B 100     -11.814  21.451   0.766  1.00 27.38           C  
ANISOU  835  CG1 VAL B 100     4309   2772   3322    308    653     80       C  
ATOM    836  CG2 VAL B 100      -9.875  20.609   2.118  1.00 28.36           C  
ANISOU  836  CG2 VAL B 100     4455   2944   3376    771    687    302       C  
ATOM    837  N   ALA B 101     -11.243  24.494  -0.093  1.00 18.92           N  
ANISOU  837  N   ALA B 101     2706   2218   2265    184    487     25       N  
ATOM    838  CA  ALA B 101     -12.153  25.609  -0.318  1.00 18.32           C  
ANISOU  838  CA  ALA B 101     2545   2211   2204     -1    424    -34       C  
ATOM    839  C   ALA B 101     -13.258  25.204  -1.277  1.00 18.45           C  
ANISOU  839  C   ALA B 101     2645   2132   2234   -136    467   -130       C  
ATOM    840  O   ALA B 101     -13.014  24.493  -2.254  1.00 19.56           O  
ANISOU  840  O   ALA B 101     2891   2192   2350    -91    509   -193       O  
ATOM    841  CB  ALA B 101     -11.418  26.842  -0.875  1.00 20.64           C  
ANISOU  841  CB  ALA B 101     2658   2677   2508    -20    337    -14       C  
ATOM    842  N   HIS B 102     -14.472  25.665  -0.997  1.00 18.47           N  
ANISOU  842  N   HIS B 102     2607   2158   2252   -281    446   -133       N  
ATOM    843  CA  HIS B 102     -15.566  25.551  -1.954  1.00 17.11           C  
ANISOU  843  CA  HIS B 102     2434   1969   2099   -449    431   -194       C  
ATOM    844  C   HIS B 102     -15.392  26.609  -3.028  1.00 15.46           C  
ANISOU  844  C   HIS B 102     2118   1891   1863   -452    378   -254       C  
ATOM    845  O   HIS B 102     -15.150  27.772  -2.712  1.00 15.50           O  
ANISOU  845  O   HIS B 102     2018   2006   1864   -409    339   -220       O  
ATOM    846  CB  HIS B 102     -16.914  25.743  -1.256  1.00 14.88           C  
ANISOU  846  CB  HIS B 102     2065   1745   1844   -569    444   -113       C  
ATOM    847  CG  HIS B 102     -17.394  24.526  -0.532  1.00 19.47           C  
ANISOU  847  CG  HIS B 102     2744   2191   2463   -653    499    -17       C  
ATOM    848  ND1 HIS B 102     -17.082  24.280   0.786  1.00 19.57           N  
ANISOU  848  ND1 HIS B 102     2803   2184   2447   -533    571     89       N  
ATOM    849  CD2 HIS B 102     -18.147  23.479  -0.944  1.00 22.53           C  
ANISOU  849  CD2 HIS B 102     3214   2438   2910   -866    472      7       C  
ATOM    850  CE1 HIS B 102     -17.633  23.136   1.161  1.00 21.09           C  
ANISOU  850  CE1 HIS B 102     3088   2238   2687   -658    617    195       C  
ATOM    851  NE2 HIS B 102     -18.282  22.629   0.130  1.00 23.53           N  
ANISOU  851  NE2 HIS B 102     3423   2454   3062   -883    546    149       N  
ATOM    852  N   LEU B 103     -15.497  26.214  -4.297  1.00 14.10           N  
ANISOU  852  N   LEU B 103     2018   1685   1654   -498    363   -339       N  
ATOM    853  CA  LEU B 103     -15.456  27.182  -5.387  1.00 15.90           C  
ANISOU  853  CA  LEU B 103     2155   2050   1836   -503    322   -370       C  
ATOM    854  C   LEU B 103     -16.870  27.721  -5.573  1.00 19.47           C  
ANISOU  854  C   LEU B 103     2511   2581   2308   -657    250   -364       C  
ATOM    855  O   LEU B 103     -17.800  26.944  -5.809  1.00 21.17           O  
ANISOU  855  O   LEU B 103     2774   2737   2534   -808    204   -388       O  
ATOM    856  CB  LEU B 103     -14.925  26.519  -6.662  1.00 15.47           C  
ANISOU  856  CB  LEU B 103     2250   1952   1676   -429    348   -459       C  
ATOM    857  CG  LEU B 103     -14.834  27.328  -7.942  1.00 30.76           C  
ANISOU  857  CG  LEU B 103     4130   4036   3520   -410    329   -476       C  
ATOM    858  CD1 LEU B 103     -14.061  28.613  -7.721  1.00 31.48           C  
ANISOU  858  CD1 LEU B 103     4017   4286   3657   -354    347   -346       C  
ATOM    859  CD2 LEU B 103     -14.160  26.460  -8.995  1.00 24.45           C  
ANISOU  859  CD2 LEU B 103     3541   3184   2563   -249    398   -560       C  
ATOM    860  N   LEU B 104     -17.047  29.034  -5.413  1.00 16.04           N  
ANISOU  860  N   LEU B 104     1943   2271   1879   -621    225   -311       N  
ATOM    861  CA  LEU B 104     -18.378  29.633  -5.368  1.00 14.97           C  
ANISOU  861  CA  LEU B 104     1689   2244   1755   -681    187   -264       C  
ATOM    862  C   LEU B 104     -18.486  30.725  -6.416  1.00 18.62           C  
ANISOU  862  C   LEU B 104     2095   2813   2165   -656    126   -265       C  
ATOM    863  O   LEU B 104     -17.520  31.452  -6.653  1.00 18.63           O  
ANISOU  863  O   LEU B 104     2127   2804   2148   -583    124   -255       O  
ATOM    864  CB  LEU B 104     -18.675  30.244  -4.002  1.00 13.22           C  
ANISOU  864  CB  LEU B 104     1425   2050   1548   -576    234   -185       C  
ATOM    865  CG  LEU B 104     -18.638  29.220  -2.870  1.00 13.63           C  
ANISOU  865  CG  LEU B 104     1528   2021   1629   -583    308   -145       C  
ATOM    866  CD1 LEU B 104     -18.638  29.949  -1.525  1.00 15.88           C  
ANISOU  866  CD1 LEU B 104     1840   2331   1862   -415    352    -88       C  
ATOM    867  CD2 LEU B 104     -19.860  28.317  -2.993  1.00 16.85           C  
ANISOU  867  CD2 LEU B 104     1847   2469   2085   -754    319    -77       C  
ATOM    868  N   PHE B 105     -19.663  30.855  -7.023  1.00 17.20           N  
ANISOU  868  N   PHE B 105     1816   2751   1968   -731     64   -241       N  
ATOM    869  CA  PHE B 105     -19.849  31.831  -8.087  1.00 14.37           C  
ANISOU  869  CA  PHE B 105     1417   2499   1542   -693     -2   -225       C  
ATOM    870  C   PHE B 105     -20.977  32.794  -7.739  1.00 18.78           C  
ANISOU  870  C   PHE B 105     1832   3195   2109   -603    -15   -118       C  
ATOM    871  O   PHE B 105     -21.824  32.527  -6.879  1.00 19.32           O  
ANISOU  871  O   PHE B 105     1788   3333   2222   -594     29    -46       O  
ATOM    872  CB  PHE B 105     -20.102  31.142  -9.444  1.00 15.91           C  
ANISOU  872  CB  PHE B 105     1659   2734   1652   -816    -94   -299       C  
ATOM    873  CG  PHE B 105     -18.936  30.320  -9.917  1.00 21.00           C  
ANISOU  873  CG  PHE B 105     2496   3251   2232   -799    -48   -404       C  
ATOM    874  CD1 PHE B 105     -17.848  30.925 -10.547  1.00 16.89           C  
ANISOU  874  CD1 PHE B 105     2019   2761   1638   -673     13   -384       C  
ATOM    875  CD2 PHE B 105     -18.896  28.950  -9.686  1.00 24.00           C  
ANISOU  875  CD2 PHE B 105     3014   3482   2621   -884    -51   -489       C  
ATOM    876  CE1 PHE B 105     -16.760  30.170 -10.974  1.00 20.37           C  
ANISOU  876  CE1 PHE B 105     2600   3143   1997   -586     98   -441       C  
ATOM    877  CE2 PHE B 105     -17.814  28.185 -10.111  1.00 26.40           C  
ANISOU  877  CE2 PHE B 105     3527   3665   2837   -783     16   -581       C  
ATOM    878  CZ  PHE B 105     -16.745  28.799 -10.764  1.00 24.58           C  
ANISOU  878  CZ  PHE B 105     3301   3524   2515   -609    105   -552       C  
ATOM    879  N   LEU B 106     -20.961  33.937  -8.408  1.00 20.13           N  
ANISOU  879  N   LEU B 106     2013   3412   2223   -504    -57    -80       N  
ATOM    880  CA  LEU B 106     -21.898  35.027  -8.181  1.00 19.93           C  
ANISOU  880  CA  LEU B 106     1906   3491   2175   -332    -61     27       C  
ATOM    881  C   LEU B 106     -22.672  35.264  -9.480  1.00 22.51           C  
ANISOU  881  C   LEU B 106     2118   4000   2436   -361   -164     81       C  
ATOM    882  O   LEU B 106     -22.563  34.492 -10.433  1.00 24.31           O  
ANISOU  882  O   LEU B 106     2348   4265   2624   -532   -242     16       O  
ATOM    883  CB  LEU B 106     -21.148  36.272  -7.698  1.00 19.60           C  
ANISOU  883  CB  LEU B 106     2054   3278   2116   -171    -50     37       C  
ATOM    884  CG  LEU B 106     -20.373  36.082  -6.383  1.00 21.76           C  
ANISOU  884  CG  LEU B 106     2459   3383   2427   -151     -1    -17       C  
ATOM    885  CD1 LEU B 106     -19.422  37.229  -6.187  1.00 29.62           C  
ANISOU  885  CD1 LEU B 106     3669   4177   3410   -104    -75    -14       C  
ATOM    886  CD2 LEU B 106     -21.327  35.977  -5.189  1.00 19.33           C  
ANISOU  886  CD2 LEU B 106     2106   3144   2094     11     90     22       C  
ATOM    887  N   ARG B 107     -23.491  36.318  -9.513  1.00 17.31           N  
ANISOU  887  N   ARG B 107     1384   3455   1737   -162   -173    199       N  
ATOM    888  CA  ARG B 107     -24.266  36.554 -10.731  1.00 18.93           C  
ANISOU  888  CA  ARG B 107     1459   3867   1868   -172   -291    276       C  
ATOM    889  C   ARG B 107     -23.400  37.143 -11.836  1.00 23.00           C  
ANISOU  889  C   ARG B 107     2157   4287   2296   -177   -344    248       C  
ATOM    890  O   ARG B 107     -23.604  36.840 -13.021  1.00 24.39           O  
ANISOU  890  O   ARG B 107     2299   4593   2376   -276   -451    243       O  
ATOM    891  CB  ARG B 107     -25.455  37.462 -10.433  1.00 20.91           C  
ANISOU  891  CB  ARG B 107     1545   4305   2093     98   -270    448       C  
ATOM    892  CG  ARG B 107     -26.393  36.869  -9.381  1.00 25.96           C  
ANISOU  892  CG  ARG B 107     1939   5124   2803    126   -181    542       C  
ATOM    893  CD  ARG B 107     -27.638  37.725  -9.179  1.00 38.52           C  
ANISOU  893  CD  ARG B 107     3310   6983   4343    456   -130    758       C  
ATOM    894  NE  ARG B 107     -27.293  39.137  -9.049  1.00 43.71           N  
ANISOU  894  NE  ARG B 107     4253   7448   4908    808    -76    754       N  
ATOM    895  CZ  ARG B 107     -27.038  39.733  -7.890  1.00 52.55           C  
ANISOU  895  CZ  ARG B 107     5601   8377   5988   1078     61    723       C  
ATOM    896  NH1 ARG B 107     -27.103  39.034  -6.759  1.00 39.60           N  
ANISOU  896  NH1 ARG B 107     3900   6764   4382   1063    187    709       N  
ATOM    897  NH2 ARG B 107     -26.723  41.023  -7.863  1.00 58.84           N  
ANISOU  897  NH2 ARG B 107     6727   8936   6694   1359     56    709       N  
ATOM    898  N   ASP B 108     -22.429  37.974 -11.469  1.00 17.49           N  
ANISOU  898  N   ASP B 108     1659   3369   1616    -89   -283    249       N  
ATOM    899  CA  ASP B 108     -21.455  38.481 -12.435  1.00 17.39           C  
ANISOU  899  CA  ASP B 108     1789   3276   1543   -133   -305    278       C  
ATOM    900  C   ASP B 108     -20.484  37.369 -12.830  1.00 19.72           C  
ANISOU  900  C   ASP B 108     2109   3559   1824   -314   -268    172       C  
ATOM    901  O   ASP B 108     -19.916  36.701 -11.962  1.00 21.00           O  
ANISOU  901  O   ASP B 108     2289   3617   2074   -379   -205     90       O  
ATOM    902  CB  ASP B 108     -20.694  39.654 -11.812  1.00 17.22           C  
ANISOU  902  CB  ASP B 108     1963   3006   1576    -51   -287    343       C  
ATOM    903  CG  ASP B 108     -19.852  40.407 -12.816  1.00 19.82           C  
ANISOU  903  CG  ASP B 108     2401   3274   1857   -105   -314    462       C  
ATOM    904  OD1 ASP B 108     -18.754  39.918 -13.156  1.00 18.77           O  
ANISOU  904  OD1 ASP B 108     2257   3140   1733   -256   -267    459       O  
ATOM    905  OD2 ASP B 108     -20.275  41.499 -13.251  1.00 20.27           O  
ANISOU  905  OD2 ASP B 108     2548   3292   1861     26   -368    589       O  
ATOM    906  N   THR B 109     -20.263  37.177 -14.134  1.00 17.37           N  
ANISOU  906  N   THR B 109     1840   3370   1388   -351   -297    181       N  
ATOM    907  CA  THR B 109     -19.476  36.021 -14.558  1.00 19.70           C  
ANISOU  907  CA  THR B 109     2199   3668   1618   -442   -244     67       C  
ATOM    908  C   THR B 109     -17.970  36.205 -14.418  1.00 22.89           C  
ANISOU  908  C   THR B 109     2659   3980   2060   -434   -116    129       C  
ATOM    909  O   THR B 109     -17.233  35.245 -14.676  1.00 21.87           O  
ANISOU  909  O   THR B 109     2577   3863   1868   -439    -35     54       O  
ATOM    910  CB  THR B 109     -19.770  35.650 -16.010  1.00 19.02           C  
ANISOU  910  CB  THR B 109     2177   3739   1309   -442   -318     34       C  
ATOM    911  OG1 THR B 109     -19.348  36.714 -16.871  1.00 19.92           O  
ANISOU  911  OG1 THR B 109     2331   3918   1318   -346   -287    199       O  
ATOM    912  CG2 THR B 109     -21.263  35.345 -16.207  1.00 20.29           C  
ANISOU  912  CG2 THR B 109     2240   4033   1438   -508   -501     -5       C  
ATOM    913  N   LYS B 110     -17.486  37.387 -14.032  1.00 16.40           N  
ANISOU  913  N   LYS B 110     1838   3063   1330   -422   -109    278       N  
ATOM    914  CA  LYS B 110     -16.051  37.650 -13.999  1.00 16.58           C  
ANISOU  914  CA  LYS B 110     1852   3044   1402   -472    -26    404       C  
ATOM    915  C   LYS B 110     -15.503  37.702 -12.578  1.00 18.81           C  
ANISOU  915  C   LYS B 110     2125   3159   1863   -539    -45    387       C  
ATOM    916  O   LYS B 110     -14.414  38.243 -12.359  1.00 18.26           O  
ANISOU  916  O   LYS B 110     2027   3035   1875   -628    -47    536       O  
ATOM    917  CB  LYS B 110     -15.736  38.954 -14.729  1.00 18.09           C  
ANISOU  917  CB  LYS B 110     2073   3237   1564   -483    -48    634       C  
ATOM    918  CG  LYS B 110     -16.109  38.919 -16.214  1.00 19.58           C  
ANISOU  918  CG  LYS B 110     2284   3624   1533   -396    -20    683       C  
ATOM    919  CD  LYS B 110     -15.526  37.709 -16.943  1.00 22.73           C  
ANISOU  919  CD  LYS B 110     2675   4194   1767   -338    109    604       C  
ATOM    920  CE  LYS B 110     -15.950  37.698 -18.401  1.00 31.49           C  
ANISOU  920  CE  LYS B 110     3871   5491   2602   -230    108    630       C  
ATOM    921  NZ  LYS B 110     -15.704  36.374 -19.022  1.00 32.08           N  
ANISOU  921  NZ  LYS B 110     4050   5675   2465   -129    188    460       N  
ATOM    922  N   THR B 111     -16.249  37.183 -11.604  1.00 16.34           N  
ANISOU  922  N   THR B 111     1828   2777   1604   -513    -73    234       N  
ATOM    923  CA  THR B 111     -15.780  37.114 -10.230  1.00 16.18           C  
ANISOU  923  CA  THR B 111     1830   2613   1704   -547    -93    200       C  
ATOM    924  C   THR B 111     -15.949  35.696  -9.709  1.00 14.03           C  
ANISOU  924  C   THR B 111     1520   2372   1440   -535    -24     55       C  
ATOM    925  O   THR B 111     -16.661  34.869 -10.291  1.00 15.96           O  
ANISOU  925  O   THR B 111     1748   2703   1612   -525      2    -32       O  
ATOM    926  CB  THR B 111     -16.532  38.090  -9.296  1.00 17.83           C  
ANISOU  926  CB  THR B 111     2161   2667   1949   -477   -187    190       C  
ATOM    927  OG1 THR B 111     -17.925  37.755  -9.282  1.00 18.30           O  
ANISOU  927  OG1 THR B 111     2175   2822   1956   -365   -161    114       O  
ATOM    928  CG2 THR B 111     -16.370  39.535  -9.762  1.00 20.10           C  
ANISOU  928  CG2 THR B 111     2567   2842   2230   -486   -280    334       C  
ATOM    929  N   LEU B 112     -15.265  35.407  -8.603  1.00 16.13           N  
ANISOU  929  N   LEU B 112     1794   2547   1788   -554    -21     42       N  
ATOM    930  CA  LEU B 112     -15.432  34.107  -7.979  1.00 13.98           C  
ANISOU  930  CA  LEU B 112     1518   2265   1527   -534     43    -68       C  
ATOM    931  C   LEU B 112     -15.025  34.228  -6.518  1.00 11.71           C  
ANISOU  931  C   LEU B 112     1274   1866   1309   -525      4    -64       C  
ATOM    932  O   LEU B 112     -14.351  35.177  -6.116  1.00 13.34           O  
ANISOU  932  O   LEU B 112     1518   2001   1551   -563    -92     12       O  
ATOM    933  CB  LEU B 112     -14.630  33.012  -8.694  1.00 27.42           C  
ANISOU  933  CB  LEU B 112     3202   4034   3181   -514    139    -87       C  
ATOM    934  CG  LEU B 112     -13.109  32.996  -8.680  1.00 20.79           C  
ANISOU  934  CG  LEU B 112     2283   3247   2369   -486    191     32       C  
ATOM    935  CD1 LEU B 112     -12.543  32.343  -7.437  1.00 31.32           C  
ANISOU  935  CD1 LEU B 112     3611   4512   3777   -459    195     21       C  
ATOM    936  CD2 LEU B 112     -12.558  32.273  -9.910  1.00 25.93           C  
ANISOU  936  CD2 LEU B 112     2933   4024   2894   -375    323     42       C  
ATOM    937  N   MET B 113     -15.452  33.252  -5.736  1.00 13.58           N  
ANISOU  937  N   MET B 113     1529   2076   1553   -494     57   -138       N  
ATOM    938  CA  MET B 113     -15.173  33.244  -4.311  1.00 11.21           C  
ANISOU  938  CA  MET B 113     1295   1688   1274   -454     28   -139       C  
ATOM    939  C   MET B 113     -14.658  31.876  -3.917  1.00 12.19           C  
ANISOU  939  C   MET B 113     1409   1805   1419   -440    106   -158       C  
ATOM    940  O   MET B 113     -15.017  30.866  -4.528  1.00 15.19           O  
ANISOU  940  O   MET B 113     1784   2197   1790   -456    183   -205       O  
ATOM    941  CB  MET B 113     -16.426  33.555  -3.469  1.00 13.35           C  
ANISOU  941  CB  MET B 113     1629   1942   1503   -364     43   -164       C  
ATOM    942  CG  MET B 113     -16.990  34.948  -3.631  1.00 15.58           C  
ANISOU  942  CG  MET B 113     1983   2199   1739   -289    -26   -144       C  
ATOM    943  SD  MET B 113     -18.354  35.232  -2.480  1.00 15.32           S  
ANISOU  943  SD  MET B 113     2018   2193   1610    -69     49   -143       S  
ATOM    944  CE  MET B 113     -19.464  33.863  -2.915  1.00 16.68           C  
ANISOU  944  CE  MET B 113     1938   2565   1834   -153    182    -99       C  
ATOM    945  N   PHE B 114     -13.816  31.853  -2.882  1.00 13.14           N  
ANISOU  945  N   PHE B 114     1560   1880   1553   -409     58   -122       N  
ATOM    946  CA  PHE B 114     -13.457  30.623  -2.180  1.00 12.83           C  
ANISOU  946  CA  PHE B 114     1545   1812   1518   -349    126   -121       C  
ATOM    947  C   PHE B 114     -14.157  30.642  -0.831  1.00 11.97           C  
ANISOU  947  C   PHE B 114     1539   1646   1361   -294    122   -132       C  
ATOM    948  O   PHE B 114     -14.014  31.606  -0.075  1.00 13.19           O  
ANISOU  948  O   PHE B 114     1775   1770   1465   -263     11   -128       O  
ATOM    949  CB  PHE B 114     -11.949  30.516  -1.940  1.00 13.04           C  
ANISOU  949  CB  PHE B 114     1498   1884   1572   -319     73    -30       C  
ATOM    950  CG  PHE B 114     -11.128  30.405  -3.197  1.00 15.94           C  
ANISOU  950  CG  PHE B 114     1732   2365   1959   -310    131     34       C  
ATOM    951  CD1 PHE B 114     -11.661  29.840  -4.343  1.00 25.82           C  
ANISOU  951  CD1 PHE B 114     3021   3621   3169   -281    248    -40       C  
ATOM    952  CD2 PHE B 114      -9.814  30.847  -3.218  1.00 19.32           C  
ANISOU  952  CD2 PHE B 114     1993   2917   2431   -328     60    190       C  
ATOM    953  CE1 PHE B 114     -10.890  29.738  -5.502  1.00 34.19           C  
ANISOU  953  CE1 PHE B 114     3995   4805   4191   -211    330     23       C  
ATOM    954  CE2 PHE B 114      -9.045  30.753  -4.373  1.00 25.83           C  
ANISOU  954  CE2 PHE B 114     2658   3903   3251   -277    159    300       C  
ATOM    955  CZ  PHE B 114      -9.579  30.198  -5.506  1.00 27.21           C  
ANISOU  955  CZ  PHE B 114     2913   4079   3346   -189    312    208       C  
ATOM    956  N   GLY B 115     -14.888  29.567  -0.521  1.00 13.38           N  
ANISOU  956  N   GLY B 115     1744   1799   1539   -281    235   -134       N  
ATOM    957  CA  GLY B 115     -15.495  29.413   0.778  1.00 13.94           C  
ANISOU  957  CA  GLY B 115     1892   1858   1548   -204    280    -94       C  
ATOM    958  C   GLY B 115     -14.606  28.531   1.641  1.00 12.44           C  
ANISOU  958  C   GLY B 115     1773   1610   1342   -136    286    -47       C  
ATOM    959  O   GLY B 115     -14.262  27.417   1.248  1.00 16.34           O  
ANISOU  959  O   GLY B 115     2270   2046   1892   -153    347    -33       O  
ATOM    960  N   SER B 116     -14.235  29.046   2.811  1.00 13.41           N  
ANISOU  960  N   SER B 116     1993   1736   1366    -35    207    -26       N  
ATOM    961  CA  SER B 116     -13.318  28.369   3.722  1.00 14.28           C  
ANISOU  961  CA  SER B 116     2167   1823   1435     51    172     37       C  
ATOM    962  C   SER B 116     -14.050  27.983   4.992  1.00 15.83           C  
ANISOU  962  C   SER B 116     2494   2014   1507    164    265     99       C  
ATOM    963  O   SER B 116     -14.777  28.804   5.554  1.00 15.34           O  
ANISOU  963  O   SER B 116     2518   1990   1323    242    269     77       O  
ATOM    964  CB  SER B 116     -12.151  29.285   4.092  1.00 16.83           C  
ANISOU  964  CB  SER B 116     2503   2174   1718     51    -54     34       C  
ATOM    965  OG  SER B 116     -11.323  29.471   2.959  1.00 17.71           O  
ANISOU  965  OG  SER B 116     2441   2337   1953    -48   -106     51       O  
ATOM    966  N   TYR B 117     -13.839  26.741   5.446  1.00 16.32           N  
ANISOU  966  N   TYR B 117     2315   1783   2102    688    674    423       N  
ATOM    967  CA  TYR B 117     -14.422  26.253   6.696  1.00 19.23           C  
ANISOU  967  CA  TYR B 117     2689   2176   2440    722    557    535       C  
ATOM    968  C   TYR B 117     -15.931  26.485   6.759  1.00 17.85           C  
ANISOU  968  C   TYR B 117     2646   1919   2219    497    483    476       C  
ATOM    969  O   TYR B 117     -16.471  26.814   7.812  1.00 16.04           O  
ANISOU  969  O   TYR B 117     2318   1838   1939    424    395    492       O  
ATOM    970  CB  TYR B 117     -13.747  26.907   7.907  1.00 16.20           C  
ANISOU  970  CB  TYR B 117     2022   2088   2044    774    428    585       C  
ATOM    971  CG  TYR B 117     -12.253  26.728   7.968  1.00 22.61           C  
ANISOU  971  CG  TYR B 117     2598   3052   2942   1000    451    617       C  
ATOM    972  CD1 TYR B 117     -11.680  25.458   7.922  1.00 21.65           C  
ANISOU  972  CD1 TYR B 117     2549   2805   2873   1295    505    696       C  
ATOM    973  CD2 TYR B 117     -11.404  27.834   8.064  1.00 19.96           C  
ANISOU  973  CD2 TYR B 117     1956   2982   2646    920    402    548       C  
ATOM    974  CE1 TYR B 117     -10.302  25.287   7.972  1.00 27.22           C  
ANISOU  974  CE1 TYR B 117     2960   3688   3697   1559    508    680       C  
ATOM    975  CE2 TYR B 117     -10.025  27.670   8.125  1.00 22.33           C  
ANISOU  975  CE2 TYR B 117     1943   3480   3060   1109    422    545       C  
ATOM    976  CZ  TYR B 117      -9.479  26.394   8.074  1.00 28.44           C  
ANISOU  976  CZ  TYR B 117     2726   4166   3913   1454    475    599       C  
ATOM    977  OH  TYR B 117      -8.107  26.225   8.122  1.00 31.43           O  
ANISOU  977  OH  TYR B 117     2788   4731   4424   1602    451    517       O  
ATOM    978  N   LEU B 118     -16.628  26.305   5.626  1.00 16.75           N  
ANISOU  978  N   LEU B 118     2717   1556   2090    390    517    385       N  
ATOM    979  CA  LEU B 118     -18.031  26.725   5.567  1.00 14.34           C  
ANISOU  979  CA  LEU B 118     2439   1223   1785    191    401    273       C  
ATOM    980  C   LEU B 118     -18.934  25.920   6.495  1.00 14.95           C  
ANISOU  980  C   LEU B 118     2525   1312   1843    100    417    338       C  
ATOM    981  O   LEU B 118     -20.042  26.375   6.804  1.00 18.58           O  
ANISOU  981  O   LEU B 118     2867   1875   2319    -53    344    223       O  
ATOM    982  CB  LEU B 118     -18.575  26.613   4.139  1.00 15.50           C  
ANISOU  982  CB  LEU B 118     2835   1114   1941    101    378    162       C  
ATOM    983  CG  LEU B 118     -17.985  27.608   3.133  1.00 14.40           C  
ANISOU  983  CG  LEU B 118     2769    943   1758     90    352     74       C  
ATOM    984  CD1 LEU B 118     -18.674  27.435   1.775  1.00 16.36           C  
ANISOU  984  CD1 LEU B 118     3121   1140   1955     -9    239    -24       C  
ATOM    985  CD2 LEU B 118     -18.138  29.032   3.629  1.00 13.33           C  
ANISOU  985  CD2 LEU B 118     2454    994   1619     34    181     -7       C  
ATOM    986  N   ASP B 119     -18.508  24.741   6.928  1.00 15.31           N  
ANISOU  986  N   ASP B 119     2721   1249   1848    184    511    507       N  
ATOM    987  CA  ASP B 119     -19.329  23.952   7.838  1.00 19.39           C  
ANISOU  987  CA  ASP B 119     3325   1750   2294     27    548    598       C  
ATOM    988  C   ASP B 119     -19.056  24.267   9.301  1.00 22.62           C  
ANISOU  988  C   ASP B 119     3590   2415   2592     58    535    693       C  
ATOM    989  O   ASP B 119     -19.565  23.557  10.173  1.00 22.27           O  
ANISOU  989  O   ASP B 119     3678   2357   2426    -84    597    806       O  
ATOM    990  CB  ASP B 119     -19.132  22.453   7.579  1.00 22.56           C  
ANISOU  990  CB  ASP B 119     4042   1862   2668     65    591    713       C  
ATOM    991  CG  ASP B 119     -17.719  21.980   7.870  1.00 37.47           C  
ANISOU  991  CG  ASP B 119     5958   3738   4539    378    570    818       C  
ATOM    992  OD1 ASP B 119     -16.809  22.811   8.059  1.00 41.48           O  
ANISOU  992  OD1 ASP B 119     6278   4410   5072    576    564    843       O  
ATOM    993  OD2 ASP B 119     -17.516  20.755   7.899  1.00 44.25           O  
ANISOU  993  OD2 ASP B 119     7022   4420   5369    432    547    871       O  
ATOM    994  N   ASP B 120     -18.285  25.318   9.595  1.00 16.18           N  
ANISOU  994  N   ASP B 120     2545   1818   1783    200    453    651       N  
ATOM    995  CA  ASP B 120     -17.840  25.597  10.964  1.00 18.64           C  
ANISOU  995  CA  ASP B 120     2766   2350   1964    259    399    743       C  
ATOM    996  C   ASP B 120     -18.121  27.063  11.287  1.00 16.69           C  
ANISOU  996  C   ASP B 120     2263   2365   1714    198    317    563       C  
ATOM    997  O   ASP B 120     -17.359  27.946  10.892  1.00 15.52           O  
ANISOU  997  O   ASP B 120     1981   2283   1633    291    223    496       O  
ATOM    998  CB  ASP B 120     -16.358  25.259  11.138  1.00 20.76           C  
ANISOU  998  CB  ASP B 120     3040   2606   2242    539    324    884       C  
ATOM    999  CG  ASP B 120     -15.862  25.488  12.553  1.00 25.48           C  
ANISOU  999  CG  ASP B 120     3587   3409   2686    608    201    987       C  
ATOM   1000  OD1 ASP B 120     -16.657  25.932  13.400  1.00 23.91           O  
ANISOU 1000  OD1 ASP B 120     3382   3361   2343    428    216    946       O  
ATOM   1001  OD2 ASP B 120     -14.669  25.213  12.826  1.00 24.19           O  
ANISOU 1001  OD2 ASP B 120     3385   3266   2540    857     81   1091       O  
ATOM   1002  N   GLU B 121     -19.185  27.308  12.056  1.00 18.26           N  
ANISOU 1002  N   GLU B 121     2409   2713   1818     34    365    478       N  
ATOM   1003  CA  GLU B 121     -19.567  28.674  12.407  1.00 15.88           C  
ANISOU 1003  CA  GLU B 121     1897   2632   1504     20    279    268       C  
ATOM   1004  C   GLU B 121     -18.476  29.402  13.189  1.00 19.83           C  
ANISOU 1004  C   GLU B 121     2344   3286   1905    148    145    314       C  
ATOM   1005  O   GLU B 121     -18.454  30.640  13.215  1.00 19.10           O  
ANISOU 1005  O   GLU B 121     2134   3298   1825    168     21    145       O  
ATOM   1006  CB  GLU B 121     -20.873  28.630  13.208  1.00 23.53           C  
ANISOU 1006  CB  GLU B 121     2793   3773   2374   -155    411    150       C  
ATOM   1007  CG  GLU B 121     -21.515  29.973  13.489  1.00 23.03           C  
ANISOU 1007  CG  GLU B 121     2510   3918   2321   -123    336   -135       C  
ATOM   1008  CD  GLU B 121     -22.839  29.820  14.222  1.00 27.52           C  
ANISOU 1008  CD  GLU B 121     2937   4707   2814   -290    531   -293       C  
ATOM   1009  OE1 GLU B 121     -23.249  28.660  14.470  1.00 28.51           O  
ANISOU 1009  OE1 GLU B 121     3160   4807   2868   -498    731   -153       O  
ATOM   1010  OE2 GLU B 121     -23.462  30.853  14.556  1.00 33.18           O  
ANISOU 1010  OE2 GLU B 121     3452   5620   3535   -223    494   -569       O  
ATOM   1011  N   LYS B 122     -17.612  28.746  13.745  1.00 18.32           N  
ANISOU 1011  N   LYS B 122     2256   3088   1618    241    125    531       N  
ATOM   1012  CA  LYS B 122     -16.502  29.348  14.468  1.00 17.74           C  
ANISOU 1012  CA  LYS B 122     2101   3174   1465    352    -52    567       C  
ATOM   1013  C   LYS B 122     -15.405  29.865  13.549  1.00 17.94           C  
ANISOU 1013  C   LYS B 122     1969   3176   1671    443   -157    539       C  
ATOM   1014  O   LYS B 122     -14.544  30.612  14.017  1.00 19.86           O  
ANISOU 1014  O   LYS B 122     2088   3575   1884    470   -320    516       O  
ATOM   1015  CB  LYS B 122     -15.890  28.343  15.450  1.00 19.74           C  
ANISOU 1015  CB  LYS B 122     2523   3429   1549    451   -105    802       C  
ATOM   1016  CG  LYS B 122     -16.804  27.982  16.608  1.00 24.96           C  
ANISOU 1016  CG  LYS B 122     3391   4159   1934    298      2    845       C  
ATOM   1017  CD  LYS B 122     -16.098  27.154  17.687  1.00 36.31           C  
ANISOU 1017  CD  LYS B 122     5108   5544   3144    393   -109   1104       C  
ATOM   1018  CE  LYS B 122     -15.732  25.759  17.195  1.00 56.12           C  
ANISOU 1018  CE  LYS B 122     7808   7760   5757    524   -101   1299       C  
ATOM   1019  NZ  LYS B 122     -15.148  24.886  18.260  1.00 65.35           N  
ANISOU 1019  NZ  LYS B 122     9049   8745   7036    340    143   1253       N  
ATOM   1020  N   ASN B 123     -15.355  29.477  12.369  1.00 15.22           N  
ANISOU 1020  N   ASN B 123     1640   2650   1492    455    -54    530       N  
ATOM   1021  CA  ASN B 123     -14.172  29.688  11.543  1.00 15.29           C  
ANISOU 1021  CA  ASN B 123     1516   2654   1639    530    -72    533       C  
ATOM   1022  C   ASN B 123     -14.455  30.087  10.106  1.00 15.72           C  
ANISOU 1022  C   ASN B 123     1622   2553   1799    427     17    413       C  
ATOM   1023  O   ASN B 123     -13.503  30.378   9.369  1.00 16.31           O  
ANISOU 1023  O   ASN B 123     1601   2645   1953    426     54    395       O  
ATOM   1024  CB  ASN B 123     -13.316  28.418  11.533  1.00 17.94           C  
ANISOU 1024  CB  ASN B 123     1864   2924   2027    751    -28    697       C  
ATOM   1025  CG  ASN B 123     -12.532  28.255  12.802  1.00 21.64           C  
ANISOU 1025  CG  ASN B 123     2251   3562   2409    895   -211    814       C  
ATOM   1026  OD1 ASN B 123     -11.660  29.067  13.095  1.00 23.38           O  
ANISOU 1026  OD1 ASN B 123     2231   3991   2661    895   -354    766       O  
ATOM   1027  ND2 ASN B 123     -12.846  27.217  13.580  1.00 22.03           N  
ANISOU 1027  ND2 ASN B 123     2536   3509   2326    989   -233    971       N  
ATOM   1028  N   TRP B 124     -15.709  30.126   9.683  1.00 16.19           N  
ANISOU 1028  N   TRP B 124     1825   2477   1851    328     48    319       N  
ATOM   1029  CA  TRP B 124     -15.985  30.220   8.261  1.00 11.77           C  
ANISOU 1029  CA  TRP B 124     1397   1713   1363    259    102    235       C  
ATOM   1030  C   TRP B 124     -15.655  31.603   7.697  1.00 14.57           C  
ANISOU 1030  C   TRP B 124     1753   2076   1708    144     -7    115       C  
ATOM   1031  O   TRP B 124     -15.541  32.601   8.418  1.00 15.70           O  
ANISOU 1031  O   TRP B 124     1809   2356   1800    100   -153     56       O  
ATOM   1032  CB  TRP B 124     -17.445  29.844   7.988  1.00 11.59           C  
ANISOU 1032  CB  TRP B 124     1501   1552   1351    187    104    155       C  
ATOM   1033  CG  TRP B 124     -18.531  30.626   8.688  1.00 13.50           C  
ANISOU 1033  CG  TRP B 124     1650   1918   1562    127    -14      3       C  
ATOM   1034  CD1 TRP B 124     -18.516  31.939   9.064  1.00 11.60           C  
ANISOU 1034  CD1 TRP B 124     1337   1788   1283    128   -172   -128       C  
ATOM   1035  CD2 TRP B 124     -19.829  30.127   9.017  1.00 13.34           C  
ANISOU 1035  CD2 TRP B 124     1597   1919   1553     58     30    -68       C  
ATOM   1036  NE1 TRP B 124     -19.737  32.288   9.623  1.00 15.75           N  
ANISOU 1036  NE1 TRP B 124     1774   2409   1801    124   -227   -299       N  
ATOM   1037  CE2 TRP B 124     -20.556  31.189   9.603  1.00 14.47           C  
ANISOU 1037  CE2 TRP B 124     1595   2226   1677     63    -86   -268       C  
ATOM   1038  CE3 TRP B 124     -20.445  28.874   8.882  1.00 16.32           C  
ANISOU 1038  CE3 TRP B 124     2054   2194   1952    -29    163      6       C  
ATOM   1039  CZ2 TRP B 124     -21.864  31.035  10.059  1.00 17.40           C  
ANISOU 1039  CZ2 TRP B 124     1821   2722   2069     -2    -37   -417       C  
ATOM   1040  CZ3 TRP B 124     -21.745  28.725   9.327  1.00 16.02           C  
ANISOU 1040  CZ3 TRP B 124     1895   2264   1927   -161    202   -117       C  
ATOM   1041  CH2 TRP B 124     -22.443  29.806   9.908  1.00 19.18           C  
ANISOU 1041  CH2 TRP B 124     2075   2888   2327   -140    119   -337       C  
ATOM   1042  N   GLY B 125     -15.471  31.643   6.379  1.00 14.92           N  
ANISOU 1042  N   GLY B 125     2540   1761   1369    568    226   -311       N  
ATOM   1043  CA  GLY B 125     -15.216  32.922   5.750  1.00 13.90           C  
ANISOU 1043  CA  GLY B 125     2293   1669   1320    498     72   -326       C  
ATOM   1044  C   GLY B 125     -15.187  32.774   4.246  1.00 12.30           C  
ANISOU 1044  C   GLY B 125     1891   1558   1226    369     65   -297       C  
ATOM   1045  O   GLY B 125     -15.315  31.675   3.700  1.00 11.72           O  
ANISOU 1045  O   GLY B 125     1786   1510   1155    331    166   -292       O  
ATOM   1046  N   LEU B 126     -15.009  33.913   3.581  1.00 11.66           N  
ANISOU 1046  N   LEU B 126     1704   1507   1218    301    -54   -278       N  
ATOM   1047  CA  LEU B 126     -15.018  33.954   2.121  1.00  9.76           C  
ANISOU 1047  CA  LEU B 126     1291   1370   1049    189    -66   -235       C  
ATOM   1048  C   LEU B 126     -13.887  34.846   1.647  1.00 11.21           C  
ANISOU 1048  C   LEU B 126     1393   1592   1273    132   -220   -189       C  
ATOM   1049  O   LEU B 126     -13.609  35.879   2.269  1.00 13.07           O  
ANISOU 1049  O   LEU B 126     1690   1744   1531    137   -332   -193       O  
ATOM   1050  CB  LEU B 126     -16.337  34.531   1.586  1.00 12.65           C  
ANISOU 1050  CB  LEU B 126     1577   1750   1480    153    -24   -207       C  
ATOM   1051  CG  LEU B 126     -17.621  33.766   1.923  1.00 12.85           C  
ANISOU 1051  CG  LEU B 126     1609   1770   1505    168    130   -225       C  
ATOM   1052  CD1 LEU B 126     -18.821  34.688   1.815  1.00 18.54           C  
ANISOU 1052  CD1 LEU B 126     2240   2504   2302    197    149   -178       C  
ATOM   1053  CD2 LEU B 126     -17.742  32.578   0.968  1.00 14.12           C  
ANISOU 1053  CD2 LEU B 126     1701   2010   1653     52    183   -242       C  
ATOM   1054  N   SER B 127     -13.268  34.472   0.526  1.00 11.97           N  
ANISOU 1054  N   SER B 127     1364   1808   1377     67   -214   -144       N  
ATOM   1055  CA  SER B 127     -12.342  35.363  -0.165  1.00 10.69           C  
ANISOU 1055  CA  SER B 127     1081   1709   1272    -16   -321    -61       C  
ATOM   1056  C   SER B 127     -12.870  35.593  -1.575  1.00 13.22           C  
ANISOU 1056  C   SER B 127     1301   2121   1600    -93   -280      2       C  
ATOM   1057  O   SER B 127     -13.530  34.722  -2.153  1.00 12.69           O  
ANISOU 1057  O   SER B 127     1236   2115   1473    -92   -184    -36       O  
ATOM   1058  CB  SER B 127     -10.902  34.800  -0.184  1.00 13.42           C  
ANISOU 1058  CB  SER B 127     1344   2153   1603      4   -343    -31       C  
ATOM   1059  OG  SER B 127     -10.856  33.420  -0.544  1.00 14.63           O  
ANISOU 1059  OG  SER B 127     1511   2367   1680     82   -204    -67       O  
ATOM   1060  N   PHE B 128     -12.606  36.788  -2.115  1.00 11.28           N  
ANISOU 1060  N   PHE B 128      987   1877   1421   -171   -365    103       N  
ATOM   1061  CA  PHE B 128     -13.279  37.299  -3.308  1.00 11.86           C  
ANISOU 1061  CA  PHE B 128      997   2017   1492   -223   -355    191       C  
ATOM   1062  C   PHE B 128     -12.225  37.675  -4.344  1.00 11.84           C  
ANISOU 1062  C   PHE B 128      880   2131   1487   -310   -365    319       C  
ATOM   1063  O   PHE B 128     -11.240  38.334  -4.006  1.00 12.59           O  
ANISOU 1063  O   PHE B 128      935   2183   1667   -369   -436    380       O  
ATOM   1064  CB  PHE B 128     -14.122  38.517  -2.916  1.00 15.42           C  
ANISOU 1064  CB  PHE B 128     1508   2322   2028   -201   -422    228       C  
ATOM   1065  CG  PHE B 128     -14.869  39.173  -4.046  1.00 13.17           C  
ANISOU 1065  CG  PHE B 128     1160   2098   1748   -221   -434    350       C  
ATOM   1066  CD1 PHE B 128     -15.779  38.468  -4.815  1.00 12.95           C  
ANISOU 1066  CD1 PHE B 128     1066   2217   1635   -212   -387    341       C  
ATOM   1067  CD2 PHE B 128     -14.719  40.529  -4.268  1.00 14.39           C  
ANISOU 1067  CD2 PHE B 128     1335   2143   1989   -248   -509    476       C  
ATOM   1068  CE1 PHE B 128     -16.505  39.112  -5.828  1.00 18.11           C  
ANISOU 1068  CE1 PHE B 128     1654   2951   2274   -215   -432    469       C  
ATOM   1069  CE2 PHE B 128     -15.435  41.173  -5.271  1.00 16.32           C  
ANISOU 1069  CE2 PHE B 128     1534   2437   2230   -233   -525    618       C  
ATOM   1070  CZ  PHE B 128     -16.319  40.463  -6.048  1.00 17.54           C  
ANISOU 1070  CZ  PHE B 128     1602   2779   2282   -207   -495    618       C  
ATOM   1071  N   TYR B 129     -12.442  37.255  -5.597  1.00 13.92           N  
ANISOU 1071  N   TYR B 129     1092   2550   1647   -328   -296    361       N  
ATOM   1072  CA  TYR B 129     -11.474  37.366  -6.681  1.00 15.84           C  
ANISOU 1072  CA  TYR B 129     1236   2944   1839   -381   -246    483       C  
ATOM   1073  C   TYR B 129     -12.190  37.819  -7.943  1.00 13.98           C  
ANISOU 1073  C   TYR B 129      995   2805   1510   -416   -247    587       C  
ATOM   1074  O   TYR B 129     -13.392  37.599  -8.109  1.00 15.35           O  
ANISOU 1074  O   TYR B 129     1217   2986   1631   -391   -276    529       O  
ATOM   1075  CB  TYR B 129     -10.765  36.035  -6.963  1.00 13.28           C  
ANISOU 1075  CB  TYR B 129      896   2746   1404   -317   -119    404       C  
ATOM   1076  CG  TYR B 129     -10.195  35.401  -5.728  1.00 14.36           C  
ANISOU 1076  CG  TYR B 129     1050   2802   1604   -242   -122    308       C  
ATOM   1077  CD1 TYR B 129     -10.994  34.633  -4.886  1.00 15.32           C  
ANISOU 1077  CD1 TYR B 129     1300   2812   1708   -176   -114    163       C  
ATOM   1078  CD2 TYR B 129      -8.866  35.602  -5.380  1.00 14.88           C  
ANISOU 1078  CD2 TYR B 129      989   2916   1749   -244   -139    386       C  
ATOM   1079  CE1 TYR B 129     -10.480  34.076  -3.734  1.00 13.06           C  
ANISOU 1079  CE1 TYR B 129     1053   2454   1455    -92   -120    100       C  
ATOM   1080  CE2 TYR B 129      -8.334  35.038  -4.236  1.00 14.06           C  
ANISOU 1080  CE2 TYR B 129      895   2762   1685   -161   -172    315       C  
ATOM   1081  CZ  TYR B 129      -9.151  34.273  -3.418  1.00 13.97           C  
ANISOU 1081  CZ  TYR B 129     1051   2630   1628    -74   -160    173       C  
ATOM   1082  OH  TYR B 129      -8.640  33.720  -2.264  1.00 14.38           O  
ANISOU 1082  OH  TYR B 129     1138   2633   1694     26   -195    125       O  
ATOM   1083  N   ALA B 130     -11.431  38.437  -8.847  1.00 15.38           N  
ANISOU 1083  N   ALA B 130     1098   3080   1665   -477   -217    759       N  
ATOM   1084  CA  ALA B 130     -12.007  38.899 -10.108  1.00 16.54           C  
ANISOU 1084  CA  ALA B 130     1256   3341   1689   -498   -220    890       C  
ATOM   1085  C   ALA B 130     -10.973  38.815 -11.225  1.00 19.30           C  
ANISOU 1085  C   ALA B 130     1542   3880   1911   -528    -95   1023       C  
ATOM   1086  O   ALA B 130      -9.768  38.677 -10.990  1.00 21.44           O  
ANISOU 1086  O   ALA B 130     1716   4182   2247   -546    -13   1056       O  
ATOM   1087  CB  ALA B 130     -12.549  40.329  -9.971  1.00 21.19           C  
ANISOU 1087  CB  ALA B 130     1863   3777   2409   -527   -332   1041       C  
ATOM   1088  N   ASP B 131     -11.454  38.935 -12.464  1.00 19.49           N  
ANISOU 1088  N   ASP B 131     1609   4053   1743   -525    -79   1116       N  
ATOM   1089  CA  ASP B 131     -10.551  38.830 -13.604  1.00 21.44           C  
ANISOU 1089  CA  ASP B 131     1833   4465   1849   -515     58   1213       C  
ATOM   1090  C   ASP B 131      -9.805  40.133 -13.886  1.00 29.26           C  
ANISOU 1090  C   ASP B 131     2746   5393   2978   -587     61   1452       C  
ATOM   1091  O   ASP B 131      -9.014  40.189 -14.836  1.00 26.96           O  
ANISOU 1091  O   ASP B 131     2432   5202   2607   -567    176   1535       O  
ATOM   1092  CB  ASP B 131     -11.334  38.379 -14.838  1.00 24.14           C  
ANISOU 1092  CB  ASP B 131     2291   4938   1944   -464     52   1151       C  
ATOM   1093  CG  ASP B 131     -12.125  39.499 -15.453  1.00 32.32           C  
ANISOU 1093  CG  ASP B 131     3344   5963   2972   -490    -60   1326       C  
ATOM   1094  OD1 ASP B 131     -12.523  40.419 -14.705  1.00 33.75           O  
ANISOU 1094  OD1 ASP B 131     3489   6001   3335   -524   -164   1436       O  
ATOM   1095  OD2 ASP B 131     -12.351  39.463 -16.681  1.00 42.21           O  
ANISOU 1095  OD2 ASP B 131     4669   7331   4036   -458    -43   1353       O  
ATOM   1096  N   LYS B 132     -10.058  41.176 -13.101  1.00 25.16           N  
ANISOU 1096  N   LYS B 132     2211   4687   2663   -670    -54   1557       N  
ATOM   1097  CA  LYS B 132      -9.339  42.443 -13.114  1.00 25.24           C  
ANISOU 1097  CA  LYS B 132     2178   4559   2853   -769    -73   1748       C  
ATOM   1098  C   LYS B 132      -8.929  42.777 -11.687  1.00 26.54           C  
ANISOU 1098  C   LYS B 132     2309   4510   3266   -852   -166   1681       C  
ATOM   1099  O   LYS B 132      -9.579  42.326 -10.739  1.00 26.98           O  
ANISOU 1099  O   LYS B 132     2397   4491   3362   -822   -236   1530       O  
ATOM   1100  CB  LYS B 132     -10.215  43.575 -13.673  1.00 36.01           C  
ANISOU 1100  CB  LYS B 132     3636   5829   4220   -775   -151   1924       C  
ATOM   1101  CG  LYS B 132     -10.754  43.330 -15.079  1.00 34.18           C  
ANISOU 1101  CG  LYS B 132     3458   5795   3733   -684   -102   1965       C  
ATOM   1102  CD  LYS B 132      -9.675  43.541 -16.130  1.00 42.70           C  
ANISOU 1102  CD  LYS B 132     4500   6985   4739   -709     44   2093       C  
ATOM   1103  CE  LYS B 132     -10.238  43.453 -17.547  1.00 54.33           C  
ANISOU 1103  CE  LYS B 132     6070   8624   5948   -623     81   2147       C  
ATOM   1104  NZ  LYS B 132     -10.994  42.198 -17.807  1.00 57.95           N  
ANISOU 1104  NZ  LYS B 132     6591   9238   6187   -533     57   1927       N  
ATOM   1105  N   PRO B 133      -7.863  43.563 -11.492  1.00 32.53           N  
ANISOU 1105  N   PRO B 133     3010   5164   4188   -960   -178   1772       N  
ATOM   1106  CA  PRO B 133      -7.404  43.840 -10.117  1.00 26.29           C  
ANISOU 1106  CA  PRO B 133     2215   4176   3599  -1038   -295   1666       C  
ATOM   1107  C   PRO B 133      -8.314  44.771  -9.335  1.00 25.30           C  
ANISOU 1107  C   PRO B 133     2231   3765   3616  -1093   -445   1663       C  
ATOM   1108  O   PRO B 133      -8.140  44.905  -8.115  1.00 26.04           O  
ANISOU 1108  O   PRO B 133     2369   3686   3838  -1136   -558   1525       O  
ATOM   1109  CB  PRO B 133      -6.019  44.466 -10.322  1.00 27.94           C  
ANISOU 1109  CB  PRO B 133     2314   4383   3918  -1161   -266   1783       C  
ATOM   1110  CG  PRO B 133      -6.058  45.038 -11.677  1.00 29.37           C  
ANISOU 1110  CG  PRO B 133     2495   4644   4022  -1177   -164   1992       C  
ATOM   1111  CD  PRO B 133      -6.965  44.147 -12.501  1.00 32.75           C  
ANISOU 1111  CD  PRO B 133     2970   5267   4207  -1018    -80   1956       C  
ATOM   1112  N   GLU B 134      -9.276  45.416  -9.980  1.00 25.94           N  
ANISOU 1112  N   GLU B 134     2411   3781   3664  -1065   -450   1806       N  
ATOM   1113  CA  GLU B 134     -10.255  46.220  -9.265  1.00 28.32           C  
ANISOU 1113  CA  GLU B 134     2890   3787   4084  -1035   -569   1790       C  
ATOM   1114  C   GLU B 134     -11.639  45.898  -9.802  1.00 30.22           C  
ANISOU 1114  C   GLU B 134     3192   4126   4165   -827   -555   1771       C  
ATOM   1115  O   GLU B 134     -11.812  45.711 -11.008  1.00 34.16           O  
ANISOU 1115  O   GLU B 134     3642   4838   4498   -796   -486   1917       O  
ATOM   1116  CB  GLU B 134      -9.976  47.718  -9.409  1.00 31.63           C  
ANISOU 1116  CB  GLU B 134     3420   3941   4656  -1136   -615   1944       C  
ATOM   1117  CG  GLU B 134      -8.621  48.141  -8.880  1.00 40.86           C  
ANISOU 1117  CG  GLU B 134     4533   5024   5967  -1323   -655   1900       C  
ATOM   1118  CD  GLU B 134      -8.579  49.610  -8.495  1.00 60.21           C  
ANISOU 1118  CD  GLU B 134     7173   7112   8593  -1425   -742   1943       C  
ATOM   1119  OE1 GLU B 134      -9.549  50.338  -8.805  1.00 64.70           O  
ANISOU 1119  OE1 GLU B 134     7914   7502   9168  -1320   -739   2032       O  
ATOM   1120  OE2 GLU B 134      -7.567  50.041  -7.904  1.00 58.97           O  
ANISOU 1120  OE2 GLU B 134     6998   6855   8554  -1595   -808   1884       O  
ATOM   1121  N   THR B 135     -12.617  45.834  -8.908  1.00 25.96           N  
ANISOU 1121  N   THR B 135     2751   3448   3665   -688   -623   1598       N  
ATOM   1122  CA  THR B 135     -13.981  45.499  -9.287  1.00 21.78           C  
ANISOU 1122  CA  THR B 135     2227   3029   3018   -504   -627   1577       C  
ATOM   1123  C   THR B 135     -14.865  46.734  -9.230  1.00 27.30           C  
ANISOU 1123  C   THR B 135     3055   3493   3822   -387   -686   1709       C  
ATOM   1124  O   THR B 135     -14.530  47.742  -8.606  1.00 27.92           O  
ANISOU 1124  O   THR B 135     3275   3263   4072   -432   -722   1740       O  
ATOM   1125  CB  THR B 135     -14.573  44.427  -8.368  1.00 23.57           C  
ANISOU 1125  CB  THR B 135     2435   3308   3213   -408   -624   1313       C  
ATOM   1126  OG1 THR B 135     -14.714  44.970  -7.052  1.00 27.70           O  
ANISOU 1126  OG1 THR B 135     3085   3552   3889   -363   -669   1198       O  
ATOM   1127  CG2 THR B 135     -13.663  43.208  -8.302  1.00 20.69           C  
ANISOU 1127  CG2 THR B 135     1979   3122   2762   -491   -560   1181       C  
ATOM   1128  N   THR B 136     -16.023  46.622  -9.867  1.00 23.77           N  
ANISOU 1128  N   THR B 136     2565   3194   3273   -229   -703   1779       N  
ATOM   1129  CA  THR B 136     -17.037  47.655  -9.750  1.00 28.17           C  
ANISOU 1129  CA  THR B 136     3216   3561   3927    -47   -740   1878       C  
ATOM   1130  C   THR B 136     -17.718  47.563  -8.388  1.00 24.47           C  
ANISOU 1130  C   THR B 136     2803   2922   3572     93   -742   1683       C  
ATOM   1131  O   THR B 136     -17.576  46.582  -7.651  1.00 22.38           O  
ANISOU 1131  O   THR B 136     2489   2737   3277     52   -713   1456       O  
ATOM   1132  CB  THR B 136     -18.095  47.526 -10.844  1.00 30.96           C  
ANISOU 1132  CB  THR B 136     3471   4163   4129     79   -744   1940       C  
ATOM   1133  OG1 THR B 136     -18.845  46.321 -10.632  1.00 24.82           O  
ANISOU 1133  OG1 THR B 136     2555   3613   3262    121   -752   1758       O  
ATOM   1134  CG2 THR B 136     -17.471  47.520 -12.236  1.00 27.76           C  
ANISOU 1134  CG2 THR B 136     3036   3948   3564    -37   -717   2083       C  
ATOM   1135  N   LYS B 137     -18.482  48.608  -8.063  1.00 24.89           N  
ANISOU 1135  N   LYS B 137     2796   2944   3716    409   -305   1152       N  
ATOM   1136  CA  LYS B 137     -19.277  48.592  -6.839  1.00 28.29           C  
ANISOU 1136  CA  LYS B 137     3243   3286   4221    542   -214   1080       C  
ATOM   1137  C   LYS B 137     -20.308  47.466  -6.862  1.00 30.58           C  
ANISOU 1137  C   LYS B 137     3297   3932   4390    501   -318   1101       C  
ATOM   1138  O   LYS B 137     -20.537  46.802  -5.844  1.00 28.93           O  
ANISOU 1138  O   LYS B 137     3116   3696   4181    473   -300    918       O  
ATOM   1139  CB  LYS B 137     -19.964  49.944  -6.647  1.00 32.31           C  
ANISOU 1139  CB  LYS B 137     3816   3573   4888    847     14   1312       C  
ATOM   1140  CG  LYS B 137     -20.937  49.987  -5.481  1.00 45.24           C  
ANISOU 1140  CG  LYS B 137     5479   5107   6601   1047    198   1298       C  
ATOM   1141  CD  LYS B 137     -21.684  51.318  -5.425  1.00 55.27           C  
ANISOU 1141  CD  LYS B 137     6830   6158   8012   1378    528   1552       C  
ATOM   1142  CE  LYS B 137     -22.388  51.501  -4.086  1.00 59.05           C  
ANISOU 1142  CE  LYS B 137     7481   6423   8534   1524    805   1439       C  
ATOM   1143  NZ  LYS B 137     -23.153  52.773  -4.026  1.00 66.92           N  
ANISOU 1143  NZ  LYS B 137     8563   7255   9608   1782   1185   1640       N  
ATOM   1144  N   GLU B 138     -20.947  47.237  -8.010  1.00 23.10           N  
ANISOU 1144  N   GLU B 138     2127   3343   3306    444   -437   1337       N  
ATOM   1145  CA  GLU B 138     -21.962  46.186  -8.064  1.00 23.57           C  
ANISOU 1145  CA  GLU B 138     1977   3777   3203    297   -558   1375       C  
ATOM   1146  C   GLU B 138     -21.338  44.807  -7.908  1.00 25.19           C  
ANISOU 1146  C   GLU B 138     2349   3969   3254     -2   -608   1030       C  
ATOM   1147  O   GLU B 138     -21.914  43.933  -7.249  1.00 24.82           O  
ANISOU 1147  O   GLU B 138     2259   4015   3158    -88   -618    918       O  
ATOM   1148  CB  GLU B 138     -22.756  46.265  -9.371  1.00 31.39           C  
ANISOU 1148  CB  GLU B 138     2724   5198   4003    178   -697   1710       C  
ATOM   1149  CG  GLU B 138     -23.793  47.364  -9.404  1.00 42.65           C  
ANISOU 1149  CG  GLU B 138     3956   6674   5576    455   -543   2039       C  
ATOM   1150  CD  GLU B 138     -24.834  47.227  -8.310  1.00 49.60           C  
ANISOU 1150  CD  GLU B 138     4706   7571   6568    611   -417   2082       C  
ATOM   1151  OE1 GLU B 138     -25.466  46.152  -8.203  1.00 45.24           O  
ANISOU 1151  OE1 GLU B 138     4040   7292   5856    366   -538   2028       O  
ATOM   1152  OE2 GLU B 138     -25.023  48.207  -7.562  1.00 55.14           O  
ANISOU 1152  OE2 GLU B 138     5467   7984   7501    960   -159   2165       O  
ATOM   1153  N   GLN B 139     -20.165  44.589  -8.513  1.00 20.39           N  
ANISOU 1153  N   GLN B 139     1936   3230   2583   -136   -591    895       N  
ATOM   1154  CA  GLN B 139     -19.466  43.315  -8.338  1.00 18.82           C  
ANISOU 1154  CA  GLN B 139     1919   2944   2287   -329   -526    629       C  
ATOM   1155  C   GLN B 139     -19.148  43.073  -6.868  1.00 23.41           C  
ANISOU 1155  C   GLN B 139     2542   3309   3043   -210   -454    460       C  
ATOM   1156  O   GLN B 139     -19.384  41.980  -6.331  1.00 17.75           O  
ANISOU 1156  O   GLN B 139     1864   2617   2263   -306   -415    318       O  
ATOM   1157  CB  GLN B 139     -18.172  43.304  -9.163  1.00 18.32           C  
ANISOU 1157  CB  GLN B 139     2026   2741   2194   -392   -436    598       C  
ATOM   1158  CG  GLN B 139     -18.368  42.975 -10.653  1.00 20.34           C  
ANISOU 1158  CG  GLN B 139     2371   3206   2153   -634   -455    670       C  
ATOM   1159  CD  GLN B 139     -17.085  43.055 -11.455  1.00 20.45           C  
ANISOU 1159  CD  GLN B 139     2563   3051   2157   -644   -302    666       C  
ATOM   1160  OE1 GLN B 139     -16.255  43.943 -11.242  1.00 20.34           O  
ANISOU 1160  OE1 GLN B 139     2491   2868   2371   -458   -279    748       O  
ATOM   1161  NE2 GLN B 139     -16.918  42.122 -12.393  1.00 23.09           N  
ANISOU 1161  NE2 GLN B 139     3150   3418   2203   -895   -163    576       N  
ATOM   1162  N   LEU B 140     -18.610  44.092  -6.197  1.00 18.12           N  
ANISOU 1162  N   LEU B 140     1901   2424   2562    -44   -430    478       N  
ATOM   1163  CA  LEU B 140     -18.268  43.946  -4.785  1.00 17.64           C  
ANISOU 1163  CA  LEU B 140     1909   2194   2597     -5   -392    335       C  
ATOM   1164  C   LEU B 140     -19.517  43.740  -3.935  1.00 20.90           C  
ANISOU 1164  C   LEU B 140     2256   2677   3009     78   -373    307       C  
ATOM   1165  O   LEU B 140     -19.483  43.012  -2.934  1.00 19.56           O  
ANISOU 1165  O   LEU B 140     2128   2471   2832     46   -347    170       O  
ATOM   1166  CB  LEU B 140     -17.492  45.181  -4.324  1.00 19.95           C  
ANISOU 1166  CB  LEU B 140     2319   2252   3010     36   -377    356       C  
ATOM   1167  CG  LEU B 140     -16.925  45.196  -2.909  1.00 23.88           C  
ANISOU 1167  CG  LEU B 140     2937   2606   3532    -40   -379    229       C  
ATOM   1168  CD1 LEU B 140     -15.957  44.064  -2.737  1.00 19.77           C  
ANISOU 1168  CD1 LEU B 140     2338   2184   2989   -156   -415    215       C  
ATOM   1169  CD2 LEU B 140     -16.250  46.541  -2.626  1.00 25.87           C  
ANISOU 1169  CD2 LEU B 140     3377   2625   3826   -119   -366    246       C  
ATOM   1170  N   GLY B 141     -20.624  44.385  -4.313  1.00 20.50           N  
ANISOU 1170  N   GLY B 141     2070   2745   2973    209   -366    492       N  
ATOM   1171  CA  GLY B 141     -21.868  44.221  -3.577  1.00 26.95           C  
ANISOU 1171  CA  GLY B 141     2761   3667   3813    323   -310    548       C  
ATOM   1172  C   GLY B 141     -22.345  42.784  -3.507  1.00 20.50           C  
ANISOU 1172  C   GLY B 141     1857   3076   2857    119   -379    451       C  
ATOM   1173  O   GLY B 141     -22.976  42.384  -2.524  1.00 19.53           O  
ANISOU 1173  O   GLY B 141     1699   2961   2759    169   -316    398       O  
ATOM   1174  N   GLU B 142     -22.055  41.989  -4.540  1.00 18.71           N  
ANISOU 1174  N   GLU B 142     1648   3000   2461   -133   -466    418       N  
ATOM   1175  CA  GLU B 142     -22.417  40.577  -4.504  1.00 17.85           C  
ANISOU 1175  CA  GLU B 142     1575   3021   2187   -388   -469    288       C  
ATOM   1176  C   GLU B 142     -21.625  39.844  -3.437  1.00 19.61           C  
ANISOU 1176  C   GLU B 142     1980   2988   2483   -353   -347     66       C  
ATOM   1177  O   GLU B 142     -22.149  38.945  -2.769  1.00 16.56           O  
ANISOU 1177  O   GLU B 142     1599   2636   2055   -430   -298    -19       O  
ATOM   1178  CB  GLU B 142     -22.152  39.930  -5.854  1.00 19.62           C  
ANISOU 1178  CB  GLU B 142     1924   3363   2169   -700   -502    263       C  
ATOM   1179  CG  GLU B 142     -23.019  40.415  -6.958  1.00 21.87           C  
ANISOU 1179  CG  GLU B 142     2011   4010   2289   -846   -672    519       C  
ATOM   1180  CD  GLU B 142     -23.130  39.360  -8.023  1.00 30.38           C  
ANISOU 1180  CD  GLU B 142     3285   5256   3001  -1322   -701    430       C  
ATOM   1181  OE1 GLU B 142     -22.388  39.451  -9.022  1.00 25.06           O  
ANISOU 1181  OE1 GLU B 142     2812   4514   2195  -1429   -663    400       O  
ATOM   1182  OE2 GLU B 142     -23.933  38.415  -7.829  1.00 30.88           O  
ANISOU 1182  OE2 GLU B 142     3384   5430   2917  -1562   -679    373       O  
ATOM   1183  N   PHE B 143     -20.347  40.194  -3.292  1.00 17.65           N  
ANISOU 1183  N   PHE B 143     1852   2519   2336   -257   -303     20       N  
ATOM   1184  CA  PHE B 143     -19.545  39.605  -2.230  1.00 13.78           C  
ANISOU 1184  CA  PHE B 143     1454   1865   1916   -215   -219    -80       C  
ATOM   1185  C   PHE B 143     -20.108  39.970  -0.864  1.00 14.82           C  
ANISOU 1185  C   PHE B 143     1554   1964   2112   -102   -233   -115       C  
ATOM   1186  O   PHE B 143     -20.169  39.126   0.038  1.00 15.30           O  
ANISOU 1186  O   PHE B 143     1649   2006   2157   -118   -175   -187       O  
ATOM   1187  CB  PHE B 143     -18.097  40.078  -2.365  1.00 13.68           C  
ANISOU 1187  CB  PHE B 143     1484   1720   1993   -171   -214    -21       C  
ATOM   1188  CG  PHE B 143     -17.241  39.767  -1.173  1.00 13.31           C  
ANISOU 1188  CG  PHE B 143     1442   1599   2016   -140   -195    -10       C  
ATOM   1189  CD1 PHE B 143     -16.902  38.465  -0.859  1.00 14.50           C  
ANISOU 1189  CD1 PHE B 143     1613   1737   2160   -137    -52      2       C  
ATOM   1190  CD2 PHE B 143     -16.748  40.796  -0.388  1.00 18.58           C  
ANISOU 1190  CD2 PHE B 143     2117   2215   2727   -146   -307     19       C  
ATOM   1191  CE1 PHE B 143     -16.068  38.196   0.236  1.00 18.84           C  
ANISOU 1191  CE1 PHE B 143     2099   2291   2767   -101    -57    111       C  
ATOM   1192  CE2 PHE B 143     -15.933  40.536   0.703  1.00 20.63           C  
ANISOU 1192  CE2 PHE B 143     2356   2494   2987   -205   -348     80       C  
ATOM   1193  CZ  PHE B 143     -15.602  39.241   1.019  1.00 17.90           C  
ANISOU 1193  CZ  PHE B 143     1941   2205   2654   -163   -243    157       C  
ATOM   1194  N   TYR B 144     -20.516  41.229  -0.689  1.00 15.56           N  
ANISOU 1194  N   TYR B 144     1627   2015   2270     26   -258    -52       N  
ATOM   1195  CA  TYR B 144     -21.123  41.635   0.572  1.00 17.29           C  
ANISOU 1195  CA  TYR B 144     1900   2148   2521    141   -183    -94       C  
ATOM   1196  C   TYR B 144     -22.398  40.847   0.836  1.00 17.57           C  
ANISOU 1196  C   TYR B 144     1792   2360   2523    155   -134    -73       C  
ATOM   1197  O   TYR B 144     -22.704  40.511   1.986  1.00 18.79           O  
ANISOU 1197  O   TYR B 144     2006   2465   2668    191    -54   -150       O  
ATOM   1198  CB  TYR B 144     -21.430  43.129   0.558  1.00 18.96           C  
ANISOU 1198  CB  TYR B 144     2183   2211   2810    308   -101     -5       C  
ATOM   1199  CG  TYR B 144     -20.220  44.049   0.559  1.00 18.98           C  
ANISOU 1199  CG  TYR B 144     2392   1995   2825    233   -129    -47       C  
ATOM   1200  CD1 TYR B 144     -19.024  43.684   1.173  1.00 18.89           C  
ANISOU 1200  CD1 TYR B 144     2484   1944   2751     36   -226   -145       C  
ATOM   1201  CD2 TYR B 144     -20.300  45.312  -0.019  1.00 21.17           C  
ANISOU 1201  CD2 TYR B 144     2741   2127   3175    346    -49     65       C  
ATOM   1202  CE1 TYR B 144     -17.927  44.561   1.193  1.00 20.94           C  
ANISOU 1202  CE1 TYR B 144     2895   2063   2997   -113   -284   -140       C  
ATOM   1203  CE2 TYR B 144     -19.221  46.176  -0.004  1.00 26.44           C  
ANISOU 1203  CE2 TYR B 144     3627   2582   3838    216    -66     23       C  
ATOM   1204  CZ  TYR B 144     -18.038  45.793   0.595  1.00 24.65           C  
ANISOU 1204  CZ  TYR B 144     3481   2358   3525    -45   -203    -84       C  
ATOM   1205  OH  TYR B 144     -16.969  46.679   0.604  1.00 25.38           O  
ANISOU 1205  OH  TYR B 144     3755   2298   3590   -253   -252    -85       O  
ATOM   1206  N   GLU B 145     -23.158  40.547  -0.219  1.00 15.98           N  
ANISOU 1206  N   GLU B 145     1400   2398   2275     79   -192     53       N  
ATOM   1207  CA  GLU B 145     -24.352  39.721  -0.059  1.00 17.22           C  
ANISOU 1207  CA  GLU B 145     1385   2789   2369    -10   -182    108       C  
ATOM   1208  C   GLU B 145     -23.997  38.327   0.457  1.00 17.19           C  
ANISOU 1208  C   GLU B 145     1524   2726   2282   -191   -142    -85       C  
ATOM   1209  O   GLU B 145     -24.669  37.794   1.351  1.00 16.89           O  
ANISOU 1209  O   GLU B 145     1450   2725   2244   -183    -68   -110       O  
ATOM   1210  CB  GLU B 145     -25.091  39.640  -1.396  1.00 25.67           C  
ANISOU 1210  CB  GLU B 145     2233   4192   3328   -189   -313    308       C  
ATOM   1211  CG  GLU B 145     -26.556  39.322  -1.311  1.00 43.99           C  
ANISOU 1211  CG  GLU B 145     4246   6860   5608   -262   -339    523       C  
ATOM   1212  CD  GLU B 145     -27.161  39.109  -2.689  1.00 55.01           C  
ANISOU 1212  CD  GLU B 145     5478   8623   6799   -571   -520    724       C  
ATOM   1213  OE1 GLU B 145     -26.538  39.539  -3.690  1.00 46.92           O  
ANISOU 1213  OE1 GLU B 145     4537   7580   5708   -622   -598    742       O  
ATOM   1214  OE2 GLU B 145     -28.250  38.503  -2.767  1.00 59.77           O  
ANISOU 1214  OE2 GLU B 145     5979   9455   7276   -761   -549    844       O  
ATOM   1215  N   ALA B 146     -22.952  37.712  -0.103  1.00 14.41           N  
ANISOU 1215  N   ALA B 146     1340   2264   1869   -325   -136   -188       N  
ATOM   1216  CA  ALA B 146     -22.562  36.382   0.362  1.00 15.47           C  
ANISOU 1216  CA  ALA B 146     1634   2289   1955   -433    -10   -312       C  
ATOM   1217  C   ALA B 146     -22.079  36.436   1.805  1.00 15.13           C  
ANISOU 1217  C   ALA B 146     1634   2106   2007   -255     39   -343       C  
ATOM   1218  O   ALA B 146     -22.384  35.547   2.608  1.00 14.84           O  
ANISOU 1218  O   ALA B 146     1638   2053   1948   -281    135   -387       O  
ATOM   1219  CB  ALA B 146     -21.480  35.804  -0.562  1.00 14.49           C  
ANISOU 1219  CB  ALA B 146     1696   2029   1779   -532     87   -350       C  
ATOM   1220  N   LEU B 147     -21.341  37.487   2.160  1.00 14.08           N  
ANISOU 1220  N   LEU B 147     1517   1886   1948   -122    -31   -313       N  
ATOM   1221  CA  LEU B 147     -20.861  37.633   3.532  1.00 12.34           C  
ANISOU 1221  CA  LEU B 147     1373   1582   1733    -57    -27   -333       C  
ATOM   1222  C   LEU B 147     -22.017  37.704   4.521  1.00 17.06           C  
ANISOU 1222  C   LEU B 147     1973   2206   2303      6     42   -379       C  
ATOM   1223  O   LEU B 147     -21.920  37.182   5.639  1.00 15.98           O  
ANISOU 1223  O   LEU B 147     1909   2047   2116      2     90   -409       O  
ATOM   1224  CB  LEU B 147     -20.014  38.894   3.652  1.00 13.81           C  
ANISOU 1224  CB  LEU B 147     1629   1683   1938    -44   -126   -307       C  
ATOM   1225  CG  LEU B 147     -18.515  38.829   3.416  1.00 30.67           C  
ANISOU 1225  CG  LEU B 147     3747   3811   4094   -115   -201   -204       C  
ATOM   1226  CD1 LEU B 147     -17.964  40.178   3.826  1.00 34.32           C  
ANISOU 1226  CD1 LEU B 147     4320   4201   4520   -197   -312   -206       C  
ATOM   1227  CD2 LEU B 147     -17.866  37.706   4.212  1.00 22.98           C  
ANISOU 1227  CD2 LEU B 147     2734   2895   3103   -130   -160   -105       C  
ATOM   1228  N   ASP B 148     -23.113  38.363   4.133  1.00 17.74           N  
ANISOU 1228  N   ASP B 148     1956   2360   2425     87     71   -332       N  
ATOM   1229  CA  ASP B 148     -24.301  38.436   4.986  1.00 15.55           C  
ANISOU 1229  CA  ASP B 148     1632   2122   2154    198    203   -309       C  
ATOM   1230  C   ASP B 148     -24.817  37.042   5.319  1.00 18.57           C  
ANISOU 1230  C   ASP B 148     1946   2622   2487     76    245   -333       C  
ATOM   1231  O   ASP B 148     -25.377  36.828   6.409  1.00 17.47           O  
ANISOU 1231  O   ASP B 148     1839   2470   2330    142    364   -350       O  
ATOM   1232  CB  ASP B 148     -25.365  39.285   4.270  1.00 18.61           C  
ANISOU 1232  CB  ASP B 148     1814   2630   2628    339    248   -124       C  
ATOM   1233  CG  ASP B 148     -26.641  39.477   5.081  1.00 26.60           C  
ANISOU 1233  CG  ASP B 148     2719   3696   3692    526    454     -5       C  
ATOM   1234  OD1 ASP B 148     -26.647  40.270   6.047  1.00 27.77           O  
ANISOU 1234  OD1 ASP B 148     3093   3607   3852    712    655    -53       O  
ATOM   1235  OD2 ASP B 148     -27.659  38.851   4.722  1.00 31.40           O  
ANISOU 1235  OD2 ASP B 148     3031   4590   4311    458    435    156       O  
ATOM   1236  N   CYS B 149     -24.615  36.077   4.402  1.00 14.59           N  
ANISOU 1236  N   CYS B 149     1407   2194   1942   -120    191   -346       N  
ATOM   1237  CA  CYS B 149     -25.050  34.699   4.639  1.00 16.90           C  
ANISOU 1237  CA  CYS B 149     1721   2531   2170   -289    280   -387       C  
ATOM   1238  C   CYS B 149     -24.283  34.074   5.801  1.00 19.03           C  
ANISOU 1238  C   CYS B 149     2159   2636   2436   -217    376   -442       C  
ATOM   1239  O   CYS B 149     -24.836  33.276   6.558  1.00 17.03           O  
ANISOU 1239  O   CYS B 149     1922   2394   2154   -252    487   -452       O  
ATOM   1240  CB  CYS B 149     -24.849  33.836   3.379  1.00 19.32           C  
ANISOU 1240  CB  CYS B 149     2102   2855   2382   -558    280   -424       C  
ATOM   1241  SG  CYS B 149     -25.578  32.176   3.518  1.00 24.49           S  
ANISOU 1241  SG  CYS B 149     2874   3518   2914   -867    445   -492       S  
ATOM   1242  N   LEU B 150     -23.000  34.406   5.927  1.00 13.42           N  
ANISOU 1242  N   LEU B 150     1541   1811   1748   -138    325   -428       N  
ATOM   1243  CA  LEU B 150     -22.159  33.946   7.022  1.00 13.95           C  
ANISOU 1243  CA  LEU B 150     1694   1813   1792    -82    362   -377       C  
ATOM   1244  C   LEU B 150     -22.236  34.862   8.237  1.00 17.37           C  
ANISOU 1244  C   LEU B 150     2191   2259   2151    -25    298   -400       C  
ATOM   1245  O   LEU B 150     -21.561  34.600   9.244  1.00 14.80           O  
ANISOU 1245  O   LEU B 150     1933   1947   1743    -41    276   -331       O  
ATOM   1246  CB  LEU B 150     -20.703  33.826   6.541  1.00 13.21           C  
ANISOU 1246  CB  LEU B 150     1606   1667   1748    -62    334   -258       C  
ATOM   1247  CG  LEU B 150     -20.461  32.824   5.395  1.00 14.08           C  
ANISOU 1247  CG  LEU B 150     1771   1675   1903   -104    514   -239       C  
ATOM   1248  CD1 LEU B 150     -18.962  32.656   5.157  1.00 15.85           C  
ANISOU 1248  CD1 LEU B 150     1968   1844   2211      4    572    -32       C  
ATOM   1249  CD2 LEU B 150     -21.083  31.455   5.692  1.00 14.85           C  
ANISOU 1249  CD2 LEU B 150     1986   1688   1970   -163    748   -269       C  
ATOM   1250  N   ARG B 151     -23.017  35.939   8.150  1.00 15.12           N  
ANISOU 1250  N   ARG B 151     1706   2382   1658    118     50   -328       N  
ATOM   1251  CA  ARG B 151     -23.286  36.832   9.284  1.00 15.55           C  
ANISOU 1251  CA  ARG B 151     1750   2413   1743    278    -15   -361       C  
ATOM   1252  C   ARG B 151     -22.011  37.502   9.798  1.00 17.60           C  
ANISOU 1252  C   ARG B 151     2040   2543   2103    330    -93   -437       C  
ATOM   1253  O   ARG B 151     -21.860  37.759  10.995  1.00 16.71           O  
ANISOU 1253  O   ARG B 151     1969   2450   1930    353   -124   -527       O  
ATOM   1254  CB  ARG B 151     -24.022  36.073  10.393  1.00 17.46           C  
ANISOU 1254  CB  ARG B 151     2055   2729   1850    296     24   -391       C  
ATOM   1255  CG  ARG B 151     -25.242  35.300   9.816  1.00 19.05           C  
ANISOU 1255  CG  ARG B 151     2218   3109   1911    151    115   -334       C  
ATOM   1256  CD  ARG B 151     -26.101  34.705  10.920  1.00 20.01           C  
ANISOU 1256  CD  ARG B 151     2389   3302   1912    177    165   -355       C  
ATOM   1257  NE  ARG B 151     -25.426  33.651  11.667  1.00 17.58           N  
ANISOU 1257  NE  ARG B 151     2215   2870   1594    197    231   -380       N  
ATOM   1258  CZ  ARG B 151     -25.513  32.354  11.386  1.00 25.07           C  
ANISOU 1258  CZ  ARG B 151     3269   3756   2501     58    424   -375       C  
ATOM   1259  NH1 ARG B 151     -26.222  31.937  10.335  1.00 21.13           N  
ANISOU 1259  NH1 ARG B 151     2773   3356   1900   -216    540   -427       N  
ATOM   1260  NH2 ARG B 151     -24.874  31.471  12.147  1.00 17.70           N  
ANISOU 1260  NH2 ARG B 151     2428   2684   1613    166    547   -297       N  
ATOM   1261  N   ILE B 152     -21.119  37.825   8.869  1.00 15.53           N  
ANISOU 1261  N   ILE B 152     1740   2206   1955    296   -120   -408       N  
ATOM   1262  CA  ILE B 152     -19.864  38.518   9.149  1.00 13.69           C  
ANISOU 1262  CA  ILE B 152     1497   1904   1800    280   -194   -469       C  
ATOM   1263  C   ILE B 152     -20.048  39.998   8.776  1.00 17.04           C  
ANISOU 1263  C   ILE B 152     1921   2189   2364    290   -136   -519       C  
ATOM   1264  O   ILE B 152     -20.520  40.274   7.667  1.00 17.09           O  
ANISOU 1264  O   ILE B 152     1858   2177   2457    333    -82   -386       O  
ATOM   1265  CB  ILE B 152     -18.697  37.911   8.344  1.00 13.95           C  
ANISOU 1265  CB  ILE B 152     1484   1916   1901    254   -210   -375       C  
ATOM   1266  CG1 ILE B 152     -18.424  36.463   8.770  1.00 13.81           C  
ANISOU 1266  CG1 ILE B 152     1481   1948   1818    303   -137   -264       C  
ATOM   1267  CG2 ILE B 152     -17.421  38.775   8.466  1.00 16.16           C  
ANISOU 1267  CG2 ILE B 152     1701   2191   2249    198   -301   -412       C  
ATOM   1268  CD1 ILE B 152     -17.561  35.672   7.753  1.00 14.50           C  
ANISOU 1268  CD1 ILE B 152     1568   1923   2019    307      4   -146       C  
ATOM   1269  N   PRO B 153     -19.680  40.931   9.640  1.00 19.18           N  
ANISOU 1269  N   PRO B 153     2263   2377   2647    222    -98   -688       N  
ATOM   1270  CA  PRO B 153     -19.867  42.348   9.303  1.00 18.19           C  
ANISOU 1270  CA  PRO B 153     2192   2005   2716    243     94   -734       C  
ATOM   1271  C   PRO B 153     -18.883  42.817   8.246  1.00 24.22           C  
ANISOU 1271  C   PRO B 153     2899   2675   3630    197     68   -675       C  
ATOM   1272  O   PRO B 153     -17.741  42.357   8.181  1.00 18.33           O  
ANISOU 1272  O   PRO B 153     2103   2043   2820     80    -93   -701       O  
ATOM   1273  CB  PRO B 153     -19.616  43.062  10.637  1.00 22.31           C  
ANISOU 1273  CB  PRO B 153     2869   2457   3153     63    205  -1027       C  
ATOM   1274  CG  PRO B 153     -18.672  42.173  11.359  1.00 21.66           C  
ANISOU 1274  CG  PRO B 153     2716   2693   2819   -106    -43  -1080       C  
ATOM   1275  CD  PRO B 153     -19.090  40.757  10.979  1.00 19.92           C  
ANISOU 1275  CD  PRO B 153     2391   2626   2551     80   -175   -841       C  
ATOM   1276  N   ARG B 154     -19.330  43.785   7.433  1.00 21.94           N  
ANISOU 1276  N   ARG B 154     2591   2188   3556    317    261   -542       N  
ATOM   1277  CA  ARG B 154     -18.447  44.349   6.413  1.00 21.67           C  
ANISOU 1277  CA  ARG B 154     2507   2047   3681    281    269   -469       C  
ATOM   1278  C   ARG B 154     -17.207  44.986   7.031  1.00 22.31           C  
ANISOU 1278  C   ARG B 154     2703   2005   3770     33    286   -746       C  
ATOM   1279  O   ARG B 154     -16.156  45.052   6.383  1.00 23.18           O  
ANISOU 1279  O   ARG B 154     2747   2135   3926    -63    189   -724       O  
ATOM   1280  CB  ARG B 154     -19.196  45.379   5.561  1.00 26.53           C  
ANISOU 1280  CB  ARG B 154     3058   2482   4539    487    534   -205       C  
ATOM   1281  CG  ARG B 154     -20.326  44.793   4.713  1.00 29.32           C  
ANISOU 1281  CG  ARG B 154     3191   3138   4811    655    476    149       C  
ATOM   1282  CD  ARG B 154     -20.988  45.875   3.865  1.00 36.58           C  
ANISOU 1282  CD  ARG B 154     3950   3988   5962    895    746    545       C  
ATOM   1283  NE  ARG B 154     -22.246  45.422   3.278  1.00 45.39           N  
ANISOU 1283  NE  ARG B 154     4819   5535   6894    983    690    909       N  
ATOM   1284  CZ  ARG B 154     -22.889  46.060   2.302  1.00 52.47           C  
ANISOU 1284  CZ  ARG B 154     5553   6612   7771   1054    795   1323       C  
ATOM   1285  NH1 ARG B 154     -22.390  47.182   1.798  1.00 50.76           N  
ANISOU 1285  NH1 ARG B 154     5371   6140   7775   1120   1001   1457       N  
ATOM   1286  NH2 ARG B 154     -24.033  45.577   1.829  1.00 48.78           N  
ANISOU 1286  NH2 ARG B 154     4887   6603   7045   1031    716   1621       N  
ATOM   1287  N   SER B 155     -17.303  45.467   8.270  1.00 22.20           N  
ANISOU 1287  N   SER B 155     2850   1908   3677   -127    424  -1019       N  
ATOM   1288  CA  SER B 155     -16.132  46.046   8.914  1.00 24.52           C  
ANISOU 1288  CA  SER B 155     3229   2212   3875   -496    437  -1318       C  
ATOM   1289  C   SER B 155     -15.012  45.031   9.135  1.00 23.77           C  
ANISOU 1289  C   SER B 155     2943   2558   3529   -646     67  -1277       C  
ATOM   1290  O   SER B 155     -13.897  45.438   9.464  1.00 27.73           O  
ANISOU 1290  O   SER B 155     3412   3207   3916   -972     17  -1433       O  
ATOM   1291  CB  SER B 155     -16.530  46.685  10.247  1.00 34.59           C  
ANISOU 1291  CB  SER B 155     4730   3381   5032   -730    693  -1663       C  
ATOM   1292  OG  SER B 155     -17.161  45.733  11.078  1.00 29.81           O  
ANISOU 1292  OG  SER B 155     4080   3054   4192   -659    527  -1642       O  
ATOM   1293  N   ASP B 156     -15.270  43.736   8.963  1.00 20.74           N  
ANISOU 1293  N   ASP B 156     2423   2396   3063   -429   -140  -1045       N  
ATOM   1294  CA  ASP B 156     -14.224  42.730   9.086  1.00 24.09           C  
ANISOU 1294  CA  ASP B 156     2648   3173   3332   -470   -379   -894       C  
ATOM   1295  C   ASP B 156     -13.488  42.479   7.779  1.00 21.51           C  
ANISOU 1295  C   ASP B 156     2208   2786   3178   -363   -425   -694       C  
ATOM   1296  O   ASP B 156     -12.490  41.749   7.775  1.00 20.25           O  
ANISOU 1296  O   ASP B 156     1870   2872   2951   -363   -547   -522       O  
ATOM   1297  CB  ASP B 156     -14.809  41.410   9.595  1.00 23.69           C  
ANISOU 1297  CB  ASP B 156     2548   3307   3147   -288   -460   -737       C  
ATOM   1298  CG  ASP B 156     -15.030  41.411  11.087  1.00 35.02           C  
ANISOU 1298  CG  ASP B 156     4002   4988   4315   -449   -494   -878       C  
ATOM   1299  OD1 ASP B 156     -14.582  42.368  11.761  1.00 35.09           O  
ANISOU 1299  OD1 ASP B 156     4055   5088   4191   -773   -464  -1126       O  
ATOM   1300  OD2 ASP B 156     -15.647  40.445  11.584  1.00 33.65           O  
ANISOU 1300  OD2 ASP B 156     3813   4929   4045   -297   -522   -758       O  
ATOM   1301  N   VAL B 157     -13.945  43.075   6.679  1.00 20.92           N  
ANISOU 1301  N   VAL B 157     2207   2423   3320   -260   -299   -666       N  
ATOM   1302  CA  VAL B 157     -13.357  42.784   5.377  1.00 19.28           C  
ANISOU 1302  CA  VAL B 157     1903   2182   3240   -180   -325   -485       C  
ATOM   1303  C   VAL B 157     -11.986  43.430   5.263  1.00 21.85           C  
ANISOU 1303  C   VAL B 157     2144   2550   3608   -370   -369   -528       C  
ATOM   1304  O   VAL B 157     -11.769  44.568   5.702  1.00 20.41           O  
ANISOU 1304  O   VAL B 157     2042   2268   3445   -583   -284   -730       O  
ATOM   1305  CB  VAL B 157     -14.290  43.263   4.254  1.00 18.28           C  
ANISOU 1305  CB  VAL B 157     1818   1860   3267    -47   -194   -385       C  
ATOM   1306  CG1 VAL B 157     -13.666  42.960   2.882  1.00 15.11           C  
ANISOU 1306  CG1 VAL B 157     1323   1478   2942    -27   -213   -225       C  
ATOM   1307  CG2 VAL B 157     -15.631  42.585   4.397  1.00 17.92           C  
ANISOU 1307  CG2 VAL B 157     1799   1887   3122     80   -170   -323       C  
ATOM   1308  N   MET B 158     -11.048  42.693   4.680  1.00 17.75           N  
ANISOU 1308  N   MET B 158     1474   2167   3104   -319   -447   -344       N  
ATOM   1309  CA  MET B 158      -9.725  43.196   4.347  1.00 19.17           C  
ANISOU 1309  CA  MET B 158     1522   2427   3334   -472   -492   -314       C  
ATOM   1310  C   MET B 158      -9.630  43.318   2.832  1.00 23.27           C  
ANISOU 1310  C   MET B 158     2054   2735   4054   -360   -405   -200       C  
ATOM   1311  O   MET B 158     -10.101  42.438   2.117  1.00 20.77           O  
ANISOU 1311  O   MET B 158     1760   2378   3755   -192   -350    -77       O  
ATOM   1312  CB  MET B 158      -8.659  42.247   4.882  1.00 22.73           C  
ANISOU 1312  CB  MET B 158     1728   3256   3653   -462   -610   -100       C  
ATOM   1313  CG  MET B 158      -8.665  42.111   6.406  1.00 31.09           C  
ANISOU 1313  CG  MET B 158     2701   4671   4442   -612   -725   -147       C  
ATOM   1314  SD  MET B 158      -7.977  40.546   6.983  1.00 33.04           S  
ANISOU 1314  SD  MET B 158     2639   5342   4573   -381   -777    304       S  
ATOM   1315  CE  MET B 158      -9.401  39.476   6.749  1.00 30.11           C  
ANISOU 1315  CE  MET B 158     2523   4611   4308    -61   -604    309       C  
ATOM   1316  N   TYR B 159      -9.039  44.410   2.339  1.00 18.99           N  
ANISOU 1316  N   TYR B 159     1507   2074   3635   -502   -360   -257       N  
ATOM   1317  CA  TYR B 159      -8.995  44.681   0.905  1.00 20.61           C  
ANISOU 1317  CA  TYR B 159     1711   2108   4011   -411   -273   -130       C  
ATOM   1318  C   TYR B 159      -7.560  44.799   0.409  1.00 20.77           C  
ANISOU 1318  C   TYR B 159     1579   2219   4092   -516   -313    -50       C  
ATOM   1319  O   TYR B 159      -6.690  45.311   1.114  1.00 24.99           O  
ANISOU 1319  O   TYR B 159     2031   2892   4573   -743   -375   -143       O  
ATOM   1320  CB  TYR B 159      -9.707  45.993   0.558  1.00 24.17           C  
ANISOU 1320  CB  TYR B 159     2286   2274   4624   -416   -102   -178       C  
ATOM   1321  CG  TYR B 159     -11.124  46.074   1.036  1.00 24.54           C  
ANISOU 1321  CG  TYR B 159     2445   2232   4648   -289    -12   -201       C  
ATOM   1322  CD1 TYR B 159     -11.416  46.513   2.314  1.00 23.31           C  
ANISOU 1322  CD1 TYR B 159     2413   2003   4441   -401     52   -425       C  
ATOM   1323  CD2 TYR B 159     -12.181  45.733   0.198  1.00 19.44           C  
ANISOU 1323  CD2 TYR B 159     1760   1630   3996    -96     26     10       C  
ATOM   1324  CE1 TYR B 159     -12.733  46.603   2.755  1.00 23.91           C  
ANISOU 1324  CE1 TYR B 159     2585   1981   4517   -255    174   -423       C  
ATOM   1325  CE2 TYR B 159     -13.494  45.828   0.632  1.00 18.44           C  
ANISOU 1325  CE2 TYR B 159     1680   1483   3844     31    112     49       C  
ATOM   1326  CZ  TYR B 159     -13.761  46.250   1.902  1.00 25.02           C  
ANISOU 1326  CZ  TYR B 159     2648   2176   4682    -14    194   -159       C  
ATOM   1327  OH  TYR B 159     -15.064  46.336   2.314  1.00 23.00           O  
ANISOU 1327  OH  TYR B 159     2429   1890   4420    140    313    -95       O  
ATOM   1328  N   THR B 160      -7.329  44.357  -0.828  1.00 21.06           N  
ANISOU 1328  N   THR B 160     1572   2220   4209   -400   -258    113       N  
ATOM   1329  CA  THR B 160      -6.075  44.670  -1.500  1.00 19.05           C  
ANISOU 1329  CA  THR B 160     1237   2008   3993   -456   -244    197       C  
ATOM   1330  C   THR B 160      -6.130  46.076  -2.078  1.00 25.65           C  
ANISOU 1330  C   THR B 160     2149   2637   4959   -549   -157    142       C  
ATOM   1331  O   THR B 160      -7.206  46.652  -2.283  1.00 23.79           O  
ANISOU 1331  O   THR B 160     2003   2208   4830   -494    -60    137       O  
ATOM   1332  CB  THR B 160      -5.781  43.700  -2.640  1.00 20.55           C  
ANISOU 1332  CB  THR B 160     1416   2205   4186   -314   -149    358       C  
ATOM   1333  OG1 THR B 160      -6.915  43.659  -3.518  1.00 21.14           O  
ANISOU 1333  OG1 THR B 160     1600   2183   4250   -271    -68    359       O  
ATOM   1334  CG2 THR B 160      -5.515  42.322  -2.099  1.00 21.74           C  
ANISOU 1334  CG2 THR B 160     1489   2478   4294   -198   -110    463       C  
ATOM   1335  N   ASP B 161      -4.947  46.608  -2.375  1.00 23.36           N  
ANISOU 1335  N   ASP B 161     1798   2398   4681   -670   -154    156       N  
ATOM   1336  CA  ASP B 161      -4.783  47.919  -3.003  1.00 24.09           C  
ANISOU 1336  CA  ASP B 161     1963   2280   4910   -754    -22    133       C  
ATOM   1337  C   ASP B 161      -3.864  47.709  -4.199  1.00 22.69           C  
ANISOU 1337  C   ASP B 161     1699   2179   4743   -688    -22    296       C  
ATOM   1338  O   ASP B 161      -2.651  47.544  -4.028  1.00 25.07           O  
ANISOU 1338  O   ASP B 161     1883   2668   4973   -801    -86    307       O  
ATOM   1339  CB  ASP B 161      -4.209  48.929  -2.017  1.00 28.28           C  
ANISOU 1339  CB  ASP B 161     2550   2796   5397  -1080     20    -89       C  
ATOM   1340  CG  ASP B 161      -3.948  50.295  -2.643  1.00 37.90           C  
ANISOU 1340  CG  ASP B 161     3888   3746   6767  -1173    230   -115       C  
ATOM   1341  OD1 ASP B 161      -4.201  50.497  -3.854  1.00 35.61           O  
ANISOU 1341  OD1 ASP B 161     3585   3315   6631   -953    322     81       O  
ATOM   1342  OD2 ASP B 161      -3.492  51.180  -1.898  1.00 40.27           O  
ANISOU 1342  OD2 ASP B 161     4296   3999   7006  -1488    315   -321       O  
ATOM   1343  N   TRP B 162      -4.438  47.719  -5.406  1.00 23.06           N  
ANISOU 1343  N   TRP B 162     1775   2135   4852   -529     56    442       N  
ATOM   1344  CA  TRP B 162      -3.647  47.369  -6.580  1.00 26.59           C  
ANISOU 1344  CA  TRP B 162     2169   2667   5266   -482     73    568       C  
ATOM   1345  C   TRP B 162      -2.491  48.334  -6.792  1.00 25.28           C  
ANISOU 1345  C   TRP B 162     1957   2466   5181   -616    103    558       C  
ATOM   1346  O   TRP B 162      -1.462  47.950  -7.357  1.00 26.78           O  
ANISOU 1346  O   TRP B 162     2069   2770   5338   -617     91    631       O  
ATOM   1347  CB  TRP B 162      -4.521  47.318  -7.832  1.00 24.78           C  
ANISOU 1347  CB  TRP B 162     1961   2445   5008   -382    146    716       C  
ATOM   1348  CG  TRP B 162      -3.751  46.865  -9.012  1.00 27.10           C  
ANISOU 1348  CG  TRP B 162     2231   2843   5222   -387    186    790       C  
ATOM   1349  CD1 TRP B 162      -3.515  47.570 -10.155  1.00 31.24           C  
ANISOU 1349  CD1 TRP B 162     2719   3372   5777   -395    246    919       C  
ATOM   1350  CD2 TRP B 162      -3.079  45.608  -9.166  1.00 29.89           C  
ANISOU 1350  CD2 TRP B 162     2585   3283   5488   -383    224    757       C  
ATOM   1351  NE1 TRP B 162      -2.744  46.823 -11.017  1.00 32.63           N  
ANISOU 1351  NE1 TRP B 162     2892   3656   5850   -428    295    921       N  
ATOM   1352  CE2 TRP B 162      -2.463  45.617 -10.431  1.00 32.56           C  
ANISOU 1352  CE2 TRP B 162     2908   3669   5794   -413    313    826       C  
ATOM   1353  CE3 TRP B 162      -2.947  44.470  -8.359  1.00 25.20           C  
ANISOU 1353  CE3 TRP B 162     1987   2708   4880   -339    241    711       C  
ATOM   1354  CZ2 TRP B 162      -1.728  44.532 -10.912  1.00 27.75           C  
ANISOU 1354  CZ2 TRP B 162     2300   3089   5153   -411    452    821       C  
ATOM   1355  CZ3 TRP B 162      -2.209  43.400  -8.836  1.00 24.46           C  
ANISOU 1355  CZ3 TRP B 162     1876   2622   4797   -299    404    761       C  
ATOM   1356  CH2 TRP B 162      -1.608  43.440 -10.099  1.00 25.61           C  
ANISOU 1356  CH2 TRP B 162     2030   2779   4923   -337    523    799       C  
ATOM   1357  N   LYS B 163      -2.618  49.575  -6.319  1.00 28.22           N  
ANISOU 1357  N   LYS B 163     2394   2663   5664   -752    189    457       N  
ATOM   1358  CA  LYS B 163      -1.512  50.520  -6.463  1.00 31.25           C  
ANISOU 1358  CA  LYS B 163     2767   3015   6093   -957    253    408       C  
ATOM   1359  C   LYS B 163      -0.271  50.066  -5.707  1.00 34.97           C  
ANISOU 1359  C   LYS B 163     3098   3792   6397  -1181    115    328       C  
ATOM   1360  O   LYS B 163       0.821  50.573  -5.971  1.00 38.60           O  
ANISOU 1360  O   LYS B 163     3484   4342   6842  -1366    134    327       O  
ATOM   1361  CB  LYS B 163      -1.946  51.909  -5.994  1.00 32.46           C  
ANISOU 1361  CB  LYS B 163     3090   2866   6379  -1099    462    275       C  
ATOM   1362  CG  LYS B 163      -3.008  52.526  -6.890  1.00 39.51           C  
ANISOU 1362  CG  LYS B 163     4027   3505   7478   -826    668    474       C  
ATOM   1363  CD  LYS B 163      -3.523  53.849  -6.354  1.00 50.43           C  
ANISOU 1363  CD  LYS B 163     5600   4536   9025   -877    985    371       C  
ATOM   1364  CE  LYS B 163      -4.557  54.442  -7.297  1.00 56.17           C  
ANISOU 1364  CE  LYS B 163     6277   5099   9967   -537   1227    693       C  
ATOM   1365  NZ  LYS B 163      -5.676  55.079  -6.549  1.00 65.81           N  
ANISOU 1365  NZ  LYS B 163     7628   6070  11305   -423   1515    662       N  
ATOM   1366  N   LYS B 164      -0.408  49.108  -4.792  1.00 30.82           N  
ANISOU 1366  N   LYS B 164     2492   3479   5739  -1161    -13    301       N  
ATOM   1367  CA  LYS B 164       0.717  48.613  -4.012  1.00 29.85           C  
ANISOU 1367  CA  LYS B 164     2139   3754   5448  -1324   -130    304       C  
ATOM   1368  C   LYS B 164       1.361  47.364  -4.600  1.00 36.09           C  
ANISOU 1368  C   LYS B 164     2773   4694   6245  -1039   -161    566       C  
ATOM   1369  O   LYS B 164       2.363  46.890  -4.053  1.00 33.37           O  
ANISOU 1369  O   LYS B 164     2196   4679   5803  -1070   -229    677       O  
ATOM   1370  CB  LYS B 164       0.278  48.331  -2.572  1.00 30.51           C  
ANISOU 1370  CB  LYS B 164     2185   4028   5378  -1459   -220    161       C  
ATOM   1371  CG  LYS B 164      -0.074  49.586  -1.803  1.00 49.91           C  
ANISOU 1371  CG  LYS B 164     4826   6378   7758  -1872   -160    -93       C  
ATOM   1372  CD  LYS B 164      -0.851  49.266  -0.544  1.00 49.97           C  
ANISOU 1372  CD  LYS B 164     4888   6457   7643  -1926   -276   -160       C  
ATOM   1373  CE  LYS B 164      -0.436  50.171   0.605  1.00 65.24           C  
ANISOU 1373  CE  LYS B 164     6817   8351   9620  -2238   -308   -398       C  
ATOM   1374  NZ  LYS B 164      -1.332  49.954   1.778  1.00 67.78           N  
ANISOU 1374  NZ  LYS B 164     7271   8732   9750  -2282   -312   -586       N  
ATOM   1375  N   ASP B 165       0.833  46.836  -5.701  1.00 33.10           N  
ANISOU 1375  N   ASP B 165     2377   4509   5690   -900     -3   1519       N  
ATOM   1376  CA  ASP B 165       1.394  45.625  -6.279  1.00 35.29           C  
ANISOU 1376  CA  ASP B 165     2748   4980   5680   -935   -208   1384       C  
ATOM   1377  C   ASP B 165       2.839  45.845  -6.711  1.00 34.06           C  
ANISOU 1377  C   ASP B 165     2683   4648   5610   -985   -152   1389       C  
ATOM   1378  O   ASP B 165       3.202  46.901  -7.238  1.00 30.48           O  
ANISOU 1378  O   ASP B 165     2172   4029   5379   -925     42   1634       O  
ATOM   1379  CB  ASP B 165       0.577  45.165  -7.485  1.00 29.22           C  
ANISOU 1379  CB  ASP B 165     1811   4581   4712   -783   -302   1589       C  
ATOM   1380  CG  ASP B 165       1.332  44.153  -8.324  1.00 33.80           C  
ANISOU 1380  CG  ASP B 165     2488   5279   5076   -833   -406   1502       C  
ATOM   1381  OD1 ASP B 165       1.527  43.016  -7.844  1.00 30.12           O  
ANISOU 1381  OD1 ASP B 165     2195   4768   4483   -925   -489   1190       O  
ATOM   1382  OD2 ASP B 165       1.771  44.504  -9.440  1.00 31.65           O  
ANISOU 1382  OD2 ASP B 165     2104   5127   4796   -761   -347   1777       O  
ATOM   1383  N   LYS B 166       3.659  44.826  -6.503  1.00 28.18           N  
ANISOU 1383  N   LYS B 166     2077   3916   4714  -1058   -268   1135       N  
ATOM   1384  CA  LYS B 166       5.032  44.831  -6.971  1.00 29.02           C  
ANISOU 1384  CA  LYS B 166     2210   3919   4898  -1087   -217   1124       C  
ATOM   1385  C   LYS B 166       5.321  43.742  -7.991  1.00 26.43           C  
ANISOU 1385  C   LYS B 166     1856   3775   4411  -1042   -271   1151       C  
ATOM   1386  O   LYS B 166       6.408  43.752  -8.587  1.00 29.11           O  
ANISOU 1386  O   LYS B 166     2165   4056   4839  -1055   -184   1192       O  
ATOM   1387  CB  LYS B 166       5.987  44.674  -5.782  1.00 26.87           C  
ANISOU 1387  CB  LYS B 166     2057   3500   4652  -1200   -257    835       C  
ATOM   1388  CG  LYS B 166       5.987  45.858  -4.823  1.00 32.19           C  
ANISOU 1388  CG  LYS B 166     2767   3978   5484  -1322   -176    767       C  
ATOM   1389  CD  LYS B 166       6.571  47.094  -5.490  1.00 35.16           C  
ANISOU 1389  CD  LYS B 166     3089   4148   6121  -1341     19    939       C  
ATOM   1390  CE  LYS B 166       6.636  48.264  -4.533  1.00 48.09           C  
ANISOU 1390  CE  LYS B 166     4810   5528   7935  -1501    129    825       C  
ATOM   1391  NZ  LYS B 166       7.686  49.241  -4.947  1.00 58.83           N  
ANISOU 1391  NZ  LYS B 166     6166   6660   9526  -1574    300    873       N  
ATOM   1392  N   CYS B 167       4.379  42.823  -8.223  1.00 25.60           N  
ANISOU 1392  N   CYS B 167     1755   3883   4090  -1011   -382   1111       N  
ATOM   1393  CA  CYS B 167       4.644  41.606  -8.971  1.00 30.69           C  
ANISOU 1393  CA  CYS B 167     2409   4664   4588  -1023   -427   1038       C  
ATOM   1394  C   CYS B 167       4.437  41.762 -10.475  1.00 29.14           C  
ANISOU 1394  C   CYS B 167     2046   4763   4262  -1000   -393   1312       C  
ATOM   1395  O   CYS B 167       5.138  41.111 -11.260  1.00 29.57           O  
ANISOU 1395  O   CYS B 167     2066   4906   4264  -1044   -343   1307       O  
ATOM   1396  CB  CYS B 167       3.737  40.481  -8.462  1.00 29.24           C  
ANISOU 1396  CB  CYS B 167     2320   4539   4251  -1031   -525    821       C  
ATOM   1397  SG  CYS B 167       4.300  39.810  -6.890  1.00 25.49           S  
ANISOU 1397  SG  CYS B 167     2007   3821   3856  -1043   -528    570       S  
ATOM   1398  N   GLU B 168       3.480  42.589 -10.899  1.00 29.28           N  
ANISOU 1398  N   GLU B 168     1922   4995   4208   -916   -398   1580       N  
ATOM   1399  CA  GLU B 168       3.173  42.677 -12.323  1.00 31.29           C  
ANISOU 1399  CA  GLU B 168     1979   5688   4220   -844   -386   1881       C  
ATOM   1400  C   GLU B 168       4.367  43.108 -13.170  1.00 32.86           C  
ANISOU 1400  C   GLU B 168     2276   5758   4451   -777   -117   2054       C  
ATOM   1401  O   GLU B 168       4.553  42.524 -14.248  1.00 36.83           O  
ANISOU 1401  O   GLU B 168     2852   6500   4642   -742    -84   2045       O  
ATOM   1402  CB  GLU B 168       1.965  43.596 -12.507  1.00 37.18           C  
ANISOU 1402  CB  GLU B 168     2655   6600   4872   -613   -426   2125       C  
ATOM   1403  CG  GLU B 168       1.352  43.548 -13.888  1.00 57.55           C  
ANISOU 1403  CG  GLU B 168     5232   9622   7014   -420   -509   2310       C  
ATOM   1404  CD  GLU B 168       2.153  44.339 -14.898  1.00 79.42           C  
ANISOU 1404  CD  GLU B 168     8157  12322   9698   -237   -244   2634       C  
ATOM   1405  OE1 GLU B 168       2.154  43.967 -16.089  1.00 91.52           O  
ANISOU 1405  OE1 GLU B 168     9775  14195  10802   -164   -273   2700       O  
ATOM   1406  OE2 GLU B 168       2.789  45.337 -14.495  1.00 84.67           O  
ANISOU 1406  OE2 GLU B 168     8872  12582  10714   -188     15   2809       O  
ATOM   1407  N   PRO B 169       5.190  44.086 -12.775  1.00 33.05           N  
ANISOU 1407  N   PRO B 169     2310   5418   4831   -781    105   2190       N  
ATOM   1408  CA  PRO B 169       6.367  44.412 -13.603  1.00 35.01           C  
ANISOU 1408  CA  PRO B 169     2615   5539   5148   -753    407   2347       C  
ATOM   1409  C   PRO B 169       7.415  43.315 -13.637  1.00 34.05           C  
ANISOU 1409  C   PRO B 169     2494   5366   5080   -891    411   2066       C  
ATOM   1410  O   PRO B 169       8.293  43.343 -14.510  1.00 36.13           O  
ANISOU 1410  O   PRO B 169     2784   5610   5334   -858    682   2173       O  
ATOM   1411  CB  PRO B 169       6.928  45.680 -12.942  1.00 37.04           C  
ANISOU 1411  CB  PRO B 169     2937   5335   5799   -734    566   2367       C  
ATOM   1412  CG  PRO B 169       5.813  46.223 -12.131  1.00 39.69           C  
ANISOU 1412  CG  PRO B 169     3242   5644   6195   -692    440   2404       C  
ATOM   1413  CD  PRO B 169       5.060  45.026 -11.653  1.00 32.36           C  
ANISOU 1413  CD  PRO B 169     2249   4989   5059   -785    121   2156       C  
ATOM   1414  N   LEU B 170       7.367  42.363 -12.716  1.00 31.49           N  
ANISOU 1414  N   LEU B 170     2188   4974   4801   -995    162   1713       N  
ATOM   1415  CA  LEU B 170       8.412  41.359 -12.616  1.00 32.19           C  
ANISOU 1415  CA  LEU B 170     2287   4943   5002  -1063    189   1472       C  
ATOM   1416  C   LEU B 170       8.033  40.031 -13.240  1.00 40.32           C  
ANISOU 1416  C   LEU B 170     3276   6262   5783  -1136    135   1378       C  
ATOM   1417  O   LEU B 170       8.927  39.285 -13.654  1.00 43.04           O  
ANISOU 1417  O   LEU B 170     3574   6570   6211  -1173    293   1303       O  
ATOM   1418  CB  LEU B 170       8.775  41.130 -11.147  1.00 29.87           C  
ANISOU 1418  CB  LEU B 170     2090   4381   4880  -1087     15   1175       C  
ATOM   1419  CG  LEU B 170       9.433  42.342 -10.489  1.00 29.52           C  
ANISOU 1419  CG  LEU B 170     2060   4101   5055  -1092     79   1186       C  
ATOM   1420  CD1 LEU B 170       9.529  42.151  -8.982  1.00 37.21           C  
ANISOU 1420  CD1 LEU B 170     3132   4964   6041  -1127   -103    936       C  
ATOM   1421  CD2 LEU B 170      10.809  42.593 -11.099  1.00 32.90           C  
ANISOU 1421  CD2 LEU B 170     2389   4425   5686  -1111    298   1247       C  
ATOM   1422  N   GLU B 171       6.733  39.727 -13.341  1.00 35.82           N  
ANISOU 1422  N   GLU B 171     2701   5994   4915  -1174    -67   1358       N  
ATOM   1423  CA  GLU B 171       6.326  38.349 -13.607  1.00 36.39           C  
ANISOU 1423  CA  GLU B 171     2822   6237   4766  -1276   -181   1090       C  
ATOM   1424  C   GLU B 171       6.905  37.808 -14.916  1.00 44.82           C  
ANISOU 1424  C   GLU B 171     4018   7422   5590  -1224     51   1021       C  
ATOM   1425  O   GLU B 171       7.181  36.604 -15.004  1.00 49.68           O  
ANISOU 1425  O   GLU B 171     4688   7980   6207  -1314     84    758       O  
ATOM   1426  CB  GLU B 171       4.796  38.230 -13.582  1.00 34.83           C  
ANISOU 1426  CB  GLU B 171     2621   6334   4278  -1305   -438   1025       C  
ATOM   1427  CG  GLU B 171       4.070  38.942 -14.681  1.00 39.19           C  
ANISOU 1427  CG  GLU B 171     3210   7239   4441  -1144   -451   1215       C  
ATOM   1428  CD  GLU B 171       2.609  38.536 -14.758  1.00 41.89           C  
ANISOU 1428  CD  GLU B 171     3477   7935   4504  -1203   -741   1089       C  
ATOM   1429  OE1 GLU B 171       1.764  39.439 -14.916  1.00 35.65           O  
ANISOU 1429  OE1 GLU B 171     2593   7353   3599  -1043   -843   1324       O  
ATOM   1430  OE2 GLU B 171       2.308  37.320 -14.670  1.00 34.40           O  
ANISOU 1430  OE2 GLU B 171     2568   7012   3490  -1391   -836    758       O  
ATOM   1431  N   LYS B 172       7.111  38.666 -15.931  1.00 43.53           N  
ANISOU 1431  N   LYS B 172     3932   7393   5215  -1072    254   1257       N  
ATOM   1432  CA  LYS B 172       7.802  38.308 -17.173  1.00 55.27           C  
ANISOU 1432  CA  LYS B 172     5572   8975   6452  -1010    557   1223       C  
ATOM   1433  C   LYS B 172       9.091  39.105 -17.308  1.00 68.72           C  
ANISOU 1433  C   LYS B 172     7210  10417   8486   -926    922   1467       C  
ATOM   1434  O   LYS B 172       9.140  40.284 -16.939  1.00 69.01           O  
ANISOU 1434  O   LYS B 172     7162  10327   8732   -873    948   1745       O  
ATOM   1435  CB  LYS B 172       6.954  38.559 -18.447  1.00 67.40           C  
ANISOU 1435  CB  LYS B 172     7302  10963   7345   -905    523   1311       C  
ATOM   1436  CG  LYS B 172       6.235  37.306 -18.958  1.00 76.31           C  
ANISOU 1436  CG  LYS B 172     8557  12382   8056  -1043    343    922       C  
ATOM   1437  CD  LYS B 172       5.760  36.565 -17.744  1.00 76.50           C  
ANISOU 1437  CD  LYS B 172     8429  12229   8409  -1225     78    679       C  
ATOM   1438  CE  LYS B 172       5.513  35.106 -17.892  1.00 78.48           C  
ANISOU 1438  CE  LYS B 172     8781  12502   8535  -1425     25    237       C  
ATOM   1439  NZ  LYS B 172       5.886  34.506 -16.524  1.00 74.76           N  
ANISOU 1439  NZ  LYS B 172     8176  11606   8622  -1528    -11    139       N  
ATOM   1440  N   GLN B 173      10.106  38.454 -17.885  1.00 74.23           N  
ANISOU 1440  N   GLN B 173     7943  11021   9240   -920   1241   1348       N  
ATOM   1441  CA  GLN B 173      11.456  38.995 -18.122  1.00 75.44           C  
ANISOU 1441  CA  GLN B 173     7984  10933   9746   -865   1656   1532       C  
ATOM   1442  C   GLN B 173      12.291  38.931 -16.850  1.00 79.98           C  
ANISOU 1442  C   GLN B 173     8242  11160  10988   -965   1572   1492       C  
ATOM   1443  O   GLN B 173      12.981  37.940 -16.600  1.00 76.43           O  
ANISOU 1443  O   GLN B 173     7680  10569  10792   -986   1629   1295       O  
ATOM   1444  CB  GLN B 173      11.421  40.436 -18.653  1.00 75.02           C  
ANISOU 1444  CB  GLN B 173     7994  10918   9594   -759   1849   1930       C  
ATOM   1445  CG  GLN B 173      12.407  40.735 -19.773  1.00 86.58           C  
ANISOU 1445  CG  GLN B 173     9546  12356  10994   -667   2394   2103       C  
ATOM   1446  CD  GLN B 173      13.709  41.335 -19.261  1.00 97.62           C  
ANISOU 1446  CD  GLN B 173    10724  13330  13036   -723   2569   2124       C  
ATOM   1447  OE1 GLN B 173      13.779  41.829 -18.137  1.00100.48           O  
ANISOU 1447  OE1 GLN B 173    10936  13456  13784   -805   2266   2062       O  
ATOM   1448  NE2 GLN B 173      14.741  41.315 -20.100  1.00101.70           N  
ANISOU 1448  NE2 GLN B 173    11282  13771  13589   -674   2978   2129       N  
HETATM 1449  C1  UCN B 201      -7.757  26.607  -0.703  1.00 19.63           C  
HETATM 1450  C10 UCN B 201      -5.492  31.403  -3.391  1.00 15.66           C  
HETATM 1451  C11 UCN B 201      -5.729  32.000  -2.127  1.00 15.42           C  
HETATM 1452  C12 UCN B 201      -5.520  33.257  -1.672  1.00 15.35           C  
HETATM 1453  C13 UCN B 201      -4.995  34.383  -2.257  1.00 13.81           C  
HETATM 1454  C14 UCN B 201      -4.891  35.551  -1.568  1.00 15.96           C  
HETATM 1455  C15 UCN B 201      -5.282  35.607  -0.275  1.00 16.61           C  
HETATM 1456  C16 UCN B 201      -5.804  34.489   0.304  1.00 15.58           C  
HETATM 1457  C17 UCN B 201      -5.932  33.286  -0.403  1.00 15.34           C  
HETATM 1458  C18 UCN B 201      -6.270  31.301  -1.081  1.00 11.38           C  
HETATM 1459  C19 UCN B 201      -6.584  29.955  -1.303  1.00 13.35           C  
HETATM 1460  C2  UCN B 201      -7.793  25.528  -1.573  1.00 22.14           C  
HETATM 1461  C20 UCN B 201      -7.264  27.820  -1.110  1.00 16.22           C  
HETATM 1462  C21 UCN B 201      -7.026  31.507   1.178  1.00 16.76           C  
HETATM 1463  C22 UCN B 201      -6.115  31.230   2.372  1.00 17.18           C  
HETATM 1464  C23 UCN B 201      -5.444  29.958   2.235  1.00 18.34           C  
HETATM 1465  C24 UCN B 201      -6.535  28.853   2.028  1.00 19.70           C  
HETATM 1466  C25 UCN B 201      -7.550  29.390   0.904  1.00 20.71           C  
HETATM 1467  C26 UCN B 201      -7.879  32.677   1.673  1.00 17.14           C  
HETATM 1468  C27 UCN B 201      -4.818  32.508   3.726  1.00 25.45           C  
HETATM 1469  C28 UCN B 201      -3.794  28.836   1.105  1.00 26.15           C  
HETATM 1470  C3  UCN B 201      -7.328  25.680  -2.870  1.00 20.79           C  
HETATM 1471  C4  UCN B 201      -6.853  26.912  -3.288  1.00 18.19           C  
HETATM 1472  C5  UCN B 201      -6.818  27.981  -2.424  1.00 20.82           C  
HETATM 1473  C6  UCN B 201      -6.394  29.353  -2.470  1.00 19.57           C  
HETATM 1474  C7  UCN B 201      -5.835  30.048  -3.581  1.00 13.69           C  
HETATM 1475  C8  UCN B 201      -5.520  29.673  -5.001  1.00 18.76           C  
HETATM 1476  C9  UCN B 201      -4.984  31.950  -4.722  1.00 18.87           C  
HETATM 1477  N1  UCN B 201      -5.012  30.851  -5.636  1.00 19.12           N  
HETATM 1478  N2  UCN B 201      -6.381  32.032  -0.001  1.00 11.80           N  
HETATM 1479  N3  UCN B 201      -7.123  28.986  -0.449  1.00 16.83           N  
HETATM 1480  N4  UCN B 201      -4.561  29.974   1.145  1.00 20.18           N  
HETATM 1481  O37 UCN B 201      -3.794  32.534  -4.661  1.00 19.00           O  
HETATM 1482  O4  UCN B 201      -7.879  30.600   0.965  1.00 17.04           O  
HETATM 1483  O5  UCN B 201      -5.690  28.693  -5.467  1.00 21.93           O  
HETATM 1484  O6  UCN B 201      -5.259  32.306   2.481  1.00 17.68           O  
TER    1485      UCN B 201                                                      
HETATM 1485  O   HOH S   1      -9.595  27.307   2.738  1.00 16.75           O  
HETATM 1486  O   HOH S   2      -9.547  45.468  -3.255  1.00 20.68           O  
HETATM 1487  O   HOH S   3     -11.573  31.760   1.364  1.00 16.12           O  
HETATM 1488  O   HOH S   4     -19.223  34.366 -10.777  1.00 19.73           O  
HETATM 1489  O   HOH S   5     -18.873  37.385  12.542  1.00 19.27           O  
HETATM 1490  O   HOH S   6     -27.167  32.973   7.753  1.00 22.03           O  
HETATM 1491  O   HOH S   7     -19.575  39.903  -8.489  1.00 20.80           O  
HETATM 1492  O   HOH S   8      -4.701  42.105  -5.762  1.00 18.24           O  
HETATM 1493  O   HOH S   9     -22.119  31.332  -4.321  1.00 19.65           O  
HETATM 1494  O   HOH S  10     -16.488  33.431 -12.787  1.00 19.50           O  
HETATM 1495  O   HOH S  11     -15.557  25.117   3.135  1.00 18.38           O  
HETATM 1496  O   HOH S  12     -22.424  32.972  14.941  1.00 23.95           O  
HETATM 1497  O   HOH S  13      -9.005  46.163  -5.987  1.00 24.53           O  
HETATM 1498  O   HOH S  14      14.201  33.564 -15.686  1.00 21.31           O  
HETATM 1499  O   HOH S  15       0.765  40.936  -6.056  1.00 21.19           O  
HETATM 1500  O   HOH S  16     -22.499  41.718   6.577  1.00 21.90           O  
HETATM 1501  O   HOH S  17       2.317  44.029   4.028  1.00 24.33           O  
HETATM 1502  O   HOH S  18     -24.815  40.807   7.591  1.00 23.66           O  
HETATM 1503  O   HOH S  19     -12.066  38.975   8.821  1.00 21.42           O  
HETATM 1504  O   HOH S  20     -18.813  24.806  -4.515  1.00 22.72           O  
HETATM 1505  O   HOH S  21      -6.023  44.397  -6.190  1.00 24.35           O  
HETATM 1506  O   HOH S  22      -7.215  48.315  -5.697  1.00 23.15           O  
HETATM 1507  O   HOH S  23     -12.296  24.725   4.286  1.00 28.11           O  
HETATM 1508  O   HOH S  24      -5.966  41.050   2.471  1.00 23.66           O  
HETATM 1509  O   HOH S  25     -22.777  33.916 -13.025  1.00 25.91           O  
HETATM 1510  O   HOH S  26     -25.973  29.092  11.017  1.00 23.39           O  
HETATM 1511  O   HOH S  27     -27.876  35.582   7.102  1.00 28.05           O  
HETATM 1512  O   HOH S  28      10.916  40.203  -3.595  1.00 26.00           O  
HETATM 1513  O   HOH S  29      -6.639  28.025   9.430  1.00 26.69           O  
HETATM 1514  O   HOH S  30      -7.673  37.901 -16.125  1.00 29.81           O  
HETATM 1515  O   HOH S  31     -21.052  25.123  12.187  1.00 25.58           O  
HETATM 1516  O   HOH S  32       8.520  39.130   4.535  1.00 31.66           O  
HETATM 1517  O   HOH S  33      -2.287  33.949   0.497  1.00 28.20           O  
HETATM 1518  O   HOH S  34      -5.251  43.428   2.641  1.00 29.85           O  
HETATM 1519  O   HOH S  35     -16.292  33.934 -17.020  1.00 34.02           O  
HETATM 1520  O   HOH S  36     -19.891  20.476  -1.327  1.00 37.82           O  
HETATM 1521  O   HOH S  37     -22.986  27.366  16.522  1.00 33.32           O  
HETATM 1522  O   HOH S  38      12.250  40.811  -1.586  1.00 29.40           O  
HETATM 1523  O   HOH S  39       3.175  43.118   6.810  1.00 29.83           O  
HETATM 1524  O   HOH S  40      -0.733  21.852  -3.129  1.00 33.88           O  
HETATM 1525  O   HOH S  41     -19.900  46.543   9.285  1.00 34.03           O  
HETATM 1526  O   HOH S  42       2.953  38.086   6.350  1.00 28.68           O  
HETATM 1527  O   HOH S  43     -22.262  44.521   7.875  1.00 32.78           O  
HETATM 1528  O   HOH S  44      -1.417  31.549  -0.947  1.00 35.49           O  
HETATM 1529  O   HOH S  45     -17.978  24.888  -8.068  1.00 28.74           O  
HETATM 1530  O   HOH S  46     -22.603  42.333   3.926  1.00 30.27           O  
HETATM 1531  O   HOH S  47      -8.963  24.723   4.924  1.00 29.02           O  
HETATM 1532  O   HOH S  48     -18.211  50.909  -9.877  1.00 35.40           O  
HETATM 1533  O   HOH S  49     -26.693  36.035   1.205  1.00 36.16           O  
HETATM 1534  O   HOH S  50     -10.198  31.279  15.111  1.00 37.92           O  
HETATM 1535  O   HOH S  51      -3.972  28.353   8.489  1.00 36.51           O  
HETATM 1536  O   HOH S  52     -22.398  20.516   6.653  1.00 37.54           O  
HETATM 1537  O   HOH S  53     -13.346  23.853  10.948  1.00 35.27           O  
HETATM 1538  O   HOH S  54     -24.707  44.137  -1.189  1.00 31.37           O  
HETATM 1539  O   HOH S  55     -20.327  28.479 -16.697  1.00 38.95           O  
HETATM 1540  O   HOH S  56       7.350  34.570 -12.997  1.00 36.05           O  
HETATM 1541  O   HOH S  57      -0.218  24.838  -2.506  1.00 39.84           O  
HETATM 1542  O   HOH S  58      -4.810  15.695 -19.119  1.00 45.03           O  
HETATM 1543  O   HOH S  59       0.091  48.742  -9.560  1.00 34.81           O  
HETATM 1544  O   HOH S  60     -14.685  44.570 -13.452  1.00 35.89           O  
HETATM 1545  O   HOH S  61       8.514  36.489   3.724  1.00 32.07           O  
HETATM 1546  O   HOH S  62       0.608  35.442   3.106  1.00 27.21           O  
HETATM 1547  O   HOH S  63       0.332  29.785 -15.899  1.00 49.03           O  
HETATM 1548  O   HOH S  64       0.754  37.086   5.128  1.00 30.79           O  
HETATM 1549  O   HOH S  65       8.165  45.657  -8.702  1.00 37.13           O  
HETATM 1550  O   HOH S  66     -15.673  44.628  12.818  1.00 52.39           O  
HETATM 1551  O   HOH S  67     -14.234  22.963   8.312  1.00 37.60           O  
HETATM 1552  O   HOH S  68      -9.773  34.915 -15.722  1.00 36.88           O  
HETATM 1553  O   HOH S  69      -6.905  19.482 -19.384  1.00 41.19           O  
HETATM 1554  O   HOH S  70     -25.479  40.688 -11.881  1.00 38.55           O  
HETATM 1555  O   HOH S  71      15.709  36.344 -19.492  1.00 41.41           O  
HETATM 1556  O   HOH S  72     -25.378  27.138  11.217  1.00 42.59           O  
HETATM 1557  O   HOH S  73     -29.748  35.362   5.139  1.00 45.87           O  
HETATM 1558  O   HOH S  74     -24.505  43.972  -6.351  1.00 33.43           O  
HETATM 1559  O   HOH S  75       4.068  48.274   4.144  1.00 41.80           O  
HETATM 1560  O   HOH S  76     -13.218  46.694   6.430  1.00 35.53           O  
HETATM 1561  O   HOH S  77     -20.306  47.594  -3.186  1.00 32.96           O  
HETATM 1562  O   HOH S  78      -0.575  39.525  10.577  1.00 52.04           O  
HETATM 1563  O   HOH S  79       3.856  48.550 -10.466  1.00 41.44           O  
HETATM 1564  O   HOH S  80      11.408  39.699   2.692  1.00 37.48           O  
HETATM 1565  O   HOH S  81     -13.321  46.881 -13.043  1.00 37.80           O  
HETATM 1566  O   HOH S  82      -5.743  13.001  -9.367  1.00 56.79           O  
HETATM 1567  O   HOH S  83     -15.613  47.341   4.705  1.00 38.65           O  
HETATM 1568  O   HOH S  84      -8.859  14.743  -6.615  1.00 39.88           O  
HETATM 1569  O   HOH S  85     -17.251  27.569 -19.271  1.00 44.19           O  
HETATM 1570  O   HOH S  86      -5.539  44.180   5.063  1.00 40.50           O  
HETATM 1571  O   HOH S  87     -13.206  46.526  -5.493  1.00 43.87           O  
HETATM 1572  O   HOH S  88      -2.822  30.938   7.020  1.00 41.48           O  
HETATM 1573  O   HOH S  89     -23.455  41.915 -10.274  1.00 31.27           O  
HETATM 1574  O   HOH S  90     -24.891  43.486   3.347  1.00 48.32           O  
HETATM 1575  O   HOH S  91      -8.094  46.239   4.257  1.00 25.72           O  
HETATM 1576  O   HOH S  92      -4.711  18.633  -2.091  1.00 41.41           O  
HETATM 1577  O   HOH S  93      -2.131  53.451  -2.112  1.00 44.39           O  
HETATM 1578  O   HOH S  94     -23.475  26.385  12.973  1.00 34.73           O  
HETATM 1579  O   HOH S  95     -18.826  24.853 -10.470  1.00 41.33           O  
HETATM 1580  O   HOH S  96     -27.727  19.547  13.027  1.00 43.30           O  
HETATM 1581  O   HOH S  97     -23.833  25.227  10.768  1.00 53.11           O  
HETATM 1582  O   HOH S  98     -12.785  14.680  -8.471  1.00 36.44           O  
HETATM 1583  O   HOH S  99       3.400  49.774  -6.774  1.00 47.15           O  
HETATM 1584  O   HOH S 100     -14.075  42.095 -13.424  1.00 44.09           O  
HETATM 1585  O   HOH S 101       0.734  35.134   9.797  1.00 40.65           O  
HETATM 1586  O   HOH S 102      -0.934  27.677   5.823  1.00 50.21           O  
HETATM 1587  O   HOH S 103      -6.806  35.209 -18.168  1.00 39.45           O  
HETATM 1588  O   HOH S 104     -20.595  26.179 -12.171  1.00 51.44           O  
HETATM 1589  O   HOH S 105     -13.904  23.784  15.012  1.00 45.62           O  
HETATM 1590  O   HOH S 106     -22.083  22.241 -11.517  1.00 44.72           O  
HETATM 1591  O   HOH S 107      -8.715  15.047  -3.999  1.00 45.08           O  
HETATM 1592  O   HOH S 108       1.392  46.777 -10.765  1.00 38.90           O  
HETATM 1593  O   HOH S 109     -17.659  43.229  14.919  1.00 45.26           O  
HETATM 1594  O   HOH S 110      -6.928  27.313  12.018  1.00 43.95           O  
HETATM 1595  O   HOH S 111      -1.635  34.022   3.182  1.00 39.01           O  
HETATM 1596  O   HOH S 112     -23.053  31.112 -13.761  1.00 41.85           O  
HETATM 1597  O   HOH S 113     -18.275  32.788 -18.400  1.00 35.62           O  
HETATM 1598  O   HOH S 114     -15.144  32.995  15.959  1.00 43.01           O  
HETATM 1599  O   HOH S 115     -12.776  31.688  15.473  1.00 43.01           O  
HETATM 1600  O   HOH S 116     -18.761  49.727  12.269  1.00 48.92           O  
HETATM 1601  O   HOH S 117     -20.103  49.164   2.332  1.00 46.07           O  
HETATM 1602  O   HOH S 118       3.447  34.928 -15.327  1.00 38.78           O  
HETATM 1603  O   HOH S 119     -16.756  38.030  13.122  1.00 48.32           O  
HETATM 1604  O   HOH S 120      -8.613  16.753   0.146  1.00 59.86           O  
HETATM 1605  O   HOH S 121      -6.643  14.910  -8.107  1.00 43.88           O  
HETATM 1606  O   HOH S 122     -14.275  42.551 -17.027  1.00 52.11           O  
HETATM 1607  O   HOH S 123     -19.457  46.857  12.178  1.00 41.56           O  
HETATM 1608  O   HOH S 124       6.178  31.274 -13.692  1.00 49.96           O  
HETATM 1609  O   HOH S 125      -2.748  47.327   1.812  1.00 48.75           O  
HETATM 1610  O   HOH S 126     -12.637  22.419   5.703  1.00 40.70           O  
HETATM 1611  O   HOH S 127     -14.003  18.109  -0.079  1.00 45.72           O  
HETATM 1612  O   HOH S 128     -18.674  49.610  -2.388  1.00 45.46           O  
HETATM 1613  O   HOH S 129      -7.939  49.337  -0.983  1.00 49.37           O  
HETATM 1614  O   HOH S 130       3.989  51.186  -3.552  1.00 55.11           O  
HETATM 1615  O   HOH S 131       1.073  46.162   4.705  1.00 44.29           O  
HETATM 1616  O   HOH S 132     -10.629  42.248   9.869  1.00 41.83           O  
HETATM 1617  O   HOH S 133     -12.026  46.629  -3.390  1.00 38.19           O  
HETATM 1618  O   HOH S 134     -17.198  49.143  -0.333  1.00 39.39           O  
HETATM 1619  O   HOH S 135      -1.377  28.272 -14.105  1.00 31.38           O  
HETATM 1620  O   HOH S 136     -11.640  47.126  -6.518  1.00 37.58           O  
HETATM 1621  O   HOH S 137     -13.893  33.292 -16.957  1.00 32.43           O  
HETATM 1622  O   HOH S 138      -9.422  36.861  13.993  1.00 38.20           O  
HETATM 1623  O   HOH S 139     -17.748  17.431 -16.753  1.00 46.05           O  
HETATM 1624  O   HOH S 140      -6.432  16.997 -19.907  1.00 47.97           O  
HETATM 1625  O   HOH S 141     -23.004  19.618 -12.295  1.00 46.18           O  
HETATM 1626  O   HOH S 142     -21.028  23.337 -14.539  1.00 49.38           O  
HETATM 1627  O   HOH S 143     -15.016  53.392 -11.895  1.00 37.83           O  
HETATM 1628  O   HOH S 144     -10.571  45.180   8.401  1.00 47.77           O  
HETATM 1629  O   HOH S 145     -23.207  45.311   9.641  1.00 52.61           O  
HETATM 1630  O   HOH S 146       3.381  38.451   9.027  1.00 42.86           O  
HETATM 1631  O   HOH S 147     -28.103  41.084 -11.317  1.00 52.34           O  
HETATM 1632  O   HOH S 148     -11.306  13.443 -14.611  1.00 55.97           O  
HETATM 1633  O   HOH S 149     -18.976  20.223 -18.322  1.00 42.11           O  
HETATM 1634  O   HOH S 150     -11.842  26.651  16.345  1.00 44.47           O  
HETATM 1635  O   HOH S 151       5.913  23.633  -6.321  1.00 47.66           O  
HETATM 1636  O   HOH S 152     -28.426  36.333   3.199  1.00 44.95           O  
HETATM 1637  O   HOH S 153       2.420  41.374 -16.518  1.00 46.95           O  
HETATM 1638  O   HOH S 154     -16.632  22.976   4.634  1.00 39.00           O  
HETATM 1639  O   HOH S 155      -9.848  24.985  12.061  1.00 55.72           O  
HETATM 1640  O   HOH S 156     -19.873   9.148  -6.860  1.00 50.10           O  
HETATM 1641  O   HOH S 157      -2.808  21.013 -18.255  1.00 49.52           O  
HETATM 1642  O   HOH S 158     -19.155  17.049 -11.384  1.00 47.91           O  
HETATM 1643  O   HOH S 159      -2.223  45.171   3.747  1.00 56.18           O  
HETATM 1644  O   HOH S 160     -13.735  38.460  11.687  1.00 43.27           O  
HETATM 1645  O   HOH S 161      -1.057  38.696 -17.945  1.00 47.71           O  
HETATM 1646  O   HOH S 162     -16.124  40.408  14.360  1.00 47.71           O  
HETATM 1647  O   HOH S 163       4.366  23.001   2.947  1.00 58.62           O  
HETATM 1648  O   HOH S 164     -19.848  26.860 -14.641  1.00 54.37           O  
HETATM 1649  O   HOH S 165     -18.855  20.237   1.214  1.00 53.19           O  
HETATM 1650  O   HOH S 166       6.871  48.333  -8.889  1.00 52.06           O  
HETATM 1651  O   HOH S 167     -16.485  18.915   1.572  1.00 45.44           O  
HETATM 1652  O   HOH S 168     -17.242  31.261 -19.734  1.00 52.20           O  
HETATM 1653  O   HOH S 169       4.350  21.141  -7.658  1.00 52.40           O  
HETATM 1654  O   HOH S 170      -1.158  31.267   3.644  1.00 52.52           O  
HETATM 1655  O   HOH S 171      -2.001  41.904 -15.059  1.00 49.60           O  
HETATM 1656  O   HOH S 172      -2.071  29.904   5.425  1.00 51.89           O  
HETATM 1657  O   HOH S 173       5.711  46.018   5.908  1.00 43.95           O  
HETATM 1658  O   HOH S 174     -26.074  42.103  -4.429  1.00 45.72           O  
HETATM 1659  O   HOH S 175     -16.551  12.613 -10.768  1.00 52.15           O  
HETATM 1660  O   HOH S 176      -3.751  13.330  -9.817  1.00 52.84           O  
HETATM 1661  O   HOH S 177       2.243  21.136  -5.309  1.00 46.03           O  
HETATM 1662  O   HOH S 178      -4.619  30.372 -19.817  1.00 50.15           O  
HETATM 1663  O   HOH S 179     -18.232  14.368 -11.252  1.00 45.45           O  
HETATM 1664  O   HOH S 180     -12.862  14.591 -17.823  1.00 54.43           O  
HETATM 1665  O   HOH S 181      -3.781  29.976 -17.309  1.00 54.83           O  
HETATM 1666  O   HOH S 182     -21.709  50.380  -0.175  1.00 54.72           O  
HETATM 1667  O   HOH S 183       4.997  21.084 -13.489  1.00 48.11           O  
HETATM 1668  O   HOH S 184     -23.475  46.436   5.859  1.00 46.86           O  
HETATM 1669  O   HOH S 185     -10.151  32.871 -17.498  1.00 66.71           O  
HETATM 1670  O   HOH S 186     -17.781  32.714  15.915  1.00 54.57           O  
HETATM 1671  O   HOH S 187     -11.022  48.957   5.931  1.00 49.95           O  
HETATM 1672  O   HOH S 188      -3.568  19.259   7.443  1.00 54.00           O  
HETATM 1673  O   HOH S 189     -17.045  25.459 -21.529  1.00 57.78           O  
HETATM 1674  O   HOH S 190     -11.173  17.381   0.072  1.00 56.03           O  
HETATM 1675  O   HOH S 191      -6.123  13.789  -3.335  1.00 59.11           O  
HETATM 1676  O   HOH S 192      -1.490  51.539 -10.141  1.00 51.76           O  
HETATM 1677  O   HOH S 193     -15.007  48.884  -5.554  1.00 54.76           O  
HETATM 1678  O   HOH S 194     -31.109  32.222   3.117  1.00 44.51           O  
HETATM 1679  O   HOH S 195     -17.377  16.329 -13.940  1.00 50.15           O  
HETATM 1680  O   HOH S 196     -12.507  15.606 -19.433  1.00 57.82           O  
HETATM 1681  O   HOH S 197     -30.968  33.132   5.702  1.00 53.18           O  
HETATM 1682  O   HOH S 198       9.622  43.406  -4.628  1.00 49.25           O  
HETATM 1683  O   HOH S 199      -6.765  11.669  -8.240  1.00 55.27           O  
HETATM 1684  O   HOH S 200     -14.721  12.275 -13.711  1.00 58.59           O  
HETATM 1685  O   HOH S 201      14.265  36.071 -17.162  1.00 37.87           O  
HETATM 1686  O   HOH S 202       5.954  41.282 -16.702  1.00 41.27           O  
HETATM 1687  O   HOH S 203       4.520  45.298   6.960  1.00 49.79           O  
HETATM 1688  O   HOH S 204      15.537  37.579 -16.075  1.00 42.58           O  
HETATM 1689  O   HOH S 205      13.458  34.813 -17.952  1.00 41.82           O  
HETATM 1690  O   HOH S 206     -25.324  24.878  14.434  1.00 54.70           O  
HETATM 1691  O   HOH S 207     -22.567  28.024 -11.403  1.00 46.70           O  
HETATM 1692  O   HOH S 208     -16.785  50.029  -4.085  1.00 55.47           O  
HETATM 1693  O   HOH S 209       6.375  48.203 -19.675  1.00 53.76           O  
HETATM 1694  O   HOH S 210      -6.061  43.472 -16.166  1.00 44.54           O  
HETATM 1695  O   HOH S 211     -15.369  50.993 -11.010  1.00 45.34           O  
HETATM 1696  O   HOH S 212       8.080  42.610 -16.864  1.00 55.40           O  
HETATM 1697  O   HOH S 213       3.790  47.341  -1.516  1.00 49.75           O  
HETATM 1698  O   HOH S 214     -26.418  42.490   1.312  1.00 47.55           O  
HETATM 1699  O   HOH S 215     -11.437  35.002 -17.220  1.00 61.74           O  
HETATM 1700  O   HOH S 216     -18.557  24.901  15.129  1.00 53.06           O  
HETATM 1701  O   HOH S 217       4.382  41.308 -18.191  1.00 55.87           O  
HETATM 1702  O   HOH S 218       0.250  48.276   2.973  1.00 46.23           O  
HETATM 1703  O   HOH S 219     -22.766  47.825  -1.971  1.00 51.89           O  
HETATM 1704  O   HOH S 220     -14.692  37.475  14.223  1.00 51.63           O  
HETATM 1705  O   HOH S 221      -4.256  19.390 -19.815  1.00 52.37           O  
HETATM 1706  O   HOH S 222      -0.114  16.348 -19.126  1.00 54.04           O  
HETATM 1707  O   HOH S 223      -6.093  38.909 -18.025  1.00 53.58           O  
HETATM 1708  O   HOH S 224     -13.637  20.026   4.426  1.00 57.07           O  
HETATM 1709  O   HOH S 225       5.058  18.216 -14.279  1.00 54.47           O  
HETATM 1710  O   HOH S 226       0.873  32.254   6.240  1.00 57.50           O  
HETATM 1711  O   HOH S 227       1.664  34.756   7.343  1.00 58.31           O  
HETATM 1712  O   HOH S 228      -2.357  45.882 -14.231  1.00 58.12           O  
HETATM 1713  O   HOH S 229      -8.702  11.125 -12.077  1.00 62.54           O  
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.