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***  LYASE 19-SEP-16 5TD9  ***

elNémo ID: 21040915035755074

Job options:

ID        	=	 21040915035755074
JOBID     	=	 LYASE 19-SEP-16 5TD9
USERID    	=	 unknown
PRIVAT    	=	 0

NMODES    	=	 1
DQMIN     	=	 -100
DQMAX     	=	 100
DQSTEP    	=	 20
DOGRAPHS  	=	 on

DOPROJMODS	=	 0
DORMSD    	=	 0

NRBL      	=	 0
CUTOFF    	=	 0
CAONLY    	=	 0


Input data for this run:


HEADER    LYASE                                   19-SEP-16   5TD9              
TITLE     STRUCTURE OF HUMAN ENOLASE 2                                          
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: GAMMA-ENOLASE;                                             
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 SYNONYM: 2-PHOSPHO-D-GLYCERATE HYDRO-LYASE, ENOLASE 2, NEURAL        
COMPND   5 ENOLASE, NEURON-SPECIFIC ENOLASE, NSE;                               
COMPND   6 EC: 4.2.1.11;                                                        
COMPND   7 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: ENO2;                                                          
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: ROSETTA2 PLYSS;                            
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PJL-H6                                    
KEYWDS    ENOLASE GAMMA, GLYCOLYSIS, NEURON SPECIFIC ENOLASE, CARBOHYDRATE      
KEYWDS   2 METABOLISM, LYASE                                                    
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    P.G.LEONARD,F.L.MULLER                                                
REVDAT   1   27-SEP-17 5TD9    0                                                
JRNL        AUTH   Y.H.LIN,N.SATANI,N.HAMMOUDI,F.FELINI,P.G.LEONARD,D.MAXWELL,  
JRNL        AUTH 2 Z.PENG,T.M.LINK,G.R.LEE,A.BOSAJOU,D.SUN,J.R.MARSZALEK,       
JRNL        AUTH 3 Y.T.SUN,J.MCMURRAY,P.J.MANDAL,R.ZIELINSKI,W.PRIEBE,          
JRNL        AUTH 4 M.E.DIFRANCESCO,B.CZAKO,Y.A.WANG,W.BORNMANN,R.A.DEPINHO,     
JRNL        AUTH 5 F.L.MULLER                                                   
JRNL        TITL   POMHEX, A CELL-PERMEABLE ENOLASE INHIBITOR FOR COLLATERAL    
JRNL        TITL 2 LETHALITY TARGETING OF ENO1-DELETED GLIOBLASTOMA             
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.32 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX 1.10.1-2155-000                               
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : NULL                                          
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.32                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 43.51                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.340                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.6                           
REMARK   3   NUMBER OF REFLECTIONS             : 40812                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.202                           
REMARK   3   R VALUE            (WORKING SET) : 0.200                           
REMARK   3   FREE R VALUE                     : 0.245                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.940                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2015                            
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        
REMARK   3     1 43.5172 -  5.5837    1.00     2975   156  0.1658 0.1994        
REMARK   3     2  5.5837 -  4.4334    1.00     2837   148  0.1577 0.2123        
REMARK   3     3  4.4334 -  3.8734    1.00     2809   144  0.1661 0.2035        
REMARK   3     4  3.8734 -  3.5194    1.00     2800   143  0.1874 0.2385        
REMARK   3     5  3.5194 -  3.2672    1.00     2776   152  0.2092 0.2583        
REMARK   3     6  3.2672 -  3.0746    1.00     2751   134  0.2201 0.2598        
REMARK   3     7  3.0746 -  2.9207    1.00     2793   134  0.2350 0.2580        
REMARK   3     8  2.9207 -  2.7936    1.00     2745   147  0.2421 0.2994        
REMARK   3     9  2.7936 -  2.6861    1.00     2745   148  0.2470 0.3027        
REMARK   3    10  2.6861 -  2.5934    1.00     2746   141  0.2431 0.3011        
REMARK   3    11  2.5934 -  2.5123    1.00     2734   143  0.2419 0.2694        
REMARK   3    12  2.5123 -  2.4405    1.00     2743   137  0.2405 0.3015        
REMARK   3    13  2.4405 -  2.3762    1.00     2741   143  0.2491 0.3019        
REMARK   3    14  2.3762 -  2.3183    0.96     2602   145  0.2561 0.2970        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : NULL                                          
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.260            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 28.840           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 33.38                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 57.99                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.006           6766                                  
REMARK   3   ANGLE     :  0.636           9136                                  
REMARK   3   CHIRALITY :  0.042           1026                                  
REMARK   3   PLANARITY :  0.004           1204                                  
REMARK   3   DIHEDRAL  : 18.286           4080                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 9                                          
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 1 THROUGH 44 )                    
REMARK   3    ORIGIN FOR THE GROUP (A):  83.5612  29.1241 -86.2478              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2638 T22:   0.7842                                     
REMARK   3      T33:   0.2186 T12:  -0.0042                                     
REMARK   3      T13:   0.0047 T23:   0.0370                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.4116 L22:   2.0362                                     
REMARK   3      L33:   3.3647 L12:   0.4061                                     
REMARK   3      L13:  -0.5139 L23:  -0.0920                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0308 S12:  -0.5613 S13:  -0.0393                       
REMARK   3      S21:   0.1586 S22:   0.0243 S23:  -0.2970                       
REMARK   3      S31:  -0.1305 S32:   0.2224 S33:  -0.0756                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 45 THROUGH 107 )                  
REMARK   3    ORIGIN FOR THE GROUP (A):  86.1362  24.8401 -78.0537              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3114 T22:   0.9902                                     
REMARK   3      T33:   0.2899 T12:   0.0436                                     
REMARK   3      T13:  -0.0368 T23:   0.0595                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.7093 L22:   2.0654                                     
REMARK   3      L33:   2.7273 L12:   0.5281                                     
REMARK   3      L13:   0.3153 L23:   0.0051                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0378 S12:  -0.7306 S13:  -0.3122                       
REMARK   3      S21:   0.3681 S22:   0.0405 S23:  -0.4260                       
REMARK   3      S31:   0.0385 S32:   0.6456 S33:  -0.1281                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 108 THROUGH 148 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  97.8888  35.0297 -91.0473              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2498 T22:   0.8898                                     
REMARK   3      T33:   0.3380 T12:  -0.0738                                     
REMARK   3      T13:   0.0034 T23:  -0.0666                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.6265 L22:   1.1734                                     
REMARK   3      L33:   1.4294 L12:  -0.9542                                     
REMARK   3      L13:  -1.0310 L23:   0.0710                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1807 S12:  -0.7512 S13:   0.2603                       
REMARK   3      S21:   0.1223 S22:  -0.0114 S23:  -0.3896                       
REMARK   3      S31:  -0.2851 S32:   0.4418 S33:  -0.1305                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 149 THROUGH 177 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  94.5989  12.4188-107.2010              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3695 T22:   0.4827                                     
REMARK   3      T33:   0.4904 T12:  -0.0322                                     
REMARK   3      T13:   0.1273 T23:  -0.0513                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.7344 L22:   5.6517                                     
REMARK   3      L33:   5.5457 L12:   1.3026                                     
REMARK   3      L13:  -1.6041 L23:  -2.7809                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.3005 S12:   0.2601 S13:  -1.0238                       
REMARK   3      S21:  -0.1382 S22:   0.1571 S23:  -0.1153                       
REMARK   3      S31:   0.8713 S32:  -0.1008 S33:   0.1173                       
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 178 THROUGH 251 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  93.0827  12.6951-113.8075              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3413 T22:   0.9234                                     
REMARK   3      T33:   0.4576 T12:   0.0505                                     
REMARK   3      T13:   0.1035 T23:  -0.1016                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.6035 L22:   3.1027                                     
REMARK   3      L33:   2.7394 L12:   0.7225                                     
REMARK   3      L13:  -1.3021 L23:  -0.3376                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2412 S12:   0.6821 S13:  -0.9214                       
REMARK   3      S21:  -0.2979 S22:  -0.0528 S23:  -0.1506                       
REMARK   3      S31:   0.7047 S32:   0.0311 S33:   0.3829                       
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 252 THROUGH 310 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): 102.3690  -0.6969-100.3131              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.7289 T22:   0.8457                                     
REMARK   3      T33:   1.3124 T12:   0.2314                                     
REMARK   3      T13:   0.1284 T23:   0.2218                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.4675 L22:   2.9091                                     
REMARK   3      L33:   4.9511 L12:  -0.4734                                     
REMARK   3      L13:   1.7878 L23:  -0.3054                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2180 S12:  -0.1716 S13:  -1.9591                       
REMARK   3      S21:   0.3002 S22:  -0.0851 S23:  -0.2823                       
REMARK   3      S31:   1.1727 S32:  -0.1139 S33:   0.1529                       
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 311 THROUGH 434 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): 100.9132  22.8326 -96.2968              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2450 T22:   0.9033                                     
REMARK   3      T33:   0.3581 T12:   0.0782                                     
REMARK   3      T13:   0.0056 T23:   0.1444                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.9634 L22:   0.7962                                     
REMARK   3      L33:   0.9289 L12:  -0.3456                                     
REMARK   3      L13:  -0.1087 L23:   0.7105                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0906 S12:  -0.5462 S13:  -0.2735                       
REMARK   3      S21:   0.1421 S22:  -0.0464 S23:  -0.2942                       
REMARK   3      S31:   0.1867 S32:   0.7399 S33:   0.1184                       
REMARK   3   TLS GROUP : 8                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 1 THROUGH 219 )                   
REMARK   3    ORIGIN FOR THE GROUP (A):  75.3239  33.4857-109.5155              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2442 T22:   0.6503                                     
REMARK   3      T33:   0.2315 T12:   0.0208                                     
REMARK   3      T13:  -0.0185 T23:   0.0933                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.7211 L22:   1.1231                                     
REMARK   3      L33:   1.1606 L12:   0.2375                                     
REMARK   3      L13:   0.0487 L23:   0.0154                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0536 S12:   0.4111 S13:   0.1243                       
REMARK   3      S21:  -0.1339 S22:  -0.0628 S23:  -0.0198                       
REMARK   3      S31:  -0.0210 S32:  -0.0411 S33:   0.1217                       
REMARK   3   TLS GROUP : 9                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 220 THROUGH 434 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  60.9244  25.4336-110.8309              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1881 T22:   0.6946                                     
REMARK   3      T33:   0.2135 T12:  -0.0041                                     
REMARK   3      T13:   0.0401 T23:   0.0325                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.9402 L22:   1.0854                                     
REMARK   3      L33:   2.3046 L12:   0.4694                                     
REMARK   3      L13:   0.9496 L23:   0.0866                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0622 S12:   0.3700 S13:  -0.0199                       
REMARK   3      S21:  -0.0612 S22:  -0.0156 S23:   0.0879                       
REMARK   3      S31:   0.0499 S32:  -0.3637 S33:   0.1001                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 5TD9 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 19-SEP-16.                  
REMARK 100 THE DEPOSITION ID IS D_1000223998.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 07-APR-16                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : PH 6.5                             
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ALS                                
REMARK 200  BEAMLINE                       : 8.3.1                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.11587                            
REMARK 200  MONOCHROMATOR                  : DOUBLE FLAT CRYSTAL, SI(111)       
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315R                  
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000 708                       
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000 708                       
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 40898                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.310                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.8                               
REMARK 200  DATA REDUNDANCY                : 8.000                              
REMARK 200  R MERGE                    (I) : 0.11000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 10.0000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.31                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.35                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 96.4                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 7.30                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.39100                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER 2.6.0                                          
REMARK 200 STARTING MODEL: PDB ENTRY 4ZCW                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 48.76                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.40                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 100 MM BIS-TRIS, PH 6.5, 200 MM          
REMARK 280  AMMONIUM ACETATE, 20% W/V PEG3350, CRYO-SOAK IN SOLUTION            
REMARK 280  CONTAINING 100 MM BIS-TRIS, PH 6.5, 200 MM AMMONIUM ACETATE, 35%    
REMARK 280  W/V PEG3350, VAPOR DIFFUSION, TEMPERATURE 293K                      
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 2 21 21                        
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   X,-Y,-Z                                                 
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   -X,-Y+1/2,Z+1/2                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       56.43400            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       59.96100            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       56.43400            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       59.96100            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 4110 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 29670 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -42.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     HIS A   435                                                      
REMARK 465     HIS A   436                                                      
REMARK 465     HIS A   437                                                      
REMARK 465     HIS A   438                                                      
REMARK 465     HIS A   439                                                      
REMARK 465     HIS A   440                                                      
REMARK 465     HIS B   435                                                      
REMARK 465     HIS B   436                                                      
REMARK 465     HIS B   437                                                      
REMARK 465     HIS B   438                                                      
REMARK 465     HIS B   439                                                      
REMARK 465     HIS B   440                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   OD1  ASP A   245     OE1  GLU A   293              1.50            
REMARK 500   OH   TYR A   200     OE1  GLU A   222              2.13            
REMARK 500   OD2  ASP A    98     OG1  THR A   100              2.15            
REMARK 500   OE2  GLU B   225     OH   TYR B   287              2.19            
REMARK 500   OH   TYR B   200     OE1  GLU B   222              2.19            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    LEU A 320   CA  -  CB  -  CG  ANGL. DEV. =  14.0 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    THR A  26     -167.39   -120.59                                   
REMARK 500    SER A 141      -33.03   -134.35                                   
REMARK 500    ASN A 216       83.61    -67.01                                   
REMARK 500    PRO A 267       -6.13    -58.75                                   
REMARK 500    VAL A 322       38.87     34.41                                   
REMARK 500    THR A 395       41.53   -145.51                                   
REMARK 500    PRO A 398       47.92    -74.53                                   
REMARK 500    ARG A 400      124.64     72.37                                   
REMARK 500    VAL B 152      -39.87   -133.77                                   
REMARK 500    HIS B 158       58.29    -96.24                                   
REMARK 500    ARG B 253     -101.58   -109.29                                   
REMARK 500    LYS B 262       55.85     37.65                                   
REMARK 500    ASP B 318      -81.70   -122.37                                   
REMARK 500    VAL B 322       40.82     37.77                                   
REMARK 500    THR B 376     -168.47   -124.80                                   
REMARK 500    ARG B 400      125.65     70.78                                   
REMARK 500    ASN B 427       44.49   -100.18                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG A 501  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 245   OD1                                                    
REMARK 620 2 GLU A 293   OE1  41.6                                              
REMARK 620 3 ASP A 318   OD1 146.5 104.8                                        
REMARK 620 4 HOH A 607   O   101.2  92.8  77.2                                  
REMARK 620 5 HOH A 608   O   116.0 153.4  96.5  76.3                            
REMARK 620 6 HOH A 636   O    98.0 113.0  95.9 154.2  79.8                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG B 501  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP B 245   OD2                                                    
REMARK 620 2 GLU B 293   OE2  67.7                                              
REMARK 620 3 ASP B 318   OD1 146.9  83.5                                        
REMARK 620 4 HOH B 605   O   100.4 154.6  99.1                                  
REMARK 620 5 HOH B 604   O    80.3  70.0  74.5  86.2                            
REMARK 620 6 HOH B 638   O   113.1 119.7  95.0  85.4 165.3                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MG A 501                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 502                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MG B 501                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL B 502                  
DBREF  5TD9 A    1   434  UNP    P09104   ENOG_HUMAN       1    434             
DBREF  5TD9 B    1   434  UNP    P09104   ENOG_HUMAN       1    434             
SEQADV 5TD9 HIS A  435  UNP  P09104              EXPRESSION TAG                 
SEQADV 5TD9 HIS A  436  UNP  P09104              EXPRESSION TAG                 
SEQADV 5TD9 HIS A  437  UNP  P09104              EXPRESSION TAG                 
SEQADV 5TD9 HIS A  438  UNP  P09104              EXPRESSION TAG                 
SEQADV 5TD9 HIS A  439  UNP  P09104              EXPRESSION TAG                 
SEQADV 5TD9 HIS A  440  UNP  P09104              EXPRESSION TAG                 
SEQADV 5TD9 HIS B  435  UNP  P09104              EXPRESSION TAG                 
SEQADV 5TD9 HIS B  436  UNP  P09104              EXPRESSION TAG                 
SEQADV 5TD9 HIS B  437  UNP  P09104              EXPRESSION TAG                 
SEQADV 5TD9 HIS B  438  UNP  P09104              EXPRESSION TAG                 
SEQADV 5TD9 HIS B  439  UNP  P09104              EXPRESSION TAG                 
SEQADV 5TD9 HIS B  440  UNP  P09104              EXPRESSION TAG                 
SEQRES   1 A  440  MET SER ILE GLU LYS ILE TRP ALA ARG GLU ILE LEU ASP          
SEQRES   2 A  440  SER ARG GLY ASN PRO THR VAL GLU VAL ASP LEU TYR THR          
SEQRES   3 A  440  ALA LYS GLY LEU PHE ARG ALA ALA VAL PRO SER GLY ALA          
SEQRES   4 A  440  SER THR GLY ILE TYR GLU ALA LEU GLU LEU ARG ASP GLY          
SEQRES   5 A  440  ASP LYS GLN ARG TYR LEU GLY LYS GLY VAL LEU LYS ALA          
SEQRES   6 A  440  VAL ASP HIS ILE ASN SER THR ILE ALA PRO ALA LEU ILE          
SEQRES   7 A  440  SER SER GLY LEU SER VAL VAL GLU GLN GLU LYS LEU ASP          
SEQRES   8 A  440  ASN LEU MET LEU GLU LEU ASP GLY THR GLU ASN LYS SER          
SEQRES   9 A  440  LYS PHE GLY ALA ASN ALA ILE LEU GLY VAL SER LEU ALA          
SEQRES  10 A  440  VAL CYS LYS ALA GLY ALA ALA GLU ARG GLU LEU PRO LEU          
SEQRES  11 A  440  TYR ARG HIS ILE ALA GLN LEU ALA GLY ASN SER ASP LEU          
SEQRES  12 A  440  ILE LEU PRO VAL PRO ALA PHE ASN VAL ILE ASN GLY GLY          
SEQRES  13 A  440  SER HIS ALA GLY ASN LYS LEU ALA MET GLN GLU PHE MET          
SEQRES  14 A  440  ILE LEU PRO VAL GLY ALA GLU SER PHE ARG ASP ALA MET          
SEQRES  15 A  440  ARG LEU GLY ALA GLU VAL TYR HIS THR LEU LYS GLY VAL          
SEQRES  16 A  440  ILE LYS ASP LYS TYR GLY LYS ASP ALA THR ASN VAL GLY          
SEQRES  17 A  440  ASP GLU GLY GLY PHE ALA PRO ASN ILE LEU GLU ASN SER          
SEQRES  18 A  440  GLU ALA LEU GLU LEU VAL LYS GLU ALA ILE ASP LYS ALA          
SEQRES  19 A  440  GLY TYR THR GLU LYS ILE VAL ILE GLY MET ASP VAL ALA          
SEQRES  20 A  440  ALA SER GLU PHE TYR ARG ASP GLY LYS TYR ASP LEU ASP          
SEQRES  21 A  440  PHE LYS SER PRO THR ASP PRO SER ARG TYR ILE THR GLY          
SEQRES  22 A  440  ASP GLN LEU GLY ALA LEU TYR GLN ASP PHE VAL ARG ASP          
SEQRES  23 A  440  TYR PRO VAL VAL SER ILE GLU ASP PRO PHE ASP GLN ASP          
SEQRES  24 A  440  ASP TRP ALA ALA TRP SER LYS PHE THR ALA ASN VAL GLY          
SEQRES  25 A  440  ILE GLN ILE VAL GLY ASP ASP LEU THR VAL THR ASN PRO          
SEQRES  26 A  440  LYS ARG ILE GLU ARG ALA VAL GLU GLU LYS ALA CYS ASN          
SEQRES  27 A  440  CYS LEU LEU LEU LYS VAL ASN GLN ILE GLY SER VAL THR          
SEQRES  28 A  440  GLU ALA ILE GLN ALA CYS LYS LEU ALA GLN GLU ASN GLY          
SEQRES  29 A  440  TRP GLY VAL MET VAL SER HIS ARG SER GLY GLU THR GLU          
SEQRES  30 A  440  ASP THR PHE ILE ALA ASP LEU VAL VAL GLY LEU CYS THR          
SEQRES  31 A  440  GLY GLN ILE LYS THR GLY ALA PRO CYS ARG SER GLU ARG          
SEQRES  32 A  440  LEU ALA LYS TYR ASN GLN LEU MET ARG ILE GLU GLU GLU          
SEQRES  33 A  440  LEU GLY ASP GLU ALA ARG PHE ALA GLY HIS ASN PHE ARG          
SEQRES  34 A  440  ASN PRO SER VAL LEU HIS HIS HIS HIS HIS HIS                  
SEQRES   1 B  440  MET SER ILE GLU LYS ILE TRP ALA ARG GLU ILE LEU ASP          
SEQRES   2 B  440  SER ARG GLY ASN PRO THR VAL GLU VAL ASP LEU TYR THR          
SEQRES   3 B  440  ALA LYS GLY LEU PHE ARG ALA ALA VAL PRO SER GLY ALA          
SEQRES   4 B  440  SER THR GLY ILE TYR GLU ALA LEU GLU LEU ARG ASP GLY          
SEQRES   5 B  440  ASP LYS GLN ARG TYR LEU GLY LYS GLY VAL LEU LYS ALA          
SEQRES   6 B  440  VAL ASP HIS ILE ASN SER THR ILE ALA PRO ALA LEU ILE          
SEQRES   7 B  440  SER SER GLY LEU SER VAL VAL GLU GLN GLU LYS LEU ASP          
SEQRES   8 B  440  ASN LEU MET LEU GLU LEU ASP GLY THR GLU ASN LYS SER          
SEQRES   9 B  440  LYS PHE GLY ALA ASN ALA ILE LEU GLY VAL SER LEU ALA          
SEQRES  10 B  440  VAL CYS LYS ALA GLY ALA ALA GLU ARG GLU LEU PRO LEU          
SEQRES  11 B  440  TYR ARG HIS ILE ALA GLN LEU ALA GLY ASN SER ASP LEU          
SEQRES  12 B  440  ILE LEU PRO VAL PRO ALA PHE ASN VAL ILE ASN GLY GLY          
SEQRES  13 B  440  SER HIS ALA GLY ASN LYS LEU ALA MET GLN GLU PHE MET          
SEQRES  14 B  440  ILE LEU PRO VAL GLY ALA GLU SER PHE ARG ASP ALA MET          
SEQRES  15 B  440  ARG LEU GLY ALA GLU VAL TYR HIS THR LEU LYS GLY VAL          
SEQRES  16 B  440  ILE LYS ASP LYS TYR GLY LYS ASP ALA THR ASN VAL GLY          
SEQRES  17 B  440  ASP GLU GLY GLY PHE ALA PRO ASN ILE LEU GLU ASN SER          
SEQRES  18 B  440  GLU ALA LEU GLU LEU VAL LYS GLU ALA ILE ASP LYS ALA          
SEQRES  19 B  440  GLY TYR THR GLU LYS ILE VAL ILE GLY MET ASP VAL ALA          
SEQRES  20 B  440  ALA SER GLU PHE TYR ARG ASP GLY LYS TYR ASP LEU ASP          
SEQRES  21 B  440  PHE LYS SER PRO THR ASP PRO SER ARG TYR ILE THR GLY          
SEQRES  22 B  440  ASP GLN LEU GLY ALA LEU TYR GLN ASP PHE VAL ARG ASP          
SEQRES  23 B  440  TYR PRO VAL VAL SER ILE GLU ASP PRO PHE ASP GLN ASP          
SEQRES  24 B  440  ASP TRP ALA ALA TRP SER LYS PHE THR ALA ASN VAL GLY          
SEQRES  25 B  440  ILE GLN ILE VAL GLY ASP ASP LEU THR VAL THR ASN PRO          
SEQRES  26 B  440  LYS ARG ILE GLU ARG ALA VAL GLU GLU LYS ALA CYS ASN          
SEQRES  27 B  440  CYS LEU LEU LEU LYS VAL ASN GLN ILE GLY SER VAL THR          
SEQRES  28 B  440  GLU ALA ILE GLN ALA CYS LYS LEU ALA GLN GLU ASN GLY          
SEQRES  29 B  440  TRP GLY VAL MET VAL SER HIS ARG SER GLY GLU THR GLU          
SEQRES  30 B  440  ASP THR PHE ILE ALA ASP LEU VAL VAL GLY LEU CYS THR          
SEQRES  31 B  440  GLY GLN ILE LYS THR GLY ALA PRO CYS ARG SER GLU ARG          
SEQRES  32 B  440  LEU ALA LYS TYR ASN GLN LEU MET ARG ILE GLU GLU GLU          
SEQRES  33 B  440  LEU GLY ASP GLU ALA ARG PHE ALA GLY HIS ASN PHE ARG          
SEQRES  34 B  440  ASN PRO SER VAL LEU HIS HIS HIS HIS HIS HIS                  
HET     MG  A 501       1                                                       
HET     CL  A 502       1                                                       
HET     MG  B 501       1                                                       
HET     CL  B 502       1                                                       
HETNAM      MG MAGNESIUM ION                                                    
HETNAM      CL CHLORIDE ION                                                     
FORMUL   3   MG    2(MG 2+)                                                     
FORMUL   4   CL    2(CL 1-)                                                     
FORMUL   7  HOH   *86(H2 O)                                                     
HELIX    1 AA1 ARG A   56  LYS A   60  5                                   5    
HELIX    2 AA2 VAL A   62  THR A   72  1                                  11    
HELIX    3 AA3 THR A   72  SER A   80  1                                   9    
HELIX    4 AA4 GLU A   86  GLY A   99  1                                  14    
HELIX    5 AA5 GLY A  107  ARG A  126  1                                  20    
HELIX    6 AA6 PRO A  129  ALA A  138  1                                  10    
HELIX    7 AA7 GLY A  156  ALA A  159  5                                   4    
HELIX    8 AA8 SER A  177  GLY A  201  1                                  25    
HELIX    9 AA9 LYS A  202  THR A  205  5                                   4    
HELIX   10 AB1 GLU A  219  GLY A  235  1                                  17    
HELIX   11 AB2 ALA A  247  GLU A  250  5                                   4    
HELIX   12 AB3 THR A  272  TYR A  287  1                                  16    
HELIX   13 AB4 ASP A  300  VAL A  311  1                                  12    
HELIX   14 AB5 ASN A  324  GLU A  334  1                                  11    
HELIX   15 AB6 LYS A  343  GLY A  348  1                                   6    
HELIX   16 AB7 SER A  349  ASN A  363  1                                  15    
HELIX   17 AB8 THR A  379  LEU A  388  1                                  10    
HELIX   18 AB9 ARG A  400  GLY A  418  1                                  19    
HELIX   19 AC1 ASP A  419  ALA A  421  5                                   3    
HELIX   20 AC2 ALA A  424  PHE A  428  5                                   5    
HELIX   21 AC3 ASN A  430  LEU A  434  5                                   5    
HELIX   22 AC4 ARG B   56  LYS B   60  5                                   5    
HELIX   23 AC5 VAL B   62  THR B   72  1                                  11    
HELIX   24 AC6 THR B   72  GLY B   81  1                                  10    
HELIX   25 AC7 GLU B   86  GLY B   99  1                                  14    
HELIX   26 AC8 GLY B  107  ARG B  126  1                                  20    
HELIX   27 AC9 PRO B  129  ALA B  138  1                                  10    
HELIX   28 AD1 GLY B  156  ALA B  159  5                                   4    
HELIX   29 AD2 SER B  177  GLY B  201  1                                  25    
HELIX   30 AD3 LYS B  202  THR B  205  5                                   4    
HELIX   31 AD4 GLU B  219  ALA B  234  1                                  16    
HELIX   32 AD5 ALA B  247  TYR B  252  5                                   6    
HELIX   33 AD6 ASP B  266  TYR B  270  5                                   5    
HELIX   34 AD7 THR B  272  TYR B  287  1                                  16    
HELIX   35 AD8 ASP B  300  ASN B  310  1                                  11    
HELIX   36 AD9 ASN B  324  GLU B  334  1                                  11    
HELIX   37 AE1 LYS B  343  GLY B  348  1                                   6    
HELIX   38 AE2 SER B  349  ASN B  363  1                                  15    
HELIX   39 AE3 THR B  379  LEU B  388  1                                  10    
HELIX   40 AE4 ARG B  400  GLY B  418  1                                  19    
HELIX   41 AE5 ASP B  419  ALA B  421  5                                   3    
HELIX   42 AE6 ALA B  424  PHE B  428  5                                   5    
HELIX   43 AE7 ASN B  430  LEU B  434  5                                   5    
SHEET    1 AA1 3 LYS A   5  LEU A  12  0                                        
SHEET    2 AA1 3 PRO A  18  THR A  26 -1  O  TYR A  25   N  LYS A   5           
SHEET    3 AA1 3 GLY A  29  ALA A  34 -1  O  ALA A  33   N  VAL A  22           
SHEET    1 AA2 9 VAL A 147  PRO A 148  0                                        
SHEET    2 AA2 9 GLN A 392  LYS A 394  1  O  ILE A 393   N  VAL A 147           
SHEET    3 AA2 9 GLY A 366  SER A 370  1  N  VAL A 369   O  LYS A 394           
SHEET    4 AA2 9 CYS A 339  LEU A 342  1  N  LEU A 340   O  MET A 368           
SHEET    5 AA2 9 GLN A 314  GLY A 317  1  N  GLY A 317   O  CYS A 339           
SHEET    6 AA2 9 VAL A 289  GLU A 293  1  N  VAL A 290   O  GLN A 314           
SHEET    7 AA2 9 VAL A 241  ASP A 245  1  N  MET A 244   O  SER A 291           
SHEET    8 AA2 9 GLU A 167  LEU A 171 -1  N  MET A 169   O  GLY A 243           
SHEET    9 AA2 9 PHE A 150  ASN A 154 -1  N  ILE A 153   O  PHE A 168           
SHEET    1 AA3 2 TYR A 252  ARG A 253  0                                        
SHEET    2 AA3 2 LYS A 256  TYR A 257 -1  O  LYS A 256   N  ARG A 253           
SHEET    1 AA4 3 LYS B   5  LEU B  12  0                                        
SHEET    2 AA4 3 PRO B  18  THR B  26 -1  O  ASP B  23   N  TRP B   7           
SHEET    3 AA4 3 GLY B  29  ALA B  34 -1  O  ALA B  33   N  VAL B  22           
SHEET    1 AA5 9 VAL B 147  PRO B 148  0                                        
SHEET    2 AA5 9 GLN B 392  LYS B 394  1  O  ILE B 393   N  VAL B 147           
SHEET    3 AA5 9 GLY B 366  SER B 370  1  N  VAL B 369   O  LYS B 394           
SHEET    4 AA5 9 CYS B 339  LEU B 342  1  N  LEU B 340   O  GLY B 366           
SHEET    5 AA5 9 GLN B 314  GLY B 317  1  N  GLY B 317   O  CYS B 339           
SHEET    6 AA5 9 VAL B 289  GLU B 293  1  N  ILE B 292   O  VAL B 316           
SHEET    7 AA5 9 VAL B 241  ASP B 245  1  N  MET B 244   O  GLU B 293           
SHEET    8 AA5 9 GLU B 167  LEU B 171 -1  N  MET B 169   O  GLY B 243           
SHEET    9 AA5 9 PHE B 150  ASN B 154 -1  N  VAL B 152   O  PHE B 168           
LINK         OD1 ASP A 245                MG    MG A 501     1555   1555  2.14  
LINK         OE1 GLU A 293                MG    MG A 501     1555   1555  2.08  
LINK         OD1 ASP A 318                MG    MG A 501     1555   1555  2.10  
LINK         OD2 ASP B 245                MG    MG B 501     1555   1555  2.15  
LINK         OE2 GLU B 293                MG    MG B 501     1555   1555  1.98  
LINK         OD1 ASP B 318                MG    MG B 501     1555   1555  2.12  
LINK        MG    MG A 501                 O   HOH A 607     1555   1555  2.21  
LINK        MG    MG A 501                 O   HOH A 608     1555   1555  2.21  
LINK        MG    MG A 501                 O   HOH A 636     1555   1555  2.18  
LINK        MG    MG B 501                 O   HOH B 605     1555   1555  2.12  
LINK        MG    MG B 501                 O   HOH B 604     1555   1555  2.36  
LINK        MG    MG B 501                 O   HOH B 638     1555   1555  2.37  
SITE     1 AC1  6 ASP A 245  GLU A 293  ASP A 318  HOH A 607                    
SITE     2 AC1  6 HOH A 608  HOH A 636                                          
SITE     1 AC2  2 LYS A 343  SER A 373                                          
SITE     1 AC3  6 ASP B 245  GLU B 293  ASP B 318  HOH B 604                    
SITE     2 AC3  6 HOH B 605  HOH B 638                                          
SITE     1 AC4  2 ARG B 372  SER B 373                                          
CRYST1   68.319  112.868  119.922  90.00  90.00  90.00 P 2 21 21     8          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.014637  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.008860  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.008339        0.00000                         
ATOM      1  N   MET A   1      92.784  45.792 -80.487  1.00104.01           N  
ANISOU    1  N   MET A   1    12366  16510  10643  -2625   -435  -2108       N  
ATOM      2  CA  MET A   1      92.409  46.018 -79.099  1.00103.89           C  
ANISOU    2  CA  MET A   1    12437  16629  10407  -2632   -517  -2284       C  
ATOM      3  C   MET A   1      91.658  44.803 -78.559  1.00 95.51           C  
ANISOU    3  C   MET A   1    11255  15801   9232  -2341   -566  -2127       C  
ATOM      4  O   MET A   1      91.965  43.668 -78.917  1.00 93.58           O  
ANISOU    4  O   MET A   1    10768  15742   9047  -2230   -614  -1909       O  
ATOM      5  CB  MET A   1      91.564  47.289 -78.973  1.00109.92           C  
ANISOU    5  CB  MET A   1    13575  17038  11150  -2637   -392  -2492       C  
ATOM      6  CG  MET A   1      91.775  48.053 -77.674  1.00118.58           C  
ANISOU    6  CG  MET A   1    14796  18213  12045  -2839   -467  -2780       C  
ATOM      7  SD  MET A   1      91.186  49.756 -77.754  1.00125.96           S  
ANISOU    7  SD  MET A   1    16185  18655  13020  -2928   -302  -3053       S  
ATOM      8  CE  MET A   1      89.445  49.513 -78.103  1.00124.94           C  
ANISOU    8  CE  MET A   1    16221  18325  12926  -2474   -146  -2928       C  
ATOM      9  N   SER A   2      90.664  45.043 -77.711  1.00 91.05           N  
ANISOU    9  N   SER A   2    10870  15217   8507  -2218   -539  -2239       N  
ATOM     10  CA  SER A   2      89.983  43.958 -77.027  1.00 80.25           C  
ANISOU   10  CA  SER A   2     9398  14094   6999  -1987   -586  -2109       C  
ATOM     11  C   SER A   2      88.968  43.274 -77.944  1.00 67.59           C  
ANISOU   11  C   SER A   2     7803  12350   5529  -1700   -467  -1895       C  
ATOM     12  O   SER A   2      88.495  43.840 -78.935  1.00 55.26           O  
ANISOU   12  O   SER A   2     6392  10480   4124  -1644   -337  -1889       O  
ATOM     13  CB  SER A   2      89.291  44.480 -75.766  1.00 82.89           C  
ANISOU   13  CB  SER A   2     9917  14482   7097  -1974   -584  -2316       C  
ATOM     14  OG  SER A   2      88.713  43.426 -75.016  1.00 84.96           O  
ANISOU   14  OG  SER A   2    10071  14956   7253  -1762   -617  -2154       O  
ATOM     15  N   ILE A   3      88.652  42.028 -77.602  1.00 65.03           N  
ANISOU   15  N   ILE A   3     7313  12260   5134  -1528   -519  -1711       N  
ATOM     16  CA  ILE A   3      87.565  41.291 -78.236  1.00 54.25           C  
ANISOU   16  CA  ILE A   3     5955  10808   3849  -1268   -419  -1527       C  
ATOM     17  C   ILE A   3      86.252  41.766 -77.629  1.00 58.91           C  
ANISOU   17  C   ILE A   3     6743  11324   4318  -1128   -325  -1640       C  
ATOM     18  O   ILE A   3      86.034  41.634 -76.420  1.00 64.30           O  
ANISOU   18  O   ILE A   3     7430  12214   4788  -1125   -375  -1715       O  
ATOM     19  CB  ILE A   3      87.738  39.778 -78.046  1.00 50.18           C  
ANISOU   19  CB  ILE A   3     5207  10553   3305  -1157   -502  -1294       C  
ATOM     20  CG1 ILE A   3      89.098  39.326 -78.575  1.00 50.25           C  
ANISOU   20  CG1 ILE A   3     5004  10655   3435  -1276   -590  -1196       C  
ATOM     21  CG2 ILE A   3      86.596  39.020 -78.714  1.00 52.04           C  
ANISOU   21  CG2 ILE A   3     5459  10692   3623   -923   -397  -1121       C  
ATOM     22  CD1 ILE A   3      89.348  37.848 -78.421  1.00 49.31           C  
ANISOU   22  CD1 ILE A   3     4667  10759   3308  -1149   -667   -964       C  
ATOM     23  N   GLU A   4      85.374  42.318 -78.464  1.00 51.69           N  
ANISOU   23  N   GLU A   4     5984  10127   3529  -1005   -187  -1648       N  
ATOM     24  CA  GLU A   4      84.121  42.865 -77.962  1.00 57.05           C  
ANISOU   24  CA  GLU A   4     6838  10722   4116   -851    -82  -1763       C  
ATOM     25  C   GLU A   4      83.021  41.814 -77.868  1.00 58.74           C  
ANISOU   25  C   GLU A   4     6955  11076   4286   -623    -42  -1590       C  
ATOM     26  O   GLU A   4      82.246  41.818 -76.906  1.00 58.46           O  
ANISOU   26  O   GLU A   4     6966  11163   4084   -533     -4  -1665       O  
ATOM     27  CB  GLU A   4      83.660  44.030 -78.843  1.00 56.98           C  
ANISOU   27  CB  GLU A   4     7046  10345   4260   -807     43  -1852       C  
ATOM     28  CG  GLU A   4      84.710  45.117 -79.057  1.00 64.97           C  
ANISOU   28  CG  GLU A   4     8181  11169   5337  -1054     24  -2014       C  
ATOM     29  CD  GLU A   4      85.145  45.819 -77.773  1.00 81.00           C  
ANISOU   29  CD  GLU A   4    10312  13283   7181  -1229    -24  -2275       C  
ATOM     30  OE1 GLU A   4      84.475  45.671 -76.726  1.00 87.40           O  
ANISOU   30  OE1 GLU A   4    11149  14254   7806  -1129    -15  -2358       O  
ATOM     31  OE2 GLU A   4      86.170  46.534 -77.817  1.00 83.92           O  
ANISOU   31  OE2 GLU A   4    10737  13566   7583  -1485    -69  -2406       O  
ATOM     32  N   LYS A   5      82.939  40.908 -78.839  1.00 52.55           N  
ANISOU   32  N   LYS A   5     6042  10282   3644   -542    -41  -1367       N  
ATOM     33  CA  LYS A   5      81.920  39.870 -78.808  1.00 52.50           C  
ANISOU   33  CA  LYS A   5     5941  10398   3607   -359     -3  -1200       C  
ATOM     34  C   LYS A   5      82.393  38.688 -79.639  1.00 46.79           C  
ANISOU   34  C   LYS A   5     5049   9722   3007   -359    -53   -974       C  
ATOM     35  O   LYS A   5      83.085  38.858 -80.647  1.00 46.68           O  
ANISOU   35  O   LYS A   5     5025   9563   3148   -431    -60   -940       O  
ATOM     36  CB  LYS A   5      80.571  40.382 -79.335  1.00 50.80           C  
ANISOU   36  CB  LYS A   5     5838  10008   3456   -174    130  -1218       C  
ATOM     37  CG  LYS A   5      79.460  39.341 -79.316  1.00 52.07           C  
ANISOU   37  CG  LYS A   5     5887  10310   3587    -11    174  -1056       C  
ATOM     38  CD  LYS A   5      78.182  39.845 -79.970  1.00 48.95           C  
ANISOU   38  CD  LYS A   5     5561   9761   3275    172    289  -1058       C  
ATOM     39  CE  LYS A   5      77.649  41.084 -79.274  1.00 51.23           C  
ANISOU   39  CE  LYS A   5     6015   9967   3483    241    374  -1279       C  
ATOM     40  NZ  LYS A   5      76.274  41.417 -79.741  1.00 56.25           N  
ANISOU   40  NZ  LYS A   5     6673  10517   4182    464    486  -1258       N  
ATOM     41  N   ILE A   6      82.017  37.491 -79.200  1.00 43.16           N  
ANISOU   41  N   ILE A   6     4468   9442   2488   -281    -76   -818       N  
ATOM     42  CA  ILE A   6      82.208  36.268 -79.969  1.00 47.93           C  
ANISOU   42  CA  ILE A   6     4937  10058   3215   -244    -95   -602       C  
ATOM     43  C   ILE A   6      80.869  35.542 -80.033  1.00 52.68           C  
ANISOU   43  C   ILE A   6     5523  10622   3872    -96    -19   -478       C  
ATOM     44  O   ILE A   6      80.276  35.236 -78.992  1.00 41.15           O  
ANISOU   44  O   ILE A   6     4053   9236   2348    -54    -10   -463       O  
ATOM     45  CB  ILE A   6      83.288  35.360 -79.360  1.00 48.34           C  
ANISOU   45  CB  ILE A   6     4845  10259   3262   -314   -207   -497       C  
ATOM     46  CG1 ILE A   6      84.651  36.054 -79.397  1.00 52.69           C  
ANISOU   46  CG1 ILE A   6     5371  10868   3780   -481   -296   -615       C  
ATOM     47  CG2 ILE A   6      83.346  34.037 -80.104  1.00 42.65           C  
ANISOU   47  CG2 ILE A   6     4010   9530   2663   -247   -202   -283       C  
ATOM     48  CD1 ILE A   6      85.787  35.202 -78.874  1.00 52.09           C  
ANISOU   48  CD1 ILE A   6     5123  10954   3714   -531   -412   -501       C  
ATOM     49  N   TRP A   7      80.391  35.269 -81.247  1.00 47.48           N  
ANISOU   49  N   TRP A   7     4858   9858   3323    -34     35   -393       N  
ATOM     50  CA  TRP A   7      79.183  34.478 -81.434  1.00 45.70           C  
ANISOU   50  CA  TRP A   7     4592   9608   3165     72     90   -270       C  
ATOM     51  C   TRP A   7      79.442  33.374 -82.448  1.00 41.35           C  
ANISOU   51  C   TRP A   7     3962   9012   2737     63     79   -109       C  
ATOM     52  O   TRP A   7      79.891  33.644 -83.566  1.00 43.08           O  
ANISOU   52  O   TRP A   7     4206   9153   3012     37     90   -113       O  
ATOM     53  CB  TRP A   7      77.993  35.338 -81.879  1.00 41.10           C  
ANISOU   53  CB  TRP A   7     4091   8944   2581    177    177   -347       C  
ATOM     54  CG  TRP A   7      76.746  34.531 -82.015  1.00 50.74           C  
ANISOU   54  CG  TRP A   7     5239  10176   3864    262    217   -229       C  
ATOM     55  CD1 TRP A   7      76.107  34.196 -83.172  1.00 51.44           C  
ANISOU   55  CD1 TRP A   7     5299  10196   4049    308    243   -142       C  
ATOM     56  CD2 TRP A   7      76.002  33.920 -80.955  1.00 60.07           C  
ANISOU   56  CD2 TRP A   7     6362  11460   5002    287    230   -186       C  
ATOM     57  NE1 TRP A   7      75.000  33.426 -82.898  1.00 51.25           N  
ANISOU   57  NE1 TRP A   7     5194  10232   4047    350    265    -58       N  
ATOM     58  CE2 TRP A   7      74.914  33.243 -81.543  1.00 57.76           C  
ANISOU   58  CE2 TRP A   7     5999  11159   4787    338    264    -80       C  
ATOM     59  CE3 TRP A   7      76.144  33.887 -79.564  1.00 59.74           C  
ANISOU   59  CE3 TRP A   7     6322  11527   4850    259    217   -227       C  
ATOM     60  CZ2 TRP A   7      73.979  32.540 -80.788  1.00 56.78           C  
ANISOU   60  CZ2 TRP A   7     5803  11132   4637    353    290    -16       C  
ATOM     61  CZ3 TRP A   7      75.212  33.189 -78.818  1.00 55.43           C  
ANISOU   61  CZ3 TRP A   7     5715  11071   4275    286    249   -155       C  
ATOM     62  CH2 TRP A   7      74.146  32.525 -79.431  1.00 54.20           C  
ANISOU   62  CH2 TRP A   7     5487  10904   4202    329    288    -51       C  
ATOM     63  N   ALA A   8      79.148  32.137 -82.055  1.00 42.02           N  
ANISOU   63  N   ALA A   8     3968   9145   2853     79     69     26       N  
ATOM     64  CA  ALA A   8      79.322  30.958 -82.885  1.00 34.97           C  
ANISOU   64  CA  ALA A   8     3017   8208   2063     74     69    171       C  
ATOM     65  C   ALA A   8      77.970  30.409 -83.310  1.00 44.30           C  
ANISOU   65  C   ALA A   8     4193   9335   3304    121    122    236       C  
ATOM     66  O   ALA A   8      76.932  30.715 -82.719  1.00 36.95           O  
ANISOU   66  O   ALA A   8     3267   8443   2329    164    152    200       O  
ATOM     67  CB  ALA A   8      80.106  29.870 -82.143  1.00 37.41           C  
ANISOU   67  CB  ALA A   8     3252   8612   2350     51     15    284       C  
ATOM     68  N   ARG A   9      77.992  29.586 -84.352  1.00 42.55           N  
ANISOU   68  N   ARG A   9     3955   9038   3173    106    134    325       N  
ATOM     69  CA  ARG A   9      76.762  28.975 -84.834  1.00 33.00           C  
ANISOU   69  CA  ARG A   9     2733   7792   2014    119    170    384       C  
ATOM     70  C   ARG A   9      77.116  27.721 -85.614  1.00 38.54           C  
ANISOU   70  C   ARG A   9     3425   8433   2787     75    175    492       C  
ATOM     71  O   ARG A   9      78.287  27.431 -85.879  1.00 37.61           O  
ANISOU   71  O   ARG A   9     3307   8300   2685     58    161    520       O  
ATOM     72  CB  ARG A   9      75.947  29.950 -85.692  1.00 32.70           C  
ANISOU   72  CB  ARG A   9     2729   7702   1993    164    198    310       C  
ATOM     73  CG  ARG A   9      76.533  30.191 -87.073  1.00 43.27           C  
ANISOU   73  CG  ARG A   9     4114   8936   3390    141    203    303       C  
ATOM     74  CD  ARG A   9      75.797  31.298 -87.814  1.00 35.43           C  
ANISOU   74  CD  ARG A   9     3169   7910   2385    202    226    243       C  
ATOM     75  NE  ARG A   9      76.692  32.399 -88.156  1.00 48.17           N  
ANISOU   75  NE  ARG A   9     4864   9470   3968    199    234    165       N  
ATOM     76  CZ  ARG A   9      76.658  33.612 -87.609  1.00 50.35           C  
ANISOU   76  CZ  ARG A   9     5199   9767   4164    249    249     61       C  
ATOM     77  NH1 ARG A   9      75.764  33.912 -86.685  1.00 49.82           N  
ANISOU   77  NH1 ARG A   9     5112   9774   4043    327    265     17       N  
ATOM     78  NH2 ARG A   9      77.524  34.530 -88.002  1.00 58.89           N  
ANISOU   78  NH2 ARG A   9     6370  10728   5277    212    247     -9       N  
ATOM     79  N   GLU A  10      76.076  26.977 -85.964  1.00 36.44           N  
ANISOU   79  N   GLU A  10     3148   8147   2551     54    200    549       N  
ATOM     80  CA  GLU A  10      76.182  25.781 -86.784  1.00 37.83           C  
ANISOU   80  CA  GLU A  10     3341   8251   2782      0    222    634       C  
ATOM     81  C   GLU A  10      75.988  26.150 -88.249  1.00 38.00           C  
ANISOU   81  C   GLU A  10     3398   8185   2856    -16    236    584       C  
ATOM     82  O   GLU A  10      75.125  26.966 -88.582  1.00 49.63           O  
ANISOU   82  O   GLU A  10     4862   9675   4319     10    231    528       O  
ATOM     83  CB  GLU A  10      75.113  24.773 -86.354  1.00 45.55           C  
ANISOU   83  CB  GLU A  10     4298   9266   3744    -47    244    715       C  
ATOM     84  CG  GLU A  10      75.473  23.305 -86.436  1.00 47.08           C  
ANISOU   84  CG  GLU A  10     4525   9411   3953   -103    276    836       C  
ATOM     85  CD  GLU A  10      74.425  22.441 -85.755  1.00 47.31           C  
ANISOU   85  CD  GLU A  10     4540   9490   3946   -167    303    918       C  
ATOM     86  OE1 GLU A  10      73.252  22.863 -85.707  1.00 52.65           O  
ANISOU   86  OE1 GLU A  10     5167  10231   4606   -186    304    870       O  
ATOM     87  OE2 GLU A  10      74.768  21.350 -85.255  1.00 45.89           O  
ANISOU   87  OE2 GLU A  10     4395   9293   3747   -195    330   1041       O  
ATOM     88  N   ILE A  11      76.803  25.559 -89.122  1.00 34.80           N  
ANISOU   88  N   ILE A  11     3031   7699   2493    -49    261    611       N  
ATOM     89  CA  ILE A  11      76.595  25.613 -90.565  1.00 33.07           C  
ANISOU   89  CA  ILE A  11     2858   7397   2309    -87    284    578       C  
ATOM     90  C   ILE A  11      76.820  24.215 -91.125  1.00 30.51           C  
ANISOU   90  C   ILE A  11     2569   7010   2011   -152    336    641       C  
ATOM     91  O   ILE A  11      77.186  23.285 -90.406  1.00 37.92           O  
ANISOU   91  O   ILE A  11     3499   7964   2947   -153    359    722       O  
ATOM     92  CB  ILE A  11      77.515  26.627 -91.282  1.00 29.86           C  
ANISOU   92  CB  ILE A  11     2488   6941   1916    -65    289    511       C  
ATOM     93  CG1 ILE A  11      78.964  26.143 -91.242  1.00 29.93           C  
ANISOU   93  CG1 ILE A  11     2488   6934   1950    -68    322    537       C  
ATOM     94  CG2 ILE A  11      77.369  28.024 -90.690  1.00 35.66           C  
ANISOU   94  CG2 ILE A  11     3214   7725   2611     -8    256    446       C  
ATOM     95  CD1 ILE A  11      79.940  27.078 -91.923  1.00 36.81           C  
ANISOU   95  CD1 ILE A  11     3377   7773   2834    -74    344    474       C  
ATOM     96  N   LEU A  12      76.573  24.071 -92.422  1.00 30.32           N  
ANISOU   96  N   LEU A  12     2597   6923   2002   -208    363    608       N  
ATOM     97  CA  LEU A  12      76.768  22.809 -93.117  1.00 33.35           C  
ANISOU   97  CA  LEU A  12     3035   7238   2398   -283    435    640       C  
ATOM     98  C   LEU A  12      78.040  22.877 -93.949  1.00 41.52           C  
ANISOU   98  C   LEU A  12     4115   8178   3482   -261    487    600       C  
ATOM     99  O   LEU A  12      78.282  23.870 -94.644  1.00 30.07           O  
ANISOU   99  O   LEU A  12     2680   6727   2019   -251    477    538       O  
ATOM    100  CB  LEU A  12      75.562  22.485 -94.004  1.00 45.58           C  
ANISOU  100  CB  LEU A  12     4610   8795   3912   -387    431    615       C  
ATOM    101  CG  LEU A  12      74.256  22.207 -93.253  1.00 31.59           C  
ANISOU  101  CG  LEU A  12     2772   7122   2108   -431    395    657       C  
ATOM    102  CD1 LEU A  12      73.192  21.668 -94.197  1.00 32.25           C  
ANISOU  102  CD1 LEU A  12     2865   7244   2147   -568    399    638       C  
ATOM    103  CD2 LEU A  12      74.492  21.244 -92.100  1.00 32.18           C  
ANISOU  103  CD2 LEU A  12     2842   7193   2191   -438    434    751       C  
ATOM    104  N   ASP A  13      78.854  21.828 -93.860  1.00 35.73           N  
ANISOU  104  N   ASP A  13     3409   7338   2830   -245    540    636       N  
ATOM    105  CA  ASP A  13      80.072  21.738 -94.651  1.00 33.86           C  
ANISOU  105  CA  ASP A  13     3201   6992   2670   -213    600    590       C  
ATOM    106  C   ASP A  13      79.715  21.254 -96.054  1.00 35.21           C  
ANISOU  106  C   ASP A  13     3479   7066   2835   -303    663    522       C  
ATOM    107  O   ASP A  13      78.541  21.101 -96.406  1.00 31.58           O  
ANISOU  107  O   ASP A  13     3056   6638   2305   -396    639    510       O  
ATOM    108  CB  ASP A  13      81.101  20.847 -93.950  1.00 32.04           C  
ANISOU  108  CB  ASP A  13     2941   6699   2535   -125    631    661       C  
ATOM    109  CG  ASP A  13      80.672  19.385 -93.858  1.00 35.24           C  
ANISOU  109  CG  ASP A  13     3425   6985   2978   -153    681    722       C  
ATOM    110  OD1 ASP A  13      79.542  19.047 -94.268  1.00 47.28           O  
ANISOU  110  OD1 ASP A  13     5017   8494   4451   -266    687    702       O  
ATOM    111  OD2 ASP A  13      81.472  18.567 -93.354  1.00 35.81           O  
ANISOU  111  OD2 ASP A  13     3491   6979   3135    -63    711    796       O  
ATOM    112  N   SER A  14      80.740  20.990 -96.866  1.00 31.94           N  
ANISOU  112  N   SER A  14     3106   6546   2484   -282    747    472       N  
ATOM    113  CA  SER A  14      80.559  20.658 -98.271  1.00 32.39           C  
ANISOU  113  CA  SER A  14     3276   6521   2511   -369    816    386       C  
ATOM    114  C   SER A  14      79.885  19.312 -98.486  1.00 33.36           C  
ANISOU  114  C   SER A  14     3497   6538   2642   -450    857    379       C  
ATOM    115  O   SER A  14      79.525  18.995 -99.623  1.00 42.01           O  
ANISOU  115  O   SER A  14     4697   7581   3683   -553    900    295       O  
ATOM    116  CB  SER A  14      81.913  20.678 -98.982  1.00 40.31           C  
ANISOU  116  CB  SER A  14     4289   7447   3580   -316    918    330       C  
ATOM    117  OG  SER A  14      82.757  19.630 -98.534  1.00 33.82           O  
ANISOU  117  OG  SER A  14     3451   6519   2880   -223    990    362       O  
ATOM    118  N   ARG A  15      79.704  18.516 -97.437  1.00 40.86           N  
ANISOU  118  N   ARG A  15     4427   7452   3644   -422    847    466       N  
ATOM    119  CA  ARG A  15      79.015  17.241 -97.551  1.00 41.91           C  
ANISOU  119  CA  ARG A  15     4667   7466   3790   -522    890    469       C  
ATOM    120  C   ARG A  15      77.629  17.256 -96.927  1.00 40.70           C  
ANISOU  120  C   ARG A  15     4474   7431   3558   -627    807    525       C  
ATOM    121  O   ARG A  15      76.959  16.218 -96.919  1.00 41.73           O  
ANISOU  121  O   ARG A  15     4684   7476   3695   -742    837    536       O  
ATOM    122  CB  ARG A  15      79.860  16.133 -96.919  1.00 50.46           C  
ANISOU  122  CB  ARG A  15     5787   8382   5004   -417    965    540       C  
ATOM    123  CG  ARG A  15      81.181  15.916 -97.630  1.00 59.12           C  
ANISOU  123  CG  ARG A  15     6915   9354   6192   -310   1071    475       C  
ATOM    124  CD  ARG A  15      82.212  15.296 -96.709  1.00 62.96           C  
ANISOU  124  CD  ARG A  15     7353   9758   6810   -132   1102    583       C  
ATOM    125  NE  ARG A  15      81.793  13.991 -96.214  1.00 69.19           N  
ANISOU  125  NE  ARG A  15     8255  10378   7655   -148   1140    662       N  
ATOM    126  CZ  ARG A  15      82.497  13.259 -95.359  1.00 78.65           C  
ANISOU  126  CZ  ARG A  15     9442  11481   8962      6   1160    789       C  
ATOM    127  NH1 ARG A  15      83.659  13.708 -94.900  1.00 78.73           N  
ANISOU  127  NH1 ARG A  15     9306  11576   9031    186   1136    842       N  
ATOM    128  NH2 ARG A  15      82.040  12.080 -94.959  1.00 81.79           N  
ANISOU  128  NH2 ARG A  15     9971  11700   9406    -25   1201    870       N  
ATOM    129  N   GLY A  16      77.174  18.398 -96.419  1.00 33.70           N  
ANISOU  129  N   GLY A  16     3469   6735   2600   -597    714    554       N  
ATOM    130  CA  GLY A  16      75.876  18.470 -95.780  1.00 36.73           C  
ANISOU  130  CA  GLY A  16     3787   7258   2911   -676    649    605       C  
ATOM    131  C   GLY A  16      75.857  18.109 -94.312  1.00 40.59           C  
ANISOU  131  C   GLY A  16     4222   7779   3423   -623    641    726       C  
ATOM    132  O   GLY A  16      74.775  17.858 -93.769  1.00 43.17           O  
ANISOU  132  O   GLY A  16     4507   8199   3695   -712    619    775       O  
ATOM    133  N   ASN A  17      77.020  18.068 -93.649  1.00 33.91           N  
ANISOU  133  N   ASN A  17     3364   6877   2644   -485    656    780       N  
ATOM    134  CA  ASN A  17      77.122  17.769 -92.229  1.00 34.56           C  
ANISOU  134  CA  ASN A  17     3399   7006   2725   -422    636    907       C  
ATOM    135  C   ASN A  17      77.403  19.041 -91.432  1.00 38.13           C  
ANISOU  135  C   ASN A  17     3733   7637   3118   -320    560    910       C  
ATOM    136  O   ASN A  17      77.996  19.988 -91.959  1.00 38.19           O  
ANISOU  136  O   ASN A  17     3712   7667   3133   -267    541    828       O  
ATOM    137  CB  ASN A  17      78.234  16.747 -91.963  1.00 35.39           C  
ANISOU  137  CB  ASN A  17     3571   6935   2942   -330    691    983       C  
ATOM    138  CG  ASN A  17      77.946  15.397 -92.591  1.00 37.76           C  
ANISOU  138  CG  ASN A  17     4018   7020   3308   -428    781    981       C  
ATOM    139  OD1 ASN A  17      76.844  14.865 -92.469  1.00 37.42           O  
ANISOU  139  OD1 ASN A  17     4018   6979   3222   -575    790   1008       O  
ATOM    140  ND2 ASN A  17      78.939  14.838 -93.274  1.00 38.93           N  
ANISOU  140  ND2 ASN A  17     4246   6982   3564   -353    856    941       N  
ATOM    141  N   PRO A  18      76.985  19.098 -90.167  1.00 37.71           N  
ANISOU  141  N   PRO A  18     3623   7711   2996   -304    525    998       N  
ATOM    142  CA  PRO A  18      77.235  20.298 -89.360  1.00 38.39           C  
ANISOU  142  CA  PRO A  18     3614   7960   3010   -218    459    979       C  
ATOM    143  C   PRO A  18      78.710  20.501 -89.040  1.00 39.17           C  
ANISOU  143  C   PRO A  18     3688   8032   3163   -103    433    992       C  
ATOM    144  O   PRO A  18      79.479  19.550 -88.868  1.00 43.28           O  
ANISOU  144  O   PRO A  18     4237   8450   3758    -54    456   1075       O  
ATOM    145  CB  PRO A  18      76.430  20.039 -88.078  1.00 38.22           C  
ANISOU  145  CB  PRO A  18     3561   8049   2910   -239    440   1067       C  
ATOM    146  CG  PRO A  18      75.416  19.000 -88.457  1.00 37.88           C  
ANISOU  146  CG  PRO A  18     3568   7955   2868   -374    502   1115       C  
ATOM    147  CD  PRO A  18      76.103  18.141 -89.474  1.00 35.35           C  
ANISOU  147  CD  PRO A  18     3349   7422   2661   -391    553   1104       C  
ATOM    148  N   THR A  19      79.094  21.772 -88.951  1.00 34.06           N  
ANISOU  148  N   THR A  19     2982   7479   2481    -61    384    909       N  
ATOM    149  CA  THR A  19      80.428  22.160 -88.523  1.00 34.47           C  
ANISOU  149  CA  THR A  19     2977   7557   2563     21    342    907       C  
ATOM    150  C   THR A  19      80.321  23.524 -87.856  1.00 37.79           C  
ANISOU  150  C   THR A  19     3346   8127   2886     29    279    832       C  
ATOM    151  O   THR A  19      79.294  24.200 -87.936  1.00 31.72           O  
ANISOU  151  O   THR A  19     2596   7377   2079     -2    271    765       O  
ATOM    152  CB  THR A  19      81.421  22.183 -89.697  1.00 38.26           C  
ANISOU  152  CB  THR A  19     3466   7911   3159     37    385    844       C  
ATOM    153  OG1 THR A  19      82.762  22.307 -89.205  1.00 32.93           O  
ANISOU  153  OG1 THR A  19     2706   7279   2529    114    348    867       O  
ATOM    154  CG2 THR A  19      81.129  23.349 -90.617  1.00 36.10           C  
ANISOU  154  CG2 THR A  19     3213   7636   2865    -14    392    721       C  
ATOM    155  N   VAL A  20      81.396  23.925 -87.205  1.00 36.74           N  
ANISOU  155  N   VAL A  20     3149   8062   2747     75    223    829       N  
ATOM    156  CA  VAL A  20      81.424  25.146 -86.410  1.00 33.52           C  
ANISOU  156  CA  VAL A  20     2708   7789   2239     72    162    749       C  
ATOM    157  C   VAL A  20      81.814  26.334 -87.280  1.00 32.10           C  
ANISOU  157  C   VAL A  20     2542   7549   2107     40    170    616       C  
ATOM    158  O   VAL A  20      82.721  26.246 -88.115  1.00 36.59           O  
ANISOU  158  O   VAL A  20     3095   8030   2779     33    195    601       O  
ATOM    159  CB  VAL A  20      82.393  24.987 -85.228  1.00 35.84           C  
ANISOU  159  CB  VAL A  20     2925   8208   2483    112     81    808       C  
ATOM    160  CG1 VAL A  20      82.454  26.266 -84.414  1.00 37.65           C  
ANISOU  160  CG1 VAL A  20     3137   8572   2596     84     19    698       C  
ATOM    161  CG2 VAL A  20      81.972  23.811 -84.368  1.00 34.82           C  
ANISOU  161  CG2 VAL A  20     2806   8129   2296    144     76    966       C  
ATOM    162  N   GLU A  21      81.126  27.455 -87.073  1.00 36.49           N  
ANISOU  162  N   GLU A  21     3133   8146   2586     26    161    523       N  
ATOM    163  CA  GLU A  21      81.501  28.756 -87.606  1.00 31.70           C  
ANISOU  163  CA  GLU A  21     2560   7482   2003     -5    160    403       C  
ATOM    164  C   GLU A  21      81.512  29.760 -86.461  1.00 32.48           C  
ANISOU  164  C   GLU A  21     2660   7686   1997     -8    109    317       C  
ATOM    165  O   GLU A  21      80.645  29.715 -85.582  1.00 40.03           O  
ANISOU  165  O   GLU A  21     3622   8697   2893     25     97    321       O  
ATOM    166  CB  GLU A  21      80.531  29.214 -88.696  1.00 33.08           C  
ANISOU  166  CB  GLU A  21     2813   7558   2197     -6    211    368       C  
ATOM    167  CG  GLU A  21      80.881  30.542 -89.335  1.00 36.46           C  
ANISOU  167  CG  GLU A  21     3306   7895   2654    -34    219    269       C  
ATOM    168  CD  GLU A  21      79.898  30.930 -90.421  1.00 37.43           C  
ANISOU  168  CD  GLU A  21     3505   7932   2783    -15    256    264       C  
ATOM    169  OE1 GLU A  21      78.725  31.210 -90.091  1.00 46.23           O  
ANISOU  169  OE1 GLU A  21     4631   9091   3842     43    249    258       O  
ATOM    170  OE2 GLU A  21      80.292  30.938 -91.607  1.00 33.52           O  
ANISOU  170  OE2 GLU A  21     3053   7336   2349    -53    290    271       O  
ATOM    171  N   VAL A  22      82.494  30.662 -86.467  1.00 41.03           N  
ANISOU  171  N   VAL A  22     3739   8747   3101    -62     80    227       N  
ATOM    172  CA  VAL A  22      82.699  31.611 -85.378  1.00 39.52           C  
ANISOU  172  CA  VAL A  22     3560   8647   2808    -92     27    122       C  
ATOM    173  C   VAL A  22      82.724  33.027 -85.938  1.00 40.95           C  
ANISOU  173  C   VAL A  22     3842   8696   3021   -139     57    -11       C  
ATOM    174  O   VAL A  22      83.475  33.315 -86.876  1.00 44.86           O  
ANISOU  174  O   VAL A  22     4343   9083   3617   -201     79    -24       O  
ATOM    175  CB  VAL A  22      84.004  31.323 -84.608  1.00 40.67           C  
ANISOU  175  CB  VAL A  22     3597   8921   2935   -140    -57    138       C  
ATOM    176  CG1 VAL A  22      84.252  32.405 -83.564  1.00 36.50           C  
ANISOU  176  CG1 VAL A  22     3096   8485   2289   -205   -117     -1       C  
ATOM    177  CG2 VAL A  22      83.955  29.945 -83.954  1.00 38.36           C  
ANISOU  177  CG2 VAL A  22     3225   8747   2602    -73    -90    291       C  
ATOM    178  N   ASP A  23      81.913  33.910 -85.356  1.00 37.71           N  
ANISOU  178  N   ASP A  23     3517   8287   2524   -108     68   -108       N  
ATOM    179  CA  ASP A  23      82.012  35.348 -85.589  1.00 42.17           C  
ANISOU  179  CA  ASP A  23     4202   8717   3105   -149     90   -246       C  
ATOM    180  C   ASP A  23      82.699  35.995 -84.389  1.00 42.13           C  
ANISOU  180  C   ASP A  23     4201   8802   3003   -234     31   -374       C  
ATOM    181  O   ASP A  23      82.231  35.857 -83.255  1.00 43.49           O  
ANISOU  181  O   ASP A  23     4363   9118   3043   -194      8   -403       O  
ATOM    182  CB  ASP A  23      80.634  35.974 -85.805  1.00 41.16           C  
ANISOU  182  CB  ASP A  23     4178   8506   2955    -36    151   -279       C  
ATOM    183  CG  ASP A  23      80.019  35.588 -87.132  1.00 48.14           C  
ANISOU  183  CG  ASP A  23     5070   9294   3927     22    194   -173       C  
ATOM    184  OD1 ASP A  23      79.014  36.221 -87.528  1.00 40.44           O  
ANISOU  184  OD1 ASP A  23     4172   8240   2955    116    233   -190       O  
ATOM    185  OD2 ASP A  23      80.528  34.652 -87.786  1.00 54.55           O  
ANISOU  185  OD2 ASP A  23     5811  10114   4801    -21    188    -76       O  
ATOM    186  N   LEU A  24      83.804  36.694 -84.640  1.00 41.92           N  
ANISOU  186  N   LEU A  24     4190   8705   3032   -367      9   -453       N  
ATOM    187  CA  LEU A  24      84.510  37.456 -83.621  1.00 43.87           C  
ANISOU  187  CA  LEU A  24     4455   9023   3191   -486    -52   -601       C  
ATOM    188  C   LEU A  24      84.430  38.934 -83.969  1.00 47.29           C  
ANISOU  188  C   LEU A  24     5071   9237   3661   -550      4   -753       C  
ATOM    189  O   LEU A  24      84.800  39.336 -85.075  1.00 52.73           O  
ANISOU  189  O   LEU A  24     5808   9754   4474   -605     51   -732       O  
ATOM    190  CB  LEU A  24      85.973  37.009 -83.502  1.00 47.10           C  
ANISOU  190  CB  LEU A  24     4704   9561   3632   -616   -136   -570       C  
ATOM    191  CG  LEU A  24      86.732  37.437 -82.238  1.00 45.62           C  
ANISOU  191  CG  LEU A  24     4476   9545   3315   -744   -240   -694       C  
ATOM    192  CD1 LEU A  24      87.790  36.421 -81.895  1.00 42.76           C  
ANISOU  192  CD1 LEU A  24     3893   9403   2950   -774   -343   -582       C  
ATOM    193  CD2 LEU A  24      87.372  38.796 -82.409  1.00 43.92           C  
ANISOU  193  CD2 LEU A  24     4362   9193   3134   -925   -229   -871       C  
ATOM    194  N   TYR A  25      83.947  39.736 -83.027  1.00 42.16           N  
ANISOU  194  N   TYR A  25     4538   8584   2898   -540     10   -904       N  
ATOM    195  CA  TYR A  25      83.798  41.171 -83.219  1.00 43.55           C  
ANISOU  195  CA  TYR A  25     4919   8524   3104   -583     72  -1061       C  
ATOM    196  C   TYR A  25      84.875  41.906 -82.440  1.00 45.71           C  
ANISOU  196  C   TYR A  25     5223   8830   3316   -799     10  -1237       C  
ATOM    197  O   TYR A  25      85.067  41.652 -81.247  1.00 48.31           O  
ANISOU  197  O   TYR A  25     5489   9373   3494   -839    -64  -1307       O  
ATOM    198  CB  TYR A  25      82.416  41.646 -82.762  1.00 49.02           C  
ANISOU  198  CB  TYR A  25     5742   9160   3725   -403    145  -1132       C  
ATOM    199  CG  TYR A  25      81.254  41.181 -83.619  1.00 46.60           C  
ANISOU  199  CG  TYR A  25     5420   8800   3487   -203    208   -981       C  
ATOM    200  CD1 TYR A  25      80.687  42.019 -84.574  1.00 50.19           C  
ANISOU  200  CD1 TYR A  25     6020   9005   4044   -117    283   -977       C  
ATOM    201  CD2 TYR A  25      80.712  39.911 -83.462  1.00 45.28           C  
ANISOU  201  CD2 TYR A  25     5094   8835   3276   -108    188   -839       C  
ATOM    202  CE1 TYR A  25      79.618  41.600 -85.358  1.00 45.96           C  
ANISOU  202  CE1 TYR A  25     5451   8454   3557     59    322   -838       C  
ATOM    203  CE2 TYR A  25      79.642  39.487 -84.243  1.00 51.56           C  
ANISOU  203  CE2 TYR A  25     5865   9599   4128     46    238   -714       C  
ATOM    204  CZ  TYR A  25      79.102  40.335 -85.187  1.00 53.03           C  
ANISOU  204  CZ  TYR A  25     6176   9567   4406    129    297   -716       C  
ATOM    205  OH  TYR A  25      78.041  39.914 -85.958  1.00 60.39           O  
ANISOU  205  OH  TYR A  25     7064  10501   5380    274    327   -591       O  
ATOM    206  N   THR A  26      85.578  42.806 -83.115  1.00 48.65           N  
ANISOU  206  N   THR A  26     5692   8999   3793   -952     39  -1304       N  
ATOM    207  CA  THR A  26      86.395  43.801 -82.437  1.00 57.47           C  
ANISOU  207  CA  THR A  26     6897  10082   4858  -1174      3  -1511       C  
ATOM    208  C   THR A  26      85.890  45.184 -82.843  1.00 58.07           C  
ANISOU  208  C   THR A  26     7258   9809   4996  -1171    113  -1636       C  
ATOM    209  O   THR A  26      84.810  45.327 -83.425  1.00 61.26           O  
ANISOU  209  O   THR A  26     7771  10050   5454   -962    200  -1564       O  
ATOM    210  CB  THR A  26      87.885  43.632 -82.755  1.00 57.72           C  
ANISOU  210  CB  THR A  26     6769  10206   4957  -1411    -67  -1487       C  
ATOM    211  OG1 THR A  26      88.201  44.325 -83.967  1.00 57.77           O  
ANISOU  211  OG1 THR A  26     6883   9947   5121  -1502     20  -1464       O  
ATOM    212  CG2 THR A  26      88.247  42.170 -82.909  1.00 52.14           C  
ANISOU  212  CG2 THR A  26     5793   9753   4265  -1335   -135  -1290       C  
ATOM    213  N   ALA A  27      86.681  46.209 -82.525  1.00 62.96           N  
ANISOU  213  N   ALA A  27     7998  10314   5610  -1406    105  -1821       N  
ATOM    214  CA  ALA A  27      86.332  47.561 -82.946  1.00 63.52           C  
ANISOU  214  CA  ALA A  27     8365  10010   5757  -1424    215  -1936       C  
ATOM    215  C   ALA A  27      86.328  47.694 -84.464  1.00 60.54           C  
ANISOU  215  C   ALA A  27     8039   9407   5555  -1392    293  -1761       C  
ATOM    216  O   ALA A  27      85.598  48.530 -85.010  1.00 60.41           O  
ANISOU  216  O   ALA A  27     8257   9088   5609  -1275    392  -1763       O  
ATOM    217  CB  ALA A  27      87.300  48.568 -82.324  1.00 57.76           C  
ANISOU  217  CB  ALA A  27     7754   9203   4991  -1731    188  -2171       C  
ATOM    218  N   LYS A  28      87.121  46.878 -85.162  1.00 59.11           N  
ANISOU  218  N   LYS A  28     7646   9372   5440  -1482    252  -1605       N  
ATOM    219  CA  LYS A  28      87.255  47.000 -86.609  1.00 62.35           C  
ANISOU  219  CA  LYS A  28     8104   9593   5991  -1489    329  -1449       C  
ATOM    220  C   LYS A  28      86.171  46.263 -87.384  1.00 60.89           C  
ANISOU  220  C   LYS A  28     7886   9414   5833  -1206    363  -1253       C  
ATOM    221  O   LYS A  28      86.079  46.442 -88.603  1.00 61.81           O  
ANISOU  221  O   LYS A  28     8080   9361   6042  -1182    430  -1124       O  
ATOM    222  CB  LYS A  28      88.630  46.499 -87.056  1.00 65.32           C  
ANISOU  222  CB  LYS A  28     8269  10126   6425  -1719    291  -1386       C  
ATOM    223  CG  LYS A  28      89.788  47.367 -86.588  1.00 69.80           C  
ANISOU  223  CG  LYS A  28     8868  10659   6994  -2049    268  -1562       C  
ATOM    224  CD  LYS A  28      90.650  47.791 -87.765  1.00 73.84           C  
ANISOU  224  CD  LYS A  28     9401  11020   7635  -2254    348  -1489       C  
ATOM    225  CE  LYS A  28      91.711  48.792 -87.350  1.00 80.33           C  
ANISOU  225  CE  LYS A  28    10283  11770   8468  -2609    340  -1673       C  
ATOM    226  NZ  LYS A  28      92.417  49.357 -88.533  1.00 81.71           N  
ANISOU  226  NZ  LYS A  28    10526  11751   8767  -2815    447  -1599       N  
ATOM    227  N   GLY A  29      85.358  45.443 -86.722  1.00 58.72           N  
ANISOU  227  N   GLY A  29     7501   9340   5471  -1009    320  -1226       N  
ATOM    228  CA  GLY A  29      84.236  44.816 -87.390  1.00 50.28           C  
ANISOU  228  CA  GLY A  29     6407   8277   4421   -759    350  -1063       C  
ATOM    229  C   GLY A  29      84.054  43.346 -87.079  1.00 50.51           C  
ANISOU  229  C   GLY A  29     6193   8605   4394   -667    286   -955       C  
ATOM    230  O   GLY A  29      84.407  42.880 -85.994  1.00 48.96           O  
ANISOU  230  O   GLY A  29     5876   8621   4106   -717    217  -1022       O  
ATOM    231  N   LEU A  30      83.483  42.615 -88.034  1.00 50.11           N  
ANISOU  231  N   LEU A  30     6083   8567   4390   -536    308   -785       N  
ATOM    232  CA  LEU A  30      83.194  41.195 -87.900  1.00 50.28           C  
ANISOU  232  CA  LEU A  30     5907   8824   4375   -444    265   -668       C  
ATOM    233  C   LEU A  30      84.298  40.383 -88.562  1.00 48.09           C  
ANISOU  233  C   LEU A  30     5483   8627   4164   -568    248   -575       C  
ATOM    234  O   LEU A  30      84.782  40.738 -89.638  1.00 54.80           O  
ANISOU  234  O   LEU A  30     6389   9337   5096   -650    297   -532       O  
ATOM    235  CB  LEU A  30      81.837  40.869 -88.535  1.00 53.91           C  
ANISOU  235  CB  LEU A  30     6390   9253   4840   -238    301   -556       C  
ATOM    236  CG  LEU A  30      81.127  39.525 -88.339  1.00 60.12           C  
ANISOU  236  CG  LEU A  30     7015  10248   5580   -123    273   -448       C  
ATOM    237  CD1 LEU A  30      79.650  39.692 -88.631  1.00 62.23           C  
ANISOU  237  CD1 LEU A  30     7333  10479   5833     68    307   -404       C  
ATOM    238  CD2 LEU A  30      81.691  38.433 -89.230  1.00 61.65           C  
ANISOU  238  CD2 LEU A  30     7093  10499   5833   -180    264   -317       C  
ATOM    239  N   PHE A  31      84.693  39.293 -87.913  1.00 44.86           N  
ANISOU  239  N   PHE A  31     4888   8442   3714   -572    185   -536       N  
ATOM    240  CA  PHE A  31      85.695  38.384 -88.459  1.00 42.48           C  
ANISOU  240  CA  PHE A  31     4426   8233   3480   -646    175   -444       C  
ATOM    241  C   PHE A  31      85.176  36.962 -88.321  1.00 42.36           C  
ANISOU  241  C   PHE A  31     4287   8368   3441   -511    152   -321       C  
ATOM    242  O   PHE A  31      85.034  36.450 -87.206  1.00 36.54           O  
ANISOU  242  O   PHE A  31     3471   7793   2619   -469     89   -325       O  
ATOM    243  CB  PHE A  31      87.044  38.569 -87.760  1.00 44.47           C  
ANISOU  243  CB  PHE A  31     4566   8602   3728   -818    113   -526       C  
ATOM    244  CG  PHE A  31      87.611  39.946 -87.931  1.00 46.77           C  
ANISOU  244  CG  PHE A  31     4986   8734   4051   -992    142   -653       C  
ATOM    245  CD1 PHE A  31      88.404  40.252 -89.024  1.00 48.18           C  
ANISOU  245  CD1 PHE A  31     5168   8806   4334  -1120    208   -621       C  
ATOM    246  CD2 PHE A  31      87.319  40.945 -87.020  1.00 49.05           C  
ANISOU  246  CD2 PHE A  31     5409   8967   4261  -1034    119   -807       C  
ATOM    247  CE1 PHE A  31      88.911  41.525 -89.189  1.00 51.17           C  
ANISOU  247  CE1 PHE A  31     5679   9018   4743  -1302    245   -729       C  
ATOM    248  CE2 PHE A  31      87.823  42.219 -87.180  1.00 51.55           C  
ANISOU  248  CE2 PHE A  31     5871   9102   4614  -1209    154   -930       C  
ATOM    249  CZ  PHE A  31      88.619  42.510 -88.264  1.00 49.47           C  
ANISOU  249  CZ  PHE A  31     5609   8726   4460  -1349    216   -884       C  
ATOM    250  N   ARG A  32      84.900  36.334 -89.459  1.00 41.13           N  
ANISOU  250  N   ARG A  32     4127   8151   3349   -457    206   -212       N  
ATOM    251  CA  ARG A  32      84.225  35.049 -89.532  1.00 39.19           C  
ANISOU  251  CA  ARG A  32     3808   7993   3090   -341    203   -101       C  
ATOM    252  C   ARG A  32      85.180  33.987 -90.054  1.00 39.20           C  
ANISOU  252  C   ARG A  32     3681   8046   3167   -372    218    -21       C  
ATOM    253  O   ARG A  32      86.000  34.257 -90.935  1.00 33.88           O  
ANISOU  253  O   ARG A  32     3005   7300   2568   -456    268    -28       O  
ATOM    254  CB  ARG A  32      82.995  35.148 -90.441  1.00 45.64           C  
ANISOU  254  CB  ARG A  32     4733   8702   3907   -251    253    -53       C  
ATOM    255  CG  ARG A  32      82.262  33.844 -90.690  1.00 47.33           C  
ANISOU  255  CG  ARG A  32     4883   8988   4113   -168    257     53       C  
ATOM    256  CD  ARG A  32      80.976  34.110 -91.457  1.00 35.40           C  
ANISOU  256  CD  ARG A  32     3461   7406   2581    -91    283     83       C  
ATOM    257  NE  ARG A  32      80.063  34.963 -90.705  1.00 33.99           N  
ANISOU  257  NE  ARG A  32     3336   7238   2341    -10    267     24       N  
ATOM    258  CZ  ARG A  32      79.224  35.832 -91.262  1.00 41.58           C  
ANISOU  258  CZ  ARG A  32     4398   8102   3297     62    285     17       C  
ATOM    259  NH1 ARG A  32      79.190  35.974 -92.577  1.00 43.94           N  
ANISOU  259  NH1 ARG A  32     4763   8297   3634     49    308     74       N  
ATOM    260  NH2 ARG A  32      78.422  36.567 -90.506  1.00 49.57           N  
ANISOU  260  NH2 ARG A  32     5449   9126   4261    159    284    -45       N  
ATOM    261  N   ALA A  33      85.068  32.784 -89.503  1.00 36.25           N  
ANISOU  261  N   ALA A  33     3206   7792   2776   -299    185     58       N  
ATOM    262  CA  ALA A  33      85.871  31.651 -89.932  1.00 35.71           C  
ANISOU  262  CA  ALA A  33     3024   7758   2787   -287    207    140       C  
ATOM    263  C   ALA A  33      85.080  30.377 -89.684  1.00 41.06           C  
ANISOU  263  C   ALA A  33     3685   8474   3441   -184    204    242       C  
ATOM    264  O   ALA A  33      84.257  30.315 -88.767  1.00 46.06           O  
ANISOU  264  O   ALA A  33     4337   9180   3984   -139    160    253       O  
ATOM    265  CB  ALA A  33      87.213  31.605 -89.194  1.00 39.30           C  
ANISOU  265  CB  ALA A  33     3328   8341   3262   -338    147    126       C  
ATOM    266  N   ALA A  34      85.332  29.363 -90.510  1.00 35.58           N  
ANISOU  266  N   ALA A  34     2967   7727   2826   -155    263    310       N  
ATOM    267  CA  ALA A  34      84.667  28.076 -90.374  1.00 35.56           C  
ANISOU  267  CA  ALA A  34     2966   7727   2818    -80    273    406       C  
ATOM    268  C   ALA A  34      85.712  26.974 -90.268  1.00 35.77           C  
ANISOU  268  C   ALA A  34     2886   7776   2929    -29    283    481       C  
ATOM    269  O   ALA A  34      86.884  27.168 -90.597  1.00 42.62           O  
ANISOU  269  O   ALA A  34     3669   8654   3870    -49    301    455       O  
ATOM    270  CB  ALA A  34      83.709  27.809 -91.542  1.00 39.18           C  
ANISOU  270  CB  ALA A  34     3532   8071   3283    -88    342    410       C  
ATOM    271  N   VAL A  35      85.267  25.807 -89.812  1.00 40.35           N  
ANISOU  271  N   VAL A  35     3469   8361   3502     40    277    581       N  
ATOM    272  CA  VAL A  35      86.142  24.704 -89.433  1.00 40.13           C  
ANISOU  272  CA  VAL A  35     3349   8352   3544    125    272    679       C  
ATOM    273  C   VAL A  35      85.856  23.526 -90.355  1.00 33.57           C  
ANISOU  273  C   VAL A  35     2595   7364   2795    161    372    724       C  
ATOM    274  O   VAL A  35      84.693  23.162 -90.530  1.00 34.57           O  
ANISOU  274  O   VAL A  35     2828   7429   2877    131    396    739       O  
ATOM    275  CB  VAL A  35      85.946  24.287 -87.964  1.00 36.77           C  
ANISOU  275  CB  VAL A  35     2883   8056   3033    178    177    778       C  
ATOM    276  CG1 VAL A  35      86.790  23.058 -87.623  1.00 35.79           C  
ANISOU  276  CG1 VAL A  35     2680   7930   2987    294    170    912       C  
ATOM    277  CG2 VAL A  35      86.287  25.439 -87.053  1.00 37.72           C  
ANISOU  277  CG2 VAL A  35     2938   8337   3057    130     79    710       C  
ATOM    278  N   PRO A  36      86.867  22.898 -90.946  1.00 34.39           N  
ANISOU  278  N   PRO A  36     2645   7404   3018    222    439    739       N  
ATOM    279  CA  PRO A  36      86.631  21.705 -91.764  1.00 34.64           C  
ANISOU  279  CA  PRO A  36     2771   7267   3125    260    545    766       C  
ATOM    280  C   PRO A  36      86.368  20.476 -90.901  1.00 52.25           C  
ANISOU  280  C   PRO A  36     5023   9460   5367    348    522    905       C  
ATOM    281  O   PRO A  36      86.562  20.474 -89.685  1.00 51.92           O  
ANISOU  281  O   PRO A  36     4905   9542   5280    401    424    997       O  
ATOM    282  CB  PRO A  36      87.931  21.559 -92.560  1.00 40.44           C  
ANISOU  282  CB  PRO A  36     3422   7964   3981    314    632    727       C  
ATOM    283  CG  PRO A  36      88.970  22.209 -91.703  1.00 36.33           C  
ANISOU  283  CG  PRO A  36     2717   7619   3467    347    540    747       C  
ATOM    284  CD  PRO A  36      88.267  23.355 -91.018  1.00 37.57           C  
ANISOU  284  CD  PRO A  36     2898   7885   3491    243    435    707       C  
ATOM    285  N   SER A  37      85.924  19.413 -91.567  1.00 52.71           N  
ANISOU  285  N   SER A  37     5205   9341   5481    353    617    920       N  
ATOM    286  CA  SER A  37      85.517  18.203 -90.864  1.00 61.86           C  
ANISOU  286  CA  SER A  37     6431  10419   6654    410    614   1055       C  
ATOM    287  C   SER A  37      86.733  17.429 -90.378  1.00 69.27           C  
ANISOU  287  C   SER A  37     7281  11336   7704    588    615   1168       C  
ATOM    288  O   SER A  37      87.700  17.236 -91.122  1.00 73.35           O  
ANISOU  288  O   SER A  37     7747  11786   8336    669    695   1120       O  
ATOM    289  CB  SER A  37      84.679  17.313 -91.776  1.00 68.76           C  
ANISOU  289  CB  SER A  37     7478  11092   7557    335    721   1019       C  
ATOM    290  OG  SER A  37      85.522  16.637 -92.698  1.00 74.94           O  
ANISOU  290  OG  SER A  37     8291  11713   8468    413    838    975       O  
ATOM    291  N   GLY A  38      86.672  16.971 -89.133  1.00 73.65           N  
ANISOU  291  N   GLY A  38     7813  11953   8217    656    531   1324       N  
ATOM    292  CA  GLY A  38      87.707  16.121 -88.579  1.00 73.64           C  
ANISOU  292  CA  GLY A  38     7737  11929   8313    847    515   1470       C  
ATOM    293  C   GLY A  38      87.137  14.843 -88.002  1.00 80.99           C  
ANISOU  293  C   GLY A  38     8812  12707   9254    897    536   1638       C  
ATOM    294  O   GLY A  38      86.035  14.425 -88.373  1.00 85.14           O  
ANISOU  294  O   GLY A  38     9506  13091   9754    772    604   1610       O  
ATOM    295  N   ALA A  39      87.870  14.219 -87.085  1.00 81.63           N  
ANISOU  295  N   ALA A  39     8827  12822   9369   1070    472   1821       N  
ATOM    296  CA  ALA A  39      87.433  12.998 -86.424  1.00 82.20           C  
ANISOU  296  CA  ALA A  39     9043  12742   9449   1130    487   2017       C  
ATOM    297  C   ALA A  39      87.292  13.248 -84.928  1.00 83.06           C  
ANISOU  297  C   ALA A  39     9088  13078   9392   1139    334   2180       C  
ATOM    298  O   ALA A  39      88.140  13.904 -84.315  1.00 84.65           O  
ANISOU  298  O   ALA A  39     9103  13516   9544   1217    210   2202       O  
ATOM    299  CB  ALA A  39      88.417  11.849 -86.676  1.00 80.30           C  
ANISOU  299  CB  ALA A  39     8817  12296   9397   1363    560   2126       C  
ATOM    300  N   SER A  40      86.208  12.734 -84.350  1.00 80.12           N  
ANISOU  300  N   SER A  40     8870  12648   8924   1040    345   2285       N  
ATOM    301  CA  SER A  40      85.998  12.766 -82.908  1.00 75.06           C  
ANISOU  301  CA  SER A  40     8207  12201   8112   1048    225   2463       C  
ATOM    302  C   SER A  40      86.655  11.591 -82.195  1.00 84.95           C  
ANISOU  302  C   SER A  40     9499  13356   9421   1251    197   2731       C  
ATOM    303  O   SER A  40      86.511  11.463 -80.974  1.00 88.47           O  
ANISOU  303  O   SER A  40     9948  13952   9714   1268     98   2915       O  
ATOM    304  CB  SER A  40      84.497  12.795 -82.591  1.00 63.04           C  
ANISOU  304  CB  SER A  40     6818  10687   6447    839    265   2459       C  
ATOM    305  OG  SER A  40      83.794  11.810 -83.328  1.00 58.98           O  
ANISOU  305  OG  SER A  40     6490   9879   6042    763    406   2464       O  
ATOM    306  N   THR A  41      87.373  10.741 -82.925  1.00 91.60           N  
ANISOU  306  N   THR A  41    10378  13953  10474   1414    284   2760       N  
ATOM    307  CA  THR A  41      88.056   9.580 -82.373  1.00 94.69           C  
ANISOU  307  CA  THR A  41    10815  14208  10955   1647    270   3018       C  
ATOM    308  C   THR A  41      89.509   9.590 -82.833  1.00 90.37           C  
ANISOU  308  C   THR A  41    10080  13680  10577   1889    254   2996       C  
ATOM    309  O   THR A  41      89.889  10.326 -83.748  1.00 91.25           O  
ANISOU  309  O   THR A  41    10071  13845  10755   1849    295   2771       O  
ATOM    310  CB  THR A  41      87.369   8.275 -82.802  1.00101.33           C  
ANISOU  310  CB  THR A  41    11933  14655  11912   1622    432   3097       C  
ATOM    311  OG1 THR A  41      86.088   8.576 -83.372  1.00101.28           O  
ANISOU  311  OG1 THR A  41    12049  14592  11841   1339    519   2921       O  
ATOM    312  CG2 THR A  41      87.185   7.346 -81.611  1.00101.95           C  
ANISOU  312  CG2 THR A  41    12141  14676  11921   1701    384   3414       C  
ATOM    313  N   GLY A  42      90.328   8.768 -82.183  1.00 87.74           N  
ANISOU  313  N   GLY A  42     9713  13314  10309   2147    196   3242       N  
ATOM    314  CA  GLY A  42      91.730   8.675 -82.547  1.00 85.31           C  
ANISOU  314  CA  GLY A  42     9201  13041  10173   2407    183   3247       C  
ATOM    315  C   GLY A  42      92.667   8.997 -81.401  1.00 84.85           C  
ANISOU  315  C   GLY A  42     8899  13325  10016   2569    -34   3428       C  
ATOM    316  O   GLY A  42      92.415   9.916 -80.616  1.00 80.09           O  
ANISOU  316  O   GLY A  42     8203  13035   9195   2416   -182   3408       O  
ATOM    317  N   ILE A  43      93.769   8.246 -81.305  1.00 86.43           N  
ANISOU  317  N   ILE A  43     8990  13476  10374   2885    -54   3601       N  
ATOM    318  CA  ILE A  43      94.635   8.336 -80.131  1.00 94.13           C  
ANISOU  318  CA  ILE A  43     9746  14770  11250   3065   -277   3827       C  
ATOM    319  C   ILE A  43      95.453   9.623 -80.153  1.00 96.13           C  
ANISOU  319  C   ILE A  43     9661  15420  11443   3000   -407   3651       C  
ATOM    320  O   ILE A  43      95.675  10.255 -79.110  1.00 94.96           O  
ANISOU  320  O   ILE A  43     9396  15586  11098   2907   -596   3677       O  
ATOM    321  CB  ILE A  43      95.527   7.080 -80.039  1.00 96.21           C  
ANISOU  321  CB  ILE A  43     9996  14845  11714   3450   -258   4086       C  
ATOM    322  CG1 ILE A  43      94.704   5.857 -79.622  1.00 95.31           C  
ANISOU  322  CG1 ILE A  43    10231  14382  11600   3495   -182   4325       C  
ATOM    323  CG2 ILE A  43      96.699   7.292 -79.078  1.00100.33           C  
ANISOU  323  CG2 ILE A  43    10253  15692  12177   3584   -469   4189       C  
ATOM    324  CD1 ILE A  43      95.501   4.547 -79.651  1.00 98.42           C  
ANISOU  324  CD1 ILE A  43    10669  14503  12223   3889   -126   4574       C  
ATOM    325  N   TYR A  44      95.888  10.053 -81.335  1.00 91.81           N  
ANISOU  325  N   TYR A  44     9003  14822  11058   2975   -281   3408       N  
ATOM    326  CA  TYR A  44      96.891  11.109 -81.442  1.00 86.65           C  
ANISOU  326  CA  TYR A  44     8009  14513  10399   2951   -383   3268       C  
ATOM    327  C   TYR A  44      96.312  12.453 -81.860  1.00 83.76           C  
ANISOU  327  C   TYR A  44     7646  14271   9909   2611   -367   2979       C  
ATOM    328  O   TYR A  44      96.647  13.477 -81.260  1.00 90.80           O  
ANISOU  328  O   TYR A  44     8373  15475  10651   2466   -522   2899       O  
ATOM    329  CB  TYR A  44      97.982  10.680 -82.421  1.00 82.35           C  
ANISOU  329  CB  TYR A  44     7294  13869  10127   3186   -253   3220       C  
ATOM    330  CG  TYR A  44      98.565   9.329 -82.102  1.00 85.50           C  
ANISOU  330  CG  TYR A  44     7731  14079  10677   3524   -236   3470       C  
ATOM    331  CD1 TYR A  44      98.176   8.198 -82.809  1.00 85.32           C  
ANISOU  331  CD1 TYR A  44     7947  13634  10837   3689    -29   3528       C  
ATOM    332  CD2 TYR A  44      99.508   9.181 -81.093  1.00 89.14           C  
ANISOU  332  CD2 TYR A  44     8057  14718  11093   3611   -410   3586       C  
ATOM    333  CE1 TYR A  44      98.714   6.958 -82.522  1.00 92.68           C  
ANISOU  333  CE1 TYR A  44     8910  14379  11924   4048    -10   3787       C  
ATOM    334  CE2 TYR A  44     100.051   7.942 -80.800  1.00 92.60           C  
ANISOU  334  CE2 TYR A  44     8540  14971  11672   3921   -397   3809       C  
ATOM    335  CZ  TYR A  44      99.649   6.837 -81.518  1.00 93.15           C  
ANISOU  335  CZ  TYR A  44     8818  14639  11936   4140   -195   3908       C  
ATOM    336  OH  TYR A  44     100.179   5.603 -81.236  1.00 96.24           O  
ANISOU  336  OH  TYR A  44     9283  14808  12475   4449   -171   4122       O  
ATOM    337  N   GLU A  45      95.457  12.474 -82.875  1.00 72.76           N  
ANISOU  337  N   GLU A  45     5772  13017   8858   2722   -592   1163       N  
ATOM    338  CA  GLU A  45      94.957  13.735 -83.395  1.00 74.25           C  
ANISOU  338  CA  GLU A  45     5984  13308   8921   2463   -465   1017       C  
ATOM    339  C   GLU A  45      93.967  14.373 -82.427  1.00 69.15           C  
ANISOU  339  C   GLU A  45     5478  12734   8063   2280   -548   1121       C  
ATOM    340  O   GLU A  45      93.219  13.683 -81.731  1.00 72.74           O  
ANISOU  340  O   GLU A  45     6080  13086   8473   2350   -642   1307       O  
ATOM    341  CB  GLU A  45      94.300  13.511 -84.755  1.00 77.07           C  
ANISOU  341  CB  GLU A  45     6438  13489   9356   2489   -276    918       C  
ATOM    342  CG  GLU A  45      93.379  12.301 -84.792  1.00 78.26           C  
ANISOU  342  CG  GLU A  45     6794  13370   9571   2656   -296   1071       C  
ATOM    343  CD  GLU A  45      92.968  11.931 -86.202  1.00 80.90           C  
ANISOU  343  CD  GLU A  45     7282  13446  10009   2659   -105    933       C  
ATOM    344  OE1 GLU A  45      93.077  10.738 -86.561  1.00 83.51           O  
ANISOU  344  OE1 GLU A  45     7684  13557  10491   2879    -96    972       O  
ATOM    345  OE2 GLU A  45      92.535  12.834 -86.950  1.00 79.14           O  
ANISOU  345  OE2 GLU A  45     7123  13235   9713   2440     29    787       O  
ATOM    346  N   ALA A  46      93.978  15.703 -82.373  1.00 65.62           N  
ANISOU  346  N   ALA A  46     4995  12456   7480   2039   -509    998       N  
ATOM    347  CA  ALA A  46      92.972  16.419 -81.600  1.00 53.06           C  
ANISOU  347  CA  ALA A  46     3545  10927   5688   1859   -554   1056       C  
ATOM    348  C   ALA A  46      91.582  16.073 -82.119  1.00 54.68           C  
ANISOU  348  C   ALA A  46     3935  10952   5888   1862   -472   1112       C  
ATOM    349  O   ALA A  46      91.382  15.838 -83.313  1.00 54.98           O  
ANISOU  349  O   ALA A  46     4041  10804   6043   1876   -326   1011       O  
ATOM    350  CB  ALA A  46      93.209  17.926 -81.673  1.00 51.99           C  
ANISOU  350  CB  ALA A  46     3354  10966   5433   1610   -505    886       C  
ATOM    351  N   LEU A  47      90.614  16.045 -81.208  1.00 57.34           N  
ANISOU  351  N   LEU A  47     4440  11260   6087   1793   -541   1247       N  
ATOM    352  CA  LEU A  47      89.292  15.499 -81.483  1.00 50.78           C  
ANISOU  352  CA  LEU A  47     3863  10169   5263   1765   -470   1322       C  
ATOM    353  C   LEU A  47      88.251  16.606 -81.560  1.00 46.29           C  
ANISOU  353  C   LEU A  47     3423   9609   4556   1529   -383   1232       C  
ATOM    354  O   LEU A  47      88.123  17.413 -80.633  1.00 46.10           O  
ANISOU  354  O   LEU A  47     3382   9770   4363   1415   -445   1239       O  
ATOM    355  CB  LEU A  47      88.897  14.484 -80.409  1.00 51.10           C  
ANISOU  355  CB  LEU A  47     4001  10154   5262   1872   -604   1565       C  
ATOM    356  CG  LEU A  47      89.901  13.346 -80.225  1.00 59.04           C  
ANISOU  356  CG  LEU A  47     4894  11132   6405   2131   -718   1680       C  
ATOM    357  CD1 LEU A  47      89.393  12.326 -79.216  1.00 61.79           C  
ANISOU  357  CD1 LEU A  47     5386  11386   6704   2218   -849   1939       C  
ATOM    358  CD2 LEU A  47      90.220  12.686 -81.563  1.00 59.77           C  
ANISOU  358  CD2 LEU A  47     4982  11010   6717   2265   -600   1576       C  
ATOM    359  N   GLU A  48      87.504  16.631 -82.660  1.00 49.19           N  
ANISOU  359  N   GLU A  48     3924   9773   4994   1463   -245   1145       N  
ATOM    360  CA  GLU A  48      86.344  17.504 -82.748  1.00 52.03           C  
ANISOU  360  CA  GLU A  48     4425  10099   5245   1272   -172   1088       C  
ATOM    361  C   GLU A  48      85.230  16.970 -81.857  1.00 46.44           C  
ANISOU  361  C   GLU A  48     3863   9330   4453   1261   -220   1267       C  
ATOM    362  O   GLU A  48      85.077  15.760 -81.670  1.00 43.39           O  
ANISOU  362  O   GLU A  48     3538   8811   4136   1381   -266   1423       O  
ATOM    363  CB  GLU A  48      85.856  17.615 -84.193  1.00 54.33           C  
ANISOU  363  CB  GLU A  48     4817  10192   5635   1211    -30    962       C  
ATOM    364  CG  GLU A  48      85.316  16.316 -84.769  1.00 57.43           C  
ANISOU  364  CG  GLU A  48     5341  10324   6155   1312     -1   1051       C  
ATOM    365  CD  GLU A  48      84.779  16.478 -86.176  1.00 58.03           C  
ANISOU  365  CD  GLU A  48     5532  10217   6302   1230    126    922       C  
ATOM    366  OE1 GLU A  48      85.078  17.510 -86.817  1.00 61.17           O  
ANISOU  366  OE1 GLU A  48     5883  10689   6670   1125    196    762       O  
ATOM    367  OE2 GLU A  48      84.053  15.572 -86.639  1.00 55.52           O  
ANISOU  367  OE2 GLU A  48     5358   9677   6059   1260    149    986       O  
ATOM    368  N   LEU A  49      84.459  17.884 -81.287  1.00 45.02           N  
ANISOU  368  N   LEU A  49     3739   9247   4119   1115   -205   1244       N  
ATOM    369  CA  LEU A  49      83.349  17.505 -80.425  1.00 48.74           C  
ANISOU  369  CA  LEU A  49     4333   9694   4490   1081   -227   1399       C  
ATOM    370  C   LEU A  49      82.093  17.353 -81.275  1.00 41.28           C  
ANISOU  370  C   LEU A  49     3534   8537   3613   1006   -117   1383       C  
ATOM    371  O   LEU A  49      81.699  18.289 -81.980  1.00 39.63           O  
ANISOU  371  O   LEU A  49     3347   8308   3403    901    -33   1231       O  
ATOM    372  CB  LEU A  49      83.143  18.541 -79.321  1.00 51.56           C  
ANISOU  372  CB  LEU A  49     4674  10278   4640    974   -258   1374       C  
ATOM    373  CG  LEU A  49      82.038  18.231 -78.312  1.00 49.80           C  
ANISOU  373  CG  LEU A  49     4560  10078   4282    930   -265   1528       C  
ATOM    374  CD1 LEU A  49      82.355  16.940 -77.578  1.00 48.49           C  
ANISOU  374  CD1 LEU A  49     4405   9898   4119   1049   -375   1752       C  
ATOM    375  CD2 LEU A  49      81.861  19.388 -77.338  1.00 52.76           C  
ANISOU  375  CD2 LEU A  49     4925  10676   4447    824   -273   1456       C  
ATOM    376  N   ARG A  50      81.484  16.170 -81.225  1.00 43.61           N  
ANISOU  376  N   ARG A  50     3930   8669   3970   1056   -129   1544       N  
ATOM    377  CA  ARG A  50      80.210  15.899 -81.876  1.00 46.95           C  
ANISOU  377  CA  ARG A  50     4487   8905   4448    971    -48   1559       C  
ATOM    378  C   ARG A  50      79.129  15.685 -80.823  1.00 49.71           C  
ANISOU  378  C   ARG A  50     4906   9308   4674    899    -59   1717       C  
ATOM    379  O   ARG A  50      79.406  15.221 -79.713  1.00 46.03           O  
ANISOU  379  O   ARG A  50     4428   8944   4117    947   -140   1867       O  
ATOM    380  CB  ARG A  50      80.304  14.668 -82.786  1.00 47.85           C  
ANISOU  380  CB  ARG A  50     4678   8763   4738   1058    -43   1606       C  
ATOM    381  CG  ARG A  50      81.223  14.841 -83.982  1.00 46.38           C  
ANISOU  381  CG  ARG A  50     4437   8511   4672   1120      2   1434       C  
ATOM    382  CD  ARG A  50      80.580  15.693 -85.065  1.00 43.07           C  
ANISOU  382  CD  ARG A  50     4069   8030   4266    987    103   1272       C  
ATOM    383  NE  ARG A  50      81.564  16.146 -86.042  1.00 42.98           N  
ANISOU  383  NE  ARG A  50     3987   8025   4318   1016    153   1099       N  
ATOM    384  CZ  ARG A  50      81.285  16.888 -87.109  1.00 39.78           C  
ANISOU  384  CZ  ARG A  50     3625   7566   3925    913    235    949       C  
ATOM    385  NH1 ARG A  50      80.040  17.268 -87.357  1.00 35.04           N  
ANISOU  385  NH1 ARG A  50     3128   6895   3290    790    264    949       N  
ATOM    386  NH2 ARG A  50      82.262  17.250 -87.931  1.00 36.65           N  
ANISOU  386  NH2 ARG A  50     3160   7192   3573    932    286    805       N  
ATOM    387  N   ASP A  51      77.886  16.028 -81.181  1.00 49.48           N  
ANISOU  387  N   ASP A  51     4943   9219   4637    779     24   1687       N  
ATOM    388  CA  ASP A  51      76.787  15.924 -80.223  1.00 43.21           C  
ANISOU  388  CA  ASP A  51     4193   8502   3724    696     41   1819       C  
ATOM    389  C   ASP A  51      76.422  14.470 -79.942  1.00 48.50           C  
ANISOU  389  C   ASP A  51     4956   9029   4444    715      0   2039       C  
ATOM    390  O   ASP A  51      76.105  14.114 -78.800  1.00 41.74           O  
ANISOU  390  O   ASP A  51     4122   8276   3462    690    -29   2203       O  
ATOM    391  CB  ASP A  51      75.561  16.684 -80.735  1.00 46.00           C  
ANISOU  391  CB  ASP A  51     4565   8836   4076    576    139   1721       C  
ATOM    392  CG  ASP A  51      75.812  18.169 -80.882  1.00 50.85           C  
ANISOU  392  CG  ASP A  51     5115   9580   4626    550    175   1519       C  
ATOM    393  OD1 ASP A  51      76.787  18.672 -80.286  1.00 36.69           O  
ANISOU  393  OD1 ASP A  51     3257   7938   2743    594    129   1470       O  
ATOM    394  OD2 ASP A  51      75.026  18.837 -81.589  1.00 50.44           O  
ANISOU  394  OD2 ASP A  51     5080   9474   4612    483    240   1413       O  
ATOM    395  N   GLY A  52      76.447  13.620 -80.968  1.00 47.57           N  
ANISOU  395  N   GLY A  52     4910   8667   4498    749     -1   2046       N  
ATOM    396  CA  GLY A  52      76.079  12.228 -80.804  1.00 53.18           C  
ANISOU  396  CA  GLY A  52     5736   9198   5271    756    -42   2246       C  
ATOM    397  C   GLY A  52      74.594  11.950 -80.695  1.00 51.37           C  
ANISOU  397  C   GLY A  52     5579   8919   5019    596     14   2347       C  
ATOM    398  O   GLY A  52      74.215  10.812 -80.395  1.00 48.38           O  
ANISOU  398  O   GLY A  52     5304   8408   4669    569    -22   2536       O  
ATOM    399  N   ASP A  53      73.741  12.946 -80.921  1.00 48.31           N  
ANISOU  399  N   ASP A  53     5136   8633   4585    487     98   2232       N  
ATOM    400  CA  ASP A  53      72.295  12.748 -80.892  1.00 50.07           C  
ANISOU  400  CA  ASP A  53     5391   8832   4801    334    157   2312       C  
ATOM    401  C   ASP A  53      71.856  12.184 -82.237  1.00 56.36           C  
ANISOU  401  C   ASP A  53     6269   9371   5773    286    162   2268       C  
ATOM    402  O   ASP A  53      71.797  12.911 -83.234  1.00 51.56           O  
ANISOU  402  O   ASP A  53     5634   8731   5227    278    194   2090       O  
ATOM    403  CB  ASP A  53      71.584  14.061 -80.575  1.00 46.91           C  
ANISOU  403  CB  ASP A  53     4887   8649   4289    265    239   2199       C  
ATOM    404  CG  ASP A  53      70.073  13.953 -80.686  1.00 50.79           C  
ANISOU  404  CG  ASP A  53     5371   9131   4796    118    308   2256       C  
ATOM    405  OD1 ASP A  53      69.410  15.009 -80.740  1.00 53.51           O  
ANISOU  405  OD1 ASP A  53     5630   9604   5098     78    376   2138       O  
ATOM    406  OD2 ASP A  53      69.544  12.821 -80.720  1.00 51.70           O  
ANISOU  406  OD2 ASP A  53     5564   9109   4971     41    290   2418       O  
ATOM    407  N   LYS A  54      71.519  10.893 -82.259  1.00 60.19           N  
ANISOU  407  N   LYS A  54     6871   9669   6331    242    125   2434       N  
ATOM    408  CA  LYS A  54      71.274  10.212 -83.524  1.00 64.01           C  
ANISOU  408  CA  LYS A  54     7461   9882   6977    206    112   2390       C  
ATOM    409  C   LYS A  54      69.993  10.669 -84.203  1.00 65.97           C  
ANISOU  409  C   LYS A  54     7681  10130   7255     45    165   2324       C  
ATOM    410  O   LYS A  54      69.851  10.477 -85.414  1.00 69.18           O  
ANISOU  410  O   LYS A  54     8156  10353   7776     14    156   2226       O  
ATOM    411  CB  LYS A  54      71.263   8.699 -83.302  1.00 65.77           C  
ANISOU  411  CB  LYS A  54     7836   9887   7266    196     49   2588       C  
ATOM    412  CG  LYS A  54      72.672   8.140 -83.194  1.00 71.52           C  
ANISOU  412  CG  LYS A  54     8613  10522   8040    398    -21   2602       C  
ATOM    413  CD  LYS A  54      72.744   6.763 -82.571  1.00 77.77           C  
ANISOU  413  CD  LYS A  54     9548  11143   8859    416    -98   2834       C  
ATOM    414  CE  LYS A  54      74.202   6.421 -82.308  1.00 80.82           C  
ANISOU  414  CE  LYS A  54     9934  11497   9276    650   -174   2842       C  
ATOM    415  NZ  LYS A  54      74.422   5.008 -81.904  1.00 84.69           N  
ANISOU  415  NZ  LYS A  54    10591  11758   9828    710   -266   3053       N  
ATOM    416  N   GLN A  55      69.065  11.275 -83.463  1.00 66.87           N  
ANISOU  416  N   GLN A  55     7691  10451   7264    -52    220   2369       N  
ATOM    417  CA  GLN A  55      67.877  11.831 -84.101  1.00 67.57           C  
ANISOU  417  CA  GLN A  55     7718  10565   7388   -179    264   2294       C  
ATOM    418  C   GLN A  55      68.220  13.032 -84.969  1.00 62.74           C  
ANISOU  418  C   GLN A  55     7052   9990   6798   -111    279   2068       C  
ATOM    419  O   GLN A  55      67.511  13.317 -85.941  1.00 64.52           O  
ANISOU  419  O   GLN A  55     7275  10145   7096   -188    279   1985       O  
ATOM    420  CB  GLN A  55      66.844  12.230 -83.050  1.00 73.09           C  
ANISOU  420  CB  GLN A  55     8300  11499   7973   -274    333   2386       C  
ATOM    421  CG  GLN A  55      66.556  11.152 -82.027  1.00 81.96           C  
ANISOU  421  CG  GLN A  55     9475  12628   9037   -354    330   2624       C  
ATOM    422  CD  GLN A  55      66.269   9.814 -82.669  1.00 88.90           C  
ANISOU  422  CD  GLN A  55    10499  13230  10048   -453    269   2739       C  
ATOM    423  OE1 GLN A  55      66.934   8.820 -82.379  1.00 90.59           O  
ANISOU  423  OE1 GLN A  55    10845  13296  10279   -408    210   2863       O  
ATOM    424  NE2 GLN A  55      65.274   9.778 -83.547  1.00 90.58           N  
ANISOU  424  NE2 GLN A  55    10694  13364  10358   -587    274   2698       N  
ATOM    425  N   ARG A  56      69.302  13.736 -84.647  1.00 53.97           N  
ANISOU  425  N   ARG A  56     5903   8985   5620     20    282   1973       N  
ATOM    426  CA  ARG A  56      69.628  15.015 -85.268  1.00 45.39           C  
ANISOU  426  CA  ARG A  56     4760   7962   4524     67    304   1771       C  
ATOM    427  C   ARG A  56      70.920  14.871 -86.064  1.00 42.63           C  
ANISOU  427  C   ARG A  56     4476   7484   4239    168    271   1668       C  
ATOM    428  O   ARG A  56      71.997  14.699 -85.481  1.00 41.51           O  
ANISOU  428  O   ARG A  56     4320   7393   4058    274    251   1688       O  
ATOM    429  CB  ARG A  56      69.745  16.103 -84.204  1.00 43.68           C  
ANISOU  429  CB  ARG A  56     4434   7998   4163    110    346   1730       C  
ATOM    430  CG  ARG A  56      69.802  17.491 -84.782  1.00 41.79           C  
ANISOU  430  CG  ARG A  56     4150   7816   3914    130    371   1535       C  
ATOM    431  CD  ARG A  56      69.786  18.577 -83.725  1.00 40.89           C  
ANISOU  431  CD  ARG A  56     3947   7932   3657    162    415   1482       C  
ATOM    432  NE  ARG A  56      69.928  19.876 -84.370  1.00 45.62           N  
ANISOU  432  NE  ARG A  56     4533   8541   4260    183    426   1295       N  
ATOM    433  CZ  ARG A  56      71.092  20.392 -84.748  1.00 40.05           C  
ANISOU  433  CZ  ARG A  56     3851   7817   3550    235    402   1177       C  
ATOM    434  NH1 ARG A  56      72.222  19.730 -84.530  1.00 38.58           N  
ANISOU  434  NH1 ARG A  56     3680   7618   3362    290    366   1221       N  
ATOM    435  NH2 ARG A  56      71.130  21.573 -85.343  1.00 30.48           N  
ANISOU  435  NH2 ARG A  56     2644   6599   2338    232    412   1021       N  
ATOM    436  N   TYR A  57      70.808  14.947 -87.395  1.00 39.34           N  
ANISOU  436  N   TYR A  57     4122   6913   3913    134    267   1557       N  
ATOM    437  CA  TYR A  57      71.950  14.816 -88.304  1.00 37.06           C  
ANISOU  437  CA  TYR A  57     3895   6502   3684    216    258   1442       C  
ATOM    438  C   TYR A  57      72.701  13.505 -88.091  1.00 42.73           C  
ANISOU  438  C   TYR A  57     4684   7090   4461    302    225   1540       C  
ATOM    439  O   TYR A  57      73.907  13.427 -88.336  1.00 44.40           O  
ANISOU  439  O   TYR A  57     4893   7279   4697    420    225   1467       O  
ATOM    440  CB  TYR A  57      72.915  15.996 -88.165  1.00 32.44           C  
ANISOU  440  CB  TYR A  57     3224   6072   3028    291    283   1305       C  
ATOM    441  CG  TYR A  57      72.444  17.291 -88.787  1.00 39.50           C  
ANISOU  441  CG  TYR A  57     4096   7018   3893    226    309   1168       C  
ATOM    442  CD1 TYR A  57      72.493  17.482 -90.161  1.00 30.43           C  
ANISOU  442  CD1 TYR A  57     3027   5732   2802    186    313   1052       C  
ATOM    443  CD2 TYR A  57      71.987  18.339 -88.000  1.00 40.18           C  
ANISOU  443  CD2 TYR A  57     4095   7285   3887    210    328   1151       C  
ATOM    444  CE1 TYR A  57      72.080  18.672 -90.734  1.00 29.41           C  
ANISOU  444  CE1 TYR A  57     2893   5637   2643    130    322    942       C  
ATOM    445  CE2 TYR A  57      71.573  19.535 -88.567  1.00 34.23           C  
ANISOU  445  CE2 TYR A  57     3335   6556   3117    167    342   1028       C  
ATOM    446  CZ  TYR A  57      71.623  19.694 -89.934  1.00 33.41           C  
ANISOU  446  CZ  TYR A  57     3313   6306   3075    127    332    933       C  
ATOM    447  OH  TYR A  57      71.212  20.878 -90.505  1.00 35.69           O  
ANISOU  447  OH  TYR A  57     3613   6605   3345     86    332    827       O  
ATOM    448  N   LEU A  58      71.993  12.473 -87.627  1.00 47.19           N  
ANISOU  448  N   LEU A  58     5310   7568   5051    245    196   1710       N  
ATOM    449  CA  LEU A  58      72.592  11.171 -87.327  1.00 52.77           C  
ANISOU  449  CA  LEU A  58     6107   8127   5817    328    151   1831       C  
ATOM    450  C   LEU A  58      73.800  11.312 -86.403  1.00 52.55           C  
ANISOU  450  C   LEU A  58     5997   8240   5730    485    131   1857       C  
ATOM    451  O   LEU A  58      74.818  10.634 -86.562  1.00 57.66           O  
ANISOU  451  O   LEU A  58     6683   8781   6446    622    101   1856       O  
ATOM    452  CB  LEU A  58      72.959  10.425 -88.610  1.00 59.83           C  
ANISOU  452  CB  LEU A  58     7138   8759   6837    358    144   1743       C  
ATOM    453  CG  LEU A  58      71.843   9.499 -89.102  1.00 67.38           C  
ANISOU  453  CG  LEU A  58     8232   9507   7864    211    117   1825       C  
ATOM    454  CD1 LEU A  58      71.577   9.688 -90.593  1.00 67.07           C  
ANISOU  454  CD1 LEU A  58     8274   9329   7881    139    132   1659       C  
ATOM    455  CD2 LEU A  58      72.161   8.042 -88.767  1.00 68.21           C  
ANISOU  455  CD2 LEU A  58     8472   9401   8042    270     66   1970       C  
ATOM    456  N   GLY A  59      73.684  12.212 -85.428  1.00 50.50           N  
ANISOU  456  N   GLY A  59     5618   8228   5341    469    145   1874       N  
ATOM    457  CA  GLY A  59      74.691  12.357 -84.398  1.00 43.49           C  
ANISOU  457  CA  GLY A  59     4650   7502   4371    588    109   1918       C  
ATOM    458  C   GLY A  59      75.869  13.242 -84.738  1.00 46.36           C  
ANISOU  458  C   GLY A  59     4917   7970   4726    685    119   1742       C  
ATOM    459  O   GLY A  59      76.832  13.275 -83.967  1.00 51.36           O  
ANISOU  459  O   GLY A  59     5477   8731   5308    790     72   1775       O  
ATOM    460  N   LYS A  60      75.823  13.973 -85.851  1.00 44.08           N  
ANISOU  460  N   LYS A  60     4627   7643   4480    641    172   1564       N  
ATOM    461  CA  LYS A  60      76.949  14.779 -86.301  1.00 47.04           C  
ANISOU  461  CA  LYS A  60     4919   8101   4852    708    192   1397       C  
ATOM    462  C   LYS A  60      76.764  16.267 -86.019  1.00 44.01           C  
ANISOU  462  C   LYS A  60     4452   7914   4355    632    223   1289       C  
ATOM    463  O   LYS A  60      77.507  17.089 -86.568  1.00 42.80           O  
ANISOU  463  O   LYS A  60     4250   7814   4199    640    249   1136       O  
ATOM    464  CB  LYS A  60      77.202  14.541 -87.789  1.00 48.60           C  
ANISOU  464  CB  LYS A  60     5190   8110   5165    713    234   1268       C  
ATOM    465  CG  LYS A  60      77.560  13.096 -88.103  1.00 57.54           C  
ANISOU  465  CG  LYS A  60     6413   9033   6415    812    209   1343       C  
ATOM    466  CD  LYS A  60      78.230  12.956 -89.455  1.00 64.11           C  
ANISOU  466  CD  LYS A  60     7290   9730   7338    858    263   1182       C  
ATOM    467  CE  LYS A  60      79.174  11.765 -89.464  1.00 68.87           C  
ANISOU  467  CE  LYS A  60     7914  10207   8046   1036    240   1223       C  
ATOM    468  NZ  LYS A  60      80.331  11.967 -88.543  1.00 71.85           N  
ANISOU  468  NZ  LYS A  60     8127  10778   8396   1175    200   1252       N  
ATOM    469  N   GLY A  61      75.798  16.626 -85.174  1.00 43.23           N  
ANISOU  469  N   GLY A  61     4342   7922   4162    559    226   1363       N  
ATOM    470  CA  GLY A  61      75.649  18.005 -84.774  1.00 33.27           C  
ANISOU  470  CA  GLY A  61     3014   6839   2789    510    253   1260       C  
ATOM    471  C   GLY A  61      76.836  18.498 -83.970  1.00 35.29           C  
ANISOU  471  C   GLY A  61     3176   7276   2955    576    217   1223       C  
ATOM    472  O   GLY A  61      77.604  17.728 -83.390  1.00 35.10           O  
ANISOU  472  O   GLY A  61     3123   7284   2931    665    159   1321       O  
ATOM    473  N   VAL A  62      76.995  19.820 -83.950  1.00 33.05           N  
ANISOU  473  N   VAL A  62     2851   7110   2596    530    241   1079       N  
ATOM    474  CA  VAL A  62      78.052  20.449 -83.166  1.00 34.13           C  
ANISOU  474  CA  VAL A  62     2900   7436   2632    559    200   1027       C  
ATOM    475  C   VAL A  62      77.446  21.516 -82.260  1.00 38.00           C  
ANISOU  475  C   VAL A  62     3383   8083   2971    496    218    983       C  
ATOM    476  O   VAL A  62      78.070  22.553 -82.007  1.00 33.53           O  
ANISOU  476  O   VAL A  62     2779   7637   2326    468    207    860       O  
ATOM    477  CB  VAL A  62      79.150  21.046 -84.067  1.00 34.23           C  
ANISOU  477  CB  VAL A  62     2868   7437   2700    558    210    870       C  
ATOM    478  CG1 VAL A  62      79.995  19.941 -84.695  1.00 33.89           C  
ANISOU  478  CG1 VAL A  62     2803   7289   2785    655    194    910       C  
ATOM    479  CG2 VAL A  62      78.536  21.936 -85.134  1.00 31.77           C  
ANISOU  479  CG2 VAL A  62     2628   7021   2422    465    274    737       C  
ATOM    480  N   LEU A  63      76.230  21.264 -81.761  1.00 33.70           N  
ANISOU  480  N   LEU A  63     2878   7541   2386    468    250   1077       N  
ATOM    481  CA  LEU A  63      75.595  22.198 -80.836  1.00 45.06           C  
ANISOU  481  CA  LEU A  63     4309   9135   3675    425    283   1033       C  
ATOM    482  C   LEU A  63      76.382  22.344 -79.543  1.00 42.08           C  
ANISOU  482  C   LEU A  63     3887   8948   3152    448    225   1056       C  
ATOM    483  O   LEU A  63      76.421  23.436 -78.963  1.00 45.34           O  
ANISOU  483  O   LEU A  63     4297   9422   3509    410    223    920       O  
ATOM    484  CB  LEU A  63      74.166  21.745 -80.521  1.00 34.18           C  
ANISOU  484  CB  LEU A  63     2957   7730   2299    393    336   1141       C  
ATOM    485  CG  LEU A  63      73.200  21.692 -81.707  1.00 34.22           C  
ANISOU  485  CG  LEU A  63     2997   7568   2436    354    383   1119       C  
ATOM    486  CD1 LEU A  63      71.838  21.175 -81.268  1.00 36.77           C  
ANISOU  486  CD1 LEU A  63     3314   7900   2755    311    429   1239       C  
ATOM    487  CD2 LEU A  63      73.083  23.060 -82.360  1.00 32.40           C  
ANISOU  487  CD2 LEU A  63     2779   7312   2220    332    408    927       C  
ATOM    488  N   LYS A  64      77.002  21.262 -79.065  1.00 45.45           N  
ANISOU  488  N   LYS A  64     4292   9413   3563    508    157   1212       N  
ATOM    489  CA  LYS A  64      77.775  21.351 -77.830  1.00 45.07           C  
ANISOU  489  CA  LYS A  64     4200   9542   3382    527     81   1243       C  
ATOM    490  C   LYS A  64      79.030  22.196 -78.020  1.00 41.63           C  
ANISOU  490  C   LYS A  64     3696   9208   2914    529     27   1097       C  
ATOM    491  O   LYS A  64      79.357  23.027 -77.166  1.00 45.20           O  
ANISOU  491  O   LYS A  64     4130   9766   3279    483      2   1001       O  
ATOM    492  CB  LYS A  64      78.138  19.952 -77.329  1.00 48.30           C  
ANISOU  492  CB  LYS A  64     4610   9958   3784    603      2   1467       C  
ATOM    493  CG  LYS A  64      76.939  19.069 -77.007  1.00 48.10           C  
ANISOU  493  CG  LYS A  64     4659   9839   3778    572     49   1626       C  
ATOM    494  CD  LYS A  64      77.384  17.708 -76.495  1.00 47.73           C  
ANISOU  494  CD  LYS A  64     4637   9765   3734    644    -43   1850       C  
ATOM    495  CE  LYS A  64      76.211  16.750 -76.381  1.00 52.30           C  
ANISOU  495  CE  LYS A  64     5302  10221   4347    591      6   2017       C  
ATOM    496  NZ  LYS A  64      76.657  15.384 -75.993  1.00 54.23           N  
ANISOU  496  NZ  LYS A  64     5600  10389   4616    662    -92   2240       N  
ATOM    497  N   ALA A  65      79.746  21.999 -79.131  1.00 40.45           N  
ANISOU  497  N   ALA A  65     3509   8940   2919    563     19   1043       N  
ATOM    498  CA  ALA A  65      80.927  22.816 -79.397  1.00 44.44           C  
ANISOU  498  CA  ALA A  65     3934   9528   3423    541    -18    895       C  
ATOM    499  C   ALA A  65      80.556  24.285 -79.547  1.00 43.75           C  
ANISOU  499  C   ALA A  65     3893   9465   3264    432     39    712       C  
ATOM    500  O   ALA A  65      81.237  25.164 -79.006  1.00 41.70           O  
ANISOU  500  O   ALA A  65     3596   9353   2894    378     -6    611       O  
ATOM    501  CB  ALA A  65      81.648  22.315 -80.651  1.00 36.71           C  
ANISOU  501  CB  ALA A  65     2910   8409   2630    591     -7    864       C  
ATOM    502  N   VAL A  66      79.473  24.567 -80.277  1.00 36.26           N  
ANISOU  502  N   VAL A  66     3031   8367   2379    399    127    669       N  
ATOM    503  CA  VAL A  66      79.019  25.944 -80.448  1.00 40.10           C  
ANISOU  503  CA  VAL A  66     3580   8814   2842    315    171    500       C  
ATOM    504  C   VAL A  66      78.694  26.572 -79.096  1.00 43.68           C  
ANISOU  504  C   VAL A  66     4054   9345   3199    288    149    462       C  
ATOM    505  O   VAL A  66      79.007  27.743 -78.847  1.00 47.10           O  
ANISOU  505  O   VAL A  66     4513   9798   3586    223    137    314       O  
ATOM    506  CB  VAL A  66      77.814  25.985 -81.410  1.00 34.92           C  
ANISOU  506  CB  VAL A  66     3005   7966   2299    305    245    488       C  
ATOM    507  CG1 VAL A  66      77.114  27.325 -81.341  1.00 32.60           C  
ANISOU  507  CG1 VAL A  66     2786   7597   2004    251    270    342       C  
ATOM    508  CG2 VAL A  66      78.282  25.713 -82.831  1.00 35.51           C  
ANISOU  508  CG2 VAL A  66     3082   7917   2493    299    266    461       C  
ATOM    509  N   ASP A  67      78.090  25.797 -78.193  1.00 37.63           N  
ANISOU  509  N   ASP A  67     3288   8620   2391    329    149    596       N  
ATOM    510  CA  ASP A  67      77.744  26.330 -76.880  1.00 44.82           C  
ANISOU  510  CA  ASP A  67     4225   9610   3194    303    146    561       C  
ATOM    511  C   ASP A  67      78.989  26.583 -76.034  1.00 41.64           C  
ANISOU  511  C   ASP A  67     3774   9370   2679    279     59    532       C  
ATOM    512  O   ASP A  67      79.073  27.599 -75.334  1.00 39.95           O  
ANISOU  512  O   ASP A  67     3597   9201   2380    222     52    407       O  
ATOM    513  CB  ASP A  67      76.786  25.378 -76.168  1.00 58.14           C  
ANISOU  513  CB  ASP A  67     5925  11306   4859    335    177    719       C  
ATOM    514  CG  ASP A  67      76.425  25.853 -74.785  1.00 71.02           C  
ANISOU  514  CG  ASP A  67     7589  13035   6361    306    187    686       C  
ATOM    515  OD1 ASP A  67      76.971  25.298 -73.808  1.00 79.23           O  
ANISOU  515  OD1 ASP A  67     8609  14195   7300    310    129    784       O  
ATOM    516  OD2 ASP A  67      75.603  26.787 -74.674  1.00 73.97           O  
ANISOU  516  OD2 ASP A  67     8015  13365   6726    285    251    563       O  
ATOM    517  N   HIS A  68      79.966  25.674 -76.086  1.00 39.24           N  
ANISOU  517  N   HIS A  68     3386   9153   2371    326    -15    648       N  
ATOM    518  CA  HIS A  68      81.224  25.892 -75.373  1.00 43.67           C  
ANISOU  518  CA  HIS A  68     3876   9875   2840    305   -115    624       C  
ATOM    519  C   HIS A  68      81.885  27.203 -75.786  1.00 40.41           C  
ANISOU  519  C   HIS A  68     3456   9479   2420    212   -123    423       C  
ATOM    520  O   HIS A  68      82.510  27.877 -74.960  1.00 48.14           O  
ANISOU  520  O   HIS A  68     4426  10564   3300    147   -180    345       O  
ATOM    521  CB  HIS A  68      82.175  24.721 -75.614  1.00 41.32           C  
ANISOU  521  CB  HIS A  68     3476   9645   2579    395   -200    774       C  
ATOM    522  CG  HIS A  68      81.877  23.521 -74.773  1.00 43.40           C  
ANISOU  522  CG  HIS A  68     3757   9919   2812    467   -237    979       C  
ATOM    523  ND1 HIS A  68      81.824  22.243 -75.288  1.00 47.29           N  
ANISOU  523  ND1 HIS A  68     4237  10335   3395    570   -254   1150       N  
ATOM    524  CD2 HIS A  68      81.625  23.403 -73.448  1.00 44.11           C  
ANISOU  524  CD2 HIS A  68     3893  10078   2788    444   -262   1043       C  
ATOM    525  CE1 HIS A  68      81.547  21.391 -74.317  1.00 46.34           C  
ANISOU  525  CE1 HIS A  68     4159  10224   3225    600   -290   1316       C  
ATOM    526  NE2 HIS A  68      81.423  22.069 -73.191  1.00 44.90           N  
ANISOU  526  NE2 HIS A  68     4009  10140   2910    522   -294   1255       N  
ATOM    527  N   ILE A  69      81.763  27.579 -77.061  1.00 38.86           N  
ANISOU  527  N   ILE A  69     3274   9168   2321    193    -68    340       N  
ATOM    528  CA  ILE A  69      82.346  28.836 -77.524  1.00 39.69           C  
ANISOU  528  CA  ILE A  69     3393   9264   2423     85    -70    156       C  
ATOM    529  C   ILE A  69      81.571  30.019 -76.962  1.00 41.61           C  
ANISOU  529  C   ILE A  69     3765   9424   2619     21    -30     27       C  
ATOM    530  O   ILE A  69      82.149  30.948 -76.383  1.00 42.72           O  
ANISOU  530  O   ILE A  69     3928   9629   2677    -67    -72    -89       O  
ATOM    531  CB  ILE A  69      82.387  28.879 -79.062  1.00 37.14           C  
ANISOU  531  CB  ILE A  69     3073   8828   2210     74    -15    113       C  
ATOM    532  CG1 ILE A  69      83.351  27.825 -79.605  1.00 49.76           C  
ANISOU  532  CG1 ILE A  69     4535  10518   3852    141    -57    211       C  
ATOM    533  CG2 ILE A  69      82.771  30.272 -79.553  1.00 36.99           C  
ANISOU  533  CG2 ILE A  69     3108   8757   2191    -58     -4    -74       C  
ATOM    534  CD1 ILE A  69      83.319  27.696 -81.110  1.00 36.01           C  
ANISOU  534  CD1 ILE A  69     2810   8586   2287    137     22    175       C  
ATOM    535  N   ASN A  70      80.248  29.996 -77.119  1.00 41.46           N  
ANISOU  535  N   ASN A  70     3834   9266   2651     68     49     43       N  
ATOM    536  CA  ASN A  70      79.437  31.160 -76.783  1.00 48.73           C  
ANISOU  536  CA  ASN A  70     4878  10097   3540     34     97    -89       C  
ATOM    537  C   ASN A  70      79.363  31.382 -75.280  1.00 39.90           C  
ANISOU  537  C   ASN A  70     3787   9093   2279     25     76   -102       C  
ATOM    538  O   ASN A  70      79.394  32.528 -74.818  1.00 44.80           O  
ANISOU  538  O   ASN A  70     4496   9701   2824    -34     77   -248       O  
ATOM    539  CB  ASN A  70      78.036  31.000 -77.378  1.00 46.71           C  
ANISOU  539  CB  ASN A  70     4679   9691   3376     98    183    -58       C  
ATOM    540  CG  ASN A  70      78.040  31.074 -78.889  1.00 40.86           C  
ANISOU  540  CG  ASN A  70     3952   8813   2760     86    205    -81       C  
ATOM    541  OD1 ASN A  70      78.833  31.806 -79.477  1.00 47.55           O  
ANISOU  541  OD1 ASN A  70     4819   9635   3613     10    183   -185       O  
ATOM    542  ND2 ASN A  70      77.157  30.313 -79.528  1.00 45.18           N  
ANISOU  542  ND2 ASN A  70     4494   9273   3401    147    250     18       N  
ATOM    543  N   SER A  71      79.278  30.304 -74.500  1.00 46.94           N  
ANISOU  543  N   SER A  71     4621  10091   3122     78     57     51       N  
ATOM    544  CA  SER A  71      79.023  30.423 -73.066  1.00 46.30           C  
ANISOU  544  CA  SER A  71     4584  10111   2896     70     51     53       C  
ATOM    545  C   SER A  71      80.292  30.462 -72.222  1.00 49.72           C  
ANISOU  545  C   SER A  71     4973  10708   3211     14    -57     52       C  
ATOM    546  O   SER A  71      80.323  31.154 -71.199  1.00 48.79           O  
ANISOU  546  O   SER A  71     4928  10651   2959    -37    -71    -35       O  
ATOM    547  CB  SER A  71      78.137  29.269 -72.590  1.00 48.25           C  
ANISOU  547  CB  SER A  71     4813  10381   3138    140     92    227       C  
ATOM    548  OG  SER A  71      76.787  29.460 -72.979  1.00 57.34           O  
ANISOU  548  OG  SER A  71     6016  11413   4358    176    196    203       O  
ATOM    549  N   THR A  72      81.334  29.727 -72.615  1.00 53.19           N  
ANISOU  549  N   THR A  72     5295  11225   3691     25   -136    144       N  
ATOM    550  CA  THR A  72      82.530  29.564 -71.794  1.00 45.87           C  
ANISOU  550  CA  THR A  72     4299  10469   2660    -11   -254    177       C  
ATOM    551  C   THR A  72      83.763  30.230 -72.388  1.00 49.46           C  
ANISOU  551  C   THR A  72     4680  10971   3143    -93   -320     65       C  
ATOM    552  O   THR A  72      84.470  30.957 -71.683  1.00 47.51           O  
ANISOU  552  O   THR A  72     4444  10815   2793   -187   -390    -27       O  
ATOM    553  CB  THR A  72      82.810  28.068 -71.565  1.00 51.63           C  
ANISOU  553  CB  THR A  72     4939  11276   3403     83   -310    397       C  
ATOM    554  OG1 THR A  72      81.657  27.442 -70.985  1.00 46.56           O  
ANISOU  554  OG1 THR A  72     4370  10592   2727    133   -246    507       O  
ATOM    555  CG2 THR A  72      84.013  27.873 -70.636  1.00 48.61           C  
ANISOU  555  CG2 THR A  72     4488  11066   2914     58   -447    444       C  
ATOM    556  N   ILE A  73      84.049  30.003 -73.673  1.00 51.01           N  
ANISOU  556  N   ILE A  73     4802  11110   3468    -73   -300     69       N  
ATOM    557  CA  ILE A  73      85.274  30.545 -74.256  1.00 49.65           C  
ANISOU  557  CA  ILE A  73     4538  11008   3320   -162   -358    -26       C  
ATOM    558  C   ILE A  73      85.161  32.052 -74.448  1.00 44.60           C  
ANISOU  558  C   ILE A  73     4014  10274   2657   -297   -323   -229       C  
ATOM    559  O   ILE A  73      86.093  32.801 -74.132  1.00 48.61           O  
ANISOU  559  O   ILE A  73     4498  10866   3104   -417   -393   -328       O  
ATOM    560  CB  ILE A  73      85.609  29.827 -75.576  1.00 43.37           C  
ANISOU  560  CB  ILE A  73     3634  10191   2654   -100   -339     35       C  
ATOM    561  CG1 ILE A  73      85.840  28.340 -75.313  1.00 43.91           C  
ANISOU  561  CG1 ILE A  73     3600  10339   2747     43   -393    238       C  
ATOM    562  CG2 ILE A  73      86.840  30.442 -76.215  1.00 43.83           C  
ANISOU  562  CG2 ILE A  73     3585  10332   2736   -210   -385    -75       C  
ATOM    563  CD1 ILE A  73      86.390  27.580 -76.486  1.00 43.17           C  
ANISOU  563  CD1 ILE A  73     3381  10247   2776    120   -399    296       C  
ATOM    564  N   ALA A  74      84.020  32.518 -74.955  1.00 43.96           N  
ANISOU  564  N   ALA A  74     4066  10008   2629   -278   -222   -288       N  
ATOM    565  CA  ALA A  74      83.857  33.941 -75.250  1.00 43.13           C  
ANISOU  565  CA  ALA A  74     4095   9776   2517   -388   -190   -471       C  
ATOM    566  C   ALA A  74      84.075  34.834 -74.036  1.00 52.83           C  
ANISOU  566  C   ALA A  74     5412  11059   3602   -471   -239   -577       C  
ATOM    567  O   ALA A  74      84.884  35.774 -74.133  1.00 57.01           O  
ANISOU  567  O   ALA A  74     5964  11596   4100   -609   -287   -702       O  
ATOM    568  CB  ALA A  74      82.482  34.179 -75.883  1.00 41.56           C  
ANISOU  568  CB  ALA A  74     4021   9371   2397   -319    -83   -494       C  
ATOM    569  N   PRO A  75      83.427  34.618 -72.884  1.00 54.28           N  
ANISOU  569  N   PRO A  75     5654  11281   3687   -409   -230   -538       N  
ATOM    570  CA  PRO A  75      83.678  35.513 -71.743  1.00 59.48           C  
ANISOU  570  CA  PRO A  75     6415  11991   4193   -496   -277   -654       C  
ATOM    571  C   PRO A  75      85.102  35.449 -71.229  1.00 49.92           C  
ANISOU  571  C   PRO A  75     5096  10963   2908   -597   -408   -645       C  
ATOM    572  O   PRO A  75      85.574  36.422 -70.628  1.00 51.62           O  
ANISOU  572  O   PRO A  75     5395  11198   3020   -715   -462   -775       O  
ATOM    573  CB  PRO A  75      82.678  35.024 -70.685  1.00 48.85           C  
ANISOU  573  CB  PRO A  75     5130  10676   2756   -396   -230   -582       C  
ATOM    574  CG  PRO A  75      82.466  33.599 -71.014  1.00 47.70           C  
ANISOU  574  CG  PRO A  75     4855  10575   2695   -288   -217   -384       C  
ATOM    575  CD  PRO A  75      82.497  33.532 -72.516  1.00 45.58           C  
ANISOU  575  CD  PRO A  75     4533  10192   2595   -274   -180   -386       C  
ATOM    576  N   ALA A  76      85.806  34.338 -71.445  1.00 49.74           N  
ANISOU  576  N   ALA A  76     4891  11072   2936   -549   -466   -496       N  
ATOM    577  CA  ALA A  76      87.184  34.241 -70.974  1.00 55.46           C  
ANISOU  577  CA  ALA A  76     5488  11981   3602   -631   -599   -478       C  
ATOM    578  C   ALA A  76      88.122  35.077 -71.839  1.00 58.94           C  
ANISOU  578  C   ALA A  76     5876  12413   4105   -777   -625   -602       C  
ATOM    579  O   ALA A  76      88.982  35.796 -71.319  1.00 58.35           O  
ANISOU  579  O   ALA A  76     5799  12421   3951   -916   -713   -691       O  
ATOM    580  CB  ALA A  76      87.628  32.781 -70.947  1.00 51.67           C  
ANISOU  580  CB  ALA A  76     4834  11633   3166   -510   -654   -276       C  
ATOM    581  N   LEU A  77      87.971  35.002 -73.164  1.00 54.31           N  
ANISOU  581  N   LEU A  77     5252  11729   3655   -760   -551   -608       N  
ATOM    582  CA  LEU A  77      88.841  35.789 -74.035  1.00 53.81           C  
ANISOU  582  CA  LEU A  77     5144  11657   3645   -917   -564   -721       C  
ATOM    583  C   LEU A  77      88.514  37.273 -73.960  1.00 53.84           C  
ANISOU  583  C   LEU A  77     5357  11502   3597  -1057   -538   -903       C  
ATOM    584  O   LEU A  77      89.401  38.114 -74.143  1.00 60.28           O  
ANISOU  584  O   LEU A  77     6164  12339   4400  -1234   -587  -1008       O  
ATOM    585  CB  LEU A  77      88.734  35.303 -75.476  1.00 47.76           C  
ANISOU  585  CB  LEU A  77     4301  10828   3019   -868   -487   -680       C  
ATOM    586  CG  LEU A  77      89.113  33.850 -75.742  1.00 49.06           C  
ANISOU  586  CG  LEU A  77     4266  11127   3249   -722   -510   -512       C  
ATOM    587  CD1 LEU A  77      89.316  33.668 -77.223  1.00 45.94           C  
ANISOU  587  CD1 LEU A  77     3794  10690   2972   -732   -447   -524       C  
ATOM    588  CD2 LEU A  77      90.367  33.465 -74.982  1.00 49.62           C  
ANISOU  588  CD2 LEU A  77     4160  11416   3276   -743   -636   -457       C  
ATOM    589  N   ILE A  78      87.251  37.610 -73.702  1.00 56.73           N  
ANISOU  589  N   ILE A  78     5912  11703   3939   -977   -462   -941       N  
ATOM    590  CA  ILE A  78      86.881  39.007 -73.511  1.00 58.11           C  
ANISOU  590  CA  ILE A  78     6306  11716   4055  -1076   -444  -1114       C  
ATOM    591  C   ILE A  78      87.519  39.558 -72.242  1.00 58.08           C  
ANISOU  591  C   ILE A  78     6346  11821   3899  -1181   -544  -1187       C  
ATOM    592  O   ILE A  78      88.015  40.692 -72.221  1.00 64.02           O  
ANISOU  592  O   ILE A  78     7201  12512   4610  -1344   -584  -1330       O  
ATOM    593  CB  ILE A  78      85.348  39.147 -73.487  1.00 49.15           C  
ANISOU  593  CB  ILE A  78     5343  10403   2931   -934   -336  -1130       C  
ATOM    594  CG1 ILE A  78      84.770  38.864 -74.877  1.00 47.02           C  
ANISOU  594  CG1 ILE A  78     5060   9993   2813   -867   -250  -1087       C  
ATOM    595  CG2 ILE A  78      84.951  40.525 -73.015  1.00 50.51           C  
ANISOU  595  CG2 ILE A  78     5748  10429   3013  -1001   -327  -1309       C  
ATOM    596  CD1 ILE A  78      83.248  38.848 -74.935  1.00 45.66           C  
ANISOU  596  CD1 ILE A  78     5012   9666   2670   -714   -148  -1079       C  
ATOM    597  N   SER A  79      87.536  38.761 -71.168  1.00 57.87           N  
ANISOU  597  N   SER A  79     6252  11955   3783  -1098   -592  -1086       N  
ATOM    598  CA  SER A  79      88.036  39.248 -69.886  1.00 62.88           C  
ANISOU  598  CA  SER A  79     6948  12690   4252  -1189   -690  -1151       C  
ATOM    599  C   SER A  79      89.544  39.393 -69.866  1.00 63.99           C  
ANISOU  599  C   SER A  79     6940  12989   4383  -1351   -818  -1162       C  
ATOM    600  O   SER A  79      90.073  40.164 -69.056  1.00 60.60           O  
ANISOU  600  O   SER A  79     6591  12603   3833  -1484   -905  -1263       O  
ATOM    601  CB  SER A  79      87.590  38.323 -68.746  1.00 62.61           C  
ANISOU  601  CB  SER A  79     6897  12778   4112  -1060   -704  -1028       C  
ATOM    602  OG  SER A  79      88.015  36.987 -68.946  1.00 75.52           O  
ANISOU  602  OG  SER A  79     8320  14558   5817   -969   -741   -839       O  
ATOM    603  N   SER A  80      90.248  38.673 -70.739  1.00 65.60           N  
ANISOU  603  N   SER A  80     6927  13287   4710  -1344   -830  -1063       N  
ATOM    604  CA  SER A  80      91.704  38.739 -70.730  1.00 65.21           C  
ANISOU  604  CA  SER A  80     6702  13412   4664  -1486   -946  -1064       C  
ATOM    605  C   SER A  80      92.199  40.124 -71.120  1.00 68.35           C  
ANISOU  605  C   SER A  80     7200  13712   5059  -1711   -958  -1238       C  
ATOM    606  O   SER A  80      93.317  40.502 -70.756  1.00 62.37           O  
ANISOU  606  O   SER A  80     6356  13084   4257  -1870  -1067  -1277       O  
ATOM    607  CB  SER A  80      92.279  37.680 -71.669  1.00 59.92           C  
ANISOU  607  CB  SER A  80     5782  12851   4134  -1409   -936   -932       C  
ATOM    608  OG  SER A  80      91.956  37.953 -73.026  1.00 55.85           O  
ANISOU  608  OG  SER A  80     5288  12191   3742  -1431   -825   -979       O  
ATOM    609  N   GLY A  81      91.382  40.894 -71.840  1.00 65.84           N  
ANISOU  609  N   GLY A  81     7068  13159   4788  -1730   -853  -1339       N  
ATOM    610  CA  GLY A  81      91.847  42.156 -72.371  1.00 67.97           C  
ANISOU  610  CA  GLY A  81     7442  13309   5073  -1945   -859  -1487       C  
ATOM    611  C   GLY A  81      92.981  42.033 -73.362  1.00 68.74           C  
ANISOU  611  C   GLY A  81     7329  13512   5276  -2082   -872  -1459       C  
ATOM    612  O   GLY A  81      93.577  43.049 -73.728  1.00 69.55           O  
ANISOU  612  O   GLY A  81     7492  13549   5384  -2298   -890  -1567       O  
ATOM    613  N   LEU A  82      93.295  40.818 -73.814  1.00 67.56           N  
ANISOU  613  N   LEU A  82     6939  13519   5210  -1963   -858  -1317       N  
ATOM    614  CA  LEU A  82      94.377  40.634 -74.777  1.00 62.65           C  
ANISOU  614  CA  LEU A  82     6099  13015   4689  -2073   -855  -1293       C  
ATOM    615  C   LEU A  82      93.993  41.195 -76.141  1.00 63.40           C  
ANISOU  615  C   LEU A  82     6297  12916   4876  -2154   -738  -1358       C  
ATOM    616  O   LEU A  82      92.854  41.047 -76.595  1.00 61.37           O  
ANISOU  616  O   LEU A  82     6178  12485   4654  -2022   -649  -1345       O  
ATOM    617  CB  LEU A  82      94.734  39.152 -74.916  1.00 58.15           C  
ANISOU  617  CB  LEU A  82     5265  12642   4188  -1887   -867  -1129       C  
ATOM    618  CG  LEU A  82      95.246  38.460 -73.655  1.00 63.77           C  
ANISOU  618  CG  LEU A  82     5854  13553   4822  -1799   -995  -1035       C  
ATOM    619  CD1 LEU A  82      95.448  36.976 -73.902  1.00 60.32           C  
ANISOU  619  CD1 LEU A  82     5197  13248   4474  -1584   -997   -865       C  
ATOM    620  CD2 LEU A  82      96.536  39.116 -73.180  1.00 63.05           C  
ANISOU  620  CD2 LEU A  82     5666  13606   4684  -2006  -1112  -1098       C  
ATOM    621  N   SER A  83      94.948  41.852 -76.794  1.00 62.04           N  
ANISOU  621  N   SER A  83     6063  12770   4740  -2380   -739  -1421       N  
ATOM    622  CA  SER A  83      94.734  42.287 -78.168  1.00 58.50           C  
ANISOU  622  CA  SER A  83     5691  12160   4377  -2475   -630  -1463       C  
ATOM    623  C   SER A  83      94.618  41.072 -79.081  1.00 61.29           C  
ANISOU  623  C   SER A  83     5859  12599   4830  -2313   -553  -1353       C  
ATOM    624  O   SER A  83      95.201  40.016 -78.820  1.00 62.89           O  
ANISOU  624  O   SER A  83     5813  13022   5059  -2192   -593  -1253       O  
ATOM    625  CB  SER A  83      95.874  43.194 -78.633  1.00 61.03           C  
ANISOU  625  CB  SER A  83     5969  12512   4707  -2769   -643  -1539       C  
ATOM    626  OG  SER A  83      95.678  43.628 -79.967  1.00 62.01           O  
ANISOU  626  OG  SER A  83     6186  12474   4902  -2879   -534  -1571       O  
ATOM    627  N   VAL A  84      93.839  41.220 -80.155  1.00 62.27           N  
ANISOU  627  N   VAL A  84     6120  12530   5010  -2299   -449  -1369       N  
ATOM    628  CA  VAL A  84      93.672  40.131 -81.109  1.00 52.09           C  
ANISOU  628  CA  VAL A  84     4684  11299   3808  -2159   -374  -1281       C  
ATOM    629  C   VAL A  84      94.948  39.820 -81.872  1.00 53.16           C  
ANISOU  629  C   VAL A  84     4558  11627   4015  -2276   -351  -1267       C  
ATOM    630  O   VAL A  84      95.025  38.780 -82.535  1.00 53.19           O  
ANISOU  630  O   VAL A  84     4387  11719   4102  -2141   -300  -1191       O  
ATOM    631  CB  VAL A  84      92.530  40.457 -82.088  1.00 49.11           C  
ANISOU  631  CB  VAL A  84     4542  10653   3463  -2133   -275  -1307       C  
ATOM    632  CG1 VAL A  84      91.200  40.352 -81.370  1.00 47.83           C  
ANISOU  632  CG1 VAL A  84     4567  10336   3270  -1928   -277  -1282       C  
ATOM    633  CG2 VAL A  84      92.718  41.852 -82.666  1.00 50.04           C  
ANISOU  633  CG2 VAL A  84     4857  10586   3571  -2392   -248  -1418       C  
ATOM    634  N   VAL A  85      95.956  40.690 -81.792  1.00 58.87           N  
ANISOU  634  N   VAL A  85     5247  12405   4715  -2517   -379  -1337       N  
ATOM    635  CA  VAL A  85      97.228  40.394 -82.439  1.00 62.35           C  
ANISOU  635  CA  VAL A  85     5426  13034   5230  -2613   -344  -1318       C  
ATOM    636  C   VAL A  85      98.017  39.356 -81.644  1.00 67.48           C  
ANISOU  636  C   VAL A  85     5799  13934   5907  -2440   -427  -1225       C  
ATOM    637  O   VAL A  85      98.828  38.620 -82.216  1.00 67.11           O  
ANISOU  637  O   VAL A  85     5517  14023   5960  -2374   -383  -1172       O  
ATOM    638  CB  VAL A  85      98.041  41.685 -82.650  1.00 62.31           C  
ANISOU  638  CB  VAL A  85     5487  12997   5191  -2937   -342  -1414       C  
ATOM    639  CG1 VAL A  85      97.234  42.698 -83.449  1.00 59.75           C  
ANISOU  639  CG1 VAL A  85     5471  12382   4847  -3092   -266  -1489       C  
ATOM    640  CG2 VAL A  85      98.474  42.278 -81.317  1.00 66.20           C  
ANISOU  640  CG2 VAL A  85     6007  13553   5593  -3018   -478  -1451       C  
ATOM    641  N   GLU A  86      97.791  39.268 -80.331  1.00 70.48           N  
ANISOU  641  N   GLU A  86     6219  14356   6205  -2348   -545  -1200       N  
ATOM    642  CA  GLU A  86      98.495  38.305 -79.492  1.00 69.38           C  
ANISOU  642  CA  GLU A  86     5850  14431   6080  -2184   -644  -1099       C  
ATOM    643  C   GLU A  86      97.966  36.899 -79.744  1.00 65.88           C  
ANISOU  643  C   GLU A  86     5316  13997   5718  -1884   -607   -974       C  
ATOM    644  O   GLU A  86      97.233  36.349 -78.916  1.00 73.18           O  
ANISOU  644  O   GLU A  86     6312  14902   6590  -1708   -664   -901       O  
ATOM    645  CB  GLU A  86      98.347  38.671 -78.012  1.00 69.21           C  
ANISOU  645  CB  GLU A  86     5932  14435   5929  -2194   -779  -1108       C  
ATOM    646  CG  GLU A  86      98.533  40.152 -77.701  1.00 75.76           C  
ANISOU  646  CG  GLU A  86     6940  15178   6669  -2475   -814  -1244       C  
ATOM    647  CD  GLU A  86      99.983  40.603 -77.764  1.00 88.30           C  
ANISOU  647  CD  GLU A  86     8343  16931   8276  -2685   -864  -1279       C  
ATOM    648  OE1 GLU A  86     100.875  39.753 -77.973  1.00 88.44           O  
ANISOU  648  OE1 GLU A  86     8083  17140   8379  -2594   -877  -1198       O  
ATOM    649  OE2 GLU A  86     100.231  41.817 -77.597  1.00 89.97           O  
ANISOU  649  OE2 GLU A  86     8694  17068   8423  -2935   -891  -1386       O  
ATOM    650  N   GLN A  87      98.337  36.310 -80.885  1.00 62.77           N  
ANISOU  650  N   GLN A  87     4779  13617   5453  -1826   -506   -947       N  
ATOM    651  CA  GLN A  87      97.762  35.028 -81.280  1.00 64.26           C  
ANISOU  651  CA  GLN A  87     4919  13762   5736  -1551   -455   -838       C  
ATOM    652  C   GLN A  87      98.136  33.924 -80.299  1.00 64.88           C  
ANISOU  652  C   GLN A  87     4852  13965   5835  -1321   -567   -707       C  
ATOM    653  O   GLN A  87      97.269  33.176 -79.830  1.00 59.12           O  
ANISOU  653  O   GLN A  87     4199  13179   5087  -1126   -593   -613       O  
ATOM    654  CB  GLN A  87      98.210  34.656 -82.693  1.00 54.89           C  
ANISOU  654  CB  GLN A  87     3622  12542   4691  -1539   -316   -848       C  
ATOM    655  CG  GLN A  87      97.665  33.317 -83.173  1.00 53.27           C  
ANISOU  655  CG  GLN A  87     3385  12254   4601  -1255   -255   -742       C  
ATOM    656  CD  GLN A  87      96.195  33.383 -83.556  1.00 59.84           C  
ANISOU  656  CD  GLN A  87     4427  12907   5403  -1224   -192   -745       C  
ATOM    657  OE1 GLN A  87      95.690  34.439 -83.933  1.00 50.32           O  
ANISOU  657  OE1 GLN A  87     3378  11614   4128  -1428   -154   -844       O  
ATOM    658  NE2 GLN A  87      95.504  32.251 -83.462  1.00 49.14           N  
ANISOU  658  NE2 GLN A  87     3081  11488   4104   -972   -189   -632       N  
ATOM    659  N   GLU A  88      99.427  33.803 -79.977  1.00 59.02           N  
ANISOU  659  N   GLU A  88     3904  13390   5132  -1344   -638   -693       N  
ATOM    660  CA  GLU A  88      99.862  32.722 -79.097  1.00 63.70           C  
ANISOU  660  CA  GLU A  88     4353  14092   5758  -1123   -755   -561       C  
ATOM    661  C   GLU A  88      99.324  32.885 -77.679  1.00 60.72           C  
ANISOU  661  C   GLU A  88     4107  13739   5226  -1115   -886   -520       C  
ATOM    662  O   GLU A  88      99.038  31.884 -77.012  1.00 60.73           O  
ANISOU  662  O   GLU A  88     4096  13747   5230   -900   -955   -388       O  
ATOM    663  CB  GLU A  88     101.391  32.625 -79.074  1.00 65.41           C  
ANISOU  663  CB  GLU A  88     4310  14486   6058  -1158   -813   -562       C  
ATOM    664  CG  GLU A  88     101.874  31.316 -78.462  1.00 65.50           C  
ANISOU  664  CG  GLU A  88     4154  14579   6155   -889   -918   -416       C  
ATOM    665  CD  GLU A  88     103.381  31.205 -78.337  1.00 73.35           C  
ANISOU  665  CD  GLU A  88     4873  15759   7238   -908   -995   -413       C  
ATOM    666  OE1 GLU A  88     103.853  30.111 -77.959  1.00 73.61           O  
ANISOU  666  OE1 GLU A  88     4754  15846   7368   -679  -1079   -298       O  
ATOM    667  OE2 GLU A  88     104.093  32.195 -78.609  1.00 72.07           O  
ANISOU  667  OE2 GLU A  88     4647  15684   7053  -1150   -977   -523       O  
ATOM    668  N   LYS A  89      99.183  34.123 -77.198  1.00 61.15           N  
ANISOU  668  N   LYS A  89     4301  13787   5146  -1347   -918   -631       N  
ATOM    669  CA  LYS A  89      98.611  34.338 -75.871  1.00 62.81           C  
ANISOU  669  CA  LYS A  89     4665  13995   5205  -1343  -1023   -610       C  
ATOM    670  C   LYS A  89      97.173  33.838 -75.807  1.00 62.23           C  
ANISOU  670  C   LYS A  89     4777  13768   5099  -1178   -961   -550       C  
ATOM    671  O   LYS A  89      96.766  33.202 -74.827  1.00 59.13           O  
ANISOU  671  O   LYS A  89     4430  13395   4642  -1036  -1035   -446       O  
ATOM    672  CB  LYS A  89      98.663  35.822 -75.507  1.00 63.85           C  
ANISOU  672  CB  LYS A  89     4946  14098   5216  -1621  -1047   -762       C  
ATOM    673  CG  LYS A  89     100.053  36.425 -75.440  1.00 65.37           C  
ANISOU  673  CG  LYS A  89     4973  14443   5419  -1817  -1120   -822       C  
ATOM    674  CD  LYS A  89     100.687  36.197 -74.081  1.00 74.20           C  
ANISOU  674  CD  LYS A  89     6011  15724   6456  -1792  -1300   -762       C  
ATOM    675  CE  LYS A  89     101.742  37.252 -73.795  1.00 81.17           C  
ANISOU  675  CE  LYS A  89     6835  16712   7292  -2062  -1383   -866       C  
ATOM    676  NZ  LYS A  89     101.175  38.623 -73.929  1.00 84.58           N  
ANISOU  676  NZ  LYS A  89     7524  16979   7635  -2297  -1324  -1021       N  
ATOM    677  N   LEU A  90      96.391  34.115 -76.850  1.00 56.49           N  
ANISOU  677  N   LEU A  90     4159  12887   4415  -1203   -828   -610       N  
ATOM    678  CA  LEU A  90      94.992  33.708 -76.856  1.00 54.09           C  
ANISOU  678  CA  LEU A  90     4031  12435   4087  -1060   -767   -560       C  
ATOM    679  C   LEU A  90      94.851  32.204 -77.055  1.00 53.39           C  
ANISOU  679  C   LEU A  90     3829  12358   4100   -800   -759   -395       C  
ATOM    680  O   LEU A  90      94.033  31.560 -76.387  1.00 52.75           O  
ANISOU  680  O   LEU A  90     3841  12232   3970   -652   -780   -292       O  
ATOM    681  CB  LEU A  90      94.238  34.487 -77.933  1.00 52.04           C  
ANISOU  681  CB  LEU A  90     3924  12002   3848  -1171   -644   -673       C  
ATOM    682  CG  LEU A  90      93.969  35.941 -77.532  1.00 57.65           C  
ANISOU  682  CG  LEU A  90     4842  12612   4450  -1383   -651   -820       C  
ATOM    683  CD1 LEU A  90      93.561  36.774 -78.726  1.00 53.09           C  
ANISOU  683  CD1 LEU A  90     4396  11862   3913  -1521   -544   -931       C  
ATOM    684  CD2 LEU A  90      92.900  36.005 -76.447  1.00 52.15           C  
ANISOU  684  CD2 LEU A  90     4343  11823   3648  -1290   -672   -801       C  
ATOM    685  N   ASP A  91      95.653  31.622 -77.950  1.00 53.74           N  
ANISOU  685  N   ASP A  91     3683  12445   4291   -741   -724   -369       N  
ATOM    686  CA  ASP A  91      95.586  30.181 -78.183  1.00 56.33           C  
ANISOU  686  CA  ASP A  91     3920  12744   4739   -484   -715   -221       C  
ATOM    687  C   ASP A  91      96.002  29.390 -76.945  1.00 59.84           C  
ANISOU  687  C   ASP A  91     4296  13290   5149   -347   -856    -84       C  
ATOM    688  O   ASP A  91      95.345  28.405 -76.584  1.00 54.72           O  
ANISOU  688  O   ASP A  91     3705  12576   4509   -161   -873     53       O  
ATOM    689  CB  ASP A  91      96.453  29.801 -79.386  1.00 60.57           C  
ANISOU  689  CB  ASP A  91     4281  13281   5451   -451   -635   -245       C  
ATOM    690  CG  ASP A  91      95.831  30.217 -80.716  1.00 62.45           C  
ANISOU  690  CG  ASP A  91     4609  13378   5743   -531   -481   -337       C  
ATOM    691  OD1 ASP A  91      94.632  30.565 -80.733  1.00 51.84           O  
ANISOU  691  OD1 ASP A  91     3449  11927   4322   -560   -447   -355       O  
ATOM    692  OD2 ASP A  91      96.540  30.184 -81.748  1.00 65.63           O  
ANISOU  692  OD2 ASP A  91     4902  13771   6262   -562   -392   -390       O  
ATOM    693  N   ASN A  92      97.091  29.796 -76.282  1.00 57.89           N  
ANISOU  693  N   ASN A  92     3930  13200   4864   -445   -965   -112       N  
ATOM    694  CA  ASN A  92      97.508  29.100 -75.065  1.00 66.64           C  
ANISOU  694  CA  ASN A  92     4980  14410   5930   -329  -1118     18       C  
ATOM    695  C   ASN A  92      96.480  29.261 -73.951  1.00 66.04           C  
ANISOU  695  C   ASN A  92     5116  14296   5680   -340  -1160     59       C  
ATOM    696  O   ASN A  92      96.275  28.337 -73.156  1.00 64.22           O  
ANISOU  696  O   ASN A  92     4906  14071   5424   -185  -1240    209       O  
ATOM    697  CB  ASN A  92      98.881  29.599 -74.600  1.00 65.95           C  
ANISOU  697  CB  ASN A  92     4719  14506   5832   -454  -1235    -32       C  
ATOM    698  CG  ASN A  92     100.018  29.127 -75.501  1.00 70.07           C  
ANISOU  698  CG  ASN A  92     4994  15084   6545   -386  -1210    -33       C  
ATOM    699  OD1 ASN A  92     100.944  29.882 -75.800  1.00 68.73           O  
ANISOU  699  OD1 ASN A  92     4700  15019   6396   -555  -1211   -138       O  
ATOM    700  ND2 ASN A  92      99.952  27.872 -75.934  1.00 68.01           N  
ANISOU  700  ND2 ASN A  92     4667  14745   6428   -140  -1182     82       N  
ATOM    701  N   LEU A  93      95.814  30.415 -73.888  1.00 62.71           N  
ANISOU  701  N   LEU A  93     4864  13820   5142   -518  -1102    -75       N  
ATOM    702  CA  LEU A  93      94.797  30.629 -72.865  1.00 58.02           C  
ANISOU  702  CA  LEU A  93     4480  13173   4392   -525  -1117    -57       C  
ATOM    703  C   LEU A  93      93.620  29.673 -73.041  1.00 69.25           C  
ANISOU  703  C   LEU A  93     6003  14463   5844   -340  -1040     66       C  
ATOM    704  O   LEU A  93      93.074  29.161 -72.055  1.00 67.89           O  
ANISOU  704  O   LEU A  93     5925  14287   5582   -259  -1085    174       O  
ATOM    705  CB  LEU A  93      94.332  32.084 -72.902  1.00 57.93           C  
ANISOU  705  CB  LEU A  93     4636  13090   4285   -736  -1057   -242       C  
ATOM    706  CG  LEU A  93      93.166  32.475 -71.997  1.00 60.73           C  
ANISOU  706  CG  LEU A  93     5228  13349   4497   -745  -1034   -264       C  
ATOM    707  CD1 LEU A  93      93.477  32.125 -70.554  1.00 59.26           C  
ANISOU  707  CD1 LEU A  93     5045  13287   4185   -717  -1170   -178       C  
ATOM    708  CD2 LEU A  93      92.869  33.958 -72.144  1.00 59.20           C  
ANISOU  708  CD2 LEU A  93     5194  13055   4243   -942   -981   -461       C  
ATOM    709  N   MET A  94      93.220  29.408 -74.288  1.00 63.20           N  
ANISOU  709  N   MET A  94     5222  13588   5202   -281   -925     56       N  
ATOM    710  CA  MET A  94      92.147  28.448 -74.530  1.00 55.93           C  
ANISOU  710  CA  MET A  94     4387  12539   4323   -111   -858    179       C  
ATOM    711  C   MET A  94      92.618  27.011 -74.354  1.00 53.26           C  
ANISOU  711  C   MET A  94     3930  12226   4080     92   -931    365       C  
ATOM    712  O   MET A  94      91.810  26.135 -74.028  1.00 52.73           O  
ANISOU  712  O   MET A  94     3954  12076   4005    222   -922    504       O  
ATOM    713  CB  MET A  94      91.568  28.640 -75.932  1.00 51.44           C  
ANISOU  713  CB  MET A  94     3851  11843   3853   -120   -725    106       C  
ATOM    714  CG  MET A  94      91.228  30.077 -76.256  1.00 58.60           C  
ANISOU  714  CG  MET A  94     4875  12699   4691   -321   -661    -81       C  
ATOM    715  SD  MET A  94      90.205  30.248 -77.730  1.00 58.78           S  
ANISOU  715  SD  MET A  94     4999  12541   4795   -319   -518   -142       S  
ATOM    716  CE  MET A  94      90.765  28.871 -78.721  1.00 54.32           C  
ANISOU  716  CE  MET A  94     4235  11987   4419   -144   -504    -24       C  
ATOM    717  N   LEU A  95      93.909  26.751 -74.566  1.00 58.26           N  
ANISOU  717  N   LEU A  95     4366  12957   4812    120  -1001    369       N  
ATOM    718  CA  LEU A  95      94.447  25.416 -74.325  1.00 60.24           C  
ANISOU  718  CA  LEU A  95     4508  13215   5166    325  -1087    539       C  
ATOM    719  C   LEU A  95      94.364  25.043 -72.849  1.00 60.50           C  
ANISOU  719  C   LEU A  95     4610  13312   5065    358  -1220    665       C  
ATOM    720  O   LEU A  95      93.940  23.935 -72.503  1.00 61.54           O  
ANISOU  720  O   LEU A  95     4795  13368   5220    518  -1253    834       O  
ATOM    721  CB  LEU A  95      95.891  25.338 -74.821  1.00 62.90           C  
ANISOU  721  CB  LEU A  95     4611  13648   5640    342  -1131    495       C  
ATOM    722  CG  LEU A  95      96.045  25.010 -76.305  1.00 66.37           C  
ANISOU  722  CG  LEU A  95     4963  13986   6267    413  -1002    444       C  
ATOM    723  CD1 LEU A  95      97.500  25.099 -76.737  1.00 63.90           C  
ANISOU  723  CD1 LEU A  95     4416  13786   6077    401  -1028    378       C  
ATOM    724  CD2 LEU A  95      95.498  23.624 -76.555  1.00 67.99           C  
ANISOU  724  CD2 LEU A  95     5210  14039   6585    650   -983    598       C  
ATOM    725  N   GLU A  96      94.769  25.956 -71.962  1.00 59.86           N  
ANISOU  725  N   GLU A  96     4540  13364   4840    199  -1301    586       N  
ATOM    726  CA  GLU A  96      94.689  25.670 -70.533  1.00 72.28           C  
ANISOU  726  CA  GLU A  96     6191  15003   6267    213  -1428    695       C  
ATOM    727  C   GLU A  96      93.243  25.631 -70.060  1.00 72.00           C  
ANISOU  727  C   GLU A  96     6384  14862   6109    209  -1347    737       C  
ATOM    728  O   GLU A  96      92.898  24.848 -69.167  1.00 77.08           O  
ANISOU  728  O   GLU A  96     7107  15497   6684    294  -1413    892       O  
ATOM    729  CB  GLU A  96      95.483  26.706 -69.736  1.00 79.36           C  
ANISOU  729  CB  GLU A  96     7052  16064   7038     32  -1534    585       C  
ATOM    730  CG  GLU A  96      96.926  26.310 -69.463  1.00 87.57           C  
ANISOU  730  CG  GLU A  96     7876  17247   8150     79  -1698    640       C  
ATOM    731  CD  GLU A  96      97.689  27.385 -68.714  1.00 97.50           C  
ANISOU  731  CD  GLU A  96     9101  18665   9281   -121  -1806    525       C  
ATOM    732  OE1 GLU A  96      97.109  28.468 -68.481  1.00 99.48           O  
ANISOU  732  OE1 GLU A  96     9505  18896   9395   -296  -1744    390       O  
ATOM    733  OE2 GLU A  96      98.866  27.150 -68.359  1.00101.44           O  
ANISOU  733  OE2 GLU A  96     9422  19300   9822   -102  -1958    567       O  
ATOM    734  N   LEU A  97      92.386  26.470 -70.645  1.00 66.59           N  
ANISOU  734  N   LEU A  97     5808  14092   5402    109  -1203    602       N  
ATOM    735  CA  LEU A  97      90.976  26.471 -70.272  1.00 64.38           C  
ANISOU  735  CA  LEU A  97     5728  13704   5028    111  -1109    628       C  
ATOM    736  C   LEU A  97      90.317  25.146 -70.622  1.00 65.21           C  
ANISOU  736  C   LEU A  97     5859  13691   5229    287  -1068    809       C  
ATOM    737  O   LEU A  97      89.492  24.630 -69.859  1.00 65.36           O  
ANISOU  737  O   LEU A  97     6003  13667   5162    325  -1061    923       O  
ATOM    738  CB  LEU A  97      90.260  27.625 -70.964  1.00 63.66           C  
ANISOU  738  CB  LEU A  97     5732  13526   4929    -12   -971    442       C  
ATOM    739  CG  LEU A  97      89.654  28.663 -70.028  1.00 72.16           C  
ANISOU  739  CG  LEU A  97     6976  14603   5839   -144   -951    328       C  
ATOM    740  CD1 LEU A  97      89.746  30.027 -70.676  1.00 72.05           C  
ANISOU  740  CD1 LEU A  97     6994  14547   5837   -297   -891    114       C  
ATOM    741  CD2 LEU A  97      88.208  28.301 -69.689  1.00 70.34           C  
ANISOU  741  CD2 LEU A  97     6907  14257   5563    -80   -851    395       C  
ATOM    742  N   ASP A  98      90.658  24.587 -71.782  1.00 63.49           N  
ANISOU  742  N   ASP A  98     5527  13409   5185    388  -1036    833       N  
ATOM    743  CA  ASP A  98      90.216  23.237 -72.104  1.00 59.44           C  
ANISOU  743  CA  ASP A  98     5032  12774   4779    564  -1023   1012       C  
ATOM    744  C   ASP A  98      90.896  22.215 -71.201  1.00 59.10           C  
ANISOU  744  C   ASP A  98     4941  12780   4734    680  -1178   1190       C  
ATOM    745  O   ASP A  98      90.262  21.254 -70.749  1.00 57.18           O  
ANISOU  745  O   ASP A  98     4799  12451   4476    771  -1193   1360       O  
ATOM    746  CB  ASP A  98      90.492  22.942 -73.576  1.00 53.35           C  
ANISOU  746  CB  ASP A  98     4154  11916   4199    643   -954    972       C  
ATOM    747  CG  ASP A  98      90.329  21.481 -73.918  1.00 52.90           C  
ANISOU  747  CG  ASP A  98     4094  11727   4279    841   -967   1152       C  
ATOM    748  OD1 ASP A  98      89.240  21.093 -74.393  1.00 54.07           O  
ANISOU  748  OD1 ASP A  98     4357  11734   4454    875   -874   1204       O  
ATOM    749  OD2 ASP A  98      91.296  20.720 -73.717  1.00 59.10           O  
ANISOU  749  OD2 ASP A  98     4764  12539   5152    963  -1076   1241       O  
ATOM    750  N   GLY A  99      92.185  22.401 -70.932  1.00 58.88           N  
ANISOU  750  N   GLY A  99     4761  12885   4725    673  -1299   1157       N  
ATOM    751  CA  GLY A  99      92.894  21.586 -69.969  1.00 65.02           C  
ANISOU  751  CA  GLY A  99     5493  13726   5485    769  -1470   1312       C  
ATOM    752  C   GLY A  99      93.157  20.150 -70.366  1.00 67.60           C  
ANISOU  752  C   GLY A  99     5763  13933   5988    990  -1520   1483       C  
ATOM    753  O   GLY A  99      93.747  19.412 -69.569  1.00 70.90           O  
ANISOU  753  O   GLY A  99     6151  14385   6402   1086  -1678   1624       O  
ATOM    754  N   THR A 100      92.748  19.721 -71.556  1.00 60.57           N  
ANISOU  754  N   THR A 100     4867  12893   5252   1079  -1401   1475       N  
ATOM    755  CA  THR A 100      92.980  18.355 -72.003  1.00 65.61           C  
ANISOU  755  CA  THR A 100     5467  13390   6074   1298  -1440   1622       C  
ATOM    756  C   THR A 100      94.083  18.318 -73.053  1.00 67.37           C  
ANISOU  756  C   THR A 100     5475  13624   6498   1387  -1426   1519       C  
ATOM    757  O   THR A 100      94.446  19.337 -73.648  1.00 67.83           O  
ANISOU  757  O   THR A 100     5439  13774   6560   1263  -1350   1336       O  
ATOM    758  CB  THR A 100      91.699  17.722 -72.565  1.00 61.71           C  
ANISOU  758  CB  THR A 100     5133  12695   5618   1350  -1321   1704       C  
ATOM    759  OG1 THR A 100      91.128  18.583 -73.555  1.00 60.78           O  
ANISOU  759  OG1 THR A 100     5027  12556   5509   1243  -1160   1538       O  
ATOM    760  CG2 THR A 100      90.679  17.489 -71.458  1.00 70.15           C  
ANISOU  760  CG2 THR A 100     6403  13741   6510   1286  -1341   1840       C  
ATOM    761  N   GLU A 101      94.616  17.115 -73.271  1.00 63.48           N  
ANISOU  761  N   GLU A 101     4913  13030   6178   1604  -1496   1637       N  
ATOM    762  CA  GLU A 101      95.715  16.942 -74.216  1.00 69.37           C  
ANISOU  762  CA  GLU A 101     5445  13781   7132   1716  -1478   1544       C  
ATOM    763  C   GLU A 101      95.231  17.051 -75.658  1.00 70.17           C  
ANISOU  763  C   GLU A 101     5556  13757   7349   1721  -1285   1427       C  
ATOM    764  O   GLU A 101      95.844  17.743 -76.478  1.00 61.32           O  
ANISOU  764  O   GLU A 101     4294  12708   6295   1652  -1199   1255       O  
ATOM    765  CB  GLU A 101      96.393  15.594 -73.973  1.00 78.00           C  
ANISOU  765  CB  GLU A 101     6471  14785   8381   1966  -1613   1701       C  
ATOM    766  CG  GLU A 101      97.347  15.154 -75.070  1.00 83.43           C  
ANISOU  766  CG  GLU A 101     6958  15424   9317   2131  -1563   1615       C  
ATOM    767  CD  GLU A 101      98.720  15.788 -74.956  1.00 90.52           C  
ANISOU  767  CD  GLU A 101     7608  16534  10252   2083  -1630   1502       C  
ATOM    768  OE1 GLU A 101      98.887  16.730 -74.150  1.00 90.41           O  
ANISOU  768  OE1 GLU A 101     7584  16705  10064   1895  -1700   1464       O  
ATOM    769  OE2 GLU A 101      99.637  15.335 -75.673  1.00 94.74           O  
ANISOU  769  OE2 GLU A 101     7955  17048  10993   2234  -1610   1448       O  
ATOM    770  N   ASN A 102      94.134  16.368 -75.987  1.00 60.21           N  
ANISOU  770  N   ASN A 102     4463  12305   6109   1790  -1218   1522       N  
ATOM    771  CA  ASN A 102      93.596  16.352 -77.339  1.00 58.80           C  
ANISOU  771  CA  ASN A 102     4310  11990   6040   1807  -1048   1428       C  
ATOM    772  C   ASN A 102      92.431  17.319 -77.511  1.00 58.32           C  
ANISOU  772  C   ASN A 102     4389  11940   5829   1605   -938   1351       C  
ATOM    773  O   ASN A 102      91.639  17.165 -78.448  1.00 53.01           O  
ANISOU  773  O   ASN A 102     3794  11129   5219   1617   -819   1325       O  
ATOM    774  CB  ASN A 102      93.174  14.933 -77.722  1.00 63.12           C  
ANISOU  774  CB  ASN A 102     4946  12303   6733   2025  -1047   1575       C  
ATOM    775  CG  ASN A 102      92.278  14.289 -76.681  1.00 70.30           C  
ANISOU  775  CG  ASN A 102     6053  13132   7526   2035  -1139   1789       C  
ATOM    776  OD1 ASN A 102      91.861  14.935 -75.718  1.00 73.41           O  
ANISOU  776  OD1 ASN A 102     6524  13647   7723   1875  -1180   1813       O  
ATOM    777  ND2 ASN A 102      91.975  13.010 -76.870  1.00 69.73           N  
ANISOU  777  ND2 ASN A 102     6075  12845   7574   2216  -1164   1940       N  
ATOM    778  N   LYS A 103      92.311  18.304 -76.618  1.00 62.70           N  
ANISOU  778  N   LYS A 103     4978  12653   6192   1426   -980   1311       N  
ATOM    779  CA  LYS A 103      91.263  19.324 -76.685  1.00 52.45           C  
ANISOU  779  CA  LYS A 103     3807  11373   4748   1238   -884   1221       C  
ATOM    780  C   LYS A 103      89.869  18.703 -76.639  1.00 51.07           C  
ANISOU  780  C   LYS A 103     3823  11044   4539   1271   -838   1352       C  
ATOM    781  O   LYS A 103      88.935  19.188 -77.274  1.00 49.25           O  
ANISOU  781  O   LYS A 103     3676  10752   4283   1186   -726   1281       O  
ATOM    782  CB  LYS A 103      91.423  20.196 -77.933  1.00 57.59           C  
ANISOU  782  CB  LYS A 103     4385  12031   5467   1141   -757   1021       C  
ATOM    783  CG  LYS A 103      92.775  20.873 -78.049  1.00 52.18           C  
ANISOU  783  CG  LYS A 103     3515  11498   4814   1074   -785    887       C  
ATOM    784  CD  LYS A 103      92.894  21.613 -79.368  1.00 56.19           C  
ANISOU  784  CD  LYS A 103     3972  11980   5396    974   -643    705       C  
ATOM    785  CE  LYS A 103      94.255  22.261 -79.504  1.00 58.90           C  
ANISOU  785  CE  LYS A 103     4134  12472   5772    889   -663    581       C  
ATOM    786  NZ  LYS A 103      95.351  21.274 -79.290  1.00 54.96           N  
ANISOU  786  NZ  LYS A 103     3472  12002   5407   1074   -750    664       N  
ATOM    787  N   SER A 104      89.719  17.629 -75.865  1.00 52.62           N  
ANISOU  787  N   SER A 104     4091  11171   4730   1385   -929   1549       N  
ATOM    788  CA  SER A 104      88.486  16.853 -75.901  1.00 51.71           C  
ANISOU  788  CA  SER A 104     4150  10886   4610   1422   -885   1694       C  
ATOM    789  C   SER A 104      87.346  17.456 -75.082  1.00 61.19           C  
ANISOU  789  C   SER A 104     5508  12133   5609   1256   -842   1710       C  
ATOM    790  O   SER A 104      86.206  17.001 -75.228  1.00 57.52           O  
ANISOU  790  O   SER A 104     5182  11538   5135   1246   -776   1802       O  
ATOM    791  CB  SER A 104      88.759  15.422 -75.430  1.00 53.96           C  
ANISOU  791  CB  SER A 104     4472  11052   4978   1600   -997   1906       C  
ATOM    792  OG  SER A 104      89.583  15.417 -74.278  1.00 60.82           O  
ANISOU  792  OG  SER A 104     5288  12053   5767   1606  -1138   1960       O  
ATOM    793  N   LYS A 105      87.603  18.459 -74.237  1.00 58.27           N  
ANISOU  793  N   LYS A 105     5120  11936   5084   1124   -869   1616       N  
ATOM    794  CA  LYS A 105      86.513  19.071 -73.480  1.00 50.57           C  
ANISOU  794  CA  LYS A 105     4288  10994   3932    979   -806   1603       C  
ATOM    795  C   LYS A 105      85.682  19.999 -74.360  1.00 49.65           C  
ANISOU  795  C   LYS A 105     4212  10841   3812    877   -663   1444       C  
ATOM    796  O   LYS A 105      84.481  19.783 -74.551  1.00 55.56           O  
ANISOU  796  O   LYS A 105     5079  11479   4551    853   -572   1494       O  
ATOM    797  CB  LYS A 105      87.051  19.834 -72.266  1.00 59.68           C  
ANISOU  797  CB  LYS A 105     5424  12328   4923    879   -883   1545       C  
ATOM    798  CG  LYS A 105      85.961  20.176 -71.250  1.00 61.54           C  
ANISOU  798  CG  LYS A 105     5814  12583   4985    765   -830   1564       C  
ATOM    799  CD  LYS A 105      86.172  21.537 -70.611  1.00 59.57           C  
ANISOU  799  CD  LYS A 105     5563  12481   4592    621   -828   1386       C  
ATOM    800  CE  LYS A 105      87.342  21.538 -69.651  1.00 55.19           C  
ANISOU  800  CE  LYS A 105     4937  12073   3959    620   -988   1415       C  
ATOM    801  NZ  LYS A 105      87.582  22.908 -69.126  1.00 55.53           N  
ANISOU  801  NZ  LYS A 105     4985  12244   3869    468   -988   1227       N  
ATOM    802  N   PHE A 106      86.304  21.052 -74.895  1.00 49.78           N  
ANISOU  802  N   PHE A 106     4134  10944   3837    806   -645   1255       N  
ATOM    803  CA  PHE A 106      85.591  21.951 -75.798  1.00 49.04           C  
ANISOU  803  CA  PHE A 106     4086  10801   3745    713   -525   1104       C  
ATOM    804  C   PHE A 106      85.469  21.378 -77.204  1.00 49.58           C  
ANISOU  804  C   PHE A 106     4125  10729   3986    799   -471   1114       C  
ATOM    805  O   PHE A 106      84.507  21.688 -77.913  1.00 49.66           O  
ANISOU  805  O   PHE A 106     4246  10582   4040    737   -347   1046       O  
ATOM    806  CB  PHE A 106      86.293  23.308 -75.866  1.00 44.97           C  
ANISOU  806  CB  PHE A 106     3505  10408   3175    584   -529    898       C  
ATOM    807  CG  PHE A 106      86.342  24.036 -74.557  1.00 46.27           C  
ANISOU  807  CG  PHE A 106     3719  10683   3179    481   -568    853       C  
ATOM    808  CD1 PHE A 106      87.327  24.976 -74.316  1.00 57.15           C  
ANISOU  808  CD1 PHE A 106     5017  12190   4508    381   -625    716       C  
ATOM    809  CD2 PHE A 106      85.400  23.791 -73.572  1.00 53.41           C  
ANISOU  809  CD2 PHE A 106     4750  11559   3984    473   -547    940       C  
ATOM    810  CE1 PHE A 106      87.377  25.654 -73.115  1.00 60.85           C  
ANISOU  810  CE1 PHE A 106     5542  12749   4827    283   -669    667       C  
ATOM    811  CE2 PHE A 106      85.444  24.469 -72.368  1.00 51.63           C  
ANISOU  811  CE2 PHE A 106     4574  11433   3610    382   -582    886       C  
ATOM    812  CZ  PHE A 106      86.435  25.401 -72.140  1.00 53.69           C  
ANISOU  812  CZ  PHE A 106     4767  11813   3820    290   -648    749       C  
ATOM    813  N   GLY A 107      86.425  20.552 -77.622  1.00 50.82           N  
ANISOU  813  N   GLY A 107     4162  10859   4289    929   -527   1168       N  
ATOM    814  CA  GLY A 107      86.468  20.060 -78.983  1.00 43.67           C  
ANISOU  814  CA  GLY A 107     3254   9746   3594    992   -430   1122       C  
ATOM    815  C   GLY A 107      87.460  20.847 -79.812  1.00 47.19           C  
ANISOU  815  C   GLY A 107     3563  10256   4111    940   -393    936       C  
ATOM    816  O   GLY A 107      87.505  22.078 -79.717  1.00 42.92           O  
ANISOU  816  O   GLY A 107     3018   9821   3467    787   -374    797       O  
ATOM    817  N   ALA A 108      88.274  20.150 -80.612  1.00 52.39           N  
ANISOU  817  N   ALA A 108     4076  11587   4243    692    152   1637       N  
ATOM    818  CA  ALA A 108      89.223  20.839 -81.484  1.00 42.05           C  
ANISOU  818  CA  ALA A 108     2770  10256   2953    593     79   1481       C  
ATOM    819  C   ALA A 108      88.513  21.766 -82.460  1.00 46.11           C  
ANISOU  819  C   ALA A 108     3344  10644   3533    474     46   1325       C  
ATOM    820  O   ALA A 108      89.071  22.797 -82.853  1.00 43.81           O  
ANISOU  820  O   ALA A 108     3084  10324   3236    384     -6   1142       O  
ATOM    821  CB  ALA A 108      90.077  19.825 -82.245  1.00 41.88           C  
ANISOU  821  CB  ALA A 108     2733  10159   3019    627     90   1597       C  
ATOM    822  N   ASN A 109      87.283  21.416 -82.854  1.00 44.53           N  
ANISOU  822  N   ASN A 109     3183  10282   3455    463    119   1367       N  
ATOM    823  CA  ASN A 109      86.519  22.252 -83.775  1.00 38.48           C  
ANISOU  823  CA  ASN A 109     2477   9357   2788    365    111   1209       C  
ATOM    824  C   ASN A 109      86.110  23.571 -83.125  1.00 41.97           C  
ANISOU  824  C   ASN A 109     2951   9908   3088    326     85   1068       C  
ATOM    825  O   ASN A 109      86.094  24.616 -83.785  1.00 37.78           O  
ANISOU  825  O   ASN A 109     2465   9312   2578    246     49    903       O  
ATOM    826  CB  ASN A 109      85.294  21.486 -84.276  1.00 38.05           C  
ANISOU  826  CB  ASN A 109     2441   9113   2904    367    199   1282       C  
ATOM    827  CG  ASN A 109      84.581  20.726 -83.168  1.00 47.27           C  
ANISOU  827  CG  ASN A 109     3588  10337   4036    446    291   1444       C  
ATOM    828  OD1 ASN A 109      85.015  20.732 -82.014  1.00 48.91           O  
ANISOU  828  OD1 ASN A 109     3777  10727   4082    519    284   1512       O  
ATOM    829  ND2 ASN A 109      83.473  20.074 -83.513  1.00 44.19           N  
ANISOU  829  ND2 ASN A 109     3211   9771   3808    437    370   1496       N  
ATOM    830  N   ALA A 110      85.783  23.545 -81.830  1.00 44.07           N  
ANISOU  830  N   ALA A 110     3204  10322   3219    391    110   1131       N  
ATOM    831  CA  ALA A 110      85.446  24.779 -81.126  1.00 45.14           C  
ANISOU  831  CA  ALA A 110     3375  10511   3264    360     81    980       C  
ATOM    832  C   ALA A 110      86.677  25.656 -80.920  1.00 47.35           C  
ANISOU  832  C   ALA A 110     3635  10881   3474    310      7    826       C  
ATOM    833  O   ALA A 110      86.611  26.880 -81.089  1.00 54.10           O  
ANISOU  833  O   ALA A 110     4537  11708   4312    230    -16    648       O  
ATOM    834  CB  ALA A 110      84.793  24.456 -79.783  1.00 43.24           C  
ANISOU  834  CB  ALA A 110     3129  10346   2953    454    127   1078       C  
ATOM    835  N   ILE A 111      87.807  25.048 -80.556  1.00 42.79           N  
ANISOU  835  N   ILE A 111     2993  10400   2866    356    -16    890       N  
ATOM    836  CA  ILE A 111      89.020  25.815 -80.289  1.00 46.29           C  
ANISOU  836  CA  ILE A 111     3413  10927   3248    305    -73    744       C  
ATOM    837  C   ILE A 111      89.591  26.394 -81.581  1.00 44.89           C  
ANISOU  837  C   ILE A 111     3266  10631   3158    198   -102    625       C  
ATOM    838  O   ILE A 111      89.993  27.564 -81.626  1.00 43.98           O  
ANISOU  838  O   ILE A 111     3170  10524   3017    111   -136    443       O  
ATOM    839  CB  ILE A 111      90.039  24.930 -79.543  1.00 43.67           C  
ANISOU  839  CB  ILE A 111     3005  10732   2856    399    -79    857       C  
ATOM    840  CG1 ILE A 111      89.569  24.694 -78.104  1.00 46.03           C  
ANISOU  840  CG1 ILE A 111     3279  11168   3041    508    -57    929       C  
ATOM    841  CG2 ILE A 111      91.437  25.532 -79.582  1.00 44.27           C  
ANISOU  841  CG2 ILE A 111     3050  10875   2897    336   -138    719       C  
ATOM    842  CD1 ILE A 111      90.417  23.717 -77.321  1.00 46.83           C  
ANISOU  842  CD1 ILE A 111     3306  11411   3077    633    -48   1066       C  
ATOM    843  N   LEU A 112      89.629  25.597 -82.653  1.00 42.74           N  
ANISOU  843  N   LEU A 112     3003  10238   2997    205    -89    724       N  
ATOM    844  CA  LEU A 112      90.170  26.094 -83.916  1.00 38.80           C  
ANISOU  844  CA  LEU A 112     2541   9604   2596    123   -115    621       C  
ATOM    845  C   LEU A 112      89.321  27.229 -84.478  1.00 37.85           C  
ANISOU  845  C   LEU A 112     2481   9401   2500     50   -112    478       C  
ATOM    846  O   LEU A 112      89.858  28.214 -84.998  1.00 42.22           O  
ANISOU  846  O   LEU A 112     3055   9915   3073    -29   -134    329       O  
ATOM    847  CB  LEU A 112      90.279  24.960 -84.936  1.00 37.94           C  
ANISOU  847  CB  LEU A 112     2441   9354   2620    160   -100    755       C  
ATOM    848  CG  LEU A 112      90.783  25.415 -86.309  1.00 43.81           C  
ANISOU  848  CG  LEU A 112     3229   9931   3485     95   -118    659       C  
ATOM    849  CD1 LEU A 112      92.195  25.965 -86.213  1.00 43.68           C  
ANISOU  849  CD1 LEU A 112     3186   9980   3433     49   -156    569       C  
ATOM    850  CD2 LEU A 112      90.717  24.294 -87.323  1.00 42.23           C  
ANISOU  850  CD2 LEU A 112     3049   9567   3430    138    -97    777       C  
ATOM    851  N   GLY A 113      87.994  27.112 -84.378  1.00 39.89           N  
ANISOU  851  N   GLY A 113     2765   9639   2753     80    -78    525       N  
ATOM    852  CA  GLY A 113      87.125  28.149 -84.915  1.00 38.26           C  
ANISOU  852  CA  GLY A 113     2638   9326   2574     28    -51    398       C  
ATOM    853  C   GLY A 113      87.398  29.515 -84.317  1.00 40.66           C  
ANISOU  853  C   GLY A 113     2970   9709   2770    -35    -64    223       C  
ATOM    854  O   GLY A 113      87.423  30.522 -85.030  1.00 38.01           O  
ANISOU  854  O   GLY A 113     2693   9280   2471   -100    -50     86       O  
ATOM    855  N   VAL A 114      87.610  29.568 -83.003  1.00 42.35           N  
ANISOU  855  N   VAL A 114     3148  10054   2890    -12    -75    221       N  
ATOM    856  CA  VAL A 114      87.959  30.829 -82.358  1.00 43.80           C  
ANISOU  856  CA  VAL A 114     3352  10296   2994    -76    -91     42       C  
ATOM    857  C   VAL A 114      89.371  31.250 -82.744  1.00 39.92           C  
ANISOU  857  C   VAL A 114     2817   9837   2515   -153   -137    -65       C  
ATOM    858  O   VAL A 114      89.632  32.430 -83.003  1.00 46.35           O  
ANISOU  858  O   VAL A 114     3666  10624   3321   -245   -136   -240       O  
ATOM    859  CB  VAL A 114      87.800  30.702 -80.832  1.00 43.05           C  
ANISOU  859  CB  VAL A 114     3227  10342   2788    -15    -98     71       C  
ATOM    860  CG1 VAL A 114      88.181  32.007 -80.149  1.00 42.30           C  
ANISOU  860  CG1 VAL A 114     3153  10312   2606    -85   -119   -129       C  
ATOM    861  CG2 VAL A 114      86.372  30.284 -80.481  1.00 40.90           C  
ANISOU  861  CG2 VAL A 114     2998  10026   2517     62    -44    184       C  
ATOM    862  N   SER A 115      90.299  30.290 -82.800  1.00 48.89           N  
ANISOU  862  N   SER A 115     3880  11019   3676   -118   -167     40       N  
ATOM    863  CA  SER A 115      91.686  30.605 -83.133  1.00 46.98           C  
ANISOU  863  CA  SER A 115     3592  10800   3458   -184   -206    -48       C  
ATOM    864  C   SER A 115      91.808  31.210 -84.527  1.00 45.32           C  
ANISOU  864  C   SER A 115     3420  10443   3357   -261   -197   -131       C  
ATOM    865  O   SER A 115      92.614  32.123 -84.746  1.00 39.85           O  
ANISOU  865  O   SER A 115     2705   9759   2675   -355   -215   -285       O  
ATOM    866  CB  SER A 115      92.545  29.348 -83.018  1.00 41.05           C  
ANISOU  866  CB  SER A 115     2779  10096   2721   -110   -223    107       C  
ATOM    867  OG  SER A 115      93.867  29.598 -83.452  1.00 41.66           O  
ANISOU  867  OG  SER A 115     2816  10175   2838   -168   -258     34       O  
ATOM    868  N   LEU A 116      91.020  30.712 -85.487  1.00 44.92           N  
ANISOU  868  N   LEU A 116     3414  10259   3395   -219   -169    -35       N  
ATOM    869  CA  LEU A 116      91.066  31.253 -86.845  1.00 40.25           C  
ANISOU  869  CA  LEU A 116     2869   9493   2931   -265   -138   -102       C  
ATOM    870  C   LEU A 116      90.470  32.655 -86.903  1.00 41.20           C  
ANISOU  870  C   LEU A 116     3085   9529   3039   -327    -75   -267       C  
ATOM    871  O   LEU A 116      91.011  33.537 -87.579  1.00 43.38           O  
ANISOU  871  O   LEU A 116     3392   9702   3388   -395    -37   -385       O  
ATOM    872  CB  LEU A 116      90.326  30.326 -87.811  1.00 35.48           C  
ANISOU  872  CB  LEU A 116     2308   8727   2445   -189   -103     35       C  
ATOM    873  CG  LEU A 116      90.829  28.890 -87.952  1.00 35.71           C  
ANISOU  873  CG  LEU A 116     2282   8766   2521   -122   -132    203       C  
ATOM    874  CD1 LEU A 116      89.857  28.067 -88.779  1.00 34.71           C  
ANISOU  874  CD1 LEU A 116     2194   8492   2503    -60    -98    307       C  
ATOM    875  CD2 LEU A 116      92.208  28.857 -88.575  1.00 35.51           C  
ANISOU  875  CD2 LEU A 116     2234   8695   2562   -150   -149    186       C  
ATOM    876  N   ALA A 117      89.348  32.874 -86.211  1.00 37.64           N  
ANISOU  876  N   ALA A 117     2688   9112   2503   -297    -48   -269       N  
ATOM    877  CA  ALA A 117      88.748  34.205 -86.173  1.00 40.07           C  
ANISOU  877  CA  ALA A 117     3091   9346   2786   -343     22   -419       C  
ATOM    878  C   ALA A 117      89.670  35.209 -85.493  1.00 44.93           C  
ANISOU  878  C   ALA A 117     3679  10063   3328   -446      2   -597       C  
ATOM    879  O   ALA A 117      89.726  36.379 -85.890  1.00 43.03           O  
ANISOU  879  O   ALA A 117     3510   9707   3134   -514     73   -744       O  
ATOM    880  CB  ALA A 117      87.396  34.151 -85.461  1.00 37.11           C  
ANISOU  880  CB  ALA A 117     2766   9010   2324   -282     52   -373       C  
ATOM    881  N   VAL A 118      90.398  34.773 -84.463  1.00 49.77           N  
ANISOU  881  N   VAL A 118     4186  10896   3827   -454    -88   -591       N  
ATOM    882  CA  VAL A 118      91.347  35.658 -83.791  1.00 45.48           C  
ANISOU  882  CA  VAL A 118     3593  10475   3213   -558   -125   -778       C  
ATOM    883  C   VAL A 118      92.425  36.115 -84.761  1.00 47.60           C  
ANISOU  883  C   VAL A 118     3832  10628   3628   -648   -106   -865       C  
ATOM    884  O   VAL A 118      92.789  37.296 -84.803  1.00 53.11           O  
ANISOU  884  O   VAL A 118     4558  11267   4355   -756    -57  -1053       O  
ATOM    885  CB  VAL A 118      91.953  34.954 -82.565  1.00 43.36           C  
ANISOU  885  CB  VAL A 118     3221  10381   2873   -510   -196   -715       C  
ATOM    886  CG1 VAL A 118      93.196  35.690 -82.083  1.00 46.50           C  
ANISOU  886  CG1 VAL A 118     3541  10883   3244   -615   -239   -898       C  
ATOM    887  CG2 VAL A 118      90.921  34.855 -81.463  1.00 43.16           C  
ANISOU  887  CG2 VAL A 118     3239  10404   2756   -430   -179   -666       C  
ATOM    888  N   CYS A 119      92.944  35.188 -85.563  1.00 45.17           N  
ANISOU  888  N   CYS A 119     3469  10273   3419   -605   -130   -727       N  
ATOM    889  CA  CYS A 119      94.008  35.531 -86.495  1.00 43.11           C  
ANISOU  889  CA  CYS A 119     3173   9907   3298   -678   -106   -788       C  
ATOM    890  C   CYS A 119      93.527  36.546 -87.527  1.00 48.73           C  
ANISOU  890  C   CYS A 119     4018  10363   4133   -711     25   -869       C  
ATOM    891  O   CYS A 119      94.210  37.540 -87.800  1.00 48.61           O  
ANISOU  891  O   CYS A 119     4004  10275   4190   -814     81  -1020       O  
ATOM    892  CB  CYS A 119      94.528  34.260 -87.162  1.00 43.99           C  
ANISOU  892  CB  CYS A 119     3218  10013   3484   -602   -148   -606       C  
ATOM    893  SG  CYS A 119      96.120  34.458 -87.970  1.00 48.92           S  
ANISOU  893  SG  CYS A 119     3746  10596   4244   -681   -147   -661       S  
ATOM    894  N   LYS A 120      92.338  36.324 -88.098  1.00 52.61           N  
ANISOU  894  N   LYS A 120     4619  10720   4649   -619     82   -772       N  
ATOM    895  CA  LYS A 120      91.778  37.287 -89.045  1.00 49.07           C  
ANISOU  895  CA  LYS A 120     4304  10048   4294   -620    209   -836       C  
ATOM    896  C   LYS A 120      91.564  38.646 -88.390  1.00 52.95           C  
ANISOU  896  C   LYS A 120     4857  10531   4731   -705    277  -1022       C  
ATOM    897  O   LYS A 120      91.790  39.689 -89.015  1.00 54.01           O  
ANISOU  897  O   LYS A 120     5062  10503   4958   -758    389  -1130       O  
ATOM    898  CB  LYS A 120      90.461  36.767 -89.619  1.00 38.60           C  
ANISOU  898  CB  LYS A 120     3065   8624   2978   -498    239   -706       C  
ATOM    899  CG  LYS A 120      90.568  35.452 -90.374  1.00 44.38           C  
ANISOU  899  CG  LYS A 120     3752   9331   3778   -416    187   -539       C  
ATOM    900  CD  LYS A 120      89.258  35.118 -91.081  1.00 47.06           C  
ANISOU  900  CD  LYS A 120     4177   9556   4148   -311    224   -452       C  
ATOM    901  CE  LYS A 120      89.318  33.761 -91.769  1.00 49.50           C  
ANISOU  901  CE  LYS A 120     4441   9840   4525   -237    171   -303       C  
ATOM    902  NZ  LYS A 120      88.033  33.420 -92.445  1.00 45.23           N  
ANISOU  902  NZ  LYS A 120     3966   9202   4016   -144    196   -242       N  
ATOM    903  N   ALA A 121      91.117  38.653 -87.131  1.00 45.47           N  
ANISOU  903  N   ALA A 121     3891   9750   3634   -710    223  -1058       N  
ATOM    904  CA  ALA A 121      90.939  39.914 -86.419  1.00 48.83           C  
ANISOU  904  CA  ALA A 121     4377  10179   3997   -792    282  -1247       C  
ATOM    905  C   ALA A 121      92.277  40.583 -86.145  1.00 51.49           C  
ANISOU  905  C   ALA A 121     4631  10565   4369   -937    269  -1426       C  
ATOM    906  O   ALA A 121      92.390  41.813 -86.217  1.00 54.81           O  
ANISOU  906  O   ALA A 121     5120  10868   4839  -1028    373  -1597       O  
ATOM    907  CB  ALA A 121      90.183  39.678 -85.113  1.00 41.32           C  
ANISOU  907  CB  ALA A 121     3422   9412   2865   -750    222  -1236       C  
ATOM    908  N   GLY A 122      93.302  39.790 -85.825  1.00 51.11           N  
ANISOU  908  N   GLY A 122     4431  10687   4300   -961    147  -1390       N  
ATOM    909  CA  GLY A 122      94.612  40.357 -85.568  1.00 53.80           C  
ANISOU  909  CA  GLY A 122     4664  11096   4680  -1101    121  -1563       C  
ATOM    910  C   GLY A 122      95.296  40.854 -86.822  1.00 52.33           C  
ANISOU  910  C   GLY A 122     4494  10691   4697  -1161    228  -1594       C  
ATOM    911  O   GLY A 122      96.157  41.737 -86.755  1.00 52.63           O  
ANISOU  911  O   GLY A 122     4487  10703   4809  -1301    270  -1777       O  
ATOM    912  N   ALA A 123      94.932  40.299 -87.980  1.00 47.51           N  
ANISOU  912  N   ALA A 123     3948   9921   4182  -1057    279  -1421       N  
ATOM    913  CA  ALA A 123      95.503  40.783 -89.232  1.00 51.91           C  
ANISOU  913  CA  ALA A 123     4540  10261   4923  -1088    399  -1434       C  
ATOM    914  C   ALA A 123      94.986  42.175 -89.567  1.00 55.92           C  
ANISOU  914  C   ALA A 123     5195  10557   5495  -1131    572  -1566       C  
ATOM    915  O   ALA A 123      95.752  43.036 -90.018  1.00 56.56           O  
ANISOU  915  O   ALA A 123     5275  10507   5709  -1232    680  -1685       O  
ATOM    916  CB  ALA A 123      95.200  39.801 -90.365  1.00 44.14           C  
ANISOU  916  CB  ALA A 123     3593   9176   4003   -948    402  -1220       C  
ATOM    917  N   ALA A 124      93.691  42.418 -89.343  1.00 48.57           N  
ANISOU  917  N   ALA A 124     4391   9586   4476  -1053    612  -1544       N  
ATOM    918  CA  ALA A 124      93.134  43.744 -89.591  1.00 49.51           C  
ANISOU  918  CA  ALA A 124     4659   9511   4640  -1077    786  -1661       C  
ATOM    919  C   ALA A 124      93.550  44.740 -88.517  1.00 54.12           C  
ANISOU  919  C   ALA A 124     5219  10161   5185  -1233    802  -1896       C  
ATOM    920  O   ALA A 124      93.691  45.934 -88.802  1.00 59.33           O  
ANISOU  920  O   ALA A 124     5961  10639   5943  -1310    963  -2035       O  
ATOM    921  CB  ALA A 124      91.613  43.672 -89.680  1.00 51.74           C  
ANISOU  921  CB  ALA A 124     5074   9747   4838   -935    822  -1560       C  
ATOM    922  N   GLU A 125      93.736  44.277 -87.280  1.00 55.21           N  
ANISOU  922  N   GLU A 125     5246  10552   5177  -1275    646  -1945       N  
ATOM    923  CA  GLU A 125      94.295  45.153 -86.257  1.00 67.11           C  
ANISOU  923  CA  GLU A 125     6706  12151   6643  -1431    637  -2190       C  
ATOM    924  C   GLU A 125      95.710  45.573 -86.623  1.00 73.56           C  
ANISOU  924  C   GLU A 125     7411  12920   7617  -1582    666  -2321       C  
ATOM    925  O   GLU A 125      96.140  46.683 -86.288  1.00 76.09           O  
ANISOU  925  O   GLU A 125     7738  13178   7995  -1730    750  -2549       O  
ATOM    926  CB  GLU A 125      94.279  44.453 -84.899  1.00 69.79           C  
ANISOU  926  CB  GLU A 125     6938  12802   6778  -1420    451  -2199       C  
ATOM    927  CG  GLU A 125      94.574  45.373 -83.736  1.00 79.62           C  
ANISOU  927  CG  GLU A 125     8159  14160   7935  -1554    434  -2461       C  
ATOM    928  CD  GLU A 125      93.405  46.279 -83.404  1.00 87.81           C  
ANISOU  928  CD  GLU A 125     9375  15082   8907  -1526    556  -2536       C  
ATOM    929  OE1 GLU A 125      92.247  45.832 -83.541  1.00 87.91           O  
ANISOU  929  OE1 GLU A 125     9486  15067   8850  -1376    572  -2362       O  
ATOM    930  OE2 GLU A 125      93.644  47.437 -83.001  1.00 90.58           O  
ANISOU  930  OE2 GLU A 125     9766  15369   9282  -1656    639  -2775       O  
ATOM    931  N   ARG A 126      96.436  44.704 -87.323  1.00 69.97           N  
ANISOU  931  N   ARG A 126     6854  12488   7244  -1549    608  -2182       N  
ATOM    932  CA  ARG A 126      97.768  44.996 -87.830  1.00 70.13           C  
ANISOU  932  CA  ARG A 126     6761  12451   7433  -1674    646  -2269       C  
ATOM    933  C   ARG A 126      97.762  45.816 -89.114  1.00 66.80           C  
ANISOU  933  C   ARG A 126     6465  11703   7212  -1677    869  -2262       C  
ATOM    934  O   ARG A 126      98.836  46.246 -89.550  1.00 64.58           O  
ANISOU  934  O   ARG A 126     6105  11339   7094  -1792    940  -2351       O  
ATOM    935  CB  ARG A 126      98.521  43.688 -88.082  1.00 70.59           C  
ANISOU  935  CB  ARG A 126     6666  12663   7491  -1615    503  -2103       C  
ATOM    936  CG  ARG A 126      99.258  43.141 -86.885  1.00 72.06           C  
ANISOU  936  CG  ARG A 126     6660  13174   7544  -1674    307  -2175       C  
ATOM    937  CD  ARG A 126     100.574  43.854 -86.705  1.00 76.38           C  
ANISOU  937  CD  ARG A 126     7059  13757   8204  -1864    317  -2393       C  
ATOM    938  NE  ARG A 126     101.561  42.975 -86.095  1.00 84.56           N  
ANISOU  938  NE  ARG A 126     7876  15088   9163  -1875    129  -2376       N  
ATOM    939  CZ  ARG A 126     102.828  43.309 -85.887  1.00 93.27           C  
ANISOU  939  CZ  ARG A 126     8798  16292  10349  -2024     92  -2541       C  
ATOM    940  NH1 ARG A 126     103.262  44.510 -86.242  1.00 94.45           N  
ANISOU  940  NH1 ARG A 126     8961  16249  10677  -2189    240  -2742       N  
ATOM    941  NH2 ARG A 126     103.657  42.442 -85.325  1.00 95.11           N  
ANISOU  941  NH2 ARG A 126     8933  16711  10495  -1943    -51  -2450       N  
ATOM    942  N   GLU A 127      96.594  46.036 -89.728  1.00 60.28           N  
ANISOU  942  N   GLU A 127     5826  10699   6377  -1545    985  -2155       N  
ATOM    943  CA  GLU A 127      96.501  46.668 -91.048  1.00 61.05           C  
ANISOU  943  CA  GLU A 127     6054  10500   6641  -1496   1196  -2103       C  
ATOM    944  C   GLU A 127      97.305  45.884 -92.085  1.00 60.74           C  
ANISOU  944  C   GLU A 127     5936  10427   6715  -1445   1179  -1951       C  
ATOM    945  O   GLU A 127      97.954  46.455 -92.964  1.00 63.27           O  
ANISOU  945  O   GLU A 127     6275  10554   7209  -1482   1335  -1972       O  
ATOM    946  CB  GLU A 127      96.948  48.131 -91.004  1.00 64.14           C  
ANISOU  946  CB  GLU A 127     6493  10710   7166  -1651   1386  -2323       C  
ATOM    947  CG  GLU A 127      96.161  48.992 -90.031  1.00 68.29           C  
ANISOU  947  CG  GLU A 127     7116  11244   7589  -1699   1426  -2485       C  
ATOM    948  CD  GLU A 127      96.983  50.139 -89.476  1.00 76.57           C  
ANISOU  948  CD  GLU A 127     8118  12234   8741  -1919   1519  -2764       C  
ATOM    949  OE1 GLU A 127      96.461  50.890 -88.623  1.00 77.74           O  
ANISOU  949  OE1 GLU A 127     8339  12390   8809  -1977   1554  -2925       O  
ATOM    950  OE2 GLU A 127      98.156  50.285 -89.886  1.00 73.98           O  
ANISOU  950  OE2 GLU A 127     7676  11852   8579  -2036   1560  -2827       O  
ATOM    951  N   LEU A 128      97.264  44.559 -91.974  1.00 59.11           N  
ANISOU  951  N   LEU A 128     5644  10403   6412  -1354    999  -1795       N  
ATOM    952  CA  LEU A 128      97.979  43.670 -92.870  1.00 55.99           C  
ANISOU  952  CA  LEU A 128     5174  10000   6102  -1292    964  -1642       C  
ATOM    953  C   LEU A 128      97.018  42.685 -93.518  1.00 50.30           C  
ANISOU  953  C   LEU A 128     4539   9262   5311  -1095    918  -1425       C  
ATOM    954  O   LEU A 128      96.032  42.276 -92.898  1.00 54.61           O  
ANISOU  954  O   LEU A 128     5120   9914   5714  -1031    830  -1382       O  
ATOM    955  CB  LEU A 128      99.060  42.878 -92.127  1.00 52.59           C  
ANISOU  955  CB  LEU A 128     4528   9819   5635  -1375    786  -1661       C  
ATOM    956  CG  LEU A 128     100.184  43.628 -91.422  1.00 57.80           C  
ANISOU  956  CG  LEU A 128     5047  10558   6359  -1578    784  -1884       C  
ATOM    957  CD1 LEU A 128     101.066  42.628 -90.701  1.00 60.86           C  
ANISOU  957  CD1 LEU A 128     5222  11233   6667  -1606    581  -1859       C  
ATOM    958  CD2 LEU A 128     100.994  44.447 -92.411  1.00 59.92           C  
ANISOU  958  CD2 LEU A 128     5324  10593   6851  -1655    973  -1942       C  
ATOM    959  N   PRO A 129      97.277  42.287 -94.761  1.00 49.48           N  
ANISOU  959  N   PRO A 129     4466   9028   5307   -998    977  -1291       N  
ATOM    960  CA  PRO A 129      96.576  41.124 -95.312  1.00 49.52           C  
ANISOU  960  CA  PRO A 129     4508   9058   5247   -829    894  -1097       C  
ATOM    961  C   PRO A 129      96.871  39.888 -94.478  1.00 49.43           C  
ANISOU  961  C   PRO A 129     4351   9291   5139   -838    694  -1031       C  
ATOM    962  O   PRO A 129      97.933  39.767 -93.864  1.00 51.98           O  
ANISOU  962  O   PRO A 129     4526   9750   5474   -947    623  -1094       O  
ATOM    963  CB  PRO A 129      97.141  41.002 -96.732  1.00 45.41           C  
ANISOU  963  CB  PRO A 129     4023   8370   4862   -749    995  -1000       C  
ATOM    964  CG  PRO A 129      98.399  41.810 -96.728  1.00 48.50           C  
ANISOU  964  CG  PRO A 129     4336   8704   5388   -896   1091  -1122       C  
ATOM    965  CD  PRO A 129      98.175  42.911 -95.744  1.00 47.38           C  
ANISOU  965  CD  PRO A 129     4210   8575   5219  -1032   1136  -1313       C  
ATOM    966  N   LEU A 130      95.906  38.966 -94.459  1.00 44.90           N  
ANISOU  966  N   LEU A 130     3817   8773   4471   -717    610   -901       N  
ATOM    967  CA  LEU A 130      95.979  37.823 -93.553  1.00 41.24           C  
ANISOU  967  CA  LEU A 130     3235   8531   3902   -710    442   -829       C  
ATOM    968  C   LEU A 130      97.262  37.021 -93.748  1.00 42.03           C  
ANISOU  968  C   LEU A 130     3197   8713   4060   -726    374   -761       C  
ATOM    969  O   LEU A 130      97.901  36.615 -92.769  1.00 39.61           O  
ANISOU  969  O   LEU A 130     2753   8611   3687   -786    263   -782       O  
ATOM    970  CB  LEU A 130      94.753  36.934 -93.743  1.00 35.80           C  
ANISOU  970  CB  LEU A 130     2616   7839   3145   -573    395   -689       C  
ATOM    971  CG  LEU A 130      94.727  35.628 -92.954  1.00 36.33           C  
ANISOU  971  CG  LEU A 130     2582   8101   3122   -539    250   -578       C  
ATOM    972  CD1 LEU A 130      94.782  35.904 -91.456  1.00 36.83           C  
ANISOU  972  CD1 LEU A 130     2572   8363   3059   -623    179   -672       C  
ATOM    973  CD2 LEU A 130      93.488  34.825 -93.332  1.00 34.29           C  
ANISOU  973  CD2 LEU A 130     2399   7794   2838   -414    233   -452       C  
ATOM    974  N   TYR A 131      97.661  36.785 -95.002  1.00 39.61           N  
ANISOU  974  N   TYR A 131     2924   8257   3870   -660    441   -677       N  
ATOM    975  CA  TYR A 131      98.878  36.019 -95.254  1.00 40.38           C  
ANISOU  975  CA  TYR A 131     2894   8421   4026   -663    389   -602       C  
ATOM    976  C   TYR A 131     100.120  36.736 -94.734  1.00 46.71           C  
ANISOU  976  C   TYR A 131     3564   9303   4882   -816    399   -741       C  
ATOM    977  O   TYR A 131     101.065  36.084 -94.274  1.00 46.50           O  
ANISOU  977  O   TYR A 131     3381   9445   4841   -845    300   -711       O  
ATOM    978  CB  TYR A 131      99.014  35.721 -96.753  1.00 36.20           C  
ANISOU  978  CB  TYR A 131     2443   7702   3607   -553    476   -492       C  
ATOM    979  CG  TYR A 131      98.993  36.942 -97.650  1.00 40.65           C  
ANISOU  979  CG  TYR A 131     3121   8050   4276   -563    650   -570       C  
ATOM    980  CD1 TYR A 131     100.155  37.656 -97.920  1.00 48.58           C  
ANISOU  980  CD1 TYR A 131     4062   8994   5404   -658    744   -645       C  
ATOM    981  CD2 TYR A 131      97.812  37.372 -98.240  1.00 40.74           C  
ANISOU  981  CD2 TYR A 131     3297   7917   4265   -469    732   -561       C  
ATOM    982  CE1 TYR A 131     100.138  38.772 -98.742  1.00 48.97           C  
ANISOU  982  CE1 TYR A 131     4221   8828   5556   -658    929   -703       C  
ATOM    983  CE2 TYR A 131      97.784  38.482 -99.064  1.00 38.84           C  
ANISOU  983  CE2 TYR A 131     3167   7478   4111   -454    907   -615       C  
ATOM    984  CZ  TYR A 131      98.948  39.180 -99.310  1.00 49.85           C  
ANISOU  984  CZ  TYR A 131     4509   8800   5633   -548   1012   -682       C  
ATOM    985  OH  TYR A 131      98.927  40.287-100.129  1.00 57.82           O  
ANISOU  985  OH  TYR A 131     5635   9596   6737   -526   1211   -724       O  
ATOM    986  N   ARG A 132     100.138  38.070 -94.801  1.00 48.09           N  
ANISOU  986  N   ARG A 132     3792   9356   5122   -913    520   -897       N  
ATOM    987  CA  ARG A 132     101.266  38.829 -94.274  1.00 43.43           C  
ANISOU  987  CA  ARG A 132     3071   8833   4598  -1080    536  -1060       C  
ATOM    988  C   ARG A 132     101.341  38.705 -92.759  1.00 47.63           C  
ANISOU  988  C   ARG A 132     3481   9630   4985  -1164    385  -1159       C  
ATOM    989  O   ARG A 132     102.420  38.489 -92.195  1.00 52.73           O  
ANISOU  989  O   ARG A 132     3949  10456   5631  -1245    297  -1211       O  
ATOM    990  CB  ARG A 132     101.146  40.296 -94.691  1.00 45.39           C  
ANISOU  990  CB  ARG A 132     3424   8864   4958  -1162    722  -1207       C  
ATOM    991  CG  ARG A 132     102.341  41.148 -94.319  1.00 56.04           C  
ANISOU  991  CG  ARG A 132     4639  10237   6418  -1349    768  -1390       C  
ATOM    992  CD  ARG A 132     103.568  40.726 -95.102  1.00 66.25           C  
ANISOU  992  CD  ARG A 132     5818  11505   7850  -1349    794  -1312       C  
ATOM    993  NE  ARG A 132     103.600  41.335 -96.427  1.00 70.49           N  
ANISOU  993  NE  ARG A 132     6481  11755   8547  -1301   1004  -1268       N  
ATOM    994  CZ  ARG A 132     104.539  41.094 -97.335  1.00 69.22           C  
ANISOU  994  CZ  ARG A 132     6264  11514   8523  -1275   1074  -1184       C  
ATOM    995  NH1 ARG A 132     104.494  41.701 -98.511  1.00 70.56           N  
ANISOU  995  NH1 ARG A 132     6564  11423   8824  -1215   1278  -1141       N  
ATOM    996  NH2 ARG A 132     105.521  40.243 -97.069  1.00 65.48           N  
ANISOU  996  NH2 ARG A 132     5605  11225   8050  -1297    948  -1134       N  
ATOM    997  N   HIS A 133     100.195  38.843 -92.086  1.00 54.00           N  
ANISOU  997  N   HIS A 133     4381  10474   5662  -1135    356  -1184       N  
ATOM    998  CA  HIS A 133     100.140  38.724 -90.632  1.00 52.53           C  
ANISOU  998  CA  HIS A 133     4102  10542   5315  -1189    220  -1268       C  
ATOM    999  C   HIS A 133     100.590  37.342 -90.169  1.00 43.25           C  
ANISOU  999  C   HIS A 133     2791   9596   4046  -1111     61  -1121       C  
ATOM   1000  O   HIS A 133     101.277  37.214 -89.150  1.00 49.65           O  
ANISOU 1000  O   HIS A 133     3455  10642   4768  -1170    -52  -1195       O  
ATOM   1001  CB  HIS A 133      98.717  39.024 -90.153  1.00 49.49           C  
ANISOU 1001  CB  HIS A 133     3861  10129   4813  -1140    237  -1283       C  
ATOM   1002  CG  HIS A 133      98.514  38.838 -88.681  1.00 52.61           C  
ANISOU 1002  CG  HIS A 133     4185  10781   5026  -1164    107  -1346       C  
ATOM   1003  ND1 HIS A 133      99.069  39.678 -87.740  1.00 56.15           N  
ANISOU 1003  ND1 HIS A 133     4551  11355   5429  -1305     78  -1563       N  
ATOM   1004  CD2 HIS A 133      97.809  37.912 -87.989  1.00 53.48           C  
ANISOU 1004  CD2 HIS A 133     4293  11045   4983  -1058      5  -1222       C  
ATOM   1005  CE1 HIS A 133      98.722  39.273 -86.532  1.00 57.23           C  
ANISOU 1005  CE1 HIS A 133     4643  11725   5378  -1273    -44  -1567       C  
ATOM   1006  NE2 HIS A 133      97.957  38.203 -86.655  1.00 56.60           N  
ANISOU 1006  NE2 HIS A 133     4612  11662   5233  -1122    -83  -1354       N  
ATOM   1007  N   ILE A 134     100.216  36.297 -90.906  1.00 41.62           N  
ANISOU 1007  N   ILE A 134     2637   9320   3856   -969     56   -914       N  
ATOM   1008  CA  ILE A 134     100.645  34.945 -90.562  1.00 41.52           C  
ANISOU 1008  CA  ILE A 134     2544   9461   3773   -874    -65   -752       C  
ATOM   1009  C   ILE A 134     102.149  34.792 -90.755  1.00 54.28           C  
ANISOU 1009  C   ILE A 134     4067  11088   5471   -908    -85   -754       C  
ATOM   1010  O   ILE A 134     102.823  34.121 -89.963  1.00 54.90           O  
ANISOU 1010  O   ILE A 134     4091  11306   5463   -870   -181   -704       O  
ATOM   1011  CB  ILE A 134      99.858  33.915 -91.390  1.00 40.64           C  
ANISOU 1011  CB  ILE A 134     2524   9236   3682   -726    -47   -550       C  
ATOM   1012  CG1 ILE A 134      98.400  33.854 -90.918  1.00 38.83           C  
ANISOU 1012  CG1 ILE A 134     2393   9013   3347   -674    -54   -529       C  
ATOM   1013  CG2 ILE A 134     100.532  32.547 -91.341  1.00 39.61           C  
ANISOU 1013  CG2 ILE A 134     2380   9138   3533   -620   -122   -373       C  
ATOM   1014  CD1 ILE A 134      97.558  32.857 -91.672  1.00 42.86           C  
ANISOU 1014  CD1 ILE A 134     2995   9405   3884   -539    -39   -353       C  
ATOM   1015  N   ALA A 135     102.700  35.405 -91.807  1.00 48.49           N  
ANISOU 1015  N   ALA A 135     3311  10207   4906   -970     22   -802       N  
ATOM   1016  CA  ALA A 135     104.139  35.333 -92.033  1.00 51.20           C  
ANISOU 1016  CA  ALA A 135     3555  10554   5344  -1008     14   -808       C  
ATOM   1017  C   ALA A 135     104.911  35.930 -90.861  1.00 53.63           C  
ANISOU 1017  C   ALA A 135     3756  11026   5594  -1129    -59   -984       C  
ATOM   1018  O   ALA A 135     105.893  35.343 -90.392  1.00 54.80           O  
ANISOU 1018  O   ALA A 135     3822  11292   5707  -1101   -145   -941       O  
ATOM   1019  CB  ALA A 135     104.504  36.037 -93.340  1.00 43.52           C  
ANISOU 1019  CB  ALA A 135     2584   9381   4570  -1059    173   -841       C  
ATOM   1020  N   GLN A 136     104.473  37.088 -90.361  1.00 51.73           N  
ANISOU 1020  N   GLN A 136     3515  10801   5337  -1259    -20  -1189       N  
ATOM   1021  CA  GLN A 136     105.117  37.679 -89.191  1.00 54.89           C  
ANISOU 1021  CA  GLN A 136     3824  11363   5670  -1371    -92  -1377       C  
ATOM   1022  C   GLN A 136     104.905  36.833 -87.940  1.00 52.20           C  
ANISOU 1022  C   GLN A 136     3484  11238   5111  -1266   -233  -1304       C  
ATOM   1023  O   GLN A 136     105.771  36.810 -87.059  1.00 55.18           O  
ANISOU 1023  O   GLN A 136     3766  11777   5422  -1291   -314  -1377       O  
ATOM   1024  CB  GLN A 136     104.601  39.103 -88.973  1.00 60.35           C  
ANISOU 1024  CB  GLN A 136     4532  12001   6396  -1533     -3  -1620       C  
ATOM   1025  CG  GLN A 136     104.795  40.008 -90.182  1.00 65.13           C  
ANISOU 1025  CG  GLN A 136     5145  12371   7229  -1636    184  -1693       C  
ATOM   1026  CD  GLN A 136     104.314  41.425 -89.942  1.00 67.65           C  
ANISOU 1026  CD  GLN A 136     5531  12579   7594  -1784    303  -1925       C  
ATOM   1027  OE1 GLN A 136     103.800  41.747 -88.870  1.00 61.00           O  
ANISOU 1027  OE1 GLN A 136     4700  11871   6607  -1825    231  -2050       O  
ATOM   1028  NE2 GLN A 136     104.481  42.283 -90.943  1.00 70.03           N  
ANISOU 1028  NE2 GLN A 136     5916  12599   8092  -1839    500  -1968       N  
ATOM   1029  N   LEU A 137     103.771  36.132 -87.842  1.00 48.35           N  
ANISOU 1029  N   LEU A 137     3099  10755   4516  -1142   -250  -1158       N  
ATOM   1030  CA  LEU A 137     103.571  35.189 -86.746  1.00 48.64           C  
ANISOU 1030  CA  LEU A 137     3142  10971   4368  -1022   -349  -1048       C  
ATOM   1031  C   LEU A 137     104.556  34.029 -86.811  1.00 48.65           C  
ANISOU 1031  C   LEU A 137     3086  11028   4370   -917   -402   -879       C  
ATOM   1032  O   LEU A 137     104.846  33.405 -85.783  1.00 50.28           O  
ANISOU 1032  O   LEU A 137     3251  11414   4439   -843   -475   -829       O  
ATOM   1033  CB  LEU A 137     102.139  34.651 -86.764  1.00 46.45           C  
ANISOU 1033  CB  LEU A 137     2985  10653   4012   -915   -333   -915       C  
ATOM   1034  CG  LEU A 137     101.154  35.208 -85.737  1.00 50.02           C  
ANISOU 1034  CG  LEU A 137     3479  11204   4323   -937   -346  -1021       C  
ATOM   1035  CD1 LEU A 137     101.227  36.729 -85.681  1.00 52.31           C  
ANISOU 1035  CD1 LEU A 137     3743  11470   4661  -1114   -302  -1287       C  
ATOM   1036  CD2 LEU A 137      99.733  34.736 -86.046  1.00 44.94           C  
ANISOU 1036  CD2 LEU A 137     2948  10480   3649   -842   -313   -884       C  
ATOM   1037  N   ALA A 138     105.067  33.716 -88.001  1.00 47.71           N  
ANISOU 1037  N   ALA A 138     2962  10761   4402   -901   -356   -786       N  
ATOM   1038  CA  ALA A 138     105.973  32.594 -88.193  1.00 52.94           C  
ANISOU 1038  CA  ALA A 138     3579  11459   5078   -798   -394   -618       C  
ATOM   1039  C   ALA A 138     107.416  33.031 -88.397  1.00 56.73           C  
ANISOU 1039  C   ALA A 138     3928  11964   5664   -885   -401   -712       C  
ATOM   1040  O   ALA A 138     108.274  32.186 -88.671  1.00 62.66           O  
ANISOU 1040  O   ALA A 138     4628  12735   6444   -808   -423   -581       O  
ATOM   1041  CB  ALA A 138     105.513  31.741 -89.377  1.00 45.78           C  
ANISOU 1041  CB  ALA A 138     2764  10373   4257   -692   -339   -422       C  
ATOM   1042  N   GLY A 139     107.703  34.322 -88.273  1.00 55.69           N  
ANISOU 1042  N   GLY A 139     3737  11825   5599  -1047   -374   -938       N  
ATOM   1043  CA  GLY A 139     109.053  34.811 -88.485  1.00 59.20           C  
ANISOU 1043  CA  GLY A 139     4047  12278   6168  -1146   -369  -1041       C  
ATOM   1044  C   GLY A 139     109.498  34.724 -89.929  1.00 65.54           C  
ANISOU 1044  C   GLY A 139     4852  12878   7173  -1142   -273   -949       C  
ATOM   1045  O   GLY A 139     110.678  34.466 -90.195  1.00 71.42           O  
ANISOU 1045  O   GLY A 139     5492  13643   8002  -1142   -284   -915       O  
ATOM   1046  N   ASN A 140     108.582  34.922 -90.871  1.00 59.38           N  
ANISOU 1046  N   ASN A 140     4184  11909   6469  -1129   -173   -902       N  
ATOM   1047  CA  ASN A 140     108.910  34.916 -92.287  1.00 56.15           C  
ANISOU 1047  CA  ASN A 140     3788  11300   6247  -1113    -57   -818       C  
ATOM   1048  C   ASN A 140     108.784  36.319 -92.868  1.00 63.00           C  
ANISOU 1048  C   ASN A 140     4658  12009   7271  -1264     89   -993       C  
ATOM   1049  O   ASN A 140     108.043  37.160 -92.364  1.00 64.16           O  
ANISOU 1049  O   ASN A 140     4843  12164   7370  -1355    111  -1146       O  
ATOM   1050  CB  ASN A 140     108.001  33.953 -93.059  1.00 51.81           C  
ANISOU 1050  CB  ASN A 140     3370  10645   5671   -954    -33   -609       C  
ATOM   1051  CG  ASN A 140     108.093  32.528 -92.543  1.00 52.00           C  
ANISOU 1051  CG  ASN A 140     3405  10792   5561   -807   -145   -430       C  
ATOM   1052  OD1 ASN A 140     109.078  32.148 -91.906  1.00 49.83           O  
ANISOU 1052  OD1 ASN A 140     3029  10661   5243   -800   -220   -422       O  
ATOM   1053  ND2 ASN A 140     107.063  31.732 -92.815  1.00 46.17           N  
ANISOU 1053  ND2 ASN A 140     2787   9996   4761   -687   -144   -287       N  
ATOM   1054  N   SER A 141     109.524  36.564 -93.942  1.00 69.67           N  
ANISOU 1054  N   SER A 141     5466  12700   8305  -1287    206   -964       N  
ATOM   1055  CA  SER A 141     109.446  37.834 -94.664  1.00 76.49           C  
ANISOU 1055  CA  SER A 141     6349  13372   9342  -1411    393  -1099       C  
ATOM   1056  C   SER A 141     109.367  37.693 -96.183  1.00 79.98           C  
ANISOU 1056  C   SER A 141     6867  13598   9924  -1320    558   -954       C  
ATOM   1057  O   SER A 141     108.734  38.536 -96.826  1.00 77.23           O  
ANISOU 1057  O   SER A 141     6610  13079   9655  -1354    728  -1012       O  
ATOM   1058  CB  SER A 141     110.656  38.714 -94.321  1.00 80.78           C  
ANISOU 1058  CB  SER A 141     6748  13931  10014  -1583    418  -1282       C  
ATOM   1059  OG  SER A 141     111.864  38.017 -94.609  1.00 83.11           O  
ANISOU 1059  OG  SER A 141     6935  14268  10376  -1530    374  -1169       O  
ATOM   1060  N   ASP A 142     109.996  36.686 -96.786  1.00 85.14           N  
ANISOU 1060  N   ASP A 142     7495  14247  10606  -1196    528   -769       N  
ATOM   1061  CA  ASP A 142     109.914  36.455 -98.224  1.00 92.56           C  
ANISOU 1061  CA  ASP A 142     8516  14998  11655  -1083    678   -623       C  
ATOM   1062  C   ASP A 142     108.757  35.490 -98.480  1.00 87.00           C  
ANISOU 1062  C   ASP A 142     7948  14297  10809   -914    622   -468       C  
ATOM   1063  O   ASP A 142     108.819  34.327 -98.076  1.00 93.49           O  
ANISOU 1063  O   ASP A 142     8761  15236  11524   -816    475   -347       O  
ATOM   1064  CB  ASP A 142     111.233  35.899 -98.749  1.00100.20           C  
ANISOU 1064  CB  ASP A 142     9382  15957  12733  -1040    685   -515       C  
ATOM   1065  CG  ASP A 142     111.103  35.309-100.136  1.00104.50           C  
ANISOU 1065  CG  ASP A 142    10021  16347  13335   -877    800   -329       C  
ATOM   1066  OD1 ASP A 142     111.498  34.137-100.326  1.00105.84           O  
ANISOU 1066  OD1 ASP A 142    10180  16571  13465   -751    716   -169       O  
ATOM   1067  OD2 ASP A 142     110.632  36.037-101.044  1.00103.87           O  
ANISOU 1067  OD2 ASP A 142    10038  16090  13339   -868    985   -346       O  
ATOM   1068  N   LEU A 143     107.703  35.962 -99.150  1.00 76.24           N  
ANISOU 1068  N   LEU A 143     6735  12781   9450   -869    743   -471       N  
ATOM   1069  CA  LEU A 143     106.502  35.163 -99.383  1.00 58.72           C  
ANISOU 1069  CA  LEU A 143     4676  10529   7107   -712    685   -347       C  
ATOM   1070  C   LEU A 143     106.615  34.359-100.679  1.00 54.86           C  
ANISOU 1070  C   LEU A 143     4272   9904   6668   -541    743   -166       C  
ATOM   1071  O   LEU A 143     107.366  34.711-101.591  1.00 56.11           O  
ANISOU 1071  O   LEU A 143     4430   9927   6962   -527    876   -142       O  
ATOM   1072  CB  LEU A 143     105.258  36.055 -99.436  1.00 55.40           C  
ANISOU 1072  CB  LEU A 143     4434   9964   6651   -717    760   -435       C  
ATOM   1073  CG  LEU A 143     104.995  36.903 -98.189  1.00 60.38           C  
ANISOU 1073  CG  LEU A 143     5013  10705   7222   -875    716   -622       C  
ATOM   1074  CD1 LEU A 143     103.720  37.708 -98.356  1.00 58.50           C  
ANISOU 1074  CD1 LEU A 143     4968  10311   6949   -850    805   -681       C  
ATOM   1075  CD2 LEU A 143     104.913  36.033 -96.947  1.00 60.10           C  
ANISOU 1075  CD2 LEU A 143     4860  10944   7032   -887    516   -606       C  
ATOM   1076  N   ILE A 144     105.851  33.269-100.757  1.00 47.88           N  
ANISOU 1076  N   ILE A 144     3465   9052   5677   -408    650    -43       N  
ATOM   1077  CA  ILE A 144     105.874  32.399-101.932  1.00 47.69           C  
ANISOU 1077  CA  ILE A 144     3528   8910   5682   -240    687    117       C  
ATOM   1078  C   ILE A 144     104.472  31.856-102.174  1.00 46.06           C  
ANISOU 1078  C   ILE A 144     3483   8643   5375   -123    642    169       C  
ATOM   1079  O   ILE A 144     103.735  31.549-101.231  1.00 47.59           O  
ANISOU 1079  O   ILE A 144     3664   8957   5462   -153    532    146       O  
ATOM   1080  CB  ILE A 144     106.897  31.254-101.764  1.00 51.93           C  
ANISOU 1080  CB  ILE A 144     3917   9591   6222   -201    604    237       C  
ATOM   1081  CG1 ILE A 144     106.882  30.319-102.970  1.00 58.18           C  
ANISOU 1081  CG1 ILE A 144     4812  10253   7039    -24    645    395       C  
ATOM   1082  CG2 ILE A 144     106.593  30.457-100.541  1.00 50.03           C  
ANISOU 1082  CG2 ILE A 144     3645   9511   5852   -215    430    255       C  
ATOM   1083  CD1 ILE A 144     107.830  30.729-104.055  1.00 63.29           C  
ANISOU 1083  CD1 ILE A 144     5461  10763   7823     10    792    427       C  
ATOM   1084  N   LEU A 145     104.104  31.749-103.448  1.00 46.13           N  
ANISOU 1084  N   LEU A 145     3639   8469   5418     13    730    235       N  
ATOM   1085  CA  LEU A 145     102.867  31.110-103.881  1.00 37.68           C  
ANISOU 1085  CA  LEU A 145     2709   7339   4268    139    687    287       C  
ATOM   1086  C   LEU A 145     103.102  29.619-104.084  1.00 36.64           C  
ANISOU 1086  C   LEU A 145     2548   7258   4116    238    602    423       C  
ATOM   1087  O   LEU A 145     104.079  29.237-104.738  1.00 43.81           O  
ANISOU 1087  O   LEU A 145     3422   8129   5093    294    649    503       O  
ATOM   1088  CB  LEU A 145     102.361  31.722-105.176  1.00 34.58           C  
ANISOU 1088  CB  LEU A 145     2487   6743   3908    253    818    281       C  
ATOM   1089  CG  LEU A 145     101.495  32.976-105.088  1.00 40.65           C  
ANISOU 1089  CG  LEU A 145     3353   7436   4656    216    895    167       C  
ATOM   1090  CD1 LEU A 145     100.236  32.685-104.280  1.00 39.91           C  
ANISOU 1090  CD1 LEU A 145     3283   7434   4448    199    777    131       C  
ATOM   1091  CD2 LEU A 145     102.274  34.153-104.514  1.00 41.60           C  
ANISOU 1091  CD2 LEU A 145     3390   7563   4855     57    980     61       C  
ATOM   1092  N   PRO A 146     102.226  28.761-103.577  1.00 35.00           N  
ANISOU 1092  N   PRO A 146     2356   7119   3823    266    494    456       N  
ATOM   1093  CA  PRO A 146     102.497  27.322-103.591  1.00 35.17           C  
ANISOU 1093  CA  PRO A 146     2338   7192   3834    344    422    584       C  
ATOM   1094  C   PRO A 146     102.163  26.675-104.928  1.00 37.24           C  
ANISOU 1094  C   PRO A 146     2733   7296   4122    498    462    649       C  
ATOM   1095  O   PRO A 146     101.436  27.221-105.759  1.00 36.16           O  
ANISOU 1095  O   PRO A 146     2726   7031   3983    559    519    596       O  
ATOM   1096  CB  PRO A 146     101.569  26.795-102.495  1.00 37.65           C  
ANISOU 1096  CB  PRO A 146     2627   7622   4055    306    313    580       C  
ATOM   1097  CG  PRO A 146     100.384  27.705-102.590  1.00 35.78           C  
ANISOU 1097  CG  PRO A 146     2499   7312   3785    285    340    471       C  
ATOM   1098  CD  PRO A 146     100.922  29.069-102.966  1.00 34.82           C  
ANISOU 1098  CD  PRO A 146     2390   7120   3718    231    446    382       C  
ATOM   1099  N   VAL A 147     102.711  25.477-105.113  1.00 37.61           N  
ANISOU 1099  N   VAL A 147     2744   7360   4187    570    432    764       N  
ATOM   1100  CA  VAL A 147     102.301  24.594-106.201  1.00 40.01           C  
ANISOU 1100  CA  VAL A 147     3167   7535   4501    712    444    821       C  
ATOM   1101  C   VAL A 147     101.045  23.850-105.760  1.00 37.51           C  
ANISOU 1101  C   VAL A 147     2889   7236   4128    717    357    810       C  
ATOM   1102  O   VAL A 147     101.068  23.151-104.734  1.00 31.78           O  
ANISOU 1102  O   VAL A 147     2073   6626   3377    668    289    863       O  
ATOM   1103  CB  VAL A 147     103.428  23.624-106.591  1.00 37.97           C  
ANISOU 1103  CB  VAL A 147     2861   7275   4292    789    463    947       C  
ATOM   1104  CG1 VAL A 147     102.937  22.623-107.618  1.00 37.34           C  
ANISOU 1104  CG1 VAL A 147     2906   7066   4217    931    466    990       C  
ATOM   1105  CG2 VAL A 147     104.608  24.395-107.148  1.00 42.90           C  
ANISOU 1105  CG2 VAL A 147     3449   7866   4985    791    564    956       C  
ATOM   1106  N   PRO A 148      99.928  23.982-106.476  1.00 33.85           N  
ANISOU 1106  N   PRO A 148     2550   6669   3644    778    360    744       N  
ATOM   1107  CA  PRO A 148      98.719  23.243-106.096  1.00 37.42           C  
ANISOU 1107  CA  PRO A 148     3025   7132   4061    776    282    729       C  
ATOM   1108  C   PRO A 148      98.813  21.779-106.496  1.00 37.58           C  
ANISOU 1108  C   PRO A 148     3062   7099   4116    857    260    813       C  
ATOM   1109  O   PRO A 148      99.387  21.432-107.531  1.00 34.79           O  
ANISOU 1109  O   PRO A 148     2766   6654   3800    958    305    849       O  
ATOM   1110  CB  PRO A 148      97.609  23.961-106.875  1.00 36.62           C  
ANISOU 1110  CB  PRO A 148     3041   6942   3929    826    300    622       C  
ATOM   1111  CG  PRO A 148      98.304  24.521-108.068  1.00 34.98           C  
ANISOU 1111  CG  PRO A 148     2908   6635   3748    921    391    622       C  
ATOM   1112  CD  PRO A 148      99.691  24.892-107.610  1.00 32.09           C  
ANISOU 1112  CD  PRO A 148     2443   6325   3424    853    440    678       C  
ATOM   1113  N   ALA A 149      98.244  20.915-105.657  1.00 33.24           N  
ANISOU 1113  N   ALA A 149     3252   5605   3771   -139    717    -66       N  
ATOM   1114  CA  ALA A 149      98.128  19.488-105.947  1.00 34.60           C  
ANISOU 1114  CA  ALA A 149     3346   5705   4096    -69    777   -103       C  
ATOM   1115  C   ALA A 149      96.648  19.146-106.089  1.00 38.79           C  
ANISOU 1115  C   ALA A 149     3930   6187   4620    -97    874   -144       C  
ATOM   1116  O   ALA A 149      95.920  19.103-105.091  1.00 40.57           O  
ANISOU 1116  O   ALA A 149     4264   6344   4806    -94    896    -56       O  
ATOM   1117  CB  ALA A 149      98.783  18.651-104.851  1.00 29.28           C  
ANISOU 1117  CB  ALA A 149     2686   4938   3499     -6    702     29       C  
ATOM   1118  N   PHE A 150      96.208  18.891-107.323  1.00 40.59           N  
ANISOU 1118  N   PHE A 150     4077   6474   4871   -144    930   -263       N  
ATOM   1119  CA  PHE A 150      94.801  18.637-107.618  1.00 37.65           C  
ANISOU 1119  CA  PHE A 150     3693   6117   4494   -224    974   -274       C  
ATOM   1120  C   PHE A 150      94.510  17.142-107.574  1.00 41.81           C  
ANISOU 1120  C   PHE A 150     4245   6486   5156   -267   1017   -337       C  
ATOM   1121  O   PHE A 150      95.045  16.380-108.385  1.00 40.83           O  
ANISOU 1121  O   PHE A 150     4123   6304   5088   -287   1053   -487       O  
ATOM   1122  CB  PHE A 150      94.415  19.175-108.995  1.00 33.65           C  
ANISOU 1122  CB  PHE A 150     3094   5793   3897   -310    961   -344       C  
ATOM   1123  CG  PHE A 150      94.707  20.626-109.194  1.00 26.91           C  
ANISOU 1123  CG  PHE A 150     2224   5060   2940   -269    940   -266       C  
ATOM   1124  CD1 PHE A 150      93.863  21.592-108.681  1.00 28.89           C  
ANISOU 1124  CD1 PHE A 150     2492   5325   3159   -228    970   -121       C  
ATOM   1125  CD2 PHE A 150      95.813  21.024-109.925  1.00 32.88           C  
ANISOU 1125  CD2 PHE A 150     2951   5892   3648   -267    928   -325       C  
ATOM   1126  CE1 PHE A 150      94.130  22.924-108.877  1.00 33.29           C  
ANISOU 1126  CE1 PHE A 150     3076   5928   3645   -191    979    -51       C  
ATOM   1127  CE2 PHE A 150      96.081  22.354-110.123  1.00 26.46           C  
ANISOU 1127  CE2 PHE A 150     2137   5158   2757   -259    915   -239       C  
ATOM   1128  CZ  PHE A 150      95.239  23.300-109.602  1.00 26.20           C  
ANISOU 1128  CZ  PHE A 150     2158   5098   2700   -225    936   -109       C  
ATOM   1129  N   ASN A 151      93.638  16.733-106.656  1.00 38.67           N  
ANISOU 1129  N   ASN A 151     3886   5996   4810   -287   1049   -225       N  
ATOM   1130  CA  ASN A 151      93.112  15.370-106.635  1.00 49.64           C  
ANISOU 1130  CA  ASN A 151     5305   7216   6342   -379   1098   -261       C  
ATOM   1131  C   ASN A 151      92.194  15.171-107.838  1.00 53.14           C  
ANISOU 1131  C   ASN A 151     5669   7763   6760   -584   1074   -383       C  
ATOM   1132  O   ASN A 151      91.083  15.708-107.866  1.00 60.76           O  
ANISOU 1132  O   ASN A 151     6516   8885   7683   -667   1049   -272       O  
ATOM   1133  CB  ASN A 151      92.357  15.136-105.327  1.00 55.90           C  
ANISOU 1133  CB  ASN A 151     6141   7922   7175   -366   1151    -67       C  
ATOM   1134  CG  ASN A 151      92.078  13.666-105.048  1.00 64.06           C  
ANISOU 1134  CG  ASN A 151     7237   8715   8387   -444   1211    -56       C  
ATOM   1135  OD1 ASN A 151      91.650  13.308-103.951  1.00 66.33           O  
ANISOU 1135  OD1 ASN A 151     7579   8908   8716   -426   1270    122       O  
ATOM   1136  ND2 ASN A 151      92.329  12.810-106.031  1.00 70.69           N  
ANISOU 1136  ND2 ASN A 151     8104   9432   9321   -537   1220   -250       N  
ATOM   1137  N   VAL A 152      92.637  14.398-108.830  1.00 44.90           N  
ANISOU 1137  N   VAL A 152     4689   6639   5731   -672   1089   -599       N  
ATOM   1138  CA  VAL A 152      91.837  14.170-110.029  1.00 39.69           C  
ANISOU 1138  CA  VAL A 152     4002   6099   4978   -929   1030   -741       C  
ATOM   1139  C   VAL A 152      91.316  12.740-110.146  1.00 43.78           C  
ANISOU 1139  C   VAL A 152     4639   6377   5617  -1145   1067   -868       C  
ATOM   1140  O   VAL A 152      90.293  12.529-110.816  1.00 39.56           O  
ANISOU 1140  O   VAL A 152     4054   5961   5014  -1437    968   -916       O  
ATOM   1141  CB  VAL A 152      92.610  14.560-111.308  1.00 41.64           C  
ANISOU 1141  CB  VAL A 152     4285   6485   5051   -936   1025   -931       C  
ATOM   1142  CG1 VAL A 152      92.911  16.050-111.309  1.00 37.41           C  
ANISOU 1142  CG1 VAL A 152     3623   6192   4399   -792    971   -781       C  
ATOM   1143  CG2 VAL A 152      93.893  13.746-111.442  1.00 41.11           C  
ANISOU 1143  CG2 VAL A 152     4375   6169   5077   -798   1181  -1107       C  
ATOM   1144  N   ILE A 153      91.972  11.759-109.531  1.00 46.45           N  
ANISOU 1144  N   ILE A 153     5130   6381   6140  -1029   1196   -901       N  
ATOM   1145  CA  ILE A 153      91.528  10.369-109.552  1.00 59.55           C  
ANISOU 1145  CA  ILE A 153     6948   7726   7954  -1226   1267  -1010       C  
ATOM   1146  C   ILE A 153      91.456   9.872-108.115  1.00 63.12           C  
ANISOU 1146  C   ILE A 153     7407   7958   8617  -1092   1337   -762       C  
ATOM   1147  O   ILE A 153      92.422  10.019-107.358  1.00 64.58           O  
ANISOU 1147  O   ILE A 153     7605   8069   8865   -801   1389   -634       O  
ATOM   1148  CB  ILE A 153      92.470   9.478-110.386  1.00 66.58           C  
ANISOU 1148  CB  ILE A 153     8080   8338   8879  -1201   1423  -1311       C  
ATOM   1149  CG1 ILE A 153      92.428   9.879-111.863  1.00 66.25           C  
ANISOU 1149  CG1 ILE A 153     8084   8526   8562  -1392   1369  -1574       C  
ATOM   1150  CG2 ILE A 153      92.106   8.009-110.217  1.00 67.64           C  
ANISOU 1150  CG2 ILE A 153     8435   8042   9223  -1370   1540  -1409       C  
ATOM   1151  CD1 ILE A 153      91.115   9.573-112.538  1.00 63.99           C  
ANISOU 1151  CD1 ILE A 153     7820   8349   8145  -1840   1213  -1678       C  
ATOM   1152  N   ASN A 154      90.321   9.282-107.743  1.00 65.98           N  
ANISOU 1152  N   ASN A 154     7751   8238   9078  -1327   1325   -668       N  
ATOM   1153  CA  ASN A 154      90.071   8.859-106.372  1.00 67.83           C  
ANISOU 1153  CA  ASN A 154     7989   8306   9477  -1236   1401   -393       C  
ATOM   1154  C   ASN A 154      89.912   7.347-106.282  1.00 75.43           C  
ANISOU 1154  C   ASN A 154     9150   8837  10675  -1396   1514   -447       C  
ATOM   1155  O   ASN A 154      89.514   6.685-107.245  1.00 79.39           O  
ANISOU 1155  O   ASN A 154     9760   9208  11195  -1695   1506   -695       O  
ATOM   1156  CB  ASN A 154      88.823   9.540-105.802  1.00 65.87           C  
ANISOU 1156  CB  ASN A 154     7523   8330   9176  -1340   1351   -152       C  
ATOM   1157  CG  ASN A 154      89.010  11.028-105.626  1.00 67.14           C  
ANISOU 1157  CG  ASN A 154     7545   8823   9144  -1126   1301    -58       C  
ATOM   1158  OD1 ASN A 154      88.780  11.804-106.550  1.00 65.67           O  
ANISOU 1158  OD1 ASN A 154     7235   8891   8827  -1194   1202   -150       O  
ATOM   1159  ND2 ASN A 154      89.444  11.436-104.439  1.00 67.11           N  
ANISOU 1159  ND2 ASN A 154     7589   8804   9105   -884   1365    132       N  
ATOM   1160  N   GLY A 155      90.225   6.816-105.109  1.00 75.54           N  
ANISOU 1160  N   GLY A 155     9236   8619  10848  -1215   1616   -208       N  
ATOM   1161  CA  GLY A 155      90.075   5.400-104.864  1.00 78.13           C  
ANISOU 1161  CA  GLY A 155     9761   8490  11436  -1335   1749   -190       C  
ATOM   1162  C   GLY A 155      90.136   5.099-103.384  1.00 73.04           C  
ANISOU 1162  C   GLY A 155     9125   7723  10902  -1153   1823    192       C  
ATOM   1163  O   GLY A 155      90.013   5.993-102.546  1.00 72.81           O  
ANISOU 1163  O   GLY A 155     8960   7996  10710  -1017   1768    419       O  
ATOM   1164  N   GLY A 156      90.336   3.822-103.073  1.00 74.01           N  
ANISOU 1164  N   GLY A 156     9450   7382  11291  -1156   1966    262       N  
ATOM   1165  CA  GLY A 156      90.390   3.418-101.679  1.00 74.78           C  
ANISOU 1165  CA  GLY A 156     9580   7348  11486  -1000   2036    665       C  
ATOM   1166  C   GLY A 156      89.023   3.500-101.027  1.00 74.58           C  
ANISOU 1166  C   GLY A 156     9446   7470  11423  -1264   2047    877       C  
ATOM   1167  O   GLY A 156      87.990   3.245-101.655  1.00 70.57           O  
ANISOU 1167  O   GLY A 156     8883   6955  10976  -1633   2040    740       O  
ATOM   1168  N   SER A 157      89.015   3.874 -99.747  1.00 77.92           N  
ANISOU 1168  N   SER A 157     9828   8051  11726  -1089   2067   1229       N  
ATOM   1169  CA  SER A 157      87.764   4.025 -99.013  1.00 87.33           C  
ANISOU 1169  CA  SER A 157    10906   9407  12867  -1280   2143   1470       C  
ATOM   1170  C   SER A 157      86.938   5.214 -99.488  1.00 91.23           C  
ANISOU 1170  C   SER A 157    11150  10344  13167  -1394   2074   1351       C  
ATOM   1171  O   SER A 157      85.784   5.350 -99.068  1.00 84.83           O  
ANISOU 1171  O   SER A 157    10184   9687  12361  -1564   2167   1539       O  
ATOM   1172  CB  SER A 157      88.050   4.162 -97.517  1.00 86.90           C  
ANISOU 1172  CB  SER A 157    10933   9418  12666  -1047   2210   1859       C  
ATOM   1173  OG  SER A 157      88.821   5.321 -97.250  1.00 85.30           O  
ANISOU 1173  OG  SER A 157    10711   9536  12162   -784   2092   1830       O  
ATOM   1174  N   HIS A 158      87.491   6.067-100.353  1.00101.17           N  
ANISOU 1174  N   HIS A 158    12349  11810  14281  -1291   1936   1081       N  
ATOM   1175  CA  HIS A 158      86.781   7.261-100.794  1.00104.19           C  
ANISOU 1175  CA  HIS A 158    12495  12599  14492  -1348   1875   1015       C  
ATOM   1176  C   HIS A 158      85.738   6.962-101.863  1.00105.50           C  
ANISOU 1176  C   HIS A 158    12485  12817  14782  -1726   1809    876       C  
ATOM   1177  O   HIS A 158      84.749   7.694-101.976  1.00109.70           O  
ANISOU 1177  O   HIS A 158    12750  13670  15260  -1824   1799    976       O  
ATOM   1178  CB  HIS A 158      87.773   8.301-101.324  1.00105.94           C  
ANISOU 1178  CB  HIS A 158    12724  13016  14513  -1117   1748    814       C  
ATOM   1179  CG  HIS A 158      88.444   9.105-100.252  1.00107.03           C  
ANISOU 1179  CG  HIS A 158    12945  13282  14440   -823   1767    977       C  
ATOM   1180  ND1 HIS A 158      88.978  10.354-100.484  1.00104.82           N  
ANISOU 1180  ND1 HIS A 158    12631  13249  13947   -664   1680    868       N  
ATOM   1181  CD2 HIS A 158      88.666   8.839 -98.943  1.00108.43           C  
ANISOU 1181  CD2 HIS A 158    13265  13375  14557   -697   1850   1241       C  
ATOM   1182  CE1 HIS A 158      89.499  10.824 -99.364  1.00104.19           C  
ANISOU 1182  CE1 HIS A 158    12684  13223  13682   -481   1698   1030       C  
ATOM   1183  NE2 HIS A 158      89.323   9.923 -98.414  1.00105.76           N  
ANISOU 1183  NE2 HIS A 158    12992  13245  13947   -495   1792   1261       N  
ATOM   1184  N   ALA A 159      85.929   5.906-102.650  1.00 95.35           N  
ANISOU 1184  N   ALA A 159    11347  11221  13659  -1948   1768    657       N  
ATOM   1185  CA  ALA A 159      85.099   5.662-103.817  1.00 86.08           C  
ANISOU 1185  CA  ALA A 159    10058  10120  12529  -2361   1641    461       C  
ATOM   1186  C   ALA A 159      84.621   4.218-103.844  1.00 84.76           C  
ANISOU 1186  C   ALA A 159    10043   9542  12619  -2724   1703    446       C  
ATOM   1187  O   ALA A 159      85.188   3.336-103.194  1.00 84.07           O  
ANISOU 1187  O   ALA A 159    10207   9042  12696  -2603   1853    521       O  
ATOM   1188  CB  ALA A 159      85.855   5.981-105.111  1.00 85.69           C  
ANISOU 1188  CB  ALA A 159    10106  10127  12325  -2345   1506     84       C  
ATOM   1189  N   GLY A 160      83.562   3.990-104.623  1.00 84.82           N  
ANISOU 1189  N   GLY A 160     9892   9668  12666  -3193   1571    370       N  
ATOM   1190  CA  GLY A 160      83.019   2.660-104.812  1.00 87.26           C  
ANISOU 1190  CA  GLY A 160    10357   9592  13207  -3647   1594    309       C  
ATOM   1191  C   GLY A 160      83.809   1.776-105.746  1.00 90.26           C  
ANISOU 1191  C   GLY A 160    11159   9528  13609  -3774   1598   -124       C  
ATOM   1192  O   GLY A 160      83.504   0.584-105.856  1.00 91.02           O  
ANISOU 1192  O   GLY A 160    11486   9184  13912  -4131   1661   -211       O  
ATOM   1193  N   ASN A 161      84.811   2.326-106.424  1.00 91.67           N  
ANISOU 1193  N   ASN A 161    11459   9787  13584  -3494   1564   -397       N  
ATOM   1194  CA  ASN A 161      85.641   1.511-107.292  1.00 97.85           C  
ANISOU 1194  CA  ASN A 161    12663  10133  14382  -3546   1647   -812       C  
ATOM   1195  C   ASN A 161      86.568   0.623-106.468  1.00100.88           C  
ANISOU 1195  C   ASN A 161    13336   9958  15036  -3202   1923   -713       C  
ATOM   1196  O   ASN A 161      86.837   0.873-105.288  1.00100.61           O  
ANISOU 1196  O   ASN A 161    13173   9970  15084  -2847   2002   -345       O  
ATOM   1197  CB  ASN A 161      86.453   2.387-108.250  1.00 94.44           C  
ANISOU 1197  CB  ASN A 161    12245   9980  13657  -3330   1569  -1091       C  
ATOM   1198  CG  ASN A 161      87.245   3.471-107.536  1.00 92.79           C  
ANISOU 1198  CG  ASN A 161    11836  10053  13366  -2772   1599   -858       C  
ATOM   1199  OD1 ASN A 161      87.541   3.369-106.345  1.00 92.76           O  
ANISOU 1199  OD1 ASN A 161    11804   9923  13518  -2479   1719   -556       O  
ATOM   1200  ND2 ASN A 161      87.596   4.520-108.271  1.00 91.05           N  
ANISOU 1200  ND2 ASN A 161    11496  10219  12880  -2655   1478   -993       N  
ATOM   1201  N   LYS A 162      87.055  -0.432-107.112  1.00105.37           N  
ANISOU 1201  N   LYS A 162    14318   9987  15733  -3314   2078  -1040       N  
ATOM   1202  CA  LYS A 162      87.989  -1.361-106.494  1.00109.10           C  
ANISOU 1202  CA  LYS A 162    15078   9869  16505  -2966   2365   -949       C  
ATOM   1203  C   LYS A 162      89.394  -0.789-106.358  1.00107.83           C  
ANISOU 1203  C   LYS A 162    14882   9798  16290  -2351   2455   -913       C  
ATOM   1204  O   LYS A 162      90.263  -1.463-105.792  1.00109.48           O  
ANISOU 1204  O   LYS A 162    15252   9584  16760  -1990   2675   -758       O  
ATOM   1205  CB  LYS A 162      88.017  -2.649-107.312  1.00114.46           C  
ANISOU 1205  CB  LYS A 162    16240   9900  17349  -3287   2547  -1340       C  
ATOM   1206  CG  LYS A 162      87.933  -2.408-108.799  1.00115.07           C  
ANISOU 1206  CG  LYS A 162    16474  10131  17118  -3610   2441  -1861       C  
ATOM   1207  CD  LYS A 162      87.493  -3.644-109.551  1.00121.78           C  
ANISOU 1207  CD  LYS A 162    17766  10488  18018  -4079   2505  -2215       C  
ATOM   1208  CE  LYS A 162      86.017  -3.563-109.890  1.00123.20           C  
ANISOU 1208  CE  LYS A 162    17735  11061  18014  -4708   2130  -2191       C  
ATOM   1209  NZ  LYS A 162      85.596  -4.660-110.801  1.00128.47           N  
ANISOU 1209  NZ  LYS A 162    18785  11431  18597  -5107   2067  -2527       N  
ATOM   1210  N   LEU A 163      89.629   0.422-106.860  1.00103.64           N  
ANISOU 1210  N   LEU A 163    14123   9805  15450  -2235   2287  -1014       N  
ATOM   1211  CA  LEU A 163      90.937   1.057-106.761  1.00102.57           C  
ANISOU 1211  CA  LEU A 163    13908   9808  15258  -1709   2342   -965       C  
ATOM   1212  C   LEU A 163      91.319   1.245-105.299  1.00 98.20           C  
ANISOU 1212  C   LEU A 163    13179   9308  14825  -1342   2344   -478       C  
ATOM   1213  O   LEU A 163      90.577   1.858-104.526  1.00 97.52           O  
ANISOU 1213  O   LEU A 163    12868   9559  14627  -1422   2199   -210       O  
ATOM   1214  CB  LEU A 163      90.915   2.400-107.490  1.00 99.13           C  
ANISOU 1214  CB  LEU A 163    13240   9962  14462  -1728   2137  -1113       C  
ATOM   1215  CG  LEU A 163      92.203   2.889-108.155  1.00 97.12           C  
ANISOU 1215  CG  LEU A 163    13006   9793  14103  -1383   2220  -1295       C  
ATOM   1216  CD1 LEU A 163      91.899   4.025-109.117  1.00 94.22           C  
ANISOU 1216  CD1 LEU A 163    12485   9941  13375  -1553   2024  -1490       C  
ATOM   1217  CD2 LEU A 163      93.205   3.337-107.115  1.00 95.53           C  
ANISOU 1217  CD2 LEU A 163    12616   9683  13998   -896   2236   -941       C  
ATOM   1218  N   ALA A 164      92.486   0.721-104.924  1.00 92.64           N  
ANISOU 1218  N   ALA A 164    12578   8283  14339   -934   2519   -350       N  
ATOM   1219  CA  ALA A 164      92.872   0.714-103.520  1.00 83.83           C  
ANISOU 1219  CA  ALA A 164    11341   7183  13330   -627   2501    141       C  
ATOM   1220  C   ALA A 164      93.511   2.020-103.079  1.00 79.57           C  
ANISOU 1220  C   ALA A 164    10520   7180  12534   -352   2309    310       C  
ATOM   1221  O   ALA A 164      93.358   2.417-101.919  1.00 76.48           O  
ANISOU 1221  O   ALA A 164    10006   7004  12048   -271   2199    668       O  
ATOM   1222  CB  ALA A 164      93.835  -0.433-103.248  1.00 84.96           C  
ANISOU 1222  CB  ALA A 164    11674   6763  13842   -303   2745    290       C  
ATOM   1223  N   MET A 165      94.236   2.687-103.966  1.00 78.95           N  
ANISOU 1223  N   MET A 165    10365   7307  12326   -227   2281     58       N  
ATOM   1224  CA  MET A 165      94.962   3.886-103.580  1.00 80.61           C  
ANISOU 1224  CA  MET A 165    10330   7971  12326     13   2107    213       C  
ATOM   1225  C   MET A 165      94.045   5.100-103.633  1.00 76.01           C  
ANISOU 1225  C   MET A 165     9602   7863  11414   -224   1913    146       C  
ATOM   1226  O   MET A 165      93.232   5.246-104.548  1.00 76.74           O  
ANISOU 1226  O   MET A 165     9717   8032  11409   -514   1898   -133       O  
ATOM   1227  CB  MET A 165      96.183   4.065-104.477  1.00 82.30           C  
ANISOU 1227  CB  MET A 165    10500   8190  12582    258   2192     22       C  
ATOM   1228  CG  MET A 165      97.123   2.880-104.367  1.00 89.49           C  
ANISOU 1228  CG  MET A 165    11518   8615  13868    567   2434    145       C  
ATOM   1229  SD  MET A 165      98.673   3.050-105.253  1.00 95.66           S  
ANISOU 1229  SD  MET A 165    12178   9409  14759    940   2601     22       S  
ATOM   1230  CE  MET A 165      99.743   2.145-104.146  1.00 99.43           C  
ANISOU 1230  CE  MET A 165    12554   9574  15649   1400   2700    552       C  
ATOM   1231  N   GLN A 166      94.186   5.973-102.635  1.00 71.92           N  
ANISOU 1231  N   GLN A 166     8946   7661  10720   -101   1767    417       N  
ATOM   1232  CA  GLN A 166      93.154   6.963-102.343  1.00 68.81           C  
ANISOU 1232  CA  GLN A 166     8454   7618  10072   -287   1657    445       C  
ATOM   1233  C   GLN A 166      93.145   8.110-103.349  1.00 65.03           C  
ANISOU 1233  C   GLN A 166     7853   7469   9385   -347   1563    188       C  
ATOM   1234  O   GLN A 166      92.113   8.398-103.962  1.00 63.25           O  
ANISOU 1234  O   GLN A 166     7575   7377   9080   -591   1541     49       O  
ATOM   1235  CB  GLN A 166      93.339   7.496-100.919  1.00 70.56           C  
ANISOU 1235  CB  GLN A 166     8652   8018  10138   -142   1577    787       C  
ATOM   1236  CG  GLN A 166      92.246   8.444-100.465  1.00 66.98           C  
ANISOU 1236  CG  GLN A 166     8143   7861   9448   -285   1553    841       C  
ATOM   1237  CD  GLN A 166      92.226   8.624 -98.960  1.00 68.54           C  
ANISOU 1237  CD  GLN A 166     8422   8133   9485   -194   1551   1171       C  
ATOM   1238  OE1 GLN A 166      91.999   7.672 -98.211  1.00 72.89           O  
ANISOU 1238  OE1 GLN A 166     9071   8470  10155   -205   1636   1404       O  
ATOM   1239  NE2 GLN A 166      92.466   9.849 -98.507  1.00 66.99           N  
ANISOU 1239  NE2 GLN A 166     8224   8231   8999   -123   1462   1190       N  
ATOM   1240  N   GLU A 167      94.278   8.789-103.522  1.00 62.76           N  
ANISOU 1240  N   GLU A 167     7496   7335   9016   -139   1494    164       N  
ATOM   1241  CA  GLU A 167      94.321  10.008-104.316  1.00 59.02           C  
ANISOU 1241  CA  GLU A 167     6909   7185   8330   -180   1404    -12       C  
ATOM   1242  C   GLU A 167      95.436   9.944-105.348  1.00 60.27           C  
ANISOU 1242  C   GLU A 167     7047   7310   8542    -59   1450   -208       C  
ATOM   1243  O   GLU A 167      96.559   9.530-105.043  1.00 65.16           O  
ANISOU 1243  O   GLU A 167     7648   7799   9310    170   1492    -96       O  
ATOM   1244  CB  GLU A 167      94.524  11.243-103.431  1.00 58.00           C  
ANISOU 1244  CB  GLU A 167     6712   7338   7989    -87   1280    170       C  
ATOM   1245  CG  GLU A 167      93.568  11.335-102.257  1.00 67.81           C  
ANISOU 1245  CG  GLU A 167     8008   8607   9148   -149   1295    385       C  
ATOM   1246  CD  GLU A 167      93.851  12.529-101.369  1.00 70.35           C  
ANISOU 1246  CD  GLU A 167     8352   9157   9220    -68   1208    515       C  
ATOM   1247  OE1 GLU A 167      94.606  13.427-101.798  1.00 67.94           O  
ANISOU 1247  OE1 GLU A 167     7993   9011   8811    -14   1112    420       O  
ATOM   1248  OE2 GLU A 167      93.319  12.567-100.239  1.00 71.86           O  
ANISOU 1248  OE2 GLU A 167     8642   9356   9305    -77   1250    706       O  
ATOM   1249  N   PHE A 168      95.115  10.369-106.570  1.00 56.77           N  
ANISOU 1249  N   PHE A 168     6587   7008   7974   -209   1450   -467       N  
ATOM   1250  CA  PHE A 168      96.085  10.562-107.644  1.00 46.20           C  
ANISOU 1250  CA  PHE A 168     5227   5719   6607   -117   1516   -662       C  
ATOM   1251  C   PHE A 168      96.030  12.032-108.038  1.00 43.11           C  
ANISOU 1251  C   PHE A 168     4699   5712   5967   -163   1382   -673       C  
ATOM   1252  O   PHE A 168      95.032  12.488-108.607  1.00 50.74           O  
ANISOU 1252  O   PHE A 168     5654   6845   6779   -370   1316   -761       O  
ATOM   1253  CB  PHE A 168      95.783   9.654-108.836  1.00 50.02           C  
ANISOU 1253  CB  PHE A 168     5887   5998   7120   -282   1665   -978       C  
ATOM   1254  CG  PHE A 168      95.974   8.190-108.550  1.00 53.17           C  
ANISOU 1254  CG  PHE A 168     6469   5934   7799   -216   1852   -994       C  
ATOM   1255  CD1 PHE A 168      95.002   7.468-107.879  1.00 52.04           C  
ANISOU 1255  CD1 PHE A 168     6418   5587   7767   -384   1835   -898       C  
ATOM   1256  CD2 PHE A 168      97.125   7.534-108.958  1.00 57.38           C  
ANISOU 1256  CD2 PHE A 168     7075   6215   8511     28   2079  -1081       C  
ATOM   1257  CE1 PHE A 168      95.176   6.125-107.613  1.00 56.23           C  
ANISOU 1257  CE1 PHE A 168     7141   5646   8578   -328   2022   -891       C  
ATOM   1258  CE2 PHE A 168      97.304   6.187-108.696  1.00 58.98           C  
ANISOU 1258  CE2 PHE A 168     7466   5935   9010    125   2290  -1075       C  
ATOM   1259  CZ  PHE A 168      96.327   5.482-108.022  1.00 58.88           C  
ANISOU 1259  CZ  PHE A 168     7575   5696   9102    -63   2252   -982       C  
ATOM   1260  N   MET A 169      97.094  12.772-107.736  1.00 42.37           N  
ANISOU 1260  N   MET A 169     4489   5756   5852     17   1332   -552       N  
ATOM   1261  CA  MET A 169      97.113  14.220-107.884  1.00 36.39           C  
ANISOU 1261  CA  MET A 169     3630   5306   4889    -20   1210   -517       C  
ATOM   1262  C   MET A 169      97.994  14.649-109.053  1.00 37.67           C  
ANISOU 1262  C   MET A 169     3720   5599   4994     18   1271   -655       C  
ATOM   1263  O   MET A 169      98.829  13.886-109.542  1.00 36.82           O  
ANISOU 1263  O   MET A 169     3615   5356   5020    134   1423   -743       O  
ATOM   1264  CB  MET A 169      97.593  14.884-106.590  1.00 34.79           C  
ANISOU 1264  CB  MET A 169     3384   5174   4660     77   1084   -273       C  
ATOM   1265  CG  MET A 169      96.545  14.888-105.495  1.00 41.80           C  
ANISOU 1265  CG  MET A 169     4366   6022   5494     12   1043   -139       C  
ATOM   1266  SD  MET A 169      97.248  15.080-103.851  1.00 45.71           S  
ANISOU 1266  SD  MET A 169     4907   6516   5945    113    921    132       S  
ATOM   1267  CE  MET A 169      97.975  13.460-103.626  1.00 41.88           C  
ANISOU 1267  CE  MET A 169     4399   5771   5743    265    984    239       C  
ATOM   1268  N   ILE A 170      97.779  15.888-109.506  1.00 36.54           N  
ANISOU 1268  N   ILE A 170     3517   5707   4658    -68   1187   -657       N  
ATOM   1269  CA  ILE A 170      98.594  16.523-110.536  1.00 42.02           C  
ANISOU 1269  CA  ILE A 170     4132   6569   5265    -50   1237   -732       C  
ATOM   1270  C   ILE A 170      99.203  17.791-109.956  1.00 41.12           C  
ANISOU 1270  C   ILE A 170     3911   6608   5103    -16   1115   -550       C  
ATOM   1271  O   ILE A 170      98.532  18.542-109.239  1.00 40.47           O  
ANISOU 1271  O   ILE A 170     3873   6565   4938    -73   1002   -447       O  
ATOM   1272  CB  ILE A 170      97.795  16.851-111.818  1.00 45.50           C  
ANISOU 1272  CB  ILE A 170     4623   7170   5496   -226   1249   -890       C  
ATOM   1273  CG1 ILE A 170      96.564  17.700-111.503  1.00 43.85           C  
ANISOU 1273  CG1 ILE A 170     4395   7091   5175   -340   1102   -770       C  
ATOM   1274  CG2 ILE A 170      97.383  15.595-112.541  1.00 46.50           C  
ANISOU 1274  CG2 ILE A 170     4896   7147   5625   -323   1365  -1121       C  
ATOM   1275  CD1 ILE A 170      95.768  18.091-112.731  1.00 42.25           C  
ANISOU 1275  CD1 ILE A 170     4185   7099   4768   -511   1061   -840       C  
ATOM   1276  N   LEU A 171     100.471  18.025-110.277  1.00 45.66           N  
ANISOU 1276  N   LEU A 171     4355   7257   5737     68   1160   -514       N  
ATOM   1277  CA  LEU A 171     101.236  19.168-109.776  1.00 43.53           C  
ANISOU 1277  CA  LEU A 171     3978   7122   5441     47   1031   -345       C  
ATOM   1278  C   LEU A 171     101.763  19.974-110.953  1.00 47.29           C  
ANISOU 1278  C   LEU A 171     4362   7780   5826     -3   1107   -385       C  
ATOM   1279  O   LEU A 171     102.698  19.518-111.637  1.00 48.70           O  
ANISOU 1279  O   LEU A 171     4413   7992   6098     89   1261   -416       O  
ATOM   1280  CB  LEU A 171     102.405  18.701-108.907  1.00 47.71           C  
ANISOU 1280  CB  LEU A 171     4361   7607   6160    165    973   -173       C  
ATOM   1281  CG  LEU A 171     102.235  18.201-107.468  1.00 44.56           C  
ANISOU 1281  CG  LEU A 171     4026   7086   5817    198    833    -24       C  
ATOM   1282  CD1 LEU A 171     101.766  19.337-106.598  1.00 49.60           C  
ANISOU 1282  CD1 LEU A 171     4802   7790   6255     42    654     42       C  
ATOM   1283  CD2 LEU A 171     101.298  17.004-107.356  1.00 32.56           C  
ANISOU 1283  CD2 LEU A 171     2652   5354   4367    258    940   -112       C  
ATOM   1284  N   PRO A 172     101.229  21.124-111.238  1.00 47.96           N  
ANISOU 1284  N   PRO A 172     4503   7972   5747   -124   1043   -364       N  
ATOM   1285  CA  PRO A 172     101.810  21.966-112.312  1.00 38.70           C  
ANISOU 1285  CA  PRO A 172     3243   6974   4487   -182   1113   -348       C  
ATOM   1286  C   PRO A 172     103.084  22.679-111.866  1.00 38.98           C  
ANISOU 1286  C   PRO A 172     3118   7071   4621   -211   1045   -183       C  
ATOM   1287  O   PRO A 172     103.146  23.904-111.696  1.00 34.42           O  
ANISOU 1287  O   PRO A 172     2571   6535   3974   -340    949    -84       O  
ATOM   1288  CB  PRO A 172     100.663  22.933-112.630  1.00 44.08           C  
ANISOU 1288  CB  PRO A 172     4047   7711   4991   -285   1054   -328       C  
ATOM   1289  CG  PRO A 172      99.855  23.007-111.364  1.00 53.17           C  
ANISOU 1289  CG  PRO A 172     5313   8715   6174   -277    941   -278       C  
ATOM   1290  CD  PRO A 172      99.956  21.656-110.719  1.00 49.01           C  
ANISOU 1290  CD  PRO A 172     4785   8063   5775   -192    951   -340       C  
ATOM   1291  N   VAL A 173     104.151  21.896-111.671  1.00 40.91           N  
ANISOU 1291  N   VAL A 173     3176   7314   5053    -99   1098   -132       N  
ATOM   1292  CA  VAL A 173     105.428  22.460-111.239  1.00 46.76           C  
ANISOU 1292  CA  VAL A 173     3691   8159   5918   -154   1001     69       C  
ATOM   1293  C   VAL A 173     106.046  23.353-112.306  1.00 43.80           C  
ANISOU 1293  C   VAL A 173     3228   7914   5501   -242   1098    114       C  
ATOM   1294  O   VAL A 173     106.893  24.196-111.985  1.00 44.18           O  
ANISOU 1294  O   VAL A 173     3126   8054   5608   -384    980    284       O  
ATOM   1295  CB  VAL A 173     106.421  21.346-110.851  1.00 36.74           C  
ANISOU 1295  CB  VAL A 173     2180   6874   4907     30   1049    179       C  
ATOM   1296  CG1 VAL A 173     105.988  20.662-109.567  1.00 38.99           C  
ANISOU 1296  CG1 VAL A 173     2571   7004   5239     81    880    226       C  
ATOM   1297  CG2 VAL A 173     106.548  20.333-111.974  1.00 38.21           C  
ANISOU 1297  CG2 VAL A 173     2329   7023   5167    233   1381     31       C  
ATOM   1298  N   GLY A 174     105.642  23.196-113.565  1.00 39.77           N  
ANISOU 1298  N   GLY A 174     2864   7366   4883   -191   1275    -22       N  
ATOM   1299  CA  GLY A 174     106.239  23.947-114.653  1.00 42.36           C  
ANISOU 1299  CA  GLY A 174     3165   7767   5163   -252   1376     37       C  
ATOM   1300  C   GLY A 174     105.454  25.169-115.084  1.00 47.00           C  
ANISOU 1300  C   GLY A 174     3925   8392   5542   -405   1297     60       C  
ATOM   1301  O   GLY A 174     105.632  25.659-116.203  1.00 53.11           O  
ANISOU 1301  O   GLY A 174     4732   9229   6218   -439   1403     88       O  
ATOM   1302  N   ALA A 175     104.593  25.678-114.209  1.00 42.06           N  
ANISOU 1302  N   ALA A 175     3400   7728   4852   -486   1140     70       N  
ATOM   1303  CA  ALA A 175     103.781  26.837-114.540  1.00 40.41           C  
ANISOU 1303  CA  ALA A 175     3339   7524   4489   -590   1103    128       C  
ATOM   1304  C   ALA A 175     104.576  28.130-114.360  1.00 41.30           C  
ANISOU 1304  C   ALA A 175     3373   7675   4644   -772   1068    304       C  
ATOM   1305  O   ALA A 175     105.539  28.200-113.593  1.00 44.63           O  
ANISOU 1305  O   ALA A 175     3635   8126   5198   -874    989    378       O  
ATOM   1306  CB  ALA A 175     102.518  26.870-113.678  1.00 39.25           C  
ANISOU 1306  CB  ALA A 175     3332   7297   4282   -580   1022     84       C  
ATOM   1307  N   GLU A 176     104.158  29.165-115.095  1.00 39.95           N  
ANISOU 1307  N   GLU A 176     3307   7509   4364   -839   1112    398       N  
ATOM   1308  CA  GLU A 176     104.809  30.469-114.987  1.00 40.68           C  
ANISOU 1308  CA  GLU A 176     3366   7593   4498  -1053   1104    577       C  
ATOM   1309  C   GLU A 176     104.452  31.156-113.676  1.00 44.65           C  
ANISOU 1309  C   GLU A 176     4071   7855   5039  -1163    958    574       C  
ATOM   1310  O   GLU A 176     105.282  31.857-113.087  1.00 48.36           O  
ANISOU 1310  O   GLU A 176     4547   8237   5591  -1379    859    645       O  
ATOM   1311  CB  GLU A 176     104.409  31.352-116.171  1.00 53.24           C  
ANISOU 1311  CB  GLU A 176     5056   9198   5976  -1058   1202    703       C  
ATOM   1312  CG  GLU A 176     104.376  30.624-117.505  1.00 59.99           C  
ANISOU 1312  CG  GLU A 176     5897  10174   6724   -912   1292    636       C  
ATOM   1313  CD  GLU A 176     105.740  30.109-117.915  1.00 65.61           C  
ANISOU 1313  CD  GLU A 176     6431  10960   7536   -906   1389    619       C  
ATOM   1314  OE1 GLU A 176     106.742  30.789-117.612  1.00 63.80           O  
ANISOU 1314  OE1 GLU A 176     6067  10728   7445  -1052   1382    756       O  
ATOM   1315  OE2 GLU A 176     105.811  29.022-118.530  1.00 69.57           O  
ANISOU 1315  OE2 GLU A 176     6926  11517   7991   -768   1489    480       O  
ATOM   1316  N   SER A 177     103.219  30.971-113.211  1.00 38.18           N  
ANISOU 1316  N   SER A 177     3451   6901   4156  -1026    941    485       N  
ATOM   1317  CA  SER A 177     102.728  31.601-111.998  1.00 38.64           C  
ANISOU 1317  CA  SER A 177     3782   6680   4218  -1077    863    452       C  
ATOM   1318  C   SER A 177     101.674  30.686-111.394  1.00 40.31           C  
ANISOU 1318  C   SER A 177     4069   6853   4394   -887    855    330       C  
ATOM   1319  O   SER A 177     101.379  29.614-111.932  1.00 41.35           O  
ANISOU 1319  O   SER A 177     4046   7154   4512   -755    886    272       O  
ATOM   1320  CB  SER A 177     102.163  32.995-112.292  1.00 41.25           C  
ANISOU 1320  CB  SER A 177     4330   6811   4534  -1110    961    576       C  
ATOM   1321  OG  SER A 177     101.033  32.912-113.144  1.00 41.65           O  
ANISOU 1321  OG  SER A 177     4355   6942   4529   -906   1070    651       O  
ATOM   1322  N   PHE A 178     101.100  31.113-110.266  1.00 38.95           N  
ANISOU 1322  N   PHE A 178     2333   8629   3839    -19    480    733       N  
ATOM   1323  CA  PHE A 178     100.004  30.340-109.692  1.00 40.25           C  
ANISOU 1323  CA  PHE A 178     2593   8770   3930     31    423    666       C  
ATOM   1324  C   PHE A 178      98.752  30.437-110.554  1.00 40.66           C  
ANISOU 1324  C   PHE A 178     2710   8779   3959     98    448    711       C  
ATOM   1325  O   PHE A 178      98.047  29.438-110.743  1.00 41.80           O  
ANISOU 1325  O   PHE A 178     2920   8945   4017    170    403    672       O  
ATOM   1326  CB  PHE A 178      99.695  30.786-108.265  1.00 37.55           C  
ANISOU 1326  CB  PHE A 178     2240   8404   3623    -72    412    587       C  
ATOM   1327  CG  PHE A 178      98.677  29.915-107.592  1.00 49.89           C  
ANISOU 1327  CG  PHE A 178     3888   9961   5107    -29    366    525       C  
ATOM   1328  CD1 PHE A 178      99.068  28.772-106.918  1.00 36.28           C  
ANISOU 1328  CD1 PHE A 178     2168   8326   3291      0    293    497       C  
ATOM   1329  CD2 PHE A 178      97.325  30.202-107.686  1.00 45.03           C  
ANISOU 1329  CD2 PHE A 178     3332   9254   4525     -8    408    516       C  
ATOM   1330  CE1 PHE A 178      98.135  27.949-106.327  1.00 39.81           C  
ANISOU 1330  CE1 PHE A 178     2680   8768   3676     34    270    458       C  
ATOM   1331  CE2 PHE A 178      96.389  29.382-107.102  1.00 35.03           C  
ANISOU 1331  CE2 PHE A 178     2129   7979   3200     22    379    460       C  
ATOM   1332  CZ  PHE A 178      96.795  28.256-106.416  1.00 41.70           C  
ANISOU 1332  CZ  PHE A 178     2983   8912   3949     36    315    430       C  
ATOM   1333  N   ARG A 179      98.447  31.633-111.071  1.00 38.35           N  
ANISOU 1333  N   ARG A 179     2379   8438   3753     71    525    803       N  
ATOM   1334  CA  ARG A 179      97.294  31.776-111.956  1.00 37.76           C  
ANISOU 1334  CA  ARG A 179     2330   8370   3646    145    536    887       C  
ATOM   1335  C   ARG A 179      97.462  30.933-113.207  1.00 47.22           C  
ANISOU 1335  C   ARG A 179     3542   9714   4687    227    498    923       C  
ATOM   1336  O   ARG A 179      96.481  30.402-113.739  1.00 46.59           O  
ANISOU 1336  O   ARG A 179     3491   9702   4509    286    456    924       O  
ATOM   1337  CB  ARG A 179      97.081  33.248-112.314  1.00 45.00           C  
ANISOU 1337  CB  ARG A 179     3174   9222   4703    116    642   1027       C  
ATOM   1338  CG  ARG A 179      96.400  34.047-111.210  1.00 57.30           C  
ANISOU 1338  CG  ARG A 179     4714  10632   6425     55    710    974       C  
ATOM   1339  CD  ARG A 179      96.459  35.544-111.451  1.00 66.80           C  
ANISOU 1339  CD  ARG A 179     5820  11738   7822      9    858   1107       C  
ATOM   1340  NE  ARG A 179      97.815  36.061-111.292  1.00 76.44           N  
ANISOU 1340  NE  ARG A 179     6978  12952   9113   -110    915   1094       N  
ATOM   1341  CZ  ARG A 179      98.151  37.338-111.444  1.00 81.38           C  
ANISOU 1341  CZ  ARG A 179     7509  13482   9930   -193   1066   1198       C  
ATOM   1342  NH1 ARG A 179      97.227  38.236-111.761  1.00 82.20           N  
ANISOU 1342  NH1 ARG A 179     7573  13478  10183   -145   1182   1349       N  
ATOM   1343  NH2 ARG A 179      99.412  37.717-111.282  1.00 82.37           N  
ANISOU 1343  NH2 ARG A 179     7565  13611  10119   -325   1110   1168       N  
ATOM   1344  N   ASP A 180      98.702  30.783-113.675  1.00 41.83           N  
ANISOU 1344  N   ASP A 180     2819   9097   3978    221    521    938       N  
ATOM   1345  CA  ASP A 180      98.977  29.858-114.760  1.00 41.15           C  
ANISOU 1345  CA  ASP A 180     2734   9157   3743    292    509    927       C  
ATOM   1346  C   ASP A 180      98.873  28.408-114.305  1.00 38.40           C  
ANISOU 1346  C   ASP A 180     2438   8813   3340    334    450    776       C  
ATOM   1347  O   ASP A 180      98.459  27.544-115.087  1.00 41.39           O  
ANISOU 1347  O   ASP A 180     2829   9297   3600    389    435    725       O  
ATOM   1348  CB  ASP A 180     100.361  30.136-115.335  1.00 46.36           C  
ANISOU 1348  CB  ASP A 180     3320   9873   4422    275    580    980       C  
ATOM   1349  CG  ASP A 180     100.595  29.412-116.628  1.00 46.18           C  
ANISOU 1349  CG  ASP A 180     3282  10018   4246    343    605    977       C  
ATOM   1350  OD1 ASP A 180      99.834  29.669-117.581  1.00 50.15           O  
ANISOU 1350  OD1 ASP A 180     3781  10644   4630    370    604   1063       O  
ATOM   1351  OD2 ASP A 180     101.528  28.586-116.691  1.00 54.09           O  
ANISOU 1351  OD2 ASP A 180     4260  11047   5245    371    632    890       O  
ATOM   1352  N   ALA A 181      99.244  28.117-113.055  1.00 39.47           N  
ANISOU 1352  N   ALA A 181     2586   8854   3555    304    423    707       N  
ATOM   1353  CA  ALA A 181      99.098  26.757-112.547  1.00 36.90           C  
ANISOU 1353  CA  ALA A 181     2297   8524   3198    352    383    601       C  
ATOM   1354  C   ALA A 181      97.636  26.348-112.472  1.00 36.05           C  
ANISOU 1354  C   ALA A 181     2255   8396   3047    362    349    553       C  
ATOM   1355  O   ALA A 181      97.319  25.159-112.579  1.00 37.68           O  
ANISOU 1355  O   ALA A 181     2477   8627   3211    407    340    467       O  
ATOM   1356  CB  ALA A 181      99.753  26.628-111.173  1.00 36.68           C  
ANISOU 1356  CB  ALA A 181     2249   8448   3242    317    354    581       C  
ATOM   1357  N   MET A 182      96.737  27.314-112.281  1.00 41.34           N  
ANISOU 1357  N   MET A 182     2941   9016   3750    321    345    604       N  
ATOM   1358  CA  MET A 182      95.308  27.016-112.288  1.00 42.39           C  
ANISOU 1358  CA  MET A 182     3108   9141   3857    330    319    570       C  
ATOM   1359  C   MET A 182      94.849  26.611-113.680  1.00 44.67           C  
ANISOU 1359  C   MET A 182     3367   9588   4016    373    307    576       C  
ATOM   1360  O   MET A 182      94.123  25.625-113.844  1.00 46.80           O  
ANISOU 1360  O   MET A 182     3644   9910   4228    384    282    479       O  
ATOM   1361  CB  MET A 182      94.519  28.228-111.800  1.00 35.07           C  
ANISOU 1361  CB  MET A 182     2176   8123   3028    292    342    635       C  
ATOM   1362  CG  MET A 182      94.885  28.692-110.408  1.00 38.38           C  
ANISOU 1362  CG  MET A 182     2603   8429   3549    228    365    596       C  
ATOM   1363  SD  MET A 182      94.124  27.667-109.142  1.00 49.74           S  
ANISOU 1363  SD  MET A 182     4097   9823   4978    211    338    483       S  
ATOM   1364  CE  MET A 182      95.365  26.425-108.869  1.00 40.24           C  
ANISOU 1364  CE  MET A 182     2893   8693   3703    237    298    447       C  
ATOM   1365  N   ARG A 183      95.266  27.373-114.695  1.00 44.82           N  
ANISOU 1365  N   ARG A 183     3335   9714   3981    387    330    687       N  
ATOM   1366  CA  ARG A 183      94.889  27.062-116.068  1.00 40.97           C  
ANISOU 1366  CA  ARG A 183     2795   9450   3322    420    313    704       C  
ATOM   1367  C   ARG A 183      95.377  25.678-116.477  1.00 38.67           C  
ANISOU 1367  C   ARG A 183     2502   9241   2949    442    323    540       C  
ATOM   1368  O   ARG A 183      94.659  24.933-117.154  1.00 51.10           O  
ANISOU 1368  O   ARG A 183     4044  10972   4400    443    299    446       O  
ATOM   1369  CB  ARG A 183      95.442  28.129-117.008  1.00 39.62           C  
ANISOU 1369  CB  ARG A 183     2559   9389   3105    431    353    880       C  
ATOM   1370  CG  ARG A 183      95.265  27.788-118.468  1.00 46.94           C  
ANISOU 1370  CG  ARG A 183     3413  10604   3816    459    338    901       C  
ATOM   1371  CD  ARG A 183      96.099  28.671-119.367  1.00 51.51           C  
ANISOU 1371  CD  ARG A 183     3933  11287   4351    469    402   1072       C  
ATOM   1372  NE  ARG A 183      96.062  28.188-120.743  1.00 61.24           N  
ANISOU 1372  NE  ARG A 183     5100  12811   5357    485    399   1055       N  
ATOM   1373  CZ  ARG A 183      96.564  28.852-121.778  1.00 61.69           C  
ANISOU 1373  CZ  ARG A 183     5099  13023   5318    492    456   1215       C  
ATOM   1374  NH1 ARG A 183      97.137  30.032-121.588  1.00 59.11           N  
ANISOU 1374  NH1 ARG A 183     4763  12576   5119    486    525   1414       N  
ATOM   1375  NH2 ARG A 183      96.486  28.340-123.000  1.00 61.33           N  
ANISOU 1375  NH2 ARG A 183     5008  13245   5051    489    461   1167       N  
ATOM   1376  N   LEU A 184      96.590  25.309-116.066  1.00 43.31           N  
ANISOU 1376  N   LEU A 184     3106   9734   3616    457    370    497       N  
ATOM   1377  CA  LEU A 184      97.112  23.987-116.400  1.00 50.57           C  
ANISOU 1377  CA  LEU A 184     4013  10696   4508    498    417    346       C  
ATOM   1378  C   LEU A 184      96.300  22.893-115.722  1.00 45.80           C  
ANISOU 1378  C   LEU A 184     3438  10019   3943    497    398    214       C  
ATOM   1379  O   LEU A 184      95.844  21.945-116.375  1.00 39.51           O  
ANISOU 1379  O   LEU A 184     2619   9324   3069    502    425     71       O  
ATOM   1380  CB  LEU A 184      98.587  23.887-116.006  1.00 39.50           C  
ANISOU 1380  CB  LEU A 184     2591   9206   3211    531    478    363       C  
ATOM   1381  CG  LEU A 184      99.616  24.208-117.089  1.00 43.80           C  
ANISOU 1381  CG  LEU A 184     3078   9864   3701    550    558    403       C  
ATOM   1382  CD1 LEU A 184      99.487  25.647-117.577  1.00 41.39           C  
ANISOU 1382  CD1 LEU A 184     2754   9623   3348    503    543    572       C  
ATOM   1383  CD2 LEU A 184     101.021  23.930-116.577  1.00 42.91           C  
ANISOU 1383  CD2 LEU A 184     2919   9665   3722    586    620    404       C  
ATOM   1384  N   GLY A 185      96.109  23.011-114.406  1.00 39.83           N  
ANISOU 1384  N   GLY A 185     2728   9101   3307    479    367    249       N  
ATOM   1385  CA  GLY A 185      95.334  22.013-113.685  1.00 36.79           C  
ANISOU 1385  CA  GLY A 185     2362   8644   2974    474    364    151       C  
ATOM   1386  C   GLY A 185      93.899  21.916-114.168  1.00 44.99           C  
ANISOU 1386  C   GLY A 185     3388   9771   3936    426    330     91       C  
ATOM   1387  O   GLY A 185      93.334  20.823-114.247  1.00 45.25           O  
ANISOU 1387  O   GLY A 185     3399   9827   3969    415    359    -47       O  
ATOM   1388  N   ALA A 186      93.289  23.055-114.510  1.00 41.33           N  
ANISOU 1388  N   ALA A 186     2918   9367   3418    397    281    198       N  
ATOM   1389  CA  ALA A 186      91.890  23.034-114.925  1.00 44.81           C  
ANISOU 1389  CA  ALA A 186     3315   9919   3790    358    239    170       C  
ATOM   1390  C   ALA A 186      91.732  22.406-116.304  1.00 46.55           C  
ANISOU 1390  C   ALA A 186     3451  10406   3828    349    234     61       C  
ATOM   1391  O   ALA A 186      90.800  21.625-116.533  1.00 45.49           O  
ANISOU 1391  O   ALA A 186     3263  10376   3646    297    222    -77       O  
ATOM   1392  CB  ALA A 186      91.308  24.448-114.909  1.00 37.03           C  
ANISOU 1392  CB  ALA A 186     2324   8925   2822    354    208    342       C  
ATOM   1393  N   GLU A 187      92.635  22.733-117.233  1.00 43.14           N  
ANISOU 1393  N   GLU A 187     2996  10105   3292    382    253    105       N  
ATOM   1394  CA  GLU A 187      92.552  22.177-118.580  1.00 42.41           C  
ANISOU 1394  CA  GLU A 187     2824  10294   2998    362    263    -15       C  
ATOM   1395  C   GLU A 187      92.833  20.680-118.581  1.00 43.93           C  
ANISOU 1395  C   GLU A 187     3038  10435   3219    352    356   -273       C  
ATOM   1396  O   GLU A 187      92.210  19.929-119.341  1.00 44.32           O  
ANISOU 1396  O   GLU A 187     3040  10674   3127    287    369   -464       O  
ATOM   1397  CB  GLU A 187      93.523  22.902-119.513  1.00 43.14           C  
ANISOU 1397  CB  GLU A 187     2895  10505   2993    399    289    104       C  
ATOM   1398  CG  GLU A 187      93.110  24.315-119.896  1.00 43.30           C  
ANISOU 1398  CG  GLU A 187     2855  10653   2944    407    221    358       C  
ATOM   1399  CD  GLU A 187      94.185  25.043-120.684  1.00 61.75           C  
ANISOU 1399  CD  GLU A 187     5175  13060   5230    439    276    495       C  
ATOM   1400  OE1 GLU A 187      94.026  26.258-120.919  1.00 57.48           O  
ANISOU 1400  OE1 GLU A 187     4587  12579   4676    456    252    734       O  
ATOM   1401  OE2 GLU A 187      95.191  24.406-121.067  1.00 58.73           O  
ANISOU 1401  OE2 GLU A 187     4824  12659   4831    448    365    372       O  
ATOM   1402  N   VAL A 188      93.772  20.230-117.747  1.00 41.78           N  
ANISOU 1402  N   VAL A 188     2832   9919   3123    411    432   -285       N  
ATOM   1403  CA  VAL A 188      94.049  18.801-117.645  1.00 42.70           C  
ANISOU 1403  CA  VAL A 188     2964   9950   3309    430    552   -501       C  
ATOM   1404  C   VAL A 188      92.896  18.076-116.959  1.00 49.79           C  
ANISOU 1404  C   VAL A 188     3849  10788   4282    369    545   -610       C  
ATOM   1405  O   VAL A 188      92.565  16.938-117.316  1.00 53.58           O  
ANISOU 1405  O   VAL A 188     4314  11300   4744    330    639   -850       O  
ATOM   1406  CB  VAL A 188      95.389  18.570-116.917  1.00 42.21           C  
ANISOU 1406  CB  VAL A 188     2933   9680   3424    533    631   -434       C  
ATOM   1407  CG1 VAL A 188      95.614  17.089-116.650  1.00 43.34           C  
ANISOU 1407  CG1 VAL A 188     3073   9703   3689    586    775   -620       C  
ATOM   1408  CG2 VAL A 188      96.524  19.121-117.750  1.00 43.12           C  
ANISOU 1408  CG2 VAL A 188     3037   9876   3471    575    672   -370       C  
ATOM   1409  N   TYR A 189      92.254  18.725-115.985  1.00 40.63           N  
ANISOU 1409  N   TYR A 189     2699   9528   3211    347    455   -457       N  
ATOM   1410  CA  TYR A 189      91.084  18.132-115.346  1.00 40.47           C  
ANISOU 1410  CA  TYR A 189     2652   9455   3272    274    453   -540       C  
ATOM   1411  C   TYR A 189      89.919  18.016-116.323  1.00 43.66           C  
ANISOU 1411  C   TYR A 189     2955  10119   3514    166    406   -678       C  
ATOM   1412  O   TYR A 189      89.211  17.001-116.339  1.00 44.17           O  
ANISOU 1412  O   TYR A 189     2964  10212   3608     79    464   -886       O  
ATOM   1413  CB  TYR A 189      90.687  18.962-114.123  1.00 38.62           C  
ANISOU 1413  CB  TYR A 189     2465   9053   3154    272    384   -348       C  
ATOM   1414  CG  TYR A 189      89.404  18.522-113.453  1.00 41.93           C  
ANISOU 1414  CG  TYR A 189     2850   9416   3664    189    384   -401       C  
ATOM   1415  CD1 TYR A 189      89.401  17.487-112.527  1.00 43.66           C  
ANISOU 1415  CD1 TYR A 189     3076   9485   4027    183    478   -461       C  
ATOM   1416  CD2 TYR A 189      88.198  19.153-113.733  1.00 45.10           C  
ANISOU 1416  CD2 TYR A 189     3197   9917   4023    121    302   -371       C  
ATOM   1417  CE1 TYR A 189      88.240  17.085-111.910  1.00 42.15           C  
ANISOU 1417  CE1 TYR A 189     2844   9242   3929     90    497   -501       C  
ATOM   1418  CE2 TYR A 189      87.027  18.757-113.120  1.00 42.60           C  
ANISOU 1418  CE2 TYR A 189     2835   9537   3814     38    309   -418       C  
ATOM   1419  CZ  TYR A 189      87.055  17.722-112.210  1.00 41.48           C  
ANISOU 1419  CZ  TYR A 189     2705   9245   3811     12    409   -489       C  
ATOM   1420  OH  TYR A 189      85.895  17.322-111.595  1.00 50.18           O  
ANISOU 1420  OH  TYR A 189     3752  10285   5028    -88    435   -528       O  
ATOM   1421  N   HIS A 190      89.695  19.048-117.139  1.00 44.45           N  
ANISOU 1421  N   HIS A 190     3010  10434   3444    160    306   -563       N  
ATOM   1422  CA  HIS A 190      88.643  18.968-118.149  1.00 49.65           C  
ANISOU 1422  CA  HIS A 190     3533  11426   3905     58    242   -672       C  
ATOM   1423  C   HIS A 190      88.987  17.960-119.237  1.00 47.58           C  
ANISOU 1423  C   HIS A 190     3275  11354   3451      0    332   -958       C  
ATOM   1424  O   HIS A 190      88.090  17.294-119.767  1.00 49.00           O  
ANISOU 1424  O   HIS A 190     3441  11625   3552   -138    268  -1162       O  
ATOM   1425  CB  HIS A 190      88.392  20.348-118.755  1.00 49.60           C  
ANISOU 1425  CB  HIS A 190     3475  11619   3751     91    126   -429       C  
ATOM   1426  CG  HIS A 190      87.875  21.350-117.771  1.00 55.02           C  
ANISOU 1426  CG  HIS A 190     4226  12062   4618    134     82   -197       C  
ATOM   1427  ND1 HIS A 190      88.284  22.666-117.761  1.00 57.73           N  
ANISOU 1427  ND1 HIS A 190     4619  12350   4965    214     71     52       N  
ATOM   1428  CD2 HIS A 190      86.984  21.225-116.758  1.00 57.26           C  
ANISOU 1428  CD2 HIS A 190     4531  12128   5097     99     75   -198       C  
ATOM   1429  CE1 HIS A 190      87.669  23.309-116.785  1.00 54.79           C  
ANISOU 1429  CE1 HIS A 190     4296  11735   4787    227     69    168       C  
ATOM   1430  NE2 HIS A 190      86.874  22.458-116.162  1.00 60.47           N  
ANISOU 1430  NE2 HIS A 190     5002  12359   5615    163     68     26       N  
ATOM   1431  N   THR A 191      90.272  17.827-119.579  1.00 46.71           N  
ANISOU 1431  N   THR A 191     3268  11149   3332     83    416   -970       N  
ATOM   1432  CA  THR A 191      90.675  16.810-120.545  1.00 50.91           C  
ANISOU 1432  CA  THR A 191     3859  11757   3729     35    524  -1264       C  
ATOM   1433  C   THR A 191      90.463  15.410-119.986  1.00 52.66           C  
ANISOU 1433  C   THR A 191     4132  11755   4122    -10    654  -1539       C  
ATOM   1434  O   THR A 191      89.976  14.518-120.692  1.00 54.68           O  
ANISOU 1434  O   THR A 191     4431  12055   4290   -143    673  -1839       O  
ATOM   1435  CB  THR A 191      92.138  17.008-120.945  1.00 53.43           C  
ANISOU 1435  CB  THR A 191     4250  11986   4063    150    611  -1191       C  
ATOM   1436  OG1 THR A 191      92.289  18.274-121.599  1.00 55.97           O  
ANISOU 1436  OG1 THR A 191     4526  12502   4240    168    503   -950       O  
ATOM   1437  CG2 THR A 191      92.591  15.902-121.885  1.00 54.53           C  
ANISOU 1437  CG2 THR A 191     4464  12151   4102    111    760  -1513       C  
ATOM   1438  N   LEU A 192      90.819  15.200-118.716  1.00 52.88           N  
ANISOU 1438  N   LEU A 192     4186  11471   4436     83    711  -1420       N  
ATOM   1439  CA  LEU A 192      90.614  13.895-118.097  1.00 54.41           C  
ANISOU 1439  CA  LEU A 192     4459  11342   4871     48    804  -1599       C  
ATOM   1440  C   LEU A 192      89.141  13.501-118.088  1.00 55.81           C  
ANISOU 1440  C   LEU A 192     4620  11520   5068   -142    706  -1733       C  
ATOM   1441  O   LEU A 192      88.817  12.316-118.230  1.00 51.62           O  
ANISOU 1441  O   LEU A 192     4155  10817   4640   -246    789  -2000       O  
ATOM   1442  CB  LEU A 192      91.178  13.900-116.677  1.00 50.07           C  
ANISOU 1442  CB  LEU A 192     3927  10516   4583    179    847  -1376       C  
ATOM   1443  CG  LEU A 192      91.054  12.599-115.883  1.00 51.62           C  
ANISOU 1443  CG  LEU A 192     4210  10351   5055    172    953  -1474       C  
ATOM   1444  CD1 LEU A 192      91.825  11.477-116.564  1.00 54.51           C  
ANISOU 1444  CD1 LEU A 192     4646  10580   5486    220   1134  -1724       C  
ATOM   1445  CD2 LEU A 192      91.532  12.797-114.454  1.00 45.66           C  
ANISOU 1445  CD2 LEU A 192     3459   9405   4485    292    952  -1195       C  
ATOM   1446  N   LYS A 193      88.238  14.476-117.936  1.00 54.37           N  
ANISOU 1446  N   LYS A 193     4333  11515   4809   -193    541  -1556       N  
ATOM   1447  CA  LYS A 193      86.810  14.172-117.935  1.00 53.15           C  
ANISOU 1447  CA  LYS A 193     4116  11392   4685   -373    439  -1664       C  
ATOM   1448  C   LYS A 193      86.378  13.555-119.260  1.00 56.03           C  
ANISOU 1448  C   LYS A 193     4477  11972   4838   -540    402  -1981       C  
ATOM   1449  O   LYS A 193      85.626  12.574-119.281  1.00 62.00           O  
ANISOU 1449  O   LYS A 193     5247  12615   5695   -710    417  -2228       O  
ATOM   1450  CB  LYS A 193      86.004  15.440-117.640  1.00 50.62           C  
ANISOU 1450  CB  LYS A 193     3658  11250   4327   -363    281  -1398       C  
ATOM   1451  CG  LYS A 193      84.501  15.296-117.830  1.00 50.83           C  
ANISOU 1451  CG  LYS A 193     3559  11394   4358   -540    152  -1486       C  
ATOM   1452  CD  LYS A 193      83.743  16.468-117.217  1.00 52.94           C  
ANISOU 1452  CD  LYS A 193     3687  11733   4696   -490     50  -1201       C  
ATOM   1453  CE  LYS A 193      82.256  16.387-117.547  1.00 65.25           C  
ANISOU 1453  CE  LYS A 193     5073  13464   6256   -654    -93  -1271       C  
ATOM   1454  NZ  LYS A 193      81.427  17.324-116.737  1.00 63.60           N  
ANISOU 1454  NZ  LYS A 193     4829  13131   6206   -583   -124  -1006       N  
ATOM   1455  N   GLY A 194      86.851  14.111-120.376  1.00 54.48           N  
ANISOU 1455  N   GLY A 194     4265  12096   4339   -512    361  -1986       N  
ATOM   1456  CA  GLY A 194      86.553  13.519-121.667  1.00 57.03           C  
ANISOU 1456  CA  GLY A 194     4603  12664   4404   -679    334  -2308       C  
ATOM   1457  C   GLY A 194      87.204  12.166-121.863  1.00 59.01           C  
ANISOU 1457  C   GLY A 194     5005  12662   4754   -714    550  -2663       C  
ATOM   1458  O   GLY A 194      86.639  11.292-122.529  1.00 62.09           O  
ANISOU 1458  O   GLY A 194     5425  13100   5068   -916    554  -3017       O  
ATOM   1459  N   VAL A 195      88.397  11.972-121.297  1.00 60.56           N  
ANISOU 1459  N   VAL A 195     5288  12587   5135   -523    734  -2580       N  
ATOM   1460  CA  VAL A 195      89.071  10.681-121.412  1.00 62.20           C  
ANISOU 1460  CA  VAL A 195     5627  12505   5503   -514    967  -2885       C  
ATOM   1461  C   VAL A 195      88.280   9.605-120.681  1.00 63.62           C  
ANISOU 1461  C   VAL A 195     5849  12327   5995   -641   1012  -3040       C  
ATOM   1462  O   VAL A 195      88.080   8.498-121.196  1.00 63.69           O  
ANISOU 1462  O   VAL A 195     5940  12207   6054   -787   1128  -3418       O  
ATOM   1463  CB  VAL A 195      90.514  10.786-120.885  1.00 64.03           C  
ANISOU 1463  CB  VAL A 195     5897  12540   5893   -257   1133  -2699       C  
ATOM   1464  CG1 VAL A 195      91.148   9.407-120.783  1.00 60.35           C  
ANISOU 1464  CG1 VAL A 195     5544  11694   5691   -209   1384  -2960       C  
ATOM   1465  CG2 VAL A 195      91.338  11.693-121.787  1.00 66.78           C  
ANISOU 1465  CG2 VAL A 195     6206  13234   5932   -167   1135  -2609       C  
ATOM   1466  N   ILE A 196      87.808   9.918-119.475  1.00 61.47           N  
ANISOU 1466  N   ILE A 196     5527  11888   5940   -601    936  -2762       N  
ATOM   1467  CA  ILE A 196      87.010   8.962-118.714  1.00 65.15           C  
ANISOU 1467  CA  ILE A 196     6027  12022   6706   -728    987  -2860       C  
ATOM   1468  C   ILE A 196      85.652   8.754-119.372  1.00 69.47           C  
ANISOU 1468  C   ILE A 196     6496  12769   7131  -1013    852  -3106       C  
ATOM   1469  O   ILE A 196      85.118   7.638-119.388  1.00 70.00           O  
ANISOU 1469  O   ILE A 196     6614  12606   7375  -1193    942  -3390       O  
ATOM   1470  CB  ILE A 196      86.876   9.435-117.256  1.00 58.01           C  
ANISOU 1470  CB  ILE A 196     5090  10938   6014   -616    951  -2486       C  
ATOM   1471  CG1 ILE A 196      88.247   9.421-116.583  1.00 54.26           C  
ANISOU 1471  CG1 ILE A 196     4688  10252   5676   -362   1081  -2281       C  
ATOM   1472  CG2 ILE A 196      85.894   8.563-116.496  1.00 58.19           C  
ANISOU 1472  CG2 ILE A 196     5130  10669   6311   -773    997  -2553       C  
ATOM   1473  CD1 ILE A 196      88.276  10.076-115.234  1.00 51.35           C  
ANISOU 1473  CD1 ILE A 196     4289   9797   5425   -250   1025  -1912       C  
ATOM   1474  N   LYS A 197      85.080   9.819-119.940  1.00 70.98           N  
ANISOU 1474  N   LYS A 197     6549  13389   7030  -1061    633  -2994       N  
ATOM   1475  CA  LYS A 197      83.767   9.712-120.569  1.00 73.49           C  
ANISOU 1475  CA  LYS A 197     6748  13958   7218  -1324    462  -3188       C  
ATOM   1476  C   LYS A 197      83.802   8.784-121.778  1.00 76.66           C  
ANISOU 1476  C   LYS A 197     7226  14457   7445  -1520    520  -3655       C  
ATOM   1477  O   LYS A 197      82.906   7.949-121.955  1.00 78.58           O  
ANISOU 1477  O   LYS A 197     7445  14639   7772  -1777    504  -3952       O  
ATOM   1478  CB  LYS A 197      83.267  11.101-120.971  1.00 74.85           C  
ANISOU 1478  CB  LYS A 197     6745  14580   7115  -1290    216  -2921       C  
ATOM   1479  CG  LYS A 197      81.932  11.103-121.700  1.00 85.18           C  
ANISOU 1479  CG  LYS A 197     7883  16224   8257  -1543     -1  -3075       C  
ATOM   1480  CD  LYS A 197      81.689  12.432-122.407  1.00 88.29           C  
ANISOU 1480  CD  LYS A 197     8123  17102   8323  -1475   -231  -2814       C  
ATOM   1481  CE  LYS A 197      80.446  12.375-123.285  1.00 92.18           C  
ANISOU 1481  CE  LYS A 197     8449  17945   8630  -1708   -449  -2947       C  
ATOM   1482  NZ  LYS A 197      80.284  13.591-124.131  1.00 92.27           N  
ANISOU 1482  NZ  LYS A 197     8403  18246   8410  -1569   -572  -2589       N  
ATOM   1483  N   ASP A 198      84.830   8.910-122.621  1.00 80.64           N  
ANISOU 1483  N   ASP A 198     7820  15115   7704  -1418    602  -3745       N  
ATOM   1484  CA  ASP A 198      84.898   8.084-123.825  1.00 84.88           C  
ANISOU 1484  CA  ASP A 198     8443  15781   8027  -1609    675  -4219       C  
ATOM   1485  C   ASP A 198      85.285   6.648-123.497  1.00 82.54           C  
ANISOU 1485  C   ASP A 198     8310  14969   8080  -1650    960  -4546       C  
ATOM   1486  O   ASP A 198      84.813   5.707-124.147  1.00 85.20           O  
ANISOU 1486  O   ASP A 198     8700  15281   8392  -1906   1014  -4995       O  
ATOM   1487  CB  ASP A 198      85.888   8.688-124.826  1.00 84.11           C  
ANISOU 1487  CB  ASP A 198     8391  16017   7548  -1485    707  -4206       C  
ATOM   1488  CG  ASP A 198      85.449  10.050-125.342  1.00 86.14           C  
ANISOU 1488  CG  ASP A 198     8494  16800   7437  -1472    430  -3902       C  
ATOM   1489  OD1 ASP A 198      84.244  10.366-125.248  1.00 88.08           O  
ANISOU 1489  OD1 ASP A 198     8585  17224   7657  -1615    197  -3821       O  
ATOM   1490  OD2 ASP A 198      86.308  10.804-125.849  1.00 88.46           O  
ANISOU 1490  OD2 ASP A 198     8804  17236   7571  -1300    450  -3666       O  
ATOM   1491  N   LYS A 199      86.137   6.457-122.490  1.00 79.09           N  
ANISOU 1491  N   LYS A 199     7952  14118   7982  -1405   1144  -4325       N  
ATOM   1492  CA  LYS A 199      86.663   5.123-122.218  1.00 83.92           C  
ANISOU 1492  CA  LYS A 199     8719  14222   8944  -1389   1437  -4583       C  
ATOM   1493  C   LYS A 199      85.737   4.317-121.317  1.00 85.89           C  
ANISOU 1493  C   LYS A 199     8970  14088   9575  -1544   1465  -4615       C  
ATOM   1494  O   LYS A 199      85.599   3.103-121.496  1.00 87.96           O  
ANISOU 1494  O   LYS A 199     9338  14024  10059  -1697   1653  -4982       O  
ATOM   1495  CB  LYS A 199      88.058   5.233-121.601  1.00 84.77           C  
ANISOU 1495  CB  LYS A 199     8890  14081   9239  -1046   1616  -4314       C  
ATOM   1496  CG  LYS A 199      88.684   3.902-121.205  1.00 88.21           C  
ANISOU 1496  CG  LYS A 199     9465  13959  10093   -966   1924  -4493       C  
ATOM   1497  CD  LYS A 199      88.821   2.970-122.398  1.00 96.63           C  
ANISOU 1497  CD  LYS A 199    10641  14994  11079  -1126   2118  -5050       C  
ATOM   1498  CE  LYS A 199      89.215   1.567-121.964  1.00100.89           C  
ANISOU 1498  CE  LYS A 199    11315  14910  12108  -1077   2436  -5246       C  
ATOM   1499  NZ  LYS A 199      88.206   0.976-121.043  1.00102.39           N  
ANISOU 1499  NZ  LYS A 199    11508  14762  12633  -1234   2405  -5184       N  
ATOM   1500  N   TYR A 200      85.078   4.970-120.358  1.00 84.18           N  
ANISOU 1500  N   TYR A 200     8640  13898   9448  -1518   1301  -4247       N  
ATOM   1501  CA  TYR A 200      84.276   4.263-119.371  1.00 88.41           C  
ANISOU 1501  CA  TYR A 200     9175  14061  10355  -1640   1357  -4212       C  
ATOM   1502  C   TYR A 200      82.794   4.608-119.394  1.00 85.12           C  
ANISOU 1502  C   TYR A 200     8586  13899   9857  -1902   1132  -4228       C  
ATOM   1503  O   TYR A 200      82.023   3.955-118.684  1.00 87.56           O  
ANISOU 1503  O   TYR A 200     8881  13918  10468  -2052   1192  -4247       O  
ATOM   1504  CB  TYR A 200      84.827   4.519-117.960  1.00 86.62           C  
ANISOU 1504  CB  TYR A 200     8978  13547  10387  -1374   1425  -3755       C  
ATOM   1505  CG  TYR A 200      86.278   4.135-117.834  1.00 91.22           C  
ANISOU 1505  CG  TYR A 200     9692  13869  11100  -1104   1634  -3701       C  
ATOM   1506  CD1 TYR A 200      87.275   5.093-117.926  1.00 90.86           C  
ANISOU 1506  CD1 TYR A 200     9616  14058  10848   -858   1578  -3462       C  
ATOM   1507  CD2 TYR A 200      86.652   2.810-117.652  1.00 96.23           C  
ANISOU 1507  CD2 TYR A 200    10464  14015  12085  -1098   1897  -3888       C  
ATOM   1508  CE1 TYR A 200      88.602   4.751-117.822  1.00 91.91           C  
ANISOU 1508  CE1 TYR A 200     9829  13978  11113   -612   1763  -3407       C  
ATOM   1509  CE2 TYR A 200      87.982   2.455-117.550  1.00 98.27           C  
ANISOU 1509  CE2 TYR A 200    10810  14038  12491   -828   2091  -3821       C  
ATOM   1510  CZ  TYR A 200      88.953   3.434-117.636  1.00 96.27           C  
ANISOU 1510  CZ  TYR A 200    10501  14059  12018   -587   2015  -3581       C  
ATOM   1511  OH  TYR A 200      90.286   3.111-117.537  1.00 99.03           O  
ANISOU 1511  OH  TYR A 200    10899  14204  12524   -316   2199  -3503       O  
ATOM   1512  N   GLY A 201      82.372   5.591-120.174  1.00 86.21           N  
ANISOU 1512  N   GLY A 201     8580  14560   9615  -1957    886  -4202       N  
ATOM   1513  CA  GLY A 201      80.964   5.907-120.291  1.00 87.84           C  
ANISOU 1513  CA  GLY A 201     8585  15040   9750  -2196    662  -4220       C  
ATOM   1514  C   GLY A 201      80.634   7.279-119.721  1.00 88.09           C  
ANISOU 1514  C   GLY A 201     8452  15326   9694  -2034    471  -3760       C  
ATOM   1515  O   GLY A 201      81.406   7.885-118.973  1.00 86.30           O  
ANISOU 1515  O   GLY A 201     8282  14980   9528  -1763    531  -3424       O  
ATOM   1516  N   LYS A 202      79.444   7.767-120.085  1.00 93.88           N  
ANISOU 1516  N   LYS A 202     8964  16412  10294  -2211    237  -3759       N  
ATOM   1517  CA  LYS A 202      79.008   9.089-119.650  1.00 95.46           C  
ANISOU 1517  CA  LYS A 202     8983  16858  10428  -2065     62  -3349       C  
ATOM   1518  C   LYS A 202      78.638   9.135-118.172  1.00 86.57           C  
ANISOU 1518  C   LYS A 202     7834  15399   9658  -1993    167  -3085       C  
ATOM   1519  O   LYS A 202      78.569  10.227-117.602  1.00 87.41           O  
ANISOU 1519  O   LYS A 202     7850  15606   9755  -1816     98  -2734       O  
ATOM   1520  CB  LYS A 202      77.819   9.559-120.490  1.00102.16           C  
ANISOU 1520  CB  LYS A 202     9573  18186  11058  -2261   -218  -3408       C  
ATOM   1521  CG  LYS A 202      78.189  10.029-121.886  1.00104.55           C  
ANISOU 1521  CG  LYS A 202     9864  18952  10907  -2262   -381  -3501       C  
ATOM   1522  CD  LYS A 202      78.030   8.933-122.923  1.00108.94           C  
ANISOU 1522  CD  LYS A 202    10489  19592  11313  -2550   -373  -4000       C  
ATOM   1523  CE  LYS A 202      76.824   9.203-123.808  1.00112.04           C  
ANISOU 1523  CE  LYS A 202    10743  20281  11546  -2663   -571  -3930       C  
ATOM   1524  NZ  LYS A 202      76.748   8.256-124.953  1.00116.42           N  
ANISOU 1524  NZ  LYS A 202    11389  20929  11917  -2904   -551  -4356       N  
ATOM   1525  N   ASP A 203      78.393   7.990-117.543  1.00 83.73           N  
ANISOU 1525  N   ASP A 203     7560  14644   9611  -2133    345  -3244       N  
ATOM   1526  CA  ASP A 203      78.029   7.946-116.133  1.00 80.23           C  
ANISOU 1526  CA  ASP A 203     7110  13894   9480  -2086    466  -2995       C  
ATOM   1527  C   ASP A 203      79.238   7.921-115.204  1.00 76.29           C  
ANISOU 1527  C   ASP A 203     6825  13067   9094  -1820    652  -2763       C  
ATOM   1528  O   ASP A 203      79.063   7.958-113.981  1.00 71.72           O  
ANISOU 1528  O   ASP A 203     6265  12262   8722  -1759    752  -2524       O  
ATOM   1529  CB  ASP A 203      77.137   6.728-115.859  1.00 81.19           C  
ANISOU 1529  CB  ASP A 203     7211  13744   9895  -2377    578  -3237       C  
ATOM   1530  CG  ASP A 203      77.600   5.484-116.597  1.00 84.53           C  
ANISOU 1530  CG  ASP A 203     7801  13958  10360  -2525    704  -3644       C  
ATOM   1531  OD1 ASP A 203      78.219   5.621-117.674  1.00 80.34           O  
ANISOU 1531  OD1 ASP A 203     7322  13654   9548  -2490    632  -3827       O  
ATOM   1532  OD2 ASP A 203      77.340   4.367-116.102  1.00 88.01           O  
ANISOU 1532  OD2 ASP A 203     8325  13995  11121  -2680    896  -3783       O  
ATOM   1533  N   ALA A 204      80.453   7.882-115.747  1.00 75.48           N  
ANISOU 1533  N   ALA A 204     6870  12961   8848  -1664    697  -2819       N  
ATOM   1534  CA  ALA A 204      81.666   7.770-114.951  1.00 67.02           C  
ANISOU 1534  CA  ALA A 204     5976  11599   7891  -1418    859  -2616       C  
ATOM   1535  C   ALA A 204      82.329   9.117-114.684  1.00 58.85           C  
ANISOU 1535  C   ALA A 204     4909  10781   6669  -1172    762  -2291       C  
ATOM   1536  O   ALA A 204      83.438   9.152-114.138  1.00 54.40           O  
ANISOU 1536  O   ALA A 204     4467  10051   6153   -966    860  -2124       O  
ATOM   1537  CB  ALA A 204      82.657   6.827-115.637  1.00 66.77           C  
ANISOU 1537  CB  ALA A 204     6109  11383   7877  -1386   1006  -2879       C  
ATOM   1538  N   THR A 205      81.675  10.222-115.037  1.00 57.65           N  
ANISOU 1538  N   THR A 205     4587  10987   6329  -1190    574  -2189       N  
ATOM   1539  CA  THR A 205      82.254  11.550-114.897  1.00 58.90           C  
ANISOU 1539  CA  THR A 205     4711  11343   6326   -980    491  -1903       C  
ATOM   1540  C   THR A 205      81.719  12.320-113.692  1.00 56.00           C  
ANISOU 1540  C   THR A 205     4271  10927   6079   -921    484  -1616       C  
ATOM   1541  O   THR A 205      82.037  13.503-113.537  1.00 54.96           O  
ANISOU 1541  O   THR A 205     4095  10948   5840   -772    418  -1394       O  
ATOM   1542  CB  THR A 205      82.028  12.359-116.175  1.00 69.00           C  
ANISOU 1542  CB  THR A 205     5861  13048   7307  -1004    305  -1949       C  
ATOM   1543  OG1 THR A 205      82.512  13.693-115.984  1.00 75.09           O  
ANISOU 1543  OG1 THR A 205     6594  13971   7967   -810    242  -1649       O  
ATOM   1544  CG2 THR A 205      80.552  12.409-116.521  1.00 67.31           C  
ANISOU 1544  CG2 THR A 205     5448  13038   7089  -1208    158  -2034       C  
ATOM   1545  N   ASN A 206      80.918  11.688-112.839  1.00 57.18           N  
ANISOU 1545  N   ASN A 206     4410  10861   6454  -1042    572  -1625       N  
ATOM   1546  CA  ASN A 206      80.527  12.342-111.599  1.00 56.34           C  
ANISOU 1546  CA  ASN A 206     4266  10687   6453   -981    613  -1369       C  
ATOM   1547  C   ASN A 206      81.683  12.311-110.599  1.00 49.57           C  
ANISOU 1547  C   ASN A 206     3592   9608   5634   -806    733  -1183       C  
ATOM   1548  O   ASN A 206      82.612  11.506-110.710  1.00 51.20           O  
ANISOU 1548  O   ASN A 206     3942   9639   5873   -752    811  -1250       O  
ATOM   1549  CB  ASN A 206      79.274  11.686-111.019  1.00 53.85           C  
ANISOU 1549  CB  ASN A 206     3870  10238   6353  -1179    685  -1428       C  
ATOM   1550  CG  ASN A 206      78.042  11.954-111.862  1.00 61.67           C  
ANISOU 1550  CG  ASN A 206     4619  11505   7309  -1342    535  -1558       C  
ATOM   1551  OD1 ASN A 206      77.786  13.091-112.259  1.00 61.75           O  
ANISOU 1551  OD1 ASN A 206     4480  11798   7185  -1260    394  -1442       O  
ATOM   1552  ND2 ASN A 206      77.282  10.905-112.157  1.00 64.32           N  
ANISOU 1552  ND2 ASN A 206     4903  11759   7776  -1578    561  -1792       N  
ATOM   1553  N   VAL A 207      81.622  13.206-109.615  1.00 45.21           N  
ANISOU 1553  N   VAL A 207     3024   9073   5080   -718    747   -952       N  
ATOM   1554  CA  VAL A 207      82.778  13.521-108.782  1.00 43.46           C  
ANISOU 1554  CA  VAL A 207     2940   8755   4819   -549    800   -763       C  
ATOM   1555  C   VAL A 207      82.565  13.052-107.344  1.00 43.79           C  
ANISOU 1555  C   VAL A 207     3074   8572   4993   -578    936   -624       C  
ATOM   1556  O   VAL A 207      81.444  12.796-106.893  1.00 44.65           O  
ANISOU 1556  O   VAL A 207     3122   8624   5217   -715   1002   -639       O  
ATOM   1557  CB  VAL A 207      83.098  15.029-108.814  1.00 44.22           C  
ANISOU 1557  CB  VAL A 207     2969   9067   4766   -427    709   -618       C  
ATOM   1558  CG1 VAL A 207      83.316  15.494-110.245  1.00 44.28           C  
ANISOU 1558  CG1 VAL A 207     2891   9309   4625   -398    582   -711       C  
ATOM   1559  CG2 VAL A 207      81.986  15.826-108.146  1.00 41.21           C  
ANISOU 1559  CG2 VAL A 207     2475   8744   4440   -477    724   -527       C  
ATOM   1560  N   GLY A 208      83.678  12.954-106.617  1.00 45.26           N  
ANISOU 1560  N   GLY A 208     3398   8650   5149   -448    978   -473       N  
ATOM   1561  CA  GLY A 208      83.683  12.609-105.213  1.00 43.15           C  
ANISOU 1561  CA  GLY A 208     3237   8218   4941   -451   1089   -293       C  
ATOM   1562  C   GLY A 208      83.698  13.831-104.316  1.00 47.79           C  
ANISOU 1562  C   GLY A 208     3814   8947   5398   -404   1073   -137       C  
ATOM   1563  O   GLY A 208      83.393  14.952-104.738  1.00 48.50           O  
ANISOU 1563  O   GLY A 208     3793   9225   5412   -390   1000   -172       O  
ATOM   1564  N   ASP A 209      84.083  13.609-103.053  1.00 46.28           N  
ANISOU 1564  N   ASP A 209     3746   8662   5178   -378   1147     43       N  
ATOM   1565  CA  ASP A 209      83.986  14.658-102.040  1.00 44.73           C  
ANISOU 1565  CA  ASP A 209     3562   8584   4849   -375   1165    156       C  
ATOM   1566  C   ASP A 209      84.876  15.859-102.345  1.00 43.15           C  
ANISOU 1566  C   ASP A 209     3329   8560   4504   -264   1046    164       C  
ATOM   1567  O   ASP A 209      84.527  16.987-101.976  1.00 41.90           O  
ANISOU 1567  O   ASP A 209     3128   8516   4278   -280   1057    166       O  
ATOM   1568  CB  ASP A 209      84.326  14.093-100.661  1.00 50.63           C  
ANISOU 1568  CB  ASP A 209     4462   9232   5544   -380   1252    351       C  
ATOM   1569  CG  ASP A 209      83.258  13.159-100.139  1.00 52.29           C  
ANISOU 1569  CG  ASP A 209     4701   9276   5889   -516   1410    376       C  
ATOM   1570  OD1 ASP A 209      83.588  12.272 -99.326  1.00 54.99           O  
ANISOU 1570  OD1 ASP A 209     5174   9478   6242   -513   1482    548       O  
ATOM   1571  OD2 ASP A 209      82.088  13.310-100.548  1.00 50.83           O  
ANISOU 1571  OD2 ASP A 209     4397   9108   5810   -627   1461    240       O  
ATOM   1572  N   GLU A 210      86.020  15.656-103.000  1.00 41.11           N  
ANISOU 1572  N   GLU A 210     3086   8315   4221   -155    955    165       N  
ATOM   1573  CA  GLU A 210      86.913  16.763-103.324  1.00 44.93           C  
ANISOU 1573  CA  GLU A 210     3527   8957   4586    -66    855    179       C  
ATOM   1574  C   GLU A 210      86.984  17.066-104.818  1.00 42.00           C  
ANISOU 1574  C   GLU A 210     3049   8679   4229    -28    781     53       C  
ATOM   1575  O   GLU A 210      87.891  17.787-105.247  1.00 50.16           O  
ANISOU 1575  O   GLU A 210     4106   9755   5195     52    684     75       O  
ATOM   1576  CB  GLU A 210      88.316  16.497-102.777  1.00 58.33           C  
ANISOU 1576  CB  GLU A 210     5301  10649   6213     32    807    313       C  
ATOM   1577  CG  GLU A 210      88.731  15.047-102.822  1.00 69.81           C  
ANISOU 1577  CG  GLU A 210     6818  11929   7779     85    841    360       C  
ATOM   1578  CD  GLU A 210      88.732  14.410-101.450  1.00 74.70           C  
ANISOU 1578  CD  GLU A 210     7550  12450   8381     65    897    546       C  
ATOM   1579  OE1 GLU A 210      89.273  15.027-100.507  1.00 72.01           O  
ANISOU 1579  OE1 GLU A 210     7243  12232   7884     75    847    674       O  
ATOM   1580  OE2 GLU A 210      88.186  13.296-101.314  1.00 78.50           O  
ANISOU 1580  OE2 GLU A 210     8089  12739   8999     25    995    565       O  
ATOM   1581  N   GLY A 211      86.059  16.537-105.619  1.00 42.52           N  
ANISOU 1581  N   GLY A 211     3055   8721   4380    -98    794    -77       N  
ATOM   1582  CA  GLY A 211      85.923  16.923-107.009  1.00 37.49           C  
ANISOU 1582  CA  GLY A 211     2344   8188   3714    -87    700   -188       C  
ATOM   1583  C   GLY A 211      86.571  16.004-108.024  1.00 44.53           C  
ANISOU 1583  C   GLY A 211     3226   9092   4600    -55    699   -308       C  
ATOM   1584  O   GLY A 211      86.434  16.249-109.230  1.00 41.75           O  
ANISOU 1584  O   GLY A 211     2796   8890   4179    -64    634   -415       O  
ATOM   1585  N   GLY A 212      87.274  14.964-107.584  1.00 41.64           N  
ANISOU 1585  N   GLY A 212     2965   8546   4309    -11    764   -287       N  
ATOM   1586  CA  GLY A 212      87.917  14.057-108.507  1.00 40.30           C  
ANISOU 1586  CA  GLY A 212     2822   8315   4175     33    789   -420       C  
ATOM   1587  C   GLY A 212      86.995  12.954-108.992  1.00 42.17           C  
ANISOU 1587  C   GLY A 212     3071   8423   4531    -99    849   -617       C  
ATOM   1588  O   GLY A 212      86.009  12.601-108.347  1.00 42.74           O  
ANISOU 1588  O   GLY A 212     3149   8386   4704   -214    895   -606       O  
ATOM   1589  N   PHE A 213      87.329  12.410-110.157  1.00 46.82           N  
ANISOU 1589  N   PHE A 213     3658   9029   5102    -98    861   -815       N  
ATOM   1590  CA  PHE A 213      86.543  11.329-110.727  1.00 53.73           C  
ANISOU 1590  CA  PHE A 213     4548   9783   6085   -249    921  -1056       C  
ATOM   1591  C   PHE A 213      86.894  10.003-110.061  1.00 59.30           C  
ANISOU 1591  C   PHE A 213     5378  10127   7026   -224   1074  -1045       C  
ATOM   1592  O   PHE A 213      87.975   9.830-109.487  1.00 59.40           O  
ANISOU 1592  O   PHE A 213     5455  10022   7093    -57   1122   -878       O  
ATOM   1593  CB  PHE A 213      86.771  11.233-112.234  1.00 49.50           C  
ANISOU 1593  CB  PHE A 213     3980   9414   5415   -275    889  -1304       C  
ATOM   1594  CG  PHE A 213      86.693  12.552-112.943  1.00 51.84           C  
ANISOU 1594  CG  PHE A 213     4164  10066   5467   -255    744  -1253       C  
ATOM   1595  CD1 PHE A 213      85.466  13.128-113.233  1.00 53.89           C  
ANISOU 1595  CD1 PHE A 213     4303  10520   5653   -385    629  -1273       C  
ATOM   1596  CD2 PHE A 213      87.849  13.214-113.327  1.00 52.40           C  
ANISOU 1596  CD2 PHE A 213     4235  10270   5404   -102    730  -1164       C  
ATOM   1597  CE1 PHE A 213      85.393  14.343-113.888  1.00 51.15           C  
ANISOU 1597  CE1 PHE A 213     3849  10479   5105   -347    501  -1184       C  
ATOM   1598  CE2 PHE A 213      87.784  14.426-113.984  1.00 51.13           C  
ANISOU 1598  CE2 PHE A 213     3980  10411   5038    -85    614  -1087       C  
ATOM   1599  CZ  PHE A 213      86.553  14.993-114.263  1.00 51.16           C  
ANISOU 1599  CZ  PHE A 213     3876  10591   4973   -200    498  -1086       C  
ATOM   1600  N   ALA A 214      85.961   9.057-110.148  1.00 57.32           N  
ANISOU 1600  N   ALA A 214     5147   9700   6932   -397   1151  -1213       N  
ATOM   1601  CA  ALA A 214      86.134   7.722-109.574  1.00 60.89           C  
ANISOU 1601  CA  ALA A 214     5720   9763   7653   -397   1321  -1205       C  
ATOM   1602  C   ALA A 214      85.658   6.669-110.565  1.00 67.52           C  
ANISOU 1602  C   ALA A 214     6580  10458   8617   -563   1409  -1561       C  
ATOM   1603  O   ALA A 214      84.634   6.009-110.355  1.00 73.89           O  
ANISOU 1603  O   ALA A 214     7387  11102   9585   -760   1473  -1659       O  
ATOM   1604  CB  ALA A 214      85.383   7.601-108.247  1.00 64.16           C  
ANISOU 1604  CB  ALA A 214     6159  10036   8182   -470   1369   -986       C  
ATOM   1605  N   PRO A 215      86.389   6.473-111.660  1.00 66.81           N  
ANISOU 1605  N   PRO A 215     6507  10422   8456   -504   1429  -1780       N  
ATOM   1606  CA  PRO A 215      86.044   5.386-112.578  1.00 74.19           C  
ANISOU 1606  CA  PRO A 215     7487  11193   9510   -669   1540  -2160       C  
ATOM   1607  C   PRO A 215      86.346   4.038-111.949  1.00 79.13           C  
ANISOU 1607  C   PRO A 215     8246  11318  10501   -633   1765  -2142       C  
ATOM   1608  O   PRO A 215      87.306   3.879-111.191  1.00 79.77           O  
ANISOU 1608  O   PRO A 215     8389  11217  10703   -405   1837  -1872       O  
ATOM   1609  CB  PRO A 215      86.938   5.650-113.795  1.00 74.11           C  
ANISOU 1609  CB  PRO A 215     7472  11392   9294   -573   1526  -2356       C  
ATOM   1610  CG  PRO A 215      88.120   6.359-113.227  1.00 73.68           C  
ANISOU 1610  CG  PRO A 215     7413  11401   9182   -297   1499  -2032       C  
ATOM   1611  CD  PRO A 215      87.600   7.197-112.090  1.00 67.35           C  
ANISOU 1611  CD  PRO A 215     6557  10693   8341   -294   1375  -1703       C  
ATOM   1612  N   ASN A 216      85.499   3.057-112.263  1.00 82.45           N  
ANISOU 1612  N   ASN A 216     8700  11515  11112   -869   1871  -2422       N  
ATOM   1613  CA  ASN A 216      85.639   1.706-111.715  1.00 82.34           C  
ANISOU 1613  CA  ASN A 216     8818  10973  11493   -867   2111  -2418       C  
ATOM   1614  C   ASN A 216      86.915   1.084-112.274  1.00 85.46           C  
ANISOU 1614  C   ASN A 216     9304  11161  12005   -662   2270  -2541       C  
ATOM   1615  O   ASN A 216      86.914   0.338-113.256  1.00 85.01           O  
ANISOU 1615  O   ASN A 216     9298  10971  12032   -775   2398  -2947       O  
ATOM   1616  CB  ASN A 216      84.406   0.872-112.025  1.00 84.73           C  
ANISOU 1616  CB  ASN A 216     9122  11098  11975  -1203   2190  -2730       C  
ATOM   1617  CG  ASN A 216      83.199   1.316-111.228  1.00 82.87           C  
ANISOU 1617  CG  ASN A 216     8787  10980  11720  -1374   2090  -2544       C  
ATOM   1618  OD1 ASN A 216      82.490   2.243-111.620  1.00 82.66           O  
ANISOU 1618  OD1 ASN A 216     8612  11363  11431  -1489   1891  -2604       O  
ATOM   1619  ND2 ASN A 216      82.970   0.671-110.090  1.00 80.17           N  
ANISOU 1619  ND2 ASN A 216     8520  10279  11661  -1380   2240  -2295       N  
ATOM   1620  N   ILE A 217      88.026   1.410-111.620  1.00 86.01           N  
ANISOU 1620  N   ILE A 217     9383  11216  12081   -361   2265  -2192       N  
ATOM   1621  CA  ILE A 217      89.358   0.971-112.008  1.00 93.00           C  
ANISOU 1621  CA  ILE A 217    10311  11940  13084   -111   2406  -2226       C  
ATOM   1622  C   ILE A 217      89.894   0.060-110.915  1.00 91.52           C  
ANISOU 1622  C   ILE A 217    10206  11289  13279     76   2572  -1905       C  
ATOM   1623  O   ILE A 217      89.847   0.412-109.731  1.00 93.18           O  
ANISOU 1623  O   ILE A 217    10404  11524  13476    152   2479  -1492       O  
ATOM   1624  CB  ILE A 217      90.295   2.171-112.228  1.00 96.47           C  
ANISOU 1624  CB  ILE A 217    10651  12792  13211     92   2246  -2069       C  
ATOM   1625  CG1 ILE A 217      89.989   2.834-113.566  1.00 98.10           C  
ANISOU 1625  CG1 ILE A 217    10798  13395  13082    -58   2145  -2418       C  
ATOM   1626  CG2 ILE A 217      91.748   1.744-112.168  1.00 97.53           C  
ANISOU 1626  CG2 ILE A 217    10794  12733  13531    400   2387  -1946       C  
ATOM   1627  CD1 ILE A 217      90.008   1.854-114.699  1.00102.34           C  
ANISOU 1627  CD1 ILE A 217    11409  13753  13721   -165   2338  -2888       C  
ATOM   1628  N   LEU A 218      90.402  -1.109-111.306  1.00 92.25           N  
ANISOU 1628  N   LEU A 218    10383  10960  13708    154   2824  -2089       N  
ATOM   1629  CA  LEU A 218      90.989  -1.996-110.310  1.00 92.22           C  
ANISOU 1629  CA  LEU A 218    10445  10499  14094    370   2987  -1742       C  
ATOM   1630  C   LEU A 218      92.391  -1.548-109.925  1.00 97.60           C  
ANISOU 1630  C   LEU A 218    11043  11304  14735    732   2925  -1398       C  
ATOM   1631  O   LEU A 218      92.694  -1.385-108.738  1.00 96.83           O  
ANISOU 1631  O   LEU A 218    10927  11196  14669    883   2839   -926       O  
ATOM   1632  CB  LEU A 218      91.012  -3.440-110.818  1.00 92.30           C  
ANISOU 1632  CB  LEU A 218    10571   9955  14543    336   3306  -2047       C  
ATOM   1633  CG  LEU A 218      91.637  -4.439-109.835  1.00 93.09           C  
ANISOU 1633  CG  LEU A 218    10737   9529  15102    585   3499  -1659       C  
ATOM   1634  CD1 LEU A 218      91.107  -4.249-108.424  1.00 90.79           C  
ANISOU 1634  CD1 LEU A 218    10460   9242  14794    561   3378  -1160       C  
ATOM   1635  CD2 LEU A 218      91.409  -5.873-110.294  1.00 96.37           C  
ANISOU 1635  CD2 LEU A 218    11284   9338  15994    494   3838  -1981       C  
ATOM   1636  N   GLU A 219      93.253  -1.330-110.910  1.00100.25           N  
ANISOU 1636  N   GLU A 219    11319  11788  14985    860   2966  -1629       N  
ATOM   1637  CA  GLU A 219      94.683  -1.207-110.678  1.00104.42           C  
ANISOU 1637  CA  GLU A 219    11751  12333  15592   1212   2981  -1359       C  
ATOM   1638  C   GLU A 219      95.151   0.234-110.813  1.00103.48           C  
ANISOU 1638  C   GLU A 219    11493  12777  15047   1263   2729  -1249       C  
ATOM   1639  O   GLU A 219      94.734   0.956-111.721  1.00100.73           O  
ANISOU 1639  O   GLU A 219    11124  12766  14381   1086   2642  -1547       O  
ATOM   1640  CB  GLU A 219      95.454  -2.099-111.646  1.00107.46           C  
ANISOU 1640  CB  GLU A 219    12153  12420  16257   1352   3269  -1682       C  
ATOM   1641  CG  GLU A 219      94.955  -3.522-111.646  1.00111.67           C  
ANISOU 1641  CG  GLU A 219    12835  12358  17236   1273   3549  -1861       C  
ATOM   1642  CD  GLU A 219      95.242  -4.214-112.949  1.00117.31           C  
ANISOU 1642  CD  GLU A 219    13601  12872  18098   1250   3826  -2403       C  
ATOM   1643  OE1 GLU A 219      95.082  -5.450-113.020  1.00122.12           O  
ANISOU 1643  OE1 GLU A 219    14327  12931  19140   1232   4110  -2577       O  
ATOM   1644  OE2 GLU A 219      95.631  -3.514-113.906  1.00117.25           O  
ANISOU 1644  OE2 GLU A 219    13524  13256  17769   1242   3774  -2660       O  
ATOM   1645  N   ASN A 220      96.051   0.626-109.912  1.00105.36           N  
ANISOU 1645  N   ASN A 220    11632  13110  15290   1504   2616   -811       N  
ATOM   1646  CA  ASN A 220      96.548   1.996-109.860  1.00104.84           C  
ANISOU 1646  CA  ASN A 220    11431  13540  14862   1548   2381   -663       C  
ATOM   1647  C   ASN A 220      97.368   2.362-111.094  1.00104.58           C  
ANISOU 1647  C   ASN A 220    11304  13712  14719   1630   2449   -937       C  
ATOM   1648  O   ASN A 220      97.428   3.541-111.467  1.00100.90           O  
ANISOU 1648  O   ASN A 220    10760  13670  13909   1561   2284   -966       O  
ATOM   1649  CB  ASN A 220      97.374   2.168-108.589  1.00106.68           C  
ANISOU 1649  CB  ASN A 220    11575  13798  15161   1774   2257   -153       C  
ATOM   1650  CG  ASN A 220      96.831   1.344-107.446  1.00108.47           C  
ANISOU 1650  CG  ASN A 220    11912  13693  15610   1765   2293    131       C  
ATOM   1651  OD1 ASN A 220      95.628   1.323-107.204  1.00105.80           O  
ANISOU 1651  OD1 ASN A 220    11688  13316  15197   1523   2274     58       O  
ATOM   1652  ND2 ASN A 220      97.713   0.640-106.750  1.00113.14           N  
ANISOU 1652  ND2 ASN A 220    12456  14044  16486   2032   2354    472       N  
ATOM   1653  N   SER A 221      98.018   1.380-111.728  1.00107.47           N  
ANISOU 1653  N   SER A 221    11677  13774  15382   1781   2710  -1131       N  
ATOM   1654  CA  SER A 221      98.744   1.649-112.965  1.00109.37           C  
ANISOU 1654  CA  SER A 221    11842  14204  15510   1841   2822  -1431       C  
ATOM   1655  C   SER A 221      97.848   2.313-114.003  1.00106.44           C  
ANISOU 1655  C   SER A 221    11533  14157  14752   1547   2749  -1806       C  
ATOM   1656  O   SER A 221      98.272   3.247-114.693  1.00105.30           O  
ANISOU 1656  O   SER A 221    11299  14401  14310   1545   2677  -1874       O  
ATOM   1657  CB  SER A 221      99.335   0.353-113.526  1.00113.49           C  
ANISOU 1657  CB  SER A 221    12398  14290  16433   2006   3165  -1663       C  
ATOM   1658  OG  SER A 221      99.831   0.537-114.844  1.00112.47           O  
ANISOU 1658  OG  SER A 221    12233  14345  16157   2007   3313  -2042       O  
ATOM   1659  N   GLU A 222      96.602   1.850-114.126  1.00102.52           N  
ANISOU 1659  N   GLU A 222    11177  13518  14258   1292   2763  -2032       N  
ATOM   1660  CA  GLU A 222      95.686   2.481-115.069  1.00100.75           C  
ANISOU 1660  CA  GLU A 222    10987  13634  13660   1010   2658  -2353       C  
ATOM   1661  C   GLU A 222      95.287   3.879-114.613  1.00 94.66           C  
ANISOU 1661  C   GLU A 222    10133  13284  12548    932   2355  -2083       C  
ATOM   1662  O   GLU A 222      95.048   4.755-115.451  1.00 94.54           O  
ANISOU 1662  O   GLU A 222    10079  13655  12186    812   2247  -2231       O  
ATOM   1663  CB  GLU A 222      94.447   1.612-115.276  1.00103.40           C  
ANISOU 1663  CB  GLU A 222    11461  13718  14109    744   2737  -2660       C  
ATOM   1664  CG  GLU A 222      93.587   2.076-116.443  1.00103.23           C  
ANISOU 1664  CG  GLU A 222    11456  14048  13718    458   2649  -3047       C  
ATOM   1665  CD  GLU A 222      92.614   1.019-116.922  1.00107.29           C  
ANISOU 1665  CD  GLU A 222    12092  14298  14375    196   2784  -3464       C  
ATOM   1666  OE1 GLU A 222      91.537   1.395-117.432  1.00107.77           O  
ANISOU 1666  OE1 GLU A 222    12147  14632  14169    -86   2631  -3667       O  
ATOM   1667  OE2 GLU A 222      92.923  -0.185-116.789  1.00110.23           O  
ANISOU 1667  OE2 GLU A 222    12554  14186  15143    268   3044  -3584       O  
ATOM   1668  N   ALA A 223      95.207   4.108-113.301  1.00 88.18           N  
ANISOU 1668  N   ALA A 223     9291  12396  11816    998   2225  -1688       N  
ATOM   1669  CA  ALA A 223      94.978   5.462-112.807  1.00 78.79           C  
ANISOU 1669  CA  ALA A 223     8023  11579  10334    949   1970  -1438       C  
ATOM   1670  C   ALA A 223      96.126   6.382-113.206  1.00 70.88           C  
ANISOU 1670  C   ALA A 223     6892  10881   9158   1106   1919  -1344       C  
ATOM   1671  O   ALA A 223      95.905   7.483-113.722  1.00 71.27           O  
ANISOU 1671  O   ALA A 223     6889  11290   8899   1008   1786  -1379       O  
ATOM   1672  CB  ALA A 223      94.794   5.447-111.289  1.00 75.67           C  
ANISOU 1672  CB  ALA A 223     7641  11047  10062    995   1875  -1053       C  
ATOM   1673  N   LEU A 224      97.366   5.933-112.993  1.00 65.55           N  
ANISOU 1673  N   LEU A 224     6149  10058   8699   1354   2034  -1212       N  
ATOM   1674  CA  LEU A 224      98.520   6.738-113.379  1.00 65.39           C  
ANISOU 1674  CA  LEU A 224     5981  10313   8552   1498   2009  -1127       C  
ATOM   1675  C   LEU A 224      98.595   6.916-114.893  1.00 72.46           C  
ANISOU 1675  C   LEU A 224     6879  11404   9249   1423   2125  -1488       C  
ATOM   1676  O   LEU A 224      98.912   8.009-115.376  1.00 69.35           O  
ANISOU 1676  O   LEU A 224     6398  11365   8587   1399   2035  -1453       O  
ATOM   1677  CB  LEU A 224      99.801   6.101-112.839  1.00 66.01           C  
ANISOU 1677  CB  LEU A 224     5956  10181   8944   1785   2117   -913       C  
ATOM   1678  CG  LEU A 224      99.884   6.013-111.311  1.00 65.60           C  
ANISOU 1678  CG  LEU A 224     5881  10009   9033   1874   1974   -499       C  
ATOM   1679  CD1 LEU A 224     100.924   4.999-110.882  1.00 63.45           C  
ANISOU 1679  CD1 LEU A 224     5531   9438   9141   2158   2115   -318       C  
ATOM   1680  CD2 LEU A 224     100.195   7.374-110.707  1.00 57.11           C  
ANISOU 1680  CD2 LEU A 224     4693   9305   7703   1848   1727   -238       C  
ATOM   1681  N   GLU A 225      98.307   5.857-115.657  1.00 76.44           N  
ANISOU 1681  N   GLU A 225     7488  11682   9873   1374   2335  -1840       N  
ATOM   1682  CA  GLU A 225      98.249   5.987-117.111  1.00 81.42           C  
ANISOU 1682  CA  GLU A 225     8147  12533  10257   1263   2441  -2217       C  
ATOM   1683  C   GLU A 225      97.143   6.946-117.531  1.00 75.73           C  
ANISOU 1683  C   GLU A 225     7455  12167   9151   1008   2226  -2277       C  
ATOM   1684  O   GLU A 225      97.321   7.744-118.460  1.00 73.28           O  
ANISOU 1684  O   GLU A 225     7102  12215   8528    957   2196  -2362       O  
ATOM   1685  CB  GLU A 225      98.036   4.618-117.760  1.00 91.18           C  
ANISOU 1685  CB  GLU A 225     9508  13437  11697   1221   2706  -2620       C  
ATOM   1686  CG  GLU A 225      99.202   3.651-117.619  1.00100.83           C  
ANISOU 1686  CG  GLU A 225    10690  14305  13317   1499   2976  -2612       C  
ATOM   1687  CD  GLU A 225     100.333   3.938-118.588  1.00107.45           C  
ANISOU 1687  CD  GLU A 225    11426  15355  14046   1636   3145  -2746       C  
ATOM   1688  OE1 GLU A 225     100.056   4.432-119.700  1.00108.54           O  
ANISOU 1688  OE1 GLU A 225    11600  15824  13815   1467   3150  -3020       O  
ATOM   1689  OE2 GLU A 225     101.500   3.663-118.237  1.00111.45           O  
ANISOU 1689  OE2 GLU A 225    11804  15711  14832   1915   3275  -2563       O  
ATOM   1690  N   LEU A 226      95.992   6.879-116.856  1.00 70.22           N  
ANISOU 1690  N   LEU A 226     6822  11377   8483    854   2084  -2215       N  
ATOM   1691  CA  LEU A 226      94.883   7.779-117.156  1.00 63.67           C  
ANISOU 1691  CA  LEU A 226     5989  10865   7338    633   1874  -2237       C  
ATOM   1692  C   LEU A 226      95.288   9.236-116.952  1.00 61.15           C  
ANISOU 1692  C   LEU A 226     5554  10879   6800    698   1700  -1933       C  
ATOM   1693  O   LEU A 226      95.055  10.087-117.820  1.00 57.53           O  
ANISOU 1693  O   LEU A 226     5061  10765   6032    604   1616  -1992       O  
ATOM   1694  CB  LEU A 226      93.682   7.418-116.280  1.00 63.94           C  
ANISOU 1694  CB  LEU A 226     6082  10704   7510    489   1780  -2179       C  
ATOM   1695  CG  LEU A 226      92.284   7.471-116.888  1.00 65.41           C  
ANISOU 1695  CG  LEU A 226     6296  11045   7512    212   1678  -2418       C  
ATOM   1696  CD1 LEU A 226      92.279   6.822-118.259  1.00 71.51           C  
ANISOU 1696  CD1 LEU A 226     7127  11875   8169    101   1814  -2857       C  
ATOM   1697  CD2 LEU A 226      91.302   6.770-115.963  1.00 65.36           C  
ANISOU 1697  CD2 LEU A 226     6345  10737   7751     94   1673  -2385       C  
ATOM   1698  N   VAL A 227      95.902   9.538-115.804  1.00 53.54           N  
ANISOU 1698  N   VAL A 227     4531   9818   5994    850   1644  -1600       N  
ATOM   1699  CA  VAL A 227      96.392  10.890-115.537  1.00 55.09           C  
ANISOU 1699  CA  VAL A 227     4617  10288   6025    902   1501  -1330       C  
ATOM   1700  C   VAL A 227      97.484  11.268-116.536  1.00 63.50           C  
ANISOU 1700  C   VAL A 227     5601  11561   6964    997   1605  -1395       C  
ATOM   1701  O   VAL A 227      97.444  12.340-117.152  1.00 65.21           O  
ANISOU 1701  O   VAL A 227     5804  12035   6936    918   1499  -1336       O  
ATOM   1702  CB  VAL A 227      96.896  10.993-114.084  1.00 49.67           C  
ANISOU 1702  CB  VAL A 227     3886   9455   5530   1028   1428  -1000       C  
ATOM   1703  CG1 VAL A 227      97.347  12.396-113.781  1.00 48.12           C  
ANISOU 1703  CG1 VAL A 227     3584   9526   5175   1043   1284   -765       C  
ATOM   1704  CG2 VAL A 227      95.821  10.562-113.105  1.00 49.09           C  
ANISOU 1704  CG2 VAL A 227     3904   9181   5566    928   1360   -935       C  
ATOM   1705  N   LYS A 228      98.479  10.390-116.699  1.00 62.10           N  
ANISOU 1705  N   LYS A 228     5402  11203   6990   1161   1803  -1477       N  
ATOM   1706  CA  LYS A 228      99.551  10.600-117.671  1.00 64.60           C  
ANISOU 1706  CA  LYS A 228     5659  11658   7227   1247   1936  -1551       C  
ATOM   1707  C   LYS A 228      98.994  10.918-119.056  1.00 69.03           C  
ANISOU 1707  C   LYS A 228     6329  12426   7473   1060   1927  -1782       C  
ATOM   1708  O   LYS A 228      99.464  11.837-119.737  1.00 72.98           O  
ANISOU 1708  O   LYS A 228     6835  13103   7791   1021   1857  -1672       O  
ATOM   1709  CB  LYS A 228     100.427   9.345-117.712  1.00 69.05           C  
ANISOU 1709  CB  LYS A 228     6186  11958   8094   1448   2202  -1692       C  
ATOM   1710  CG  LYS A 228     101.767   9.452-118.407  1.00 71.15           C  
ANISOU 1710  CG  LYS A 228     6392  12244   8398   1570   2343  -1673       C  
ATOM   1711  CD  LYS A 228     102.553   8.178-118.116  1.00 75.59           C  
ANISOU 1711  CD  LYS A 228     6870  12508   9345   1820   2602  -1757       C  
ATOM   1712  CE  LYS A 228     103.530   7.826-119.220  1.00 80.83           C  
ANISOU 1712  CE  LYS A 228     7541  13124  10046   1896   2851  -1932       C  
ATOM   1713  NZ  LYS A 228     104.751   8.672-119.185  1.00 83.27           N  
ANISOU 1713  NZ  LYS A 228     7716  13546  10377   1972   2796  -1642       N  
ATOM   1714  N   GLU A 229      97.982  10.160-119.480  1.00 64.49           N  
ANISOU 1714  N   GLU A 229     5833  11839   6832    932   1991  -2105       N  
ATOM   1715  CA  GLU A 229      97.351  10.384-120.776  1.00 69.77           C  
ANISOU 1715  CA  GLU A 229     6595  12743   7173    736   1951  -2331       C  
ATOM   1716  C   GLU A 229      96.755  11.785-120.872  1.00 69.47           C  
ANISOU 1716  C   GLU A 229     6533  12987   6876    618   1675  -2077       C  
ATOM   1717  O   GLU A 229      96.973  12.499-121.857  1.00 73.41           O  
ANISOU 1717  O   GLU A 229     7052  13705   7136    561   1619  -2039       O  
ATOM   1718  CB  GLU A 229      96.281   9.315-121.000  1.00 80.83           C  
ANISOU 1718  CB  GLU A 229     8073  14056   8583    584   2033  -2720       C  
ATOM   1719  CG  GLU A 229      95.422   9.471-122.238  1.00 84.89           C  
ANISOU 1719  CG  GLU A 229     8665  14852   8738    345   1945  -2969       C  
ATOM   1720  CD  GLU A 229      94.453   8.314-122.391  1.00 86.74           C  
ANISOU 1720  CD  GLU A 229     8991  14922   9045    166   2017  -3362       C  
ATOM   1721  OE1 GLU A 229      93.584   8.371-123.283  1.00 88.38           O  
ANISOU 1721  OE1 GLU A 229     9232  15400   8948    -59   1925  -3600       O  
ATOM   1722  OE2 GLU A 229      94.564   7.345-121.609  1.00 85.24           O  
ANISOU 1722  OE2 GLU A 229     8849  14297   9241    238   2139  -3395       O  
ATOM   1723  N   ALA A 230      96.001  12.198-119.850  1.00 65.78           N  
ANISOU 1723  N   ALA A 230     6018  12503   6471    588   1517  -1893       N  
ATOM   1724  CA  ALA A 230      95.326  13.492-119.901  1.00 59.25           C  
ANISOU 1724  CA  ALA A 230     5165  11900   5447    488   1276  -1670       C  
ATOM   1725  C   ALA A 230      96.324  14.645-119.895  1.00 52.96           C  
ANISOU 1725  C   ALA A 230     4342  11142   4639    575   1202  -1365       C  
ATOM   1726  O   ALA A 230      96.113  15.658-120.573  1.00 50.63           O  
ANISOU 1726  O   ALA A 230     4039  11059   4140    506   1078  -1252       O  
ATOM   1727  CB  ALA A 230      94.343  13.617-118.736  1.00 55.40           C  
ANISOU 1727  CB  ALA A 230     4637  11343   5071    445   1163  -1554       C  
ATOM   1728  N   ILE A 231      97.412  14.511-119.133  1.00 50.33           N  
ANISOU 1728  N   ILE A 231     3978  10612   4534    722   1277  -1229       N  
ATOM   1729  CA  ILE A 231      98.478  15.511-119.165  1.00 58.85           C  
ANISOU 1729  CA  ILE A 231     5025  11718   5618    782   1233   -990       C  
ATOM   1730  C   ILE A 231      99.032  15.650-120.578  1.00 61.44           C  
ANISOU 1730  C   ILE A 231     5372  12207   5765    762   1331  -1094       C  
ATOM   1731  O   ILE A 231      99.205  16.762-121.093  1.00 64.32           O  
ANISOU 1731  O   ILE A 231     5726  12727   5985    716   1241   -935       O  
ATOM   1732  CB  ILE A 231      99.591  15.141-118.167  1.00 50.27           C  
ANISOU 1732  CB  ILE A 231     3874  10420   4805    935   1306   -867       C  
ATOM   1733  CG1 ILE A 231      99.065  15.175-116.734  1.00 47.25           C  
ANISOU 1733  CG1 ILE A 231     3478   9917   4558    941   1186   -718       C  
ATOM   1734  CG2 ILE A 231     100.777  16.069-118.330  1.00 49.24           C  
ANISOU 1734  CG2 ILE A 231     3696  10331   4683    972   1287   -678       C  
ATOM   1735  CD1 ILE A 231      99.850  14.293-115.794  1.00 50.00           C  
ANISOU 1735  CD1 ILE A 231     3749  10078   5170   1101   1282   -662       C  
ATOM   1736  N   ASP A 232      99.318  14.518-121.228  1.00 59.06           N  
ANISOU 1736  N   ASP A 232     5103  11860   5476    796   1537  -1369       N  
ATOM   1737  CA  ASP A 232      99.891  14.560-122.570  1.00 66.99           C  
ANISOU 1737  CA  ASP A 232     6140  13010   6301    774   1661  -1488       C  
ATOM   1738  C   ASP A 232      98.866  15.011-123.605  1.00 64.68           C  
ANISOU 1738  C   ASP A 232     5901  13002   5670    603   1541  -1571       C  
ATOM   1739  O   ASP A 232      99.207  15.732-124.550  1.00 63.22           O  
ANISOU 1739  O   ASP A 232     5719  13013   5288    564   1534  -1492       O  
ATOM   1740  CB  ASP A 232     100.470  13.187-122.928  1.00 83.73           C  
ANISOU 1740  CB  ASP A 232     8293  14969   8552    861   1938  -1783       C  
ATOM   1741  CG  ASP A 232     101.691  12.836-122.085  1.00 93.74           C  
ANISOU 1741  CG  ASP A 232     9462  15996  10160   1062   2069  -1652       C  
ATOM   1742  OD1 ASP A 232     102.428  13.771-121.699  1.00 90.38           O  
ANISOU 1742  OD1 ASP A 232     8954  15598   9789   1103   1979  -1370       O  
ATOM   1743  OD2 ASP A 232     101.896  11.634-121.791  1.00 99.63           O  
ANISOU 1743  OD2 ASP A 232    10201  16521  11133   1175   2257  -1830       O  
ATOM   1744  N   LYS A 233      97.607  14.592-123.451  1.00 69.91           N  
ANISOU 1744  N   LYS A 233     6590  13706   6267    496   1447  -1718       N  
ATOM   1745  CA  LYS A 233      96.561  15.060-124.355  1.00 67.25           C  
ANISOU 1745  CA  LYS A 233     6264  13670   5619    331   1296  -1763       C  
ATOM   1746  C   LYS A 233      96.404  16.573-124.274  1.00 59.89           C  
ANISOU 1746  C   LYS A 233     5258  12893   4606    330   1099  -1400       C  
ATOM   1747  O   LYS A 233      96.198  17.239-125.295  1.00 58.42           O  
ANISOU 1747  O   LYS A 233     5058  12966   4173    259   1031  -1333       O  
ATOM   1748  CB  LYS A 233      95.241  14.357-124.035  1.00 70.39           C  
ANISOU 1748  CB  LYS A 233     6671  14071   6005    211   1225  -1973       C  
ATOM   1749  CG  LYS A 233      95.213  12.875-124.397  1.00 76.30           C  
ANISOU 1749  CG  LYS A 233     7508  14691   6792    161   1424  -2397       C  
ATOM   1750  CD  LYS A 233      94.662  12.647-125.797  1.00 84.97           C  
ANISOU 1750  CD  LYS A 233     8665  16055   7565    -23   1399  -2655       C  
ATOM   1751  CE  LYS A 233      93.266  12.031-125.759  1.00 86.21           C  
ANISOU 1751  CE  LYS A 233     8825  16276   7657   -219   1298  -2911       C  
ATOM   1752  NZ  LYS A 233      93.296  10.559-125.518  1.00 85.34           N  
ANISOU 1752  NZ  LYS A 233     8806  15868   7752   -248   1517  -3309       N  
ATOM   1753  N   ALA A 234      96.512  17.136-123.068  1.00 55.97           N  
ANISOU 1753  N   ALA A 234     4713  12228   4323    407   1018  -1162       N  
ATOM   1754  CA  ALA A 234      96.464  18.582-122.885  1.00 55.83           C  
ANISOU 1754  CA  ALA A 234     4638  12292   4283    415    865   -836       C  
ATOM   1755  C   ALA A 234      97.764  19.279-123.276  1.00 60.98           C  
ANISOU 1755  C   ALA A 234     5282  12937   4949    482    945   -676       C  
ATOM   1756  O   ALA A 234      97.791  20.514-123.336  1.00 60.00           O  
ANISOU 1756  O   ALA A 234     5117  12891   4790    477    850   -424       O  
ATOM   1757  CB  ALA A 234      96.120  18.917-121.432  1.00 48.75           C  
ANISOU 1757  CB  ALA A 234     3721  11197   3604    451    764   -676       C  
ATOM   1758  N   GLY A 235      98.834  18.530-123.523  1.00 59.02           N  
ANISOU 1758  N   GLY A 235     5063  12590   4772    547   1135   -814       N  
ATOM   1759  CA  GLY A 235     100.076  19.123-123.987  1.00 61.50           C  
ANISOU 1759  CA  GLY A 235     5352  12921   5093    597   1237   -686       C  
ATOM   1760  C   GLY A 235     100.930  19.771-122.921  1.00 66.83           C  
ANISOU 1760  C   GLY A 235     5972  13409   6013    670   1209   -463       C  
ATOM   1761  O   GLY A 235     101.545  20.815-123.175  1.00 71.83           O  
ANISOU 1761  O   GLY A 235     6568  14099   6626    662   1202   -270       O  
ATOM   1762  N   TYR A 236     101.003  19.175-121.733  1.00 65.29           N  
ANISOU 1762  N   TYR A 236     5768  12998   6042    732   1197   -486       N  
ATOM   1763  CA  TYR A 236     101.795  19.698-120.623  1.00 60.90           C  
ANISOU 1763  CA  TYR A 236     5158  12279   5704    783   1151   -295       C  
ATOM   1764  C   TYR A 236     102.674  18.604-120.030  1.00 63.68           C  
ANISOU 1764  C   TYR A 236     5460  12454   6282    901   1284   -383       C  
ATOM   1765  O   TYR A 236     102.786  18.456-118.812  1.00 60.83           O  
ANISOU 1765  O   TYR A 236     5068  11945   6100    945   1214   -298       O  
ATOM   1766  CB  TYR A 236     100.895  20.295-119.550  1.00 46.88           C  
ANISOU 1766  CB  TYR A 236     3408  10434   3972    735    961   -166       C  
ATOM   1767  CG  TYR A 236     100.111  21.514-119.988  1.00 55.07           C  
ANISOU 1767  CG  TYR A 236     4461  11614   4850    649    839    -30       C  
ATOM   1768  CD1 TYR A 236     100.758  22.676-120.391  1.00 46.63           C  
ANISOU 1768  CD1 TYR A 236     3358  10607   3752    628    845    145       C  
ATOM   1769  CD2 TYR A 236      98.719  21.512-119.969  1.00 49.16           C  
ANISOU 1769  CD2 TYR A 236     3739  10937   4003    593    730    -62       C  
ATOM   1770  CE1 TYR A 236     100.041  23.795-120.781  1.00 46.38           C  
ANISOU 1770  CE1 TYR A 236     3324  10695   3605    572    754    298       C  
ATOM   1771  CE2 TYR A 236      97.997  22.625-120.355  1.00 45.20           C  
ANISOU 1771  CE2 TYR A 236     3220  10572   3384    540    627     91       C  
ATOM   1772  CZ  TYR A 236      98.660  23.762-120.759  1.00 45.86           C  
ANISOU 1772  CZ  TYR A 236     3273  10703   3448    538    644    278       C  
ATOM   1773  OH  TYR A 236      97.938  24.868-121.140  1.00 46.36           O  
ANISOU 1773  OH  TYR A 236     3303  10892   3419    506    564    458       O  
ATOM   1774  N   THR A 237     103.340  17.841-120.897  1.00 71.67           N  
ANISOU 1774  N   THR A 237     6455  13485   7291    961   1489   -545       N  
ATOM   1775  CA  THR A 237     104.042  16.637-120.457  1.00 77.50           C  
ANISOU 1775  CA  THR A 237     7133  14046   8269   1100   1650   -652       C  
ATOM   1776  C   THR A 237     105.107  16.942-119.406  1.00 71.98           C  
ANISOU 1776  C   THR A 237     6307  13233   7811   1181   1606   -446       C  
ATOM   1777  O   THR A 237     105.187  16.261-118.376  1.00 75.18           O  
ANISOU 1777  O   THR A 237     6660  13489   8418   1274   1586   -417       O  
ATOM   1778  CB  THR A 237     104.663  15.932-121.656  1.00 83.82           C  
ANISOU 1778  CB  THR A 237     7937  14883   9029   1149   1908   -859       C  
ATOM   1779  OG1 THR A 237     103.613  15.485-122.524  1.00 84.94           O  
ANISOU 1779  OG1 THR A 237     8203  15134   8937   1059   1935  -1090       O  
ATOM   1780  CG2 THR A 237     105.494  14.742-121.198  1.00 83.00           C  
ANISOU 1780  CG2 THR A 237     7741  14566   9230   1326   2103   -946       C  
ATOM   1781  N   GLU A 238     105.938  17.953-119.642  1.00 63.00           N  
ANISOU 1781  N   GLU A 238     5109  12175   6654   1143   1588   -300       N  
ATOM   1782  CA  GLU A 238     107.019  18.261-118.715  1.00 64.64           C  
ANISOU 1782  CA  GLU A 238     5180  12306   7076   1195   1542   -130       C  
ATOM   1783  C   GLU A 238     106.695  19.411-117.771  1.00 62.77           C  
ANISOU 1783  C   GLU A 238     4968  12079   6802   1088   1313     58       C  
ATOM   1784  O   GLU A 238     107.530  19.754-116.924  1.00 69.67           O  
ANISOU 1784  O   GLU A 238     5736  12915   7821   1101   1248    189       O  
ATOM   1785  CB  GLU A 238     108.320  18.557-119.477  1.00 67.56           C  
ANISOU 1785  CB  GLU A 238     5435  12736   7501   1221   1704   -110       C  
ATOM   1786  CG  GLU A 238     108.234  19.665-120.515  1.00 71.53           C  
ANISOU 1786  CG  GLU A 238     5995  13404   7779   1097   1717    -67       C  
ATOM   1787  CD  GLU A 238     109.459  19.702-121.416  1.00 87.51           C  
ANISOU 1787  CD  GLU A 238     7911  15487   9851   1131   1938    -88       C  
ATOM   1788  OE1 GLU A 238     109.860  20.805-121.846  1.00 92.60           O  
ANISOU 1788  OE1 GLU A 238     8529  16236  10419   1041   1936     36       O  
ATOM   1789  OE2 GLU A 238     110.024  18.624-121.692  1.00 88.58           O  
ANISOU 1789  OE2 GLU A 238     7982  15553  10121   1252   2135   -230       O  
ATOM   1790  N   LYS A 239     105.510  20.007-117.882  1.00 54.61           N  
ANISOU 1790  N   LYS A 239     4062  11099   5586    984   1196     65       N  
ATOM   1791  CA  LYS A 239     105.106  21.059-116.961  1.00 54.69           C  
ANISOU 1791  CA  LYS A 239     4109  11090   5582    889   1013    215       C  
ATOM   1792  C   LYS A 239     104.319  20.537-115.767  1.00 54.06           C  
ANISOU 1792  C   LYS A 239     4078  10908   5556    902    902    211       C  
ATOM   1793  O   LYS A 239     104.181  21.258-114.770  1.00 50.63           O  
ANISOU 1793  O   LYS A 239     3660  10437   5140    836    774    321       O  
ATOM   1794  CB  LYS A 239     104.255  22.107-117.684  1.00 57.11           C  
ANISOU 1794  CB  LYS A 239     4503  11499   5696    782    957    256       C  
ATOM   1795  CG  LYS A 239     104.742  22.494-119.066  1.00 56.28           C  
ANISOU 1795  CG  LYS A 239     4370  11533   5479    768   1080    255       C  
ATOM   1796  CD  LYS A 239     106.105  23.153-119.020  1.00 57.36           C  
ANISOU 1796  CD  LYS A 239     4395  11666   5734    759   1146    364       C  
ATOM   1797  CE  LYS A 239     106.361  23.959-120.287  1.00 66.03           C  
ANISOU 1797  CE  LYS A 239     5483  12908   6696    707   1244    426       C  
ATOM   1798  NZ  LYS A 239     105.516  25.186-120.327  1.00 66.21           N  
ANISOU 1798  NZ  LYS A 239     5566  12973   6618    614   1132    567       N  
ATOM   1799  N   ILE A 240     103.798  19.316-115.838  1.00 51.43           N  
ANISOU 1799  N   ILE A 240     3766  10526   5248    977    966     79       N  
ATOM   1800  CA  ILE A 240     102.896  18.791-114.822  1.00 54.24           C  
ANISOU 1800  CA  ILE A 240     4170  10797   5642    981    883     75       C  
ATOM   1801  C   ILE A 240     103.385  17.419-114.379  1.00 56.00           C  
ANISOU 1801  C   ILE A 240     4306  10917   6053   1132    984     30       C  
ATOM   1802  O   ILE A 240     103.777  16.592-115.210  1.00 60.41           O  
ANISOU 1802  O   ILE A 240     4826  11459   6669   1222   1156   -105       O  
ATOM   1803  CB  ILE A 240     101.445  18.720-115.345  1.00 50.31           C  
ANISOU 1803  CB  ILE A 240     3780  10343   4993    905    859    -40       C  
ATOM   1804  CG1 ILE A 240     100.932  20.129-115.665  1.00 45.32           C  
ANISOU 1804  CG1 ILE A 240     3205   9802   4212    785    749     53       C  
ATOM   1805  CG2 ILE A 240     100.548  18.016-114.342  1.00 42.84           C  
ANISOU 1805  CG2 ILE A 240     2864   9302   4112    912    815    -61       C  
ATOM   1806  CD1 ILE A 240      99.514  20.171-116.168  1.00 41.96           C  
ANISOU 1806  CD1 ILE A 240     2847   9453   3644    715    701    -25       C  
ATOM   1807  N   VAL A 241     103.356  17.181-113.066  1.00 45.48           N  
ANISOU 1807  N   VAL A 241     2941   9518   4820   1166    891    148       N  
ATOM   1808  CA  VAL A 241     103.883  15.968-112.455  1.00 55.56           C  
ANISOU 1808  CA  VAL A 241     4107  10698   6304   1335    962    181       C  
ATOM   1809  C   VAL A 241     102.841  15.416-111.483  1.00 55.50           C  
ANISOU 1809  C   VAL A 241     4146  10632   6309   1338    905    213       C  
ATOM   1810  O   VAL A 241     101.959  16.134-111.005  1.00 47.81           O  
ANISOU 1810  O   VAL A 241     3268   9700   5197   1201    783    247       O  
ATOM   1811  CB  VAL A 241     105.239  16.238-111.751  1.00 57.54           C  
ANISOU 1811  CB  VAL A 241     4214  10971   6678   1397    892    363       C  
ATOM   1812  CG1 VAL A 241     105.059  17.079-110.501  1.00 46.62           C  
ANISOU 1812  CG1 VAL A 241     2858   9650   5208   1287    691    524       C  
ATOM   1813  CG2 VAL A 241     105.973  14.953-111.443  1.00 65.25           C  
ANISOU 1813  CG2 VAL A 241     5042  11845   7903   1614    991    410       C  
ATOM   1814  N   ILE A 242     102.946  14.112-111.204  1.00 54.58           N  
ANISOU 1814  N   ILE A 242     3953  10405   6381   1508   1019    207       N  
ATOM   1815  CA  ILE A 242     101.933  13.370-110.455  1.00 55.61           C  
ANISOU 1815  CA  ILE A 242     4112  10466   6552   1536   1026    224       C  
ATOM   1816  C   ILE A 242     102.350  13.233-108.997  1.00 56.74           C  
ANISOU 1816  C   ILE A 242     4167  10611   6781   1619    899    505       C  
ATOM   1817  O   ILE A 242     103.512  12.931-108.691  1.00 56.22           O  
ANISOU 1817  O   ILE A 242     3973  10524   6865   1763    887    652       O  
ATOM   1818  CB  ILE A 242     101.692  11.983-111.085  1.00 60.45           C  
ANISOU 1818  CB  ILE A 242     4713  10925   7330   1676   1260     38       C  
ATOM   1819  CG1 ILE A 242     101.086  12.124-112.485  1.00 60.20           C  
ANISOU 1819  CG1 ILE A 242     4778  10955   7141   1553   1365   -267       C  
ATOM   1820  CG2 ILE A 242     100.811  11.126-110.184  1.00 50.15           C  
ANISOU 1820  CG2 ILE A 242     3555   9360   6140   1650   1233     99       C  
ATOM   1821  CD1 ILE A 242     100.900  10.805-113.207  1.00 59.85           C  
ANISOU 1821  CD1 ILE A 242     4806  10688   7247   1619   1584   -524       C  
ATOM   1822  N   GLY A 243     101.396  13.450-108.094  1.00 54.86           N  
ANISOU 1822  N   GLY A 243     3991  10412   6440   1521    802    586       N  
ATOM   1823  CA  GLY A 243     101.575  13.144-106.689  1.00 59.50           C  
ANISOU 1823  CA  GLY A 243     4579  10954   7076   1563    680    844       C  
ATOM   1824  C   GLY A 243     100.522  12.148-106.241  1.00 61.10           C  
ANISOU 1824  C   GLY A 243     4964  10894   7357   1538    738    841       C  
ATOM   1825  O   GLY A 243      99.435  12.074-106.816  1.00 60.18           O  
ANISOU 1825  O   GLY A 243     4976  10694   7195   1417    815    635       O  
ATOM   1826  N   MET A 244     100.851  11.380-105.203  1.00 64.13           N  
ANISOU 1826  N   MET A 244     5348  11157   7862   1649    696   1090       N  
ATOM   1827  CA  MET A 244      99.997  10.286-104.758  1.00 65.93           C  
ANISOU 1827  CA  MET A 244     5738  11094   8217   1647    782   1130       C  
ATOM   1828  C   MET A 244      99.749  10.352-103.259  1.00 66.77           C  
ANISOU 1828  C   MET A 244     5906  11251   8213   1596    642   1414       C  
ATOM   1829  O   MET A 244     100.651  10.679-102.481  1.00 58.10           O  
ANISOU 1829  O   MET A 244     4691  10337   7048   1667    490   1652       O  
ATOM   1830  CB  MET A 244     100.611   8.926-105.112  1.00 68.77           C  
ANISOU 1830  CB  MET A 244     6063  11160   8906   1871    944   1164       C  
ATOM   1831  CG  MET A 244     100.539   8.588-106.590  1.00 76.19           C  
ANISOU 1831  CG  MET A 244     7011  11984   9952   1885   1141    820       C  
ATOM   1832  SD  MET A 244     101.439   7.086-107.017  1.00 86.00           S  
ANISOU 1832  SD  MET A 244     8192  12873  11612   2169   1367    831       S  
ATOM   1833  CE  MET A 244     100.500   5.857-106.121  1.00 84.74           C  
ANISOU 1833  CE  MET A 244     8227  12315  11655   2150   1440    975       C  
ATOM   1834  N   ASP A 245      98.513  10.038-102.868  1.00 68.67           N  
ANISOU 1834  N   ASP A 245     6323  11348   8421   1458    695   1381       N  
ATOM   1835  CA  ASP A 245      98.130   9.777-101.481  1.00 72.04           C  
ANISOU 1835  CA  ASP A 245     6846  11755   8769   1414    627   1650       C  
ATOM   1836  C   ASP A 245      97.618   8.340-101.453  1.00 71.75           C  
ANISOU 1836  C   ASP A 245     6927  11336   9000   1478    800   1704       C  
ATOM   1837  O   ASP A 245      96.493   8.066-101.883  1.00 74.65           O  
ANISOU 1837  O   ASP A 245     7412  11537   9415   1338    926   1495       O  
ATOM   1838  CB  ASP A 245      97.077  10.772-100.989  1.00 76.77           C  
ANISOU 1838  CB  ASP A 245     7543  12526   9098   1176    569   1564       C  
ATOM   1839  CG  ASP A 245      96.691  10.561 -99.525  1.00 85.40           C  
ANISOU 1839  CG  ASP A 245     8745  13640  10062   1113    518   1830       C  
ATOM   1840  OD1 ASP A 245      96.653  11.557 -98.770  1.00 87.84           O  
ANISOU 1840  OD1 ASP A 245     9058  14212  10103    994    395   1870       O  
ATOM   1841  OD2 ASP A 245      96.406   9.413 -99.123  1.00 90.17           O  
ANISOU 1841  OD2 ASP A 245     9439  13994  10827   1172    615   1994       O  
ATOM   1842  N   VAL A 246      98.446   7.424-100.952  1.00 72.73           N  
ANISOU 1842  N   VAL A 246     7004  11313   9316   1686    806   1992       N  
ATOM   1843  CA  VAL A 246      98.095   6.009-100.991  1.00 70.91           C  
ANISOU 1843  CA  VAL A 246     6876  10662   9404   1772    999   2054       C  
ATOM   1844  C   VAL A 246      97.070   5.670 -99.917  1.00 69.50           C  
ANISOU 1844  C   VAL A 246     6870  10386   9149   1630   1019   2241       C  
ATOM   1845  O   VAL A 246      96.128   4.908-100.167  1.00 70.42           O  
ANISOU 1845  O   VAL A 246     7116  10196   9443   1538   1200   2120       O  
ATOM   1846  CB  VAL A 246      99.364   5.145-100.860  1.00 75.79           C  
ANISOU 1846  CB  VAL A 246     7367  11129  10300   2076   1017   2326       C  
ATOM   1847  CG1 VAL A 246      99.000   3.671-100.753  1.00 78.85           C  
ANISOU 1847  CG1 VAL A 246     7874  11036  11048   2170   1231   2437       C  
ATOM   1848  CG2 VAL A 246     100.300   5.383-102.041  1.00 76.60           C  
ANISOU 1848  CG2 VAL A 246     7298  11293  10514   2209   1058   2099       C  
ATOM   1849  N   ALA A 247      97.224   6.238 -98.720  1.00 60.49           N  
ANISOU 1849  N   ALA A 247     5731   9518   7735   1590    844   2520       N  
ATOM   1850  CA  ALA A 247      96.394   5.895 -97.568  1.00 64.34           C  
ANISOU 1850  CA  ALA A 247     6379   9950   8119   1474    870   2754       C  
ATOM   1851  C   ALA A 247      96.415   4.387 -97.327  1.00 71.68           C  
ANISOU 1851  C   ALA A 247     7381  10460   9395   1622   1033   3009       C  
ATOM   1852  O   ALA A 247      95.378   3.728 -97.222  1.00 69.49           O  
ANISOU 1852  O   ALA A 247     7253   9908   9243   1499   1209   2979       O  
ATOM   1853  CB  ALA A 247      94.964   6.412 -97.740  1.00 59.23           C  
ANISOU 1853  CB  ALA A 247     5850   9318   7335   1199    958   2466       C  
ATOM   1854  N   ALA A 248      97.631   3.839 -97.241  1.00 74.47           N  
ANISOU 1854  N   ALA A 248     7611  10754   9932   1894    980   3274       N  
ATOM   1855  CA  ALA A 248      97.808   2.394 -97.152  1.00 76.98           C  
ANISOU 1855  CA  ALA A 248     7973  10624  10654   2085   1154   3518       C  
ATOM   1856  C   ALA A 248      97.288   1.812 -95.843  1.00 81.06           C  
ANISOU 1856  C   ALA A 248     8638  11055  11107   2042   1170   3940       C  
ATOM   1857  O   ALA A 248      97.102   0.593 -95.758  1.00 81.27           O  
ANISOU 1857  O   ALA A 248     8750  10644  11485   2140   1364   4122       O  
ATOM   1858  CB  ALA A 248      99.283   2.034 -97.332  1.00 75.85           C  
ANISOU 1858  CB  ALA A 248     7625  10467  10729   2413   1086   3730       C  
ATOM   1859  N   SER A 249      97.053   2.646 -94.825  1.00 84.34           N  
ANISOU 1859  N   SER A 249     9094  11867  11084   1891    990   4096       N  
ATOM   1860  CA  SER A 249      96.460   2.153 -93.586  1.00 89.94           C  
ANISOU 1860  CA  SER A 249     9965  12535  11675   1815   1026   4478       C  
ATOM   1861  C   SER A 249      95.058   1.600 -93.799  1.00 94.99           C  
ANISOU 1861  C   SER A 249    10788  12824  12480   1608   1297   4291       C  
ATOM   1862  O   SER A 249      94.582   0.811 -92.975  1.00 99.68           O  
ANISOU 1862  O   SER A 249    11519  13220  13135   1583   1414   4623       O  
ATOM   1863  CB  SER A 249      96.422   3.265 -92.536  1.00 85.69           C  
ANISOU 1863  CB  SER A 249     9443  12523  10591   1656    802   4590       C  
ATOM   1864  OG  SER A 249      97.724   3.733 -92.240  1.00 87.54           O  
ANISOU 1864  OG  SER A 249     9496  13099  10668   1821    536   4785       O  
ATOM   1865  N   GLU A 250      94.389   1.989 -94.887  1.00 95.22           N  
ANISOU 1865  N   GLU A 250    10812  12784  12583   1453   1395   3784       N  
ATOM   1866  CA  GLU A 250      93.032   1.513 -95.136  1.00 97.20           C  
ANISOU 1866  CA  GLU A 250    11201  12739  12990   1231   1630   3576       C  
ATOM   1867  C   GLU A 250      93.010   0.052 -95.568  1.00100.97           C  
ANISOU 1867  C   GLU A 250    11734  12649  13980   1341   1871   3635       C  
ATOM   1868  O   GLU A 250      92.035  -0.655 -95.291  1.00101.32           O  
ANISOU 1868  O   GLU A 250    11914  12400  14185   1187   2072   3679       O  
ATOM   1869  CB  GLU A 250      92.360   2.386 -96.196  1.00 91.61           C  
ANISOU 1869  CB  GLU A 250    10443  12167  12197   1040   1632   3034       C  
ATOM   1870  CG  GLU A 250      92.247   3.853 -95.813  1.00 86.50           C  
ANISOU 1870  CG  GLU A 250     9752  12018  11096    914   1439   2944       C  
ATOM   1871  CD  GLU A 250      91.348   4.071 -94.613  1.00 86.22           C  
ANISOU 1871  CD  GLU A 250     9841  12113  10805    725   1475   3131       C  
ATOM   1872  OE1 GLU A 250      90.273   3.439 -94.556  1.00 85.62           O  
ANISOU 1872  OE1 GLU A 250     9864  11778  10891    573   1679   3093       O  
ATOM   1873  OE2 GLU A 250      91.720   4.866 -93.724  1.00 88.15           O  
ANISOU 1873  OE2 GLU A 250    10083  12725  10685    716   1312   3303       O  
ATOM   1874  N   PHE A 251      94.058  -0.422 -96.246  1.00104.59           N  
ANISOU 1874  N   PHE A 251    12088  12929  14721   1598   1876   3626       N  
ATOM   1875  CA  PHE A 251      94.074  -1.784 -96.769  1.00108.06           C  
ANISOU 1875  CA  PHE A 251    12579  12791  15687   1708   2135   3615       C  
ATOM   1876  C   PHE A 251      95.256  -2.602 -96.247  1.00112.68           C  
ANISOU 1876  C   PHE A 251    13105  13184  16523   2058   2126   4106       C  
ATOM   1877  O   PHE A 251      95.736  -3.517 -96.922  1.00111.50           O  
ANISOU 1877  O   PHE A 251    12927  12612  16828   2246   2304   4045       O  
ATOM   1878  CB  PHE A 251      94.042  -1.778 -98.300  1.00106.68           C  
ANISOU 1878  CB  PHE A 251    12345  12475  15714   1673   2239   3049       C  
ATOM   1879  CG  PHE A 251      95.100  -0.917 -98.951  1.00101.66           C  
ANISOU 1879  CG  PHE A 251    11529  12182  14914   1830   2055   2890       C  
ATOM   1880  CD1 PHE A 251      94.782   0.341 -99.441  1.00 94.92           C  
ANISOU 1880  CD1 PHE A 251    10619  11746  13700   1654   1905   2555       C  
ATOM   1881  CD2 PHE A 251      96.399  -1.380 -99.110  1.00102.08           C  
ANISOU 1881  CD2 PHE A 251    11458  12121  15207   2157   2053   3078       C  
ATOM   1882  CE1 PHE A 251      95.744   1.130-100.052  1.00 92.39           C  
ANISOU 1882  CE1 PHE A 251    10136  11722  13245   1781   1758   2421       C  
ATOM   1883  CE2 PHE A 251      97.365  -0.593 -99.719  1.00 97.16           C  
ANISOU 1883  CE2 PHE A 251    10655  11815  14448   2286   1905   2930       C  
ATOM   1884  CZ  PHE A 251      97.035   0.662-100.191  1.00 92.59           C  
ANISOU 1884  CZ  PHE A 251    10035  11647  13496   2088   1760   2601       C  
ATOM   1885  N   TYR A 252      95.719  -2.293 -95.039  1.00119.38           N  
ANISOU 1885  N   TYR A 252    12802  14503  18055    509   1574   4389       N  
ATOM   1886  CA  TYR A 252      96.702  -3.109 -94.332  1.00126.72           C  
ANISOU 1886  CA  TYR A 252    13903  15004  19240    589   1415   4732       C  
ATOM   1887  C   TYR A 252      95.963  -4.266 -93.668  1.00134.40           C  
ANISOU 1887  C   TYR A 252    14902  15711  20453    210   1395   5198       C  
ATOM   1888  O   TYR A 252      95.273  -4.074 -92.661  1.00135.35           O  
ANISOU 1888  O   TYR A 252    14970  16199  20258     23   1506   5602       O  
ATOM   1889  CB  TYR A 252      97.445  -2.243 -93.314  1.00127.23           C  
ANISOU 1889  CB  TYR A 252    14036  15411  18896    835   1403   4960       C  
ATOM   1890  CG  TYR A 252      98.575  -2.904 -92.541  1.00131.80           C  
ANISOU 1890  CG  TYR A 252    14778  15629  19672    978   1216   5308       C  
ATOM   1891  CD1 TYR A 252      98.636  -2.809 -91.155  1.00133.67           C  
ANISOU 1891  CD1 TYR A 252    15093  16084  19612    953   1198   5812       C  
ATOM   1892  CD2 TYR A 252      99.591  -3.597 -93.190  1.00133.35           C  
ANISOU 1892  CD2 TYR A 252    15043  15300  20322   1169   1053   5125       C  
ATOM   1893  CE1 TYR A 252      99.665  -3.393 -90.437  1.00136.01           C  
ANISOU 1893  CE1 TYR A 252    15537  16070  20071   1096   1003   6146       C  
ATOM   1894  CE2 TYR A 252     100.628  -4.188 -92.474  1.00135.40           C  
ANISOU 1894  CE2 TYR A 252    15434  15244  20767   1335    864   5446       C  
ATOM   1895  CZ  TYR A 252     100.655  -4.082 -91.099  1.00135.86           C  
ANISOU 1895  CZ  TYR A 252    15572  15515  20533   1289    830   5966       C  
ATOM   1896  OH  TYR A 252     101.671  -4.663 -90.376  1.00136.53           O  
ANISOU 1896  OH  TYR A 252    15787  15301  20788   1460    618   6302       O  
ATOM   1897  N   ARG A 253      96.092  -5.466 -94.234  1.00139.02           N  
ANISOU 1897  N   ARG A 253    15572  15660  21589     93   1249   5141       N  
ATOM   1898  CA  ARG A 253      95.341  -6.633 -93.782  1.00144.89           C  
ANISOU 1898  CA  ARG A 253    16350  16063  22638   -324   1199   5555       C  
ATOM   1899  C   ARG A 253      96.297  -7.783 -93.497  1.00146.64           C  
ANISOU 1899  C   ARG A 253    16810  15573  23333   -236    955   5797       C  
ATOM   1900  O   ARG A 253      97.068  -8.184 -94.376  1.00146.94           O  
ANISOU 1900  O   ARG A 253    16938  15157  23735      6    811   5409       O  
ATOM   1901  CB  ARG A 253      94.302  -7.053 -94.827  1.00147.54           C  
ANISOU 1901  CB  ARG A 253    16561  16264  23234   -632   1222   5230       C  
ATOM   1902  CG  ARG A 253      93.205  -6.031 -95.094  1.00145.32           C  
ANISOU 1902  CG  ARG A 253    16019  16674  22522   -748   1444   5031       C  
ATOM   1903  CD  ARG A 253      92.154  -6.020 -93.991  1.00148.70           C  
ANISOU 1903  CD  ARG A 253    16304  17518  22679  -1102   1598   5569       C  
ATOM   1904  NE  ARG A 253      90.972  -5.252 -94.375  1.00147.15           N  
ANISOU 1904  NE  ARG A 253    15824  17915  22172  -1239   1787   5350       N  
ATOM   1905  CZ  ARG A 253      90.764  -3.981 -94.045  1.00142.91           C  
ANISOU 1905  CZ  ARG A 253    15165  18055  21079  -1020   1962   5275       C  
ATOM   1906  NH1 ARG A 253      91.659  -3.329 -93.316  1.00140.25           N  
ANISOU 1906  NH1 ARG A 253    14974  17885  20431   -685   1966   5398       N  
ATOM   1907  NH2 ARG A 253      89.660  -3.362 -94.440  1.00141.16           N  
ANISOU 1907  NH2 ARG A 253    14679  18333  20620  -1127   2111   5068       N  
ATOM   1908  N   ASP A 254      96.242  -8.306 -92.269  1.00149.19           N  
ANISOU 1908  N   ASP A 254    17233  15820  23633   -413    909   6441       N  
ATOM   1909  CA  ASP A 254      96.960  -9.523 -91.879  1.00151.62           C  
ANISOU 1909  CA  ASP A 254    17782  15414  24413   -395    654   6778       C  
ATOM   1910  C   ASP A 254      98.472  -9.381 -92.033  1.00147.50           C  
ANISOU 1910  C   ASP A 254    17376  14676  23990    133    496   6566       C  
ATOM   1911  O   ASP A 254      99.163 -10.342 -92.383  1.00152.03           O  
ANISOU 1911  O   ASP A 254    18113  14575  25076    279    271   6501       O  
ATOM   1912  CB  ASP A 254      96.455 -10.734 -92.670  1.00154.09           C  
ANISOU 1912  CB  ASP A 254    18171  15043  25335   -686    510   6646       C  
ATOM   1913  CG  ASP A 254      94.983 -11.013 -92.428  1.00155.96           C  
ANISOU 1913  CG  ASP A 254    18272  15455  25531  -1268    634   6942       C  
ATOM   1914  OD1 ASP A 254      94.469 -12.021 -92.960  1.00159.92           O  
ANISOU 1914  OD1 ASP A 254    18834  15402  26526  -1587    495   6900       O  
ATOM   1915  OD2 ASP A 254      94.341 -10.227 -91.698  1.00154.29           O  
ANISOU 1915  OD2 ASP A 254    17885  15945  24795  -1403    862   7210       O  
ATOM   1916  N   GLY A 255      99.001  -8.185 -91.767  1.00139.37           N  
ANISOU 1916  N   GLY A 255    16256  14214  22482    427    599   6453       N  
ATOM   1917  CA  GLY A 255     100.418  -7.922 -91.879  1.00134.27           C  
ANISOU 1917  CA  GLY A 255    15661  13472  21884    899    465   6268       C  
ATOM   1918  C   GLY A 255     100.892  -7.541 -93.266  1.00129.63           C  
ANISOU 1918  C   GLY A 255    14974  12848  21432   1169    492   5574       C  
ATOM   1919  O   GLY A 255     101.998  -7.007 -93.403  1.00126.54           O  
ANISOU 1919  O   GLY A 255    14546  12574  20960   1546    443   5383       O  
ATOM   1920  N   LYS A 256     100.090  -7.794 -94.292  1.00129.92           N  
ANISOU 1920  N   LYS A 256    14952  12755  21656    977    566   5203       N  
ATOM   1921  CA  LYS A 256     100.396  -7.454 -95.673  1.00126.25           C  
ANISOU 1921  CA  LYS A 256    14395  12298  21277   1199    610   4540       C  
ATOM   1922  C   LYS A 256      99.476  -6.321 -96.124  1.00126.18           C  
ANISOU 1922  C   LYS A 256    14208  12910  20825   1052    839   4278       C  
ATOM   1923  O   LYS A 256      98.706  -5.767 -95.335  1.00123.40           O  
ANISOU 1923  O   LYS A 256    13795  12989  20101    836    961   4586       O  
ATOM   1924  CB  LYS A 256     100.260  -8.699 -96.551  1.00126.94           C  
ANISOU 1924  CB  LYS A 256    14587  11706  21940   1134    468   4279       C  
ATOM   1925  CG  LYS A 256     100.122  -9.974 -95.728  1.00131.91           C  
ANISOU 1925  CG  LYS A 256    15415  11739  22965    922    272   4795       C  
ATOM   1926  CD  LYS A 256      99.849 -11.219 -96.567  1.00135.70           C  
ANISOU 1926  CD  LYS A 256    16032  11494  24033    806    100   4536       C  
ATOM   1927  CE  LYS A 256      98.948 -12.195 -95.799  1.00139.96           C  
ANISOU 1927  CE  LYS A 256    16707  11646  24826    315     -8   5089       C  
ATOM   1928  NZ  LYS A 256      98.401 -13.274 -96.668  1.00142.42           N  
ANISOU 1928  NZ  LYS A 256    17136  11308  25668     90   -172   4806       N  
ATOM   1929  N   TYR A 257      99.563  -5.967 -97.405  1.00127.65           N  
ANISOU 1929  N   TYR A 257    14309  13158  21034   1195    894   3702       N  
ATOM   1930  CA  TYR A 257      98.772  -4.882 -97.975  1.00127.14           C  
ANISOU 1930  CA  TYR A 257    14088  13648  20574   1107   1080   3412       C  
ATOM   1931  C   TYR A 257      97.922  -5.422 -99.117  1.00129.69           C  
ANISOU 1931  C   TYR A 257    14371  13765  21141    906   1083   3023       C  
ATOM   1932  O   TYR A 257      98.434  -6.104-100.011  1.00132.84           O  
ANISOU 1932  O   TYR A 257    14837  13744  21894   1057    978   2671       O  
ATOM   1933  CB  TYR A 257      99.675  -3.736 -98.444  1.00122.75           C  
ANISOU 1933  CB  TYR A 257    13459  13459  19720   1459   1142   3107       C  
ATOM   1934  CG  TYR A 257     100.415  -3.077 -97.298  1.00119.75           C  
ANISOU 1934  CG  TYR A 257    13106  13335  19057   1617   1119   3472       C  
ATOM   1935  CD1 TYR A 257      99.871  -1.989 -96.627  1.00116.40           C  
ANISOU 1935  CD1 TYR A 257    12634  13450  18142   1536   1231   3640       C  
ATOM   1936  CD2 TYR A 257     101.646  -3.557 -96.872  1.00118.90           C  
ANISOU 1936  CD2 TYR A 257    13073  12931  19173   1862    967   3636       C  
ATOM   1937  CE1 TYR A 257     100.538  -1.389 -95.573  1.00113.75           C  
ANISOU 1937  CE1 TYR A 257    12345  13341  17533   1679   1182   3942       C  
ATOM   1938  CE2 TYR A 257     102.319  -2.964 -95.817  1.00116.77           C  
ANISOU 1938  CE2 TYR A 257    12824  12905  18638   1994    915   3964       C  
ATOM   1939  CZ  TYR A 257     101.760  -1.880 -95.172  1.00112.69           C  
ANISOU 1939  CZ  TYR A 257    12280  12913  17622   1891   1018   4108       C  
ATOM   1940  OH  TYR A 257     102.422  -1.285 -94.120  1.00108.48           O  
ANISOU 1940  OH  TYR A 257    11791  12619  16810   2022    941   4402       O  
ATOM   1941  N   ASP A 258      96.627  -5.118 -99.075  1.00130.85           N  
ANISOU 1941  N   ASP A 258    14401  14230  21087    582   1194   3076       N  
ATOM   1942  CA  ASP A 258      95.626  -5.696 -99.968  1.00133.32           C  
ANISOU 1942  CA  ASP A 258    14657  14369  21629    301   1170   2795       C  
ATOM   1943  C   ASP A 258      95.075  -4.600-100.868  1.00125.77           C  
ANISOU 1943  C   ASP A 258    13535  13947  20305    353   1306   2376       C  
ATOM   1944  O   ASP A 258      94.189  -3.843-100.463  1.00125.93           O  
ANISOU 1944  O   ASP A 258    13410  14468  19970    199   1438   2524       O  
ATOM   1945  CB  ASP A 258      94.508  -6.354 -99.161  1.00138.46           C  
ANISOU 1945  CB  ASP A 258    15269  14949  22391   -164   1167   3249       C  
ATOM   1946  CG  ASP A 258      93.395  -6.916-100.038  1.00141.54           C  
ANISOU 1946  CG  ASP A 258    15567  15196  23016   -509   1122   2979       C  
ATOM   1947  OD1 ASP A 258      93.601  -7.047-101.263  1.00142.07           O  
ANISOU 1947  OD1 ASP A 258    15663  15077  23240   -369   1047   2438       O  
ATOM   1948  OD2 ASP A 258      92.321  -7.256 -99.493  1.00144.02           O  
ANISOU 1948  OD2 ASP A 258    15771  15594  23356   -931   1153   3317       O  
ATOM   1949  N   LEU A 259      95.573  -4.530-102.099  1.00116.85           N  
ANISOU 1949  N   LEU A 259    12425  12720  19252    579   1272   1854       N  
ATOM   1950  CA  LEU A 259      95.042  -3.576-103.057  1.00105.22           C  
ANISOU 1950  CA  LEU A 259    10818  11709  17452    620   1372   1456       C  
ATOM   1951  C   LEU A 259      93.855  -4.134-103.840  1.00111.05           C  
ANISOU 1951  C   LEU A 259    11475  12358  18361    305   1318   1205       C  
ATOM   1952  O   LEU A 259      93.500  -3.592-104.891  1.00106.47           O  
ANISOU 1952  O   LEU A 259    10812  12046  17596    361   1348    788       O  
ATOM   1953  CB  LEU A 259      96.153  -3.076-103.986  1.00 94.35           C  
ANISOU 1953  CB  LEU A 259     9482  10385  15983   1012   1385   1050       C  
ATOM   1954  CG  LEU A 259      96.965  -3.979-104.901  1.00 91.60           C  
ANISOU 1954  CG  LEU A 259     9239   9564  16003   1208   1276    676       C  
ATOM   1955  CD1 LEU A 259      96.359  -3.901-106.283  1.00 90.35           C  
ANISOU 1955  CD1 LEU A 259     9026   9522  15783   1168   1277    150       C  
ATOM   1956  CD2 LEU A 259      98.395  -3.493-104.925  1.00 85.53           C  
ANISOU 1956  CD2 LEU A 259     8490   8877  15133   1606   1314    632       C  
ATOM   1957  N   ASP A 260      93.235  -5.197-103.334  1.00117.75           N  
ANISOU 1957  N   ASP A 260    12346  12841  19554    -43   1223   1473       N  
ATOM   1958  CA  ASP A 260      91.921  -5.666-103.755  1.00125.90           C  
ANISOU 1958  CA  ASP A 260    13251  13862  20725   -447   1171   1377       C  
ATOM   1959  C   ASP A 260      91.000  -5.721-102.543  1.00122.60           C  
ANISOU 1959  C   ASP A 260    12696  13655  20231   -811   1250   1943       C  
ATOM   1960  O   ASP A 260      90.264  -6.687-102.340  1.00129.20           O  
ANISOU 1960  O   ASP A 260    13503  14190  21398  -1220   1153   2136       O  
ATOM   1961  CB  ASP A 260      92.017  -7.031-104.439  1.00136.04           C  
ANISOU 1961  CB  ASP A 260    14690  14441  22556   -574    946   1123       C  
ATOM   1962  CG  ASP A 260      91.045  -7.180-105.597  1.00140.77           C  
ANISOU 1962  CG  ASP A 260    15180  15099  23208   -789    864    667       C  
ATOM   1963  OD1 ASP A 260      90.379  -6.186-105.958  1.00138.75           O  
ANISOU 1963  OD1 ASP A 260    14722  15444  22553   -791    984    526       O  
ATOM   1964  OD2 ASP A 260      90.960  -8.293-106.159  1.00146.61           O  
ANISOU 1964  OD2 ASP A 260    16048  15269  24389   -940    655    435       O  
ATOM   1965  N   PHE A 261      91.045  -4.675-101.709  1.00112.92           N  
ANISOU 1965  N   PHE A 261    11385  12960  18558   -670   1426   2221       N  
ATOM   1966  CA  PHE A 261      90.414  -4.728-100.393  1.00111.56           C  
ANISOU 1966  CA  PHE A 261    11113  13009  18266   -934   1525   2801       C  
ATOM   1967  C   PHE A 261      88.906  -4.511-100.433  1.00113.75           C  
ANISOU 1967  C   PHE A 261    11092  13736  18392  -1284   1620   2844       C  
ATOM   1968  O   PHE A 261      88.251  -4.670 -99.398  1.00113.55           O  
ANISOU 1968  O   PHE A 261    10939  13921  18282  -1555   1717   3327       O  
ATOM   1969  CB  PHE A 261      91.077  -3.717 -99.439  1.00103.85           C  
ANISOU 1969  CB  PHE A 261    10181  12424  16854   -621   1657   3057       C  
ATOM   1970  CG  PHE A 261      90.529  -2.309 -99.528  1.00 97.30           C  
ANISOU 1970  CG  PHE A 261     9175  12301  15495   -468   1819   2899       C  
ATOM   1971  CD1 PHE A 261      89.455  -1.913 -98.741  1.00 94.28           C  
ANISOU 1971  CD1 PHE A 261     8582  12425  14816   -661   1969   3196       C  
ATOM   1972  CD2 PHE A 261      91.117  -1.369-100.362  1.00 91.20           C  
ANISOU 1972  CD2 PHE A 261     8451  11690  14510   -114   1820   2473       C  
ATOM   1973  CE1 PHE A 261      88.957  -0.622 -98.807  1.00 88.48           C  
ANISOU 1973  CE1 PHE A 261     7701  12310  13607   -471   2097   3033       C  
ATOM   1974  CE2 PHE A 261      90.622  -0.071-100.431  1.00 87.34           C  
ANISOU 1974  CE2 PHE A 261     7836  11793  13555     38   1936   2345       C  
ATOM   1975  CZ  PHE A 261      89.541   0.301 -99.651  1.00 85.74           C  
ANISOU 1975  CZ  PHE A 261     7439  12057  13082   -121   2065   2609       C  
ATOM   1976  N   LYS A 262      88.339  -4.160-101.588  1.00113.62           N  
ANISOU 1976  N   LYS A 262    10943  13902  18324  -1282   1594   2365       N  
ATOM   1977  CA  LYS A 262      86.891  -4.080-101.727  1.00115.99           C  
ANISOU 1977  CA  LYS A 262    10929  14594  18547  -1627   1645   2377       C  
ATOM   1978  C   LYS A 262      86.260  -5.451-101.927  1.00128.71           C  
ANISOU 1978  C   LYS A 262    12503  15726  20674  -2126   1481   2460       C  
ATOM   1979  O   LYS A 262      85.037  -5.546-102.093  1.00131.31           O  
ANISOU 1979  O   LYS A 262    12543  16334  21013  -2480   1491   2475       O  
ATOM   1980  CB  LYS A 262      86.535  -3.127-102.884  1.00107.35           C  
ANISOU 1980  CB  LYS A 262     9713  13899  17178  -1413   1654   1843       C  
ATOM   1981  CG  LYS A 262      86.262  -3.760-104.262  1.00106.79           C  
ANISOU 1981  CG  LYS A 262     9648  13510  17418  -1549   1457   1348       C  
ATOM   1982  CD  LYS A 262      87.345  -4.720-104.748  1.00105.56           C  
ANISOU 1982  CD  LYS A 262     9809  12622  17676  -1454   1283   1148       C  
ATOM   1983  CE  LYS A 262      86.707  -5.828-105.572  1.00107.88           C  
ANISOU 1983  CE  LYS A 262    10084  12497  18407  -1817   1062    884       C  
ATOM   1984  NZ  LYS A 262      87.635  -6.955-105.843  1.00106.29           N  
ANISOU 1984  NZ  LYS A 262    10197  11514  18674  -1767    874    753       N  
ATOM   1985  N   SER A 263      87.069  -6.498-101.906  1.00134.97           N  
ANISOU 1985  N   SER A 263    13576  15802  21903  -2155   1314   2516       N  
ATOM   1986  CA  SER A 263      86.705  -7.862-102.248  1.00144.48           C  
ANISOU 1986  CA  SER A 263    14846  16380  23671  -2572   1089   2509       C  
ATOM   1987  C   SER A 263      86.404  -8.653-100.988  1.00147.07           C  
ANISOU 1987  C   SER A 263    15169  16509  24203  -2972   1100   3200       C  
ATOM   1988  O   SER A 263      86.672  -8.198 -99.872  1.00147.13           O  
ANISOU 1988  O   SER A 263    15169  16821  23915  -2858   1275   3650       O  
ATOM   1989  CB  SER A 263      87.849  -8.518-103.021  1.00147.99           C  
ANISOU 1989  CB  SER A 263    15634  16124  24470  -2293    881   2117       C  
ATOM   1990  OG  SER A 263      88.955  -8.768-102.170  1.00147.99           O  
ANISOU 1990  OG  SER A 263    15875  15805  24551  -2063    886   2454       O  
ATOM   1991  N   PRO A 264      85.840  -9.854-101.116  1.00147.94           N  
ANISOU 1991  N   PRO A 264    15293  16107  24812  -3462    903   3315       N  
ATOM   1992  CA  PRO A 264      85.777 -10.730 -99.943  1.00149.23           C  
ANISOU 1992  CA  PRO A 264    15532  15945  25225  -3826    877   4006       C  
ATOM   1993  C   PRO A 264      87.189 -11.113 -99.534  1.00147.50           C  
ANISOU 1993  C   PRO A 264    15707  15165  25171  -3458    781   4126       C  
ATOM   1994  O   PRO A 264      87.997 -11.520-100.372  1.00146.06           O  
ANISOU 1994  O   PRO A 264    15781  14431  25282  -3182    586   3672       O  
ATOM   1995  CB  PRO A 264      84.976 -11.938-100.440  1.00155.80           C  
ANISOU 1995  CB  PRO A 264    16343  16237  26619  -4405    621   3980       C  
ATOM   1996  CG  PRO A 264      85.232 -11.965-101.904  1.00154.43           C  
ANISOU 1996  CG  PRO A 264    16283  15788  26606  -4169    432   3197       C  
ATOM   1997  CD  PRO A 264      85.240 -10.506-102.301  1.00147.73           C  
ANISOU 1997  CD  PRO A 264    15235  15743  25154  -3735    668   2849       C  
ATOM   1998  N   THR A 265      87.488 -10.953 -98.243  1.00147.57           N  
ANISOU 1998  N   THR A 265    15745  15363  24961  -3427    922   4728       N  
ATOM   1999  CA  THR A 265      88.836 -11.177 -97.721  1.00147.20           C  
ANISOU 1999  CA  THR A 265    16030  14901  24998  -3046    843   4895       C  
ATOM   2000  C   THR A 265      89.414 -12.483 -98.248  1.00158.44           C  
ANISOU 2000  C   THR A 265    17777  15336  27085  -3085    513   4743       C  
ATOM   2001  O   THR A 265      88.815 -13.549 -98.087  1.00163.23           O  
ANISOU 2001  O   THR A 265    18433  15464  28124  -3581    344   5030       O  
ATOM   2002  CB  THR A 265      88.812 -11.181 -96.192  1.00145.13           C  
ANISOU 2002  CB  THR A 265    15760  14874  24511  -3189    976   5669       C  
ATOM   2003  OG1 THR A 265      88.550  -9.855 -95.717  1.00138.02           O  
ANISOU 2003  OG1 THR A 265    14621  14870  22951  -2988   1270   5711       O  
ATOM   2004  CG2 THR A 265      90.143 -11.660 -95.639  1.00145.01           C  
ANISOU 2004  CG2 THR A 265    16097  14317  24683  -2869    824   5896       C  
ATOM   2005  N   ASP A 266      90.563 -12.385 -98.912  1.00160.85           N  
ANISOU 2005  N   ASP A 266    18296  15348  27474  -2560    416   4274       N  
ATOM   2006  CA  ASP A 266      91.178 -13.527 -99.572  1.00171.74           C  
ANISOU 2006  CA  ASP A 266    19980  15824  29450  -2479    105   3989       C  
ATOM   2007  C   ASP A 266      92.698 -13.445 -99.474  1.00171.54           C  
ANISOU 2007  C   ASP A 266    20186  15554  29438  -1872     56   3884       C  
ATOM   2008  O   ASP A 266      93.303 -12.499 -99.993  1.00166.69           O  
ANISOU 2008  O   ASP A 266    19496  15357  28481  -1424    194   3472       O  
ATOM   2009  CB  ASP A 266      90.729 -13.593-101.032  1.00173.43           C  
ANISOU 2009  CB  ASP A 266    20137  15950  29806  -2507      7   3261       C  
ATOM   2010  CG  ASP A 266      91.774 -14.195-101.940  1.00175.68           C  
ANISOU 2010  CG  ASP A 266    20715  15581  30456  -2086   -217   2714       C  
ATOM   2011  OD1 ASP A 266      92.594 -13.423-102.481  1.00171.41           O  
ANISOU 2011  OD1 ASP A 266    20159  15343  29625  -1564   -102   2300       O  
ATOM   2012  OD2 ASP A 266      91.772 -15.431-102.121  1.00182.21           O  
ANISOU 2012  OD2 ASP A 266    21782  15598  31853  -2275   -510   2695       O  
ATOM   2013  N   PRO A 267      93.345 -14.411 -98.814  1.00177.00           N  
ANISOU 2013  N   PRO A 267    21148  15582  30521  -1847   -147   4266       N  
ATOM   2014  CA  PRO A 267      94.813 -14.370 -98.679  1.00174.65           C  
ANISOU 2014  CA  PRO A 267    21038  15066  30256  -1255   -211   4187       C  
ATOM   2015  C   PRO A 267      95.590 -14.352-100.002  1.00171.07           C  
ANISOU 2015  C   PRO A 267    20655  14401  29944   -778   -289   3398       C  
ATOM   2016  O   PRO A 267      96.817 -14.194 -99.959  1.00170.09           O  
ANISOU 2016  O   PRO A 267    20615  14211  29800   -263   -307   3295       O  
ATOM   2017  CB  PRO A 267      95.132 -15.651 -97.888  1.00181.67           C  
ANISOU 2017  CB  PRO A 267    22221  15150  31656  -1397   -483   4713       C  
ATOM   2018  CG  PRO A 267      93.829 -16.134 -97.309  1.00185.96           C  
ANISOU 2018  CG  PRO A 267    22697  15665  32295  -2103   -488   5233       C  
ATOM   2019  CD  PRO A 267      92.704 -15.291 -97.823  1.00182.52           C  
ANISOU 2019  CD  PRO A 267    21922  15945  31483  -2379   -252   4972       C  
ATOM   2020  N   SER A 268      94.937 -14.497-101.159  1.00169.27           N  
ANISOU 2020  N   SER A 268    20378  14104  29833   -924   -335   2847       N  
ATOM   2021  CA  SER A 268      95.662 -14.818-102.390  1.00165.65           C  
ANISOU 2021  CA  SER A 268    20051  13284  29604   -504   -467   2126       C  
ATOM   2022  C   SER A 268      96.397 -13.635-103.014  1.00154.19           C  
ANISOU 2022  C   SER A 268    18434  12472  27678     -2   -239   1687       C  
ATOM   2023  O   SER A 268      97.276 -13.851-103.855  1.00154.05           O  
ANISOU 2023  O   SER A 268    18514  12218  27799    443   -312   1173       O  
ATOM   2024  CB  SER A 268      94.708 -15.417-103.430  1.00168.37           C  
ANISOU 2024  CB  SER A 268    20422  13327  30224   -840   -625   1667       C  
ATOM   2025  OG  SER A 268      95.167 -15.186-104.753  1.00166.25           O  
ANISOU 2025  OG  SER A 268    20160  13124  29885   -438   -624    889       O  
ATOM   2026  N   ARG A 269      96.074 -12.399-102.641  1.00145.47           N  
ANISOU 2026  N   ARG A 269    17086  12166  26019    -52     28   1871       N  
ATOM   2027  CA  ARG A 269      96.636 -11.252-103.340  1.00136.22           C  
ANISOU 2027  CA  ARG A 269    15763  11585  24409    350    224   1448       C  
ATOM   2028  C   ARG A 269      97.506 -10.342-102.482  1.00131.86           C  
ANISOU 2028  C   ARG A 269    15136  11469  23494    646    381   1784       C  
ATOM   2029  O   ARG A 269      98.183  -9.470-103.037  1.00126.14           O  
ANISOU 2029  O   ARG A 269    14313  11149  22466   1004    511   1459       O  
ATOM   2030  CB  ARG A 269      95.510 -10.415-103.978  1.00131.44           C  
ANISOU 2030  CB  ARG A 269    14936  11573  23431     96    378   1200       C  
ATOM   2031  CG  ARG A 269      95.950  -9.639-105.220  1.00127.43           C  
ANISOU 2031  CG  ARG A 269    14347  11436  22636    461    483    571       C  
ATOM   2032  CD  ARG A 269      96.192  -8.157-104.942  1.00121.81           C  
ANISOU 2032  CD  ARG A 269    13453  11483  21347    644    730    686       C  
ATOM   2033  NE  ARG A 269      96.953  -7.528-106.018  1.00120.78           N  
ANISOU 2033  NE  ARG A 269    13284  11611  20995   1044    812    171       N  
ATOM   2034  CZ  ARG A 269      96.411  -7.089-107.148  1.00119.85           C  
ANISOU 2034  CZ  ARG A 269    13079  11791  20666   1022    860   -290       C  
ATOM   2035  NH1 ARG A 269      97.171  -6.537-108.083  1.00116.11           N  
ANISOU 2035  NH1 ARG A 269    12577  11565  19974   1384    944   -705       N  
ATOM   2036  NH2 ARG A 269      95.107  -7.221-107.349  1.00120.64           N  
ANISOU 2036  NH2 ARG A 269    13109  11958  20773    630    817   -322       N  
ATOM   2037  N   TYR A 270      97.531 -10.515-101.164  1.00133.32           N  
ANISOU 2037  N   TYR A 270    15370  11592  23693    500    360   2423       N  
ATOM   2038  CA  TYR A 270      98.234  -9.568-100.308  1.00128.47           C  
ANISOU 2038  CA  TYR A 270    14679  11452  22683    738    495   2736       C  
ATOM   2039  C   TYR A 270      99.742  -9.732-100.448  1.00129.55           C  
ANISOU 2039  C   TYR A 270    14899  11346  22977   1253    403   2583       C  
ATOM   2040  O   TYR A 270     100.254 -10.853-100.529  1.00133.39           O  
ANISOU 2040  O   TYR A 270    15564  11171  23946   1379    194   2557       O  
ATOM   2041  CB  TYR A 270      97.852  -9.749 -98.840  1.00128.07           C  
ANISOU 2041  CB  TYR A 270    14667  11423  22570    452    488   3464       C  
ATOM   2042  CG  TYR A 270      96.393  -9.975 -98.512  1.00129.42           C  
ANISOU 2042  CG  TYR A 270    14762  11693  22718   -101    539   3740       C  
ATOM   2043  CD1 TYR A 270      95.381  -9.615 -99.389  1.00128.06           C  
ANISOU 2043  CD1 TYR A 270    14426  11806  22426   -319    636   3366       C  
ATOM   2044  CD2 TYR A 270      96.032 -10.542 -97.296  1.00133.00           C  
ANISOU 2044  CD2 TYR A 270    15288  11994  23252   -410    491   4407       C  
ATOM   2045  CE1 TYR A 270      94.059  -9.824 -99.069  1.00129.07           C  
ANISOU 2045  CE1 TYR A 270    14434  12067  22541   -828    683   3633       C  
ATOM   2046  CE2 TYR A 270      94.709 -10.752 -96.969  1.00134.92           C  
ANISOU 2046  CE2 TYR A 270    15419  12380  23465   -935    558   4695       C  
ATOM   2047  CZ  TYR A 270      93.729 -10.390 -97.862  1.00132.50           C  
ANISOU 2047  CZ  TYR A 270    14919  12365  23062  -1140    655   4298       C  
ATOM   2048  OH  TYR A 270      92.407 -10.590 -97.560  1.00134.18           O  
ANISOU 2048  OH  TYR A 270    14968  12765  23251  -1665    722   4578       O  
ATOM   2049  N   ILE A 271     100.459  -8.605-100.460  1.00124.47           N  
ANISOU 2049  N   ILE A 271    14120  11240  21934   1552    548   2490       N  
ATOM   2050  CA  ILE A 271     101.910  -8.611-100.589  1.00123.45           C  
ANISOU 2050  CA  ILE A 271    13995  11008  21901   2035    488   2355       C  
ATOM   2051  C   ILE A 271     102.526  -7.812 -99.446  1.00116.24           C  
ANISOU 2051  C   ILE A 271    13022  10483  20662   2143    530   2804       C  
ATOM   2052  O   ILE A 271     101.868  -7.006 -98.784  1.00112.00           O  
ANISOU 2052  O   ILE A 271    12423  10402  19730   1910    650   3084       O  
ATOM   2053  CB  ILE A 271     102.391  -8.056-101.952  1.00122.75           C  
ANISOU 2053  CB  ILE A 271    13778  11181  21681   2331    601   1713       C  
ATOM   2054  CG1 ILE A 271     102.567  -6.537-101.890  1.00118.65           C  
ANISOU 2054  CG1 ILE A 271    13076  11400  20606   2394    798   1721       C  
ATOM   2055  CG2 ILE A 271     101.415  -8.425-103.063  1.00123.37           C  
ANISOU 2055  CG2 ILE A 271    13880  11128  21865   2124    610   1266       C  
ATOM   2056  CD1 ILE A 271     102.938  -5.914-103.219  1.00115.67           C  
ANISOU 2056  CD1 ILE A 271    12569  11334  20048   2622    925   1156       C  
ATOM   2057  N   THR A 272     103.813  -8.056 -99.228  1.00115.05           N  
ANISOU 2057  N   THR A 272    12884  10152  20680   2523    417   2848       N  
ATOM   2058  CA  THR A 272     104.600  -7.435 -98.176  1.00110.13           C  
ANISOU 2058  CA  THR A 272    12211   9823  19811   2675    394   3244       C  
ATOM   2059  C   THR A 272     105.013  -6.012 -98.579  1.00109.25           C  
ANISOU 2059  C   THR A 272    11899  10370  19242   2820    566   2997       C  
ATOM   2060  O   THR A 272     105.040  -5.660 -99.761  1.00105.97           O  
ANISOU 2060  O   THR A 272    11379  10111  18772   2917    682   2503       O  
ATOM   2061  CB  THR A 272     105.813  -8.333 -97.873  1.00110.92           C  
ANISOU 2061  CB  THR A 272    12380   9447  20319   3034    175   3362       C  
ATOM   2062  OG1 THR A 272     105.380  -9.491 -97.145  1.00115.92           O  
ANISOU 2062  OG1 THR A 272    13236   9508  21302   2842     -9   3769       O  
ATOM   2063  CG2 THR A 272     106.874  -7.633 -97.063  1.00107.59           C  
ANISOU 2063  CG2 THR A 272    11851   9368  19660   3277    133   3634       C  
ATOM   2064  N   GLY A 273     105.298  -5.176 -97.567  1.00109.45           N  
ANISOU 2064  N   GLY A 273    11888  10781  18918   2814    570   3359       N  
ATOM   2065  CA  GLY A 273     105.788  -3.827 -97.818  1.00108.23           C  
ANISOU 2065  CA  GLY A 273    11572  11190  18359   2940    683   3183       C  
ATOM   2066  C   GLY A 273     106.984  -3.754 -98.750  1.00109.38           C  
ANISOU 2066  C   GLY A 273    11562  11348  18649   3299    683   2803       C  
ATOM   2067  O   GLY A 273     107.097  -2.814 -99.542  1.00108.64           O  
ANISOU 2067  O   GLY A 273    11334  11649  18295   3339    824   2489       O  
ATOM   2068  N   ASP A 274     107.897  -4.729 -98.668  1.00113.26           N  
ANISOU 2068  N   ASP A 274    12061  11427  19546   3574    528   2840       N  
ATOM   2069  CA  ASP A 274     109.025  -4.765 -99.597  1.00116.04           C  
ANISOU 2069  CA  ASP A 274    12228  11809  20051   3947    548   2456       C  
ATOM   2070  C   ASP A 274     108.540  -4.868-101.040  1.00111.71           C  
ANISOU 2070  C   ASP A 274    11649  11255  19540   3943    706   1904       C  
ATOM   2071  O   ASP A 274     109.002  -4.133-101.922  1.00106.74           O  
ANISOU 2071  O   ASP A 274    10836  11011  18710   4076    849   1573       O  
ATOM   2072  CB  ASP A 274     109.954  -5.940 -99.261  1.00122.85           C  
ANISOU 2072  CB  ASP A 274    13119  12174  21385   4271    338   2572       C  
ATOM   2073  CG  ASP A 274     110.381  -5.962 -97.795  1.00126.21           C  
ANISOU 2073  CG  ASP A 274    13602  12569  21782   4271    146   3151       C  
ATOM   2074  OD1 ASP A 274     111.400  -5.306 -97.461  1.00126.65           O  
ANISOU 2074  OD1 ASP A 274    13518  13010  21592   4399     95   3191       O  
ATOM   2075  OD2 ASP A 274     109.690  -6.635 -96.992  1.00128.70           O  
ANISOU 2075  OD2 ASP A 274    14142  12540  22217   4061     35   3517       O  
ATOM   2076  N   GLN A 275     107.615  -5.795-101.299  1.00110.57           N  
ANISOU 2076  N   GLN A 275    11685  10677  19650   3776    667   1809       N  
ATOM   2077  CA  GLN A 275     107.069  -5.950-102.643  1.00104.61           C  
ANISOU 2077  CA  GLN A 275    10924   9900  18921   3752    783   1275       C  
ATOM   2078  C   GLN A 275     106.210  -4.756-103.038  1.00 99.31           C  
ANISOU 2078  C   GLN A 275    10188   9768  17776   3480    970   1170       C  
ATOM   2079  O   GLN A 275     106.051  -4.476-104.231  1.00 98.36           O  
ANISOU 2079  O   GLN A 275     9996   9838  17537   3526   1094    717       O  
ATOM   2080  CB  GLN A 275     106.259  -7.242-102.725  1.00106.91           C  
ANISOU 2080  CB  GLN A 275    11437   9563  19622   3595    649   1231       C  
ATOM   2081  CG  GLN A 275     106.579  -8.234-101.616  1.00112.37           C  
ANISOU 2081  CG  GLN A 275    12285   9720  20689   3635    421   1681       C  
ATOM   2082  CD  GLN A 275     105.873  -9.562-101.800  1.00118.61           C  
ANISOU 2082  CD  GLN A 275    13309   9819  21938   3482    259   1617       C  
ATOM   2083  OE1 GLN A 275     105.598 -10.272-100.833  1.00122.46           O  
ANISOU 2083  OE1 GLN A 275    13969   9898  22661   3308     91   2077       O  
ATOM   2084  NE2 GLN A 275     105.579  -9.907-103.048  1.00120.10           N  
ANISOU 2084  NE2 GLN A 275    13515   9869  22249   3535    294   1051       N  
ATOM   2085  N   LEU A 276     105.647  -4.048-102.056  1.00 94.81           N  
ANISOU 2085  N   LEU A 276     9651   9454  16920   3218    984   1574       N  
ATOM   2086  CA  LEU A 276     104.883  -2.842-102.352  1.00 90.01           C  
ANISOU 2086  CA  LEU A 276     8983   9359  15857   3010   1140   1489       C  
ATOM   2087  C   LEU A 276     105.791  -1.728-102.860  1.00 87.40           C  
ANISOU 2087  C   LEU A 276     8483   9489  15235   3214   1238   1318       C  
ATOM   2088  O   LEU A 276     105.423  -0.987-103.779  1.00 86.64           O  
ANISOU 2088  O   LEU A 276     8326   9720  14876   3163   1370   1022       O  
ATOM   2089  CB  LEU A 276     104.118  -2.397-101.106  1.00 86.37           C  
ANISOU 2089  CB  LEU A 276     8599   9055  15162   2735   1125   1954       C  
ATOM   2090  CG  LEU A 276     103.062  -1.305-101.268  1.00 82.94           C  
ANISOU 2090  CG  LEU A 276     8134   9081  14298   2506   1261   1895       C  
ATOM   2091  CD1 LEU A 276     102.008  -1.733-102.277  1.00 83.90           C  
ANISOU 2091  CD1 LEU A 276     8262   9101  14514   2334   1321   1554       C  
ATOM   2092  CD2 LEU A 276     102.428  -0.978 -99.922  1.00 79.64           C  
ANISOU 2092  CD2 LEU A 276     7783   8817  13659   2300   1244   2361       C  
ATOM   2093  N   GLY A 277     106.985  -1.601-102.277  1.00 86.29           N  
ANISOU 2093  N   GLY A 277     8259   9385  15141   3432   1161   1521       N  
ATOM   2094  CA  GLY A 277     107.942  -0.622-102.762  1.00 88.27           C  
ANISOU 2094  CA  GLY A 277     8321  10054  15165   3600   1238   1386       C  
ATOM   2095  C   GLY A 277     108.426  -0.904-104.170  1.00 87.54           C  
ANISOU 2095  C   GLY A 277     8096   9989  15177   3821   1351    905       C  
ATOM   2096  O   GLY A 277     108.718   0.029-104.924  1.00 83.12           O  
ANISOU 2096  O   GLY A 277     7401   9848  14333   3842   1480    717       O  
ATOM   2097  N   ALA A 278     108.523  -2.184-104.542  1.00 90.17           N  
ANISOU 2097  N   ALA A 278     8477   9877  15906   3991   1297    703       N  
ATOM   2098  CA  ALA A 278     108.871  -2.532-105.917  1.00 92.77           C  
ANISOU 2098  CA  ALA A 278     8707  10231  16312   4220   1408    190       C  
ATOM   2099  C   ALA A 278     107.834  -2.000-106.898  1.00 97.19           C  
ANISOU 2099  C   ALA A 278     9316  11036  16578   4006   1546   -116       C  
ATOM   2100  O   ALA A 278     108.184  -1.524-107.985  1.00 99.73           O  
ANISOU 2100  O   ALA A 278     9502  11698  16692   4127   1694   -445       O  
ATOM   2101  CB  ALA A 278     109.014  -4.048-106.055  1.00 94.90           C  
ANISOU 2101  CB  ALA A 278     9080   9903  17074   4435   1283     13       C  
ATOM   2102  N   LEU A 279     106.551  -2.075-106.534  1.00 94.81           N  
ANISOU 2102  N   LEU A 279     9188  10592  16242   3686   1500      3       N  
ATOM   2103  CA  LEU A 279     105.515  -1.468-107.362  1.00 93.70           C  
ANISOU 2103  CA  LEU A 279     9075  10726  15799   3474   1607   -241       C  
ATOM   2104  C   LEU A 279     105.653   0.049-107.380  1.00 88.99           C  
ANISOU 2104  C   LEU A 279     8379  10693  14742   3403   1714   -119       C  
ATOM   2105  O   LEU A 279     105.413   0.689-108.412  1.00 87.75           O  
ANISOU 2105  O   LEU A 279     8173  10862  14307   3386   1829   -398       O  
ATOM   2106  CB  LEU A 279     104.131  -1.883-106.859  1.00 95.99           C  
ANISOU 2106  CB  LEU A 279     9527  10774  16172   3144   1527    -97       C  
ATOM   2107  CG  LEU A 279     102.912  -1.394-107.647  1.00 96.97           C  
ANISOU 2107  CG  LEU A 279     9668  11145  16031   2915   1600   -339       C  
ATOM   2108  CD1 LEU A 279     103.023  -1.784-109.114  1.00 99.22           C  
ANISOU 2108  CD1 LEU A 279     9930  11423  16345   3072   1648   -889       C  
ATOM   2109  CD2 LEU A 279     101.624  -1.939-107.043  1.00 98.68           C  
ANISOU 2109  CD2 LEU A 279     9992  11114  16388   2585   1513   -155       C  
ATOM   2110  N   TYR A 280     106.050   0.640-106.251  1.00 85.26           N  
ANISOU 2110  N   TYR A 280     7892  10325  14179   3362   1656    296       N  
ATOM   2111  CA  TYR A 280     106.258   2.083-106.200  1.00 87.51           C  
ANISOU 2111  CA  TYR A 280     8110  11082  14059   3296   1715    418       C  
ATOM   2112  C   TYR A 280     107.426   2.496-107.084  1.00 91.15           C  
ANISOU 2112  C   TYR A 280     8378  11819  14436   3508   1812    221       C  
ATOM   2113  O   TYR A 280     107.323   3.457-107.856  1.00 86.15           O  
ANISOU 2113  O   TYR A 280     7699  11555  13478   3446   1914     89       O  
ATOM   2114  CB  TYR A 280     106.503   2.537-104.760  1.00 91.40           C  
ANISOU 2114  CB  TYR A 280     8644  11593  14491   3226   1599    877       C  
ATOM   2115  CG  TYR A 280     105.321   2.383-103.832  1.00 94.77           C  
ANISOU 2115  CG  TYR A 280     9236  11887  14885   2997   1539   1118       C  
ATOM   2116  CD1 TYR A 280     105.442   2.671-102.481  1.00 96.11           C  
ANISOU 2116  CD1 TYR A 280     9468  12070  14978   2942   1434   1525       C  
ATOM   2117  CD2 TYR A 280     104.087   1.953-104.302  1.00 94.18           C  
ANISOU 2117  CD2 TYR A 280     9237  11709  14839   2833   1586    942       C  
ATOM   2118  CE1 TYR A 280     104.373   2.535-101.625  1.00 95.29           C  
ANISOU 2118  CE1 TYR A 280     9491  11910  14806   2742   1408   1757       C  
ATOM   2119  CE2 TYR A 280     103.014   1.812-103.451  1.00 94.23           C  
ANISOU 2119  CE2 TYR A 280     9344  11650  14810   2611   1552   1184       C  
ATOM   2120  CZ  TYR A 280     103.160   2.107-102.114  1.00 94.88           C  
ANISOU 2120  CZ  TYR A 280     9481  11777  14794   2572   1478   1596       C  
ATOM   2121  OH  TYR A 280     102.092   1.971-101.258  1.00 95.10           O  
ANISOU 2121  OH  TYR A 280     9587  11801  14746   2359   1472   1848       O  
ATOM   2122  N   GLN A 281     108.554   1.788-106.972  1.00 94.36           N  
ANISOU 2122  N   GLN A 281     8656  12069  15128   3762   1781    219       N  
ATOM   2123  CA  GLN A 281     109.697   2.076-107.832  1.00 97.26           C  
ANISOU 2123  CA  GLN A 281     8877  12744  15333   3874   1817    -19       C  
ATOM   2124  C   GLN A 281     109.323   1.933-109.301  1.00104.39           C  
ANISOU 2124  C   GLN A 281     9766  13789  16109   3923   1961   -479       C  
ATOM   2125  O   GLN A 281     109.774   2.719-110.143  1.00105.74           O  
ANISOU 2125  O   GLN A 281     9844  14347  15986   3851   2036   -637       O  
ATOM   2126  CB  GLN A 281     110.869   1.154-107.485  1.00 97.34           C  
ANISOU 2126  CB  GLN A 281     8788  12552  15646   4131   1712     -8       C  
ATOM   2127  CG  GLN A 281     111.417   1.319-106.071  1.00 96.09           C  
ANISOU 2127  CG  GLN A 281     8627  12306  15579   4099   1546    438       C  
ATOM   2128  CD  GLN A 281     112.165   2.624-105.875  1.00 96.06           C  
ANISOU 2128  CD  GLN A 281     8514  12727  15258   3942   1520    604       C  
ATOM   2129  OE1 GLN A 281     112.403   3.368-106.827  1.00 97.69           O  
ANISOU 2129  OE1 GLN A 281     8630  13274  15213   3858   1631    403       O  
ATOM   2130  NE2 GLN A 281     112.544   2.908-104.633  1.00 94.56           N  
ANISOU 2130  NE2 GLN A 281     8338  12497  15092   3892   1364    985       N  
ATOM   2131  N   ASP A 282     108.496   0.936-109.627  1.00108.11           N  
ANISOU 2131  N   ASP A 282    10327  13908  16840   4008   1997   -695       N  
ATOM   2132  CA  ASP A 282     107.976   0.831-110.986  1.00113.97           C  
ANISOU 2132  CA  ASP A 282    11089  14786  17427   4036   2117  -1137       C  
ATOM   2133  C   ASP A 282     107.033   1.983-111.306  1.00109.17           C  
ANISOU 2133  C   ASP A 282    10528  14509  16441   3777   2191  -1096       C  
ATOM   2134  O   ASP A 282     106.990   2.447-112.450  1.00108.71           O  
ANISOU 2134  O   ASP A 282    10454  14750  16099   3749   2308  -1338       O  
ATOM   2135  CB  ASP A 282     107.275  -0.513-111.184  1.00120.25           C  
ANISOU 2135  CB  ASP A 282    12022  15067  18602   4093   2048  -1414       C  
ATOM   2136  CG  ASP A 282     108.249  -1.678-111.233  1.00126.30           C  
ANISOU 2136  CG  ASP A 282    12752  15514  19722   4433   1992  -1573       C  
ATOM   2137  OD1 ASP A 282     107.908  -2.764-110.718  1.00129.66           O  
ANISOU 2137  OD1 ASP A 282    13309  15378  20580   4457   1847  -1567       O  
ATOM   2138  OD2 ASP A 282     109.356  -1.509-111.789  1.00127.21           O  
ANISOU 2138  OD2 ASP A 282    12772  15968  19594   4635   2061  -1645       O  
ATOM   2139  N   PHE A 283     106.278   2.461-110.315  1.00102.84           N  
ANISOU 2139  N   PHE A 283     9850  13644  15580   3529   2092   -761       N  
ATOM   2140  CA  PHE A 283     105.480   3.666-110.515  1.00 95.52           C  
ANISOU 2140  CA  PHE A 283     8985  13055  14255   3310   2120   -692       C  
ATOM   2141  C   PHE A 283     106.375   4.874-110.768  1.00 89.66           C  
ANISOU 2141  C   PHE A 283     8169  12699  13200   3261   2143   -591       C  
ATOM   2142  O   PHE A 283     106.131   5.661-111.689  1.00 91.57           O  
ANISOU 2142  O   PHE A 283     8452  13207  13133   3133   2196   -725       O  
ATOM   2143  CB  PHE A 283     104.579   3.911-109.304  1.00 97.10           C  
ANISOU 2143  CB  PHE A 283     9320  13121  14452   3090   2004   -360       C  
ATOM   2144  CG  PHE A 283     103.383   3.003-109.232  1.00 98.57           C  
ANISOU 2144  CG  PHE A 283     9618  13008  14828   2954   1947   -467       C  
ATOM   2145  CD1 PHE A 283     102.638   2.919-108.067  1.00 96.20           C  
ANISOU 2145  CD1 PHE A 283     9405  12555  14590   2773   1860   -154       C  
ATOM   2146  CD2 PHE A 283     102.999   2.241-110.324  1.00101.28           C  
ANISOU 2146  CD2 PHE A 283     9970  13241  15272   2994   1974   -878       C  
ATOM   2147  CE1 PHE A 283     101.534   2.093-107.989  1.00 96.52           C  
ANISOU 2147  CE1 PHE A 283     9515  12346  14812   2603   1811   -213       C  
ATOM   2148  CE2 PHE A 283     101.892   1.412-110.252  1.00102.65           C  
ANISOU 2148  CE2 PHE A 283    10235  13125  15642   2824   1893   -966       C  
ATOM   2149  CZ  PHE A 283     101.159   1.339-109.083  1.00100.78           C  
ANISOU 2149  CZ  PHE A 283    10060  12746  15487   2612   1816   -616       C  
ATOM   2150  N   VAL A 284     107.429   5.029-109.963  1.00 87.07           N  
ANISOU 2150  N   VAL A 284     7775  12348  12961   3289   2065   -336       N  
ATOM   2151  CA  VAL A 284     108.289   6.202-110.086  1.00 82.91           C  
ANISOU 2151  CA  VAL A 284     7203  12123  12178   3163   2048   -197       C  
ATOM   2152  C   VAL A 284     109.134   6.135-111.356  1.00 88.35           C  
ANISOU 2152  C   VAL A 284     7760  13000  12810   3217   2171   -467       C  
ATOM   2153  O   VAL A 284     109.436   7.172-111.962  1.00 83.45           O  
ANISOU 2153  O   VAL A 284     7135  12670  11901   3074   2219   -416       O  
ATOM   2154  CB  VAL A 284     109.160   6.348-108.823  1.00 76.82           C  
ANISOU 2154  CB  VAL A 284     6375  11280  11531   3185   1921    155       C  
ATOM   2155  CG1 VAL A 284     110.073   7.564-108.928  1.00 75.30           C  
ANISOU 2155  CG1 VAL A 284     6109  11393  11108   3060   1901    317       C  
ATOM   2156  CG2 VAL A 284     108.277   6.445-107.583  1.00 68.71           C  
ANISOU 2156  CG2 VAL A 284     5491  10084  10534   3122   1827    444       C  
ATOM   2157  N   ARG A 285     109.521   4.934-111.792  1.00 91.51           N  
ANISOU 2157  N   ARG A 285     8059  13231  13480   3437   2232   -739       N  
ATOM   2158  CA  ARG A 285     110.323   4.828-113.006  1.00 95.66           C  
ANISOU 2158  CA  ARG A 285     8465  13930  13950   3504   2392   -972       C  
ATOM   2159  C   ARG A 285     109.471   4.906-114.267  1.00 93.82           C  
ANISOU 2159  C   ARG A 285     8366  13804  13477   3452   2525  -1217       C  
ATOM   2160  O   ARG A 285     109.952   5.380-115.303  1.00 94.45           O  
ANISOU 2160  O   ARG A 285     8411  14173  13302   3412   2644  -1292       O  
ATOM   2161  CB  ARG A 285     111.140   3.531-112.999  1.00104.76           C  
ANISOU 2161  CB  ARG A 285     9472  14846  15485   3798   2418  -1155       C  
ATOM   2162  CG  ARG A 285     110.339   2.263-113.257  1.00110.77           C  
ANISOU 2162  CG  ARG A 285    10353  15233  16500   4007   2465  -1395       C  
ATOM   2163  CD  ARG A 285     111.240   1.034-113.304  1.00118.70           C  
ANISOU 2163  CD  ARG A 285    11295  15993  17813   4356   2508  -1467       C  
ATOM   2164  NE  ARG A 285     111.943   0.815-112.042  1.00121.54           N  
ANISOU 2164  NE  ARG A 285    11509  16273  18399   4410   2186  -1415       N  
ATOM   2165  CZ  ARG A 285     112.815  -0.166-111.832  1.00128.40           C  
ANISOU 2165  CZ  ARG A 285    12339  17096  19351   4785   2040  -1508       C  
ATOM   2166  NH1 ARG A 285     113.099  -1.025-112.802  1.00133.69           N  
ANISOU 2166  NH1 ARG A 285    13107  17549  20141   5078   2433  -1436       N  
ATOM   2167  NH2 ARG A 285     113.406  -0.288-110.651  1.00129.11           N  
ANISOU 2167  NH2 ARG A 285    12349  17050  19654   4888   1899  -1201       N  
ATOM   2168  N   ASP A 286     108.214   4.459-114.205  1.00 90.54           N  
ANISOU 2168  N   ASP A 286     8099  13198  13104   3458   2491  -1333       N  
ATOM   2169  CA  ASP A 286     107.329   4.511-115.364  1.00 85.52           C  
ANISOU 2169  CA  ASP A 286     7600  12693  12200   3413   2556  -1584       C  
ATOM   2170  C   ASP A 286     106.537   5.808-115.443  1.00 81.90           C  
ANISOU 2170  C   ASP A 286     7254  12480  11386   3155   2501  -1428       C  
ATOM   2171  O   ASP A 286     106.136   6.213-116.541  1.00 80.03           O  
ANISOU 2171  O   ASP A 286     7099  12467  10840   3089   2544  -1579       O  
ATOM   2172  CB  ASP A 286     106.348   3.333-115.347  1.00 88.07           C  
ANISOU 2172  CB  ASP A 286     8011  12719  12733   3553   2504  -1850       C  
ATOM   2173  CG  ASP A 286     107.029   1.992-115.551  1.00 95.68           C  
ANISOU 2173  CG  ASP A 286     8936  13422  13995   3849   2524  -2091       C  
ATOM   2174  OD1 ASP A 286     108.022   1.930-116.308  1.00 97.39           O  
ANISOU 2174  OD1 ASP A 286     9086  13795  14122   3961   2641  -2181       O  
ATOM   2175  OD2 ASP A 286     106.565   0.995-114.955  1.00 98.23           O  
ANISOU 2175  OD2 ASP A 286     9294  13362  14666   3959   2404  -2209       O  
ATOM   2176  N   TYR A 287     106.302   6.461-114.313  1.00 79.11           N  
ANISOU 2176  N   TYR A 287     6919  12093  11047   3032   2388  -1129       N  
ATOM   2177  CA  TYR A 287     105.449   7.635-114.270  1.00 78.02           C  
ANISOU 2177  CA  TYR A 287     6915  12135  10593   2837   2314   -978       C  
ATOM   2178  C   TYR A 287     106.166   8.788-113.591  1.00 72.76           C  
ANISOU 2178  C   TYR A 287     6239  11610   9797   2729   2243   -631       C  
ATOM   2179  O   TYR A 287     107.073   8.573-112.781  1.00 75.91           O  
ANISOU 2179  O   TYR A 287     6530  11916  10396   2788   2211   -469       O  
ATOM   2180  CB  TYR A 287     104.145   7.339-113.516  1.00 77.28           C  
ANISOU 2180  CB  TYR A 287     6894  11874  10593   2813   2234   -958       C  
ATOM   2181  CG  TYR A 287     103.411   6.127-114.026  1.00 82.97           C  
ANISOU 2181  CG  TYR A 287     7597  12441  11489   2929   2275  -1298       C  
ATOM   2182  CD1 TYR A 287     102.500   6.232-115.067  1.00 81.50           C  
ANISOU 2182  CD1 TYR A 287     7489  12402  11074   2869   2276  -1552       C  
ATOM   2183  CD2 TYR A 287     103.629   4.875-113.468  1.00 89.78           C  
ANISOU 2183  CD2 TYR A 287     8364  13002  12745   3112   2276  -1382       C  
ATOM   2184  CE1 TYR A 287     101.825   5.126-115.536  1.00 85.85           C  
ANISOU 2184  CE1 TYR A 287     8017  12813  11787   2953   2267  -1922       C  
ATOM   2185  CE2 TYR A 287     102.960   3.762-113.929  1.00 93.50           C  
ANISOU 2185  CE2 TYR A 287     8870  13238  13418   3149   2245  -1723       C  
ATOM   2186  CZ  TYR A 287     102.059   3.892-114.963  1.00 92.39           C  
ANISOU 2186  CZ  TYR A 287     8780  13275  13048   3078   2246  -2025       C  
ATOM   2187  OH  TYR A 287     101.390   2.783-115.425  1.00 98.29           O  
ANISOU 2187  OH  TYR A 287     9588  13750  14009   3063   2175  -2368       O  
ATOM   2188  N   PRO A 288     105.791   9.994-113.895  1.00 68.36           N  
ANISOU 2188  N   PRO A 288     5790  11272   8914   2595   2200   -512       N  
ATOM   2189  CA  PRO A 288     106.340  11.145-113.156  1.00 64.30           C  
ANISOU 2189  CA  PRO A 288     5282  10872   8279   2511   2111   -169       C  
ATOM   2190  C   PRO A 288     105.680  11.303-111.787  1.00 62.26           C  
ANISOU 2190  C   PRO A 288     5115  10441   8100   2502   1984     31       C  
ATOM   2191  O   PRO A 288     104.831  12.152-111.546  1.00 65.55           O  
ANISOU 2191  O   PRO A 288     5672  10923   8311   2442   1903    128       O  
ATOM   2192  CB  PRO A 288     106.029  12.319-114.087  1.00 64.31           C  
ANISOU 2192  CB  PRO A 288     5376  11160   7900   2411   2113   -139       C  
ATOM   2193  CG  PRO A 288     104.785  11.901-114.795  1.00 62.00           C  
ANISOU 2193  CG  PRO A 288     5194  10836   7526   2422   2123   -407       C  
ATOM   2194  CD  PRO A 288     104.896  10.414-114.990  1.00 65.33           C  
ANISOU 2194  CD  PRO A 288     5521  11061   8240   2535   2216   -676       C  
ATOM   2195  N   VAL A 289     106.069  10.444-110.853  1.00 62.44           N  
ANISOU 2195  N   VAL A 289     5057  10245   8421   2587   1964     98       N  
ATOM   2196  CA  VAL A 289     105.567  10.488-109.485  1.00 65.44           C  
ANISOU 2196  CA  VAL A 289     5511  10477   8877   2592   1859    325       C  
ATOM   2197  C   VAL A 289     106.677  11.052-108.609  1.00 65.05           C  
ANISOU 2197  C   VAL A 289     5398  10463   8856   2595   1772    625       C  
ATOM   2198  O   VAL A 289     107.727  10.421-108.437  1.00 68.35           O  
ANISOU 2198  O   VAL A 289     5667  10809   9495   2669   1783    652       O  
ATOM   2199  CB  VAL A 289     105.114   9.106-108.996  1.00 68.13           C  
ANISOU 2199  CB  VAL A 289     5808  10548   9529   2691   1889    248       C  
ATOM   2200  CG1 VAL A 289     104.674   9.179-107.542  1.00 68.08           C  
ANISOU 2200  CG1 VAL A 289     5865  10427   9576   2689   1800    543       C  
ATOM   2201  CG2 VAL A 289     103.989   8.577-109.874  1.00 69.62           C  
ANISOU 2201  CG2 VAL A 289     6023  10729   9698   2687   1967    -49       C  
ATOM   2202  N   VAL A 290     106.450  12.243-108.055  1.00 62.84           N  
ANISOU 2202  N   VAL A 290     5217  10302   8359   2536   1672    842       N  
ATOM   2203  CA  VAL A 290     107.431  12.901-107.197  1.00 59.35           C  
ANISOU 2203  CA  VAL A 290     4702   9918   7930   2536   1563   1137       C  
ATOM   2204  C   VAL A 290     107.028  12.910-105.733  1.00 60.40           C  
ANISOU 2204  C   VAL A 290     4986   9870   8093   2533   1403   1324       C  
ATOM   2205  O   VAL A 290     107.873  13.228-104.880  1.00 65.47           O  
ANISOU 2205  O   VAL A 290     5609  10488   8780   2511   1261   1541       O  
ATOM   2206  CB  VAL A 290     107.716  14.344-107.663  1.00 56.54           C  
ANISOU 2206  CB  VAL A 290     4416   9769   7299   2396   1488   1236       C  
ATOM   2207  CG1 VAL A 290     108.424  14.332-108.995  1.00 59.36           C  
ANISOU 2207  CG1 VAL A 290     4573  10362   7619   2386   1654   1130       C  
ATOM   2208  CG2 VAL A 290     106.427  15.134-107.755  1.00 60.22           C  
ANISOU 2208  CG2 VAL A 290     5140  10241   7499   2351   1420   1178       C  
ATOM   2209  N   SER A 291     105.781  12.583-105.407  1.00 62.12           N  
ANISOU 2209  N   SER A 291     5340   9992   8270   2548   1418   1254       N  
ATOM   2210  CA  SER A 291     105.316  12.660-104.030  1.00 54.24           C  
ANISOU 2210  CA  SER A 291     4487   8890   7233   2546   1291   1437       C  
ATOM   2211  C   SER A 291     104.357  11.515-103.761  1.00 52.05           C  
ANISOU 2211  C   SER A 291     4205   8468   7103   2575   1384   1376       C  
ATOM   2212  O   SER A 291     103.412  11.303-104.526  1.00 72.17           O  
ANISOU 2212  O   SER A 291     6755  11054   9611   2555   1488   1173       O  
ATOM   2213  CB  SER A 291     104.631  14.002-103.755  1.00 50.11           C  
ANISOU 2213  CB  SER A 291     4180   8484   6376   2499   1170   1468       C  
ATOM   2214  OG  SER A 291     104.606  14.278-102.371  1.00 50.08           O  
ANISOU 2214  OG  SER A 291     4305   8428   6296   2516   1018   1661       O  
ATOM   2215  N   ILE A 292     104.599  10.780-102.679  1.00 58.61           N  
ANISOU 2215  N   ILE A 292     5028   9135   8105   2603   1331   1568       N  
ATOM   2216  CA  ILE A 292     103.739   9.675-102.275  1.00 65.75           C  
ANISOU 2216  CA  ILE A 292     5937   9876   9168   2588   1398   1585       C  
ATOM   2217  C   ILE A 292     103.374   9.853-100.807  1.00 63.65           C  
ANISOU 2217  C   ILE A 292     5796   9618   8769   2569   1298   1855       C  
ATOM   2218  O   ILE A 292     104.258  10.022 -99.960  1.00 59.52           O  
ANISOU 2218  O   ILE A 292     5296   9069   8251   2610   1168   2063       O  
ATOM   2219  CB  ILE A 292     104.411   8.309-102.510  1.00 70.87           C  
ANISOU 2219  CB  ILE A 292     6450  10270  10208   2654   1446   1560       C  
ATOM   2220  CG1 ILE A 292     104.788   8.153-103.984  1.00 72.66           C  
ANISOU 2220  CG1 ILE A 292     6551  10539  10519   2708   1559   1255       C  
ATOM   2221  CG2 ILE A 292     103.488   7.186-102.075  1.00 73.88           C  
ANISOU 2221  CG2 ILE A 292     6863  10437  10772   2591   1486   1611       C  
ATOM   2222  CD1 ILE A 292     105.190   6.748-104.373  1.00 76.40           C  
ANISOU 2222  CD1 ILE A 292     6915  10745  11370   2808   1616   1133       C  
ATOM   2223  N   GLU A 293     102.077   9.816-100.511  1.00 67.57           N  
ANISOU 2223  N   GLU A 293     6357  10187   9131   2509   1356   1850       N  
ATOM   2224  CA  GLU A 293     101.563   9.999 -99.161  1.00 68.47           C  
ANISOU 2224  CA  GLU A 293     6578  10383   9054   2501   1300   2086       C  
ATOM   2225  C   GLU A 293     101.054   8.671 -98.616  1.00 68.88           C  
ANISOU 2225  C   GLU A 293     6576  10267   9327   2420   1373   2250       C  
ATOM   2226  O   GLU A 293     100.402   7.905 -99.332  1.00 68.64           O  
ANISOU 2226  O   GLU A 293     6458  10135   9488   2335   1483   2112       O  
ATOM   2227  CB  GLU A 293     100.439  11.039 -99.144  1.00 73.53           C  
ANISOU 2227  CB  GLU A 293     7310  11291   9338   2511   1317   1979       C  
ATOM   2228  CG  GLU A 293     100.003  11.493 -97.763  1.00 78.24           C  
ANISOU 2228  CG  GLU A 293     8028  12049   9649   2557   1255   2179       C  
ATOM   2229  CD  GLU A 293      98.801  12.418 -97.817  1.00 83.47           C  
ANISOU 2229  CD  GLU A 293     8751  12982   9982   2614   1290   2033       C  
ATOM   2230  OE1 GLU A 293      97.659  11.920 -97.720  1.00 90.79           O  
ANISOU 2230  OE1 GLU A 293     9582  14025  10889   2560   1425   2036       O  
ATOM   2231  OE2 GLU A 293      98.997  13.642 -97.974  1.00 83.84           O  
ANISOU 2231  OE2 GLU A 293     8933  13120   9802   2713   1170   1919       O  
ATOM   2232  N   ASP A 294     101.348   8.414 -97.342  1.00 70.58           N  
ANISOU 2232  N   ASP A 294     6856  10450   9510   2433   1293   2556       N  
ATOM   2233  CA  ASP A 294     101.020   7.174 -96.640  1.00 72.28           C  
ANISOU 2233  CA  ASP A 294     7049  10486   9927   2342   1330   2807       C  
ATOM   2234  C   ASP A 294     101.324   5.929 -97.482  1.00 70.25           C  
ANISOU 2234  C   ASP A 294     6690   9876  10126   2303   1372   2709       C  
ATOM   2235  O   ASP A 294     100.413   5.142 -97.779  1.00 75.43           O  
ANISOU 2235  O   ASP A 294     7299  10422  10939   2163   1467   2673       O  
ATOM   2236  CB  ASP A 294      99.569   7.177 -96.173  1.00 70.90           C  
ANISOU 2236  CB  ASP A 294     6875  10523   9541   2224   1448   2882       C  
ATOM   2237  CG  ASP A 294      99.352   8.045 -94.945  1.00 68.85           C  
ANISOU 2237  CG  ASP A 294     6733  10570   8858   2297   1397   3067       C  
ATOM   2238  OD1 ASP A 294     100.354   8.440 -94.309  1.00 68.76           O  
ANISOU 2238  OD1 ASP A 294     6822  10545   8760   2406   1244   3189       O  
ATOM   2239  OD2 ASP A 294      98.180   8.321 -94.610  1.00 66.99           O  
ANISOU 2239  OD2 ASP A 294     6478  10606   8370   2254   1505   3078       O  
ATOM   2240  N   PRO A 295     102.583   5.715 -97.878  1.00 67.74           N  
ANISOU 2240  N   PRO A 295     6328   9378  10031   2429   1293   2651       N  
ATOM   2241  CA  PRO A 295     102.913   4.488 -98.619  1.00 70.26           C  
ANISOU 2241  CA  PRO A 295     6566   9346  10783   2448   1320   2533       C  
ATOM   2242  C   PRO A 295     102.721   3.214 -97.812  1.00 80.98           C  
ANISOU 2242  C   PRO A 295     7970  10387  12413   2373   1275   2827       C  
ATOM   2243  O   PRO A 295     102.522   2.146 -98.406  1.00 80.63           O  
ANISOU 2243  O   PRO A 295     7898  10021  12715   2329   1301   2712       O  
ATOM   2244  CB  PRO A 295     104.386   4.695 -98.997  1.00 69.34           C  
ANISOU 2244  CB  PRO A 295     6370   9196  10782   2640   1242   2453       C  
ATOM   2245  CG  PRO A 295     104.894   5.690 -98.023  1.00 64.95           C  
ANISOU 2245  CG  PRO A 295     5875   8870   9934   2676   1121   2675       C  
ATOM   2246  CD  PRO A 295     103.750   6.608 -97.774  1.00 63.09           C  
ANISOU 2246  CD  PRO A 295     5741   8913   9316   2563   1176   2655       C  
ATOM   2247  N   PHE A 296     102.784   3.284 -96.484  1.00 88.81           N  
ANISOU 2247  N   PHE A 296     9046  11444  13252   2354   1194   3204       N  
ATOM   2248  CA  PHE A 296     102.621   2.106 -95.640  1.00 98.03           C  
ANISOU 2248  CA  PHE A 296    10276  12321  14649   2266   1139   3554       C  
ATOM   2249  C   PHE A 296     101.704   2.462 -94.473  1.00 96.22           C  
ANISOU 2249  C   PHE A 296    10124  12376  14061   2117   1180   3870       C  
ATOM   2250  O   PHE A 296     101.143   3.560 -94.409  1.00 94.33           O  
ANISOU 2250  O   PHE A 296     9886  12528  13429   2109   1252   3761       O  
ATOM   2251  CB  PHE A 296     103.985   1.583 -95.163  1.00105.56           C  
ANISOU 2251  CB  PHE A 296    11242  13023  15841   2457    963   3748       C  
ATOM   2252  CG  PHE A 296     105.009   1.477 -96.256  1.00103.81           C  
ANISOU 2252  CG  PHE A 296    10903  12654  15886   2659    940   3421       C  
ATOM   2253  CD1 PHE A 296     104.950   0.451 -97.183  1.00105.35           C  
ANISOU 2253  CD1 PHE A 296    11061  12489  16479   2682    978   3195       C  
ATOM   2254  CD2 PHE A 296     106.029   2.408 -96.356  1.00101.68           C  
ANISOU 2254  CD2 PHE A 296    10555  12622  15459   2821    878   3334       C  
ATOM   2255  CE1 PHE A 296     105.891   0.355 -98.191  1.00106.56           C  
ANISOU 2255  CE1 PHE A 296    11091  12561  16837   2900    980   2873       C  
ATOM   2256  CE2 PHE A 296     106.972   2.316 -97.361  1.00102.74           C  
ANISOU 2256  CE2 PHE A 296    10539  12685  15812   3000    886   3054       C  
ATOM   2257  CZ  PHE A 296     106.903   1.289 -98.279  1.00105.37           C  
ANISOU 2257  CZ  PHE A 296    10827  12699  16508   3058    950   2816       C  
ATOM   2258  N   ASP A 297     101.554   1.525 -93.540  1.00 99.03           N  
ANISOU 2258  N   ASP A 297    10547  12539  14541   2014   1131   4268       N  
ATOM   2259  CA  ASP A 297     100.666   1.722 -92.405  1.00 98.78           C  
ANISOU 2259  CA  ASP A 297    10570  12805  14160   1865   1196   4603       C  
ATOM   2260  C   ASP A 297     101.237   2.770 -91.451  1.00 97.60           C  
ANISOU 2260  C   ASP A 297    10504  13002  13576   2032   1102   4730       C  
ATOM   2261  O   ASP A 297     102.440   3.048 -91.431  1.00 94.92           O  
ANISOU 2261  O   ASP A 297    10189  12584  13292   2224    942   4690       O  
ATOM   2262  CB  ASP A 297     100.436   0.398 -91.671  1.00102.73           C  
ANISOU 2262  CB  ASP A 297    11128  12991  14912   1690   1156   5044       C  
ATOM   2263  CG  ASP A 297      99.315   0.478 -90.652  1.00100.98           C  
ANISOU 2263  CG  ASP A 297    10915  13116  14337   1480   1281   5389       C  
ATOM   2264  OD1 ASP A 297      98.139   0.320 -91.043  1.00 98.05           O  
ANISOU 2264  OD1 ASP A 297    10438  12847  13971   1255   1443   5314       O  
ATOM   2265  OD2 ASP A 297      99.612   0.692 -89.457  1.00101.65           O  
ANISOU 2265  OD2 ASP A 297    11098  13401  14124   1541   1215   5736       O  
ATOM   2266  N   GLN A 298     100.344   3.360 -90.653  1.00 98.37           N  
ANISOU 2266  N   GLN A 298    10635  13508  13233   1960   1198   4871       N  
ATOM   2267  CA  GLN A 298     100.716   4.398 -89.697  1.00 99.21           C  
ANISOU 2267  CA  GLN A 298    10852  13970  12875   2116   1104   4955       C  
ATOM   2268  C   GLN A 298     101.613   3.889 -88.575  1.00104.60           C  
ANISOU 2268  C   GLN A 298    11646  14537  13561   2182    916   5363       C  
ATOM   2269  O   GLN A 298     102.161   4.708 -87.830  1.00105.82           O  
ANISOU 2269  O   GLN A 298    11902  14934  13372   2331    779   5406       O  
ATOM   2270  CB  GLN A 298      99.457   5.027 -89.100  1.00100.53           C  
ANISOU 2270  CB  GLN A 298    11019  14611  12567   2052   1269   4996       C  
ATOM   2271  CG  GLN A 298      98.395   4.015 -88.696  1.00104.61           C  
ANISOU 2271  CG  GLN A 298    11460  15139  13148   1798   1435   5317       C  
ATOM   2272  CD  GLN A 298      97.140   4.670 -88.153  1.00105.62           C  
ANISOU 2272  CD  GLN A 298    11530  15809  12790   1759   1626   5335       C  
ATOM   2273  OE1 GLN A 298      97.202   5.705 -87.489  1.00103.22           O  
ANISOU 2273  OE1 GLN A 298    11324  15877  12020   1951   1591   5277       O  
ATOM   2274  NE2 GLN A 298      95.989   4.070 -88.438  1.00108.45           N  
ANISOU 2274  NE2 GLN A 298    11723  16224  13261   1516   1819   5400       N  
ATOM   2275  N   ASP A 299     101.769   2.571 -88.429  1.00107.11           N  
ANISOU 2275  N   ASP A 299    11963  14480  14255   2079    881   5660       N  
ATOM   2276  CA  ASP A 299     102.658   2.002 -87.424  1.00107.38           C  
ANISOU 2276  CA  ASP A 299    12105  14363  14332   2159    676   6068       C  
ATOM   2277  C   ASP A 299     103.678   1.040 -88.021  1.00107.29           C  
ANISOU 2277  C   ASP A 299    12056  13815  14894   2252    524   6058       C  
ATOM   2278  O   ASP A 299     104.326   0.299 -87.271  1.00112.77           O  
ANISOU 2278  O   ASP A 299    12830  14292  15724   2308    348   6432       O  
ATOM   2279  CB  ASP A 299     101.850   1.292 -86.331  1.00108.62           C  
ANISOU 2279  CB  ASP A 299    12338  14614  14320   1964    748   6571       C  
ATOM   2280  CG  ASP A 299     101.114   2.263 -85.428  1.00108.28           C  
ANISOU 2280  CG  ASP A 299    12343  15171  13628   1962    856   6638       C  
ATOM   2281  OD1 ASP A 299     101.686   3.326 -85.108  1.00106.66           O  
ANISOU 2281  OD1 ASP A 299    12208  15229  13088   2168    735   6471       O  
ATOM   2282  OD2 ASP A 299      99.965   1.964 -85.039  1.00110.12           O  
ANISOU 2282  OD2 ASP A 299    12538  15618  13684   1756   1055   6852       O  
ATOM   2283  N   ASP A 300     103.839   1.028 -89.341  1.00101.15           N  
ANISOU 2283  N   ASP A 300    11161  12833  14438   2293    583   5641       N  
ATOM   2284  CA  ASP A 300     104.816   0.166 -90.008  1.00101.03           C  
ANISOU 2284  CA  ASP A 300    11091  12345  14951   2434    459   5555       C  
ATOM   2285  C   ASP A 300     106.084   0.956 -90.330  1.00 95.60           C  
ANISOU 2285  C   ASP A 300    10315  11770  14239   2686    326   5320       C  
ATOM   2286  O   ASP A 300     106.502   1.086 -91.480  1.00 91.30           O  
ANISOU 2286  O   ASP A 300     9642  11133  13916   2782    371   4940       O  
ATOM   2287  CB  ASP A 300     104.205  -0.445 -91.268  1.00102.22           C  
ANISOU 2287  CB  ASP A 300    11164  12210  15465   2325    606   5239       C  
ATOM   2288  CG  ASP A 300     105.048  -1.571 -91.845  1.00106.79           C  
ANISOU 2288  CG  ASP A 300    11720  12248  16606   2475    481   5179       C  
ATOM   2289  OD1 ASP A 300     106.146  -1.841 -91.313  1.00108.79           O  
ANISOU 2289  OD1 ASP A 300    11990  12365  16981   2683    283   5379       O  
ATOM   2290  OD2 ASP A 300     104.612  -2.185 -92.843  1.00108.19           O  
ANISOU 2290  OD2 ASP A 300    11862  12143  17101   2404    566   4912       O  
ATOM   2291  N   TRP A 301     106.708   1.468 -89.267  1.00 94.50           N  
ANISOU 2291  N   TRP A 301    10240  11853  13812   2781    152   5568       N  
ATOM   2292  CA  TRP A 301     107.815   2.408 -89.421  1.00 93.39           C  
ANISOU 2292  CA  TRP A 301    10011  11902  13572   2960     10   5378       C  
ATOM   2293  C   TRP A 301     109.008   1.791 -90.140  1.00 95.89           C  
ANISOU 2293  C   TRP A 301    10163  11908  14363   3155    -96   5249       C  
ATOM   2294  O   TRP A 301     109.803   2.516 -90.750  1.00 92.14           O  
ANISOU 2294  O   TRP A 301     9554  11579  13876   3235   -128   4946       O  
ATOM   2295  CB  TRP A 301     108.244   2.929 -88.051  1.00 93.27           C  
ANISOU 2295  CB  TRP A 301    10131  12149  13158   2959   -188   5603       C  
ATOM   2296  CG  TRP A 301     107.135   3.547 -87.256  1.00 88.81           C  
ANISOU 2296  CG  TRP A 301     9718  11935  12092   2837    -90   5746       C  
ATOM   2297  CD1 TRP A 301     106.129   2.893 -86.604  1.00 89.44           C  
ANISOU 2297  CD1 TRP A 301     9897  12024  12063   2703     24   6079       C  
ATOM   2298  CD2 TRP A 301     106.930   4.942 -87.013  1.00 84.41           C  
ANISOU 2298  CD2 TRP A 301     9228  11782  11062   2838    -99   5542       C  
ATOM   2299  NE1 TRP A 301     105.305   3.796 -85.979  1.00 88.52           N  
ANISOU 2299  NE1 TRP A 301     9879  12345  11410   2642    114   6075       N  
ATOM   2300  CE2 TRP A 301     105.776   5.062 -86.213  1.00 85.24           C  
ANISOU 2300  CE2 TRP A 301     9464  12153  10771   2743     28   5730       C  
ATOM   2301  CE3 TRP A 301     107.608   6.103 -87.397  1.00 83.07           C  
ANISOU 2301  CE3 TRP A 301     9027  11765  10772   2900   -207   5217       C  
ATOM   2302  CZ2 TRP A 301     105.285   6.295 -85.791  1.00 83.39           C  
ANISOU 2302  CZ2 TRP A 301     9337  12320  10026   2756     45   5554       C  
ATOM   2303  CZ3 TRP A 301     107.119   7.327 -86.977  1.00 81.44           C  
ANISOU 2303  CZ3 TRP A 301     8955  11902  10086   2882   -215   5073       C  
ATOM   2304  CH2 TRP A 301     105.969   7.413 -86.183  1.00 82.01           C  
ANISOU 2304  CH2 TRP A 301     9165  12224   9770   2835    -91   5217       C  
ATOM   2305  N   ALA A 302     109.159   0.465 -90.078  1.00101.98           N  
ANISOU 2305  N   ALA A 302    10961  12264  15523   3194   -149   5413       N  
ATOM   2306  CA  ALA A 302     110.304  -0.183 -90.713  1.00105.82           C  
ANISOU 2306  CA  ALA A 302    11317  12474  16415   3384   -249   5202       C  
ATOM   2307  C   ALA A 302     110.296   0.038 -92.220  1.00106.39           C  
ANISOU 2307  C   ALA A 302    11198  12521  16705   3475    -68   4778       C  
ATOM   2308  O   ALA A 302     111.313   0.422 -92.809  1.00106.09           O  
ANISOU 2308  O   ALA A 302    10996  12604  16708   3597   -103   4490       O  
ATOM   2309  CB  ALA A 302     110.311  -1.677 -90.386  1.00109.67           C  
ANISOU 2309  CB  ALA A 302    11915  12476  17279   3417   -347   5442       C  
ATOM   2310  N   ALA A 303     109.151  -0.201 -92.864  1.00107.90           N  
ANISOU 2310  N   ALA A 303    11443  12607  16947   3321    135   4632       N  
ATOM   2311  CA  ALA A 303     109.050   0.035 -94.299  1.00106.63           C  
ANISOU 2311  CA  ALA A 303    11150  12474  16892   3343    313   4147       C  
ATOM   2312  C   ALA A 303     109.159   1.517 -94.634  1.00102.15           C  
ANISOU 2312  C   ALA A 303    10498  12379  15935   3300    384   3935       C  
ATOM   2313  O   ALA A 303     109.666   1.872 -95.704  1.00104.45           O  
ANISOU 2313  O   ALA A 303    10625  12764  16297   3396    464   3598       O  
ATOM   2314  CB  ALA A 303     107.736  -0.534 -94.836  1.00105.90           C  
ANISOU 2314  CB  ALA A 303    11157  12188  16893   3134    480   4019       C  
ATOM   2315  N   TRP A 304     108.697   2.391 -93.737  1.00 97.29           N  
ANISOU 2315  N   TRP A 304    10002  12063  14900   3163    349   4129       N  
ATOM   2316  CA  TRP A 304     108.766   3.828 -93.984  1.00 90.16           C  
ANISOU 2316  CA  TRP A 304     9067  11554  13635   3119    376   3941       C  
ATOM   2317  C   TRP A 304     110.212   4.305 -94.053  1.00 91.11           C  
ANISOU 2317  C   TRP A 304     9019  11786  13814   3278    218   3917       C  
ATOM   2318  O   TRP A 304     110.628   4.934 -95.033  1.00 87.88           O  
ANISOU 2318  O   TRP A 304     8464  11525  13403   3298    291   3635       O  
ATOM   2319  CB  TRP A 304     108.009   4.582 -92.893  1.00 88.02           C  
ANISOU 2319  CB  TRP A 304     8982  11547  12913   2986    340   4148       C  
ATOM   2320  CG  TRP A 304     106.520   4.560 -93.034  1.00 86.28           C  
ANISOU 2320  CG  TRP A 304     8862  11385  12534   2811    536   4086       C  
ATOM   2321  CD1 TRP A 304     105.672   3.567 -92.643  1.00 86.76           C  
ANISOU 2321  CD1 TRP A 304     8993  11264  12707   2697    610   4291       C  
ATOM   2322  CD2 TRP A 304     105.700   5.593 -93.586  1.00 81.74           C  
ANISOU 2322  CD2 TRP A 304     8311  11083  11663   2724    669   3819       C  
ATOM   2323  NE1 TRP A 304     104.373   3.915 -92.921  1.00 83.82           N  
ANISOU 2323  NE1 TRP A 304     8651  11070  12126   2537    792   4160       N  
ATOM   2324  CE2 TRP A 304     104.363   5.155 -93.502  1.00 81.28           C  
ANISOU 2324  CE2 TRP A 304     8306  11027  11551   2574    827   3861       C  
ATOM   2325  CE3 TRP A 304     105.965   6.849 -94.141  1.00 80.39           C  
ANISOU 2325  CE3 TRP A 304     8121  11147  11276   2753    655   3567       C  
ATOM   2326  CZ2 TRP A 304     103.297   5.925 -93.952  1.00 78.89           C  
ANISOU 2326  CZ2 TRP A 304     8017  10976  10983   2489    970   3640       C  
ATOM   2327  CZ3 TRP A 304     104.905   7.611 -94.589  1.00 80.22           C  
ANISOU 2327  CZ3 TRP A 304     8154  11331  10996   2671    785   3358       C  
ATOM   2328  CH2 TRP A 304     103.588   7.150 -94.485  1.00 78.93           C  
ANISOU 2328  CH2 TRP A 304     8024  11187  10778   2559    940   3387       C  
ATOM   2329  N   SER A 305     110.990   4.024 -93.004  1.00 93.41           N  
ANISOU 2329  N   SER A 305     9340  12032  14118   3341     -3   4192       N  
ATOM   2330  CA  SER A 305     112.393   4.429 -92.986  1.00 90.96           C  
ANISOU 2330  CA  SER A 305     8899  11840  13823   3391   -171   4098       C  
ATOM   2331  C   SER A 305     113.174   3.763 -94.110  1.00 89.27           C  
ANISOU 2331  C   SER A 305     8461  11473  13984   3538    -94   3840       C  
ATOM   2332  O   SER A 305     114.026   4.394 -94.746  1.00 84.84           O  
ANISOU 2332  O   SER A 305     7717  11111  13407   3549    -95   3637       O  
ATOM   2333  CB  SER A 305     113.021   4.092 -91.633  1.00 90.87           C  
ANISOU 2333  CB  SER A 305     8989  11787  13750   3407   -427   4388       C  
ATOM   2334  OG  SER A 305     112.408   4.822 -90.584  1.00 92.61           O  
ANISOU 2334  OG  SER A 305     9420  12213  13553   3278   -504   4571       O  
ATOM   2335  N   LYS A 306     112.891   2.484 -94.370  1.00 93.65           N  
ANISOU 2335  N   LYS A 306     9033  11675  14874   3651    -30   3843       N  
ATOM   2336  CA  LYS A 306     113.589   1.761 -95.426  1.00 96.82           C  
ANISOU 2336  CA  LYS A 306     9254  11918  15614   3831     37   3550       C  
ATOM   2337  C   LYS A 306     113.263   2.323 -96.805  1.00 98.08           C  
ANISOU 2337  C   LYS A 306     9294  12250  15721   3796    274   3179       C  
ATOM   2338  O   LYS A 306     114.081   2.217 -97.725  1.00 96.62           O  
ANISOU 2338  O   LYS A 306     8921  12134  15658   3913    330   2893       O  
ATOM   2339  CB  LYS A 306     113.235   0.274 -95.349  1.00 97.06           C  
ANISOU 2339  CB  LYS A 306     9386  11476  16017   3956     22   3632       C  
ATOM   2340  CG  LYS A 306     114.056  -0.639 -96.245  1.00 96.89           C  
ANISOU 2340  CG  LYS A 306     9220  11246  16350   4205     31   3331       C  
ATOM   2341  CD  LYS A 306     113.272  -1.065 -97.475  1.00 92.33           C  
ANISOU 2341  CD  LYS A 306     8635  10493  15954   4235    253   3005       C  
ATOM   2342  CE  LYS A 306     113.612  -2.492 -97.870  1.00 94.94           C  
ANISOU 2342  CE  LYS A 306     8987  10373  16714   4484    192   2852       C  
ATOM   2343  NZ  LYS A 306     113.216  -3.461 -96.809  1.00 97.53           N  
ANISOU 2343  NZ  LYS A 306     9538  10260  17258   4463     16   3243       N  
ATOM   2344  N   PHE A 307     112.088   2.933 -96.965  1.00 97.63           N  
ANISOU 2344  N   PHE A 307     9341  12299  15456   3643    413   3175       N  
ATOM   2345  CA  PHE A 307     111.703   3.470 -98.265  1.00 98.42           C  
ANISOU 2345  CA  PHE A 307     9356  12570  15471   3597    627   2824       C  
ATOM   2346  C   PHE A 307     112.284   4.860 -98.495  1.00 94.98           C  
ANISOU 2346  C   PHE A 307     8835  12530  14724   3486    606   2751       C  
ATOM   2347  O   PHE A 307     112.682   5.189 -99.618  1.00 97.09           O  
ANISOU 2347  O   PHE A 307     8962  12958  14971   3486    726   2465       O  
ATOM   2348  CB  PHE A 307     110.181   3.502 -98.386  1.00 97.03           C  
ANISOU 2348  CB  PHE A 307     9357  12341  15169   3436    765   2790       C  
ATOM   2349  CG  PHE A 307     109.687   3.748 -99.781  1.00102.13           C  
ANISOU 2349  CG  PHE A 307     9952  13090  15764   3392    971   2395       C  
ATOM   2350  CD1 PHE A 307     109.548   2.699-100.675  1.00106.92           C  
ANISOU 2350  CD1 PHE A 307    10514  13438  16673   3499   1073   2134       C  
ATOM   2351  CD2 PHE A 307     109.350   5.026-100.197  1.00102.16           C  
ANISOU 2351  CD2 PHE A 307     9973  13433  15411   3251   1039   2281       C  
ATOM   2352  CE1 PHE A 307     109.089   2.919-101.960  1.00107.13           C  
ANISOU 2352  CE1 PHE A 307    10501  13586  16617   3464   1247   1762       C  
ATOM   2353  CE2 PHE A 307     108.890   5.253-101.481  1.00102.47           C  
ANISOU 2353  CE2 PHE A 307     9974  13581  15378   3215   1213   1943       C  
ATOM   2354  CZ  PHE A 307     108.760   4.198-102.364  1.00104.42           C  
ANISOU 2354  CZ  PHE A 307    10165  13611  15899   3320   1321   1681       C  
ATOM   2355  N   THR A 308     112.342   5.687 -97.448  1.00 91.21           N  
ANISOU 2355  N   THR A 308     8450  12209  13998   3385    443   3012       N  
ATOM   2356  CA  THR A 308     112.806   7.062 -97.608  1.00 81.71           C  
ANISOU 2356  CA  THR A 308     7190  11329  12526   3265    389   2976       C  
ATOM   2357  C   THR A 308     114.282   7.109 -97.987  1.00 84.72           C  
ANISOU 2357  C   THR A 308     7326  11821  13044   3314    319   2902       C  
ATOM   2358  O   THR A 308     114.676   7.849 -98.897  1.00 81.45           O  
ANISOU 2358  O   THR A 308     6769  11633  12547   3242    406   2738       O  
ATOM   2359  CB  THR A 308     112.548   7.853 -96.325  1.00 75.44           C  
ANISOU 2359  CB  THR A 308     6579  10640  11443   3171    190   3248       C  
ATOM   2360  OG1 THR A 308     111.138   8.063 -96.172  1.00 74.51           O  
ANISOU 2360  OG1 THR A 308     6679  10520  11110   3094    294   3242       O  
ATOM   2361  CG2 THR A 308     113.259   9.199 -96.367  1.00 71.79           C  
ANISOU 2361  CG2 THR A 308     6054  10450  10774   3058     57   3243       C  
ATOM   2362  N   ALA A 309     115.117   6.326 -97.300  1.00 90.65           N  
ANISOU 2362  N   ALA A 309     8012  12433  13998   3436    162   3036       N  
ATOM   2363  CA  ALA A 309     116.536   6.295 -97.636  1.00 90.97           C  
ANISOU 2363  CA  ALA A 309     7779  12605  14182   3512     98   2964       C  
ATOM   2364  C   ALA A 309     116.776   5.660 -99.000  1.00 97.49           C  
ANISOU 2364  C   ALA A 309     8430  13415  15197   3642    317   2629       C  
ATOM   2365  O   ALA A 309     117.751   6.000 -99.679  1.00100.62           O  
ANISOU 2365  O   ALA A 309     8573  14049  15610   3651    356   2500       O  
ATOM   2366  CB  ALA A 309     117.316   5.547 -96.556  1.00 93.97           C  
ANISOU 2366  CB  ALA A 309     8142  12836  14726   3643   -137   3174       C  
ATOM   2367  N   ASN A 310     115.900   4.747 -99.417  1.00101.69           N  
ANISOU 2367  N   ASN A 310     9087  13687  15863   3738    456   2483       N  
ATOM   2368  CA  ASN A 310     116.043   4.073-100.701  1.00107.03           C  
ANISOU 2368  CA  ASN A 310     9637  14329  16699   3883    642   2121       C  
ATOM   2369  C   ASN A 310     115.613   4.943-101.877  1.00 97.95           C  
ANISOU 2369  C   ASN A 310     8457  13445  15315   3732    851   1882       C  
ATOM   2370  O   ASN A 310     116.051   4.698-103.007  1.00101.64           O  
ANISOU 2370  O   ASN A 310     8764  14027  15827   3822    993   1578       O  
ATOM   2371  CB  ASN A 310     115.233   2.772-100.682  1.00116.23           C  
ANISOU 2371  CB  ASN A 310    10965  15081  18117   4032    678   2060       C  
ATOM   2372  CG  ASN A 310     115.141   2.115-102.043  1.00122.84           C  
ANISOU 2372  CG  ASN A 310    11726  15866  19082   4178    863   1641       C  
ATOM   2373  OD1 ASN A 310     114.201   2.362-102.799  1.00123.92           O  
ANISOU 2373  OD1 ASN A 310    11946  16041  19097   4075   1030   1456       O  
ATOM   2374  ND2 ASN A 310     116.116   1.273-102.362  1.00125.75           N  
ANISOU 2374  ND2 ASN A 310    11936  16163  19678   4440    821   1470       N  
ATOM   2375  N   VAL A 311     114.792   5.962-101.638  1.00 83.13           N  
ANISOU 2375  N   VAL A 311     6730  13739  11118   3163    272   1775       N  
ATOM   2376  CA  VAL A 311     114.188   6.751-102.701  1.00 75.08           C  
ANISOU 2376  CA  VAL A 311     5769  12721  10037   3007    343   1598       C  
ATOM   2377  C   VAL A 311     114.623   8.208-102.545  1.00 72.03           C  
ANISOU 2377  C   VAL A 311     5378  12610   9381   2840    311   1583       C  
ATOM   2378  O   VAL A 311     115.202   8.605-101.533  1.00 69.67           O  
ANISOU 2378  O   VAL A 311     5043  12485   8942   2839    236   1705       O  
ATOM   2379  CB  VAL A 311     112.652   6.629-102.698  1.00 69.11           C  
ANISOU 2379  CB  VAL A 311     5163  11762   9333   2973    405   1634       C  
ATOM   2380  CG1 VAL A 311     112.062   7.558-101.660  1.00 66.87           C  
ANISOU 2380  CG1 VAL A 311     4977  11599   8830   2872    374   1795       C  
ATOM   2381  CG2 VAL A 311     112.079   6.891-104.081  1.00 66.49           C  
ANISOU 2381  CG2 VAL A 311     4868  11351   9047   2879    486   1408       C  
ATOM   2382  N   GLY A 312     114.339   9.006-103.574  1.00 67.32           N  
ANISOU 2382  N   GLY A 312     4814  12048   8715   2697    368   1424       N  
ATOM   2383  CA  GLY A 312     114.700  10.409-103.560  1.00 69.95           C  
ANISOU 2383  CA  GLY A 312     5144  12612   8823   2526    348   1395       C  
ATOM   2384  C   GLY A 312     113.515  11.348-103.667  1.00 75.12           C  
ANISOU 2384  C   GLY A 312     5937  13244   9361   2375    382   1391       C  
ATOM   2385  O   GLY A 312     113.663  12.563-103.503  1.00 84.15           O  
ANISOU 2385  O   GLY A 312     7090  14556  10328   2226    359   1385       O  
ATOM   2386  N   ILE A 313     112.331  10.799-103.938  1.00 66.79           N  
ANISOU 2386  N   ILE A 313     4985  11974   8418   2410    436   1386       N  
ATOM   2387  CA  ILE A 313     111.127  11.608-104.098  1.00 60.01           C  
ANISOU 2387  CA  ILE A 313     4258  11074   7469   2278    470   1369       C  
ATOM   2388  C   ILE A 313     110.606  12.032-102.731  1.00 57.67           C  
ANISOU 2388  C   ILE A 313     4024  10830   7058   2248    415   1543       C  
ATOM   2389  O   ILE A 313     111.128  11.609-101.694  1.00 63.90           O  
ANISOU 2389  O   ILE A 313     4763  11678   7840   2339    356   1682       O  
ATOM   2390  CB  ILE A 313     110.043  10.849-104.885  1.00 58.41           C  
ANISOU 2390  CB  ILE A 313     4134  10625   7435   2327    547   1280       C  
ATOM   2391  CG1 ILE A 313     109.562   9.629-104.097  1.00 55.65           C  
ANISOU 2391  CG1 ILE A 313     3805  10082   7256   2482    545   1406       C  
ATOM   2392  CG2 ILE A 313     110.566  10.434-106.250  1.00 54.60           C  
ANISOU 2392  CG2 ILE A 313     3580  10110   7055   2353    599   1088       C  
ATOM   2393  CD1 ILE A 313     108.422   8.886-104.761  1.00 54.30           C  
ANISOU 2393  CD1 ILE A 313     3710   9652   7268   2522    622   1310       C  
ATOM   2394  N   GLN A 314     109.570  12.865-102.720  1.00 52.10           N  
ANISOU 2394  N   GLN A 314     3426  10109   6259   2123    432   1533       N  
ATOM   2395  CA  GLN A 314     108.993  13.343-101.471  1.00 56.01           C  
ANISOU 2395  CA  GLN A 314     3979  10664   6639   2079    383   1674       C  
ATOM   2396  C   GLN A 314     108.049  12.302-100.881  1.00 53.12           C  
ANISOU 2396  C   GLN A 314     3682  10104   6397   2200    409   1798       C  
ATOM   2397  O   GLN A 314     107.173  11.778-101.578  1.00 52.86           O  
ANISOU 2397  O   GLN A 314     3716   9866   6503   2229    481   1730       O  
ATOM   2398  CB  GLN A 314     108.246  14.657-101.698  1.00 57.79           C  
ANISOU 2398  CB  GLN A 314     4284  10942   6731   1894    388   1604       C  
ATOM   2399  CG  GLN A 314     107.445  15.127-100.496  1.00 48.73           C  
ANISOU 2399  CG  GLN A 314     3201   9835   5480   1842    344   1718       C  
ATOM   2400  CD  GLN A 314     106.865  16.514-100.683  1.00 46.94           C  
ANISOU 2400  CD  GLN A 314     3033   9674   5129   1652    334   1632       C  
ATOM   2401  OE1 GLN A 314     107.482  17.512-100.312  1.00 47.08           O  
ANISOU 2401  OE1 GLN A 314     3000   9870   5019   1540    276   1612       O  
ATOM   2402  NE2 GLN A 314     105.672  16.584-101.260  1.00 45.38           N  
ANISOU 2402  NE2 GLN A 314     2938   9323   4982   1615    390   1572       N  
ATOM   2403  N   ILE A 315     108.230  12.003 -99.596  1.00 55.98           N  
ANISOU 2403  N   ILE A 315     4026  10534   6711   2270    355   1979       N  
ATOM   2404  CA  ILE A 315     107.340  11.117 -98.849  1.00 60.98           C  
ANISOU 2404  CA  ILE A 315     4726  11005   7439   2373    380   2140       C  
ATOM   2405  C   ILE A 315     106.726  11.931 -97.718  1.00 59.67           C  
ANISOU 2405  C   ILE A 315     4614  10973   7084   2281    336   2249       C  
ATOM   2406  O   ILE A 315     107.446  12.453 -96.859  1.00 60.77           O  
ANISOU 2406  O   ILE A 315     4696  11333   7059   2252    258   2311       O  
ATOM   2407  CB  ILE A 315     108.067   9.875 -98.305  1.00 61.23           C  
ANISOU 2407  CB  ILE A 315     4689  10982   7592   2557    361   2284       C  
ATOM   2408  CG1 ILE A 315     108.285   8.836 -99.407  1.00 62.37           C  
ANISOU 2408  CG1 ILE A 315     4799  10917   7984   2662    420   2169       C  
ATOM   2409  CG2 ILE A 315     107.242   9.220 -97.217  1.00 56.56           C  
ANISOU 2409  CG2 ILE A 315     4167  10288   7036   2636    375   2503       C  
ATOM   2410  CD1 ILE A 315     109.297   9.215-100.446  1.00 63.19           C  
ANISOU 2410  CD1 ILE A 315     4811  11126   8073   2620    410   1976       C  
ATOM   2411  N   VAL A 316     105.401  12.041 -97.719  1.00 59.21           N  
ANISOU 2411  N   VAL A 316     4658  10787   7052   2234    386   2252       N  
ATOM   2412  CA  VAL A 316     104.680  12.920 -96.807  1.00 60.48           C  
ANISOU 2412  CA  VAL A 316     4871  11071   7038   2125    348   2310       C  
ATOM   2413  C   VAL A 316     103.864  12.071 -95.843  1.00 56.78           C  
ANISOU 2413  C   VAL A 316     4457  10495   6624   2224    376   2514       C  
ATOM   2414  O   VAL A 316     103.150  11.151 -96.261  1.00 57.97           O  
ANISOU 2414  O   VAL A 316     4658  10395   6975   2309    460   2537       O  
ATOM   2415  CB  VAL A 316     103.790  13.913 -97.575  1.00 58.18           C  
ANISOU 2415  CB  VAL A 316     4649  10744   6713   1969    376   2138       C  
ATOM   2416  CG1 VAL A 316     103.191  13.249 -98.798  1.00 58.62           C  
ANISOU 2416  CG1 VAL A 316     4756  10549   6970   2017    473   2026       C  
ATOM   2417  CG2 VAL A 316     102.702  14.485 -96.670  1.00 48.48           C  
ANISOU 2417  CG2 VAL A 316     3486   9561   5372   1889    357   2201       C  
ATOM   2418  N   GLY A 317     103.978  12.378 -94.552  1.00 54.64           N  
ANISOU 2418  N   GLY A 317     4173  10411   6176   2209    311   2654       N  
ATOM   2419  CA  GLY A 317     103.242  11.665 -93.530  1.00 61.69           C  
ANISOU 2419  CA  GLY A 317     5117  11240   7083   2290    337   2869       C  
ATOM   2420  C   GLY A 317     101.908  12.311 -93.219  1.00 60.29           C  
ANISOU 2420  C   GLY A 317     5024  11058   6827   2180    353   2852       C  
ATOM   2421  O   GLY A 317     101.847  13.495 -92.872  1.00 61.36           O  
ANISOU 2421  O   GLY A 317     5154  11393   6766   2036    287   2758       O  
ATOM   2422  N   ASP A 318     100.828  11.542 -93.352  1.00 58.65           N  
ANISOU 2422  N   ASP A 318     4887  10609   6788   2243    443   2929       N  
ATOM   2423  CA  ASP A 318      99.481  12.019 -93.052  1.00 59.60           C  
ANISOU 2423  CA  ASP A 318     5118  10673   6853   2126    475   2896       C  
ATOM   2424  C   ASP A 318      98.932  11.277 -91.840  1.00 59.60           C  
ANISOU 2424  C   ASP A 318     5164  10647   6835   2198    505   3153       C  
ATOM   2425  O   ASP A 318      98.780  11.869 -90.769  1.00 56.06           O  
ANISOU 2425  O   ASP A 318     4720  10421   6158   2132    443   3226       O  
ATOM   2426  CB  ASP A 318      98.565  11.856 -94.273  1.00 58.73           C  
ANISOU 2426  CB  ASP A 318     5112  10260   6942   2067    577   2697       C  
ATOM   2427  CG  ASP A 318      97.113  12.267 -93.996  1.00 63.67           C  
ANISOU 2427  CG  ASP A 318     5888  10774   7528   1922    622   2623       C  
ATOM   2428  OD1 ASP A 318      96.213  11.816 -94.742  1.00 61.44           O  
ANISOU 2428  OD1 ASP A 318     5692  10219   7432   1910    718   2515       O  
ATOM   2429  OD2 ASP A 318      96.865  13.050 -93.051  1.00 63.51           O  
ANISOU 2429  OD2 ASP A 318     5891  10947   7295   1820    561   2653       O  
ATOM   2430  N   ASP A 319      98.648   9.981 -91.975  1.00 63.92           N  
ANISOU 2430  N   ASP A 319     5736  10929   7621   2336    601   3294       N  
ATOM   2431  CA  ASP A 319      98.087   9.226 -90.864  1.00 69.57           C  
ANISOU 2431  CA  ASP A 319     6499  11595   8339   2403    647   3563       C  
ATOM   2432  C   ASP A 319      99.117   8.890 -89.797  1.00 71.69           C  
ANISOU 2432  C   ASP A 319     6693  12078   8469   2495    583   3777       C  
ATOM   2433  O   ASP A 319      98.728   8.584 -88.666  1.00 81.23           O  
ANISOU 2433  O   ASP A 319     7938  13344   9581   2503    604   3977       O  
ATOM   2434  CB  ASP A 319      97.436   7.938 -91.369  1.00 75.71           C  
ANISOU 2434  CB  ASP A 319     7334  11981   9451   2497    785   3625       C  
ATOM   2435  CG  ASP A 319      96.074   8.177 -91.983  1.00 77.22           C  
ANISOU 2435  CG  ASP A 319     7659  11939   9742   2345    878   3410       C  
ATOM   2436  OD1 ASP A 319      95.468   9.232 -91.699  1.00 73.87           O  
ANISOU 2436  OD1 ASP A 319     7303  11654   9111   2176    843   3287       O  
ATOM   2437  OD2 ASP A 319      95.607   7.303 -92.743  1.00 78.89           O  
ANISOU 2437  OD2 ASP A 319     7898  11829  10246   2400    984   3354       O  
ATOM   2438  N   LEU A 320     100.415   8.928 -90.114  1.00 70.24           N  
ANISOU 2438  N   LEU A 320     6418  12000   8269   2538    518   3705       N  
ATOM   2439  CA  LEU A 320     101.402   8.590 -89.096  1.00 73.70           C  
ANISOU 2439  CA  LEU A 320     6794  12626   8584   2612    464   3868       C  
ATOM   2440  C   LEU A 320     101.909   9.797 -88.317  1.00 69.17           C  
ANISOU 2440  C   LEU A 320     6169  12422   7692   2496    358   3781       C  
ATOM   2441  O   LEU A 320     102.417   9.622 -87.205  1.00 76.94           O  
ANISOU 2441  O   LEU A 320     7109  13590   8533   2540    322   3919       O  
ATOM   2442  CB  LEU A 320     102.591   7.822 -89.701  1.00 82.57           C  
ANISOU 2442  CB  LEU A 320     7840  13660   9873   2744    452   3863       C  
ATOM   2443  CG  LEU A 320     103.558   8.247 -90.814  1.00 81.84           C  
ANISOU 2443  CG  LEU A 320     7672  13603   9820   2727    402   3630       C  
ATOM   2444  CD1 LEU A 320     104.206   9.601 -90.606  1.00 83.57           C  
ANISOU 2444  CD1 LEU A 320     7835  14148   9772   2596    300   3475       C  
ATOM   2445  CD2 LEU A 320     104.641   7.196 -90.882  1.00 77.50           C  
ANISOU 2445  CD2 LEU A 320     7051  12982   9415   2888    392   3721       C  
ATOM   2446  N   THR A 321     101.789  11.008 -88.859  1.00 57.18           N  
ANISOU 2446  N   THR A 321     4646  11008   6070   2350    309   3545       N  
ATOM   2447  CA  THR A 321     102.144  12.204 -88.105  1.00 56.99           C  
ANISOU 2447  CA  THR A 321     4576  11304   5776   2221    218   3434       C  
ATOM   2448  C   THR A 321     100.937  12.947 -87.548  1.00 58.94           C  
ANISOU 2448  C   THR A 321     4894  11614   5887   2083    222   3388       C  
ATOM   2449  O   THR A 321     101.088  13.678 -86.564  1.00 56.95           O  
ANISOU 2449  O   THR A 321     4602  11614   5421   2000    163   3342       O  
ATOM   2450  CB  THR A 321     102.959  13.170 -88.972  1.00 55.62           C  
ANISOU 2450  CB  THR A 321     4337  11223   5571   2129    154   3190       C  
ATOM   2451  OG1 THR A 321     102.413  13.203 -90.295  1.00 63.86           O  
ANISOU 2451  OG1 THR A 321     5430  12045   6791   2101    204   3068       O  
ATOM   2452  CG2 THR A 321     104.427  12.748 -89.029  1.00 60.27           C  
ANISOU 2452  CG2 THR A 321     4825  11893   6183   2234    114   3216       C  
ATOM   2453  N   VAL A 322      99.758  12.774 -88.155  1.00 58.24           N  
ANISOU 2453  N   VAL A 322     4902  11302   5925   2061    289   3381       N  
ATOM   2454  CA  VAL A 322      98.493  13.414 -87.783  1.00 57.88           C  
ANISOU 2454  CA  VAL A 322     4941  11275   5774   1930    299   3326       C  
ATOM   2455  C   VAL A 322      98.688  14.834 -87.255  1.00 54.68           C  
ANISOU 2455  C   VAL A 322     4492  11149   5136   1760    203   3121       C  
ATOM   2456  O   VAL A 322      98.000  15.258 -86.318  1.00 56.65           O  
ANISOU 2456  O   VAL A 322     4771  11514   5239   1671    195   3108       O  
ATOM   2457  CB  VAL A 322      97.707  12.552 -86.771  1.00 58.55           C  
ANISOU 2457  CB  VAL A 322     5091  11299   5856   1986    376   3560       C  
ATOM   2458  CG1 VAL A 322      97.363  11.206 -87.383  1.00 61.70           C  
ANISOU 2458  CG1 VAL A 322     5542  11366   6536   2135    486   3740       C  
ATOM   2459  CG2 VAL A 322      98.475  12.360 -85.469  1.00 57.03           C  
ANISOU 2459  CG2 VAL A 322     4817  11345   5507   2034    338   3685       C  
ATOM   2460  N   THR A 323      99.614  15.580 -87.866  1.00 53.24           N  
ANISOU 2460  N   THR A 323     4234  11059   4936   1708    137   2945       N  
ATOM   2461  CA  THR A 323      99.933  16.952 -87.458  1.00 55.45           C  
ANISOU 2461  CA  THR A 323     4460  11571   5039   1547     52   2735       C  
ATOM   2462  C   THR A 323     100.233  17.025 -85.962  1.00 66.45           C  
ANISOU 2462  C   THR A 323     5791  13206   6251   1552     20   2800       C  
ATOM   2463  O   THR A 323      99.997  18.047 -85.313  1.00 75.07           O  
ANISOU 2463  O   THR A 323     6859  14465   7199   1418    -30   2645       O  
ATOM   2464  CB  THR A 323      98.806  17.925 -87.833  1.00 55.98           C  
ANISOU 2464  CB  THR A 323     4604  11583   5083   1382     41   2551       C  
ATOM   2465  OG1 THR A 323      98.150  17.475 -89.025  1.00 52.25           O  
ANISOU 2465  OG1 THR A 323     4207  10859   4787   1423     96   2564       O  
ATOM   2466  CG2 THR A 323      99.359  19.327 -88.077  1.00 47.64           C  
ANISOU 2466  CG2 THR A 323     3486  10661   3954   1224    -36   2300       C  
ATOM   2467  N   ASN A 324     100.747  15.923 -85.406  1.00 67.08           N  
ANISOU 2467  N   ASN A 324     5839  13300   6349   1713     48   3025       N  
ATOM   2468  CA  ASN A 324     101.005  15.807 -83.979  1.00 70.16           C  
ANISOU 2468  CA  ASN A 324     6167  13918   6574   1749     25   3122       C  
ATOM   2469  C   ASN A 324     102.491  16.005 -83.729  1.00 75.47           C  
ANISOU 2469  C   ASN A 324     6714  14791   7169   1798    -43   3084       C  
ATOM   2470  O   ASN A 324     103.297  15.164 -84.157  1.00 71.58           O  
ANISOU 2470  O   ASN A 324     6196  14219   6782   1934    -32   3205       O  
ATOM   2471  CB  ASN A 324     100.554  14.443 -83.460  1.00 72.89           C  
ANISOU 2471  CB  ASN A 324     6562  14146   6989   1896    104   3414       C  
ATOM   2472  CG  ASN A 324     100.781  14.280 -81.971  1.00 78.42           C  
ANISOU 2472  CG  ASN A 324     7194  15090   7511   1941     83   3531       C  
ATOM   2473  OD1 ASN A 324     101.808  13.755 -81.540  1.00 79.46           O  
ANISOU 2473  OD1 ASN A 324     7246  15334   7611   2064     58   3652       O  
ATOM   2474  ND2 ASN A 324      99.816  14.726 -81.175  1.00 80.87           N  
ANISOU 2474  ND2 ASN A 324     7531  15492   7704   1845     89   3491       N  
ATOM   2475  N   PRO A 325     102.898  17.076 -83.043  1.00 77.80           N  
ANISOU 2475  N   PRO A 325     6926  15340   7293   1695   -114   2911       N  
ATOM   2476  CA  PRO A 325     104.335  17.386 -82.948  1.00 83.01           C  
ANISOU 2476  CA  PRO A 325     7469  16181   7891   1726   -181   2838       C  
ATOM   2477  C   PRO A 325     105.183  16.260 -82.376  1.00 79.39           C  
ANISOU 2477  C   PRO A 325     6952  15793   7419   1919   -180   3066       C  
ATOM   2478  O   PRO A 325     106.258  15.976 -82.919  1.00 78.23           O  
ANISOU 2478  O   PRO A 325     6752  15632   7339   1995   -205   3069       O  
ATOM   2479  CB  PRO A 325     104.355  18.631 -82.049  1.00 87.06           C  
ANISOU 2479  CB  PRO A 325     7910  16949   8220   1590   -241   2636       C  
ATOM   2480  CG  PRO A 325     103.013  19.266 -82.269  1.00 79.17           C  
ANISOU 2480  CG  PRO A 325     7004  15835   7243   1444   -216   2518       C  
ATOM   2481  CD  PRO A 325     102.060  18.117 -82.421  1.00 78.81           C  
ANISOU 2481  CD  PRO A 325     7063  15584   7297   1538   -137   2744       C  
ATOM   2482  N   LYS A 326     104.734  15.600 -81.306  1.00 69.56           N  
ANISOU 2482  N   LYS A 326     5713  14620   6096   2001   -153   3257       N  
ATOM   2483  CA  LYS A 326     105.560  14.555 -80.712  1.00 78.82           C  
ANISOU 2483  CA  LYS A 326     6829  15868   7252   2187   -158   3482       C  
ATOM   2484  C   LYS A 326     105.643  13.324 -81.607  1.00 79.65           C  
ANISOU 2484  C   LYS A 326     6998  15681   7586   2322    -99   3666       C  
ATOM   2485  O   LYS A 326     106.662  12.622 -81.598  1.00 75.31           O  
ANISOU 2485  O   LYS A 326     6389  15150   7077   2464   -122   3777       O  
ATOM   2486  CB  LYS A 326     105.036  14.180 -79.326  1.00 83.14           C  
ANISOU 2486  CB  LYS A 326     7364  16571   7654   2237   -140   3649       C  
ATOM   2487  CG  LYS A 326     106.021  13.349 -78.516  1.00 87.63           C  
ANISOU 2487  CG  LYS A 326     7848  17295   8152   2417   -168   3851       C  
ATOM   2488  CD  LYS A 326     105.880  13.599 -77.022  1.00 91.89           C  
ANISOU 2488  CD  LYS A 326     8315  18142   8457   2423   -194   3892       C  
ATOM   2489  CE  LYS A 326     104.492  13.236 -76.517  1.00 88.10           C  
ANISOU 2489  CE  LYS A 326     7923  17576   7976   2394   -117   4029       C  
ATOM   2490  NZ  LYS A 326     104.383  13.431 -75.044  1.00 91.80           N  
ANISOU 2490  NZ  LYS A 326     8310  18362   8210   2410   -141   4077       N  
ATOM   2491  N   ARG A 327     104.597  13.043 -82.386  1.00 77.46           N  
ANISOU 2491  N   ARG A 327     6835  15129   7467   2285    -25   3691       N  
ATOM   2492  CA  ARG A 327     104.703  11.981 -83.380  1.00 80.95           C  
ANISOU 2492  CA  ARG A 327     7327  15279   8153   2404     32   3814       C  
ATOM   2493  C   ARG A 327     105.625  12.384 -84.526  1.00 80.29           C  
ANISOU 2493  C   ARG A 327     7195  15158   8154   2383    -12   3630       C  
ATOM   2494  O   ARG A 327     106.333  11.535 -85.079  1.00 81.25           O  
ANISOU 2494  O   ARG A 327     7293  15152   8428   2514     -3   3712       O  
ATOM   2495  CB  ARG A 327     103.319  11.608 -83.912  1.00 78.90           C  
ANISOU 2495  CB  ARG A 327     7195  14740   8045   2370    126   3870       C  
ATOM   2496  CG  ARG A 327     102.647  10.468 -83.158  1.00 80.33           C  
ANISOU 2496  CG  ARG A 327     7431  14808   8283   2477    206   4154       C  
ATOM   2497  CD  ARG A 327     101.903   9.555 -84.119  1.00 79.89           C  
ANISOU 2497  CD  ARG A 327     7474  14374   8506   2534    307   4249       C  
ATOM   2498  NE  ARG A 327     102.148   8.143 -83.840  1.00 85.74           N  
ANISOU 2498  NE  ARG A 327     8217  14953   9407   2709    366   4520       N  
ATOM   2499  CZ  ARG A 327     102.054   7.173 -84.744  1.00 84.97           C  
ANISOU 2499  CZ  ARG A 327     8159  14527   9599   2806    438   4592       C  
ATOM   2500  NH1 ARG A 327     101.728   7.457 -85.997  1.00 73.78           N  
ANISOU 2500  NH1 ARG A 327     6777  12925   8329   2753    460   4410       N  
ATOM   2501  NH2 ARG A 327     102.296   5.916 -84.397  1.00 89.80           N  
ANISOU 2501  NH2 ARG A 327     8767  14991  10362   2958    488   4835       N  
ATOM   2502  N   ILE A 328     105.631  13.670 -84.889  1.00 76.62           N  
ANISOU 2502  N   ILE A 328     6712  14799   7601   2218    -57   3378       N  
ATOM   2503  CA  ILE A 328     106.555  14.161 -85.908  1.00 67.03           C  
ANISOU 2503  CA  ILE A 328     5442  13579   6449   2181    -97   3198       C  
ATOM   2504  C   ILE A 328     107.994  14.003 -85.437  1.00 70.43           C  
ANISOU 2504  C   ILE A 328     5750  14205   6805   2274   -165   3217       C  
ATOM   2505  O   ILE A 328     108.881  13.631 -86.217  1.00 70.99           O  
ANISOU 2505  O   ILE A 328     5774  14204   6993   2346   -176   3193       O  
ATOM   2506  CB  ILE A 328     106.230  15.626 -86.255  1.00 63.94           C  
ANISOU 2506  CB  ILE A 328     5056  13263   5974   1974   -129   2938       C  
ATOM   2507  CG1 ILE A 328     104.846  15.733 -86.900  1.00 61.14           C  
ANISOU 2507  CG1 ILE A 328     4822  12694   5715   1894    -68   2910       C  
ATOM   2508  CG2 ILE A 328     107.296  16.217 -87.164  1.00 64.90           C  
ANISOU 2508  CG2 ILE A 328     5107  13415   6139   1924   -171   2759       C  
ATOM   2509  CD1 ILE A 328     104.329  17.150 -86.996  1.00 55.50           C  
ANISOU 2509  CD1 ILE A 328     4124  12056   4907   1691   -102   2680       C  
ATOM   2510  N   GLU A 329     108.246  14.279 -84.152  1.00 73.61           N  
ANISOU 2510  N   GLU A 329     6092  14866   7011   2279   -212   3251       N  
ATOM   2511  CA  GLU A 329     109.585  14.118 -83.592  1.00 75.82           C  
ANISOU 2511  CA  GLU A 329     6249  15353   7204   2379   -282   3273       C  
ATOM   2512  C   GLU A 329     110.102  12.701 -83.796  1.00 77.24           C  
ANISOU 2512  C   GLU A 329     6425  15389   7535   2582   -261   3491       C  
ATOM   2513  O   GLU A 329     111.293  12.496 -84.056  1.00 72.03           O  
ANISOU 2513  O   GLU A 329     5675  14786   6906   2663   -312   3460       O  
ATOM   2514  CB  GLU A 329     109.577  14.469 -82.104  1.00 77.50           C  
ANISOU 2514  CB  GLU A 329     6405  15854   7187   2374   -322   3305       C  
ATOM   2515  CG  GLU A 329     109.174  15.900 -81.790  1.00 83.50           C  
ANISOU 2515  CG  GLU A 329     7149  16774   7805   2178   -352   3066       C  
ATOM   2516  CD  GLU A 329     110.350  16.855 -81.755  1.00 92.81           C  
ANISOU 2516  CD  GLU A 329     8205  18165   8893   2115   -434   2848       C  
ATOM   2517  OE1 GLU A 329     111.473  16.444 -82.120  1.00 96.54           O  
ANISOU 2517  OE1 GLU A 329     8608  18652   9422   2213   -468   2867       O  
ATOM   2518  OE2 GLU A 329     110.151  18.021 -81.353  1.00 93.76           O  
ANISOU 2518  OE2 GLU A 329     8294  18432   8897   1967   -465   2649       O  
ATOM   2519  N   ARG A 330     109.217  11.710 -83.684  1.00 78.50           N  
ANISOU 2519  N   ARG A 330     6677  15349   7802   2666   -186   3706       N  
ATOM   2520  CA  ARG A 330     109.621  10.325 -83.899  1.00 79.11           C  
ANISOU 2520  CA  ARG A 330     6756  15245   8058   2858   -159   3914       C  
ATOM   2521  C   ARG A 330     109.973  10.074 -85.362  1.00 76.88           C  
ANISOU 2521  C   ARG A 330     6477  14731   8001   2874   -140   3804       C  
ATOM   2522  O   ARG A 330     110.996   9.449 -85.664  1.00 79.99           O  
ANISOU 2522  O   ARG A 330     6801  15099   8494   2999   -173   3833       O  
ATOM   2523  CB  ARG A 330     108.510   9.382 -83.439  1.00 79.51           C  
ANISOU 2523  CB  ARG A 330     6907  15114   8189   2925    -71   4162       C  
ATOM   2524  CG  ARG A 330     108.790   7.921 -83.727  1.00 84.32           C  
ANISOU 2524  CG  ARG A 330     7528  15478   9030   3114    -31   4376       C  
ATOM   2525  CD  ARG A 330     107.704   7.028 -83.154  1.00 88.87           C  
ANISOU 2525  CD  ARG A 330     8198  15883   9685   3169     62   4632       C  
ATOM   2526  NE  ARG A 330     107.963   5.617 -83.425  1.00 91.49           N  
ANISOU 2526  NE  ARG A 330     8541  15953  10269   3345    105   4834       N  
ATOM   2527  CZ  ARG A 330     107.178   4.622 -83.024  1.00 89.73           C  
ANISOU 2527  CZ  ARG A 330     8390  15526  10176   3418    195   5080       C  
ATOM   2528  NH1 ARG A 330     106.078   4.880 -82.331  1.00 88.52           N  
ANISOU 2528  NH1 ARG A 330     8305  15416   9912   3330    252   5157       N  
ATOM   2529  NH2 ARG A 330     107.494   3.367 -83.317  1.00 89.26           N  
ANISOU 2529  NH2 ARG A 330     8330  15214  10371   3575    229   5241       N  
ATOM   2530  N   ALA A 331     109.136  10.557 -86.287  1.00 72.21           N  
ANISOU 2530  N   ALA A 331     5963  13977   7495   2751    -89   3669       N  
ATOM   2531  CA  ALA A 331     109.387  10.341 -87.710  1.00 69.18           C  
ANISOU 2531  CA  ALA A 331     5580  13382   7323   2761    -62   3549       C  
ATOM   2532  C   ALA A 331     110.644  11.055 -88.196  1.00 71.45           C  
ANISOU 2532  C   ALA A 331     5757  13835   7556   2716   -136   3348       C  
ATOM   2533  O   ALA A 331     111.228  10.639 -89.204  1.00 70.89           O  
ANISOU 2533  O   ALA A 331     5648  13633   7653   2773   -126   3278       O  
ATOM   2534  CB  ALA A 331     108.180  10.793 -88.533  1.00 68.05           C  
ANISOU 2534  CB  ALA A 331     5539  13059   7256   2635      5   3440       C  
ATOM   2535  N   VAL A 332     111.067  12.117 -87.509  1.00 74.64           N  
ANISOU 2535  N   VAL A 332     6101  14521   7740   2612   -204   3241       N  
ATOM   2536  CA  VAL A 332     112.328  12.775 -87.847  1.00 73.07           C  
ANISOU 2536  CA  VAL A 332     5784  14487   7491   2572   -272   3062       C  
ATOM   2537  C   VAL A 332     113.505  11.857 -87.542  1.00 79.34           C  
ANISOU 2537  C   VAL A 332     6481  15339   8327   2756   -319   3171       C  
ATOM   2538  O   VAL A 332     114.305  11.527 -88.425  1.00 70.82           O  
ANISOU 2538  O   VAL A 332     5341  14182   7386   2811   -325   3098       O  
ATOM   2539  CB  VAL A 332     112.460  14.111 -87.095  1.00 70.82           C  
ANISOU 2539  CB  VAL A 332     5454  14476   6979   2419   -331   2917       C  
ATOM   2540  CG1 VAL A 332     113.903  14.590 -87.126  1.00 74.12           C  
ANISOU 2540  CG1 VAL A 332     5730  15090   7340   2416   -407   2779       C  
ATOM   2541  CG2 VAL A 332     111.548  15.151 -87.704  1.00 64.52           C  
ANISOU 2541  CG2 VAL A 332     4731  13605   6178   2224   -298   2753       C  
ATOM   2542  N   GLU A 333     113.632  11.438 -86.279  1.00 81.90           N  
ANISOU 2542  N   GLU A 333     6781  15808   8528   2856   -354   3343       N  
ATOM   2543  CA  GLU A 333     114.768  10.616 -85.880  1.00 94.89           C  
ANISOU 2543  CA  GLU A 333     8328  17530  10195   3035   -411   3451       C  
ATOM   2544  C   GLU A 333     114.732   9.243 -86.538  1.00 94.29           C  
ANISOU 2544  C   GLU A 333     8287  17162  10379   3197   -364   3597       C  
ATOM   2545  O   GLU A 333     115.786   8.636 -86.759  1.00 98.00           O  
ANISOU 2545  O   GLU A 333     8665  17630  10940   3327   -409   3607       O  
ATOM   2546  CB  GLU A 333     114.808  10.485 -84.359  1.00101.95           C  
ANISOU 2546  CB  GLU A 333     9197  18649  10891   3105   -453   3613       C  
ATOM   2547  CG  GLU A 333     114.980  11.818 -83.656  1.00105.28           C  
ANISOU 2547  CG  GLU A 333     9560  19376  11068   2959   -508   3440       C  
ATOM   2548  CD  GLU A 333     114.559  11.779 -82.201  1.00109.97           C  
ANISOU 2548  CD  GLU A 333    10157  20165  11463   2993   -521   3585       C  
ATOM   2549  OE1 GLU A 333     114.927  10.817 -81.492  1.00112.61           O  
ANISOU 2549  OE1 GLU A 333    10461  20541  11784   3169   -540   3800       O  
ATOM   2550  OE2 GLU A 333     113.849  12.713 -81.771  1.00109.29           O  
ANISOU 2550  OE2 GLU A 333    10098  20189  11237   2844   -510   3481       O  
ATOM   2551  N   GLU A 334     113.543   8.740 -86.859  1.00 90.47           N  
ANISOU 2551  N   GLU A 334     7924  16423  10026   3192   -274   3697       N  
ATOM   2552  CA  GLU A 334     113.414   7.482 -87.579  1.00 87.23           C  
ANISOU 2552  CA  GLU A 334     7546  15700   9895   3329   -218   3800       C  
ATOM   2553  C   GLU A 334     113.521   7.658 -89.088  1.00 87.29           C  
ANISOU 2553  C   GLU A 334     7547  15541  10080   3271   -184   3583       C  
ATOM   2554  O   GLU A 334     113.574   6.654 -89.808  1.00 74.47           O  
ANISOU 2554  O   GLU A 334     5925  13667   8705   3384   -145   3612       O  
ATOM   2555  CB  GLU A 334     112.082   6.806 -87.227  1.00 86.85           C  
ANISOU 2555  CB  GLU A 334     7626  15441   9931   3355   -128   4003       C  
ATOM   2556  CG  GLU A 334     112.166   5.292 -87.141  1.00 91.04           C  
ANISOU 2556  CG  GLU A 334     8166  15735  10689   3551    -96   4225       C  
ATOM   2557  CD  GLU A 334     111.148   4.704 -86.187  1.00 96.33           C  
ANISOU 2557  CD  GLU A 334     8929  16323  11347   3588    -32   4488       C  
ATOM   2558  OE1 GLU A 334     110.765   3.532 -86.373  1.00101.24           O  
ANISOU 2558  OE1 GLU A 334     9598  16655  12215   3701     35   4649       O  
ATOM   2559  OE2 GLU A 334     110.733   5.411 -85.246  1.00 96.24           O  
ANISOU 2559  OE2 GLU A 334     8939  16536  11091   3499    -45   4526       O  
ATOM   2560  N   LYS A 335     113.559   8.902 -89.573  1.00 83.79           N  
ANISOU 2560  N   LYS A 335     7090  15228   9520   3096   -197   3362       N  
ATOM   2561  CA  LYS A 335     113.647   9.212 -91.003  1.00 84.55           C  
ANISOU 2561  CA  LYS A 335     7176  15199   9751   3020   -160   3148       C  
ATOM   2562  C   LYS A 335     112.603   8.444 -91.808  1.00 85.96           C  
ANISOU 2562  C   LYS A 335     7454  15048  10158   3054    -62   3181       C  
ATOM   2563  O   LYS A 335     112.872   7.941 -92.902  1.00 88.01           O  
ANISOU 2563  O   LYS A 335     7685  15138  10618   3102    -27   3075       O  
ATOM   2564  CB  LYS A 335     115.055   8.951 -91.540  1.00 85.83           C  
ANISOU 2564  CB  LYS A 335     7203  15419   9990   3100   -210   3046       C  
ATOM   2565  CG  LYS A 335     116.075   9.977 -91.076  1.00 89.38           C  
ANISOU 2565  CG  LYS A 335     7546  16185  10231   3019   -295   2932       C  
ATOM   2566  CD  LYS A 335     117.415   9.799 -91.762  1.00 94.26           C  
ANISOU 2566  CD  LYS A 335     8026  16850  10938   3079   -333   2803       C  
ATOM   2567  CE  LYS A 335     118.396  10.873 -91.318  1.00 95.41           C  
ANISOU 2567  CE  LYS A 335     8063  17302  10888   2985   -410   2676       C  
ATOM   2568  NZ  LYS A 335     117.858  12.243 -91.550  1.00 92.09           N  
ANISOU 2568  NZ  LYS A 335     7690  16959  10342   2761   -386   2526       N  
ATOM   2569  N   ALA A 336     111.390   8.358 -91.253  1.00 81.06           N  
ANISOU 2569  N   ALA A 336     6945  14342   9510   3027    -13   3313       N  
ATOM   2570  CA  ALA A 336     110.309   7.662 -91.938  1.00 71.45           C  
ANISOU 2570  CA  ALA A 336     5824  12810   8513   3053     85   3340       C  
ATOM   2571  C   ALA A 336     109.856   8.413 -93.182  1.00 68.63           C  
ANISOU 2571  C   ALA A 336     5499  12381   8197   2913    129   3102       C  
ATOM   2572  O   ALA A 336     109.468   7.786 -94.174  1.00 74.71           O  
ANISOU 2572  O   ALA A 336     6296  12900   9190   2954    199   3030       O  
ATOM   2573  CB  ALA A 336     109.130   7.457 -90.987  1.00 73.68           C  
ANISOU 2573  CB  ALA A 336     6211  13039   8744   3047    129   3540       C  
ATOM   2574  N   CYS A 337     109.903   9.742 -93.154  1.00 65.80           N  
ANISOU 2574  N   CYS A 337     5134  12233   7634   2748     89   2968       N  
ATOM   2575  CA  CYS A 337     109.436  10.550 -94.270  1.00 63.17           C  
ANISOU 2575  CA  CYS A 337     4836  11846   7319   2605    129   2758       C  
ATOM   2576  C   CYS A 337     110.196  11.871 -94.282  1.00 63.42           C  
ANISOU 2576  C   CYS A 337     4802  12139   7158   2460     63   2607       C  
ATOM   2577  O   CYS A 337     111.005  12.156 -93.395  1.00 66.18           O  
ANISOU 2577  O   CYS A 337     5078  12706   7362   2469    -12   2652       O  
ATOM   2578  CB  CYS A 337     107.923  10.775 -94.184  1.00 60.51           C  
ANISOU 2578  CB  CYS A 337     4624  11385   6982   2529    187   2788       C  
ATOM   2579  SG  CYS A 337     107.370  11.558 -92.663  1.00 62.16           S  
ANISOU 2579  SG  CYS A 337     4873  11813   6931   2440    134   2908       S  
ATOM   2580  N   ASN A 338     109.923  12.682 -95.307  1.00 61.53           N  
ANISOU 2580  N   ASN A 338     4586  11869   6924   2323     94   2422       N  
ATOM   2581  CA  ASN A 338     110.576  13.973 -95.481  1.00 63.77           C  
ANISOU 2581  CA  ASN A 338     4811  12357   7061   2167     47   2269       C  
ATOM   2582  C   ASN A 338     109.581  15.108 -95.689  1.00 61.98           C  
ANISOU 2582  C   ASN A 338     4669  12128   6751   1985     63   2172       C  
ATOM   2583  O   ASN A 338     109.993  16.216 -96.055  1.00 57.01           O  
ANISOU 2583  O   ASN A 338     4005  11616   6040   1840     40   2031       O  
ATOM   2584  CB  ASN A 338     111.552  13.927 -96.664  1.00 56.76           C  
ANISOU 2584  CB  ASN A 338     3841  11458   6268   2172     66   2126       C  
ATOM   2585  CG  ASN A 338     110.891  13.458 -97.944  1.00 62.83           C  
ANISOU 2585  CG  ASN A 338     4670  11993   7208   2187    156   2042       C  
ATOM   2586  OD1 ASN A 338     109.951  14.083 -98.437  1.00 59.64           O  
ANISOU 2586  OD1 ASN A 338     4353  11520   6788   2071    197   1967       O  
ATOM   2587  ND2 ASN A 338     111.383  12.356 -98.495  1.00 61.48           N  
ANISOU 2587  ND2 ASN A 338     4450  11703   7208   2331    186   2039       N  
ATOM   2588  N   CYS A 339     108.288  14.867 -95.485  1.00 53.04           N  
ANISOU 2588  N   CYS A 339     3645  10859   5650   1988    103   2242       N  
ATOM   2589  CA  CYS A 339     107.300  15.915 -95.684  1.00 51.15           C  
ANISOU 2589  CA  CYS A 339     3483  10609   5342   1823    113   2144       C  
ATOM   2590  C   CYS A 339     106.160  15.749 -94.690  1.00 50.85           C  
ANISOU 2590  C   CYS A 339     3525  10544   5252   1833    113   2269       C  
ATOM   2591  O   CYS A 339     105.765  14.628 -94.362  1.00 54.75           O  
ANISOU 2591  O   CYS A 339     4049  10911   5841   1974    152   2422       O  
ATOM   2592  CB  CYS A 339     106.761  15.909 -97.116  1.00 49.30           C  
ANISOU 2592  CB  CYS A 339     3303  10185   5243   1787    191   2017       C  
ATOM   2593  SG  CYS A 339     105.537  17.199 -97.446  1.00 50.01           S  
ANISOU 2593  SG  CYS A 339     3490  10249   5263   1589    202   1892       S  
ATOM   2594  N   LEU A 340     105.635  16.875 -94.220  1.00 49.51           N  
ANISOU 2594  N   LEU A 340     3385  10486   4941   1680     74   2199       N  
ATOM   2595  CA  LEU A 340     104.567  16.895 -93.234  1.00 50.92           C  
ANISOU 2595  CA  LEU A 340     3630  10676   5041   1663     67   2290       C  
ATOM   2596  C   LEU A 340     103.277  17.373 -93.887  1.00 54.68           C  
ANISOU 2596  C   LEU A 340     4198  11006   5570   1564    109   2192       C  
ATOM   2597  O   LEU A 340     103.255  18.427 -94.531  1.00 51.05           O  
ANISOU 2597  O   LEU A 340     3743  10567   5086   1418     95   2023       O  
ATOM   2598  CB  LEU A 340     104.931  17.802 -92.055  1.00 49.99           C  
ANISOU 2598  CB  LEU A 340     3465  10811   4717   1566    -16   2262       C  
ATOM   2599  CG  LEU A 340     103.797  18.143 -91.085  1.00 54.06           C  
ANISOU 2599  CG  LEU A 340     4046  11372   5122   1501    -29   2295       C  
ATOM   2600  CD1 LEU A 340     103.235  16.889 -90.428  1.00 51.43           C  
ANISOU 2600  CD1 LEU A 340     3757  10957   4826   1655     17   2522       C  
ATOM   2601  CD2 LEU A 340     104.266  19.142 -90.038  1.00 54.98           C  
ANISOU 2601  CD2 LEU A 340     4101  11739   5049   1393   -106   2208       C  
ATOM   2602  N   LEU A 341     102.212  16.592 -93.736  1.00 55.53           N  
ANISOU 2602  N   LEU A 341     4377  10958   5762   1644    165   2300       N  
ATOM   2603  CA  LEU A 341     100.890  17.061 -94.123  1.00 49.68           C  
ANISOU 2603  CA  LEU A 341     3717  10105   5053   1552    199   2210       C  
ATOM   2604  C   LEU A 341     100.336  17.898 -92.980  1.00 44.58           C  
ANISOU 2604  C   LEU A 341     3102   9615   4219   1431    132   2202       C  
ATOM   2605  O   LEU A 341     100.229  17.414 -91.849  1.00 48.75           O  
ANISOU 2605  O   LEU A 341     3625  10235   4663   1502    113   2365       O  
ATOM   2606  CB  LEU A 341      99.959  15.895 -94.444  1.00 49.28           C  
ANISOU 2606  CB  LEU A 341     3781   9759   5183   1647    308   2277       C  
ATOM   2607  CG  LEU A 341      98.724  16.354 -95.220  1.00 49.54           C  
ANISOU 2607  CG  LEU A 341     3963   9581   5280   1514    370   2093       C  
ATOM   2608  CD1 LEU A 341      99.156  16.869 -96.576  1.00 53.25           C  
ANISOU 2608  CD1 LEU A 341     4404  10021   5806   1464    382   1917       C  
ATOM   2609  CD2 LEU A 341      97.695  15.254 -95.371  1.00 44.79           C  
ANISOU 2609  CD2 LEU A 341     3469   8697   4853   1591    476   2143       C  
ATOM   2610  N   LEU A 342     100.005  19.153 -93.265  1.00 48.89           N  
ANISOU 2610  N   LEU A 342     3681  10192   4703   1249     99   2011       N  
ATOM   2611  CA  LEU A 342      99.550  20.093 -92.244  1.00 47.79           C  
ANISOU 2611  CA  LEU A 342     3549  10214   4393   1121     26   1956       C  
ATOM   2612  C   LEU A 342      98.034  20.232 -92.337  1.00 47.43           C  
ANISOU 2612  C   LEU A 342     3675   9958   4388   1029     84   1873       C  
ATOM   2613  O   LEU A 342      97.517  21.015 -93.138  1.00 42.13           O  
ANISOU 2613  O   LEU A 342     3075   9165   3768    902     97   1695       O  
ATOM   2614  CB  LEU A 342     100.237  21.446 -92.399  1.00 46.06           C  
ANISOU 2614  CB  LEU A 342     3265  10136   4101    966    -45   1777       C  
ATOM   2615  CG  LEU A 342     100.097  22.357 -91.175  1.00 48.85           C  
ANISOU 2615  CG  LEU A 342     3607  10666   4288    846   -115   1698       C  
ATOM   2616  CD1 LEU A 342     101.012  21.882 -90.063  1.00 45.35           C  
ANISOU 2616  CD1 LEU A 342     3086  10410   3736    938   -138   1813       C  
ATOM   2617  CD2 LEU A 342     100.386  23.807 -91.518  1.00 51.74           C  
ANISOU 2617  CD2 LEU A 342     3952  11063   4644    662   -162   1483       C  
ATOM   2618  N   LYS A 343      97.324  19.468 -91.515  1.00 52.00           N  
ANISOU 2618  N   LYS A 343     4314  10500   4943   1095    121   2009       N  
ATOM   2619  CA  LYS A 343      95.884  19.629 -91.332  1.00 41.00           C  
ANISOU 2619  CA  LYS A 343     3063   8958   3558   1002    169   1935       C  
ATOM   2620  C   LYS A 343      95.694  20.419 -90.042  1.00 45.55           C  
ANISOU 2620  C   LYS A 343     3597   9788   3923    912     84   1913       C  
ATOM   2621  O   LYS A 343      95.846  19.877 -88.944  1.00 43.83           O  
ANISOU 2621  O   LYS A 343     3330   9735   3588    997     70   2089       O  
ATOM   2622  CB  LYS A 343      95.181  18.277 -91.276  1.00 41.52           C  
ANISOU 2622  CB  LYS A 343     3215   8811   3749   1120    278   2091       C  
ATOM   2623  CG  LYS A 343      95.224  17.491 -92.574  1.00 42.08           C  
ANISOU 2623  CG  LYS A 343     3324   8616   4047   1205    366   2070       C  
ATOM   2624  CD  LYS A 343      94.618  16.110 -92.390  1.00 44.49           C  
ANISOU 2624  CD  LYS A 343     3690   8715   4499   1327    472   2233       C  
ATOM   2625  CE  LYS A 343      94.398  15.417 -93.723  1.00 46.64           C  
ANISOU 2625  CE  LYS A 343     4007   8701   5012   1388    563   2147       C  
ATOM   2626  NZ  LYS A 343      93.816  14.058 -93.540  1.00 49.43           N  
ANISOU 2626  NZ  LYS A 343     4406   8830   5545   1503    672   2294       N  
ATOM   2627  N   VAL A 344      95.365  21.707 -90.179  1.00 42.60           N  
ANISOU 2627  N   VAL A 344     3234   9452   3501    744     28   1695       N  
ATOM   2628  CA  VAL A 344      95.294  22.591 -89.017  1.00 44.67           C  
ANISOU 2628  CA  VAL A 344     3427   9974   3571    650    -65   1624       C  
ATOM   2629  C   VAL A 344      94.276  22.099 -87.991  1.00 46.04           C  
ANISOU 2629  C   VAL A 344     3666  10174   3652    666    -26   1714       C  
ATOM   2630  O   VAL A 344      94.486  22.245 -86.781  1.00 52.60           O  
ANISOU 2630  O   VAL A 344     4417  11231   4336    666    -68   1746       O  
ATOM   2631  CB  VAL A 344      94.992  24.038 -89.471  1.00 50.29           C  
ANISOU 2631  CB  VAL A 344     4151  10657   4300    465   -121   1360       C  
ATOM   2632  CG1 VAL A 344      93.645  24.114 -90.181  1.00 53.90           C  
ANISOU 2632  CG1 VAL A 344     4775  10823   4880    394    -49   1245       C  
ATOM   2633  CG2 VAL A 344      95.030  24.983 -88.283  1.00 54.16           C  
ANISOU 2633  CG2 VAL A 344     4559  11382   4637    363   -203   1242       C  
ATOM   2634  N   ASN A 345      93.171  21.500 -88.443  1.00 42.77           N  
ANISOU 2634  N   ASN A 345     3396   9487   3366    670     79   1723       N  
ATOM   2635  CA  ASN A 345      92.162  21.008 -87.510  1.00 41.29           C  
ANISOU 2635  CA  ASN A 345     3271   9310   3106    675    133   1811       C  
ATOM   2636  C   ASN A 345      92.568  19.708 -86.831  1.00 45.75           C  
ANISOU 2636  C   ASN A 345     3802   9942   3640    846    183   2117       C  
ATOM   2637  O   ASN A 345      91.900  19.290 -85.879  1.00 51.15           O  
ANISOU 2637  O   ASN A 345     4512  10694   4227    859    225   2236       O  
ATOM   2638  CB  ASN A 345      90.815  20.819 -88.220  1.00 44.07           C  
ANISOU 2638  CB  ASN A 345     3779   9346   3620    615    232   1703       C  
ATOM   2639  CG  ASN A 345      90.713  19.494 -88.946  1.00 45.93           C  
ANISOU 2639  CG  ASN A 345     4081   9313   4057    744    349   1850       C  
ATOM   2640  OD1 ASN A 345      91.568  19.146 -89.759  1.00 43.96           O  
ANISOU 2640  OD1 ASN A 345     3795   8992   3915    827    351   1889       O  
ATOM   2641  ND2 ASN A 345      89.658  18.744 -88.652  1.00 46.29           N  
ANISOU 2641  ND2 ASN A 345     4215   9208   4166    758    452   1921       N  
ATOM   2642  N   GLN A 346      93.638  19.059 -87.291  1.00 46.00           N  
ANISOU 2642  N   GLN A 346     3771   9953   3753    979    183   2252       N  
ATOM   2643  CA  GLN A 346      94.156  17.892 -86.593  1.00 53.30           C  
ANISOU 2643  CA  GLN A 346     4644  10960   4646   1154    211   2554       C  
ATOM   2644  C   GLN A 346      94.967  18.268 -85.361  1.00 58.17           C  
ANISOU 2644  C   GLN A 346     5127  11871   5102   1153    130   2558       C  
ATOM   2645  O   GLN A 346      95.175  17.418 -84.488  1.00 50.31           O  
ANISOU 2645  O   GLN A 346     4100  10936   4079   1262    163   2762       O  
ATOM   2646  CB  GLN A 346      95.011  17.045 -87.537  1.00 51.57           C  
ANISOU 2646  CB  GLN A 346     4399  10573   4623   1294    246   2650       C  
ATOM   2647  CG  GLN A 346      94.378  15.720 -87.928  1.00 54.21           C  
ANISOU 2647  CG  GLN A 346     4831  10589   5179   1396    383   2799       C  
ATOM   2648  CD  GLN A 346      95.197  14.954 -88.951  1.00 62.91           C  
ANISOU 2648  CD  GLN A 346     5895  11518   6490   1528    414   2843       C  
ATOM   2649  OE1 GLN A 346      96.220  15.440 -89.442  1.00 63.00           O  
ANISOU 2649  OE1 GLN A 346     5813  11646   6478   1535    339   2758       O  
ATOM   2650  NE2 GLN A 346      94.749  13.748 -89.282  1.00 59.33           N  
ANISOU 2650  NE2 GLN A 346     5502  10785   6254   1629    530   2967       N  
ATOM   2651  N   ILE A 347      95.430  19.515 -85.271  1.00 51.75           N  
ANISOU 2651  N   ILE A 347     4237  11225   4201   1031     37   2329       N  
ATOM   2652  CA  ILE A 347      96.139  19.981 -84.093  1.00 51.98           C  
ANISOU 2652  CA  ILE A 347     4141  11527   4083   1015    -23   2289       C  
ATOM   2653  C   ILE A 347      95.316  20.973 -83.275  1.00 54.95           C  
ANISOU 2653  C   ILE A 347     4515  12023   4342    864    -59   2098       C  
ATOM   2654  O   ILE A 347      95.465  21.012 -82.048  1.00 63.25           O  
ANISOU 2654  O   ILE A 347     5486  13284   5262    878    -77   2126       O  
ATOM   2655  CB  ILE A 347      97.516  20.577 -84.464  1.00 54.38           C  
ANISOU 2655  CB  ILE A 347     4336  11944   4382   1006    -88   2184       C  
ATOM   2656  CG1 ILE A 347      98.357  20.804 -83.206  1.00 66.19           C  
ANISOU 2656  CG1 ILE A 347     5704  13721   5723   1029   -132   2185       C  
ATOM   2657  CG2 ILE A 347      97.371  21.867 -85.265  1.00 48.63           C  
ANISOU 2657  CG2 ILE A 347     3624  11166   3690    839   -135   1916       C  
ATOM   2658  CD1 ILE A 347      98.521  19.566 -82.343  1.00 65.23           C  
ANISOU 2658  CD1 ILE A 347     5562  13665   5559   1194    -91   2457       C  
ATOM   2659  N   GLY A 348      94.446  21.766 -83.908  1.00 52.40           N  
ANISOU 2659  N   GLY A 348     4272  11576   4063    726    -68   1902       N  
ATOM   2660  CA  GLY A 348      93.406  22.488 -83.201  1.00 47.91           C  
ANISOU 2660  CA  GLY A 348     3725  11063   3415    599    -82   1740       C  
ATOM   2661  C   GLY A 348      93.609  23.976 -82.997  1.00 46.35           C  
ANISOU 2661  C   GLY A 348     3453  10989   3170    446   -161   1451       C  
ATOM   2662  O   GLY A 348      92.729  24.621 -82.416  1.00 49.16           O  
ANISOU 2662  O   GLY A 348     3820  11386   3474    341   -172   1297       O  
ATOM   2663  N   SER A 349      94.725  24.548 -83.443  1.00 48.58           N  
ANISOU 2663  N   SER A 349     3662  11317   3478    429   -205   1368       N  
ATOM   2664  CA  SER A 349      94.947  25.976 -83.245  1.00 49.08           C  
ANISOU 2664  CA  SER A 349     3669  11459   3519    283   -263   1097       C  
ATOM   2665  C   SER A 349      95.978  26.470 -84.247  1.00 45.46           C  
ANISOU 2665  C   SER A 349     3191  10931   3153    257   -293   1029       C  
ATOM   2666  O   SER A 349      96.774  25.693 -84.782  1.00 45.75           O  
ANISOU 2666  O   SER A 349     3210  10945   3228    368   -277   1194       O  
ATOM   2667  CB  SER A 349      95.403  26.287 -81.814  1.00 52.53           C  
ANISOU 2667  CB  SER A 349     3983  12172   3805    291   -288   1055       C  
ATOM   2668  OG  SER A 349      96.757  25.918 -81.612  1.00 52.45           O  
ANISOU 2668  OG  SER A 349     3876  12305   3747    393   -303   1164       O  
ATOM   2669  N   VAL A 350      95.954  27.784 -84.484  1.00 44.72           N  
ANISOU 2669  N   VAL A 350     3099  10787   3105    110   -334    783       N  
ATOM   2670  CA  VAL A 350      96.876  28.393 -85.437  1.00 53.09           C  
ANISOU 2670  CA  VAL A 350     4144  11763   4266     62   -363    705       C  
ATOM   2671  C   VAL A 350      98.298  28.377 -84.891  1.00 46.15           C  
ANISOU 2671  C   VAL A 350     3140  11083   3313    122   -390    739       C  
ATOM   2672  O   VAL A 350      99.254  28.075 -85.618  1.00 46.22           O  
ANISOU 2672  O   VAL A 350     3119  11066   3377    174   -390    818       O  
ATOM   2673  CB  VAL A 350      96.413  29.822 -85.784  1.00 48.32           C  
ANISOU 2673  CB  VAL A 350     3584  11020   3755   -109   -398    446       C  
ATOM   2674  CG1 VAL A 350      97.493  30.568 -86.547  1.00 51.00           C  
ANISOU 2674  CG1 VAL A 350     3883  11301   4193   -166   -431    366       C  
ATOM   2675  CG2 VAL A 350      95.133  29.781 -86.594  1.00 48.01           C  
ANISOU 2675  CG2 VAL A 350     3671  10760   3809   -156   -374    420       C  
ATOM   2676  N   THR A 351      98.460  28.696 -83.605  1.00 47.89           N  
ANISOU 2676  N   THR A 351     3278  11513   3405    118   -412    671       N  
ATOM   2677  CA  THR A 351      99.783  28.705 -82.991  1.00 49.98           C  
ANISOU 2677  CA  THR A 351     3416  11989   3584    178   -443    684       C  
ATOM   2678  C   THR A 351     100.464  27.349 -83.125  1.00 50.81           C  
ANISOU 2678  C   THR A 351     3492  12152   3660    350   -415    948       C  
ATOM   2679  O   THR A 351     101.618  27.260 -83.559  1.00 55.07           O  
ANISOU 2679  O   THR A 351     3975  12719   4230    393   -433    978       O  
ATOM   2680  CB  THR A 351      99.671  29.100 -81.516  1.00 56.97           C  
ANISOU 2680  CB  THR A 351     4217  13111   4319    169   -463    587       C  
ATOM   2681  OG1 THR A 351      99.364  30.496 -81.410  1.00 57.81           O  
ANISOU 2681  OG1 THR A 351     4327  13160   4476     17   -498    311       O  
ATOM   2682  CG2 THR A 351     100.969  28.808 -80.787  1.00 54.29           C  
ANISOU 2682  CG2 THR A 351     3742  13022   3865    270   -490    647       C  
ATOM   2683  N   GLU A 352      99.763  26.277 -82.757  1.00 54.38           N  
ANISOU 2683  N   GLU A 352     3984  12610   4069    453   -369   1143       N  
ATOM   2684  CA  GLU A 352     100.383  24.958 -82.787  1.00 52.56           C  
ANISOU 2684  CA  GLU A 352     3729  12413   3828    630   -340   1403       C  
ATOM   2685  C   GLU A 352     100.606  24.472 -84.213  1.00 54.79           C  
ANISOU 2685  C   GLU A 352     4077  12474   4266    668   -313   1486       C  
ATOM   2686  O   GLU A 352     101.522  23.680 -84.459  1.00 57.68           O  
ANISOU 2686  O   GLU A 352     4401  12859   4654    795   -304   1635       O  
ATOM   2687  CB  GLU A 352      99.532  23.961 -82.006  1.00 52.89           C  
ANISOU 2687  CB  GLU A 352     3802  12487   3806    727   -294   1597       C  
ATOM   2688  CG  GLU A 352      99.315  24.344 -80.556  1.00 60.72           C  
ANISOU 2688  CG  GLU A 352     4715  13724   4633    705   -315   1532       C  
ATOM   2689  CD  GLU A 352      98.301  23.454 -79.868  1.00 63.78           C  
ANISOU 2689  CD  GLU A 352     5146  14115   4972    774   -267   1713       C  
ATOM   2690  OE1 GLU A 352      98.700  22.416 -79.298  1.00 60.56           O  
ANISOU 2690  OE1 GLU A 352     4702  13799   4508    925   -245   1947       O  
ATOM   2691  OE2 GLU A 352      97.099  23.789 -79.911  1.00 68.87           O  
ANISOU 2691  OE2 GLU A 352     5867  14659   5641    678   -251   1624       O  
ATOM   2692  N   ALA A 353      99.787  24.928 -85.162  1.00 51.88           N  
ANISOU 2692  N   ALA A 353     3805  11901   4007    567   -301   1387       N  
ATOM   2693  CA  ALA A 353     100.017  24.560 -86.554  1.00 46.97           C  
ANISOU 2693  CA  ALA A 353     3230  11089   3529    599   -277   1442       C  
ATOM   2694  C   ALA A 353     101.252  25.260 -87.109  1.00 55.60           C  
ANISOU 2694  C   ALA A 353     4248  12214   4662    548   -315   1330       C  
ATOM   2695  O   ALA A 353     102.009  24.670 -87.889  1.00 47.33           O  
ANISOU 2695  O   ALA A 353     3180  11113   3691    634   -295   1425       O  
ATOM   2696  CB  ALA A 353      98.784  24.883 -87.397  1.00 51.73           C  
ANISOU 2696  CB  ALA A 353     3948  11481   4228    508   -257   1361       C  
ATOM   2697  N   ILE A 354     101.476  26.516 -86.714  1.00 47.50           N  
ANISOU 2697  N   ILE A 354     3180  11267   3600    409   -365   1121       N  
ATOM   2698  CA  ILE A 354     102.667  27.232 -87.161  1.00 52.85           C  
ANISOU 2698  CA  ILE A 354     3781  11977   4324    352   -402   1012       C  
ATOM   2699  C   ILE A 354     103.919  26.576 -86.595  1.00 58.17           C  
ANISOU 2699  C   ILE A 354     4343  12842   4916    482   -416   1120       C  
ATOM   2700  O   ILE A 354     104.901  26.349 -87.313  1.00 59.59           O  
ANISOU 2700  O   ILE A 354     4476  13005   5162    525   -415   1156       O  
ATOM   2701  CB  ILE A 354     102.584  28.719 -86.770  1.00 55.41           C  
ANISOU 2701  CB  ILE A 354     4082  12324   4647    181   -452    763       C  
ATOM   2702  CG1 ILE A 354     101.482  29.420 -87.564  1.00 60.60           C  
ANISOU 2702  CG1 ILE A 354     4851  12755   5421     52   -441    653       C  
ATOM   2703  CG2 ILE A 354     103.923  29.412 -86.995  1.00 54.80           C  
ANISOU 2703  CG2 ILE A 354     3901  12310   4610    133   -491    661       C  
ATOM   2704  CD1 ILE A 354     101.355  30.896 -87.254  1.00 63.67           C  
ANISOU 2704  CD1 ILE A 354     5226  13116   5849   -110   -488    411       C  
ATOM   2705  N   GLN A 355     103.899  26.251 -85.299  1.00 56.65           N  
ANISOU 2705  N   GLN A 355     4102  12843   4581    551   -429   1171       N  
ATOM   2706  CA  GLN A 355     105.062  25.624 -84.685  1.00 56.54           C  
ANISOU 2706  CA  GLN A 355     3978  13022   4480    684   -448   1276       C  
ATOM   2707  C   GLN A 355     105.299  24.225 -85.242  1.00 56.66           C  
ANISOU 2707  C   GLN A 355     4020  12951   4556    852   -402   1517       C  
ATOM   2708  O   GLN A 355     106.453  23.804 -85.377  1.00 58.78           O  
ANISOU 2708  O   GLN A 355     4211  13292   4832    944   -417   1575       O  
ATOM   2709  CB  GLN A 355     104.902  25.593 -83.161  1.00 59.80           C  
ANISOU 2709  CB  GLN A 355     4331  13668   4721    723   -468   1283       C  
ATOM   2710  CG  GLN A 355     103.928  24.553 -82.633  1.00 69.34           C  
ANISOU 2710  CG  GLN A 355     5602  14863   5881    826   -417   1487       C  
ATOM   2711  CD  GLN A 355     103.656  24.696 -81.144  1.00 76.71           C  
ANISOU 2711  CD  GLN A 355     6470  16034   6643    839   -434   1469       C  
ATOM   2712  OE1 GLN A 355     104.060  25.676 -80.516  1.00 77.31           O  
ANISOU 2712  OE1 GLN A 355     6463  16275   6637    758   -483   1273       O  
ATOM   2713  NE2 GLN A 355     102.964  23.715 -80.572  1.00 75.91           N  
ANISOU 2713  NE2 GLN A 355     6402  15948   6493    942   -390   1673       N  
ATOM   2714  N   ALA A 356     104.233  23.502 -85.593  1.00 56.51           N  
ANISOU 2714  N   ALA A 356     4107  12766   4597    897   -346   1647       N  
ATOM   2715  CA  ALA A 356     104.412  22.192 -86.209  1.00 55.11           C  
ANISOU 2715  CA  ALA A 356     3959  12466   4513   1057   -297   1860       C  
ATOM   2716  C   ALA A 356     105.048  22.320 -87.587  1.00 57.93           C  
ANISOU 2716  C   ALA A 356     4314  12687   5010   1037   -289   1802       C  
ATOM   2717  O   ALA A 356     105.883  21.492 -87.973  1.00 55.53           O  
ANISOU 2717  O   ALA A 356     3969  12367   4764   1166   -275   1913       O  
ATOM   2718  CB  ALA A 356     103.074  21.460 -86.296  1.00 51.92           C  
ANISOU 2718  CB  ALA A 356     3669  11899   4159   1100   -237   1992       C  
ATOM   2719  N   CYS A 357     104.673  23.355 -88.339  1.00 54.74           N  
ANISOU 2719  N   CYS A 357     3949  12184   4667    878   -296   1625       N  
ATOM   2720  CA  CYS A 357     105.285  23.584 -89.642  1.00 57.15           C  
ANISOU 2720  CA  CYS A 357     4241  12376   5097    844   -283   1562       C  
ATOM   2721  C   CYS A 357     106.747  23.990 -89.493  1.00 59.65           C  
ANISOU 2721  C   CYS A 357     4432  12850   5381    836   -329   1490       C  
ATOM   2722  O   CYS A 357     107.629  23.422 -90.147  1.00 56.88           O  
ANISOU 2722  O   CYS A 357     4034  12480   5099    922   -313   1548       O  
ATOM   2723  CB  CYS A 357     104.502  24.649 -90.411  1.00 50.64           C  
ANISOU 2723  CB  CYS A 357     3487  11411   4343    671   -279   1400       C  
ATOM   2724  SG  CYS A 357     105.316  25.228 -91.919  1.00 53.56           S  
ANISOU 2724  SG  CYS A 357     3824  11677   4849    593   -262   1302       S  
ATOM   2725  N   LYS A 358     107.022  24.970 -88.625  1.00 59.37           N  
ANISOU 2725  N   LYS A 358     4337  12972   5248    735   -387   1350       N  
ATOM   2726  CA  LYS A 358     108.394  25.424 -88.432  1.00 61.11           C  
ANISOU 2726  CA  LYS A 358     4429  13348   5443    721   -435   1262       C  
ATOM   2727  C   LYS A 358     109.277  24.318 -87.872  1.00 55.52           C  
ANISOU 2727  C   LYS A 358     3643  12781   4669    907   -444   1416       C  
ATOM   2728  O   LYS A 358     110.482  24.291 -88.140  1.00 65.18           O  
ANISOU 2728  O   LYS A 358     4769  14080   5918    941   -466   1389       O  
ATOM   2729  CB  LYS A 358     108.422  26.641 -87.507  1.00 62.49           C  
ANISOU 2729  CB  LYS A 358     4551  13657   5533    589   -493   1073       C  
ATOM   2730  CG  LYS A 358     107.639  27.834 -88.031  1.00 63.45           C  
ANISOU 2730  CG  LYS A 358     4741  13625   5741    401   -492    905       C  
ATOM   2731  CD  LYS A 358     108.529  29.057 -88.194  1.00 69.59           C  
ANISOU 2731  CD  LYS A 358     5426  14438   6579    266   -534    711       C  
ATOM   2732  CE  LYS A 358     109.607  28.830 -89.247  1.00 71.56           C  
ANISOU 2732  CE  LYS A 358     5613  14651   6926    290   -513    748       C  
ATOM   2733  NZ  LYS A 358     110.489  30.020 -89.421  1.00 74.04           N  
ANISOU 2733  NZ  LYS A 358     5824  14992   7316    152   -546    568       N  
ATOM   2734  N   LEU A 359     108.698  23.404 -87.092  1.00 57.64           N  
ANISOU 2734  N   LEU A 359     3952  13086   4864   1030   -427   1581       N  
ATOM   2735  CA  LEU A 359     109.466  22.273 -86.585  1.00 62.47           C  
ANISOU 2735  CA  LEU A 359     4500  13805   5432   1219   -433   1754       C  
ATOM   2736  C   LEU A 359     109.921  21.373 -87.725  1.00 62.91           C  
ANISOU 2736  C   LEU A 359     4567  13701   5636   1324   -392   1857       C  
ATOM   2737  O   LEU A 359     111.066  20.903 -87.739  1.00 71.56           O  
ANISOU 2737  O   LEU A 359     5570  14881   6739   1427   -416   1895       O  
ATOM   2738  CB  LEU A 359     108.630  21.493 -85.567  1.00 66.87           C  
ANISOU 2738  CB  LEU A 359     5106  14403   5899   1319   -412   1926       C  
ATOM   2739  CG  LEU A 359     109.271  20.372 -84.738  1.00 75.72           C  
ANISOU 2739  CG  LEU A 359     6164  15654   6950   1515   -422   2125       C  
ATOM   2740  CD1 LEU A 359     109.120  19.016 -85.425  1.00 78.52           C  
ANISOU 2740  CD1 LEU A 359     6583  15802   7448   1668   -363   2338       C  
ATOM   2741  CD2 LEU A 359     110.739  20.675 -84.429  1.00 74.46           C  
ANISOU 2741  CD2 LEU A 359     5863  15702   6726   1544   -490   2039       C  
ATOM   2742  N   ALA A 360     109.043  21.134 -88.700  1.00 59.02           N  
ANISOU 2742  N   ALA A 360     4180  12980   5266   1302   -332   1886       N  
ATOM   2743  CA  ALA A 360     109.426  20.328 -89.853  1.00 62.14           C  
ANISOU 2743  CA  ALA A 360     4582  13216   5813   1396   -286   1953       C  
ATOM   2744  C   ALA A 360     110.401  21.080 -90.752  1.00 55.28           C  
ANISOU 2744  C   ALA A 360     3638  12366   5002   1303   -300   1792       C  
ATOM   2745  O   ALA A 360     111.344  20.484 -91.286  1.00 56.24           O  
ANISOU 2745  O   ALA A 360     3693  12481   5194   1399   -292   1823       O  
ATOM   2746  CB  ALA A 360     108.181  19.905 -90.632  1.00 53.48           C  
ANISOU 2746  CB  ALA A 360     3610  11878   4830   1399   -215   2008       C  
ATOM   2747  N   GLN A 361     110.206  22.393 -90.911  1.00 54.23           N  
ANISOU 2747  N   GLN A 361     3508  12252   4846   1115   -320   1619       N  
ATOM   2748  CA  GLN A 361     111.060  23.172 -91.803  1.00 59.81           C  
ANISOU 2748  CA  GLN A 361     4146  12958   5620   1010   -322   1477       C  
ATOM   2749  C   GLN A 361     112.494  23.256 -91.286  1.00 62.62           C  
ANISOU 2749  C   GLN A 361     4355  13515   5922   1049   -377   1435       C  
ATOM   2750  O   GLN A 361     113.447  23.149 -92.068  1.00 59.67           O  
ANISOU 2750  O   GLN A 361     3907  13139   5625   1066   -363   1403       O  
ATOM   2751  CB  GLN A 361     110.470  24.569 -91.999  1.00 52.70           C  
ANISOU 2751  CB  GLN A 361     3285  12013   4726    800   -331   1314       C  
ATOM   2752  CG  GLN A 361     109.162  24.564 -92.780  1.00 56.47           C  
ANISOU 2752  CG  GLN A 361     3897  12280   5279    753   -275   1333       C  
ATOM   2753  CD  GLN A 361     108.664  25.955 -93.119  1.00 57.83           C  
ANISOU 2753  CD  GLN A 361     4105  12387   5483    549   -284   1174       C  
ATOM   2754  OE1 GLN A 361     108.597  26.834 -92.260  1.00 57.05           O  
ANISOU 2754  OE1 GLN A 361     3981  12379   5318    450   -338   1068       O  
ATOM   2755  NE2 GLN A 361     108.310  26.160 -94.381  1.00 57.48           N  
ANISOU 2755  NE2 GLN A 361     4115  12178   5547    491   -228   1152       N  
ATOM   2756  N   GLU A 362     112.673  23.447 -89.976  1.00 66.49           N  
ANISOU 2756  N   GLU A 362     4795  14191   6278   1066   -438   1425       N  
ATOM   2757  CA  GLU A 362     114.018  23.501 -89.415  1.00 77.59           C  
ANISOU 2757  CA  GLU A 362     6055  15802   7625   1115   -496   1379       C  
ATOM   2758  C   GLU A 362     114.759  22.178 -89.557  1.00 78.50           C  
ANISOU 2758  C   GLU A 362     6124  15931   7772   1316   -488   1531       C  
ATOM   2759  O   GLU A 362     115.990  22.154 -89.441  1.00 89.72           O  
ANISOU 2759  O   GLU A 362     7417  17490   9182   1361   -529   1484       O  
ATOM   2760  CB  GLU A 362     113.967  23.903 -87.940  1.00 91.11           C  
ANISOU 2760  CB  GLU A 362     7724  17719   9174   1108   -559   1340       C  
ATOM   2761  CG  GLU A 362     113.649  25.369 -87.696  1.00 98.87           C  
ANISOU 2761  CG  GLU A 362     8700  18727  10137    906   -586   1132       C  
ATOM   2762  CD  GLU A 362     113.706  25.737 -86.224  1.00106.40           C  
ANISOU 2762  CD  GLU A 362     9592  19905  10930    912   -647   1070       C  
ATOM   2763  OE1 GLU A 362     113.672  24.818 -85.379  1.00109.46           O  
ANISOU 2763  OE1 GLU A 362     9974  20410  11207   1067   -656   1221       O  
ATOM   2764  OE2 GLU A 362     113.792  26.944 -85.911  1.00108.66           O  
ANISOU 2764  OE2 GLU A 362     9831  20247  11206    765   -684    871       O  
ATOM   2765  N   ASN A 363     114.045  21.079 -89.799  1.00 71.29           N  
ANISOU 2765  N   ASN A 363     5305  14869   6913   1440   -439   1703       N  
ATOM   2766  CA  ASN A 363     114.655  19.770 -89.980  1.00 67.81           C  
ANISOU 2766  CA  ASN A 363     4829  14397   6538   1636   -428   1849       C  
ATOM   2767  C   ASN A 363     114.705  19.348 -91.443  1.00 64.12           C  
ANISOU 2767  C   ASN A 363     4390  13729   6244   1652   -362   1839       C  
ATOM   2768  O   ASN A 363     114.775  18.149 -91.734  1.00 61.64           O  
ANISOU 2768  O   ASN A 363     4089  13308   6024   1814   -333   1967       O  
ATOM   2769  CB  ASN A 363     113.915  18.723 -89.150  1.00 70.22           C  
ANISOU 2769  CB  ASN A 363     5206  14670   6803   1784   -417   2058       C  
ATOM   2770  CG  ASN A 363     114.437  18.634 -87.730  1.00 82.04           C  
ANISOU 2770  CG  ASN A 363     6624  16409   8138   1860   -486   2113       C  
ATOM   2771  OD1 ASN A 363     114.962  17.601 -87.314  1.00 84.17           O  
ANISOU 2771  OD1 ASN A 363     6852  16717   8411   2038   -502   2264       O  
ATOM   2772  ND2 ASN A 363     114.312  19.724 -86.983  1.00 83.97           N  
ANISOU 2772  ND2 ASN A 363     6841  16817   8247   1729   -527   1983       N  
ATOM   2773  N   GLY A 364     114.668  20.305 -92.366  1.00 59.56           N  
ANISOU 2773  N   GLY A 364     3819  13095   5717   1488   -335   1687       N  
ATOM   2774  CA  GLY A 364     114.775  19.990 -93.775  1.00 64.18           C  
ANISOU 2774  CA  GLY A 364     4419  13520   6449   1494   -267   1659       C  
ATOM   2775  C   GLY A 364     113.592  19.265 -94.371  1.00 62.63           C  
ANISOU 2775  C   GLY A 364     4353  13097   6347   1550   -196   1750       C  
ATOM   2776  O   GLY A 364     113.698  18.759 -95.492  1.00 60.20           O  
ANISOU 2776  O   GLY A 364     4052  12655   6165   1594   -137   1735       O  
ATOM   2777  N   TRP A 365     112.471  19.190 -93.663  1.00 63.30           N  
ANISOU 2777  N   TRP A 365     4536  13138   6376   1550   -198   1832       N  
ATOM   2778  CA  TRP A 365     111.284  18.548 -94.204  1.00 56.92           C  
ANISOU 2778  CA  TRP A 365     3849  12111   5666   1595   -129   1906       C  
ATOM   2779  C   TRP A 365     110.519  19.502 -95.110  1.00 52.48           C  
ANISOU 2779  C   TRP A 365     3361  11446   5134   1426    -89   1778       C  
ATOM   2780  O   TRP A 365     110.571  20.726 -94.954  1.00 51.99           O  
ANISOU 2780  O   TRP A 365     3282  11476   4994   1263   -123   1664       O  
ATOM   2781  CB  TRP A 365     110.348  18.077 -93.089  1.00 58.44           C  
ANISOU 2781  CB  TRP A 365     4115  12297   5794   1659   -140   2052       C  
ATOM   2782  CG  TRP A 365     110.647  16.722 -92.522  1.00 63.32           C  
ANISOU 2782  CG  TRP A 365     4712  12897   6452   1864   -139   2236       C  
ATOM   2783  CD1 TRP A 365     111.828  16.046 -92.579  1.00 58.68           C  
ANISOU 2783  CD1 TRP A 365     4025  12360   5912   1991   -161   2272       C  
ATOM   2784  CD2 TRP A 365     109.733  15.876 -91.811  1.00 63.37           C  
ANISOU 2784  CD2 TRP A 365     4795  12815   6466   1966   -114   2417       C  
ATOM   2785  NE1 TRP A 365     111.709  14.832 -91.945  1.00 60.22           N  
ANISOU 2785  NE1 TRP A 365     4234  12496   6149   2168   -156   2468       N  
ATOM   2786  CE2 TRP A 365     110.432  14.703 -91.466  1.00 63.45           C  
ANISOU 2786  CE2 TRP A 365     4753  12818   6536   2153   -122   2567       C  
ATOM   2787  CE3 TRP A 365     108.391  15.998 -91.432  1.00 55.82           C  
ANISOU 2787  CE3 TRP A 365     3945  11784   5479   1915    -85   2468       C  
ATOM   2788  CZ2 TRP A 365     109.835  13.659 -90.760  1.00 64.74           C  
ANISOU 2788  CZ2 TRP A 365     4971  12891   6736   2287    -95   2779       C  
ATOM   2789  CZ3 TRP A 365     107.801  14.962 -90.733  1.00 56.82           C  
ANISOU 2789  CZ3 TRP A 365     4122  11833   5635   2045    -55   2673       C  
ATOM   2790  CH2 TRP A 365     108.522  13.809 -90.402  1.00 59.11           C  
ANISOU 2790  CH2 TRP A 365     4362  12107   5990   2227    -57   2833       C  
ATOM   2791  N   GLY A 366     109.803  18.922 -96.068  1.00 51.28           N  
ANISOU 2791  N   GLY A 366     3287  11092   5106   1470    -15   1793       N  
ATOM   2792  CA  GLY A 366     108.759  19.655 -96.741  1.00 54.43           C  
ANISOU 2792  CA  GLY A 366     3781  11377   5525   1337     23   1707       C  
ATOM   2793  C   GLY A 366     107.482  19.690 -95.920  1.00 56.08           C  
ANISOU 2793  C   GLY A 366     4083  11542   5682   1320     13   1770       C  
ATOM   2794  O   GLY A 366     107.286  18.920 -94.981  1.00 60.64           O  
ANISOU 2794  O   GLY A 366     4667  12142   6232   1434     -2   1906       O  
ATOM   2795  N   VAL A 367     106.607  20.624 -96.263  1.00 46.54           N  
ANISOU 2795  N   VAL A 367     2946  10278   4460   1173     22   1673       N  
ATOM   2796  CA  VAL A 367     105.301  20.749 -95.629  1.00 45.50           C  
ANISOU 2796  CA  VAL A 367     2903  10096   4289   1139     16   1703       C  
ATOM   2797  C   VAL A 367     104.278  20.968 -96.729  1.00 51.22           C  
ANISOU 2797  C   VAL A 367     3719  10634   5107   1079     79   1624       C  
ATOM   2798  O   VAL A 367     104.528  21.727 -97.668  1.00 49.51           O  
ANISOU 2798  O   VAL A 367     3499  10395   4917    974     95   1510       O  
ATOM   2799  CB  VAL A 367     105.262  21.906 -94.608  1.00 45.62           C  
ANISOU 2799  CB  VAL A 367     2899  10273   4161    996    -62   1632       C  
ATOM   2800  CG1 VAL A 367     103.843  22.136 -94.114  1.00 44.40           C  
ANISOU 2800  CG1 VAL A 367     2838  10058   3973    941    -65   1630       C  
ATOM   2801  CG2 VAL A 367     106.187  21.618 -93.436  1.00 55.65           C  
ANISOU 2801  CG2 VAL A 367     4081  11737   5327   1070   -118   1705       C  
ATOM   2802  N   MET A 368     103.140  20.288 -96.634  1.00 46.71           N  
ANISOU 2802  N   MET A 368     3227   9928   4592   1150    122   1687       N  
ATOM   2803  CA  MET A 368     102.052  20.476 -97.587  1.00 45.85           C  
ANISOU 2803  CA  MET A 368     3208   9644   4568   1098    185   1598       C  
ATOM   2804  C   MET A 368     100.787  20.811 -96.810  1.00 40.18           C  
ANISOU 2804  C   MET A 368     2564   8905   3798   1035    166   1598       C  
ATOM   2805  O   MET A 368     100.245  19.957 -96.101  1.00 40.63           O  
ANISOU 2805  O   MET A 368     2673   8899   3867   1128    184   1709       O  
ATOM   2806  CB  MET A 368     101.850  19.239 -98.464  1.00 45.84           C  
ANISOU 2806  CB  MET A 368     3239   9456   4724   1248    279   1629       C  
ATOM   2807  CG  MET A 368     100.591  19.307 -99.326  1.00 48.97           C  
ANISOU 2807  CG  MET A 368     3744   9659   5202   1209    352   1527       C  
ATOM   2808  SD  MET A 368     100.523  18.123-100.690  1.00 55.02           S  
ANISOU 2808  SD  MET A 368     4537  10215   6154   1348    461   1476       S  
ATOM   2809  CE  MET A 368     100.552  16.546 -99.838  1.00 61.06           C  
ANISOU 2809  CE  MET A 368     5273  10894   7033   1550    486   1654       C  
ATOM   2810  N   VAL A 369     100.333  22.061 -96.927  1.00 45.25           N  
ANISOU 2810  N   VAL A 369     3254   9551   4386    858    133   1463       N  
ATOM   2811  CA  VAL A 369      99.074  22.453 -96.313  1.00 45.41           C  
ANISOU 2811  CA  VAL A 369     3400   9490   4365    769    119   1413       C  
ATOM   2812  C   VAL A 369      97.942  21.680 -96.973  1.00 46.80           C  
ANISOU 2812  C   VAL A 369     3725   9399   4659    824    212   1397       C  
ATOM   2813  O   VAL A 369      97.904  21.522 -98.202  1.00 45.37           O  
ANISOU 2813  O   VAL A 369     3577   9087   4576    843    273   1332       O  
ATOM   2814  CB  VAL A 369      98.874  23.973 -96.430  1.00 44.19           C  
ANISOU 2814  CB  VAL A 369     3255   9375   4162    575     63   1256       C  
ATOM   2815  CG1 VAL A 369      97.544  24.391 -95.808  1.00 38.72           C  
ANISOU 2815  CG1 VAL A 369     2684   8596   3432    486     45   1183       C  
ATOM   2816  CG2 VAL A 369     100.045  24.709 -95.779  1.00 38.46           C  
ANISOU 2816  CG2 VAL A 369     2363   8908   3343    519    -26   1252       C  
ATOM   2817  N   SER A 370      97.016  21.178 -96.156  1.00 44.39           N  
ANISOU 2817  N   SER A 370     3501   9024   4342    851    227   1451       N  
ATOM   2818  CA  SER A 370      96.000  20.247 -96.623  1.00 43.14           C  
ANISOU 2818  CA  SER A 370     3462   8616   4313    921    322   1451       C  
ATOM   2819  C   SER A 370      94.605  20.697 -96.220  1.00 48.47           C  
ANISOU 2819  C   SER A 370     4265   9189   4961    814    325   1360       C  
ATOM   2820  O   SER A 370      94.399  21.286 -95.155  1.00 47.93           O  
ANISOU 2820  O   SER A 370     4187   9257   4768    736    263   1366       O  
ATOM   2821  CB  SER A 370      96.231  18.837 -96.075  1.00 43.70           C  
ANISOU 2821  CB  SER A 370     3500   8657   4448   1093    369   1641       C  
ATOM   2822  OG  SER A 370      95.240  17.945 -96.556  1.00 37.49           O  
ANISOU 2822  OG  SER A 370     2818   7611   3817   1151    467   1624       O  
ATOM   2823  N   HIS A 371      93.649  20.383 -97.089  1.00 45.67           N  
ANISOU 2823  N   HIS A 371     4020   8604   4728    818    398   1263       N  
ATOM   2824  CA  HIS A 371      92.231  20.504 -96.801  1.00 37.86           C  
ANISOU 2824  CA  HIS A 371     3153   7478   3752    748    423   1179       C  
ATOM   2825  C   HIS A 371      91.749  19.265 -96.048  1.00 37.40           C  
ANISOU 2825  C   HIS A 371     3120   7335   3753    849    494   1320       C  
ATOM   2826  O   HIS A 371      92.517  18.349 -95.743  1.00 38.98           O  
ANISOU 2826  O   HIS A 371     3247   7578   3987    976    516   1491       O  
ATOM   2827  CB  HIS A 371      91.445  20.674 -98.098  1.00 34.34           C  
ANISOU 2827  CB  HIS A 371     2801   6833   3413    720    469   1006       C  
ATOM   2828  CG  HIS A 371      91.560  19.500 -99.028  1.00 37.46           C  
ANISOU 2828  CG  HIS A 371     3191   7077   3966    859    560   1023       C  
ATOM   2829  ND1 HIS A 371      90.715  19.312-100.101  1.00 33.00           N  
ANISOU 2829  ND1 HIS A 371     2704   6325   3511    868    618    872       N  
ATOM   2830  CD2 HIS A 371      92.426  18.458 -99.048  1.00 33.62           C  
ANISOU 2830  CD2 HIS A 371     2619   6604   3553    999    599   1156       C  
ATOM   2831  CE1 HIS A 371      91.050  18.203-100.736  1.00 33.58           C  
ANISOU 2831  CE1 HIS A 371     2735   6305   3720   1004    690    900       C  
ATOM   2832  NE2 HIS A 371      92.086  17.666-100.118  1.00 35.39           N  
ANISOU 2832  NE2 HIS A 371     2866   6642   3937   1085    681   1074       N  
ATOM   2833  N   ARG A 372      90.450  19.226 -95.766  1.00 37.29           N  
ANISOU 2833  N   ARG A 372     3210   7193   3766    793    533   1251       N  
ATOM   2834  CA  ARG A 372      89.780  18.023 -95.299  1.00 40.33           C  
ANISOU 2834  CA  ARG A 372     3635   7434   4253    875    627   1362       C  
ATOM   2835  C   ARG A 372      88.732  17.610 -96.326  1.00 35.05           C  
ANISOU 2835  C   ARG A 372     3059   6495   3763    880    713   1206       C  
ATOM   2836  O   ARG A 372      88.300  18.411 -97.159  1.00 35.36           O  
ANISOU 2836  O   ARG A 372     3148   6487   3800    801    685   1011       O  
ATOM   2837  CB  ARG A 372      89.125  18.232 -93.922  1.00 35.02           C  
ANISOU 2837  CB  ARG A 372     2988   6866   3452    806    613   1428       C  
ATOM   2838  CG  ARG A 372      90.079  18.710 -92.829  1.00 36.15           C  
ANISOU 2838  CG  ARG A 372     3030   7311   3394    798    519   1555       C  
ATOM   2839  CD  ARG A 372      91.325  17.842 -92.745  1.00 37.73           C  
ANISOU 2839  CD  ARG A 372     3129   7585   3621    952    523   1763       C  
ATOM   2840  NE  ARG A 372      91.021  16.450 -92.433  1.00 45.02           N  
ANISOU 2840  NE  ARG A 372     4074   8359   4671   1076    625   1950       N  
ATOM   2841  CZ  ARG A 372      91.075  15.927 -91.211  1.00 49.45           C  
ANISOU 2841  CZ  ARG A 372     4606   9040   5142   1131    634   2168       C  
ATOM   2842  NH1 ARG A 372      91.421  16.676 -90.171  1.00 42.60           N  
ANISOU 2842  NH1 ARG A 372     3679   8467   4040   1076    541   2206       N  
ATOM   2843  NH2 ARG A 372      90.783  14.649 -91.026  1.00 49.85           N  
ANISOU 2843  NH2 ARG A 372     4680   8919   5342   1243    738   2347       N  
ATOM   2844  N   SER A 373      88.335  16.335 -96.265  1.00 38.77           N  
ANISOU 2844  N   SER A 373     3546   6788   4397    980    816   1295       N  
ATOM   2845  CA  SER A 373      87.280  15.854 -97.151  1.00 43.33           C  
ANISOU 2845  CA  SER A 373     4196   7109   5158    987    903   1132       C  
ATOM   2846  C   SER A 373      85.975  16.609 -96.924  1.00 48.29           C  
ANISOU 2846  C   SER A 373     4920   7698   5730    851    893    970       C  
ATOM   2847  O   SER A 373      85.212  16.831 -97.872  1.00 46.68           O  
ANISOU 2847  O   SER A 373     4773   7356   5606    820    911    762       O  
ATOM   2848  CB  SER A 373      87.081  14.349 -96.962  1.00 47.40           C  
ANISOU 2848  CB  SER A 373     4699   7433   5880   1108   1020   1264       C  
ATOM   2849  OG  SER A 373      87.149  13.990 -95.594  1.00 62.00           O  
ANISOU 2849  OG  SER A 373     6533   9368   7656   1118   1032   1496       O  
ATOM   2850  N   GLY A 374      85.707  17.021 -95.686  1.00 49.03           N  
ANISOU 2850  N   GLY A 374     5024   7927   5680    773    861   1052       N  
ATOM   2851  CA  GLY A 374      84.610  17.927 -95.412  1.00 43.98           C  
ANISOU 2851  CA  GLY A 374     4457   7295   4960    636    830    884       C  
ATOM   2852  C   GLY A 374      85.106  19.349 -95.245  1.00 40.75           C  
ANISOU 2852  C   GLY A 374     4024   7098   4363    536    700    811       C  
ATOM   2853  O   GLY A 374      85.712  19.681 -94.222  1.00 43.82           O  
ANISOU 2853  O   GLY A 374     4351   7700   4598    513    642    933       O  
ATOM   2854  N   GLU A 375      84.858  20.199 -96.238  1.00 34.62           N  
ANISOU 2854  N   GLU A 375     3286   6267   3601    478    652    614       N  
ATOM   2855  CA  GLU A 375      85.336  21.574 -96.240  1.00 33.79           C  
ANISOU 2855  CA  GLU A 375     3155   6321   3361    380    534    538       C  
ATOM   2856  C   GLU A 375      84.164  22.545 -96.186  1.00 33.28           C  
ANISOU 2856  C   GLU A 375     3164   6210   3269    257    492    334       C  
ATOM   2857  O   GLU A 375      82.996  22.154 -96.200  1.00 35.52           O  
ANISOU 2857  O   GLU A 375     3518   6348   3632    249    553    243       O  
ATOM   2858  CB  GLU A 375      86.201  21.859 -97.478  1.00 35.84           C  
ANISOU 2858  CB  GLU A 375     3387   6575   3658    418    508    507       C  
ATOM   2859  CG  GLU A 375      87.705  21.678 -97.275  1.00 39.85           C  
ANISOU 2859  CG  GLU A 375     3783   7250   4107    479    480    678       C  
ATOM   2860  CD  GLU A 375      88.260  22.563 -96.177  1.00 42.60           C  
ANISOU 2860  CD  GLU A 375     4063   7829   4293    393    385    724       C  
ATOM   2861  OE1 GLU A 375      89.210  22.138 -95.486  1.00 35.93           O  
ANISOU 2861  OE1 GLU A 375     3127   7138   3385    454    373    890       O  
ATOM   2862  OE2 GLU A 375      87.744  23.685 -96.001  1.00 29.31           O  
ANISOU 2862  OE2 GLU A 375     2410   6176   2551    269    319    585       O  
ATOM   2863  N   THR A 376      84.495  23.831 -96.093  1.00 30.91           N  
ANISOU 2863  N   THR A 376     2839   6034   2870    159    386    256       N  
ATOM   2864  CA  THR A 376      83.490  24.886 -96.141  1.00 33.62           C  
ANISOU 2864  CA  THR A 376     3242   6327   3203     46    329     52       C  
ATOM   2865  C   THR A 376      83.929  25.936 -97.151  1.00 32.46           C  
ANISOU 2865  C   THR A 376     3097   6167   3068      4    254    -35       C  
ATOM   2866  O   THR A 376      84.939  25.758 -97.836  1.00 36.47           O  
ANISOU 2866  O   THR A 376     3564   6704   3590     61    262     58       O  
ATOM   2867  CB  THR A 376      83.279  25.540 -94.765  1.00 37.42           C  
ANISOU 2867  CB  THR A 376     3684   6979   3557    -52    267     28       C  
ATOM   2868  OG1 THR A 376      84.439  26.307 -94.418  1.00 35.96           O  
ANISOU 2868  OG1 THR A 376     3402   6986   3275    -92    178     80       O  
ATOM   2869  CG2 THR A 376      83.013  24.497 -93.675  1.00 29.66           C  
ANISOU 2869  CG2 THR A 376     2685   6054   2531     -7    345    163       C  
ATOM   2870  N   GLU A 377      83.184  27.031 -97.242  1.00 32.43           N  
ANISOU 2870  N   GLU A 377     3138   6121   3063    -96    186   -207       N  
ATOM   2871  CA  GLU A 377      83.552  28.163 -98.082  1.00 30.81           C  
ANISOU 2871  CA  GLU A 377     2933   5900   2872   -150    110   -274       C  
ATOM   2872  C   GLU A 377      84.663  29.022 -97.479  1.00 35.99           C  
ANISOU 2872  C   GLU A 377     3487   6738   3451   -226     30   -216       C  
ATOM   2873  O   GLU A 377      85.020  30.044 -98.075  1.00 39.46           O  
ANISOU 2873  O   GLU A 377     3915   7163   3914   -288    -31   -260       O  
ATOM   2874  CB  GLU A 377      82.310  29.024 -98.354  1.00 29.32           C  
ANISOU 2874  CB  GLU A 377     2826   5586   2730   -222     61   -477       C  
ATOM   2875  CG  GLU A 377      81.624  29.573 -97.096  1.00 32.86           C  
ANISOU 2875  CG  GLU A 377     3258   6100   3129   -319      9   -585       C  
ATOM   2876  CD  GLU A 377      80.497  28.691 -96.565  1.00 39.14           C  
ANISOU 2876  CD  GLU A 377     4101   6834   3936   -291     84   -636       C  
ATOM   2877  OE1 GLU A 377      79.530  29.246 -96.000  1.00 42.65           O  
ANISOU 2877  OE1 GLU A 377     4565   7266   4374   -367     46   -793       O  
ATOM   2878  OE2 GLU A 377      80.568  27.451 -96.698  1.00 35.50           O  
ANISOU 2878  OE2 GLU A 377     3652   6333   3503   -196    183   -524       O  
ATOM   2879  N   ASP A 378      85.205  28.641 -96.319  1.00 40.71           N  
ANISOU 2879  N   ASP A 378     4002   7505   3960   -221     29   -117       N  
ATOM   2880  CA  ASP A 378      86.310  29.370 -95.701  1.00 33.84           C  
ANISOU 2880  CA  ASP A 378     3013   6830   3014   -283    -48    -75       C  
ATOM   2881  C   ASP A 378      87.590  29.215 -96.522  1.00 36.78           C  
ANISOU 2881  C   ASP A 378     3330   7238   3408   -230    -32     52       C  
ATOM   2882  O   ASP A 378      87.841  28.170 -97.129  1.00 35.88           O  
ANISOU 2882  O   ASP A 378     3236   7068   3327   -116     47    158       O  
ATOM   2883  CB  ASP A 378      86.528  28.867 -94.270  1.00 40.38           C  
ANISOU 2883  CB  ASP A 378     3765   7854   3723   -267    -49      6       C  
ATOM   2884  CG  ASP A 378      87.710  29.527 -93.583  1.00 46.63           C  
ANISOU 2884  CG  ASP A 378     4414   8875   4427   -317   -131     38       C  
ATOM   2885  OD1 ASP A 378      88.791  28.901 -93.526  1.00 49.70           O  
ANISOU 2885  OD1 ASP A 378     4728   9378   4776   -237   -110    199       O  
ATOM   2886  OD2 ASP A 378      87.558  30.666 -93.091  1.00 49.26           O  
ANISOU 2886  OD2 ASP A 378     4700   9275   4740   -434   -217   -111       O  
ATOM   2887  N   THR A 379      88.408  30.273 -96.541  1.00 27.87           N  
ANISOU 2887  N   THR A 379     2118   6201   2270   -317   -106     28       N  
ATOM   2888  CA  THR A 379      89.620  30.297 -97.357  1.00 35.69           C  
ANISOU 2888  CA  THR A 379     3045   7232   3283   -290    -91    131       C  
ATOM   2889  C   THR A 379      90.862  30.584 -96.520  1.00 40.46           C  
ANISOU 2889  C   THR A 379     3494   8064   3815   -322   -144    193       C  
ATOM   2890  O   THR A 379      91.823  31.179 -97.018  1.00 33.48           O  
ANISOU 2890  O   THR A 379     2533   7229   2959   -366   -164    216       O  
ATOM   2891  CB  THR A 379      89.509  31.329 -98.480  1.00 30.50           C  
ANISOU 2891  CB  THR A 379     2433   6447   2710   -364   -113     56       C  
ATOM   2892  OG1 THR A 379      89.448  32.645 -97.915  1.00 31.75           O  
ANISOU 2892  OG1 THR A 379     2544   6637   2884   -505   -206    -60       O  
ATOM   2893  CG2 THR A 379      88.269  31.087 -99.304  1.00 26.62           C  
ANISOU 2893  CG2 THR A 379     2085   5753   2277   -324    -73    -19       C  
ATOM   2894  N   PHE A 380      90.864  30.161 -95.251  1.00 33.36           N  
ANISOU 2894  N   PHE A 380     2539   7318   2817   -299   -164    221       N  
ATOM   2895  CA  PHE A 380      91.971  30.502 -94.364  1.00 31.60           C  
ANISOU 2895  CA  PHE A 380     2157   7340   2511   -329   -229    252       C  
ATOM   2896  C   PHE A 380      93.277  29.855 -94.811  1.00 34.54           C  
ANISOU 2896  C   PHE A 380     2444   7799   2878   -236   -193    410       C  
ATOM   2897  O   PHE A 380      94.329  30.506 -94.800  1.00 33.17           O  
ANISOU 2897  O   PHE A 380     2146   7754   2702   -292   -241    402       O  
ATOM   2898  CB  PHE A 380      91.648  30.096 -92.923  1.00 32.38           C  
ANISOU 2898  CB  PHE A 380     2215   7608   2479   -305   -254    264       C  
ATOM   2899  CG  PHE A 380      92.666  30.570 -91.920  1.00 33.89           C  
ANISOU 2899  CG  PHE A 380     2238   8070   2568   -340   -335    257       C  
ATOM   2900  CD1 PHE A 380      93.786  29.805 -91.632  1.00 37.43           C  
ANISOU 2900  CD1 PHE A 380     2594   8679   2947   -233   -319    420       C  
ATOM   2901  CD2 PHE A 380      92.509  31.787 -91.278  1.00 34.28           C  
ANISOU 2901  CD2 PHE A 380     2297   8096   2634   -460   -375     73       C  
ATOM   2902  CE1 PHE A 380      94.730  30.244 -90.720  1.00 47.20           C  
ANISOU 2902  CE1 PHE A 380     3748  10070   4115   -253   -349    391       C  
ATOM   2903  CE2 PHE A 380      93.444  32.232 -90.364  1.00 35.81           C  
ANISOU 2903  CE2 PHE A 380     2401   8439   2768   -476   -402     42       C  
ATOM   2904  CZ  PHE A 380      94.557  31.458 -90.083  1.00 55.25           C  
ANISOU 2904  CZ  PHE A 380     4768  11080   5144   -376   -391    198       C  
ATOM   2905  N   ILE A 381      93.241  28.574 -95.192  1.00 32.18           N  
ANISOU 2905  N   ILE A 381     2199   7434   2593    -95   -109    542       N  
ATOM   2906  CA  ILE A 381      94.482  27.870 -95.500  1.00 37.11           C  
ANISOU 2906  CA  ILE A 381     2730   8156   3213      8    -79    686       C  
ATOM   2907  C   ILE A 381      95.170  28.427 -96.741  1.00 38.38           C  
ANISOU 2907  C   ILE A 381     2866   8264   3455    -33    -64    664       C  
ATOM   2908  O   ILE A 381      96.367  28.183 -96.938  1.00 38.22           O  
ANISOU 2908  O   ILE A 381     2731   8365   3425     15    -58    749       O  
ATOM   2909  CB  ILE A 381      94.238  26.356 -95.652  1.00 42.67           C  
ANISOU 2909  CB  ILE A 381     3494   8774   3945    172     10    820       C  
ATOM   2910  CG1 ILE A 381      93.374  26.053 -96.878  1.00 33.19           C  
ANISOU 2910  CG1 ILE A 381     2430   7322   2860    195     87    765       C  
ATOM   2911  CG2 ILE A 381      93.587  25.792 -94.404  1.00 33.55           C  
ANISOU 2911  CG2 ILE A 381     2360   7676   2710    209      6    872       C  
ATOM   2912  CD1 ILE A 381      93.150  24.568 -97.095  1.00 31.93           C  
ANISOU 2912  CD1 ILE A 381     2313   7056   2763    352    179    872       C  
ATOM   2913  N   ALA A 382      94.453  29.177 -97.583  1.00 31.78           N  
ANISOU 2913  N   ALA A 382     2126   7257   2690   -119    -57    559       N  
ATOM   2914  CA  ALA A 382      95.100  29.836 -98.715  1.00 43.82           C  
ANISOU 2914  CA  ALA A 382     3622   8750   4276   -173    -42    553       C  
ATOM   2915  C   ALA A 382      96.098  30.886 -98.235  1.00 43.18           C  
ANISOU 2915  C   ALA A 382     3394   8830   4183   -291   -114    523       C  
ATOM   2916  O   ALA A 382      97.247  30.918 -98.689  1.00 46.88           O  
ANISOU 2916  O   ALA A 382     3756   9395   4662   -285    -95    587       O  
ATOM   2917  CB  ALA A 382      94.051  30.462 -99.636  1.00 30.63           C  
ANISOU 2917  CB  ALA A 382     2089   6873   2677   -234    -28    458       C  
ATOM   2918  N   ASP A 383      95.676  31.754 -97.311  1.00 36.79           N  
ANISOU 2918  N   ASP A 383     2565   8057   3358   -401   -195    409       N  
ATOM   2919  CA  ASP A 383      96.610  32.693 -96.701  1.00 38.36           C  
ANISOU 2919  CA  ASP A 383     2610   8411   3552   -508   -266    354       C  
ATOM   2920  C   ASP A 383      97.645  31.975 -95.842  1.00 42.48           C  
ANISOU 2920  C   ASP A 383     3046   9119   3977   -413   -271    435       C  
ATOM   2921  O   ASP A 383      98.786  32.439 -95.729  1.00 42.72           O  
ANISOU 2921  O   ASP A 383     2989   9228   4016   -451   -286    426       O  
ATOM   2922  CB  ASP A 383      95.853  33.720 -95.856  1.00 35.76           C  
ANISOU 2922  CB  ASP A 383     2331   8016   3239   -623   -336    185       C  
ATOM   2923  CG  ASP A 383      95.007  34.668 -96.693  1.00 41.75           C  
ANISOU 2923  CG  ASP A 383     3165   8580   4117   -732   -347     95       C  
ATOM   2924  OD1 ASP A 383      93.916  34.258 -97.152  1.00 42.35           O  
ANISOU 2924  OD1 ASP A 383     3377   8512   4201   -685   -315     92       O  
ATOM   2925  OD2 ASP A 383      95.427  35.832 -96.874  1.00 40.93           O  
ANISOU 2925  OD2 ASP A 383     3029   8410   4111   -848   -375     25       O  
ATOM   2926  N   LEU A 384      97.265  30.848 -95.231  1.00 42.46           N  
ANISOU 2926  N   LEU A 384     3059   9189   3886   -288   -257    518       N  
ATOM   2927  CA  LEU A 384      98.190  30.110 -94.374  1.00 40.65           C  
ANISOU 2927  CA  LEU A 384     2750   9139   3558   -184   -265    613       C  
ATOM   2928  C   LEU A 384      99.386  29.580 -95.161  1.00 42.97           C  
ANISOU 2928  C   LEU A 384     2971   9472   3884   -105   -220    723       C  
ATOM   2929  O   LEU A 384     100.527  29.665 -94.694  1.00 42.86           O  
ANISOU 2929  O   LEU A 384     2866   9590   3827    -94   -244    735       O  
ATOM   2930  CB  LEU A 384      97.454  28.964 -93.681  1.00 37.66           C  
ANISOU 2930  CB  LEU A 384     2405   8807   3096    -60   -249    713       C  
ATOM   2931  CG  LEU A 384      98.249  28.146 -92.660  1.00 45.97           C  
ANISOU 2931  CG  LEU A 384     3383  10048   4035     58   -258    834       C  
ATOM   2932  CD1 LEU A 384      98.609  29.002 -91.461  1.00 42.72           C  
ANISOU 2932  CD1 LEU A 384     2922   9775   3534    -28   -318    719       C  
ATOM   2933  CD2 LEU A 384      97.471  26.921 -92.217  1.00 48.50           C  
ANISOU 2933  CD2 LEU A 384     3744  10378   4307    192   -226    975       C  
ATOM   2934  N   VAL A 385      99.149  29.031 -96.358  1.00 44.26           N  
ANISOU 2934  N   VAL A 385     3171   9524   4123    -45   -149    789       N  
ATOM   2935  CA  VAL A 385     100.242  28.434 -97.120  1.00 43.90           C  
ANISOU 2935  CA  VAL A 385     3064   9509   4106     43    -96    881       C  
ATOM   2936  C   VAL A 385     101.172  29.511 -97.667  1.00 37.76           C  
ANISOU 2936  C   VAL A 385     2227   8747   3375    -81   -106    816       C  
ATOM   2937  O   VAL A 385     102.360  29.256 -97.904  1.00 38.85           O  
ANISOU 2937  O   VAL A 385     2282   8968   3510    -37    -90    864       O  
ATOM   2938  CB  VAL A 385      99.684  27.531 -98.239  1.00 47.72           C  
ANISOU 2938  CB  VAL A 385     3623   9849   4661    149     -2    942       C  
ATOM   2939  CG1 VAL A 385      98.966  28.353 -99.300  1.00 45.30           C  
ANISOU 2939  CG1 VAL A 385     3429   9361   4423     41     29    851       C  
ATOM   2940  CG2 VAL A 385     100.786  26.679 -98.858  1.00 37.05           C  
ANISOU 2940  CG2 VAL A 385     2200   8544   3332    272     51   1034       C  
ATOM   2941  N   VAL A 386     100.667  30.730 -97.853  1.00 37.24           N  
ANISOU 2941  N   VAL A 386     2194   8595   3360   -238   -133    707       N  
ATOM   2942  CA  VAL A 386     101.514  31.816 -98.329  1.00 38.02           C  
ANISOU 2942  CA  VAL A 386     2228   8692   3524   -366   -138    655       C  
ATOM   2943  C   VAL A 386     102.372  32.373 -97.198  1.00 42.66           C  
ANISOU 2943  C   VAL A 386     2723   9408   4078   -420   -208    582       C  
ATOM   2944  O   VAL A 386     103.567  32.625 -97.382  1.00 44.74           O  
ANISOU 2944  O   VAL A 386     2888   9747   4365   -443   -201    587       O  
ATOM   2945  CB  VAL A 386     100.656  32.912 -98.981  1.00 40.81           C  
ANISOU 2945  CB  VAL A 386     2647   8889   3970   -508   -138    580       C  
ATOM   2946  CG1 VAL A 386     101.543  34.028 -99.496  1.00 38.16           C  
ANISOU 2946  CG1 VAL A 386     2236   8540   3723   -642   -132    551       C  
ATOM   2947  CG2 VAL A 386      99.822  32.329-100.109  1.00 38.30           C  
ANISOU 2947  CG2 VAL A 386     2414   8465   3672   -442    -63    643       C  
ATOM   2948  N   GLY A 387     101.784  32.577 -96.016  1.00 39.96           N  
ANISOU 2948  N   GLY A 387     2407   9098   3679   -438   -271    503       N  
ATOM   2949  CA  GLY A 387     102.552  33.102 -94.900  1.00 41.88           C  
ANISOU 2949  CA  GLY A 387     2560   9470   3881   -477   -332    415       C  
ATOM   2950  C   GLY A 387     103.566  32.119 -94.350  1.00 42.93           C  
ANISOU 2950  C   GLY A 387     2608   9792   3910   -341   -332    509       C  
ATOM   2951  O   GLY A 387     104.641  32.522 -93.893  1.00 50.04           O  
ANISOU 2951  O   GLY A 387     3400  10809   4802   -368   -363    455       O  
ATOM   2952  N   LEU A 388     103.243  30.826 -94.378  1.00 41.81           N  
ANISOU 2952  N   LEU A 388     2508   9676   3701   -190   -298    646       N  
ATOM   2953  CA  LEU A 388     104.155  29.782 -93.924  1.00 43.06           C  
ANISOU 2953  CA  LEU A 388     2593   9991   3777    -42   -295    759       C  
ATOM   2954  C   LEU A 388     105.255  29.475 -94.932  1.00 52.94           C  
ANISOU 2954  C   LEU A 388     3777  11248   5091      0   -251    819       C  
ATOM   2955  O   LEU A 388     106.210  28.772 -94.581  1.00 44.90           O  
ANISOU 2955  O   LEU A 388     2678  10361   4022    109   -256    887       O  
ATOM   2956  CB  LEU A 388     103.376  28.500 -93.621  1.00 42.50           C  
ANISOU 2956  CB  LEU A 388     2589   9914   3645    109   -268    895       C  
ATOM   2957  CG  LEU A 388     102.928  28.219 -92.187  1.00 52.96           C  
ANISOU 2957  CG  LEU A 388     3919  11361   4843    154   -308    910       C  
ATOM   2958  CD1 LEU A 388     102.395  29.472 -91.511  1.00 52.65           C  
ANISOU 2958  CD1 LEU A 388     3896  11323   4785     -1   -360    731       C  
ATOM   2959  CD2 LEU A 388     101.875  27.120 -92.194  1.00 42.26           C  
ANISOU 2959  CD2 LEU A 388     2650   9932   3477    268   -266   1041       C  
ATOM   2960  N   CYS A 389     105.139  29.981 -96.164  1.00 49.84           N  
ANISOU 2960  N   CYS A 389     3412  10721   4803    -83   -204    795       N  
ATOM   2961  CA  CYS A 389     106.106  29.722 -97.233  1.00 52.30           C  
ANISOU 2961  CA  CYS A 389     3666  11034   5172    -52   -147    846       C  
ATOM   2962  C   CYS A 389     106.308  28.225 -97.451  1.00 51.30           C  
ANISOU 2962  C   CYS A 389     3543  10931   5017    142   -105    976       C  
ATOM   2963  O   CYS A 389     107.422  27.753 -97.689  1.00 51.31           O  
ANISOU 2963  O   CYS A 389     3459  11016   5021    214    -89   1014       O  
ATOM   2964  CB  CYS A 389     107.437  30.422 -96.965  1.00 50.22           C  
ANISOU 2964  CB  CYS A 389     3270  10892   4921   -126   -179    776       C  
ATOM   2965  SG  CYS A 389     107.293  32.208 -96.943  1.00 53.35           S  
ANISOU 2965  SG  CYS A 389     3648  11212   5411   -356   -211    621       S  
ATOM   2966  N   THR A 390     105.203  27.485 -97.385  1.00 42.19           N  
ANISOU 2966  N   THR A 390     2487   9691   3853    227    -85   1036       N  
ATOM   2967  CA  THR A 390     105.234  26.035 -97.515  1.00 43.84           C  
ANISOU 2967  CA  THR A 390     2707   9885   4065    416    -42   1159       C  
ATOM   2968  C   THR A 390     105.565  25.608 -98.944  1.00 50.08           C  
ANISOU 2968  C   THR A 390     3502  10585   4943    464     39   1175       C  
ATOM   2969  O   THR A 390     106.330  24.659 -99.155  1.00 48.46           O  
ANISOU 2969  O   THR A 390     3244  10413   4757    597     65   1238       O  
ATOM   2970  CB  THR A 390     103.883  25.481 -97.051  1.00 50.97           C  
ANISOU 2970  CB  THR A 390     3708  10704   4955    474    -37   1205       C  
ATOM   2971  OG1 THR A 390     103.996  24.981 -95.712  1.00 62.57           O  
ANISOU 2971  OG1 THR A 390     5145  12299   6330    552    -87   1277       O  
ATOM   2972  CG2 THR A 390     103.387  24.398 -97.955  1.00 48.05           C  
ANISOU 2972  CG2 THR A 390     3396  10189   4670    603     46   1273       C  
ATOM   2973  N   GLY A 391     105.013  26.298 -99.937  1.00 49.74           N  
ANISOU 2973  N   GLY A 391     3518  10430   4951    361     81   1113       N  
ATOM   2974  CA  GLY A 391     105.326  25.992-101.313  1.00 48.71           C  
ANISOU 2974  CA  GLY A 391     3393  10232   4881    397    161   1116       C  
ATOM   2975  C   GLY A 391     104.482  24.913-101.953  1.00 47.98           C  
ANISOU 2975  C   GLY A 391     3388  10002   4838    530    229   1146       C  
ATOM   2976  O   GLY A 391     104.667  24.639-103.143  1.00 39.96           O  
ANISOU 2976  O   GLY A 391     2385   8932   3867    565    297   1127       O  
ATOM   2977  N   GLN A 392     103.558  24.295-101.220  1.00 47.87           N  
ANISOU 2977  N   GLN A 392     3432   9932   4823    604    217   1184       N  
ATOM   2978  CA  GLN A 392     102.742  23.230-101.793  1.00 48.71           C  
ANISOU 2978  CA  GLN A 392     3616   9887   5003    732    288   1200       C  
ATOM   2979  C   GLN A 392     101.470  23.060-100.978  1.00 45.46           C  
ANISOU 2979  C   GLN A 392     3279   9407   4587    742    274   1218       C  
ATOM   2980  O   GLN A 392     101.524  22.889 -99.758  1.00 44.80           O  
ANISOU 2980  O   GLN A 392     3162   9411   4451    766    218   1286       O  
ATOM   2981  CB  GLN A 392     103.523  21.910-101.853  1.00 45.77           C  
ANISOU 2981  CB  GLN A 392     3185   9520   4684    908    316   1269       C  
ATOM   2982  CG  GLN A 392     104.481  21.708-100.694  1.00 45.36           C  
ANISOU 2982  CG  GLN A 392     3035   9624   4575    950    247   1353       C  
ATOM   2983  CD  GLN A 392     105.070  20.309-100.642  1.00 45.68           C  
ANISOU 2983  CD  GLN A 392     3029   9642   4687   1139    272   1436       C  
ATOM   2984  OE1 GLN A 392     104.558  19.381-101.270  1.00 49.99           O  
ANISOU 2984  OE1 GLN A 392     3623  10032   5340   1245    340   1435       O  
ATOM   2985  NE2 GLN A 392     106.151  20.152 -99.888  1.00 44.26           N  
ANISOU 2985  NE2 GLN A 392     2750   9609   4457   1182    218   1497       N  
ATOM   2986  N   ILE A 393     100.330  23.092-101.655  1.00 49.59           N  
ANISOU 2986  N   ILE A 393     3902   9782   5157    726    329   1153       N  
ATOM   2987  CA  ILE A 393      99.037  22.943-101.004  1.00 35.58           C  
ANISOU 2987  CA  ILE A 393     2265   7866   3386    714    318   1136       C  
ATOM   2988  C   ILE A 393      98.201  21.966-101.816  1.00 45.03           C  
ANISOU 2988  C   ILE A 393     3561   8859   4688    819    405   1100       C  
ATOM   2989  O   ILE A 393      98.226  21.990-103.051  1.00 42.61           O  
ANISOU 2989  O   ILE A 393     3265   8502   4421    830    458   1029       O  
ATOM   2990  CB  ILE A 393      98.321  24.303-100.854  1.00 34.54           C  
ANISOU 2990  CB  ILE A 393     2213   7708   3202    533    267   1038       C  
ATOM   2991  CG1 ILE A 393      97.012  24.150-100.089  1.00 33.74           C  
ANISOU 2991  CG1 ILE A 393     2237   7484   3096    519    254   1010       C  
ATOM   2992  CG2 ILE A 393      98.076  24.957-102.217  1.00 33.76           C  
ANISOU 2992  CG2 ILE A 393     2170   7521   3134    464    307    948       C  
ATOM   2993  CD1 ILE A 393      96.272  25.447 -99.960  1.00 32.80           C  
ANISOU 2993  CD1 ILE A 393     2191   7329   2943    354    200    897       C  
ATOM   2994  N   LYS A 394      97.485  21.084-101.124  1.00 40.01           N  
ANISOU 2994  N   LYS A 394     2987   8115   4098    900    423   1149       N  
ATOM   2995  CA  LYS A 394      96.456  20.270-101.755  1.00 40.31           C  
ANISOU 2995  CA  LYS A 394     3130   7935   4252    973    502   1086       C  
ATOM   2996  C   LYS A 394      95.121  20.618-101.110  1.00 43.65           C  
ANISOU 2996  C   LYS A 394     3684   8246   4655    887    485   1037       C  
ATOM   2997  O   LYS A 394      94.957  20.481 -99.892  1.00 42.04           O  
ANISOU 2997  O   LYS A 394     3482   8087   4406    882    453   1125       O  
ATOM   2998  CB  LYS A 394      96.766  18.771-101.654  1.00 38.37           C  
ANISOU 2998  CB  LYS A 394     2829   7621   4127   1154    560   1180       C  
ATOM   2999  CG  LYS A 394      96.741  18.158-100.260  1.00 43.46           C  
ANISOU 2999  CG  LYS A 394     3462   8286   4764   1210    538   1338       C  
ATOM   3000  CD  LYS A 394      96.661  16.639-100.351  1.00 47.14           C  
ANISOU 3000  CD  LYS A 394     3914   8594   5403   1384    617   1412       C  
ATOM   3001  CE  LYS A 394      96.103  16.020 -99.077  1.00 45.60           C  
ANISOU 3001  CE  LYS A 394     3762   8342   5220   1422    623   1561       C  
ATOM   3002  NZ  LYS A 394      95.936  14.542 -99.203  1.00 42.39           N  
ANISOU 3002  NZ  LYS A 394     3347   7740   5019   1584    710   1636       N  
ATOM   3003  N   THR A 395      94.184  21.108-101.920  1.00 46.68           N  
ANISOU 3003  N   THR A 395     4170   8505   5060    821    504    895       N  
ATOM   3004  CA  THR A 395      92.870  21.469-101.409  1.00 42.26           C  
ANISOU 3004  CA  THR A 395     3732   7835   4491    740    489    822       C  
ATOM   3005  C   THR A 395      91.798  21.179-102.456  1.00 40.56           C  
ANISOU 3005  C   THR A 395     3616   7427   4369    767    551    680       C  
ATOM   3006  O   THR A 395      90.874  21.974-102.660  1.00 35.39           O  
ANISOU 3006  O   THR A 395     3053   6706   3688    672    524    563       O  
ATOM   3007  CB  THR A 395      92.830  22.933-100.951  1.00 36.84           C  
ANISOU 3007  CB  THR A 395     3057   7252   3688    577    399    777       C  
ATOM   3008  OG1 THR A 395      91.499  23.277-100.553  1.00 44.50           O  
ANISOU 3008  OG1 THR A 395     4140   8108   4658    504    386    681       O  
ATOM   3009  CG2 THR A 395      93.295  23.869-102.054  1.00 31.36           C  
ANISOU 3009  CG2 THR A 395     2345   6599   2973    510    382    711       C  
ATOM   3010  N   GLY A 396      91.917  20.043-103.132  1.00 36.58           N  
ANISOU 3010  N   GLY A 396     3083   6835   3981    902    628    675       N  
ATOM   3011  CA  GLY A 396      90.861  19.502-103.963  1.00 33.49           C  
ANISOU 3011  CA  GLY A 396     2767   6259   3699    951    693    532       C  
ATOM   3012  C   GLY A 396      91.149  19.645-105.450  1.00 37.42           C  
ANISOU 3012  C   GLY A 396     3238   6780   4200    989    718    424       C  
ATOM   3013  O   GLY A 396      92.103  20.294-105.882  1.00 42.57           O  
ANISOU 3013  O   GLY A 396     3827   7585   4763    957    687    462       O  
ATOM   3014  N   ALA A 397      90.293  18.984-106.235  1.00 39.63           N  
ANISOU 3014  N   ALA A 397     3560   6911   4587   1061    780    282       N  
ATOM   3015  CA  ALA A 397      90.268  19.177-107.676  1.00 37.38           C  
ANISOU 3015  CA  ALA A 397     3265   6653   4284   1094    800    147       C  
ATOM   3016  C   ALA A 397      89.850  20.611-107.991  1.00 33.63           C  
ANISOU 3016  C   ALA A 397     2870   6234   3673    964    733     99       C  
ATOM   3017  O   ALA A 397      89.324  21.316-107.129  1.00 32.29           O  
ANISOU 3017  O   ALA A 397     2773   6037   3460    857    677    123       O  
ATOM   3018  CB  ALA A 397      89.298  18.189-108.328  1.00 32.82           C  
ANISOU 3018  CB  ALA A 397     2713   5906   3853   1194    872    -21       C  
ATOM   3019  N   PRO A 398      90.078  21.077-109.223  1.00 29.08           N  
ANISOU 3019  N   PRO A 398     2279   5742   3028    974    737     34       N  
ATOM   3020  CA  PRO A 398      89.525  22.368-109.653  1.00 34.07           C  
ANISOU 3020  CA  PRO A 398     2996   6395   3556    868    679    -13       C  
ATOM   3021  C   PRO A 398      88.025  22.277-109.926  1.00 36.75           C  
ANISOU 3021  C   PRO A 398     3440   6580   3943    882    679   -182       C  
ATOM   3022  O   PRO A 398      87.535  22.725-110.962  1.00 38.87           O  
ANISOU 3022  O   PRO A 398     3748   6863   4158    894    671   -283       O  
ATOM   3023  CB  PRO A 398      90.326  22.673-110.922  1.00 32.54           C  
ANISOU 3023  CB  PRO A 398     2735   6352   3276    900    701     -5       C  
ATOM   3024  CG  PRO A 398      90.638  21.339-111.472  1.00 29.81           C  
ANISOU 3024  CG  PRO A 398     2303   6005   3018   1052    780    -70       C  
ATOM   3025  CD  PRO A 398      90.896  20.459-110.281  1.00 30.37           C  
ANISOU 3025  CD  PRO A 398     2337   6000   3202   1085    795     10       C  
ATOM   3026  N   CYS A 399      87.297  21.675-108.988  1.00 32.60           N  
ANISOU 3026  N   CYS A 399     2955   5917   3516    884    691   -209       N  
ATOM   3027  CA  CYS A 399      85.863  21.462-109.082  1.00 34.18           C  
ANISOU 3027  CA  CYS A 399     3241   5961   3786    895    700   -376       C  
ATOM   3028  C   CYS A 399      85.297  21.463-107.668  1.00 31.03           C  
ANISOU 3028  C   CYS A 399     2893   5472   3427    817    681   -331       C  
ATOM   3029  O   CYS A 399      85.963  21.018-106.728  1.00 30.02           O  
ANISOU 3029  O   CYS A 399     2714   5373   3320    818    696   -188       O  
ATOM   3030  CB  CYS A 399      85.543  20.149-109.811  1.00 34.27           C  
ANISOU 3030  CB  CYS A 399     3206   5886   3929   1037    787   -509       C  
ATOM   3031  SG  CYS A 399      83.786  19.748-109.949  1.00 41.20           S  
ANISOU 3031  SG  CYS A 399     4176   6553   4924   1046    804   -733       S  
ATOM   3032  N   ARG A 400      84.064  21.971-107.533  1.00 25.76           N  
ANISOU 3032  N   ARG A 400     2317   4709   2761    756    647   -456       N  
ATOM   3033  CA  ARG A 400      83.400  22.221-106.248  1.00 28.78           C  
ANISOU 3033  CA  ARG A 400     2752   5030   3152    663    620   -440       C  
ATOM   3034  C   ARG A 400      84.030  23.423-105.548  1.00 34.67           C  
ANISOU 3034  C   ARG A 400     3495   5901   3775    543    532   -323       C  
ATOM   3035  O   ARG A 400      85.244  23.449-105.307  1.00 34.46           O  
ANISOU 3035  O   ARG A 400     3394   5998   3701    543    525   -174       O  
ATOM   3036  CB  ARG A 400      83.435  20.988-105.334  1.00 25.33           C  
ANISOU 3036  CB  ARG A 400     2279   4523   2824    712    697   -360       C  
ATOM   3037  CG  ARG A 400      82.862  19.719-105.949  1.00 30.00           C  
ANISOU 3037  CG  ARG A 400     2854   4965   3578    828    793   -477       C  
ATOM   3038  CD  ARG A 400      83.124  18.504-105.053  1.00 33.42           C  
ANISOU 3038  CD  ARG A 400     3239   5325   4133    881    874   -348       C  
ATOM   3039  NE  ARG A 400      82.466  18.603-103.748  1.00 32.02           N  
ANISOU 3039  NE  ARG A 400     3110   5108   3947    795    872   -291       N  
ATOM   3040  CZ  ARG A 400      81.597  17.713-103.276  1.00 31.52           C  
ANISOU 3040  CZ  ARG A 400     3064   4887   4025    812    955   -325       C  
ATOM   3041  NH1 ARG A 400      81.276  16.643-103.990  1.00 30.72           N  
ANISOU 3041  NH1 ARG A 400     2931   4633   4106    912   1043   -426       N  
ATOM   3042  NH2 ARG A 400      81.050  17.885-102.081  1.00 26.86           N  
ANISOU 3042  NH2 ARG A 400     2512   4294   3398    726    954   -262       N  
ATOM   3043  N   SER A 401      83.208  24.418-105.200  1.00 23.61           N  
ANISOU 3043  N   SER A 401     2165   4469   2335    441    462   -407       N  
ATOM   3044  CA  SER A 401      83.730  25.710-104.762  1.00 32.53           C  
ANISOU 3044  CA  SER A 401     3287   5701   3371    324    371   -341       C  
ATOM   3045  C   SER A 401      84.291  25.720-103.343  1.00 34.57           C  
ANISOU 3045  C   SER A 401     3492   6051   3591    262    351   -222       C  
ATOM   3046  O   SER A 401      84.915  26.716-102.964  1.00 32.80           O  
ANISOU 3046  O   SER A 401     3234   5930   3298    170    280   -169       O  
ATOM   3047  CB  SER A 401      82.654  26.787-104.886  1.00 26.52           C  
ANISOU 3047  CB  SER A 401     2610   4865   2600    243    297   -484       C  
ATOM   3048  OG  SER A 401      82.289  26.974-106.247  1.00 33.83           O  
ANISOU 3048  OG  SER A 401     3577   5746   3530    301    297   -571       O  
ATOM   3049  N   GLU A 402      84.089  24.670-102.540  1.00 28.24           N  
ANISOU 3049  N   GLU A 402     2677   5222   2832    308    412   -178       N  
ATOM   3050  CA  GLU A 402      84.852  24.597-101.298  1.00 28.87           C  
ANISOU 3050  CA  GLU A 402     2687   5432   2849    276    395    -31       C  
ATOM   3051  C   GLU A 402      86.325  24.346-101.577  1.00 30.74           C  
ANISOU 3051  C   GLU A 402     2828   5793   3059    332    403    118       C  
ATOM   3052  O   GLU A 402      87.166  24.588-100.704  1.00 34.39           O  
ANISOU 3052  O   GLU A 402     3217   6403   3448    296    363    231       O  
ATOM   3053  CB  GLU A 402      84.315  23.505-100.375  1.00 25.43           C  
ANISOU 3053  CB  GLU A 402     2257   4942   2461    320    465     14       C  
ATOM   3054  CG  GLU A 402      84.592  22.091-100.850  1.00 27.76           C  
ANISOU 3054  CG  GLU A 402     2525   5154   2867    458    567     85       C  
ATOM   3055  CD  GLU A 402      83.523  21.556-101.779  1.00 29.85           C  
ANISOU 3055  CD  GLU A 402     2853   5231   3257    511    629    -79       C  
ATOM   3056  OE1 GLU A 402      82.630  22.327-102.186  1.00 24.65           O  
ANISOU 3056  OE1 GLU A 402     2263   4518   2584    449    588   -241       O  
ATOM   3057  OE2 GLU A 402      83.566  20.350-102.090  1.00 30.41           O  
ANISOU 3057  OE2 GLU A 402     2898   5206   3450    619    719    -53       O  
ATOM   3058  N   ARG A 403      86.641  23.845-102.769  1.00 26.56           N  
ANISOU 3058  N   ARG A 403     2288   5220   2584    424    454    107       N  
ATOM   3059  CA  ARG A 403      88.010  23.735-103.245  1.00 28.89           C  
ANISOU 3059  CA  ARG A 403     2488   5637   2852    472    461    219       C  
ATOM   3060  C   ARG A 403      88.443  25.008-103.971  1.00 32.25           C  
ANISOU 3060  C   ARG A 403     2909   6137   3209    387    401    193       C  
ATOM   3061  O   ARG A 403      89.478  25.592-103.633  1.00 26.85           O  
ANISOU 3061  O   ARG A 403     2146   5592   2463    331    359    286       O  
ATOM   3062  CB  ARG A 403      88.146  22.507-104.156  1.00 29.67           C  
ANISOU 3062  CB  ARG A 403     2562   5663   3048    617    552    208       C  
ATOM   3063  CG  ARG A 403      87.318  21.301-103.706  1.00 27.14           C  
ANISOU 3063  CG  ARG A 403     2273   5194   2844    693    624    185       C  
ATOM   3064  CD  ARG A 403      87.780  20.742-102.362  1.00 35.47           C  
ANISOU 3064  CD  ARG A 403     3279   6304   3895    707    630    352       C  
ATOM   3065  NE  ARG A 403      86.746  19.909-101.756  1.00 39.45           N  
ANISOU 3065  NE  ARG A 403     3835   6659   4495    732    692    335       N  
ATOM   3066  CZ  ARG A 403      86.825  19.364-100.548  1.00 38.38           C  
ANISOU 3066  CZ  ARG A 403     3678   6547   4357    744    710    478       C  
ATOM   3067  NH1 ARG A 403      87.904  19.550 -99.801  1.00 40.36           N  
ANISOU 3067  NH1 ARG A 403     3852   6976   4508    742    662    641       N  
ATOM   3068  NH2 ARG A 403      85.821  18.629-100.084  1.00 32.96           N  
ANISOU 3068  NH2 ARG A 403     3042   5714   3768    758    779    463       N  
ATOM   3069  N   LEU A 404      87.637  25.469-104.940  1.00 32.58           N  
ANISOU 3069  N   LEU A 404     3029   6085   3263    376    396     70       N  
ATOM   3070  CA  LEU A 404      88.018  26.631-105.745  1.00 30.93           C  
ANISOU 3070  CA  LEU A 404     2821   5933   3000    307    351     70       C  
ATOM   3071  C   LEU A 404      88.145  27.902-104.913  1.00 28.92           C  
ANISOU 3071  C   LEU A 404     2560   5723   2703    159    261     87       C  
ATOM   3072  O   LEU A 404      88.923  28.793-105.274  1.00 37.01           O  
ANISOU 3072  O   LEU A 404     3541   6826   3696     90    230    145       O  
ATOM   3073  CB  LEU A 404      87.011  26.867-106.874  1.00 28.39           C  
ANISOU 3073  CB  LEU A 404     2591   5506   2692    336    356    -60       C  
ATOM   3074  CG  LEU A 404      87.168  26.110-108.193  1.00 31.07           C  
ANISOU 3074  CG  LEU A 404     2911   5857   3039    463    428    -91       C  
ATOM   3075  CD1 LEU A 404      88.637  25.920-108.574  1.00 29.39           C  
ANISOU 3075  CD1 LEU A 404     2585   5796   2786    494    464     40       C  
ATOM   3076  CD2 LEU A 404      86.461  24.778-108.106  1.00 39.85           C  
ANISOU 3076  CD2 LEU A 404     4037   6862   4243    572    494   -183       C  
ATOM   3077  N   ALA A 405      87.388  28.018-103.818  1.00 28.74           N  
ANISOU 3077  N   ALA A 405     2575   5655   2690    105    223     29       N  
ATOM   3078  CA  ALA A 405      87.483  29.216-102.986  1.00 31.47           C  
ANISOU 3078  CA  ALA A 405     2900   6052   3007    -33    134     15       C  
ATOM   3079  C   ALA A 405      88.908  29.435-102.490  1.00 28.33           C  
ANISOU 3079  C   ALA A 405     2376   5824   2564    -70    115    139       C  
ATOM   3080  O   ALA A 405      89.372  30.578-102.397  1.00 27.75           O  
ANISOU 3080  O   ALA A 405     2260   5800   2485   -181     53    138       O  
ATOM   3081  CB  ALA A 405      86.518  29.123-101.806  1.00 24.87           C  
ANISOU 3081  CB  ALA A 405     2102   5177   2171    -70    107    -69       C  
ATOM   3082  N   LYS A 406      89.618  28.352-102.167  1.00 26.76           N  
ANISOU 3082  N   LYS A 406     2109   5712   2347     23    167    243       N  
ATOM   3083  CA  LYS A 406      91.022  28.476-101.785  1.00 34.78           C  
ANISOU 3083  CA  LYS A 406     2993   6902   3320      6    149    356       C  
ATOM   3084  C   LYS A 406      91.879  28.829-102.991  1.00 37.68           C  
ANISOU 3084  C   LYS A 406     3317   7304   3695      7    176    403       C  
ATOM   3085  O   LYS A 406      92.709  29.744-102.934  1.00 45.68           O  
ANISOU 3085  O   LYS A 406     4251   8412   4694    -89    135    435       O  
ATOM   3086  CB  LYS A 406      91.521  27.178-101.145  1.00 34.01           C  
ANISOU 3086  CB  LYS A 406     2835   6881   3207    123    195    462       C  
ATOM   3087  CG  LYS A 406      91.019  26.899 -99.734  1.00 35.60           C  
ANISOU 3087  CG  LYS A 406     3041   7118   3369    113    167    467       C  
ATOM   3088  CD  LYS A 406      89.617  26.312 -99.727  1.00 33.89           C  
ANISOU 3088  CD  LYS A 406     2945   6731   3202    150    211    390       C  
ATOM   3089  CE  LYS A 406      89.287  25.718 -98.371  1.00 28.62           C  
ANISOU 3089  CE  LYS A 406     2266   6118   2491    168    214    444       C  
ATOM   3090  NZ  LYS A 406      87.874  25.275 -98.313  1.00 30.64           N  
ANISOU 3090  NZ  LYS A 406     2632   6209   2802    179    260    356       N  
ATOM   3091  N   TYR A 407      91.696  28.098-104.093  1.00 33.64           N  
ANISOU 3091  N   TYR A 407     2847   6725   3209    112    249    401       N  
ATOM   3092  CA  TYR A 407      92.453  28.382-105.307  1.00 33.22           C  
ANISOU 3092  CA  TYR A 407     2751   6725   3145    120    284    445       C  
ATOM   3093  C   TYR A 407      92.179  29.793-105.810  1.00 30.83           C  
ANISOU 3093  C   TYR A 407     2495   6378   2842     -6    237    412       C  
ATOM   3094  O   TYR A 407      93.096  30.482-106.271  1.00 32.48           O  
ANISOU 3094  O   TYR A 407     2632   6672   3037    -69    239    482       O  
ATOM   3095  CB  TYR A 407      92.115  27.346-106.382  1.00 34.52           C  
ANISOU 3095  CB  TYR A 407     2954   6830   3331    261    366    413       C  
ATOM   3096  CG  TYR A 407      92.579  25.945-106.046  1.00 37.93           C  
ANISOU 3096  CG  TYR A 407     3319   7296   3796    393    421    461       C  
ATOM   3097  CD1 TYR A 407      91.719  24.856-106.164  1.00 32.94           C  
ANISOU 3097  CD1 TYR A 407     2747   6539   3231    503    472    393       C  
ATOM   3098  CD2 TYR A 407      93.879  25.708-105.617  1.00 29.72           C  
ANISOU 3098  CD2 TYR A 407     2150   6406   2736    409    423    572       C  
ATOM   3099  CE1 TYR A 407      92.145  23.570-105.854  1.00 32.53           C  
ANISOU 3099  CE1 TYR A 407     2630   6492   3237    626    525    448       C  
ATOM   3100  CE2 TYR A 407      94.310  24.432-105.312  1.00 30.34           C  
ANISOU 3100  CE2 TYR A 407     2165   6505   2857    540    468    626       C  
ATOM   3101  CZ  TYR A 407      93.446  23.367-105.429  1.00 35.62           C  
ANISOU 3101  CZ  TYR A 407     2899   7031   3605    648    520    571       C  
ATOM   3102  OH  TYR A 407      93.896  22.103-105.117  1.00 30.81           O  
ANISOU 3102  OH  TYR A 407     2222   6421   3065    779    566    636       O  
ATOM   3103  N   ASN A 408      90.926  30.248-105.727  1.00 30.75           N  
ANISOU 3103  N   ASN A 408     2599   6229   2856    -43    196    307       N  
ATOM   3104  CA  ASN A 408      90.629  31.613-106.151  1.00 34.73           C  
ANISOU 3104  CA  ASN A 408     3147   6671   3379   -157    143    282       C  
ATOM   3105  C   ASN A 408      91.308  32.625-105.240  1.00 31.13           C  
ANISOU 3105  C   ASN A 408     2605   6279   2943   -299     76    307       C  
ATOM   3106  O   ASN A 408      91.809  33.655-105.706  1.00 36.45           O  
ANISOU 3106  O   ASN A 408     3246   6958   3645   -393     60    354       O  
ATOM   3107  CB  ASN A 408      89.120  31.846-106.191  1.00 26.41           C  
ANISOU 3107  CB  ASN A 408     2225   5455   2356   -156    106    151       C  
ATOM   3108  CG  ASN A 408      88.444  31.063-107.296  1.00 31.78           C  
ANISOU 3108  CG  ASN A 408     2979   6072   3022    -27    166    105       C  
ATOM   3109  OD1 ASN A 408      89.057  30.762-108.324  1.00 26.50           O  
ANISOU 3109  OD1 ASN A 408     2278   5475   2317     38    224    172       O  
ATOM   3110  ND2 ASN A 408      87.179  30.722-107.090  1.00 25.13           N  
ANISOU 3110  ND2 ASN A 408     2228   5111   2209     11    153    -23       N  
ATOM   3111  N   GLN A 409      91.350  32.340-103.939  1.00 34.61           N  
ANISOU 3111  N   GLN A 409     3000   6776   3374   -315     40    277       N  
ATOM   3112  CA  GLN A 409      91.994  33.259-103.007  1.00 32.49           C  
ANISOU 3112  CA  GLN A 409     2630   6594   3121   -443    -29    271       C  
ATOM   3113  C   GLN A 409      93.499  33.316-103.241  1.00 29.91           C  
ANISOU 3113  C   GLN A 409     2165   6418   2780   -461      0    385       C  
ATOM   3114  O   GLN A 409      94.102  34.391-103.157  1.00 36.82           O  
ANISOU 3114  O   GLN A 409     2964   7324   3703   -586    -38    388       O  
ATOM   3115  CB  GLN A 409      91.669  32.855-101.568  1.00 28.62           C  
ANISOU 3115  CB  GLN A 409     2116   6165   2594   -440    -72    212       C  
ATOM   3116  CG  GLN A 409      92.410  33.650-100.503  1.00 34.61           C  
ANISOU 3116  CG  GLN A 409     2744   7059   3349   -553   -146    186       C  
ATOM   3117  CD  GLN A 409      92.026  35.123-100.459  1.00 39.10           C  
ANISOU 3117  CD  GLN A 409     3319   7533   4005   -702   -221     77       C  
ATOM   3118  OE1 GLN A 409      91.134  35.576-101.179  1.00 34.00           O  
ANISOU 3118  OE1 GLN A 409     2786   6716   3418   -718   -223     28       O  
ATOM   3119  NE2 GLN A 409      92.701  35.878 -99.597  1.00 41.54           N  
ANISOU 3119  NE2 GLN A 409     3496   7955   4332   -808   -285     29       N  
ATOM   3120  N   LEU A 410      94.120  32.177-103.556  1.00 30.11           N  
ANISOU 3120  N   LEU A 410     2149   6533   2758   -338     69    470       N  
ATOM   3121  CA  LEU A 410      95.547  32.189-103.870  1.00 34.24           C  
ANISOU 3121  CA  LEU A 410     2536   7207   3269   -345    102    570       C  
ATOM   3122  C   LEU A 410      95.831  33.027-105.111  1.00 38.02           C  
ANISOU 3122  C   LEU A 410     3021   7645   3779   -413    138    614       C  
ATOM   3123  O   LEU A 410      96.849  33.725-105.174  1.00 33.16           O  
ANISOU 3123  O   LEU A 410     2292   7119   3188   -507    137    665       O  
ATOM   3124  CB  LEU A 410      96.062  30.760-104.045  1.00 31.43           C  
ANISOU 3124  CB  LEU A 410     2138   6936   2869   -186    170    639       C  
ATOM   3125  CG  LEU A 410      96.168  29.945-102.754  1.00 32.31           C  
ANISOU 3125  CG  LEU A 410     2201   7128   2947   -120    140    650       C  
ATOM   3126  CD1 LEU A 410      96.292  28.457-103.041  1.00 31.61           C  
ANISOU 3126  CD1 LEU A 410     2113   7045   2852     55    212    710       C  
ATOM   3127  CD2 LEU A 410      97.351  30.432-101.936  1.00 32.79           C  
ANISOU 3127  CD2 LEU A 410     2101   7373   2985   -191     89    683       C  
ATOM   3128  N   MET A 411      94.935  32.984-106.103  1.00 41.96           N  
ANISOU 3128  N   MET A 411     3649   8018   4278   -366    170    596       N  
ATOM   3129  CA  MET A 411      95.083  33.854-107.267  1.00 35.60           C  
ANISOU 3129  CA  MET A 411     2862   7176   3489   -429    199    654       C  
ATOM   3130  C   MET A 411      94.942  35.323-106.880  1.00 40.85           C  
ANISOU 3130  C   MET A 411     3525   7755   4242   -598    127    631       C  
ATOM   3131  O   MET A 411      95.628  36.187-107.438  1.00 37.58           O  
ANISOU 3131  O   MET A 411     3052   7357   3868   -694    149    713       O  
ATOM   3132  CB  MET A 411      94.062  33.482-108.347  1.00 33.19           C  
ANISOU 3132  CB  MET A 411     2692   6769   3150   -329    236    628       C  
ATOM   3133  CG  MET A 411      94.327  32.150-109.051  1.00 41.92           C  
ANISOU 3133  CG  MET A 411     3779   7961   4189   -168    321    646       C  
ATOM   3134  SD  MET A 411      93.496  32.004-110.654  1.00 41.38           S  
ANISOU 3134  SD  MET A 411     3819   7838   4065    -71    374    626       S  
ATOM   3135  CE  MET A 411      91.795  31.825-110.131  1.00 32.43           C  
ANISOU 3135  CE  MET A 411     2837   6513   2972    -35    309    471       C  
ATOM   3136  N   ARG A 412      94.057  35.626-105.926  1.00 44.54           N  
ANISOU 3136  N   ARG A 412     4047   8126   4749   -638     46    515       N  
ATOM   3137  CA  ARG A 412      93.933  37.001-105.449  1.00 40.81           C  
ANISOU 3137  CA  ARG A 412     3554   7570   4382   -796    -30    463       C  
ATOM   3138  C   ARG A 412      95.177  37.430-104.684  1.00 37.92           C  
ANISOU 3138  C   ARG A 412     3014   7340   4053   -899    -50    479       C  
ATOM   3139  O   ARG A 412      95.584  38.595-104.755  1.00 34.86           O  
ANISOU 3139  O   ARG A 412     2566   6908   3773  -1038    -72    489       O  
ATOM   3140  CB  ARG A 412      92.695  37.151-104.566  1.00 36.80           C  
ANISOU 3140  CB  ARG A 412     3130   6951   3902   -807   -112    311       C  
ATOM   3141  CG  ARG A 412      91.374  36.922-105.276  1.00 33.26           C  
ANISOU 3141  CG  ARG A 412     2845   6352   3439   -725   -106    266       C  
ATOM   3142  CD  ARG A 412      90.211  37.334-104.389  1.00 33.59           C  
ANISOU 3142  CD  ARG A 412     2950   6282   3531   -767   -192    104       C  
ATOM   3143  NE  ARG A 412      88.955  36.764-104.858  1.00 43.40           N  
ANISOU 3143  NE  ARG A 412     4332   7417   4742   -663   -180     39       N  
ATOM   3144  CZ  ARG A 412      88.411  35.654-104.373  1.00 43.21           C  
ANISOU 3144  CZ  ARG A 412     4343   7419   4656   -568   -157    -21       C  
ATOM   3145  NH1 ARG A 412      89.006  34.992-103.386  1.00 35.36           N  
ANISOU 3145  NH1 ARG A 412     3262   6559   3613   -557   -146     -5       N  
ATOM   3146  NH2 ARG A 412      87.266  35.206-104.871  1.00 36.91           N  
ANISOU 3146  NH2 ARG A 412     3662   6514   3849   -483   -144    -95       N  
ATOM   3147  N   ILE A 413      95.787  36.503-103.943  1.00 41.39           N  
ANISOU 3147  N   ILE A 413     3367   7943   4416   -830    -42    480       N  
ATOM   3148  CA  ILE A 413      96.995  36.822-103.189  1.00 45.68           C  
ANISOU 3148  CA  ILE A 413     3732   8646   4980   -910    -67    482       C  
ATOM   3149  C   ILE A 413      98.155  37.109-104.133  1.00 45.73           C  
ANISOU 3149  C   ILE A 413     3644   8719   5013   -952      7    604       C  
ATOM   3150  O   ILE A 413      98.931  38.048-103.915  1.00 53.21           O  
ANISOU 3150  O   ILE A 413     4466   9701   6049  -1089    -12    598       O  
ATOM   3151  CB  ILE A 413      97.325  35.679-102.212  1.00 42.23           C  
ANISOU 3151  CB  ILE A 413     3230   8374   4440   -801    -78    473       C  
ATOM   3152  CG1 ILE A 413      96.288  35.621-101.084  1.00 38.11           C  
ANISOU 3152  CG1 ILE A 413     2770   7815   3896   -797   -155    350       C  
ATOM   3153  CG2 ILE A 413      98.726  35.842-101.656  1.00 35.55           C  
ANISOU 3153  CG2 ILE A 413     2187   7726   3594   -851    -92    494       C  
ATOM   3154  CD1 ILE A 413      96.291  34.318-100.310  1.00 33.02           C  
ANISOU 3154  CD1 ILE A 413     2114   7292   3141   -660   -147    377       C  
ATOM   3155  N   GLU A 414      98.287  36.311-105.197  1.00 45.72           N  
ANISOU 3155  N   GLU A 414     3689   8741   4941   -839     96    705       N  
ATOM   3156  CA  GLU A 414      99.340  36.545-106.181  1.00 36.40           C  
ANISOU 3156  CA  GLU A 414     2422   7641   3768   -874    178    823       C  
ATOM   3157  C   GLU A 414      99.170  37.896-106.862  1.00 41.25           C  
ANISOU 3157  C   GLU A 414     3069   8119   4487  -1017    184    867       C  
ATOM   3158  O   GLU A 414     100.148  38.622-107.073  1.00 47.06           O  
ANISOU 3158  O   GLU A 414     3682   8907   5293  -1134    216    929       O  
ATOM   3159  CB  GLU A 414      99.346  35.425-107.224  1.00 44.73           C  
ANISOU 3159  CB  GLU A 414     3528   8747   4720   -715    269    897       C  
ATOM   3160  CG  GLU A 414     100.514  35.510-108.213  1.00 37.37           C  
ANISOU 3160  CG  GLU A 414     2486   7943   3770   -736    364   1013       C  
ATOM   3161  CD  GLU A 414     100.585  34.311-109.137  1.00 41.72           C  
ANISOU 3161  CD  GLU A 414     3060   8576   4218   -568    448   1053       C  
ATOM   3162  OE1 GLU A 414      99.739  34.207-110.051  1.00 45.87           O  
ANISOU 3162  OE1 GLU A 414     3713   9013   4702   -507    479   1062       O  
ATOM   3163  OE2 GLU A 414     101.484  33.464-108.944  1.00 43.15           O  
ANISOU 3163  OE2 GLU A 414     3122   8911   4361   -490    478   1063       O  
ATOM   3164  N   GLU A 415      97.933  38.242-107.225  1.00 38.28           N  
ANISOU 3164  N   GLU A 415     2852   7562   4130  -1007    156    839       N  
ATOM   3165  CA  GLU A 415      97.669  39.537-107.844  1.00 43.62           C  
ANISOU 3165  CA  GLU A 415     3571   8086   4918  -1131    153    893       C  
ATOM   3166  C   GLU A 415      97.976  40.688-106.893  1.00 46.55           C  
ANISOU 3166  C   GLU A 415     3839   8397   5448  -1304     79    815       C  
ATOM   3167  O   GLU A 415      98.434  41.750-107.330  1.00 49.09           O  
ANISOU 3167  O   GLU A 415     4108   8649   5894  -1438    103    892       O  
ATOM   3168  CB  GLU A 415      96.213  39.593-108.307  1.00 53.07           C  
ANISOU 3168  CB  GLU A 415     4956   9108   6099  -1064    121    858       C  
ATOM   3169  CG  GLU A 415      95.721  40.974-108.696  1.00 58.34           C  
ANISOU 3169  CG  GLU A 415     5680   9584   6903  -1183     86    892       C  
ATOM   3170  CD  GLU A 415      94.215  41.032-108.810  1.00 62.04           C  
ANISOU 3170  CD  GLU A 415     6318   9884   7369  -1116     24    808       C  
ATOM   3171  OE1 GLU A 415      93.619  40.045-109.290  1.00 60.68           O  
ANISOU 3171  OE1 GLU A 415     6239   9748   7068   -966     52    794       O  
ATOM   3172  OE2 GLU A 415      93.627  42.058-108.406  1.00 66.06           O  
ANISOU 3172  OE2 GLU A 415     6857  10225   8019  -1213    -55    740       O  
ATOM   3173  N   GLU A 416      97.739  40.496-105.594  1.00 52.95           N  
ANISOU 3173  N   GLU A 416     4614   9241   6265  -1306     -7    662       N  
ATOM   3174  CA  GLU A 416      98.007  41.559-104.630  1.00 55.36           C  
ANISOU 3174  CA  GLU A 416     4804   9512   6718  -1464    -84    550       C  
ATOM   3175  C   GLU A 416      99.504  41.737-104.402  1.00 51.70           C  
ANISOU 3175  C   GLU A 416     4136   9216   6292  -1548    -50    585       C  
ATOM   3176  O   GLU A 416      99.986  42.866-104.251  1.00 53.70           O  
ANISOU 3176  O   GLU A 416     4283   9409   6713  -1709    -66    559       O  
ATOM   3177  CB  GLU A 416      97.294  41.257-103.314  1.00 53.21           C  
ANISOU 3177  CB  GLU A 416     4545   9263   6411  -1431   -183    370       C  
ATOM   3178  CG  GLU A 416      97.300  42.408-102.329  1.00 63.15           C  
ANISOU 3178  CG  GLU A 416     5700  10471   7825  -1585   -277    212       C  
ATOM   3179  CD  GLU A 416      96.435  42.132-101.115  1.00 71.53           C  
ANISOU 3179  CD  GLU A 416     6788  11560   8830  -1547   -371     32       C  
ATOM   3180  OE1 GLU A 416      96.523  41.016-100.559  1.00 73.34           O  
ANISOU 3180  OE1 GLU A 416     7010  11958   8899  -1431   -366     31       O  
ATOM   3181  OE2 GLU A 416      95.658  43.028-100.724  1.00 72.59           O  
ANISOU 3181  OE2 GLU A 416     6949  11547   9084  -1630   -446   -103       O  
ATOM   3182  N   LEU A 417     100.254  40.634-104.362  1.00 46.60           N  
ANISOU 3182  N   LEU A 417     3423   8774   5508  -1440     -3    634       N  
ATOM   3183  CA  LEU A 417     101.697  40.731-104.187  1.00 48.73           C  
ANISOU 3183  CA  LEU A 417     3501   9209   5804  -1500     30    659       C  
ATOM   3184  C   LEU A 417     102.370  41.366-105.401  1.00 55.11           C  
ANISOU 3184  C   LEU A 417     4266   9982   6692  -1594    132    811       C  
ATOM   3185  O   LEU A 417     103.417  42.007-105.259  1.00 53.27           O  
ANISOU 3185  O   LEU A 417     3922   9756   6562  -1687    148    797       O  
ATOM   3186  CB  LEU A 417     102.279  39.348-103.910  1.00 44.42           C  
ANISOU 3186  CB  LEU A 417     2936   8847   5094  -1328     51    675       C  
ATOM   3187  CG  LEU A 417     101.914  38.777-102.541  1.00 40.24           C  
ANISOU 3187  CG  LEU A 417     2425   8374   4491  -1244    -43    544       C  
ATOM   3188  CD1 LEU A 417     102.117  37.274-102.515  1.00 41.33           C  
ANISOU 3188  CD1 LEU A 417     2579   8650   4472  -1058    -11    606       C  
ATOM   3189  CD2 LEU A 417     102.753  39.455-101.469  1.00 41.70           C  
ANISOU 3189  CD2 LEU A 417     2502   8595   4748  -1320   -108    421       C  
ATOM   3190  N   GLY A 418     101.788  41.201-106.587  1.00 61.98           N  
ANISOU 3190  N   GLY A 418     5282  10759   7509  -1532    200    938       N  
ATOM   3191  CA  GLY A 418     102.315  41.793-107.799  1.00 70.42           C  
ANISOU 3191  CA  GLY A 418     6332  11797   8627  -1608    304   1105       C  
ATOM   3192  C   GLY A 418     103.694  41.297-108.180  1.00 76.25           C  
ANISOU 3192  C   GLY A 418     6923  12743   9304  -1592    396   1182       C  
ATOM   3193  O   GLY A 418     103.904  40.094-108.368  1.00 76.40           O  
ANISOU 3193  O   GLY A 418     6961  12898   9168  -1430    426   1190       O  
ATOM   3194  N   ASP A 419     104.650  42.221-108.287  1.00 83.53           N  
ANISOU 3194  N   ASP A 419     7744  13630  10364  -1729    431   1211       N  
ATOM   3195  CA  ASP A 419     106.002  41.865-108.702  1.00 87.40           C  
ANISOU 3195  CA  ASP A 419     8139  14258  10812  -1700    513   1258       C  
ATOM   3196  C   ASP A 419     106.783  41.134-107.613  1.00 84.35           C  
ANISOU 3196  C   ASP A 419     7658  14013  10378  -1619    450   1112       C  
ATOM   3197  O   ASP A 419     107.785  40.476-107.920  1.00 78.92           O  
ANISOU 3197  O   ASP A 419     6905  13466   9613  -1544    503   1139       O  
ATOM   3198  CB  ASP A 419     106.760  43.120-109.137  1.00 93.86           C  
ANISOU 3198  CB  ASP A 419     8870  14984  11809  -1881    578   1331       C  
ATOM   3199  CG  ASP A 419     105.969  43.962-110.117  1.00 99.63           C  
ANISOU 3199  CG  ASP A 419     9698  15553  12605  -1969    631   1495       C  
ATOM   3200  OD1 ASP A 419     105.341  43.378-111.026  1.00 98.78           O  
ANISOU 3200  OD1 ASP A 419     9705  15483  12343  -1861    678   1612       O  
ATOM   3201  OD2 ASP A 419     105.956  45.202-109.967  1.00103.21           O  
ANISOU 3201  OD2 ASP A 419    10112  15834  13269  -2139    621   1504       O  
ATOM   3202  N   GLU A 420     106.353  41.231-106.355  1.00 86.27           N  
ANISOU 3202  N   GLU A 420     7894  14226  10659  -1626    335    960       N  
ATOM   3203  CA  GLU A 420     106.985  40.508-105.258  1.00 84.73           C  
ANISOU 3203  CA  GLU A 420     7626  14172  10395  -1533    268    837       C  
ATOM   3204  C   GLU A 420     106.488  39.075-105.134  1.00 79.55           C  
ANISOU 3204  C   GLU A 420     7056  13615   9553  -1336    250    849       C  
ATOM   3205  O   GLU A 420     106.882  38.376-104.193  1.00 73.04           O  
ANISOU 3205  O   GLU A 420     6189  12904   8658  -1242    191    771       O  
ATOM   3206  CB  GLU A 420     106.752  41.245-103.935  1.00 86.51           C  
ANISOU 3206  CB  GLU A 420     7810  14332  10727  -1614    155    664       C  
ATOM   3207  CG  GLU A 420     106.478  42.741-104.077  1.00 95.33           C  
ANISOU 3207  CG  GLU A 420     8906  15253  12061  -1806    151    639       C  
ATOM   3208  CD  GLU A 420     107.718  43.572-104.395  1.00106.46           C  
ANISOU 3208  CD  GLU A 420    10171  16650  13627  -1936    217    657       C  
ATOM   3209  OE1 GLU A 420     108.703  43.035-104.947  1.00107.71           O  
ANISOU 3209  OE1 GLU A 420    10269  16941  13714  -1888    296    738       O  
ATOM   3210  OE2 GLU A 420     107.702  44.783-104.087  1.00109.67           O  
ANISOU 3210  OE2 GLU A 420    10521  16904  14246  -2086    191    579       O  
ATOM   3211  N   ALA A 421     105.631  38.629-106.046  1.00 76.90           N  
ANISOU 3211  N   ALA A 421     6838  13237   9146  -1269    302    946       N  
ATOM   3212  CA  ALA A 421     105.110  37.273-105.999  1.00 70.25           C  
ANISOU 3212  CA  ALA A 421     6074  12461   8158  -1082    296    951       C  
ATOM   3213  C   ALA A 421     106.120  36.299-106.590  1.00 62.82           C  
ANISOU 3213  C   ALA A 421     5084  11653   7131   -960    364   1010       C  
ATOM   3214  O   ALA A 421     106.722  36.562-107.634  1.00 66.42           O  
ANISOU 3214  O   ALA A 421     5511  12125   7598   -996    451   1092       O  
ATOM   3215  CB  ALA A 421     103.785  37.184-106.757  1.00 61.32           C  
ANISOU 3215  CB  ALA A 421     5079  11227   6994  -1052    326   1006       C  
ATOM   3216  N   ARG A 422     106.310  35.176-105.906  1.00 56.07           N  
ANISOU 3216  N   ARG A 422     4219  10891   6195   -813    324    969       N  
ATOM   3217  CA  ARG A 422     107.157  34.093-106.378  1.00 51.96           C  
ANISOU 3217  CA  ARG A 422     3658  10484   5603   -675    374   1008       C  
ATOM   3218  C   ARG A 422     106.347  32.807-106.425  1.00 53.01           C  
ANISOU 3218  C   ARG A 422     3888  10601   5653   -495    375   1015       C  
ATOM   3219  O   ARG A 422     105.597  32.502-105.494  1.00 57.76           O  
ANISOU 3219  O   ARG A 422     4537  11172   6238   -454    309    973       O  
ATOM   3220  CB  ARG A 422     108.377  33.909-105.473  1.00 57.03           C  
ANISOU 3220  CB  ARG A 422     4166  11255   6247   -662    327    956       C  
ATOM   3221  CG  ARG A 422     109.352  35.068-105.491  1.00 68.04           C  
ANISOU 3221  CG  ARG A 422     5443  12671   7739   -827    341    933       C  
ATOM   3222  CD  ARG A 422     110.279  34.993-106.691  1.00 74.89           C  
ANISOU 3222  CD  ARG A 422     6253  13595   8606   -830    443   1003       C  
ATOM   3223  NE  ARG A 422     110.421  36.291-107.342  1.00 81.12           N  
ANISOU 3223  NE  ARG A 422     7017  14306   9499  -1011    501   1044       N  
ATOM   3224  CZ  ARG A 422     111.263  37.241-106.946  1.00 82.15           C  
ANISOU 3224  CZ  ARG A 422     7026  14445   9743  -1153    495    997       C  
ATOM   3225  NH1 ARG A 422     112.047  37.042-105.894  1.00 82.53           N  
ANISOU 3225  NH1 ARG A 422     6965  14594   9798  -1129    427    897       N  
ATOM   3226  NH2 ARG A 422     111.317  38.391-107.604  1.00 82.78           N  
ANISOU 3226  NH2 ARG A 422     7090  14428   9935  -1315    559   1053       N  
ATOM   3227  N   PHE A 423     106.490  32.059-107.514  1.00 50.55           N  
ANISOU 3227  N   PHE A 423     3604  10305   5297   -390    452   1061       N  
ATOM   3228  CA  PHE A 423     105.863  30.751-107.650  1.00 45.85           C  
ANISOU 3228  CA  PHE A 423     3085   9684   4651   -210    463   1053       C  
ATOM   3229  C   PHE A 423     106.896  29.678-107.332  1.00 47.37           C  
ANISOU 3229  C   PHE A 423     3190   9985   4825    -81    457   1049       C  
ATOM   3230  O   PHE A 423     108.016  29.718-107.853  1.00 53.68           O  
ANISOU 3230  O   PHE A 423     3897  10874   5624    -93    495   1061       O  
ATOM   3231  CB  PHE A 423     105.288  30.556-109.056  1.00 40.71           C  
ANISOU 3231  CB  PHE A 423     2522   8977   3970   -163    545   1078       C  
ATOM   3232  CG  PHE A 423     104.568  29.249-109.241  1.00 42.94           C  
ANISOU 3232  CG  PHE A 423     2881   9207   4226     16    560   1043       C  
ATOM   3233  CD1 PHE A 423     105.001  28.329-110.184  1.00 40.30           C  
ANISOU 3233  CD1 PHE A 423     2534   8911   3869    140    619   1032       C  
ATOM   3234  CD2 PHE A 423     103.467  28.933-108.462  1.00 38.39           C  
ANISOU 3234  CD2 PHE A 423     2383   8542   3661     56    516   1010       C  
ATOM   3235  CE1 PHE A 423     104.342  27.122-110.352  1.00 45.88           C  
ANISOU 3235  CE1 PHE A 423     3304   9550   4581    300    635    983       C  
ATOM   3236  CE2 PHE A 423     102.807  27.728-108.623  1.00 37.65           C  
ANISOU 3236  CE2 PHE A 423     2356   8383   3568    216    538    975       C  
ATOM   3237  CZ  PHE A 423     103.243  26.822-109.568  1.00 43.94           C  
ANISOU 3237  CZ  PHE A 423     3136   9199   4358    337    597    958       C  
ATOM   3238  N   ALA A 424     106.523  28.732-106.465  1.00 48.26           N  
ANISOU 3238  N   ALA A 424     3325  10087   4924     41    411   1037       N  
ATOM   3239  CA  ALA A 424     107.483  27.735-105.998  1.00 43.39           C  
ANISOU 3239  CA  ALA A 424     2620   9567   4298    166    395   1046       C  
ATOM   3240  C   ALA A 424     108.003  26.887-107.149  1.00 43.09           C  
ANISOU 3240  C   ALA A 424     2563   9545   4264    276    471   1047       C  
ATOM   3241  O   ALA A 424     109.196  26.564-107.199  1.00 44.49           O  
ANISOU 3241  O   ALA A 424     2631   9830   4442    313    478   1047       O  
ATOM   3242  CB  ALA A 424     106.847  26.851-104.924  1.00 41.80           C  
ANISOU 3242  CB  ALA A 424     2459   9335   4088    282    343   1059       C  
ATOM   3243  N   GLY A 425     107.122  26.517-108.075  1.00 42.17           N  
ANISOU 3243  N   GLY A 425     2546   9329   4148    331    526   1033       N  
ATOM   3244  CA  GLY A 425     107.536  25.775-109.254  1.00 42.83           C  
ANISOU 3244  CA  GLY A 425     2613   9430   4231    428    598   1009       C  
ATOM   3245  C   GLY A 425     108.150  24.437-108.897  1.00 43.60           C  
ANISOU 3245  C   GLY A 425     2646   9555   4365    592    590    997       C  
ATOM   3246  O   GLY A 425     107.582  23.643-108.139  1.00 43.01           O  
ANISOU 3246  O   GLY A 425     2611   9407   4325    693    559   1007       O  
ATOM   3247  N   HIS A 426     109.333  24.179-109.451  1.00 45.08           N  
ANISOU 3247  N   HIS A 426     2729   9847   4552    619    622    981       N  
ATOM   3248  CA  HIS A 426     110.042  22.935-109.187  1.00 46.10           C  
ANISOU 3248  CA  HIS A 426     2781  10005   4729    774    617    966       C  
ATOM   3249  C   HIS A 426     110.702  22.905-107.817  1.00 49.03           C  
ANISOU 3249  C   HIS A 426     3072  10454   5104    783    540   1015       C  
ATOM   3250  O   HIS A 426     111.238  21.860-107.433  1.00 50.46           O  
ANISOU 3250  O   HIS A 426     3190  10652   5329    922    524   1022       O  
ATOM   3251  CB  HIS A 426     111.086  22.689-110.279  1.00 47.57           C  
ANISOU 3251  CB  HIS A 426     2876  10287   4913    798    677    917       C  
ATOM   3252  CG  HIS A 426     110.486  22.405-111.620  1.00 50.25           C  
ANISOU 3252  CG  HIS A 426     3283  10567   5243    834    749    856       C  
ATOM   3253  ND1 HIS A 426     110.214  21.127-112.057  1.00 50.98           N  
ANISOU 3253  ND1 HIS A 426     3390  10580   5400    991    778    785       N  
ATOM   3254  CD2 HIS A 426     110.079  23.236-112.608  1.00 50.63           C  
ANISOU 3254  CD2 HIS A 426     3386  10623   5226    735    795    852       C  
ATOM   3255  CE1 HIS A 426     109.680  21.181-113.264  1.00 50.21           C  
ANISOU 3255  CE1 HIS A 426     3350  10457   5269    987    835    724       C  
ATOM   3256  NE2 HIS A 426     109.586  22.449-113.621  1.00 53.39           N  
ANISOU 3256  NE2 HIS A 426     3782  10921   5584    838    846    773       N  
ATOM   3257  N   ASN A 427     110.668  24.009-107.071  1.00 46.48           N  
ANISOU 3257  N   ASN A 427     2745  10177   4740    644    489   1043       N  
ATOM   3258  CA  ASN A 427     111.198  24.079-105.710  1.00 47.16           C  
ANISOU 3258  CA  ASN A 427     2758  10350   4809    645    406   1074       C  
ATOM   3259  C   ASN A 427     110.092  24.040-104.663  1.00 56.31           C  
ANISOU 3259  C   ASN A 427     4007  11434   5953    657    351   1113       C  
ATOM   3260  O   ASN A 427     110.192  24.695-103.621  1.00 51.44           O  
ANISOU 3260  O   ASN A 427     3361  10887   5296    579    282   1120       O  
ATOM   3261  CB  ASN A 427     112.043  25.335-105.533  1.00 48.04           C  
ANISOU 3261  CB  ASN A 427     2780  10578   4895    479    385   1051       C  
ATOM   3262  CG  ASN A 427     113.300  25.309-106.367  1.00 55.71           C  
ANISOU 3262  CG  ASN A 427     3637  11650   5881    473    436   1019       C  
ATOM   3263  OD1 ASN A 427     113.415  26.033-107.354  1.00 49.73           O  
ANISOU 3263  OD1 ASN A 427     2880  10892   5123    366    498   1004       O  
ATOM   3264  ND2 ASN A 427     114.256  24.476-105.972  1.00 50.95           N  
ANISOU 3264  ND2 ASN A 427     2932  11138   5290    592    412   1014       N  
ATOM   3265  N   PHE A 428     109.023  23.281-104.915  1.00 52.18           N  
ANISOU 3265  N   PHE A 428     3589  10773   5464    751    382   1125       N  
ATOM   3266  CA  PHE A 428     107.932  23.182-103.954  1.00 49.68           C  
ANISOU 3266  CA  PHE A 428     3355  10384   5136    766    339   1163       C  
ATOM   3267  C   PHE A 428     108.357  22.505-102.653  1.00 51.24           C  
ANISOU 3267  C   PHE A 428     3494  10658   5317    868    275   1235       C  
ATOM   3268  O   PHE A 428     107.722  22.733-101.618  1.00 48.20           O  
ANISOU 3268  O   PHE A 428     3147  10280   4888    843    222   1269       O  
ATOM   3269  CB  PHE A 428     106.747  22.440-104.583  1.00 47.21           C  
ANISOU 3269  CB  PHE A 428     3157   9900   4882    852    398   1150       C  
ATOM   3270  CG  PHE A 428     107.071  21.042-105.046  1.00 44.47           C  
ANISOU 3270  CG  PHE A 428     2784   9496   4616   1029    444   1152       C  
ATOM   3271  CD1 PHE A 428     107.690  20.822-106.270  1.00 43.96           C  
ANISOU 3271  CD1 PHE A 428     2681   9443   4580   1052    502   1086       C  
ATOM   3272  CD2 PHE A 428     106.738  19.946-104.264  1.00 43.57           C  
ANISOU 3272  CD2 PHE A 428     2681   9312   4560   1171    430   1218       C  
ATOM   3273  CE1 PHE A 428     107.984  19.538-106.697  1.00 44.82           C  
ANISOU 3273  CE1 PHE A 428     2758   9491   4782   1210    541   1063       C  
ATOM   3274  CE2 PHE A 428     107.028  18.660-104.686  1.00 50.76           C  
ANISOU 3274  CE2 PHE A 428     3563  10144   5578   1331    473   1213       C  
ATOM   3275  CZ  PHE A 428     107.653  18.455-105.907  1.00 50.40           C  
ANISOU 3275  CZ  PHE A 428     3474  10106   5569   1349    525   1122       C  
ATOM   3276  N   ARG A 429     109.419  21.697-102.671  1.00 51.03           N  
ANISOU 3276  N   ARG A 429     3372  10699   5318    984    277   1257       N  
ATOM   3277  CA  ARG A 429     109.880  21.058-101.442  1.00 51.47           C  
ANISOU 3277  CA  ARG A 429     3369  10837   5351   1090    214   1339       C  
ATOM   3278  C   ARG A 429     110.735  21.989-100.587  1.00 50.46           C  
ANISOU 3278  C   ARG A 429     3148  10892   5132    988    140   1320       C  
ATOM   3279  O   ARG A 429     110.723  21.871 -99.357  1.00 54.19           O  
ANISOU 3279  O   ARG A 429     3605  11444   5543   1024     74   1378       O  
ATOM   3280  CB  ARG A 429     110.664  19.784-101.770  1.00 52.80           C  
ANISOU 3280  CB  ARG A 429     3468  10992   5602   1264    241   1367       C  
ATOM   3281  CG  ARG A 429     109.824  18.692-102.422  1.00 51.58           C  
ANISOU 3281  CG  ARG A 429     3394  10641   5562   1388    308   1376       C  
ATOM   3282  CD  ARG A 429     110.675  17.522-102.900  1.00 50.98           C  
ANISOU 3282  CD  ARG A 429     3237  10540   5592   1544    336   1369       C  
ATOM   3283  NE  ARG A 429     111.354  16.847-101.799  1.00 56.41           N  
ANISOU 3283  NE  ARG A 429     3849  11302   6282   1664    275   1474       N  
ATOM   3284  CZ  ARG A 429     112.159  15.800-101.951  1.00 64.93           C  
ANISOU 3284  CZ  ARG A 429     4845  12366   7460   1812    279   1486       C  
ATOM   3285  NH1 ARG A 429     112.386  15.305-103.162  1.00 61.31           N  
ANISOU 3285  NH1 ARG A 429     4364  11824   7108   1854    344   1383       N  
ATOM   3286  NH2 ARG A 429     112.740  15.248-100.895  1.00 71.37           N  
ANISOU 3286  NH2 ARG A 429     5597  13253   8267   1921    217   1595       N  
ATOM   3287  N   ASN A 430     111.475  22.911-101.203  1.00 52.53           N  
ANISOU 3287  N   ASN A 430     3347  11225   5388    861    152   1238       N  
ATOM   3288  CA  ASN A 430     112.398  23.796-100.486  1.00 53.47           C  
ANISOU 3288  CA  ASN A 430     3360  11507   5448    761     89   1194       C  
ATOM   3289  C   ASN A 430     112.347  25.197-101.088  1.00 50.38           C  
ANISOU 3289  C   ASN A 430     2973  11104   5066    557    110   1110       C  
ATOM   3290  O   ASN A 430     113.329  25.689-101.656  1.00 55.83           O  
ANISOU 3290  O   ASN A 430     3569  11863   5780    487    135   1058       O  
ATOM   3291  CB  ASN A 430     113.823  23.227-100.515  1.00 62.82           C  
ANISOU 3291  CB  ASN A 430     4407  12816   6647    854     81   1190       C  
ATOM   3292  CG  ASN A 430     114.369  23.026-101.939  1.00 72.15           C  
ANISOU 3292  CG  ASN A 430     5554  13962   7899    859    164   1146       C  
ATOM   3293  OD1 ASN A 430     113.621  23.015-102.922  1.00 72.63           O  
ANISOU 3293  OD1 ASN A 430     5704  13895   7995    836    232   1136       O  
ATOM   3294  ND2 ASN A 430     115.685  22.862-102.044  1.00 73.65           N  
ANISOU 3294  ND2 ASN A 430     5608  14275   8101    892    159   1112       N  
ATOM   3295  N   PRO A 431     111.207  25.885-100.964  1.00 47.85           N  
ANISOU 3295  N   PRO A 431     2755  10690   4736    456    103   1096       N  
ATOM   3296  CA  PRO A 431     111.083  27.207-101.602  1.00 49.30           C  
ANISOU 3296  CA  PRO A 431     2949  10832   4951    266    128   1031       C  
ATOM   3297  C   PRO A 431     111.969  28.283-100.988  1.00 50.41           C  
ANISOU 3297  C   PRO A 431     2977  11087   5090    132     77    956       C  
ATOM   3298  O   PRO A 431     112.036  29.388-101.539  1.00 48.70           O  
ANISOU 3298  O   PRO A 431     2747  10830   4926    -28    105    909       O  
ATOM   3299  CB  PRO A 431     109.595  27.544-101.430  1.00 48.62           C  
ANISOU 3299  CB  PRO A 431     2997  10616   4860    215    118   1032       C  
ATOM   3300  CG  PRO A 431     109.155  26.744-100.259  1.00 53.49           C  
ANISOU 3300  CG  PRO A 431     3641  11262   5421    334     62   1079       C  
ATOM   3301  CD  PRO A 431     109.966  25.481-100.280  1.00 54.51           C  
ANISOU 3301  CD  PRO A 431     3707  11453   5550    511     77   1144       C  
ATOM   3302  N   SER A 432     112.666  27.997 -99.890  1.00 49.96           N  
ANISOU 3302  N   SER A 432     2833  11167   4983    194      8    945       N  
ATOM   3303  CA  SER A 432     113.492  29.006 -99.239  1.00 51.34           C  
ANISOU 3303  CA  SER A 432     2893  11451   5161     73    -43    850       C  
ATOM   3304  C   SER A 432     114.735  29.383-100.045  1.00 60.54           C  
ANISOU 3304  C   SER A 432     3936  12675   6392     10      5    810       C  
ATOM   3305  O   SER A 432     115.492  30.251 -99.597  1.00 62.04           O  
ANISOU 3305  O   SER A 432     4016  12945   6610    -97    -28    720       O  
ATOM   3306  CB  SER A 432     113.903  28.511 -97.854  1.00 54.79           C  
ANISOU 3306  CB  SER A 432     3269  12038   5510    176   -129    848       C  
ATOM   3307  OG  SER A 432     114.555  27.259 -97.951  1.00 58.14           O  
ANISOU 3307  OG  SER A 432     3648  12530   5911    355   -117    927       O  
ATOM   3308  N   VAL A 433     114.963  28.768-101.209  1.00 52.61           N  
ANISOU 3308  N   VAL A 433     2941  11633   5415     73     86    862       N  
ATOM   3309  CA  VAL A 433     116.131  29.066-102.034  1.00 60.42           C  
ANISOU 3309  CA  VAL A 433     3814  12686   6458     17    143    829       C  
ATOM   3310  C   VAL A 433     115.837  30.094-103.118  1.00 53.56           C  
ANISOU 3310  C   VAL A 433     2980  11712   5656   -150    222    824       C  
ATOM   3311  O   VAL A 433     116.751  30.481-103.857  1.00 60.66           O  
ANISOU 3311  O   VAL A 433     3785  12658   6604   -220    283    804       O  
ATOM   3312  CB  VAL A 433     116.697  27.780-102.672  1.00 54.57           C  
ANISOU 3312  CB  VAL A 433     3042  11986   5706    188    186    874       C  
ATOM   3313  CG1 VAL A 433     117.009  26.745-101.599  1.00 55.28           C  
ANISOU 3313  CG1 VAL A 433     3093  12167   5742    360    110    900       C  
ATOM   3314  CG2 VAL A 433     115.723  27.220-103.699  1.00 53.00           C  
ANISOU 3314  CG2 VAL A 433     2978  11648   5514    246    257    934       C  
ATOM   3315  N   LEU A 434     114.596  30.553-103.230  1.00 57.04           N  
ANISOU 3315  N   LEU A 434     3551  12018   6104   -214    225    847       N  
ATOM   3316  CA  LEU A 434     114.200  31.469-104.296  1.00 59.01           C  
ANISOU 3316  CA  LEU A 434     3850  12159   6414   -357    302    866       C  
ATOM   3317  C   LEU A 434     114.225  32.929-103.843  1.00 62.93           C  
ANISOU 3317  C   LEU A 434     4301  12615   6994   -555    275    803       C  
ATOM   3318  O   LEU A 434     114.405  33.225-102.659  1.00 72.05           O  
ANISOU 3318  O   LEU A 434     5402  13823   8152   -577    190    727       O  
ATOM   3319  CB  LEU A 434     112.804  31.100-104.807  1.00 49.51           C  
ANISOU 3319  CB  LEU A 434     2811  10820   5179   -305    327    925       C  
ATOM   3320  CG  LEU A 434     112.663  29.684-105.372  1.00 49.00           C  
ANISOU 3320  CG  LEU A 434     2796  10759   5062   -114    364    972       C  
ATOM   3321  CD1 LEU A 434     111.208  29.331-105.639  1.00 47.53           C  
ANISOU 3321  CD1 LEU A 434     2767  10434   4856    -61    374   1005       C  
ATOM   3322  CD2 LEU A 434     113.478  29.553-106.643  1.00 50.05           C  
ANISOU 3322  CD2 LEU A 434     2872  10938   5207   -111    456    985       C  
TER    3323      LEU A 434                                                      
ATOM   3324  N   MET B   1      78.279  56.978-101.765  1.00 99.79           N  
ANISOU 3324  N   MET B   1    11612  12907  13397     92   -865   1615       N  
ATOM   3325  CA  MET B   1      79.166  58.010-102.288  1.00100.15           C  
ANISOU 3325  CA  MET B   1    11665  12821  13565     15   -899   1761       C  
ATOM   3326  C   MET B   1      79.738  57.579-103.641  1.00 92.23           C  
ANISOU 3326  C   MET B   1    10620  11957  12465    -23   -884   1964       C  
ATOM   3327  O   MET B   1      79.332  56.557-104.196  1.00 89.90           O  
ANISOU 3327  O   MET B   1    10293  11844  12019     22   -853   1984       O  
ATOM   3328  CB  MET B   1      80.290  58.306-101.288  1.00104.60           C  
ANISOU 3328  CB  MET B   1    12254  13305  14186    -98   -911   1667       C  
ATOM   3329  CG  MET B   1      80.856  59.726-101.341  1.00110.65           C  
ANISOU 3329  CG  MET B   1    13047  13847  15148   -165   -957   1740       C  
ATOM   3330  SD  MET B   1      79.650  61.012-100.946  1.00116.17           S  
ANISOU 3330  SD  MET B   1    13796  14295  16047    -61   -993   1665       S  
ATOM   3331  CE  MET B   1      79.137  61.548-102.579  1.00115.09           C  
ANISOU 3331  CE  MET B   1    13635  14130  15963      1  -1014   1929       C  
ATOM   3332  N   SER B   2      80.675  58.365-104.166  1.00 88.06           N  
ANISOU 3332  N   SER B   2    10090  11343  12024   -112   -904   2111       N  
ATOM   3333  CA  SER B   2      81.285  58.059-105.451  1.00 78.95           C  
ANISOU 3333  CA  SER B   2     8897  10322  10780   -158   -882   2309       C  
ATOM   3334  C   SER B   2      82.089  56.766-105.378  1.00 69.73           C  
ANISOU 3334  C   SER B   2     7689   9359   9446   -210   -831   2262       C  
ATOM   3335  O   SER B   2      82.596  56.378-104.322  1.00 64.01           O  
ANISOU 3335  O   SER B   2     6969   8638   8713   -251   -825   2117       O  
ATOM   3336  CB  SER B   2      82.191  59.206-105.899  1.00 77.32           C  
ANISOU 3336  CB  SER B   2     8695   9971  10710   -257   -907   2470       C  
ATOM   3337  OG  SER B   2      81.484  60.431-105.942  1.00 77.99           O  
ANISOU 3337  OG  SER B   2     8821   9843  10970   -208   -958   2516       O  
ATOM   3338  N   ILE B   3      82.199  56.097-106.520  1.00 64.66           N  
ANISOU 3338  N   ILE B   3     7008   8890   8668   -205   -795   2386       N  
ATOM   3339  CA  ILE B   3      83.009  54.891-106.623  1.00 62.79           C  
ANISOU 3339  CA  ILE B   3     6729   8845   8285   -249   -742   2360       C  
ATOM   3340  C   ILE B   3      84.467  55.294-106.788  1.00 67.46           C  
ANISOU 3340  C   ILE B   3     7287   9419   8926   -374   -731   2457       C  
ATOM   3341  O   ILE B   3      84.808  56.087-107.673  1.00 74.25           O  
ANISOU 3341  O   ILE B   3     8138  10235   9839   -421   -735   2634       O  
ATOM   3342  CB  ILE B   3      82.542  54.019-107.796  1.00 61.06           C  
ANISOU 3342  CB  ILE B   3     6480   8819   7900   -194   -704   2438       C  
ATOM   3343  CG1 ILE B   3      81.064  53.664-107.637  1.00 61.32           C  
ANISOU 3343  CG1 ILE B   3     6535   8868   7894    -77   -720   2345       C  
ATOM   3344  CG2 ILE B   3      83.393  52.769-107.887  1.00 57.72           C  
ANISOU 3344  CG2 ILE B   3     6013   8578   7339   -233   -644   2399       C  
ATOM   3345  CD1 ILE B   3      80.494  52.902-108.809  1.00 60.65           C  
ANISOU 3345  CD1 ILE B   3     6425   8964   7656    -26   -696   2417       C  
ATOM   3346  N   GLU B   4      85.334  54.747-105.936  1.00 67.59           N  
ANISOU 3346  N   GLU B   4     7282   9472   8927   -431   -719   2348       N  
ATOM   3347  CA  GLU B   4      86.751  55.082-106.017  1.00 69.43           C  
ANISOU 3347  CA  GLU B   4     7469   9699   9214   -553   -710   2428       C  
ATOM   3348  C   GLU B   4      87.465  54.227-107.058  1.00 64.59           C  
ANISOU 3348  C   GLU B   4     6787   9291   8464   -577   -642   2533       C  
ATOM   3349  O   GLU B   4      88.252  54.742-107.859  1.00 68.87           O  
ANISOU 3349  O   GLU B   4     7289   9843   9034   -657   -621   2691       O  
ATOM   3350  CB  GLU B   4      87.412  54.921-104.647  1.00 75.62           C  
ANISOU 3350  CB  GLU B   4     8251  10437  10045   -605   -737   2271       C  
ATOM   3351  CG  GLU B   4      87.017  55.985-103.633  1.00 82.83           C  
ANISOU 3351  CG  GLU B   4     9227  11134  11112   -615   -802   2174       C  
ATOM   3352  CD  GLU B   4      87.791  55.867-102.330  1.00 90.30           C  
ANISOU 3352  CD  GLU B   4    10168  12051  12091   -684   -834   2029       C  
ATOM   3353  OE1 GLU B   4      88.286  54.760-102.023  1.00 88.68           O  
ANISOU 3353  OE1 GLU B   4     9923  11999  11774   -686   -810   1970       O  
ATOM   3354  OE2 GLU B   4      87.909  56.883-101.614  1.00 93.28           O  
ANISOU 3354  OE2 GLU B   4    10582  12252  12609   -737   -886   1973       O  
ATOM   3355  N   LYS B   5      87.200  52.923-107.067  1.00 60.81           N  
ANISOU 3355  N   LYS B   5     6293   8973   7840   -512   -603   2445       N  
ATOM   3356  CA  LYS B   5      87.897  52.014-107.963  1.00 58.75           C  
ANISOU 3356  CA  LYS B   5     5966   8906   7450   -528   -532   2513       C  
ATOM   3357  C   LYS B   5      87.040  50.781-108.214  1.00 54.64           C  
ANISOU 3357  C   LYS B   5     5458   8526   6779   -427   -499   2429       C  
ATOM   3358  O   LYS B   5      86.372  50.282-107.306  1.00 57.08           O  
ANISOU 3358  O   LYS B   5     5803   8807   7078   -369   -522   2281       O  
ATOM   3359  CB  LYS B   5      89.259  51.604-107.385  1.00 58.05           C  
ANISOU 3359  CB  LYS B   5     5812   8863   7381   -605   -514   2470       C  
ATOM   3360  CG  LYS B   5      90.119  50.774-108.330  1.00 62.71           C  
ANISOU 3360  CG  LYS B   5     6322   9645   7861   -626   -433   2544       C  
ATOM   3361  CD  LYS B   5      91.447  50.369-107.692  1.00 63.90           C  
ANISOU 3361  CD  LYS B   5     6396   9837   8048   -692   -423   2497       C  
ATOM   3362  CE  LYS B   5      92.329  51.574-107.389  1.00 67.28           C  
ANISOU 3362  CE  LYS B   5     6795  10140   8627   -811   -461   2573       C  
ATOM   3363  NZ  LYS B   5      93.652  51.171-106.828  1.00 69.18           N  
ANISOU 3363  NZ  LYS B   5     6945  10438   8901   -879   -456   2536       N  
ATOM   3364  N   ILE B   6      87.062  50.304-109.457  1.00 53.10           N  
ANISOU 3364  N   ILE B   6     5232   8482   6463   -412   -444   2524       N  
ATOM   3365  CA  ILE B   6      86.448  49.038-109.842  1.00 51.57           C  
ANISOU 3365  CA  ILE B   6     5037   8439   6117   -333   -404   2448       C  
ATOM   3366  C   ILE B   6      87.516  48.206-110.536  1.00 56.55           C  
ANISOU 3366  C   ILE B   6     5598   9238   6651   -368   -325   2482       C  
ATOM   3367  O   ILE B   6      88.018  48.597-111.597  1.00 63.74           O  
ANISOU 3367  O   ILE B   6     6474  10218   7527   -414   -286   2626       O  
ATOM   3368  CB  ILE B   6      85.238  49.232-110.770  1.00 48.58           C  
ANISOU 3368  CB  ILE B   6     4694   8093   5670   -270   -417   2514       C  
ATOM   3369  CG1 ILE B   6      84.199  50.143-110.121  1.00 50.12           C  
ANISOU 3369  CG1 ILE B   6     4947   8115   5980   -229   -493   2486       C  
ATOM   3370  CG2 ILE B   6      84.625  47.886-111.130  1.00 42.52           C  
ANISOU 3370  CG2 ILE B   6     3924   7482   4750   -200   -379   2419       C  
ATOM   3371  CD1 ILE B   6      83.103  50.573-111.062  1.00 53.67           C  
ANISOU 3371  CD1 ILE B   6     5420   8581   6393   -172   -520   2583       C  
ATOM   3372  N   TRP B   7      87.867  47.070-109.942  1.00 51.13           N  
ANISOU 3372  N   TRP B   7     4888   8615   5922   -344   -298   2354       N  
ATOM   3373  CA  TRP B   7      88.839  46.156-110.525  1.00 47.64           C  
ANISOU 3373  CA  TRP B   7     4374   8329   5396   -358   -220   2361       C  
ATOM   3374  C   TRP B   7      88.189  44.794-110.718  1.00 47.80           C  
ANISOU 3374  C   TRP B   7     4412   8460   5292   -274   -184   2247       C  
ATOM   3375  O   TRP B   7      87.641  44.222-109.770  1.00 47.13           O  
ANISOU 3375  O   TRP B   7     4364   8323   5220   -228   -217   2119       O  
ATOM   3376  CB  TRP B   7      90.089  46.031-109.649  1.00 39.47           C  
ANISOU 3376  CB  TRP B   7     3281   7266   4448   -411   -220   2323       C  
ATOM   3377  CG  TRP B   7      91.164  45.206-110.289  1.00 44.72           C  
ANISOU 3377  CG  TRP B   7     3858   8085   5047   -424   -136   2341       C  
ATOM   3378  CD1 TRP B   7      91.607  43.980-109.887  1.00 47.45           C  
ANISOU 3378  CD1 TRP B   7     4167   8502   5359   -381   -105   2232       C  
ATOM   3379  CD2 TRP B   7      91.917  45.538-111.466  1.00 51.36           C  
ANISOU 3379  CD2 TRP B   7     4635   9032   5850   -478    -66   2476       C  
ATOM   3380  NE1 TRP B   7      92.597  43.533-110.731  1.00 53.43           N  
ANISOU 3380  NE1 TRP B   7     4835   9397   6068   -399    -19   2281       N  
ATOM   3381  CE2 TRP B   7      92.806  44.470-111.709  1.00 56.24           C  
ANISOU 3381  CE2 TRP B   7     5172   9785   6413   -462     10   2428       C  
ATOM   3382  CE3 TRP B   7      91.930  46.637-112.333  1.00 50.35           C  
ANISOU 3382  CE3 TRP B   7     4507   8894   5728   -540    -59   2637       C  
ATOM   3383  CZ2 TRP B   7      93.698  44.468-112.783  1.00 56.21           C  
ANISOU 3383  CZ2 TRP B   7     5084   9918   6356   -505    101   2526       C  
ATOM   3384  CZ3 TRP B   7      92.818  46.633-113.401  1.00 51.41           C  
ANISOU 3384  CZ3 TRP B   7     4564   9167   5802   -591     28   2747       C  
ATOM   3385  CH2 TRP B   7      93.689  45.556-113.615  1.00 53.31           C  
ANISOU 3385  CH2 TRP B   7     4721   9552   5983   -573    111   2685       C  
ATOM   3386  N   ALA B   8      88.248  44.283-111.943  1.00 46.64           N  
ANISOU 3386  N   ALA B   8     4237   8464   5021   -261   -117   2292       N  
ATOM   3387  CA  ALA B   8      87.679  42.988-112.278  1.00 44.00           C  
ANISOU 3387  CA  ALA B   8     3915   8238   4565   -191    -78   2185       C  
ATOM   3388  C   ALA B   8      88.795  41.990-112.555  1.00 37.59           C  
ANISOU 3388  C   ALA B   8     3032   7543   3706   -193      4   2145       C  
ATOM   3389  O   ALA B   8      89.892  42.360-112.977  1.00 41.16           O  
ANISOU 3389  O   ALA B   8     3417   8044   4177   -249     49   2235       O  
ATOM   3390  CB  ALA B   8      86.746  43.089-113.489  1.00 39.23           C  
ANISOU 3390  CB  ALA B   8     3341   7725   3840   -166    -70   2243       C  
ATOM   3391  N   ARG B   9      88.507  40.718-112.301  1.00 39.32           N  
ANISOU 3391  N   ARG B   9     3263   7804   3875   -132     26   2010       N  
ATOM   3392  CA  ARG B   9      89.476  39.655-112.515  1.00 39.14           C  
ANISOU 3392  CA  ARG B   9     3175   7879   3819   -115    104   1953       C  
ATOM   3393  C   ARG B   9      88.729  38.401-112.942  1.00 35.65           C  
ANISOU 3393  C   ARG B   9     2766   7513   3267    -47    139   1836       C  
ATOM   3394  O   ARG B   9      87.498  38.365-112.970  1.00 37.30           O  
ANISOU 3394  O   ARG B   9     3041   7698   3432    -19     98   1799       O  
ATOM   3395  CB  ARG B   9      90.311  39.386-111.257  1.00 38.07           C  
ANISOU 3395  CB  ARG B   9     3006   7660   3801   -120     77   1901       C  
ATOM   3396  CG  ARG B   9      89.572  38.594-110.179  1.00 39.48           C  
ANISOU 3396  CG  ARG B   9     3244   7756   4000    -65     29   1772       C  
ATOM   3397  CD  ARG B   9      90.474  38.287-108.986  1.00 44.00           C  
ANISOU 3397  CD  ARG B   9     3780   8265   4674    -71      0   1733       C  
ATOM   3398  NE  ARG B   9      91.042  39.504-108.416  1.00 42.96           N  
ANISOU 3398  NE  ARG B   9     3627   8054   4642   -142    -55   1813       N  
ATOM   3399  CZ  ARG B   9      90.402  40.289-107.556  1.00 41.93           C  
ANISOU 3399  CZ  ARG B   9     3559   7803   4568   -164   -134   1807       C  
ATOM   3400  NH1 ARG B   9      89.174  39.981-107.159  1.00 41.21           N  
ANISOU 3400  NH1 ARG B   9     3549   7666   4442   -118   -164   1729       N  
ATOM   3401  NH2 ARG B   9      90.985  41.384-107.096  1.00 38.37           N  
ANISOU 3401  NH2 ARG B   9     3087   7279   4214   -234   -181   1871       N  
ATOM   3402  N   GLU B  10      89.494  37.362-113.245  1.00 38.67           N  
ANISOU 3402  N   GLU B  10     3096   7982   3615    -19    215   1772       N  
ATOM   3403  CA  GLU B  10      88.978  36.083-113.705  1.00 38.63           C  
ANISOU 3403  CA  GLU B  10     3114   8049   3516     41    260   1650       C  
ATOM   3404  C   GLU B  10      89.232  35.028-112.633  1.00 49.94           C  
ANISOU 3404  C   GLU B  10     4546   9403   5025     87    251   1535       C  
ATOM   3405  O   GLU B  10      90.375  34.836-112.209  1.00 60.20           O  
ANISOU 3405  O   GLU B  10     5779  10694   6401     87    273   1541       O  
ATOM   3406  CB  GLU B  10      89.642  35.715-115.031  1.00 43.84           C  
ANISOU 3406  CB  GLU B  10     3716   8874   4068     40    365   1663       C  
ATOM   3407  CG  GLU B  10      89.430  34.310-115.537  1.00 46.93           C  
ANISOU 3407  CG  GLU B  10     4116   9342   4374     99    429   1521       C  
ATOM   3408  CD  GLU B  10      90.259  34.045-116.781  1.00 44.29           C  
ANISOU 3408  CD  GLU B  10     3714   9174   3940     95    542   1532       C  
ATOM   3409  OE1 GLU B  10      89.693  33.611-117.801  1.00 42.21           O  
ANISOU 3409  OE1 GLU B  10     3478   9024   3535    107    583   1481       O  
ATOM   3410  OE2 GLU B  10      91.480  34.291-116.738  1.00 43.22           O  
ANISOU 3410  OE2 GLU B  10     3493   9065   3865     76    590   1589       O  
ATOM   3411  N   ILE B  11      88.168  34.362-112.185  1.00 43.95           N  
ANISOU 3411  N   ILE B  11     3858   8590   4251    124    215   1437       N  
ATOM   3412  CA  ILE B  11      88.262  33.279-111.212  1.00 43.50           C  
ANISOU 3412  CA  ILE B  11     3814   8458   4256    168    205   1334       C  
ATOM   3413  C   ILE B  11      87.648  32.030-111.835  1.00 43.23           C  
ANISOU 3413  C   ILE B  11     3810   8477   4138    215    254   1216       C  
ATOM   3414  O   ILE B  11      87.039  32.079-112.902  1.00 45.84           O  
ANISOU 3414  O   ILE B  11     4158   8900   4360    209    281   1210       O  
ATOM   3415  CB  ILE B  11      87.563  33.619-109.881  1.00 46.03           C  
ANISOU 3415  CB  ILE B  11     4195   8646   4649    158    114   1324       C  
ATOM   3416  CG1 ILE B  11      86.058  33.762-110.109  1.00 46.69           C  
ANISOU 3416  CG1 ILE B  11     4350   8722   4668    160     82   1293       C  
ATOM   3417  CG2 ILE B  11      88.153  34.884-109.261  1.00 45.55           C  
ANISOU 3417  CG2 ILE B  11     4109   8525   4672    107     63   1425       C  
ATOM   3418  CD1 ILE B  11      85.323  34.379-108.948  1.00 50.67           C  
ANISOU 3418  CD1 ILE B  11     4906   9111   5235    145      2   1296       C  
ATOM   3419  N   LEU B  12      87.819  30.901-111.152  1.00 39.92           N  
ANISOU 3419  N   LEU B  12     3399   7997   3771    258    260   1125       N  
ATOM   3420  CA  LEU B  12      87.234  29.635-111.579  1.00 38.68           C  
ANISOU 3420  CA  LEU B  12     3278   7860   3560    299    301   1001       C  
ATOM   3421  C   LEU B  12      85.919  29.384-110.850  1.00 43.72           C  
ANISOU 3421  C   LEU B  12     3998   8411   4204    294    237    949       C  
ATOM   3422  O   LEU B  12      85.820  29.607-109.640  1.00 34.52           O  
ANISOU 3422  O   LEU B  12     2856   7143   3117    286    177    971       O  
ATOM   3423  CB  LEU B  12      88.201  28.479-111.326  1.00 33.57           C  
ANISOU 3423  CB  LEU B  12     2589   7188   2978    353    351    934       C  
ATOM   3424  CG  LEU B  12      89.484  28.532-112.153  1.00 37.63           C  
ANISOU 3424  CG  LEU B  12     3009   7805   3483    368    433    963       C  
ATOM   3425  CD1 LEU B  12      90.285  27.251-111.972  1.00 35.25           C  
ANISOU 3425  CD1 LEU B  12     2668   7475   3252    438    485    876       C  
ATOM   3426  CD2 LEU B  12      89.162  28.804-113.628  1.00 35.48           C  
ANISOU 3426  CD2 LEU B  12     2734   7677   3071    347    494    959       C  
ATOM   3427  N   ASP B  13      84.909  28.916-111.592  1.00 35.57           N  
ANISOU 3427  N   ASP B  13     3005   7429   3081    295    252    875       N  
ATOM   3428  CA  ASP B  13      83.623  28.590-110.999  1.00 31.59           C  
ANISOU 3428  CA  ASP B  13     2567   6855   2580    287    202    817       C  
ATOM   3429  C   ASP B  13      83.635  27.142-110.512  1.00 31.70           C  
ANISOU 3429  C   ASP B  13     2607   6798   2640    320    226    709       C  
ATOM   3430  O   ASP B  13      84.667  26.464-110.532  1.00 32.04           O  
ANISOU 3430  O   ASP B  13     2616   6832   2726    357    273    686       O  
ATOM   3431  CB  ASP B  13      82.475  28.890-111.973  1.00 35.01           C  
ANISOU 3431  CB  ASP B  13     3023   7376   2903    265    191    801       C  
ATOM   3432  CG  ASP B  13      82.385  27.910-113.145  1.00 36.12           C  
ANISOU 3432  CG  ASP B  13     3161   7613   2949    279    254    700       C  
ATOM   3433  OD1 ASP B  13      82.980  26.815-113.127  1.00 33.01           O  
ANISOU 3433  OD1 ASP B  13     2762   7195   2586    311    308    616       O  
ATOM   3434  OD2 ASP B  13      81.667  28.241-114.108  1.00 46.04           O  
ANISOU 3434  OD2 ASP B  13     4424   8971   4099    259    247    701       O  
ATOM   3435  N   SER B  14      82.466  26.647-110.093  1.00 31.08           N  
ANISOU 3435  N   SER B  14     2585   6667   2558    306    195    645       N  
ATOM   3436  CA  SER B  14      82.384  25.354-109.420  1.00 31.02           C  
ANISOU 3436  CA  SER B  14     2612   6564   2611    326    206    562       C  
ATOM   3437  C   SER B  14      82.644  24.179-110.350  1.00 40.81           C  
ANISOU 3437  C   SER B  14     3846   7838   3823    357    276    455       C  
ATOM   3438  O   SER B  14      82.840  23.059-109.867  1.00 41.59           O  
ANISOU 3438  O   SER B  14     3966   7846   3990    383    294    392       O  
ATOM   3439  CB  SER B  14      81.011  25.188-108.775  1.00 38.67           C  
ANISOU 3439  CB  SER B  14     3637   7476   3578    292    161    526       C  
ATOM   3440  OG  SER B  14      79.986  25.113-109.753  1.00 42.47           O  
ANISOU 3440  OG  SER B  14     4129   8037   3971    269    167    465       O  
ATOM   3441  N   ARG B  15      82.635  24.396-111.660  1.00 32.61           N  
ANISOU 3441  N   ARG B  15     2782   6924   2683    353    316    430       N  
ATOM   3442  CA  ARG B  15      82.975  23.354-112.614  1.00 41.77           C  
ANISOU 3442  CA  ARG B  15     3934   8131   3807    383    391    317       C  
ATOM   3443  C   ARG B  15      84.412  23.462-113.101  1.00 39.70           C  
ANISOU 3443  C   ARG B  15     3603   7927   3555    425    456    347       C  
ATOM   3444  O   ARG B  15      84.878  22.577-113.825  1.00 39.08           O  
ANISOU 3444  O   ARG B  15     3508   7881   3459    461    530    247       O  
ATOM   3445  CB  ARG B  15      82.012  23.394-113.808  1.00 41.38           C  
ANISOU 3445  CB  ARG B  15     3902   8200   3622    348    397    251       C  
ATOM   3446  CG  ARG B  15      80.640  22.798-113.518  1.00 43.06           C  
ANISOU 3446  CG  ARG B  15     4171   8357   3831    313    355    170       C  
ATOM   3447  CD  ARG B  15      79.743  22.783-114.755  1.00 47.82           C  
ANISOU 3447  CD  ARG B  15     4782   9091   4296    278    355     99       C  
ATOM   3448  NE  ARG B  15      79.439  24.129-115.231  1.00 55.86           N  
ANISOU 3448  NE  ARG B  15     5776  10221   5229    254    313    211       N  
ATOM   3449  CZ  ARG B  15      78.428  24.423-116.044  1.00 59.62           C  
ANISOU 3449  CZ  ARG B  15     6257  10804   5592    218    278    192       C  
ATOM   3450  NH1 ARG B  15      78.224  25.674-116.428  1.00 55.83           N  
ANISOU 3450  NH1 ARG B  15     5754  10411   5048    205    236    312       N  
ATOM   3451  NH2 ARG B  15      77.613  23.466-116.463  1.00 59.80           N  
ANISOU 3451  NH2 ARG B  15     6307  10843   5573    194    279     57       N  
ATOM   3452  N   GLY B  16      85.126  24.510-112.702  1.00 34.04           N  
ANISOU 3452  N   GLY B  16     2842   7222   2871    419    433    475       N  
ATOM   3453  CA  GLY B  16      86.479  24.741-113.144  1.00 34.81           C  
ANISOU 3453  CA  GLY B  16     2860   7385   2980    448    494    517       C  
ATOM   3454  C   GLY B  16      86.621  25.686-114.312  1.00 39.87           C  
ANISOU 3454  C   GLY B  16     3465   8182   3502    416    527    577       C  
ATOM   3455  O   GLY B  16      87.700  25.740-114.911  1.00 47.43           O  
ANISOU 3455  O   GLY B  16     4352   9220   4448    436    598    593       O  
ATOM   3456  N   ASN B  17      85.576  26.424-114.656  1.00 39.12           N  
ANISOU 3456  N   ASN B  17     3409   8135   3320    367    478    615       N  
ATOM   3457  CA  ASN B  17      85.596  27.310-115.804  1.00 43.15           C  
ANISOU 3457  CA  ASN B  17     3895   8795   3707    334    501    683       C  
ATOM   3458  C   ASN B  17      85.685  28.763-115.362  1.00 35.22           C  
ANISOU 3458  C   ASN B  17     2874   7770   2736    295    440    844       C  
ATOM   3459  O   ASN B  17      85.105  29.137-114.339  1.00 35.65           O  
ANISOU 3459  O   ASN B  17     2966   7714   2867    283    362    877       O  
ATOM   3460  CB  ASN B  17      84.346  27.115-116.669  1.00 43.13           C  
ANISOU 3460  CB  ASN B  17     3942   8873   3573    310    485    616       C  
ATOM   3461  CG  ASN B  17      84.249  25.718-117.239  1.00 40.81           C  
ANISOU 3461  CG  ASN B  17     3665   8605   3236    339    548    444       C  
ATOM   3462  OD1 ASN B  17      83.235  25.042-117.087  1.00 48.37           O  
ANISOU 3462  OD1 ASN B  17     4676   9516   4187    332    515    348       O  
ATOM   3463  ND2 ASN B  17      85.311  25.273-117.889  1.00 37.88           N  
ANISOU 3463  ND2 ASN B  17     3245   8307   2841    371    644    400       N  
ATOM   3464  N   PRO B  18      86.404  29.596-116.106  1.00 37.53           N  
ANISOU 3464  N   PRO B  18     3115   8167   2977    271    477    944       N  
ATOM   3465  CA  PRO B  18      86.561  30.994-115.697  1.00 35.66           C  
ANISOU 3465  CA  PRO B  18     2864   7896   2789    229    420   1099       C  
ATOM   3466  C   PRO B  18      85.242  31.750-115.684  1.00 37.19           C  
ANISOU 3466  C   PRO B  18     3116   8070   2943    201    336   1145       C  
ATOM   3467  O   PRO B  18      84.318  31.459-116.448  1.00 36.06           O  
ANISOU 3467  O   PRO B  18     3007   8004   2692    200    332   1094       O  
ATOM   3468  CB  PRO B  18      87.528  31.567-116.742  1.00 36.92           C  
ANISOU 3468  CB  PRO B  18     2956   8192   2878    204    493   1187       C  
ATOM   3469  CG  PRO B  18      87.592  30.556-117.832  1.00 42.12           C  
ANISOU 3469  CG  PRO B  18     3607   8979   3417    231    582   1073       C  
ATOM   3470  CD  PRO B  18      87.292  29.238-117.222  1.00 37.34           C  
ANISOU 3470  CD  PRO B  18     3035   8282   2871    283    582    917       C  
ATOM   3471  N   THR B  19      85.161  32.724-114.780  1.00 34.46           N  
ANISOU 3471  N   THR B  19     2779   7620   2694    179    266   1236       N  
ATOM   3472  CA  THR B  19      84.024  33.629-114.712  1.00 34.12           C  
ANISOU 3472  CA  THR B  19     2779   7547   2638    159    187   1296       C  
ATOM   3473  C   THR B  19      84.483  34.939-114.085  1.00 42.69           C  
ANISOU 3473  C   THR B  19     3850   8549   3823    127    141   1426       C  
ATOM   3474  O   THR B  19      85.608  35.055-113.590  1.00 36.93           O  
ANISOU 3474  O   THR B  19     3078   7781   3173    116    162   1457       O  
ATOM   3475  CB  THR B  19      82.857  33.023-113.927  1.00 37.62           C  
ANISOU 3475  CB  THR B  19     3277   7905   3111    181    135   1194       C  
ATOM   3476  OG1 THR B  19      81.720  33.888-114.032  1.00 40.44           O  
ANISOU 3476  OG1 THR B  19     3662   8255   3449    169     66   1247       O  
ATOM   3477  CG2 THR B  19      83.222  32.848-112.458  1.00 33.40           C  
ANISOU 3477  CG2 THR B  19     2751   7230   2709    190    110   1168       C  
ATOM   3478  N   VAL B  20      83.594  35.925-114.109  1.00 39.58           N  
ANISOU 3478  N   VAL B  20     3486   8124   3430    112     74   1498       N  
ATOM   3479  CA  VAL B  20      83.947  37.288-113.728  1.00 39.29           C  
ANISOU 3479  CA  VAL B  20     3440   8010   3481     77     31   1626       C  
ATOM   3480  C   VAL B  20      83.851  37.455-112.218  1.00 44.23           C  
ANISOU 3480  C   VAL B  20     4088   8480   4237     82    -23   1585       C  
ATOM   3481  O   VAL B  20      82.924  36.950-111.577  1.00 46.26           O  
ANISOU 3481  O   VAL B  20     4386   8685   4504    110    -55   1492       O  
ATOM   3482  CB  VAL B  20      83.039  38.296-114.453  1.00 37.84           C  
ANISOU 3482  CB  VAL B  20     3277   7852   3249     68    -18   1727       C  
ATOM   3483  CG1 VAL B  20      83.245  39.698-113.901  1.00 38.63           C  
ANISOU 3483  CG1 VAL B  20     3379   7833   3466     37    -73   1844       C  
ATOM   3484  CG2 VAL B  20      83.292  38.260-115.958  1.00 35.88           C  
ANISOU 3484  CG2 VAL B  20     3004   7771   2859     52     34   1792       C  
ATOM   3485  N   GLU B  21      84.824  38.167-111.645  1.00 45.62           N  
ANISOU 3485  N   GLU B  21     4236   8587   4509     47    -33   1652       N  
ATOM   3486  CA  GLU B  21      84.762  38.669-110.278  1.00 40.81           C  
ANISOU 3486  CA  GLU B  21     3652   7836   4018     37    -95   1636       C  
ATOM   3487  C   GLU B  21      85.076  40.158-110.300  1.00 40.74           C  
ANISOU 3487  C   GLU B  21     3634   7763   4082    -10   -133   1761       C  
ATOM   3488  O   GLU B  21      85.957  40.600-111.044  1.00 46.25           O  
ANISOU 3488  O   GLU B  21     4285   8518   4770    -49    -98   1861       O  
ATOM   3489  CB  GLU B  21      85.746  37.941-109.355  1.00 36.97           C  
ANISOU 3489  CB  GLU B  21     3140   7316   3590     37    -80   1575       C  
ATOM   3490  CG  GLU B  21      85.569  38.289-107.883  1.00 42.91           C  
ANISOU 3490  CG  GLU B  21     3928   7938   4439     28   -146   1536       C  
ATOM   3491  CD  GLU B  21      86.488  37.497-106.975  1.00 46.44           C  
ANISOU 3491  CD  GLU B  21     4350   8363   4931     31   -141   1483       C  
ATOM   3492  OE1 GLU B  21      87.697  37.818-106.910  1.00 40.29           O  
ANISOU 3492  OE1 GLU B  21     3513   7590   4204     -2   -135   1539       O  
ATOM   3493  OE2 GLU B  21      86.000  36.545-106.331  1.00 54.57           O  
ANISOU 3493  OE2 GLU B  21     5416   9372   5946     66   -146   1391       O  
ATOM   3494  N   VAL B  22      84.357  40.932-109.488  1.00 37.51           N  
ANISOU 3494  N   VAL B  22     3268   7234   3749    -10   -200   1755       N  
ATOM   3495  CA  VAL B  22      84.461  42.387-109.499  1.00 41.94           C  
ANISOU 3495  CA  VAL B  22     3833   7710   4393    -49   -244   1865       C  
ATOM   3496  C   VAL B  22      84.724  42.879-108.082  1.00 43.31           C  
ANISOU 3496  C   VAL B  22     4025   7744   4687    -73   -294   1818       C  
ATOM   3497  O   VAL B  22      83.989  42.527-107.153  1.00 43.90           O  
ANISOU 3497  O   VAL B  22     4140   7764   4775    -40   -322   1713       O  
ATOM   3498  CB  VAL B  22      83.187  43.043-110.069  1.00 45.35           C  
ANISOU 3498  CB  VAL B  22     4300   8128   4802    -18   -281   1910       C  
ATOM   3499  CG1 VAL B  22      83.236  44.551-109.883  1.00 42.79           C  
ANISOU 3499  CG1 VAL B  22     3988   7679   4593    -52   -334   2012       C  
ATOM   3500  CG2 VAL B  22      83.016  42.690-111.544  1.00 49.05           C  
ANISOU 3500  CG2 VAL B  22     4749   8748   5140     -8   -240   1973       C  
ATOM   3501  N   ASP B  23      85.770  43.687-107.918  1.00 41.01           N  
ANISOU 3501  N   ASP B  23     3702   7402   4478   -135   -304   1895       N  
ATOM   3502  CA  ASP B  23      86.062  44.364-106.659  1.00 38.70           C  
ANISOU 3502  CA  ASP B  23     3428   6976   4302   -171   -361   1859       C  
ATOM   3503  C   ASP B  23      85.744  45.843-106.829  1.00 42.94           C  
ANISOU 3503  C   ASP B  23     3988   7400   4928   -200   -405   1948       C  
ATOM   3504  O   ASP B  23      86.373  46.525-107.645  1.00 46.05           O  
ANISOU 3504  O   ASP B  23     4347   7806   5343   -249   -391   2077       O  
ATOM   3505  CB  ASP B  23      87.524  44.182-106.245  1.00 39.77           C  
ANISOU 3505  CB  ASP B  23     3503   7126   4480   -227   -350   1869       C  
ATOM   3506  CG  ASP B  23      87.849  42.758-105.828  1.00 44.34           C  
ANISOU 3506  CG  ASP B  23     4063   7784   5000   -191   -320   1774       C  
ATOM   3507  OD1 ASP B  23      86.911  41.958-105.630  1.00 49.88           O  
ANISOU 3507  OD1 ASP B  23     4809   8503   5639   -131   -315   1688       O  
ATOM   3508  OD2 ASP B  23      89.052  42.446-105.684  1.00 49.20           O  
ANISOU 3508  OD2 ASP B  23     4614   8438   5640   -222   -304   1790       O  
ATOM   3509  N   LEU B  24      84.772  46.335-106.071  1.00 42.92           N  
ANISOU 3509  N   LEU B  24     4042   7288   4979   -170   -455   1881       N  
ATOM   3510  CA  LEU B  24      84.400  47.742-106.102  1.00 45.36           C  
ANISOU 3510  CA  LEU B  24     4379   7463   5394   -186   -502   1949       C  
ATOM   3511  C   LEU B  24      84.797  48.387-104.782  1.00 45.81           C  
ANISOU 3511  C   LEU B  24     4458   7382   5566   -230   -550   1875       C  
ATOM   3512  O   LEU B  24      84.504  47.846-103.711  1.00 43.29           O  
ANISOU 3512  O   LEU B  24     4165   7049   5232   -208   -563   1742       O  
ATOM   3513  CB  LEU B  24      82.900  47.915-106.357  1.00 44.76           C  
ANISOU 3513  CB  LEU B  24     4343   7365   5299   -107   -521   1929       C  
ATOM   3514  CG  LEU B  24      82.463  49.355-106.643  1.00 43.01           C  
ANISOU 3514  CG  LEU B  24     4143   7010   5187   -108   -568   2023       C  
ATOM   3515  CD1 LEU B  24      81.433  49.385-107.758  1.00 50.26           C  
ANISOU 3515  CD1 LEU B  24     5063   7992   6043    -44   -569   2101       C  
ATOM   3516  CD2 LEU B  24      81.920  50.032-105.390  1.00 38.66           C  
ANISOU 3516  CD2 LEU B  24     3639   6299   4752    -91   -615   1913       C  
ATOM   3517  N   TYR B  25      85.461  49.535-104.859  1.00 46.01           N  
ANISOU 3517  N   TYR B  25     4474   7306   5701   -299   -578   1963       N  
ATOM   3518  CA  TYR B  25      85.943  50.248-103.687  1.00 47.90           C  
ANISOU 3518  CA  TYR B  25     4733   7412   6056   -357   -628   1895       C  
ATOM   3519  C   TYR B  25      85.183  51.557-103.529  1.00 50.36           C  
ANISOU 3519  C   TYR B  25     5096   7550   6488   -345   -675   1906       C  
ATOM   3520  O   TYR B  25      85.029  52.311-104.497  1.00 54.77           O  
ANISOU 3520  O   TYR B  25     5651   8069   7089   -348   -676   2041       O  
ATOM   3521  CB  TYR B  25      87.444  50.530-103.797  1.00 51.40           C  
ANISOU 3521  CB  TYR B  25     5115   7864   6550   -460   -627   1974       C  
ATOM   3522  CG  TYR B  25      88.327  49.303-103.718  1.00 50.17           C  
ANISOU 3522  CG  TYR B  25     4900   7858   6305   -470   -589   1945       C  
ATOM   3523  CD1 TYR B  25      88.628  48.564-104.854  1.00 51.27           C  
ANISOU 3523  CD1 TYR B  25     4987   8144   6348   -452   -523   2028       C  
ATOM   3524  CD2 TYR B  25      88.870  48.892-102.507  1.00 53.40           C  
ANISOU 3524  CD2 TYR B  25     5304   8260   6726   -495   -621   1835       C  
ATOM   3525  CE1 TYR B  25      89.438  47.444-104.786  1.00 50.71           C  
ANISOU 3525  CE1 TYR B  25     4858   8198   6211   -451   -486   1996       C  
ATOM   3526  CE2 TYR B  25      89.682  47.774-102.428  1.00 51.59           C  
ANISOU 3526  CE2 TYR B  25     5016   8157   6428   -495   -593   1817       C  
ATOM   3527  CZ  TYR B  25      89.963  47.055-103.569  1.00 49.65           C  
ANISOU 3527  CZ  TYR B  25     4716   8045   6104   -470   -523   1895       C  
ATOM   3528  OH  TYR B  25      90.769  45.943-103.490  1.00 49.26           O  
ANISOU 3528  OH  TYR B  25     4606   8110   6001   -460   -492   1871       O  
ATOM   3529  N   THR B  26      84.708  51.820-102.314  1.00 49.63           N  
ANISOU 3529  N   THR B  26     5053   7357   6449   -329   -712   1764       N  
ATOM   3530  CA  THR B  26      84.192  53.137-101.966  1.00 57.86           C  
ANISOU 3530  CA  THR B  26     6141   8210   7631   -328   -757   1750       C  
ATOM   3531  C   THR B  26      84.924  53.620-100.721  1.00 64.61           C  
ANISOU 3531  C   THR B  26     7015   8964   8570   -406   -800   1644       C  
ATOM   3532  O   THR B  26      85.875  52.973-100.271  1.00 62.62           O  
ANISOU 3532  O   THR B  26     6730   8796   8266   -463   -798   1612       O  
ATOM   3533  CB  THR B  26      82.681  53.100-101.734  1.00 64.47           C  
ANISOU 3533  CB  THR B  26     7022   9019   8456   -219   -757   1662       C  
ATOM   3534  OG1 THR B  26      82.226  54.416-101.392  1.00 72.56           O  
ANISOU 3534  OG1 THR B  26     8087   9849   9634   -211   -799   1643       O  
ATOM   3535  CG2 THR B  26      82.356  52.161-100.592  1.00 58.76           C  
ANISOU 3535  CG2 THR B  26     6318   8361   7647   -192   -745   1489       C  
ATOM   3536  N   ALA B  27      84.489  54.744-100.149  1.00 68.28           N  
ANISOU 3536  N   ALA B  27     7530   9249   9165   -407   -841   1585       N  
ATOM   3537  CA  ALA B  27      85.086  55.199 -98.898  1.00 73.08           C  
ANISOU 3537  CA  ALA B  27     8163   9763   9842   -481   -885   1460       C  
ATOM   3538  C   ALA B  27      84.847  54.219 -97.757  1.00 71.89           C  
ANISOU 3538  C   ALA B  27     8032   9708   9575   -454   -879   1292       C  
ATOM   3539  O   ALA B  27      85.557  54.276 -96.747  1.00 74.44           O  
ANISOU 3539  O   ALA B  27     8363  10013   9907   -525   -916   1197       O  
ATOM   3540  CB  ALA B  27      84.549  56.581 -98.518  1.00 75.94           C  
ANISOU 3540  CB  ALA B  27     8581   9905  10368   -476   -925   1410       C  
ATOM   3541  N   LYS B  28      83.873  53.321 -97.896  1.00 67.85           N  
ANISOU 3541  N   LYS B  28     7527   9300   8953   -358   -837   1257       N  
ATOM   3542  CA  LYS B  28      83.578  52.318 -96.882  1.00 60.24           C  
ANISOU 3542  CA  LYS B  28     6582   8433   7871   -332   -824   1117       C  
ATOM   3543  C   LYS B  28      84.274  50.985 -97.132  1.00 54.87           C  
ANISOU 3543  C   LYS B  28     5856   7928   7065   -346   -798   1164       C  
ATOM   3544  O   LYS B  28      84.039  50.035 -96.380  1.00 55.98           O  
ANISOU 3544  O   LYS B  28     6011   8155   7103   -323   -786   1069       O  
ATOM   3545  CB  LYS B  28      82.066  52.092 -96.782  1.00 59.47           C  
ANISOU 3545  CB  LYS B  28     6518   8342   7735   -225   -791   1039       C  
ATOM   3546  CG  LYS B  28      81.310  53.229 -96.120  1.00 62.50           C  
ANISOU 3546  CG  LYS B  28     6953   8563   8233   -198   -812    934       C  
ATOM   3547  CD  LYS B  28      79.981  52.746 -95.561  1.00 66.45           C  
ANISOU 3547  CD  LYS B  28     7477   9105   8665   -108   -774    808       C  
ATOM   3548  CE  LYS B  28      79.214  53.876 -94.894  1.00 68.77           C  
ANISOU 3548  CE  LYS B  28     7815   9239   9076    -71   -786    690       C  
ATOM   3549  NZ  LYS B  28      79.993  54.495 -93.786  1.00 71.17           N  
ANISOU 3549  NZ  LYS B  28     8160   9454   9428   -157   -826    580       N  
ATOM   3550  N   GLY B  29      85.107  50.881 -98.164  1.00 52.81           N  
ANISOU 3550  N   GLY B  29     5536   7719   6809   -382   -785   1307       N  
ATOM   3551  CA  GLY B  29      85.913  49.687 -98.333  1.00 53.26           C  
ANISOU 3551  CA  GLY B  29     5542   7927   6766   -397   -761   1340       C  
ATOM   3552  C   GLY B  29      85.666  48.894 -99.600  1.00 48.56           C  
ANISOU 3552  C   GLY B  29     4909   7450   6090   -342   -702   1439       C  
ATOM   3553  O   GLY B  29      85.156  49.425-100.590  1.00 47.31           O  
ANISOU 3553  O   GLY B  29     4750   7265   5960   -314   -686   1527       O  
ATOM   3554  N   LEU B  30      86.032  47.613 -99.571  1.00 47.05           N  
ANISOU 3554  N   LEU B  30     4689   7391   5798   -326   -673   1424       N  
ATOM   3555  CA  LEU B  30      85.931  46.733-100.727  1.00 49.93           C  
ANISOU 3555  CA  LEU B  30     5016   7878   6078   -281   -614   1497       C  
ATOM   3556  C   LEU B  30      84.607  45.981-100.714  1.00 50.20           C  
ANISOU 3556  C   LEU B  30     5091   7955   6028   -196   -586   1425       C  
ATOM   3557  O   LEU B  30      84.113  45.586 -99.654  1.00 53.75           O  
ANISOU 3557  O   LEU B  30     5582   8391   6451   -178   -599   1312       O  
ATOM   3558  CB  LEU B  30      87.098  45.739-100.745  1.00 52.13           C  
ANISOU 3558  CB  LEU B  30     5233   8265   6307   -306   -594   1517       C  
ATOM   3559  CG  LEU B  30      87.048  44.533-101.691  1.00 57.89           C  
ANISOU 3559  CG  LEU B  30     5930   9131   6937   -253   -529   1549       C  
ATOM   3560  CD1 LEU B  30      88.423  44.239-102.245  1.00 66.35           C  
ANISOU 3560  CD1 LEU B  30     6917  10280   8014   -295   -502   1629       C  
ATOM   3561  CD2 LEU B  30      86.516  43.296-100.987  1.00 55.88           C  
ANISOU 3561  CD2 LEU B  30     5707   8924   6602   -200   -519   1443       C  
ATOM   3562  N   PHE B  31      84.040  45.779-101.905  1.00 45.44           N  
ANISOU 3562  N   PHE B  31     4474   7411   5379   -152   -549   1493       N  
ATOM   3563  CA  PHE B  31      82.819  44.997-102.072  1.00 46.35           C  
ANISOU 3563  CA  PHE B  31     4614   7584   5413    -79   -521   1433       C  
ATOM   3564  C   PHE B  31      82.990  44.092-103.281  1.00 48.33           C  
ANISOU 3564  C   PHE B  31     4824   7966   5572    -58   -470   1496       C  
ATOM   3565  O   PHE B  31      83.191  44.574-104.400  1.00 47.57           O  
ANISOU 3565  O   PHE B  31     4700   7897   5477    -67   -458   1606       O  
ATOM   3566  CB  PHE B  31      81.597  45.908-102.220  1.00 39.81           C  
ANISOU 3566  CB  PHE B  31     3817   6676   4633    -36   -542   1430       C  
ATOM   3567  CG  PHE B  31      81.398  46.816-101.046  1.00 45.42           C  
ANISOU 3567  CG  PHE B  31     4568   7253   5437    -51   -584   1352       C  
ATOM   3568  CD1 PHE B  31      80.647  46.408 -99.959  1.00 50.29           C  
ANISOU 3568  CD1 PHE B  31     5223   7860   6026    -23   -583   1218       C  
ATOM   3569  CD2 PHE B  31      81.997  48.063-101.009  1.00 45.61           C  
ANISOU 3569  CD2 PHE B  31     4594   7161   5574   -101   -622   1407       C  
ATOM   3570  CE1 PHE B  31      80.479  47.236 -98.865  1.00 50.65           C  
ANISOU 3570  CE1 PHE B  31     5308   7792   6146    -38   -615   1131       C  
ATOM   3571  CE2 PHE B  31      81.833  48.892 -99.917  1.00 46.69           C  
ANISOU 3571  CE2 PHE B  31     4772   7171   5797   -117   -660   1317       C  
ATOM   3572  CZ  PHE B  31      81.073  48.481 -98.847  1.00 47.72           C  
ANISOU 3572  CZ  PHE B  31     4940   7302   5889    -83   -655   1174       C  
ATOM   3573  N   ARG B  32      82.918  42.785-103.049  1.00 47.50           N  
ANISOU 3573  N   ARG B  32     4718   7941   5386    -32   -439   1426       N  
ATOM   3574  CA  ARG B  32      83.279  41.777-104.032  1.00 43.68           C  
ANISOU 3574  CA  ARG B  32     4197   7579   4820    -17   -387   1458       C  
ATOM   3575  C   ARG B  32      82.050  40.981-104.444  1.00 36.97           C  
ANISOU 3575  C   ARG B  32     3369   6789   3888     39   -362   1402       C  
ATOM   3576  O   ARG B  32      81.171  40.705-103.622  1.00 36.23           O  
ANISOU 3576  O   ARG B  32     3314   6661   3792     62   -375   1313       O  
ATOM   3577  CB  ARG B  32      84.353  40.845-103.460  1.00 45.87           C  
ANISOU 3577  CB  ARG B  32     4450   7893   5087    -34   -373   1424       C  
ATOM   3578  CG  ARG B  32      84.720  39.657-104.328  1.00 44.62           C  
ANISOU 3578  CG  ARG B  32     4255   7849   4851     -8   -312   1429       C  
ATOM   3579  CD  ARG B  32      85.950  38.974-103.762  1.00 40.58           C  
ANISOU 3579  CD  ARG B  32     3704   7353   4360    -23   -307   1417       C  
ATOM   3580  NE  ARG B  32      87.100  39.870-103.786  1.00 41.84           N  
ANISOU 3580  NE  ARG B  32     3813   7493   4591    -80   -325   1497       N  
ATOM   3581  CZ  ARG B  32      88.148  39.759-102.979  1.00 41.21           C  
ANISOU 3581  CZ  ARG B  32     3699   7396   4562   -110   -353   1493       C  
ATOM   3582  NH1 ARG B  32      88.187  38.791-102.073  1.00 45.85           N  
ANISOU 3582  NH1 ARG B  32     4305   7983   5134    -84   -367   1419       N  
ATOM   3583  NH2 ARG B  32      89.153  40.620-103.073  1.00 32.26           N  
ANISOU 3583  NH2 ARG B  32     2511   6247   3498   -170   -370   1567       N  
ATOM   3584  N   ALA B  33      81.986  40.624-105.724  1.00 39.08           N  
ANISOU 3584  N   ALA B  33     3610   7154   4086     55   -326   1453       N  
ATOM   3585  CA  ALA B  33      80.893  39.815-106.237  1.00 35.36           C  
ANISOU 3585  CA  ALA B  33     3151   6752   3532     99   -305   1399       C  
ATOM   3586  C   ALA B  33      81.383  39.041-107.451  1.00 36.55           C  
ANISOU 3586  C   ALA B  33     3267   7026   3594    102   -252   1429       C  
ATOM   3587  O   ALA B  33      82.136  39.570-108.272  1.00 38.69           O  
ANISOU 3587  O   ALA B  33     3504   7337   3859     78   -237   1526       O  
ATOM   3588  CB  ALA B  33      79.677  40.674-106.594  1.00 32.67           C  
ANISOU 3588  CB  ALA B  33     2824   6385   3203    126   -341   1425       C  
ATOM   3589  N   ALA B  34      80.967  37.783-107.543  1.00 40.00           N  
ANISOU 3589  N   ALA B  34     3713   7522   3964    128   -221   1341       N  
ATOM   3590  CA  ALA B  34      81.316  36.908-108.649  1.00 37.94           C  
ANISOU 3590  CA  ALA B  34     3425   7376   3614    137   -165   1337       C  
ATOM   3591  C   ALA B  34      80.054  36.536-109.416  1.00 40.86           C  
ANISOU 3591  C   ALA B  34     3810   7816   3901    161   -167   1298       C  
ATOM   3592  O   ALA B  34      78.951  36.527-108.858  1.00 36.77           O  
ANISOU 3592  O   ALA B  34     3318   7255   3399    176   -200   1243       O  
ATOM   3593  CB  ALA B  34      82.029  35.643-108.153  1.00 30.02           C  
ANISOU 3593  CB  ALA B  34     2417   6377   2612    145   -126   1259       C  
ATOM   3594  N   VAL B  35      80.226  36.235-110.701  1.00 34.19           N  
ANISOU 3594  N   VAL B  35     2941   7088   2961    162   -130   1323       N  
ATOM   3595  CA  VAL B  35      79.115  35.931-111.599  1.00 36.51           C  
ANISOU 3595  CA  VAL B  35     3241   7471   3161    178   -138   1294       C  
ATOM   3596  C   VAL B  35      79.047  34.427-111.844  1.00 40.92           C  
ANISOU 3596  C   VAL B  35     3806   8090   3654    188    -89   1173       C  
ATOM   3597  O   VAL B  35      80.087  33.790-112.055  1.00 35.73           O  
ANISOU 3597  O   VAL B  35     3131   7462   2982    186    -33   1154       O  
ATOM   3598  CB  VAL B  35      79.257  36.703-112.921  1.00 39.81           C  
ANISOU 3598  CB  VAL B  35     3635   7988   3503    167   -139   1410       C  
ATOM   3599  CG1 VAL B  35      78.164  36.316-113.897  1.00 41.17           C  
ANISOU 3599  CG1 VAL B  35     3810   8271   3562    180   -154   1377       C  
ATOM   3600  CG2 VAL B  35      79.225  38.196-112.662  1.00 43.58           C  
ANISOU 3600  CG2 VAL B  35     4113   8384   4063    157   -193   1532       C  
ATOM   3601  N   PRO B  36      77.864  33.816-111.815  1.00 43.33           N  
ANISOU 3601  N   PRO B  36     4129   8407   3926    197   -108   1086       N  
ATOM   3602  CA  PRO B  36      77.742  32.401-112.179  1.00 36.00           C  
ANISOU 3602  CA  PRO B  36     3209   7533   2937    200    -63    968       C  
ATOM   3603  C   PRO B  36      77.779  32.219-113.693  1.00 35.92           C  
ANISOU 3603  C   PRO B  36     3180   7670   2797    195    -37    974       C  
ATOM   3604  O   PRO B  36      77.735  33.177-114.463  1.00 33.97           O  
ANISOU 3604  O   PRO B  36     2916   7492   2500    189    -60   1077       O  
ATOM   3605  CB  PRO B  36      76.379  32.012-111.602  1.00 34.22           C  
ANISOU 3605  CB  PRO B  36     3005   7269   2729    199   -100    888       C  
ATOM   3606  CG  PRO B  36      75.591  33.282-111.677  1.00 31.94           C  
ANISOU 3606  CG  PRO B  36     2702   6979   2453    206   -162    971       C  
ATOM   3607  CD  PRO B  36      76.578  34.380-111.367  1.00 30.78           C  
ANISOU 3607  CD  PRO B  36     2550   6775   2370    206   -169   1084       C  
ATOM   3608  N   SER B  37      77.858  30.956-114.110  1.00 42.50           N  
ANISOU 3608  N   SER B  37     4021   8552   3576    196     13    860       N  
ATOM   3609  CA  SER B  37      77.926  30.632-115.532  1.00 44.34           C  
ANISOU 3609  CA  SER B  37     4240   8934   3672    189     46    838       C  
ATOM   3610  C   SER B  37      76.578  30.861-116.201  1.00 45.80           C  
ANISOU 3610  C   SER B  37     4427   9203   3771    177    -14    831       C  
ATOM   3611  O   SER B  37      75.544  30.397-115.711  1.00 50.57           O  
ANISOU 3611  O   SER B  37     5046   9764   4406    172    -49    752       O  
ATOM   3612  CB  SER B  37      78.347  29.178-115.729  1.00 45.35           C  
ANISOU 3612  CB  SER B  37     4378   9074   3778    197    116    697       C  
ATOM   3613  OG  SER B  37      77.269  28.310-115.404  1.00 51.37           O  
ANISOU 3613  OG  SER B  37     5170   9798   4551    187     92    581       O  
ATOM   3614  N   GLY B  38      76.593  31.551-117.337  1.00 49.11           N  
ANISOU 3614  N   GLY B  38     4829   9751   4082    168    -26    917       N  
ATOM   3615  CA  GLY B  38      75.383  31.775-118.105  1.00 43.84           C  
ANISOU 3615  CA  GLY B  38     4155   9184   3319    158    -91    921       C  
ATOM   3616  C   GLY B  38      75.423  31.092-119.456  1.00 48.69           C  
ANISOU 3616  C   GLY B  38     4768   9953   3780    138    -56    851       C  
ATOM   3617  O   GLY B  38      75.859  29.942-119.562  1.00 51.69           O  
ANISOU 3617  O   GLY B  38     5160  10357   4122    135     10    723       O  
ATOM   3618  N   ALA B  39      74.971  31.789-120.497  1.00 51.53           N  
ANISOU 3618  N   ALA B  39     5114  10383   4083    125    -97    920       N  
ATOM   3619  CA  ALA B  39      75.015  31.283-121.861  1.00 48.77           C  
ANISOU 3619  CA  ALA B  39     4763  10164   3602    101    -69    858       C  
ATOM   3620  C   ALA B  39      75.662  32.319-122.767  1.00 42.71           C  
ANISOU 3620  C   ALA B  39     3983   9450   2796     91    -59   1004       C  
ATOM   3621  O   ALA B  39      75.506  33.527-122.568  1.00 43.84           O  
ANISOU 3621  O   ALA B  39     4116   9539   3002     98   -109   1153       O  
ATOM   3622  CB  ALA B  39      73.613  30.934-122.387  1.00 43.44           C  
ANISOU 3622  CB  ALA B  39     4086   9549   2870     83   -138    781       C  
ATOM   3623  N   SER B  40      76.396  31.837-123.768  1.00 43.70           N  
ANISOU 3623  N   SER B  40     4108   9681   2816     74      7    958       N  
ATOM   3624  CA  SER B  40      77.037  32.730-124.722  1.00 50.76           C  
ANISOU 3624  CA  SER B  40     4988  10642   3655     55     24   1090       C  
ATOM   3625  C   SER B  40      76.250  32.891-126.016  1.00 61.18           C  
ANISOU 3625  C   SER B  40     6312  12082   4853     29    -23   1099       C  
ATOM   3626  O   SER B  40      76.504  33.844-126.762  1.00 64.03           O  
ANISOU 3626  O   SER B  40     6665  12490   5175     13    -34   1240       O  
ATOM   3627  CB  SER B  40      78.460  32.245-125.040  1.00 48.60           C  
ANISOU 3627  CB  SER B  40     4706  10416   3344     52    134   1053       C  
ATOM   3628  OG  SER B  40      78.481  30.875-125.405  1.00 50.99           O  
ANISOU 3628  OG  SER B  40     5023  10782   3571     53    187    863       O  
ATOM   3629  N   THR B  41      75.307  31.991-126.299  1.00 57.37           N  
ANISOU 3629  N   THR B  41     5840  11650   4308     21    -53    956       N  
ATOM   3630  CA  THR B  41      74.411  32.116-127.440  1.00 57.94           C  
ANISOU 3630  CA  THR B  41     5912  11835   4268     -5   -112    959       C  
ATOM   3631  C   THR B  41      72.981  31.893-126.969  1.00 62.19           C  
ANISOU 3631  C   THR B  41     6445  12336   4848      1   -199    900       C  
ATOM   3632  O   THR B  41      72.729  31.066-126.086  1.00 60.46           O  
ANISOU 3632  O   THR B  41     6231  12052   4690      9   -190    778       O  
ATOM   3633  CB  THR B  41      74.759  31.120-128.568  1.00 55.99           C  
ANISOU 3633  CB  THR B  41     5679  11726   3869    -35    -53    821       C  
ATOM   3634  OG1 THR B  41      74.541  29.777-128.121  1.00 59.76           O  
ANISOU 3634  OG1 THR B  41     6171  12184   4352    -34    -25    621       O  
ATOM   3635  CG2 THR B  41      76.213  31.273-129.003  1.00 60.97           C  
ANISOU 3635  CG2 THR B  41     6308  12397   4461    -38     45    867       C  
ATOM   3636  N   GLY B  42      72.049  32.641-127.556  1.00 63.24           N  
ANISOU 3636  N   GLY B  42     6565  12511   4951     -5   -284    992       N  
ATOM   3637  CA  GLY B  42      70.658  32.577-127.153  1.00 59.20           C  
ANISOU 3637  CA  GLY B  42     6037  11970   4487      3   -371    955       C  
ATOM   3638  C   GLY B  42      69.839  33.714-127.725  1.00 67.25           C  
ANISOU 3638  C   GLY B  42     7039  13015   5499     12   -462   1105       C  
ATOM   3639  O   GLY B  42      70.298  34.861-127.768  1.00 60.45           O  
ANISOU 3639  O   GLY B  42     6179  12111   4678     30   -467   1274       O  
ATOM   3640  N   ILE B  43      68.614  33.408-128.157  1.00 75.18           N  
ANISOU 3640  N   ILE B  43     8025  14086   6455      0   -536   1044       N  
ATOM   3641  CA  ILE B  43      67.802  34.386-128.875  1.00 73.81           C  
ANISOU 3641  CA  ILE B  43     7834  13958   6254      9   -627   1179       C  
ATOM   3642  C   ILE B  43      67.196  35.409-127.921  1.00 67.55           C  
ANISOU 3642  C   ILE B  43     7019  13028   5620     62   -688   1295       C  
ATOM   3643  O   ILE B  43      67.101  36.597-128.250  1.00 70.93           O  
ANISOU 3643  O   ILE B  43     7445  13435   6071     86   -737   1465       O  
ATOM   3644  CB  ILE B  43      66.723  33.658-129.700  1.00 79.84           C  
ANISOU 3644  CB  ILE B  43     8580  14850   6907    -25   -688   1068       C  
ATOM   3645  CG1 ILE B  43      67.380  32.791-130.779  1.00 84.67           C  
ANISOU 3645  CG1 ILE B  43     9219  15600   7350    -76   -628    964       C  
ATOM   3646  CG2 ILE B  43      65.752  34.653-130.328  1.00 75.79           C  
ANISOU 3646  CG2 ILE B  43     8043  14376   6379     -7   -795   1207       C  
ATOM   3647  CD1 ILE B  43      66.560  31.583-131.182  1.00 85.44           C  
ANISOU 3647  CD1 ILE B  43     9308  15791   7364   -119   -655    773       C  
ATOM   3648  N   TYR B  44      66.790  34.978-126.724  1.00 59.70           N  
ANISOU 3648  N   TYR B  44     6009  11935   4738     81   -687   1205       N  
ATOM   3649  CA  TYR B  44      66.077  35.843-125.784  1.00 58.06           C  
ANISOU 3649  CA  TYR B  44     5776  11603   4680    133   -746   1286       C  
ATOM   3650  C   TYR B  44      66.946  36.306-124.620  1.00 58.72           C  
ANISOU 3650  C   TYR B  44     5879  11541   4890    162   -693   1338       C  
ATOM   3651  O   TYR B  44      66.972  37.499-124.302  1.00 65.37           O  
ANISOU 3651  O   TYR B  44     6721  12292   5827    202   -726   1482       O  
ATOM   3652  CB  TYR B  44      64.832  35.126-125.240  1.00 51.69           C  
ANISOU 3652  CB  TYR B  44     4929  10796   3915    133   -792   1154       C  
ATOM   3653  CG  TYR B  44      63.977  34.440-126.289  1.00 49.67           C  
ANISOU 3653  CG  TYR B  44     4651  10686   3534     92   -841   1068       C  
ATOM   3654  CD1 TYR B  44      63.823  33.059-126.291  1.00 49.39           C  
ANISOU 3654  CD1 TYR B  44     4615  10712   3440     42   -810    880       C  
ATOM   3655  CD2 TYR B  44      63.327  35.171-127.277  1.00 53.73           C  
ANISOU 3655  CD2 TYR B  44     5146  11275   3992    102   -923   1174       C  
ATOM   3656  CE1 TYR B  44      63.045  32.422-127.248  1.00 52.91           C  
ANISOU 3656  CE1 TYR B  44     5041  11290   3773     -3   -858    793       C  
ATOM   3657  CE2 TYR B  44      62.546  34.541-128.242  1.00 60.08           C  
ANISOU 3657  CE2 TYR B  44     5930  12220   4677     61   -975   1093       C  
ATOM   3658  CZ  TYR B  44      62.410  33.165-128.221  1.00 59.37           C  
ANISOU 3658  CZ  TYR B  44     5839  12189   4531      7   -941    899       C  
ATOM   3659  OH  TYR B  44      61.639  32.523-129.168  1.00 64.59           O  
ANISOU 3659  OH  TYR B  44     6479  12987   5074    -41   -995    810       O  
ATOM   3660  N   GLU B  45      67.657  35.387-123.973  1.00 49.06           N  
ANISOU 3660  N   GLU B  45     4673  10292   3674    144   -617   1223       N  
ATOM   3661  CA  GLU B  45      68.352  35.699-122.735  1.00 51.54           C  
ANISOU 3661  CA  GLU B  45     5002  10471   4111    169   -576   1253       C  
ATOM   3662  C   GLU B  45      69.576  36.577-122.986  1.00 55.27           C  
ANISOU 3662  C   GLU B  45     5499  10914   4589    171   -537   1396       C  
ATOM   3663  O   GLU B  45      70.136  36.620-124.085  1.00 43.03           O  
ANISOU 3663  O   GLU B  45     3958   9460   2929    143   -512   1439       O  
ATOM   3664  CB  GLU B  45      68.778  34.411-122.029  1.00 47.28           C  
ANISOU 3664  CB  GLU B  45     4475   9921   3567    148   -510   1094       C  
ATOM   3665  CG  GLU B  45      69.604  33.485-122.902  1.00 50.19           C  
ANISOU 3665  CG  GLU B  45     4866  10397   3806    108   -443   1012       C  
ATOM   3666  CD  GLU B  45      69.831  32.132-122.265  1.00 59.41           C  
ANISOU 3666  CD  GLU B  45     6047  11554   4971     90   -389    843       C  
ATOM   3667  OE1 GLU B  45      70.296  32.084-121.105  1.00 59.19           O  
ANISOU 3667  OE1 GLU B  45     6031  11422   5038    109   -360    841       O  
ATOM   3668  OE2 GLU B  45      69.537  31.112-122.924  1.00 66.97           O  
ANISOU 3668  OE2 GLU B  45     7008  12605   5831     55   -380    712       O  
ATOM   3669  N   ALA B  46      69.988  37.286-121.936  1.00 52.27           N  
ANISOU 3669  N   ALA B  46     5125  10399   4336    200   -532   1467       N  
ATOM   3670  CA  ALA B  46      71.234  38.037-121.987  1.00 47.52           C  
ANISOU 3670  CA  ALA B  46     4542   9757   3755    193   -489   1591       C  
ATOM   3671  C   ALA B  46      72.412  37.077-122.109  1.00 46.82           C  
ANISOU 3671  C   ALA B  46     4467   9726   3595    159   -395   1509       C  
ATOM   3672  O   ALA B  46      72.419  35.998-121.509  1.00 44.63           O  
ANISOU 3672  O   ALA B  46     4193   9446   3318    157   -361   1367       O  
ATOM   3673  CB  ALA B  46      71.383  38.913-120.745  1.00 41.13           C  
ANISOU 3673  CB  ALA B  46     3736   8788   3103    227   -509   1665       C  
ATOM   3674  N   LEU B  47      73.411  37.479-122.891  1.00 45.47           N  
ANISOU 3674  N   LEU B  47     4301   9608   3366    134   -352   1601       N  
ATOM   3675  CA  LEU B  47      74.514  36.612-123.285  1.00 44.73           C  
ANISOU 3675  CA  LEU B  47     4212   9595   3188    105   -261   1527       C  
ATOM   3676  C   LEU B  47      75.784  36.990-122.538  1.00 45.10           C  
ANISOU 3676  C   LEU B  47     4259   9560   3316    104   -205   1594       C  
ATOM   3677  O   LEU B  47      76.159  38.167-122.497  1.00 45.57           O  
ANISOU 3677  O   LEU B  47     4316   9562   3437    100   -223   1750       O  
ATOM   3678  CB  LEU B  47      74.760  36.698-124.796  1.00 43.31           C  
ANISOU 3678  CB  LEU B  47     4031   9556   2868     72   -244   1569       C  
ATOM   3679  CG  LEU B  47      73.580  36.328-125.697  1.00 50.23           C  
ANISOU 3679  CG  LEU B  47     4906  10536   3643     65   -301   1509       C  
ATOM   3680  CD1 LEU B  47      73.966  36.382-127.167  1.00 46.23           C  
ANISOU 3680  CD1 LEU B  47     4402  10176   2987     29   -278   1549       C  
ATOM   3681  CD2 LEU B  47      73.038  34.955-125.330  1.00 53.08           C  
ANISOU 3681  CD2 LEU B  47     5269  10918   3981     66   -291   1308       C  
ATOM   3682  N   GLU B  48      76.444  35.989-121.961  1.00 41.58           N  
ANISOU 3682  N   GLU B  48     3815   9110   2874    106   -140   1478       N  
ATOM   3683  CA  GLU B  48      77.771  36.180-121.396  1.00 44.49           C  
ANISOU 3683  CA  GLU B  48     4175   9429   3299    100    -78   1530       C  
ATOM   3684  C   GLU B  48      78.822  36.146-122.502  1.00 44.20           C  
ANISOU 3684  C   GLU B  48     4122   9504   3169     69     -4   1565       C  
ATOM   3685  O   GLU B  48      78.678  35.441-123.506  1.00 46.80           O  
ANISOU 3685  O   GLU B  48     4454   9951   3378     58     22   1480       O  
ATOM   3686  CB  GLU B  48      78.069  35.109-120.345  1.00 44.86           C  
ANISOU 3686  CB  GLU B  48     4228   9428   3387    119    -37   1398       C  
ATOM   3687  CG  GLU B  48      78.253  33.701-120.893  1.00 43.05           C  
ANISOU 3687  CG  GLU B  48     4003   9297   3058    117     28   1236       C  
ATOM   3688  CD  GLU B  48      78.480  32.679-119.795  1.00 44.70           C  
ANISOU 3688  CD  GLU B  48     4223   9443   3317    138     64   1118       C  
ATOM   3689  OE1 GLU B  48      78.595  33.086-118.615  1.00 50.13           O  
ANISOU 3689  OE1 GLU B  48     4914  10009   4125    151     40   1163       O  
ATOM   3690  OE2 GLU B  48      78.541  31.470-120.110  1.00 42.18           O  
ANISOU 3690  OE2 GLU B  48     3912   9180   2933    141    116    973       O  
ATOM   3691  N   LEU B  49      79.880  36.929-122.317  1.00 45.23           N  
ANISOU 3691  N   LEU B  49     4234   9598   3355     51     28   1689       N  
ATOM   3692  CA  LEU B  49      80.939  37.053-123.313  1.00 44.33           C  
ANISOU 3692  CA  LEU B  49     4095   9583   3165     18     99   1742       C  
ATOM   3693  C   LEU B  49      82.062  36.072-122.991  1.00 46.11           C  
ANISOU 3693  C   LEU B  49     4298   9832   3391     25    197   1638       C  
ATOM   3694  O   LEU B  49      82.681  36.154-121.922  1.00 40.73           O  
ANISOU 3694  O   LEU B  49     3601   9061   2814     34    214   1658       O  
ATOM   3695  CB  LEU B  49      81.468  38.486-123.358  1.00 42.72           C  
ANISOU 3695  CB  LEU B  49     3877   9328   3026    -14     81   1943       C  
ATOM   3696  CG  LEU B  49      82.588  38.797-124.351  1.00 50.14           C  
ANISOU 3696  CG  LEU B  49     4789  10365   3899    -59    153   2025       C  
ATOM   3697  CD1 LEU B  49      82.103  38.622-125.786  1.00 50.51           C  
ANISOU 3697  CD1 LEU B  49     4848  10550   3792    -73    151   2009       C  
ATOM   3698  CD2 LEU B  49      83.127  40.204-124.117  1.00 48.72           C  
ANISOU 3698  CD2 LEU B  49     4594  10102   3814    -96    132   2223       C  
ATOM   3699  N   ARG B  50      82.312  35.143-123.910  1.00 45.12           N  
ANISOU 3699  N   ARG B  50     4170   9825   3151     24    260   1525       N  
ATOM   3700  CA  ARG B  50      83.419  34.204-123.814  1.00 46.86           C  
ANISOU 3700  CA  ARG B  50     4363  10076   3366     38    362   1422       C  
ATOM   3701  C   ARG B  50      84.525  34.623-124.773  1.00 47.99           C  
ANISOU 3701  C   ARG B  50     4470  10312   3453      4    434   1500       C  
ATOM   3702  O   ARG B  50      84.265  35.198-125.834  1.00 45.53           O  
ANISOU 3702  O   ARG B  50     4167  10081   3050    -28    414   1575       O  
ATOM   3703  CB  ARG B  50      82.960  32.780-124.136  1.00 52.30           C  
ANISOU 3703  CB  ARG B  50     5076  10821   3974     64    392   1220       C  
ATOM   3704  CG  ARG B  50      83.057  31.797-122.973  1.00 59.75           C  
ANISOU 3704  CG  ARG B  50     6023  11678   5002    105    418   1097       C  
ATOM   3705  CD  ARG B  50      82.332  32.293-121.727  1.00 54.85           C  
ANISOU 3705  CD  ARG B  50     5420  10933   4487    114    334   1156       C  
ATOM   3706  NE  ARG B  50      82.079  31.206-120.783  1.00 54.85           N  
ANISOU 3706  NE  ARG B  50     5438  10870   4534    148    348   1021       N  
ATOM   3707  CZ  ARG B  50      81.792  31.381-119.497  1.00 63.93           C  
ANISOU 3707  CZ  ARG B  50     6600  11884   5806    161    298   1040       C  
ATOM   3708  NH1 ARG B  50      81.731  32.605-118.991  1.00 70.47           N  
ANISOU 3708  NH1 ARG B  50     7424  12641   6709    146    237   1186       N  
ATOM   3709  NH2 ARG B  50      81.574  30.334-118.712  1.00 62.06           N  
ANISOU 3709  NH2 ARG B  50     6385  11546   5649    187    302    904       N  
ATOM   3710  N   ASP B  51      85.769  34.330-124.389  1.00 48.00           N  
ANISOU 3710  N   ASP B  51     4426  10301   3511     12    517   1484       N  
ATOM   3711  CA  ASP B  51      86.902  34.753-125.206  1.00 50.98           C  
ANISOU 3711  CA  ASP B  51     4760  10761   3850    -23    591   1561       C  
ATOM   3712  C   ASP B  51      86.923  34.032-126.548  1.00 53.57           C  
ANISOU 3712  C   ASP B  51     5099  11234   4020    -26    650   1455       C  
ATOM   3713  O   ASP B  51      87.151  34.658-127.590  1.00 48.77           O  
ANISOU 3713  O   ASP B  51     4487  10720   3325    -68    665   1546       O  
ATOM   3714  CB  ASP B  51      88.213  34.521-124.452  1.00 50.53           C  
ANISOU 3714  CB  ASP B  51     4640  10658   3899    -10    667   1554       C  
ATOM   3715  CG  ASP B  51      88.397  35.479-123.292  1.00 47.79           C  
ANISOU 3715  CG  ASP B  51     4273  10187   3697    -29    613   1692       C  
ATOM   3716  OD1 ASP B  51      89.246  35.194-122.421  1.00 52.72           O  
ANISOU 3716  OD1 ASP B  51     4850  10757   4426    -12    653   1671       O  
ATOM   3717  OD2 ASP B  51      87.695  36.512-123.244  1.00 47.35           O  
ANISOU 3717  OD2 ASP B  51     4249  10087   3656    -58    530   1818       O  
ATOM   3718  N   GLY B  52      86.682  32.724-126.547  1.00 51.42           N  
ANISOU 3718  N   GLY B  52     4846  10982   3711     16    686   1263       N  
ATOM   3719  CA  GLY B  52      86.765  31.934-127.755  1.00 52.98           C  
ANISOU 3719  CA  GLY B  52     5055  11310   3764     15    751   1138       C  
ATOM   3720  C   GLY B  52      88.137  31.373-128.061  1.00 56.88           C  
ANISOU 3720  C   GLY B  52     5499  11857   4257     30    880   1071       C  
ATOM   3721  O   GLY B  52      88.301  30.715-129.095  1.00 58.40           O  
ANISOU 3721  O   GLY B  52     5700  12161   4328     30    947    961       O  
ATOM   3722  N   ASP B  53      89.127  31.608-127.203  1.00 53.79           N  
ANISOU 3722  N   ASP B  53     5050  11390   3998     44    917   1131       N  
ATOM   3723  CA  ASP B  53      90.478  31.086-127.406  1.00 59.52           C  
ANISOU 3723  CA  ASP B  53     5712  12157   4745     65   1041   1070       C  
ATOM   3724  C   ASP B  53      90.478  29.593-127.107  1.00 67.55           C  
ANISOU 3724  C   ASP B  53     6736  13146   5784    135   1097    854       C  
ATOM   3725  O   ASP B  53      90.589  29.180-125.951  1.00 69.48           O  
ANISOU 3725  O   ASP B  53     6961  13278   6159    180   1087    818       O  
ATOM   3726  CB  ASP B  53      91.470  31.822-126.512  1.00 54.77           C  
ANISOU 3726  CB  ASP B  53     5041  11478   4292     55   1050   1204       C  
ATOM   3727  CG  ASP B  53      92.918  31.569-126.902  1.00 61.73           C  
ANISOU 3727  CG  ASP B  53     5843  12421   5192     62   1173   1180       C  
ATOM   3728  OD1 ASP B  53      93.780  32.347-126.450  1.00 63.81           O  
ANISOU 3728  OD1 ASP B  53     6042  12649   5553     33   1181   1311       O  
ATOM   3729  OD2 ASP B  53      93.201  30.611-127.658  1.00 59.08           O  
ANISOU 3729  OD2 ASP B  53     5505  12167   4776     94   1262   1030       O  
ATOM   3730  N   LYS B  54      90.379  28.773-128.157  1.00 69.36           N  
ANISOU 3730  N   LYS B  54     6990  13477   5887    145   1159    708       N  
ATOM   3731  CA  LYS B  54      90.326  27.325-127.977  1.00 72.57           C  
ANISOU 3731  CA  LYS B  54     7408  13852   6312    210   1215    491       C  
ATOM   3732  C   LYS B  54      91.596  26.765-127.349  1.00 72.29           C  
ANISOU 3732  C   LYS B  54     7295  13761   6413    271   1312    440       C  
ATOM   3733  O   LYS B  54      91.587  25.623-126.876  1.00 73.44           O  
ANISOU 3733  O   LYS B  54     7441  13840   6623    337   1349    282       O  
ATOM   3734  CB  LYS B  54      90.063  26.640-129.318  1.00 80.34           C  
ANISOU 3734  CB  LYS B  54     8433  14963   7131    200   1269    347       C  
ATOM   3735  CG  LYS B  54      88.653  26.843-129.845  1.00 83.58           C  
ANISOU 3735  CG  LYS B  54     8919  15418   7418    154   1166    348       C  
ATOM   3736  CD  LYS B  54      88.486  26.239-131.230  1.00 86.70           C  
ANISOU 3736  CD  LYS B  54     9348  15952   7641    135   1219    214       C  
ATOM   3737  CE  LYS B  54      89.313  26.988-132.264  1.00 88.02           C  
ANISOU 3737  CE  LYS B  54     9482  16251   7710     93   1282    321       C  
ATOM   3738  NZ  LYS B  54      88.897  28.414-132.378  1.00 86.67           N  
ANISOU 3738  NZ  LYS B  54     9316  16101   7512     31   1185    549       N  
ATOM   3739  N   GLN B  55      92.686  27.535-127.336  1.00 70.73           N  
ANISOU 3739  N   GLN B  55     7024  13584   6266    251   1354    571       N  
ATOM   3740  CA  GLN B  55      93.906  27.109-126.663  1.00 66.92           C  
ANISOU 3740  CA  GLN B  55     6452  13045   5931    307   1432    543       C  
ATOM   3741  C   GLN B  55      93.865  27.352-125.160  1.00 63.54           C  
ANISOU 3741  C   GLN B  55     5998  12474   5668    329   1357    622       C  
ATOM   3742  O   GLN B  55      94.600  26.691-124.418  1.00 66.20           O  
ANISOU 3742  O   GLN B  55     6271  12742   6140    394   1403    561       O  
ATOM   3743  CB  GLN B  55      95.116  27.833-127.260  1.00 73.34           C  
ANISOU 3743  CB  GLN B  55     7187  13943   6734    270   1508    649       C  
ATOM   3744  CG  GLN B  55      95.431  27.452-128.696  1.00 78.00           C  
ANISOU 3744  CG  GLN B  55     7784  14679   7174    259   1611    555       C  
ATOM   3745  CD  GLN B  55      95.866  26.007-128.830  1.00 82.07           C  
ANISOU 3745  CD  GLN B  55     8276  15188   7718    347   1718    333       C  
ATOM   3746  OE1 GLN B  55      95.056  25.129-129.131  1.00 83.11           O  
ANISOU 3746  OE1 GLN B  55     8478  15320   7780    374   1714    176       O  
ATOM   3747  NE2 GLN B  55      97.151  25.750-128.605  1.00 81.94           N  
ANISOU 3747  NE2 GLN B  55     8158  15161   7814    392   1815    315       N  
ATOM   3748  N   ARG B  56      93.023  28.271-124.695  1.00 58.22           N  
ANISOU 3748  N   ARG B  56     5371  11757   4993    278   1244    753       N  
ATOM   3749  CA  ARG B  56      93.014  28.702-123.301  1.00 53.51           C  
ANISOU 3749  CA  ARG B  56     4750  11036   4543    283   1171    849       C  
ATOM   3750  C   ARG B  56      91.646  28.403-122.700  1.00 51.93           C  
ANISOU 3750  C   ARG B  56     4633  10765   4334    294   1081    802       C  
ATOM   3751  O   ARG B  56      90.649  29.034-123.073  1.00 55.77           O  
ANISOU 3751  O   ARG B  56     5184  11276   4730    245   1007    862       O  
ATOM   3752  CB  ARG B  56      93.351  30.189-123.206  1.00 53.60           C  
ANISOU 3752  CB  ARG B  56     4734  11050   4580    209   1123   1058       C  
ATOM   3753  CG  ARG B  56      93.577  30.700-121.805  1.00 45.14           C  
ANISOU 3753  CG  ARG B  56     3625   9859   3668    206   1059   1158       C  
ATOM   3754  CD  ARG B  56      93.859  32.189-121.814  1.00 45.30           C  
ANISOU 3754  CD  ARG B  56     3624   9880   3708    124   1014   1356       C  
ATOM   3755  NE  ARG B  56      94.097  32.688-120.465  1.00 57.94           N  
ANISOU 3755  NE  ARG B  56     5187  11366   5461    115    953   1442       N  
ATOM   3756  CZ  ARG B  56      93.135  33.011-119.606  1.00 52.32           C  
ANISOU 3756  CZ  ARG B  56     4528  10567   4783    107    860   1478       C  
ATOM   3757  NH1 ARG B  56      91.859  32.892-119.952  1.00 42.13           N  
ANISOU 3757  NH1 ARG B  56     3329   9287   3391    112    815   1439       N  
ATOM   3758  NH2 ARG B  56      93.452  33.455-118.398  1.00 47.84           N  
ANISOU 3758  NH2 ARG B  56     3920   9904   4354     94    811   1550       N  
ATOM   3759  N   TYR B  57      91.600  27.439-121.777  1.00 44.28           N  
ANISOU 3759  N   TYR B  57     3655   9707   3464    359   1089    698       N  
ATOM   3760  CA  TYR B  57      90.367  27.039-121.095  1.00 48.13           C  
ANISOU 3760  CA  TYR B  57     4212  10121   3954    371   1016    644       C  
ATOM   3761  C   TYR B  57      89.308  26.545-122.076  1.00 54.44           C  
ANISOU 3761  C   TYR B  57     5094  10989   4604    356   1008    529       C  
ATOM   3762  O   TYR B  57      88.108  26.600-121.784  1.00 47.54           O  
ANISOU 3762  O   TYR B  57     4284  10082   3697    336    927    523       O  
ATOM   3763  CB  TYR B  57      89.799  28.178-120.239  1.00 44.00           C  
ANISOU 3763  CB  TYR B  57     3709   9532   3477    323    910    805       C  
ATOM   3764  CG  TYR B  57      90.545  28.444-118.944  1.00 41.98           C  
ANISOU 3764  CG  TYR B  57     3406   9136   3408    338    871    877       C  
ATOM   3765  CD1 TYR B  57      91.292  29.604-118.772  1.00 41.99           C  
ANISOU 3765  CD1 TYR B  57     3347   9154   3454    292    862   1038       C  
ATOM   3766  CD2 TYR B  57      90.486  27.543-117.890  1.00 42.04           C  
ANISOU 3766  CD2 TYR B  57     3435   8990   3548    392    836    786       C  
ATOM   3767  CE1 TYR B  57      91.964  29.856-117.586  1.00 40.05           C  
ANISOU 3767  CE1 TYR B  57     3060   8783   3376    298    816   1096       C  
ATOM   3768  CE2 TYR B  57      91.156  27.784-116.701  1.00 49.72           C  
ANISOU 3768  CE2 TYR B  57     4369   9842   4680    403    789    853       C  
ATOM   3769  CZ  TYR B  57      91.895  28.941-116.555  1.00 54.11           C  
ANISOU 3769  CZ  TYR B  57     4862  10426   5273    355    777   1002       C  
ATOM   3770  OH  TYR B  57      92.560  29.182-115.373  1.00 55.84           O  
ANISOU 3770  OH  TYR B  57     5041  10532   5644    359    724   1060       O  
ATOM   3771  N   LEU B  58      89.745  26.062-123.242  1.00 57.84           N  
ANISOU 3771  N   LEU B  58     5517  11518   4942    363   1090    434       N  
ATOM   3772  CA  LEU B  58      88.833  25.600-124.287  1.00 56.83           C  
ANISOU 3772  CA  LEU B  58     5461  11470   4664    341   1084    319       C  
ATOM   3773  C   LEU B  58      87.842  26.696-124.667  1.00 54.18           C  
ANISOU 3773  C   LEU B  58     5174  11177   4236    270    978    449       C  
ATOM   3774  O   LEU B  58      86.643  26.451-124.817  1.00 54.13           O  
ANISOU 3774  O   LEU B  58     5230  11174   4164    252    912    389       O  
ATOM   3775  CB  LEU B  58      88.099  24.328-123.858  1.00 64.62           C  
ANISOU 3775  CB  LEU B  58     6490  12391   5671    384   1084    138       C  
ATOM   3776  CG  LEU B  58      88.871  23.011-123.925  1.00 68.89           C  
ANISOU 3776  CG  LEU B  58     6998  12911   6266    460   1198    -42       C  
ATOM   3777  CD1 LEU B  58      88.229  21.967-123.017  1.00 70.20           C  
ANISOU 3777  CD1 LEU B  58     7193  12967   6513    507   1183   -168       C  
ATOM   3778  CD2 LEU B  58      88.939  22.514-125.365  1.00 65.70           C  
ANISOU 3778  CD2 LEU B  58     6618  12624   5720    448   1267   -173       C  
ATOM   3779  N   GLY B  59      88.342  27.923-124.798  1.00 51.51           N  
ANISOU 3779  N   GLY B  59     4801  10864   3905    229    959    629       N  
ATOM   3780  CA  GLY B  59      87.513  29.041-125.192  1.00 46.21           C  
ANISOU 3780  CA  GLY B  59     4167  10226   3165    170    865    767       C  
ATOM   3781  C   GLY B  59      86.647  29.635-124.104  1.00 44.03           C  
ANISOU 3781  C   GLY B  59     3916   9841   2971    163    757    856       C  
ATOM   3782  O   GLY B  59      85.914  30.592-124.381  1.00 49.47           O  
ANISOU 3782  O   GLY B  59     4631  10543   3620    122    675    972       O  
ATOM   3783  N   LYS B  60      86.710  29.117-122.875  1.00 47.28           N  
ANISOU 3783  N   LYS B  60     4320  10145   3501    203    756    809       N  
ATOM   3784  CA  LYS B  60      85.817  29.559-121.807  1.00 47.50           C  
ANISOU 3784  CA  LYS B  60     4378  10072   3598    198    661    872       C  
ATOM   3785  C   LYS B  60      86.307  30.807-121.087  1.00 47.81           C  
ANISOU 3785  C   LYS B  60     4383  10048   3735    173    624   1056       C  
ATOM   3786  O   LYS B  60      85.653  31.239-120.129  1.00 50.41           O  
ANISOU 3786  O   LYS B  60     4737  10289   4129    170    549   1112       O  
ATOM   3787  CB  LYS B  60      85.624  28.436-120.785  1.00 48.38           C  
ANISOU 3787  CB  LYS B  60     4499  10096   3787    247    677    743       C  
ATOM   3788  CG  LYS B  60      85.024  27.156-121.340  1.00 52.31           C  
ANISOU 3788  CG  LYS B  60     5037  10635   4204    267    708    550       C  
ATOM   3789  CD  LYS B  60      83.522  27.275-121.514  1.00 61.72           C  
ANISOU 3789  CD  LYS B  60     6292  11834   5324    234    613    531       C  
ATOM   3790  CE  LYS B  60      82.908  25.943-121.920  1.00 67.27           C  
ANISOU 3790  CE  LYS B  60     7033  12560   5965    246    638    329       C  
ATOM   3791  NZ  LYS B  60      83.297  24.843-120.992  1.00 67.95           N  
ANISOU 3791  NZ  LYS B  60     7126  12483   6209    294    668    212       N  
ATOM   3792  N   GLY B  61      87.429  31.388-121.508  1.00 44.84           N  
ANISOU 3792  N   GLY B  61     3952   9715   3372    152    675   1147       N  
ATOM   3793  CA  GLY B  61      87.986  32.515-120.781  1.00 40.90           C  
ANISOU 3793  CA  GLY B  61     3415   9150   2977    121    645   1312       C  
ATOM   3794  C   GLY B  61      87.078  33.730-120.822  1.00 42.13           C  
ANISOU 3794  C   GLY B  61     3613   9277   3117     79    546   1448       C  
ATOM   3795  O   GLY B  61      86.279  33.908-121.744  1.00 41.30           O  
ANISOU 3795  O   GLY B  61     3548   9234   2909     64    511   1449       O  
ATOM   3796  N   VAL B  62      87.206  34.576-119.797  1.00 44.09           N  
ANISOU 3796  N   VAL B  62     3850   9428   3477     60    499   1564       N  
ATOM   3797  CA  VAL B  62      86.408  35.795-119.700  1.00 39.56           C  
ANISOU 3797  CA  VAL B  62     3314   8801   2917     27    404   1698       C  
ATOM   3798  C   VAL B  62      87.321  37.014-119.603  1.00 40.11           C  
ANISOU 3798  C   VAL B  62     3338   8840   3061    -27    408   1869       C  
ATOM   3799  O   VAL B  62      86.963  38.025-118.987  1.00 39.65           O  
ANISOU 3799  O   VAL B  62     3302   8677   3087    -50    331   1976       O  
ATOM   3800  CB  VAL B  62      85.435  35.737-118.503  1.00 42.54           C  
ANISOU 3800  CB  VAL B  62     3743   9028   3394     55    312   1645       C  
ATOM   3801  CG1 VAL B  62      84.360  34.685-118.733  1.00 37.73           C  
ANISOU 3801  CG1 VAL B  62     3179   8455   2700     93    300   1497       C  
ATOM   3802  CG2 VAL B  62      86.184  35.442-117.222  1.00 41.18           C  
ANISOU 3802  CG2 VAL B  62     3548   8719   3380     70    314   1597       C  
ATOM   3803  N   LEU B  63      88.499  36.936-120.228  1.00 49.01           N  
ANISOU 3803  N   LEU B  63     4404  10042   4174    -49    491   1885       N  
ATOM   3804  CA  LEU B  63      89.418  38.073-120.229  1.00 46.42           C  
ANISOU 3804  CA  LEU B  63     4027   9692   3917   -112    499   2047       C  
ATOM   3805  C   LEU B  63      88.829  39.287-120.945  1.00 49.58           C  
ANISOU 3805  C   LEU B  63     4467  10091   4281   -157    439   2195       C  
ATOM   3806  O   LEU B  63      89.104  40.427-120.553  1.00 51.20           O  
ANISOU 3806  O   LEU B  63     4660  10216   4577   -208    402   2344       O  
ATOM   3807  CB  LEU B  63      90.745  37.677-120.877  1.00 47.37           C  
ANISOU 3807  CB  LEU B  63     4074   9905   4019   -123    603   2023       C  
ATOM   3808  CG  LEU B  63      91.493  36.494-120.262  1.00 48.31           C  
ANISOU 3808  CG  LEU B  63     4139  10023   4192    -71    670   1884       C  
ATOM   3809  CD1 LEU B  63      92.663  36.101-121.147  1.00 44.21           C  
ANISOU 3809  CD1 LEU B  63     3555   9608   3634    -73    773   1850       C  
ATOM   3810  CD2 LEU B  63      91.966  36.830-118.856  1.00 41.67           C  
ANISOU 3810  CD2 LEU B  63     3252   9070   3510    -84    638   1934       C  
ATOM   3811  N   LYS B  64      88.026  39.071-121.994  1.00 43.48           N  
ANISOU 3811  N   LYS B  64     3737   9399   3383   -142    425   2158       N  
ATOM   3812  CA  LYS B  64      87.442  40.198-122.717  1.00 44.45           C  
ANISOU 3812  CA  LYS B  64     3892   9521   3475   -179    365   2302       C  
ATOM   3813  C   LYS B  64      86.406  40.922-121.864  1.00 48.18           C  
ANISOU 3813  C   LYS B  64     4412   9858   4035   -167    258   2363       C  
ATOM   3814  O   LYS B  64      86.385  42.158-121.810  1.00 51.00           O  
ANISOU 3814  O   LYS B  64     4777  10140   4462   -206    210   2524       O  
ATOM   3815  CB  LYS B  64      86.814  39.726-124.028  1.00 50.68           C  
ANISOU 3815  CB  LYS B  64     4711  10439   4106   -166    374   2239       C  
ATOM   3816  CG  LYS B  64      87.790  39.152-125.034  1.00 51.83           C  
ANISOU 3816  CG  LYS B  64     4818  10723   4150   -183    478   2189       C  
ATOM   3817  CD  LYS B  64      87.091  38.872-126.354  1.00 51.66           C  
ANISOU 3817  CD  LYS B  64     4834  10828   3967   -182    473   2149       C  
ATOM   3818  CE  LYS B  64      88.046  38.288-127.376  1.00 54.93           C  
ANISOU 3818  CE  LYS B  64     5216  11385   4271   -198    582   2090       C  
ATOM   3819  NZ  LYS B  64      87.425  38.257-128.729  1.00 57.96           N  
ANISOU 3819  NZ  LYS B  64     5635  11897   4490   -214    573   2086       N  
ATOM   3820  N   ALA B  65      85.527  40.166-121.202  1.00 44.79           N  
ANISOU 3820  N   ALA B  65     4018   9392   3608   -111    220   2235       N  
ATOM   3821  CA  ALA B  65      84.565  40.776-120.288  1.00 45.76           C  
ANISOU 3821  CA  ALA B  65     4183   9384   3821    -91    122   2274       C  
ATOM   3822  C   ALA B  65      85.270  41.539-119.173  1.00 42.73           C  
ANISOU 3822  C   ALA B  65     3781   8879   3575   -122    108   2371       C  
ATOM   3823  O   ALA B  65      84.845  42.639-118.801  1.00 40.64           O  
ANISOU 3823  O   ALA B  65     3543   8498   3401   -134     31   2480       O  
ATOM   3824  CB  ALA B  65      83.641  39.705-119.706  1.00 39.82           C  
ANISOU 3824  CB  ALA B  65     3463   8620   3047    -32     97   2106       C  
ATOM   3825  N   VAL B  66      86.353  40.970-118.632  1.00 41.31           N  
ANISOU 3825  N   VAL B  66     3555   8692   3449   -131    173   2305       N  
ATOM   3826  CA  VAL B  66      87.104  41.639-117.571  1.00 43.37           C  
ANISOU 3826  CA  VAL B  66     3793   8801   3886   -165    148   2345       C  
ATOM   3827  C   VAL B  66      87.718  42.935-118.088  1.00 46.31           C  
ANISOU 3827  C   VAL B  66     4140   9168   4287   -240    151   2543       C  
ATOM   3828  O   VAL B  66      87.729  43.957-117.389  1.00 51.82           O  
ANISOU 3828  O   VAL B  66     4852   9711   5126   -271     86   2617       O  
ATOM   3829  CB  VAL B  66      88.177  40.692-116.995  1.00 41.80           C  
ANISOU 3829  CB  VAL B  66     3538   8611   3733   -156    214   2234       C  
ATOM   3830  CG1 VAL B  66      89.143  41.453-116.101  1.00 39.34           C  
ANISOU 3830  CG1 VAL B  66     3186   8179   3583   -208    194   2297       C  
ATOM   3831  CG2 VAL B  66      87.530  39.555-116.219  1.00 37.96           C  
ANISOU 3831  CG2 VAL B  66     3088   8076   3258    -87    192   2054       C  
ATOM   3832  N   ASP B  67      88.237  42.919-119.319  1.00 46.98           N  
ANISOU 3832  N   ASP B  67     4188   9417   4243   -275    228   2626       N  
ATOM   3833  CA  ASP B  67      88.829  44.128-119.881  1.00 46.33           C  
ANISOU 3833  CA  ASP B  67     4085   9316   4204   -351    230   2803       C  
ATOM   3834  C   ASP B  67      87.775  45.204-120.113  1.00 54.03           C  
ANISOU 3834  C   ASP B  67     5126  10202   5202   -352    134   2920       C  
ATOM   3835  O   ASP B  67      88.047  46.395-119.923  1.00 59.26           O  
ANISOU 3835  O   ASP B  67     5789  10759   5969   -409     98   3075       O  
ATOM   3836  CB  ASP B  67      89.560  43.804-121.182  1.00 51.39           C  
ANISOU 3836  CB  ASP B  67     4684  10108   4736   -374    317   2800       C  
ATOM   3837  CG  ASP B  67      90.129  45.041-121.850  1.00 61.54           C  
ANISOU 3837  CG  ASP B  67     5951  11379   6052   -456    321   2987       C  
ATOM   3838  OD1 ASP B  67      91.083  45.627-121.297  1.00 66.60           O  
ANISOU 3838  OD1 ASP B  67     6542  11954   6810   -520    338   3070       O  
ATOM   3839  OD2 ASP B  67      89.625  45.427-122.927  1.00 64.12           O  
ANISOU 3839  OD2 ASP B  67     6312  11761   6288   -462    305   3052       O  
ATOM   3840  N   HIS B  68      86.570  44.805-120.526  1.00 52.74           N  
ANISOU 3840  N   HIS B  68     5013  10072   4954   -288     90   2846       N  
ATOM   3841  CA  HIS B  68      85.491  45.773-120.697  1.00 51.55           C  
ANISOU 3841  CA  HIS B  68     4916   9833   4838   -274     -6   2945       C  
ATOM   3842  C   HIS B  68      85.163  46.472-119.385  1.00 53.12           C  
ANISOU 3842  C   HIS B  68     5142   9849   5191   -264    -86   2987       C  
ATOM   3843  O   HIS B  68      84.881  47.675-119.367  1.00 54.47           O  
ANISOU 3843  O   HIS B  68     5339   9903   5454   -284   -150   3129       O  
ATOM   3844  CB  HIS B  68      84.250  45.081-121.255  1.00 51.70           C  
ANISOU 3844  CB  HIS B  68     4971   9925   4748   -207    -37   2834       C  
ATOM   3845  CG  HIS B  68      84.324  44.805-122.723  1.00 60.41           C  
ANISOU 3845  CG  HIS B  68     6064  11185   5703   -223      9   2839       C  
ATOM   3846  ND1 HIS B  68      84.110  43.552-123.256  1.00 66.26           N  
ANISOU 3846  ND1 HIS B  68     6801  12061   6313   -191     53   2680       N  
ATOM   3847  CD2 HIS B  68      84.579  45.622-123.772  1.00 59.06           C  
ANISOU 3847  CD2 HIS B  68     5890  11057   5492   -271     14   2985       C  
ATOM   3848  CE1 HIS B  68      84.233  43.608-124.570  1.00 66.79           C  
ANISOU 3848  CE1 HIS B  68     6864  12252   6261   -218     84   2722       C  
ATOM   3849  NE2 HIS B  68      84.517  44.853-124.909  1.00 64.46           N  
ANISOU 3849  NE2 HIS B  68     6570  11909   6014   -266     61   2909       N  
ATOM   3850  N   ILE B  69      85.196  45.732-118.274  1.00 52.22           N  
ANISOU 3850  N   ILE B  69     5027   9673   5141   -229    -85   2824       N  
ATOM   3851  CA  ILE B  69      84.961  46.338-116.968  1.00 47.18           C  
ANISOU 3851  CA  ILE B  69     4414   8822   4690   -219   -157   2783       C  
ATOM   3852  C   ILE B  69      86.089  47.302-116.618  1.00 50.20           C  
ANISOU 3852  C   ILE B  69     4768   9101   5206   -302   -149   2891       C  
ATOM   3853  O   ILE B  69      85.849  48.476-116.312  1.00 48.79           O  
ANISOU 3853  O   ILE B  69     4618   8768   5153   -322   -215   2986       O  
ATOM   3854  CB  ILE B  69      84.803  45.253-115.889  1.00 39.62           C  
ANISOU 3854  CB  ILE B  69     3462   7830   3763   -170   -153   2574       C  
ATOM   3855  CG1 ILE B  69      83.614  44.341-116.210  1.00 42.78           C  
ANISOU 3855  CG1 ILE B  69     3891   8319   4045    -98   -166   2468       C  
ATOM   3856  CG2 ILE B  69      84.638  45.894-114.516  1.00 41.93           C  
ANISOU 3856  CG2 ILE B  69     3781   7917   4232   -167   -221   2528       C  
ATOM   3857  CD1 ILE B  69      83.499  43.136-115.293  1.00 37.54           C  
ANISOU 3857  CD1 ILE B  69     3232   7640   3393    -57   -149   2274       C  
ATOM   3858  N   ASN B  70      87.336  46.822-116.665  1.00 50.06           N  
ANISOU 3858  N   ASN B  70     4688   9162   5172   -351    -69   2876       N  
ATOM   3859  CA  ASN B  70      88.455  47.615-116.166  1.00 53.41           C  
ANISOU 3859  CA  ASN B  70     5072   9486   5736   -434    -64   2951       C  
ATOM   3860  C   ASN B  70      88.753  48.810-117.061  1.00 58.41           C  
ANISOU 3860  C   ASN B  70     5699  10115   6378   -510    -62   3172       C  
ATOM   3861  O   ASN B  70      89.151  49.869-116.561  1.00 57.41           O  
ANISOU 3861  O   ASN B  70     5573   9832   6406   -573   -103   3254       O  
ATOM   3862  CB  ASN B  70      89.705  46.744-116.026  1.00 52.42           C  
ANISOU 3862  CB  ASN B  70     4866   9460   5590   -461     21   2879       C  
ATOM   3863  CG  ASN B  70      89.571  45.696-114.940  1.00 49.18           C  
ANISOU 3863  CG  ASN B  70     4461   9014   5209   -398      7   2680       C  
ATOM   3864  OD1 ASN B  70      88.821  45.870-113.979  1.00 53.43           O  
ANISOU 3864  OD1 ASN B  70     5056   9415   5830   -362    -70   2603       O  
ATOM   3865  ND2 ASN B  70      90.310  44.599-115.083  1.00 41.79           N  
ANISOU 3865  ND2 ASN B  70     3466   8202   4209   -383     85   2598       N  
ATOM   3866  N   SER B  71      88.567  48.668-118.372  1.00 60.33           N  
ANISOU 3866  N   SER B  71     5940  10526   6458   -511    -16   3271       N  
ATOM   3867  CA  SER B  71      88.934  49.714-119.319  1.00 64.09           C  
ANISOU 3867  CA  SER B  71     6407  11025   6920   -590     -2   3498       C  
ATOM   3868  C   SER B  71      87.787  50.643-119.685  1.00 68.68           C  
ANISOU 3868  C   SER B  71     7060  11509   7526   -559    -95   3605       C  
ATOM   3869  O   SER B  71      88.028  51.829-119.935  1.00 69.46           O  
ANISOU 3869  O   SER B  71     7168  11503   7720   -622   -123   3771       O  
ATOM   3870  CB  SER B  71      89.493  49.089-120.604  1.00 65.24           C  
ANISOU 3870  CB  SER B  71     6508  11371   6911   -602     93   3475       C  
ATOM   3871  OG  SER B  71      90.577  48.223-120.321  1.00 67.99           O  
ANISOU 3871  OG  SER B  71     6781  11809   7244   -620    181   3376       O  
ATOM   3872  N   THR B  72      86.547  50.150-119.731  1.00 63.95           N  
ANISOU 3872  N   THR B  72     6508  10932   6857   -462   -145   3509       N  
ATOM   3873  CA  THR B  72      85.427  50.944-120.232  1.00 61.51           C  
ANISOU 3873  CA  THR B  72     6254  10551   6565   -421   -229   3595       C  
ATOM   3874  C   THR B  72      84.387  51.240-119.159  1.00 60.52           C  
ANISOU 3874  C   THR B  72     6177  10266   6553   -348   -330   3554       C  
ATOM   3875  O   THR B  72      84.062  52.410-118.933  1.00 59.14           O  
ANISOU 3875  O   THR B  72     6033   9914   6521   -353   -402   3665       O  
ATOM   3876  CB  THR B  72      84.773  50.234-121.424  1.00 60.14           C  
ANISOU 3876  CB  THR B  72     6087  10551   6213   -375   -208   3528       C  
ATOM   3877  OG1 THR B  72      85.684  50.204-122.530  1.00 62.34           O  
ANISOU 3877  OG1 THR B  72     6329  10964   6395   -442   -127   3592       O  
ATOM   3878  CG2 THR B  72      83.503  50.957-121.842  1.00 56.53           C  
ANISOU 3878  CG2 THR B  72     5681  10024   5776   -322   -302   3601       C  
ATOM   3879  N   ILE B  73      83.844  50.216-118.498  1.00 59.97           N  
ANISOU 3879  N   ILE B  73     6111  10219   6456   -277   -333   3345       N  
ATOM   3880  CA  ILE B  73      82.749  50.435-117.556  1.00 59.70           C  
ANISOU 3880  CA  ILE B  73     6118  10027   6540   -200   -417   3244       C  
ATOM   3881  C   ILE B  73      83.239  51.199-116.331  1.00 56.52           C  
ANISOU 3881  C   ILE B  73     5724   9402   6348   -233   -445   3212       C  
ATOM   3882  O   ILE B  73      82.611  52.174-115.898  1.00 57.79           O  
ANISOU 3882  O   ILE B  73     5921   9387   6650   -205   -519   3250       O  
ATOM   3883  CB  ILE B  73      82.100  49.096-117.163  1.00 57.91           C  
ANISOU 3883  CB  ILE B  73     5890   9890   6223   -129   -403   3033       C  
ATOM   3884  CG1 ILE B  73      81.504  48.402-118.391  1.00 56.05           C  
ANISOU 3884  CG1 ILE B  73     5649   9866   5782    -99   -389   3056       C  
ATOM   3885  CG2 ILE B  73      81.027  49.310-116.107  1.00 50.31           C  
ANISOU 3885  CG2 ILE B  73     4960   8771   5384    -57   -478   2922       C  
ATOM   3886  CD1 ILE B  73      80.813  47.090-118.070  1.00 50.37           C  
ANISOU 3886  CD1 ILE B  73     4930   9229   4981    -37   -378   2853       C  
ATOM   3887  N   ALA B  74      84.364  50.773-115.758  1.00 53.58           N  
ANISOU 3887  N   ALA B  74     5318   9036   6004   -291   -387   3136       N  
ATOM   3888  CA  ALA B  74      84.848  51.393-114.525  1.00 55.76           C  
ANISOU 3888  CA  ALA B  74     5602   9117   6468   -327   -417   3082       C  
ATOM   3889  C   ALA B  74      85.126  52.885-114.674  1.00 57.22           C  
ANISOU 3889  C   ALA B  74     5802   9142   6796   -389   -460   3256       C  
ATOM   3890  O   ALA B  74      84.658  53.660-113.821  1.00 55.20           O  
ANISOU 3890  O   ALA B  74     5587   8689   6699   -369   -527   3216       O  
ATOM   3891  CB  ALA B  74      86.085  50.642-114.015  1.00 52.03           C  
ANISOU 3891  CB  ALA B  74     5077   8706   5987   -382   -352   2990       C  
ATOM   3892  N   PRO B  75      85.855  53.361-115.693  1.00 55.13           N  
ANISOU 3892  N   PRO B  75     5510   8944   6492   -467   -422   3445       N  
ATOM   3893  CA  PRO B  75      86.087  54.814-115.785  1.00 55.08           C  
ANISOU 3893  CA  PRO B  75     5525   8762   6642   -532   -467   3617       C  
ATOM   3894  C   PRO B  75      84.810  55.624-115.920  1.00 58.18           C  
ANISOU 3894  C   PRO B  75     5978   9025   7102   -454   -555   3684       C  
ATOM   3895  O   PRO B  75      84.753  56.754-115.421  1.00 61.88           O  
ANISOU 3895  O   PRO B  75     6480   9273   7759   -474   -613   3734       O  
ATOM   3896  CB  PRO B  75      86.972  54.952-117.033  1.00 49.61           C  
ANISOU 3896  CB  PRO B  75     4789   8217   5845   -622   -397   3814       C  
ATOM   3897  CG  PRO B  75      87.608  53.626-117.199  1.00 56.65           C  
ANISOU 3897  CG  PRO B  75     5621   9322   6580   -625   -306   3702       C  
ATOM   3898  CD  PRO B  75      86.586  52.633-116.746  1.00 55.09           C  
ANISOU 3898  CD  PRO B  75     5453   9170   6311   -509   -331   3509       C  
ATOM   3899  N   ALA B  76      83.779  55.076-116.566  1.00 55.74           N  
ANISOU 3899  N   ALA B  76     5681   8843   6653   -364   -570   3679       N  
ATOM   3900  CA  ALA B  76      82.558  55.837-116.801  1.00 55.08           C  
ANISOU 3900  CA  ALA B  76     5642   8655   6631   -283   -658   3759       C  
ATOM   3901  C   ALA B  76      81.719  55.979-115.535  1.00 56.91           C  
ANISOU 3901  C   ALA B  76     5903   8710   7009   -201   -716   3579       C  
ATOM   3902  O   ALA B  76      81.196  57.065-115.257  1.00 61.37           O  
ANISOU 3902  O   ALA B  76     6503   9076   7739   -170   -786   3638       O  
ATOM   3903  CB  ALA B  76      81.741  55.180-117.916  1.00 55.13           C  
ANISOU 3903  CB  ALA B  76     5641   8873   6432   -219   -660   3808       C  
ATOM   3904  N   LEU B  77      81.574  54.901-114.757  1.00 54.83           N  
ANISOU 3904  N   LEU B  77     5629   8516   6690   -164   -687   3362       N  
ATOM   3905  CA  LEU B  77      80.778  54.976-113.534  1.00 54.20           C  
ANISOU 3905  CA  LEU B  77     5575   8289   6729    -91   -732   3186       C  
ATOM   3906  C   LEU B  77      81.446  55.863-112.489  1.00 60.28           C  
ANISOU 3906  C   LEU B  77     6366   8840   7697   -151   -749   3149       C  
ATOM   3907  O   LEU B  77      80.765  56.603-111.769  1.00 61.89           O  
ANISOU 3907  O   LEU B  77     6605   8859   8052    -99   -805   3093       O  
ATOM   3908  CB  LEU B  77      80.539  53.575-112.972  1.00 48.73           C  
ANISOU 3908  CB  LEU B  77     4866   7729   5920    -52   -690   2978       C  
ATOM   3909  CG  LEU B  77      79.791  52.599-113.882  1.00 49.75           C  
ANISOU 3909  CG  LEU B  77     4976   8067   5860      7   -676   2974       C  
ATOM   3910  CD1 LEU B  77      79.504  51.299-113.150  1.00 48.60           C  
ANISOU 3910  CD1 LEU B  77     4822   8006   5638     43   -641   2760       C  
ATOM   3911  CD2 LEU B  77      78.505  53.221-114.398  1.00 44.18           C  
ANISOU 3911  CD2 LEU B  77     4283   7323   5179     91   -751   3058       C  
ATOM   3912  N   ILE B  78      82.775  55.793-112.385  1.00 57.41           N  
ANISOU 3912  N   ILE B  78     5978   8498   7337   -259   -702   3171       N  
ATOM   3913  CA  ILE B  78      83.499  56.674-111.474  1.00 56.88           C  
ANISOU 3913  CA  ILE B  78     5925   8231   7454   -333   -724   3147       C  
ATOM   3914  C   ILE B  78      83.366  58.125-111.919  1.00 60.84           C  
ANISOU 3914  C   ILE B  78     6459   8549   8109   -355   -777   3328       C  
ATOM   3915  O   ILE B  78      83.177  59.028-111.094  1.00 67.08           O  
ANISOU 3915  O   ILE B  78     7287   9116   9083   -353   -828   3275       O  
ATOM   3916  CB  ILE B  78      84.974  56.244-111.384  1.00 59.14           C  
ANISOU 3916  CB  ILE B  78     6162   8604   7703   -447   -664   3147       C  
ATOM   3917  CG1 ILE B  78      85.086  54.840-110.784  1.00 57.09           C  
ANISOU 3917  CG1 ILE B  78     5877   8492   7322   -415   -621   2958       C  
ATOM   3918  CG2 ILE B  78      85.778  57.254-110.577  1.00 61.86           C  
ANISOU 3918  CG2 ILE B  78     6516   8747   8240   -542   -694   3145       C  
ATOM   3919  CD1 ILE B  78      86.481  54.268-110.824  1.00 57.88           C  
ANISOU 3919  CD1 ILE B  78     5914   8706   7370   -508   -559   2962       C  
ATOM   3920  N   SER B  79      83.457  58.371-113.229  1.00 58.86           N  
ANISOU 3920  N   SER B  79     6196   8386   7783   -378   -766   3543       N  
ATOM   3921  CA  SER B  79      83.358  59.733-113.742  1.00 60.66           C  
ANISOU 3921  CA  SER B  79     6455   8441   8152   -403   -818   3745       C  
ATOM   3922  C   SER B  79      81.983  60.331-113.491  1.00 61.52           C  
ANISOU 3922  C   SER B  79     6609   8397   8369   -278   -897   3719       C  
ATOM   3923  O   SER B  79      81.858  61.549-113.316  1.00 58.89           O  
ANISOU 3923  O   SER B  79     6312   7831   8230   -284   -952   3800       O  
ATOM   3924  CB  SER B  79      83.667  59.747-115.236  1.00 69.36           C  
ANISOU 3924  CB  SER B  79     7533   9703   9116   -448   -787   3985       C  
ATOM   3925  OG  SER B  79      84.866  59.044-115.510  1.00 74.34           O  
ANISOU 3925  OG  SER B  79     8112  10508   9628   -548   -700   3990       O  
ATOM   3926  N   SER B  80      80.942  59.494-113.475  1.00 63.24           N  
ANISOU 3926  N   SER B  80     6819   8737   8472   -164   -903   3605       N  
ATOM   3927  CA  SER B  80      79.588  59.981-113.239  1.00 65.14           C  
ANISOU 3927  CA  SER B  80     7086   8855   8810    -37   -974   3570       C  
ATOM   3928  C   SER B  80      79.411  60.541-111.836  1.00 64.82           C  
ANISOU 3928  C   SER B  80     7078   8584   8968    -14  -1000   3391       C  
ATOM   3929  O   SER B  80      78.492  61.338-111.615  1.00 65.86           O  
ANISOU 3929  O   SER B  80     7233   8545   9245     75  -1060   3391       O  
ATOM   3930  CB  SER B  80      78.574  58.860-113.479  1.00 60.06           C  
ANISOU 3930  CB  SER B  80     6416   8411   7993     66   -968   3471       C  
ATOM   3931  OG  SER B  80      78.692  57.842-112.498  1.00 56.81           O  
ANISOU 3931  OG  SER B  80     5993   8070   7523     67   -921   3236       O  
ATOM   3932  N   GLY B  81      80.264  60.148-110.891  1.00 65.06           N  
ANISOU 3932  N   GLY B  81     7105   8608   9006    -90   -958   3237       N  
ATOM   3933  CA  GLY B  81      80.154  60.626-109.528  1.00 61.06           C  
ANISOU 3933  CA  GLY B  81     6632   7904   8664    -79   -980   3052       C  
ATOM   3934  C   GLY B  81      78.875  60.190-108.845  1.00 56.73           C  
ANISOU 3934  C   GLY B  81     6088   7362   8103     53   -993   2867       C  
ATOM   3935  O   GLY B  81      78.542  60.689-107.767  1.00 56.14           O  
ANISOU 3935  O   GLY B  81     6044   7119   8168     84  -1013   2715       O  
ATOM   3936  N   LEU B  82      78.149  59.264-109.464  1.00 57.29           N  
ANISOU 3936  N   LEU B  82     6128   7633   8008    125   -978   2874       N  
ATOM   3937  CA  LEU B  82      76.895  58.789-108.901  1.00 62.15           C  
ANISOU 3937  CA  LEU B  82     6735   8275   8603    244   -986   2710       C  
ATOM   3938  C   LEU B  82      77.140  58.052-107.593  1.00 64.45           C  
ANISOU 3938  C   LEU B  82     7034   8591   8864    221   -943   2473       C  
ATOM   3939  O   LEU B  82      78.099  57.285-107.464  1.00 63.07           O  
ANISOU 3939  O   LEU B  82     6849   8532   8582    136   -898   2441       O  
ATOM   3940  CB  LEU B  82      76.182  57.870-109.892  1.00 58.92           C  
ANISOU 3940  CB  LEU B  82     6285   8091   8012    305   -980   2769       C  
ATOM   3941  CG  LEU B  82      75.611  58.530-111.149  1.00 57.88           C  
ANISOU 3941  CG  LEU B  82     6143   7958   7892    356  -1036   2990       C  
ATOM   3942  CD1 LEU B  82      75.033  57.484-112.081  1.00 52.64           C  
ANISOU 3942  CD1 LEU B  82     5437   7544   7018    396  -1028   3024       C  
ATOM   3943  CD2 LEU B  82      74.553  59.555-110.772  1.00 59.86           C  
ANISOU 3943  CD2 LEU B  82     6404   8005   8335    465  -1101   2977       C  
ATOM   3944  N   SER B  83      76.269  58.297-106.616  1.00 68.04           N  
ANISOU 3944  N   SER B  83     7503   8936   9411    300   -956   2309       N  
ATOM   3945  CA  SER B  83      76.336  57.563-105.362  1.00 68.09           C  
ANISOU 3945  CA  SER B  83     7520   8981   9370    287   -917   2085       C  
ATOM   3946  C   SER B  83      76.046  56.090-105.607  1.00 63.08           C  
ANISOU 3946  C   SER B  83     6849   8586   8531    306   -873   2034       C  
ATOM   3947  O   SER B  83      75.269  55.723-106.492  1.00 63.80           O  
ANISOU 3947  O   SER B  83     6908   8788   8544    371   -880   2109       O  
ATOM   3948  CB  SER B  83      75.343  58.132-104.350  1.00 72.85           C  
ANISOU 3948  CB  SER B  83     8142   9435  10102    374   -932   1923       C  
ATOM   3949  OG  SER B  83      75.304  57.335-103.180  1.00 76.03           O  
ANISOU 3949  OG  SER B  83     8554   9903  10431    364   -889   1714       O  
ATOM   3950  N   VAL B  84      76.688  55.236-104.810  1.00 59.73           N  
ANISOU 3950  N   VAL B  84     6432   8240   8023    246   -831   1907       N  
ATOM   3951  CA  VAL B  84      76.544  53.801-105.009  1.00 57.92           C  
ANISOU 3951  CA  VAL B  84     6175   8223   7612    254   -787   1859       C  
ATOM   3952  C   VAL B  84      75.164  53.301-104.613  1.00 55.98           C  
ANISOU 3952  C   VAL B  84     5914   8023   7331    351   -779   1733       C  
ATOM   3953  O   VAL B  84      74.814  52.155-104.919  1.00 56.49           O  
ANISOU 3953  O   VAL B  84     5954   8256   7256    367   -748   1704       O  
ATOM   3954  CB  VAL B  84      77.663  53.069-104.237  1.00 61.95           C  
ANISOU 3954  CB  VAL B  84     6694   8787   8057    165   -751   1771       C  
ATOM   3955  CG1 VAL B  84      77.332  52.974-102.758  1.00 63.64           C  
ANISOU 3955  CG1 VAL B  84     6938   8936   8305    178   -745   1573       C  
ATOM   3956  CG2 VAL B  84      77.931  51.711-104.858  1.00 62.88           C  
ANISOU 3956  CG2 VAL B  84     6779   9112   8000    151   -708   1792       C  
ATOM   3957  N   VAL B  85      74.365  54.139-103.950  1.00 52.57           N  
ANISOU 3957  N   VAL B  85     5497   7445   7033    415   -802   1655       N  
ATOM   3958  CA  VAL B  85      73.000  53.755-103.629  1.00 51.18           C  
ANISOU 3958  CA  VAL B  85     5294   7315   6837    511   -791   1545       C  
ATOM   3959  C   VAL B  85      72.094  53.848-104.846  1.00 58.83           C  
ANISOU 3959  C   VAL B  85     6216   8346   7792    589   -825   1673       C  
ATOM   3960  O   VAL B  85      71.039  53.204-104.881  1.00 60.87           O  
ANISOU 3960  O   VAL B  85     6433   8706   7988    654   -813   1607       O  
ATOM   3961  CB  VAL B  85      72.441  54.623-102.482  1.00 49.37           C  
ANISOU 3961  CB  VAL B  85     5088   6915   6756    560   -796   1404       C  
ATOM   3962  CG1 VAL B  85      73.279  54.456-101.210  1.00 46.36           C  
ANISOU 3962  CG1 VAL B  85     4755   6495   6365    479   -766   1262       C  
ATOM   3963  CG2 VAL B  85      72.372  56.078-102.906  1.00 52.19           C  
ANISOU 3963  CG2 VAL B  85     5456   7079   7294    596   -851   1511       C  
ATOM   3964  N   GLU B  86      72.482  54.627-105.857  1.00 58.12           N  
ANISOU 3964  N   GLU B  86     6128   8203   7753    578   -869   1860       N  
ATOM   3965  CA  GLU B  86      71.673  54.811-107.063  1.00 57.86           C  
ANISOU 3965  CA  GLU B  86     6052   8229   7702    649   -914   2003       C  
ATOM   3966  C   GLU B  86      71.849  53.597-107.975  1.00 56.31           C  
ANISOU 3966  C   GLU B  86     5829   8265   7302    612   -890   2057       C  
ATOM   3967  O   GLU B  86      72.498  53.645-109.022  1.00 56.55           O  
ANISOU 3967  O   GLU B  86     5860   8359   7267    565   -902   2219       O  
ATOM   3968  CB  GLU B  86      72.060  56.101-107.772  1.00 62.17           C  
ANISOU 3968  CB  GLU B  86     6617   8630   8374    644   -969   2194       C  
ATOM   3969  CG  GLU B  86      72.075  57.347-106.891  1.00 68.65           C  
ANISOU 3969  CG  GLU B  86     7475   9198   9411    665   -991   2140       C  
ATOM   3970  CD  GLU B  86      70.688  57.865-106.563  1.00 74.07           C  
ANISOU 3970  CD  GLU B  86     8131   9795  10218    798  -1021   2069       C  
ATOM   3971  OE1 GLU B  86      70.578  58.744-105.681  1.00 73.19           O  
ANISOU 3971  OE1 GLU B  86     8047   9485  10276    827  -1026   1974       O  
ATOM   3972  OE2 GLU B  86      69.710  57.400-107.186  1.00 75.95           O  
ANISOU 3972  OE2 GLU B  86     8313  10162  10383    875  -1040   2100       O  
ATOM   3973  N   GLN B  87      71.247  52.485-107.546  1.00 49.38           N  
ANISOU 3973  N   GLN B  87     4927   7512   6324    632   -853   1912       N  
ATOM   3974  CA  GLN B  87      71.359  51.240-108.298  1.00 44.77           C  
ANISOU 3974  CA  GLN B  87     4320   7137   5553    599   -826   1929       C  
ATOM   3975  C   GLN B  87      70.767  51.381-109.693  1.00 50.94           C  
ANISOU 3975  C   GLN B  87     5063   8016   6276    641   -878   2083       C  
ATOM   3976  O   GLN B  87      71.363  50.931-110.678  1.00 49.26           O  
ANISOU 3976  O   GLN B  87     4850   7931   5937    590   -870   2185       O  
ATOM   3977  CB  GLN B  87      70.667  50.106-107.546  1.00 43.52           C  
ANISOU 3977  CB  GLN B  87     4143   7071   5322    616   -783   1747       C  
ATOM   3978  CG  GLN B  87      70.856  48.736-108.177  1.00 45.74           C  
ANISOU 3978  CG  GLN B  87     4408   7547   5422    574   -749   1736       C  
ATOM   3979  CD  GLN B  87      72.198  48.130-107.839  1.00 50.80           C  
ANISOU 3979  CD  GLN B  87     5088   8209   6004    485   -696   1710       C  
ATOM   3980  OE1 GLN B  87      72.798  48.465-106.822  1.00 53.55           O  
ANISOU 3980  OE1 GLN B  87     5471   8446   6431    455   -680   1648       O  
ATOM   3981  NE2 GLN B  87      72.677  47.234-108.689  1.00 48.02           N  
ANISOU 3981  NE2 GLN B  87     4727   8005   5514    445   -671   1752       N  
ATOM   3982  N   GLU B  88      69.591  52.001-109.798  1.00 55.29           N  
ANISOU 3982  N   GLU B  88     5577   8514   6915    737   -932   2100       N  
ATOM   3983  CA  GLU B  88      68.936  52.116-111.095  1.00 57.32           C  
ANISOU 3983  CA  GLU B  88     5791   8876   7111    783   -994   2247       C  
ATOM   3984  C   GLU B  88      69.735  53.004-112.043  1.00 61.78           C  
ANISOU 3984  C   GLU B  88     6385   9394   7693    747  -1031   2465       C  
ATOM   3985  O   GLU B  88      69.874  52.685-113.230  1.00 59.18           O  
ANISOU 3985  O   GLU B  88     6044   9216   7226    722  -1049   2593       O  
ATOM   3986  CB  GLU B  88      67.510  52.641-110.914  1.00 54.24           C  
ANISOU 3986  CB  GLU B  88     5345   8430   6832    901  -1049   2217       C  
ATOM   3987  CG  GLU B  88      66.770  52.897-112.216  1.00 63.58           C  
ANISOU 3987  CG  GLU B  88     6479   9709   7970    958  -1132   2381       C  
ATOM   3988  CD  GLU B  88      65.267  52.766-112.070  1.00 67.25           C  
ANISOU 3988  CD  GLU B  88     6862  10216   8475   1062  -1171   2301       C  
ATOM   3989  OE1 GLU B  88      64.596  52.457-113.078  1.00 61.30           O  
ANISOU 3989  OE1 GLU B  88     6054   9615   7623   1091  -1229   2383       O  
ATOM   3990  OE2 GLU B  88      64.757  52.959-110.946  1.00 65.50           O  
ANISOU 3990  OE2 GLU B  88     6625   9884   8378   1111  -1142   2152       O  
ATOM   3991  N   LYS B  89      70.282  54.111-111.535  1.00 60.26           N  
ANISOU 3991  N   LYS B  89     6233   8996   7666    737  -1040   2509       N  
ATOM   3992  CA  LYS B  89      71.076  55.005-112.374  1.00 57.38           C  
ANISOU 3992  CA  LYS B  89     5898   8570   7334    691  -1072   2724       C  
ATOM   3993  C   LYS B  89      72.308  54.296-112.925  1.00 59.30           C  
ANISOU 3993  C   LYS B  89     6160   8954   7418    577  -1015   2776       C  
ATOM   3994  O   LYS B  89      72.564  54.318-114.135  1.00 65.30           O  
ANISOU 3994  O   LYS B  89     6913   9826   8070    549  -1032   2947       O  
ATOM   3995  CB  LYS B  89      71.495  56.241-111.576  1.00 59.26           C  
ANISOU 3995  CB  LYS B  89     6178   8549   7790    687  -1084   2729       C  
ATOM   3996  CG  LYS B  89      70.360  57.033-110.954  1.00 58.68           C  
ANISOU 3996  CG  LYS B  89     6087   8311   7897    804  -1131   2663       C  
ATOM   3997  CD  LYS B  89      69.933  58.179-111.851  1.00 63.24           C  
ANISOU 3997  CD  LYS B  89     6658   8788   8583    867  -1217   2878       C  
ATOM   3998  CE  LYS B  89      69.282  59.297-111.054  1.00 68.73           C  
ANISOU 3998  CE  LYS B  89     7357   9235   9522    962  -1253   2820       C  
ATOM   3999  NZ  LYS B  89      70.257  60.365-110.699  1.00 72.20           N  
ANISOU 3999  NZ  LYS B  89     7862   9447  10125    897  -1254   2879       N  
ATOM   4000  N   LEU B  90      73.084  53.661-112.044  1.00 57.73           N  
ANISOU 4000  N   LEU B  90     5982   8755   7199    513   -946   2630       N  
ATOM   4001  CA  LEU B  90      74.324  53.018-112.470  1.00 57.25           C  
ANISOU 4001  CA  LEU B  90     5930   8812   7010    411   -887   2669       C  
ATOM   4002  C   LEU B  90      74.054  51.836-113.394  1.00 56.31           C  
ANISOU 4002  C   LEU B  90     5781   8935   6681    412   -865   2668       C  
ATOM   4003  O   LEU B  90      74.797  51.618-114.359  1.00 52.58           O  
ANISOU 4003  O   LEU B  90     5306   8582   6090    352   -840   2784       O  
ATOM   4004  CB  LEU B  90      75.132  52.585-111.244  1.00 55.44           C  
ANISOU 4004  CB  LEU B  90     5723   8526   6817    354   -829   2508       C  
ATOM   4005  CG  LEU B  90      75.624  53.729-110.355  1.00 52.01           C  
ANISOU 4005  CG  LEU B  90     5323   7864   6576    329   -847   2503       C  
ATOM   4006  CD1 LEU B  90      76.054  53.227-108.988  1.00 55.11           C  
ANISOU 4006  CD1 LEU B  90     5733   8213   6993    296   -806   2309       C  
ATOM   4007  CD2 LEU B  90      76.767  54.451-111.034  1.00 48.42           C  
ANISOU 4007  CD2 LEU B  90     4879   7367   6149    242   -847   2686       C  
ATOM   4008  N   ASP B  91      72.998  51.063-113.120  1.00 59.18           N  
ANISOU 4008  N   ASP B  91     6118   9374   6994    474   -870   2532       N  
ATOM   4009  CA  ASP B  91      72.627  49.976-114.025  1.00 60.19           C  
ANISOU 4009  CA  ASP B  91     6216   9722   6931    475   -859   2522       C  
ATOM   4010  C   ASP B  91      72.187  50.514-115.382  1.00 60.85           C  
ANISOU 4010  C   ASP B  91     6281   9887   6951    501   -924   2713       C  
ATOM   4011  O   ASP B  91      72.577  49.974-116.424  1.00 59.03           O  
ANISOU 4011  O   ASP B  91     6050   9821   6557    454   -898   2773       O  
ATOM   4012  CB  ASP B  91      71.526  49.113-113.398  1.00 57.99           C  
ANISOU 4012  CB  ASP B  91     5910   9491   6633    531   -857   2339       C  
ATOM   4013  CG  ASP B  91      72.056  48.179-112.318  1.00 58.97           C  
ANISOU 4013  CG  ASP B  91     6053   9606   6746    488   -783   2161       C  
ATOM   4014  OD1 ASP B  91      73.260  47.862-112.350  1.00 61.71           O  
ANISOU 4014  OD1 ASP B  91     6424   9976   7047    416   -731   2175       O  
ATOM   4015  OD2 ASP B  91      71.272  47.757-111.440  1.00 62.14           O  
ANISOU 4015  OD2 ASP B  91     6443   9983   7184    526   -776   2013       O  
ATOM   4016  N   ASN B  92      71.382  51.583-115.391  1.00 61.25           N  
ANISOU 4016  N   ASN B  92     6321   9818   7132    574  -1002   2799       N  
ATOM   4017  CA  ASN B  92      70.974  52.191-116.655  1.00 63.97           C  
ANISOU 4017  CA  ASN B  92     6661  10210   7434    594  -1061   2977       C  
ATOM   4018  C   ASN B  92      72.173  52.718-117.429  1.00 61.36           C  
ANISOU 4018  C   ASN B  92     6371   9875   7069    504  -1031   3143       C  
ATOM   4019  O   ASN B  92      72.270  52.526-118.647  1.00 64.34           O  
ANISOU 4019  O   ASN B  92     6758  10377   7310    462  -1012   3205       O  
ATOM   4020  CB  ASN B  92      69.978  53.324-116.404  1.00 68.48           C  
ANISOU 4020  CB  ASN B  92     7212  10623   8185    697  -1153   3045       C  
ATOM   4021  CG  ASN B  92      68.599  52.821-116.061  1.00 74.29           C  
ANISOU 4021  CG  ASN B  92     7894  11406   8927    785  -1184   2902       C  
ATOM   4022  OD1 ASN B  92      68.195  51.743-116.493  1.00 79.88           O  
ANISOU 4022  OD1 ASN B  92     8587  12282   9482    764  -1155   2795       O  
ATOM   4023  ND2 ASN B  92      67.862  53.601-115.278  1.00 76.93           N  
ANISOU 4023  ND2 ASN B  92     8200  11581   9451    880  -1234   2882       N  
ATOM   4024  N   LEU B  93      73.093  53.396-116.739  1.00 55.31           N  
ANISOU 4024  N   LEU B  93     5624   8962   6427    469  -1023   3208       N  
ATOM   4025  CA  LEU B  93      74.269  53.943-117.407  1.00 54.85           C  
ANISOU 4025  CA  LEU B  93     5594   8896   6350    376   -993   3378       C  
ATOM   4026  C   LEU B  93      75.105  52.847-118.049  1.00 57.67           C  
ANISOU 4026  C   LEU B  93     5949   9455   6508    290   -898   3324       C  
ATOM   4027  O   LEU B  93      75.696  53.060-119.114  1.00 66.28           O  
ANISOU 4027  O   LEU B  93     7050  10617   7515    225   -866   3441       O  
ATOM   4028  CB  LEU B  93      75.106  54.744-116.409  1.00 52.45           C  
ANISOU 4028  CB  LEU B  93     5320   8370   6238    333   -975   3370       C  
ATOM   4029  CG  LEU B  93      76.350  55.464-116.928  1.00 54.05           C  
ANISOU 4029  CG  LEU B  93     5544   8529   6462    230   -950   3555       C  
ATOM   4030  CD1 LEU B  93      76.001  56.363-118.100  1.00 52.22           C  
ANISOU 4030  CD1 LEU B  93     5321   8295   6225    243  -1011   3792       C  
ATOM   4031  CD2 LEU B  93      76.983  56.272-115.809  1.00 56.02           C  
ANISOU 4031  CD2 LEU B  93     5822   8537   6926    191   -944   3507       C  
ATOM   4032  N   MET B  94      75.160  51.667-117.428  1.00 53.55           N  
ANISOU 4032  N   MET B  94     5410   9025   5911    292   -852   3144       N  
ATOM   4033  CA  MET B  94      75.890  50.556-118.028  1.00 55.58           C  
ANISOU 4033  CA  MET B  94     5661   9465   5991    225   -762   3076       C  
ATOM   4034  C   MET B  94      75.126  49.950-119.197  1.00 58.80           C  
ANISOU 4034  C   MET B  94     6063  10032   6247    240   -757   3038       C  
ATOM   4035  O   MET B  94      75.742  49.465-120.154  1.00 53.87           O  
ANISOU 4035  O   MET B  94     5437   9548   5484    181   -695   3054       O  
ATOM   4036  CB  MET B  94      76.178  49.490-116.976  1.00 52.91           C  
ANISOU 4036  CB  MET B  94     5312   9154   5637    225   -716   2894       C  
ATOM   4037  CG  MET B  94      77.057  49.967-115.834  1.00 54.91           C  
ANISOU 4037  CG  MET B  94     5583   9226   6053    184   -688   2849       C  
ATOM   4038  SD  MET B  94      77.338  48.656-114.635  1.00 57.75           S  
ANISOU 4038  SD  MET B  94     5941   9602   6401    179   -624   2600       S  
ATOM   4039  CE  MET B  94      77.977  47.377-115.706  1.00 46.45           C  
ANISOU 4039  CE  MET B  94     4485   8414   4749    136   -546   2592       C  
ATOM   4040  N   LEU B  95      73.791  49.973-119.140  1.00 60.40           N  
ANISOU 4040  N   LEU B  95     6256  10217   6475    319   -824   2986       N  
ATOM   4041  CA  LEU B  95      72.990  49.439-120.236  1.00 59.65           C  
ANISOU 4041  CA  LEU B  95     6151  10269   6242    330   -834   2954       C  
ATOM   4042  C   LEU B  95      73.178  50.242-121.520  1.00 51.58           C  
ANISOU 4042  C   LEU B  95     5144   9281   5172    299   -854   3136       C  
ATOM   4043  O   LEU B  95      73.137  49.670-122.614  1.00 49.05           O  
ANISOU 4043  O   LEU B  95     4821   9124   4693    267   -828   3123       O  
ATOM   4044  CB  LEU B  95      71.514  49.409-119.839  1.00 58.80           C  
ANISOU 4044  CB  LEU B  95     6021  10126   6194    420   -909   2873       C  
ATOM   4045  CG  LEU B  95      70.957  48.065-119.368  1.00 60.17           C  
ANISOU 4045  CG  LEU B  95     6172  10393   6296    434   -879   2664       C  
ATOM   4046  CD1 LEU B  95      71.877  47.429-118.340  1.00 64.07           C  
ANISOU 4046  CD1 LEU B  95     6673  10863   6807    401   -810   2564       C  
ATOM   4047  CD2 LEU B  95      69.559  48.248-118.798  1.00 62.08           C  
ANISOU 4047  CD2 LEU B  95     6381  10575   6634    523   -953   2601       C  
ATOM   4048  N   GLU B  96      73.387  51.555-121.409  1.00 51.60           N  
ANISOU 4048  N   GLU B  96     5163   9130   5311    304   -900   3304       N  
ATOM   4049  CA  GLU B  96      73.547  52.408-122.579  1.00 51.58           C  
ANISOU 4049  CA  GLU B  96     5178   9142   5277    273   -923   3491       C  
ATOM   4050  C   GLU B  96      74.969  52.418-123.122  1.00 61.17           C  
ANISOU 4050  C   GLU B  96     6402  10422   6418    170   -839   3574       C  
ATOM   4051  O   GLU B  96      75.157  52.527-124.342  1.00 69.22           O  
ANISOU 4051  O   GLU B  96     7426  11555   7319    127   -825   3668       O  
ATOM   4052  CB  GLU B  96      73.115  53.839-122.247  1.00 56.52           C  
ANISOU 4052  CB  GLU B  96     5819   9559   6097    327  -1012   3639       C  
ATOM   4053  CG  GLU B  96      71.618  54.030-122.286  1.00 68.48           C  
ANISOU 4053  CG  GLU B  96     7316  11046   7656    431  -1105   3611       C  
ATOM   4054  CD  GLU B  96      71.173  55.266-121.546  1.00 78.94           C  
ANISOU 4054  CD  GLU B  96     8647  12137   9211    506  -1184   3700       C  
ATOM   4055  OE1 GLU B  96      70.865  55.151-120.342  1.00 77.33           O  
ANISOU 4055  OE1 GLU B  96     8423  11833   9124    562  -1195   3586       O  
ATOM   4056  OE2 GLU B  96      71.136  56.350-122.166  1.00 86.37           O  
ANISOU 4056  OE2 GLU B  96     9608  12990  10217    511  -1235   3880       O  
ATOM   4057  N   LEU B  97      75.975  52.325-122.249  1.00 59.16           N  
ANISOU 4057  N   LEU B  97     6145  10102   6229    127   -784   3546       N  
ATOM   4058  CA  LEU B  97      77.345  52.162-122.725  1.00 59.22           C  
ANISOU 4058  CA  LEU B  97     6146  10194   6160     29   -694   3599       C  
ATOM   4059  C   LEU B  97      77.500  50.860-123.500  1.00 63.05           C  
ANISOU 4059  C   LEU B  97     6611  10905   6440      6   -621   3473       C  
ATOM   4060  O   LEU B  97      78.198  50.812-124.520  1.00 69.40           O  
ANISOU 4060  O   LEU B  97     7409  11830   7132    -57   -566   3540       O  
ATOM   4061  CB  LEU B  97      78.317  52.211-121.550  1.00 57.35           C  
ANISOU 4061  CB  LEU B  97     5903   9851   6036     -7   -656   3575       C  
ATOM   4062  CG  LEU B  97      78.554  53.597-120.956  1.00 56.58           C  
ANISOU 4062  CG  LEU B  97     5827   9531   6141    -18   -712   3731       C  
ATOM   4063  CD1 LEU B  97      79.001  53.482-119.513  1.00 54.58           C  
ANISOU 4063  CD1 LEU B  97     5568   9161   6008    -17   -709   3651       C  
ATOM   4064  CD2 LEU B  97      79.585  54.349-121.782  1.00 54.37           C  
ANISOU 4064  CD2 LEU B  97     5548   9254   5855   -115   -673   3912       C  
ATOM   4065  N   ASP B  98      76.853  49.791-123.030  1.00 59.09           N  
ANISOU 4065  N   ASP B  98     6099  10460   5892     55   -618   3285       N  
ATOM   4066  CA  ASP B  98      76.852  48.538-123.777  1.00 58.50           C  
ANISOU 4066  CA  ASP B  98     6009  10583   5635     40   -560   3155       C  
ATOM   4067  C   ASP B  98      76.032  48.665-125.056  1.00 66.26           C  
ANISOU 4067  C   ASP B  98     6999  11673   6505     52   -605   3209       C  
ATOM   4068  O   ASP B  98      76.433  48.163-126.113  1.00 68.84           O  
ANISOU 4068  O   ASP B  98     7318  12161   6676      7   -553   3202       O  
ATOM   4069  CB  ASP B  98      76.330  47.410-122.888  1.00 58.06           C  
ANISOU 4069  CB  ASP B  98     5945  10539   5578     86   -551   2948       C  
ATOM   4070  CG  ASP B  98      75.812  46.234-123.681  1.00 69.87           C  
ANISOU 4070  CG  ASP B  98     7431  12209   6909     91   -528   2813       C  
ATOM   4071  OD1 ASP B  98      76.629  45.399-124.125  1.00 67.80           O  
ANISOU 4071  OD1 ASP B  98     7156  12068   6536     48   -445   2745       O  
ATOM   4072  OD2 ASP B  98      74.577  46.142-123.849  1.00 75.89           O  
ANISOU 4072  OD2 ASP B  98     8193  12983   7658    139   -596   2772       O  
ATOM   4073  N   GLY B  99      74.881  49.329-124.979  1.00 65.54           N  
ANISOU 4073  N   GLY B  99     6918  11495   6489    113   -703   3261       N  
ATOM   4074  CA  GLY B  99      74.143  49.739-126.154  1.00 70.30           C  
ANISOU 4074  CA  GLY B  99     7528  12173   7011    124   -763   3358       C  
ATOM   4075  C   GLY B  99      73.398  48.652-126.895  1.00 70.71           C  
ANISOU 4075  C   GLY B  99     7566  12402   6897    135   -765   3225       C  
ATOM   4076  O   GLY B  99      72.707  48.964-127.871  1.00 77.36           O  
ANISOU 4076  O   GLY B  99     8413  13316   7666    146   -826   3302       O  
ATOM   4077  N   THR B 100      73.512  47.394-126.486  1.00 68.18           N  
ANISOU 4077  N   THR B 100     7231  12156   6518    130   -706   3033       N  
ATOM   4078  CA  THR B 100      72.781  46.320-127.138  1.00 72.35           C  
ANISOU 4078  CA  THR B 100     7747  12842   6901    135   -711   2896       C  
ATOM   4079  C   THR B 100      71.736  45.741-126.193  1.00 73.76           C  
ANISOU 4079  C   THR B 100     7909  12965   7150    195   -752   2746       C  
ATOM   4080  O   THR B 100      71.825  45.869-124.968  1.00 73.66           O  
ANISOU 4080  O   THR B 100     7895  12817   7274    223   -748   2708       O  
ATOM   4081  CB  THR B 100      73.723  45.214-127.633  1.00 80.68           C  
ANISOU 4081  CB  THR B 100     8797  14047   7810     77   -606   2787       C  
ATOM   4082  OG1 THR B 100      72.950  44.117-128.137  1.00 88.08           O  
ANISOU 4082  OG1 THR B 100     9725  15118   8624     84   -616   2635       O  
ATOM   4083  CG2 THR B 100      74.611  44.718-126.524  1.00 76.48           C  
ANISOU 4083  CG2 THR B 100     8259  13444   7356     69   -531   2695       C  
ATOM   4084  N   GLU B 101      70.735  45.093-126.791  1.00 72.49           N  
ANISOU 4084  N   GLU B 101     7735  12917   6891    209   -793   2659       N  
ATOM   4085  CA  GLU B 101      69.562  44.660-126.041  1.00 74.35           C  
ANISOU 4085  CA  GLU B 101     7946  13109   7193    264   -845   2537       C  
ATOM   4086  C   GLU B 101      69.855  43.449-125.160  1.00 71.52           C  
ANISOU 4086  C   GLU B 101     7583  12756   6838    252   -773   2345       C  
ATOM   4087  O   GLU B 101      69.320  43.347-124.050  1.00 71.08           O  
ANISOU 4087  O   GLU B 101     7513  12599   6895    294   -794   2270       O  
ATOM   4088  CB  GLU B 101      68.414  44.362-127.009  1.00 76.63           C  
ANISOU 4088  CB  GLU B 101     8216  13523   7376    274   -916   2512       C  
ATOM   4089  CG  GLU B 101      67.039  44.340-126.364  1.00 79.20           C  
ANISOU 4089  CG  GLU B 101     8507  13790   7796    339   -997   2445       C  
ATOM   4090  CD  GLU B 101      66.683  42.983-125.792  1.00 84.31           C  
ANISOU 4090  CD  GLU B 101     9134  14487   8415    327   -958   2231       C  
ATOM   4091  OE1 GLU B 101      67.349  41.992-126.159  1.00 87.61           O  
ANISOU 4091  OE1 GLU B 101     9565  15007   8714    271   -883   2133       O  
ATOM   4092  OE2 GLU B 101      65.738  42.907-124.978  1.00 84.44           O  
ANISOU 4092  OE2 GLU B 101     9116  14436   8530    375  -1002   2161       O  
ATOM   4093  N   ASN B 102      70.693  42.522-125.629  1.00 65.67           N  
ANISOU 4093  N   ASN B 102     6850  12128   5974    198   -690   2264       N  
ATOM   4094  CA  ASN B 102      70.992  41.298-124.896  1.00 52.25           C  
ANISOU 4094  CA  ASN B 102     5146  10438   4268    187   -624   2083       C  
ATOM   4095  C   ASN B 102      72.352  41.339-124.208  1.00 47.17           C  
ANISOU 4095  C   ASN B 102     4516   9726   3681    167   -543   2100       C  
ATOM   4096  O   ASN B 102      72.874  40.286-123.824  1.00 46.03           O  
ANISOU 4096  O   ASN B 102     4372   9612   3506    151   -475   1966       O  
ATOM   4097  CB  ASN B 102      70.909  40.087-125.828  1.00 56.59           C  
ANISOU 4097  CB  ASN B 102     5693  11157   4652    150   -590   1953       C  
ATOM   4098  CG  ASN B 102      71.854  40.194-127.011  1.00 56.50           C  
ANISOU 4098  CG  ASN B 102     5694  11260   4513    102   -540   2026       C  
ATOM   4099  OD1 ASN B 102      72.434  41.250-127.263  1.00 59.48           O  
ANISOU 4099  OD1 ASN B 102     6080  11600   4920     94   -541   2191       O  
ATOM   4100  ND2 ASN B 102      72.003  39.100-127.752  1.00 54.25           N  
ANISOU 4100  ND2 ASN B 102     5410  11117   4088     69   -495   1899       N  
ATOM   4101  N   LYS B 103      72.932  42.530-124.047  1.00 52.61           N  
ANISOU 4101  N   LYS B 103     5215  10321   4454    167   -552   2263       N  
ATOM   4102  CA  LYS B 103      74.231  42.703-123.387  1.00 53.54           C  
ANISOU 4102  CA  LYS B 103     5338  10369   4634    142   -485   2297       C  
ATOM   4103  C   LYS B 103      75.308  41.834-124.034  1.00 51.03           C  
ANISOU 4103  C   LYS B 103     5016  10181   4193     93   -389   2236       C  
ATOM   4104  O   LYS B 103      76.107  41.192-123.350  1.00 43.34           O  
ANISOU 4104  O   LYS B 103     4036   9189   3241     84   -324   2153       O  
ATOM   4105  CB  LYS B 103      74.128  42.424-121.885  1.00 59.92           C  
ANISOU 4105  CB  LYS B 103     6147  11056   5566    175   -486   2204       C  
ATOM   4106  CG  LYS B 103      73.412  43.517-121.114  1.00 56.52           C  
ANISOU 4106  CG  LYS B 103     5718  10473   5284    223   -568   2286       C  
ATOM   4107  CD  LYS B 103      72.424  42.952-120.119  1.00 56.61           C  
ANISOU 4107  CD  LYS B 103     5718  10434   5356    270   -600   2146       C  
ATOM   4108  CE  LYS B 103      71.512  44.050-119.607  1.00 62.24           C  
ANISOU 4108  CE  LYS B 103     6424  11022   6203    329   -688   2222       C  
ATOM   4109  NZ  LYS B 103      70.322  43.498-118.912  1.00 56.50           N  
ANISOU 4109  NZ  LYS B 103     5672  10281   5514    376   -723   2088       N  
ATOM   4110  N   SER B 104      75.334  41.820-125.368  1.00 51.35           N  
ANISOU 4110  N   SER B 104     5056  10355   4101     64   -382   2277       N  
ATOM   4111  CA  SER B 104      76.247  40.971-126.123  1.00 49.09           C  
ANISOU 4111  CA  SER B 104     4762  10206   3685     23   -293   2207       C  
ATOM   4112  C   SER B 104      77.587  41.632-126.422  1.00 50.51           C  
ANISOU 4112  C   SER B 104     4933  10389   3868    -21   -231   2337       C  
ATOM   4113  O   SER B 104      78.532  40.927-126.794  1.00 49.42           O  
ANISOU 4113  O   SER B 104     4782  10344   3651    -48   -144   2271       O  
ATOM   4114  CB  SER B 104      75.592  40.531-127.437  1.00 51.68           C  
ANISOU 4114  CB  SER B 104     5094  10691   3853      9   -313   2167       C  
ATOM   4115  OG  SER B 104      75.090  41.645-128.157  1.00 57.78           O  
ANISOU 4115  OG  SER B 104     5874  11468   4613      6   -384   2334       O  
ATOM   4116  N   LYS B 105      77.700  42.953-126.271  1.00 52.39           N  
ANISOU 4116  N   LYS B 105     5178  10528   4201    -28   -273   2518       N  
ATOM   4117  CA  LYS B 105      78.981  43.608-126.518  1.00 53.60           C  
ANISOU 4117  CA  LYS B 105     5318  10679   4368    -79   -214   2648       C  
ATOM   4118  C   LYS B 105      79.913  43.464-125.319  1.00 60.52           C  
ANISOU 4118  C   LYS B 105     6178  11459   5359    -83   -164   2615       C  
ATOM   4119  O   LYS B 105      80.983  42.855-125.420  1.00 67.01           O  
ANISOU 4119  O   LYS B 105     6975  12349   6136   -111    -75   2561       O  
ATOM   4120  CB  LYS B 105      78.776  45.086-126.859  1.00 54.31           C  
ANISOU 4120  CB  LYS B 105     5423  10694   4520    -93   -280   2862       C  
ATOM   4121  CG  LYS B 105      80.027  45.733-127.443  1.00 57.43           C  
ANISOU 4121  CG  LYS B 105     5804  11120   4895   -161   -218   3005       C  
ATOM   4122  CD  LYS B 105      79.759  47.131-127.958  1.00 59.20           C  
ANISOU 4122  CD  LYS B 105     6049  11280   5163   -179   -285   3220       C  
ATOM   4123  CE  LYS B 105      79.487  48.093-126.823  1.00 61.10           C  
ANISOU 4123  CE  LYS B 105     6304  11310   5603   -152   -351   3305       C  
ATOM   4124  NZ  LYS B 105      79.021  49.401-127.345  1.00 64.64           N  
ANISOU 4124  NZ  LYS B 105     6777  11683   6100   -155   -429   3502       N  
ATOM   4125  N   PHE B 106      79.520  44.025-124.174  1.00 64.08           N  
ANISOU 4125  N   PHE B 106     6640  11749   5957    -54   -222   2645       N  
ATOM   4126  CA  PHE B 106      80.332  43.899-122.972  1.00 52.84           C  
ANISOU 4126  CA  PHE B 106     5203  10233   4639    -58   -186   2613       C  
ATOM   4127  C   PHE B 106      80.190  42.527-122.336  1.00 49.85           C  
ANISOU 4127  C   PHE B 106     4821   9887   4232    -24   -152   2412       C  
ATOM   4128  O   PHE B 106      81.132  42.028-121.717  1.00 49.69           O  
ANISOU 4128  O   PHE B 106     4781   9860   4239    -36    -91   2360       O  
ATOM   4129  CB  PHE B 106      79.955  44.984-121.966  1.00 49.13           C  
ANISOU 4129  CB  PHE B 106     4752   9580   4335    -39   -263   2710       C  
ATOM   4130  CG  PHE B 106      80.281  46.379-122.418  1.00 55.37           C  
ANISOU 4130  CG  PHE B 106     5548  10305   5184    -79   -292   2918       C  
ATOM   4131  CD1 PHE B 106      79.695  47.472-121.804  1.00 62.28           C  
ANISOU 4131  CD1 PHE B 106     6447  11016   6201    -53   -378   3018       C  
ATOM   4132  CD2 PHE B 106      81.182  46.602-123.450  1.00 51.87           C  
ANISOU 4132  CD2 PHE B 106     5087   9961   4663   -141   -232   3013       C  
ATOM   4133  CE1 PHE B 106      79.993  48.759-122.209  1.00 61.32           C  
ANISOU 4133  CE1 PHE B 106     6335  10817   6148    -90   -407   3213       C  
ATOM   4134  CE2 PHE B 106      81.483  47.889-123.859  1.00 53.93           C  
ANISOU 4134  CE2 PHE B 106     5354  10153   4983   -184   -258   3211       C  
ATOM   4135  CZ  PHE B 106      80.886  48.968-123.239  1.00 56.40           C  
ANISOU 4135  CZ  PHE B 106     5694  10290   5443   -159   -347   3313       C  
ATOM   4136  N   GLY B 107      79.036  41.902-122.483  1.00 49.13           N  
ANISOU 4136  N   GLY B 107     4746   9831   4089     15   -193   2302       N  
ATOM   4137  CA  GLY B 107      78.763  40.608-121.884  1.00 49.83           C  
ANISOU 4137  CA  GLY B 107     4836   9940   4157     45   -169   2114       C  
ATOM   4138  C   GLY B 107      77.846  40.764-120.682  1.00 50.17           C  
ANISOU 4138  C   GLY B 107     4896   9854   4314     89   -240   2075       C  
ATOM   4139  O   GLY B 107      77.965  41.720-119.901  1.00 46.17           O  
ANISOU 4139  O   GLY B 107     4393   9219   3928     94   -278   2171       O  
ATOM   4140  N   ALA B 108      76.913  39.827-120.535  1.00 39.71           N  
ANISOU 4140  N   ALA B 108     3577   8559   2951    118   -257   1930       N  
ATOM   4141  CA  ALA B 108      76.035  39.839-119.366  1.00 47.63           C  
ANISOU 4141  CA  ALA B 108     4589   9452   4056    158   -315   1872       C  
ATOM   4142  C   ALA B 108      76.811  39.557-118.087  1.00 44.05           C  
ANISOU 4142  C   ALA B 108     4138   8914   3685    160   -283   1830       C  
ATOM   4143  O   ALA B 108      76.429  40.031-117.011  1.00 42.52           O  
ANISOU 4143  O   ALA B 108     3951   8602   3603    186   -333   1837       O  
ATOM   4144  CB  ALA B 108      74.907  38.821-119.540  1.00 45.08           C  
ANISOU 4144  CB  ALA B 108     4266   9193   3669    177   -334   1724       C  
ATOM   4145  N   ASN B 109      77.900  38.790-118.190  1.00 44.67           N  
ANISOU 4145  N   ASN B 109     4208   9055   3709    136   -203   1784       N  
ATOM   4146  CA  ASN B 109      78.745  38.533-117.028  1.00 43.40           C  
ANISOU 4146  CA  ASN B 109     4048   8807   3636    135   -171   1748       C  
ATOM   4147  C   ASN B 109      79.478  39.795-116.589  1.00 42.58           C  
ANISOU 4147  C   ASN B 109     3937   8593   3649    112   -187   1885       C  
ATOM   4148  O   ASN B 109      79.644  40.037-115.389  1.00 46.78           O  
ANISOU 4148  O   ASN B 109     4478   8978   4316    116   -204   1853       O  
ATOM   4149  CB  ASN B 109      79.734  37.411-117.344  1.00 42.50           C  
ANISOU 4149  CB  ASN B 109     3918   8778   3452    121    -77   1661       C  
ATOM   4150  CG  ASN B 109      80.329  37.536-118.734  1.00 42.82           C  
ANISOU 4150  CG  ASN B 109     3937   8963   3371     92    -26   1731       C  
ATOM   4151  OD1 ASN B 109      80.163  38.560-119.398  1.00 40.12           O  
ANISOU 4151  OD1 ASN B 109     3593   8624   3027     73    -59   1856       O  
ATOM   4152  ND2 ASN B 109      81.025  36.496-119.180  1.00 37.68           N  
ANISOU 4152  ND2 ASN B 109     3270   8404   2643     88     59   1637       N  
ATOM   4153  N   ALA B 110      79.917  40.617-117.544  1.00 44.13           N  
ANISOU 4153  N   ALA B 110     4120   8857   3792     82   -182   2040       N  
ATOM   4154  CA  ALA B 110      80.620  41.843-117.182  1.00 46.58           C  
ANISOU 4154  CA  ALA B 110     4423   9054   4219     50   -198   2177       C  
ATOM   4155  C   ALA B 110      79.685  42.838-116.508  1.00 50.47           C  
ANISOU 4155  C   ALA B 110     4941   9397   4836     79   -290   2219       C  
ATOM   4156  O   ALA B 110      80.048  43.456-115.501  1.00 53.86           O  
ANISOU 4156  O   ALA B 110     5379   9673   5413     69   -308   2225       O  
ATOM   4157  CB  ALA B 110      81.264  42.467-118.418  1.00 39.94           C  
ANISOU 4157  CB  ALA B 110     3563   8312   3300      4   -166   2331       C  
ATOM   4158  N   ILE B 111      78.476  43.003-117.046  1.00 49.44           N  
ANISOU 4158  N   ILE B 111     4820   9313   4650    118   -350   2241       N  
ATOM   4159  CA  ILE B 111      77.557  44.002-116.515  1.00 47.57           C  
ANISOU 4159  CA  ILE B 111     4598   8940   4535    156   -435   2288       C  
ATOM   4160  C   ILE B 111      77.009  43.567-115.160  1.00 43.02           C  
ANISOU 4160  C   ILE B 111     4035   8250   4063    191   -448   2126       C  
ATOM   4161  O   ILE B 111      76.893  44.380-114.233  1.00 43.08           O  
ANISOU 4161  O   ILE B 111     4055   8097   4216    203   -484   2133       O  
ATOM   4162  CB  ILE B 111      76.436  44.285-117.533  1.00 48.12           C  
ANISOU 4162  CB  ILE B 111     4669   9067   4546    185   -483   2330       C  
ATOM   4163  CG1 ILE B 111      77.001  45.074-118.712  1.00 50.83           C  
ANISOU 4163  CG1 ILE B 111     5013   9453   4848    141   -471   2494       C  
ATOM   4164  CG2 ILE B 111      75.294  45.058-116.899  1.00 43.08           C  
ANISOU 4164  CG2 ILE B 111     4034   8309   4026    246   -572   2345       C  
ATOM   4165  CD1 ILE B 111      75.953  45.613-119.656  1.00 56.02           C  
ANISOU 4165  CD1 ILE B 111     5675  10136   5475    168   -531   2562       C  
ATOM   4166  N   LEU B 112      76.677  42.283-115.014  1.00 36.71           N  
ANISOU 4166  N   LEU B 112     3232   7527   3187    203   -415   1976       N  
ATOM   4167  CA  LEU B 112      76.121  41.824-113.746  1.00 38.60           C  
ANISOU 4167  CA  LEU B 112     3485   7669   3512    230   -423   1832       C  
ATOM   4168  C   LEU B 112      77.147  41.926-112.624  1.00 38.59           C  
ANISOU 4168  C   LEU B 112     3498   7548   3617    201   -391   1799       C  
ATOM   4169  O   LEU B 112      76.809  42.332-111.506  1.00 42.42           O  
ANISOU 4169  O   LEU B 112     4000   7904   4215    217   -419   1750       O  
ATOM   4170  CB  LEU B 112      75.608  40.392-113.876  1.00 39.18           C  
ANISOU 4170  CB  LEU B 112     3555   7847   3486    238   -392   1690       C  
ATOM   4171  CG  LEU B 112      75.035  39.840-112.571  1.00 40.34           C  
ANISOU 4171  CG  LEU B 112     3715   7902   3710    256   -392   1549       C  
ATOM   4172  CD1 LEU B 112      73.823  40.650-112.147  1.00 43.76           C  
ANISOU 4172  CD1 LEU B 112     4141   8261   4224    299   -458   1558       C  
ATOM   4173  CD2 LEU B 112      74.688  38.369-112.684  1.00 44.01           C  
ANISOU 4173  CD2 LEU B 112     4181   8455   4088    252   -355   1415       C  
ATOM   4174  N   GLY B 113      78.404  41.575-112.909  1.00 42.04           N  
ANISOU 4174  N   GLY B 113     3924   8033   4017    159   -334   1823       N  
ATOM   4175  CA  GLY B 113      79.440  41.654-111.889  1.00 42.26           C  
ANISOU 4175  CA  GLY B 113     3954   7961   4141    129   -312   1798       C  
ATOM   4176  C   GLY B 113      79.530  43.024-111.250  1.00 41.44           C  
ANISOU 4176  C   GLY B 113     3864   7709   4174    117   -362   1874       C  
ATOM   4177  O   GLY B 113      79.539  43.154-110.026  1.00 37.62           O  
ANISOU 4177  O   GLY B 113     3399   7111   3786    117   -379   1800       O  
ATOM   4178  N   VAL B 114      79.582  44.071-112.076  1.00 44.18           N  
ANISOU 4178  N   VAL B 114     4203   8053   4530    104   -387   2022       N  
ATOM   4179  CA  VAL B 114      79.580  45.430-111.546  1.00 42.39           C  
ANISOU 4179  CA  VAL B 114     3992   7668   4446     94   -439   2095       C  
ATOM   4180  C   VAL B 114      78.270  45.723-110.822  1.00 45.29           C  
ANISOU 4180  C   VAL B 114     4383   7942   4882    156   -493   2018       C  
ATOM   4181  O   VAL B 114      78.266  46.334-109.746  1.00 47.56           O  
ANISOU 4181  O   VAL B 114     4691   8085   5293    155   -519   1973       O  
ATOM   4182  CB  VAL B 114      79.840  46.440-112.677  1.00 44.74           C  
ANISOU 4182  CB  VAL B 114     4280   7984   4737     68   -455   2285       C  
ATOM   4183  CG1 VAL B 114      79.919  47.850-112.121  1.00 42.54           C  
ANISOU 4183  CG1 VAL B 114     4020   7520   4623     54   -508   2361       C  
ATOM   4184  CG2 VAL B 114      81.111  46.079-113.421  1.00 47.00           C  
ANISOU 4184  CG2 VAL B 114     4533   8384   4940      6   -388   2353       C  
ATOM   4185  N   SER B 115      77.141  45.287-111.391  1.00 40.97           N  
ANISOU 4185  N   SER B 115     3828   7482   4255    207   -510   1994       N  
ATOM   4186  CA  SER B 115      75.841  45.586-110.798  1.00 44.29           C  
ANISOU 4186  CA  SER B 115     4256   7830   4743    269   -558   1927       C  
ATOM   4187  C   SER B 115      75.714  44.982-109.403  1.00 45.63           C  
ANISOU 4187  C   SER B 115     4443   7936   4958    273   -536   1762       C  
ATOM   4188  O   SER B 115      75.186  45.622-108.486  1.00 45.36           O  
ANISOU 4188  O   SER B 115     4423   7779   5031    301   -564   1712       O  
ATOM   4189  CB  SER B 115      74.723  45.078-111.716  1.00 44.78           C  
ANISOU 4189  CB  SER B 115     4293   8023   4699    314   -578   1928       C  
ATOM   4190  OG  SER B 115      73.435  45.445-111.244  1.00 45.56           O  
ANISOU 4190  OG  SER B 115     4382   8059   4869    378   -626   1877       O  
ATOM   4191  N   LEU B 116      76.206  43.755-109.222  1.00 44.79           N  
ANISOU 4191  N   LEU B 116     4338   7912   4770    246   -484   1677       N  
ATOM   4192  CA  LEU B 116      76.161  43.124-107.908  1.00 41.86           C  
ANISOU 4192  CA  LEU B 116     3986   7488   4429    243   -463   1537       C  
ATOM   4193  C   LEU B 116      77.044  43.865-106.911  1.00 45.26           C  
ANISOU 4193  C   LEU B 116     4440   7791   4968    208   -472   1539       C  
ATOM   4194  O   LEU B 116      76.619  44.157-105.787  1.00 45.19           O  
ANISOU 4194  O   LEU B 116     4453   7687   5030    221   -488   1455       O  
ATOM   4195  CB  LEU B 116      76.587  41.662-108.018  1.00 40.25           C  
ANISOU 4195  CB  LEU B 116     3779   7391   4123    223   -410   1466       C  
ATOM   4196  CG  LEU B 116      75.715  40.724-108.848  1.00 37.04           C  
ANISOU 4196  CG  LEU B 116     3356   7109   3608    248   -398   1426       C  
ATOM   4197  CD1 LEU B 116      76.358  39.347-108.913  1.00 33.92           C  
ANISOU 4197  CD1 LEU B 116     2963   6791   3135    224   -341   1356       C  
ATOM   4198  CD2 LEU B 116      74.313  40.645-108.267  1.00 36.78           C  
ANISOU 4198  CD2 LEU B 116     3323   7051   3602    287   -422   1339       C  
ATOM   4199  N   ALA B 117      78.281  44.177-107.306  1.00 42.34           N  
ANISOU 4199  N   ALA B 117     4060   7422   4606    159   -461   1630       N  
ATOM   4200  CA  ALA B 117      79.195  44.871-106.404  1.00 40.57           C  
ANISOU 4200  CA  ALA B 117     3850   7082   4484    113   -475   1633       C  
ATOM   4201  C   ALA B 117      78.692  46.265-106.057  1.00 41.56           C  
ANISOU 4201  C   ALA B 117     3996   7065   4732    128   -527   1663       C  
ATOM   4202  O   ALA B 117      78.945  46.759-104.952  1.00 45.42           O  
ANISOU 4202  O   ALA B 117     4509   7441   5309    107   -546   1601       O  
ATOM   4203  CB  ALA B 117      80.590  44.949-107.027  1.00 44.89           C  
ANISOU 4203  CB  ALA B 117     4367   7671   5019     54   -451   1734       C  
ATOM   4204  N   VAL B 118      77.988  46.915-106.986  1.00 41.99           N  
ANISOU 4204  N   VAL B 118     4039   7119   4794    165   -553   1757       N  
ATOM   4205  CA  VAL B 118      77.370  48.204-106.691  1.00 45.30           C  
ANISOU 4205  CA  VAL B 118     4476   7392   5342    196   -604   1783       C  
ATOM   4206  C   VAL B 118      76.296  48.044-105.625  1.00 49.61           C  
ANISOU 4206  C   VAL B 118     5039   7888   5923    250   -610   1632       C  
ATOM   4207  O   VAL B 118      76.132  48.902-104.748  1.00 53.97           O  
ANISOU 4207  O   VAL B 118     5615   8299   6591    259   -634   1581       O  
ATOM   4208  CB  VAL B 118      76.799  48.824-107.981  1.00 46.38           C  
ANISOU 4208  CB  VAL B 118     4595   7555   5473    232   -635   1928       C  
ATOM   4209  CG1 VAL B 118      75.784  49.905-107.653  1.00 43.95           C  
ANISOU 4209  CG1 VAL B 118     4298   7108   5294    296   -688   1927       C  
ATOM   4210  CG2 VAL B 118      77.919  49.388-108.832  1.00 46.94           C  
ANISOU 4210  CG2 VAL B 118     4657   7629   5548    167   -632   2091       C  
ATOM   4211  N   CYS B 119      75.560  46.934-105.674  1.00 47.68           N  
ANISOU 4211  N   CYS B 119     4781   7760   5578    283   -584   1553       N  
ATOM   4212  CA  CYS B 119      74.470  46.723-104.730  1.00 45.90           C  
ANISOU 4212  CA  CYS B 119     4561   7505   5374    331   -581   1416       C  
ATOM   4213  C   CYS B 119      74.996  46.487-103.319  1.00 44.09           C  
ANISOU 4213  C   CYS B 119     4367   7219   5167    292   -559   1297       C  
ATOM   4214  O   CYS B 119      74.494  47.073-102.352  1.00 41.97           O  
ANISOU 4214  O   CYS B 119     4118   6852   4977    314   -569   1211       O  
ATOM   4215  CB  CYS B 119      73.608  45.551-105.191  1.00 47.66           C  
ANISOU 4215  CB  CYS B 119     4756   7871   5483    361   -557   1369       C  
ATOM   4216  SG  CYS B 119      71.971  45.548-104.458  1.00 47.28           S  
ANISOU 4216  SG  CYS B 119     4689   7803   5474    431   -560   1246       S  
ATOM   4217  N   LYS B 120      76.005  45.621-103.180  1.00 43.55           N  
ANISOU 4217  N   LYS B 120     4305   7214   5027    236   -531   1289       N  
ATOM   4218  CA  LYS B 120      76.617  45.395-101.875  1.00 44.21           C  
ANISOU 4218  CA  LYS B 120     4421   7253   5123    194   -522   1195       C  
ATOM   4219  C   LYS B 120      77.194  46.684-101.305  1.00 44.93           C  
ANISOU 4219  C   LYS B 120     4536   7203   5334    163   -560   1207       C  
ATOM   4220  O   LYS B 120      77.073  46.951-100.104  1.00 49.28           O  
ANISOU 4220  O   LYS B 120     5118   7682   5923    155   -566   1101       O  
ATOM   4221  CB  LYS B 120      77.707  44.327-101.982  1.00 43.54           C  
ANISOU 4221  CB  LYS B 120     4329   7257   4957    146   -495   1211       C  
ATOM   4222  CG  LYS B 120      77.204  42.988-102.482  1.00 42.57           C  
ANISOU 4222  CG  LYS B 120     4191   7260   4725    170   -456   1183       C  
ATOM   4223  CD  LYS B 120      78.305  41.943-102.478  1.00 45.90           C  
ANISOU 4223  CD  LYS B 120     4606   7749   5085    131   -428   1187       C  
ATOM   4224  CE  LYS B 120      77.783  40.607-102.981  1.00 51.61           C  
ANISOU 4224  CE  LYS B 120     5320   8580   5711    154   -389   1149       C  
ATOM   4225  NZ  LYS B 120      78.853  39.574-103.028  1.00 51.32           N  
ANISOU 4225  NZ  LYS B 120     5274   8598   5628    129   -359   1152       N  
ATOM   4226  N   ALA B 121      77.825  47.498-102.154  1.00 45.41           N  
ANISOU 4226  N   ALA B 121     4582   7222   5451    141   -583   1335       N  
ATOM   4227  CA  ALA B 121      78.357  48.771-101.687  1.00 49.22           C  
ANISOU 4227  CA  ALA B 121     5085   7555   6060    105   -621   1351       C  
ATOM   4228  C   ALA B 121      77.246  49.748-101.334  1.00 46.40           C  
ANISOU 4228  C   ALA B 121     4748   7077   5805    166   -646   1301       C  
ATOM   4229  O   ALA B 121      77.402  50.560-100.415  1.00 44.15           O  
ANISOU 4229  O   ALA B 121     4495   6665   5616    147   -668   1230       O  
ATOM   4230  CB  ALA B 121      79.283  49.372-102.746  1.00 48.41           C  
ANISOU 4230  CB  ALA B 121     4959   7440   5995     58   -635   1514       C  
ATOM   4231  N   GLY B 122      76.123  49.694-102.052  1.00 47.62           N  
ANISOU 4231  N   GLY B 122     4879   7272   5943    242   -644   1331       N  
ATOM   4232  CA  GLY B 122      75.011  50.569-101.725  1.00 42.99           C  
ANISOU 4232  CA  GLY B 122     4298   6576   5460    314   -665   1280       C  
ATOM   4233  C   GLY B 122      74.397  50.249-100.377  1.00 45.82           C  
ANISOU 4233  C   GLY B 122     4678   6923   5809    334   -638   1097       C  
ATOM   4234  O   GLY B 122      73.984  51.151 -99.644  1.00 52.33           O  
ANISOU 4234  O   GLY B 122     5523   7618   6740    362   -650   1017       O  
ATOM   4235  N   ALA B 123      74.332  48.960-100.033  1.00 44.59           N  
ANISOU 4235  N   ALA B 123     4518   6899   5526    318   -598   1028       N  
ATOM   4236  CA  ALA B 123      73.781  48.560 -98.744  1.00 43.63           C  
ANISOU 4236  CA  ALA B 123     4418   6785   5375    326   -566    866       C  
ATOM   4237  C   ALA B 123      74.610  49.112 -97.592  1.00 48.03           C  
ANISOU 4237  C   ALA B 123     5025   7245   5979    267   -579    789       C  
ATOM   4238  O   ALA B 123      74.059  49.626 -96.612  1.00 52.04           O  
ANISOU 4238  O   ALA B 123     5557   7681   6536    290   -571    665       O  
ATOM   4239  CB  ALA B 123      73.698  47.036 -98.664  1.00 37.76           C  
ANISOU 4239  CB  ALA B 123     3665   6194   4488    308   -524    832       C  
ATOM   4240  N   ALA B 124      75.939  49.017 -97.690  1.00 47.53           N  
ANISOU 4240  N   ALA B 124     4973   7185   5901    191   -599    854       N  
ATOM   4241  CA  ALA B 124      76.794  49.580 -96.652  1.00 44.87           C  
ANISOU 4241  CA  ALA B 124     4677   6761   5610    126   -624    787       C  
ATOM   4242  C   ALA B 124      76.690  51.098 -96.602  1.00 48.76           C  
ANISOU 4242  C   ALA B 124     5188   7080   6260    138   -660    783       C  
ATOM   4243  O   ALA B 124      76.838  51.694 -95.528  1.00 52.22           O  
ANISOU 4243  O   ALA B 124     5666   7428   6748    111   -674    668       O  
ATOM   4244  CB  ALA B 124      78.243  49.150 -96.873  1.00 43.28           C  
ANISOU 4244  CB  ALA B 124     4467   6609   5369     43   -642    869       C  
ATOM   4245  N   GLU B 125      76.439  51.740 -97.744  1.00 52.23           N  
ANISOU 4245  N   GLU B 125     5601   7467   6779    176   -679    909       N  
ATOM   4246  CA  GLU B 125      76.220  53.183 -97.748  1.00 61.10           C  
ANISOU 4246  CA  GLU B 125     6741   8407   8067    200   -714    914       C  
ATOM   4247  C   GLU B 125      74.940  53.549 -97.006  1.00 61.96           C  
ANISOU 4247  C   GLU B 125     6860   8456   8225    284   -694    769       C  
ATOM   4248  O   GLU B 125      74.872  54.599 -96.359  1.00 62.00           O  
ANISOU 4248  O   GLU B 125     6899   8306   8354    290   -712    687       O  
ATOM   4249  CB  GLU B 125      76.174  53.700 -99.185  1.00 68.62           C  
ANISOU 4249  CB  GLU B 125     7661   9331   9081    227   -739   1100       C  
ATOM   4250  CG  GLU B 125      76.411  55.191 -99.322  1.00 74.90           C  
ANISOU 4250  CG  GLU B 125     8478   9923  10056    218   -785   1155       C  
ATOM   4251  CD  GLU B 125      77.789  55.590 -98.853  1.00 80.83           C  
ANISOU 4251  CD  GLU B 125     9257  10604  10851    102   -809   1156       C  
ATOM   4252  OE1 GLU B 125      77.889  56.493 -97.998  1.00 82.85           O  
ANISOU 4252  OE1 GLU B 125     9553  10703  11223     81   -832   1055       O  
ATOM   4253  OE2 GLU B 125      78.773  54.988 -99.330  1.00 80.32           O  
ANISOU 4253  OE2 GLU B 125     9169  10643  10705     30   -804   1251       O  
ATOM   4254  N   ARG B 126      73.920  52.698 -97.090  1.00 62.08           N  
ANISOU 4254  N   ARG B 126     6845   8593   8151    349   -654    730       N  
ATOM   4255  CA  ARG B 126      72.700  52.857 -96.314  1.00 68.10           C  
ANISOU 4255  CA  ARG B 126     7604   9332   8939    425   -621    581       C  
ATOM   4256  C   ARG B 126      72.832  52.321 -94.894  1.00 65.79           C  
ANISOU 4256  C   ARG B 126     7351   9088   8558    379   -583    412       C  
ATOM   4257  O   ARG B 126      71.881  52.448 -94.113  1.00 66.95           O  
ANISOU 4257  O   ARG B 126     7498   9224   8715    432   -545    272       O  
ATOM   4258  CB  ARG B 126      71.538  52.152 -97.021  1.00 70.38           C  
ANISOU 4258  CB  ARG B 126     7833   9741   9170    505   -594    615       C  
ATOM   4259  CG  ARG B 126      71.109  52.802 -98.324  1.00 74.74           C  
ANISOU 4259  CG  ARG B 126     8341  10244   9812    571   -636    764       C  
ATOM   4260  CD  ARG B 126      69.924  53.734 -98.117  1.00 80.10           C  
ANISOU 4260  CD  ARG B 126     8995  10811  10628    679   -639    698       C  
ATOM   4261  NE  ARG B 126      69.531  54.404 -99.354  1.00 85.41           N  
ANISOU 4261  NE  ARG B 126     9628  11432  11393    746   -691    856       N  
ATOM   4262  CZ  ARG B 126      69.854  55.657 -99.658  1.00 87.78           C  
ANISOU 4262  CZ  ARG B 126     9950  11554  11850    760   -740    935       C  
ATOM   4263  NH1 ARG B 126      70.572  56.382 -98.810  1.00 89.64           N  
ANISOU 4263  NH1 ARG B 126    10245  11643  12171    708   -743    856       N  
ATOM   4264  NH2 ARG B 126      69.455  56.189-100.804  1.00 86.45           N  
ANISOU 4264  NH2 ARG B 126     9745  11351  11752    822   -790   1095       N  
ATOM   4265  N   GLU B 127      73.980  51.738 -94.545  1.00 59.86           N  
ANISOU 4265  N   GLU B 127     6630   8396   7720    284   -593    425       N  
ATOM   4266  CA  GLU B 127      74.183  51.092 -93.248  1.00 55.93           C  
ANISOU 4266  CA  GLU B 127     6170   7967   7114    234   -566    290       C  
ATOM   4267  C   GLU B 127      73.084  50.065 -92.977  1.00 52.42           C  
ANISOU 4267  C   GLU B 127     5702   7654   6560    281   -503    224       C  
ATOM   4268  O   GLU B 127      72.512  49.996 -91.886  1.00 52.31           O  
ANISOU 4268  O   GLU B 127     5712   7658   6508    289   -463     78       O  
ATOM   4269  CB  GLU B 127      74.278  52.128 -92.124  1.00 58.65           C  
ANISOU 4269  CB  GLU B 127     6566   8184   7537    215   -578    145       C  
ATOM   4270  CG  GLU B 127      75.697  52.655 -91.916  1.00 65.99           C  
ANISOU 4270  CG  GLU B 127     7530   9037   8508    117   -638    176       C  
ATOM   4271  CD  GLU B 127      75.744  54.118 -91.545  1.00 70.12           C  
ANISOU 4271  CD  GLU B 127     8086   9367   9191    117   -669    100       C  
ATOM   4272  OE1 GLU B 127      76.861  54.668 -91.451  1.00 68.05           O  
ANISOU 4272  OE1 GLU B 127     7846   9025   8984     32   -723    128       O  
ATOM   4273  OE2 GLU B 127      74.670  54.721 -91.355  1.00 72.39           O  
ANISOU 4273  OE2 GLU B 127     8373   9577   9555    201   -641     10       O  
ATOM   4274  N   LEU B 128      72.799  49.260 -93.995  1.00 46.59           N  
ANISOU 4274  N   LEU B 128     4919   7014   5771    307   -493    331       N  
ATOM   4275  CA  LEU B 128      71.796  48.210 -93.972  1.00 42.45           C  
ANISOU 4275  CA  LEU B 128     4362   6616   5150    342   -439    294       C  
ATOM   4276  C   LEU B 128      72.405  46.899 -94.441  1.00 43.47           C  
ANISOU 4276  C   LEU B 128     4485   6870   5160    293   -434    379       C  
ATOM   4277  O   LEU B 128      73.309  46.895 -95.284  1.00 45.40           O  
ANISOU 4277  O   LEU B 128     4723   7111   5415    265   -470    498       O  
ATOM   4278  CB  LEU B 128      70.609  48.552 -94.886  1.00 45.26           C  
ANISOU 4278  CB  LEU B 128     4655   6964   5577    436   -434    332       C  
ATOM   4279  CG  LEU B 128      69.750  49.775 -94.578  1.00 52.17           C  
ANISOU 4279  CG  LEU B 128     5516   7718   6586    513   -432    253       C  
ATOM   4280  CD1 LEU B 128      68.843  50.057 -95.761  1.00 49.71           C  
ANISOU 4280  CD1 LEU B 128     5135   7406   6345    601   -451    344       C  
ATOM   4281  CD2 LEU B 128      68.930  49.553 -93.317  1.00 54.65           C  
ANISOU 4281  CD2 LEU B 128     5837   8069   6858    528   -367     78       C  
ATOM   4282  N   PRO B 129      71.932  45.771 -93.915  1.00 43.58           N  
ANISOU 4282  N   PRO B 129     4500   6993   5064    281   -387    320       N  
ATOM   4283  CA  PRO B 129      72.285  44.481 -94.519  1.00 44.71           C  
ANISOU 4283  CA  PRO B 129     4630   7246   5111    252   -378    399       C  
ATOM   4284  C   PRO B 129      71.798  44.416 -95.960  1.00 47.48           C  
ANISOU 4284  C   PRO B 129     4925   7628   5488    301   -387    496       C  
ATOM   4285  O   PRO B 129      70.835  45.086 -96.342  1.00 50.01           O  
ANISOU 4285  O   PRO B 129     5208   7916   5878    365   -389    487       O  
ATOM   4286  CB  PRO B 129      71.568  43.458 -93.630  1.00 39.11           C  
ANISOU 4286  CB  PRO B 129     3931   6626   4303    238   -321    307       C  
ATOM   4287  CG  PRO B 129      70.542  44.239 -92.875  1.00 46.13           C  
ANISOU 4287  CG  PRO B 129     4815   7472   5239    280   -291    190       C  
ATOM   4288  CD  PRO B 129      71.130  45.605 -92.693  1.00 42.79           C  
ANISOU 4288  CD  PRO B 129     4418   6921   4920    285   -335    179       C  
ATOM   4289  N   LEU B 130      72.479  43.589 -96.759  1.00 40.26           N  
ANISOU 4289  N   LEU B 130     4001   6781   4514    272   -394    586       N  
ATOM   4290  CA  LEU B 130      72.220  43.547 -98.196  1.00 41.44           C  
ANISOU 4290  CA  LEU B 130     4104   6971   4670    306   -409    685       C  
ATOM   4291  C   LEU B 130      70.756  43.242 -98.495  1.00 41.80           C  
ANISOU 4291  C   LEU B 130     4103   7075   4704    360   -385    644       C  
ATOM   4292  O   LEU B 130      70.119  43.932 -99.298  1.00 46.57           O  
ANISOU 4292  O   LEU B 130     4666   7662   5367    416   -411    691       O  
ATOM   4293  CB  LEU B 130      73.134  42.518 -98.862  1.00 37.17           C  
ANISOU 4293  CB  LEU B 130     3563   6509   4049    265   -404    757       C  
ATOM   4294  CG  LEU B 130      72.968  42.355-100.375  1.00 39.93           C  
ANISOU 4294  CG  LEU B 130     3871   6923   4379    290   -415    854       C  
ATOM   4295  CD1 LEU B 130      73.153  43.688-101.088  1.00 41.60           C  
ANISOU 4295  CD1 LEU B 130     4068   7061   4678    314   -459    947       C  
ATOM   4296  CD2 LEU B 130      73.940  41.316-100.918  1.00 38.74           C  
ANISOU 4296  CD2 LEU B 130     3722   6848   4150    250   -399    902       C  
ATOM   4297  N   TYR B 131      70.200  42.214 -97.847  1.00 41.39           N  
ANISOU 4297  N   TYR B 131     4053   7093   4579    343   -339    561       N  
ATOM   4298  CA  TYR B 131      68.815  41.838 -98.118  1.00 42.94           C  
ANISOU 4298  CA  TYR B 131     4195   7356   4763    382   -314    519       C  
ATOM   4299  C   TYR B 131      67.843  42.961 -97.781  1.00 51.73           C  
ANISOU 4299  C   TYR B 131     5276   8407   5974    448   -317    465       C  
ATOM   4300  O   TYR B 131      66.787  43.079 -98.414  1.00 56.82           O  
ANISOU 4300  O   TYR B 131     5854   9087   6646    502   -323    471       O  
ATOM   4301  CB  TYR B 131      68.455  40.565 -97.346  1.00 43.69           C  
ANISOU 4301  CB  TYR B 131     4304   7526   4772    338   -258    441       C  
ATOM   4302  CG  TYR B 131      68.622  40.666 -95.841  1.00 46.78           C  
ANISOU 4302  CG  TYR B 131     4745   7880   5150    307   -227    352       C  
ATOM   4303  CD1 TYR B 131      67.602  41.161 -95.044  1.00 39.41           C  
ANISOU 4303  CD1 TYR B 131     3791   6934   4248    338   -191    254       C  
ATOM   4304  CD2 TYR B 131      69.792  40.251 -95.218  1.00 45.99           C  
ANISOU 4304  CD2 TYR B 131     4708   7766   5001    249   -232    364       C  
ATOM   4305  CE1 TYR B 131      67.740  41.258 -93.674  1.00 43.95           C  
ANISOU 4305  CE1 TYR B 131     4415   7489   4794    306   -159    166       C  
ATOM   4306  CE2 TYR B 131      69.939  40.340 -93.839  1.00 46.08           C  
ANISOU 4306  CE2 TYR B 131     4767   7757   4984    217   -210    285       C  
ATOM   4307  CZ  TYR B 131      68.906  40.846 -93.074  1.00 50.88           C  
ANISOU 4307  CZ  TYR B 131     5362   8359   5612    242   -171    184       C  
ATOM   4308  OH  TYR B 131      69.033  40.943 -91.706  1.00 56.13           O  
ANISOU 4308  OH  TYR B 131     6078   9017   6233    207   -145     99       O  
ATOM   4309  N   ARG B 132      68.171  43.793 -96.792  1.00 51.87           N  
ANISOU 4309  N   ARG B 132     5333   8329   6044    447   -314    406       N  
ATOM   4310  CA  ARG B 132      67.286  44.901 -96.448  1.00 49.79           C  
ANISOU 4310  CA  ARG B 132     5040   7992   5885    517   -313    343       C  
ATOM   4311  C   ARG B 132      67.415  46.041 -97.448  1.00 45.80           C  
ANISOU 4311  C   ARG B 132     4513   7399   5490    572   -375    444       C  
ATOM   4312  O   ARG B 132      66.439  46.754 -97.705  1.00 44.53           O  
ANISOU 4312  O   ARG B 132     4298   7202   5418    651   -386    433       O  
ATOM   4313  CB  ARG B 132      67.586  45.383 -95.028  1.00 54.69           C  
ANISOU 4313  CB  ARG B 132     5717   8542   6520    493   -285    229       C  
ATOM   4314  CG  ARG B 132      66.486  46.217 -94.391  1.00 64.85           C  
ANISOU 4314  CG  ARG B 132     6971   9779   7891    562   -254    116       C  
ATOM   4315  CD  ARG B 132      66.084  45.636 -93.044  1.00 69.26           C  
ANISOU 4315  CD  ARG B 132     7551  10400   8365    526   -179    -21       C  
ATOM   4316  NE  ARG B 132      64.742  45.060 -93.071  1.00 73.17           N  
ANISOU 4316  NE  ARG B 132     7971  10992   8838    561   -125    -71       N  
ATOM   4317  CZ  ARG B 132      64.203  44.382 -92.062  1.00 76.23           C  
ANISOU 4317  CZ  ARG B 132     8361  11460   9142    526    -50   -173       C  
ATOM   4318  NH1 ARG B 132      62.975  43.894 -92.166  1.00 77.40           N  
ANISOU 4318  NH1 ARG B 132     8429  11696   9282    554      0   -210       N  
ATOM   4319  NH2 ARG B 132      64.896  44.186 -90.947  1.00 74.46           N  
ANISOU 4319  NH2 ARG B 132     8216  11235   8839    459    -26   -231       N  
ATOM   4320  N   HIS B 133      68.608  46.222 -98.025  1.00 46.06           N  
ANISOU 4320  N   HIS B 133     4582   7397   5521    531   -417    550       N  
ATOM   4321  CA  HIS B 133      68.782  47.202 -99.094  1.00 40.64           C  
ANISOU 4321  CA  HIS B 133     3877   6640   4925    570   -476    673       C  
ATOM   4322  C   HIS B 133      68.071  46.755-100.365  1.00 40.95           C  
ANISOU 4322  C   HIS B 133     3852   6781   4926    610   -495    759       C  
ATOM   4323  O   HIS B 133      67.479  47.576-101.076  1.00 39.04           O  
ANISOU 4323  O   HIS B 133     3569   6499   4767    678   -537    825       O  
ATOM   4324  CB  HIS B 133      70.273  47.417 -99.354  1.00 42.30           C  
ANISOU 4324  CB  HIS B 133     4136   6804   5131    503   -505    764       C  
ATOM   4325  CG  HIS B 133      70.570  48.358-100.479  1.00 46.40           C  
ANISOU 4325  CG  HIS B 133     4641   7258   5729    526   -560    908       C  
ATOM   4326  ND1 HIS B 133      70.145  49.670-100.489  1.00 50.29           N  
ANISOU 4326  ND1 HIS B 133     5127   7615   6364    586   -594    923       N  
ATOM   4327  CD2 HIS B 133      71.273  48.181-101.623  1.00 49.16           C  
ANISOU 4327  CD2 HIS B 133     4984   7659   6036    497   -584   1049       C  
ATOM   4328  CE1 HIS B 133      70.565  50.256-101.597  1.00 50.59           C  
ANISOU 4328  CE1 HIS B 133     5158   7621   6444    588   -641   1080       C  
ATOM   4329  NE2 HIS B 133      71.253  49.375-102.302  1.00 50.67           N  
ANISOU 4329  NE2 HIS B 133     5166   7751   6334    532   -633   1157       N  
ATOM   4330  N   ILE B 134      68.119  45.455-100.662  1.00 38.35           N  
ANISOU 4330  N   ILE B 134     3516   6584   4473    567   -469    758       N  
ATOM   4331  CA  ILE B 134      67.371  44.918-101.796  1.00 39.05           C  
ANISOU 4331  CA  ILE B 134     3543   6784   4510    595   -486    814       C  
ATOM   4332  C   ILE B 134      65.875  45.115-101.583  1.00 39.06           C  
ANISOU 4332  C   ILE B 134     3477   6803   4563    667   -480    742       C  
ATOM   4333  O   ILE B 134      65.131  45.412-102.526  1.00 41.01           O  
ANISOU 4333  O   ILE B 134     3660   7086   4834    723   -524    807       O  
ATOM   4334  CB  ILE B 134      67.731  43.434-102.011  1.00 35.93           C  
ANISOU 4334  CB  ILE B 134     3161   6511   3980    530   -452    800       C  
ATOM   4335  CG1 ILE B 134      69.179  43.299-102.474  1.00 35.92           C  
ANISOU 4335  CG1 ILE B 134     3206   6504   3937    475   -463    888       C  
ATOM   4336  CG2 ILE B 134      66.787  42.769-103.002  1.00 39.94           C  
ANISOU 4336  CG2 ILE B 134     3604   7142   4429    551   -464    819       C  
ATOM   4337  CD1 ILE B 134      69.606  41.871-102.672  1.00 37.43           C  
ANISOU 4337  CD1 ILE B 134     3410   6798   4012    420   -428    870       C  
ATOM   4338  N   ALA B 135      65.413  44.973-100.336  1.00 38.19           N  
ANISOU 4338  N   ALA B 135     3371   6672   4466    665   -426    608       N  
ATOM   4339  CA  ALA B 135      63.995  45.158-100.044  1.00 37.48           C  
ANISOU 4339  CA  ALA B 135     3206   6605   4430    732   -408    528       C  
ATOM   4340  C   ALA B 135      63.560  46.600-100.281  1.00 41.53           C  
ANISOU 4340  C   ALA B 135     3684   7004   5090    827   -454    563       C  
ATOM   4341  O   ALA B 135      62.445  46.846-100.757  1.00 47.21           O  
ANISOU 4341  O   ALA B 135     4318   7757   5862    902   -476    571       O  
ATOM   4342  CB  ALA B 135      63.693  44.736 -98.606  1.00 34.59           C  
ANISOU 4342  CB  ALA B 135     2858   6244   4039    703   -330    379       C  
ATOM   4343  N   GLN B 136      64.421  47.568 -99.959  1.00 43.39           N  
ANISOU 4343  N   GLN B 136     3983   7101   5402    826   -473    586       N  
ATOM   4344  CA  GLN B 136      64.085  48.966-100.206  1.00 45.45           C  
ANISOU 4344  CA  GLN B 136     4221   7230   5819    914   -520    628       C  
ATOM   4345  C   GLN B 136      64.170  49.322-101.686  1.00 54.44           C  
ANISOU 4345  C   GLN B 136     5331   8380   6974    944   -599    806       C  
ATOM   4346  O   GLN B 136      63.436  50.202-102.150  1.00 57.34           O  
ANISOU 4346  O   GLN B 136     5644   8688   7455   1037   -646    856       O  
ATOM   4347  CB  GLN B 136      64.997  49.884 -99.389  1.00 46.69           C  
ANISOU 4347  CB  GLN B 136     4458   7226   6057    892   -517    591       C  
ATOM   4348  CG  GLN B 136      64.897  49.659 -97.891  1.00 54.40           C  
ANISOU 4348  CG  GLN B 136     5467   8193   7012    864   -444    412       C  
ATOM   4349  CD  GLN B 136      65.606  50.728 -97.083  1.00 59.92           C  
ANISOU 4349  CD  GLN B 136     6235   8725   7807    854   -450    356       C  
ATOM   4350  OE1 GLN B 136      66.280  51.600 -97.635  1.00 60.31           O  
ANISOU 4350  OE1 GLN B 136     6312   8658   7945    856   -507    458       O  
ATOM   4351  NE2 GLN B 136      65.453  50.668 -95.764  1.00 60.59           N  
ANISOU 4351  NE2 GLN B 136     6348   8801   7873    837   -389    192       N  
ATOM   4352  N   LEU B 137      65.055  48.665-102.440  1.00 55.74           N  
ANISOU 4352  N   LEU B 137     5529   8622   7027    871   -615    904       N  
ATOM   4353  CA  LEU B 137      65.090  48.880-103.882  1.00 49.80           C  
ANISOU 4353  CA  LEU B 137     4749   7914   6259    891   -683   1071       C  
ATOM   4354  C   LEU B 137      63.857  48.295-104.557  1.00 50.84           C  
ANISOU 4354  C   LEU B 137     4790   8185   6342    939   -702   1072       C  
ATOM   4355  O   LEU B 137      63.428  48.792-105.605  1.00 56.21           O  
ANISOU 4355  O   LEU B 137     5424   8884   7050    995   -771   1194       O  
ATOM   4356  CB  LEU B 137      66.361  48.274-104.480  1.00 44.04           C  
ANISOU 4356  CB  LEU B 137     4074   7245   5414    798   -681   1158       C  
ATOM   4357  CG  LEU B 137      67.682  48.941-104.085  1.00 46.04           C  
ANISOU 4357  CG  LEU B 137     4403   7370   5719    745   -679   1195       C  
ATOM   4358  CD1 LEU B 137      68.877  48.167-104.626  1.00 39.79           C  
ANISOU 4358  CD1 LEU B 137     3648   6665   4806    656   -664   1264       C  
ATOM   4359  CD2 LEU B 137      67.717  50.385-104.565  1.00 48.18           C  
ANISOU 4359  CD2 LEU B 137     4675   7500   6131    797   -740   1313       C  
ATOM   4360  N   ALA B 138      63.273  47.255-103.972  1.00 45.98           N  
ANISOU 4360  N   ALA B 138     4146   7669   5654    915   -646    944       N  
ATOM   4361  CA  ALA B 138      62.076  46.629-104.512  1.00 48.92           C  
ANISOU 4361  CA  ALA B 138     4427   8178   5983    947   -661    927       C  
ATOM   4362  C   ALA B 138      60.791  47.183-103.909  1.00 54.56           C  
ANISOU 4362  C   ALA B 138     5058   8856   6816   1039   -653    839       C  
ATOM   4363  O   ALA B 138      59.704  46.783-104.334  1.00 49.91           O  
ANISOU 4363  O   ALA B 138     4374   8377   6212   1074   -671    825       O  
ATOM   4364  CB  ALA B 138      62.135  45.113-104.299  1.00 42.80           C  
ANISOU 4364  CB  ALA B 138     3661   7534   5066    860   -604    843       C  
ATOM   4365  N   GLY B 139      60.883  48.088-102.941  1.00 60.51           N  
ANISOU 4365  N   GLY B 139     5839   9463   7690   1079   -625    774       N  
ATOM   4366  CA  GLY B 139      59.691  48.606-102.290  1.00 63.20           C  
ANISOU 4366  CA  GLY B 139     6098   9768   8146   1171   -603    672       C  
ATOM   4367  C   GLY B 139      59.021  47.619-101.359  1.00 63.86           C  
ANISOU 4367  C   GLY B 139     6147   9953   8164   1133   -515    513       C  
ATOM   4368  O   GLY B 139      57.786  47.586-101.283  1.00 66.18           O  
ANISOU 4368  O   GLY B 139     6333  10307   8506   1196   -504    454       O  
ATOM   4369  N   ASN B 140      59.803  46.809-100.652  1.00 65.03           N  
ANISOU 4369  N   ASN B 140     6377  10125   8206   1032   -453    451       N  
ATOM   4370  CA  ASN B 140      59.286  45.827 -99.712  1.00 62.83           C  
ANISOU 4370  CA  ASN B 140     6081   9937   7855    980   -366    315       C  
ATOM   4371  C   ASN B 140      59.672  46.210 -98.289  1.00 60.97           C  
ANISOU 4371  C   ASN B 140     5912   9607   7645    965   -295    196       C  
ATOM   4372  O   ASN B 140      60.680  46.885 -98.060  1.00 55.21           O  
ANISOU 4372  O   ASN B 140     5269   8759   6948    953   -315    223       O  
ATOM   4373  CB  ASN B 140      59.811  44.424-100.031  1.00 62.73           C  
ANISOU 4373  CB  ASN B 140     6109  10039   7687    871   -352    341       C  
ATOM   4374  CG  ASN B 140      59.265  43.881-101.336  1.00 65.01           C  
ANISOU 4374  CG  ASN B 140     6324  10446   7931    877   -409    422       C  
ATOM   4375  OD1 ASN B 140      58.175  44.258-101.771  1.00 66.89           O  
ANISOU 4375  OD1 ASN B 140     6457  10721   8236    952   -443    427       O  
ATOM   4376  ND2 ASN B 140      60.018  42.986-101.968  1.00 58.48           N  
ANISOU 4376  ND2 ASN B 140     5549   9683   6989    798   -423    481       N  
ATOM   4377  N   SER B 141      58.866  45.765 -97.337  1.00 64.86           N  
ANISOU 4377  N   SER B 141     6365  10161   8119    957   -213     64       N  
ATOM   4378  CA  SER B 141      59.083  46.107 -95.935  1.00 65.34           C  
ANISOU 4378  CA  SER B 141     6482  10156   8189    943   -140    -65       C  
ATOM   4379  C   SER B 141      59.149  44.892 -95.022  1.00 73.20           C  
ANISOU 4379  C   SER B 141     7515  11254   9045    840    -57   -144       C  
ATOM   4380  O   SER B 141      59.977  44.866 -94.109  1.00 72.83           O  
ANISOU 4380  O   SER B 141     7563  11164   8944    782    -26   -192       O  
ATOM   4381  CB  SER B 141      57.977  47.059 -95.452  1.00 62.95           C  
ANISOU 4381  CB  SER B 141     6093   9806   8019   1053   -107   -167       C  
ATOM   4382  OG  SER B 141      56.700  46.451 -95.550  1.00 63.20           O  
ANISOU 4382  OG  SER B 141     6004   9967   8041   1074    -68   -211       O  
ATOM   4383  N   ASP B 142      58.301  43.891 -95.241  1.00 79.09           N  
ANISOU 4383  N   ASP B 142     8186  12132   9733    812    -26   -157       N  
ATOM   4384  CA  ASP B 142      58.242  42.704 -94.395  1.00 87.83           C  
ANISOU 4384  CA  ASP B 142     9321  13333  10717    713     55   -222       C  
ATOM   4385  C   ASP B 142      58.893  41.541 -95.129  1.00 84.18           C  
ANISOU 4385  C   ASP B 142     8902  12930  10153    627     20   -126       C  
ATOM   4386  O   ASP B 142      58.389  41.100 -96.167  1.00 90.09           O  
ANISOU 4386  O   ASP B 142     9581  13747  10901    635    -20    -69       O  
ATOM   4387  CB  ASP B 142      56.799  42.368 -94.022  1.00 99.78           C  
ANISOU 4387  CB  ASP B 142    10718  14950  12246    730    128   -314       C  
ATOM   4388  CG  ASP B 142      56.207  43.356 -93.035  1.00108.13           C  
ANISOU 4388  CG  ASP B 142    11740  15959  13383    803    191   -440       C  
ATOM   4389  OD1 ASP B 142      56.209  43.059 -91.821  1.00107.27           O  
ANISOU 4389  OD1 ASP B 142    11674  15880  13202    748    281   -539       O  
ATOM   4390  OD2 ASP B 142      55.741  44.429 -93.473  1.00112.00           O  
ANISOU 4390  OD2 ASP B 142    12164  16384  14008    916    152   -439       O  
ATOM   4391  N   LEU B 143      59.992  41.037 -94.577  1.00 69.70           N  
ANISOU 4391  N   LEU B 143     7179  11073   8232    548     33   -114       N  
ATOM   4392  CA  LEU B 143      60.815  40.031 -95.230  1.00 51.60           C  
ANISOU 4392  CA  LEU B 143     4938   8812   5856    478     -1    -25       C  
ATOM   4393  C   LEU B 143      60.336  38.621 -94.895  1.00 50.00           C  
ANISOU 4393  C   LEU B 143     4725   8711   5563    395     59    -58       C  
ATOM   4394  O   LEU B 143      59.611  38.396 -93.924  1.00 55.48           O  
ANISOU 4394  O   LEU B 143     5396   9447   6238    373    135   -146       O  
ATOM   4395  CB  LEU B 143      62.277  40.202 -94.823  1.00 44.00           C  
ANISOU 4395  CB  LEU B 143     4090   7769   4858    440    -23     11       C  
ATOM   4396  CG  LEU B 143      62.774  41.646 -94.882  1.00 48.73           C  
ANISOU 4396  CG  LEU B 143     4709   8251   5553    505    -70     27       C  
ATOM   4397  CD1 LEU B 143      64.225  41.732 -94.459  1.00 48.34           C  
ANISOU 4397  CD1 LEU B 143     4764   8136   5467    454    -93     60       C  
ATOM   4398  CD2 LEU B 143      62.587  42.220 -96.276  1.00 52.70           C  
ANISOU 4398  CD2 LEU B 143     5155   8738   6131    572   -143    122       C  
ATOM   4399  N   ILE B 144      60.761  37.665 -95.721  1.00 45.45           N  
ANISOU 4399  N   ILE B 144     4167   8171   4932    346     27     12       N  
ATOM   4400  CA  ILE B 144      60.344  36.271 -95.614  1.00 44.63           C  
ANISOU 4400  CA  ILE B 144     4053   8147   4756    264     72     -7       C  
ATOM   4401  C   ILE B 144      61.539  35.380 -95.933  1.00 40.02           C  
ANISOU 4401  C   ILE B 144     3559   7543   4105    204     48     60       C  
ATOM   4402  O   ILE B 144      62.325  35.674 -96.840  1.00 37.20           O  
ANISOU 4402  O   ILE B 144     3223   7152   3757    232    -15    132       O  
ATOM   4403  CB  ILE B 144      59.155  35.966 -96.555  1.00 53.55           C  
ANISOU 4403  CB  ILE B 144     5068   9362   5916    280     57    -14       C  
ATOM   4404  CG1 ILE B 144      57.841  36.499 -95.968  1.00 59.48           C  
ANISOU 4404  CG1 ILE B 144     5719  10154   6726    320    107    -99       C  
ATOM   4405  CG2 ILE B 144      59.053  34.474 -96.868  1.00 56.32           C  
ANISOU 4405  CG2 ILE B 144     5426   9775   6197    188     75     -8       C  
ATOM   4406  CD1 ILE B 144      57.435  37.872 -96.487  1.00 61.07           C  
ANISOU 4406  CD1 ILE B 144     5850  10321   7032    436     55    -89       C  
ATOM   4407  N   LEU B 145      61.686  34.291 -95.167  1.00 39.26           N  
ANISOU 4407  N   LEU B 145     3513   7464   3941    123    101     41       N  
ATOM   4408  CA  LEU B 145      62.694  33.300 -95.522  1.00 30.37           C  
ANISOU 4408  CA  LEU B 145     2457   6319   2762     72     80    100       C  
ATOM   4409  C   LEU B 145      62.086  32.207 -96.396  1.00 36.06           C  
ANISOU 4409  C   LEU B 145     3132   7100   3468     31     81    100       C  
ATOM   4410  O   LEU B 145      60.983  31.730 -96.116  1.00 48.10           O  
ANISOU 4410  O   LEU B 145     4601   8682   4993     -5    127     47       O  
ATOM   4411  CB  LEU B 145      63.304  32.681 -94.272  1.00 31.36           C  
ANISOU 4411  CB  LEU B 145     2670   6419   2828      9    124     95       C  
ATOM   4412  CG  LEU B 145      64.384  33.594 -93.701  1.00 32.02           C  
ANISOU 4412  CG  LEU B 145     2818   6434   2913     39     95    116       C  
ATOM   4413  CD1 LEU B 145      64.169  33.768 -92.217  1.00 35.37           C  
ANISOU 4413  CD1 LEU B 145     3277   6864   3298     10    150     58       C  
ATOM   4414  CD2 LEU B 145      65.787  33.063 -94.023  1.00 29.25           C  
ANISOU 4414  CD2 LEU B 145     2538   6040   2537     19     53    192       C  
ATOM   4415  N   PRO B 146      62.786  31.788 -97.445  1.00 40.46           N  
ANISOU 4415  N   PRO B 146     3711   7650   4012     32     35    151       N  
ATOM   4416  CA  PRO B 146      62.191  30.888 -98.436  1.00 40.01           C  
ANISOU 4416  CA  PRO B 146     3606   7652   3942     -1     25    138       C  
ATOM   4417  C   PRO B 146      62.262  29.419 -98.039  1.00 36.82           C  
ANISOU 4417  C   PRO B 146     3248   7240   3500    -89     71    120       C  
ATOM   4418  O   PRO B 146      63.115  28.988 -97.264  1.00 37.81           O  
ANISOU 4418  O   PRO B 146     3457   7308   3602   -117     93    145       O  
ATOM   4419  CB  PRO B 146      63.063  31.136 -99.676  1.00 33.15           C  
ANISOU 4419  CB  PRO B 146     2754   6777   3065     39    -39    199       C  
ATOM   4420  CG  PRO B 146      64.422  31.409 -99.077  1.00 30.33           C  
ANISOU 4420  CG  PRO B 146     2483   6341   2700     49    -40    246       C  
ATOM   4421  CD  PRO B 146      64.171  32.163 -97.795  1.00 29.31           C  
ANISOU 4421  CD  PRO B 146     2363   6180   2594     61    -10    218       C  
ATOM   4422  N   VAL B 147      61.360  28.645 -98.627  1.00 34.20           N  
ANISOU 4422  N   VAL B 147     2860   6965   3169   -133     77     80       N  
ATOM   4423  CA  VAL B 147      61.477  27.188 -98.584  1.00 35.26           C  
ANISOU 4423  CA  VAL B 147     3038   7080   3281   -216    107     67       C  
ATOM   4424  C   VAL B 147      62.569  26.759 -99.561  1.00 39.70           C  
ANISOU 4424  C   VAL B 147     3652   7609   3824   -200     66    100       C  
ATOM   4425  O   VAL B 147      62.526  27.154-100.736  1.00 40.52           O  
ANISOU 4425  O   VAL B 147     3713   7760   3921   -160     16    103       O  
ATOM   4426  CB  VAL B 147      60.149  26.529 -98.924  1.00 33.39           C  
ANISOU 4426  CB  VAL B 147     2718   6911   3057   -276    125      5       C  
ATOM   4427  CG1 VAL B 147      60.322  25.021 -99.033  1.00 33.55           C  
ANISOU 4427  CG1 VAL B 147     2788   6893   3066   -364    149    -11       C  
ATOM   4428  CG2 VAL B 147      59.107  26.879 -97.876  1.00 31.92           C  
ANISOU 4428  CG2 VAL B 147     2475   6762   2890   -296    181    -30       C  
ATOM   4429  N   PRO B 148      63.561  25.981 -99.124  1.00 40.66           N  
ANISOU 4429  N   PRO B 148     3860   7655   3932   -227     85    129       N  
ATOM   4430  CA  PRO B 148      64.603  25.523-100.052  1.00 34.71           C  
ANISOU 4430  CA  PRO B 148     3148   6874   3166   -208     56    150       C  
ATOM   4431  C   PRO B 148      64.141  24.326-100.869  1.00 35.76           C  
ANISOU 4431  C   PRO B 148     3268   7023   3297   -263     62     93       C  
ATOM   4432  O   PRO B 148      63.474  23.420-100.361  1.00 33.85           O  
ANISOU 4432  O   PRO B 148     3030   6763   3071   -337    101     58       O  
ATOM   4433  CB  PRO B 148      65.757  25.145 -99.120  1.00 31.86           C  
ANISOU 4433  CB  PRO B 148     2875   6424   2805   -211     75    200       C  
ATOM   4434  CG  PRO B 148      65.070  24.727 -97.852  1.00 34.30           C  
ANISOU 4434  CG  PRO B 148     3199   6717   3116   -273    124    189       C  
ATOM   4435  CD  PRO B 148      63.832  25.576 -97.734  1.00 29.72           C  
ANISOU 4435  CD  PRO B 148     2539   6212   2540   -267    132    149       C  
ATOM   4436  N   ALA B 149      64.503  24.327-102.152  1.00 29.96           N  
ANISOU 4436  N   ALA B 149     2519   6324   2540   -233     25     83       N  
ATOM   4437  CA  ALA B 149      64.224  23.215-103.056  1.00 30.53           C  
ANISOU 4437  CA  ALA B 149     2587   6411   2602   -282     26     16       C  
ATOM   4438  C   ALA B 149      65.559  22.566-103.417  1.00 44.49           C  
ANISOU 4438  C   ALA B 149     4427   8113   4365   -261     33     29       C  
ATOM   4439  O   ALA B 149      66.309  23.085-104.250  1.00 36.97           O  
ANISOU 4439  O   ALA B 149     3473   7194   3381   -204      6     54       O  
ATOM   4440  CB  ALA B 149      63.470  23.690-104.295  1.00 30.98           C  
ANISOU 4440  CB  ALA B 149     2564   6582   2624   -268    -23    -20       C  
ATOM   4441  N   PHE B 150      65.851  21.428-102.790  1.00 42.16           N  
ANISOU 4441  N   PHE B 150     4191   7722   4105   -306     72     18       N  
ATOM   4442  CA  PHE B 150      67.134  20.756-102.950  1.00 36.72           C  
ANISOU 4442  CA  PHE B 150     3567   6955   3431   -279     84     33       C  
ATOM   4443  C   PHE B 150      67.079  19.788-104.122  1.00 31.13           C  
ANISOU 4443  C   PHE B 150     2860   6254   2716   -302     87    -56       C  
ATOM   4444  O   PHE B 150      66.320  18.815-104.087  1.00 34.86           O  
ANISOU 4444  O   PHE B 150     3335   6694   3215   -375    106   -121       O  
ATOM   4445  CB  PHE B 150      67.512  19.997-101.680  1.00 37.25           C  
ANISOU 4445  CB  PHE B 150     3701   6907   3546   -308    117     74       C  
ATOM   4446  CG  PHE B 150      67.555  20.848-100.453  1.00 42.03           C  
ANISOU 4446  CG  PHE B 150     4314   7510   4146   -296    117    148       C  
ATOM   4447  CD1 PHE B 150      68.649  21.655-100.196  1.00 29.33           C  
ANISOU 4447  CD1 PHE B 150     2722   5893   2527   -229     94    216       C  
ATOM   4448  CD2 PHE B 150      66.507  20.828 -99.544  1.00 34.93           C  
ANISOU 4448  CD2 PHE B 150     3401   6620   3249   -356    142    144       C  
ATOM   4449  CE1 PHE B 150      68.697  22.435 -99.065  1.00 30.98           C  
ANISOU 4449  CE1 PHE B 150     2943   6101   2728   -222     91    271       C  
ATOM   4450  CE2 PHE B 150      66.549  21.604 -98.408  1.00 32.06           C  
ANISOU 4450  CE2 PHE B 150     3049   6262   2870   -345    147    199       C  
ATOM   4451  CZ  PHE B 150      67.648  22.408 -98.165  1.00 30.38           C  
ANISOU 4451  CZ  PHE B 150     2860   6037   2645   -278    119    258       C  
ATOM   4452  N   ASN B 151      67.892  20.042-105.146  1.00 32.69           N  
ANISOU 4452  N   ASN B 151     3053   6492   2876   -246     72    -62       N  
ATOM   4453  CA  ASN B 151      68.072  19.066-106.214  1.00 43.87           C  
ANISOU 4453  CA  ASN B 151     4482   7906   4280   -260     84   -154       C  
ATOM   4454  C   ASN B 151      68.656  17.785-105.631  1.00 42.29           C  
ANISOU 4454  C   ASN B 151     4350   7561   4156   -278    125   -172       C  
ATOM   4455  O   ASN B 151      69.618  17.825-104.863  1.00 49.75           O  
ANISOU 4455  O   ASN B 151     5334   8430   5140   -235    137    -95       O  
ATOM   4456  CB  ASN B 151      68.985  19.639-107.299  1.00 55.81           C  
ANISOU 4456  CB  ASN B 151     5980   9493   5731   -191     72   -145       C  
ATOM   4457  CG  ASN B 151      69.324  18.629-108.376  1.00 67.24           C  
ANISOU 4457  CG  ASN B 151     7446  10942   7160   -198     95   -250       C  
ATOM   4458  OD1 ASN B 151      70.495  18.325-108.608  1.00 69.62           O  
ANISOU 4458  OD1 ASN B 151     7777  11202   7474   -146    124   -247       O  
ATOM   4459  ND2 ASN B 151      68.301  18.099-109.038  1.00 66.45           N  
ANISOU 4459  ND2 ASN B 151     7325  10891   7032   -261     83   -351       N  
ATOM   4460  N   VAL B 152      68.057  16.646-105.966  1.00 37.63           N  
ANISOU 4460  N   VAL B 152     3774   6928   3594   -344    142   -269       N  
ATOM   4461  CA  VAL B 152      68.382  15.413-105.256  1.00 40.45           C  
ANISOU 4461  CA  VAL B 152     4198   7129   4041   -373    178   -274       C  
ATOM   4462  C   VAL B 152      68.611  14.268-106.237  1.00 42.63           C  
ANISOU 4462  C   VAL B 152     4501   7355   4342   -385    199   -395       C  
ATOM   4463  O   VAL B 152      69.523  13.454-106.052  1.00 47.16           O  
ANISOU 4463  O   VAL B 152     5128   7806   4985   -351    227   -396       O  
ATOM   4464  CB  VAL B 152      67.277  15.079-104.232  1.00 45.11           C  
ANISOU 4464  CB  VAL B 152     4791   7676   4672   -463    187   -256       C  
ATOM   4465  CG1 VAL B 152      67.399  13.665-103.749  1.00 42.54           C  
ANISOU 4465  CG1 VAL B 152     4533   7191   4439   -513    221   -275       C  
ATOM   4466  CG2 VAL B 152      67.357  16.024-103.041  1.00 41.67           C  
ANISOU 4466  CG2 VAL B 152     4353   7257   4225   -440    181   -136       C  
ATOM   4467  N   ILE B 153      67.800  14.198-107.290  1.00 41.50           N  
ANISOU 4467  N   ILE B 153     4317   7307   4144   -430    182   -502       N  
ATOM   4468  CA  ILE B 153      67.967  13.217-108.357  1.00 43.78           C  
ANISOU 4468  CA  ILE B 153     4626   7571   4435   -445    199   -640       C  
ATOM   4469  C   ILE B 153      68.097  13.966-109.676  1.00 44.97           C  
ANISOU 4469  C   ILE B 153     4730   7891   4467   -404    175   -687       C  
ATOM   4470  O   ILE B 153      67.373  14.938-109.920  1.00 44.03           O  
ANISOU 4470  O   ILE B 153     4550   7908   4271   -416    132   -656       O  
ATOM   4471  CB  ILE B 153      66.795  12.213-108.408  1.00 49.73           C  
ANISOU 4471  CB  ILE B 153     5383   8276   5234   -562    200   -744       C  
ATOM   4472  CG1 ILE B 153      66.717  11.408-107.109  1.00 49.80           C  
ANISOU 4472  CG1 ILE B 153     5447   8111   5362   -608    230   -684       C  
ATOM   4473  CG2 ILE B 153      66.953  11.263-109.585  1.00 46.91           C  
ANISOU 4473  CG2 ILE B 153     5049   7902   4873   -578    214   -905       C  
ATOM   4474  CD1 ILE B 153      67.807  10.371-106.973  1.00 52.96           C  
ANISOU 4474  CD1 ILE B 153     5925   8340   5857   -563    269   -698       C  
ATOM   4475  N   ASN B 154      69.022  13.517-110.525  1.00 46.90           N  
ANISOU 4475  N   ASN B 154     4999   8127   4693   -353    204   -759       N  
ATOM   4476  CA  ASN B 154      69.330  14.211-111.767  1.00 42.94           C  
ANISOU 4476  CA  ASN B 154     4459   7788   4067   -310    191   -791       C  
ATOM   4477  C   ASN B 154      69.217  13.280-112.964  1.00 46.49           C  
ANISOU 4477  C   ASN B 154     4924   8265   4477   -343    208   -966       C  
ATOM   4478  O   ASN B 154      69.582  12.102-112.893  1.00 39.51           O  
ANISOU 4478  O   ASN B 154     4092   7241   3680   -350    251  -1055       O  
ATOM   4479  CB  ASN B 154      70.727  14.825-111.717  1.00 48.90           C  
ANISOU 4479  CB  ASN B 154     5219   8549   4813   -206    217   -698       C  
ATOM   4480  CG  ASN B 154      70.824  15.941-110.706  1.00 54.03           C  
ANISOU 4480  CG  ASN B 154     5847   9203   5478   -177    190   -535       C  
ATOM   4481  OD1 ASN B 154      71.175  15.716-109.549  1.00 57.95           O  
ANISOU 4481  OD1 ASN B 154     6376   9575   6069   -165    203   -464       O  
ATOM   4482  ND2 ASN B 154      70.485  17.154-111.131  1.00 54.83           N  
ANISOU 4482  ND2 ASN B 154     5898   9449   5487   -166    149   -477       N  
ATOM   4483  N   GLY B 155      68.705  13.826-114.054  1.00 46.90           N  
ANISOU 4483  N   GLY B 155     4930   8494   4395   -362    170  -1015       N  
ATOM   4484  CA  GLY B 155      68.630  13.133-115.328  1.00 45.74           C  
ANISOU 4484  CA  GLY B 155     4791   8415   4171   -391    181  -1184       C  
ATOM   4485  C   GLY B 155      68.794  14.155-116.427  1.00 46.30           C  
ANISOU 4485  C   GLY B 155     4818   8699   4076   -355    153  -1159       C  
ATOM   4486  O   GLY B 155      69.427  15.198-116.229  1.00 50.23           O  
ANISOU 4486  O   GLY B 155     5295   9247   4545   -285    152  -1018       O  
ATOM   4487  N   GLY B 156      68.217  13.866-117.589  1.00 49.35           N  
ANISOU 4487  N   GLY B 156     5190   9213   4349   -408    127  -1292       N  
ATOM   4488  CA  GLY B 156      68.268  14.836-118.664  1.00 54.69           C  
ANISOU 4488  CA  GLY B 156     5824  10104   4851   -383     93  -1258       C  
ATOM   4489  C   GLY B 156      69.658  14.962-119.264  1.00 60.42           C  
ANISOU 4489  C   GLY B 156     6572  10868   5518   -299    162  -1254       C  
ATOM   4490  O   GLY B 156      70.448  14.013-119.294  1.00 51.11           O  
ANISOU 4490  O   GLY B 156     5439   9581   4401   -273    236  -1355       O  
ATOM   4491  N   SER B 157      69.962  16.173-119.735  1.00 69.04           N  
ANISOU 4491  N   SER B 157     7626  12112   6494   -255    140  -1130       N  
ATOM   4492  CA  SER B 157      71.191  16.393-120.492  1.00 79.79           C  
ANISOU 4492  CA  SER B 157     8995  13554   7770   -189    205  -1125       C  
ATOM   4493  C   SER B 157      72.428  16.143-119.640  1.00 86.84           C  
ANISOU 4493  C   SER B 157     9913  14283   8802   -114    282  -1074       C  
ATOM   4494  O   SER B 157      73.390  15.517-120.099  1.00 90.13           O  
ANISOU 4494  O   SER B 157    10350  14682   9215    -72    361  -1164       O  
ATOM   4495  CB  SER B 157      71.211  17.814-121.048  1.00 81.68           C  
ANISOU 4495  CB  SER B 157     9187  13975   7873   -166    159   -974       C  
ATOM   4496  OG  SER B 157      70.010  18.095-121.741  1.00 86.77           O  
ANISOU 4496  OG  SER B 157     9801  14767   8399   -230     73  -1001       O  
ATOM   4497  N   HIS B 158      72.421  16.622-118.402  1.00 87.45           N  
ANISOU 4497  N   HIS B 158     9983  14244   8999    -95    259   -935       N  
ATOM   4498  CA  HIS B 158      73.604  16.564-117.545  1.00 91.62           C  
ANISOU 4498  CA  HIS B 158    10525  14636   9649    -23    315   -859       C  
ATOM   4499  C   HIS B 158      73.551  15.345-116.623  1.00 82.65           C  
ANISOU 4499  C   HIS B 158     9437  13292   8676    -35    340   -932       C  
ATOM   4500  O   HIS B 158      73.592  15.451-115.397  1.00 89.52           O  
ANISOU 4500  O   HIS B 158    10316  14034   9663    -25    326   -832       O  
ATOM   4501  CB  HIS B 158      73.743  17.862-116.751  1.00 99.98           C  
ANISOU 4501  CB  HIS B 158    11554  15700  10735      5    275   -661       C  
ATOM   4502  CG  HIS B 158      72.538  18.211-115.929  1.00104.26           C  
ANISOU 4502  CG  HIS B 158    12088  16203  11322    -46    203   -605       C  
ATOM   4503  ND1 HIS B 158      71.950  17.326-115.050  1.00105.49           N  
ANISOU 4503  ND1 HIS B 158    12275  16214  11592    -88    200   -659       N  
ATOM   4504  CD2 HIS B 158      71.826  19.359-115.837  1.00102.67           C  
ANISOU 4504  CD2 HIS B 158    11849  16088  11075    -60    136   -498       C  
ATOM   4505  CE1 HIS B 158      70.922  17.910-114.461  1.00104.31           C  
ANISOU 4505  CE1 HIS B 158    12102  16075  11456   -128    140   -593       C  
ATOM   4506  NE2 HIS B 158      70.827  19.145-114.919  1.00102.76           N  
ANISOU 4506  NE2 HIS B 158    11862  16013  11168   -106    100   -499       N  
ATOM   4507  N   ALA B 159      73.461  14.169-117.238  1.00 71.19           N  
ANISOU 4507  N   ALA B 159     8017  11805   7226    -59    377  -1110       N  
ATOM   4508  CA  ALA B 159      73.478  12.917-116.495  1.00 58.83           C  
ANISOU 4508  CA  ALA B 159     6502  10030   5820    -70    406  -1187       C  
ATOM   4509  C   ALA B 159      73.731  11.773-117.463  1.00 71.78           C  
ANISOU 4509  C   ALA B 159     8173  11655   7444    -71    463  -1393       C  
ATOM   4510  O   ALA B 159      73.165  11.746-118.558  1.00 74.00           O  
ANISOU 4510  O   ALA B 159     8446  12080   7591   -121    449  -1508       O  
ATOM   4511  CB  ALA B 159      72.167  12.684-115.737  1.00 51.27           C  
ANISOU 4511  CB  ALA B 159     5557   9000   4924   -160    346  -1178       C  
ATOM   4512  N   GLY B 160      74.577  10.834-117.047  1.00 78.22           N  
ANISOU 4512  N   GLY B 160     9025  12297   8398    -15    525  -1440       N  
ATOM   4513  CA  GLY B 160      74.902   9.674-117.850  1.00 80.82           C  
ANISOU 4513  CA  GLY B 160     9387  12576   8744     -4    589  -1644       C  
ATOM   4514  C   GLY B 160      73.861   8.585-117.880  1.00 86.17           C  
ANISOU 4514  C   GLY B 160    10113  13146   9480   -100    568  -1796       C  
ATOM   4515  O   GLY B 160      74.034   7.601-118.604  1.00 90.75           O  
ANISOU 4515  O   GLY B 160    10726  13681  10072   -101    617  -1987       O  
ATOM   4516  N   ASN B 161      72.774   8.722-117.121  1.00 79.07           N  
ANISOU 4516  N   ASN B 161     9217  12205   8621   -185    499  -1723       N  
ATOM   4517  CA  ASN B 161      71.738   7.704-117.080  1.00 73.94           C  
ANISOU 4517  CA  ASN B 161     8607  11450   8039   -290    477  -1854       C  
ATOM   4518  C   ASN B 161      70.792   7.855-118.270  1.00 77.30           C  
ANISOU 4518  C   ASN B 161     9006  12067   8297   -377    435  -1989       C  
ATOM   4519  O   ASN B 161      70.992   8.685-119.161  1.00 78.16           O  
ANISOU 4519  O   ASN B 161     9076  12386   8236   -349    428  -1981       O  
ATOM   4520  CB  ASN B 161      70.974   7.777-115.759  1.00 71.21           C  
ANISOU 4520  CB  ASN B 161     8265  10989   7801   -349    429  -1718       C  
ATOM   4521  CG  ASN B 161      70.412   9.160-115.476  1.00 67.25           C  
ANISOU 4521  CG  ASN B 161     7702  10652   7197   -365    366  -1559       C  
ATOM   4522  OD1 ASN B 161      70.344  10.013-116.362  1.00 64.09           O  
ANISOU 4522  OD1 ASN B 161     7257  10455   6640   -353    343  -1560       O  
ATOM   4523  ND2 ASN B 161      70.003   9.387-114.233  1.00 63.41           N  
ANISOU 4523  ND2 ASN B 161     7216  10077   6799   -390    339  -1420       N  
ATOM   4524  N   LYS B 162      69.743   7.036-118.284  1.00 75.97           N  
ANISOU 4524  N   LYS B 162     8860  11828   8176   -488    404  -2109       N  
ATOM   4525  CA  LYS B 162      68.707   7.096-119.308  1.00 78.68           C  
ANISOU 4525  CA  LYS B 162     9176  12345   8375   -587    348  -2239       C  
ATOM   4526  C   LYS B 162      67.555   8.015-118.926  1.00 76.60           C  
ANISOU 4526  C   LYS B 162     8848  12200   8056   -656    259  -2110       C  
ATOM   4527  O   LYS B 162      66.618   8.173-119.716  1.00 74.97           O  
ANISOU 4527  O   LYS B 162     8604  12153   7729   -738    197  -2194       O  
ATOM   4528  CB  LYS B 162      68.155   5.692-119.586  1.00 84.61           C  
ANISOU 4528  CB  LYS B 162     9977  12959   9212   -682    358  -2455       C  
ATOM   4529  CG  LYS B 162      69.207   4.619-119.815  1.00 90.13           C  
ANISOU 4529  CG  LYS B 162    10744  13490  10012   -614    449  -2595       C  
ATOM   4530  CD  LYS B 162      69.719   4.626-121.243  1.00 93.50           C  
ANISOU 4530  CD  LYS B 162    11169  14086  10271   -578    486  -2763       C  
ATOM   4531  CE  LYS B 162      70.325   3.280-121.603  1.00 96.25           C  
ANISOU 4531  CE  LYS B 162    11586  14255  10729   -554    566  -2977       C  
ATOM   4532  NZ  LYS B 162      69.334   2.179-121.437  1.00 96.17           N  
ANISOU 4532  NZ  LYS B 162    11619  14083  10837   -683    535  -3121       N  
ATOM   4533  N   LEU B 163      67.608   8.622-117.740  1.00 69.29           N  
ANISOU 4533  N   LEU B 163     7907  11205   7214   -623    250  -1914       N  
ATOM   4534  CA  LEU B 163      66.480   9.371-117.196  1.00 59.89           C  
ANISOU 4534  CA  LEU B 163     6658  10091   6008   -687    176  -1801       C  
ATOM   4535  C   LEU B 163      66.275  10.671-117.966  1.00 56.56           C  
ANISOU 4535  C   LEU B 163     6168   9919   5404   -659    121  -1732       C  
ATOM   4536  O   LEU B 163      67.166  11.526-118.006  1.00 54.89           O  
ANISOU 4536  O   LEU B 163     5948   9768   5138   -561    141  -1617       O  
ATOM   4537  CB  LEU B 163      66.725   9.660-115.718  1.00 59.52           C  
ANISOU 4537  CB  LEU B 163     6620   9902   6092   -650    193  -1620       C  
ATOM   4538  CG  LEU B 163      65.547  10.149-114.884  1.00 51.38           C  
ANISOU 4538  CG  LEU B 163     5538   8891   5091   -722    139  -1520       C  
ATOM   4539  CD1 LEU B 163      64.504   9.058-114.829  1.00 49.41           C  
ANISOU 4539  CD1 LEU B 163     5297   8558   4918   -852    127  -1648       C  
ATOM   4540  CD2 LEU B 163      66.013  10.522-113.487  1.00 49.88           C  
ANISOU 4540  CD2 LEU B 163     5366   8582   5003   -669    164  -1343       C  
ATOM   4541  N   ALA B 164      65.080  10.836-118.539  1.00 53.84           N  
ANISOU 4541  N   ALA B 164     5770   9714   4973   -747     46  -1792       N  
ATOM   4542  CA  ALA B 164      64.817  11.957-119.438  1.00 51.79           C  
ANISOU 4542  CA  ALA B 164     5448   9698   4533   -727    -17  -1741       C  
ATOM   4543  C   ALA B 164      64.663  13.282-118.696  1.00 48.05           C  
ANISOU 4543  C   ALA B 164     4921   9272   4065   -674    -53  -1526       C  
ATOM   4544  O   ALA B 164      65.191  14.306-119.143  1.00 47.05           O  
ANISOU 4544  O   ALA B 164     4773   9271   3832   -600    -64  -1424       O  
ATOM   4545  CB  ALA B 164      63.567  11.676-120.269  1.00 53.87           C  
ANISOU 4545  CB  ALA B 164     5665  10097   4707   -838    -96  -1873       C  
ATOM   4546  N   MET B 165      63.934  13.295-117.583  1.00 49.20           N  
ANISOU 4546  N   MET B 165     5043   9320   4332   -714    -70  -1456       N  
ATOM   4547  CA  MET B 165      63.658  14.547-116.893  1.00 42.82           C  
ANISOU 4547  CA  MET B 165     4180   8561   3529   -669   -106  -1274       C  
ATOM   4548  C   MET B 165      64.848  14.972-116.046  1.00 43.19           C  
ANISOU 4548  C   MET B 165     4272   8496   3644   -572    -46  -1142       C  
ATOM   4549  O   MET B 165      65.604  14.144-115.534  1.00 44.03           O  
ANISOU 4549  O   MET B 165     4443   8439   3846   -557     21  -1172       O  
ATOM   4550  CB  MET B 165      62.398  14.422-116.041  1.00 45.99           C  
ANISOU 4550  CB  MET B 165     4531   8919   4023   -751   -139  -1260       C  
ATOM   4551  CG  MET B 165      61.142  14.367-116.890  1.00 52.32           C  
ANISOU 4551  CG  MET B 165     5257   9876   4745   -838   -220  -1355       C  
ATOM   4552  SD  MET B 165      59.724  13.621-116.075  1.00 50.67           S  
ANISOU 4552  SD  MET B 165     4999   9590   4664   -970   -237  -1412       S  
ATOM   4553  CE  MET B 165      58.620  13.413-117.471  1.00 47.26           C  
ANISOU 4553  CE  MET B 165     4490   9361   4107  -1064   -335  -1561       C  
ATOM   4554  N   GLN B 166      64.995  16.287-115.890  1.00 43.31           N  
ANISOU 4554  N   GLN B 166     4247   8595   3614   -506    -75   -991       N  
ATOM   4555  CA  GLN B 166      66.271  16.848-115.462  1.00 41.35           C  
ANISOU 4555  CA  GLN B 166     4033   8290   3388   -410    -28   -876       C  
ATOM   4556  C   GLN B 166      66.467  16.767-113.949  1.00 40.60           C  
ANISOU 4556  C   GLN B 166     3965   8025   3437   -398      5   -789       C  
ATOM   4557  O   GLN B 166      67.433  16.161-113.478  1.00 40.63           O  
ANISOU 4557  O   GLN B 166     4026   7896   3515   -364     64   -790       O  
ATOM   4558  CB  GLN B 166      66.387  18.292-115.960  1.00 41.40           C  
ANISOU 4558  CB  GLN B 166     3991   8449   3290   -351    -74   -752       C  
ATOM   4559  CG  GLN B 166      67.729  18.946-115.678  1.00 47.18           C  
ANISOU 4559  CG  GLN B 166     4749   9142   4034   -261    -31   -636       C  
ATOM   4560  CD  GLN B 166      67.984  20.137-116.577  1.00 48.93           C  
ANISOU 4560  CD  GLN B 166     4934   9527   4130   -216    -66   -545       C  
ATOM   4561  OE1 GLN B 166      68.363  19.981-117.737  1.00 53.60           O  
ANISOU 4561  OE1 GLN B 166     5531  10230   4605   -213    -56   -604       O  
ATOM   4562  NE2 GLN B 166      67.764  21.334-116.053  1.00 45.87           N  
ANISOU 4562  NE2 GLN B 166     4512   9153   3764   -183   -107   -403       N  
ATOM   4563  N   GLU B 167      65.571  17.377-113.167  1.00 36.90           N  
ANISOU 4563  N   GLU B 167     3452   7563   3007   -421    -32   -712       N  
ATOM   4564  CA  GLU B 167      65.768  17.496-111.727  1.00 41.05           C  
ANISOU 4564  CA  GLU B 167     4001   7955   3642   -406     -3   -617       C  
ATOM   4565  C   GLU B 167      64.563  16.999-110.942  1.00 44.10           C  
ANISOU 4565  C   GLU B 167     4365   8289   4101   -493     -9   -647       C  
ATOM   4566  O   GLU B 167      63.414  17.261-111.307  1.00 44.42           O  
ANISOU 4566  O   GLU B 167     4337   8435   4106   -542    -57   -679       O  
ATOM   4567  CB  GLU B 167      66.035  18.942-111.307  1.00 42.64           C  
ANISOU 4567  CB  GLU B 167     4172   8207   3824   -335    -27   -470       C  
ATOM   4568  CG  GLU B 167      66.862  19.769-112.266  1.00 52.20           C  
ANISOU 4568  CG  GLU B 167     5374   9521   4940   -264    -40   -423       C  
ATOM   4569  CD  GLU B 167      66.884  21.231-111.871  1.00 50.17           C  
ANISOU 4569  CD  GLU B 167     5080   9307   4676   -210    -74   -284       C  
ATOM   4570  OE1 GLU B 167      67.573  22.018-112.552  1.00 50.89           O  
ANISOU 4570  OE1 GLU B 167     5163   9474   4700   -156    -85   -221       O  
ATOM   4571  OE2 GLU B 167      66.205  21.593-110.882  1.00 40.66           O  
ANISOU 4571  OE2 GLU B 167     3854   8061   3535   -224    -87   -240       O  
ATOM   4572  N   PHE B 168      64.844  16.325-109.830  1.00 43.49           N  
ANISOU 4572  N   PHE B 168     4341   8056   4126   -511     38   -623       N  
ATOM   4573  CA  PHE B 168      63.855  15.980-108.818  1.00 37.20           C  
ANISOU 4573  CA  PHE B 168     3530   7200   3404   -589     47   -615       C  
ATOM   4574  C   PHE B 168      64.276  16.637-107.511  1.00 40.99           C  
ANISOU 4574  C   PHE B 168     4029   7617   3927   -543     68   -482       C  
ATOM   4575  O   PHE B 168      65.349  16.333-106.976  1.00 45.24           O  
ANISOU 4575  O   PHE B 168     4636   8047   4508   -500    102   -434       O  
ATOM   4576  CB  PHE B 168      63.744  14.464-108.664  1.00 36.90           C  
ANISOU 4576  CB  PHE B 168     3546   7028   3446   -670     85   -708       C  
ATOM   4577  CG  PHE B 168      63.271  13.767-109.907  1.00 43.98           C  
ANISOU 4577  CG  PHE B 168     4426   7981   4303   -728     63   -859       C  
ATOM   4578  CD1 PHE B 168      64.169  13.399-110.895  1.00 47.24           C  
ANISOU 4578  CD1 PHE B 168     4879   8396   4673   -682     74   -934       C  
ATOM   4579  CD2 PHE B 168      61.926  13.491-110.094  1.00 46.87           C  
ANISOU 4579  CD2 PHE B 168     4731   8407   4671   -831     33   -932       C  
ATOM   4580  CE1 PHE B 168      63.736  12.766-112.044  1.00 49.60           C  
ANISOU 4580  CE1 PHE B 168     5168   8756   4923   -739     54  -1085       C  
ATOM   4581  CE2 PHE B 168      61.485  12.856-111.241  1.00 40.31           C  
ANISOU 4581  CE2 PHE B 168     3883   7635   3797   -892      5  -1078       C  
ATOM   4582  CZ  PHE B 168      62.394  12.492-112.217  1.00 51.73           C  
ANISOU 4582  CZ  PHE B 168     5380   9083   5192   -846     15  -1158       C  
ATOM   4583  N   MET B 169      63.436  17.532-107.000  1.00 34.40           N  
ANISOU 4583  N   MET B 169     3133   6854   3084   -550     47   -428       N  
ATOM   4584  CA  MET B 169      63.757  18.355-105.844  1.00 39.62           C  
ANISOU 4584  CA  MET B 169     3804   7482   3767   -503     61   -314       C  
ATOM   4585  C   MET B 169      62.885  17.983-104.650  1.00 40.92           C  
ANISOU 4585  C   MET B 169     3962   7596   3989   -578     94   -301       C  
ATOM   4586  O   MET B 169      61.810  17.395-104.797  1.00 37.94           O  
ANISOU 4586  O   MET B 169     3543   7241   3631   -665     96   -371       O  
ATOM   4587  CB  MET B 169      63.578  19.840-106.179  1.00 36.13           C  
ANISOU 4587  CB  MET B 169     3298   7162   3269   -436     16   -258       C  
ATOM   4588  CG  MET B 169      64.591  20.393-107.162  1.00 44.95           C  
ANISOU 4588  CG  MET B 169     4427   8327   4325   -357    -10   -234       C  
ATOM   4589  SD  MET B 169      64.037  21.953-107.887  1.00 52.31           S  
ANISOU 4589  SD  MET B 169     5272   9411   5191   -302    -76   -184       S  
ATOM   4590  CE  MET B 169      62.932  21.390-109.187  1.00 33.73           C  
ANISOU 4590  CE  MET B 169     2856   7179   2780   -365   -120   -296       C  
ATOM   4591  N   ILE B 170      63.371  18.330-103.457  1.00 39.27           N  
ANISOU 4591  N   ILE B 170     3794   7324   3805   -551    121   -210       N  
ATOM   4592  CA  ILE B 170      62.626  18.171-102.213  1.00 37.41           C  
ANISOU 4592  CA  ILE B 170     3554   7057   3605   -614    159   -181       C  
ATOM   4593  C   ILE B 170      62.469  19.539-101.567  1.00 38.05           C  
ANISOU 4593  C   ILE B 170     3595   7205   3659   -559    151   -116       C  
ATOM   4594  O   ILE B 170      63.396  20.358-101.584  1.00 33.61           O  
ANISOU 4594  O   ILE B 170     3055   6642   3072   -474    129    -60       O  
ATOM   4595  CB  ILE B 170      63.302  17.184-101.237  1.00 37.97           C  
ANISOU 4595  CB  ILE B 170     3719   6984   3725   -645    202   -134       C  
ATOM   4596  CG1 ILE B 170      64.732  17.627-100.902  1.00 40.06           C  
ANISOU 4596  CG1 ILE B 170     4045   7198   3979   -553    193    -53       C  
ATOM   4597  CG2 ILE B 170      63.286  15.782-101.809  1.00 34.51           C  
ANISOU 4597  CG2 ILE B 170     3317   6462   3334   -708    215   -208       C  
ATOM   4598  CD1 ILE B 170      65.406  16.791 -99.815  1.00 36.75           C  
ANISOU 4598  CD1 ILE B 170     3713   6647   3604   -573    224     14       C  
ATOM   4599  N   LEU B 171      61.291  19.781-101.004  1.00 36.43           N  
ANISOU 4599  N   LEU B 171     3325   7053   3462   -608    170   -129       N  
ATOM   4600  CA  LEU B 171      60.937  21.068-100.407  1.00 37.79           C  
ANISOU 4600  CA  LEU B 171     3448   7291   3618   -558    168    -90       C  
ATOM   4601  C   LEU B 171      60.394  20.812 -99.010  1.00 44.45           C  
ANISOU 4601  C   LEU B 171     4301   8108   4478   -621    232    -69       C  
ATOM   4602  O   LEU B 171      59.279  20.264 -98.877  1.00 50.13           O  
ANISOU 4602  O   LEU B 171     4966   8860   5220   -706    263   -115       O  
ATOM   4603  CB  LEU B 171      59.897  21.808-101.249  1.00 41.68           C  
ANISOU 4603  CB  LEU B 171     3827   7908   4102   -539    128   -137       C  
ATOM   4604  CG  LEU B 171      60.239  22.373-102.633  1.00 41.12           C  
ANISOU 4604  CG  LEU B 171     3729   7900   3996   -471     58   -145       C  
ATOM   4605  CD1 LEU B 171      60.390  21.276-103.676  1.00 33.07           C  
ANISOU 4605  CD1 LEU B 171     2730   6873   2963   -518     42   -209       C  
ATOM   4606  CD2 LEU B 171      59.171  23.366-103.064  1.00 39.99           C  
ANISOU 4606  CD2 LEU B 171     3470   7874   3850   -438     18   -159       C  
ATOM   4607  N   PRO B 172      61.141  21.192 -97.921  1.00 43.81           N  
ANISOU 4607  N   PRO B 172     4287   7977   4381   -589    254      1       N  
ATOM   4608  CA  PRO B 172      60.624  20.980 -96.553  1.00 37.07           C  
ANISOU 4608  CA  PRO B 172     3447   7115   3524   -653    318     24       C  
ATOM   4609  C   PRO B 172      59.623  22.060 -96.154  1.00 40.70           C  
ANISOU 4609  C   PRO B 172     3816   7676   3974   -634    338     -4       C  
ATOM   4610  O   PRO B 172      59.882  22.931 -95.315  1.00 36.55           O  
ANISOU 4610  O   PRO B 172     3306   7159   3421   -588    352     25       O  
ATOM   4611  CB  PRO B 172      61.905  21.005 -95.704  1.00 32.11           C  
ANISOU 4611  CB  PRO B 172     2925   6405   2871   -619    319    104       C  
ATOM   4612  CG  PRO B 172      63.063  21.243 -96.664  1.00 31.38           C  
ANISOU 4612  CG  PRO B 172     2862   6279   2782   -536    258    119       C  
ATOM   4613  CD  PRO B 172      62.478  21.799 -97.909  1.00 44.44           C  
ANISOU 4613  CD  PRO B 172     4429   8014   4440   -503    221     59       C  
ATOM   4614  N   VAL B 173      58.438  21.999 -96.770  1.00 41.05           N  
ANISOU 4614  N   VAL B 173     3755   7797   4043   -668    338    -68       N  
ATOM   4615  CA  VAL B 173      57.404  22.994 -96.511  1.00 38.80           C  
ANISOU 4615  CA  VAL B 173     3365   7612   3766   -641    354   -103       C  
ATOM   4616  C   VAL B 173      56.906  22.925 -95.069  1.00 42.18           C  
ANISOU 4616  C   VAL B 173     3797   8051   4177   -697    441    -94       C  
ATOM   4617  O   VAL B 173      56.505  23.947 -94.498  1.00 35.35           O  
ANISOU 4617  O   VAL B 173     2883   7243   3306   -648    465   -109       O  
ATOM   4618  CB  VAL B 173      56.243  22.833 -97.509  1.00 34.59           C  
ANISOU 4618  CB  VAL B 173     2709   7165   3267   -670    328   -170       C  
ATOM   4619  CG1 VAL B 173      56.679  23.245 -98.901  1.00 34.13           C  
ANISOU 4619  CG1 VAL B 173     2638   7126   3205   -596    239   -176       C  
ATOM   4620  CG2 VAL B 173      55.723  21.400 -97.508  1.00 35.41           C  
ANISOU 4620  CG2 VAL B 173     2816   7245   3392   -801    364   -200       C  
ATOM   4621  N   GLY B 174      56.915  21.740 -94.456  1.00 34.89           N  
ANISOU 4621  N   GLY B 174     2933   7076   3248   -801    492    -69       N  
ATOM   4622  CA  GLY B 174      56.426  21.578 -93.103  1.00 41.75           C  
ANISOU 4622  CA  GLY B 174     3809   7966   4087   -868    580    -51       C  
ATOM   4623  C   GLY B 174      57.423  21.870 -92.002  1.00 43.66           C  
ANISOU 4623  C   GLY B 174     4162   8159   4268   -840    597     16       C  
ATOM   4624  O   GLY B 174      57.135  21.607 -90.833  1.00 45.63           O  
ANISOU 4624  O   GLY B 174     4437   8425   4474   -906    670     41       O  
ATOM   4625  N   ALA B 175      58.589  22.412 -92.339  1.00 44.06           N  
ANISOU 4625  N   ALA B 175     4275   8157   4308   -748    530     46       N  
ATOM   4626  CA  ALA B 175      59.620  22.705 -91.359  1.00 36.81           C  
ANISOU 4626  CA  ALA B 175     3459   7194   3333   -720    530    108       C  
ATOM   4627  C   ALA B 175      59.242  23.921 -90.515  1.00 39.82           C  
ANISOU 4627  C   ALA B 175     3804   7650   3675   -678    566     74       C  
ATOM   4628  O   ALA B 175      58.446  24.774 -90.920  1.00 40.29           O  
ANISOU 4628  O   ALA B 175     3763   7777   3767   -631    568      8       O  
ATOM   4629  CB  ALA B 175      60.963  22.938 -92.055  1.00 33.33           C  
ANISOU 4629  CB  ALA B 175     3078   6681   2903   -638    448    145       C  
ATOM   4630  N   GLU B 176      59.839  23.988 -89.319  1.00 43.39           N  
ANISOU 4630  N   GLU B 176     4343   8088   4058   -694    591    119       N  
ATOM   4631  CA  GLU B 176      59.563  25.054 -88.361  1.00 47.72           C  
ANISOU 4631  CA  GLU B 176     4876   8702   4555   -664    632     78       C  
ATOM   4632  C   GLU B 176      60.295  26.349 -88.690  1.00 44.71           C  
ANISOU 4632  C   GLU B 176     4499   8300   4190   -551    565     57       C  
ATOM   4633  O   GLU B 176      59.847  27.428 -88.281  1.00 38.91           O  
ANISOU 4633  O   GLU B 176     3718   7615   3450   -505    591     -7       O  
ATOM   4634  CB  GLU B 176      59.952  24.596 -86.951  1.00 56.29           C  
ANISOU 4634  CB  GLU B 176     6057   9788   5542   -733    679    135       C  
ATOM   4635  CG  GLU B 176      59.568  23.152 -86.631  1.00 69.98           C  
ANISOU 4635  CG  GLU B 176     7820  11507   7263   -851    729    194       C  
ATOM   4636  CD  GLU B 176      58.064  22.941 -86.571  1.00 84.21           C  
ANISOU 4636  CD  GLU B 176     9516  13396   9084   -920    818    134       C  
ATOM   4637  OE1 GLU B 176      57.360  23.824 -86.037  1.00 85.76           O  
ANISOU 4637  OE1 GLU B 176     9649  13686   9252   -899    875     64       O  
ATOM   4638  OE2 GLU B 176      57.586  21.894 -87.061  1.00 87.71           O  
ANISOU 4638  OE2 GLU B 176     9936  13813   9576   -995    832    152       O  
ATOM   4639  N   SER B 177      61.405  26.264 -89.413  1.00 39.20           N  
ANISOU 4639  N   SER B 177     3852   7526   3518   -507    484    108       N  
ATOM   4640  CA  SER B 177      62.239  27.419 -89.715  1.00 40.11           C  
ANISOU 4640  CA  SER B 177     3979   7611   3649   -413    419    105       C  
ATOM   4641  C   SER B 177      63.090  27.069 -90.925  1.00 36.35           C  
ANISOU 4641  C   SER B 177     3519   7073   3220   -379    345    152       C  
ATOM   4642  O   SER B 177      63.078  25.932 -91.405  1.00 33.83           O  
ANISOU 4642  O   SER B 177     3211   6729   2914   -425    347    179       O  
ATOM   4643  CB  SER B 177      63.118  27.797 -88.521  1.00 39.93           C  
ANISOU 4643  CB  SER B 177     4046   7572   3555   -416    415    132       C  
ATOM   4644  OG  SER B 177      64.106  26.800 -88.303  1.00 35.90           O  
ANISOU 4644  OG  SER B 177     3622   7004   3013   -456    387    219       O  
ATOM   4645  N   PHE B 178      63.848  28.050 -91.412  1.00 33.91           N  
ANISOU 4645  N   PHE B 178     3212   6736   2936   -300    284    160       N  
ATOM   4646  CA  PHE B 178      64.781  27.738 -92.485  1.00 34.13           C  
ANISOU 4646  CA  PHE B 178     3259   6714   2995   -269    222    209       C  
ATOM   4647  C   PHE B 178      65.883  26.807 -91.998  1.00 32.96           C  
ANISOU 4647  C   PHE B 178     3201   6506   2815   -303    210    278       C  
ATOM   4648  O   PHE B 178      66.319  25.915 -92.737  1.00 34.02           O  
ANISOU 4648  O   PHE B 178     3351   6603   2974   -311    192    307       O  
ATOM   4649  CB  PHE B 178      65.388  29.006 -93.075  1.00 33.84           C  
ANISOU 4649  CB  PHE B 178     3205   6662   2991   -186    164    214       C  
ATOM   4650  CG  PHE B 178      66.231  28.732 -94.275  1.00 40.68           C  
ANISOU 4650  CG  PHE B 178     4075   7497   3883   -155    112    259       C  
ATOM   4651  CD1 PHE B 178      65.652  28.639 -95.530  1.00 28.84           C  
ANISOU 4651  CD1 PHE B 178     2512   6031   2413   -137     98    240       C  
ATOM   4652  CD2 PHE B 178      67.591  28.497 -94.144  1.00 38.31           C  
ANISOU 4652  CD2 PHE B 178     3840   7142   3573   -148     79    319       C  
ATOM   4653  CE1 PHE B 178      66.418  28.355 -96.636  1.00 35.44           C  
ANISOU 4653  CE1 PHE B 178     3355   6852   3259   -114     58    274       C  
ATOM   4654  CE2 PHE B 178      68.362  28.207 -95.244  1.00 38.76           C  
ANISOU 4654  CE2 PHE B 178     3895   7180   3653   -120     43    353       C  
ATOM   4655  CZ  PHE B 178      67.778  28.137 -96.495  1.00 41.26           C  
ANISOU 4655  CZ  PHE B 178     4154   7534   3989   -104     36    328       C  
ATOM   4656  N   ARG B 179      66.348  27.004 -90.761  1.00 33.77           N  
ANISOU 4656  N   ARG B 179     3364   6602   2866   -322    218    301       N  
ATOM   4657  CA  ARG B 179      67.380  26.137 -90.200  1.00 37.20           C  
ANISOU 4657  CA  ARG B 179     3880   6984   3269   -351    198    377       C  
ATOM   4658  C   ARG B 179      66.879  24.708 -90.057  1.00 36.35           C  
ANISOU 4658  C   ARG B 179     3793   6859   3157   -424    242    401       C  
ATOM   4659  O   ARG B 179      67.599  23.754 -90.375  1.00 39.41           O  
ANISOU 4659  O   ARG B 179     4221   7182   3570   -430    218    456       O  
ATOM   4660  CB  ARG B 179      67.837  26.680 -88.848  1.00 39.74           C  
ANISOU 4660  CB  ARG B 179     4258   7321   3521   -364    194    393       C  
ATOM   4661  CG  ARG B 179      69.134  27.459 -88.902  1.00 56.47           C  
ANISOU 4661  CG  ARG B 179     6399   9406   5649   -309    122    423       C  
ATOM   4662  CD  ARG B 179      69.332  28.279 -87.643  1.00 63.94           C  
ANISOU 4662  CD  ARG B 179     7384  10383   6526   -322    118    403       C  
ATOM   4663  NE  ARG B 179      68.683  29.582 -87.746  1.00 67.00           N  
ANISOU 4663  NE  ARG B 179     7722  10800   6935   -284    133    316       N  
ATOM   4664  CZ  ARG B 179      68.338  30.328 -86.701  1.00 72.24           C  
ANISOU 4664  CZ  ARG B 179     8402  11504   7543   -298    160    257       C  
ATOM   4665  NH1 ARG B 179      68.564  29.896 -85.468  1.00 75.43           N  
ANISOU 4665  NH1 ARG B 179     8872  11939   7849   -356    174    279       N  
ATOM   4666  NH2 ARG B 179      67.753  31.501 -86.888  1.00 73.34           N  
ANISOU 4666  NH2 ARG B 179     8490  11653   7722   -253    173    174       N  
ATOM   4667  N   ASP B 180      65.649  24.540 -89.566  1.00 35.84           N  
ANISOU 4667  N   ASP B 180     3700   6848   3069   -482    309    360       N  
ATOM   4668  CA  ASP B 180      65.049  23.214 -89.524  1.00 33.71           C  
ANISOU 4668  CA  ASP B 180     3440   6559   2808   -562    355    380       C  
ATOM   4669  C   ASP B 180      64.876  22.643 -90.928  1.00 34.61           C  
ANISOU 4669  C   ASP B 180     3511   6641   2998   -551    336    353       C  
ATOM   4670  O   ASP B 180      64.992  21.428 -91.123  1.00 37.14           O  
ANISOU 4670  O   ASP B 180     3866   6898   3347   -597    342    385       O  
ATOM   4671  CB  ASP B 180      63.708  23.280 -88.789  1.00 39.43           C  
ANISOU 4671  CB  ASP B 180     4124   7363   3495   -628    436    334       C  
ATOM   4672  CG  ASP B 180      63.188  21.911 -88.393  1.00 43.78           C  
ANISOU 4672  CG  ASP B 180     4703   7891   4041   -732    489    375       C  
ATOM   4673  OD1 ASP B 180      63.963  21.118 -87.815  1.00 40.41           O  
ANISOU 4673  OD1 ASP B 180     4364   7400   3589   -763    475    463       O  
ATOM   4674  OD2 ASP B 180      62.000  21.628 -88.662  1.00 51.73           O  
ANISOU 4674  OD2 ASP B 180     5639   8942   5074   -784    542    324       O  
ATOM   4675  N   ALA B 181      64.616  23.504 -91.919  1.00 36.11           N  
ANISOU 4675  N   ALA B 181     3628   6870   3221   -489    309    295       N  
ATOM   4676  CA  ALA B 181      64.478  23.034 -93.295  1.00 39.35           C  
ANISOU 4676  CA  ALA B 181     3999   7267   3686   -478    285    265       C  
ATOM   4677  C   ALA B 181      65.809  22.525 -93.836  1.00 33.04           C  
ANISOU 4677  C   ALA B 181     3257   6388   2908   -440    238    313       C  
ATOM   4678  O   ALA B 181      65.844  21.560 -94.610  1.00 30.49           O  
ANISOU 4678  O   ALA B 181     2938   6025   2621   -460    236    300       O  
ATOM   4679  CB  ALA B 181      63.922  24.150 -94.182  1.00 30.46           C  
ANISOU 4679  CB  ALA B 181     2783   6210   2579   -418    260    208       C  
ATOM   4680  N   MET B 182      66.913  23.158 -93.433  1.00 30.69           N  
ANISOU 4680  N   MET B 182     2999   6069   2591   -386    201    363       N  
ATOM   4681  CA  MET B 182      68.233  22.639 -93.778  1.00 32.80           C  
ANISOU 4681  CA  MET B 182     3316   6265   2882   -351    162    415       C  
ATOM   4682  C   MET B 182      68.489  21.289 -93.116  1.00 36.70           C  
ANISOU 4682  C   MET B 182     3878   6683   3384   -405    182    466       C  
ATOM   4683  O   MET B 182      69.091  20.398 -93.727  1.00 35.71           O  
ANISOU 4683  O   MET B 182     3774   6488   3304   -392    169    479       O  
ATOM   4684  CB  MET B 182      69.320  23.644 -93.385  1.00 32.05           C  
ANISOU 4684  CB  MET B 182     3239   6170   2767   -292    117    459       C  
ATOM   4685  CG  MET B 182      69.314  24.933 -94.196  1.00 28.55           C  
ANISOU 4685  CG  MET B 182     2737   5776   2335   -231     88    425       C  
ATOM   4686  SD  MET B 182      69.299  24.628 -95.975  1.00 50.05           S  
ANISOU 4686  SD  MET B 182     5410   8510   5097   -198     74    391       S  
ATOM   4687  CE  MET B 182      70.744  23.580 -96.159  1.00 35.72           C  
ANISOU 4687  CE  MET B 182     3650   6614   3308   -180     58    445       C  
ATOM   4688  N   ARG B 183      68.039  21.111 -91.870  1.00 34.67           N  
ANISOU 4688  N   ARG B 183     3656   6435   3083   -465    215    497       N  
ATOM   4689  CA  ARG B 183      68.192  19.810 -91.223  1.00 33.34           C  
ANISOU 4689  CA  ARG B 183     3554   6191   2923   -523    234    561       C  
ATOM   4690  C   ARG B 183      67.385  18.733 -91.944  1.00 38.61           C  
ANISOU 4690  C   ARG B 183     4204   6819   3648   -579    270    518       C  
ATOM   4691  O   ARG B 183      67.885  17.623 -92.166  1.00 37.73           O  
ANISOU 4691  O   ARG B 183     4138   6609   3590   -588    263    550       O  
ATOM   4692  CB  ARG B 183      67.780  19.892 -89.752  1.00 36.68           C  
ANISOU 4692  CB  ARG B 183     4016   6651   3270   -585    268    606       C  
ATOM   4693  CG  ARG B 183      67.820  18.550 -89.042  1.00 37.49           C  
ANISOU 4693  CG  ARG B 183     4190   6678   3378   -656    289    689       C  
ATOM   4694  CD  ARG B 183      67.070  18.570 -87.719  1.00 40.14           C  
ANISOU 4694  CD  ARG B 183     4551   7073   3626   -739    343    721       C  
ATOM   4695  NE  ARG B 183      66.774  17.209 -87.284  1.00 47.10           N  
ANISOU 4695  NE  ARG B 183     5486   7882   4527   -825    378    792       N  
ATOM   4696  CZ  ARG B 183      66.440  16.864 -86.044  1.00 62.85           C  
ANISOU 4696  CZ  ARG B 183     7531   9901   6447   -905    417    866       C  
ATOM   4697  NH1 ARG B 183      66.360  17.783 -85.089  1.00 70.68           N  
ANISOU 4697  NH1 ARG B 183     8529  10998   7330   -907    429    866       N  
ATOM   4698  NH2 ARG B 183      66.193  15.593 -85.758  1.00 62.57           N  
ANISOU 4698  NH2 ARG B 183     7545   9785   6444   -984    446    940       N  
ATOM   4699  N   LEU B 184      66.140  19.042 -92.326  1.00 32.06           N  
ANISOU 4699  N   LEU B 184     3305   6062   2815   -617    306    440       N  
ATOM   4700  CA  LEU B 184      65.310  18.048 -93.008  1.00 37.27           C  
ANISOU 4700  CA  LEU B 184     3940   6694   3528   -682    336    389       C  
ATOM   4701  C   LEU B 184      65.892  17.678 -94.370  1.00 37.09           C  
ANISOU 4701  C   LEU B 184     3908   6623   3561   -630    297    345       C  
ATOM   4702  O   LEU B 184      65.927  16.496 -94.737  1.00 37.00           O  
ANISOU 4702  O   LEU B 184     3927   6525   3606   -669    307    335       O  
ATOM   4703  CB  LEU B 184      63.872  18.559 -93.171  1.00 32.88           C  
ANISOU 4703  CB  LEU B 184     3293   6242   2957   -726    373    312       C  
ATOM   4704  CG  LEU B 184      63.016  18.981 -91.967  1.00 42.48           C  
ANISOU 4704  CG  LEU B 184     4492   7530   4118   -781    430    324       C  
ATOM   4705  CD1 LEU B 184      61.559  18.572 -92.164  1.00 39.34           C  
ANISOU 4705  CD1 LEU B 184     4018   7185   3745   -869    483    262       C  
ATOM   4706  CD2 LEU B 184      63.542  18.429 -90.660  1.00 33.87           C  
ANISOU 4706  CD2 LEU B 184     3495   6387   2987   -824    451    423       C  
ATOM   4707  N   GLY B 185      66.352  18.669 -95.135  1.00 31.54           N  
ANISOU 4707  N   GLY B 185     3165   5975   2844   -546    257    317       N  
ATOM   4708  CA  GLY B 185      66.945  18.370 -96.429  1.00 32.86           C  
ANISOU 4708  CA  GLY B 185     3323   6115   3047   -497    227    276       C  
ATOM   4709  C   GLY B 185      68.194  17.515 -96.315  1.00 37.54           C  
ANISOU 4709  C   GLY B 185     3988   6595   3681   -466    214    330       C  
ATOM   4710  O   GLY B 185      68.347  16.517 -97.026  1.00 35.29           O  
ANISOU 4710  O   GLY B 185     3720   6241   3449   -475    221    290       O  
ATOM   4711  N   ALA B 186      69.102  17.892 -95.409  1.00 36.93           N  
ANISOU 4711  N   ALA B 186     3951   6496   3584   -427    194    416       N  
ATOM   4712  CA  ALA B 186      70.352  17.153 -95.246  1.00 31.47           C  
ANISOU 4712  CA  ALA B 186     3317   5703   2937   -386    173    478       C  
ATOM   4713  C   ALA B 186      70.103  15.721 -94.789  1.00 33.89           C  
ANISOU 4713  C   ALA B 186     3682   5897   3297   -451    201    504       C  
ATOM   4714  O   ALA B 186      70.763  14.788 -95.261  1.00 34.93           O  
ANISOU 4714  O   ALA B 186     3843   5928   3500   -423    196    502       O  
ATOM   4715  CB  ALA B 186      71.264  17.875 -94.252  1.00 31.10           C  
ANISOU 4715  CB  ALA B 186     3295   5669   2851   -345    138    568       C  
ATOM   4716  N   GLU B 187      69.157  15.528 -93.865  1.00 34.98           N  
ANISOU 4716  N   GLU B 187     3837   6047   3407   -538    235    531       N  
ATOM   4717  CA  GLU B 187      68.881  14.184 -93.367  1.00 36.20           C  
ANISOU 4717  CA  GLU B 187     4050   6089   3614   -612    263    572       C  
ATOM   4718  C   GLU B 187      68.262  13.307 -94.448  1.00 42.06           C  
ANISOU 4718  C   GLU B 187     4773   6779   4428   -653    288    473       C  
ATOM   4719  O   GLU B 187      68.594  12.121 -94.555  1.00 45.03           O  
ANISOU 4719  O   GLU B 187     5201   7022   4887   -667    293    487       O  
ATOM   4720  CB  GLU B 187      67.971  14.250 -92.137  1.00 38.03           C  
ANISOU 4720  CB  GLU B 187     4299   6364   3786   -705    302    625       C  
ATOM   4721  CG  GLU B 187      68.665  14.769 -90.889  1.00 34.47           C  
ANISOU 4721  CG  GLU B 187     3893   5938   3265   -681    277    732       C  
ATOM   4722  CD  GLU B 187      67.778  14.746 -89.657  1.00 45.36           C  
ANISOU 4722  CD  GLU B 187     5294   7366   4572   -778    325    783       C  
ATOM   4723  OE1 GLU B 187      66.719  14.078 -89.676  1.00 35.90           O  
ANISOU 4723  OE1 GLU B 187     4087   6156   3399   -872    379    758       O  
ATOM   4724  OE2 GLU B 187      68.148  15.399 -88.661  1.00 46.26           O  
ANISOU 4724  OE2 GLU B 187     5434   7539   4603   -765    309    845       O  
ATOM   4725  N   VAL B 188      67.358  13.864 -95.257  1.00 42.62           N  
ANISOU 4725  N   VAL B 188     4770   6950   4472   -673    299    372       N  
ATOM   4726  CA  VAL B 188      66.802  13.098 -96.369  1.00 40.47           C  
ANISOU 4726  CA  VAL B 188     4475   6645   4258   -712    312    265       C  
ATOM   4727  C   VAL B 188      67.867  12.855 -97.429  1.00 39.15           C  
ANISOU 4727  C   VAL B 188     4317   6427   4130   -623    284    220       C  
ATOM   4728  O   VAL B 188      67.970  11.753 -97.984  1.00 40.58           O  
ANISOU 4728  O   VAL B 188     4528   6503   4387   -642    295    167       O  
ATOM   4729  CB  VAL B 188      65.571  13.814 -96.953  1.00 38.37           C  
ANISOU 4729  CB  VAL B 188     4118   6516   3946   -752    320    175       C  
ATOM   4730  CG1 VAL B 188      65.131  13.159 -98.266  1.00 35.18           C  
ANISOU 4730  CG1 VAL B 188     3683   6100   3584   -782    317     54       C  
ATOM   4731  CG2 VAL B 188      64.445  13.799 -95.946  1.00 35.11           C  
ANISOU 4731  CG2 VAL B 188     3689   6140   3512   -852    363    206       C  
ATOM   4732  N   TYR B 189      68.677  13.876 -97.723  1.00 36.51           N  
ANISOU 4732  N   TYR B 189     3957   6167   3749   -527    251    235       N  
ATOM   4733  CA  TYR B 189      69.731  13.728 -98.724  1.00 34.64           C  
ANISOU 4733  CA  TYR B 189     3719   5901   3540   -440    233    196       C  
ATOM   4734  C   TYR B 189      70.686  12.604 -98.344  1.00 39.43           C  
ANISOU 4734  C   TYR B 189     4396   6351   4235   -413    237    246       C  
ATOM   4735  O   TYR B 189      71.022  11.749 -99.172  1.00 41.13           O  
ANISOU 4735  O   TYR B 189     4625   6488   4515   -392    248    174       O  
ATOM   4736  CB  TYR B 189      70.483  15.051 -98.888  1.00 34.12           C  
ANISOU 4736  CB  TYR B 189     3616   5937   3413   -352    201    231       C  
ATOM   4737  CG  TYR B 189      71.673  14.971 -99.815  1.00 45.66           C  
ANISOU 4737  CG  TYR B 189     5071   7381   4898   -262    190    205       C  
ATOM   4738  CD1 TYR B 189      71.512  15.052-101.193  1.00 45.23           C  
ANISOU 4738  CD1 TYR B 189     4974   7391   4821   -247    195    102       C  
ATOM   4739  CD2 TYR B 189      72.961  14.817 -99.314  1.00 50.96           C  
ANISOU 4739  CD2 TYR B 189     5772   7982   5608   -194    174    286       C  
ATOM   4740  CE1 TYR B 189      72.595  14.978-102.045  1.00 43.31           C  
ANISOU 4740  CE1 TYR B 189     4722   7145   4591   -167    197     75       C  
ATOM   4741  CE2 TYR B 189      74.050  14.741-100.161  1.00 52.36           C  
ANISOU 4741  CE2 TYR B 189     5931   8153   5811   -111    173    260       C  
ATOM   4742  CZ  TYR B 189      73.861  14.821-101.526  1.00 46.39           C  
ANISOU 4742  CZ  TYR B 189     5135   7463   5028    -99    189    152       C  
ATOM   4743  OH  TYR B 189      74.943  14.747-102.374  1.00 43.22           O  
ANISOU 4743  OH  TYR B 189     4712   7065   4643    -19    199    122       O  
ATOM   4744  N   HIS B 190      71.124  12.581 -97.085  1.00 39.04           N  
ANISOU 4744  N   HIS B 190     4392   6254   4189   -410    225    369       N  
ATOM   4745  CA  HIS B 190      71.985  11.499 -96.626  1.00 40.29           C  
ANISOU 4745  CA  HIS B 190     4615   6257   4436   -382    219    437       C  
ATOM   4746  C   HIS B 190      71.248  10.167 -96.605  1.00 47.02           C  
ANISOU 4746  C   HIS B 190     5514   6982   5370   -469    254    406       C  
ATOM   4747  O   HIS B 190      71.861   9.118 -96.840  1.00 46.38           O  
ANISOU 4747  O   HIS B 190     5474   6757   5391   -437    257    401       O  
ATOM   4748  CB  HIS B 190      72.540  11.831 -95.243  1.00 41.46           C  
ANISOU 4748  CB  HIS B 190     4799   6401   4552   -368    189    583       C  
ATOM   4749  CG  HIS B 190      73.398  13.057 -95.222  1.00 44.21           C  
ANISOU 4749  CG  HIS B 190     5107   6853   4840   -286    150    614       C  
ATOM   4750  ND1 HIS B 190      73.490  13.884 -94.123  1.00 48.75           N  
ANISOU 4750  ND1 HIS B 190     5689   7496   5338   -295    124    702       N  
ATOM   4751  CD2 HIS B 190      74.205  13.595 -96.166  1.00 39.76           C  
ANISOU 4751  CD2 HIS B 190     4494   6334   4278   -200    135    566       C  
ATOM   4752  CE1 HIS B 190      74.317  14.879 -94.391  1.00 44.88           C  
ANISOU 4752  CE1 HIS B 190     5157   7079   4817   -220     90    706       C  
ATOM   4753  NE2 HIS B 190      74.764  14.727 -95.625  1.00 44.76           N  
ANISOU 4753  NE2 HIS B 190     5105   7053   4848   -163     98    630       N  
ATOM   4754  N   THR B 191      69.940  10.189 -96.331  1.00 36.72           N  
ANISOU 4754  N   THR B 191     4198   5723   4030   -579    282    383       N  
ATOM   4755  CA  THR B 191      69.156   8.958 -96.359  1.00 41.75           C  
ANISOU 4755  CA  THR B 191     4871   6244   4747   -678    316    349       C  
ATOM   4756  C   THR B 191      69.094   8.375 -97.765  1.00 42.46           C  
ANISOU 4756  C   THR B 191     4942   6293   4898   -668    325    197       C  
ATOM   4757  O   THR B 191      69.251   7.162 -97.950  1.00 44.47           O  
ANISOU 4757  O   THR B 191     5248   6386   5261   -688    340    171       O  
ATOM   4758  CB  THR B 191      67.742   9.213 -95.832  1.00 42.67           C  
ANISOU 4758  CB  THR B 191     4960   6445   4809   -801    347    348       C  
ATOM   4759  OG1 THR B 191      67.804   9.710 -94.488  1.00 46.15           O  
ANISOU 4759  OG1 THR B 191     5425   6927   5184   -813    346    481       O  
ATOM   4760  CG2 THR B 191      66.932   7.929 -95.851  1.00 39.54           C  
ANISOU 4760  CG2 THR B 191     4597   5925   4503   -917    384    317       C  
ATOM   4761  N   LEU B 192      68.867   9.222 -98.771  1.00 41.91           N  
ANISOU 4761  N   LEU B 192     4801   6365   4758   -639    316     95       N  
ATOM   4762  CA  LEU B 192      68.797   8.729-100.143  1.00 44.87           C  
ANISOU 4762  CA  LEU B 192     5157   6726   5165   -633    323    -56       C  
ATOM   4763  C   LEU B 192      70.136   8.161-100.602  1.00 52.41           C  
ANISOU 4763  C   LEU B 192     6149   7573   6193   -527    321    -71       C  
ATOM   4764  O   LEU B 192      70.173   7.183-101.359  1.00 55.19           O  
ANISOU 4764  O   LEU B 192     6524   7824   6622   -536    340   -179       O  
ATOM   4765  CB  LEU B 192      68.344   9.843-101.081  1.00 46.02           C  
ANISOU 4765  CB  LEU B 192     5219   7062   5205   -617    307   -139       C  
ATOM   4766  CG  LEU B 192      68.225   9.358-102.525  1.00 42.14           C  
ANISOU 4766  CG  LEU B 192     4709   6580   4724   -619    311   -300       C  
ATOM   4767  CD1 LEU B 192      66.876   8.715-102.788  1.00 43.82           C  
ANISOU 4767  CD1 LEU B 192     4906   6785   4959   -750    323   -394       C  
ATOM   4768  CD2 LEU B 192      68.476  10.487-103.472  1.00 41.47           C  
ANISOU 4768  CD2 LEU B 192     4558   6663   4534   -548    287   -342       C  
ATOM   4769  N   LYS B 193      71.246   8.764-100.161  1.00 53.77           N  
ANISOU 4769  N   LYS B 193     6321   7764   6345   -425    299     28       N  
ATOM   4770  CA  LYS B 193      72.566   8.213-100.457  1.00 51.25           C  
ANISOU 4770  CA  LYS B 193     6027   7340   6106   -319    298     29       C  
ATOM   4771  C   LYS B 193      72.664   6.757-100.018  1.00 47.98           C  
ANISOU 4771  C   LYS B 193     5688   6711   5830   -345    314     49       C  
ATOM   4772  O   LYS B 193      73.228   5.920-100.733  1.00 44.08           O  
ANISOU 4772  O   LYS B 193     5212   6107   5428   -293    332    -37       O  
ATOM   4773  CB  LYS B 193      73.645   9.055 -99.770  1.00 54.83           C  
ANISOU 4773  CB  LYS B 193     6467   7843   6524   -227    265    159       C  
ATOM   4774  CG  LYS B 193      75.074   8.795-100.238  1.00 53.57           C  
ANISOU 4774  CG  LYS B 193     6299   7628   6429   -101    262    153       C  
ATOM   4775  CD  LYS B 193      76.055   9.675 -99.468  1.00 57.26           C  
ANISOU 4775  CD  LYS B 193     6743   8153   6859    -28    221    287       C  
ATOM   4776  CE  LYS B 193      77.392   9.813-100.188  1.00 61.45           C  
ANISOU 4776  CE  LYS B 193     7229   8697   7421     94    223    261       C  
ATOM   4777  NZ  LYS B 193      78.212   8.572-100.134  1.00 63.00           N  
ANISOU 4777  NZ  LYS B 193     7459   8719   7760    161    233    266       N  
ATOM   4778  N   GLY B 194      72.109   6.436 -98.848  1.00 50.58           N  
ANISOU 4778  N   GLY B 194     6062   6976   6178   -426    310    161       N  
ATOM   4779  CA  GLY B 194      72.117   5.056 -98.390  1.00 51.55           C  
ANISOU 4779  CA  GLY B 194     6263   6887   6438   -463    324    197       C  
ATOM   4780  C   GLY B 194      71.229   4.153 -99.226  1.00 58.55           C  
ANISOU 4780  C   GLY B 194     7161   7695   7390   -552    359     46       C  
ATOM   4781  O   GLY B 194      71.600   3.018 -99.535  1.00 64.27           O  
ANISOU 4781  O   GLY B 194     7935   8238   8248   -533    373     -2       O  
ATOM   4782  N   VAL B 195      70.047   4.643 -99.608  1.00 59.44           N  
ANISOU 4782  N   VAL B 195     7226   7940   7418   -650    370    -35       N  
ATOM   4783  CA  VAL B 195      69.137   3.838-100.419  1.00 57.09           C  
ANISOU 4783  CA  VAL B 195     6931   7587   7174   -748    395   -186       C  
ATOM   4784  C   VAL B 195      69.700   3.616-101.819  1.00 60.39           C  
ANISOU 4784  C   VAL B 195     7331   8004   7611   -671    401   -356       C  
ATOM   4785  O   VAL B 195      69.480   2.559-102.425  1.00 59.87           O  
ANISOU 4785  O   VAL B 195     7298   7807   7642   -714    422   -478       O  
ATOM   4786  CB  VAL B 195      67.749   4.499-100.465  1.00 52.66           C  
ANISOU 4786  CB  VAL B 195     6307   7190   6513   -864    398   -224       C  
ATOM   4787  CG1 VAL B 195      66.753   3.593-101.170  1.00 56.52           C  
ANISOU 4787  CG1 VAL B 195     6794   7615   7064   -985    417   -370       C  
ATOM   4788  CG2 VAL B 195      67.277   4.836 -99.057  1.00 51.11           C  
ANISOU 4788  CG2 VAL B 195     6120   7018   6280   -928    402    -60       C  
ATOM   4789  N   ILE B 196      70.434   4.593-102.356  1.00 59.72           N  
ANISOU 4789  N   ILE B 196     7195   8063   7434   -562    387   -369       N  
ATOM   4790  CA  ILE B 196      71.025   4.437-103.682  1.00 60.24           C  
ANISOU 4790  CA  ILE B 196     7241   8148   7500   -487    401   -524       C  
ATOM   4791  C   ILE B 196      72.196   3.462-103.638  1.00 62.24           C  
ANISOU 4791  C   ILE B 196     7548   8205   7893   -390    419   -521       C  
ATOM   4792  O   ILE B 196      72.325   2.588-104.503  1.00 61.38           O  
ANISOU 4792  O   ILE B 196     7462   7999   7860   -380    447   -672       O  
ATOM   4793  CB  ILE B 196      71.449   5.810-104.234  1.00 58.31           C  
ANISOU 4793  CB  ILE B 196     6923   8120   7112   -407    384   -522       C  
ATOM   4794  CG1 ILE B 196      70.213   6.637-104.592  1.00 53.13           C  
ANISOU 4794  CG1 ILE B 196     6208   7645   6333   -497    366   -566       C  
ATOM   4795  CG2 ILE B 196      72.384   5.654-105.433  1.00 60.03           C  
ANISOU 4795  CG2 ILE B 196     7126   8353   7331   -306    406   -646       C  
ATOM   4796  CD1 ILE B 196      70.536   8.012-105.094  1.00 52.85           C  
ANISOU 4796  CD1 ILE B 196     6105   7812   6165   -428    345   -548       C  
ATOM   4797  N   LYS B 197      73.065   3.591-102.632  1.00 65.16           N  
ANISOU 4797  N   LYS B 197     7939   8515   8303   -314    401   -355       N  
ATOM   4798  CA  LYS B 197      74.212   2.695-102.534  1.00 72.55           C  
ANISOU 4798  CA  LYS B 197     8915   9266   9383   -209    411   -336       C  
ATOM   4799  C   LYS B 197      73.781   1.257-102.271  1.00 73.66           C  
ANISOU 4799  C   LYS B 197     9137   9168   9683   -278    428   -361       C  
ATOM   4800  O   LYS B 197      74.466   0.319-102.694  1.00 77.80           O  
ANISOU 4800  O   LYS B 197     9693   9528  10341   -206    451   -435       O  
ATOM   4801  CB  LYS B 197      75.173   3.200-101.451  1.00 76.76           C  
ANISOU 4801  CB  LYS B 197     9446   9804   9916   -121    375   -139       C  
ATOM   4802  CG  LYS B 197      75.642   2.169-100.434  1.00 81.65           C  
ANISOU 4802  CG  LYS B 197    10137  10199  10687    -99    359     -9       C  
ATOM   4803  CD  LYS B 197      74.805   2.237 -99.165  1.00 87.11           C  
ANISOU 4803  CD  LYS B 197    10871  10882  11344   -214    335    144       C  
ATOM   4804  CE  LYS B 197      75.382   1.358 -98.069  1.00 87.86           C  
ANISOU 4804  CE  LYS B 197    11037  10779  11568   -184    309    310       C  
ATOM   4805  NZ  LYS B 197      74.497   1.328 -96.873  1.00 83.19           N  
ANISOU 4805  NZ  LYS B 197    10492  10180  10935   -311    296    453       N  
ATOM   4806  N   ASP B 198      72.644   1.062-101.602  1.00 69.59           N  
ANISOU 4806  N   ASP B 198     8652   8628   9162   -419    423   -306       N  
ATOM   4807  CA  ASP B 198      72.176  -0.293-101.336  1.00 69.96           C  
ANISOU 4807  CA  ASP B 198     8776   8443   9364   -503    440   -321       C  
ATOM   4808  C   ASP B 198      71.528  -0.919-102.565  1.00 71.15           C  
ANISOU 4808  C   ASP B 198     8925   8560   9549   -570    472   -552       C  
ATOM   4809  O   ASP B 198      71.710  -2.114-102.823  1.00 73.13           O  
ANISOU 4809  O   ASP B 198     9234   8593   9958   -569    493   -629       O  
ATOM   4810  CB  ASP B 198      71.196  -0.293-100.161  1.00 74.18           C  
ANISOU 4810  CB  ASP B 198     9339   8969   9878   -639    430   -174       C  
ATOM   4811  CG  ASP B 198      71.892  -0.167 -98.817  1.00 78.67           C  
ANISOU 4811  CG  ASP B 198     9944   9489  10460   -584    400     57       C  
ATOM   4812  OD1 ASP B 198      71.305   0.443 -97.898  1.00 79.04           O  
ANISOU 4812  OD1 ASP B 198     9983   9640  10408   -659    388    182       O  
ATOM   4813  OD2 ASP B 198      73.022  -0.682 -98.676  1.00 81.69           O  
ANISOU 4813  OD2 ASP B 198    10357   9731  10949   -465    386    110       O  
ATOM   4814  N   LYS B 199      70.778  -0.132-103.338  1.00 68.80           N  
ANISOU 4814  N   LYS B 199     8561   8471   9107   -627    471   -665       N  
ATOM   4815  CA  LYS B 199      70.039  -0.671-104.473  1.00 69.04           C  
ANISOU 4815  CA  LYS B 199     8586   8498   9149   -709    490   -883       C  
ATOM   4816  C   LYS B 199      70.850  -0.698-105.764  1.00 70.63           C  
ANISOU 4816  C   LYS B 199     8767   8738   9333   -598    511  -1059       C  
ATOM   4817  O   LYS B 199      70.669  -1.613-106.576  1.00 67.32           O  
ANISOU 4817  O   LYS B 199     8377   8209   8991   -631    535  -1240       O  
ATOM   4818  CB  LYS B 199      68.752   0.132-104.690  1.00 66.42           C  
ANISOU 4818  CB  LYS B 199     8187   8376   8672   -832    472   -919       C  
ATOM   4819  CG  LYS B 199      67.906  -0.352-105.857  1.00 69.72           C  
ANISOU 4819  CG  LYS B 199     8589   8818   9083   -930    479  -1142       C  
ATOM   4820  CD  LYS B 199      66.476   0.162-105.769  1.00 73.17           C  
ANISOU 4820  CD  LYS B 199     8965   9409   9427  -1078    457  -1145       C  
ATOM   4821  CE  LYS B 199      65.719  -0.493-104.620  1.00 75.86           C  
ANISOU 4821  CE  LYS B 199     9346   9607   9873  -1207    467  -1029       C  
ATOM   4822  NZ  LYS B 199      64.283  -0.088-104.575  1.00 76.80           N  
ANISOU 4822  NZ  LYS B 199     9393   9872   9916  -1356    454  -1049       N  
ATOM   4823  N   TYR B 200      71.746   0.270-105.975  1.00 70.78           N  
ANISOU 4823  N   TYR B 200     8734   8908   9251   -470    506  -1014       N  
ATOM   4824  CA  TYR B 200      72.481   0.375-107.228  1.00 73.60           C  
ANISOU 4824  CA  TYR B 200     9060   9340   9564   -371    533  -1175       C  
ATOM   4825  C   TYR B 200      73.980   0.141-107.092  1.00 74.92           C  
ANISOU 4825  C   TYR B 200     9236   9406   9822   -205    555  -1126       C  
ATOM   4826  O   TYR B 200      74.661   0.015-108.116  1.00 74.83           O  
ANISOU 4826  O   TYR B 200     9204   9425   9802   -119    593  -1271       O  
ATOM   4827  CB  TYR B 200      72.244   1.751-107.869  1.00 70.85           C  
ANISOU 4827  CB  TYR B 200     8628   9281   9008   -367    514  -1192       C  
ATOM   4828  CG  TYR B 200      70.784   2.064-108.094  1.00 73.15           C  
ANISOU 4828  CG  TYR B 200     8893   9695   9206   -516    487  -1245       C  
ATOM   4829  CD1 TYR B 200      70.092   1.510-109.164  1.00 76.20           C  
ANISOU 4829  CD1 TYR B 200     9279  10097   9574   -596    495  -1451       C  
ATOM   4830  CD2 TYR B 200      70.096   2.909-107.235  1.00 73.74           C  
ANISOU 4830  CD2 TYR B 200     8935   9873   9210   -576    452  -1094       C  
ATOM   4831  CE1 TYR B 200      68.755   1.791-109.370  1.00 75.61           C  
ANISOU 4831  CE1 TYR B 200     9167  10141   9419   -733    463  -1497       C  
ATOM   4832  CE2 TYR B 200      68.761   3.196-107.435  1.00 73.08           C  
ANISOU 4832  CE2 TYR B 200     8813   9904   9051   -705    428  -1142       C  
ATOM   4833  CZ  TYR B 200      68.096   2.636-108.501  1.00 75.88           C  
ANISOU 4833  CZ  TYR B 200     9162  10276   9394   -783    430  -1339       C  
ATOM   4834  OH  TYR B 200      66.766   2.926-108.694  1.00 81.13           O  
ANISOU 4834  OH  TYR B 200     9776  11063   9988   -911    399  -1383       O  
ATOM   4835  N   GLY B 201      74.511   0.083-105.881  1.00 75.78           N  
ANISOU 4835  N   GLY B 201     9371   9408  10014   -158    533   -930       N  
ATOM   4836  CA  GLY B 201      75.923  -0.157-105.683  1.00 78.26           C  
ANISOU 4836  CA  GLY B 201     9683   9625  10426      0    545   -871       C  
ATOM   4837  C   GLY B 201      76.642   1.072-105.144  1.00 78.09           C  
ANISOU 4837  C   GLY B 201     9601   9769  10301     80    513   -706       C  
ATOM   4838  O   GLY B 201      76.160   2.205-105.228  1.00 76.59           O  
ANISOU 4838  O   GLY B 201     9362   9789   9948     33    493   -676       O  
ATOM   4839  N   LYS B 202      77.830   0.827-104.583  1.00 78.28           N  
ANISOU 4839  N   LYS B 202     9625   9689  10430    205    505   -598       N  
ATOM   4840  CA  LYS B 202      78.617   1.900-103.983  1.00 78.32           C  
ANISOU 4840  CA  LYS B 202     9572   9827  10357    281    469   -437       C  
ATOM   4841  C   LYS B 202      79.124   2.902-105.012  1.00 75.33           C  
ANISOU 4841  C   LYS B 202     9109   9667   9847    344    494   -524       C  
ATOM   4842  O   LYS B 202      79.427   4.044-104.649  1.00 72.43           O  
ANISOU 4842  O   LYS B 202     8690   9456   9375    363    462   -410       O  
ATOM   4843  CB  LYS B 202      79.803   1.319-103.210  1.00 83.33           C  
ANISOU 4843  CB  LYS B 202    10218  10298  11145    402    449   -310       C  
ATOM   4844  CG  LYS B 202      79.424   0.364-102.088  1.00 85.30           C  
ANISOU 4844  CG  LYS B 202    10555  10330  11523    348    417   -185       C  
ATOM   4845  CD  LYS B 202      80.545   0.260-101.062  1.00 83.52           C  
ANISOU 4845  CD  LYS B 202    10325  10021  11389    459    368      7       C  
ATOM   4846  CE  LYS B 202      80.212  -0.732 -99.959  1.00 83.16           C  
ANISOU 4846  CE  LYS B 202    10371   9755  11470    408    334    146       C  
ATOM   4847  NZ  LYS B 202      80.265  -2.138-100.443  1.00 83.83           N  
ANISOU 4847  NZ  LYS B 202    10511   9591  11750    436    373     34       N  
ATOM   4848  N   ASP B 203      79.227   2.504-106.280  1.00 74.24           N  
ANISOU 4848  N   ASP B 203     8957   9542   9711    372    551   -722       N  
ATOM   4849  CA  ASP B 203      79.704   3.392-107.331  1.00 73.08           C  
ANISOU 4849  CA  ASP B 203     8732   9605   9431    426    583   -805       C  
ATOM   4850  C   ASP B 203      78.648   4.382-107.806  1.00 68.43           C  
ANISOU 4850  C   ASP B 203     8120   9224   8655    317    565   -838       C  
ATOM   4851  O   ASP B 203      78.970   5.268-108.605  1.00 66.45           O  
ANISOU 4851  O   ASP B 203     7807   9164   8278    350    582   -876       O  
ATOM   4852  CB  ASP B 203      80.201   2.564-108.516  1.00 78.46           C  
ANISOU 4852  CB  ASP B 203     9409  10231  10173    494    656  -1013       C  
ATOM   4853  CG  ASP B 203      79.181   1.541-108.974  1.00 81.48           C  
ANISOU 4853  CG  ASP B 203     9862  10492  10603    396    675  -1177       C  
ATOM   4854  OD1 ASP B 203      79.098   0.462-108.350  1.00 83.56           O  
ANISOU 4854  OD1 ASP B 203    10191  10520  11036    389    669  -1158       O  
ATOM   4855  OD2 ASP B 203      78.459   1.817-109.954  1.00 81.65           O  
ANISOU 4855  OD2 ASP B 203     9874  10656  10496    323    691  -1321       O  
ATOM   4856  N   ALA B 204      77.406   4.261-107.337  1.00 65.11           N  
ANISOU 4856  N   ALA B 204     7744   8776   8218    189    533   -818       N  
ATOM   4857  CA  ALA B 204      76.312   5.112-107.782  1.00 53.47           C  
ANISOU 4857  CA  ALA B 204     6243   7488   6584     87    512   -854       C  
ATOM   4858  C   ALA B 204      76.076   6.310-106.868  1.00 51.72           C  
ANISOU 4858  C   ALA B 204     5993   7382   6276     62    461   -675       C  
ATOM   4859  O   ALA B 204      75.063   6.999-107.020  1.00 55.94           O  
ANISOU 4859  O   ALA B 204     6506   8049   6699    -24    438   -683       O  
ATOM   4860  CB  ALA B 204      75.027   4.291-107.900  1.00 48.04           C  
ANISOU 4860  CB  ALA B 204     5607   6717   5929    -43    511   -958       C  
ATOM   4861  N   THR B 205      76.990   6.584-105.939  1.00 51.13           N  
ANISOU 4861  N   THR B 205     5913   7265   6251    138    441   -521       N  
ATOM   4862  CA  THR B 205      76.785   7.599-104.913  1.00 53.93           C  
ANISOU 4862  CA  THR B 205     6252   7700   6538    110    392   -355       C  
ATOM   4863  C   THR B 205      77.446   8.932-105.236  1.00 54.20           C  
ANISOU 4863  C   THR B 205     6214   7916   6463    173    380   -306       C  
ATOM   4864  O   THR B 205      77.297   9.883-104.460  1.00 53.72           O  
ANISOU 4864  O   THR B 205     6138   7931   6342    152    339   -183       O  
ATOM   4865  CB  THR B 205      77.302   7.095-103.562  1.00 58.51           C  
ANISOU 4865  CB  THR B 205     6876   8124   7231    138    365   -203       C  
ATOM   4866  OG1 THR B 205      78.733   7.166-103.538  1.00 64.04           O  
ANISOU 4866  OG1 THR B 205     7542   8805   7984    266    365   -153       O  
ATOM   4867  CG2 THR B 205      76.881   5.658-103.346  1.00 63.54           C  
ANISOU 4867  CG2 THR B 205     7586   8553   8001     93    382   -248       C  
ATOM   4868  N   ASN B 206      78.174   9.029-106.345  1.00 54.19           N  
ANISOU 4868  N   ASN B 206     6169   7984   6436    245    418   -399       N  
ATOM   4869  CA  ASN B 206      78.836  10.279-106.680  1.00 52.39           C  
ANISOU 4869  CA  ASN B 206     5871   7923   6110    297    411   -344       C  
ATOM   4870  C   ASN B 206      77.826  11.291-107.213  1.00 46.37           C  
ANISOU 4870  C   ASN B 206     5085   7333   5201    221    392   -368       C  
ATOM   4871  O   ASN B 206      76.705  10.946-107.596  1.00 53.27           O  
ANISOU 4871  O   ASN B 206     5982   8215   6043    139    393   -458       O  
ATOM   4872  CB  ASN B 206      79.956  10.035-107.686  1.00 57.12           C  
ANISOU 4872  CB  ASN B 206     6429   8549   6727    395    467   -430       C  
ATOM   4873  CG  ASN B 206      81.096   9.243-107.088  1.00 58.53           C  
ANISOU 4873  CG  ASN B 206     6611   8573   7057    491    477   -382       C  
ATOM   4874  OD1 ASN B 206      82.017   9.807-106.498  1.00 55.86           O  
ANISOU 4874  OD1 ASN B 206     6230   8256   6737    553    453   -258       O  
ATOM   4875  ND2 ASN B 206      81.031   7.924-107.220  1.00 65.85           N  
ANISOU 4875  ND2 ASN B 206     7587   9336   8099    504    509   -478       N  
ATOM   4876  N   VAL B 207      78.234  12.558-107.224  1.00 43.20           N  
ANISOU 4876  N   VAL B 207     4631   7066   4718    248    371   -280       N  
ATOM   4877  CA  VAL B 207      77.302  13.661-107.406  1.00 42.37           C  
ANISOU 4877  CA  VAL B 207     4503   7104   4494    184    338   -257       C  
ATOM   4878  C   VAL B 207      77.635  14.418-108.683  1.00 42.36           C  
ANISOU 4878  C   VAL B 207     4446   7266   4385    214    358   -303       C  
ATOM   4879  O   VAL B 207      78.768  14.407-109.171  1.00 46.19           O  
ANISOU 4879  O   VAL B 207     4899   7771   4879    289    395   -310       O  
ATOM   4880  CB  VAL B 207      77.301  14.619-106.194  1.00 40.09           C  
ANISOU 4880  CB  VAL B 207     4208   6825   4200    175    288   -103       C  
ATOM   4881  CG1 VAL B 207      77.176  13.831-104.899  1.00 43.13           C  
ANISOU 4881  CG1 VAL B 207     4650   7055   4684    153    272    -43       C  
ATOM   4882  CG2 VAL B 207      78.558  15.485-106.185  1.00 33.91           C  
ANISOU 4882  CG2 VAL B 207     3376   6103   3407    251    283    -16       C  
ATOM   4883  N   GLY B 208      76.615  15.085-109.220  1.00 41.59           N  
ANISOU 4883  N   GLY B 208     4332   7289   4181    154    334   -328       N  
ATOM   4884  CA  GLY B 208      76.753  15.929-110.386  1.00 34.97           C  
ANISOU 4884  CA  GLY B 208     3445   6619   3222    168    341   -348       C  
ATOM   4885  C   GLY B 208      77.070  17.365-110.026  1.00 39.66           C  
ANISOU 4885  C   GLY B 208     4000   7297   3774    187    306   -206       C  
ATOM   4886  O   GLY B 208      77.514  17.678-108.917  1.00 33.18           O  
ANISOU 4886  O   GLY B 208     3184   6404   3020    206    284   -100       O  
ATOM   4887  N   ASP B 209      76.820  18.255-110.990  1.00 33.84           N  
ANISOU 4887  N   ASP B 209     3225   6713   2921    178    296   -204       N  
ATOM   4888  CA  ASP B 209      77.237  19.647-110.852  1.00 38.82           C  
ANISOU 4888  CA  ASP B 209     3815   7421   3512    199    268    -74       C  
ATOM   4889  C   ASP B 209      76.500  20.355-109.729  1.00 41.81           C  
ANISOU 4889  C   ASP B 209     4203   7760   3922    165    210     15       C  
ATOM   4890  O   ASP B 209      77.075  21.228-109.069  1.00 42.22           O  
ANISOU 4890  O   ASP B 209     4240   7802   4000    188    189    125       O  
ATOM   4891  CB  ASP B 209      77.020  20.401-112.167  1.00 37.92           C  
ANISOU 4891  CB  ASP B 209     3665   7477   3267    190    267    -84       C  
ATOM   4892  CG  ASP B 209      77.873  19.864-113.295  1.00 44.56           C  
ANISOU 4892  CG  ASP B 209     4491   8382   4059    226    333   -165       C  
ATOM   4893  OD1 ASP B 209      77.465  20.009-114.465  1.00 46.59           O  
ANISOU 4893  OD1 ASP B 209     4736   8772   4195    205    339   -221       O  
ATOM   4894  OD2 ASP B 209      78.951  19.297-113.018  1.00 43.89           O  
ANISOU 4894  OD2 ASP B 209     4404   8222   4052    278    381   -173       O  
ATOM   4895  N   GLU B 210      75.235  20.000-109.500  1.00 40.66           N  
ANISOU 4895  N   GLU B 210     4079   7596   3774    107    187    -36       N  
ATOM   4896  CA  GLU B 210      74.411  20.638-108.484  1.00 39.74           C  
ANISOU 4896  CA  GLU B 210     3965   7454   3679     73    142     31       C  
ATOM   4897  C   GLU B 210      74.476  19.939-107.132  1.00 38.30           C  
ANISOU 4897  C   GLU B 210     3828   7131   3594     60    146     52       C  
ATOM   4898  O   GLU B 210      73.916  20.455-106.160  1.00 44.41           O  
ANISOU 4898  O   GLU B 210     4607   7884   4384     34    118    110       O  
ATOM   4899  CB  GLU B 210      72.948  20.703-108.949  1.00 43.42           C  
ANISOU 4899  CB  GLU B 210     4416   7992   4090     15    114    -29       C  
ATOM   4900  CG  GLU B 210      72.683  21.655-110.107  1.00 53.15           C  
ANISOU 4900  CG  GLU B 210     5602   9375   5219     24     87    -17       C  
ATOM   4901  CD  GLU B 210      72.867  20.996-111.460  1.00 70.95           C  
ANISOU 4901  CD  GLU B 210     7853  11706   7399     23    115   -117       C  
ATOM   4902  OE1 GLU B 210      72.884  21.715-112.483  1.00 76.57           O  
ANISOU 4902  OE1 GLU B 210     8532  12550   8013     35     99    -97       O  
ATOM   4903  OE2 GLU B 210      72.994  19.754-111.499  1.00 72.32           O  
ANISOU 4903  OE2 GLU B 210     8060  11808   7612      9    153   -217       O  
ATOM   4904  N   GLY B 211      75.131  18.782-107.045  1.00 34.36           N  
ANISOU 4904  N   GLY B 211     3361   6537   3158     79    182      9       N  
ATOM   4905  CA  GLY B 211      75.273  18.064-105.796  1.00 33.96           C  
ANISOU 4905  CA  GLY B 211     3356   6350   3198     70    183     45       C  
ATOM   4906  C   GLY B 211      74.372  16.857-105.638  1.00 40.39           C  
ANISOU 4906  C   GLY B 211     4211   7081   4054      9    199    -36       C  
ATOM   4907  O   GLY B 211      74.510  16.129-104.647  1.00 41.52           O  
ANISOU 4907  O   GLY B 211     4399   7101   4274     -1    203     -1       O  
ATOM   4908  N   GLY B 212      73.458  16.620-106.584  1.00 41.55           N  
ANISOU 4908  N   GLY B 212     4345   7292   4151    -36    205   -139       N  
ATOM   4909  CA  GLY B 212      72.559  15.488-106.500  1.00 40.66           C  
ANISOU 4909  CA  GLY B 212     4265   7101   4081   -107    218   -225       C  
ATOM   4910  C   GLY B 212      73.106  14.228-107.164  1.00 45.62           C  
ANISOU 4910  C   GLY B 212     4925   7645   4762    -88    259   -329       C  
ATOM   4911  O   GLY B 212      74.103  14.242-107.889  1.00 39.93           O  
ANISOU 4911  O   GLY B 212     4192   6952   4029    -18    283   -355       O  
ATOM   4912  N   PHE B 213      72.423  13.118-106.901  1.00 44.13           N  
ANISOU 4912  N   PHE B 213     4777   7349   4640   -154    272   -394       N  
ATOM   4913  CA  PHE B 213      72.826  11.821-107.421  1.00 42.60           C  
ANISOU 4913  CA  PHE B 213     4623   7044   4520   -143    311   -503       C  
ATOM   4914  C   PHE B 213      72.209  11.568-108.793  1.00 44.80           C  
ANISOU 4914  C   PHE B 213     4881   7414   4727   -183    319   -661       C  
ATOM   4915  O   PHE B 213      71.207  12.177-109.178  1.00 42.42           O  
ANISOU 4915  O   PHE B 213     4541   7239   4338   -242    287   -683       O  
ATOM   4916  CB  PHE B 213      72.423  10.706-106.456  1.00 39.03           C  
ANISOU 4916  CB  PHE B 213     4231   6413   4186   -201    319   -490       C  
ATOM   4917  CG  PHE B 213      72.832  10.957-105.033  1.00 41.34           C  
ANISOU 4917  CG  PHE B 213     4546   6633   4527   -180    303   -329       C  
ATOM   4918  CD1 PHE B 213      71.911  11.413-104.106  1.00 37.86           C  
ANISOU 4918  CD1 PHE B 213     4105   6220   4062   -253    280   -251       C  
ATOM   4919  CD2 PHE B 213      74.139  10.741-104.622  1.00 47.49           C  
ANISOU 4919  CD2 PHE B 213     5344   7326   5373    -88    310   -259       C  
ATOM   4920  CE1 PHE B 213      72.282  11.645-102.795  1.00 39.54           C  
ANISOU 4920  CE1 PHE B 213     4343   6378   4303   -239    266   -111       C  
ATOM   4921  CE2 PHE B 213      74.517  10.974-103.311  1.00 42.99           C  
ANISOU 4921  CE2 PHE B 213     4796   6702   4837    -74    285   -111       C  
ATOM   4922  CZ  PHE B 213      73.585  11.428-102.397  1.00 41.92           C  
ANISOU 4922  CZ  PHE B 213     4667   6598   4662   -152    263    -39       C  
ATOM   4923  N   ALA B 214      72.826  10.647-109.533  1.00 50.55           N  
ANISOU 4923  N   ALA B 214     5634   8078   5494   -149    360   -777       N  
ATOM   4924  CA  ALA B 214      72.384  10.286-110.882  1.00 51.54           C  
ANISOU 4924  CA  ALA B 214     5749   8288   5547   -183    373   -947       C  
ATOM   4925  C   ALA B 214      72.530   8.784-111.084  1.00 53.19           C  
ANISOU 4925  C   ALA B 214     6015   8326   5868   -197    414  -1083       C  
ATOM   4926  O   ALA B 214      73.424   8.318-111.799  1.00 52.48           O  
ANISOU 4926  O   ALA B 214     5934   8215   5791   -126    461  -1174       O  
ATOM   4927  CB  ALA B 214      73.172  11.063-111.939  1.00 51.23           C  
ANISOU 4927  CB  ALA B 214     5665   8409   5390   -108    388   -965       C  
ATOM   4928  N   PRO B 215      71.653   7.990-110.473  1.00 58.04           N  
ANISOU 4928  N   PRO B 215     6668   8814   6571   -288    403  -1102       N  
ATOM   4929  CA  PRO B 215      71.700   6.542-110.693  1.00 61.24           C  
ANISOU 4929  CA  PRO B 215     7132   9041   7094   -312    440  -1237       C  
ATOM   4930  C   PRO B 215      71.173   6.175-112.069  1.00 67.37           C  
ANISOU 4930  C   PRO B 215     7899   9907   7792   -364    447  -1443       C  
ATOM   4931  O   PRO B 215      70.330   6.868-112.646  1.00 71.26           O  
ANISOU 4931  O   PRO B 215     8344  10579   8152   -424    408  -1472       O  
ATOM   4932  CB  PRO B 215      70.797   5.988-109.588  1.00 65.25           C  
ANISOU 4932  CB  PRO B 215     7677   9411   7704   -413    420  -1172       C  
ATOM   4933  CG  PRO B 215      69.815   7.086-109.346  1.00 65.56           C  
ANISOU 4933  CG  PRO B 215     7659   9619   7632   -477    373  -1094       C  
ATOM   4934  CD  PRO B 215      70.576   8.372-109.542  1.00 60.89           C  
ANISOU 4934  CD  PRO B 215     7018   9184   6933   -376    362  -1003       C  
ATOM   4935  N   ASN B 216      71.678   5.060-112.593  1.00 69.41           N  
ANISOU 4935  N   ASN B 216     8204  10036   8133   -338    494  -1589       N  
ATOM   4936  CA  ASN B 216      71.323   4.608-113.938  1.00 73.29           C  
ANISOU 4936  CA  ASN B 216     8695  10603   8548   -381    508  -1808       C  
ATOM   4937  C   ASN B 216      69.925   4.004-113.900  1.00 74.42           C  
ANISOU 4937  C   ASN B 216     8854  10703   8720   -533    470  -1894       C  
ATOM   4938  O   ASN B 216      69.741   2.804-113.688  1.00 71.82           O  
ANISOU 4938  O   ASN B 216     8583  10172   8534   -583    491  -1983       O  
ATOM   4939  CB  ASN B 216      72.354   3.616-114.465  1.00 77.90           C  
ANISOU 4939  CB  ASN B 216     9322  11055   9221   -297    578  -1947       C  
ATOM   4940  CG  ASN B 216      73.691   4.272-114.787  1.00 78.42           C  
ANISOU 4940  CG  ASN B 216     9351  11215   9229   -153    620  -1894       C  
ATOM   4941  OD1 ASN B 216      73.747   5.431-115.204  1.00 78.48           O  
ANISOU 4941  OD1 ASN B 216     9301  11439   9078   -134    601  -1829       O  
ATOM   4942  ND2 ASN B 216      74.776   3.528-114.595  1.00 75.53           N  
ANISOU 4942  ND2 ASN B 216     9014  10683   9001    -51    678  -1917       N  
ATOM   4943  N   ILE B 217      68.922   4.857-114.105  1.00 75.85           N  
ANISOU 4943  N   ILE B 217     8976  11072   8772   -609    413  -1864       N  
ATOM   4944  CA  ILE B 217      67.534   4.432-114.220  1.00 76.28           C  
ANISOU 4944  CA  ILE B 217     9020  11134   8830   -759    371  -1952       C  
ATOM   4945  C   ILE B 217      66.910   5.116-115.426  1.00 76.62           C  
ANISOU 4945  C   ILE B 217     9000  11431   8682   -798    324  -2048       C  
ATOM   4946  O   ILE B 217      67.335   6.198-115.844  1.00 73.88           O  
ANISOU 4946  O   ILE B 217     8608  11263   8199   -720    312  -1977       O  
ATOM   4947  CB  ILE B 217      66.725   4.736-112.944  1.00 74.06           C  
ANISOU 4947  CB  ILE B 217     8720  10808   8612   -828    339  -1786       C  
ATOM   4948  CG1 ILE B 217      66.761   6.233-112.637  1.00 71.50           C  
ANISOU 4948  CG1 ILE B 217     8330  10667   8170   -770    306  -1618       C  
ATOM   4949  CG2 ILE B 217      67.280   3.948-111.779  1.00 77.92           C  
ANISOU 4949  CG2 ILE B 217     9280  11046   9282   -804    380  -1694       C  
ATOM   4950  CD1 ILE B 217      65.836   6.647-111.510  1.00 71.25           C  
ANISOU 4950  CD1 ILE B 217     8266  10632   8173   -841    276  -1479       C  
ATOM   4951  N   LEU B 218      65.897   4.465-115.994  1.00 78.92           N  
ANISOU 4951  N   LEU B 218     9286  11735   8964   -922    294  -2208       N  
ATOM   4952  CA  LEU B 218      65.189   4.958-117.169  1.00 76.28           C  
ANISOU 4952  CA  LEU B 218     8892  11638   8451   -976    237  -2315       C  
ATOM   4953  C   LEU B 218      63.849   5.592-116.818  1.00 73.44           C  
ANISOU 4953  C   LEU B 218     8453  11397   8052  -1075    161  -2235       C  
ATOM   4954  O   LEU B 218      63.531   6.679-117.308  1.00 71.36           O  
ANISOU 4954  O   LEU B 218     8121  11356   7638  -1055    107  -2178       O  
ATOM   4955  CB  LEU B 218      64.993   3.810-118.171  1.00 77.70           C  
ANISOU 4955  CB  LEU B 218     9114  11777   8633  -1049    248  -2573       C  
ATOM   4956  CG  LEU B 218      63.972   3.928-119.307  1.00 73.53           C  
ANISOU 4956  CG  LEU B 218     8532  11456   7949  -1155    176  -2723       C  
ATOM   4957  CD1 LEU B 218      64.221   5.145-120.187  1.00 71.35           C  
ANISOU 4957  CD1 LEU B 218     8201  11458   7452  -1082    143  -2675       C  
ATOM   4958  CD2 LEU B 218      63.972   2.650-120.138  1.00 72.09           C  
ANISOU 4958  CD2 LEU B 218     8409  11182   7798  -1220    202  -2988       C  
ATOM   4959  N   GLU B 219      63.065   4.941-115.963  1.00 75.85           N  
ANISOU 4959  N   GLU B 219     8766  11556   8497  -1178    157  -2221       N  
ATOM   4960  CA  GLU B 219      61.729   5.420-115.632  1.00 77.24           C  
ANISOU 4960  CA  GLU B 219     8857  11840   8651  -1281     93  -2165       C  
ATOM   4961  C   GLU B 219      61.801   6.657-114.748  1.00 73.64           C  
ANISOU 4961  C   GLU B 219     8354  11456   8170  -1205     83  -1941       C  
ATOM   4962  O   GLU B 219      62.434   6.634-113.688  1.00 66.65           O  
ANISOU 4962  O   GLU B 219     7515  10426   7385  -1148    132  -1811       O  
ATOM   4963  CB  GLU B 219      60.940   4.317-114.934  1.00 77.92           C  
ANISOU 4963  CB  GLU B 219     8965  11740   8901  -1418    105  -2212       C  
ATOM   4964  CG  GLU B 219      60.424   3.250-115.878  1.00 84.98           C  
ANISOU 4964  CG  GLU B 219     9877  12606   9807  -1533     87  -2448       C  
ATOM   4965  CD  GLU B 219      59.299   3.757-116.754  1.00 89.20           C  
ANISOU 4965  CD  GLU B 219    10309  13383  10199  -1620     -2  -2530       C  
ATOM   4966  OE1 GLU B 219      58.123   3.528-116.400  1.00 92.26           O  
ANISOU 4966  OE1 GLU B 219    10637  13774  10644  -1753    -38  -2538       O  
ATOM   4967  OE2 GLU B 219      59.591   4.397-117.787  1.00 89.14           O  
ANISOU 4967  OE2 GLU B 219    10277  13570  10023  -1556    -35  -2578       O  
ATOM   4968  N   ASN B 220      61.143   7.736-115.184  1.00 71.67           N  
ANISOU 4968  N   ASN B 220     7838  10991   8402   -975    -25  -1532       N  
ATOM   4969  CA  ASN B 220      60.974   8.890-114.309  1.00 68.48           C  
ANISOU 4969  CA  ASN B 220     7390  10713   7917   -964     43  -1272       C  
ATOM   4970  C   ASN B 220      60.170   8.522-113.073  1.00 70.37           C  
ANISOU 4970  C   ASN B 220     7673  10816   8248  -1126     -4  -1087       C  
ATOM   4971  O   ASN B 220      60.398   9.083-111.995  1.00 72.00           O  
ANISOU 4971  O   ASN B 220     7891  11003   8464  -1100     31   -888       O  
ATOM   4972  CB  ASN B 220      60.296  10.039-115.057  1.00 68.63           C  
ANISOU 4972  CB  ASN B 220     7285  11076   7715   -962    106  -1245       C  
ATOM   4973  CG  ASN B 220      61.148  10.583-116.185  1.00 72.14           C  
ANISOU 4973  CG  ASN B 220     7676  11694   8037   -813    162  -1372       C  
ATOM   4974  OD1 ASN B 220      62.226  11.128-115.957  1.00 71.03           O  
ANISOU 4974  OD1 ASN B 220     7541  11545   7903   -676    215  -1316       O  
ATOM   4975  ND2 ASN B 220      60.658  10.456-117.411  1.00 74.71           N  
ANISOU 4975  ND2 ASN B 220     7944  12203   8241   -852    150  -1538       N  
ATOM   4976  N   SER B 221      59.235   7.578-113.208  1.00 71.85           N  
ANISOU 4976  N   SER B 221     7883  10920   8495  -1304    -85  -1151       N  
ATOM   4977  CA  SER B 221      58.460   7.128-112.059  1.00 69.61           C  
ANISOU 4977  CA  SER B 221     7635  10520   8294  -1487   -133   -969       C  
ATOM   4978  C   SER B 221      59.349   6.512-110.985  1.00 68.66           C  
ANISOU 4978  C   SER B 221     7637  10093   8356  -1458   -181   -863       C  
ATOM   4979  O   SER B 221      59.065   6.653-109.791  1.00 70.36           O  
ANISOU 4979  O   SER B 221     7867  10284   8584  -1544   -177   -642       O  
ATOM   4980  CB  SER B 221      57.395   6.121-112.504  1.00 69.40           C  
ANISOU 4980  CB  SER B 221     7615  10439   8315  -1698   -225  -1072       C  
ATOM   4981  OG  SER B 221      57.932   4.811-112.567  1.00 71.38           O  
ANISOU 4981  OG  SER B 221     7996  10352   8774  -1723   -334  -1198       O  
ATOM   4982  N   GLU B 222      60.425   5.825-111.384  1.00 68.45           N  
ANISOU 4982  N   GLU B 222     7693   9848   8467  -1332   -229  -1019       N  
ATOM   4983  CA  GLU B 222      61.319   5.234-110.393  1.00 65.63           C  
ANISOU 4983  CA  GLU B 222     7448   9195   8295  -1286   -291   -915       C  
ATOM   4984  C   GLU B 222      62.073   6.306-109.614  1.00 53.79           C  
ANISOU 4984  C   GLU B 222     5917   7800   6719  -1150   -203   -740       C  
ATOM   4985  O   GLU B 222      62.338   6.139-108.418  1.00 56.19           O  
ANISOU 4985  O   GLU B 222     6283   7961   7104  -1184   -238   -547       O  
ATOM   4986  CB  GLU B 222      62.303   4.275-111.061  1.00 73.96           C  
ANISOU 4986  CB  GLU B 222     8578   9999   9522  -1155   -366  -1148       C  
ATOM   4987  CG  GLU B 222      63.235   3.599-110.067  1.00 80.37           C  
ANISOU 4987  CG  GLU B 222     9502  10486  10547  -1095   -452  -1040       C  
ATOM   4988  CD  GLU B 222      64.274   2.725-110.728  1.00 87.53           C  
ANISOU 4988  CD  GLU B 222    10467  11155  11634   -925   -524  -1288       C  
ATOM   4989  OE1 GLU B 222      65.157   2.217-110.007  1.00 89.77           O  
ANISOU 4989  OE1 GLU B 222    10829  11179  12099   -836   -598  -1215       O  
ATOM   4990  OE2 GLU B 222      64.213   2.544-111.963  1.00 90.29           O  
ANISOU 4990  OE2 GLU B 222    10777  11587  11941   -874   -509  -1561       O  
ATOM   4991  N   ALA B 223      62.432   7.409-110.274  1.00 45.57           N  
ANISOU 4991  N   ALA B 223     4783   7009   5522  -1006    -99   -800       N  
ATOM   4992  CA  ALA B 223      63.103   8.498-109.574  1.00 43.06           C  
ANISOU 4992  CA  ALA B 223     4434   6794   5131   -891    -22   -642       C  
ATOM   4993  C   ALA B 223      62.210   9.089-108.487  1.00 50.05           C  
ANISOU 4993  C   ALA B 223     5295   7789   5933  -1018      7   -415       C  
ATOM   4994  O   ALA B 223      62.676   9.372-107.377  1.00 47.09           O  
ANISOU 4994  O   ALA B 223     4953   7357   5580   -995     12   -248       O  
ATOM   4995  CB  ALA B 223      63.528   9.579-110.567  1.00 40.94           C  
ANISOU 4995  CB  ALA B 223     4070   6777   4708   -745     73   -738       C  
ATOM   4996  N   LEU B 224      60.922   9.278-108.785  1.00 51.78           N  
ANISOU 4996  N   LEU B 224     5445   8182   6047  -1151     24   -415       N  
ATOM   4997  CA  LEU B 224      60.005   9.809-107.783  1.00 51.20           C  
ANISOU 4997  CA  LEU B 224     5326   8242   5888  -1268     58   -224       C  
ATOM   4998  C   LEU B 224      59.812   8.828-106.631  1.00 51.49           C  
ANISOU 4998  C   LEU B 224     5448   8075   6041  -1428    -18    -79       C  
ATOM   4999  O   LEU B 224      59.750   9.237-105.465  1.00 48.87           O  
ANISOU 4999  O   LEU B 224     5114   7788   5666  -1463      9    103       O  
ATOM   5000  CB  LEU B 224      58.664  10.153-108.433  1.00 47.52           C  
ANISOU 5000  CB  LEU B 224     4747   8015   5293  -1369     86   -271       C  
ATOM   5001  CG  LEU B 224      58.670  11.396-109.322  1.00 48.97           C  
ANISOU 5001  CG  LEU B 224     4831   8448   5328  -1227    162   -338       C  
ATOM   5002  CD1 LEU B 224      57.401  11.466-110.168  1.00 47.71           C  
ANISOU 5002  CD1 LEU B 224     4566   8492   5068  -1326    157   -413       C  
ATOM   5003  CD2 LEU B 224      58.840  12.646-108.471  1.00 36.69           C  
ANISOU 5003  CD2 LEU B 224     3235   7014   3690  -1135    234   -187       C  
ATOM   5004  N   GLU B 225      59.717   7.532-106.936  1.00 55.67           N  
ANISOU 5004  N   GLU B 225     6055   8378   6719  -1532   -121   -157       N  
ATOM   5005  CA  GLU B 225      59.604   6.527-105.883  1.00 57.30           C  
ANISOU 5005  CA  GLU B 225     6358   8358   7056  -1695   -215      0       C  
ATOM   5006  C   GLU B 225      60.856   6.500-105.014  1.00 60.38           C  
ANISOU 5006  C   GLU B 225     6835   8570   7537  -1572   -241    111       C  
ATOM   5007  O   GLU B 225      60.772   6.303-103.796  1.00 63.86           O  
ANISOU 5007  O   GLU B 225     7317   8955   7991  -1680   -273    324       O  
ATOM   5008  CB  GLU B 225      59.352   5.150-106.498  1.00 63.90           C  
ANISOU 5008  CB  GLU B 225     7273   8945   8060  -1814   -339   -126       C  
ATOM   5009  CG  GLU B 225      58.604   4.178-105.596  1.00 72.73           C  
ANISOU 5009  CG  GLU B 225     8453   9910   9269  -2078   -438     54       C  
ATOM   5010  CD  GLU B 225      57.104   4.247-105.799  1.00 80.25           C  
ANISOU 5010  CD  GLU B 225     9300  11088  10102  -2296   -411     70       C  
ATOM   5011  OE1 GLU B 225      56.351   3.773-104.920  1.00 80.03           O  
ANISOU 5011  OE1 GLU B 225     9278  11048  10082  -2530   -453    262       O  
ATOM   5012  OE2 GLU B 225      56.681   4.781-106.846  1.00 84.78           O  
ANISOU 5012  OE2 GLU B 225     9777  11868  10569  -2237   -352   -102       O  
ATOM   5013  N   LEU B 226      62.026   6.694-105.628  1.00 61.54           N  
ANISOU 5013  N   LEU B 226     6999   8648   7736  -1353   -230    -27       N  
ATOM   5014  CA  LEU B 226      63.276   6.771-104.877  1.00 61.50           C  
ANISOU 5014  CA  LEU B 226     7053   8507   7809  -1217   -251     66       C  
ATOM   5015  C   LEU B 226      63.244   7.906-103.859  1.00 51.38           C  
ANISOU 5015  C   LEU B 226     5720   7431   6372  -1210   -167    254       C  
ATOM   5016  O   LEU B 226      63.603   7.720-102.691  1.00 53.01           O  
ANISOU 5016  O   LEU B 226     5984   7543   6616  -1249   -212    437       O  
ATOM   5017  CB  LEU B 226      64.444   6.962-105.845  1.00 64.85           C  
ANISOU 5017  CB  LEU B 226     7462   8902   8277   -983   -228   -134       C  
ATOM   5018  CG  LEU B 226      65.533   5.895-105.943  1.00 70.50           C  
ANISOU 5018  CG  LEU B 226     8267   9303   9216   -874   -337   -223       C  
ATOM   5019  CD1 LEU B 226      64.934   4.500-105.923  1.00 73.05           C  
ANISOU 5019  CD1 LEU B 226     8689   9355   9713  -1032   -472   -243       C  
ATOM   5020  CD2 LEU B 226      66.330   6.120-107.218  1.00 72.86           C  
ANISOU 5020  CD2 LEU B 226     8506   9669   9507   -673   -285   -478       C  
ATOM   5021  N   VAL B 227      62.823   9.097-104.292  1.00 45.68           N  
ANISOU 5021  N   VAL B 227     4891   6991   5475  -1157    -54    208       N  
ATOM   5022  CA  VAL B 227      62.787  10.259-103.407  1.00 46.07           C  
ANISOU 5022  CA  VAL B 227     4889   7232   5382  -1130     25    348       C  
ATOM   5023  C   VAL B 227      61.739  10.066-102.315  1.00 51.59           C  
ANISOU 5023  C   VAL B 227     5581   8004   6017  -1333     19    522       C  
ATOM   5024  O   VAL B 227      61.998  10.313-101.130  1.00 52.98           O  
ANISOU 5024  O   VAL B 227     5780   8197   6154  -1354     20    681       O  
ATOM   5025  CB  VAL B 227      62.528  11.538-104.225  1.00 41.41           C  
ANISOU 5025  CB  VAL B 227     4191   6898   4645  -1024    128    249       C  
ATOM   5026  CG1 VAL B 227      62.347  12.736-103.309  1.00 42.26           C  
ANISOU 5026  CG1 VAL B 227     4248   7190   4619  -1001    198    373       C  
ATOM   5027  CG2 VAL B 227      63.659  11.778-105.226  1.00 37.55           C  
ANISOU 5027  CG2 VAL B 227     3702   6370   4197   -838    140    105       C  
ATOM   5028  N   LYS B 228      60.539   9.624-102.702  1.00 48.75           N  
ANISOU 5028  N   LYS B 228     5179   7711   5633  -1491     13    491       N  
ATOM   5029  CA  LYS B 228      59.484   9.334-101.735  1.00 46.33           C  
ANISOU 5029  CA  LYS B 228     4847   7495   5262  -1710      8    653       C  
ATOM   5030  C   LYS B 228      59.946   8.321-100.692  1.00 47.10           C  
ANISOU 5030  C   LYS B 228     5062   7358   5474  -1822    -94    828       C  
ATOM   5031  O   LYS B 228      59.668   8.476 -99.496  1.00 50.98           O  
ANISOU 5031  O   LYS B 228     5544   7951   5876  -1929    -79   1012       O  
ATOM   5032  CB  LYS B 228      58.249   8.830-102.486  1.00 52.75           C  
ANISOU 5032  CB  LYS B 228     5599   8379   6066  -1868     -4    574       C  
ATOM   5033  CG  LYS B 228      57.072   8.378-101.640  1.00 61.99           C  
ANISOU 5033  CG  LYS B 228     6724   9652   7176  -2127    -14    733       C  
ATOM   5034  CD  LYS B 228      55.879   8.099-102.554  1.00 70.54           C  
ANISOU 5034  CD  LYS B 228     7717  10851   8235  -2256    -16    624       C  
ATOM   5035  CE  LYS B 228      54.675   7.561-101.798  1.00 75.12           C  
ANISOU 5035  CE  LYS B 228     8237  11544   8761  -2539    -30    779       C  
ATOM   5036  NZ  LYS B 228      54.749   6.090-101.577  1.00 78.79           N  
ANISOU 5036  NZ  LYS B 228     8830  11705   9400  -2741   -169    865       N  
ATOM   5037  N   GLU B 229      60.668   7.285-101.124  1.00 50.95           N  
ANISOU 5037  N   GLU B 229     5661   7538   6160  -1794   -205    771       N  
ATOM   5038  CA  GLU B 229      61.197   6.299-100.186  1.00 55.83           C  
ANISOU 5038  CA  GLU B 229     6401   7897   6916  -1880   -327    945       C  
ATOM   5039  C   GLU B 229      62.195   6.927 -99.215  1.00 50.38           C  
ANISOU 5039  C   GLU B 229     5733   7232   6178  -1756   -309   1069       C  
ATOM   5040  O   GLU B 229      62.213   6.587 -98.026  1.00 50.88           O  
ANISOU 5040  O   GLU B 229     5845   7260   6229  -1880   -362   1288       O  
ATOM   5041  CB  GLU B 229      61.842   5.152-100.965  1.00 62.93           C  
ANISOU 5041  CB  GLU B 229     7406   8448   8055  -1825   -454    816       C  
ATOM   5042  CG  GLU B 229      62.587   4.136-100.124  1.00 71.01           C  
ANISOU 5042  CG  GLU B 229     8565   9153   9262  -1862   -604    979       C  
ATOM   5043  CD  GLU B 229      63.135   2.997-100.958  1.00 78.16           C  
ANISOU 5043  CD  GLU B 229     9568   9705  10423  -1792   -734    817       C  
ATOM   5044  OE1 GLU B 229      62.820   2.936-102.166  1.00 81.29           O  
ANISOU 5044  OE1 GLU B 229     9928  10124  10835  -1749   -705    579       O  
ATOM   5045  OE2 GLU B 229      63.882   2.165-100.407  1.00 80.09           O  
ANISOU 5045  OE2 GLU B 229     9925   9653  10854  -1773   -873    922       O  
ATOM   5046  N   ALA B 230      63.033   7.846 -99.701  1.00 48.64           N  
ANISOU 5046  N   ALA B 230     5473   7085   5923  -1525   -239    941       N  
ATOM   5047  CA  ALA B 230      64.008   8.492 -98.827  1.00 48.40           C  
ANISOU 5047  CA  ALA B 230     5457   7086   5848  -1409   -226   1044       C  
ATOM   5048  C   ALA B 230      63.334   9.433 -97.838  1.00 48.46           C  
ANISOU 5048  C   ALA B 230     5393   7379   5640  -1494   -135   1170       C  
ATOM   5049  O   ALA B 230      63.761   9.535 -96.683  1.00 40.44           O  
ANISOU 5049  O   ALA B 230     4411   6376   4578  -1520   -161   1334       O  
ATOM   5050  CB  ALA B 230      65.043   9.248 -99.657  1.00 44.82           C  
ANISOU 5050  CB  ALA B 230     4969   6649   5412  -1163   -175    874       C  
ATOM   5051  N   ILE B 231      62.294  10.145 -98.278  1.00 49.93           N  
ANISOU 5051  N   ILE B 231     5473   7807   5690  -1526    -32   1086       N  
ATOM   5052  CA  ILE B 231      61.540  11.005 -97.370  1.00 48.28           C  
ANISOU 5052  CA  ILE B 231     5182   7881   5281  -1598     56   1176       C  
ATOM   5053  C   ILE B 231      60.921  10.178 -96.253  1.00 49.41           C  
ANISOU 5053  C   ILE B 231     5354   8032   5390  -1838      6   1383       C  
ATOM   5054  O   ILE B 231      60.975  10.554 -95.076  1.00 46.89           O  
ANISOU 5054  O   ILE B 231     5026   7846   4945  -1884     28   1519       O  
ATOM   5055  CB  ILE B 231      60.464  11.797 -98.140  1.00 46.86           C  
ANISOU 5055  CB  ILE B 231     4874   7940   4989  -1584    159   1041       C  
ATOM   5056  CG1 ILE B 231      61.102  12.730 -99.167  1.00 39.32           C  
ANISOU 5056  CG1 ILE B 231     3892   7002   4048  -1358    206    872       C  
ATOM   5057  CG2 ILE B 231      59.576  12.588 -97.183  1.00 47.54           C  
ANISOU 5057  CG2 ILE B 231     4861   8323   4881  -1657    247   1115       C  
ATOM   5058  CD1 ILE B 231      60.088  13.500 -99.984  1.00 41.61           C  
ANISOU 5058  CD1 ILE B 231     4062   7510   4240  -1333    285    754       C  
ATOM   5059  N   ASP B 232      60.330   9.032 -96.601  1.00 57.16           N  
ANISOU 5059  N   ASP B 232     6369   8874   6475  -2007    -68   1412       N  
ATOM   5060  CA  ASP B 232      59.645   8.226 -95.597  1.00 65.19           C  
ANISOU 5060  CA  ASP B 232     7406   9910   7454  -2270   -120   1629       C  
ATOM   5061  C   ASP B 232      60.630   7.611 -94.609  1.00 66.53           C  
ANISOU 5061  C   ASP B 232     7701   9877   7701  -2294   -234   1824       C  
ATOM   5062  O   ASP B 232      60.350   7.549 -93.405  1.00 70.99           O  
ANISOU 5062  O   ASP B 232     8260  10574   8139  -2450   -236   2028       O  
ATOM   5063  CB  ASP B 232      58.800   7.140 -96.271  1.00 72.63           C  
ANISOU 5063  CB  ASP B 232     8361  10726   8510  -2457   -188   1613       C  
ATOM   5064  CG  ASP B 232      57.717   7.716 -97.179  1.00 77.71           C  
ANISOU 5064  CG  ASP B 232     8865  11604   9059  -2459    -86   1442       C  
ATOM   5065  OD1 ASP B 232      57.576   8.956 -97.241  1.00 80.09           O  
ANISOU 5065  OD1 ASP B 232     9060  12160   9211  -2317     35   1351       O  
ATOM   5066  OD2 ASP B 232      56.999   6.925 -97.829  1.00 74.50           O  
ANISOU 5066  OD2 ASP B 232     8454  11120   8732  -2606   -137   1400       O  
ATOM   5067  N   LYS B 233      61.792   7.159 -95.088  1.00 60.22           N  
ANISOU 5067  N   LYS B 233     7005   8775   7101  -2137   -329   1764       N  
ATOM   5068  CA  LYS B 233      62.760   6.558 -94.175  1.00 59.57           C  
ANISOU 5068  CA  LYS B 233     7035   8490   7107  -2142   -454   1953       C  
ATOM   5069  C   LYS B 233      63.365   7.590 -93.235  1.00 57.16           C  
ANISOU 5069  C   LYS B 233     6696   8386   6636  -2043   -391   2020       C  
ATOM   5070  O   LYS B 233      63.701   7.262 -92.091  1.00 55.27           O  
ANISOU 5070  O   LYS B 233     6513   8129   6360  -2137   -466   2239       O  
ATOM   5071  CB  LYS B 233      63.852   5.827 -94.954  1.00 59.92           C  
ANISOU 5071  CB  LYS B 233     7180   8172   7416  -1977   -572   1848       C  
ATOM   5072  CG  LYS B 233      63.445   4.414 -95.336  1.00 67.50           C  
ANISOU 5072  CG  LYS B 233     8229   8839   8579  -2130   -708   1881       C  
ATOM   5073  CD  LYS B 233      64.585   3.625 -95.946  1.00 73.06           C  
ANISOU 5073  CD  LYS B 233     9034   9170   9555  -1953   -841   1779       C  
ATOM   5074  CE  LYS B 233      64.120   2.219 -96.296  1.00 77.03           C  
ANISOU 5074  CE  LYS B 233     9636   9360  10272  -2113   -990   1800       C  
ATOM   5075  NZ  LYS B 233      65.229   1.338 -96.750  1.00 77.26           N  
ANISOU 5075  NZ  LYS B 233     9770   8996  10588  -1939  -1141   1709       N  
ATOM   5076  N   ALA B 234      63.500   8.839 -93.684  1.00 50.86           N  
ANISOU 5076  N   ALA B 234     5811   7781   5733  -1864   -264   1842       N  
ATOM   5077  CA  ALA B 234      63.902   9.897 -92.767  1.00 50.43           C  
ANISOU 5077  CA  ALA B 234     5718   7939   5505  -1794   -201   1888       C  
ATOM   5078  C   ALA B 234      62.797  10.284 -91.792  1.00 50.68           C  
ANISOU 5078  C   ALA B 234     5670   8284   5301  -1975   -119   1995       C  
ATOM   5079  O   ALA B 234      63.059  11.072 -90.877  1.00 47.26           O  
ANISOU 5079  O   ALA B 234     5210   8039   4708  -1943    -75   2040       O  
ATOM   5080  CB  ALA B 234      64.348  11.133 -93.542  1.00 39.87           C  
ANISOU 5080  CB  ALA B 234     4315   6695   4139  -1561   -102   1672       C  
ATOM   5081  N   GLY B 235      61.582   9.765 -91.968  1.00 50.86           N  
ANISOU 5081  N   GLY B 235     5647   8385   5293  -2165    -97   2025       N  
ATOM   5082  CA  GLY B 235      60.478  10.097 -91.087  1.00 47.10           C  
ANISOU 5082  CA  GLY B 235     5069   8240   4586  -2341     -9   2115       C  
ATOM   5083  C   GLY B 235      59.868  11.466 -91.294  1.00 50.56           C  
ANISOU 5083  C   GLY B 235     5366   8986   4857  -2222    148   1931       C  
ATOM   5084  O   GLY B 235      59.324  12.042 -90.348  1.00 55.62           O  
ANISOU 5084  O   GLY B 235     5938   9876   5319  -2245    204   1933       O  
ATOM   5085  N   TYR B 236      59.920  12.001 -92.515  1.00 51.01           N  
ANISOU 5085  N   TYR B 236     5391   8988   5001  -2044    190   1721       N  
ATOM   5086  CA  TYR B 236      59.456  13.356 -92.798  1.00 49.41           C  
ANISOU 5086  CA  TYR B 236     5068   9032   4674  -1900    315   1548       C  
ATOM   5087  C   TYR B 236      58.382  13.387 -93.884  1.00 48.04           C  
ANISOU 5087  C   TYR B 236     4795   8937   4520  -1917    366   1419       C  
ATOM   5088  O   TYR B 236      58.263  14.373 -94.613  1.00 51.27           O  
ANISOU 5088  O   TYR B 236     5136   9430   4914  -1747    431   1252       O  
ATOM   5089  CB  TYR B 236      60.630  14.252 -93.192  1.00 40.02           C  
ANISOU 5089  CB  TYR B 236     3923   7736   3545  -1650    315   1428       C  
ATOM   5090  CG  TYR B 236      61.609  14.515 -92.071  1.00 47.54           C  
ANISOU 5090  CG  TYR B 236     4941   8679   4442  -1615    280   1528       C  
ATOM   5091  CD1 TYR B 236      62.921  14.068 -92.146  1.00 50.65           C  
ANISOU 5091  CD1 TYR B 236     5449   8814   4983  -1537    179   1578       C  
ATOM   5092  CD2 TYR B 236      61.220  15.210 -90.935  1.00 56.16           C  
ANISOU 5092  CD2 TYR B 236     5977  10016   5344  -1643    335   1546       C  
ATOM   5093  CE1 TYR B 236      63.817  14.308 -91.121  1.00 54.35           C  
ANISOU 5093  CE1 TYR B 236     5968   9286   5396  -1511    137   1673       C  
ATOM   5094  CE2 TYR B 236      62.108  15.451 -89.905  1.00 55.93           C  
ANISOU 5094  CE2 TYR B 236     6008   9981   5261  -1613    291   1619       C  
ATOM   5095  CZ  TYR B 236      63.405  15.000 -90.005  1.00 53.10           C  
ANISOU 5095  CZ  TYR B 236     5756   9396   5026  -1566    198   1708       C  
ATOM   5096  OH  TYR B 236      64.298  15.239 -88.988  1.00 55.95           O  
ANISOU 5096  OH  TYR B 236     6166   9773   5319  -1547    149   1795       O  
ATOM   5097  N   THR B 237      57.587  12.319 -93.992  1.00 47.80           N  
ANISOU 5097  N   THR B 237     4756   8882   4525  -2132    328   1504       N  
ATOM   5098  CA  THR B 237      56.564  12.254 -95.032  1.00 52.27           C  
ANISOU 5098  CA  THR B 237     5225   9524   5112  -2168    361   1386       C  
ATOM   5099  C   THR B 237      55.595  13.425 -94.936  1.00 57.32           C  
ANISOU 5099  C   THR B 237     5738  10427   5614  -2040    444   1240       C  
ATOM   5100  O   THR B 237      55.184  13.985 -95.960  1.00 58.73           O  
ANISOU 5100  O   THR B 237     5846  10656   5812  -1924    478   1087       O  
ATOM   5101  CB  THR B 237      55.807  10.928 -94.949  1.00 55.67           C  
ANISOU 5101  CB  THR B 237     5665   9896   5589  -2447    294   1515       C  
ATOM   5102  OG1 THR B 237      56.719   9.845 -95.167  1.00 64.70           O  
ANISOU 5102  OG1 THR B 237     6977  10672   6932  -2474    160   1582       O  
ATOM   5103  CG2 THR B 237      54.698  10.869 -95.993  1.00 50.56           C  
ANISOU 5103  CG2 THR B 237     4904   9354   4951  -2500    324   1390       C  
ATOM   5104  N   GLU B 238      55.232  13.823 -93.717  1.00 57.19           N  
ANISOU 5104  N   GLU B 238     5705  10547   5478  -2032    452   1266       N  
ATOM   5105  CA  GLU B 238      54.319  14.951 -93.555  1.00 67.17           C  
ANISOU 5105  CA  GLU B 238     6861  12015   6647  -1888    504   1109       C  
ATOM   5106  C   GLU B 238      54.921  16.241 -94.097  1.00 59.84           C  
ANISOU 5106  C   GLU B 238     5934  11054   5749  -1628    536    956       C  
ATOM   5107  O   GLU B 238      54.211  17.078 -94.668  1.00 66.08           O  
ANISOU 5107  O   GLU B 238     6642  11935   6530  -1499    561    815       O  
ATOM   5108  CB  GLU B 238      53.961  15.139 -92.081  1.00 81.79           C  
ANISOU 5108  CB  GLU B 238     8687  14023   8366  -1935    508   1158       C  
ATOM   5109  CG  GLU B 238      53.458  13.907 -91.358  1.00 92.62           C  
ANISOU 5109  CG  GLU B 238    10068  15432   9692  -2199    465   1337       C  
ATOM   5110  CD  GLU B 238      53.472  14.101 -89.855  1.00105.86           C  
ANISOU 5110  CD  GLU B 238    11737  17250  11237  -2235    463   1400       C  
ATOM   5111  OE1 GLU B 238      53.887  13.172 -89.131  1.00111.38           O  
ANISOU 5111  OE1 GLU B 238    12514  17880  11926  -2407    402   1591       O  
ATOM   5112  OE2 GLU B 238      53.088  15.199 -89.399  1.00109.14           O  
ANISOU 5112  OE2 GLU B 238    12068  17838  11560  -2091    515   1259       O  
ATOM   5113  N   LYS B 239      56.231  16.416 -93.935  1.00 51.74           N  
ANISOU 5113  N   LYS B 239     5001   9893   4765  -1553    524    995       N  
ATOM   5114  CA  LYS B 239      56.840  17.739 -93.973  1.00 47.01           C  
ANISOU 5114  CA  LYS B 239     4410   9284   4167  -1326    545    875       C  
ATOM   5115  C   LYS B 239      57.520  18.087 -95.291  1.00 42.48           C  
ANISOU 5115  C   LYS B 239     3859   8585   3696  -1195    548    803       C  
ATOM   5116  O   LYS B 239      57.790  19.268 -95.533  1.00 39.31           O  
ANISOU 5116  O   LYS B 239     3451   8181   3304  -1012    559    696       O  
ATOM   5117  CB  LYS B 239      57.871  17.862 -92.843  1.00 53.18           C  
ANISOU 5117  CB  LYS B 239     5271  10027   4909  -1319    527    956       C  
ATOM   5118  CG  LYS B 239      57.423  17.308 -91.496  1.00 58.10           C  
ANISOU 5118  CG  LYS B 239     5886  10762   5425  -1478    511   1064       C  
ATOM   5119  CD  LYS B 239      57.196  18.431 -90.491  1.00 60.14           C  
ANISOU 5119  CD  LYS B 239     6096  11175   5579  -1373    539    961       C  
ATOM   5120  CE  LYS B 239      57.544  18.004 -89.070  1.00 55.37           C  
ANISOU 5120  CE  LYS B 239     5529  10632   4876  -1493    511   1086       C  
ATOM   5121  NZ  LYS B 239      56.583  17.005 -88.535  1.00 54.23           N  
ANISOU 5121  NZ  LYS B 239     5341  10603   4663  -1703    497   1199       N  
ATOM   5122  N   ILE B 240      57.812  17.108 -96.140  1.00 37.98           N  
ANISOU 5122  N   ILE B 240     3312   7917   3202  -1293    536    860       N  
ATOM   5123  CA  ILE B 240      58.623  17.326 -97.329  1.00 37.88           C  
ANISOU 5123  CA  ILE B 240     3316   7802   3275  -1182    541    799       C  
ATOM   5124  C   ILE B 240      57.833  16.908 -98.562  1.00 42.24           C  
ANISOU 5124  C   ILE B 240     3808   8366   3874  -1222    537    723       C  
ATOM   5125  O   ILE B 240      57.314  15.786 -98.625  1.00 49.52           O  
ANISOU 5125  O   ILE B 240     4736   9249   4830  -1395    502    775       O  
ATOM   5126  CB  ILE B 240      59.957  16.568 -97.242  1.00 41.22           C  
ANISOU 5126  CB  ILE B 240     3882   7961   3820  -1178    461    869       C  
ATOM   5127  CG1 ILE B 240      60.724  17.015 -95.992  1.00 41.54           C  
ANISOU 5127  CG1 ILE B 240     3971   8013   3798  -1145    458    949       C  
ATOM   5128  CG2 ILE B 240      60.773  16.803 -98.494  1.00 32.79           C  
ANISOU 5128  CG2 ILE B 240     2850   6746   2863  -1025    438    763       C  
ATOM   5129  CD1 ILE B 240      62.057  16.344 -95.811  1.00 42.20           C  
ANISOU 5129  CD1 ILE B 240     4179   7856   3999  -1127    372   1026       C  
ATOM   5130  N   VAL B 241      57.745  17.818 -99.534  1.00 36.29           N  
ANISOU 5130  N   VAL B 241     3010   7649   3129  -1064    552    603       N  
ATOM   5131  CA  VAL B 241      57.082  17.575-100.810  1.00 40.64           C  
ANISOU 5131  CA  VAL B 241     3493   8242   3704  -1084    548    523       C  
ATOM   5132  C   VAL B 241      58.130  17.604-101.916  1.00 44.44           C  
ANISOU 5132  C   VAL B 241     4051   8554   4281   -965    510    456       C  
ATOM   5133  O   VAL B 241      59.315  17.845-101.660  1.00 42.38           O  
ANISOU 5133  O   VAL B 241     3876   8162   4065   -873    495    478       O  
ATOM   5134  CB  VAL B 241      55.962  18.601-101.064  1.00 38.89           C  
ANISOU 5134  CB  VAL B 241     3202   8141   3434   -973    540    433       C  
ATOM   5135  CG1 VAL B 241      54.782  18.330-100.138  1.00 43.54           C  
ANISOU 5135  CG1 VAL B 241     3735   8854   3954  -1087    544    465       C  
ATOM   5136  CG2 VAL B 241      56.479  20.022-100.871  1.00 32.63           C  
ANISOU 5136  CG2 VAL B 241     2440   7318   2641   -769    537    391       C  
ATOM   5137  N   ILE B 242      57.707  17.353-103.152  1.00 40.33           N  
ANISOU 5137  N   ILE B 242     3490   8053   3781   -972    492    371       N  
ATOM   5138  CA  ILE B 242      58.622  17.102-104.258  1.00 39.51           C  
ANISOU 5138  CA  ILE B 242     3450   7807   3753   -895    456    296       C  
ATOM   5139  C   ILE B 242      58.363  18.119-105.362  1.00 38.89           C  
ANISOU 5139  C   ILE B 242     3294   7866   3618   -777    475    221       C  
ATOM   5140  O   ILE B 242      57.207  18.395-105.699  1.00 43.06           O  
ANISOU 5140  O   ILE B 242     3715   8566   4080   -809    487    196       O  
ATOM   5141  CB  ILE B 242      58.478  15.667-104.794  1.00 38.67           C  
ANISOU 5141  CB  ILE B 242     3388   7576   3728  -1027    401    250       C  
ATOM   5142  CG1 ILE B 242      58.891  14.658-103.717  1.00 37.25           C  
ANISOU 5142  CG1 ILE B 242     3306   7218   3629  -1136    359    349       C  
ATOM   5143  CG2 ILE B 242      59.284  15.485-106.081  1.00 38.56           C  
ANISOU 5143  CG2 ILE B 242     3412   7472   3768   -933    375    131       C  
ATOM   5144  CD1 ILE B 242      58.698  13.210-104.118  1.00 37.56           C  
ANISOU 5144  CD1 ILE B 242     3401   7096   3774  -1278    285    314       C  
ATOM   5145  N   GLY B 243      59.440  18.672-105.914  1.00 34.79           N  
ANISOU 5145  N   GLY B 243     2818   7279   3121   -646    472    197       N  
ATOM   5146  CA  GLY B 243      59.360  19.531-107.073  1.00 38.41           C  
ANISOU 5146  CA  GLY B 243     3217   7847   3528   -549    475    148       C  
ATOM   5147  C   GLY B 243      60.169  18.935-108.207  1.00 42.75           C  
ANISOU 5147  C   GLY B 243     3809   8323   4112   -533    453     66       C  
ATOM   5148  O   GLY B 243      61.115  18.170-107.976  1.00 35.30           O  
ANISOU 5148  O   GLY B 243     2948   7216   3249   -539    439     52       O  
ATOM   5149  N   MET B 244      59.798  19.285-109.432  1.00 36.75           N  
ANISOU 5149  N   MET B 244     2984   7693   3285   -506    446      9       N  
ATOM   5150  CA  MET B 244      60.413  18.713-110.622  1.00 38.49           C  
ANISOU 5150  CA  MET B 244     3223   7898   3504   -498    431    -94       C  
ATOM   5151  C   MET B 244      60.815  19.812-111.589  1.00 36.08           C  
ANISOU 5151  C   MET B 244     2873   7719   3115   -397    440    -78       C  
ATOM   5152  O   MET B 244      60.112  20.817-111.724  1.00 38.52           O  
ANISOU 5152  O   MET B 244     3123   8148   3364   -362    429    -15       O  
ATOM   5153  CB  MET B 244      59.464  17.749-111.334  1.00 36.47           C  
ANISOU 5153  CB  MET B 244     2930   7700   3228   -613    400   -198       C  
ATOM   5154  CG  MET B 244      59.082  16.528-110.524  1.00 39.60           C  
ANISOU 5154  CG  MET B 244     3376   7956   3715   -743    376   -208       C  
ATOM   5155  SD  MET B 244      57.873  15.519-111.408  1.00 41.80           S  
ANISOU 5155  SD  MET B 244     3601   8313   3969   -897    327   -330       S  
ATOM   5156  CE  MET B 244      58.863  14.855-112.746  1.00 38.39           C  
ANISOU 5156  CE  MET B 244     3217   7819   3549   -844    306   -512       C  
ATOM   5157  N   ASP B 245      61.951  19.614-112.248  1.00 34.90           N  
ANISOU 5157  N   ASP B 245     2755   7535   2970   -350    449   -132       N  
ATOM   5158  CA  ASP B 245      62.326  20.353-113.451  1.00 33.04           C  
ANISOU 5158  CA  ASP B 245     2470   7451   2633   -295    454   -135       C  
ATOM   5159  C   ASP B 245      62.502  19.315-114.553  1.00 40.24           C  
ANISOU 5159  C   ASP B 245     3371   8409   3508   -333    451   -298       C  
ATOM   5160  O   ASP B 245      63.525  18.625-114.606  1.00 37.28           O  
ANISOU 5160  O   ASP B 245     3039   7935   3190   -305    467   -382       O  
ATOM   5161  CB  ASP B 245      63.593  21.172-113.242  1.00 31.28           C  
ANISOU 5161  CB  ASP B 245     2288   7162   2437   -207    466    -51       C  
ATOM   5162  CG  ASP B 245      63.962  21.993-114.467  1.00 35.80           C  
ANISOU 5162  CG  ASP B 245     2843   7834   2926   -170    431    -21       C  
ATOM   5163  OD1 ASP B 245      63.172  21.999-115.442  1.00 43.66           O  
ANISOU 5163  OD1 ASP B 245     3786   8973   3830   -204    403    -56       O  
ATOM   5164  OD2 ASP B 245      65.029  22.647-114.457  1.00 35.40           O  
ANISOU 5164  OD2 ASP B 245     2820   7736   2895   -119    431     47       O  
ATOM   5165  N   VAL B 246      61.507  19.208-115.432  1.00 44.40           N  
ANISOU 5165  N   VAL B 246     3836   9095   3940   -391    425   -354       N  
ATOM   5166  CA  VAL B 246      61.589  18.231-116.510  1.00 44.91           C  
ANISOU 5166  CA  VAL B 246     3888   9220   3955   -433    416   -534       C  
ATOM   5167  C   VAL B 246      62.533  18.709-117.612  1.00 39.45           C  
ANISOU 5167  C   VAL B 246     3159   8681   3148   -369    446   -562       C  
ATOM   5168  O   VAL B 246      63.198  17.890-118.257  1.00 43.48           O  
ANISOU 5168  O   VAL B 246     3676   9197   3646   -361    462   -727       O  
ATOM   5169  CB  VAL B 246      60.177  17.912-117.042  1.00 44.97           C  
ANISOU 5169  CB  VAL B 246     3836   9357   3894   -533    370   -590       C  
ATOM   5170  CG1 VAL B 246      59.179  18.955-116.578  1.00 49.83           C  
ANISOU 5170  CG1 VAL B 246     4393  10061   4479   -530    354   -429       C  
ATOM   5171  CG2 VAL B 246      60.161  17.816-118.548  1.00 41.35           C  
ANISOU 5171  CG2 VAL B 246     3319   9110   3283   -548    358   -707       C  
ATOM   5172  N   ALA B 247      62.644  20.023-117.809  1.00 37.82           N  
ANISOU 5172  N   ALA B 247     2934   8550   2885   -322    427   -399       N  
ATOM   5173  CA  ALA B 247      63.467  20.621-118.861  1.00 42.60           C  
ANISOU 5173  CA  ALA B 247     3528   9246   3411   -283    407   -374       C  
ATOM   5174  C   ALA B 247      63.103  20.034-120.222  1.00 45.11           C  
ANISOU 5174  C   ALA B 247     3781   9768   3591   -337    395   -523       C  
ATOM   5175  O   ALA B 247      63.910  19.403-120.906  1.00 48.30           O  
ANISOU 5175  O   ALA B 247     4172  10227   3952   -326    429   -669       O  
ATOM   5176  CB  ALA B 247      64.963  20.455-118.559  1.00 36.09           C  
ANISOU 5176  CB  ALA B 247     2743   8316   2654   -221    457   -396       C  
ATOM   5177  N   ALA B 248      61.847  20.264-120.601  1.00 47.20           N  
ANISOU 5177  N   ALA B 248     3995  10157   3784   -392    344   -493       N  
ATOM   5178  CA  ALA B 248      61.261  19.555-121.731  1.00 46.31           C  
ANISOU 5178  CA  ALA B 248     3817  10239   3540   -465    327   -654       C  
ATOM   5179  C   ALA B 248      61.832  19.992-123.070  1.00 43.77           C  
ANISOU 5179  C   ALA B 248     3446  10079   3106   -456    302   -647       C  
ATOM   5180  O   ALA B 248      61.700  19.255-124.051  1.00 43.77           O  
ANISOU 5180  O   ALA B 248     3400  10226   3005   -505    302   -822       O  
ATOM   5181  CB  ALA B 248      59.748  19.737-121.733  1.00 47.02           C  
ANISOU 5181  CB  ALA B 248     3847  10435   3582   -529    273   -607       C  
ATOM   5182  N   SER B 249      62.456  21.169-123.139  1.00 39.34           N  
ANISOU 5182  N   SER B 249     2889   9504   2555   -406    280   -455       N  
ATOM   5183  CA  SER B 249      63.094  21.581-124.384  1.00 48.68           C  
ANISOU 5183  CA  SER B 249     4013  10854   3628   -416    267   -433       C  
ATOM   5184  C   SER B 249      64.195  20.612-124.789  1.00 48.46           C  
ANISOU 5184  C   SER B 249     3992  10836   3583   -400    330   -636       C  
ATOM   5185  O   SER B 249      64.488  20.464-125.981  1.00 57.58           O  
ANISOU 5185  O   SER B 249     5080  12178   4621   -428    330   -715       O  
ATOM   5186  CB  SER B 249      63.663  22.995-124.246  1.00 40.01           C  
ANISOU 5186  CB  SER B 249     2923   9723   2555   -379    239   -187       C  
ATOM   5187  OG  SER B 249      62.688  23.900-123.753  1.00 47.33           O  
ANISOU 5187  OG  SER B 249     3843  10624   3516   -369    186    -15       O  
ATOM   5188  N   GLU B 250      64.801  19.928-123.815  1.00 42.94           N  
ANISOU 5188  N   GLU B 250     3362   9951   3001   -350    388   -729       N  
ATOM   5189  CA  GLU B 250      65.942  19.066-124.108  1.00 45.38           C  
ANISOU 5189  CA  GLU B 250     3668  10260   3313   -306    451   -922       C  
ATOM   5190  C   GLU B 250      65.529  17.853-124.931  1.00 51.32           C  
ANISOU 5190  C   GLU B 250     4380  11136   3984   -342    464  -1200       C  
ATOM   5191  O   GLU B 250      66.304  17.372-125.766  1.00 56.14           O  
ANISOU 5191  O   GLU B 250     4945  11850   4534   -317    493  -1361       O  
ATOM   5192  CB  GLU B 250      66.619  18.624-122.812  1.00 48.65           C  
ANISOU 5192  CB  GLU B 250     4152  10447   3884   -237    507   -949       C  
ATOM   5193  CG  GLU B 250      67.217  19.762-121.995  1.00 53.87           C  
ANISOU 5193  CG  GLU B 250     4856  10982   4630   -199    496   -704       C  
ATOM   5194  CD  GLU B 250      68.293  20.517-122.744  1.00 65.40           C  
ANISOU 5194  CD  GLU B 250     6276  12548   6024   -186    493   -618       C  
ATOM   5195  OE1 GLU B 250      68.237  21.764-122.768  1.00 68.52           O  
ANISOU 5195  OE1 GLU B 250     6672  12960   6400   -208    446   -398       O  
ATOM   5196  OE2 GLU B 250      69.187  19.862-123.321  1.00 70.12           O  
ANISOU 5196  OE2 GLU B 250     6833  13222   6587   -155    537   -778       O  
ATOM   5197  N   PHE B 251      64.317  17.340-124.713  1.00 47.01           N  
ANISOU 5197  N   PHE B 251     3845  10585   3433   -405    440  -1273       N  
ATOM   5198  CA  PHE B 251      63.835  16.183-125.456  1.00 45.46           C  
ANISOU 5198  CA  PHE B 251     3622  10489   3160   -455    437  -1553       C  
ATOM   5199  C   PHE B 251      62.644  16.520-126.352  1.00 52.36           C  
ANISOU 5199  C   PHE B 251     4429  11559   3907   -552    368  -1505       C  
ATOM   5200  O   PHE B 251      61.881  15.627-126.734  1.00 47.70           O  
ANISOU 5200  O   PHE B 251     3830  11025   3268   -622    345  -1706       O  
ATOM   5201  CB  PHE B 251      63.501  15.028-124.507  1.00 48.00           C  
ANISOU 5201  CB  PHE B 251     4018  10642   3576   -467    463  -1745       C  
ATOM   5202  CG  PHE B 251      62.501  15.368-123.429  1.00 53.88           C  
ANISOU 5202  CG  PHE B 251     4805  11237   4428   -522    420  -1553       C  
ATOM   5203  CD1 PHE B 251      62.916  15.918-122.222  1.00 45.04           C  
ANISOU 5203  CD1 PHE B 251     3735   9923   3456   -465    443  -1355       C  
ATOM   5204  CD2 PHE B 251      61.155  15.086-123.601  1.00 51.36           C  
ANISOU 5204  CD2 PHE B 251     4471  10960   4082   -634    348  -1578       C  
ATOM   5205  CE1 PHE B 251      62.005  16.207-121.226  1.00 44.11           C  
ANISOU 5205  CE1 PHE B 251     3648   9672   3441   -512    403  -1193       C  
ATOM   5206  CE2 PHE B 251      60.235  15.371-122.604  1.00 54.06           C  
ANISOU 5206  CE2 PHE B 251     4835  11172   4535   -683    310  -1406       C  
ATOM   5207  CZ  PHE B 251      60.660  15.933-121.417  1.00 40.97           C  
ANISOU 5207  CZ  PHE B 251     3223   9334   3010   -618    342  -1219       C  
ATOM   5208  N   TYR B 252      62.479  17.792-126.701  1.00 48.99           N  
ANISOU 5208  N   TYR B 252     3952  11231   3430   -558    328  -1249       N  
ATOM   5209  CA  TYR B 252      61.531  18.207-127.728  1.00 50.32           C  
ANISOU 5209  CA  TYR B 252     4032  11615   3470   -632    268  -1191       C  
ATOM   5210  C   TYR B 252      62.214  18.117-129.087  1.00 57.36           C  
ANISOU 5210  C   TYR B 252     4853  12706   4237   -640    283  -1283       C  
ATOM   5211  O   TYR B 252      63.262  18.736-129.302  1.00 59.94           O  
ANISOU 5211  O   TYR B 252     5167  13056   4552   -594    304  -1181       O  
ATOM   5212  CB  TYR B 252      61.034  19.627-127.462  1.00 48.12           C  
ANISOU 5212  CB  TYR B 252     3729  11348   3205   -625    216   -881       C  
ATOM   5213  CG  TYR B 252      60.130  20.191-128.534  1.00 47.44           C  
ANISOU 5213  CG  TYR B 252     3541  11490   2994   -687    159   -789       C  
ATOM   5214  CD1 TYR B 252      58.773  19.893-128.555  1.00 49.16           C  
ANISOU 5214  CD1 TYR B 252     3721  11771   3185   -749    119   -824       C  
ATOM   5215  CD2 TYR B 252      60.631  21.037-129.513  1.00 52.79           C  
ANISOU 5215  CD2 TYR B 252     4155  12325   3577   -690    146   -656       C  
ATOM   5216  CE1 TYR B 252      57.939  20.417-129.529  1.00 49.31           C  
ANISOU 5216  CE1 TYR B 252     3645  11996   3093   -798     72   -731       C  
ATOM   5217  CE2 TYR B 252      59.810  21.563-130.490  1.00 62.24           C  
ANISOU 5217  CE2 TYR B 252     5260  13729   4658   -747     99   -558       C  
ATOM   5218  CZ  TYR B 252      58.466  21.251-130.494  1.00 69.52           C  
ANISOU 5218  CZ  TYR B 252     6149  14703   5561   -794     64   -596       C  
ATOM   5219  OH  TYR B 252      57.655  21.779-131.470  1.00 71.91           O  
ANISOU 5219  OH  TYR B 252     6364  15210   5747   -845     20   -493       O  
ATOM   5220  N   ARG B 253      61.621  17.349-130.006  1.00 67.56           N  
ANISOU 5220  N   ARG B 253     6093  14151   5427   -705    270  -1479       N  
ATOM   5221  CA  ARG B 253      62.252  17.073-131.284  1.00 81.04           C  
ANISOU 5221  CA  ARG B 253     7728  16056   7007   -712    292  -1615       C  
ATOM   5222  C   ARG B 253      61.485  17.818-132.365  1.00 88.44           C  
ANISOU 5222  C   ARG B 253     8565  17242   7797   -790    241  -1470       C  
ATOM   5223  O   ARG B 253      61.683  19.036-132.529  1.00 95.17           O  
ANISOU 5223  O   ARG B 253     9380  18161   8619   -787    220  -1204       O  
ATOM   5224  CB  ARG B 253      62.353  15.559-131.500  1.00 82.91           C  
ANISOU 5224  CB  ARG B 253     7993  16259   7252   -710    322  -1982       C  
ATOM   5225  CG  ARG B 253      63.314  14.901-130.519  1.00 81.73           C  
ANISOU 5225  CG  ARG B 253     7932  15874   7248   -614    377  -2116       C  
ATOM   5226  CD  ARG B 253      64.682  15.568-130.600  1.00 80.27           C  
ANISOU 5226  CD  ARG B 253     7720  15714   7064   -533    424  -1997       C  
ATOM   5227  NE  ARG B 253      65.461  15.449-129.368  1.00 78.00           N  
ANISOU 5227  NE  ARG B 253     7517  15184   6936   -443    466  -1978       N  
ATOM   5228  CZ  ARG B 253      66.209  14.396-129.056  1.00 79.56           C  
ANISOU 5228  CZ  ARG B 253     7751  15256   7221   -360    515  -2232       C  
ATOM   5229  NH1 ARG B 253      66.269  13.357-129.877  1.00 83.49           N  
ANISOU 5229  NH1 ARG B 253     8218  15832   7673   -352    523  -2540       N  
ATOM   5230  NH2 ARG B 253      66.892  14.379-127.920  1.00 79.65           N  
ANISOU 5230  NH2 ARG B 253     7828  15058   7379   -278    553  -2184       N  
ATOM   5231  N   ASP B 254      60.623  17.160-133.133  1.00 84.23           N  
ANISOU 5231  N   ASP B 254     7987  16846   7169   -864    218  -1630       N  
ATOM   5232  CA  ASP B 254      59.947  17.855-134.223  1.00 87.10           C  
ANISOU 5232  CA  ASP B 254     8250  17463   7383   -936    174  -1492       C  
ATOM   5233  C   ASP B 254      58.645  18.497-133.760  1.00 88.61           C  
ANISOU 5233  C   ASP B 254     8435  17623   7608   -971    112  -1290       C  
ATOM   5234  O   ASP B 254      58.440  19.700-133.943  1.00 92.18           O  
ANISOU 5234  O   ASP B 254     8842  18152   8029   -969     79  -1018       O  
ATOM   5235  CB  ASP B 254      59.693  16.892-135.385  1.00 80.64           C  
ANISOU 5235  CB  ASP B 254     7378  16836   6428   -997    178  -1759       C  
ATOM   5236  CG  ASP B 254      60.960  16.556-136.142  1.00 80.90           C  
ANISOU 5236  CG  ASP B 254     7371  16985   6381   -960    235  -1914       C  
ATOM   5237  OD1 ASP B 254      61.905  17.370-136.092  1.00 76.32           O  
ANISOU 5237  OD1 ASP B 254     6773  16424   5801   -917    259  -1741       O  
ATOM   5238  OD2 ASP B 254      61.014  15.486-136.785  1.00 85.42           O  
ANISOU 5238  OD2 ASP B 254     7930  17633   6893   -975    254  -2213       O  
ATOM   5239  N   GLY B 255      57.765  17.710-133.157  1.00 81.93           N  
ANISOU 5239  N   GLY B 255     7635  16667   6830  -1004     94  -1423       N  
ATOM   5240  CA  GLY B 255      56.531  18.235-132.615  1.00 70.12           C  
ANISOU 5240  CA  GLY B 255     6126  15141   5374  -1030     41  -1251       C  
ATOM   5241  C   GLY B 255      56.073  17.398-131.444  1.00 63.86           C  
ANISOU 5241  C   GLY B 255     5413  14142   4710  -1044     39  -1379       C  
ATOM   5242  O   GLY B 255      55.020  17.651-130.854  1.00 53.80           O  
ANISOU 5242  O   GLY B 255     4127  12833   3481  -1071     -2  -1273       O  
ATOM   5243  N   LYS B 256      56.873  16.392-131.107  1.00 59.13           N  
ANISOU 5243  N   LYS B 256     4891  13407   4170  -1027     81  -1609       N  
ATOM   5244  CA  LYS B 256      56.606  15.460-130.024  1.00 58.90           C  
ANISOU 5244  CA  LYS B 256     4951  13168   4261  -1054     76  -1758       C  
ATOM   5245  C   LYS B 256      57.683  15.606-128.949  1.00 56.93           C  
ANISOU 5245  C   LYS B 256     4785  12716   4130   -957    131  -1710       C  
ATOM   5246  O   LYS B 256      58.513  16.522-128.987  1.00 51.34           O  
ANISOU 5246  O   LYS B 256     4062  12021   3423   -874    163  -1536       O  
ATOM   5247  CB  LYS B 256      56.553  14.025-130.553  1.00 62.57           C  
ANISOU 5247  CB  LYS B 256     5450  13617   4706  -1122     63  -2102       C  
ATOM   5248  CG  LYS B 256      56.059  13.875-131.982  1.00 61.08           C  
ANISOU 5248  CG  LYS B 256     5177  13664   4365  -1185     36  -2190       C  
ATOM   5249  CD  LYS B 256      54.554  13.997-132.076  1.00 61.83           C  
ANISOU 5249  CD  LYS B 256     5222  13845   4427  -1291    -37  -2105       C  
ATOM   5250  CE  LYS B 256      54.024  13.226-133.275  1.00 65.52           C  
ANISOU 5250  CE  LYS B 256     5649  14465   4780  -1382    -76  -2319       C  
ATOM   5251  NZ  LYS B 256      54.108  11.752-133.074  1.00 67.27           N  
ANISOU 5251  NZ  LYS B 256     5963  14507   5087  -1438   -101  -2653       N  
ATOM   5252  N   TYR B 257      57.669  14.680-127.991  1.00 59.68           N  
ANISOU 5252  N   TYR B 257     5224  12870   4581   -980    131  -1865       N  
ATOM   5253  CA  TYR B 257      58.668  14.614-126.934  1.00 53.79           C  
ANISOU 5253  CA  TYR B 257     4566  11924   3947   -893    189  -1857       C  
ATOM   5254  C   TYR B 257      59.182  13.186-126.830  1.00 58.68           C  
ANISOU 5254  C   TYR B 257     5269  12402   4626   -902    196  -2191       C  
ATOM   5255  O   TYR B 257      58.401  12.230-126.895  1.00 56.69           O  
ANISOU 5255  O   TYR B 257     5041  12084   4413  -1010    124  -2371       O  
ATOM   5256  CB  TYR B 257      58.090  15.087-125.593  1.00 52.54           C  
ANISOU 5256  CB  TYR B 257     4442  11649   3872   -906    175  -1664       C  
ATOM   5257  CG  TYR B 257      57.597  16.520-125.617  1.00 51.39           C  
ANISOU 5257  CG  TYR B 257     4219  11604   3702   -873    157  -1355       C  
ATOM   5258  CD1 TYR B 257      58.422  17.568-125.219  1.00 44.69           C  
ANISOU 5258  CD1 TYR B 257     3385  10685   2910   -765    194  -1145       C  
ATOM   5259  CD2 TYR B 257      56.310  16.826-126.048  1.00 46.96           C  
ANISOU 5259  CD2 TYR B 257     3572  11192   3079   -946     89  -1282       C  
ATOM   5260  CE1 TYR B 257      57.976  18.880-125.247  1.00 44.03           C  
ANISOU 5260  CE1 TYR B 257     3244  10666   2819   -732    152   -887       C  
ATOM   5261  CE2 TYR B 257      55.856  18.133-126.080  1.00 46.29           C  
ANISOU 5261  CE2 TYR B 257     3417  11190   2983   -898     66  -1020       C  
ATOM   5262  CZ  TYR B 257      56.690  19.155-125.679  1.00 44.98           C  
ANISOU 5262  CZ  TYR B 257     3277  10942   2873   -791     92   -830       C  
ATOM   5263  OH  TYR B 257      56.238  20.454-125.713  1.00 45.42           O  
ANISOU 5263  OH  TYR B 257     3272  11058   2927   -741     53   -589       O  
ATOM   5264  N   ASP B 258      60.499  13.048-126.681  1.00 57.26           N  
ANISOU 5264  N   ASP B 258     5127  12132   4498   -784    270  -2261       N  
ATOM   5265  CA  ASP B 258      61.176  11.751-126.656  1.00 59.22           C  
ANISOU 5265  CA  ASP B 258     5446  12184   4869   -744    275  -2564       C  
ATOM   5266  C   ASP B 258      61.718  11.513-125.248  1.00 59.36           C  
ANISOU 5266  C   ASP B 258     5561  11828   5165   -677    289  -2457       C  
ATOM   5267  O   ASP B 258      62.829  11.929-124.918  1.00 58.12           O  
ANISOU 5267  O   ASP B 258     5406  11634   5042   -556    361  -2382       O  
ATOM   5268  CB  ASP B 258      62.293  11.701-127.699  1.00 59.97           C  
ANISOU 5268  CB  ASP B 258     5483  12434   4869   -643    339  -2710       C  
ATOM   5269  CG  ASP B 258      63.004  10.360-127.732  1.00 62.46           C  
ANISOU 5269  CG  ASP B 258     5860  12584   5288   -576    344  -3077       C  
ATOM   5270  OD1 ASP B 258      62.487   9.396-127.130  1.00 67.27           O  
ANISOU 5270  OD1 ASP B 258     6563  12905   6090   -632    266  -3192       O  
ATOM   5271  OD2 ASP B 258      64.076  10.267-128.369  1.00 63.04           O  
ANISOU 5271  OD2 ASP B 258     5883  12722   5346   -465    402  -3178       O  
ATOM   5272  N   LEU B 259      60.927  10.820-124.425  1.00 64.25           N  
ANISOU 5272  N   LEU B 259     6256  12181   5974   -768    216  -2445       N  
ATOM   5273  CA  LEU B 259      61.350  10.491-123.069  1.00 62.57           C  
ANISOU 5273  CA  LEU B 259     6141  11617   6016   -727    214  -2339       C  
ATOM   5274  C   LEU B 259      62.426   9.416-123.028  1.00 65.66           C  
ANISOU 5274  C   LEU B 259     6604  11778   6567   -627    212  -2573       C  
ATOM   5275  O   LEU B 259      63.011   9.186-121.964  1.00 59.90           O  
ANISOU 5275  O   LEU B 259     5948  10773   6038   -566    212  -2481       O  
ATOM   5276  CB  LEU B 259      60.152  10.049-122.232  1.00 64.31           C  
ANISOU 5276  CB  LEU B 259     6410  11653   6372   -876    133  -2245       C  
ATOM   5277  CG  LEU B 259      59.505  11.141-121.382  1.00 64.94           C  
ANISOU 5277  CG  LEU B 259     6454  11789   6432   -907    153  -1929       C  
ATOM   5278  CD1 LEU B 259      58.710  12.094-122.252  1.00 63.80           C  
ANISOU 5278  CD1 LEU B 259     6192  11994   6056   -946    155  -1856       C  
ATOM   5279  CD2 LEU B 259      58.620  10.514-120.328  1.00 67.36           C  
ANISOU 5279  CD2 LEU B 259     6816  11869   6908  -1040     90  -1848       C  
ATOM   5280  N   ASP B 260      62.694   8.744-124.141  1.00 72.14           N  
ANISOU 5280  N   ASP B 260     7399  12705   7306   -603    205  -2879       N  
ATOM   5281  CA  ASP B 260      63.826   7.834-124.245  1.00 72.93           C  
ANISOU 5281  CA  ASP B 260     7542  12629   7540   -468    213  -3131       C  
ATOM   5282  C   ASP B 260      64.898   8.423-125.155  1.00 68.51           C  
ANISOU 5282  C   ASP B 260     6874  12379   6778   -331    321  -3221       C  
ATOM   5283  O   ASP B 260      65.527   7.716-125.943  1.00 78.00           O  
ANISOU 5283  O   ASP B 260     8052  13631   7953   -246    334  -3535       O  
ATOM   5284  CB  ASP B 260      63.387   6.459-124.740  1.00 81.62           C  
ANISOU 5284  CB  ASP B 260     8704  13570   8737   -531    114  -3457       C  
ATOM   5285  CG  ASP B 260      64.342   5.356-124.321  1.00 86.80           C  
ANISOU 5285  CG  ASP B 260     9450  13875   9657   -402     76  -3656       C  
ATOM   5286  OD1 ASP B 260      63.945   4.173-124.372  1.00 89.22           O  
ANISOU 5286  OD1 ASP B 260     9843  13929  10127   -463    -33  -3871       O  
ATOM   5287  OD2 ASP B 260      65.485   5.674-123.928  1.00 88.79           O  
ANISOU 5287  OD2 ASP B 260     9682  14092   9962   -242    145  -3591       O  
ATOM   5288  N   PHE B 261      65.107   9.733-125.063  1.00 61.84           N  
ANISOU 5288  N   PHE B 261     5958  11751   5786   -314    396  -2951       N  
ATOM   5289  CA  PHE B 261      66.205  10.371-125.776  1.00 70.51           C  
ANISOU 5289  CA  PHE B 261     6951  13134   6705   -203    501  -2980       C  
ATOM   5290  C   PHE B 261      67.506   9.972-125.079  1.00 86.78           C  
ANISOU 5290  C   PHE B 261     9039  14967   8967    -44    537  -3028       C  
ATOM   5291  O   PHE B 261      67.518   9.136-124.170  1.00 94.86           O  
ANISOU 5291  O   PHE B 261    10168  15619  10256    -21    470  -3061       O  
ATOM   5292  CB  PHE B 261      65.984  11.880-125.858  1.00 64.44           C  
ANISOU 5292  CB  PHE B 261     6110  12630   5743   -251    548  -2658       C  
ATOM   5293  CG  PHE B 261      66.508  12.650-124.674  1.00 66.09           C  
ANISOU 5293  CG  PHE B 261     6351  12672   6088   -197    577  -2367       C  
ATOM   5294  CD1 PHE B 261      67.600  13.494-124.812  1.00 65.48           C  
ANISOU 5294  CD1 PHE B 261     6216  12691   5974   -121    631  -2216       C  
ATOM   5295  CD2 PHE B 261      65.905  12.543-123.430  1.00 66.78           C  
ANISOU 5295  CD2 PHE B 261     6536  12455   6381   -241    518  -2206       C  
ATOM   5296  CE1 PHE B 261      68.088  14.211-123.731  1.00 64.01           C  
ANISOU 5296  CE1 PHE B 261     6058  12372   5890    -79    656  -1977       C  
ATOM   5297  CE2 PHE B 261      66.389  13.259-122.344  1.00 62.81           C  
ANISOU 5297  CE2 PHE B 261     6061  11817   5986   -193    542  -1958       C  
ATOM   5298  CZ  PHE B 261      67.482  14.093-122.496  1.00 61.30           C  
ANISOU 5298  CZ  PHE B 261     5803  11776   5712   -108    619  -1861       C  
ATOM   5299  N   LYS B 262      68.614  10.588-125.486  1.00 85.55           N  
ANISOU 5299  N   LYS B 262     8782  15040   8685     59    637  -3014       N  
ATOM   5300  CA  LYS B 262      69.967  10.126-125.161  1.00 91.30           C  
ANISOU 5300  CA  LYS B 262     9492  15641   9559    228    679  -3138       C  
ATOM   5301  C   LYS B 262      70.018   8.596-125.186  1.00102.89           C  
ANISOU 5301  C   LYS B 262    11031  16833  11230    298    606  -3480       C  
ATOM   5302  O   LYS B 262      70.384   7.923-124.222  1.00108.43           O  
ANISOU 5302  O   LYS B 262    11821  17169  12209    373    547  -3482       O  
ATOM   5303  CB  LYS B 262      70.476  10.707-123.833  1.00 80.34           C  
ANISOU 5303  CB  LYS B 262     8146  14036   8341    269    683  -2839       C  
ATOM   5304  CG  LYS B 262      69.584  10.565-122.612  1.00 72.26           C  
ANISOU 5304  CG  LYS B 262     7259  12677   7518    180    590  -2642       C  
ATOM   5305  CD  LYS B 262      70.149  11.334-121.432  1.00 66.25           C  
ANISOU 5305  CD  LYS B 262     6519  11792   6862    217    609  -2349       C  
ATOM   5306  CE  LYS B 262      69.297  11.133-120.194  1.00 60.51           C  
ANISOU 5306  CE  LYS B 262     5918  10757   6317    130    523  -2170       C  
ATOM   5307  NZ  LYS B 262      69.912  11.745-118.979  1.00 56.18           N  
ANISOU 5307  NZ  LYS B 262     5397  10070   5879    174    533  -1921       N  
ATOM   5308  N   SER B 263      69.615   8.068-126.340  1.00105.15           N  
ANISOU 5308  N   SER B 263    11281  17306  11367    266    598  -3770       N  
ATOM   5309  CA  SER B 263      69.447   6.658-126.662  1.00104.60           C  
ANISOU 5309  CA  SER B 263    11275  17026  11441    302    517  -4140       C  
ATOM   5310  C   SER B 263      69.361   6.562-128.182  1.00111.97           C  
ANISOU 5310  C   SER B 263    12110  18268  12165    273    533  -4319       C  
ATOM   5311  O   SER B 263      69.292   7.604-128.848  1.00112.05           O  
ANISOU 5311  O   SER B 263    12023  18586  11963    197    579  -4079       O  
ATOM   5312  CB  SER B 263      68.196   6.094-125.983  1.00 97.02           C  
ANISOU 5312  CB  SER B 263    10463  15736  10665    149    383  -4060       C  
ATOM   5313  OG  SER B 263      68.429   5.848-124.608  1.00 96.95           O  
ANISOU 5313  OG  SER B 263    10559  15331  10947    183    327  -3870       O  
ATOM   5314  N   PRO B 264      69.380   5.367-128.778  1.00117.30           N  
ANISOU 5314  N   PRO B 264    12810  18831  12927    324    477  -4682       N  
ATOM   5315  CA  PRO B 264      69.250   5.287-130.241  1.00119.31           C  
ANISOU 5315  CA  PRO B 264    12966  19371  12993    282    486  -4805       C  
ATOM   5316  C   PRO B 264      67.934   5.893-130.712  1.00114.04           C  
ANISOU 5316  C   PRO B 264    12293  18907  12131     75    456  -4632       C  
ATOM   5317  O   PRO B 264      66.856   5.527-130.239  1.00111.87           O  
ANISOU 5317  O   PRO B 264    12123  18462  11920    -43    373  -4659       O  
ATOM   5318  CB  PRO B 264      69.322   3.781-130.524  1.00122.73           C  
ANISOU 5318  CB  PRO B 264    13466  19555  13609    367    407  -5232       C  
ATOM   5319  CG  PRO B 264      69.014   3.123-129.219  1.00122.64           C  
ANISOU 5319  CG  PRO B 264    13618  19106  13875    376    317  -5293       C  
ATOM   5320  CD  PRO B 264      69.591   4.035-128.186  1.00121.18           C  
ANISOU 5320  CD  PRO B 264    13417  18916  13710    431    391  -4997       C  
ATOM   5321  N   THR B 265      68.038   6.828-131.656  1.00110.88           N  
ANISOU 5321  N   THR B 265    11764  18866  11499     25    510  -4449       N  
ATOM   5322  CA  THR B 265      66.885   7.611-132.083  1.00105.64           C  
ANISOU 5322  CA  THR B 265    11074  18409  10656   -150    483  -4224       C  
ATOM   5323  C   THR B 265      65.831   6.730-132.744  1.00106.61           C  
ANISOU 5323  C   THR B 265    11231  18523  10751   -251    404  -4470       C  
ATOM   5324  O   THR B 265      66.140   5.875-133.579  1.00108.09           O  
ANISOU 5324  O   THR B 265    11392  18743  10934   -197    397  -4776       O  
ATOM   5325  CB  THR B 265      67.328   8.713-133.049  1.00102.78           C  
ANISOU 5325  CB  THR B 265    10567  18408  10077   -174    538  -4006       C  
ATOM   5326  OG1 THR B 265      68.347   9.509-132.431  1.00 96.41           O  
ANISOU 5326  OG1 THR B 265     9738  17584   9310    -94    595  -3780       O  
ATOM   5327  CG2 THR B 265      66.154   9.607-133.420  1.00102.29           C  
ANISOU 5327  CG2 THR B 265    10475  18532   9859   -336    499  -3745       C  
ATOM   5328  N   ASP B 266      64.573   6.948-132.360  1.00102.94           N  
ANISOU 5328  N   ASP B 266    10823  18017  10271   -401    339  -4332       N  
ATOM   5329  CA  ASP B 266      63.430   6.226-132.905  1.00106.80           C  
ANISOU 5329  CA  ASP B 266    11347  18499  10734   -530    250  -4511       C  
ATOM   5330  C   ASP B 266      62.180   7.085-132.748  1.00104.34           C  
ANISOU 5330  C   ASP B 266    11017  18312  10314   -693    211  -4211       C  
ATOM   5331  O   ASP B 266      61.624   7.173-131.648  1.00103.03           O  
ANISOU 5331  O   ASP B 266    10932  17958  10256   -756    167  -4085       O  
ATOM   5332  CB  ASP B 266      63.256   4.879-132.200  1.00109.09           C  
ANISOU 5332  CB  ASP B 266    11785  18394  11271   -526    159  -4807       C  
ATOM   5333  CG  ASP B 266      62.281   3.959-132.917  1.00113.58           C  
ANISOU 5333  CG  ASP B 266    12389  18931  11834   -649     58  -5046       C  
ATOM   5334  OD1 ASP B 266      62.486   2.729-132.874  1.00116.92           O  
ANISOU 5334  OD1 ASP B 266    12904  19075  12444   -605    -11  -5371       O  
ATOM   5335  OD2 ASP B 266      61.311   4.458-133.523  1.00114.36           O  
ANISOU 5335  OD2 ASP B 266    12425  19267  11757   -787     39  -4908       O  
ATOM   5336  N   PRO B 267      61.708   7.734-133.817  1.00 99.30           N  
ANISOU 5336  N   PRO B 267    10268  17994   9469   -764    220  -4089       N  
ATOM   5337  CA  PRO B 267      60.521   8.597-133.691  1.00 91.95           C  
ANISOU 5337  CA  PRO B 267     9306  17180   8451   -898    179  -3796       C  
ATOM   5338  C   PRO B 267      59.238   7.855-133.344  1.00 90.79           C  
ANISOU 5338  C   PRO B 267     9236  16881   8380  -1039     73  -3898       C  
ATOM   5339  O   PRO B 267      58.227   8.515-133.072  1.00 88.88           O  
ANISOU 5339  O   PRO B 267     8967  16710   8094  -1142     35  -3656       O  
ATOM   5340  CB  PRO B 267      60.418   9.255-135.073  1.00 92.79           C  
ANISOU 5340  CB  PRO B 267     9275  17648   8332   -929    201  -3709       C  
ATOM   5341  CG  PRO B 267      61.802   9.182-135.630  1.00 94.69           C  
ANISOU 5341  CG  PRO B 267     9463  17981   8536   -802    280  -3829       C  
ATOM   5342  CD  PRO B 267      62.363   7.885-135.127  1.00 97.39           C  
ANISOU 5342  CD  PRO B 267     9907  18036   9061   -714    275  -4170       C  
ATOM   5343  N   SER B 268      59.235   6.518-133.345  1.00 92.80           N  
ANISOU 5343  N   SER B 268     9581  16918   8762  -1052     14  -4240       N  
ATOM   5344  CA  SER B 268      58.015   5.790-133.010  1.00 92.57           C  
ANISOU 5344  CA  SER B 268     9625  16722   8827  -1217   -107  -4323       C  
ATOM   5345  C   SER B 268      57.652   5.946-131.539  1.00 87.64           C  
ANISOU 5345  C   SER B 268     9075  15863   8361  -1277   -149  -4147       C  
ATOM   5346  O   SER B 268      56.465   5.944-131.191  1.00 86.78           O  
ANISOU 5346  O   SER B 268     8969  15731   8274  -1437   -231  -4036       O  
ATOM   5347  CB  SER B 268      58.165   4.309-133.360  1.00 96.96           C  
ANISOU 5347  CB  SER B 268    10271  17055   9514  -1219   -178  -4730       C  
ATOM   5348  OG  SER B 268      58.477   4.133-134.732  1.00103.71           O  
ANISOU 5348  OG  SER B 268    11048  18146  10211  -1167   -140  -4909       O  
ATOM   5349  N   ARG B 269      58.651   6.080-130.667  1.00 83.34           N  
ANISOU 5349  N   ARG B 269     8582  15158   7926  -1156    -96  -4115       N  
ATOM   5350  CA  ARG B 269      58.409   6.269-129.243  1.00 79.03           C  
ANISOU 5350  CA  ARG B 269     8100  14408   7518  -1211   -132  -3945       C  
ATOM   5351  C   ARG B 269      58.019   7.696-128.891  1.00 75.29           C  
ANISOU 5351  C   ARG B 269     7543  14149   6914  -1219    -80  -3555       C  
ATOM   5352  O   ARG B 269      57.657   7.951-127.735  1.00 73.90           O  
ANISOU 5352  O   ARG B 269     7405  13783   6890  -1256    -96  -3321       O  
ATOM   5353  CB  ARG B 269      59.654   5.877-128.443  1.00 73.30           C  
ANISOU 5353  CB  ARG B 269     7464  13380   7007  -1052    -87  -4001       C  
ATOM   5354  CG  ARG B 269      60.841   6.788-128.697  1.00 69.38           C  
ANISOU 5354  CG  ARG B 269     6895  13102   6364   -874     47  -3919       C  
ATOM   5355  CD  ARG B 269      62.086   6.314-127.974  1.00 73.70           C  
ANISOU 5355  CD  ARG B 269     7517  13341   7146   -705     88  -3979       C  
ATOM   5356  NE  ARG B 269      63.211   7.224-128.176  1.00 72.43           N  
ANISOU 5356  NE  ARG B 269     7272  13404   6845   -552    216  -3881       N  
ATOM   5357  CZ  ARG B 269      64.350   6.891-128.775  1.00 72.03           C  
ANISOU 5357  CZ  ARG B 269     7180  13413   6776   -400    280  -4100       C  
ATOM   5358  NH1 ARG B 269      64.530   5.656-129.222  1.00 76.57           N  
ANISOU 5358  NH1 ARG B 269     7798  13832   7463   -360    227  -4459       N  
ATOM   5359  NH2 ARG B 269      65.316   7.789-128.915  1.00 65.69           N  
ANISOU 5359  NH2 ARG B 269     6288  12777   5894   -291    384  -3911       N  
ATOM   5360  N   TYR B 270      58.097   8.626-129.843  1.00 71.00           N  
ANISOU 5360  N   TYR B 270     6889  13906   6180  -1164    -10  -3405       N  
ATOM   5361  CA  TYR B 270      57.771  10.017-129.559  1.00 66.57           C  
ANISOU 5361  CA  TYR B 270     6253  13509   5529  -1155     27  -3034       C  
ATOM   5362  C   TYR B 270      56.327  10.130-129.088  1.00 68.00           C  
ANISOU 5362  C   TYR B 270     6417  13688   5732  -1306    -60  -2897       C  
ATOM   5363  O   TYR B 270      55.430   9.470-129.619  1.00 74.54           O  
ANISOU 5363  O   TYR B 270     7231  14542   6547  -1428   -133  -3030       O  
ATOM   5364  CB  TYR B 270      57.979  10.886-130.801  1.00 68.34           C  
ANISOU 5364  CB  TYR B 270     6360  14033   5573  -1105     79  -2914       C  
ATOM   5365  CG  TYR B 270      59.415  11.115-131.225  1.00 72.37           C  
ANISOU 5365  CG  TYR B 270     6849  14596   6054   -965    168  -2949       C  
ATOM   5366  CD1 TYR B 270      59.713  11.998-132.259  1.00 76.64           C  
ANISOU 5366  CD1 TYR B 270     7278  15399   6442   -940    202  -2803       C  
ATOM   5367  CD2 TYR B 270      60.469  10.452-130.609  1.00 74.31           C  
ANISOU 5367  CD2 TYR B 270     7175  14632   6428   -865    209  -3124       C  
ATOM   5368  CE1 TYR B 270      61.016  12.218-132.663  1.00 74.49           C  
ANISOU 5368  CE1 TYR B 270     6970  15190   6141   -834    271  -2822       C  
ATOM   5369  CE2 TYR B 270      61.778  10.665-131.011  1.00 78.64           C  
ANISOU 5369  CE2 TYR B 270     7684  15244   6954   -736    288  -3149       C  
ATOM   5370  CZ  TYR B 270      62.044  11.549-132.037  1.00 75.72           C  
ANISOU 5370  CZ  TYR B 270     7198  15147   6425   -730    317  -2994       C  
ATOM   5371  OH  TYR B 270      63.342  11.765-132.437  1.00 74.10           O  
ANISOU 5371  OH  TYR B 270     6944  15017   6195   -627    383  -3010       O  
ATOM   5372  N   ILE B 271      56.103  10.967-128.079  1.00 65.82           N  
ANISOU 5372  N   ILE B 271     6133  13382   5494  -1296    -52  -2629       N  
ATOM   5373  CA  ILE B 271      54.770  11.161-127.525  1.00 66.30           C  
ANISOU 5373  CA  ILE B 271     6153  13449   5590  -1422   -125  -2473       C  
ATOM   5374  C   ILE B 271      54.380  12.623-127.686  1.00 60.17           C  
ANISOU 5374  C   ILE B 271     5275  12876   4710  -1358    -88  -2154       C  
ATOM   5375  O   ILE B 271      55.233  13.513-127.763  1.00 60.39           O  
ANISOU 5375  O   ILE B 271     5293  12957   4694  -1230    -17  -2012       O  
ATOM   5376  CB  ILE B 271      54.684  10.728-126.042  1.00 62.90           C  
ANISOU 5376  CB  ILE B 271     5807  12679   5411  -1455   -135  -2391       C  
ATOM   5377  CG1 ILE B 271      55.807  11.360-125.225  1.00 66.99           C  
ANISOU 5377  CG1 ILE B 271     6382  13048   6024  -1292    -39  -2224       C  
ATOM   5378  CG2 ILE B 271      54.732   9.212-125.917  1.00 60.40           C  
ANISOU 5378  CG2 ILE B 271     5594  12085   5271  -1545   -194  -2653       C  
ATOM   5379  CD1 ILE B 271      55.422  12.642-124.528  1.00 70.71           C  
ANISOU 5379  CD1 ILE B 271     6795  13593   6479  -1248     -9  -1904       C  
ATOM   5380  N   THR B 272      53.074  12.866-127.727  1.00 55.46           N  
ANISOU 5380  N   THR B 272     4603  12374   4096  -1450   -144  -2040       N  
ATOM   5381  CA  THR B 272      52.563  14.212-127.917  1.00 58.11           C  
ANISOU 5381  CA  THR B 272     4841  12883   4354  -1386   -128  -1758       C  
ATOM   5382  C   THR B 272      52.540  14.986-126.597  1.00 58.77           C  
ANISOU 5382  C   THR B 272     4931  12862   4536  -1325   -112  -1537       C  
ATOM   5383  O   THR B 272      52.802  14.449-125.517  1.00 49.86           O  
ANISOU 5383  O   THR B 272     3868  11548   3527  -1356   -119  -1588       O  
ATOM   5384  CB  THR B 272      51.161  14.173-128.519  1.00 66.26           C  
ANISOU 5384  CB  THR B 272     5785  14065   5325  -1487   -190  -1736       C  
ATOM   5385  OG1 THR B 272      50.616  15.490-128.504  1.00 71.77           O  
ANISOU 5385  OG1 THR B 272     6397  14890   5981  -1412   -184  -1460       O  
ATOM   5386  CG2 THR B 272      50.255  13.277-127.710  1.00 55.24           C  
ANISOU 5386  CG2 THR B 272     4405  12535   4050  -1629   -252  -1816       C  
ATOM   5387  N   GLY B 273      52.210  16.276-126.700  1.00 55.39           N  
ANISOU 5387  N   GLY B 273     4430  12551   4065  -1240   -100  -1289       N  
ATOM   5388  CA  GLY B 273      52.098  17.102-125.509  1.00 48.15           C  
ANISOU 5388  CA  GLY B 273     3511  11546   3239  -1168    -87  -1084       C  
ATOM   5389  C   GLY B 273      50.943  16.697-124.612  1.00 57.41           C  
ANISOU 5389  C   GLY B 273     4648  12658   4505  -1261   -128  -1073       C  
ATOM   5390  O   GLY B 273      51.045  16.771-123.384  1.00 59.94           O  
ANISOU 5390  O   GLY B 273     4989  12840   4945  -1246   -116  -1003       O  
ATOM   5391  N   ASP B 274      49.824  16.274-125.207  1.00 58.21           N  
ANISOU 5391  N   ASP B 274     4689  12866   4564  -1364   -175  -1132       N  
ATOM   5392  CA  ASP B 274      48.707  15.773-124.409  1.00 58.13           C  
ANISOU 5392  CA  ASP B 274     4641  12798   4649  -1474   -208  -1127       C  
ATOM   5393  C   ASP B 274      49.111  14.521-123.642  1.00 52.01           C  
ANISOU 5393  C   ASP B 274     3938  11819   4004  -1600   -222  -1287       C  
ATOM   5394  O   ASP B 274      48.803  14.380-122.453  1.00 54.26           O  
ANISOU 5394  O   ASP B 274     4217  11982   4419  -1645   -213  -1211       O  
ATOM   5395  CB  ASP B 274      47.494  15.485-125.302  1.00 63.99           C  
ANISOU 5395  CB  ASP B 274     5304  13698   5309  -1571   -261  -1174       C  
ATOM   5396  CG  ASP B 274      46.666  16.729-125.601  1.00 68.73           C  
ANISOU 5396  CG  ASP B 274     5813  14465   5838  -1465   -265   -971       C  
ATOM   5397  OD1 ASP B 274      47.230  17.842-125.649  1.00 74.70           O  
ANISOU 5397  OD1 ASP B 274     6576  15242   6566  -1313   -234   -823       O  
ATOM   5398  OD2 ASP B 274      45.440  16.588-125.800  1.00 77.79           O  
ANISOU 5398  OD2 ASP B 274     6881  15711   6964  -1537   -308   -962       O  
ATOM   5399  N   GLN B 275      49.798  13.593-124.314  1.00 54.34           N  
ANISOU 5399  N   GLN B 275     4304  12067   4274  -1658   -244  -1511       N  
ATOM   5400  CA  GLN B 275      50.278  12.393-123.636  1.00 58.65           C  
ANISOU 5400  CA  GLN B 275     4954  12352   4978  -1755   -258  -1664       C  
ATOM   5401  C   GLN B 275      51.223  12.749-122.498  1.00 61.44           C  
ANISOU 5401  C   GLN B 275     5406  12463   5474  -1626   -168  -1525       C  
ATOM   5402  O   GLN B 275      51.166  12.147-121.420  1.00 70.50           O  
ANISOU 5402  O   GLN B 275     6619  13372   6796  -1691   -158  -1491       O  
ATOM   5403  CB  GLN B 275      50.972  11.465-124.633  1.00 61.08           C  
ANISOU 5403  CB  GLN B 275     5343  12625   5241  -1781   -282  -1941       C  
ATOM   5404  CG  GLN B 275      50.039  10.583-125.450  1.00 64.14           C  
ANISOU 5404  CG  GLN B 275     5697  13088   5586  -1948   -368  -2121       C  
ATOM   5405  CD  GLN B 275      50.765   9.866-126.574  1.00 67.11           C  
ANISOU 5405  CD  GLN B 275     6142  13462   5893  -1928   -376  -2397       C  
ATOM   5406  OE1 GLN B 275      51.546  10.471-127.306  1.00 63.05           O  
ANISOU 5406  OE1 GLN B 275     5623  13082   5251  -1783   -311  -2396       O  
ATOM   5407  NE2 GLN B 275      50.517   8.569-126.710  1.00 73.82           N  
ANISOU 5407  NE2 GLN B 275     7056  14152   6841  -2074   -453  -2631       N  
ATOM   5408  N   LEU B 276      52.090  13.739-122.717  1.00 58.55           N  
ANISOU 5408  N   LEU B 276     5050  12166   5032  -1454   -107  -1432       N  
ATOM   5409  CA  LEU B 276      53.038  14.141-121.684  1.00 55.41           C  
ANISOU 5409  CA  LEU B 276     4739  11555   4758  -1331    -27  -1304       C  
ATOM   5410  C   LEU B 276      52.322  14.782-120.502  1.00 51.29           C  
ANISOU 5410  C   LEU B 276     4168  11006   4315  -1327    -11  -1095       C  
ATOM   5411  O   LEU B 276      52.710  14.575-119.346  1.00 51.80           O  
ANISOU 5411  O   LEU B 276     4310  10846   4526  -1315     31  -1027       O  
ATOM   5412  CB  LEU B 276      54.074  15.095-122.278  1.00 52.17           C  
ANISOU 5412  CB  LEU B 276     4335  11252   4235  -1171     24  -1249       C  
ATOM   5413  CG  LEU B 276      55.264  15.493-121.410  1.00 52.64           C  
ANISOU 5413  CG  LEU B 276     4485  11109   4405  -1042    102  -1148       C  
ATOM   5414  CD1 LEU B 276      56.028  14.262-120.956  1.00 53.93           C  
ANISOU 5414  CD1 LEU B 276     4769  10996   4725  -1065    117  -1301       C  
ATOM   5415  CD2 LEU B 276      56.176  16.439-122.176  1.00 54.45           C  
ANISOU 5415  CD2 LEU B 276     4698  11492   4498   -920    141  -1092       C  
ATOM   5416  N   GLY B 277      51.277  15.564-120.773  1.00 47.67           N  
ANISOU 5416  N   GLY B 277     3572  10786   3755  -1333    -47   -995       N  
ATOM   5417  CA  GLY B 277      50.483  16.116-119.690  1.00 47.18           C  
ANISOU 5417  CA  GLY B 277     3438  10729   3760  -1327    -32   -832       C  
ATOM   5418  C   GLY B 277      49.761  15.042-118.901  1.00 46.93           C  
ANISOU 5418  C   GLY B 277     3407  10586   3840  -1504    -48   -875       C  
ATOM   5419  O   GLY B 277      49.637  15.134-117.678  1.00 44.19           O  
ANISOU 5419  O   GLY B 277     3069  10130   3591  -1507     -4   -766       O  
ATOM   5420  N   ALA B 278      49.285  14.002-119.588  1.00 50.95           N  
ANISOU 5420  N   ALA B 278     3906  11123   4329  -1666   -115  -1035       N  
ATOM   5421  CA  ALA B 278      48.646  12.893-118.888  1.00 54.30           C  
ANISOU 5421  CA  ALA B 278     4343  11419   4871  -1865   -145  -1071       C  
ATOM   5422  C   ALA B 278      49.641  12.136-118.019  1.00 55.46           C  
ANISOU 5422  C   ALA B 278     4661  11227   5182  -1871   -109  -1082       C  
ATOM   5423  O   ALA B 278      49.267  11.615-116.963  1.00 55.33           O  
ANISOU 5423  O   ALA B 278     4662  11084   5277  -1990   -105  -1005       O  
ATOM   5424  CB  ALA B 278      47.982  11.946-119.887  1.00 50.25           C  
ANISOU 5424  CB  ALA B 278     3793  10991   4309  -2042   -240  -1254       C  
ATOM   5425  N   LEU B 279      50.905  12.062-118.441  1.00 52.26           N  
ANISOU 5425  N   LEU B 279     4375  10689   4791  -1748    -85  -1169       N  
ATOM   5426  CA  LEU B 279      51.923  11.458-117.589  1.00 57.42           C  
ANISOU 5426  CA  LEU B 279     5182  11028   5606  -1720    -56  -1164       C  
ATOM   5427  C   LEU B 279      52.201  12.327-116.367  1.00 51.67           C  
ANISOU 5427  C   LEU B 279     4456  10257   4917  -1618     20   -953       C  
ATOM   5428  O   LEU B 279      52.435  11.806-115.270  1.00 51.99           O  
ANISOU 5428  O   LEU B 279     4577  10088   5088  -1671     30   -881       O  
ATOM   5429  CB  LEU B 279      53.203  11.218-118.390  1.00 62.10           C  
ANISOU 5429  CB  LEU B 279     5873  11527   6196  -1598    -45  -1322       C  
ATOM   5430  CG  LEU B 279      54.374  10.605-117.621  1.00 70.10           C  
ANISOU 5430  CG  LEU B 279     7035  12219   7380  -1539    -25  -1331       C  
ATOM   5431  CD1 LEU B 279      53.942   9.324-116.920  1.00 74.90           C  
ANISOU 5431  CD1 LEU B 279     7719  12581   8159  -1721    -95  -1355       C  
ATOM   5432  CD2 LEU B 279      55.547  10.342-118.550  1.00 69.59           C  
ANISOU 5432  CD2 LEU B 279     7032  12111   7297  -1415    -15  -1520       C  
ATOM   5433  N   TYR B 280      52.181  13.653-116.536  1.00 50.88           N  
ANISOU 5433  N   TYR B 280     4275  10352   4706  -1473     64   -851       N  
ATOM   5434  CA  TYR B 280      52.322  14.546-115.389  1.00 41.22           C  
ANISOU 5434  CA  TYR B 280     3043   9105   3513  -1377    128   -671       C  
ATOM   5435  C   TYR B 280      51.163  14.373-114.417  1.00 56.15           C  
ANISOU 5435  C   TYR B 280     4851  11050   5433  -1509    127   -579       C  
ATOM   5436  O   TYR B 280      51.368  14.334-113.199  1.00 41.13           O  
ANISOU 5436  O   TYR B 280     2994   9025   3607  -1518    168   -476       O  
ATOM   5437  CB  TYR B 280      52.398  16.001-115.847  1.00 44.41           C  
ANISOU 5437  CB  TYR B 280     3371   9700   3805  -1207    153   -589       C  
ATOM   5438  CG  TYR B 280      53.599  16.349-116.693  1.00 43.42           C  
ANISOU 5438  CG  TYR B 280     3312   9552   3632  -1080    167   -638       C  
ATOM   5439  CD1 TYR B 280      54.813  15.694-116.524  1.00 45.61           C  
ANISOU 5439  CD1 TYR B 280     3720   9612   3997  -1053    192   -708       C  
ATOM   5440  CD2 TYR B 280      53.519  17.343-117.659  1.00 44.21           C  
ANISOU 5440  CD2 TYR B 280     3336   9862   3598   -988    153   -605       C  
ATOM   5441  CE1 TYR B 280      55.915  16.018-117.301  1.00 38.92           C  
ANISOU 5441  CE1 TYR B 280     2912   8781   3096   -941    214   -756       C  
ATOM   5442  CE2 TYR B 280      54.609  17.673-118.437  1.00 47.94           C  
ANISOU 5442  CE2 TYR B 280     3858  10347   4010   -893    170   -634       C  
ATOM   5443  CZ  TYR B 280      55.806  17.010-118.256  1.00 45.94           C  
ANISOU 5443  CZ  TYR B 280     3720   9899   3836   -871    208   -716       C  
ATOM   5444  OH  TYR B 280      56.885  17.349-119.043  1.00 41.19           O  
ANISOU 5444  OH  TYR B 280     3144   9346   3161   -781    234   -748       O  
ATOM   5445  N   GLN B 281      49.936  14.277-114.943  1.00 53.90           N  
ANISOU 5445  N   GLN B 281     4432  10973   5076  -1618     81   -612       N  
ATOM   5446  CA  GLN B 281      48.762  14.125-114.088  1.00 53.66           C  
ANISOU 5446  CA  GLN B 281     4289  11043   5056  -1755     85   -529       C  
ATOM   5447  C   GLN B 281      48.883  12.900-113.192  1.00 56.18           C  
ANISOU 5447  C   GLN B 281     4710  11137   5500  -1935     76   -515       C  
ATOM   5448  O   GLN B 281      48.531  12.950-112.007  1.00 53.80           O  
ANISOU 5448  O   GLN B 281     4376  10840   5225  -1992    118   -391       O  
ATOM   5449  CB  GLN B 281      47.496  14.037-114.944  1.00 55.97           C  
ANISOU 5449  CB  GLN B 281     4456  11552   5257  -1844     25   -585       C  
ATOM   5450  CG  GLN B 281      47.165  15.294-115.737  1.00 56.66           C  
ANISOU 5450  CG  GLN B 281     4497  11811   5220  -1644     22   -554       C  
ATOM   5451  CD  GLN B 281      46.551  16.388-114.890  1.00 62.96           C  
ANISOU 5451  CD  GLN B 281     5273  12652   5999  -1498     64   -416       C  
ATOM   5452  OE1 GLN B 281      46.334  16.216-113.689  1.00 71.49           O  
ANISOU 5452  OE1 GLN B 281     6368  13658   7136  -1541    105   -349       O  
ATOM   5453  NE2 GLN B 281      46.263  17.523-115.513  1.00 56.18           N  
ANISOU 5453  NE2 GLN B 281     4377  11913   5057  -1328     45   -378       N  
ATOM   5454  N   ASP B 282      49.377  11.786-113.740  1.00 55.94           N  
ANISOU 5454  N   ASP B 282     4799  10909   5546  -2026     15   -641       N  
ATOM   5455  CA  ASP B 282      49.562  10.591-112.924  1.00 59.38           C  
ANISOU 5455  CA  ASP B 282     5349  11087   6124  -2193    -17   -616       C  
ATOM   5456  C   ASP B 282      50.636  10.793-111.864  1.00 58.22           C  
ANISOU 5456  C   ASP B 282     5323  10741   6056  -2080     39   -504       C  
ATOM   5457  O   ASP B 282      50.540  10.219-110.774  1.00 62.89           O  
ANISOU 5457  O   ASP B 282     5961  11208   6728  -2208     35   -391       O  
ATOM   5458  CB  ASP B 282      49.906   9.388-113.804  1.00 62.64           C  
ANISOU 5458  CB  ASP B 282     5871  11306   6622  -2287   -109   -802       C  
ATOM   5459  CG  ASP B 282      48.709   8.872-114.576  1.00 74.64           C  
ANISOU 5459  CG  ASP B 282     7285  12985   8092  -2478   -185   -901       C  
ATOM   5460  OD1 ASP B 282      47.589   9.373-114.341  1.00 78.42           O  
ANISOU 5460  OD1 ASP B 282     7597  13719   8480  -2551   -167   -807       O  
ATOM   5461  OD2 ASP B 282      48.883   7.955-115.410  1.00 80.32           O  
ANISOU 5461  OD2 ASP B 282     8079  13576   8863  -2554   -267  -1083       O  
ATOM   5462  N   PHE B 283      51.661  11.598-112.154  1.00 56.27           N  
ANISOU 5462  N   PHE B 283     5125  10475   5781  -1856     85   -522       N  
ATOM   5463  CA  PHE B 283      52.685  11.879-111.150  1.00 54.23           C  
ANISOU 5463  CA  PHE B 283     4967  10051   5587  -1746    134   -415       C  
ATOM   5464  C   PHE B 283      52.103  12.650-109.972  1.00 50.13           C  
ANISOU 5464  C   PHE B 283     4362   9673   5014  -1749    198   -248       C  
ATOM   5465  O   PHE B 283      52.306  12.279-108.810  1.00 49.34           O  
ANISOU 5465  O   PHE B 283     4322   9450   4974  -1818    210   -136       O  
ATOM   5466  CB  PHE B 283      53.841  12.664-111.771  1.00 48.73           C  
ANISOU 5466  CB  PHE B 283     4316   9339   4860  -1520    170   -468       C  
ATOM   5467  CG  PHE B 283      54.719  11.848-112.669  1.00 43.94           C  
ANISOU 5467  CG  PHE B 283     3811   8566   4319  -1493    124   -633       C  
ATOM   5468  CD1 PHE B 283      54.691  10.465-112.622  1.00 44.59           C  
ANISOU 5468  CD1 PHE B 283     3979   8435   4528  -1639     50   -714       C  
ATOM   5469  CD2 PHE B 283      55.584  12.469-113.555  1.00 45.31           C  
ANISOU 5469  CD2 PHE B 283     3989   8797   4429  -1323    153   -711       C  
ATOM   5470  CE1 PHE B 283      55.505   9.713-113.449  1.00 51.20           C  
ANISOU 5470  CE1 PHE B 283     4905   9116   5435  -1592      6   -897       C  
ATOM   5471  CE2 PHE B 283      56.402  11.723-114.387  1.00 51.14           C  
ANISOU 5471  CE2 PHE B 283     4803   9415   5214  -1287    122   -886       C  
ATOM   5472  CZ  PHE B 283      56.363  10.343-114.333  1.00 53.91           C  
ANISOU 5472  CZ  PHE B 283     5238   9549   5699  -1411     49   -993       C  
ATOM   5473  N   VAL B 284      51.388  13.742-110.259  1.00 45.70           N  
ANISOU 5473  N   VAL B 284     3655   9374   4333  -1665    236   -232       N  
ATOM   5474  CA  VAL B 284      50.800  14.567-109.206  1.00 50.44           C  
ANISOU 5474  CA  VAL B 284     4155  10133   4875  -1637    299   -110       C  
ATOM   5475  C   VAL B 284      49.857  13.738-108.347  1.00 56.40           C  
ANISOU 5475  C   VAL B 284     4855  10932   5643  -1868    294    -39       C  
ATOM   5476  O   VAL B 284      49.804  13.892-107.120  1.00 62.35           O  
ANISOU 5476  O   VAL B 284     5623  11680   6388  -1881    338     73       O  
ATOM   5477  CB  VAL B 284      50.089  15.786-109.826  1.00 47.70           C  
ANISOU 5477  CB  VAL B 284     3702   9998   4423  -1482    303   -129       C  
ATOM   5478  CG1 VAL B 284      49.197  16.492-108.800  1.00 50.87           C  
ANISOU 5478  CG1 VAL B 284     4083  10468   4779  -1418    323    -47       C  
ATOM   5479  CG2 VAL B 284      51.116  16.751-110.419  1.00 39.80           C  
ANISOU 5479  CG2 VAL B 284     2754   8958   3410  -1268    315   -147       C  
ATOM   5480  N   ARG B 285      49.121  12.825-108.974  1.00 59.09           N  
ANISOU 5480  N   ARG B 285     5157  11296   5999  -2052    229   -103       N  
ATOM   5481  CA  ARG B 285      48.165  12.014-108.235  1.00 62.93           C  
ANISOU 5481  CA  ARG B 285     5585  11832   6495  -2299    215    -23       C  
ATOM   5482  C   ARG B 285      48.858  10.944-107.399  1.00 62.34           C  
ANISOU 5482  C   ARG B 285     5672  11475   6540  -2437    183     58       C  
ATOM   5483  O   ARG B 285      48.383  10.611-106.307  1.00 62.11           O  
ANISOU 5483  O   ARG B 285     5609  11491   6500  -2597    203    195       O  
ATOM   5484  CB  ARG B 285      47.181  11.384-109.216  1.00 66.66           C  
ANISOU 5484  CB  ARG B 285     5983  12390   6952  -2449    141   -120       C  
ATOM   5485  CG  ARG B 285      45.837  11.007-108.637  1.00 76.35           C  
ANISOU 5485  CG  ARG B 285     7152  13722   8135  -2602    135    -40       C  
ATOM   5486  CD  ARG B 285      45.182  10.023-109.577  1.00 83.08           C  
ANISOU 5486  CD  ARG B 285     7971  14575   9022  -2810     42   -137       C  
ATOM   5487  NE  ARG B 285      46.125   8.955-109.898  1.00 86.22           N  
ANISOU 5487  NE  ARG B 285     8469  14729   9563  -2967    -38   -211       N  
ATOM   5488  CZ  ARG B 285      46.174   8.312-111.061  1.00 86.83           C  
ANISOU 5488  CZ  ARG B 285     8596  14712   9685  -3019   -129   -379       C  
ATOM   5489  NH1 ARG B 285      47.074   7.356-111.246  1.00 85.03           N  
ANISOU 5489  NH1 ARG B 285     8565  14142   9600  -3047   -200   -455       N  
ATOM   5490  NH2 ARG B 285      45.334   8.626-112.038  1.00 85.90           N  
ANISOU 5490  NH2 ARG B 285     8348  14822   9466  -3012   -152   -476       N  
ATOM   5491  N   ASP B 286      49.983  10.408-107.877  1.00 59.59           N  
ANISOU 5491  N   ASP B 286     5497  10840   6303  -2369    130    -18       N  
ATOM   5492  CA  ASP B 286      50.646   9.295-107.207  1.00 64.36           C  
ANISOU 5492  CA  ASP B 286     6267  11137   7049  -2488     71     51       C  
ATOM   5493  C   ASP B 286      51.774   9.718-106.274  1.00 58.47           C  
ANISOU 5493  C   ASP B 286     5625  10261   6329  -2338    116    153       C  
ATOM   5494  O   ASP B 286      52.195   8.913-105.437  1.00 59.76           O  
ANISOU 5494  O   ASP B 286     5902  10215   6590  -2446     70    263       O  
ATOM   5495  CB  ASP B 286      51.201   8.306-108.242  1.00 69.29           C  
ANISOU 5495  CB  ASP B 286     7018  11504   7804  -2505    -30   -112       C  
ATOM   5496  CG  ASP B 286      50.115   7.718-109.130  1.00 79.92           C  
ANISOU 5496  CG  ASP B 286     8280  12949   9137  -2686    -96   -222       C  
ATOM   5497  OD1 ASP B 286      50.452   7.187-110.211  1.00 83.09           O  
ANISOU 5497  OD1 ASP B 286     8748  13224   9598  -2662   -163   -406       O  
ATOM   5498  OD2 ASP B 286      48.925   7.797-108.755  1.00 82.31           O  
ANISOU 5498  OD2 ASP B 286     8440  13474   9361  -2852    -79   -135       O  
ATOM   5499  N   TYR B 287      52.269  10.942-106.391  1.00 47.17           N  
ANISOU 5499  N   TYR B 287     4160   8944   4819  -2105    191    128       N  
ATOM   5500  CA  TYR B 287      53.383  11.416-105.587  1.00 43.58           C  
ANISOU 5500  CA  TYR B 287     3798   8376   4385  -1958    228    208       C  
ATOM   5501  C   TYR B 287      53.090  12.833-105.121  1.00 43.10           C  
ANISOU 5501  C   TYR B 287     3622   8568   4188  -1822    324    254       C  
ATOM   5502  O   TYR B 287      52.295  13.545-105.744  1.00 47.54           O  
ANISOU 5502  O   TYR B 287     4049   9353   4661  -1773    354    191       O  
ATOM   5503  CB  TYR B 287      54.696  11.380-106.383  1.00 52.20           C  
ANISOU 5503  CB  TYR B 287     5007   9263   5562  -1782    200     95       C  
ATOM   5504  CG  TYR B 287      55.033  10.002-106.898  1.00 56.30           C  
ANISOU 5504  CG  TYR B 287     5640   9521   6229  -1882    100     11       C  
ATOM   5505  CD1 TYR B 287      54.644   9.602-108.167  1.00 58.51           C  
ANISOU 5505  CD1 TYR B 287     5892   9823   6515  -1913     57   -159       C  
ATOM   5506  CD2 TYR B 287      55.724   9.095-106.109  1.00 58.74           C  
ANISOU 5506  CD2 TYR B 287     6084   9559   6676  -1943     38     96       C  
ATOM   5507  CE1 TYR B 287      54.941   8.345-108.641  1.00 59.59           C  
ANISOU 5507  CE1 TYR B 287     6135   9711   6796  -1996    -40   -265       C  
ATOM   5508  CE2 TYR B 287      56.027   7.832-106.577  1.00 61.33           C  
ANISOU 5508  CE2 TYR B 287     6520   9619   7164  -2019    -68      8       C  
ATOM   5509  CZ  TYR B 287      55.630   7.464-107.844  1.00 62.56           C  
ANISOU 5509  CZ  TYR B 287     6648   9793   7328  -2043   -105   -185       C  
ATOM   5510  OH  TYR B 287      55.923   6.209-108.325  1.00 68.73           O  
ANISOU 5510  OH  TYR B 287     7540  10298   8276  -2111   -216   -304       O  
ATOM   5511  N   PRO B 288      53.736  13.288-103.983  1.00 44.41           N  
ANISOU 5511  N   PRO B 288     3837   8698   4338  -1752    366    361       N  
ATOM   5512  CA  PRO B 288      53.543  14.674-103.514  1.00 40.95           C  
ANISOU 5512  CA  PRO B 288     3303   8472   3786  -1605    449    379       C  
ATOM   5513  C   PRO B 288      54.293  15.696-104.366  1.00 41.95           C  
ANISOU 5513  C   PRO B 288     3447   8581   3913  -1371    461    289       C  
ATOM   5514  O   PRO B 288      55.130  16.459-103.877  1.00 42.31           O  
ANISOU 5514  O   PRO B 288     3542   8580   3954  -1230    489    318       O  
ATOM   5515  CB  PRO B 288      54.070  14.605-102.075  1.00 38.09           C  
ANISOU 5515  CB  PRO B 288     3009   8049   3413  -1637    469    510       C  
ATOM   5516  CG  PRO B 288      55.107  13.535-102.114  1.00 38.89           C  
ANISOU 5516  CG  PRO B 288     3277   7845   3653  -1684    391    540       C  
ATOM   5517  CD  PRO B 288      54.558  12.497-103.049  1.00 43.58           C  
ANISOU 5517  CD  PRO B 288     3871   8365   4320  -1823    325    472       C  
ATOM   5518  N   VAL B 289      53.991  15.716-105.663  1.00 49.58           N  
ANISOU 5518  N   VAL B 289     4368   9593   4878  -1342    434    183       N  
ATOM   5519  CA  VAL B 289      54.592  16.669-106.594  1.00 41.89           C  
ANISOU 5519  CA  VAL B 289     3396   8634   3886  -1148    440    115       C  
ATOM   5520  C   VAL B 289      53.785  17.959-106.549  1.00 41.39           C  
ANISOU 5520  C   VAL B 289     3253   8731   3744  -1020    450    119       C  
ATOM   5521  O   VAL B 289      52.601  17.973-106.897  1.00 47.53           O  
ANISOU 5521  O   VAL B 289     3946   9638   4474  -1063    424     89       O  
ATOM   5522  CB  VAL B 289      54.642  16.103-108.022  1.00 42.97           C  
ANISOU 5522  CB  VAL B 289     3543   8739   4043  -1168    389     -1       C  
ATOM   5523  CG1 VAL B 289      55.107  17.173-109.012  1.00 34.79           C  
ANISOU 5523  CG1 VAL B 289     2484   7778   2956   -989    397    -47       C  
ATOM   5524  CG2 VAL B 289      55.544  14.881-108.080  1.00 36.22           C  
ANISOU 5524  CG2 VAL B 289     2828   7630   3304  -1232    343    -39       C  
ATOM   5525  N   VAL B 290      54.425  19.048-106.127  1.00 41.31           N  
ANISOU 5525  N   VAL B 290     3303   8654   3740   -847    456    147       N  
ATOM   5526  CA  VAL B 290      53.748  20.330-105.959  1.00 34.34           C  
ANISOU 5526  CA  VAL B 290     2385   7842   2820   -706    435    143       C  
ATOM   5527  C   VAL B 290      54.228  21.382-106.941  1.00 34.96           C  
ANISOU 5527  C   VAL B 290     2475   7906   2901   -546    405    123       C  
ATOM   5528  O   VAL B 290      53.637  22.474-106.993  1.00 33.11           O  
ANISOU 5528  O   VAL B 290     2195   7741   2643   -431    382    122       O  
ATOM   5529  CB  VAL B 290      53.895  20.861-104.517  1.00 35.19           C  
ANISOU 5529  CB  VAL B 290     2530   7910   2930   -657    460    188       C  
ATOM   5530  CG1 VAL B 290      53.370  19.845-103.511  1.00 34.62           C  
ANISOU 5530  CG1 VAL B 290     2442   7875   2835   -830    484    230       C  
ATOM   5531  CG2 VAL B 290      55.348  21.211-104.224  1.00 35.33           C  
ANISOU 5531  CG2 VAL B 290     2650   7778   2996   -575    472    219       C  
ATOM   5532  N   SER B 291      55.275  21.102-107.712  1.00 32.31           N  
ANISOU 5532  N   SER B 291     2190   7498   2588   -537    407    112       N  
ATOM   5533  CA  SER B 291      55.857  22.094-108.601  1.00 40.64           C  
ANISOU 5533  CA  SER B 291     3261   8543   3636   -404    379    117       C  
ATOM   5534  C   SER B 291      56.492  21.381-109.780  1.00 31.73           C  
ANISOU 5534  C   SER B 291     2139   7424   2493   -451    380     67       C  
ATOM   5535  O   SER B 291      57.147  20.348-109.611  1.00 36.25           O  
ANISOU 5535  O   SER B 291     2743   7932   3098   -534    417     38       O  
ATOM   5536  CB  SER B 291      56.898  22.952-107.876  1.00 30.60           C  
ANISOU 5536  CB  SER B 291     2069   7147   2412   -296    391    170       C  
ATOM   5537  OG  SER B 291      57.162  24.142-108.591  1.00 42.72           O  
ANISOU 5537  OG  SER B 291     3595   8702   3934   -175    358    200       O  
ATOM   5538  N   ILE B 292      56.285  21.934-110.973  1.00 32.02           N  
ANISOU 5538  N   ILE B 292     2132   7562   2472   -399    340     55       N  
ATOM   5539  CA  ILE B 292      56.862  21.403-112.201  1.00 40.21           C  
ANISOU 5539  CA  ILE B 292     3164   8647   3467   -431    340     -7       C  
ATOM   5540  C   ILE B 292      57.393  22.572-113.014  1.00 36.67           C  
ANISOU 5540  C   ILE B 292     2726   8231   2978   -316    305     52       C  
ATOM   5541  O   ILE B 292      56.632  23.477-113.378  1.00 35.72           O  
ANISOU 5541  O   ILE B 292     2545   8216   2812   -261    260    104       O  
ATOM   5542  CB  ILE B 292      55.849  20.592-113.025  1.00 40.98           C  
ANISOU 5542  CB  ILE B 292     3168   8907   3498   -546    322    -93       C  
ATOM   5543  CG1 ILE B 292      55.533  19.279-112.310  1.00 34.14           C  
ANISOU 5543  CG1 ILE B 292     2288   7999   2683   -698    357   -147       C  
ATOM   5544  CG2 ILE B 292      56.398  20.320-114.415  1.00 34.10           C  
ANISOU 5544  CG2 ILE B 292     2278   8127   2550   -554    316   -171       C  
ATOM   5545  CD1 ILE B 292      54.572  18.398-113.054  1.00 35.58           C  
ANISOU 5545  CD1 ILE B 292     2406   8285   2827   -833    315   -242       C  
ATOM   5546  N   GLU B 293      58.691  22.558-113.289  1.00 35.93           N  
ANISOU 5546  N   GLU B 293     2694   8058   2898   -285    327     53       N  
ATOM   5547  CA  GLU B 293      59.348  23.574-114.094  1.00 32.56           C  
ANISOU 5547  CA  GLU B 293     2274   7670   2428   -206    297    123       C  
ATOM   5548  C   GLU B 293      59.547  23.045-115.508  1.00 32.28           C  
ANISOU 5548  C   GLU B 293     2202   7771   2293   -253    290     47       C  
ATOM   5549  O   GLU B 293      59.875  21.870-115.696  1.00 37.09           O  
ANISOU 5549  O   GLU B 293     2819   8373   2900   -317    330    -77       O  
ATOM   5550  CB  GLU B 293      60.694  23.964-113.469  1.00 37.37           C  
ANISOU 5550  CB  GLU B 293     2967   8123   3110   -150    324    176       C  
ATOM   5551  CG  GLU B 293      61.655  24.673-114.416  1.00 55.52           C  
ANISOU 5551  CG  GLU B 293     5270  10464   5360   -111    307    234       C  
ATOM   5552  CD  GLU B 293      63.010  24.953-113.784  1.00 61.32           C  
ANISOU 5552  CD  GLU B 293     6074  11058   6167    -73    334    279       C  
ATOM   5553  OE1 GLU B 293      63.050  25.387-112.614  1.00 62.56           O  
ANISOU 5553  OE1 GLU B 293     6267  11106   6399    -39    341    329       O  
ATOM   5554  OE2 GLU B 293      64.036  24.730-114.459  1.00 63.47           O  
ANISOU 5554  OE2 GLU B 293     6356  11346   6415    -79    348    256       O  
ATOM   5555  N   ASP B 294      59.337  23.916-116.492  1.00 43.41           N  
ANISOU 5555  N   ASP B 294     3559   9323   3612   -223    240    117       N  
ATOM   5556  CA  ASP B 294      59.451  23.580-117.908  1.00 36.23           C  
ANISOU 5556  CA  ASP B 294     2601   8583   2581   -268    222     57       C  
ATOM   5557  C   ASP B 294      58.769  22.260-118.274  1.00 38.56           C  
ANISOU 5557  C   ASP B 294     2853   8970   2827   -367    239   -111       C  
ATOM   5558  O   ASP B 294      59.419  21.338-118.779  1.00 36.93           O  
ANISOU 5558  O   ASP B 294     2663   8776   2591   -408    277   -246       O  
ATOM   5559  CB  ASP B 294      60.912  23.557-118.337  1.00 33.89           C  
ANISOU 5559  CB  ASP B 294     2357   8237   2283   -249    249     46       C  
ATOM   5560  CG  ASP B 294      61.472  24.943-118.587  1.00 43.25           C  
ANISOU 5560  CG  ASP B 294     3542   9437   3455   -191    215    219       C  
ATOM   5561  OD1 ASP B 294      60.679  25.905-118.673  1.00 34.00           O  
ANISOU 5561  OD1 ASP B 294     2317   8350   2251   -163    166    342       O  
ATOM   5562  OD2 ASP B 294      62.709  25.069-118.712  1.00 50.25           O  
ANISOU 5562  OD2 ASP B 294     4468  10265   4359   -178    239    236       O  
ATOM   5563  N   PRO B 295      57.460  22.134-118.042  1.00 41.61           N  
ANISOU 5563  N   PRO B 295     3172   9435   3202   -410    215   -117       N  
ATOM   5564  CA  PRO B 295      56.779  20.893-118.442  1.00 40.65           C  
ANISOU 5564  CA  PRO B 295     2991   9424   3028   -531    229   -276       C  
ATOM   5565  C   PRO B 295      56.790  20.663-119.942  1.00 46.60           C  
ANISOU 5565  C   PRO B 295     3692  10391   3623   -573    202   -364       C  
ATOM   5566  O   PRO B 295      56.736  19.508-120.385  1.00 44.02           O  
ANISOU 5566  O   PRO B 295     3371  10085   3270   -661    208   -541       O  
ATOM   5567  CB  PRO B 295      55.354  21.091-117.906  1.00 40.25           C  
ANISOU 5567  CB  PRO B 295     2864   9430   3000   -561    191   -227       C  
ATOM   5568  CG  PRO B 295      55.182  22.572-117.854  1.00 36.26           C  
ANISOU 5568  CG  PRO B 295     2351   8941   2486   -438    143    -62       C  
ATOM   5569  CD  PRO B 295      56.522  23.104-117.445  1.00 39.79           C  
ANISOU 5569  CD  PRO B 295     2902   9216   3002   -354    174      6       C  
ATOM   5570  N   PHE B 296      56.873  21.727-120.739  1.00 38.11           N  
ANISOU 5570  N   PHE B 296     2583   9428   2468   -515    145   -245       N  
ATOM   5571  CA  PHE B 296      56.805  21.615-122.184  1.00 39.64           C  
ANISOU 5571  CA  PHE B 296     2711   9832   2520   -560    106   -303       C  
ATOM   5572  C   PHE B 296      57.861  22.517-122.803  1.00 43.71           C  
ANISOU 5572  C   PHE B 296     3244  10342   3021   -493     97   -186       C  
ATOM   5573  O   PHE B 296      58.515  23.308-122.119  1.00 38.43           O  
ANISOU 5573  O   PHE B 296     2635   9529   2438   -416    107    -55       O  
ATOM   5574  CB  PHE B 296      55.402  21.956-122.701  1.00 40.75           C  
ANISOU 5574  CB  PHE B 296     2726  10184   2572   -599     41   -254       C  
ATOM   5575  CG  PHE B 296      54.324  21.144-122.059  1.00 40.93           C  
ANISOU 5575  CG  PHE B 296     2716  10238   2596   -682     41   -353       C  
ATOM   5576  CD1 PHE B 296      54.079  19.844-122.471  1.00 45.84           C  
ANISOU 5576  CD1 PHE B 296     3343  10883   3192   -803     35   -558       C  
ATOM   5577  CD2 PHE B 296      53.571  21.668-121.022  1.00 46.77           C  
ANISOU 5577  CD2 PHE B 296     3422  10903   3446   -638     31   -244       C  
ATOM   5578  CE1 PHE B 296      53.089  19.087-121.867  1.00 42.38           C  
ANISOU 5578  CE1 PHE B 296     2876  10387   2841   -899     14   -627       C  
ATOM   5579  CE2 PHE B 296      52.586  20.916-120.416  1.00 40.55           C  
ANISOU 5579  CE2 PHE B 296     2608  10071   2727   -724     24   -318       C  
ATOM   5580  CZ  PHE B 296      52.344  19.625-120.839  1.00 41.63           C  
ANISOU 5580  CZ  PHE B 296     2733  10245   2841   -868     12   -498       C  
ATOM   5581  N   ASP B 297      58.021  22.386-124.117  1.00 49.38           N  
ANISOU 5581  N   ASP B 297     3905  11228   3627   -536     83   -237       N  
ATOM   5582  CA  ASP B 297      59.078  23.085-124.829  1.00 44.91           C  
ANISOU 5582  CA  ASP B 297     3342  10691   3029   -504     85   -143       C  
ATOM   5583  C   ASP B 297      58.934  24.600-124.688  1.00 43.13           C  
ANISOU 5583  C   ASP B 297     3094  10466   2827   -445     42    116       C  
ATOM   5584  O   ASP B 297      57.848  25.135-124.444  1.00 47.41           O  
ANISOU 5584  O   ASP B 297     3585  11053   3375   -427      6    213       O  
ATOM   5585  CB  ASP B 297      59.073  22.689-126.306  1.00 43.53           C  
ANISOU 5585  CB  ASP B 297     3092  10733   2714   -572     79   -240       C  
ATOM   5586  CG  ASP B 297      60.208  23.322-127.075  1.00 44.20           C  
ANISOU 5586  CG  ASP B 297     3168  10877   2748   -559     88   -152       C  
ATOM   5587  OD1 ASP B 297      59.951  24.282-127.828  1.00 45.18           O  
ANISOU 5587  OD1 ASP B 297     3225  11139   2802   -574     49     19       O  
ATOM   5588  OD2 ASP B 297      61.363  22.873-126.904  1.00 47.27           O  
ANISOU 5588  OD2 ASP B 297     3613  11178   3169   -535    138   -246       O  
ATOM   5589  N   GLN B 298      60.065  25.288-124.859  1.00 42.36           N  
ANISOU 5589  N   GLN B 298     3030  10322   2743   -417     53    223       N  
ATOM   5590  CA  GLN B 298      60.144  26.733-124.684  1.00 45.37           C  
ANISOU 5590  CA  GLN B 298     3408  10675   3158   -369     19    469       C  
ATOM   5591  C   GLN B 298      59.204  27.504-125.611  1.00 47.68           C  
ANISOU 5591  C   GLN B 298     3612  11141   3363   -391    -32    609       C  
ATOM   5592  O   GLN B 298      58.872  28.658-125.317  1.00 48.97           O  
ANISOU 5592  O   GLN B 298     3786  11254   3568   -338    -69    806       O  
ATOM   5593  CB  GLN B 298      61.604  27.158-124.875  1.00 46.97           C  
ANISOU 5593  CB  GLN B 298     3652  10825   3370   -370     43    535       C  
ATOM   5594  CG  GLN B 298      61.845  28.393-125.708  1.00 60.95           C  
ANISOU 5594  CG  GLN B 298     5377  12700   5083   -397      5    756       C  
ATOM   5595  CD  GLN B 298      63.297  28.525-126.115  1.00 70.71           C  
ANISOU 5595  CD  GLN B 298     6625  13945   6295   -432     33    775       C  
ATOM   5596  OE1 GLN B 298      63.657  29.411-126.889  1.00 80.65           O  
ANISOU 5596  OE1 GLN B 298     7844  15304   7494   -481      7    944       O  
ATOM   5597  NE2 GLN B 298      64.141  27.636-125.598  1.00 61.65           N  
ANISOU 5597  NE2 GLN B 298     5535  12695   5194   -411     88    607       N  
ATOM   5598  N   ASP B 299      58.739  26.896-126.703  1.00 43.83           N  
ANISOU 5598  N   ASP B 299     3053  10842   2758   -462    -38    511       N  
ATOM   5599  CA  ASP B 299      57.801  27.568-127.596  1.00 51.62           C  
ANISOU 5599  CA  ASP B 299     3971  11986   3657   -484    -90    643       C  
ATOM   5600  C   ASP B 299      56.498  26.799-127.805  1.00 46.16           C  
ANISOU 5600  C   ASP B 299     3222  11404   2914   -516   -103    513       C  
ATOM   5601  O   ASP B 299      55.724  27.152-128.701  1.00 60.18           O  
ANISOU 5601  O   ASP B 299     4940  13330   4597   -546   -149    590       O  
ATOM   5602  CB  ASP B 299      58.468  27.857-128.944  1.00 50.34           C  
ANISOU 5602  CB  ASP B 299     3765  11989   3372   -556    -98    706       C  
ATOM   5603  CG  ASP B 299      59.437  29.023-128.867  1.00 57.18           C  
ANISOU 5603  CG  ASP B 299     4674  12773   4280   -539   -111    920       C  
ATOM   5604  OD1 ASP B 299      60.537  28.937-129.451  1.00 51.97           O  
ANISOU 5604  OD1 ASP B 299     4003  12180   3565   -591    -84    904       O  
ATOM   5605  OD2 ASP B 299      59.093  30.030-128.212  1.00 64.21           O  
ANISOU 5605  OD2 ASP B 299     5609  13529   5257   -475   -153   1100       O  
ATOM   5606  N   ASP B 300      56.222  25.775-126.997  1.00 46.80           N  
ANISOU 5606  N   ASP B 300     3321  11411   3050   -520    -71    330       N  
ATOM   5607  CA  ASP B 300      54.954  25.047-127.083  1.00 45.78           C  
ANISOU 5607  CA  ASP B 300     3140  11375   2881   -567    -85    211       C  
ATOM   5608  C   ASP B 300      53.931  25.705-126.158  1.00 45.11           C  
ANISOU 5608  C   ASP B 300     3054  11214   2870   -491   -115    326       C  
ATOM   5609  O   ASP B 300      53.472  25.138-125.168  1.00 48.83           O  
ANISOU 5609  O   ASP B 300     3540  11608   3407   -489    -95    232       O  
ATOM   5610  CB  ASP B 300      55.157  23.579-126.738  1.00 45.36           C  
ANISOU 5610  CB  ASP B 300     3113  11279   2842   -631    -45    -44       C  
ATOM   5611  CG  ASP B 300      53.974  22.714-127.128  1.00 46.63           C  
ANISOU 5611  CG  ASP B 300     3218  11564   2935   -718    -62   -186       C  
ATOM   5612  OD1 ASP B 300      52.962  23.241-127.650  1.00 47.79           O  
ANISOU 5612  OD1 ASP B 300     3301  11833   3023   -721   -107    -86       O  
ATOM   5613  OD2 ASP B 300      54.060  21.491-126.904  1.00 54.39           O  
ANISOU 5613  OD2 ASP B 300     4231  12508   3928   -786    -39   -399       O  
ATOM   5614  N   TRP B 301      53.568  26.937-126.520  1.00 45.89           N  
ANISOU 5614  N   TRP B 301     3141  11334   2960   -430   -173    533       N  
ATOM   5615  CA  TRP B 301      52.699  27.744-125.670  1.00 48.48           C  
ANISOU 5615  CA  TRP B 301     3477  11562   3381   -326   -221    646       C  
ATOM   5616  C   TRP B 301      51.356  27.068-125.421  1.00 47.31           C  
ANISOU 5616  C   TRP B 301     3269  11480   3226   -351   -236    530       C  
ATOM   5617  O   TRP B 301      50.795  27.181-124.326  1.00 47.06           O  
ANISOU 5617  O   TRP B 301     3244  11342   3293   -286   -238    521       O  
ATOM   5618  CB  TRP B 301      52.491  29.119-126.300  1.00 49.07           C  
ANISOU 5618  CB  TRP B 301     3547  11646   3454   -262   -311    874       C  
ATOM   5619  CG  TRP B 301      53.731  29.944-126.341  1.00 49.49           C  
ANISOU 5619  CG  TRP B 301     3667  11598   3539   -239   -310   1017       C  
ATOM   5620  CD1 TRP B 301      54.645  30.004-127.355  1.00 48.41           C  
ANISOU 5620  CD1 TRP B 301     3529  11555   3310   -320   -295   1065       C  
ATOM   5621  CD2 TRP B 301      54.203  30.829-125.321  1.00 45.16           C  
ANISOU 5621  CD2 TRP B 301     3193  10840   3125   -138   -328   1128       C  
ATOM   5622  NE1 TRP B 301      55.655  30.875-127.030  1.00 48.00           N  
ANISOU 5622  NE1 TRP B 301     3546  11364   3327   -285   -301   1210       N  
ATOM   5623  CE2 TRP B 301      55.408  31.395-125.785  1.00 56.37           C  
ANISOU 5623  CE2 TRP B 301     4660  12230   4528   -174   -324   1251       C  
ATOM   5624  CE3 TRP B 301      53.725  31.199-124.061  1.00 44.65           C  
ANISOU 5624  CE3 TRP B 301     3153  10615   3199    -24   -348   1126       C  
ATOM   5625  CZ2 TRP B 301      56.140  32.311-125.029  1.00 51.66           C  
ANISOU 5625  CZ2 TRP B 301     4144  11439   4047   -106   -346   1378       C  
ATOM   5626  CZ3 TRP B 301      54.453  32.108-123.314  1.00 45.80           C  
ANISOU 5626  CZ3 TRP B 301     3373  10569   3461     56   -371   1238       C  
ATOM   5627  CH2 TRP B 301      55.645  32.654-123.800  1.00 49.32           C  
ANISOU 5627  CH2 TRP B 301     3876  10978   3886     11   -374   1367       C  
ATOM   5628  N   ALA B 302      50.819  26.369-126.424  1.00 52.08           N  
ANISOU 5628  N   ALA B 302     3811  12262   3717   -451   -247    437       N  
ATOM   5629  CA  ALA B 302      49.505  25.754-126.264  1.00 50.10           C  
ANISOU 5629  CA  ALA B 302     3496  12081   3456   -491   -270    339       C  
ATOM   5630  C   ALA B 302      49.529  24.670-125.198  1.00 46.96           C  
ANISOU 5630  C   ALA B 302     3130  11590   3122   -545   -211    168       C  
ATOM   5631  O   ALA B 302      48.580  24.536-124.418  1.00 46.89           O  
ANISOU 5631  O   ALA B 302     3093  11546   3176   -533   -223    144       O  
ATOM   5632  CB  ALA B 302      49.015  25.184-127.595  1.00 50.31           C  
ANISOU 5632  CB  ALA B 302     3455  12316   3343   -600   -299    266       C  
ATOM   5633  N   ALA B 303      50.604  23.883-125.148  1.00 46.11           N  
ANISOU 5633  N   ALA B 303     3076  11437   3007   -607   -152     48       N  
ATOM   5634  CA  ALA B 303      50.698  22.859-124.115  1.00 45.24           C  
ANISOU 5634  CA  ALA B 303     3006  11218   2967   -665   -112   -100       C  
ATOM   5635  C   ALA B 303      50.813  23.487-122.731  1.00 45.52           C  
ANISOU 5635  C   ALA B 303     3090  11081   3125   -562    -97     -4       C  
ATOM   5636  O   ALA B 303      50.216  22.992-121.768  1.00 51.86           O  
ANISOU 5636  O   ALA B 303     3894  11806   4004   -592    -90    -62       O  
ATOM   5637  CB  ALA B 303      51.879  21.934-124.396  1.00 44.70           C  
ANISOU 5637  CB  ALA B 303     2986  11123   2877   -735    -70   -253       C  
ATOM   5638  N   TRP B 304      51.555  24.592-122.620  1.00 45.36           N  
ANISOU 5638  N   TRP B 304     3107  10991   3136   -448    -96    146       N  
ATOM   5639  CA  TRP B 304      51.716  25.270-121.336  1.00 41.53           C  
ANISOU 5639  CA  TRP B 304     2673  10330   2776   -341    -88    229       C  
ATOM   5640  C   TRP B 304      50.377  25.766-120.803  1.00 41.96           C  
ANISOU 5640  C   TRP B 304     2672  10376   2895   -277   -126    273       C  
ATOM   5641  O   TRP B 304      49.983  25.444-119.676  1.00 43.56           O  
ANISOU 5641  O   TRP B 304     2885  10481   3186   -276   -100    218       O  
ATOM   5642  CB  TRP B 304      52.687  26.441-121.477  1.00 40.71           C  
ANISOU 5642  CB  TRP B 304     2611  10160   2695   -241    -97    389       C  
ATOM   5643  CG  TRP B 304      54.136  26.083-121.467  1.00 50.45           C  
ANISOU 5643  CG  TRP B 304     3903  11348   3918   -273    -45    354       C  
ATOM   5644  CD1 TRP B 304      54.872  25.593-122.509  1.00 41.98           C  
ANISOU 5644  CD1 TRP B 304     2814  10362   2776   -348    -31    294       C  
ATOM   5645  CD2 TRP B 304      55.045  26.230-120.368  1.00 44.76           C  
ANISOU 5645  CD2 TRP B 304     3261  10458   3288   -221    -16    371       C  
ATOM   5646  NE1 TRP B 304      56.178  25.410-122.120  1.00 39.75           N  
ANISOU 5646  NE1 TRP B 304     2614   9937   2553   -337     -8    266       N  
ATOM   5647  CE2 TRP B 304      56.311  25.795-120.812  1.00 38.33           C  
ANISOU 5647  CE2 TRP B 304     2498   9591   2475   -264      4    320       C  
ATOM   5648  CE3 TRP B 304      54.907  26.678-119.049  1.00 43.60           C  
ANISOU 5648  CE3 TRP B 304     3158  10114   3292   -139     -6    407       C  
ATOM   5649  CZ2 TRP B 304      57.431  25.795-119.984  1.00 38.05           C  
ANISOU 5649  CZ2 TRP B 304     2584   9322   2549   -228     55    319       C  
ATOM   5650  CZ3 TRP B 304      56.022  26.678-118.229  1.00 35.72           C  
ANISOU 5650  CZ3 TRP B 304     2260   8919   2394   -114     47    406       C  
ATOM   5651  CH2 TRP B 304      57.267  26.242-118.700  1.00 41.79           C  
ANISOU 5651  CH2 TRP B 304     3099   9639   3140   -159     76    369       C  
ATOM   5652  N   SER B 305      49.673  26.576-121.600  1.00 45.83           N  
ANISOU 5652  N   SER B 305     3097  10966   3348   -222   -189    374       N  
ATOM   5653  CA  SER B 305      48.426  27.182-121.137  1.00 44.03           C  
ANISOU 5653  CA  SER B 305     2801  10740   3190   -134   -234    415       C  
ATOM   5654  C   SER B 305      47.381  26.123-120.819  1.00 44.62           C  
ANISOU 5654  C   SER B 305     2817  10891   3247   -237   -214    279       C  
ATOM   5655  O   SER B 305      46.666  26.225-119.814  1.00 44.57           O  
ANISOU 5655  O   SER B 305     2780  10833   3323   -192   -202    258       O  
ATOM   5656  CB  SER B 305      47.891  28.155-122.188  1.00 48.02           C  
ANISOU 5656  CB  SER B 305     3246  11342   3659    -66   -323    547       C  
ATOM   5657  OG  SER B 305      48.856  29.136-122.531  1.00 53.73           O  
ANISOU 5657  OG  SER B 305     4029  11983   4401      6   -354    693       O  
ATOM   5658  N   LYS B 306      47.278  25.097-121.668  1.00 48.03           N  
ANISOU 5658  N   LYS B 306     3228  11450   3572   -384   -210    182       N  
ATOM   5659  CA  LYS B 306      46.298  24.040-121.443  1.00 49.18           C  
ANISOU 5659  CA  LYS B 306     3318  11664   3706   -508   -203     58       C  
ATOM   5660  C   LYS B 306      46.593  23.275-120.160  1.00 51.02           C  
ANISOU 5660  C   LYS B 306     3608  11749   4029   -567   -143    -25       C  
ATOM   5661  O   LYS B 306      45.671  22.914-119.418  1.00 45.40           O  
ANISOU 5661  O   LYS B 306     2848  11038   3362   -610   -134    -61       O  
ATOM   5662  CB  LYS B 306      46.271  23.091-122.640  1.00 51.64           C  
ANISOU 5662  CB  LYS B 306     3605  12119   3899   -657   -218    -46       C  
ATOM   5663  CG  LYS B 306      45.397  21.867-122.439  1.00 55.71           C  
ANISOU 5663  CG  LYS B 306     4073  12682   4413   -816   -217   -184       C  
ATOM   5664  CD  LYS B 306      45.353  21.002-123.686  1.00 54.00           C  
ANISOU 5664  CD  LYS B 306     3832  12601   4085   -955   -244   -301       C  
ATOM   5665  CE  LYS B 306      44.474  19.781-123.470  1.00 63.19           C  
ANISOU 5665  CE  LYS B 306     4952  13790   5265  -1129   -255   -436       C  
ATOM   5666  NZ  LYS B 306      44.271  19.008-124.726  1.00 73.91           N  
ANISOU 5666  NZ  LYS B 306     6281  15283   6519  -1258   -296   -560       N  
ATOM   5667  N   PHE B 307      47.873  23.024-119.876  1.00 43.45           N  
ANISOU 5667  N   PHE B 307     2745  10666   3098   -575   -103    -47       N  
ATOM   5668  CA  PHE B 307      48.239  22.256-118.690  1.00 50.89           C  
ANISOU 5668  CA  PHE B 307     3747  11451   4139   -639    -50   -113       C  
ATOM   5669  C   PHE B 307      48.113  23.084-117.416  1.00 48.61           C  
ANISOU 5669  C   PHE B 307     3480  11034   3953   -515    -26    -30       C  
ATOM   5670  O   PHE B 307      47.687  22.564-116.379  1.00 49.66           O  
ANISOU 5670  O   PHE B 307     3615  11103   4152   -572      8    -66       O  
ATOM   5671  CB  PHE B 307      49.660  21.721-118.836  1.00 41.30           C  
ANISOU 5671  CB  PHE B 307     2616  10145   2931   -677    -18   -169       C  
ATOM   5672  CG  PHE B 307      50.088  20.818-117.716  1.00 40.43           C  
ANISOU 5672  CG  PHE B 307     2565   9861   2935   -757     37   -232       C  
ATOM   5673  CD1 PHE B 307      49.620  19.518-117.641  1.00 41.32           C  
ANISOU 5673  CD1 PHE B 307     2647   9987   3067   -933     40   -348       C  
ATOM   5674  CD2 PHE B 307      50.975  21.263-116.749  1.00 38.90           C  
ANISOU 5674  CD2 PHE B 307     2460   9483   2837   -665     83   -168       C  
ATOM   5675  CE1 PHE B 307      50.020  18.683-116.619  1.00 40.76           C  
ANISOU 5675  CE1 PHE B 307     2625   9754   3107  -1020     89   -382       C  
ATOM   5676  CE2 PHE B 307      51.376  20.433-115.726  1.00 41.29           C  
ANISOU 5676  CE2 PHE B 307     2821   9627   3240   -741    138   -207       C  
ATOM   5677  CZ  PHE B 307      50.898  19.141-115.660  1.00 42.38           C  
ANISOU 5677  CZ  PHE B 307     2919   9787   3395   -919    143   -306       C  
ATOM   5678  N   THR B 308      48.496  24.362-117.467  1.00 44.64           N  
ANISOU 5678  N   THR B 308     2994  10498   3468   -353    -43     80       N  
ATOM   5679  CA  THR B 308      48.336  25.230-116.304  1.00 40.46           C  
ANISOU 5679  CA  THR B 308     2474   9858   3040   -225    -25    135       C  
ATOM   5680  C   THR B 308      46.864  25.394-115.936  1.00 48.60           C  
ANISOU 5680  C   THR B 308     3400  10988   4078   -204    -39    119       C  
ATOM   5681  O   THR B 308      46.510  25.399-114.749  1.00 44.08           O  
ANISOU 5681  O   THR B 308     2825  10355   3569   -186      0     94       O  
ATOM   5682  CB  THR B 308      48.992  26.589-116.572  1.00 40.06           C  
ANISOU 5682  CB  THR B 308     2447   9756   3017    -64    -55    253       C  
ATOM   5683  OG1 THR B 308      50.416  26.446-116.541  1.00 46.19           O  
ANISOU 5683  OG1 THR B 308     3323  10420   3806    -81    -24    266       O  
ATOM   5684  CG2 THR B 308      48.584  27.615-115.525  1.00 42.80           C  
ANISOU 5684  CG2 THR B 308     2773  10021   3469     85    -53    288       C  
ATOM   5685  N   ALA B 309      45.987  25.508-116.939  1.00 43.35           N  
ANISOU 5685  N   ALA B 309     2641  10488   3341   -212    -93    130       N  
ATOM   5686  CA  ALA B 309      44.568  25.714-116.659  1.00 55.98           C  
ANISOU 5686  CA  ALA B 309     4124  12198   4949   -182   -111    115       C  
ATOM   5687  C   ALA B 309      43.869  24.446-116.189  1.00 45.46           C  
ANISOU 5687  C   ALA B 309     2757  10923   3592   -359    -76     21       C  
ATOM   5688  O   ALA B 309      42.749  24.528-115.676  1.00 56.95           O  
ANISOU 5688  O   ALA B 309     4116  12464   5058   -348    -73      3       O  
ATOM   5689  CB  ALA B 309      43.849  26.256-117.894  1.00 46.52           C  
ANISOU 5689  CB  ALA B 309     2831  11153   3690   -134   -189    169       C  
ATOM   5690  N   ASN B 310      44.495  23.282-116.351  1.00 44.84           N  
ANISOU 5690  N   ASN B 310     2746  10801   3489   -523    -53    -41       N  
ATOM   5691  CA  ASN B 310      43.896  22.015-115.958  1.00 48.13           C  
ANISOU 5691  CA  ASN B 310     3134  11252   3900   -714    -30   -119       C  
ATOM   5692  C   ASN B 310      44.639  21.373-114.792  1.00 48.63           C  
ANISOU 5692  C   ASN B 310     3292  11144   4041   -785     31   -137       C  
ATOM   5693  O   ASN B 310      44.623  20.150-114.634  1.00 47.59           O  
ANISOU 5693  O   ASN B 310     3173  10990   3920   -971     47   -194       O  
ATOM   5694  CB  ASN B 310      43.838  21.059-117.148  1.00 52.33           C  
ANISOU 5694  CB  ASN B 310     3647  11879   4356   -870    -65   -191       C  
ATOM   5695  CG  ASN B 310      42.795  21.466-118.170  1.00 63.56           C  
ANISOU 5695  CG  ASN B 310     4956  13498   5697   -843   -126   -176       C  
ATOM   5696  OD1 ASN B 310      41.757  22.041-117.826  1.00 75.69           O  
ANISOU 5696  OD1 ASN B 310     6398  15119   7243   -770   -137   -138       O  
ATOM   5697  ND2 ASN B 310      43.060  21.167-119.434  1.00 66.77           N  
ANISOU 5697  ND2 ASN B 310     5364  13984   6021   -900   -165   -213       N  
ATOM   5698  N   VAL B 311      45.287  22.189-113.962  1.00 43.05           N  
ANISOU 5698  N   VAL B 311     2649  10310   3397   -645     62    -85       N  
ATOM   5699  CA  VAL B 311      46.074  21.691-112.843  1.00 47.16           C  
ANISOU 5699  CA  VAL B 311     3265  10664   3991   -696    119    -86       C  
ATOM   5700  C   VAL B 311      46.077  22.757-111.756  1.00 41.36           C  
ANISOU 5700  C   VAL B 311     2541   9868   3304   -537    146    -41       C  
ATOM   5701  O   VAL B 311      45.805  23.934-112.009  1.00 41.59           O  
ANISOU 5701  O   VAL B 311     2526   9945   3331   -371    119    -10       O  
ATOM   5702  CB  VAL B 311      47.511  21.317-113.291  1.00 44.37           C  
ANISOU 5702  CB  VAL B 311     3019  10179   3662   -718    127    -98       C  
ATOM   5703  CG1 VAL B 311      48.502  22.425-112.953  1.00 46.59           C  
ANISOU 5703  CG1 VAL B 311     3379  10335   3990   -542    139    -34       C  
ATOM   5704  CG2 VAL B 311      47.933  19.979-112.694  1.00 45.74           C  
ANISOU 5704  CG2 VAL B 311     3244  10249   3887   -897    168   -140       C  
ATOM   5705  N   GLY B 312      46.366  22.327-110.527  1.00 40.87           N  
ANISOU 5705  N   GLY B 312     2532   9706   3289   -594    199    -40       N  
ATOM   5706  CA  GLY B 312      46.377  23.216-109.379  1.00 40.56           C  
ANISOU 5706  CA  GLY B 312     2503   9621   3287   -464    231    -20       C  
ATOM   5707  C   GLY B 312      47.751  23.454-108.783  1.00 38.87           C  
ANISOU 5707  C   GLY B 312     2416   9215   3137   -409    260      8       C  
ATOM   5708  O   GLY B 312      47.906  24.306-107.904  1.00 38.57           O  
ANISOU 5708  O   GLY B 312     2393   9133   3130   -290    282     15       O  
ATOM   5709  N   ILE B 313      48.758  22.719-109.259  1.00 44.30           N  
ANISOU 5709  N   ILE B 313     3190   9797   3846   -492    262     14       N  
ATOM   5710  CA  ILE B 313      50.118  22.811-108.727  1.00 47.80           C  
ANISOU 5710  CA  ILE B 313     3753  10058   4350   -455    292     43       C  
ATOM   5711  C   ILE B 313      50.841  24.017-109.314  1.00 46.18           C  
ANISOU 5711  C   ILE B 313     3578   9806   4160   -285    265     76       C  
ATOM   5712  O   ILE B 313      50.338  24.679-110.229  1.00 36.17           O  
ANISOU 5712  O   ILE B 313     2243   8645   2855   -210    221     85       O  
ATOM   5713  CB  ILE B 313      50.912  21.523-109.012  1.00 48.53           C  
ANISOU 5713  CB  ILE B 313     3910  10065   4464   -604    310     28       C  
ATOM   5714  CG1 ILE B 313      51.144  21.379-110.524  1.00 47.36           C  
ANISOU 5714  CG1 ILE B 313     3742   9973   4279   -611    272     -6       C  
ATOM   5715  CG2 ILE B 313      50.182  20.314-108.442  1.00 37.10           C  
ANISOU 5715  CG2 ILE B 313     2424   8665   3009   -795    331     16       C  
ATOM   5716  CD1 ILE B 313      52.005  20.198-110.925  1.00 46.62           C  
ANISOU 5716  CD1 ILE B 313     3697   9809   4209   -735    293    -52       C  
ATOM   5717  N   GLN B 314      52.032  24.305-108.796  1.00 34.34           N  
ANISOU 5717  N   GLN B 314     2179   8154   2716   -234    290    105       N  
ATOM   5718  CA  GLN B 314      52.844  25.389-109.328  1.00 33.64           C  
ANISOU 5718  CA  GLN B 314     2121   8015   2645    -99    267    151       C  
ATOM   5719  C   GLN B 314      53.484  24.974-110.649  1.00 36.27           C  
ANISOU 5719  C   GLN B 314     2474   8361   2945   -144    244    158       C  
ATOM   5720  O   GLN B 314      53.984  23.853-110.788  1.00 33.15           O  
ANISOU 5720  O   GLN B 314     2124   7917   2554   -257    267    119       O  
ATOM   5721  CB  GLN B 314      53.918  25.794-108.319  1.00 43.71           C  
ANISOU 5721  CB  GLN B 314     3489   9136   3982    -45    301    177       C  
ATOM   5722  CG  GLN B 314      54.993  26.691-108.896  1.00 37.73           C  
ANISOU 5722  CG  GLN B 314     2775   8315   3248     53    283    236       C  
ATOM   5723  CD  GLN B 314      55.882  27.298-107.830  1.00 41.90           C  
ANISOU 5723  CD  GLN B 314     3370   8717   3833    119    311    257       C  
ATOM   5724  OE1 GLN B 314      55.550  28.332-107.247  1.00 39.71           O  
ANISOU 5724  OE1 GLN B 314     3052   8460   3575    230    308    255       O  
ATOM   5725  NE2 GLN B 314      57.020  26.660-107.570  1.00 30.14           N  
ANISOU 5725  NE2 GLN B 314     1976   7106   2371     56    338    268       N  
ATOM   5726  N   ILE B 315      53.445  25.882-111.624  1.00 33.72           N  
ANISOU 5726  N   ILE B 315     2106   8121   2585    -54    198    206       N  
ATOM   5727  CA  ILE B 315      54.008  25.666-112.954  1.00 33.78           C  
ANISOU 5727  CA  ILE B 315     2116   8187   2533    -89    173    219       C  
ATOM   5728  C   ILE B 315      55.063  26.741-113.175  1.00 40.14           C  
ANISOU 5728  C   ILE B 315     2961   8933   3358     14    163    312       C  
ATOM   5729  O   ILE B 315      54.732  27.928-113.296  1.00 33.63           O  
ANISOU 5729  O   ILE B 315     2078   8157   2541    126    124    390       O  
ATOM   5730  CB  ILE B 315      52.936  25.714-114.052  1.00 46.52           C  
ANISOU 5730  CB  ILE B 315     3621  10002   4054   -105    120    215       C  
ATOM   5731  CG1 ILE B 315      51.849  24.671-113.791  1.00 45.58           C  
ANISOU 5731  CG1 ILE B 315     3450   9950   3916   -222    129    127       C  
ATOM   5732  CG2 ILE B 315      53.564  25.482-115.415  1.00 35.35           C  
ANISOU 5732  CG2 ILE B 315     2203   8678   2552   -149     96    220       C  
ATOM   5733  CD1 ILE B 315      52.365  23.250-113.785  1.00 43.58           C  
ANISOU 5733  CD1 ILE B 315     3247   9641   3672   -371    166     42       C  
ATOM   5734  N   VAL B 316      56.327  26.331-113.243  1.00 32.31           N  
ANISOU 5734  N   VAL B 316     2058   7836   2385    -22    194    308       N  
ATOM   5735  CA  VAL B 316      57.456  27.253-113.260  1.00 31.71           C  
ANISOU 5735  CA  VAL B 316     2027   7687   2336     51    195    399       C  
ATOM   5736  C   VAL B 316      57.973  27.392-114.685  1.00 39.69           C  
ANISOU 5736  C   VAL B 316     3014   8814   3254     29    168    448       C  
ATOM   5737  O   VAL B 316      58.181  26.390-115.381  1.00 40.54           O  
ANISOU 5737  O   VAL B 316     3135   8963   3307    -57    178    364       O  
ATOM   5738  CB  VAL B 316      58.574  26.776-112.316  1.00 35.30           C  
ANISOU 5738  CB  VAL B 316     2591   7952   2868     28    247    370       C  
ATOM   5739  CG1 VAL B 316      59.658  27.834-112.194  1.00 30.11           C  
ANISOU 5739  CG1 VAL B 316     1969   7228   2242     99    247    469       C  
ATOM   5740  CG2 VAL B 316      57.998  26.421-110.950  1.00 30.34           C  
ANISOU 5740  CG2 VAL B 316     1980   7248   2300     18    275    321       C  
ATOM   5741  N   GLY B 317      58.181  28.632-115.119  1.00 32.61           N  
ANISOU 5741  N   GLY B 317     2068   7984   2340    102    132    583       N  
ATOM   5742  CA  GLY B 317      58.817  28.908-116.395  1.00 33.23           C  
ANISOU 5742  CA  GLY B 317     2136   8172   2319     71    105    664       C  
ATOM   5743  C   GLY B 317      60.304  29.147-116.204  1.00 38.36           C  
ANISOU 5743  C   GLY B 317     2874   8701   3000     64    141    713       C  
ATOM   5744  O   GLY B 317      60.713  29.949-115.360  1.00 33.35           O  
ANISOU 5744  O   GLY B 317     2294   7909   2468    126    127    779       O  
ATOM   5745  N   ASP B 318      61.109  28.427-116.989  1.00 37.37           N  
ANISOU 5745  N   ASP B 318     2786   8592   2822     -7    152    653       N  
ATOM   5746  CA  ASP B 318      62.562  28.565-116.971  1.00 34.58           C  
ANISOU 5746  CA  ASP B 318     2498   8140   2501    -20    176    685       C  
ATOM   5747  C   ASP B 318      63.048  28.928-118.368  1.00 34.14           C  
ANISOU 5747  C   ASP B 318     2398   8236   2339    -66    142    761       C  
ATOM   5748  O   ASP B 318      63.283  30.104-118.662  1.00 39.53           O  
ANISOU 5748  O   ASP B 318     3063   8960   2998    -57    104    941       O  
ATOM   5749  CB  ASP B 318      63.222  27.273-116.474  1.00 36.08           C  
ANISOU 5749  CB  ASP B 318     2757   8196   2756    -49    231    522       C  
ATOM   5750  CG  ASP B 318      64.738  27.381-116.375  1.00 38.44           C  
ANISOU 5750  CG  ASP B 318     3105   8407   3093    -51    258    547       C  
ATOM   5751  OD1 ASP B 318      65.401  26.330-116.207  1.00 31.83           O  
ANISOU 5751  OD1 ASP B 318     2304   7502   2289    -67    303    424       O  
ATOM   5752  OD2 ASP B 318      65.269  28.510-116.458  1.00 35.62           O  
ANISOU 5752  OD2 ASP B 318     2741   8062   2732    -38    236    695       O  
ATOM   5753  N   ASP B 319      63.193  27.929-119.244  1.00 36.43           N  
ANISOU 5753  N   ASP B 319     2669   8611   2563   -123    154    630       N  
ATOM   5754  CA  ASP B 319      63.473  28.225-120.645  1.00 37.23           C  
ANISOU 5754  CA  ASP B 319     2705   8891   2551   -174    124    685       C  
ATOM   5755  C   ASP B 319      62.310  28.942-121.318  1.00 45.15           C  
ANISOU 5755  C   ASP B 319     3623  10055   3477   -178     61    803       C  
ATOM   5756  O   ASP B 319      62.517  29.629-122.323  1.00 48.31           O  
ANISOU 5756  O   ASP B 319     3975  10573   3807   -217     28    928       O  
ATOM   5757  CB  ASP B 319      63.807  26.941-121.407  1.00 44.85           C  
ANISOU 5757  CB  ASP B 319     3658   9932   3452   -225    158    490       C  
ATOM   5758  CG  ASP B 319      65.144  26.348-121.002  1.00 58.43           C  
ANISOU 5758  CG  ASP B 319     5440  11528   5231   -214    219    399       C  
ATOM   5759  OD1 ASP B 319      65.369  25.153-121.293  1.00 64.16           O  
ANISOU 5759  OD1 ASP B 319     6168  12275   5935   -230    260    212       O  
ATOM   5760  OD2 ASP B 319      65.967  27.067-120.392  1.00 59.02           O  
ANISOU 5760  OD2 ASP B 319     5556  11495   5376   -189    226    510       O  
ATOM   5761  N   LEU B 320      61.096  28.798-120.785  1.00 47.30           N  
ANISOU 5761  N   LEU B 320     3873  10336   3764   -140     46    770       N  
ATOM   5762  CA  LEU B 320      59.952  29.533-121.317  1.00 48.23           C  
ANISOU 5762  CA  LEU B 320     3915  10588   3824   -122    -15    887       C  
ATOM   5763  C   LEU B 320      60.177  31.039-121.216  1.00 42.46           C  
ANISOU 5763  C   LEU B 320     3219   9776   3137    -70    -75   1117       C  
ATOM   5764  O   LEU B 320      60.059  31.765-122.209  1.00 42.88           O  
ANISOU 5764  O   LEU B 320     3248   9902   3144    -98   -131   1254       O  
ATOM   5765  CB  LEU B 320      58.683  29.114-120.567  1.00 50.92           C  
ANISOU 5765  CB  LEU B 320     4223  10943   4182    -81    -21    802       C  
ATOM   5766  CG  LEU B 320      57.270  29.472-121.056  1.00 59.33           C  
ANISOU 5766  CG  LEU B 320     5212  12122   5208    -59    -85    847       C  
ATOM   5767  CD1 LEU B 320      56.880  30.894-120.681  1.00 63.95           C  
ANISOU 5767  CD1 LEU B 320     5818  12587   5891     53   -170   1020       C  
ATOM   5768  CD2 LEU B 320      57.119  29.250-122.558  1.00 59.65           C  
ANISOU 5768  CD2 LEU B 320     5195  12339   5131   -143    -98    846       C  
ATOM   5769  N   THR B 321      60.527  31.520-120.022  1.00 38.22           N  
ANISOU 5769  N   THR B 321     2751   9072   2701      0    -78   1160       N  
ATOM   5770  CA  THR B 321      60.603  32.949-119.744  1.00 43.08           C  
ANISOU 5770  CA  THR B 321     3409   9552   3407     67   -173   1353       C  
ATOM   5771  C   THR B 321      62.021  33.510-119.764  1.00 46.99           C  
ANISOU 5771  C   THR B 321     3969   9959   3924     17   -161   1467       C  
ATOM   5772  O   THR B 321      62.181  34.717-119.985  1.00 50.70           O  
ANISOU 5772  O   THR B 321     4472  10341   4452     27   -253   1655       O  
ATOM   5773  CB  THR B 321      59.962  33.251-118.381  1.00 43.13           C  
ANISOU 5773  CB  THR B 321     3432   9396   3559    188   -203   1305       C  
ATOM   5774  OG1 THR B 321      60.275  32.197-117.463  1.00 40.48           O  
ANISOU 5774  OG1 THR B 321     3127   8989   3264    168    -85   1124       O  
ATOM   5775  CG2 THR B 321      58.453  33.349-118.509  1.00 45.30           C  
ANISOU 5775  CG2 THR B 321     3625   9742   3844    258   -265   1278       C  
ATOM   5776  N   VAL B 322      63.040  32.666-119.551  1.00 41.70           N  
ANISOU 5776  N   VAL B 322     3317   9294   3234    -38    -57   1355       N  
ATOM   5777  CA  VAL B 322      64.459  33.035-119.497  1.00 39.27           C  
ANISOU 5777  CA  VAL B 322     3053   8912   2958    -92    -31   1429       C  
ATOM   5778  C   VAL B 322      64.671  34.382-118.811  1.00 40.12           C  
ANISOU 5778  C   VAL B 322     3230   8851   3163    -46   -123   1618       C  
ATOM   5779  O   VAL B 322      65.497  35.192-119.251  1.00 49.30           O  
ANISOU 5779  O   VAL B 322     4412   9980   4341   -114   -161   1775       O  
ATOM   5780  CB  VAL B 322      65.116  33.024-120.899  1.00 38.26           C  
ANISOU 5780  CB  VAL B 322     2867   8929   2743   -197    -28   1473       C  
ATOM   5781  CG1 VAL B 322      65.120  31.618-121.484  1.00 40.76           C  
ANISOU 5781  CG1 VAL B 322     3132   9369   2986   -226     32   1250       C  
ATOM   5782  CG2 VAL B 322      64.450  33.999-121.867  1.00 43.75           C  
ANISOU 5782  CG2 VAL B 322     3532   9699   3392   -224   -121   1658       C  
ATOM   5783  N   THR B 323      63.929  34.622-117.726  1.00 36.56           N  
ANISOU 5783  N   THR B 323     2815   8227   2849     62   -156   1559       N  
ATOM   5784  CA  THR B 323      64.050  35.841-116.919  1.00 42.40           C  
ANISOU 5784  CA  THR B 323     3627   8727   3757    128   -246   1659       C  
ATOM   5785  C   THR B 323      63.943  37.102-117.784  1.00 47.70           C  
ANISOU 5785  C   THR B 323     4302   9396   4427    113   -390   1900       C  
ATOM   5786  O   THR B 323      64.491  38.153-117.450  1.00 47.22           O  
ANISOU 5786  O   THR B 323     4309   9150   4482    113   -472   2030       O  
ATOM   5787  CB  THR B 323      65.355  35.830-116.101  1.00 43.10           C  
ANISOU 5787  CB  THR B 323     3782   8676   3918     87   -188   1636       C  
ATOM   5788  OG1 THR B 323      65.590  34.515-115.574  1.00 35.61           O  
ANISOU 5788  OG1 THR B 323     2822   7770   2940     78    -60   1442       O  
ATOM   5789  CG2 THR B 323      65.281  36.790-114.920  1.00 35.79           C  
ANISOU 5789  CG2 THR B 323     2935   7486   3178    175   -260   1644       C  
ATOM   5790  N   ASN B 324      63.220  37.013-118.908  1.00 47.83           N  
ANISOU 5790  N   ASN B 324     4252   9592   4330     90   -424   1955       N  
ATOM   5791  CA  ASN B 324      63.104  38.123-119.847  1.00 47.28           C  
ANISOU 5791  CA  ASN B 324     4197   9488   4280     52   -540   2166       C  
ATOM   5792  C   ASN B 324      61.728  38.763-119.751  1.00 54.89           C  
ANISOU 5792  C   ASN B 324     5147  10370   5337    189   -664   2192       C  
ATOM   5793  O   ASN B 324      60.716  38.066-119.907  1.00 54.55           O  
ANISOU 5793  O   ASN B 324     5033  10457   5237    236   -628   2064       O  
ATOM   5794  CB  ASN B 324      63.357  37.652-121.282  1.00 45.57           C  
ANISOU 5794  CB  ASN B 324     3917   9500   3897    -86   -479   2193       C  
ATOM   5795  CG  ASN B 324      63.021  38.715-122.307  1.00 56.25           C  
ANISOU 5795  CG  ASN B 324     5274  10846   5254   -127   -604   2409       C  
ATOM   5796  OD1 ASN B 324      61.978  38.659-122.958  1.00 62.10           O  
ANISOU 5796  OD1 ASN B 324     5966  11682   5945    -96   -647   2409       O  
ATOM   5797  ND2 ASN B 324      63.898  39.701-122.445  1.00 63.26           N  
ANISOU 5797  ND2 ASN B 324     6220  11615   6201   -204   -673   2602       N  
ATOM   5798  N   PRO B 325      61.650  40.081-119.529  1.00 55.68           N  
ANISOU 5798  N   PRO B 325     5308  10256   5591    255   -816   2352       N  
ATOM   5799  CA  PRO B 325      60.338  40.710-119.284  1.00 57.04           C  
ANISOU 5799  CA  PRO B 325     5458  10328   5886    423   -940   2347       C  
ATOM   5800  C   PRO B 325      59.341  40.553-120.423  1.00 56.81           C  
ANISOU 5800  C   PRO B 325     5360  10464   5760    411   -968   2376       C  
ATOM   5801  O   PRO B 325      58.149  40.332-120.165  1.00 52.86           O  
ANISOU 5801  O   PRO B 325     4792  10003   5291    533   -984   2260       O  
ATOM   5802  CB  PRO B 325      60.705  42.184-119.053  1.00 56.79           C  
ANISOU 5802  CB  PRO B 325     5521  10021   6037    466  -1110   2538       C  
ATOM   5803  CG  PRO B 325      62.127  42.158-118.607  1.00 54.26           C  
ANISOU 5803  CG  PRO B 325     5267   9635   5715    353  -1052   2575       C  
ATOM   5804  CD  PRO B 325      62.760  41.034-119.369  1.00 53.24           C  
ANISOU 5804  CD  PRO B 325     5089   9767   5371    187   -886   2524       C  
ATOM   5805  N   LYS B 326      59.787  40.672-121.676  1.00 59.55           N  
ANISOU 5805  N   LYS B 326     5711  10924   5989    262   -973   2524       N  
ATOM   5806  CA  LYS B 326      58.861  40.543-122.799  1.00 59.12           C  
ANISOU 5806  CA  LYS B 326     5588  11041   5834    242  -1008   2559       C  
ATOM   5807  C   LYS B 326      58.294  39.132-122.893  1.00 54.13           C  
ANISOU 5807  C   LYS B 326     4862  10643   5061    227   -868   2338       C  
ATOM   5808  O   LYS B 326      57.096  38.955-123.140  1.00 53.32           O  
ANISOU 5808  O   LYS B 326     4692  10623   4945    296   -904   2282       O  
ATOM   5809  CB  LYS B 326      59.554  40.936-124.105  1.00 62.72           C  
ANISOU 5809  CB  LYS B 326     6057  11592   6181     72  -1032   2757       C  
ATOM   5810  CG  LYS B 326      59.897  42.421-124.220  1.00 70.72           C  
ANISOU 5810  CG  LYS B 326     7162  12373   7336     71  -1204   3009       C  
ATOM   5811  CD  LYS B 326      58.739  43.237-124.795  1.00 78.92           C  
ANISOU 5811  CD  LYS B 326     8192  13356   8440    164  -1379   3132       C  
ATOM   5812  CE  LYS B 326      57.815  43.784-123.713  1.00 81.13           C  
ANISOU 5812  CE  LYS B 326     8489  13404   8934    398  -1493   3057       C  
ATOM   5813  NZ  LYS B 326      56.717  44.612-124.290  1.00 80.17           N  
ANISOU 5813  NZ  LYS B 326     8353  13219   8889    504  -1676   3175       N  
ATOM   5814  N   ARG B 327      59.138  38.115-122.702  1.00 55.37           N  
ANISOU 5814  N   ARG B 327     5013  10904   5122    136   -715   2209       N  
ATOM   5815  CA  ARG B 327      58.643  36.743-122.645  1.00 54.24           C  
ANISOU 5815  CA  ARG B 327     4795  10942   4874    124   -594   1986       C  
ATOM   5816  C   ARG B 327      57.701  36.537-121.464  1.00 53.61           C  
ANISOU 5816  C   ARG B 327     4692  10775   4902    268   -599   1843       C  
ATOM   5817  O   ARG B 327      56.735  35.770-121.563  1.00 50.81           O  
ANISOU 5817  O   ARG B 327     4262  10552   4491    282   -563   1709       O  
ATOM   5818  CB  ARG B 327      59.815  35.765-122.560  1.00 48.73           C  
ANISOU 5818  CB  ARG B 327     4103  10325   4088     19   -450   1873       C  
ATOM   5819  CG  ARG B 327      60.708  35.759-123.785  1.00 47.25           C  
ANISOU 5819  CG  ARG B 327     3895  10278   3780   -127   -420   1961       C  
ATOM   5820  CD  ARG B 327      60.089  34.965-124.921  1.00 44.95           C  
ANISOU 5820  CD  ARG B 327     3510  10231   3339   -192   -386   1873       C  
ATOM   5821  NE  ARG B 327      59.998  33.543-124.602  1.00 44.94           N  
ANISOU 5821  NE  ARG B 327     3465  10323   3287   -197   -276   1622       N  
ATOM   5822  CZ  ARG B 327      59.677  32.603-125.488  1.00 47.51           C  
ANISOU 5822  CZ  ARG B 327     3711  10850   3489   -265   -233   1491       C  
ATOM   5823  NH1 ARG B 327      59.420  32.932-126.746  1.00 45.78           N  
ANISOU 5823  NH1 ARG B 327     3441  10787   3167   -332   -280   1589       N  
ATOM   5824  NH2 ARG B 327      59.615  31.332-125.116  1.00 44.79           N  
ANISOU 5824  NH2 ARG B 327     3341  10545   3130   -269   -157   1262       N  
ATOM   5825  N   ILE B 328      57.968  37.207-120.341  1.00 49.80           N  
ANISOU 5825  N   ILE B 328     4265  10080   4575    370   -643   1862       N  
ATOM   5826  CA  ILE B 328      57.082  37.105-119.187  1.00 44.20           C  
ANISOU 5826  CA  ILE B 328     3517   9300   3978    513   -644   1717       C  
ATOM   5827  C   ILE B 328      55.729  37.738-119.493  1.00 47.67           C  
ANISOU 5827  C   ILE B 328     3894   9737   4480    626   -758   1751       C  
ATOM   5828  O   ILE B 328      54.677  37.208-119.109  1.00 44.52           O  
ANISOU 5828  O   ILE B 328     3412   9418   4084    688   -722   1603       O  
ATOM   5829  CB  ILE B 328      57.742  37.738-117.949  1.00 48.89           C  
ANISOU 5829  CB  ILE B 328     4177   9677   4722    598   -669   1722       C  
ATOM   5830  CG1 ILE B 328      59.000  36.959-117.558  1.00 45.24           C  
ANISOU 5830  CG1 ILE B 328     3763   9231   4195    490   -548   1662       C  
ATOM   5831  CG2 ILE B 328      56.772  37.769-116.787  1.00 47.30           C  
ANISOU 5831  CG2 ILE B 328     3918   9416   4638    756   -670   1568       C  
ATOM   5832  CD1 ILE B 328      59.924  37.716-116.619  1.00 46.71           C  
ANISOU 5832  CD1 ILE B 328     4060   9156   4532    517   -559   1691       C  
ATOM   5833  N   GLU B 329      55.729  38.878-120.191  1.00 44.97           N  
ANISOU 5833  N   GLU B 329     3590   9304   4193    649   -899   1950       N  
ATOM   5834  CA  GLU B 329      54.469  39.525-120.540  1.00 48.45           C  
ANISOU 5834  CA  GLU B 329     3971   9734   4703    767  -1026   1992       C  
ATOM   5835  C   GLU B 329      53.584  38.598-121.361  1.00 47.29           C  
ANISOU 5835  C   GLU B 329     3727   9839   4403    698   -971   1913       C  
ATOM   5836  O   GLU B 329      52.372  38.513-121.127  1.00 48.08           O  
ANISOU 5836  O   GLU B 329     3738   9985   4545    800   -996   1817       O  
ATOM   5837  CB  GLU B 329      54.730  40.825-121.300  1.00 54.87           C  
ANISOU 5837  CB  GLU B 329     4852  10407   5587    773  -1197   2242       C  
ATOM   5838  CG  GLU B 329      55.144  41.991-120.418  1.00 65.62           C  
ANISOU 5838  CG  GLU B 329     6296  11473   7162    899  -1312   2314       C  
ATOM   5839  CD  GLU B 329      53.988  42.601-119.638  1.00 78.08           C  
ANISOU 5839  CD  GLU B 329     7814  12927   8927   1134  -1414   2219       C  
ATOM   5840  OE1 GLU B 329      54.172  43.708-119.091  1.00 79.83           O  
ANISOU 5840  OE1 GLU B 329     8098  12891   9342   1262  -1546   2288       O  
ATOM   5841  OE2 GLU B 329      52.901  41.988-119.565  1.00 82.43           O  
ANISOU 5841  OE2 GLU B 329     8252  13633   9436   1193  -1363   2069       O  
ATOM   5842  N   ARG B 330      54.176  37.883-122.317  1.00 47.06           N  
ANISOU 5842  N   ARG B 330     3705   9982   4195    525   -892   1938       N  
ATOM   5843  CA  ARG B 330      53.399  36.943-123.113  1.00 53.20           C  
ANISOU 5843  CA  ARG B 330     4393  11001   4821    450   -840   1847       C  
ATOM   5844  C   ARG B 330      52.942  35.756-122.277  1.00 51.15           C  
ANISOU 5844  C   ARG B 330     4077  10817   4540    453   -716   1610       C  
ATOM   5845  O   ARG B 330      51.822  35.260-122.453  1.00 53.77           O  
ANISOU 5845  O   ARG B 330     4320  11277   4832    464   -713   1517       O  
ATOM   5846  CB  ARG B 330      54.212  36.466-124.313  1.00 53.16           C  
ANISOU 5846  CB  ARG B 330     4400  11161   4635    272   -782   1906       C  
ATOM   5847  CG  ARG B 330      53.495  35.394-125.103  1.00 53.81           C  
ANISOU 5847  CG  ARG B 330     4391  11494   4560    187   -723   1783       C  
ATOM   5848  CD  ARG B 330      54.125  35.157-126.451  1.00 54.60           C  
ANISOU 5848  CD  ARG B 330     4483  11771   4493     35   -697   1852       C  
ATOM   5849  NE  ARG B 330      53.484  34.039-127.131  1.00 57.19           N  
ANISOU 5849  NE  ARG B 330     4722  12331   4676    -45   -638   1700       N  
ATOM   5850  CZ  ARG B 330      53.966  33.461-128.225  1.00 63.78           C  
ANISOU 5850  CZ  ARG B 330     5523  13359   5352   -180   -586   1673       C  
ATOM   5851  NH1 ARG B 330      55.098  33.897-128.760  1.00 53.87           N  
ANISOU 5851  NH1 ARG B 330     4305  12107   4056   -254   -576   1792       N  
ATOM   5852  NH2 ARG B 330      53.318  32.448-128.782  1.00 69.44           N  
ANISOU 5852  NH2 ARG B 330     6161  14269   5953   -245   -546   1518       N  
ATOM   5853  N   ALA B 331      53.794  35.285-121.365  1.00 43.92           N  
ANISOU 5853  N   ALA B 331     3212   9825   3650    434   -618   1518       N  
ATOM   5854  CA  ALA B 331      53.422  34.157-120.519  1.00 50.90           C  
ANISOU 5854  CA  ALA B 331     4055  10765   4521    422   -508   1308       C  
ATOM   5855  C   ALA B 331      52.270  34.515-119.585  1.00 52.82           C  
ANISOU 5855  C   ALA B 331     4236  10941   4891    565   -543   1235       C  
ATOM   5856  O   ALA B 331      51.404  33.676-119.310  1.00 50.65           O  
ANISOU 5856  O   ALA B 331     3890  10774   4580    542   -485   1092       O  
ATOM   5857  CB  ALA B 331      54.636  33.678-119.725  1.00 42.90           C  
ANISOU 5857  CB  ALA B 331     3112   9669   3520    378   -414   1247       C  
ATOM   5858  N   VAL B 332      52.244  35.753-119.086  1.00 55.14           N  
ANISOU 5858  N   VAL B 332     4553  11058   5338    711   -640   1324       N  
ATOM   5859  CA  VAL B 332      51.134  36.198-118.244  1.00 55.69           C  
ANISOU 5859  CA  VAL B 332     4550  11075   5536    869   -677   1239       C  
ATOM   5860  C   VAL B 332      49.850  36.282-119.060  1.00 60.95           C  
ANISOU 5860  C   VAL B 332     5117  11875   6168    896   -750   1257       C  
ATOM   5861  O   VAL B 332      48.789  35.811-118.633  1.00 58.83           O  
ANISOU 5861  O   VAL B 332     4753  11699   5901    926   -709   1122       O  
ATOM   5862  CB  VAL B 332      51.466  37.550-117.583  1.00 53.58           C  
ANISOU 5862  CB  VAL B 332     4332  10576   5452   1033   -782   1318       C  
ATOM   5863  CG1 VAL B 332      50.207  38.184-116.996  1.00 46.23           C  
ANISOU 5863  CG1 VAL B 332     3306   9606   4655   1220   -848   1237       C  
ATOM   5864  CG2 VAL B 332      52.549  37.384-116.515  1.00 54.11           C  
ANISOU 5864  CG2 VAL B 332     4474  10526   5560   1020   -699   1258       C  
ATOM   5865  N   GLU B 333      49.936  36.884-120.250  1.00 66.15           N  
ANISOU 5865  N   GLU B 333     5794  12549   6791    874   -860   1431       N  
ATOM   5866  CA  GLU B 333      48.770  37.059-121.112  1.00 65.56           C  
ANISOU 5866  CA  GLU B 333     5626  12598   6685    901   -950   1472       C  
ATOM   5867  C   GLU B 333      48.096  35.728-121.421  1.00 56.69           C  
ANISOU 5867  C   GLU B 333     4422  11708   5410    776   -846   1330       C  
ATOM   5868  O   GLU B 333      46.872  35.594-121.308  1.00 55.73           O  
ANISOU 5868  O   GLU B 333     4193  11677   5307    831   -866   1252       O  
ATOM   5869  CB  GLU B 333      49.195  37.751-122.407  1.00 74.80           C  
ANISOU 5869  CB  GLU B 333     6850  13767   7805    849  -1067   1692       C  
ATOM   5870  CG  GLU B 333      48.823  39.217-122.498  1.00 86.96           C  
ANISOU 5870  CG  GLU B 333     8399  15130   9514   1014  -1258   1847       C  
ATOM   5871  CD  GLU B 333      47.369  39.418-122.876  1.00 99.14           C  
ANISOU 5871  CD  GLU B 333     9817  16768  11085   1110  -1355   1830       C  
ATOM   5872  OE1 GLU B 333      46.669  40.184-122.179  1.00100.31           O  
ANISOU 5872  OE1 GLU B 333     9914  16783  11414   1304  -1445   1794       O  
ATOM   5873  OE2 GLU B 333      46.924  38.800-123.868  1.00103.33           O  
ANISOU 5873  OE2 GLU B 333    10292  17511  11457    995  -1340   1843       O  
ATOM   5874  N   GLU B 334      48.880  34.733-121.820  1.00 54.89           N  
ANISOU 5874  N   GLU B 334     4240  11578   5036    607   -742   1290       N  
ATOM   5875  CA  GLU B 334      48.355  33.436-122.218  1.00 54.00           C  
ANISOU 5875  CA  GLU B 334     4066  11671   4781    474   -660   1156       C  
ATOM   5876  C   GLU B 334      48.298  32.441-121.062  1.00 50.64           C  
ANISOU 5876  C   GLU B 334     3635  11233   4371    437   -536    969       C  
ATOM   5877  O   GLU B 334      47.977  31.267-121.283  1.00 46.09           O  
ANISOU 5877  O   GLU B 334     3027  10797   3689    310   -470    849       O  
ATOM   5878  CB  GLU B 334      49.189  32.898-123.383  1.00 48.80           C  
ANISOU 5878  CB  GLU B 334     3451  11131   3960    316   -628   1199       C  
ATOM   5879  CG  GLU B 334      49.382  33.966-124.470  1.00 56.40           C  
ANISOU 5879  CG  GLU B 334     4432  12091   4905    336   -748   1411       C  
ATOM   5880  CD  GLU B 334      50.198  33.495-125.655  1.00 55.38           C  
ANISOU 5880  CD  GLU B 334     4330  12105   4606    177   -708   1449       C  
ATOM   5881  OE1 GLU B 334      50.491  34.324-126.545  1.00 51.48           O  
ANISOU 5881  OE1 GLU B 334     3859  11617   4083    165   -794   1632       O  
ATOM   5882  OE2 GLU B 334      50.541  32.297-125.697  1.00 51.77           O  
ANISOU 5882  OE2 GLU B 334     3867  11753   4051     65   -594   1292       O  
ATOM   5883  N   LYS B 335      48.581  32.898-119.838  1.00 47.15           N  
ANISOU 5883  N   LYS B 335     3228  10624   4062    542   -514    942       N  
ATOM   5884  CA  LYS B 335      48.489  32.077-118.628  1.00 48.46           C  
ANISOU 5884  CA  LYS B 335     3393  10765   4254    513   -405    782       C  
ATOM   5885  C   LYS B 335      49.252  30.768-118.789  1.00 48.89           C  
ANISOU 5885  C   LYS B 335     3504  10876   4196    338   -309    700       C  
ATOM   5886  O   LYS B 335      48.774  29.694-118.418  1.00 49.07           O  
ANISOU 5886  O   LYS B 335     3503  10966   4178    243   -246    570       O  
ATOM   5887  CB  LYS B 335      47.027  31.828-118.246  1.00 49.54           C  
ANISOU 5887  CB  LYS B 335     3417  11000   4405    542   -402    684       C  
ATOM   5888  CG  LYS B 335      46.253  33.124-118.055  1.00 51.81           C  
ANISOU 5888  CG  LYS B 335     3634  11230   4820    737   -502    742       C  
ATOM   5889  CD  LYS B 335      45.036  32.949-117.170  1.00 63.30           C  
ANISOU 5889  CD  LYS B 335     4983  12747   6319    791   -467    613       C  
ATOM   5890  CE  LYS B 335      44.366  34.289-116.912  1.00 72.40           C  
ANISOU 5890  CE  LYS B 335     6064  13827   7619   1011   -569    648       C  
ATOM   5891  NZ  LYS B 335      43.284  34.203-115.892  1.00 77.62           N  
ANISOU 5891  NZ  LYS B 335     6618  14549   8327   1079   -518    506       N  
ATOM   5892  N   ALA B 336      50.461  30.866-119.347  1.00 41.91           N  
ANISOU 5892  N   ALA B 336     2696   9959   3268    294   -308    777       N  
ATOM   5893  CA  ALA B 336      51.240  29.671-119.638  1.00 40.95           C  
ANISOU 5893  CA  ALA B 336     2617   9900   3043    145   -230    689       C  
ATOM   5894  C   ALA B 336      51.753  29.017-118.368  1.00 39.30           C  
ANISOU 5894  C   ALA B 336     2463   9570   2900    123   -147    583       C  
ATOM   5895  O   ALA B 336      51.935  27.794-118.328  1.00 42.06           O  
ANISOU 5895  O   ALA B 336     2830   9955   3196      2    -91    463       O  
ATOM   5896  CB  ALA B 336      52.404  30.020-120.566  1.00 40.95           C  
ANISOU 5896  CB  ALA B 336     2671   9912   2978    111   -245    797       C  
ATOM   5897  N   CYS B 337      51.982  29.806-117.325  1.00 39.45           N  
ANISOU 5897  N   CYS B 337     2511   9433   3044    237   -145    621       N  
ATOM   5898  CA  CYS B 337      52.514  29.289-116.073  1.00 42.19           C  
ANISOU 5898  CA  CYS B 337     2919   9650   3460    218    -65    536       C  
ATOM   5899  C   CYS B 337      52.161  30.267-114.963  1.00 37.23           C  
ANISOU 5899  C   CYS B 337     2280   8907   2957    361    -76    551       C  
ATOM   5900  O   CYS B 337      51.658  31.365-115.213  1.00 44.22           O  
ANISOU 5900  O   CYS B 337     3119   9792   3891    484   -155    628       O  
ATOM   5901  CB  CYS B 337      54.026  29.079-116.164  1.00 44.70           C  
ANISOU 5901  CB  CYS B 337     3321   9893   3769    171    -29    562       C  
ATOM   5902  SG  CYS B 337      54.938  30.570-116.621  1.00 42.14           S  
ANISOU 5902  SG  CYS B 337     3022   9510   3481    272   -105    750       S  
ATOM   5903  N   ASN B 338      52.445  29.860-113.725  1.00 36.20           N  
ANISOU 5903  N   ASN B 338     2201   8671   2884    346     -2    472       N  
ATOM   5904  CA  ASN B 338      52.119  30.676-112.565  1.00 43.66           C  
ANISOU 5904  CA  ASN B 338     3131   9528   3929    473      2    450       C  
ATOM   5905  C   ASN B 338      53.313  30.910-111.644  1.00 45.37           C  
ANISOU 5905  C   ASN B 338     3436   9588   4214    496     46    456       C  
ATOM   5906  O   ASN B 338      53.116  31.320-110.492  1.00 41.98           O  
ANISOU 5906  O   ASN B 338     3006   9095   3851    573     72    400       O  
ATOM   5907  CB  ASN B 338      50.966  30.044-111.774  1.00 39.17           C  
ANISOU 5907  CB  ASN B 338     2515   9022   3347    435     48    336       C  
ATOM   5908  CG  ASN B 338      51.226  28.592-111.425  1.00 43.23           C  
ANISOU 5908  CG  ASN B 338     3093   9518   3814    260    114    269       C  
ATOM   5909  OD1 ASN B 338      52.346  28.212-111.068  1.00 40.25           O  
ANISOU 5909  OD1 ASN B 338     2815   9019   3460    211    151    274       O  
ATOM   5910  ND2 ASN B 338      50.192  27.768-111.534  1.00 36.88           N  
ANISOU 5910  ND2 ASN B 338     2231   8826   2956    165    118    210       N  
ATOM   5911  N   CYS B 339      54.537  30.658-112.110  1.00 45.74           N  
ANISOU 5911  N   CYS B 339     3553   9587   4241    431     58    513       N  
ATOM   5912  CA  CYS B 339      55.730  30.901-111.308  1.00 44.82           C  
ANISOU 5912  CA  CYS B 339     3514   9327   4188    448     97    529       C  
ATOM   5913  C   CYS B 339      56.908  31.204-112.221  1.00 44.99           C  
ANISOU 5913  C   CYS B 339     3612   9291   4193    418     63    636       C  
ATOM   5914  O   CYS B 339      57.160  30.466-113.177  1.00 41.42           O  
ANISOU 5914  O   CYS B 339     3153   8932   3651    320     77    641       O  
ATOM   5915  CB  CYS B 339      56.063  29.704-110.414  1.00 50.85           C  
ANISOU 5915  CB  CYS B 339     4368  10011   4943    335    186    433       C  
ATOM   5916  SG  CYS B 339      57.504  29.979-109.340  1.00 59.07           S  
ANISOU 5916  SG  CYS B 339     5511  10878   6054    353    233    451       S  
ATOM   5917  N   LEU B 340      57.637  32.271-111.906  1.00 32.62           N  
ANISOU 5917  N   LEU B 340     2121   7568   2707    492     19    712       N  
ATOM   5918  CA  LEU B 340      58.823  32.671-112.652  1.00 32.48           C  
ANISOU 5918  CA  LEU B 340     2179   7486   2676    451    -13    830       C  
ATOM   5919  C   LEU B 340      60.078  32.152-111.960  1.00 39.57           C  
ANISOU 5919  C   LEU B 340     3172   8269   3596    386     64    794       C  
ATOM   5920  O   LEU B 340      60.257  32.361-110.756  1.00 33.33           O  
ANISOU 5920  O   LEU B 340     2426   7355   2882    428     86    744       O  
ATOM   5921  CB  LEU B 340      58.892  34.194-112.774  1.00 33.46           C  
ANISOU 5921  CB  LEU B 340     2330   7495   2888    553   -129    957       C  
ATOM   5922  CG  LEU B 340      60.183  34.782-113.341  1.00 37.72           C  
ANISOU 5922  CG  LEU B 340     2953   7948   3431    498   -168   1101       C  
ATOM   5923  CD1 LEU B 340      60.352  34.391-114.799  1.00 42.30           C  
ANISOU 5923  CD1 LEU B 340     3491   8708   3872    402   -177   1187       C  
ATOM   5924  CD2 LEU B 340      60.189  36.292-113.180  1.00 38.70           C  
ANISOU 5924  CD2 LEU B 340     3120   7904   3681    598   -294   1214       C  
ATOM   5925  N   LEU B 341      60.941  31.472-112.718  1.00 45.93           N  
ANISOU 5925  N   LEU B 341     3997   9127   4326    289    103    811       N  
ATOM   5926  CA  LEU B 341      62.292  31.191-112.244  1.00 40.56           C  
ANISOU 5926  CA  LEU B 341     3396   8339   3675    243    154    807       C  
ATOM   5927  C   LEU B 341      63.159  32.411-112.509  1.00 39.63           C  
ANISOU 5927  C   LEU B 341     3325   8133   3598    260     87    950       C  
ATOM   5928  O   LEU B 341      63.215  32.906-113.639  1.00 31.27           O  
ANISOU 5928  O   LEU B 341     2240   7162   2481    237     34   1062       O  
ATOM   5929  CB  LEU B 341      62.886  29.964-112.937  1.00 29.70           C  
ANISOU 5929  CB  LEU B 341     2011   7059   2214    149    222    747       C  
ATOM   5930  CG  LEU B 341      64.122  29.387-112.237  1.00 29.97           C  
ANISOU 5930  CG  LEU B 341     2110   6983   2295    118    281    705       C  
ATOM   5931  CD1 LEU B 341      63.702  28.772-110.928  1.00 34.90           C  
ANISOU 5931  CD1 LEU B 341     2772   7500   2989    129    309    610       C  
ATOM   5932  CD2 LEU B 341      64.862  28.361-113.077  1.00 28.92           C  
ANISOU 5932  CD2 LEU B 341     2002   6861   2125     55    294    631       C  
ATOM   5933  N   LEU B 342      63.827  32.906-111.473  1.00 39.12           N  
ANISOU 5933  N   LEU B 342     3330   7903   3629    286     83    954       N  
ATOM   5934  CA  LEU B 342      64.580  34.154-111.561  1.00 36.52           C  
ANISOU 5934  CA  LEU B 342     3052   7458   3365    295      4   1087       C  
ATOM   5935  C   LEU B 342      66.071  33.832-111.552  1.00 35.13           C  
ANISOU 5935  C   LEU B 342     2912   7259   3176    209     50   1116       C  
ATOM   5936  O   LEU B 342      66.649  33.555-110.497  1.00 32.77           O  
ANISOU 5936  O   LEU B 342     2658   6859   2932    209     88   1048       O  
ATOM   5937  CB  LEU B 342      64.199  35.092-110.419  1.00 38.94           C  
ANISOU 5937  CB  LEU B 342     3406   7595   3797    394    -54   1059       C  
ATOM   5938  CG  LEU B 342      64.570  36.565-110.597  1.00 45.89           C  
ANISOU 5938  CG  LEU B 342     4338   8329   4770    422   -176   1196       C  
ATOM   5939  CD1 LEU B 342      63.759  37.170-111.714  1.00 49.51           C  
ANISOU 5939  CD1 LEU B 342     4748   8855   5209    457   -266   1310       C  
ATOM   5940  CD2 LEU B 342      64.342  37.344-109.321  1.00 47.03           C  
ANISOU 5940  CD2 LEU B 342     4536   8291   5041    522   -222   1116       C  
ATOM   5941  N   LYS B 343      66.692  33.862-112.734  1.00 40.28           N  
ANISOU 5941  N   LYS B 343     3532   8027   3745    133     48   1217       N  
ATOM   5942  CA  LYS B 343      68.141  33.730-112.869  1.00 34.59           C  
ANISOU 5942  CA  LYS B 343     2820   7315   3007     53     85   1261       C  
ATOM   5943  C   LYS B 343      68.700  35.122-113.137  1.00 33.08           C  
ANISOU 5943  C   LYS B 343     2661   7044   2866     17    -13   1446       C  
ATOM   5944  O   LYS B 343      68.442  35.706-114.194  1.00 34.51           O  
ANISOU 5944  O   LYS B 343     2813   7313   2987    -15    -72   1581       O  
ATOM   5945  CB  LYS B 343      68.511  32.757-113.987  1.00 35.68           C  
ANISOU 5945  CB  LYS B 343     2885   7665   3006    -13    160   1229       C  
ATOM   5946  CG  LYS B 343      67.661  31.494-114.016  1.00 42.80           C  
ANISOU 5946  CG  LYS B 343     3756   8647   3860     14    224   1064       C  
ATOM   5947  CD  LYS B 343      68.502  30.234-114.144  1.00 39.08           C  
ANISOU 5947  CD  LYS B 343     3293   8170   3387    -14    279    922       C  
ATOM   5948  CE  LYS B 343      68.164  29.464-115.407  1.00 30.49           C  
ANISOU 5948  CE  LYS B 343     2168   7211   2207    -43    275    836       C  
ATOM   5949  NZ  LYS B 343      68.421  28.006-115.236  1.00 36.23           N  
ANISOU 5949  NZ  LYS B 343     2921   7885   2960    -39    322    651       N  
ATOM   5950  N   VAL B 344      69.456  35.658-112.176  1.00 31.76           N  
ANISOU 5950  N   VAL B 344     2555   6706   2806     14    -40   1460       N  
ATOM   5951  CA  VAL B 344      69.891  37.051-112.263  1.00 37.40           C  
ANISOU 5951  CA  VAL B 344     3316   7294   3600    -23   -154   1627       C  
ATOM   5952  C   VAL B 344      70.787  37.266-113.476  1.00 34.10           C  
ANISOU 5952  C   VAL B 344     2847   7025   3085   -152   -156   1796       C  
ATOM   5953  O   VAL B 344      70.678  38.284-114.173  1.00 42.90           O  
ANISOU 5953  O   VAL B 344     3972   8120   4206   -196   -259   1978       O  
ATOM   5954  CB  VAL B 344      70.593  37.475-110.960  1.00 42.24           C  
ANISOU 5954  CB  VAL B 344     4002   7708   4338    -15   -179   1584       C  
ATOM   5955  CG1 VAL B 344      70.801  38.984-110.936  1.00 36.92           C  
ANISOU 5955  CG1 VAL B 344     3394   6854   3779    -39   -321   1734       C  
ATOM   5956  CG2 VAL B 344      69.780  37.031-109.768  1.00 43.23           C  
ANISOU 5956  CG2 VAL B 344     4160   7752   4515     97   -147   1402       C  
ATOM   5957  N   ASN B 345      71.683  36.315-113.755  1.00 35.86           N  
ANISOU 5957  N   ASN B 345     3006   7405   3214   -214    -48   1741       N  
ATOM   5958  CA  ASN B 345      72.591  36.477-114.887  1.00 41.33           C  
ANISOU 5958  CA  ASN B 345     3628   8284   3792   -341    -33   1885       C  
ATOM   5959  C   ASN B 345      71.890  36.284-116.228  1.00 39.93           C  
ANISOU 5959  C   ASN B 345     3387   8325   3461   -362    -27   1938       C  
ATOM   5960  O   ASN B 345      72.413  36.726-117.257  1.00 41.59           O  
ANISOU 5960  O   ASN B 345     3545   8652   3605   -468    -52   2070       O  
ATOM   5961  CB  ASN B 345      73.773  35.512-114.762  1.00 36.94           C  
ANISOU 5961  CB  ASN B 345     3005   7843   3187   -380     82   1785       C  
ATOM   5962  CG  ASN B 345      73.369  34.063-114.940  1.00 43.27           C  
ANISOU 5962  CG  ASN B 345     3768   8746   3929   -306    178   1569       C  
ATOM   5963  OD1 ASN B 345      72.248  33.669-114.612  1.00 42.41           O  
ANISOU 5963  OD1 ASN B 345     3687   8601   3824   -227    188   1482       O  
ATOM   5964  ND2 ASN B 345      74.286  33.258-115.459  1.00 51.38           N  
ANISOU 5964  ND2 ASN B 345     4746   9853   4924   -324    219   1458       N  
ATOM   5965  N   GLN B 346      70.723  35.638-116.242  1.00 38.30           N  
ANISOU 5965  N   GLN B 346     3178   8146   3230   -269     -5   1808       N  
ATOM   5966  CA  GLN B 346      69.940  35.547-117.466  1.00 44.64           C  
ANISOU 5966  CA  GLN B 346     3924   9128   3910   -285    -24   1846       C  
ATOM   5967  C   GLN B 346      69.376  36.901-117.877  1.00 47.37           C  
ANISOU 5967  C   GLN B 346     4305   9407   4285   -297   -170   2071       C  
ATOM   5968  O   GLN B 346      69.040  37.089-119.052  1.00 49.15           O  
ANISOU 5968  O   GLN B 346     4480   9753   4443   -349   -197   2140       O  
ATOM   5969  CB  GLN B 346      68.812  34.530-117.283  1.00 46.93           C  
ANISOU 5969  CB  GLN B 346     4199   9465   4167   -193     27   1659       C  
ATOM   5970  CG  GLN B 346      68.575  33.636-118.485  1.00 47.87           C  
ANISOU 5970  CG  GLN B 346     4238   9760   4191   -225     63   1539       C  
ATOM   5971  CD  GLN B 346      67.659  32.470-118.167  1.00 49.91           C  
ANISOU 5971  CD  GLN B 346     4493  10028   4444   -156    111   1331       C  
ATOM   5972  OE1 GLN B 346      66.820  32.551-117.269  1.00 47.90           O  
ANISOU 5972  OE1 GLN B 346     4271   9696   4233    -84    108   1315       O  
ATOM   5973  NE2 GLN B 346      67.821  31.374-118.900  1.00 53.31           N  
ANISOU 5973  NE2 GLN B 346     4888  10552   4817   -180    146   1170       N  
ATOM   5974  N   ILE B 347      69.266  37.840-116.936  1.00 46.36           N  
ANISOU 5974  N   ILE B 347     4264   9018   4331   -242   -265   2128       N  
ATOM   5975  CA  ILE B 347      68.845  39.199-117.236  1.00 42.76           C  
ANISOU 5975  CA  ILE B 347     3857   8436   3956   -242   -427   2337       C  
ATOM   5976  C   ILE B 347      70.005  40.192-117.169  1.00 45.46           C  
ANISOU 5976  C   ILE B 347     4245   8658   4369   -360   -498   2526       C  
ATOM   5977  O   ILE B 347      70.011  41.168-117.928  1.00 41.22           O  
ANISOU 5977  O   ILE B 347     3722   8104   3836   -436   -617   2755       O  
ATOM   5978  CB  ILE B 347      67.684  39.633-116.307  1.00 50.54           C  
ANISOU 5978  CB  ILE B 347     4901   9194   5107    -76   -505   2242       C  
ATOM   5979  CG1 ILE B 347      66.564  40.319-117.097  1.00 56.97           C  
ANISOU 5979  CG1 ILE B 347     5700  10029   5918    -22   -634   2376       C  
ATOM   5980  CG2 ILE B 347      68.156  40.526-115.159  1.00 57.58           C  
ANISOU 5980  CG2 ILE B 347     5893   9790   6196    -45   -577   2245       C  
ATOM   5981  CD1 ILE B 347      66.951  41.605-117.779  1.00 65.52           C  
ANISOU 5981  CD1 ILE B 347     6823  11029   7042   -107   -789   2662       C  
ATOM   5982  N   GLY B 348      70.997  39.964-116.309  1.00 42.86           N  
ANISOU 5982  N   GLY B 348     3938   8245   4103   -390   -434   2439       N  
ATOM   5983  CA  GLY B 348      72.224  40.735-116.378  1.00 45.79           C  
ANISOU 5983  CA  GLY B 348     4326   8565   4509   -536   -483   2615       C  
ATOM   5984  C   GLY B 348      72.246  42.031-115.604  1.00 47.98           C  
ANISOU 5984  C   GLY B 348     4718   8514   4999   -523   -639   2707       C  
ATOM   5985  O   GLY B 348      73.164  42.832-115.802  1.00 50.62           O  
ANISOU 5985  O   GLY B 348     5070   8793   5370   -667   -712   2895       O  
ATOM   5986  N   SER B 349      71.280  42.268-114.720  1.00 47.50           N  
ANISOU 5986  N   SER B 349     4730   8240   5080   -359   -694   2572       N  
ATOM   5987  CA  SER B 349      71.279  43.497-113.937  1.00 46.26           C  
ANISOU 5987  CA  SER B 349     4685   7757   5133   -327   -846   2619       C  
ATOM   5988  C   SER B 349      70.425  43.308-112.693  1.00 46.50           C  
ANISOU 5988  C   SER B 349     4764   7629   5276   -137   -832   2368       C  
ATOM   5989  O   SER B 349      69.383  42.651-112.745  1.00 51.21           O  
ANISOU 5989  O   SER B 349     5315   8330   5813    -17   -771   2243       O  
ATOM   5990  CB  SER B 349      70.751  44.679-114.751  1.00 53.45           C  
ANISOU 5990  CB  SER B 349     5636   8559   6112   -343  -1027   2857       C  
ATOM   5991  OG  SER B 349      70.623  45.821-113.927  1.00 59.65           O  
ANISOU 5991  OG  SER B 349     6538   8997   7127   -280  -1182   2859       O  
ATOM   5992  N   VAL B 350      70.871  43.902-111.583  1.00 44.34           N  
ANISOU 5992  N   VAL B 350     4575   7119   5154   -120   -889   2296       N  
ATOM   5993  CA  VAL B 350      70.085  43.869-110.351  1.00 46.01           C  
ANISOU 5993  CA  VAL B 350     4831   7186   5464     54   -885   2060       C  
ATOM   5994  C   VAL B 350      68.772  44.619-110.544  1.00 49.12           C  
ANISOU 5994  C   VAL B 350     5248   7458   5956    207  -1004   2066       C  
ATOM   5995  O   VAL B 350      67.693  44.120-110.202  1.00 39.50           O  
ANISOU 5995  O   VAL B 350     3988   6306   4714    356   -948   1899       O  
ATOM   5996  CB  VAL B 350      70.898  44.447-109.177  1.00 46.70           C  
ANISOU 5996  CB  VAL B 350     5007   7055   5683     27   -937   1986       C  
ATOM   5997  CG1 VAL B 350      70.013  44.640-107.946  1.00 47.17           C  
ANISOU 5997  CG1 VAL B 350     5115   6965   5843    211   -956   1748       C  
ATOM   5998  CG2 VAL B 350      72.094  43.554-108.852  1.00 40.73           C  
ANISOU 5998  CG2 VAL B 350     4208   6441   4827    -94   -810   1947       C  
ATOM   5999  N   THR B 351      68.848  45.828-111.107  1.00 46.96           N  
ANISOU 5999  N   THR B 351     5034   7009   5800    169  -1178   2269       N  
ATOM   6000  CA  THR B 351      67.652  46.638-111.313  1.00 51.26           C  
ANISOU 6000  CA  THR B 351     5601   7409   6467    328  -1320   2290       C  
ATOM   6001  C   THR B 351      66.627  45.909-112.175  1.00 53.45           C  
ANISOU 6001  C   THR B 351     5770   7938   6600    394  -1255   2300       C  
ATOM   6002  O   THR B 351      65.434  45.891-111.851  1.00 55.18           O  
ANISOU 6002  O   THR B 351     5957   8142   6865    578  -1267   2158       O  
ATOM   6003  CB  THR B 351      68.034  47.974-111.951  1.00 54.03           C  
ANISOU 6003  CB  THR B 351     6034   7537   6957    241  -1528   2558       C  
ATOM   6004  OG1 THR B 351      68.723  48.786-110.991  1.00 50.06           O  
ANISOU 6004  OG1 THR B 351     5643   6746   6633    219  -1619   2502       O  
ATOM   6005  CG2 THR B 351      66.797  48.707-112.447  1.00 48.52           C  
ANISOU 6005  CG2 THR B 351     5341   6729   6367    400  -1683   2628       C  
ATOM   6006  N   GLU B 352      67.075  45.290-113.269  1.00 46.94           N  
ANISOU 6006  N   GLU B 352     4878   7363   5593    244  -1184   2455       N  
ATOM   6007  CA  GLU B 352      66.151  44.567-114.131  1.00 48.06           C  
ANISOU 6007  CA  GLU B 352     4917   7758   5585    288  -1127   2457       C  
ATOM   6008  C   GLU B 352      65.660  43.277-113.486  1.00 44.85           C  
ANISOU 6008  C   GLU B 352     4444   7514   5083    368   -950   2190       C  
ATOM   6009  O   GLU B 352      64.511  42.875-113.709  1.00 46.99           O  
ANISOU 6009  O   GLU B 352     4644   7902   5308    475   -932   2112       O  
ATOM   6010  CB  GLU B 352      66.813  44.275-115.477  1.00 49.94           C  
ANISOU 6010  CB  GLU B 352     5101   8233   5639     99  -1100   2678       C  
ATOM   6011  CG  GLU B 352      67.188  45.518-116.257  1.00 55.35           C  
ANISOU 6011  CG  GLU B 352     5842   8795   6394     -5  -1283   2987       C  
ATOM   6012  CD  GLU B 352      67.846  45.197-117.583  1.00 60.58           C  
ANISOU 6012  CD  GLU B 352     6433   9743   6840   -205  -1242   3202       C  
ATOM   6013  OE1 GLU B 352      67.124  45.073-118.598  1.00 60.64           O  
ANISOU 6013  OE1 GLU B 352     6389   9897   6752   -203  -1242   3245       O  
ATOM   6014  OE2 GLU B 352      69.087  45.059-117.605  1.00 62.96           O  
ANISOU 6014  OE2 GLU B 352     6733  10106   7084   -368  -1174   3258       O  
ATOM   6015  N   ALA B 353      66.505  42.613-112.693  1.00 44.22           N  
ANISOU 6015  N   ALA B 353     4381   7447   4975    310   -828   2060       N  
ATOM   6016  CA  ALA B 353      66.062  41.412-111.989  1.00 38.72           C  
ANISOU 6016  CA  ALA B 353     3634   6875   4205    376   -676   1825       C  
ATOM   6017  C   ALA B 353      64.956  41.735-110.992  1.00 39.69           C  
ANISOU 6017  C   ALA B 353     3766   6872   4443    559   -710   1651       C  
ATOM   6018  O   ALA B 353      64.015  40.951-110.823  1.00 44.71           O  
ANISOU 6018  O   ALA B 353     4329   7647   5011    635   -629   1513       O  
ATOM   6019  CB  ALA B 353      67.245  40.744-111.286  1.00 35.70           C  
ANISOU 6019  CB  ALA B 353     3274   6501   3789    282   -566   1743       C  
ATOM   6020  N   ILE B 354      65.058  42.882-110.315  1.00 38.54           N  
ANISOU 6020  N   ILE B 354     3704   6470   4469    627   -829   1648       N  
ATOM   6021  CA  ILE B 354      63.993  43.317-109.415  1.00 43.40           C  
ANISOU 6021  CA  ILE B 354     4319   6974   5196    819   -870   1471       C  
ATOM   6022  C   ILE B 354      62.727  43.633-110.203  1.00 48.13           C  
ANISOU 6022  C   ILE B 354     4846   7631   5811    938   -952   1525       C  
ATOM   6023  O   ILE B 354      61.616  43.272-109.794  1.00 44.67           O  
ANISOU 6023  O   ILE B 354     4328   7285   5359   1072   -905   1363       O  
ATOM   6024  CB  ILE B 354      64.466  44.524-108.582  1.00 45.20           C  
ANISOU 6024  CB  ILE B 354     4661   6901   5614    865   -995   1443       C  
ATOM   6025  CG1 ILE B 354      65.524  44.095-107.559  1.00 45.21           C  
ANISOU 6025  CG1 ILE B 354     4714   6877   5588    773   -903   1334       C  
ATOM   6026  CG2 ILE B 354      63.294  45.204-107.893  1.00 47.23           C  
ANISOU 6026  CG2 ILE B 354     4909   7035   6003   1087  -1070   1275       C  
ATOM   6027  CD1 ILE B 354      66.120  45.249-106.783  1.00 40.39           C  
ANISOU 6027  CD1 ILE B 354     4218   5978   5149    787  -1029   1306       C  
ATOM   6028  N   GLN B 355      62.874  44.300-111.351  1.00 46.85           N  
ANISOU 6028  N   GLN B 355     4699   7431   5670    882  -1078   1765       N  
ATOM   6029  CA  GLN B 355      61.725  44.583-112.205  1.00 46.65           C  
ANISOU 6029  CA  GLN B 355     4600   7478   5648    984  -1170   1848       C  
ATOM   6030  C   GLN B 355      61.046  43.296-112.654  1.00 46.60           C  
ANISOU 6030  C   GLN B 355     4468   7788   5450    965  -1030   1772       C  
ATOM   6031  O   GLN B 355      59.819  43.164-112.567  1.00 48.08           O  
ANISOU 6031  O   GLN B 355     4565   8058   5644   1106  -1036   1667       O  
ATOM   6032  CB  GLN B 355      62.161  45.410-113.414  1.00 50.66           C  
ANISOU 6032  CB  GLN B 355     5150   7922   6177    884  -1325   2155       C  
ATOM   6033  CG  GLN B 355      62.599  46.822-113.075  1.00 61.03           C  
ANISOU 6033  CG  GLN B 355     6586   8886   7715    915  -1508   2253       C  
ATOM   6034  CD  GLN B 355      63.170  47.557-114.272  1.00 67.94           C  
ANISOU 6034  CD  GLN B 355     7506   9713   8593    767  -1654   2592       C  
ATOM   6035  OE1 GLN B 355      63.500  46.946-115.290  1.00 73.15           O  
ANISOU 6035  OE1 GLN B 355     8109  10628   9057    613  -1589   2742       O  
ATOM   6036  NE2 GLN B 355      63.288  48.875-114.157  1.00 67.28           N  
ANISOU 6036  NE2 GLN B 355     7526   9307   8728    808  -1858   2712       N  
ATOM   6037  N   ALA B 356      61.833  42.331-113.140  1.00 40.47           N  
ANISOU 6037  N   ALA B 356     3678   7194   4505    792   -908   1814       N  
ATOM   6038  CA  ALA B 356      61.265  41.064-113.591  1.00 41.88           C  
ANISOU 6038  CA  ALA B 356     3751   7654   4509    759   -784   1731       C  
ATOM   6039  C   ALA B 356      60.523  40.348-112.472  1.00 48.04           C  
ANISOU 6039  C   ALA B 356     4483   8473   5296    857   -675   1479       C  
ATOM   6040  O   ALA B 356      59.516  39.676-112.725  1.00 50.71           O  
ANISOU 6040  O   ALA B 356     4718   8994   5554    894   -631   1402       O  
ATOM   6041  CB  ALA B 356      62.364  40.164-114.154  1.00 43.13           C  
ANISOU 6041  CB  ALA B 356     3912   7965   4509    572   -671   1781       C  
ATOM   6042  N   CYS B 357      61.001  40.478-111.232  1.00 49.57           N  
ANISOU 6042  N   CYS B 357     4744   8513   5576    886   -635   1354       N  
ATOM   6043  CA  CYS B 357      60.331  39.830-110.111  1.00 42.65           C  
ANISOU 6043  CA  CYS B 357     3822   7694   4691    963   -532   1129       C  
ATOM   6044  C   CYS B 357      59.058  40.569-109.716  1.00 44.17           C  
ANISOU 6044  C   CYS B 357     3953   7843   4987   1158   -611   1039       C  
ATOM   6045  O   CYS B 357      58.025  39.938-109.470  1.00 40.63           O  
ANISOU 6045  O   CYS B 357     3397   7561   4480   1214   -542    913       O  
ATOM   6046  CB  CYS B 357      61.279  39.731-108.919  1.00 41.47           C  
ANISOU 6046  CB  CYS B 357     3760   7420   4578    924   -469   1032       C  
ATOM   6047  SG  CYS B 357      60.513  39.030-107.445  1.00 45.66           S  
ANISOU 6047  SG  CYS B 357     4239   8028   5081   1002   -350    778       S  
ATOM   6048  N   LYS B 358      59.116  41.902-109.644  1.00 44.88           N  
ANISOU 6048  N   LYS B 358     4105   7708   5239   1262   -760   1098       N  
ATOM   6049  CA  LYS B 358      57.925  42.674-109.312  1.00 49.76           C  
ANISOU 6049  CA  LYS B 358     4659   8271   5977   1474   -850   1002       C  
ATOM   6050  C   LYS B 358      56.865  42.575-110.402  1.00 53.61           C  
ANISOU 6050  C   LYS B 358     5026   8926   6418   1525   -907   1094       C  
ATOM   6051  O   LYS B 358      55.671  42.716-110.115  1.00 49.39           O  
ANISOU 6051  O   LYS B 358     4379   8463   5924   1688   -924    972       O  
ATOM   6052  CB  LYS B 358      58.294  44.136-109.058  1.00 55.14           C  
ANISOU 6052  CB  LYS B 358     5448   8637   6865   1574  -1019   1048       C  
ATOM   6053  CG  LYS B 358      58.585  44.453-107.599  1.00 64.08           C  
ANISOU 6053  CG  LYS B 358     6644   9623   8082   1646   -984    835       C  
ATOM   6054  CD  LYS B 358      57.445  43.969-106.707  1.00 69.10           C  
ANISOU 6054  CD  LYS B 358     7153  10431   8670   1785   -880    585       C  
ATOM   6055  CE  LYS B 358      57.645  44.356-105.246  1.00 67.97           C  
ANISOU 6055  CE  LYS B 358     7062  10171   8593   1869   -851    358       C  
ATOM   6056  NZ  LYS B 358      57.377  45.801-104.994  1.00 69.17           N  
ANISOU 6056  NZ  LYS B 358     7263  10055   8965   2066  -1026    296       N  
ATOM   6057  N   LEU B 359      57.275  42.339-111.651  1.00 54.13           N  
ANISOU 6057  N   LEU B 359     5100   9077   6390   1387   -936   1301       N  
ATOM   6058  CA  LEU B 359      56.299  42.123-112.714  1.00 52.54           C  
ANISOU 6058  CA  LEU B 359     4778   9072   6111   1411   -985   1386       C  
ATOM   6059  C   LEU B 359      55.537  40.823-112.491  1.00 45.70           C  
ANISOU 6059  C   LEU B 359     3788   8475   5102   1382   -831   1220       C  
ATOM   6060  O   LEU B 359      54.315  40.776-112.666  1.00 44.09           O  
ANISOU 6060  O   LEU B 359     3451   8408   4893   1490   -861   1166       O  
ATOM   6061  CB  LEU B 359      56.998  42.120-114.079  1.00 55.17           C  
ANISOU 6061  CB  LEU B 359     5151   9466   6344   1249  -1041   1637       C  
ATOM   6062  CG  LEU B 359      56.192  42.257-115.383  1.00 65.93           C  
ANISOU 6062  CG  LEU B 359     6420  10992   7639   1262  -1151   1799       C  
ATOM   6063  CD1 LEU B 359      55.516  40.956-115.794  1.00 70.02           C  
ANISOU 6063  CD1 LEU B 359     6811  11826   7969   1196  -1030   1700       C  
ATOM   6064  CD2 LEU B 359      55.164  43.373-115.287  1.00 61.68           C  
ANISOU 6064  CD2 LEU B 359     5836  10321   7280   1484  -1325   1819       C  
ATOM   6065  N   ALA B 360      56.239  39.760-112.092  1.00 42.66           N  
ANISOU 6065  N   ALA B 360     3440   8163   4607   1236   -675   1140       N  
ATOM   6066  CA  ALA B 360      55.574  38.477-111.889  1.00 41.87           C  
ANISOU 6066  CA  ALA B 360     3236   8294   4380   1182   -540    999       C  
ATOM   6067  C   ALA B 360      54.660  38.512-110.670  1.00 45.32           C  
ANISOU 6067  C   ALA B 360     3594   8747   4877   1317   -493    801       C  
ATOM   6068  O   ALA B 360      53.523  38.027-110.727  1.00 42.93           O  
ANISOU 6068  O   ALA B 360     3151   8640   4521   1353   -463    721       O  
ATOM   6069  CB  ALA B 360      56.610  37.362-111.752  1.00 37.10           C  
ANISOU 6069  CB  ALA B 360     2700   7728   3667   1001   -405    972       C  
ATOM   6070  N   GLN B 361      55.137  39.083-109.559  1.00 43.21           N  
ANISOU 6070  N   GLN B 361     3409   8297   4711   1386   -486    713       N  
ATOM   6071  CA  GLN B 361      54.327  39.125-108.347  1.00 47.57           C  
ANISOU 6071  CA  GLN B 361     3882   8893   5298   1511   -429    510       C  
ATOM   6072  C   GLN B 361      53.085  39.992-108.522  1.00 46.47           C  
ANISOU 6072  C   GLN B 361     3620   8781   5256   1720   -538    472       C  
ATOM   6073  O   GLN B 361      52.053  39.723-107.895  1.00 42.74           O  
ANISOU 6073  O   GLN B 361     3009   8473   4759   1805   -476    313       O  
ATOM   6074  CB  GLN B 361      55.169  39.623-107.169  1.00 39.54           C  
ANISOU 6074  CB  GLN B 361     2986   7678   4359   1539   -411    420       C  
ATOM   6075  CG  GLN B 361      56.147  38.582-106.643  1.00 39.04           C  
ANISOU 6075  CG  GLN B 361     3002   7642   4191   1356   -279    401       C  
ATOM   6076  CD  GLN B 361      57.240  39.173-105.766  1.00 43.71           C  
ANISOU 6076  CD  GLN B 361     3733   8018   4859   1356   -295    370       C  
ATOM   6077  OE1 GLN B 361      57.605  40.341-105.904  1.00 44.44           O  
ANISOU 6077  OE1 GLN B 361     3899   7902   5083   1437   -420    424       O  
ATOM   6078  NE2 GLN B 361      57.775  38.359-104.860  1.00 40.46           N  
ANISOU 6078  NE2 GLN B 361     3357   7651   4366   1254   -179    291       N  
ATOM   6079  N   GLU B 362      53.157  41.026-109.365  1.00 46.37           N  
ANISOU 6079  N   GLU B 362     3646   8617   5354   1804   -705    623       N  
ATOM   6080  CA  GLU B 362      51.988  41.869-109.597  1.00 51.45           C  
ANISOU 6080  CA  GLU B 362     4170   9270   6109   2019   -832    602       C  
ATOM   6081  C   GLU B 362      50.869  41.096-110.277  1.00 50.45           C  
ANISOU 6081  C   GLU B 362     3877   9427   5866   1988   -796    603       C  
ATOM   6082  O   GLU B 362      49.689  41.417-110.094  1.00 50.57           O  
ANISOU 6082  O   GLU B 362     3789   9486   5940   2120   -818    494       O  
ATOM   6083  CB  GLU B 362      52.360  43.084-110.445  1.00 61.78           C  
ANISOU 6083  CB  GLU B 362     5571  10340   7561   2088  -1036    804       C  
ATOM   6084  CG  GLU B 362      52.914  44.258-109.666  1.00 74.85           C  
ANISOU 6084  CG  GLU B 362     7354  11674   9412   2212  -1129    751       C  
ATOM   6085  CD  GLU B 362      53.237  45.438-110.562  1.00 90.87           C  
ANISOU 6085  CD  GLU B 362     9476  13457  11594   2259  -1349    981       C  
ATOM   6086  OE1 GLU B 362      53.356  45.240-111.791  1.00 93.58           O  
ANISOU 6086  OE1 GLU B 362     9815  13890  11852   2141  -1404   1209       O  
ATOM   6087  OE2 GLU B 362      53.367  46.565-110.039  1.00 96.53           O  
ANISOU 6087  OE2 GLU B 362    10271  13892  12512   2408  -1474    934       O  
ATOM   6088  N   ASN B 363      51.218  40.085-111.065  1.00 49.21           N  
ANISOU 6088  N   ASN B 363     3741   9405   5551   1775   -726    703       N  
ATOM   6089  CA  ASN B 363      50.241  39.279-111.777  1.00 48.49           C  
ANISOU 6089  CA  ASN B 363     3563   9517   5345   1680   -678    692       C  
ATOM   6090  C   ASN B 363      49.873  38.008-111.026  1.00 48.77           C  
ANISOU 6090  C   ASN B 363     3550   9723   5257   1559   -496    525       C  
ATOM   6091  O   ASN B 363      49.241  37.120-111.607  1.00 43.63           O  
ANISOU 6091  O   ASN B 363     2847   9239   4490   1437   -446    520       O  
ATOM   6092  CB  ASN B 363      50.769  38.947-113.171  1.00 48.23           C  
ANISOU 6092  CB  ASN B 363     3585   9532   5210   1523   -722    886       C  
ATOM   6093  CG  ASN B 363      50.916  40.181-114.038  1.00 55.89           C  
ANISOU 6093  CG  ASN B 363     4600  10352   6285   1614   -914   1081       C  
ATOM   6094  OD1 ASN B 363      50.027  41.033-114.076  1.00 64.35           O  
ANISOU 6094  OD1 ASN B 363     5609  11360   7480   1784  -1029   1074       O  
ATOM   6095  ND2 ASN B 363      52.042  40.290-114.732  1.00 50.46           N  
ANISOU 6095  ND2 ASN B 363     4020   9600   5551   1497   -953   1259       N  
ATOM   6096  N   GLY B 364      50.245  37.902-109.752  1.00 42.88           N  
ANISOU 6096  N   GLY B 364     2829   8935   4531   1582   -406    395       N  
ATOM   6097  CA  GLY B 364      49.876  36.739-108.973  1.00 42.00           C  
ANISOU 6097  CA  GLY B 364     2689   8965   4304   1454   -247    259       C  
ATOM   6098  C   GLY B 364      50.734  35.521-109.201  1.00 45.52           C  
ANISOU 6098  C   GLY B 364     3215   9452   4630   1234   -157    310       C  
ATOM   6099  O   GLY B 364      50.325  34.412-108.844  1.00 44.73           O  
ANISOU 6099  O   GLY B 364     3104   9462   4430   1097    -54    234       O  
ATOM   6100  N   TRP B 365      51.911  35.688-109.794  1.00 45.95           N  
ANISOU 6100  N   TRP B 365     3353   9411   4696   1193   -203    440       N  
ATOM   6101  CA  TRP B 365      52.832  34.579-109.964  1.00 41.36           C  
ANISOU 6101  CA  TRP B 365     2845   8852   4017   1004   -118    470       C  
ATOM   6102  C   TRP B 365      53.646  34.353-108.699  1.00 39.95           C  
ANISOU 6102  C   TRP B 365     2733   8587   3859    980    -31    396       C  
ATOM   6103  O   TRP B 365      53.874  35.270-107.905  1.00 39.17           O  
ANISOU 6103  O   TRP B 365     2680   8349   3853   1098    -59    355       O  
ATOM   6104  CB  TRP B 365      53.797  34.841-111.120  1.00 39.95           C  
ANISOU 6104  CB  TRP B 365     2732   8620   3827    955   -194    635       C  
ATOM   6105  CG  TRP B 365      53.233  34.642-112.480  1.00 41.92           C  
ANISOU 6105  CG  TRP B 365     2935   8996   3999    904   -250    716       C  
ATOM   6106  CD1 TRP B 365      51.915  34.645-112.840  1.00 45.55           C  
ANISOU 6106  CD1 TRP B 365     3304   9562   4440    943   -277    678       C  
ATOM   6107  CD2 TRP B 365      53.976  34.401-113.677  1.00 45.28           C  
ANISOU 6107  CD2 TRP B 365     3406   9461   4339    795   -279    840       C  
ATOM   6108  NE1 TRP B 365      51.795  34.425-114.192  1.00 39.61           N  
ANISOU 6108  NE1 TRP B 365     2541   8910   3599    865   -326    774       N  
ATOM   6109  CE2 TRP B 365      53.046  34.271-114.729  1.00 45.54           C  
ANISOU 6109  CE2 TRP B 365     3377   9627   4301    772   -324    870       C  
ATOM   6110  CE3 TRP B 365      55.342  34.284-113.964  1.00 41.49           C  
ANISOU 6110  CE3 TRP B 365     303