CNRS Nantes University UFIP UFIP
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***  CELL ADHESION 14-JUL-16 5KVM  ***

elNémo ID: 210322194818105268

Job options:

ID        	=	 210322194818105268
JOBID     	=	 CELL ADHESION 14-JUL-16 5KVM
USERID    	=	 unknown
PRIVAT    	=	 0

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

DOPROJMODS	=	 0
DORMSD    	=	 0

NRBL      	=	 0
CUTOFF    	=	 0
CAONLY    	=	 0


Input data for this run:


HEADER    CELL ADHESION                           14-JUL-16   5KVM              
TITLE     EXTRACELLULAR REGION OF MOUSE GPR56/ADGRG1 IN COMPLEX WITH FN3        
TITLE    2 MONOBODY                                                             
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: ADHESION G-PROTEIN COUPLED RECEPTOR G1;                    
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: N-TERMINAL FRAGMENT (UNP RESIDUES 28-382);                 
COMPND   5 SYNONYM: G-PROTEIN COUPLED RECEPTOR 56,SERPENTINE RECEPTOR CYT28;    
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MOL_ID: 2;                                                           
COMPND   8 MOLECULE: ADHESION G-PROTEIN COUPLED RECEPTOR G1;                    
COMPND   9 CHAIN: B;                                                            
COMPND  10 FRAGMENT: C-TERMINAL FRAGMENT (UNP RESIDUES 383-391);                
COMPND  11 SYNONYM: G-PROTEIN COUPLED RECEPTOR 56,SERPENTINE RECEPTOR CYT28;    
COMPND  12 ENGINEERED: YES;                                                     
COMPND  13 MOL_ID: 3;                                                           
COMPND  14 MOLECULE: FN3 MONOBODY ALPHA5;                                       
COMPND  15 CHAIN: C;                                                            
COMPND  16 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: MUS MUSCULUS;                                   
SOURCE   3 ORGANISM_COMMON: MOUSE;                                              
SOURCE   4 ORGANISM_TAXID: 10090;                                               
SOURCE   5 GENE: ADGRG1, CYT28, GPR56;                                          
SOURCE   6 EXPRESSION_SYSTEM: TRICHOPLUSIA NI;                                  
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 7111;                                       
SOURCE   8 EXPRESSION_SYSTEM_CELL: HIGH FIVE;                                   
SOURCE   9 MOL_ID: 2;                                                           
SOURCE  10 ORGANISM_SCIENTIFIC: MUS MUSCULUS;                                   
SOURCE  11 ORGANISM_COMMON: MOUSE;                                              
SOURCE  12 ORGANISM_TAXID: 10090;                                               
SOURCE  13 GENE: ADGRG1, CYT28, GPR56;                                          
SOURCE  14 EXPRESSION_SYSTEM: TRICHOPLUSIA NI;                                  
SOURCE  15 EXPRESSION_SYSTEM_TAXID: 7111;                                       
SOURCE  16 EXPRESSION_SYSTEM_CELL: HIGH FIVE;                                   
SOURCE  17 MOL_ID: 3;                                                           
SOURCE  18 ORGANISM_SCIENTIFIC: SYNTHETIC CONSTRUCT;                            
SOURCE  19 ORGANISM_TAXID: 32630;                                               
SOURCE  20 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  21 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE  22 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)                                  
KEYWDS    ADHESION-GPCR, MONOBODY, PLL, GAIN, CELL ADHESION                     
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    G.S.SALZMAN,C.DING,S.KOIDE,D.ARAC                                     
REVDAT   5   29-JUL-20 5KVM    1       COMPND REMARK HETNAM LINK                
REVDAT   5 2                   1       SITE   ATOM                              
REVDAT   4   25-DEC-19 5KVM    1       REMARK                                   
REVDAT   3   18-APR-18 5KVM    1       JRNL                                     
REVDAT   2   27-SEP-17 5KVM    1       JRNL   REMARK                            
REVDAT   1   28-SEP-16 5KVM    0                                                
JRNL        AUTH   G.S.SALZMAN,S.D.ACKERMAN,C.DING,A.KOIDE,K.LEON,R.LUO,        
JRNL        AUTH 2 H.M.STOVEKEN,C.G.FERNANDEZ,G.G.TALL,X.PIAO,K.R.MONK,S.KOIDE, 
JRNL        AUTH 3 D.ARAC                                                       
JRNL        TITL   STRUCTURAL BASIS FOR REGULATION OF GPR56/ADGRG1 BY ITS       
JRNL        TITL 2 ALTERNATIVELY SPLICED EXTRACELLULAR DOMAINS.                 
JRNL        REF    NEURON                        V.  91  1292 2016              
JRNL        REFN                   ISSN 1097-4199                               
JRNL        PMID   27657451                                                     
JRNL        DOI    10.1016/J.NEURON.2016.08.022                                 
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.45 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (1.10_2155: ???)                              
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 : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.45                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 46.39                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.350                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 22242                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.217                           
REMARK   3   R VALUE            (WORKING SET) : 0.215                           
REMARK   3   FREE R VALUE                     : 0.263                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.220                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1162                            
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 46.3994 -  4.8958    1.00     2708   143  0.1982 0.2221        
REMARK   3     2  4.8958 -  3.8866    1.00     2624   162  0.1838 0.2410        
REMARK   3     3  3.8866 -  3.3955    1.00     2659   136  0.2225 0.2834        
REMARK   3     4  3.3955 -  3.0851    1.00     2624   145  0.2242 0.2792        
REMARK   3     5  3.0851 -  2.8640    1.00     2602   148  0.2501 0.3267        
REMARK   3     6  2.8640 -  2.6952    1.00     2629   144  0.2542 0.3397        
REMARK   3     7  2.6952 -  2.5602    1.00     2617   140  0.2740 0.3091        
REMARK   3     8  2.5602 -  2.4488    0.99     2617   144  0.2927 0.3463        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.380            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 30.660           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
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      :  0.003           3783                                  
REMARK   3   ANGLE     :  0.611           5182                                  
REMARK   3   CHIRALITY :  0.043            601                                  
REMARK   3   PLANARITY :  0.004            656                                  
REMARK   3   DIHEDRAL  : 13.315           2237                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 8                                          
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 28 THROUGH 175 )                  
REMARK   3    ORIGIN FOR THE GROUP (A):  35.0126  17.3927  19.4839              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6885 T22:   0.6684                                     
REMARK   3      T33:   0.5559 T12:   0.2151                                     
REMARK   3      T13:  -0.0055 T23:   0.0083                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   7.0355 L22:   4.7209                                     
REMARK   3      L33:   4.5864 L12:  -0.7876                                     
REMARK   3      L13:  -1.1051 L23:   0.9204                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0373 S12:   0.6548 S13:  -0.0504                       
REMARK   3      S21:   0.1365 S22:  -0.0729 S23:   0.3793                       
REMARK   3      S31:  -0.0629 S32:  -0.9045 S33:   0.0485                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 176 THROUGH 382 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  50.6748  12.5054 -15.9711              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.9274 T22:   0.4696                                     
REMARK   3      T33:   0.5396 T12:   0.3188                                     
REMARK   3      T13:  -0.1937 T23:  -0.0854                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.5490 L22:   2.4503                                     
REMARK   3      L33:   5.4765 L12:   0.1498                                     
REMARK   3      L13:   0.5413 L23:   1.2037                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1029 S12:   0.3214 S13:   0.2804                       
REMARK   3      S21:  -0.4666 S22:  -0.3331 S23:   0.3630                       
REMARK   3      S31:  -1.0900 S32:  -0.7760 S33:   0.2165                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 383 THROUGH 391 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  55.7722  15.4427 -24.6810              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.2221 T22:   0.5103                                     
REMARK   3      T33:   0.6703 T12:   0.2346                                     
REMARK   3      T13:  -0.2258 T23:  -0.0478                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.9618 L22:   3.5443                                     
REMARK   3      L33:   7.0465 L12:  -0.1495                                     
REMARK   3      L13:  -2.3020 L23:  -0.8512                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.4870 S12:   0.5650 S13:  -0.2391                       
REMARK   3      S21:  -0.5418 S22:  -0.2884 S23:  -0.1913                       
REMARK   3      S31:  -1.7588 S32:  -0.1374 S33:  -0.0625                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: CHAIN 'C' AND (RESID 5 THROUGH 9 )                     
REMARK   3    ORIGIN FOR THE GROUP (A):  71.5185   7.2707  11.6813              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.9129 T22:   0.7348                                     
REMARK   3      T33:   0.9064 T12:  -0.0923                                     
REMARK   3      T13:   0.0979 T23:   0.6588                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.7600 L22:   4.9559                                     
REMARK   3      L33:   7.2750 L12:  -4.6158                                     
REMARK   3      L13:   1.7702 L23:   0.0337                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.5855 S12:   0.3476 S13:   0.2598                       
REMARK   3      S21:  -2.0944 S22:   0.8379 S23:   0.6415                       
REMARK   3      S31:   0.3367 S32:  -0.1174 S33:  -0.1167                       
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION: CHAIN 'C' AND (RESID 10 THROUGH 40 )                   
REMARK   3    ORIGIN FOR THE GROUP (A):  67.8725  12.2997  20.3869              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.9115 T22:   0.3851                                     
REMARK   3      T33:   0.4853 T12:  -0.0586                                     
REMARK   3      T13:  -0.1261 T23:  -0.0094                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.0852 L22:   5.6740                                     
REMARK   3      L33:   6.1394 L12:   0.4313                                     
REMARK   3      L13:  -2.7213 L23:  -3.4267                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1665 S12:  -0.4888 S13:   0.1252                       
REMARK   3      S21:   0.4259 S22:  -0.1323 S23:   0.0630                       
REMARK   3      S31:  -1.0742 S32:   0.6129 S33:   0.2897                       
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    SELECTION: CHAIN 'C' AND (RESID 41 THROUGH 54 )                   
REMARK   3    ORIGIN FOR THE GROUP (A):  55.1252  11.8808  20.8186              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.9964 T22:   0.3448                                     
REMARK   3      T33:   0.5865 T12:   0.0716                                     
REMARK   3      T13:  -0.0339 T23:  -0.0948                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.1246 L22:   1.5763                                     
REMARK   3      L33:   0.8735 L12:  -0.4077                                     
REMARK   3      L13:  -0.5343 L23:  -0.9947                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.3351 S12:  -0.2492 S13:  -0.8920                       
REMARK   3      S21:   0.4297 S22:   0.3397 S23:   0.1122                       
REMARK   3      S31:  -1.2428 S32:  -0.3034 S33:  -0.0689                       
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    SELECTION: CHAIN 'C' AND (RESID 55 THROUGH 78 )                   
REMARK   3    ORIGIN FOR THE GROUP (A):  63.5589  10.9936  23.5303              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.9293 T22:   0.3492                                     
REMARK   3      T33:   0.5102 T12:   0.0023                                     
REMARK   3      T13:  -0.0062 T23:  -0.0263                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.2438 L22:   1.5331                                     
REMARK   3      L33:   5.9118 L12:   0.3110                                     
REMARK   3      L13:  -3.2123 L23:  -1.8790                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1512 S12:  -0.5726 S13:  -0.3636                       
REMARK   3      S21:   0.6312 S22:  -0.0934 S23:   0.0166                       
REMARK   3      S31:  -0.5900 S32:   0.6674 S33:  -0.0283                       
REMARK   3   TLS GROUP : 8                                                      
REMARK   3    SELECTION: CHAIN 'C' AND (RESID 79 THROUGH 99 )                   
REMARK   3    ORIGIN FOR THE GROUP (A):  63.7790  10.9546  10.4944              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.7636 T22:   0.2350                                     
REMARK   3      T33:   0.4982 T12:  -0.0229                                     
REMARK   3      T13:  -0.0720 T23:  -0.0383                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.2092 L22:   3.0281                                     
REMARK   3      L33:   0.2069 L12:  -0.7460                                     
REMARK   3      L13:  -0.1401 L23:   0.1536                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0963 S12:  -0.0016 S13:  -0.0604                       
REMARK   3      S21:   0.3238 S22:  -0.2669 S23:   0.0373                       
REMARK   3      S31:  -1.2850 S32:   0.0264 S33:   0.2007                       
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 5KVM COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 20-JUL-16.                  
REMARK 100 THE DEPOSITION ID IS D_1000222801.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 13-AUG-14                          
REMARK 200  TEMPERATURE           (KELVIN) : 120                                
REMARK 200  PH                             : 4.6                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 23-ID-B                            
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.033                              
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARMOSAIC 300 MM CCD               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 22286                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.449                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 46.391                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY                : 5.700                              
REMARK 200  R MERGE                    (I) : 0.03500                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 19.7500                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.45                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.49                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.5                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 5.70                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.42100                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : 1.500                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD                          
REMARK 200 SOFTWARE USED: CRANK2                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 58.20                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.94                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 80 MM SODIUM ACETATE PH 4.6, 19.5%       
REMARK 280  GLYCEROL, 16.9% PEG 600, 7.6% PEG 1000, VAPOR DIFFUSION, SITTING    
REMARK 280  DROP, TEMPERATURE 298K                                              
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 65                             
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z+2/3                                            
REMARK 290       3555   -X+Y,-X,Z+1/3                                           
REMARK 290       4555   -X,-Y,Z+1/2                                             
REMARK 290       5555   Y,-X+Y,Z+1/6                                            
REMARK 290       6555   X-Y,X,Z+5/6                                             
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 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       48.56667            
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       24.28333            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       36.42500            
REMARK 290   SMTRY1   5  0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   5 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000       12.14167            
REMARK 290   SMTRY1   6  0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   6  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       60.70833            
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: TRIMERIC                          
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC                   
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 6620 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 22360 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -7.0 KCAL/MOL                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E                         
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 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     ARG A  79    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS A 107    CG   CD   CE   NZ                                   
REMARK 470     VAL A 168    CG1  CG2                                            
REMARK 470     LYS A 195    CG   CD   CE   NZ                                   
REMARK 470     LEU A 246    CG   CD1  CD2                                       
REMARK 470     GLU A 247    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 255    CG   CD   CE   NZ                                   
REMARK 470     GLU A 256    CG   CD   OE1  OE2                                  
REMARK 470     GLU A 258    CG   CD   OE1  OE2                                  
REMARK 470     GLN A 259    CG   CD   OE1  NE2                                  
REMARK 470     SER A 260    OG                                                  
REMARK 470     GLU A 261    CG   CD   OE1  OE2                                  
REMARK 470     ARG A 280    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG A 281    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG A 282    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ASP A 283    CG   OD1  OD2                                       
REMARK 470     ASP A 284    CG   OD1  OD2                                       
REMARK 470     LYS A 302    CG   CD   CE   NZ                                   
REMARK 470     LYS A 340    CG   CD   CE   NZ                                   
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   OE2  GLU A   213     O    HOH A  1001              2.18            
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    SER A 160     -165.87   -129.39                                   
REMARK 500    GLN A 259       57.89    -90.55                                   
REMARK 500    GLU A 261       -9.56     84.37                                   
REMARK 500    ARG A 282       -9.04     85.61                                   
REMARK 500    ASN A 303       -2.28     77.36                                   
REMARK 500    ASN A 380       31.52    -92.98                                   
REMARK 500    ALA C  28       37.93    -81.68                                   
REMARK 500    TYR C  88      -40.16     65.72                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
DBREF  5KVM A   28   382  UNP    Q8K209   AGRG1_MOUSE     28    382             
DBREF  5KVM B  383   391  UNP    Q8K209   AGRG1_MOUSE    383    391             
DBREF  5KVM C    5    99  PDB    5KVM     5KVM             5     99             
SEQRES   1 A  355  PRO ARG GLU ASP PHE ARG PHE CYS GLY GLN ARG ASN GLN          
SEQRES   2 A  355  THR GLN GLN SER THR LEU HIS TYR ASP GLN SER SER GLU          
SEQRES   3 A  355  PRO HIS ILE PHE VAL TRP ASN THR GLU GLU THR LEU THR          
SEQRES   4 A  355  ILE ARG ALA PRO PHE LEU ALA ALA PRO ASP ILE PRO ARG          
SEQRES   5 A  355  PHE PHE PRO GLU PRO ARG GLY LEU TYR HIS PHE CYS LEU          
SEQRES   6 A  355  TYR TRP SER ARG HIS THR GLY ARG LEU HIS LEU ARG TYR          
SEQRES   7 A  355  GLY LYS HIS ASP TYR LEU LEU SER SER GLN ALA SER ARG          
SEQRES   8 A  355  LEU LEU CYS PHE GLN LYS GLN GLU GLN SER LEU LYS GLN          
SEQRES   9 A  355  GLY ALA PRO LEU ILE ALA THR SER VAL SER SER TRP GLN          
SEQRES  10 A  355  ILE PRO GLN ASN THR SER LEU PRO GLY ALA PRO SER PHE          
SEQRES  11 A  355  ILE PHE SER PHE HIS ASN ALA PRO HIS LYS VAL SER HIS          
SEQRES  12 A  355  ASN ALA SER VAL ASP MET CYS ASP LEU LYS LYS GLU LEU          
SEQRES  13 A  355  GLN GLN LEU SER ARG TYR LEU GLN HIS PRO GLN LYS ALA          
SEQRES  14 A  355  ALA LYS ARG PRO THR ALA ALA PHE ILE SER GLN GLN LEU          
SEQRES  15 A  355  GLN SER LEU GLU SER LYS LEU THR SER VAL SER PHE LEU          
SEQRES  16 A  355  GLY ASP THR LEU SER PHE GLU GLU ASP ARG VAL ASN ALA          
SEQRES  17 A  355  THR VAL TRP LYS LEU PRO PRO THR ALA GLY LEU GLU ASP          
SEQRES  18 A  355  LEU HIS ILE HIS SER GLN LYS GLU GLU GLU GLN SER GLU          
SEQRES  19 A  355  VAL GLN ALA TYR SER LEU LEU LEU PRO ARG ALA VAL PHE          
SEQRES  20 A  355  GLN GLN THR ARG GLY ARG ARG ARG ASP ASP ALA LYS ARG          
SEQRES  21 A  355  LEU LEU VAL VAL ASP PHE SER SER GLN ALA LEU PHE GLN          
SEQRES  22 A  355  ASP LYS ASN SER SER GLN VAL LEU GLY GLU LYS VAL LEU          
SEQRES  23 A  355  GLY ILE VAL VAL GLN ASN THR LYS VAL THR ASN LEU SER          
SEQRES  24 A  355  ASP PRO VAL VAL LEU THR PHE GLN HIS GLN PRO GLN PRO          
SEQRES  25 A  355  LYS ASN VAL THR LEU GLN CYS VAL PHE TRP VAL GLU ASP          
SEQRES  26 A  355  PRO ALA SER SER SER THR GLY SER TRP SER SER ALA GLY          
SEQRES  27 A  355  CYS GLU THR VAL SER ARG ASP THR GLN THR SER CYS LEU          
SEQRES  28 A  355  CYS ASN HIS LEU                                              
SEQRES   1 B    9  THR TYR PHE ALA VAL LEU MET VAL SER                          
SEQRES   1 C   95  SER VAL PRO THR LYS LEU GLU VAL VAL ALA ALA THR PRO          
SEQRES   2 C   95  THR SER LEU LEU ILE SER TRP ASP ALA PRO ALA VAL THR          
SEQRES   3 C   95  VAL ASP HIS TYR VAL ILE THR TYR GLY GLU THR GLY GLY          
SEQRES   4 C   95  SER PRO TRP SER TRP GLN GLU PHE GLU VAL PRO GLY SER          
SEQRES   5 C   95  LYS SER THR ALA THR ILE SER GLY LEU LYS PRO GLY VAL          
SEQRES   6 C   95  ASP TYR THR ILE THR VAL TYR ALA SER SER PHE ASP TRP          
SEQRES   7 C   95  THR ILE PHE PRO ASN TYR TYR SER SER PRO ILE SER ILE          
SEQRES   8 C   95  ASN TYR ARG THR                                              
HET    NAG  D   1      14                                                       
HET    NAG  D   2      14                                                       
HET    BMA  D   3      11                                                       
HET    BMA  D   4      11                                                       
HET    NAG  E   1      14                                                       
HET    NAG  E   2      14                                                       
HET    NAG  A 900      14                                                       
HET    GOL  A 907       6                                                       
HETNAM     NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE                         
HETNAM     BMA BETA-D-MANNOPYRANOSE                                             
HETNAM     GOL GLYCEROL                                                         
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL                                    
FORMUL   4  NAG    5(C8 H15 N O6)                                               
FORMUL   4  BMA    2(C6 H12 O6)                                                 
FORMUL   7  GOL    C3 H8 O3                                                     
FORMUL   8  HOH   *24(H2 O)                                                     
HELIX    1 AA1 ASP A  175  HIS A  192  1                                  18    
HELIX    2 AA2 PRO A  193  ALA A  196  5                                   4    
HELIX    3 AA3 THR A  201  VAL A  219  1                                  19    
HELIX    4 AA4 PRO A  241  GLU A  247  5                                   7    
HELIX    5 AA5 PRO A  270  GLN A  275  1                                   6    
HELIX    6 AA6 VAL A  307  GLY A  309  5                                   3    
HELIX    7 AA7 SER C   44  TRP C   48  5                                   5    
SHEET    1 AA1 6 HIS A 108  SER A 113  0                                        
SHEET    2 AA1 6 ARG A 100  TYR A 105 -1  N  LEU A 103   O  TYR A 110           
SHEET    3 AA1 6 GLY A  86  SER A  95 -1  N  TYR A  93   O  HIS A 102           
SHEET    4 AA1 6 PHE A  32  GLN A  40 -1  N  PHE A  34   O  LEU A  92           
SHEET    5 AA1 6 ILE A 136  SER A 142 -1  O  ILE A 136   N  GLN A  37           
SHEET    6 AA1 6 THR A 149  SER A 150 -1  O  THR A 149   N  VAL A 140           
SHEET    1 AA2 5 THR A  45  GLN A  50  0                                        
SHEET    2 AA2 5 THR A  64  ALA A  69  1  O  ILE A  67   N  HIS A  47           
SHEET    3 AA2 5 ILE A  56  ASN A  60 -1  N  TRP A  59   O  THR A  66           
SHEET    4 AA2 5 SER A 156  SER A 160 -1  O  PHE A 157   N  VAL A  58           
SHEET    5 AA2 5 LYS A 124  GLU A 126 -1  N  LYS A 124   O  SER A 160           
SHEET    1 AA3 7 THR A 225  GLU A 230  0                                        
SHEET    2 AA3 7 VAL A 233  LYS A 239 -1  O  ALA A 235   N  PHE A 228           
SHEET    3 AA3 7 ARG A 287  SER A 294 -1  O  ASP A 292   N  ASN A 234           
SHEET    4 AA3 7 LYS A 311  VAL A 317 -1  O  GLY A 314   N  VAL A 291           
SHEET    5 AA3 7 TYR B 384  VAL B 390 -1  O  PHE B 385   N  LEU A 313           
SHEET    6 AA3 7 THR A 343  VAL A 350 -1  N  THR A 343   O  VAL B 390           
SHEET    7 AA3 7 SER A 360  SER A 362 -1  O  SER A 362   N  PHE A 348           
SHEET    1 AA4 5 LEU A 249  HIS A 252  0                                        
SHEET    2 AA4 5 VAL A 262  LEU A 269 -1  O  LEU A 269   N  LEU A 249           
SHEET    3 AA4 5 VAL A 329  HIS A 335 -1  O  GLN A 334   N  GLN A 263           
SHEET    4 AA4 5 GLN A 374  CYS A 379 -1  O  CYS A 377   N  LEU A 331           
SHEET    5 AA4 5 CYS A 366  SER A 370 -1  N  GLU A 367   O  LEU A 378           
SHEET    1 AA5 3 LEU C  10  ALA C  15  0                                        
SHEET    2 AA5 3 LEU C  20  TRP C  24 -1  O  SER C  23   N  GLU C  11           
SHEET    3 AA5 3 THR C  59  ILE C  62 -1  O  ILE C  62   N  LEU C  20           
SHEET    1 AA6 4 GLN C  49  PRO C  54  0                                        
SHEET    2 AA6 4 HIS C  33  GLU C  40 -1  N  TYR C  34   O  VAL C  53           
SHEET    3 AA6 4 TYR C  71  SER C  78 -1  O  TYR C  76   N  VAL C  35           
SHEET    4 AA6 4 ILE C  93  TYR C  97 -1  O  TYR C  97   N  TYR C  71           
SSBOND   1 CYS A   35    CYS A   91                          1555   1555  2.03  
SSBOND   2 CYS A  121    CYS A  177                          1555   1555  2.03  
SSBOND   3 CYS A  346    CYS A  377                          1555   1555  2.02  
SSBOND   4 CYS A  366    CYS A  379                          1555   1555  2.03  
LINK         ND2 ASN A  39                 C1  NAG A 900     1555   1555  1.44  
LINK         ND2 ASN A 148                 C1  NAG D   1     1555   1555  1.44  
LINK         ND2 ASN A 234                 C1  NAG E   1     1555   1555  1.44  
LINK         O4  NAG D   1                 C1  NAG D   2     1555   1555  1.44  
LINK         O4  NAG D   2                 C1  BMA D   3     1555   1555  1.44  
LINK         O6  BMA D   3                 C1  BMA D   4     1555   1555  1.44  
LINK         O4  NAG E   1                 C1  NAG E   2     1555   1555  1.44  
CRYST1  120.336  120.336   72.850  90.00  90.00 120.00 P 65          6          
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      0.008310  0.004798  0.000000        0.00000                         
SCALE2      0.000000  0.009596  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.013727        0.00000                         
ATOM      1  N   PRO A  28      36.710   5.023   9.894  1.00129.17           N  
ANISOU    1  N   PRO A  28    15989  17279  15809    309     -6  -3801       N  
ATOM      2  CA  PRO A  28      35.665   4.418   9.062  1.00128.00           C  
ANISOU    2  CA  PRO A  28    15577  17466  15592     66   -110  -4324       C  
ATOM      3  C   PRO A  28      34.660   5.431   8.533  1.00127.31           C  
ANISOU    3  C   PRO A  28    15250  18057  15065    134   -340  -4222       C  
ATOM      4  O   PRO A  28      34.805   5.920   7.415  1.00132.17           O  
ANISOU    4  O   PRO A  28    15794  19226  15200    275   -472  -4322       O  
ATOM      5  CB  PRO A  28      34.983   3.435  10.017  1.00127.61           C  
ANISOU    5  CB  PRO A  28    15505  16887  16093   -228     15  -4430       C  
ATOM      6  CG  PRO A  28      36.042   3.074  10.992  1.00129.70           C  
ANISOU    6  CG  PRO A  28    16079  16495  16706   -122    210  -4133       C  
ATOM      7  CD  PRO A  28      36.864   4.319  11.180  1.00125.87           C  
ANISOU    7  CD  PRO A  28    15738  16184  15904    214    156  -3642       C  
ATOM      8  N   ARG A  29      33.648   5.748   9.339  1.00118.50           N  
ANISOU    8  N   ARG A  29    14010  16911  14106     57   -375  -4004       N  
ATOM      9  CA  ARG A  29      32.539   6.551   8.840  1.00107.77           C  
ANISOU    9  CA  ARG A  29    12359  16183  12408    116   -606  -3972       C  
ATOM     10  C   ARG A  29      32.828   8.044   8.896  1.00 89.21           C  
ANISOU   10  C   ARG A  29    10110  14075   9709    481   -681  -3407       C  
ATOM     11  O   ARG A  29      32.261   8.806   8.109  1.00 77.95           O  
ANISOU   11  O   ARG A  29     8498  13242   7877    636   -891  -3355       O  
ATOM     12  CB  ARG A  29      31.270   6.233   9.631  1.00110.33           C  
ANISOU   12  CB  ARG A  29    12445  16398  13077   -125   -588  -4023       C  
ATOM     13  CG  ARG A  29      31.081   4.749   9.917  1.00112.57           C  
ANISOU   13  CG  ARG A  29    12696  16215  13861   -518   -422  -4464       C  
ATOM     14  CD  ARG A  29      29.726   4.495  10.549  1.00118.72           C  
ANISOU   14  CD  ARG A  29    13172  16985  14950   -788   -393  -4529       C  
ATOM     15  NE  ARG A  29      28.656   5.038   9.719  1.00125.72           N  
ANISOU   15  NE  ARG A  29    13641  18614  15513   -769   -680  -4730       N  
ATOM     16  CZ  ARG A  29      27.379   5.093  10.081  1.00131.15           C  
ANISOU   16  CZ  ARG A  29    13962  19494  16375   -936   -716  -4779       C  
ATOM     17  NH1 ARG A  29      27.002   4.638  11.269  1.00129.76           N  
ANISOU   17  NH1 ARG A  29    13807  18815  16681  -1157   -443  -4630       N  
ATOM     18  NH2 ARG A  29      26.479   5.608   9.255  1.00136.12           N  
ANISOU   18  NH2 ARG A  29    14189  20845  16684   -867  -1020  -4962       N  
ATOM     19  N   GLU A  30      33.692   8.482   9.805  1.00 80.92           N  
ANISOU   19  N   GLU A  30     9348  12578   8821    625   -525  -2986       N  
ATOM     20  CA  GLU A  30      34.024   9.893   9.930  1.00 85.14           C  
ANISOU   20  CA  GLU A  30     9994  13245   9109    939   -568  -2475       C  
ATOM     21  C   GLU A  30      35.525  10.046  10.120  1.00 80.47           C  
ANISOU   21  C   GLU A  30     9704  12310   8560   1062   -423  -2273       C  
ATOM     22  O   GLU A  30      36.247   9.079  10.375  1.00 90.44           O  
ANISOU   22  O   GLU A  30    11091  13189  10084    938   -289  -2473       O  
ATOM     23  CB  GLU A  30      33.289  10.568  11.104  1.00 85.87           C  
ANISOU   23  CB  GLU A  30    10062  13174   9391    997   -548  -2134       C  
ATOM     24  CG  GLU A  30      31.805  10.254  11.213  1.00 95.29           C  
ANISOU   24  CG  GLU A  30    10924  14600  10684    831   -629  -2343       C  
ATOM     25  CD  GLU A  30      31.559   9.065  12.109  1.00106.07           C  
ANISOU   25  CD  GLU A  30    12298  15504  12499    514   -446  -2551       C  
ATOM     26  OE1 GLU A  30      32.484   8.734  12.880  1.00100.73           O  
ANISOU   26  OE1 GLU A  30    11921  14316  12037    507   -272  -2402       O  
ATOM     27  OE2 GLU A  30      30.466   8.457  12.043  1.00113.28           O  
ANISOU   27  OE2 GLU A  30    12914  16564  13562    273   -472  -2849       O  
ATOM     28  N   ASP A  31      35.984  11.288   9.988  1.00 72.70           N  
ANISOU   28  N   ASP A  31     8817  11457   7347   1314   -447  -1869       N  
ATOM     29  CA  ASP A  31      37.375  11.619  10.264  1.00 67.90           C  
ANISOU   29  CA  ASP A  31     8447  10536   6815   1426   -313  -1640       C  
ATOM     30  C   ASP A  31      37.654  11.672  11.760  1.00 74.68           C  
ANISOU   30  C   ASP A  31     9467  10862   8047   1416   -226  -1421       C  
ATOM     31  O   ASP A  31      38.730  11.260  12.204  1.00 64.13           O  
ANISOU   31  O   ASP A  31     8285   9166   6915   1407   -123  -1416       O  
ATOM     32  CB  ASP A  31      37.731  12.961   9.629  1.00 71.13           C  
ANISOU   32  CB  ASP A  31     8896  11234   6898   1662   -345  -1275       C  
ATOM     33  CG  ASP A  31      37.842  12.883   8.129  1.00 73.77           C  
ANISOU   33  CG  ASP A  31     9141  12090   6798   1704   -386  -1441       C  
ATOM     34  OD1 ASP A  31      38.982  12.831   7.626  1.00 79.85           O  
ANISOU   34  OD1 ASP A  31    10014  12842   7484   1738   -250  -1445       O  
ATOM     35  OD2 ASP A  31      36.792  12.873   7.457  1.00 83.62           O  
ANISOU   35  OD2 ASP A  31    10200  13798   7774   1710   -553  -1577       O  
ATOM     36  N   PHE A  32      36.712  12.192  12.547  1.00 70.67           N  
ANISOU   36  N   PHE A  32     8913  10330   7610   1439   -271  -1241       N  
ATOM     37  CA  PHE A  32      36.945  12.429  13.966  1.00 66.72           C  
ANISOU   37  CA  PHE A  32     8580   9406   7364   1466   -194  -1010       C  
ATOM     38  C   PHE A  32      35.649  12.217  14.733  1.00 72.99           C  
ANISOU   38  C   PHE A  32     9259  10191   8283   1366   -186  -1039       C  
ATOM     39  O   PHE A  32      34.609  12.765  14.357  1.00 77.89           O  
ANISOU   39  O   PHE A  32     9678  11158   8759   1420   -275  -1023       O  
ATOM     40  CB  PHE A  32      37.482  13.849  14.202  1.00 69.34           C  
ANISOU   40  CB  PHE A  32     9029   9708   7611   1687   -211   -647       C  
ATOM     41  CG  PHE A  32      37.803  14.152  15.643  1.00 74.25           C  
ANISOU   41  CG  PHE A  32     9826   9940   8446   1723   -158   -464       C  
ATOM     42  CD1 PHE A  32      39.056  13.872  16.163  1.00 76.25           C  
ANISOU   42  CD1 PHE A  32    10249   9874   8851   1720   -113   -435       C  
ATOM     43  CD2 PHE A  32      36.854  14.726  16.474  1.00 65.66           C  
ANISOU   43  CD2 PHE A  32     8717   8844   7389   1777   -158   -341       C  
ATOM     44  CE1 PHE A  32      39.354  14.151  17.484  1.00 66.19           C  
ANISOU   44  CE1 PHE A  32     9131   8305   7714   1764   -102   -289       C  
ATOM     45  CE2 PHE A  32      37.147  15.005  17.794  1.00 71.23           C  
ANISOU   45  CE2 PHE A  32     9595   9241   8226   1816   -109   -209       C  
ATOM     46  CZ  PHE A  32      38.398  14.717  18.299  1.00 71.93           C  
ANISOU   46  CZ  PHE A  32     9864   9041   8425   1807    -96   -185       C  
ATOM     47  N   ARG A  33      35.717  11.432  15.809  1.00 65.04           N  
ANISOU   47  N   ARG A  33     8369   8803   7541   1236    -69  -1058       N  
ATOM     48  CA  ARG A  33      34.565  11.174  16.668  1.00 61.48           C  
ANISOU   48  CA  ARG A  33     7826   8305   7228   1117      8  -1054       C  
ATOM     49  C   ARG A  33      35.018  11.255  18.118  1.00 69.77           C  
ANISOU   49  C   ARG A  33     9128   8971   8409   1168    120   -809       C  
ATOM     50  O   ARG A  33      35.857  10.460  18.551  1.00 70.51           O  
ANISOU   50  O   ARG A  33     9409   8727   8654   1113    183   -809       O  
ATOM     51  CB  ARG A  33      33.943   9.804  16.373  1.00 60.58           C  
ANISOU   51  CB  ARG A  33     7560   8157   7302    824     72  -1390       C  
ATOM     52  CG  ARG A  33      32.506   9.649  16.852  1.00 61.47           C  
ANISOU   52  CG  ARG A  33     7442   8387   7525    668    143  -1440       C  
ATOM     53  CD  ARG A  33      32.101   8.180  16.919  1.00 71.00           C  
ANISOU   53  CD  ARG A  33     8574   9364   9041    327    279  -1723       C  
ATOM     54  NE  ARG A  33      32.078   7.523  15.613  1.00 92.76           N  
ANISOU   54  NE  ARG A  33    11150  12318  11776    184    167  -2140       N  
ATOM     55  CZ  ARG A  33      30.964   7.180  14.972  1.00 99.51           C  
ANISOU   55  CZ  ARG A  33    11653  13497  12659    -21    100  -2469       C  
ATOM     56  NH1 ARG A  33      29.783   7.433  15.517  1.00104.93           N  
ANISOU   56  NH1 ARG A  33    12102  14335  13430   -104    151  -2405       N  
ATOM     57  NH2 ARG A  33      31.030   6.581  13.789  1.00108.85           N  
ANISOU   57  NH2 ARG A  33    12697  14879  13783   -144    -18  -2893       N  
ATOM     58  N   PHE A  34      34.479  12.222  18.858  1.00 75.56           N  
ANISOU   58  N   PHE A  34     9865   9772   9073   1297    135   -610       N  
ATOM     59  CA  PHE A  34      34.766  12.398  20.278  1.00 71.43           C  
ANISOU   59  CA  PHE A  34     9571   8971   8598   1358    232   -407       C  
ATOM     60  C   PHE A  34      33.452  12.336  21.042  1.00 74.11           C  
ANISOU   60  C   PHE A  34     9787   9392   8978   1276    378   -389       C  
ATOM     61  O   PHE A  34      32.578  13.186  20.845  1.00 80.03           O  
ANISOU   61  O   PHE A  34    10342  10420   9647   1377    352   -384       O  
ATOM     62  CB  PHE A  34      35.481  13.725  20.541  1.00 64.77           C  
ANISOU   62  CB  PHE A  34     8868   8112   7632   1602    141   -224       C  
ATOM     63  CG  PHE A  34      35.524  14.113  21.993  1.00 71.03           C  
ANISOU   63  CG  PHE A  34     9851   8728   8407   1682    217    -75       C  
ATOM     64  CD1 PHE A  34      36.365  13.453  22.875  1.00 72.05           C  
ANISOU   64  CD1 PHE A  34    10214   8582   8580   1653    243     -6       C  
ATOM     65  CD2 PHE A  34      34.726  15.137  22.474  1.00 58.12           C  
ANISOU   65  CD2 PHE A  34     8161   7224   6696   1813    256    -13       C  
ATOM     66  CE1 PHE A  34      36.407  13.806  24.211  1.00 56.03           C  
ANISOU   66  CE1 PHE A  34     8371   6457   6461   1739    293    119       C  
ATOM     67  CE2 PHE A  34      34.764  15.495  23.808  1.00 56.58           C  
ANISOU   67  CE2 PHE A  34     8151   6905   6442   1890    335     73       C  
ATOM     68  CZ  PHE A  34      35.606  14.828  24.678  1.00 58.21           C  
ANISOU   68  CZ  PHE A  34     8600   6882   6634   1847    347    137       C  
ATOM     69  N   CYS A  35      33.318  11.341  21.915  1.00 63.41           N  
ANISOU   69  N   CYS A  35     8540   7795   7758   1108    549   -358       N  
ATOM     70  CA  CYS A  35      32.059  11.052  22.581  1.00 61.16           C  
ANISOU   70  CA  CYS A  35     8110   7581   7545    965    751   -353       C  
ATOM     71  C   CYS A  35      32.249  11.038  24.090  1.00 68.45           C  
ANISOU   71  C   CYS A  35     9310   8291   8408   1018    918   -113       C  
ATOM     72  O   CYS A  35      33.369  10.958  24.600  1.00 64.27           O  
ANISOU   72  O   CYS A  35     9077   7526   7817   1124    858     23       O  
ATOM     73  CB  CYS A  35      31.487   9.706  22.123  1.00 67.26           C  
ANISOU   73  CB  CYS A  35     8710   8282   8564    640    859   -554       C  
ATOM     74  SG  CYS A  35      31.089   9.575  20.370  1.00 83.52           S  
ANISOU   74  SG  CYS A  35    10410  10679  10644    542    657   -917       S  
ATOM     75  N   GLY A  36      31.126  11.109  24.796  1.00 64.25           N  
ANISOU   75  N   GLY A  36     8655   7884   7875    950   1130    -72       N  
ATOM     76  CA  GLY A  36      31.144  11.087  26.246  1.00 71.53           C  
ANISOU   76  CA  GLY A  36     9828   8679   8673    995   1328    151       C  
ATOM     77  C   GLY A  36      29.765  11.403  26.786  1.00 77.79           C  
ANISOU   77  C   GLY A  36    10390   9717   9451    946   1573    142       C  
ATOM     78  O   GLY A  36      28.776  11.373  26.052  1.00 72.63           O  
ANISOU   78  O   GLY A  36     9357   9287   8950    826   1595    -36       O  
ATOM     79  N   GLN A  37      29.719  11.715  28.077  1.00 72.32           N  
ANISOU   79  N   GLN A  37     9911   9014   8553   1054   1751    316       N  
ATOM     80  CA  GLN A  37      28.491  12.128  28.731  1.00 69.84           C  
ANISOU   80  CA  GLN A  37     9400   8951   8186   1054   2022    308       C  
ATOM     81  C   GLN A  37      28.709  13.461  29.431  1.00 71.22           C  
ANISOU   81  C   GLN A  37     9729   9252   8082   1385   1973    314       C  
ATOM     82  O   GLN A  37      29.810  13.765  29.901  1.00 67.67           O  
ANISOU   82  O   GLN A  37     9623   8649   7438   1543   1820    395       O  
ATOM     83  CB  GLN A  37      28.008  11.080  29.741  1.00 82.05           C  
ANISOU   83  CB  GLN A  37    11045  10384   9746    819   2401    502       C  
ATOM     84  CG  GLN A  37      27.780   9.696  29.163  1.00 80.92           C  
ANISOU   84  CG  GLN A  37    10774  10027   9945    457   2498    488       C  
ATOM     85  CD  GLN A  37      27.309   8.700  30.205  1.00 90.99           C  
ANISOU   85  CD  GLN A  37    12172  11138  11262    219   2916    742       C  
ATOM     86  OE1 GLN A  37      26.892   9.075  31.301  1.00102.74           O  
ANISOU   86  OE1 GLN A  37    13756  12779  12500    307   3173    902       O  
ATOM     87  NE2 GLN A  37      27.376   7.421  29.866  1.00 96.28           N  
ANISOU   87  NE2 GLN A  37    12849  11482  12249    -83   3008    780       N  
ATOM     88  N   ARG A  38      27.644  14.256  29.501  1.00 68.10           N  
ANISOU   88  N   ARG A  38     9051   9133   7693   1491   2100    198       N  
ATOM     89  CA  ARG A  38      27.673  15.539  30.187  1.00 77.83           C  
ANISOU   89  CA  ARG A  38    10394  10467   8710   1804   2104    148       C  
ATOM     90  C   ARG A  38      26.599  15.574  31.265  1.00 77.55           C  
ANISOU   90  C   ARG A  38    10264  10639   8562   1797   2504    157       C  
ATOM     91  O   ARG A  38      25.425  15.301  30.991  1.00 79.49           O  
ANISOU   91  O   ARG A  38    10113  11085   9002   1664   2705     94       O  
ATOM     92  CB  ARG A  38      27.475  16.707  29.217  1.00 77.56           C  
ANISOU   92  CB  ARG A  38    10120  10549   8801   2037   1874     -8       C  
ATOM     93  CG  ARG A  38      27.452  18.048  29.922  1.00 67.31           C  
ANISOU   93  CG  ARG A  38     8932   9288   7356   2359   1906    -93       C  
ATOM     94  CD  ARG A  38      27.760  19.203  28.991  1.00 65.50           C  
ANISOU   94  CD  ARG A  38     8627   9009   7252   2607   1626   -165       C  
ATOM     95  NE  ARG A  38      27.859  20.454  29.738  1.00 76.93           N  
ANISOU   95  NE  ARG A  38    10229  10394   8605   2896   1666   -272       N  
ATOM     96  CZ  ARG A  38      26.820  21.222  30.048  1.00 72.79           C  
ANISOU   96  CZ  ARG A  38     9487  10034   8137   3107   1850   -390       C  
ATOM     97  NH1 ARG A  38      25.599  20.870  29.663  1.00 71.51           N  
ANISOU   97  NH1 ARG A  38     8907  10143   8121   3058   1996   -398       N  
ATOM     98  NH2 ARG A  38      27.001  22.342  30.738  1.00 70.58           N  
ANISOU   98  NH2 ARG A  38     9382   9645   7791   3368   1888   -532       N  
ATOM     99  N   ASN A  39      27.010  15.915  32.484  1.00 82.24           N  
ANISOU   99  N   ASN A  39    11202  11216   8830   1938   2617    215       N  
ATOM    100  CA  ASN A  39      26.112  16.054  33.624  1.00 91.32           C  
ANISOU  100  CA  ASN A  39    12323  12593   9783   1974   3023    216       C  
ATOM    101  C   ASN A  39      25.586  17.487  33.635  1.00 90.75           C  
ANISOU  101  C   ASN A  39    12070  12697   9716   2296   3017    -38       C  
ATOM    102  O   ASN A  39      26.347  18.434  33.865  1.00 91.50           O  
ANISOU  102  O   ASN A  39    12413  12690   9663   2544   2812   -150       O  
ATOM    103  CB  ASN A  39      26.860  15.709  34.913  1.00104.89           C  
ANISOU  103  CB  ASN A  39    14524  14247  11082   1993   3124    392       C  
ATOM    104  CG  ASN A  39      25.943  15.289  36.058  1.00118.26           C  
ANISOU  104  CG  ASN A  39    16219  16166  12549   1904   3627    512       C  
ATOM    105  OD1 ASN A  39      24.729  15.155  35.897  1.00115.66           O  
ANISOU  105  OD1 ASN A  39    15497  16022  12427   1784   3931    461       O  
ATOM    106  ND2 ASN A  39      26.546  15.070  37.229  1.00144.75           N  
ANISOU  106  ND2 ASN A  39    20008  19534  15456   1965   3715    680       N  
ATOM    107  N   GLN A  40      24.295  17.652  33.351  1.00100.13           N  
ANISOU  107  N   GLN A  40    12801  14127  11117   2295   3233   -141       N  
ATOM    108  CA  GLN A  40      23.659  18.967  33.347  1.00117.51           C  
ANISOU  108  CA  GLN A  40    14782  16485  13381   2634   3263   -369       C  
ATOM    109  C   GLN A  40      23.154  19.275  34.751  1.00126.22           C  
ANISOU  109  C   GLN A  40    15993  17779  14187   2750   3674   -447       C  
ATOM    110  O   GLN A  40      22.170  18.685  35.208  1.00129.26           O  
ANISOU  110  O   GLN A  40    16139  18399  14576   2589   4073   -399       O  
ATOM    111  CB  GLN A  40      22.519  19.024  32.334  1.00125.43           C  
ANISOU  111  CB  GLN A  40    15198  17701  14760   2626   3262   -450       C  
ATOM    112  CG  GLN A  40      22.965  19.394  30.931  1.00126.71           C  
ANISOU  112  CG  GLN A  40    15253  17746  15144   2716   2813   -458       C  
ATOM    113  CD  GLN A  40      22.007  20.349  30.240  1.00128.64           C  
ANISOU  113  CD  GLN A  40    15041  18203  15635   3009   2748   -591       C  
ATOM    114  OE1 GLN A  40      20.830  20.045  30.056  1.00129.15           O  
ANISOU  114  OE1 GLN A  40    14622  18568  15880   2939   2922   -652       O  
ATOM    115  NE2 GLN A  40      22.510  21.516  29.858  1.00124.15           N  
ANISOU  115  NE2 GLN A  40    14606  17468  15098   3346   2499   -624       N  
ATOM    116  N   THR A  41      23.824  20.200  35.433  1.00129.92           N  
ANISOU  116  N   THR A  41    16811  18157  14396   3016   3593   -590       N  
ATOM    117  CA  THR A  41      23.419  20.627  36.763  1.00137.47           C  
ANISOU  117  CA  THR A  41    17902  19319  15011   3172   3959   -733       C  
ATOM    118  C   THR A  41      22.645  21.937  36.746  1.00130.34           C  
ANISOU  118  C   THR A  41    16729  18517  14277   3534   4060  -1050       C  
ATOM    119  O   THR A  41      22.293  22.446  37.815  1.00137.25           O  
ANISOU  119  O   THR A  41    17702  19564  14882   3713   4368  -1248       O  
ATOM    120  CB  THR A  41      24.642  20.773  37.674  1.00144.77           C  
ANISOU  120  CB  THR A  41    19394  20119  15491   3233   3815   -751       C  
ATOM    121  OG1 THR A  41      25.252  22.048  37.445  1.00151.39           O  
ANISOU  121  OG1 THR A  41    20347  20756  16417   3517   3513  -1024       O  
ATOM    122  CG2 THR A  41      25.658  19.676  37.386  1.00141.50           C  
ANISOU  122  CG2 THR A  41    19237  19505  15021   2963   3563   -445       C  
ATOM    123  N   GLN A  42      22.383  22.495  35.567  1.00115.60           N  
ANISOU  123  N   GLN A  42    14537  16550  12835   3670   3811  -1097       N  
ATOM    124  CA  GLN A  42      21.674  23.762  35.431  1.00109.03           C  
ANISOU  124  CA  GLN A  42    13439  15754  12234   4063   3868  -1354       C  
ATOM    125  C   GLN A  42      21.362  23.975  33.957  1.00 97.00           C  
ANISOU  125  C   GLN A  42    11528  14173  11153   4134   3566  -1261       C  
ATOM    126  O   GLN A  42      21.817  23.225  33.090  1.00 91.65           O  
ANISOU  126  O   GLN A  42    10845  13422  10558   3881   3301  -1051       O  
ATOM    127  CB  GLN A  42      22.495  24.936  35.974  1.00 98.14           C  
ANISOU  127  CB  GLN A  42    12460  14109  10719   4351   3738  -1602       C  
ATOM    128  CG  GLN A  42      23.715  25.272  35.129  1.00 96.24           C  
ANISOU  128  CG  GLN A  42    12466  13480  10621   4342   3253  -1516       C  
ATOM    129  CD  GLN A  42      24.594  26.323  35.769  1.00 98.04           C  
ANISOU  129  CD  GLN A  42    13092  13431  10728   4545   3140  -1787       C  
ATOM    130  OE1 GLN A  42      24.982  26.199  36.929  1.00108.88           O  
ANISOU  130  OE1 GLN A  42    14785  14890  11695   4499   3274  -1935       O  
ATOM    131  NE2 GLN A  42      24.912  27.370  35.016  1.00 90.62           N  
ANISOU  131  NE2 GLN A  42    12134  12161  10137   4766   2895  -1854       N  
ATOM    132  N   GLN A  43      20.573  25.013  33.685  1.00102.09           N  
ANISOU  132  N   GLN A  43    11852  14869  12070   4506   3610  -1424       N  
ATOM    133  CA  GLN A  43      20.353  25.447  32.313  1.00100.38           C  
ANISOU  133  CA  GLN A  43    11320  14596  12226   4673   3281  -1320       C  
ATOM    134  C   GLN A  43      21.681  25.878  31.705  1.00103.02           C  
ANISOU  134  C   GLN A  43    12059  14520  12564   4694   2873  -1215       C  
ATOM    135  O   GLN A  43      22.348  26.777  32.225  1.00104.77           O  
ANISOU  135  O   GLN A  43    12632  14443  12734   4888   2846  -1362       O  
ATOM    136  CB  GLN A  43      19.340  26.592  32.281  1.00 97.38           C  
ANISOU  136  CB  GLN A  43    10574  14298  12127   5144   3412  -1499       C  
ATOM    137  CG  GLN A  43      19.004  27.105  30.891  1.00 97.25           C  
ANISOU  137  CG  GLN A  43    10210  14270  12469   5389   3074  -1349       C  
ATOM    138  CD  GLN A  43      17.963  28.207  30.916  1.00118.14           C  
ANISOU  138  CD  GLN A  43    12477  16993  15418   5901   3213  -1501       C  
ATOM    139  OE1 GLN A  43      17.443  28.563  31.973  1.00121.81           O  
ANISOU  139  OE1 GLN A  43    12909  17534  15840   6061   3594  -1760       O  
ATOM    140  NE2 GLN A  43      17.655  28.753  29.747  1.00118.41           N  
ANISOU  140  NE2 GLN A  43    12223  17021  15746   6187   2910  -1335       N  
ATOM    141  N   SER A  44      22.076  25.224  30.616  1.00 95.58           N  
ANISOU  141  N   SER A  44    11058  13569  11690   4476   2573   -988       N  
ATOM    142  CA  SER A  44      23.406  25.404  30.058  1.00 96.37           C  
ANISOU  142  CA  SER A  44    11533  13322  11760   4416   2233   -865       C  
ATOM    143  C   SER A  44      23.321  25.757  28.579  1.00 98.30           C  
ANISOU  143  C   SER A  44    11539  13559  12252   4554   1919   -684       C  
ATOM    144  O   SER A  44      22.299  25.542  27.921  1.00102.10           O  
ANISOU  144  O   SER A  44    11559  14358  12877   4611   1908   -638       O  
ATOM    145  CB  SER A  44      24.263  24.148  30.252  1.00 96.59           C  
ANISOU  145  CB  SER A  44    11832  13325  11544   3992   2181   -754       C  
ATOM    146  OG  SER A  44      25.590  24.362  29.813  1.00108.07           O  
ANISOU  146  OG  SER A  44    13628  14458  12976   3949   1881   -668       O  
ATOM    147  N   THR A  45      24.424  26.296  28.066  1.00 91.61           N  
ANISOU  147  N   THR A  45    11001  12372  11437   4601   1663   -579       N  
ATOM    148  CA  THR A  45      24.508  26.802  26.705  1.00 96.54           C  
ANISOU  148  CA  THR A  45    11490  12947  12243   4771   1380   -364       C  
ATOM    149  C   THR A  45      25.580  26.060  25.915  1.00 86.38           C  
ANISOU  149  C   THR A  45    10394  11594  10834   4467   1135   -194       C  
ATOM    150  O   THR A  45      26.522  25.494  26.476  1.00 72.33           O  
ANISOU  150  O   THR A  45     8935   9658   8890   4201   1148   -243       O  
ATOM    151  CB  THR A  45      24.820  28.306  26.690  1.00 92.81           C  
ANISOU  151  CB  THR A  45    11195  12083  11987   5149   1341   -358       C  
ATOM    152  OG1 THR A  45      25.982  28.565  27.488  1.00100.00           O  
ANISOU  152  OG1 THR A  45    12564  12620  12811   5024   1365   -490       O  
ATOM    153  CG2 THR A  45      23.653  29.097  27.239  1.00 93.56           C  
ANISOU  153  CG2 THR A  45    11035  12250  12265   5525   1566   -522       C  
ATOM    154  N   LEU A  46      25.420  26.074  24.595  1.00 90.82           N  
ANISOU  154  N   LEU A  46    10743  12304  11460   4535    908      3       N  
ATOM    155  CA  LEU A  46      26.435  25.598  23.666  1.00 78.87           C  
ANISOU  155  CA  LEU A  46     9395  10728   9844   4324    678    165       C  
ATOM    156  C   LEU A  46      27.143  26.800  23.058  1.00 71.35           C  
ANISOU  156  C   LEU A  46     8643   9450   9017   4573    542    361       C  
ATOM    157  O   LEU A  46      26.489  27.758  22.633  1.00 80.83           O  
ANISOU  157  O   LEU A  46     9675  10654  10381   4935    512    482       O  
ATOM    158  CB  LEU A  46      25.816  24.738  22.562  1.00 77.30           C  
ANISOU  158  CB  LEU A  46     8836  10958   9576   4203    524    230       C  
ATOM    159  CG  LEU A  46      26.727  24.350  21.394  1.00 78.99           C  
ANISOU  159  CG  LEU A  46     9168  11179   9667   4054    287    385       C  
ATOM    160  CD1 LEU A  46      27.863  23.465  21.867  1.00 70.21           C  
ANISOU  160  CD1 LEU A  46     8379   9849   8448   3697    330    303       C  
ATOM    161  CD2 LEU A  46      25.932  23.662  20.297  1.00 84.29           C  
ANISOU  161  CD2 LEU A  46     9441  12331  10255   3995    121    386       C  
ATOM    162  N   HIS A  47      28.472  26.754  23.025  1.00 80.28           N  
ANISOU  162  N   HIS A  47    10116  10288  10098   4388    472    407       N  
ATOM    163  CA  HIS A  47      29.268  27.835  22.462  1.00 73.07           C  
ANISOU  163  CA  HIS A  47     9406   9026   9333   4551    381    603       C  
ATOM    164  C   HIS A  47      30.322  27.255  21.535  1.00 65.06           C  
ANISOU  164  C   HIS A  47     8505   8029   8186   4308    227    762       C  
ATOM    165  O   HIS A  47      31.033  26.316  21.908  1.00 67.34           O  
ANISOU  165  O   HIS A  47     8923   8319   8344   3999    226    632       O  
ATOM    166  CB  HIS A  47      29.937  28.672  23.556  1.00 68.09           C  
ANISOU  166  CB  HIS A  47     9085   7932   8855   4589    500    432       C  
ATOM    167  CG  HIS A  47      30.561  29.932  23.047  1.00 72.14           C  
ANISOU  167  CG  HIS A  47     9765   8023   9621   4773    458    618       C  
ATOM    168  ND1 HIS A  47      29.829  31.071  22.788  1.00 78.68           N  
ANISOU  168  ND1 HIS A  47    10498   8697  10699   5164    504    746       N  
ATOM    169  CD2 HIS A  47      31.844  30.230  22.733  1.00 68.47           C  
ANISOU  169  CD2 HIS A  47     9542   7239   9234   4617    394    717       C  
ATOM    170  CE1 HIS A  47      30.636  32.019  22.345  1.00 74.80           C  
ANISOU  170  CE1 HIS A  47    10207   7781  10433   5190    478    928       C  
ATOM    171  NE2 HIS A  47      31.863  31.534  22.300  1.00 71.69           N  
ANISOU  171  NE2 HIS A  47    10014   7284   9942   4883    423    914       N  
ATOM    172  N   TYR A  48      30.422  27.818  20.334  1.00 66.44           N  
ANISOU  172  N   TYR A  48     8634   8223   8387   4472    109   1057       N  
ATOM    173  CA  TYR A  48      31.406  27.397  19.348  1.00 64.65           C  
ANISOU  173  CA  TYR A  48     8505   8040   8020   4281     -3   1223       C  
ATOM    174  C   TYR A  48      32.169  28.614  18.855  1.00 66.23           C  
ANISOU  174  C   TYR A  48     8906   7859   8400   4433      8   1501       C  
ATOM    175  O   TYR A  48      31.570  29.655  18.570  1.00 75.09           O  
ANISOU  175  O   TYR A  48     9976   8874   9680   4769     21   1708       O  
ATOM    176  CB  TYR A  48      30.752  26.673  18.164  1.00 77.29           C  
ANISOU  176  CB  TYR A  48     9826  10162   9380   4285   -152   1328       C  
ATOM    177  CG  TYR A  48      31.724  26.339  17.050  1.00 70.14           C  
ANISOU  177  CG  TYR A  48     9018   9338   8294   4136   -244   1496       C  
ATOM    178  CD1 TYR A  48      32.558  25.233  17.137  1.00 67.55           C  
ANISOU  178  CD1 TYR A  48     8781   9031   7853   3791   -239   1309       C  
ATOM    179  CD2 TYR A  48      31.811  27.134  15.915  1.00 73.92           C  
ANISOU  179  CD2 TYR A  48     9502   9873   8712   4362   -314   1857       C  
ATOM    180  CE1 TYR A  48      33.454  24.926  16.124  1.00 73.43           C  
ANISOU  180  CE1 TYR A  48     9597   9865   8437   3670   -290   1428       C  
ATOM    181  CE2 TYR A  48      32.702  26.834  14.898  1.00 85.07           C  
ANISOU  181  CE2 TYR A  48    11003  11397   9921   4226   -356   2009       C  
ATOM    182  CZ  TYR A  48      33.520  25.730  15.006  1.00 82.81           C  
ANISOU  182  CZ  TYR A  48    10784  11145   9533   3878   -338   1769       C  
ATOM    183  OH  TYR A  48      34.405  25.434  13.992  1.00 77.85           O  
ANISOU  183  OH  TYR A  48    10226  10646   8707   3760   -349   1889       O  
ATOM    184  N   ASP A  49      33.487  28.476  18.759  1.00 72.31           N  
ANISOU  184  N   ASP A  49     9889   8409   9177   4190     18   1515       N  
ATOM    185  CA  ASP A  49      34.346  29.499  18.188  1.00 65.88           C  
ANISOU  185  CA  ASP A  49     9249   7239   8544   4250     60   1794       C  
ATOM    186  C   ASP A  49      35.254  28.859  17.153  1.00 69.58           C  
ANISOU  186  C   ASP A  49     9735   7898   8802   4036     13   1946       C  
ATOM    187  O   ASP A  49      35.565  27.668  17.228  1.00 76.02           O  
ANISOU  187  O   ASP A  49    10506   8955   9424   3789    -37   1735       O  
ATOM    188  CB  ASP A  49      35.210  30.194  19.248  1.00 79.04           C  
ANISOU  188  CB  ASP A  49    11149   8364  10520   4146    162   1607       C  
ATOM    189  CG  ASP A  49      34.407  30.688  20.427  1.00 67.05           C  
ANISOU  189  CG  ASP A  49     9634   6680   9161   4322    231   1351       C  
ATOM    190  OD1 ASP A  49      33.613  31.635  20.252  1.00 70.46           O  
ANISOU  190  OD1 ASP A  49    10016   6983   9774   4650    279   1503       O  
ATOM    191  OD2 ASP A  49      34.599  30.151  21.536  1.00 65.11           O  
ANISOU  191  OD2 ASP A  49     9451   6433   8855   4150    245   1005       O  
ATOM    192  N   GLN A  50      35.677  29.658  16.183  1.00 77.80           N  
ANISOU  192  N   GLN A  50    10848   8819   9891   4143     53   2322       N  
ATOM    193  CA  GLN A  50      36.707  29.237  15.249  1.00 79.21           C  
ANISOU  193  CA  GLN A  50    11072   9123   9901   3940     72   2471       C  
ATOM    194  C   GLN A  50      38.061  29.585  15.852  1.00 65.33           C  
ANISOU  194  C   GLN A  50     9495   6890   8439   3696    188   2367       C  
ATOM    195  O   GLN A  50      38.327  30.751  16.160  1.00 72.86           O  
ANISOU  195  O   GLN A  50    10577   7369   9736   3771    292   2485       O  
ATOM    196  CB  GLN A  50      36.526  29.904  13.887  1.00 70.20           C  
ANISOU  196  CB  GLN A  50     9923   8132   8617   4167     86   2963       C  
ATOM    197  CG  GLN A  50      37.580  29.487  12.870  1.00 70.12           C  
ANISOU  197  CG  GLN A  50     9956   8300   8385   3966    150   3121       C  
ATOM    198  CD  GLN A  50      37.507  30.280  11.576  1.00 74.71           C  
ANISOU  198  CD  GLN A  50    10583   8998   8806   4196    208   3672       C  
ATOM    199  OE1 GLN A  50      36.534  30.990  11.317  1.00 77.96           O  
ANISOU  199  OE1 GLN A  50    10932   9460   9230   4429    141   3850       O  
ATOM    200  NE2 GLN A  50      38.549  30.171  10.759  1.00 75.46           N  
ANISOU  200  NE2 GLN A  50    10751   9160   8762   4024    342   3856       N  
ATOM    201  N   SER A  51      38.903  28.578  16.036  1.00 67.03           N  
ANISOU  201  N   SER A  51     9699   7217   8552   3409    165   2125       N  
ATOM    202  CA  SER A  51      40.218  28.784  16.619  1.00 74.75           C  
ANISOU  202  CA  SER A  51    10785   7822   9797   3170    234   1986       C  
ATOM    203  C   SER A  51      41.219  29.187  15.544  1.00 80.48           C  
ANISOU  203  C   SER A  51    11532   8480  10565   3072    370   2295       C  
ATOM    204  O   SER A  51      41.085  28.822  14.374  1.00 71.92           O  
ANISOU  204  O   SER A  51    10383   7763   9180   3123    389   2528       O  
ATOM    205  CB  SER A  51      40.699  27.518  17.325  1.00 62.51           C  
ANISOU  205  CB  SER A  51     9196   6421   8136   2947    142   1617       C  
ATOM    206  OG  SER A  51      40.723  26.425  16.421  1.00 72.16           O  
ANISOU  206  OG  SER A  51    10307   8060   9049   2880    111   1641       O  
ATOM    207  N   SER A  52      42.228  29.957  15.955  1.00 77.45           N  
ANISOU  207  N   SER A  52    11232   7641  10555   2919    475   2279       N  
ATOM    208  CA  SER A  52      43.331  30.272  15.054  1.00 83.38           C  
ANISOU  208  CA  SER A  52    11976   8310  11395   2760    648   2539       C  
ATOM    209  C   SER A  52      44.272  29.088  14.883  1.00 87.27           C  
ANISOU  209  C   SER A  52    12350   9088  11722   2524    625   2326       C  
ATOM    210  O   SER A  52      44.906  28.951  13.830  1.00 92.73           O  
ANISOU  210  O   SER A  52    12988   9955  12291   2445    769   2546       O  
ATOM    211  CB  SER A  52      44.106  31.485  15.570  1.00 94.34           C  
ANISOU  211  CB  SER A  52    13450   9090  13306   2633    779   2554       C  
ATOM    212  OG  SER A  52      43.307  32.657  15.534  1.00115.23           O  
ANISOU  212  OG  SER A  52    16219  11412  16152   2874    848   2810       O  
ATOM    213  N   GLU A  53      44.373  28.231  15.903  1.00 78.75           N  
ANISOU  213  N   GLU A  53    11233   8058  10631   2432    461   1915       N  
ATOM    214  CA  GLU A  53      45.208  27.044  15.929  1.00 74.74           C  
ANISOU  214  CA  GLU A  53    10614   7768  10014   2255    412   1681       C  
ATOM    215  C   GLU A  53      44.447  25.841  15.373  1.00 64.24           C  
ANISOU  215  C   GLU A  53     9228   6908   8271   2342    336   1634       C  
ATOM    216  O   GLU A  53      43.227  25.743  15.532  1.00 73.32           O  
ANISOU  216  O   GLU A  53    10404   8193   9259   2503    246   1631       O  
ATOM    217  CB  GLU A  53      45.671  26.751  17.352  1.00 70.80           C  
ANISOU  217  CB  GLU A  53    10124   7072   9706   2146    258   1303       C  
ATOM    218  CG  GLU A  53      46.626  27.790  17.907  1.00 79.16           C  
ANISOU  218  CG  GLU A  53    11188   7704  11186   1998    302   1240       C  
ATOM    219  CD  GLU A  53      47.054  27.486  19.326  1.00 99.87           C  
ANISOU  219  CD  GLU A  53    13813  10214  13920   1916    103    844       C  
ATOM    220  OE1 GLU A  53      46.174  27.185  20.158  1.00106.04           O  
ANISOU  220  OE1 GLU A  53    14695  11060  14534   2043    -23    689       O  
ATOM    221  OE2 GLU A  53      48.268  27.540  19.609  1.00101.81           O  
ANISOU  221  OE2 GLU A  53    13944  10335  14403   1728     73    691       O  
ATOM    222  N   PRO A  54      45.145  24.931  14.701  1.00 64.40           N  
ANISOU  222  N   PRO A  54     9148   7176   8145   2233    382   1571       N  
ATOM    223  CA  PRO A  54      44.491  23.755  14.101  1.00 61.77           C  
ANISOU  223  CA  PRO A  54     8753   7265   7452   2284    321   1468       C  
ATOM    224  C   PRO A  54      44.239  22.641  15.114  1.00 68.10           C  
ANISOU  224  C   PRO A  54     9549   8066   8261   2239    164   1126       C  
ATOM    225  O   PRO A  54      44.670  21.495  14.951  1.00 60.23           O  
ANISOU  225  O   PRO A  54     8484   7210   7190   2157    151    930       O  
ATOM    226  CB  PRO A  54      45.492  23.353  13.010  1.00 65.42           C  
ANISOU  226  CB  PRO A  54     9121   7929   7805   2185    477   1514       C  
ATOM    227  CG  PRO A  54      46.798  23.759  13.559  1.00 68.40           C  
ANISOU  227  CG  PRO A  54     9462   7977   8549   2031    550   1470       C  
ATOM    228  CD  PRO A  54      46.562  25.033  14.309  1.00 64.80           C  
ANISOU  228  CD  PRO A  54     9112   7139   8371   2060    529   1600       C  
ATOM    229  N   HIS A  55      43.524  22.979  16.184  1.00 70.71           N  
ANISOU  229  N   HIS A  55     9960   8221   8686   2305     67   1064       N  
ATOM    230  CA  HIS A  55      43.138  22.028  17.212  1.00 58.77           C  
ANISOU  230  CA  HIS A  55     8472   6707   7152   2278    -49    811       C  
ATOM    231  C   HIS A  55      41.622  21.920  17.274  1.00 54.69           C  
ANISOU  231  C   HIS A  55     7943   6370   6467   2394    -88    819       C  
ATOM    232  O   HIS A  55      40.889  22.751  16.726  1.00 70.24           O  
ANISOU  232  O   HIS A  55     9890   8421   8376   2532    -62   1012       O  
ATOM    233  CB  HIS A  55      43.667  22.432  18.590  1.00 63.20           C  
ANISOU  233  CB  HIS A  55     9127   6950   7938   2243   -120    686       C  
ATOM    234  CG  HIS A  55      45.128  22.739  18.622  1.00 72.99           C  
ANISOU  234  CG  HIS A  55    10328   8005   9400   2127   -106    661       C  
ATOM    235  ND1 HIS A  55      46.029  22.237  17.707  1.00 86.30           N  
ANISOU  235  ND1 HIS A  55    11895   9810  11086   2042    -29    685       N  
ATOM    236  CD2 HIS A  55      45.846  23.498  19.481  1.00 78.37           C  
ANISOU  236  CD2 HIS A  55    11044   8408  10325   2072   -159    576       C  
ATOM    237  CE1 HIS A  55      47.240  22.675  18.003  1.00 81.75           C  
ANISOU  237  CE1 HIS A  55    11257   9037  10766   1939    -26    640       C  
ATOM    238  NE2 HIS A  55      47.155  23.441  19.076  1.00 64.05           N  
ANISOU  238  NE2 HIS A  55     9105   6553   8680   1944   -120    564       N  
ATOM    239  N   ILE A  56      41.159  20.842  17.895  1.00 48.74           N  
ANISOU  239  N   ILE A  56     7182   5687   5648   2339   -142    624       N  
ATOM    240  CA  ILE A  56      39.780  20.717  18.362  1.00 50.59           C  
ANISOU  240  CA  ILE A  56     7388   6034   5800   2410   -161    582       C  
ATOM    241  C   ILE A  56      39.796  20.829  19.880  1.00 64.51           C  
ANISOU  241  C   ILE A  56     9282   7562   7669   2410   -175    479       C  
ATOM    242  O   ILE A  56      40.297  19.934  20.573  1.00 56.06           O  
ANISOU  242  O   ILE A  56     8276   6413   6611   2310   -204    356       O  
ATOM    243  CB  ILE A  56      39.136  19.397  17.903  1.00 54.04           C  
ANISOU  243  CB  ILE A  56     7707   6734   6091   2315   -171    438       C  
ATOM    244  CG1 ILE A  56      39.041  19.372  16.377  1.00 55.17           C  
ANISOU  244  CG1 ILE A  56     7720   7183   6058   2336   -177    501       C  
ATOM    245  CG2 ILE A  56      37.761  19.235  18.512  1.00 48.60           C  
ANISOU  245  CG2 ILE A  56     6950   6147   5369   2348   -164    380       C  
ATOM    246  CD1 ILE A  56      38.389  18.123  15.801  1.00 58.64           C  
ANISOU  246  CD1 ILE A  56     8018   7901   6361   2225   -204    290       C  
ATOM    247  N   PHE A  57      39.190  21.893  20.396  1.00 66.16           N  
ANISOU  247  N   PHE A  57     9530   7674   7932   2546   -153    530       N  
ATOM    248  CA  PHE A  57      39.205  22.213  21.819  1.00 59.26           C  
ANISOU  248  CA  PHE A  57     8793   6606   7117   2572   -157    407       C  
ATOM    249  C   PHE A  57      37.791  22.102  22.367  1.00 55.17           C  
ANISOU  249  C   PHE A  57     8225   6234   6504   2660    -88    360       C  
ATOM    250  O   PHE A  57      36.868  22.730  21.838  1.00 59.90           O  
ANISOU  250  O   PHE A  57     8707   6941   7112   2804    -50    451       O  
ATOM    251  CB  PHE A  57      39.768  23.619  22.044  1.00 55.89           C  
ANISOU  251  CB  PHE A  57     8455   5900   6882   2649   -158    436       C  
ATOM    252  CG  PHE A  57      39.755  24.059  23.478  1.00 52.35           C  
ANISOU  252  CG  PHE A  57     8146   5280   6464   2687   -173    246       C  
ATOM    253  CD1 PHE A  57      40.475  23.370  24.439  1.00 53.41           C  
ANISOU  253  CD1 PHE A  57     8379   5392   6522   2583   -259     92       C  
ATOM    254  CD2 PHE A  57      39.029  25.174  23.862  1.00 56.67           C  
ANISOU  254  CD2 PHE A  57     8727   5702   7102   2852   -104    217       C  
ATOM    255  CE1 PHE A  57      40.466  23.778  25.760  1.00 56.67           C  
ANISOU  255  CE1 PHE A  57     8930   5713   6888   2629   -287    -99       C  
ATOM    256  CE2 PHE A  57      39.013  25.589  25.177  1.00 70.41           C  
ANISOU  256  CE2 PHE A  57    10602   7314   8835   2892   -105    -12       C  
ATOM    257  CZ  PHE A  57      39.735  24.890  26.130  1.00 63.71           C  
ANISOU  257  CZ  PHE A  57     9860   6496   7850   2773   -202   -175       C  
ATOM    258  N   VAL A  58      37.628  21.288  23.405  1.00 55.51           N  
ANISOU  258  N   VAL A  58     8342   6293   6454   2585    -62    241       N  
ATOM    259  CA  VAL A  58      36.346  21.068  24.065  1.00 54.58           C  
ANISOU  259  CA  VAL A  58     8170   6321   6246   2631     53    189       C  
ATOM    260  C   VAL A  58      36.527  21.394  25.540  1.00 68.27           C  
ANISOU  260  C   VAL A  58    10100   7924   7916   2676     88     74       C  
ATOM    261  O   VAL A  58      37.341  20.761  26.221  1.00 61.68           O  
ANISOU  261  O   VAL A  58     9417   7016   7003   2582     29     37       O  
ATOM    262  CB  VAL A  58      35.846  19.625  23.883  1.00 49.58           C  
ANISOU  262  CB  VAL A  58     7437   5865   5535   2465    105    176       C  
ATOM    263  CG1 VAL A  58      34.590  19.390  24.695  1.00 51.13           C  
ANISOU  263  CG1 VAL A  58     7565   6196   5664   2475    267    129       C  
ATOM    264  CG2 VAL A  58      35.594  19.332  22.412  1.00 56.47           C  
ANISOU  264  CG2 VAL A  58     8102   6922   6430   2423     53    219       C  
ATOM    265  N   TRP A  59      35.762  22.364  26.035  1.00 66.21           N  
ANISOU  265  N   TRP A  59     9831   7655   7672   2842    178      9       N  
ATOM    266  CA  TRP A  59      35.871  22.831  27.411  1.00 67.75           C  
ANISOU  266  CA  TRP A  59    10211   7758   7771   2911    221   -156       C  
ATOM    267  C   TRP A  59      34.474  22.917  28.004  1.00 57.88           C  
ANISOU  267  C   TRP A  59     8873   6690   6431   3021    428   -216       C  
ATOM    268  O   TRP A  59      33.632  23.675  27.509  1.00 57.06           O  
ANISOU  268  O   TRP A  59     8600   6618   6463   3183    495   -202       O  
ATOM    269  CB  TRP A  59      36.573  24.189  27.474  1.00 71.79           C  
ANISOU  269  CB  TRP A  59    10821   7998   8456   3015    138   -256       C  
ATOM    270  CG  TRP A  59      36.807  24.708  28.862  1.00 70.10           C  
ANISOU  270  CG  TRP A  59    10803   7700   8132   3072    146   -505       C  
ATOM    271  CD1 TRP A  59      36.553  24.063  30.041  1.00 74.61           C  
ANISOU  271  CD1 TRP A  59    11496   8447   8406   3054    212   -602       C  
ATOM    272  CD2 TRP A  59      37.345  25.988  29.216  1.00 66.17           C  
ANISOU  272  CD2 TRP A  59    10409   6928   7803   3151     91   -704       C  
ATOM    273  NE1 TRP A  59      36.898  24.864  31.104  1.00 64.79           N  
ANISOU  273  NE1 TRP A  59    10426   7112   7081   3134    182   -871       N  
ATOM    274  CE2 TRP A  59      37.389  26.049  30.624  1.00 62.18           C  
ANISOU  274  CE2 TRP A  59    10078   6486   7060   3182    101   -969       C  
ATOM    275  CE3 TRP A  59      37.795  27.088  28.478  1.00 61.21           C  
ANISOU  275  CE3 TRP A  59     9749   5995   7511   3189     48   -682       C  
ATOM    276  CZ2 TRP A  59      37.864  27.165  31.307  1.00 63.39           C  
ANISOU  276  CZ2 TRP A  59    10360   6418   7307   3241     46  -1278       C  
ATOM    277  CZ3 TRP A  59      38.267  28.194  29.159  1.00 65.98           C  
ANISOU  277  CZ3 TRP A  59    10481   6319   8268   3230     18   -956       C  
ATOM    278  CH2 TRP A  59      38.297  28.225  30.559  1.00 69.92           C  
ANISOU  278  CH2 TRP A  59    11138   6897   8531   3252      5  -1285       C  
ATOM    279  N   ASN A  60      34.236  22.150  29.064  1.00 59.65           N  
ANISOU  279  N   ASN A  60     9200   7038   6428   2949    539   -262       N  
ATOM    280  CA  ASN A  60      32.935  22.079  29.715  1.00 69.30           C  
ANISOU  280  CA  ASN A  60    10323   8466   7542   3016    789   -313       C  
ATOM    281  C   ASN A  60      32.997  22.797  31.056  1.00 69.63           C  
ANISOU  281  C   ASN A  60    10575   8482   7400   3152    874   -521       C  
ATOM    282  O   ASN A  60      33.717  22.366  31.964  1.00 79.12           O  
ANISOU  282  O   ASN A  60    12018   9685   8358   3082    823   -554       O  
ATOM    283  CB  ASN A  60      32.496  20.629  29.918  1.00 65.60           C  
ANISOU  283  CB  ASN A  60     9809   8171   6945   2813    922   -186       C  
ATOM    284  CG  ASN A  60      31.036  20.520  30.307  1.00 77.32           C  
ANISOU  284  CG  ASN A  60    11089   9895   8396   2841   1212   -216       C  
ATOM    285  OD1 ASN A  60      30.185  21.206  29.745  1.00 81.22           O  
ANISOU  285  OD1 ASN A  60    11324  10479   9058   2982   1258   -268       O  
ATOM    286  ND2 ASN A  60      30.742  19.674  31.290  1.00 82.36           N  
ANISOU  286  ND2 ASN A  60    11831  10644   8819   2723   1421   -163       N  
ATOM    287  N   THR A  61      32.252  23.889  31.174  1.00 73.83           N  
ANISOU  287  N   THR A  61    11013   9001   8038   3367    992   -671       N  
ATOM    288  CA  THR A  61      31.944  24.486  32.463  1.00 72.16           C  
ANISOU  288  CA  THR A  61    10948   8840   7630   3511   1156   -921       C  
ATOM    289  C   THR A  61      30.515  24.124  32.854  1.00 76.44           C  
ANISOU  289  C   THR A  61    11291   9678   8074   3560   1481   -913       C  
ATOM    290  O   THR A  61      29.759  23.542  32.073  1.00 76.41           O  
ANISOU  290  O   THR A  61    11006   9814   8211   3487   1548   -740       O  
ATOM    291  CB  THR A  61      32.127  26.007  32.431  1.00 68.40           C  
ANISOU  291  CB  THR A  61    10514   8093   7381   3732   1099  -1151       C  
ATOM    292  OG1 THR A  61      31.174  26.592  31.536  1.00 76.18           O  
ANISOU  292  OG1 THR A  61    11219   9056   8670   3910   1183  -1070       O  
ATOM    293  CG2 THR A  61      33.533  26.367  31.981  1.00 75.66           C  
ANISOU  293  CG2 THR A  61    11582   8710   8454   3637    808  -1149       C  
ATOM    294  N   GLU A  62      30.151  24.472  34.089  1.00 88.04           N  
ANISOU  294  N   GLU A  62    12889  11269   9292   3677   1691  -1130       N  
ATOM    295  CA  GLU A  62      28.813  24.156  34.573  1.00 87.76           C  
ANISOU  295  CA  GLU A  62    12653  11539   9152   3719   2055  -1139       C  
ATOM    296  C   GLU A  62      27.733  24.845  33.745  1.00 84.29           C  
ANISOU  296  C   GLU A  62    11829  11118   9080   3916   2144  -1167       C  
ATOM    297  O   GLU A  62      26.644  24.289  33.563  1.00 78.83           O  
ANISOU  297  O   GLU A  62    10824  10687   8442   3869   2359  -1072       O  
ATOM    298  CB  GLU A  62      28.689  24.549  36.045  1.00 94.03           C  
ANISOU  298  CB  GLU A  62    13675  12476   9575   3845   2275  -1404       C  
ATOM    299  CG  GLU A  62      27.846  23.590  36.847  1.00101.12           C  
ANISOU  299  CG  GLU A  62    14529  13731  10159   3733   2642  -1287       C  
ATOM    300  CD  GLU A  62      27.323  24.199  38.130  1.00123.23           C  
ANISOU  300  CD  GLU A  62    17442  16746  12633   3930   2955  -1586       C  
ATOM    301  OE1 GLU A  62      28.012  25.070  38.698  1.00121.86           O  
ANISOU  301  OE1 GLU A  62    17531  16450  12318   4083   2815  -1889       O  
ATOM    302  OE2 GLU A  62      26.214  23.815  38.563  1.00121.25           O  
ANISOU  302  OE2 GLU A  62    16998  16793  12277   3923   3353  -1546       O  
ATOM    303  N   GLU A  63      28.019  26.042  33.222  1.00 92.03           N  
ANISOU  303  N   GLU A  63    12810  11820  10336   4136   1978  -1280       N  
ATOM    304  CA  GLU A  63      27.030  26.824  32.493  1.00 99.22           C  
ANISOU  304  CA  GLU A  63    13380  12729  11592   4401   2041  -1285       C  
ATOM    305  C   GLU A  63      27.139  26.706  30.979  1.00 98.67           C  
ANISOU  305  C   GLU A  63    13106  12588  11794   4364   1785  -1007       C  
ATOM    306  O   GLU A  63      26.153  26.979  30.286  1.00 96.23           O  
ANISOU  306  O   GLU A  63    12442  12415  11704   4544   1824   -933       O  
ATOM    307  CB  GLU A  63      27.136  28.309  32.871  1.00106.09           C  
ANISOU  307  CB  GLU A  63    14376  13299  12634   4721   2064  -1567       C  
ATOM    308  CG  GLU A  63      28.383  29.026  32.353  1.00109.84           C  
ANISOU  308  CG  GLU A  63    15097  13334  13305   4712   1763  -1553       C  
ATOM    309  CD  GLU A  63      29.623  28.730  33.180  1.00114.11           C  
ANISOU  309  CD  GLU A  63    16012  13787  13556   4489   1639  -1699       C  
ATOM    310  OE1 GLU A  63      30.714  29.216  32.814  1.00103.14           O  
ANISOU  310  OE1 GLU A  63    14795  12066  12329   4427   1400  -1706       O  
ATOM    311  OE2 GLU A  63      29.507  28.016  34.199  1.00119.71           O  
ANISOU  311  OE2 GLU A  63    16833  14777  13875   4380   1783  -1793       O  
ATOM    312  N   THR A  64      28.297  26.323  30.444  1.00 92.39           N  
ANISOU  312  N   THR A  64    12509  11620  10974   4157   1525   -860       N  
ATOM    313  CA  THR A  64      28.494  26.367  29.001  1.00 85.47           C  
ANISOU  313  CA  THR A  64    11479  10678  10316   4154   1294   -619       C  
ATOM    314  C   THR A  64      29.466  25.283  28.563  1.00 72.13           C  
ANISOU  314  C   THR A  64     9919   8992   8496   3828   1115   -466       C  
ATOM    315  O   THR A  64      30.554  25.151  29.132  1.00 76.32           O  
ANISOU  315  O   THR A  64    10751   9346   8900   3699   1035   -528       O  
ATOM    316  CB  THR A  64      29.015  27.743  28.564  1.00 89.73           C  
ANISOU  316  CB  THR A  64    12133  10838  11120   4391   1167   -621       C  
ATOM    317  OG1 THR A  64      28.095  28.760  28.981  1.00 82.19           O  
ANISOU  317  OG1 THR A  64    11061   9833  10332   4730   1347   -781       O  
ATOM    318  CG2 THR A  64      29.172  27.804  27.050  1.00 85.51           C  
ANISOU  318  CG2 THR A  64    11452  10286  10753   4410    958   -320       C  
ATOM    319  N   LEU A  65      29.065  24.515  27.554  1.00 74.89           N  
ANISOU  319  N   LEU A  65    10019   9554   8884   3711   1042   -295       N  
ATOM    320  CA  LEU A  65      29.976  23.632  26.840  1.00 71.87           C  
ANISOU  320  CA  LEU A  65     9720   9140   8447   3456    857   -160       C  
ATOM    321  C   LEU A  65      30.565  24.406  25.668  1.00 70.88           C  
ANISOU  321  C   LEU A  65     9595   8853   8481   3573    650    -17       C  
ATOM    322  O   LEU A  65      29.826  24.890  24.803  1.00 62.48           O  
ANISOU  322  O   LEU A  65     8287   7918   7535   3758    609     88       O  
ATOM    323  CB  LEU A  65      29.261  22.374  26.352  1.00 64.06           C  
ANISOU  323  CB  LEU A  65     8470   8452   7418   3245    898   -105       C  
ATOM    324  CG  LEU A  65      30.110  21.473  25.451  1.00 72.99           C  
ANISOU  324  CG  LEU A  65     9652   9554   8527   3013    715     -6       C  
ATOM    325  CD1 LEU A  65      31.276  20.882  26.231  1.00 71.34           C  
ANISOU  325  CD1 LEU A  65     9781   9127   8196   2843    702    -17       C  
ATOM    326  CD2 LEU A  65      29.270  20.379  24.807  1.00 65.38           C  
ANISOU  326  CD2 LEU A  65     8381   8876   7583   2821    741    -14       C  
ATOM    327  N   THR A  66      31.888  24.536  25.648  1.00 58.97           N  
ANISOU  327  N   THR A  66     8348   7083   6974   3476    525      4       N  
ATOM    328  CA  THR A  66      32.589  25.309  24.632  1.00 68.72           C  
ANISOU  328  CA  THR A  66     9620   8126   8364   3555    379    161       C  
ATOM    329  C   THR A  66      33.348  24.369  23.705  1.00 68.57           C  
ANISOU  329  C   THR A  66     9591   8199   8265   3331    247    282       C  
ATOM    330  O   THR A  66      34.078  23.487  24.170  1.00 54.31           O  
ANISOU  330  O   THR A  66     7917   6361   6357   3118    225    206       O  
ATOM    331  CB  THR A  66      33.550  26.314  25.274  1.00 59.07           C  
ANISOU  331  CB  THR A  66     8661   6514   7270   3605    363     58       C  
ATOM    332  OG1 THR A  66      32.807  27.236  26.080  1.00 64.55           O  
ANISOU  332  OG1 THR A  66     9364   7108   8053   3837    500   -101       O  
ATOM    333  CG2 THR A  66      34.310  27.086  24.201  1.00 59.11           C  
ANISOU  333  CG2 THR A  66     8699   6289   7470   3645    260    260       C  
ATOM    334  N   ILE A  67      33.164  24.558  22.398  1.00 56.49           N  
ANISOU  334  N   ILE A  67     7904   6795   6764   3405    161    469       N  
ATOM    335  CA  ILE A  67      33.837  23.775  21.367  1.00 59.63           C  
ANISOU  335  CA  ILE A  67     8276   7314   7068   3227     53    561       C  
ATOM    336  C   ILE A  67      34.533  24.741  20.419  1.00 55.53           C  
ANISOU  336  C   ILE A  67     7820   6641   6637   3338     -9    781       C  
ATOM    337  O   ILE A  67      33.918  25.704  19.949  1.00 58.43           O  
ANISOU  337  O   ILE A  67     8107   7012   7083   3586     -7    948       O  
ATOM    338  CB  ILE A  67      32.852  22.875  20.595  1.00 62.96           C  
ANISOU  338  CB  ILE A  67     8418   8144   7360   3175     17    553       C  
ATOM    339  CG1 ILE A  67      32.229  21.840  21.534  1.00 55.13           C  
ANISOU  339  CG1 ILE A  67     7366   7254   6326   3008    125    359       C  
ATOM    340  CG2 ILE A  67      33.547  22.204  19.412  1.00 54.40           C  
ANISOU  340  CG2 ILE A  67     7313   7194   6162   3027    -91    611       C  
ATOM    341  CD1 ILE A  67      31.105  21.038  20.906  1.00 56.53           C  
ANISOU  341  CD1 ILE A  67     7219   7812   6449   2932    111    295       C  
ATOM    342  N   ARG A  68      35.812  24.494  20.148  1.00 53.97           N  
ANISOU  342  N   ARG A  68     7757   6302   6446   3167    -46    803       N  
ATOM    343  CA  ARG A  68      36.582  25.308  19.218  1.00 56.71           C  
ANISOU  343  CA  ARG A  68     8161   6510   6877   3218    -57   1033       C  
ATOM    344  C   ARG A  68      37.268  24.405  18.202  1.00 63.05           C  
ANISOU  344  C   ARG A  68     8914   7526   7515   3047   -101   1078       C  
ATOM    345  O   ARG A  68      37.852  23.379  18.565  1.00 57.54           O  
ANISOU  345  O   ARG A  68     8247   6842   6774   2847   -118    895       O  
ATOM    346  CB  ARG A  68      37.619  26.171  19.951  1.00 55.11           C  
ANISOU  346  CB  ARG A  68     8157   5862   6919   3176    -16    987       C  
ATOM    347  CG  ARG A  68      37.024  27.201  20.901  1.00 56.96           C  
ANISOU  347  CG  ARG A  68     8463   5844   7335   3359     44    899       C  
ATOM    348  CD  ARG A  68      38.000  28.346  21.138  1.00 60.45           C  
ANISOU  348  CD  ARG A  68     9066   5827   8075   3340     83    910       C  
ATOM    349  NE  ARG A  68      37.506  29.317  22.113  1.00 64.77           N  
ANISOU  349  NE  ARG A  68     9700   6093   8816   3504    146    744       N  
ATOM    350  CZ  ARG A  68      38.130  29.632  23.245  1.00 61.04           C  
ANISOU  350  CZ  ARG A  68     9371   5358   8465   3405    137    445       C  
ATOM    351  NH1 ARG A  68      39.287  29.063  23.549  1.00 59.35           N  
ANISOU  351  NH1 ARG A  68     9210   5132   8209   3153     47    312       N  
ATOM    352  NH2 ARG A  68      37.604  30.525  24.072  1.00 77.26           N  
ANISOU  352  NH2 ARG A  68    11501   7177  10676   3573    210    254       N  
ATOM    353  N   ALA A  69      37.189  24.793  16.933  1.00 69.60           N  
ANISOU  353  N   ALA A  69     9673   8530   8242   3150   -111   1327       N  
ATOM    354  CA  ALA A  69      37.760  24.040  15.825  1.00 56.33           C  
ANISOU  354  CA  ALA A  69     7937   7112   6356   3024   -131   1362       C  
ATOM    355  C   ALA A  69      38.163  25.032  14.744  1.00 64.08           C  
ANISOU  355  C   ALA A  69     8959   8083   7307   3150    -75   1718       C  
ATOM    356  O   ALA A  69      37.641  26.153  14.704  1.00 67.60           O  
ANISOU  356  O   ALA A  69     9431   8394   7858   3374    -55   1957       O  
ATOM    357  CB  ALA A  69      36.763  23.002  15.287  1.00 55.51           C  
ANISOU  357  CB  ALA A  69     7633   7462   5994   3008   -223   1224       C  
ATOM    358  N   PRO A  70      39.100  24.656  13.853  1.00 64.67           N  
ANISOU  358  N   PRO A  70     9043   8283   7248   3023    -22   1780       N  
ATOM    359  CA  PRO A  70      39.637  25.638  12.894  1.00 60.89           C  
ANISOU  359  CA  PRO A  70     8631   7755   6750   3112     91   2165       C  
ATOM    360  C   PRO A  70      38.665  26.008  11.787  1.00 70.07           C  
ANISOU  360  C   PRO A  70     9715   9304   7605   3366     28   2462       C  
ATOM    361  O   PRO A  70      39.032  26.755  10.875  1.00 80.35           O  
ANISOU  361  O   PRO A  70    11086  10627   8817   3465    130   2844       O  
ATOM    362  CB  PRO A  70      40.873  24.935  12.311  1.00 60.26           C  
ANISOU  362  CB  PRO A  70     8547   7773   6576   2892    186   2085       C  
ATOM    363  CG  PRO A  70      41.100  23.730  13.170  1.00 56.91           C  
ANISOU  363  CG  PRO A  70     8082   7319   6221   2708    111   1663       C  
ATOM    364  CD  PRO A  70      39.779  23.356  13.738  1.00 56.03           C  
ANISOU  364  CD  PRO A  70     7906   7333   6048   2797    -27   1507       C  
ATOM    365  N   PHE A  71      37.430  25.526  11.865  1.00 70.40           N  
ANISOU  365  N   PHE A  71     9603   9660   7488   3478   -135   2313       N  
ATOM    366  CA  PHE A  71      36.466  25.675  10.788  1.00 76.67           C  
ANISOU  366  CA  PHE A  71    10259  10935   7936   3717   -259   2527       C  
ATOM    367  C   PHE A  71      35.553  26.868  11.037  1.00 84.08           C  
ANISOU  367  C   PHE A  71    11189  11715   9043   4050   -296   2818       C  
ATOM    368  O   PHE A  71      35.275  27.236  12.182  1.00 80.26           O  
ANISOU  368  O   PHE A  71    10736  10860   8900   4076   -264   2689       O  
ATOM    369  CB  PHE A  71      35.644  24.397  10.638  1.00 77.83           C  
ANISOU  369  CB  PHE A  71    10181  11557   7836   3624   -429   2152       C  
ATOM    370  CG  PHE A  71      36.469  23.145  10.691  1.00 78.93           C  
ANISOU  370  CG  PHE A  71    10337  11721   7932   3301   -379   1791       C  
ATOM    371  CD1 PHE A  71      37.392  22.866   9.694  1.00 65.05           C  
ANISOU  371  CD1 PHE A  71     8636  10147   5934   3213   -300   1844       C  
ATOM    372  CD2 PHE A  71      36.322  22.247  11.735  1.00 70.15           C  
ANISOU  372  CD2 PHE A  71     9187  10445   7021   3105   -390   1416       C  
ATOM    373  CE1 PHE A  71      38.152  21.714   9.739  1.00 63.01           C  
ANISOU  373  CE1 PHE A  71     8378   9887   5675   2954   -244   1495       C  
ATOM    374  CE2 PHE A  71      37.078  21.094  11.785  1.00 67.35           C  
ANISOU  374  CE2 PHE A  71     8856  10068   6666   2848   -344   1116       C  
ATOM    375  CZ  PHE A  71      37.995  20.828  10.787  1.00 66.71           C  
ANISOU  375  CZ  PHE A  71     8815  10150   6383   2781   -277   1138       C  
ATOM    376  N   LEU A  72      35.092  27.465   9.940  1.00 77.20           N  
ANISOU  376  N   LEU A  72    10277  11146   7909   4329   -362   3213       N  
ATOM    377  CA  LEU A  72      34.251  28.650  10.016  1.00 87.75           C  
ANISOU  377  CA  LEU A  72    11598  12323   9421   4674   -393   3529       C  
ATOM    378  C   LEU A  72      32.929  28.322  10.695  1.00 96.13           C  
ANISOU  378  C   LEU A  72    12408  13569  10549   4808   -558   3251       C  
ATOM    379  O   LEU A  72      32.312  27.287  10.431  1.00102.38           O  
ANISOU  379  O   LEU A  72    12964  14874  11062   4739   -726   2979       O  
ATOM    380  CB  LEU A  72      34.000  29.207   8.615  1.00 89.17           C  
ANISOU  380  CB  LEU A  72    11754  12836   9291   4817   -435   3905       C  
ATOM    381  CG  LEU A  72      33.201  30.510   8.523  1.00 96.56           C  
ANISOU  381  CG  LEU A  72    12679  13555  10455   5067   -445   4190       C  
ATOM    382  CD1 LEU A  72      34.057  31.704   8.920  1.00 96.91           C  
ANISOU  382  CD1 LEU A  72    12994  12880  10945   5016   -198   4436       C  
ATOM    383  CD2 LEU A  72      32.621  30.702   7.129  1.00 93.07           C  
ANISOU  383  CD2 LEU A  72    12134  13639   9590   5253   -584   4478       C  
ATOM    384  N   ALA A  73      32.489  29.224  11.566  1.00 88.13           N  
ANISOU  384  N   ALA A  73    11425  12119   9939   4923   -482   3252       N  
ATOM    385  CA  ALA A  73      31.297  28.978  12.362  1.00 82.50           C  
ANISOU  385  CA  ALA A  73    10474  11533   9339   5053   -574   2984       C  
ATOM    386  C   ALA A  73      30.043  29.064  11.501  1.00 92.32           C  
ANISOU  386  C   ALA A  73    11418  13302  10356   5281   -777   3092       C  
ATOM    387  O   ALA A  73      29.849  30.033  10.760  1.00 98.02           O  
ANISOU  387  O   ALA A  73    12184  13983  11077   5451   -791   3431       O  
ATOM    388  CB  ALA A  73      31.218  29.979  13.512  1.00 77.91           C  
ANISOU  388  CB  ALA A  73    10020  10351   9232   5123   -415   2931       C  
ATOM    389  N   ALA A  74      29.194  28.045  11.594  1.00101.53           N  
ANISOU  389  N   ALA A  74    12265  14966  11344   5281   -941   2800       N  
ATOM    390  CA  ALA A  74      27.879  28.128  10.981  1.00107.59           C  
ANISOU  390  CA  ALA A  74    12682  16227  11969   5492  -1148   2823       C  
ATOM    391  C   ALA A  74      27.094  29.271  11.623  1.00109.82           C  
ANISOU  391  C   ALA A  74    12920  16166  12641   5749  -1071   2923       C  
ATOM    392  O   ALA A  74      27.142  29.445  12.846  1.00109.59           O  
ANISOU  392  O   ALA A  74    12964  15726  12948   5731   -900   2742       O  
ATOM    393  CB  ALA A  74      27.123  26.808  11.141  1.00108.48           C  
ANISOU  393  CB  ALA A  74    12410  16894  11913   5394  -1318   2418       C  
ATOM    394  N   PRO A  75      26.358  30.062  10.839  1.00107.80           N  
ANISOU  394  N   PRO A  75    12547  16074  12340   6006  -1195   3192       N  
ATOM    395  CA  PRO A  75      25.808  31.323  11.354  1.00112.37           C  
ANISOU  395  CA  PRO A  75    13149  16224  13321   6272  -1105   3340       C  
ATOM    396  C   PRO A  75      24.571  31.183  12.231  1.00116.38           C  
ANISOU  396  C   PRO A  75    13301  16864  14054   6422  -1126   3046       C  
ATOM    397  O   PRO A  75      24.084  32.201  12.736  1.00111.92           O  
ANISOU  397  O   PRO A  75    12739  15942  13842   6654  -1038   3117       O  
ATOM    398  CB  PRO A  75      25.472  32.087  10.067  1.00109.79           C  
ANISOU  398  CB  PRO A  75    12809  16095  12811   6509  -1260   3757       C  
ATOM    399  CG  PRO A  75      25.115  31.011   9.099  1.00104.08           C  
ANISOU  399  CG  PRO A  75    11827  16134  11586   6434  -1507   3653       C  
ATOM    400  CD  PRO A  75      26.011  29.842   9.424  1.00 97.96           C  
ANISOU  400  CD  PRO A  75    11148  15417  10656   6079  -1432   3361       C  
ATOM    401  N   ASP A  76      24.051  29.972  12.441  1.00114.53           N  
ANISOU  401  N   ASP A  76    12743  17120  13653   6294  -1220   2705       N  
ATOM    402  CA  ASP A  76      22.761  29.785  13.097  1.00122.42           C  
ANISOU  402  CA  ASP A  76    13315  18361  14837   6431  -1240   2440       C  
ATOM    403  C   ASP A  76      22.856  28.929  14.354  1.00111.74           C  
ANISOU  403  C   ASP A  76    11901  16936  13620   6231  -1049   2045       C  
ATOM    404  O   ASP A  76      21.830  28.435  14.835  1.00114.31           O  
ANISOU  404  O   ASP A  76    11807  17590  14035   6259  -1047   1771       O  
ATOM    405  CB  ASP A  76      21.764  29.158  12.121  1.00140.52           C  
ANISOU  405  CB  ASP A  76    15149  21403  16838   6476  -1546   2375       C  
ATOM    406  CG  ASP A  76      22.222  27.799  11.621  1.00141.19           C  
ANISOU  406  CG  ASP A  76    15160  21935  16550   6153  -1676   2154       C  
ATOM    407  OD1 ASP A  76      23.449  27.597  11.489  1.00128.15           O  
ANISOU  407  OD1 ASP A  76    13889  20042  14761   5970  -1590   2240       O  
ATOM    408  OD2 ASP A  76      21.357  26.932  11.368  1.00147.47           O  
ANISOU  408  OD2 ASP A  76    15498  23316  17220   6067  -1861   1866       O  
ATOM    409  N   ILE A  77      24.056  28.747  14.896  1.00114.38           N  
ANISOU  409  N   ILE A  77    12627  16856  13976   6029   -876   2012       N  
ATOM    410  CA  ILE A  77      24.299  27.801  15.985  1.00101.95           C  
ANISOU  410  CA  ILE A  77    11067  15212  12459   5749   -699   1644       C  
ATOM    411  C   ILE A  77      23.414  28.133  17.180  1.00 99.54           C  
ANISOU  411  C   ILE A  77    10578  14786  12455   5900   -493   1428       C  
ATOM    412  O   ILE A  77      23.528  29.226  17.753  1.00 96.47           O  
ANISOU  412  O   ILE A  77    10399  13933  12323   6126   -344   1517       O  
ATOM    413  CB  ILE A  77      25.782  27.786  16.379  1.00 85.39           C  
ANISOU  413  CB  ILE A  77     9486  12589  10370   5465   -548   1656       C  
ATOM    414  CG1 ILE A  77      26.629  27.316  15.194  1.00 83.03           C  
ANISOU  414  CG1 ILE A  77     9318  12470   9758   5287   -711   1821       C  
ATOM    415  CG2 ILE A  77      25.998  26.897  17.595  1.00 76.29           C  
ANISOU  415  CG2 ILE A  77     8418  11288   9279   5076   -347   1269       C  
ATOM    416  CD1 ILE A  77      28.122  27.402  15.426  1.00 79.77           C  
ANISOU  416  CD1 ILE A  77     9358  11574   9377   5050   -578   1874       C  
ATOM    417  N   PRO A  78      22.516  27.228  17.575  1.00 98.45           N  
ANISOU  417  N   PRO A  78    10063  15030  12314   5709   -453   1112       N  
ATOM    418  CA  PRO A  78      21.629  27.507  18.710  1.00100.17           C  
ANISOU  418  CA  PRO A  78    10074  15193  12794   5848   -213    901       C  
ATOM    419  C   PRO A  78      22.409  27.832  19.977  1.00 98.20           C  
ANISOU  419  C   PRO A  78    10271  14370  12669   5738     85    780       C  
ATOM    420  O   PRO A  78      23.541  27.385  20.173  1.00 91.21           O  
ANISOU  420  O   PRO A  78     9776  13219  11660   5408    119    753       O  
ATOM    421  CB  PRO A  78      20.834  26.206  18.864  1.00 96.95           C  
ANISOU  421  CB  PRO A  78     9254  15261  12321   5492   -187    585       C  
ATOM    422  CG  PRO A  78      20.847  25.603  17.504  1.00 96.63           C  
ANISOU  422  CG  PRO A  78     9029  15654  12032   5383   -523    662       C  
ATOM    423  CD  PRO A  78      22.186  25.954  16.916  1.00 99.56           C  
ANISOU  423  CD  PRO A  78     9905  15694  12229   5376   -621    930       C  
ATOM    424  N   ARG A  79      21.779  28.618  20.848  1.00102.80           N  
ANISOU  424  N   ARG A  79    10774  14791  13496   6038    293    679       N  
ATOM    425  CA  ARG A  79      22.437  29.111  22.050  1.00100.93           C  
ANISOU  425  CA  ARG A  79    10946  14038  13365   6006    554    529       C  
ATOM    426  C   ARG A  79      22.307  28.156  23.234  1.00 97.69           C  
ANISOU  426  C   ARG A  79    10544  13724  12850   5641    814    197       C  
ATOM    427  O   ARG A  79      23.273  27.969  23.982  1.00 87.11           O  
ANISOU  427  O   ARG A  79     9619  12066  11412   5397    924     95       O  
ATOM    428  CB  ARG A  79      21.869  30.484  22.427  1.00 93.87           C  
ANISOU  428  CB  ARG A  79    10017  12866  12782   6451    666    539       C  
ATOM    429  N   PHE A  80      21.140  27.542  23.423  1.00105.88           N  
ANISOU  429  N   PHE A  80    11120  15204  13904   5598    917     43       N  
ATOM    430  CA  PHE A  80      20.828  26.847  24.666  1.00107.58           C  
ANISOU  430  CA  PHE A  80    11323  15492  14060   5334   1248   -230       C  
ATOM    431  C   PHE A  80      20.615  25.355  24.446  1.00101.58           C  
ANISOU  431  C   PHE A  80    10357  15080  13157   4863   1237   -294       C  
ATOM    432  O   PHE A  80      20.070  24.934  23.420  1.00 98.69           O  
ANISOU  432  O   PHE A  80     9609  15077  12814   4828   1018   -240       O  
ATOM    433  CB  PHE A  80      19.585  27.454  25.336  1.00107.24           C  
ANISOU  433  CB  PHE A  80    10910  15617  14221   5672   1504   -399       C  
ATOM    434  CG  PHE A  80      19.801  28.846  25.852  1.00109.08           C  
ANISOU  434  CG  PHE A  80    11394  15428  14622   6101   1606   -431       C  
ATOM    435  CD1 PHE A  80      19.657  29.938  25.014  1.00108.59           C  
ANISOU  435  CD1 PHE A  80    11256  15216  14788   6540   1395   -221       C  
ATOM    436  CD2 PHE A  80      20.164  29.061  27.170  1.00107.55           C  
ANISOU  436  CD2 PHE A  80    11535  14972  14356   6049   1906   -673       C  
ATOM    437  CE1 PHE A  80      19.869  31.223  25.482  1.00104.26           C  
ANISOU  437  CE1 PHE A  80    10993  14159  14462   6739   1469   -269       C  
ATOM    438  CE2 PHE A  80      20.375  30.341  27.644  1.00107.04           C  
ANISOU  438  CE2 PHE A  80    11704  14495  14473   6422   1998   -774       C  
ATOM    439  CZ  PHE A  80      20.227  31.423  26.800  1.00105.12           C  
ANISOU  439  CZ  PHE A  80    11407  14006  14529   6679   1767   -574       C  
ATOM    440  N   PHE A  81      21.048  24.564  25.428  1.00 95.95           N  
ANISOU  440  N   PHE A  81     9906  14249  12300   4507   1471   -415       N  
ATOM    441  CA  PHE A  81      20.826  23.128  25.458  1.00 95.19           C  
ANISOU  441  CA  PHE A  81     9657  14384  12126   4045   1551   -484       C  
ATOM    442  C   PHE A  81      19.445  22.817  26.031  1.00 99.13           C  
ANISOU  442  C   PHE A  81     9666  15242  12757   4015   1853   -649       C  
ATOM    443  O   PHE A  81      18.817  23.678  26.653  1.00 93.55           O  
ANISOU  443  O   PHE A  81     8828  14568  12148   4345   2053   -733       O  
ATOM    444  CB  PHE A  81      21.908  22.448  26.294  1.00 86.79           C  
ANISOU  444  CB  PHE A  81     9106  13011  10859   3721   1679   -480       C  
ATOM    445  CG  PHE A  81      23.166  22.144  25.531  1.00 87.03           C  
ANISOU  445  CG  PHE A  81     9467  12814  10786   3570   1385   -347       C  
ATOM    446  CD1 PHE A  81      23.141  21.271  24.456  1.00 81.95           C  
ANISOU  446  CD1 PHE A  81     8626  12358  10152   3335   1182   -321       C  
ATOM    447  CD2 PHE A  81      24.373  22.718  25.897  1.00 85.89           C  
ANISOU  447  CD2 PHE A  81     9807  12285  10542   3653   1322   -287       C  
ATOM    448  CE1 PHE A  81      24.293  20.981  23.754  1.00 80.16           C  
ANISOU  448  CE1 PHE A  81     8688  11945   9824   3210    948   -223       C  
ATOM    449  CE2 PHE A  81      25.530  22.432  25.199  1.00 87.45           C  
ANISOU  449  CE2 PHE A  81    10264  12296  10667   3512   1082   -172       C  
ATOM    450  CZ  PHE A  81      25.489  21.561  24.125  1.00 83.14           C  
ANISOU  450  CZ  PHE A  81     9527  11946  10118   3302    909   -133       C  
ATOM    451  N   PRO A  82      18.945  21.595  25.824  1.00103.38           N  
ANISOU  451  N   PRO A  82     9907  16043  13332   3616   1911   -717       N  
ATOM    452  CA  PRO A  82      17.625  21.232  26.358  1.00101.40           C  
ANISOU  452  CA  PRO A  82     9141  16141  13244   3527   2234   -875       C  
ATOM    453  C   PRO A  82      17.507  21.504  27.852  1.00112.93           C  
ANISOU  453  C   PRO A  82    10812  17482  14616   3588   2690   -936       C  
ATOM    454  O   PRO A  82      18.429  21.247  28.628  1.00106.82           O  
ANISOU  454  O   PRO A  82    10575  16400  13611   3435   2814   -873       O  
ATOM    455  CB  PRO A  82      17.527  19.737  26.046  1.00103.20           C  
ANISOU  455  CB  PRO A  82     9217  16485  13509   2975   2253   -924       C  
ATOM    456  CG  PRO A  82      18.295  19.596  24.787  1.00 94.51           C  
ANISOU  456  CG  PRO A  82     8251  15319  12339   2944   1798   -850       C  
ATOM    457  CD  PRO A  82      19.446  20.572  24.888  1.00 95.79           C  
ANISOU  457  CD  PRO A  82     8971  15102  12322   3258   1656   -683       C  
ATOM    458  N   GLU A  83      16.347  22.032  28.244  1.00121.91           N  
ANISOU  458  N   GLU A  83    11497  18903  15922   3833   2934  -1070       N  
ATOM    459  CA  GLU A  83      16.121  22.442  29.630  1.00128.46           C  
ANISOU  459  CA  GLU A  83    12481  19684  16645   3962   3389  -1172       C  
ATOM    460  C   GLU A  83      16.277  21.313  30.647  1.00130.71           C  
ANISOU  460  C   GLU A  83    12995  19944  16726   3498   3779  -1142       C  
ATOM    461  O   GLU A  83      16.948  21.532  31.672  1.00133.30           O  
ANISOU  461  O   GLU A  83    13835  20047  16765   3541   3969  -1130       O  
ATOM    462  CB  GLU A  83      14.739  23.098  29.734  1.00136.57           C  
ANISOU  462  CB  GLU A  83    12877  21077  17937   4299   3594  -1340       C  
ATOM    463  CG  GLU A  83      14.087  22.961  31.097  1.00144.89           C  
ANISOU  463  CG  GLU A  83    13850  22287  18913   4240   4187  -1485       C  
ATOM    464  CD  GLU A  83      14.749  23.815  32.160  1.00147.58           C  
ANISOU  464  CD  GLU A  83    14755  22330  18988   4518   4375  -1561       C  
ATOM    465  OE1 GLU A  83      14.867  25.040  31.946  1.00150.71           O  
ANISOU  465  OE1 GLU A  83    15214  22555  19493   5002   4200  -1636       O  
ATOM    466  OE2 GLU A  83      15.149  23.263  33.208  1.00146.61           O  
ANISOU  466  OE2 GLU A  83    15015  22141  18548   4256   4692  -1546       O  
ATOM    467  N   PRO A  84      15.703  20.120  30.459  1.00130.33           N  
ANISOU  467  N   PRO A  84    12607  20106  16807   3055   3915  -1127       N  
ATOM    468  CA  PRO A  84      15.700  19.134  31.550  1.00130.35           C  
ANISOU  468  CA  PRO A  84    12807  20076  16643   2658   4376  -1053       C  
ATOM    469  C   PRO A  84      17.100  18.776  32.038  1.00125.04           C  
ANISOU  469  C   PRO A  84    12890  18996  15623   2523   4297   -870       C  
ATOM    470  O   PRO A  84      18.001  18.479  31.249  1.00125.15           O  
ANISOU  470  O   PRO A  84    13147  18770  15633   2422   3901   -776       O  
ATOM    471  CB  PRO A  84      14.991  17.921  30.931  1.00130.84           C  
ANISOU  471  CB  PRO A  84    12377  20335  17001   2182   4419  -1064       C  
ATOM    472  CG  PRO A  84      15.032  18.142  29.454  1.00125.06           C  
ANISOU  472  CG  PRO A  84    11369  19677  16470   2291   3869  -1133       C  
ATOM    473  CD  PRO A  84      14.940  19.622  29.299  1.00124.49           C  
ANISOU  473  CD  PRO A  84    11253  19665  16383   2893   3688  -1192       C  
ATOM    474  N   ARG A  85      17.271  18.815  33.358  1.00121.68           N  
ANISOU  474  N   ARG A  85    12816  18532  14885   2542   4679   -829       N  
ATOM    475  CA  ARG A  85      18.510  18.371  33.981  1.00116.04           C  
ANISOU  475  CA  ARG A  85    12778  17503  13811   2408   4637   -644       C  
ATOM    476  C   ARG A  85      18.684  16.868  33.812  1.00112.59           C  
ANISOU  476  C   ARG A  85    12388  16947  13445   1901   4704   -427       C  
ATOM    477  O   ARG A  85      17.711  16.109  33.829  1.00118.69           O  
ANISOU  477  O   ARG A  85    12747  17909  14440   1599   5022   -414       O  
ATOM    478  CB  ARG A  85      18.516  18.724  35.470  1.00113.18           C  
ANISOU  478  CB  ARG A  85    12736  17222  13046   2552   5048   -664       C  
ATOM    479  CG  ARG A  85      19.266  19.998  35.814  1.00105.56           C  
ANISOU  479  CG  ARG A  85    12149  16109  11850   2983   4838   -831       C  
ATOM    480  CD  ARG A  85      18.953  20.479  37.221  1.00110.69           C  
ANISOU  480  CD  ARG A  85    12973  16953  12131   3169   5281   -967       C  
ATOM    481  NE  ARG A  85      18.394  21.828  37.204  1.00110.13           N  
ANISOU  481  NE  ARG A  85    12664  16973  12209   3616   5306  -1289       N  
ATOM    482  CZ  ARG A  85      17.115  22.114  37.422  1.00118.54           C  
ANISOU  482  CZ  ARG A  85    13229  18366  13446   3749   5690  -1450       C  
ATOM    483  NH1 ARG A  85      16.251  21.146  37.693  1.00123.53           N  
ANISOU  483  NH1 ARG A  85    13532  19285  14119   3428   6100  -1322       N  
ATOM    484  NH2 ARG A  85      16.702  23.373  37.380  1.00120.70           N  
ANISOU  484  NH2 ARG A  85    13317  18659  13884   4204   5682  -1740       N  
ATOM    485  N   GLY A  86      19.927  16.436  33.660  1.00106.70           N  
ANISOU  485  N   GLY A  86    12130  15865  12547   1804   4419   -266       N  
ATOM    486  CA  GLY A  86      20.208  15.018  33.588  1.00107.74           C  
ANISOU  486  CA  GLY A  86    12381  15803  12752   1365   4494    -51       C  
ATOM    487  C   GLY A  86      21.492  14.739  32.831  1.00106.92           C  
ANISOU  487  C   GLY A  86    12620  15357  12646   1337   4024     24       C  
ATOM    488  O   GLY A  86      22.228  15.648  32.448  1.00 99.99           O  
ANISOU  488  O   GLY A  86    11921  14397  11675   1639   3664    -62       O  
ATOM    489  N   LEU A  87      21.732  13.446  32.625  1.00103.18           N  
ANISOU  489  N   LEU A  87    12221  14669  12314    960   4067    183       N  
ATOM    490  CA  LEU A  87      22.929  12.955  31.956  1.00 93.09           C  
ANISOU  490  CA  LEU A  87    11252  13055  11063    894   3690    257       C  
ATOM    491  C   LEU A  87      22.671  12.887  30.456  1.00 94.45           C  
ANISOU  491  C   LEU A  87    11019  13286  11582    806   3372     41       C  
ATOM    492  O   LEU A  87      21.715  12.241  30.015  1.00102.64           O  
ANISOU  492  O   LEU A  87    11618  14454  12926    517   3518    -66       O  
ATOM    493  CB  LEU A  87      23.311  11.580  32.501  1.00 94.36           C  
ANISOU  493  CB  LEU A  87    11707  12918  11226    565   3912    534       C  
ATOM    494  CG  LEU A  87      24.750  11.372  32.969  1.00 91.41           C  
ANISOU  494  CG  LEU A  87    11928  12235  10567    688   3718    755       C  
ATOM    495  CD1 LEU A  87      25.148  12.443  33.966  1.00 94.52           C  
ANISOU  495  CD1 LEU A  87    12626  12780  10510   1050   3712    771       C  
ATOM    496  CD2 LEU A  87      24.889   9.994  33.586  1.00 96.15           C  
ANISOU  496  CD2 LEU A  87    12773  12558  11204    388   4008   1077       C  
ATOM    497  N   TYR A  88      23.528  13.543  29.677  1.00 84.47           N  
ANISOU  497  N   TYR A  88     9892  11946  10259   1042   2944    -31       N  
ATOM    498  CA  TYR A  88      23.349  13.674  28.236  1.00 86.58           C  
ANISOU  498  CA  TYR A  88     9814  12337  10746   1039   2613   -222       C  
ATOM    499  C   TYR A  88      24.518  13.024  27.510  1.00 85.90           C  
ANISOU  499  C   TYR A  88    10003  11957  10680    923   2328   -190       C  
ATOM    500  O   TYR A  88      25.667  13.449  27.672  1.00 84.36           O  
ANISOU  500  O   TYR A  88    10207  11560  10287   1121   2145    -87       O  
ATOM    501  CB  TYR A  88      23.224  15.145  27.836  1.00 85.82           C  
ANISOU  501  CB  TYR A  88     9590  12448  10571   1458   2389   -317       C  
ATOM    502  CG  TYR A  88      21.822  15.692  27.954  1.00101.25           C  
ANISOU  502  CG  TYR A  88    11048  14772  12651   1569   2578   -445       C  
ATOM    503  CD1 TYR A  88      20.740  14.997  27.428  1.00107.61           C  
ANISOU  503  CD1 TYR A  88    11327  15831  13729   1300   2664   -583       C  
ATOM    504  CD2 TYR A  88      21.577  16.897  28.600  1.00109.28           C  
ANISOU  504  CD2 TYR A  88    12096  15884  13543   1942   2673   -460       C  
ATOM    505  CE1 TYR A  88      19.454  15.492  27.534  1.00115.75           C  
ANISOU  505  CE1 TYR A  88    11845  17234  14903   1415   2831   -710       C  
ATOM    506  CE2 TYR A  88      20.297  17.399  28.709  1.00113.55           C  
ANISOU  506  CE2 TYR A  88    12155  16763  14227   2081   2858   -588       C  
ATOM    507  CZ  TYR A  88      19.240  16.695  28.176  1.00119.95           C  
ANISOU  507  CZ  TYR A  88    12416  17853  15305   1824   2933   -700       C  
ATOM    508  OH  TYR A  88      17.965  17.197  28.288  1.00128.16           O  
ANISOU  508  OH  TYR A  88    12922  19262  16513   1977   3112   -836       O  
ATOM    509  N   HIS A  89      24.222  11.998  26.716  1.00 81.93           N  
ANISOU  509  N   HIS A  89     9262  11434  10434    598   2297   -313       N  
ATOM    510  CA  HIS A  89      25.215  11.445  25.807  1.00 84.69           C  
ANISOU  510  CA  HIS A  89     9786  11564  10830    515   2014   -365       C  
ATOM    511  C   HIS A  89      25.461  12.413  24.657  1.00 79.74           C  
ANISOU  511  C   HIS A  89     9026  11160  10111    786   1633   -491       C  
ATOM    512  O   HIS A  89      24.529  13.027  24.130  1.00 86.51           O  
ANISOU  512  O   HIS A  89     9480  12380  11011    893   1557   -620       O  
ATOM    513  CB  HIS A  89      24.752  10.093  25.262  1.00 86.62           C  
ANISOU  513  CB  HIS A  89     9794  11722  11394     85   2104   -529       C  
ATOM    514  CG  HIS A  89      25.044   8.940  26.171  1.00 87.68           C  
ANISOU  514  CG  HIS A  89    10225  11449  11640   -182   2414   -333       C  
ATOM    515  ND1 HIS A  89      24.102   8.403  27.023  1.00 89.54           N  
ANISOU  515  ND1 HIS A  89    10319  11679  12022   -431   2828   -241       N  
ATOM    516  CD2 HIS A  89      26.174   8.218  26.358  1.00 88.22           C  
ANISOU  516  CD2 HIS A  89    10718  11096  11705   -220   2383   -182       C  
ATOM    517  CE1 HIS A  89      24.640   7.401  27.695  1.00 88.21           C  
ANISOU  517  CE1 HIS A  89    10510  11085  11921   -612   3042     -6       C  
ATOM    518  NE2 HIS A  89      25.896   7.268  27.310  1.00 91.24           N  
ANISOU  518  NE2 HIS A  89    11235  11209  12222   -472   2761     29       N  
ATOM    519  N   PHE A  90      26.727  12.556  24.273  1.00 67.39           N  
ANISOU  519  N   PHE A  90     7794   9389   8422    911   1402   -428       N  
ATOM    520  CA  PHE A  90      27.097  13.446  23.185  1.00 65.38           C  
ANISOU  520  CA  PHE A  90     7472   9309   8061   1156   1077   -486       C  
ATOM    521  C   PHE A  90      28.186  12.796  22.345  1.00 68.36           C  
ANISOU  521  C   PHE A  90     8030   9503   8440   1053    887   -543       C  
ATOM    522  O   PHE A  90      28.890  11.888  22.794  1.00 64.17           O  
ANISOU  522  O   PHE A  90     7764   8642   7976    889    984   -492       O  
ATOM    523  CB  PHE A  90      27.575  14.816  23.701  1.00 71.63           C  
ANISOU  523  CB  PHE A  90     8488  10060   8668   1523   1021   -323       C  
ATOM    524  CG  PHE A  90      28.937  14.787  24.351  1.00 74.33           C  
ANISOU  524  CG  PHE A  90     9299  10047   8895   1572   1002   -180       C  
ATOM    525  CD1 PHE A  90      30.089  14.966  23.597  1.00 58.06           C  
ANISOU  525  CD1 PHE A  90     7410   7864   6786   1647    766   -161       C  
ATOM    526  CD2 PHE A  90      29.064  14.594  25.718  1.00 74.34           C  
ANISOU  526  CD2 PHE A  90     9550   9878   8816   1551   1220    -64       C  
ATOM    527  CE1 PHE A  90      31.336  14.940  24.191  1.00 64.11           C  
ANISOU  527  CE1 PHE A  90     8544   8337   7477   1693    730    -52       C  
ATOM    528  CE2 PHE A  90      30.311  14.573  26.317  1.00 74.87           C  
ANISOU  528  CE2 PHE A  90    10014   9674   8758   1617   1155     54       C  
ATOM    529  CZ  PHE A  90      31.448  14.743  25.550  1.00 69.66           C  
ANISOU  529  CZ  PHE A  90     9478   8888   8100   1684    900     49       C  
ATOM    530  N   CYS A  91      28.315  13.284  21.113  1.00 75.41           N  
ANISOU  530  N   CYS A  91     8775  10627   9248   1180    626   -635       N  
ATOM    531  CA  CYS A  91      29.419  12.924  20.233  1.00 70.81           C  
ANISOU  531  CA  CYS A  91     8363   9934   8610   1154    449   -690       C  
ATOM    532  C   CYS A  91      29.710  14.109  19.324  1.00 63.39           C  
ANISOU  532  C   CYS A  91     7387   9227   7471   1450    217   -613       C  
ATOM    533  O   CYS A  91      28.788  14.674  18.729  1.00 70.53           O  
ANISOU  533  O   CYS A  91     7981  10499   8320   1566    114   -654       O  
ATOM    534  CB  CYS A  91      29.099  11.681  19.394  1.00 82.91           C  
ANISOU  534  CB  CYS A  91     9683  11539  10281    843    423   -983       C  
ATOM    535  SG  CYS A  91      29.125  10.087  20.260  1.00109.16           S  
ANISOU  535  SG  CYS A  91    13142  14426  13910    465    705  -1042       S  
ATOM    536  N   LEU A  92      30.984  14.485  19.233  1.00 59.82           N  
ANISOU  536  N   LEU A  92     7238   8563   6929   1575    145   -483       N  
ATOM    537  CA  LEU A  92      31.438  15.541  18.337  1.00 61.38           C  
ANISOU  537  CA  LEU A  92     7450   8914   6959   1820    -32   -366       C  
ATOM    538  C   LEU A  92      31.984  14.896  17.070  1.00 63.39           C  
ANISOU  538  C   LEU A  92     7663   9305   7116   1714   -155   -518       C  
ATOM    539  O   LEU A  92      32.952  14.129  17.128  1.00 62.61           O  
ANISOU  539  O   LEU A  92     7756   8953   7080   1581   -111   -587       O  
ATOM    540  CB  LEU A  92      32.504  16.407  19.009  1.00 54.15           C  
ANISOU  540  CB  LEU A  92     6855   7686   6032   1994     -9   -152       C  
ATOM    541  CG  LEU A  92      33.138  17.519  18.174  1.00 58.13           C  
ANISOU  541  CG  LEU A  92     7419   8246   6423   2215   -135     15       C  
ATOM    542  CD1 LEU A  92      32.104  18.562  17.812  1.00 63.21           C  
ANISOU  542  CD1 LEU A  92     7855   9149   7012   2453   -196    127       C  
ATOM    543  CD2 LEU A  92      34.293  18.147  18.930  1.00 51.59           C  
ANISOU  543  CD2 LEU A  92     6890   7054   5658   2293    -98    150       C  
ATOM    544  N   TYR A  93      31.363  15.206  15.934  1.00 76.28           N  
ANISOU  544  N   TYR A  93     9042  11360   8582   1797   -313   -576       N  
ATOM    545  CA  TYR A  93      31.666  14.569  14.659  1.00 73.24           C  
ANISOU  545  CA  TYR A  93     8572  11217   8038   1696   -433   -783       C  
ATOM    546  C   TYR A  93      32.375  15.548  13.734  1.00 73.09           C  
ANISOU  546  C   TYR A  93     8654  11359   7757   1943   -543   -562       C  
ATOM    547  O   TYR A  93      31.969  16.710  13.619  1.00 71.49           O  
ANISOU  547  O   TYR A  93     8401  11303   7459   2203   -612   -305       O  
ATOM    548  CB  TYR A  93      30.392  14.066  13.978  1.00 71.42           C  
ANISOU  548  CB  TYR A  93     7948  11431   7758   1579   -553  -1058       C  
ATOM    549  CG  TYR A  93      29.626  13.017  14.744  1.00 72.92           C  
ANISOU  549  CG  TYR A  93     7988  11477   8241   1276   -414  -1297       C  
ATOM    550  CD1 TYR A  93      29.941  11.673  14.615  1.00 73.81           C  
ANISOU  550  CD1 TYR A  93     8136  11399   8509    961   -339  -1601       C  
ATOM    551  CD2 TYR A  93      28.570  13.367  15.574  1.00 73.46           C  
ANISOU  551  CD2 TYR A  93     7869  11590   8452   1303   -329  -1218       C  
ATOM    552  CE1 TYR A  93      29.237  10.707  15.300  1.00 76.93           C  
ANISOU  552  CE1 TYR A  93     8404  11613   9210    661   -178  -1783       C  
ATOM    553  CE2 TYR A  93      27.857  12.407  16.262  1.00 77.52           C  
ANISOU  553  CE2 TYR A  93     8235  11979   9241   1000   -155  -1407       C  
ATOM    554  CZ  TYR A  93      28.197  11.078  16.122  1.00 82.96           C  
ANISOU  554  CZ  TYR A  93     8981  12444  10096    669    -78  -1671       C  
ATOM    555  OH  TYR A  93      27.493  10.115  16.808  1.00 90.52           O  
ANISOU  555  OH  TYR A  93     9805  13222  11367    345    130  -1821       O  
ATOM    556  N   TRP A  94      33.424  15.072  13.067  1.00 68.71           N  
ANISOU  556  N   TRP A  94     8238  10765   7105   1868   -536   -652       N  
ATOM    557  CA  TRP A  94      34.049  15.805  11.975  1.00 67.69           C  
ANISOU  557  CA  TRP A  94     8166  10869   6684   2052   -608   -476       C  
ATOM    558  C   TRP A  94      34.244  14.861  10.800  1.00 75.67           C  
ANISOU  558  C   TRP A  94     9080  12195   7475   1913   -668   -802       C  
ATOM    559  O   TRP A  94      34.759  13.751  10.967  1.00 71.69           O  
ANISOU  559  O   TRP A  94     8640  11467   7133   1695   -577  -1089       O  
ATOM    560  CB  TRP A  94      35.392  16.426  12.375  1.00 57.98           C  
ANISOU  560  CB  TRP A  94     7227   9256   5546   2134   -485   -217       C  
ATOM    561  CG  TRP A  94      36.042  17.121  11.207  1.00 74.64           C  
ANISOU  561  CG  TRP A  94     9385  11603   7370   2285   -504    -17       C  
ATOM    562  CD1 TRP A  94      35.466  18.054  10.392  1.00 66.15           C  
ANISOU  562  CD1 TRP A  94     8219  10890   6026   2510   -608    231       C  
ATOM    563  CD2 TRP A  94      37.375  16.927  10.710  1.00 76.37           C  
ANISOU  563  CD2 TRP A  94     9747  11735   7537   2235   -394    -21       C  
ATOM    564  NE1 TRP A  94      36.355  18.456   9.428  1.00 63.27           N  
ANISOU  564  NE1 TRP A  94     7959  10660   5420   2588   -552    411       N  
ATOM    565  CE2 TRP A  94      37.534  17.780   9.599  1.00 73.00           C  
ANISOU  565  CE2 TRP A  94     9319  11630   6785   2410   -408    242       C  
ATOM    566  CE3 TRP A  94      38.449  16.119  11.098  1.00 69.38           C  
ANISOU  566  CE3 TRP A  94     8973  10535   6852   2078   -277   -204       C  
ATOM    567  CZ2 TRP A  94      38.722  17.853   8.874  1.00 71.60           C  
ANISOU  567  CZ2 TRP A  94     9245  11484   6476   2402   -274    316       C  
ATOM    568  CZ3 TRP A  94      39.629  16.191  10.373  1.00 67.41           C  
ANISOU  568  CZ3 TRP A  94     8794  10320   6497   2090   -169   -161       C  
ATOM    569  CH2 TRP A  94      39.755  17.051   9.274  1.00 65.19           C  
ANISOU  569  CH2 TRP A  94     8505  10376   5888   2234   -151     90       C  
ATOM    570  N   SER A  95      33.820  15.305   9.619  1.00 80.60           N  
ANISOU  570  N   SER A  95     9558  13344   7724   2059   -822   -762       N  
ATOM    571  CA  SER A  95      34.013  14.572   8.374  1.00 80.08           C  
ANISOU  571  CA  SER A  95     9407  13676   7342   1968   -894  -1079       C  
ATOM    572  C   SER A  95      34.562  15.545   7.344  1.00 81.34           C  
ANISOU  572  C   SER A  95     9664  14155   7088   2222   -919   -746       C  
ATOM    573  O   SER A  95      33.955  16.590   7.090  1.00 72.20           O  
ANISOU  573  O   SER A  95     8439  13247   5747   2473  -1037   -402       O  
ATOM    574  CB  SER A  95      32.704  13.941   7.888  1.00 88.02           C  
ANISOU  574  CB  SER A  95    10071  15138   8234   1856  -1097  -1451       C  
ATOM    575  OG  SER A  95      32.877  13.305   6.633  1.00 97.99           O  
ANISOU  575  OG  SER A  95    11254  16840   9136   1784  -1189  -1799       O  
ATOM    576  N   ARG A  96      35.712  15.201   6.758  1.00 87.18           N  
ANISOU  576  N   ARG A  96    10556  14875   7693   2168   -784   -829       N  
ATOM    577  CA  ARG A  96      36.408  16.133   5.876  1.00 82.02           C  
ANISOU  577  CA  ARG A  96    10029  14453   6681   2380   -724   -457       C  
ATOM    578  C   ARG A  96      35.697  16.286   4.536  1.00 84.29           C  
ANISOU  578  C   ARG A  96    10157  15482   6388   2524   -923   -481       C  
ATOM    579  O   ARG A  96      35.571  17.404   4.022  1.00 86.65           O  
ANISOU  579  O   ARG A  96    10499  16023   6401   2793   -967    -10       O  
ATOM    580  CB  ARG A  96      37.848  15.673   5.663  1.00 76.28           C  
ANISOU  580  CB  ARG A  96     9471  13517   5997   2271   -490   -565       C  
ATOM    581  CG  ARG A  96      38.669  16.629   4.824  1.00 82.81           C  
ANISOU  581  CG  ARG A  96    10428  14534   6502   2449   -355   -155       C  
ATOM    582  CD  ARG A  96      39.932  15.965   4.318  1.00 88.62           C  
ANISOU  582  CD  ARG A  96    11236  15253   7181   2334   -131   -385       C  
ATOM    583  NE  ARG A  96      39.644  14.646   3.768  1.00 89.92           N  
ANISOU  583  NE  ARG A  96    11276  15702   7188   2186   -202   -989       N  
ATOM    584  CZ  ARG A  96      39.153  14.436   2.552  1.00 80.47           C  
ANISOU  584  CZ  ARG A  96     9977  15158   5438   2238   -315  -1183       C  
ATOM    585  NH1 ARG A  96      38.894  15.460   1.753  1.00 89.95           N  
ANISOU  585  NH1 ARG A  96    11199  16817   6160   2465   -372   -755       N  
ATOM    586  NH2 ARG A  96      38.918  13.199   2.140  1.00 86.50           N  
ANISOU  586  NH2 ARG A  96    10624  16113   6128   2070   -375  -1807       N  
ATOM    587  N   HIS A  97      35.235  15.180   3.945  1.00 87.86           N  
ANISOU  587  N   HIS A  97    10427  16300   6655   2357  -1049  -1026       N  
ATOM    588  CA  HIS A  97      34.636  15.261   2.615  1.00101.19           C  
ANISOU  588  CA  HIS A  97    11958  18771   7720   2492  -1268  -1109       C  
ATOM    589  C   HIS A  97      33.184  15.721   2.657  1.00103.70           C  
ANISOU  589  C   HIS A  97    12006  19435   7960   2640  -1574  -1010       C  
ATOM    590  O   HIS A  97      32.708  16.329   1.692  1.00106.80           O  
ANISOU  590  O   HIS A  97    12307  20444   7827   2896  -1775   -795       O  
ATOM    591  CB  HIS A  97      34.748  13.917   1.888  1.00112.93           C  
ANISOU  591  CB  HIS A  97    13343  20552   9014   2252  -1294  -1802       C  
ATOM    592  CG  HIS A  97      33.889  12.834   2.463  1.00117.40           C  
ANISOU  592  CG  HIS A  97    13679  20968   9959   1966  -1414  -2353       C  
ATOM    593  ND1 HIS A  97      33.667  12.696   3.815  1.00118.86           N  
ANISOU  593  ND1 HIS A  97    13873  20530  10760   1834  -1327  -2288       N  
ATOM    594  CD2 HIS A  97      33.201  11.832   1.865  1.00121.73           C  
ANISOU  594  CD2 HIS A  97    13980  21907  10365   1767  -1596  -2984       C  
ATOM    595  CE1 HIS A  97      32.877  11.659   4.027  1.00121.41           C  
ANISOU  595  CE1 HIS A  97    13968  20845  11318   1562  -1422  -2808       C  
ATOM    596  NE2 HIS A  97      32.580  11.117   2.860  1.00121.25           N  
ANISOU  596  NE2 HIS A  97    13779  21413  10878   1503  -1592  -3259       N  
ATOM    597  N   THR A  98      32.464  15.443   3.747  1.00 99.14           N  
ANISOU  597  N   THR A  98    11285  18504   7880   2503  -1609  -1148       N  
ATOM    598  CA  THR A  98      31.142  16.034   3.919  1.00 94.89           C  
ANISOU  598  CA  THR A  98    10473  18239   7343   2682  -1854   -990       C  
ATOM    599  C   THR A  98      31.234  17.504   4.314  1.00 92.82           C  
ANISOU  599  C   THR A  98    10370  17748   7148   3029  -1793   -298       C  
ATOM    600  O   THR A  98      30.244  18.231   4.188  1.00100.44           O  
ANISOU  600  O   THR A  98    11132  19020   8010   3296  -2002    -58       O  
ATOM    601  CB  THR A  98      30.341  15.251   4.964  1.00110.27           C  
ANISOU  601  CB  THR A  98    12200  19889   9808   2406  -1856  -1362       C  
ATOM    602  OG1 THR A  98      30.613  13.852   4.825  1.00114.47           O  
ANISOU  602  OG1 THR A  98    12700  20350  10442   2036  -1795  -1964       O  
ATOM    603  CG2 THR A  98      28.843  15.471   4.780  1.00121.29           C  
ANISOU  603  CG2 THR A  98    13170  21794  11119   2520  -2158  -1432       C  
ATOM    604  N   GLY A  99      32.407  17.956   4.758  1.00 84.33           N  
ANISOU  604  N   GLY A  99     9636  16144   6263   3037  -1517      7       N  
ATOM    605  CA  GLY A  99      32.590  19.327   5.188  1.00 81.94           C  
ANISOU  605  CA  GLY A  99     9507  15526   6102   3318  -1425    611       C  
ATOM    606  C   GLY A  99      31.811  19.705   6.423  1.00 83.80           C  
ANISOU  606  C   GLY A  99     9644  15394   6802   3364  -1434    674       C  
ATOM    607  O   GLY A  99      31.539  20.888   6.635  1.00 82.69           O  
ANISOU  607  O   GLY A  99     9551  15130   6739   3663  -1440   1122       O  
ATOM    608  N   ARG A 100      31.455  18.731   7.258  1.00 76.53           N  
ANISOU  608  N   ARG A 100     8598  14275   6204   3080  -1407    242       N  
ATOM    609  CA  ARG A 100      30.544  18.942   8.374  1.00 83.03           C  
ANISOU  609  CA  ARG A 100     9271  14869   7405   3104  -1408    237       C  
ATOM    610  C   ARG A 100      31.252  18.698   9.698  1.00 87.21           C  
ANISOU  610  C   ARG A 100    10040  14726   8371   2904  -1153    189       C  
ATOM    611  O   ARG A 100      31.859  17.640   9.899  1.00 86.27           O  
ANISOU  611  O   ARG A 100    10007  14420   8351   2609  -1051   -120       O  
ATOM    612  CB  ARG A 100      29.327  18.021   8.257  1.00 83.84           C  
ANISOU  612  CB  ARG A 100     8971  15377   7507   2938  -1588   -206       C  
ATOM    613  CG  ARG A 100      28.471  18.277   7.036  1.00 89.16           C  
ANISOU  613  CG  ARG A 100     9342  16792   7744   3158  -1904   -194       C  
ATOM    614  CD  ARG A 100      27.813  19.638   7.107  1.00 86.08           C  
ANISOU  614  CD  ARG A 100     8870  16490   7345   3599  -2003    292       C  
ATOM    615  NE  ARG A 100      26.880  19.838   6.004  1.00107.23           N  
ANISOU  615  NE  ARG A 100    11211  19921   9609   3843  -2349    310       N  
ATOM    616  CZ  ARG A 100      25.626  19.400   6.003  1.00116.23           C  
ANISOU  616  CZ  ARG A 100    11880  21479  10802   3800  -2569    -13       C  
ATOM    617  NH1 ARG A 100      25.158  18.734   7.049  1.00113.31           N  
ANISOU  617  NH1 ARG A 100    11346  20815  10894   3504  -2431   -352       N  
ATOM    618  NH2 ARG A 100      24.842  19.624   4.956  1.00116.82           N  
ANISOU  618  NH2 ARG A 100    11637  22288  10461   4052  -2925     12       N  
ATOM    619  N   LEU A 101      31.174  19.678  10.594  1.00 79.58           N  
ANISOU  619  N   LEU A 101     9180  13403   7654   3086  -1060    486       N  
ATOM    620  CA  LEU A 101      31.514  19.508  12.006  1.00 74.21           C  
ANISOU  620  CA  LEU A 101     8664  12177   7355   2934   -865    415       C  
ATOM    621  C   LEU A 101      30.231  19.748  12.789  1.00 78.93           C  
ANISOU  621  C   LEU A 101     9027  12818   8143   3025   -880    376       C  
ATOM    622  O   LEU A 101      29.797  20.895  12.936  1.00 84.80           O  
ANISOU  622  O   LEU A 101     9747  13537   8935   3333   -900    654       O  
ATOM    623  CB  LEU A 101      32.612  20.468  12.449  1.00 67.32           C  
ANISOU  623  CB  LEU A 101     8123  10845   6613   3049   -722    728       C  
ATOM    624  CG  LEU A 101      32.907  20.399  13.949  1.00 59.93           C  
ANISOU  624  CG  LEU A 101     7348   9411   6012   2934   -563    649       C  
ATOM    625  CD1 LEU A 101      33.812  19.224  14.260  1.00 57.49           C  
ANISOU  625  CD1 LEU A 101     7169   8904   5768   2632   -481    402       C  
ATOM    626  CD2 LEU A 101      33.514  21.693  14.447  1.00 68.56           C  
ANISOU  626  CD2 LEU A 101     8668  10118   7264   3123   -475    944       C  
ATOM    627  N   HIS A 102      29.615  18.678  13.279  1.00 79.18           N  
ANISOU  627  N   HIS A 102     8875  12900   8308   2762   -846     36       N  
ATOM    628  CA  HIS A 102      28.370  18.793  14.017  1.00 74.69           C  
ANISOU  628  CA  HIS A 102     8037  12414   7927   2808   -818    -32       C  
ATOM    629  C   HIS A 102      28.488  18.069  15.349  1.00 76.32           C  
ANISOU  629  C   HIS A 102     8366  12227   8407   2543   -582   -193       C  
ATOM    630  O   HIS A 102      29.211  17.077  15.479  1.00 83.57           O  
ANISOU  630  O   HIS A 102     9449  12938   9365   2264   -505   -357       O  
ATOM    631  CB  HIS A 102      27.180  18.240  13.211  1.00 74.19           C  
ANISOU  631  CB  HIS A 102     7514  12925   7750   2753  -1015   -279       C  
ATOM    632  CG  HIS A 102      27.271  16.778  12.896  1.00 72.89           C  
ANISOU  632  CG  HIS A 102     7263  12844   7587   2347  -1019   -685       C  
ATOM    633  ND1 HIS A 102      26.457  15.840  13.493  1.00 77.78           N  
ANISOU  633  ND1 HIS A 102     7634  13462   8458   2050   -921   -992       N  
ATOM    634  CD2 HIS A 102      28.061  16.094  12.034  1.00 72.94           C  
ANISOU  634  CD2 HIS A 102     7394  12919   7402   2189  -1086   -850       C  
ATOM    635  CE1 HIS A 102      26.747  14.640  13.022  1.00 76.78           C  
ANISOU  635  CE1 HIS A 102     7495  13351   8328   1720   -936  -1330       C  
ATOM    636  NE2 HIS A 102      27.718  14.766  12.136  1.00 75.67           N  
ANISOU  636  NE2 HIS A 102     7577  13263   7911   1810  -1040  -1270       N  
ATOM    637  N   LEU A 103      27.763  18.584  16.340  1.00 77.36           N  
ANISOU  637  N   LEU A 103     8416  12262   8715   2659   -459   -132       N  
ATOM    638  CA  LEU A 103      27.704  18.000  17.673  1.00 74.88           C  
ANISOU  638  CA  LEU A 103     8203  11643   8604   2449   -215   -240       C  
ATOM    639  C   LEU A 103      26.307  17.428  17.889  1.00 84.31           C  
ANISOU  639  C   LEU A 103     8974  13132   9927   2312   -154   -448       C  
ATOM    640  O   LEU A 103      25.323  18.174  17.950  1.00100.70           O  
ANISOU  640  O   LEU A 103    10769  15447  12046   2548   -175   -398       O  
ATOM    641  CB  LEU A 103      28.053  19.032  18.748  1.00 69.10           C  
ANISOU  641  CB  LEU A 103     7736  10570   7949   2670    -73    -42       C  
ATOM    642  CG  LEU A 103      27.733  18.524  20.156  1.00 70.54           C  
ANISOU  642  CG  LEU A 103     7976  10560   8267   2505    184   -139       C  
ATOM    643  CD1 LEU A 103      28.742  17.465  20.578  1.00 64.76           C  
ANISOU  643  CD1 LEU A 103     7541   9527   7537   2214    263   -193       C  
ATOM    644  CD2 LEU A 103      27.638  19.658  21.174  1.00 62.58           C  
ANISOU  644  CD2 LEU A 103     7107   9363   7308   2772    315    -27       C  
ATOM    645  N   ARG A 104      26.218  16.105  17.980  1.00 82.84           N  
ANISOU  645  N   ARG A 104     8722  12914   9840   1932    -69   -686       N  
ATOM    646  CA  ARG A 104      24.987  15.439  18.384  1.00 88.48           C  
ANISOU  646  CA  ARG A 104     9056  13812  10749   1713     66   -890       C  
ATOM    647  C   ARG A 104      24.958  15.324  19.908  1.00100.60           C  
ANISOU  647  C   ARG A 104    10786  15008  12431   1633    402   -795       C  
ATOM    648  O   ARG A 104      25.940  14.897  20.527  1.00 94.95           O  
ANISOU  648  O   ARG A 104    10474  13896  11706   1519    522   -711       O  
ATOM    649  CB  ARG A 104      24.887  14.060  17.736  1.00 90.29           C  
ANISOU  649  CB  ARG A 104     9122  14124  11060   1313     20  -1205       C  
ATOM    650  CG  ARG A 104      23.477  13.464  17.697  1.00113.10           C  
ANISOU  650  CG  ARG A 104    11476  17340  14157   1077     69  -1476       C  
ATOM    651  CD  ARG A 104      23.475  12.179  16.902  1.00118.79           C  
ANISOU  651  CD  ARG A 104    12048  18121  14964    685    -17  -1840       C  
ATOM    652  NE  ARG A 104      22.275  11.408  17.166  1.00124.08           N  
ANISOU  652  NE  ARG A 104    12266  18939  15940    345    126  -2108       N  
ATOM    653  CZ  ARG A 104      22.123  10.631  18.229  1.00122.42           C  
ANISOU  653  CZ  ARG A 104    12140  18354  16022     36    489  -2092       C  
ATOM    654  NH1 ARG A 104      23.096  10.519  19.125  1.00121.48           N  
ANISOU  654  NH1 ARG A 104    12546  17725  15887     59    704  -1823       N  
ATOM    655  NH2 ARG A 104      20.996   9.963  18.392  1.00120.79           N  
ANISOU  655  NH2 ARG A 104    11478  18297  16119   -298    637  -2335       N  
ATOM    656  N   TYR A 105      23.821  15.672  20.506  1.00107.24           N  
ANISOU  656  N   TYR A 105    11322  16038  13388   1703    557   -813       N  
ATOM    657  CA  TYR A 105      23.741  15.874  21.948  1.00102.06           C  
ANISOU  657  CA  TYR A 105    10855  15143  12782   1730    880   -696       C  
ATOM    658  C   TYR A 105      22.385  15.386  22.432  1.00100.60           C  
ANISOU  658  C   TYR A 105    10229  15193  12801   1537   1127   -840       C  
ATOM    659  O   TYR A 105      21.359  15.998  22.120  1.00100.32           O  
ANISOU  659  O   TYR A 105     9755  15530  12832   1727   1067   -911       O  
ATOM    660  CB  TYR A 105      23.945  17.349  22.298  1.00 95.61           C  
ANISOU  660  CB  TYR A 105    10199  14272  11855   2174    846   -518       C  
ATOM    661  CG  TYR A 105      24.023  17.642  23.782  1.00 99.57           C  
ANISOU  661  CG  TYR A 105    10957  14538  12336   2231   1155   -441       C  
ATOM    662  CD1 TYR A 105      22.878  17.906  24.520  1.00107.04           C  
ANISOU  662  CD1 TYR A 105    11616  15679  13376   2302   1411   -502       C  
ATOM    663  CD2 TYR A 105      25.244  17.669  24.440  1.00 96.93           C  
ANISOU  663  CD2 TYR A 105    11134  13828  11868   2228   1185   -325       C  
ATOM    664  CE1 TYR A 105      22.946  18.182  25.869  1.00101.39           C  
ANISOU  664  CE1 TYR A 105    11147  14797  12578   2367   1707   -455       C  
ATOM    665  CE2 TYR A 105      25.323  17.945  25.793  1.00 92.42           C  
ANISOU  665  CE2 TYR A 105    10802  13102  11211   2293   1437   -281       C  
ATOM    666  CZ  TYR A 105      24.170  18.201  26.503  1.00101.41           C  
ANISOU  666  CZ  TYR A 105    11682  14448  12403   2362   1706   -348       C  
ATOM    667  OH  TYR A 105      24.239  18.476  27.851  1.00107.22           O  
ANISOU  667  OH  TYR A 105    12669  15077  12994   2436   1974   -328       O  
ATOM    668  N   GLY A 106      22.381  14.291  23.192  1.00 94.03           N  
ANISOU  668  N   GLY A 106     9500  14143  12084   1170   1415   -863       N  
ATOM    669  CA  GLY A 106      21.145  13.711  23.678  1.00 93.63           C  
ANISOU  669  CA  GLY A 106     9034  14277  12262    914   1711   -984       C  
ATOM    670  C   GLY A 106      20.274  13.195  22.552  1.00102.02           C  
ANISOU  670  C   GLY A 106     9533  15708  13522    706   1522  -1273       C  
ATOM    671  O   GLY A 106      20.604  12.194  21.911  1.00112.33           O  
ANISOU  671  O   GLY A 106    10856  16905  14918    386   1417  -1430       O  
ATOM    672  N   LYS A 107      19.162  13.879  22.298  1.00105.79           N  
ANISOU  672  N   LYS A 107     9492  16633  14073    902   1463  -1373       N  
ATOM    673  CA  LYS A 107      18.258  13.523  21.215  1.00107.05           C  
ANISOU  673  CA  LYS A 107     9045  17241  14387    756   1224  -1671       C  
ATOM    674  C   LYS A 107      18.349  14.478  20.033  1.00106.44           C  
ANISOU  674  C   LYS A 107     8844  17509  14090   1173    754  -1663       C  
ATOM    675  O   LYS A 107      17.646  14.279  19.039  1.00110.60           O  
ANISOU  675  O   LYS A 107     8873  18486  14665   1115    480  -1907       O  
ATOM    676  CB  LYS A 107      16.814  13.473  21.726  1.00 97.62           C  
ANISOU  676  CB  LYS A 107     7242  16378  13472    649   1488  -1809       C  
ATOM    677  N   HIS A 108      19.194  15.501  20.112  1.00102.41           N  
ANISOU  677  N   HIS A 108     8769  16805  13338   1582    654  -1386       N  
ATOM    678  CA  HIS A 108      19.298  16.510  19.070  1.00103.14           C  
ANISOU  678  CA  HIS A 108     8792  17173  13225   2011    262  -1286       C  
ATOM    679  C   HIS A 108      20.706  16.520  18.486  1.00 97.45           C  
ANISOU  679  C   HIS A 108     8603  16170  12253   2042     73  -1151       C  
ATOM    680  O   HIS A 108      21.618  15.853  18.983  1.00101.40           O  
ANISOU  680  O   HIS A 108     9524  16249  12754   1787    238  -1130       O  
ATOM    681  CB  HIS A 108      18.932  17.899  19.609  1.00111.85           C  
ANISOU  681  CB  HIS A 108     9871  18297  14330   2515    331  -1066       C  
ATOM    682  CG  HIS A 108      18.421  18.837  18.560  1.00121.91           C  
ANISOU  682  CG  HIS A 108    10815  19994  15512   2952    -35   -989       C  
ATOM    683  ND1 HIS A 108      18.468  20.207  18.699  1.00123.78           N  
ANISOU  683  ND1 HIS A 108    11173  20144  15715   3478    -70   -725       N  
ATOM    684  CD2 HIS A 108      17.846  18.601  17.356  1.00120.61           C  
ANISOU  684  CD2 HIS A 108    10206  20346  15276   2955   -390  -1135       C  
ATOM    685  CE1 HIS A 108      17.949  20.775  17.625  1.00122.03           C  
ANISOU  685  CE1 HIS A 108    10610  20346  15409   3809   -423   -655       C  
ATOM    686  NE2 HIS A 108      17.564  19.822  16.795  1.00125.44           N  
ANISOU  686  NE2 HIS A 108    10689  21188  15784   3506   -637   -904       N  
ATOM    687  N   ASP A 109      20.870  17.291  17.413  1.00 88.28           N  
ANISOU  687  N   ASP A 109     7402  15264  10875   2375   -270  -1039       N  
ATOM    688  CA  ASP A 109      22.134  17.394  16.695  1.00 85.83           C  
ANISOU  688  CA  ASP A 109     7526  14775  10311   2430   -449   -904       C  
ATOM    689  C   ASP A 109      22.373  18.848  16.312  1.00 84.96           C  
ANISOU  689  C   ASP A 109     7545  14696  10041   2949   -611   -565       C  
ATOM    690  O   ASP A 109      21.495  19.487  15.725  1.00 89.61           O  
ANISOU  690  O   ASP A 109     7753  15701  10591   3252   -812   -513       O  
ATOM    691  CB  ASP A 109      22.129  16.504  15.446  1.00 85.97           C  
ANISOU  691  CB  ASP A 109     7343  15138  10185   2190   -714  -1171       C  
ATOM    692  CG  ASP A 109      23.345  16.718  14.573  1.00 92.00           C  
ANISOU  692  CG  ASP A 109     8494  15818  10644   2301   -893  -1026       C  
ATOM    693  OD1 ASP A 109      24.398  16.112  14.860  1.00 97.00           O  
ANISOU  693  OD1 ASP A 109     9520  16041  11294   2074   -751  -1049       O  
ATOM    694  OD2 ASP A 109      23.247  17.491  13.596  1.00103.05           O  
ANISOU  694  OD2 ASP A 109     9794  17573  11786   2628  -1165   -871       O  
ATOM    695  N   TYR A 110      23.558  19.361  16.638  1.00 82.77           N  
ANISOU  695  N   TYR A 110     7786  13968   9694   3050   -526   -333       N  
ATOM    696  CA  TYR A 110      23.914  20.759  16.424  1.00 77.77           C  
ANISOU  696  CA  TYR A 110     7345  13219   8985   3498   -610      6       C  
ATOM    697  C   TYR A 110      25.002  20.856  15.362  1.00 80.74           C  
ANISOU  697  C   TYR A 110     8002  13574   9101   3523   -794    166       C  
ATOM    698  O   TYR A 110      26.050  20.217  15.486  1.00 83.07           O  
ANISOU  698  O   TYR A 110     8617  13589   9356   3251   -711    101       O  
ATOM    699  CB  TYR A 110      24.399  21.404  17.726  1.00 76.17           C  
ANISOU  699  CB  TYR A 110     7494  12498   8950   3590   -338    121       C  
ATOM    700  CG  TYR A 110      23.391  21.364  18.853  1.00 87.92           C  
ANISOU  700  CG  TYR A 110     8747  14007  10652   3585    -97    -27       C  
ATOM    701  CD1 TYR A 110      23.210  20.213  19.610  1.00 86.58           C  
ANISOU  701  CD1 TYR A 110     8538  13794  10562   3185    116   -253       C  
ATOM    702  CD2 TYR A 110      22.627  22.481  19.168  1.00 89.38           C  
ANISOU  702  CD2 TYR A 110     8753  14238  10968   3990    -53     73       C  
ATOM    703  CE1 TYR A 110      22.291  20.171  20.639  1.00 88.51           C  
ANISOU  703  CE1 TYR A 110     8568  14085  10976   3167    384   -364       C  
ATOM    704  CE2 TYR A 110      21.705  22.449  20.200  1.00 91.15           C  
ANISOU  704  CE2 TYR A 110     8746  14514  11375   3994    205    -83       C  
ATOM    705  CZ  TYR A 110      21.542  21.291  20.930  1.00 92.12           C  
ANISOU  705  CZ  TYR A 110     8829  14634  11536   3571    432   -295       C  
ATOM    706  OH  TYR A 110      20.628  21.251  21.956  1.00104.14           O  
ANISOU  706  OH  TYR A 110    10120  16233  13215   3561    736   -426       O  
ATOM    707  N   LEU A 111      24.762  21.674  14.337  1.00 77.69           N  
ANISOU  707  N   LEU A 111     7495  13488   8535   3871  -1029    399       N  
ATOM    708  CA  LEU A 111      25.706  21.856  13.238  1.00 78.95           C  
ANISOU  708  CA  LEU A 111     7896  13702   8401   3928  -1180    596       C  
ATOM    709  C   LEU A 111      26.642  23.007  13.582  1.00 75.31           C  
ANISOU  709  C   LEU A 111     7855  12734   8027   4157  -1047    959       C  
ATOM    710  O   LEU A 111      26.229  24.171  13.595  1.00 89.90           O  
ANISOU  710  O   LEU A 111     9669  14524   9963   4549  -1070   1241       O  
ATOM    711  CB  LEU A 111      24.966  22.121  11.929  1.00 87.48           C  
ANISOU  711  CB  LEU A 111     8642  15406   9189   4189  -1501    697       C  
ATOM    712  CG  LEU A 111      24.137  20.971  11.351  1.00100.08           C  
ANISOU  712  CG  LEU A 111     9799  17572  10655   3935  -1694    284       C  
ATOM    713  CD1 LEU A 111      23.311  21.448  10.167  1.00104.31           C  
ANISOU  713  CD1 LEU A 111     9975  18770  10886   4282  -2052    415       C  
ATOM    714  CD2 LEU A 111      25.035  19.819  10.935  1.00 98.86           C  
ANISOU  714  CD2 LEU A 111     9842  17381  10341   3519  -1670      9       C  
ATOM    715  N   LEU A 112      27.907  22.686  13.851  1.00 71.51           N  
ANISOU  715  N   LEU A 112     7748  11870   7553   3914   -910    940       N  
ATOM    716  CA  LEU A 112      28.852  23.715  14.270  1.00 77.08           C  
ANISOU  716  CA  LEU A 112     8825  12066   8395   4060   -773   1217       C  
ATOM    717  C   LEU A 112      29.487  24.411  13.073  1.00 77.53           C  
ANISOU  717  C   LEU A 112     9024  12198   8235   4251   -872   1577       C  
ATOM    718  O   LEU A 112      29.676  25.633  13.087  1.00 77.41           O  
ANISOU  718  O   LEU A 112     9163  11905   8344   4536   -822   1914       O  
ATOM    719  CB  LEU A 112      29.916  23.099  15.177  1.00 70.84           C  
ANISOU  719  CB  LEU A 112     8331  10852   7732   3730   -594   1034       C  
ATOM    720  CG  LEU A 112      29.379  22.382  16.417  1.00 80.08           C  
ANISOU  720  CG  LEU A 112     9422  11929   9077   3535   -459    739       C  
ATOM    721  CD1 LEU A 112      30.515  21.900  17.317  1.00 79.96           C  
ANISOU  721  CD1 LEU A 112     9735  11496   9152   3280   -312    633       C  
ATOM    722  CD2 LEU A 112      28.415  23.273  17.196  1.00 70.09           C  
ANISOU  722  CD2 LEU A 112     8029  10601   8000   3808   -377    785       C  
ATOM    723  N   SER A 113      29.816  23.656  12.029  1.00 79.53           N  
ANISOU  723  N   SER A 113     9234  12815   8167   4097   -990   1509       N  
ATOM    724  CA  SER A 113      30.402  24.228  10.828  1.00 84.62           C  
ANISOU  724  CA  SER A 113    10009  13614   8530   4266  -1057   1860       C  
ATOM    725  C   SER A 113      29.855  23.521   9.599  1.00 89.75           C  
ANISOU  725  C   SER A 113    10395  14958   8748   4260  -1294   1740       C  
ATOM    726  O   SER A 113      29.636  22.306   9.614  1.00 87.49           O  
ANISOU  726  O   SER A 113     9943  14897   8402   3962  -1346   1306       O  
ATOM    727  CB  SER A 113      31.929  24.126  10.847  1.00 78.15           C  
ANISOU  727  CB  SER A 113     9533  12422   7737   4041   -875   1904       C  
ATOM    728  OG  SER A 113      32.471  24.637   9.646  1.00 73.87           O  
ANISOU  728  OG  SER A 113     9100  12068   6898   4184   -895   2255       O  
ATOM    729  N   SER A 114      29.640  24.297   8.537  1.00 93.26           N  
ANISOU  729  N   SER A 114    10811  15733   8891   4594  -1437   2127       N  
ATOM    730  CA  SER A 114      29.213  23.771   7.252  1.00103.58           C  
ANISOU  730  CA  SER A 114    11899  17764   9692   4635  -1690   2052       C  
ATOM    731  C   SER A 114      30.338  23.719   6.229  1.00 99.68           C  
ANISOU  731  C   SER A 114    11666  17395   8815   4574  -1622   2227       C  
ATOM    732  O   SER A 114      30.147  23.133   5.160  1.00 89.93           O  
ANISOU  732  O   SER A 114    10288  16779   7103   4555  -1807   2081       O  
ATOM    733  CB  SER A 114      28.060  24.612   6.694  1.00 90.91           C  
ANISOU  733  CB  SER A 114    10061  16488   7991   5001  -1887   2318       C  
ATOM    734  OG  SER A 114      27.684  24.161   5.405  1.00 95.34           O  
ANISOU  734  OG  SER A 114    10446  17704   8075   4979  -2106   2208       O  
ATOM    735  N   GLN A 115      31.494  24.316   6.526  1.00 90.08           N  
ANISOU  735  N   GLN A 115    10805  15633   7789   4537  -1354   2509       N  
ATOM    736  CA  GLN A 115      32.633  24.344   5.613  1.00 84.70           C  
ANISOU  736  CA  GLN A 115    10360  15031   6790   4471  -1222   2707       C  
ATOM    737  C   GLN A 115      33.873  23.808   6.330  1.00 81.17           C  
ANISOU  737  C   GLN A 115    10124  14066   6651   4102   -959   2458       C  
ATOM    738  O   GLN A 115      34.872  24.504   6.504  1.00 82.56           O  
ANISOU  738  O   GLN A 115    10552  13801   7015   4090   -731   2755       O  
ATOM    739  CB  GLN A 115      32.875  25.755   5.080  1.00 89.81           C  
ANISOU  739  CB  GLN A 115    11201  15460   7462   4709  -1093   3305       C  
ATOM    740  CG  GLN A 115      31.746  26.310   4.220  1.00100.87           C  
ANISOU  740  CG  GLN A 115    12418  17255   8655   4952  -1289   3485       C  
ATOM    741  CD  GLN A 115      31.775  25.791   2.792  1.00112.45           C  
ANISOU  741  CD  GLN A 115    13816  19393   9516   4925  -1403   3432       C  
ATOM    742  OE1 GLN A 115      32.558  24.904   2.456  1.00119.79           O  
ANISOU  742  OE1 GLN A 115    14807  20532  10176   4708  -1341   3185       O  
ATOM    743  NE2 GLN A 115      30.921  26.351   1.942  1.00117.27           N  
ANISOU  743  NE2 GLN A 115    14304  20347   9906   5158  -1569   3650       N  
ATOM    744  N   ALA A 116      33.801  22.547   6.753  1.00 76.92           N  
ANISOU  744  N   ALA A 116     9462  13575   6190   3798   -994   1908       N  
ATOM    745  CA  ALA A 116      34.907  21.888   7.434  1.00 88.46           C  
ANISOU  745  CA  ALA A 116    11087  14595   7928   3478   -787   1647       C  
ATOM    746  C   ALA A 116      35.776  21.085   6.472  1.00 84.30           C  
ANISOU  746  C   ALA A 116    10606  14352   7072   3307   -718   1458       C  
ATOM    747  O   ALA A 116      36.392  20.092   6.870  1.00 86.75           O  
ANISOU  747  O   ALA A 116    10942  14470   7549   3036   -625   1079       O  
ATOM    748  CB  ALA A 116      34.382  20.993   8.556  1.00 75.20           C  
ANISOU  748  CB  ALA A 116     9284  12714   6574   3265   -823   1212       C  
ATOM    749  N   SER A 117      35.839  21.503   5.207  1.00 96.10           N  
ANISOU  749  N   SER A 117    12115  16309   8090   3486   -749   1727       N  
ATOM    750  CA  SER A 117      36.541  20.748   4.170  1.00103.88           C  
ANISOU  750  CA  SER A 117    13121  17677   8671   3358   -679   1515       C  
ATOM    751  C   SER A 117      37.987  21.231   4.095  1.00100.64           C  
ANISOU  751  C   SER A 117    12949  16924   8366   3300   -362   1794       C  
ATOM    752  O   SER A 117      38.376  22.016   3.228  1.00113.79           O  
ANISOU  752  O   SER A 117    14727  18786   9723   3462   -248   2234       O  
ATOM    753  CB  SER A 117      35.823  20.892   2.834  1.00 99.59           C  
ANISOU  753  CB  SER A 117    12458  17899   7482   3582   -883   1632       C  
ATOM    754  OG  SER A 117      35.556  22.254   2.547  1.00110.92           O  
ANISOU  754  OG  SER A 117    13982  19355   8806   3921   -897   2284       O  
ATOM    755  N   ARG A 118      38.797  20.735   5.029  1.00 91.76           N  
ANISOU  755  N   ARG A 118    11886  15288   7690   3061   -212   1544       N  
ATOM    756  CA  ARG A 118      40.204  21.097   5.123  1.00 94.04           C  
ANISOU  756  CA  ARG A 118    12335  15219   8177   2965     75   1725       C  
ATOM    757  C   ARG A 118      41.008  19.875   5.542  1.00 88.21           C  
ANISOU  757  C   ARG A 118    11564  14296   7655   2705    163   1227       C  
ATOM    758  O   ARG A 118      40.575  19.106   6.404  1.00 93.68           O  
ANISOU  758  O   ARG A 118    12191  14791   8611   2591     39    878       O  
ATOM    759  CB  ARG A 118      40.412  22.247   6.119  1.00 92.95           C  
ANISOU  759  CB  ARG A 118    12319  14486   8511   3020    153   2087       C  
ATOM    760  CG  ARG A 118      41.862  22.547   6.447  1.00 92.25           C  
ANISOU  760  CG  ARG A 118    12338  13967   8744   2861    420   2181       C  
ATOM    761  CD  ARG A 118      41.964  23.659   7.474  1.00 98.53           C  
ANISOU  761  CD  ARG A 118    13238  14181  10016   2896    459   2447       C  
ATOM    762  NE  ARG A 118      43.337  23.869   7.923  1.00103.42           N  
ANISOU  762  NE  ARG A 118    13908  14387  11001   2704    671   2448       N  
ATOM    763  CZ  ARG A 118      43.702  24.827   8.768  1.00105.15           C  
ANISOU  763  CZ  ARG A 118    14210  14081  11660   2676    735   2618       C  
ATOM    764  NH1 ARG A 118      42.794  25.665   9.252  1.00102.54           N  
ANISOU  764  NH1 ARG A 118    13947  13551  11461   2849    628   2806       N  
ATOM    765  NH2 ARG A 118      44.973  24.950   9.128  1.00101.30           N  
ANISOU  765  NH2 ARG A 118    13716  13276  11499   2479    902   2568       N  
ATOM    766  N   LEU A 119      42.177  19.696   4.928  1.00 94.03           N  
ANISOU  766  N   LEU A 119    12341  15095   8291   2625    396   1217       N  
ATOM    767  CA  LEU A 119      43.010  18.518   5.171  1.00 88.67           C  
ANISOU  767  CA  LEU A 119    11614  14276   7802   2429    493    752       C  
ATOM    768  C   LEU A 119      43.707  18.653   6.520  1.00 79.31           C  
ANISOU  768  C   LEU A 119    10475  12451   7209   2325    544    763       C  
ATOM    769  O   LEU A 119      44.695  19.379   6.656  1.00 72.03           O  
ANISOU  769  O   LEU A 119     9601  11279   6487   2302    729   1024       O  
ATOM    770  CB  LEU A 119      44.022  18.337   4.046  1.00 91.43           C  
ANISOU  770  CB  LEU A 119    11957  14939   7842   2410    746    734       C  
ATOM    771  CG  LEU A 119      45.018  17.187   4.215  1.00 97.31           C  
ANISOU  771  CG  LEU A 119    12634  15527   8814   2253    885    271       C  
ATOM    772  CD1 LEU A 119      44.305  15.900   4.600  1.00 99.58           C  
ANISOU  772  CD1 LEU A 119    12851  15791   9194   2169    681   -261       C  
ATOM    773  CD2 LEU A 119      45.823  16.990   2.939  1.00104.76           C  
ANISOU  773  CD2 LEU A 119    13546  16904   9355   2266   1147    211       C  
ATOM    774  N   LEU A 120      43.197  17.936   7.519  1.00 73.47           N  
ANISOU  774  N   LEU A 120     9711  11464   6742   2250    381    473       N  
ATOM    775  CA  LEU A 120      43.819  17.845   8.830  1.00 68.88           C  
ANISOU  775  CA  LEU A 120     9174  10348   6649   2162    391    421       C  
ATOM    776  C   LEU A 120      43.729  16.405   9.314  1.00 62.68           C  
ANISOU  776  C   LEU A 120     8343   9458   6015   2049    320    -27       C  
ATOM    777  O   LEU A 120      42.826  15.660   8.924  1.00 59.58           O  
ANISOU  777  O   LEU A 120     7887   9318   5432   2022    219   -277       O  
ATOM    778  CB  LEU A 120      43.158  18.791   9.845  1.00 72.08           C  
ANISOU  778  CB  LEU A 120     9656  10465   7267   2232    277    672       C  
ATOM    779  CG  LEU A 120      43.318  20.295   9.613  1.00 70.20           C  
ANISOU  779  CG  LEU A 120     9491  10151   7030   2343    363   1130       C  
ATOM    780  CD1 LEU A 120      42.505  21.080  10.627  1.00 62.42           C  
ANISOU  780  CD1 LEU A 120     8571   8888   6259   2432    241   1275       C  
ATOM    781  CD2 LEU A 120      44.783  20.695   9.680  1.00 69.84           C  
ANISOU  781  CD2 LEU A 120     9464   9847   7226   2247    561   1234       C  
ATOM    782  N   CYS A 121      44.676  16.017  10.165  1.00 61.19           N  
ANISOU  782  N   CYS A 121     8177   8885   6186   1985    367   -122       N  
ATOM    783  CA  CYS A 121      44.758  14.654  10.683  1.00 70.88           C  
ANISOU  783  CA  CYS A 121     9389   9928   7615   1904    327   -483       C  
ATOM    784  C   CYS A 121      44.902  14.720  12.195  1.00 69.51           C  
ANISOU  784  C   CYS A 121     9301   9315   7797   1895    236   -400       C  
ATOM    785  O   CYS A 121      45.962  15.093  12.702  1.00 81.24           O  
ANISOU  785  O   CYS A 121    10794  10573   9501   1912    272   -297       O  
ATOM    786  CB  CYS A 121      45.932  13.894  10.063  1.00 74.30           C  
ANISOU  786  CB  CYS A 121     9746  10390   8093   1885    486   -715       C  
ATOM    787  SG  CYS A 121      45.862  13.729   8.259  1.00 74.60           S  
ANISOU  787  SG  CYS A 121     9699  11010   7637   1902    624   -872       S  
ATOM    788  N   PHE A 122      43.851  14.346  12.917  1.00 56.90           N  
ANISOU  788  N   PHE A 122     7750   7626   6242   1864    121   -458       N  
ATOM    789  CA  PHE A 122      43.862  14.404  14.374  1.00 52.88           C  
ANISOU  789  CA  PHE A 122     7345   6762   5985   1868     43   -370       C  
ATOM    790  C   PHE A 122      44.296  13.048  14.917  1.00 57.75           C  
ANISOU  790  C   PHE A 122     7990   7128   6822   1820     46   -586       C  
ATOM    791  O   PHE A 122      43.589  12.049  14.759  1.00 56.29           O  
ANISOU  791  O   PHE A 122     7792   6960   6638   1738     56   -790       O  
ATOM    792  CB  PHE A 122      42.494  14.820  14.909  1.00 49.41           C  
ANISOU  792  CB  PHE A 122     6938   6368   5468   1875    -37   -274       C  
ATOM    793  CG  PHE A 122      42.113  16.224  14.537  1.00 53.23           C  
ANISOU  793  CG  PHE A 122     7410   7013   5801   1976    -49    -20       C  
ATOM    794  CD1 PHE A 122      42.737  17.306  15.139  1.00 57.26           C  
ANISOU  794  CD1 PHE A 122     8001   7306   6448   2039    -44    190       C  
ATOM    795  CD2 PHE A 122      41.147  16.464  13.577  1.00 51.29           C  
ANISOU  795  CD2 PHE A 122     7066   7127   5296   2017    -73      5       C  
ATOM    796  CE1 PHE A 122      42.400  18.599  14.792  1.00 52.88           C  
ANISOU  796  CE1 PHE A 122     7454   6823   5816   2140    -30    438       C  
ATOM    797  CE2 PHE A 122      40.806  17.756  13.229  1.00 52.12           C  
ANISOU  797  CE2 PHE A 122     7172   7348   5281   2155    -83    290       C  
ATOM    798  CZ  PHE A 122      41.432  18.823  13.835  1.00 51.35           C  
ANISOU  798  CZ  PHE A 122     7180   6964   5365   2216    -45    516       C  
ATOM    799  N   GLN A 123      45.462  13.021  15.559  1.00 57.49           N  
ANISOU  799  N   GLN A 123     7986   6853   7005   1873     34   -538       N  
ATOM    800  CA  GLN A 123      46.028  11.787  16.081  1.00 65.55           C  
ANISOU  800  CA  GLN A 123     9036   7613   8259   1888     28   -686       C  
ATOM    801  C   GLN A 123      46.761  11.984  17.399  1.00 58.59           C  
ANISOU  801  C   GLN A 123     8233   6466   7563   1973    -88   -533       C  
ATOM    802  O   GLN A 123      47.371  11.031  17.894  1.00 56.78           O  
ANISOU  802  O   GLN A 123     8027   6013   7533   2037   -116   -596       O  
ATOM    803  CB  GLN A 123      46.988  11.169  15.051  1.00 56.26           C  
ANISOU  803  CB  GLN A 123     7729   6507   7141   1912    145   -899       C  
ATOM    804  CG  GLN A 123      48.207  12.032  14.752  1.00 66.82           C  
ANISOU  804  CG  GLN A 123     8953   7921   8516   1971    191   -793       C  
ATOM    805  CD  GLN A 123      48.247  12.519  13.318  1.00 88.61           C  
ANISOU  805  CD  GLN A 123    11607  11040  11023   1938    348   -827       C  
ATOM    806  OE1 GLN A 123      47.340  12.247  12.533  1.00105.25           O  
ANISOU  806  OE1 GLN A 123    13724  13382  12885   1889    382   -945       O  
ATOM    807  NE2 GLN A 123      49.303  13.247  12.970  1.00 92.74           N  
ANISOU  807  NE2 GLN A 123    12014  11629  11592   1958    446   -719       N  
ATOM    808  N   LYS A 124      46.720  13.181  17.981  1.00 55.32           N  
ANISOU  808  N   LYS A 124     7859   6069   7091   1991   -165   -349       N  
ATOM    809  CA  LYS A 124      47.490  13.506  19.172  1.00 55.26           C  
ANISOU  809  CA  LYS A 124     7901   5878   7216   2066   -305   -255       C  
ATOM    810  C   LYS A 124      46.617  14.271  20.151  1.00 56.46           C  
ANISOU  810  C   LYS A 124     8199   6007   7246   2063   -382   -126       C  
ATOM    811  O   LYS A 124      45.954  15.241  19.771  1.00 61.23           O  
ANISOU  811  O   LYS A 124     8797   6736   7732   2030   -335    -61       O  
ATOM    812  CB  LYS A 124      48.724  14.341  18.814  1.00 48.67           C  
ANISOU  812  CB  LYS A 124     6912   5083   6500   2076   -306   -241       C  
ATOM    813  CG  LYS A 124      49.450  14.930  20.016  1.00 63.69           C  
ANISOU  813  CG  LYS A 124     8828   6849   8523   2124   -487   -187       C  
ATOM    814  CD  LYS A 124      50.582  15.841  19.571  1.00 57.45           C  
ANISOU  814  CD  LYS A 124     7839   6094   7895   2077   -459   -194       C  
ATOM    815  CE  LYS A 124      51.428  16.282  20.746  1.00 66.40           C  
ANISOU  815  CE  LYS A 124     8933   7115   9183   2109   -675   -221       C  
ATOM    816  NZ  LYS A 124      52.586  17.111  20.316  1.00 72.18           N  
ANISOU  816  NZ  LYS A 124     9419   7862  10145   2021   -634   -259       N  
ATOM    817  N   GLN A 125      46.623  13.842  21.409  1.00 64.28           N  
ANISOU  817  N   GLN A 125     9324   6849   8252   2122   -491    -81       N  
ATOM    818  CA  GLN A 125      45.950  14.562  22.479  1.00 63.97           C  
ANISOU  818  CA  GLN A 125     9427   6803   8077   2140   -555      8       C  
ATOM    819  C   GLN A 125      46.972  15.384  23.253  1.00 55.79           C  
ANISOU  819  C   GLN A 125     8384   5713   7099   2201   -722      3       C  
ATOM    820  O   GLN A 125      47.994  14.852  23.695  1.00 55.36           O  
ANISOU  820  O   GLN A 125     8297   5587   7150   2274   -851    -18       O  
ATOM    821  CB  GLN A 125      45.222  13.606  23.426  1.00 49.00           C  
ANISOU  821  CB  GLN A 125     7700   4822   6097   2157   -542     73       C  
ATOM    822  CG  GLN A 125      44.472  14.324  24.542  1.00 62.08           C  
ANISOU  822  CG  GLN A 125     9502   6519   7567   2185   -567    144       C  
ATOM    823  CD  GLN A 125      43.746  13.376  25.474  1.00 57.88           C  
ANISOU  823  CD  GLN A 125     9138   5924   6927   2188   -501    251       C  
ATOM    824  OE1 GLN A 125      44.009  12.174  25.484  1.00 57.12           O  
ANISOU  824  OE1 GLN A 125     9081   5689   6933   2190   -478    300       O  
ATOM    825  NE2 GLN A 125      42.823  13.913  26.262  1.00 48.82           N  
ANISOU  825  NE2 GLN A 125     8094   4862   5593   2192   -443    294       N  
ATOM    826  N   GLU A 126      46.697  16.673  23.404  1.00 47.98           N  
ANISOU  826  N   GLU A 126     7409   4753   6068   2177   -729      5       N  
ATOM    827  CA  GLU A 126      47.522  17.555  24.209  1.00 56.65           C  
ANISOU  827  CA  GLU A 126     8503   5789   7233   2199   -890    -60       C  
ATOM    828  C   GLU A 126      46.971  17.620  25.627  1.00 56.39           C  
ANISOU  828  C   GLU A 126     8671   5758   6995   2272   -991    -71       C  
ATOM    829  O   GLU A 126      45.786  17.375  25.866  1.00 61.60           O  
ANISOU  829  O   GLU A 126     9458   6464   7484   2284   -877     -5       O  
ATOM    830  CB  GLU A 126      47.567  18.957  23.597  1.00 53.00           C  
ANISOU  830  CB  GLU A 126     7959   5295   6885   2124   -816    -70       C  
ATOM    831  CG  GLU A 126      47.938  18.980  22.123  1.00 60.90           C  
ANISOU  831  CG  GLU A 126     8789   6344   8006   2055   -663     -8       C  
ATOM    832  CD  GLU A 126      49.433  19.124  21.886  1.00 88.91           C  
ANISOU  832  CD  GLU A 126    12140   9846  11795   2000   -712    -76       C  
ATOM    833  OE1 GLU A 126      49.826  19.441  20.741  1.00 95.74           O  
ANISOU  833  OE1 GLU A 126    12865  10753  12761   1928   -552    -15       O  
ATOM    834  OE2 GLU A 126      50.214  18.929  22.842  1.00 91.14           O  
ANISOU  834  OE2 GLU A 126    12395  10080  12154   2033   -907   -185       O  
ATOM    835  N   GLN A 127      47.848  17.950  26.571  1.00 62.28           N  
ANISOU  835  N   GLN A 127     9427   6490   7748   2317  -1202   -169       N  
ATOM    836  CA  GLN A 127      47.419  18.126  27.951  1.00 58.42           C  
ANISOU  836  CA  GLN A 127     9139   6056   7002   2397  -1307   -209       C  
ATOM    837  C   GLN A 127      46.608  19.407  28.075  1.00 64.64           C  
ANISOU  837  C   GLN A 127     9990   6820   7751   2360  -1209   -306       C  
ATOM    838  O   GLN A 127      47.033  20.471  27.615  1.00 70.53           O  
ANISOU  838  O   GLN A 127    10622   7463   8711   2286  -1212   -410       O  
ATOM    839  CB  GLN A 127      48.624  18.161  28.887  1.00 73.97           C  
ANISOU  839  CB  GLN A 127    11077   8070   8958   2465  -1603   -328       C  
ATOM    840  CG  GLN A 127      48.253  18.327  30.344  1.00 82.47           C  
ANISOU  840  CG  GLN A 127    12376   9268   9690   2565  -1730   -387       C  
ATOM    841  CD  GLN A 127      49.404  18.025  31.284  1.00 90.82           C  
ANISOU  841  CD  GLN A 127    13408  10445  10654   2678  -2066   -459       C  
ATOM    842  OE1 GLN A 127      49.467  16.949  31.882  1.00 88.41           O  
ANISOU  842  OE1 GLN A 127    13225  10221  10146   2825  -2148   -272       O  
ATOM    843  NE2 GLN A 127      50.319  18.979  31.427  1.00 94.94           N  
ANISOU  843  NE2 GLN A 127    13761  10975  11336   2611  -2267   -724       N  
ATOM    844  N   SER A 128      45.427  19.299  28.681  1.00 68.62           N  
ANISOU  844  N   SER A 128    10665   7397   8010   2416  -1095   -261       N  
ATOM    845  CA  SER A 128      44.503  20.420  28.815  1.00 58.53           C  
ANISOU  845  CA  SER A 128     9441   6098   6701   2428   -971   -352       C  
ATOM    846  C   SER A 128      44.189  20.610  30.293  1.00 66.71           C  
ANISOU  846  C   SER A 128    10674   7238   7435   2520  -1033   -479       C  
ATOM    847  O   SER A 128      43.457  19.810  30.884  1.00 73.89           O  
ANISOU  847  O   SER A 128    11714   8279   8084   2573   -937   -360       O  
ATOM    848  CB  SER A 128      43.231  20.176  28.004  1.00 61.44           C  
ANISOU  848  CB  SER A 128     9769   6510   7066   2419   -732   -203       C  
ATOM    849  OG  SER A 128      42.427  21.337  27.967  1.00 75.08           O  
ANISOU  849  OG  SER A 128    11499   8197   8831   2468   -622   -275       O  
ATOM    850  N   LEU A 129      44.731  21.674  30.885  1.00 76.63           N  
ANISOU  850  N   LEU A 129    11952   8439   8726   2526  -1174   -733       N  
ATOM    851  CA  LEU A 129      44.667  21.894  32.323  1.00 78.58           C  
ANISOU  851  CA  LEU A 129    12384   8829   8643   2617  -1282   -924       C  
ATOM    852  C   LEU A 129      43.571  22.873  32.727  1.00 87.90           C  
ANISOU  852  C   LEU A 129    13663   9992   9743   2679  -1094  -1091       C  
ATOM    853  O   LEU A 129      43.630  23.435  33.826  1.00 95.82           O  
ANISOU  853  O   LEU A 129    14800  11079  10528   2742  -1182  -1362       O  
ATOM    854  CB  LEU A 129      46.020  22.388  32.834  1.00 74.54           C  
ANISOU  854  CB  LEU A 129    11815   8305   8201   2583  -1597  -1183       C  
ATOM    855  CG  LEU A 129      47.224  21.487  32.558  1.00 76.13           C  
ANISOU  855  CG  LEU A 129    11877   8549   8500   2561  -1813  -1060       C  
ATOM    856  CD1 LEU A 129      48.522  22.200  32.912  1.00 80.61           C  
ANISOU  856  CD1 LEU A 129    12298   9098   9231   2495  -2115  -1366       C  
ATOM    857  CD2 LEU A 129      47.095  20.180  33.323  1.00 68.34           C  
ANISOU  857  CD2 LEU A 129    11053   7777   7138   2701  -1875   -841       C  
ATOM    858  N   LYS A 130      42.579  23.093  31.870  1.00 82.97           N  
ANISOU  858  N   LYS A 130    12963   9281   9282   2682   -848   -958       N  
ATOM    859  CA  LYS A 130      41.498  24.006  32.206  1.00 74.26           C  
ANISOU  859  CA  LYS A 130    11916   8153   8145   2782   -658  -1105       C  
ATOM    860  C   LYS A 130      40.651  23.446  33.341  1.00 83.09           C  
ANISOU  860  C   LYS A 130    13199   9540   8830   2879   -533  -1112       C  
ATOM    861  O   LYS A 130      40.511  22.231  33.505  1.00 93.00           O  
ANISOU  861  O   LYS A 130    14498  10963   9875   2855   -500   -878       O  
ATOM    862  CB  LYS A 130      40.615  24.268  30.986  1.00 70.83           C  
ANISOU  862  CB  LYS A 130    11326   7616   7968   2797   -453   -918       C  
ATOM    863  CG  LYS A 130      41.278  25.085  29.892  1.00 79.23           C  
ANISOU  863  CG  LYS A 130    12260   8411   9433   2732   -508   -890       C  
ATOM    864  CD  LYS A 130      41.683  26.455  30.406  1.00 76.51           C  
ANISOU  864  CD  LYS A 130    11980   7818   9274   2753   -563  -1196       C  
ATOM    865  CE  LYS A 130      42.065  27.378  29.266  1.00 60.17           C  
ANISOU  865  CE  LYS A 130     9792   5432   7640   2700   -525  -1099       C  
ATOM    866  NZ  LYS A 130      43.169  26.826  28.436  1.00 68.28           N  
ANISOU  866  NZ  LYS A 130    10693   6453   8798   2533   -636   -930       N  
ATOM    867  N   GLN A 131      40.080  24.351  34.127  1.00 84.42           N  
ANISOU  867  N   GLN A 131    13464   9731   8882   2990   -435  -1383       N  
ATOM    868  CA  GLN A 131      39.179  23.996  35.212  1.00 77.96           C  
ANISOU  868  CA  GLN A 131    12795   9190   7638   3093   -250  -1415       C  
ATOM    869  C   GLN A 131      37.736  24.132  34.744  1.00 76.03           C  
ANISOU  869  C   GLN A 131    12421   8964   7502   3163     77  -1311       C  
ATOM    870  O   GLN A 131      37.424  24.940  33.866  1.00 69.02           O  
ANISOU  870  O   GLN A 131    11380   7865   6981   3201    129  -1338       O  
ATOM    871  CB  GLN A 131      39.427  24.884  36.433  1.00 77.97           C  
ANISOU  871  CB  GLN A 131    12971   9259   7394   3190   -329  -1837       C  
ATOM    872  CG  GLN A 131      40.898  25.015  36.805  1.00 82.68           C  
ANISOU  872  CG  GLN A 131    13623   9826   7964   3117   -706  -2027       C  
ATOM    873  CD  GLN A 131      41.121  25.862  38.044  1.00104.61           C  
ANISOU  873  CD  GLN A 131    16568  12718  10462   3198   -810  -2510       C  
ATOM    874  OE1 GLN A 131      40.742  27.033  38.087  1.00106.21           O  
ANISOU  874  OE1 GLN A 131    16761  12724  10868   3248   -703  -2845       O  
ATOM    875  NE2 GLN A 131      41.737  25.270  39.062  1.00113.19           N  
ANISOU  875  NE2 GLN A 131    17812  14126  11071   3229  -1027  -2555       N  
ATOM    876  N   GLY A 132      36.858  23.329  35.327  1.00 74.76           N  
ANISOU  876  N   GLY A 132    12308   9067   7031   3184    301  -1172       N  
ATOM    877  CA  GLY A 132      35.458  23.362  34.939  1.00 67.17           C  
ANISOU  877  CA  GLY A 132    11168   8179   6175   3237    612  -1087       C  
ATOM    878  C   GLY A 132      34.736  22.112  35.417  1.00 75.21           C  
ANISOU  878  C   GLY A 132    12208   9462   6905   3162    840   -843       C  
ATOM    879  O   GLY A 132      35.111  21.512  36.425  1.00 83.33           O  
ANISOU  879  O   GLY A 132    13464  10651   7547   3148    826   -795       O  
ATOM    880  N   ALA A 133      33.690  21.745  34.670  1.00 76.68           N  
ANISOU  880  N   ALA A 133    12147   9695   7294   3113   1048   -682       N  
ATOM    881  CA  ALA A 133      32.889  20.573  34.991  1.00 74.31           C  
ANISOU  881  CA  ALA A 133    11809   9598   6826   2993   1311   -452       C  
ATOM    882  C   ALA A 133      33.349  19.405  34.135  1.00 76.16           C  
ANISOU  882  C   ALA A 133    11986   9716   7235   2790   1187   -181       C  
ATOM    883  O   ALA A 133      33.063  19.388  32.928  1.00 92.75           O  
ANISOU  883  O   ALA A 133    13836  11739   9665   2728   1146   -142       O  
ATOM    884  CB  ALA A 133      31.406  20.852  34.759  1.00 69.53           C  
ANISOU  884  CB  ALA A 133    10915   9143   6360   3044   1624   -497       C  
ATOM    885  N   PRO A 134      34.038  18.412  34.700  1.00 74.83           N  
ANISOU  885  N   PRO A 134    12040   9539   6852   2704   1126      6       N  
ATOM    886  CA  PRO A 134      34.607  17.340  33.872  1.00 69.71           C  
ANISOU  886  CA  PRO A 134    11350   8722   6415   2540    995    221       C  
ATOM    887  C   PRO A 134      33.539  16.560  33.118  1.00 68.37           C  
ANISOU  887  C   PRO A 134    10923   8572   6481   2362   1226    342       C  
ATOM    888  O   PRO A 134      32.435  16.333  33.615  1.00 66.59           O  
ANISOU  888  O   PRO A 134    10622   8510   6167   2314   1541    385       O  
ATOM    889  CB  PRO A 134      35.334  16.453  34.891  1.00 67.86           C  
ANISOU  889  CB  PRO A 134    11420   8497   5866   2540    948    421       C  
ATOM    890  CG  PRO A 134      35.603  17.347  36.053  1.00 67.84           C  
ANISOU  890  CG  PRO A 134    11626   8665   5487   2723    891    235       C  
ATOM    891  CD  PRO A 134      34.443  18.297  36.111  1.00 71.40           C  
ANISOU  891  CD  PRO A 134    11920   9249   5959   2790   1138     16       C  
ATOM    892  N   LEU A 135      33.883  16.160  31.896  1.00 73.03           N  
ANISOU  892  N   LEU A 135    11358   9015   7374   2254   1073    369       N  
ATOM    893  CA  LEU A 135      33.027  15.301  31.098  1.00 80.18           C  
ANISOU  893  CA  LEU A 135    12016   9933   8515   2053   1232    434       C  
ATOM    894  C   LEU A 135      33.228  13.842  31.503  1.00 80.13           C  
ANISOU  894  C   LEU A 135    12164   9787   8495   1877   1346    662       C  
ATOM    895  O   LEU A 135      34.256  13.462  32.069  1.00 73.63           O  
ANISOU  895  O   LEU A 135    11616   8831   7528   1939   1214    792       O  
ATOM    896  CB  LEU A 135      33.312  15.500  29.609  1.00 75.04           C  
ANISOU  896  CB  LEU A 135    11149   9219   8142   2025   1020    335       C  
ATOM    897  CG  LEU A 135      32.990  16.905  29.092  1.00 74.39           C  
ANISOU  897  CG  LEU A 135    10902   9244   8117   2206    937    180       C  
ATOM    898  CD1 LEU A 135      33.482  17.092  27.666  1.00 54.56           C  
ANISOU  898  CD1 LEU A 135     8246   6680   5805   2197    719    147       C  
ATOM    899  CD2 LEU A 135      31.497  17.181  29.184  1.00 68.08           C  
ANISOU  899  CD2 LEU A 135     9845   8674   7348   2223   1174    121       C  
ATOM    900  N   ILE A 136      32.225  13.021  31.201  1.00 83.51           N  
ANISOU  900  N   ILE A 136    12394  10235   9103   1659   1591    711       N  
ATOM    901  CA  ILE A 136      32.103  11.683  31.763  1.00 84.38           C  
ANISOU  901  CA  ILE A 136    12645  10188   9228   1471   1813    955       C  
ATOM    902  C   ILE A 136      32.051  10.661  30.636  1.00 85.44           C  
ANISOU  902  C   ILE A 136    12595  10120   9747   1232   1791    914       C  
ATOM    903  O   ILE A 136      31.434  10.904  29.592  1.00 93.27           O  
ANISOU  903  O   ILE A 136    13255  11234  10950   1143   1751    695       O  
ATOM    904  CB  ILE A 136      30.853  11.582  32.664  1.00 78.84           C  
ANISOU  904  CB  ILE A 136    11881   9676   8397   1381   2220   1045       C  
ATOM    905  CG1 ILE A 136      30.911  12.657  33.754  1.00 71.08           C  
ANISOU  905  CG1 ILE A 136    11082   8923   7001   1640   2244   1013       C  
ATOM    906  CG2 ILE A 136      30.736  10.202  33.278  1.00 73.66           C  
ANISOU  906  CG2 ILE A 136    11400   8818   7771   1173   2492   1359       C  
ATOM    907  CD1 ILE A 136      29.562  13.027  34.334  1.00 83.58           C  
ANISOU  907  CD1 ILE A 136    12480  10789   8489   1617   2621    961       C  
ATOM    908  N   ALA A 137      32.708   9.517  30.855  1.00 81.37           N  
ANISOU  908  N   ALA A 137    12302   9301   9315   1147   1807   1116       N  
ATOM    909  CA  ALA A 137      32.712   8.397  29.913  1.00 78.39           C  
ANISOU  909  CA  ALA A 137    11798   8663   9324    912   1823   1057       C  
ATOM    910  C   ALA A 137      33.230   8.830  28.543  1.00 71.74           C  
ANISOU  910  C   ALA A 137    10763   7865   8630    962   1516    769       C  
ATOM    911  O   ALA A 137      32.688   8.451  27.504  1.00 74.50           O  
ANISOU  911  O   ALA A 137    10836   8234   9236    768   1530    554       O  
ATOM    912  CB  ALA A 137      31.325   7.761  29.798  1.00 77.36           C  
ANISOU  912  CB  ALA A 137    11404   8561   9427    594   2161   1018       C  
ATOM    913  N   THR A 138      34.301   9.618  28.544  1.00 71.48           N  
ANISOU  913  N   THR A 138    10871   7865   8424   1214   1243    757       N  
ATOM    914  CA  THR A 138      34.838  10.178  27.316  1.00 74.63           C  
ANISOU  914  CA  THR A 138    11107   8336   8912   1282    988    532       C  
ATOM    915  C   THR A 138      35.608   9.129  26.525  1.00 70.77           C  
ANISOU  915  C   THR A 138    10633   7583   8671   1192    905    473       C  
ATOM    916  O   THR A 138      36.263   8.248  27.089  1.00 66.72           O  
ANISOU  916  O   THR A 138    10344   6784   8221   1206    934    647       O  
ATOM    917  CB  THR A 138      35.745  11.373  27.619  1.00 77.29           C  
ANISOU  917  CB  THR A 138    11574   8760   9031   1544    763    539       C  
ATOM    918  OG1 THR A 138      36.689  11.018  28.639  1.00 82.47           O  
ANISOU  918  OG1 THR A 138    12530   9249   9557   1660    702    731       O  
ATOM    919  CG2 THR A 138      34.918  12.563  28.082  1.00 71.14           C  
ANISOU  919  CG2 THR A 138    10722   8239   8070   1645    832    494       C  
ATOM    920  N   SER A 139      35.519   9.237  25.202  1.00 65.71           N  
ANISOU  920  N   SER A 139     9754   7055   8159   1124    804    224       N  
ATOM    921  CA  SER A 139      36.230   8.351  24.291  1.00 62.37           C  
ANISOU  921  CA  SER A 139     9311   6433   7954   1053    732     82       C  
ATOM    922  C   SER A 139      36.392   9.071  22.962  1.00 66.19           C  
ANISOU  922  C   SER A 139     9581   7181   8388   1101    558   -151       C  
ATOM    923  O   SER A 139      35.701  10.054  22.681  1.00 60.82           O  
ANISOU  923  O   SER A 139     8738   6807   7564   1146    521   -192       O  
ATOM    924  CB  SER A 139      35.498   7.017  24.108  1.00 68.61           C  
ANISOU  924  CB  SER A 139    10024   7016   9029    769    938     -7       C  
ATOM    925  OG  SER A 139      34.114   7.231  23.911  1.00 76.68           O  
ANISOU  925  OG  SER A 139    10782   8293  10058    589   1060   -127       O  
ATOM    926  N   VAL A 140      37.323   8.577  22.147  1.00 73.59           N  
ANISOU  926  N   VAL A 140    10524   8000   9438   1116    466   -285       N  
ATOM    927  CA  VAL A 140      37.666   9.240  20.896  1.00 70.06           C  
ANISOU  927  CA  VAL A 140     9916   7810   8894   1183    322   -460       C  
ATOM    928  C   VAL A 140      38.133   8.201  19.887  1.00 80.69           C  
ANISOU  928  C   VAL A 140    11199   9048  10413   1081    329   -718       C  
ATOM    929  O   VAL A 140      38.676   7.153  20.245  1.00 77.41           O  
ANISOU  929  O   VAL A 140    10918   8276  10218   1049    399   -714       O  
ATOM    930  CB  VAL A 140      38.743  10.333  21.113  1.00 62.93           C  
ANISOU  930  CB  VAL A 140     9123   6942   7847   1416    180   -308       C  
ATOM    931  CG1 VAL A 140      40.093   9.703  21.425  1.00 51.03           C  
ANISOU  931  CG1 VAL A 140     7773   5144   6473   1502    134   -260       C  
ATOM    932  CG2 VAL A 140      38.826  11.263  19.899  1.00 55.82           C  
ANISOU  932  CG2 VAL A 140     8056   6346   6808   1479     84   -403       C  
ATOM    933  N   SER A 141      37.899   8.504  18.611  1.00 74.06           N  
ANISOU  933  N   SER A 141    10156   8524   9459   1049    259   -945       N  
ATOM    934  CA  SER A 141      38.404   7.719  17.496  1.00 73.91           C  
ANISOU  934  CA  SER A 141    10063   8496   9522    984    256  -1249       C  
ATOM    935  C   SER A 141      38.542   8.650  16.302  1.00 71.86           C  
ANISOU  935  C   SER A 141     9659   8672   8974   1083    141  -1331       C  
ATOM    936  O   SER A 141      37.694   9.520  16.088  1.00 83.01           O  
ANISOU  936  O   SER A 141    10944  10412  10185   1107     76  -1261       O  
ATOM    937  CB  SER A 141      37.478   6.547  17.152  1.00 80.29           C  
ANISOU  937  CB  SER A 141    10744   9229  10531    712    354  -1553       C  
ATOM    938  OG  SER A 141      36.216   7.015  16.714  1.00 86.04           O  
ANISOU  938  OG  SER A 141    11233  10354  11105    604    307  -1658       O  
ATOM    939  N   SER A 142      39.618   8.475  15.539  1.00 59.20           N  
ANISOU  939  N   SER A 142     8071   7072   7351   1159    133  -1455       N  
ATOM    940  CA  SER A 142      39.871   9.289  14.359  1.00 59.81           C  
ANISOU  940  CA  SER A 142     8038   7559   7128   1254     68  -1496       C  
ATOM    941  C   SER A 142      40.167   8.377  13.175  1.00 64.21           C  
ANISOU  941  C   SER A 142     8502   8231   7663   1173    111  -1896       C  
ATOM    942  O   SER A 142      40.201   7.152  13.301  1.00 65.39           O  
ANISOU  942  O   SER A 142     8676   8089   8082   1047    190  -2152       O  
ATOM    943  CB  SER A 142      41.026  10.270  14.593  1.00 54.90           C  
ANISOU  943  CB  SER A 142     7518   6887   6454   1447     52  -1215       C  
ATOM    944  OG  SER A 142      42.275   9.602  14.588  1.00 71.18           O  
ANISOU  944  OG  SER A 142     9640   8702   8703   1492    114  -1307       O  
ATOM    945  N   TRP A 143      40.376   8.989  12.008  1.00 67.86           N  
ANISOU  945  N   TRP A 143     8871   9117   7796   1252     76  -1950       N  
ATOM    946  CA  TRP A 143      40.726   8.212  10.824  1.00 66.97           C  
ANISOU  946  CA  TRP A 143     8677   9186   7584   1200    130  -2359       C  
ATOM    947  C   TRP A 143      42.082   7.541  10.995  1.00 67.34           C  
ANISOU  947  C   TRP A 143     8824   8867   7897   1268    262  -2445       C  
ATOM    948  O   TRP A 143      42.253   6.367  10.650  1.00 73.43           O  
ANISOU  948  O   TRP A 143     9578   9472   8852   1182    343  -2835       O  
ATOM    949  CB  TRP A 143      40.722   9.112   9.588  1.00 66.74           C  
ANISOU  949  CB  TRP A 143     8553   9731   7074   1304     82  -2320       C  
ATOM    950  CG  TRP A 143      40.865   8.360   8.297  1.00 74.61           C  
ANISOU  950  CG  TRP A 143     9452  11039   7856   1246    123  -2787       C  
ATOM    951  CD1 TRP A 143      41.993   8.235   7.536  1.00 68.70           C  
ANISOU  951  CD1 TRP A 143     8726  10390   6987   1337    264  -2911       C  
ATOM    952  CD2 TRP A 143      39.844   7.615   7.625  1.00 75.93           C  
ANISOU  952  CD2 TRP A 143     9468  11479   7904   1075     32  -3238       C  
ATOM    953  NE1 TRP A 143      41.733   7.464   6.428  1.00 86.30           N  
ANISOU  953  NE1 TRP A 143    10852  12945   8991   1250    272  -3421       N  
ATOM    954  CE2 TRP A 143      40.420   7.072   6.460  1.00 75.45           C  
ANISOU  954  CE2 TRP A 143     9369  11681   7618   1081    112  -3644       C  
ATOM    955  CE3 TRP A 143      38.498   7.359   7.895  1.00 80.53           C  
ANISOU  955  CE3 TRP A 143     9916  12126   8556    907   -104  -3365       C  
ATOM    956  CZ2 TRP A 143      39.694   6.287   5.566  1.00 85.57           C  
ANISOU  956  CZ2 TRP A 143    10501  13287   8724    922     34  -4201       C  
ATOM    957  CZ3 TRP A 143      37.780   6.582   7.006  1.00 89.55           C  
ANISOU  957  CZ3 TRP A 143    10878  13583   9563    733   -186  -3902       C  
ATOM    958  CH2 TRP A 143      38.379   6.055   5.856  1.00 82.72           C  
ANISOU  958  CH2 TRP A 143     9997  12976   8457    740   -130  -4329       C  
ATOM    959  N   GLN A 144      43.053   8.270  11.546  1.00 72.90           N  
ANISOU  959  N   GLN A 144     9613   9427   8659   1426    282  -2105       N  
ATOM    960  CA  GLN A 144      44.385   7.723  11.763  1.00 72.23           C  
ANISOU  960  CA  GLN A 144     9573   9030   8843   1525    382  -2158       C  
ATOM    961  C   GLN A 144      44.420   6.760  12.943  1.00 67.79           C  
ANISOU  961  C   GLN A 144     9127   7931   8699   1504    380  -2143       C  
ATOM    962  O   GLN A 144      45.216   5.815  12.939  1.00 64.22           O  
ANISOU  962  O   GLN A 144     8691   7189   8522   1563    466  -2329       O  
ATOM    963  CB  GLN A 144      45.387   8.858  11.981  1.00 75.69           C  
ANISOU  963  CB  GLN A 144    10015   9517   9226   1675    384  -1815       C  
ATOM    964  CG  GLN A 144      45.504   9.835  10.815  1.00 81.02           C  
ANISOU  964  CG  GLN A 144    10600  10672   9512   1710    437  -1749       C  
ATOM    965  CD  GLN A 144      44.298  10.753  10.679  1.00 86.84           C  
ANISOU  965  CD  GLN A 144    11342  11699   9954   1677    323  -1547       C  
ATOM    966  OE1 GLN A 144      43.543  10.953  11.633  1.00 81.37           O  
ANISOU  966  OE1 GLN A 144    10712  10832   9374   1647    216  -1391       O  
ATOM    967  NE2 GLN A 144      44.107  11.305   9.487  1.00 88.06           N  
ANISOU  967  NE2 GLN A 144    11424  12319   9715   1706    354  -1541       N  
ATOM    968  N   ILE A 145      43.583   6.983  13.952  1.00 77.79           N  
ANISOU  968  N   ILE A 145    10480   9062  10014   1441    301  -1907       N  
ATOM    969  CA  ILE A 145      43.478   6.090  15.102  1.00 69.56           C  
ANISOU  969  CA  ILE A 145     9577   7542   9312   1414    321  -1827       C  
ATOM    970  C   ILE A 145      42.038   5.597  15.172  1.00 69.65           C  
ANISOU  970  C   ILE A 145     9563   7552   9347   1185    346  -1955       C  
ATOM    971  O   ILE A 145      41.242   6.109  15.972  1.00 71.88           O  
ANISOU  971  O   ILE A 145     9886   7861   9564   1140    306  -1707       O  
ATOM    972  CB  ILE A 145      43.903   6.797  16.400  1.00 63.32           C  
ANISOU  972  CB  ILE A 145     8916   6594   8547   1552    232  -1409       C  
ATOM    973  CG1 ILE A 145      45.207   7.566  16.174  1.00 62.90           C  
ANISOU  973  CG1 ILE A 145     8808   6654   8438   1731    188  -1313       C  
ATOM    974  CG2 ILE A 145      44.088   5.795  17.526  1.00 57.50           C  
ANISOU  974  CG2 ILE A 145     8344   5380   8124   1587    257  -1290       C  
ATOM    975  CD1 ILE A 145      45.727   8.301  17.385  1.00 60.13           C  
ANISOU  975  CD1 ILE A 145     8552   6183   8110   1856     68   -980       C  
ATOM    976  N   PRO A 146      41.659   4.612  14.350  1.00 75.58           N  
ANISOU  976  N   PRO A 146    10226   8285  10206   1026    421  -2372       N  
ATOM    977  CA  PRO A 146      40.242   4.234  14.244  1.00 76.02           C  
ANISOU  977  CA  PRO A 146    10181   8424  10279    768    431  -2556       C  
ATOM    978  C   PRO A 146      39.712   3.453  15.433  1.00 78.74           C  
ANISOU  978  C   PRO A 146    10649   8288  10979    636    533  -2401       C  
ATOM    979  O   PRO A 146      38.523   3.116  15.447  1.00 82.89           O  
ANISOU  979  O   PRO A 146    11066   8852  11578    390    573  -2538       O  
ATOM    980  CB  PRO A 146      40.211   3.386  12.965  1.00 74.80           C  
ANISOU  980  CB  PRO A 146     9894   8380  10147    641    475  -3115       C  
ATOM    981  CG  PRO A 146      41.569   2.789  12.895  1.00 69.36           C  
ANISOU  981  CG  PRO A 146     9315   7361   9677    812    569  -3191       C  
ATOM    982  CD  PRO A 146      42.510   3.831  13.432  1.00 65.71           C  
ANISOU  982  CD  PRO A 146     8935   6965   9067   1071    505  -2745       C  
ATOM    983  N   GLN A 147      40.537   3.164  16.432  1.00 76.78           N  
ANISOU  983  N   GLN A 147    10612   7616  10944    791    577  -2104       N  
ATOM    984  CA  GLN A 147      40.086   2.394  17.579  1.00 74.88           C  
ANISOU  984  CA  GLN A 147    10528   6918  11005    688    699  -1890       C  
ATOM    985  C   GLN A 147      39.313   3.280  18.549  1.00 74.12           C  
ANISOU  985  C   GLN A 147    10466   7004  10695    676    671  -1521       C  
ATOM    986  O   GLN A 147      39.570   4.481  18.669  1.00 74.01           O  
ANISOU  986  O   GLN A 147    10441   7309  10370    846    540  -1330       O  
ATOM    987  CB  GLN A 147      41.274   1.744  18.295  1.00 77.70           C  
ANISOU  987  CB  GLN A 147    11105   6790  11630    909    732  -1676       C  
ATOM    988  CG  GLN A 147      42.098   0.804  17.422  1.00 96.35           C  
ANISOU  988  CG  GLN A 147    13433   8909  14265    964    792  -2047       C  
ATOM    989  CD  GLN A 147      43.033   1.540  16.473  1.00104.00           C  
ANISOU  989  CD  GLN A 147    14268  10271  14977   1149    685  -2216       C  
ATOM    990  OE1 GLN A 147      43.332   2.720  16.667  1.00 87.23           O  
ANISOU  990  OE1 GLN A 147    12121   8482  12541   1281    559  -1965       O  
ATOM    991  NE2 GLN A 147      43.494   0.845  15.437  1.00107.18           N  
ANISOU  991  NE2 GLN A 147    14580  10622  15522   1150    763  -2654       N  
ATOM    992  N   ASN A 148      38.347   2.673  19.236  1.00 76.23           N  
ANISOU  992  N   ASN A 148    10765   7046  11152    464    823  -1436       N  
ATOM    993  CA  ASN A 148      37.566   3.371  20.256  1.00 77.99           C  
ANISOU  993  CA  ASN A 148    11024   7412  11197    449    856  -1101       C  
ATOM    994  C   ASN A 148      38.425   3.478  21.509  1.00 86.19           C  
ANISOU  994  C   ASN A 148    12354   8197  12197    692    843   -665       C  
ATOM    995  O   ASN A 148      38.522   2.532  22.295  1.00 84.71           O  
ANISOU  995  O   ASN A 148    12360   7576  12249    665    986   -465       O  
ATOM    996  CB  ASN A 148      36.260   2.634  20.533  1.00 81.75           C  
ANISOU  996  CB  ASN A 148    11404   7752  11903    117   1065  -1168       C  
ATOM    997  CG  ASN A 148      35.321   3.425  21.426  1.00 91.99           C  
ANISOU  997  CG  ASN A 148    12668   9294  12990     93   1127   -892       C  
ATOM    998  OD1 ASN A 148      35.721   4.398  22.062  1.00 88.84           O  
ANISOU  998  OD1 ASN A 148    12392   9060  12303    339   1030   -613       O  
ATOM    999  ND2 ASN A 148      34.062   3.007  21.476  1.00114.37           N  
ANISOU  999  ND2 ASN A 148    15312  12152  15990   -212   1301  -1003       N  
ATOM   1000  N   THR A 149      39.053   4.635  21.698  1.00 79.80           N  
ANISOU 1000  N   THR A 149    11576   7658  11087    931    667   -514       N  
ATOM   1001  CA  THR A 149      40.002   4.847  22.782  1.00 66.95           C  
ANISOU 1001  CA  THR A 149    10183   5875   9379   1182    585   -174       C  
ATOM   1002  C   THR A 149      39.340   5.655  23.892  1.00 69.68           C  
ANISOU 1002  C   THR A 149    10618   6402   9456   1207    607    101       C  
ATOM   1003  O   THR A 149      38.976   6.817  23.687  1.00 65.27           O  
ANISOU 1003  O   THR A 149     9938   6201   8660   1237    528     48       O  
ATOM   1004  CB  THR A 149      41.252   5.565  22.277  1.00 61.48           C  
ANISOU 1004  CB  THR A 149     9444   5338   8578   1408    379   -239       C  
ATOM   1005  OG1 THR A 149      41.898   4.765  21.279  1.00 73.12           O  
ANISOU 1005  OG1 THR A 149    10835   6655  10291   1405    395   -508       O  
ATOM   1006  CG2 THR A 149      42.216   5.818  23.426  1.00 57.78           C  
ANISOU 1006  CG2 THR A 149     9170   4758   8026   1656    251     71       C  
ATOM   1007  N   SER A 150      39.188   5.041  25.060  1.00 69.23           N  
ANISOU 1007  N   SER A 150    10780   6093   9432   1213    732    399       N  
ATOM   1008  CA  SER A 150      38.622   5.751  26.196  1.00 75.98           C  
ANISOU 1008  CA  SER A 150    11743   7135   9990   1258    781    649       C  
ATOM   1009  C   SER A 150      39.647   6.720  26.771  1.00 70.39           C  
ANISOU 1009  C   SER A 150    11152   6584   9009   1545    538    768       C  
ATOM   1010  O   SER A 150      40.846   6.431  26.811  1.00 67.25           O  
ANISOU 1010  O   SER A 150    10841   6027   8683   1724    377    820       O  
ATOM   1011  CB  SER A 150      38.166   4.764  27.267  1.00 78.63           C  
ANISOU 1011  CB  SER A 150    12297   7179  10401   1176   1019    963       C  
ATOM   1012  OG  SER A 150      39.271   4.056  27.792  1.00 89.01           O  
ANISOU 1012  OG  SER A 150    13851   8175  11793   1379    934   1198       O  
ATOM   1013  N   LEU A 151      39.170   7.882  27.206  1.00 62.09           N  
ANISOU 1013  N   LEU A 151    10077   5842   7673   1589    511    779       N  
ATOM   1014  CA  LEU A 151      40.028   8.929  27.733  1.00 63.98           C  
ANISOU 1014  CA  LEU A 151    10399   6239   7673   1816    285    818       C  
ATOM   1015  C   LEU A 151      39.643   9.263  29.169  1.00 60.73           C  
ANISOU 1015  C   LEU A 151    10196   5934   6947   1899    346   1034       C  
ATOM   1016  O   LEU A 151      38.468   9.172  29.536  1.00 67.44           O  
ANISOU 1016  O   LEU A 151    11041   6858   7726   1768    587   1093       O  
ATOM   1017  CB  LEU A 151      39.933  10.200  26.880  1.00 53.70           C  
ANISOU 1017  CB  LEU A 151     8888   5196   6321   1823    182    588       C  
ATOM   1018  CG  LEU A 151      40.190  10.042  25.382  1.00 54.26           C  
ANISOU 1018  CG  LEU A 151     8744   5268   6605   1744    142    370       C  
ATOM   1019  CD1 LEU A 151      39.888  11.347  24.657  1.00 54.54           C  
ANISOU 1019  CD1 LEU A 151     8607   5575   6541   1763     80    236       C  
ATOM   1020  CD2 LEU A 151      41.621   9.591  25.125  1.00 52.36           C  
ANISOU 1020  CD2 LEU A 151     8538   4852   6507   1861     -8    358       C  
ATOM   1021  N   PRO A 152      40.608   9.648  30.003  1.00 65.22           N  
ANISOU 1021  N   PRO A 152    10928   6544   7308   2112    137   1132       N  
ATOM   1022  CA  PRO A 152      40.267  10.078  31.364  1.00 64.24           C  
ANISOU 1022  CA  PRO A 152    11009   6595   6806   2208    178   1284       C  
ATOM   1023  C   PRO A 152      39.338  11.282  31.334  1.00 68.94           C  
ANISOU 1023  C   PRO A 152    11487   7450   7260   2159    273   1093       C  
ATOM   1024  O   PRO A 152      39.503  12.196  30.524  1.00 75.62           O  
ANISOU 1024  O   PRO A 152    12149   8370   8213   2163    153    863       O  
ATOM   1025  CB  PRO A 152      41.627  10.429  31.979  1.00 61.18           C  
ANISOU 1025  CB  PRO A 152    10739   6254   6253   2444   -151   1308       C  
ATOM   1026  CG  PRO A 152      42.621   9.655  31.173  1.00 60.66           C  
ANISOU 1026  CG  PRO A 152    10581   5946   6521   2478   -288   1306       C  
ATOM   1027  CD  PRO A 152      42.063   9.598  29.780  1.00 69.24           C  
ANISOU 1027  CD  PRO A 152    11430   6962   7918   2275   -141   1100       C  
ATOM   1028  N   GLY A 153      38.339  11.263  32.214  1.00 63.74           N  
ANISOU 1028  N   GLY A 153    10929   6916   6372   2123    514   1210       N  
ATOM   1029  CA  GLY A 153      37.426  12.389  32.298  1.00 60.93           C  
ANISOU 1029  CA  GLY A 153    10457   6802   5890   2120    625   1026       C  
ATOM   1030  C   GLY A 153      38.158  13.653  32.713  1.00 60.15           C  
ANISOU 1030  C   GLY A 153    10423   6837   5594   2311    377    845       C  
ATOM   1031  O   GLY A 153      39.076  13.621  33.535  1.00 70.59           O  
ANISOU 1031  O   GLY A 153    11948   8177   6697   2450    187    910       O  
ATOM   1032  N   ALA A 154      37.750  14.777  32.128  1.00 58.34           N  
ANISOU 1032  N   ALA A 154    10011   6694   5463   2322    369    612       N  
ATOM   1033  CA  ALA A 154      38.448  16.035  32.350  1.00 66.14           C  
ANISOU 1033  CA  ALA A 154    11030   7726   6373   2464    150    402       C  
ATOM   1034  C   ALA A 154      37.532  17.183  31.963  1.00 70.19           C  
ANISOU 1034  C   ALA A 154    11379   8323   6968   2491    270    214       C  
ATOM   1035  O   ALA A 154      36.629  16.998  31.140  1.00 68.97           O  
ANISOU 1035  O   ALA A 154    11019   8190   6996   2402    428    241       O  
ATOM   1036  CB  ALA A 154      39.750  16.093  31.538  1.00 64.11           C  
ANISOU 1036  CB  ALA A 154    10697   7311   6349   2467   -131    349       C  
ATOM   1037  N   PRO A 155      37.728  18.370  32.541  1.00 69.39           N  
ANISOU 1037  N   PRO A 155    11350   8266   6750   2623    190      9       N  
ATOM   1038  CA  PRO A 155      36.923  19.525  32.114  1.00 57.92           C  
ANISOU 1038  CA  PRO A 155     9741   6826   5438   2691    296   -160       C  
ATOM   1039  C   PRO A 155      37.170  19.931  30.672  1.00 64.93           C  
ANISOU 1039  C   PRO A 155    10422   7573   6677   2655    191   -157       C  
ATOM   1040  O   PRO A 155      36.248  20.432  30.016  1.00 56.28           O  
ANISOU 1040  O   PRO A 155     9142   6517   5724   2694    313   -171       O  
ATOM   1041  CB  PRO A 155      37.348  20.630  33.092  1.00 70.02           C  
ANISOU 1041  CB  PRO A 155    11437   8365   6802   2831    201   -413       C  
ATOM   1042  CG  PRO A 155      37.897  19.902  34.281  1.00 77.22           C  
ANISOU 1042  CG  PRO A 155    12593   9406   7342   2843    130   -353       C  
ATOM   1043  CD  PRO A 155      38.554  18.676  33.721  1.00 68.91           C  
ANISOU 1043  CD  PRO A 155    11521   8264   6399   2729     20    -94       C  
ATOM   1044  N   SER A 156      38.380  19.732  30.156  1.00 59.86           N  
ANISOU 1044  N   SER A 156     9790   6793   6160   2597    -25   -127       N  
ATOM   1045  CA  SER A 156      38.709  20.178  28.812  1.00 53.53           C  
ANISOU 1045  CA  SER A 156     8814   5882   5642   2567   -100   -111       C  
ATOM   1046  C   SER A 156      39.575  19.144  28.105  1.00 57.23           C  
ANISOU 1046  C   SER A 156     9240   6300   6206   2450   -207      2       C  
ATOM   1047  O   SER A 156      40.310  18.383  28.741  1.00 55.19           O  
ANISOU 1047  O   SER A 156     9104   6016   5851   2431   -303     37       O  
ATOM   1048  CB  SER A 156      39.418  21.537  28.833  1.00 52.42           C  
ANISOU 1048  CB  SER A 156     8702   5578   5638   2639   -223   -265       C  
ATOM   1049  OG  SER A 156      40.685  21.442  29.454  1.00 56.75           O  
ANISOU 1049  OG  SER A 156     9363   6057   6143   2606   -425   -353       O  
ATOM   1050  N   PHE A 157      39.475  19.129  26.776  1.00 52.95           N  
ANISOU 1050  N   PHE A 157     8520   5759   5840   2399   -189     57       N  
ATOM   1051  CA  PHE A 157      40.232  18.226  25.921  1.00 54.89           C  
ANISOU 1051  CA  PHE A 157     8695   5969   6190   2300   -256    116       C  
ATOM   1052  C   PHE A 157      40.804  19.016  24.755  1.00 51.81           C  
ANISOU 1052  C   PHE A 157     8179   5539   5967   2303   -310    118       C  
ATOM   1053  O   PHE A 157      40.157  19.933  24.242  1.00 59.88           O  
ANISOU 1053  O   PHE A 157     9126   6602   7025   2366   -250    144       O  
ATOM   1054  CB  PHE A 157      39.360  17.080  25.388  1.00 49.43           C  
ANISOU 1054  CB  PHE A 157     7908   5381   5491   2198   -127    168       C  
ATOM   1055  CG  PHE A 157      38.840  16.161  26.455  1.00 61.35           C  
ANISOU 1055  CG  PHE A 157     9542   6891   6878   2158    -24    221       C  
ATOM   1056  CD1 PHE A 157      37.737  16.511  27.215  1.00 61.22           C  
ANISOU 1056  CD1 PHE A 157     9546   6987   6729   2193    124    221       C  
ATOM   1057  CD2 PHE A 157      39.447  14.938  26.686  1.00 58.05           C  
ANISOU 1057  CD2 PHE A 157     9217   6352   6488   2096    -47    292       C  
ATOM   1058  CE1 PHE A 157      37.256  15.662  28.193  1.00 60.90           C  
ANISOU 1058  CE1 PHE A 157     9625   6958   6556   2141    267    309       C  
ATOM   1059  CE2 PHE A 157      38.971  14.084  27.663  1.00 57.19           C  
ANISOU 1059  CE2 PHE A 157     9247   6213   6268   2060     77    406       C  
ATOM   1060  CZ  PHE A 157      37.875  14.446  28.417  1.00 65.01           C  
ANISOU 1060  CZ  PHE A 157    10265   7337   7097   2069    245    425       C  
ATOM   1061  N   ILE A 158      42.018  18.665  24.343  1.00 51.51           N  
ANISOU 1061  N   ILE A 158     8113   5424   6033   2252   -406    114       N  
ATOM   1062  CA  ILE A 158      42.674  19.297  23.204  1.00 48.54           C  
ANISOU 1062  CA  ILE A 158     7615   5024   5803   2230   -414    145       C  
ATOM   1063  C   ILE A 158      43.168  18.195  22.279  1.00 53.60           C  
ANISOU 1063  C   ILE A 158     8157   5732   6479   2155   -397    149       C  
ATOM   1064  O   ILE A 158      43.974  17.353  22.691  1.00 57.26           O  
ANISOU 1064  O   ILE A 158     8648   6120   6988   2137   -469    103       O  
ATOM   1065  CB  ILE A 158      43.841  20.203  23.631  1.00 58.13           C  
ANISOU 1065  CB  ILE A 158     8853   6069   7166   2230   -521     84       C  
ATOM   1066  CG1 ILE A 158      43.334  21.368  24.483  1.00 59.00           C  
ANISOU 1066  CG1 ILE A 158     9066   6084   7267   2304   -524     17       C  
ATOM   1067  CG2 ILE A 158      44.594  20.724  22.407  1.00 55.44           C  
ANISOU 1067  CG2 ILE A 158     8372   5697   6994   2174   -474    155       C  
ATOM   1068  CD1 ILE A 158      44.421  22.332  24.900  1.00 57.59           C  
ANISOU 1068  CD1 ILE A 158     8894   5714   7275   2268   -632   -104       C  
ATOM   1069  N   PHE A 159      42.694  18.202  21.035  1.00 51.35           N  
ANISOU 1069  N   PHE A 159     7752   5599   6159   2133   -311    193       N  
ATOM   1070  CA  PHE A 159      43.085  17.214  20.037  1.00 58.31           C  
ANISOU 1070  CA  PHE A 159     8534   6577   7045   2065   -274    140       C  
ATOM   1071  C   PHE A 159      43.866  17.910  18.932  1.00 52.80           C  
ANISOU 1071  C   PHE A 159     7735   5939   6387   2063   -231    203       C  
ATOM   1072  O   PHE A 159      43.345  18.817  18.273  1.00 56.16           O  
ANISOU 1072  O   PHE A 159     8127   6473   6739   2107   -181    329       O  
ATOM   1073  CB  PHE A 159      41.862  16.489  19.476  1.00 45.76           C  
ANISOU 1073  CB  PHE A 159     6877   5179   5331   2020   -209     88       C  
ATOM   1074  CG  PHE A 159      41.114  15.710  20.507  1.00 58.37           C  
ANISOU 1074  CG  PHE A 159     8554   6702   6921   1982   -194     47       C  
ATOM   1075  CD1 PHE A 159      41.566  14.465  20.910  1.00 55.38           C  
ANISOU 1075  CD1 PHE A 159     8239   6173   6630   1922   -190    -18       C  
ATOM   1076  CD2 PHE A 159      39.975  16.230  21.095  1.00 49.52           C  
ANISOU 1076  CD2 PHE A 159     7448   5647   5722   2019   -158     95       C  
ATOM   1077  CE1 PHE A 159      40.888  13.744  21.872  1.00 58.45           C  
ANISOU 1077  CE1 PHE A 159     8724   6471   7012   1878   -139      4       C  
ATOM   1078  CE2 PHE A 159      39.291  15.513  22.059  1.00 51.66           C  
ANISOU 1078  CE2 PHE A 159     7787   5865   5975   1967    -95     81       C  
ATOM   1079  CZ  PHE A 159      39.749  14.267  22.447  1.00 50.30           C  
ANISOU 1079  CZ  PHE A 159     7700   5535   5876   1886    -79     56       C  
ATOM   1080  N   SER A 160      45.118  17.498  18.749  1.00 52.64           N  
ANISOU 1080  N   SER A 160     7660   5849   6492   2028   -237    142       N  
ATOM   1081  CA  SER A 160      45.977  18.069  17.722  1.00 54.86           C  
ANISOU 1081  CA  SER A 160     7827   6195   6823   2002   -147    206       C  
ATOM   1082  C   SER A 160      46.594  16.950  16.897  1.00 65.69           C  
ANISOU 1082  C   SER A 160     9091   7680   8188   1970    -76     69       C  
ATOM   1083  O   SER A 160      46.156  15.796  16.970  1.00 66.57           O  
ANISOU 1083  O   SER A 160     9225   7813   8257   1964    -94    -72       O  
ATOM   1084  CB  SER A 160      47.065  18.943  18.353  1.00 62.42           C  
ANISOU 1084  CB  SER A 160     8768   6943   8007   1981   -196    236       C  
ATOM   1085  OG  SER A 160      46.518  19.795  19.344  1.00 86.27           O  
ANISOU 1085  OG  SER A 160    11910   9818  11049   2016   -279    272       O  
ATOM   1086  N   PHE A 161      47.614  17.279  16.117  1.00 60.98           N  
ANISOU 1086  N   PHE A 161     8372   7140   7659   1943     30     97       N  
ATOM   1087  CA  PHE A 161      48.286  16.314  15.269  1.00 55.76           C  
ANISOU 1087  CA  PHE A 161     7589   6605   6993   1932    135    -62       C  
ATOM   1088  C   PHE A 161      49.738  16.153  15.690  1.00 66.53           C  
ANISOU 1088  C   PHE A 161     8826   7811   8642   1935    121   -134       C  
ATOM   1089  O   PHE A 161      50.349  17.068  16.249  1.00 58.37           O  
ANISOU 1089  O   PHE A 161     7756   6644   7781   1904     71    -38       O  
ATOM   1090  CB  PHE A 161      48.229  16.748  13.805  1.00 57.75           C  
ANISOU 1090  CB  PHE A 161     7769   7155   7020   1914    319     23       C  
ATOM   1091  CG  PHE A 161      48.809  18.110  13.556  1.00 62.25           C  
ANISOU 1091  CG  PHE A 161     8301   7691   7661   1881    422    275       C  
ATOM   1092  CD1 PHE A 161      48.019  19.241  13.663  1.00 58.51           C  
ANISOU 1092  CD1 PHE A 161     7935   7179   7117   1906    396    516       C  
ATOM   1093  CD2 PHE A 161      50.145  18.262  13.215  1.00 62.24           C  
ANISOU 1093  CD2 PHE A 161     8140   7670   7840   1824    564    270       C  
ATOM   1094  CE1 PHE A 161      48.547  20.493  13.434  1.00 66.72           C  
ANISOU 1094  CE1 PHE A 161     8957   8112   8281   1865    515    761       C  
ATOM   1095  CE2 PHE A 161      50.681  19.519  12.989  1.00 56.52           C  
ANISOU 1095  CE2 PHE A 161     7370   6871   7234   1752    692    510       C  
ATOM   1096  CZ  PHE A 161      49.878  20.634  13.098  1.00 63.09           C  
ANISOU 1096  CZ  PHE A 161     8344   7615   8011   1768    670    763       C  
ATOM   1097  N   HIS A 162      50.286  14.978  15.408  1.00 66.78           N  
ANISOU 1097  N   HIS A 162     8769   7856   8748   1975    162   -332       N  
ATOM   1098  CA  HIS A 162      51.726  14.804  15.425  1.00 73.46           C  
ANISOU 1098  CA  HIS A 162     9416   8643   9854   2003    197   -414       C  
ATOM   1099  C   HIS A 162      52.311  15.352  14.129  1.00 70.37           C  
ANISOU 1099  C   HIS A 162     8860   8484   9393   1938    452   -376       C  
ATOM   1100  O   HIS A 162      51.741  15.166  13.050  1.00 68.92           O  
ANISOU 1100  O   HIS A 162     8711   8543   8932   1926    604   -401       O  
ATOM   1101  CB  HIS A 162      52.088  13.327  15.587  1.00 82.14           C  
ANISOU 1101  CB  HIS A 162    10478   9642  11091   2113    165   -633       C  
ATOM   1102  CG  HIS A 162      51.598  12.721  16.866  1.00 86.14           C  
ANISOU 1102  CG  HIS A 162    11157   9908  11662   2184    -52   -612       C  
ATOM   1103  ND1 HIS A 162      52.190  12.970  18.086  1.00 87.06           N  
ANISOU 1103  ND1 HIS A 162    11270   9865  11943   2251   -259   -532       N  
ATOM   1104  CD2 HIS A 162      50.581  11.861  17.112  1.00 82.29           C  
ANISOU 1104  CD2 HIS A 162    10848   9332  11086   2191    -79   -654       C  
ATOM   1105  CE1 HIS A 162      51.553  12.297  19.028  1.00 75.31           C  
ANISOU 1105  CE1 HIS A 162     9979   8217  10420   2317   -394   -489       C  
ATOM   1106  NE2 HIS A 162      50.571  11.618  18.464  1.00 68.90           N  
ANISOU 1106  NE2 HIS A 162     9276   7420   9483   2269   -270   -553       N  
ATOM   1107  N   ASN A 163      53.449  16.044  14.237  1.00 67.98           N  
ANISOU 1107  N   ASN A 163     8369   8132   9331   1887    504   -316       N  
ATOM   1108  CA  ASN A 163      54.142  16.490  13.030  1.00 85.84           C  
ANISOU 1108  CA  ASN A 163    10451  10609  11555   1815    801   -261       C  
ATOM   1109  C   ASN A 163      54.923  15.352  12.385  1.00 79.05           C  
ANISOU 1109  C   ASN A 163     9401   9885  10751   1898    951   -522       C  
ATOM   1110  O   ASN A 163      54.960  15.240  11.154  1.00 83.13           O  
ANISOU 1110  O   ASN A 163     9867  10682  11035   1885   1216   -555       O  
ATOM   1111  CB  ASN A 163      55.076  17.660  13.347  1.00 97.81           C  
ANISOU 1111  CB  ASN A 163    11799  12003  13362   1687    844   -115       C  
ATOM   1112  CG  ASN A 163      54.577  18.970  12.773  1.00 98.75           C  
ANISOU 1112  CG  ASN A 163    12029  12157  13334   1572   1003    195       C  
ATOM   1113  OD1 ASN A 163      53.709  18.985  11.901  1.00 98.00           O  
ANISOU 1113  OD1 ASN A 163    12087  12274  12877   1610   1117    315       O  
ATOM   1114  ND2 ASN A 163      55.127  20.079  13.255  1.00 99.77           N  
ANISOU 1114  ND2 ASN A 163    12077  12075  13758   1437   1002    322       N  
ATOM   1115  N   ALA A 164      55.538  14.498  13.198  1.00 68.96           N  
ANISOU 1115  N   ALA A 164     8021   8421   9761   2010    788   -708       N  
ATOM   1116  CA  ALA A 164      56.323  13.393  12.677  1.00 68.36           C  
ANISOU 1116  CA  ALA A 164     7749   8412   9811   2132    925   -974       C  
ATOM   1117  C   ALA A 164      55.411  12.298  12.127  1.00 69.71           C  
ANISOU 1117  C   ALA A 164     8106   8641   9742   2204    968  -1172       C  
ATOM   1118  O   ALA A 164      54.284  12.122  12.596  1.00 61.44           O  
ANISOU 1118  O   ALA A 164     7308   7486   8549   2189    796  -1122       O  
ATOM   1119  CB  ALA A 164      57.217  12.814  13.768  1.00 71.46           C  
ANISOU 1119  CB  ALA A 164     7980   8566  10603   2275    704  -1077       C  
ATOM   1120  N   PRO A 165      55.880  11.541  11.131  1.00 71.61           N  
ANISOU 1120  N   PRO A 165     8207   9052   9950   2271   1208  -1431       N  
ATOM   1121  CA  PRO A 165      55.056  10.458  10.582  1.00 80.15           C  
ANISOU 1121  CA  PRO A 165     9444  10171  10839   2316   1247  -1700       C  
ATOM   1122  C   PRO A 165      55.078   9.220  11.465  1.00109.27           C  
ANISOU 1122  C   PRO A 165    13188  13476  14855   2465   1068  -1875       C  
ATOM   1123  O   PRO A 165      56.030   8.434  11.431  1.00121.32           O  
ANISOU 1123  O   PRO A 165    14530  14887  16678   2625   1145  -2084       O  
ATOM   1124  CB  PRO A 165      55.695  10.196   9.214  1.00 77.46           C  
ANISOU 1124  CB  PRO A 165     8919  10163  10349   2340   1592  -1941       C  
ATOM   1125  CG  PRO A 165      57.126  10.563   9.403  1.00 72.53           C  
ANISOU 1125  CG  PRO A 165     7982   9516  10058   2390   1701  -1882       C  
ATOM   1126  CD  PRO A 165      57.161  11.681  10.415  1.00 69.95           C  
ANISOU 1126  CD  PRO A 165     7676   9028   9873   2290   1484  -1519       C  
ATOM   1127  N   HIS A 166      54.025   9.039  12.263  1.00125.12           N  
ANISOU 1127  N   HIS A 166    15445  15276  16821   2425    849  -1769       N  
ATOM   1128  CA  HIS A 166      53.961   7.902  13.171  1.00137.51           C  
ANISOU 1128  CA  HIS A 166    17112  16450  18688   2555    696  -1849       C  
ATOM   1129  C   HIS A 166      53.559   6.609  12.476  1.00138.80           C  
ANISOU 1129  C   HIS A 166    17332  16524  18882   2582    836  -2217       C  
ATOM   1130  O   HIS A 166      53.818   5.529  13.018  1.00142.78           O  
ANISOU 1130  O   HIS A 166    17869  16658  19724   2730    788  -2321       O  
ATOM   1131  CB  HIS A 166      52.989   8.194  14.316  1.00140.35           C  
ANISOU 1131  CB  HIS A 166    17714  16629  18985   2488    455  -1584       C  
ATOM   1132  CG  HIS A 166      53.526   9.153  15.332  1.00144.75           C  
ANISOU 1132  CG  HIS A 166    18230  17147  19623   2515    266  -1299       C  
ATOM   1133  ND1 HIS A 166      52.908   9.376  16.544  1.00150.52           N  
ANISOU 1133  ND1 HIS A 166    19158  17710  20324   2506     45  -1080       N  
ATOM   1134  CD2 HIS A 166      54.623   9.946  15.318  1.00149.09           C  
ANISOU 1134  CD2 HIS A 166    18547  17813  20285   2535    272  -1233       C  
ATOM   1135  CE1 HIS A 166      53.603  10.263  17.234  1.00151.67           C  
ANISOU 1135  CE1 HIS A 166    19208  17878  20540   2528   -100   -923       C  
ATOM   1136  NE2 HIS A 166      54.647  10.628  16.511  1.00150.49           N  
ANISOU 1136  NE2 HIS A 166    18788  17886  20505   2532     28  -1013       N  
ATOM   1137  N   LYS A 167      52.935   6.689  11.301  1.00132.83           N  
ANISOU 1137  N   LYS A 167    16592  16091  17788   2451    999  -2419       N  
ATOM   1138  CA  LYS A 167      52.563   5.482  10.575  1.00128.47           C  
ANISOU 1138  CA  LYS A 167    16075  15478  17259   2449   1129  -2854       C  
ATOM   1139  C   LYS A 167      53.813   4.689  10.216  1.00127.92           C  
ANISOU 1139  C   LYS A 167    15810  15288  17504   2655   1308  -3141       C  
ATOM   1140  O   LYS A 167      54.774   5.236   9.668  1.00127.72           O  
ANISOU 1140  O   LYS A 167    15567  15539  17422   2718   1465  -3139       O  
ATOM   1141  CB  LYS A 167      51.776   5.831   9.309  1.00122.18           C  
ANISOU 1141  CB  LYS A 167    15292  15163  15968   2288   1247  -3039       C  
ATOM   1142  CG  LYS A 167      50.635   6.822   9.512  1.00113.65           C  
ANISOU 1142  CG  LYS A 167    14342  14287  14552   2127   1086  -2727       C  
ATOM   1143  CD  LYS A 167      49.788   6.469  10.723  1.00107.05           C  
ANISOU 1143  CD  LYS A 167    13679  13062  13934   2073    876  -2579       C  
ATOM   1144  CE  LYS A 167      49.478   7.711  11.542  1.00 94.92           C  
ANISOU 1144  CE  LYS A 167    12210  11565  12291   2041    715  -2118       C  
ATOM   1145  NZ  LYS A 167      49.046   7.376  12.924  1.00 90.63           N  
ANISOU 1145  NZ  LYS A 167    11818  10620  11998   2045    544  -1936       N  
ATOM   1146  N   VAL A 168      53.800   3.397  10.533  1.00130.96           N  
ANISOU 1146  N   VAL A 168    16263  15240  18255   2764   1305  -3380       N  
ATOM   1147  CA  VAL A 168      54.964   2.544  10.325  1.00133.56           C  
ANISOU 1147  CA  VAL A 168    16409  15369  18968   3015   1459  -3651       C  
ATOM   1148  C   VAL A 168      55.037   2.127   8.861  1.00140.89           C  
ANISOU 1148  C   VAL A 168    17237  16602  19694   2987   1755  -4175       C  
ATOM   1149  O   VAL A 168      54.152   2.459   8.065  1.00140.21           O  
ANISOU 1149  O   VAL A 168    17238  16883  19153   2774   1801  -4307       O  
ATOM   1150  CB  VAL A 168      54.921   1.315  11.251  1.00130.60           C  
ANISOU 1150  CB  VAL A 168    16172  14355  19097   3175   1352  -3667       C  
ATOM   1151  N   SER A 169      56.099   1.403   8.498  1.00146.40           N  
ANISOU 1151  N   SER A 169    17737  17180  20707   3223   1952  -4487       N  
ATOM   1152  CA  SER A 169      56.275   0.894   7.137  1.00147.64           C  
ANISOU 1152  CA  SER A 169    17793  17614  20691   3235   2265  -5053       C  
ATOM   1153  C   SER A 169      55.514  -0.424   6.962  1.00157.89           C  
ANISOU 1153  C   SER A 169    19314  18543  22135   3149   2251  -5398       C  
ATOM   1154  O   SER A 169      56.060  -1.462   6.589  1.00159.00           O  
ANISOU 1154  O   SER A 169    19432  18470  22509   3252   2377  -5648       O  
ATOM   1155  CB  SER A 169      57.757   0.730   6.820  1.00139.24           C  
ANISOU 1155  CB  SER A 169    16432  16616  19856   3475   2476  -5132       C  
ATOM   1156  OG  SER A 169      57.956   0.248   5.501  1.00133.11           O  
ANISOU 1156  OG  SER A 169    15612  16146  18818   3439   2758  -5554       O  
ATOM   1157  N   HIS A 170      54.212  -0.354   7.244  1.00180.06           N  
ANISOU 1157  N   HIS A 170    22331  21280  24805   2933   2089  -5385       N  
ATOM   1158  CA  HIS A 170      53.344  -1.520   7.147  1.00191.48           C  
ANISOU 1158  CA  HIS A 170    23978  22375  26401   2769   2056  -5663       C  
ATOM   1159  C   HIS A 170      52.976  -1.842   5.703  1.00194.01           C  
ANISOU 1159  C   HIS A 170    24275  23121  26318   2603   2214  -6186       C  
ATOM   1160  O   HIS A 170      52.657  -2.997   5.399  1.00206.12           O  
ANISOU 1160  O   HIS A 170    25902  24362  28052   2517   2248  -6521       O  
ATOM   1161  CB  HIS A 170      52.079  -1.284   7.984  1.00191.28           C  
ANISOU 1161  CB  HIS A 170    24139  22150  26388   2576   1840  -5459       C  
ATOM   1162  CG  HIS A 170      51.193  -2.486   8.123  1.00196.32           C  
ANISOU 1162  CG  HIS A 170    24962  22335  27296   2386   1809  -5667       C  
ATOM   1163  ND1 HIS A 170      51.025  -3.417   7.121  1.00203.36           N  
ANISOU 1163  ND1 HIS A 170    25851  23257  28159   2269   1937  -6166       N  
ATOM   1164  CD2 HIS A 170      50.416  -2.901   9.152  1.00193.60           C  
ANISOU 1164  CD2 HIS A 170    24802  21494  27265   2278   1681  -5438       C  
ATOM   1165  CE1 HIS A 170      50.188  -4.355   7.526  1.00203.39           C  
ANISOU 1165  CE1 HIS A 170    26012  22784  28484   2085   1884  -6251       C  
ATOM   1166  NE2 HIS A 170      49.803  -4.065   8.756  1.00198.37           N  
ANISOU 1166  NE2 HIS A 170    25494  21824  28055   2083   1746  -5798       N  
ATOM   1167  N   ASN A 171      53.006  -0.847   4.815  1.00173.56           N  
ANISOU 1167  N   ASN A 171    21569  21224  23151   2559   2306  -6243       N  
ATOM   1168  CA  ASN A 171      52.469  -0.920   3.457  1.00158.12           C  
ANISOU 1168  CA  ASN A 171    19615  19808  20655   2385   2394  -6657       C  
ATOM   1169  C   ASN A 171      50.961  -1.154   3.436  1.00151.87           C  
ANISOU 1169  C   ASN A 171    18967  19026  19711   2100   2189  -6831       C  
ATOM   1170  O   ASN A 171      50.381  -1.343   2.360  1.00143.20           O  
ANISOU 1170  O   ASN A 171    17864  18351  18193   1937   2196  -7198       O  
ATOM   1171  CB  ASN A 171      53.177  -1.995   2.616  1.00146.04           C  
ANISOU 1171  CB  ASN A 171    18035  18197  19255   2467   2601  -7082       C  
ATOM   1172  CG  ASN A 171      54.640  -1.676   2.371  1.00131.11           C  
ANISOU 1172  CG  ASN A 171    15947  16462  17405   2728   2841  -6971       C  
ATOM   1173  OD1 ASN A 171      55.021  -0.511   2.255  1.00133.00           O  
ANISOU 1173  OD1 ASN A 171    16064  17145  17324   2773   2915  -6691       O  
ATOM   1174  ND2 ASN A 171      55.469  -2.712   2.290  1.00114.40           N  
ANISOU 1174  ND2 ASN A 171    13782  13982  15703   2899   2977  -7186       N  
ATOM   1175  N   ALA A 172      50.307  -1.139   4.600  1.00154.81           N  
ANISOU 1175  N   ALA A 172    19446  18964  20410   2032   2002  -6571       N  
ATOM   1176  CA  ALA A 172      48.861  -1.327   4.639  1.00157.43           C  
ANISOU 1176  CA  ALA A 172    19869  19310  20637   1744   1823  -6727       C  
ATOM   1177  C   ALA A 172      48.140  -0.116   4.064  1.00150.17           C  
ANISOU 1177  C   ALA A 172    18896  19147  19016   1645   1713  -6643       C  
ATOM   1178  O   ALA A 172      47.317  -0.246   3.150  1.00158.67           O  
ANISOU 1178  O   ALA A 172    19943  20650  19694   1456   1643  -6979       O  
ATOM   1179  CB  ALA A 172      48.404  -1.600   6.073  1.00152.82           C  
ANISOU 1179  CB  ALA A 172    19415  18062  20587   1707   1693  -6420       C  
ATOM   1180  N   SER A 173      48.442   1.073   4.580  1.00132.07           N  
ANISOU 1180  N   SER A 173    16606  17021  16555   1735   1636  -5984       N  
ATOM   1181  CA  SER A 173      47.821   2.296   4.097  1.00118.44           C  
ANISOU 1181  CA  SER A 173    14858  15948  14196   1658   1512  -5682       C  
ATOM   1182  C   SER A 173      48.788   3.454   4.286  1.00110.08           C  
ANISOU 1182  C   SER A 173    13760  15057  13009   1831   1588  -5126       C  
ATOM   1183  O   SER A 173      49.650   3.424   5.168  1.00106.25           O  
ANISOU 1183  O   SER A 173    13269  14130  12969   1962   1626  -4866       O  
ATOM   1184  CB  SER A 173      46.502   2.585   4.823  1.00115.31           C  
ANISOU 1184  CB  SER A 173    14535  15461  13816   1469   1245  -5416       C  
ATOM   1185  OG  SER A 173      46.720   2.803   6.206  1.00116.38           O  
ANISOU 1185  OG  SER A 173    14760  15074  14383   1524   1171  -4914       O  
ATOM   1186  N   VAL A 174      48.634   4.474   3.448  1.00104.71           N  
ANISOU 1186  N   VAL A 174    13043  15019  11721   1828   1604  -4942       N  
ATOM   1187  CA  VAL A 174      49.441   5.686   3.509  1.00 89.27           C  
ANISOU 1187  CA  VAL A 174    11047  13251   9619   1941   1699  -4404       C  
ATOM   1188  C   VAL A 174      48.583   6.800   4.090  1.00 80.16           C  
ANISOU 1188  C   VAL A 174     9980  12163   8312   1868   1463  -3854       C  
ATOM   1189  O   VAL A 174      47.400   6.921   3.755  1.00 85.52           O  
ANISOU 1189  O   VAL A 174    10699  13130   8664   1765   1291  -3912       O  
ATOM   1190  CB  VAL A 174      49.984   6.070   2.118  1.00 96.79           C  
ANISOU 1190  CB  VAL A 174    11913  14849  10012   2009   1954  -4533       C  
ATOM   1191  CG1 VAL A 174      50.651   7.436   2.157  1.00 91.11           C  
ANISOU 1191  CG1 VAL A 174    11159  14317   9141   2071   2062  -3915       C  
ATOM   1192  CG2 VAL A 174      50.957   5.010   1.620  1.00 92.43           C  
ANISOU 1192  CG2 VAL A 174    11253  14207   9660   2114   2229  -5084       C  
ATOM   1193  N   ASP A 175      49.176   7.605   4.969  1.00 76.70           N  
ANISOU 1193  N   ASP A 175     9550  11464   8129   1929   1448  -3357       N  
ATOM   1194  CA  ASP A 175      48.458   8.691   5.621  1.00 73.09           C  
ANISOU 1194  CA  ASP A 175     9179  10997   7593   1883   1249  -2854       C  
ATOM   1195  C   ASP A 175      48.414   9.922   4.725  1.00 74.22           C  
ANISOU 1195  C   ASP A 175     9312  11672   7214   1912   1328  -2527       C  
ATOM   1196  O   ASP A 175      49.415  10.291   4.105  1.00 76.24           O  
ANISOU 1196  O   ASP A 175     9490  12128   7350   1976   1573  -2449       O  
ATOM   1197  CB  ASP A 175      49.117   9.031   6.958  1.00 74.24           C  
ANISOU 1197  CB  ASP A 175     9344  10640   8226   1931   1189  -2513       C  
ATOM   1198  CG  ASP A 175      48.493  10.234   7.621  1.00 71.77           C  
ANISOU 1198  CG  ASP A 175     9119  10310   7841   1899   1021  -2029       C  
ATOM   1199  OD1 ASP A 175      47.485  10.062   8.338  1.00 72.62           O  
ANISOU 1199  OD1 ASP A 175     9319  10241   8033   1837    827  -2000       O  
ATOM   1200  OD2 ASP A 175      49.016  11.351   7.424  1.00 75.88           O  
ANISOU 1200  OD2 ASP A 175     9608  10976   8245   1931   1108  -1687       O  
ATOM   1201  N   MET A 176      47.239  10.558   4.668  1.00 58.11           N  
ANISOU 1201  N   MET A 176     8897   7239   5941   2116   -197  -2187       N  
ATOM   1202  CA  MET A 176      47.037  11.698   3.776  1.00 70.70           C  
ANISOU 1202  CA  MET A 176    10537   8700   7627   2460   -368  -2307       C  
ATOM   1203  C   MET A 176      47.973  12.849   4.125  1.00 70.33           C  
ANISOU 1203  C   MET A 176    10826   8339   7558   2584   -511  -2287       C  
ATOM   1204  O   MET A 176      48.637  13.411   3.246  1.00 61.27           O  
ANISOU 1204  O   MET A 176     9867   6894   6518   2673   -679  -2188       O  
ATOM   1205  CB  MET A 176      45.584  12.166   3.839  1.00 88.07           C  
ANISOU 1205  CB  MET A 176    12464  11231   9766   2726   -309  -2612       C  
ATOM   1206  CG  MET A 176      44.564  11.048   3.862  1.00 99.05           C  
ANISOU 1206  CG  MET A 176    13486  13017  11129   2536   -121  -2680       C  
ATOM   1207  SD  MET A 176      42.955  11.633   4.423  1.00107.12           S  
ANISOU 1207  SD  MET A 176    14153  14527  12019   2810     -1  -3078       S  
ATOM   1208  CE  MET A 176      42.663  12.970   3.269  1.00 86.65           C  
ANISOU 1208  CE  MET A 176    11619  11763   9542   3345   -274  -3226       C  
ATOM   1209  N   CYS A 177      48.031  13.219   5.408  1.00 62.39           N  
ANISOU 1209  N   CYS A 177     9907   7402   6395   2569   -444  -2388       N  
ATOM   1210  CA  CYS A 177      48.856  14.350   5.822  1.00 61.76           C  
ANISOU 1210  CA  CYS A 177    10151   7036   6279   2668   -582  -2409       C  
ATOM   1211  C   CYS A 177      50.341  14.081   5.605  1.00 63.01           C  
ANISOU 1211  C   CYS A 177    10524   6905   6512   2424   -682  -2135       C  
ATOM   1212  O   CYS A 177      51.091  15.003   5.263  1.00 77.47           O  
ANISOU 1212  O   CYS A 177    12605   8435   8396   2491   -841  -2104       O  
ATOM   1213  CB  CYS A 177      48.575  14.688   7.288  1.00 66.73           C  
ANISOU 1213  CB  CYS A 177    10811   7841   6700   2683   -477  -2592       C  
ATOM   1214  SG  CYS A 177      46.914  15.329   7.589  1.00 70.20           S  
ANISOU 1214  SG  CYS A 177    11012   8623   7039   3048   -377  -2980       S  
ATOM   1215  N   ASP A 178      50.785  12.834   5.784  1.00 59.47           N  
ANISOU 1215  N   ASP A 178     9988   6543   6066   2141   -595  -1940       N  
ATOM   1216  CA  ASP A 178      52.173  12.503   5.479  1.00 57.30           C  
ANISOU 1216  CA  ASP A 178     9863   6037   5872   1948   -696  -1696       C  
ATOM   1217  C   ASP A 178      52.447  12.648   3.988  1.00 52.35           C  
ANISOU 1217  C   ASP A 178     9245   5221   5424   2016   -803  -1602       C  
ATOM   1218  O   ASP A 178      53.450  13.245   3.584  1.00 54.48           O  
ANISOU 1218  O   ASP A 178     9704   5245   5753   1988   -934  -1509       O  
ATOM   1219  CB  ASP A 178      52.495  11.083   5.950  1.00 57.30           C  
ANISOU 1219  CB  ASP A 178     9775   6163   5833   1687   -591  -1518       C  
ATOM   1220  CG  ASP A 178      52.403  10.933   7.454  1.00 70.61           C  
ANISOU 1220  CG  ASP A 178    11506   8016   7306   1588   -497  -1568       C  
ATOM   1221  OD1 ASP A 178      52.612  11.942   8.159  1.00 75.49           O  
ANISOU 1221  OD1 ASP A 178    12274   8587   7821   1675   -557  -1695       O  
ATOM   1222  OD2 ASP A 178      52.115   9.812   7.930  1.00 73.22           O  
ANISOU 1222  OD2 ASP A 178    11746   8515   7559   1413   -365  -1480       O  
ATOM   1223  N   LEU A 179      51.560  12.100   3.153  1.00 51.25           N  
ANISOU 1223  N   LEU A 179     8900   5214   5358   2084   -747  -1629       N  
ATOM   1224  CA  LEU A 179      51.711  12.254   1.712  1.00 52.91           C  
ANISOU 1224  CA  LEU A 179     9123   5274   5706   2168   -849  -1556       C  
ATOM   1225  C   LEU A 179      51.607  13.719   1.309  1.00 52.81           C  
ANISOU 1225  C   LEU A 179     9302   5066   5695   2419   -990  -1663       C  
ATOM   1226  O   LEU A 179      52.271  14.162   0.363  1.00 67.03           O  
ANISOU 1226  O   LEU A 179    11260   6637   7572   2427  -1105  -1549       O  
ATOM   1227  CB  LEU A 179      50.663  11.412   0.986  1.00 66.25           C  
ANISOU 1227  CB  LEU A 179    10546   7178   7448   2198   -770  -1603       C  
ATOM   1228  CG  LEU A 179      50.653  11.387  -0.543  1.00 62.74           C  
ANISOU 1228  CG  LEU A 179    10080   6641   7119   2282   -864  -1541       C  
ATOM   1229  CD1 LEU A 179      52.052  11.186  -1.068  1.00 49.85           C  
ANISOU 1229  CD1 LEU A 179     8610   4774   5556   2120   -928  -1320       C  
ATOM   1230  CD2 LEU A 179      49.732  10.276  -1.042  1.00 51.02           C  
ANISOU 1230  CD2 LEU A 179     8315   5399   5671   2222   -769  -1584       C  
ATOM   1231  N   LYS A 180      50.788  14.491   2.028  1.00 52.85           N  
ANISOU 1231  N   LYS A 180     9320   5155   5607   2627   -979  -1884       N  
ATOM   1232  CA  LYS A 180      50.641  15.911   1.723  1.00 54.62           C  
ANISOU 1232  CA  LYS A 180     9777   5153   5824   2901  -1127  -2002       C  
ATOM   1233  C   LYS A 180      51.956  16.658   1.920  1.00 71.87           C  
ANISOU 1233  C   LYS A 180    12291   7009   8008   2754  -1235  -1884       C  
ATOM   1234  O   LYS A 180      52.342  17.487   1.085  1.00 77.18           O  
ANISOU 1234  O   LYS A 180    13105   7480   8740   2751  -1350  -1759       O  
ATOM   1235  CB  LYS A 180      49.538  16.516   2.590  1.00 68.18           C  
ANISOU 1235  CB  LYS A 180    11428   7048   7430   3164  -1082  -2289       C  
ATOM   1236  CG  LYS A 180      49.419  18.021   2.515  1.00 59.85           C  
ANISOU 1236  CG  LYS A 180    10541   5819   6381   3331  -1216  -2312       C  
ATOM   1237  CD  LYS A 180      48.822  18.484   1.199  1.00 76.98           C  
ANISOU 1237  CD  LYS A 180    12665   7954   8630   3526  -1335  -2259       C  
ATOM   1238  CE  LYS A 180      48.340  19.927   1.300  1.00 79.79           C  
ANISOU 1238  CE  LYS A 180    13168   8202   8947   3766  -1454  -2351       C  
ATOM   1239  NZ  LYS A 180      47.847  20.444  -0.012  1.00 82.52           N  
ANISOU 1239  NZ  LYS A 180    13537   8487   9332   3955  -1600  -2282       N  
ATOM   1240  N   LYS A 181      52.668  16.364   3.010  1.00 64.52           N  
ANISOU 1240  N   LYS A 181    11397   6112   7005   2535  -1180  -1852       N  
ATOM   1241  CA  LYS A 181      53.965  16.996   3.232  1.00 61.23           C  
ANISOU 1241  CA  LYS A 181    11253   5428   6584   2358  -1286  -1756       C  
ATOM   1242  C   LYS A 181      54.985  16.543   2.196  1.00 51.71           C  
ANISOU 1242  C   LYS A 181    10049   4105   5495   2152  -1329  -1511       C  
ATOM   1243  O   LYS A 181      55.834  17.334   1.767  1.00 63.20           O  
ANISOU 1243  O   LYS A 181    11737   5300   6978   2065  -1438  -1438       O  
ATOM   1244  CB  LYS A 181      54.471  16.699   4.645  1.00 54.05           C  
ANISOU 1244  CB  LYS A 181    10344   4638   5555   2175  -1232  -1780       C  
ATOM   1245  CG  LYS A 181      53.571  17.205   5.760  1.00 78.08           C  
ANISOU 1245  CG  LYS A 181    13406   7812   8450   2357  -1176  -2037       C  
ATOM   1246  CD  LYS A 181      54.383  17.473   7.016  1.00 83.30           C  
ANISOU 1246  CD  LYS A 181    14224   8450   8975   2184  -1203  -2070       C  
ATOM   1247  CE  LYS A 181      53.749  16.846   8.244  1.00 88.01           C  
ANISOU 1247  CE  LYS A 181    14665   9375   9399   2174  -1051  -2178       C  
ATOM   1248  NZ  LYS A 181      53.773  15.360   8.167  1.00 97.55           N  
ANISOU 1248  NZ  LYS A 181    15628  10807  10630   1990   -932  -1981       N  
ATOM   1249  N   GLU A 182      54.917  15.277   1.778  1.00 57.08           N  
ANISOU 1249  N   GLU A 182    10478   4976   6235   2060  -1237  -1392       N  
ATOM   1250  CA  GLU A 182      55.834  14.785   0.755  1.00 48.06           C  
ANISOU 1250  CA  GLU A 182     9313   3754   5194   1899  -1264  -1187       C  
ATOM   1251  C   GLU A 182      55.615  15.501  -0.572  1.00 56.42           C  
ANISOU 1251  C   GLU A 182    10493   4634   6308   2035  -1348  -1165       C  
ATOM   1252  O   GLU A 182      56.578  15.826  -1.278  1.00 52.80           O  
ANISOU 1252  O   GLU A 182    10168   4006   5887   1897  -1409  -1029       O  
ATOM   1253  CB  GLU A 182      55.665  13.276   0.584  1.00 46.37           C  
ANISOU 1253  CB  GLU A 182     8833   3758   5026   1812  -1152  -1097       C  
ATOM   1254  CG  GLU A 182      56.042  12.459   1.808  1.00 54.77           C  
ANISOU 1254  CG  GLU A 182     9823   4965   6024   1655  -1083  -1062       C  
ATOM   1255  CD  GLU A 182      55.996  10.968   1.542  1.00 62.06           C  
ANISOU 1255  CD  GLU A 182    10553   6027   6999   1557   -991   -949       C  
ATOM   1256  OE1 GLU A 182      55.780  10.580   0.374  1.00 66.59           O  
ANISOU 1256  OE1 GLU A 182    11042   6589   7669   1595   -984   -906       O  
ATOM   1257  OE2 GLU A 182      56.176  10.184   2.497  1.00 63.48           O  
ANISOU 1257  OE2 GLU A 182    10694   6314   7113   1444   -934   -902       O  
ATOM   1258  N   LEU A 183      54.355  15.764  -0.925  1.00 59.15           N  
ANISOU 1258  N   LEU A 183    10794   5035   6644   2305  -1355  -1299       N  
ATOM   1259  CA  LEU A 183      54.073  16.451  -2.180  1.00 56.96           C  
ANISOU 1259  CA  LEU A 183    10568   4683   6393   2404  -1435  -1228       C  
ATOM   1260  C   LEU A 183      54.396  17.935  -2.092  1.00 57.96           C  
ANISOU 1260  C   LEU A 183    10956   4600   6467   2403  -1535  -1214       C  
ATOM   1261  O   LEU A 183      54.783  18.540  -3.097  1.00 59.47           O  
ANISOU 1261  O   LEU A 183    11295   4642   6657   2354  -1605  -1087       O  
ATOM   1262  CB  LEU A 183      52.618  16.225  -2.585  1.00 51.04           C  
ANISOU 1262  CB  LEU A 183     9617   4134   5642   2673  -1422  -1362       C  
ATOM   1263  CG  LEU A 183      52.446  14.954  -3.420  1.00 55.62           C  
ANISOU 1263  CG  LEU A 183    10000   4845   6288   2644  -1367  -1313       C  
ATOM   1264  CD1 LEU A 183      51.008  14.476  -3.433  1.00 58.71           C  
ANISOU 1264  CD1 LEU A 183    10133   5502   6672   2861  -1325  -1502       C  
ATOM   1265  CD2 LEU A 183      52.943  15.192  -4.837  1.00 48.87           C  
ANISOU 1265  CD2 LEU A 183     9237   3876   5455   2589  -1442  -1139       C  
ATOM   1266  N   GLN A 184      54.249  18.534  -0.908  1.00 54.68           N  
ANISOU 1266  N   GLN A 184    10625   4161   5992   2448  -1540  -1351       N  
ATOM   1267  CA  GLN A 184      54.756  19.886  -0.705  1.00 56.06           C  
ANISOU 1267  CA  GLN A 184    11083   4096   6120   2393  -1635  -1338       C  
ATOM   1268  C   GLN A 184      56.269  19.937  -0.874  1.00 55.23           C  
ANISOU 1268  C   GLN A 184    11138   3810   6034   2063  -1659  -1178       C  
ATOM   1269  O   GLN A 184      56.807  20.943  -1.350  1.00 78.47           O  
ANISOU 1269  O   GLN A 184    14324   6534   8958   1962  -1736  -1097       O  
ATOM   1270  CB  GLN A 184      54.358  20.395   0.681  1.00 57.84           C  
ANISOU 1270  CB  GLN A 184    11354   4349   6273   2493  -1627  -1534       C  
ATOM   1271  CG  GLN A 184      52.872  20.654   0.857  1.00 59.67           C  
ANISOU 1271  CG  GLN A 184    11452   4747   6473   2837  -1615  -1720       C  
ATOM   1272  CD  GLN A 184      52.526  21.078   2.275  1.00 71.02           C  
ANISOU 1272  CD  GLN A 184    12917   6244   7825   2925  -1581  -1930       C  
ATOM   1273  OE1 GLN A 184      53.163  20.644   3.235  1.00 75.26           O  
ANISOU 1273  OE1 GLN A 184    13469   6811   8315   2745  -1524  -1960       O  
ATOM   1274  NE2 GLN A 184      51.520  21.938   2.411  1.00 64.47           N  
ANISOU 1274  NE2 GLN A 184    12100   5438   6957   3211  -1624  -2084       N  
ATOM   1275  N   GLN A 185      56.965  18.862  -0.502  1.00 53.96           N  
ANISOU 1275  N   GLN A 185    10856   3740   5906   1891  -1598  -1138       N  
ATOM   1276  CA  GLN A 185      58.412  18.806  -0.678  1.00 63.89           C  
ANISOU 1276  CA  GLN A 185    12223   4864   7188   1586  -1627  -1005       C  
ATOM   1277  C   GLN A 185      58.789  18.795  -2.156  1.00 66.43           C  
ANISOU 1277  C   GLN A 185    12567   5117   7557   1509  -1632   -832       C  
ATOM   1278  O   GLN A 185      59.718  19.495  -2.574  1.00 58.32           O  
ANISOU 1278  O   GLN A 185    11739   3904   6515   1295  -1680   -736       O  
ATOM   1279  CB  GLN A 185      58.976  17.574   0.032  1.00 50.56           C  
ANISOU 1279  CB  GLN A 185    10342   3352   5516   1454  -1566   -991       C  
ATOM   1280  CG  GLN A 185      60.478  17.392  -0.127  1.00 50.14           C  
ANISOU 1280  CG  GLN A 185    10257   3304   5492   1132  -1582   -843       C  
ATOM   1281  CD  GLN A 185      61.264  18.549   0.456  1.00 78.45           C  
ANISOU 1281  CD  GLN A 185    14102   6686   9017    943  -1681   -894       C  
ATOM   1282  OE1 GLN A 185      61.503  18.606   1.660  1.00 58.41           O  
ANISOU 1282  OE1 GLN A 185    11565   4214   6414    879  -1707   -990       O  
ATOM   1283  NE2 GLN A 185      61.660  19.488  -0.398  1.00106.58           N  
ANISOU 1283  NE2 GLN A 185    17911   9996  12587    834  -1739   -832       N  
ATOM   1284  N   LEU A 186      58.081  17.998  -2.961  1.00 58.88           N  
ANISOU 1284  N   LEU A 186    11419   4312   6642   1663  -1580   -800       N  
ATOM   1285  CA  LEU A 186      58.354  17.960  -4.393  1.00 57.93           C  
ANISOU 1285  CA  LEU A 186    11326   4147   6538   1613  -1584   -652       C  
ATOM   1286  C   LEU A 186      58.033  19.300  -5.038  1.00 62.76           C  
ANISOU 1286  C   LEU A 186    12181   4586   7077   1679  -1665   -625       C  
ATOM   1287  O   LEU A 186      58.823  19.828  -5.830  1.00 65.76           O  
ANISOU 1287  O   LEU A 186    12757   4803   7427   1498  -1691   -491       O  
ATOM   1288  CB  LEU A 186      57.550  16.838  -5.051  1.00 58.55           C  
ANISOU 1288  CB  LEU A 186    11152   4432   6661   1778  -1524   -658       C  
ATOM   1289  CG  LEU A 186      57.597  16.769  -6.578  1.00 64.57           C  
ANISOU 1289  CG  LEU A 186    11940   5179   7416   1782  -1533   -535       C  
ATOM   1290  CD1 LEU A 186      59.032  16.611  -7.054  1.00 54.76           C  
ANISOU 1290  CD1 LEU A 186    10794   3827   6187   1509  -1511   -385       C  
ATOM   1291  CD2 LEU A 186      56.728  15.630  -7.098  1.00 47.21           C  
ANISOU 1291  CD2 LEU A 186     9487   3192   5259   1945  -1486   -580       C  
ATOM   1292  N   SER A 187      56.866  19.860  -4.712  1.00 59.95           N  
ANISOU 1292  N   SER A 187    11832   4262   6684   1942  -1709   -752       N  
ATOM   1293  CA  SER A 187      56.506  21.179  -5.215  1.00 57.18           C  
ANISOU 1293  CA  SER A 187    11742   3726   6256   2045  -1810   -739       C  
ATOM   1294  C   SER A 187      57.570  22.208  -4.865  1.00 62.40           C  
ANISOU 1294  C   SER A 187    12711   4120   6878   1793  -1855   -684       C  
ATOM   1295  O   SER A 187      57.883  23.090  -5.672  1.00 71.24           O  
ANISOU 1295  O   SER A 187    14098   5034   7935   1713  -1914   -577       O  
ATOM   1296  CB  SER A 187      55.152  21.600  -4.648  1.00 60.03           C  
ANISOU 1296  CB  SER A 187    12047   4172   6588   2379  -1856   -920       C  
ATOM   1297  OG  SER A 187      54.888  22.958  -4.945  1.00 68.75           O  
ANISOU 1297  OG  SER A 187    13446   5061   7614   2489  -1971   -920       O  
ATOM   1298  N   ARG A 188      58.141  22.102  -3.664  1.00 67.26           N  
ANISOU 1298  N   ARG A 188    13306   4734   7516   1650  -1831   -760       N  
ATOM   1299  CA  ARG A 188      59.230  22.986  -3.268  1.00 63.48           C  
ANISOU 1299  CA  ARG A 188    13095   4020   7004   1364  -1876   -727       C  
ATOM   1300  C   ARG A 188      60.391  22.905  -4.255  1.00 60.29           C  
ANISOU 1300  C   ARG A 188    12790   3514   6605   1046  -1856   -539       C  
ATOM   1301  O   ARG A 188      60.983  23.928  -4.614  1.00 67.51           O  
ANISOU 1301  O   ARG A 188    13997   4192   7460    847  -1903   -462       O  
ATOM   1302  CB  ARG A 188      59.687  22.621  -1.854  1.00 75.91           C  
ANISOU 1302  CB  ARG A 188    14582   5665   8595   1253  -1857   -847       C  
ATOM   1303  CG  ARG A 188      60.149  23.779  -0.996  1.00 63.71           C  
ANISOU 1303  CG  ARG A 188    13301   3912   6993   1115  -1930   -930       C  
ATOM   1304  CD  ARG A 188      60.300  23.350   0.466  1.00 70.54           C  
ANISOU 1304  CD  ARG A 188    14057   4901   7845   1088  -1919  -1087       C  
ATOM   1305  NE  ARG A 188      59.032  22.942   1.072  1.00 69.01           N  
ANISOU 1305  NE  ARG A 188    13685   4898   7637   1429  -1875  -1233       N  
ATOM   1306  CZ  ARG A 188      58.814  21.759   1.642  1.00 71.67           C  
ANISOU 1306  CZ  ARG A 188    13774   5472   7984   1486  -1802  -1289       C  
ATOM   1307  NH1 ARG A 188      59.783  20.859   1.700  1.00 83.23           N  
ANISOU 1307  NH1 ARG A 188    15147   7000   9478   1257  -1785  -1212       N  
ATOM   1308  NH2 ARG A 188      57.630  21.480   2.169  1.00 83.48           N  
ANISOU 1308  NH2 ARG A 188    15125   7142   9452   1769  -1748  -1431       N  
ATOM   1309  N   TYR A 189      60.718  21.698  -4.720  1.00 57.61           N  
ANISOU 1309  N   TYR A 189    12219   3344   6326    989  -1781   -466       N  
ATOM   1310  CA  TYR A 189      61.836  21.543  -5.645  1.00 68.00           C  
ANISOU 1310  CA  TYR A 189    13610   4585   7641    687  -1749   -298       C  
ATOM   1311  C   TYR A 189      61.494  22.067  -7.034  1.00 80.76           C  
ANISOU 1311  C   TYR A 189    15394   6106   9184    747  -1761   -170       C  
ATOM   1312  O   TYR A 189      62.351  22.643  -7.712  1.00 74.57           O  
ANISOU 1312  O   TYR A 189    14837   5155   8340    463  -1757    -35       O  
ATOM   1313  CB  TYR A 189      62.250  20.077  -5.721  1.00 54.65           C  
ANISOU 1313  CB  TYR A 189    11635   3094   6034    649  -1674   -270       C  
ATOM   1314  CG  TYR A 189      63.272  19.776  -6.791  1.00 54.65           C  
ANISOU 1314  CG  TYR A 189    11567   3174   6023    375  -1597   -101       C  
ATOM   1315  CD1 TYR A 189      64.593  20.169  -6.645  1.00 59.18           C  
ANISOU 1315  CD1 TYR A 189    12164   3747   6576    -22  -1575    -42       C  
ATOM   1316  CD2 TYR A 189      62.917  19.082  -7.940  1.00 53.45           C  
ANISOU 1316  CD2 TYR A 189    11284   3156   5870    502  -1536    -17       C  
ATOM   1317  CE1 TYR A 189      65.530  19.887  -7.616  1.00 66.50           C  
ANISOU 1317  CE1 TYR A 189    12970   4820   7477   -278  -1478     95       C  
ATOM   1318  CE2 TYR A 189      63.847  18.796  -8.917  1.00 53.71           C  
ANISOU 1318  CE2 TYR A 189    11225   3311   5870    260  -1444    120       C  
ATOM   1319  CZ  TYR A 189      65.151  19.201  -8.749  1.00 64.57           C  
ANISOU 1319  CZ  TYR A 189    12610   4703   7223   -127  -1407    175       C  
ATOM   1320  OH  TYR A 189      66.087  18.922  -9.714  1.00 63.70           O  
ANISOU 1320  OH  TYR A 189    12375   4762   7067   -374  -1296    293       O  
ATOM   1321  N   LEU A 190      60.252  21.867  -7.481  1.00 69.10           N  
ANISOU 1321  N   LEU A 190    13815   4743   7697   1094  -1778   -214       N  
ATOM   1322  CA  LEU A 190      59.872  22.322  -8.814  1.00 75.95           C  
ANISOU 1322  CA  LEU A 190    14850   5532   8475   1178  -1812   -103       C  
ATOM   1323  C   LEU A 190      59.913  23.840  -8.919  1.00 78.26           C  
ANISOU 1323  C   LEU A 190    15531   5540   8663   1124  -1904    -71       C  
ATOM   1324  O   LEU A 190      60.152  24.379 -10.006  1.00 89.97           O  
ANISOU 1324  O   LEU A 190    17258   6880  10048   1028  -1924     73       O  
ATOM   1325  CB  LEU A 190      58.480  21.800  -9.171  1.00 59.01           C  
ANISOU 1325  CB  LEU A 190    12499   3585   6338   1561  -1837   -190       C  
ATOM   1326  CG  LEU A 190      58.326  20.279  -9.132  1.00 61.99           C  
ANISOU 1326  CG  LEU A 190    12508   4234   6812   1620  -1747   -228       C  
ATOM   1327  CD1 LEU A 190      56.887  19.862  -9.394  1.00 55.24           C  
ANISOU 1327  CD1 LEU A 190    11457   3573   5960   1967  -1780   -338       C  
ATOM   1328  CD2 LEU A 190      59.276  19.626 -10.123  1.00 54.65           C  
ANISOU 1328  CD2 LEU A 190    11576   3311   5877   1406  -1678    -69       C  
ATOM   1329  N   GLN A 191      59.692  24.544  -7.808  1.00 65.15           N  
ANISOU 1329  N   GLN A 191    13955   3786   7012   1181  -1960   -200       N  
ATOM   1330  CA  GLN A 191      59.724  26.001  -7.845  1.00 71.17           C  
ANISOU 1330  CA  GLN A 191    15112   4252   7679   1141  -2055   -181       C  
ATOM   1331  C   GLN A 191      61.146  26.518  -8.016  1.00 71.84           C  
ANISOU 1331  C   GLN A 191    15439   4133   7725    670  -2024    -48       C  
ATOM   1332  O   GLN A 191      61.373  27.497  -8.736  1.00 78.81           O  
ANISOU 1332  O   GLN A 191    16668   4777   8500    548  -2069     65       O  
ATOM   1333  CB  GLN A 191      59.105  26.578  -6.573  1.00 71.66           C  
ANISOU 1333  CB  GLN A 191    15196   4272   7758   1338  -2120   -372       C  
ATOM   1334  CG  GLN A 191      57.673  26.153  -6.317  1.00 69.32           C  
ANISOU 1334  CG  GLN A 191    14658   4190   7489   1777  -2145   -521       C  
ATOM   1335  CD  GLN A 191      57.137  26.689  -5.004  1.00 78.60           C  
ANISOU 1335  CD  GLN A 191    15852   5341   8673   1949  -2189   -716       C  
ATOM   1336  OE1 GLN A 191      57.256  27.879  -4.713  1.00 89.54           O  
ANISOU 1336  OE1 GLN A 191    17559   6463   9998   1928  -2273   -744       O  
ATOM   1337  NE2 GLN A 191      56.548  25.811  -4.199  1.00 73.25           N  
ANISOU 1337  NE2 GLN A 191    14843   4929   8060   2112  -2128   -856       N  
ATOM   1338  N   HIS A 192      62.113  25.881  -7.359  1.00 70.62           N  
ANISOU 1338  N   HIS A 192    15113   4073   7648    388  -1950    -62       N  
ATOM   1339  CA  HIS A 192      63.504  26.335  -7.376  1.00 73.07           C  
ANISOU 1339  CA  HIS A 192    15604   4232   7926   -105  -1919     35       C  
ATOM   1340  C   HIS A 192      64.434  25.134  -7.501  1.00 71.10           C  
ANISOU 1340  C   HIS A 192    15080   4184   7749   -359  -1816     94       C  
ATOM   1341  O   HIS A 192      65.214  24.835  -6.593  1.00 70.86           O  
ANISOU 1341  O   HIS A 192    14931   4212   7779   -591  -1807     19       O  
ATOM   1342  CB  HIS A 192      63.821  27.146  -6.121  1.00 85.49           C  
ANISOU 1342  CB  HIS A 192    17314   5662   9505   -233  -1982    -98       C  
ATOM   1343  CG  HIS A 192      62.810  28.206  -5.815  1.00109.60           C  
ANISOU 1343  CG  HIS A 192    20606   8532  12503     79  -2088   -193       C  
ATOM   1344  ND1 HIS A 192      61.762  28.005  -4.943  1.00107.94           N  
ANISOU 1344  ND1 HIS A 192    20235   8438  12337    466  -2126   -371       N  
ATOM   1345  CD2 HIS A 192      62.684  29.476  -6.268  1.00111.49           C  
ANISOU 1345  CD2 HIS A 192    21243   8479  12640     60  -2165   -137       C  
ATOM   1346  CE1 HIS A 192      61.035  29.106  -4.870  1.00109.08           C  
ANISOU 1346  CE1 HIS A 192    20653   8377  12415    684  -2225   -430       C  
ATOM   1347  NE2 HIS A 192      61.573  30.014  -5.665  1.00107.86           N  
ANISOU 1347  NE2 HIS A 192    20852   7958  12173    455  -2259   -289       N  
ATOM   1348  N   PRO A 193      64.386  24.427  -8.632  1.00 69.41           N  
ANISOU 1348  N   PRO A 193    14772   4080   7521   -321  -1748    222       N  
ATOM   1349  CA  PRO A 193      65.267  23.261  -8.795  1.00 64.31           C  
ANISOU 1349  CA  PRO A 193    13882   3613   6941   -544  -1653    279       C  
ATOM   1350  C   PRO A 193      66.731  23.634  -8.845  1.00 66.46           C  
ANISOU 1350  C   PRO A 193    14211   3865   7174  -1099  -1592    363       C  
ATOM   1351  O   PRO A 193      67.584  22.789  -8.549  1.00 74.13           O  
ANISOU 1351  O   PRO A 193    14744   5217   8207  -1274  -1496    333       O  
ATOM   1352  CB  PRO A 193      64.795  22.647 -10.117  1.00 73.68           C  
ANISOU 1352  CB  PRO A 193    15015   4896   8085   -362  -1598    402       C  
ATOM   1353  CG  PRO A 193      64.254  23.809 -10.883  1.00 66.21           C  
ANISOU 1353  CG  PRO A 193    14394   3759   7004   -283  -1654    477       C  
ATOM   1354  CD  PRO A 193      63.627  24.722  -9.861  1.00 67.63           C  
ANISOU 1354  CD  PRO A 193    14693   3804   7199   -106  -1764    325       C  
ATOM   1355  N   GLN A 194      67.047  24.875  -9.207  1.00 79.92           N  
ANISOU 1355  N   GLN A 194    16290   5308   8767  -1353  -1616    448       N  
ATOM   1356  CA  GLN A 194      68.425  25.342  -9.177  1.00 88.19           C  
ANISOU 1356  CA  GLN A 194    17416   6323   9770  -1947  -1558    511       C  
ATOM   1357  C   GLN A 194      68.952  25.478  -7.757  1.00 85.80           C  
ANISOU 1357  C   GLN A 194    17012   6042   9547  -2121  -1628    332       C  
ATOM   1358  O   GLN A 194      70.171  25.464  -7.554  1.00 87.50           O  
ANISOU 1358  O   GLN A 194    17017   6473   9757  -2570  -1560    329       O  
ATOM   1359  CB  GLN A 194      68.531  26.685  -9.902  1.00 91.24           C  
ANISOU 1359  CB  GLN A 194    18199   6466  10001  -2141  -1559    636       C  
ATOM   1360  CG  GLN A 194      67.562  27.753  -9.391  1.00 92.39           C  
ANISOU 1360  CG  GLN A 194    18624   6359  10122  -1809  -1700    537       C  
ATOM   1361  CD  GLN A 194      66.175  27.655 -10.007  1.00101.13           C  
ANISOU 1361  CD  GLN A 194    19780   7443  11204  -1262  -1759    547       C  
ATOM   1362  OE1 GLN A 194      65.981  27.005 -11.034  1.00114.69           O  
ANISOU 1362  OE1 GLN A 194    21411   9280  12886  -1171  -1697    662       O  
ATOM   1363  NE2 GLN A 194      65.205  28.310  -9.380  1.00102.44           N  
ANISOU 1363  NE2 GLN A 194    20073   7472  11378   -907  -1881    417       N  
ATOM   1364  N   LYS A 195      68.062  25.606  -6.774  1.00 83.08           N  
ANISOU 1364  N   LYS A 195    16664   5648   9255  -1732  -1731    169       N  
ATOM   1365  CA  LYS A 195      68.487  25.856  -5.405  1.00 83.53           C  
ANISOU 1365  CA  LYS A 195    16673   5713   9352  -1874  -1808     -6       C  
ATOM   1366  C   LYS A 195      68.813  24.581  -4.636  1.00 69.48           C  
ANISOU 1366  C   LYS A 195    14411   4319   7668  -1816  -1787   -111       C  
ATOM   1367  O   LYS A 195      69.473  24.658  -3.596  1.00 84.78           O  
ANISOU 1367  O   LYS A 195    16224   6370   9617  -2020  -1839   -235       O  
ATOM   1368  CB  LYS A 195      67.409  26.650  -4.666  1.00 75.79           C  
ANISOU 1368  CB  LYS A 195    15877   4566   8353  -1490  -1904   -133       C  
ATOM   1369  N   ALA A 196      68.389  23.420  -5.126  1.00 66.23           N  
ANISOU 1369  N   ALA A 196    13658   4195   7310  -1519  -1701    -58       N  
ATOM   1370  CA  ALA A 196      68.622  22.174  -4.411  1.00 66.53           C  
ANISOU 1370  CA  ALA A 196    13197   4654   7429  -1392  -1668   -136       C  
ATOM   1371  C   ALA A 196      70.115  21.882  -4.304  1.00 77.52           C  
ANISOU 1371  C   ALA A 196    14258   6371   8824  -1800  -1616   -120       C  
ATOM   1372  O   ALA A 196      70.923  22.340  -5.115  1.00 92.22           O  
ANISOU 1372  O   ALA A 196    16170   8235  10634  -2162  -1547    -19       O  
ATOM   1373  CB  ALA A 196      67.910  21.019  -5.112  1.00 65.21           C  
ANISOU 1373  CB  ALA A 196    12779   4686   7314  -1037  -1582    -74       C  
ATOM   1374  N   ALA A 197      70.478  21.104  -3.280  1.00 70.81           N  
ANISOU 1374  N   ALA A 197    13062   5820   8022  -1738  -1653   -224       N  
ATOM   1375  CA  ALA A 197      71.888  20.812  -3.041  1.00 64.73           C  
ANISOU 1375  CA  ALA A 197    11940   5400   7255  -2075  -1637   -241       C  
ATOM   1376  C   ALA A 197      72.482  19.944  -4.141  1.00 64.02           C  
ANISOU 1376  C   ALA A 197    11500   5631   7192  -2108  -1493   -130       C  
ATOM   1377  O   ALA A 197      73.674  20.064  -4.447  1.00 66.29           O  
ANISOU 1377  O   ALA A 197    11579   6155   7455  -2472  -1440   -115       O  
ATOM   1378  CB  ALA A 197      72.068  20.135  -1.683  1.00 63.71           C  
ANISOU 1378  CB  ALA A 197    11546   5510   7151  -1938  -1736   -369       C  
ATOM   1379  N   LYS A 198      71.684  19.066  -4.739  1.00 61.19           N  
ANISOU 1379  N   LYS A 198    11060   5310   6879  -1742  -1425    -71       N  
ATOM   1380  CA  LYS A 198      72.173  18.176  -5.778  1.00 61.98           C  
ANISOU 1380  CA  LYS A 198    10844   5707   6999  -1726  -1289      9       C  
ATOM   1381  C   LYS A 198      71.314  18.308  -7.024  1.00 63.45           C  
ANISOU 1381  C   LYS A 198    11271   5688   7148  -1584  -1206    121       C  
ATOM   1382  O   LYS A 198      70.155  18.730  -6.968  1.00 62.98           O  
ANISOU 1382  O   LYS A 198    11537   5311   7080  -1361  -1268    123       O  
ATOM   1383  CB  LYS A 198      72.175  16.705  -5.331  1.00 61.17           C  
ANISOU 1383  CB  LYS A 198    10346   5911   6984  -1407  -1292    -41       C  
ATOM   1384  CG  LYS A 198      72.971  16.418  -4.077  1.00 76.69           C  
ANISOU 1384  CG  LYS A 198    12063   8106   8971  -1473  -1399   -143       C  
ATOM   1385  CD  LYS A 198      73.206  14.926  -3.897  1.00 69.14           C  
ANISOU 1385  CD  LYS A 198    10722   7464   8085  -1186  -1392   -159       C  
ATOM   1386  CE  LYS A 198      71.916  14.163  -3.663  1.00 67.78           C  
ANISOU 1386  CE  LYS A 198    10661   7136   7957   -787  -1401   -147       C  
ATOM   1387  NZ  LYS A 198      72.182  12.723  -3.377  1.00 62.37           N  
ANISOU 1387  NZ  LYS A 198     9662   6703   7332   -533  -1411   -157       N  
ATOM   1388  N   ARG A 199      71.903  17.943  -8.161  1.00 60.40           N  
ANISOU 1388  N   ARG A 199    10708   5514   6727  -1704  -1068    203       N  
ATOM   1389  CA  ARG A 199      71.122  17.654  -9.353  1.00 59.21           C  
ANISOU 1389  CA  ARG A 199    10675   5283   6540  -1495   -989    294       C  
ATOM   1390  C   ARG A 199      70.754  16.179  -9.290  1.00 57.45           C  
ANISOU 1390  C   ARG A 199    10119   5295   6415  -1122   -966    235       C  
ATOM   1391  O   ARG A 199      71.651  15.326  -9.371  1.00 67.31           O  
ANISOU 1391  O   ARG A 199    10987   6888   7699  -1154   -897    200       O  
ATOM   1392  CB  ARG A 199      71.904  17.969 -10.621  1.00 70.68           C  
ANISOU 1392  CB  ARG A 199    12123   6855   7875  -1809   -841    404       C  
ATOM   1393  CG  ARG A 199      71.068  17.872 -11.882  1.00 78.71           C  
ANISOU 1393  CG  ARG A 199    13342   7753   8812  -1621   -780    508       C  
ATOM   1394  CD  ARG A 199      71.638  18.728 -13.001  1.00101.54           C  
ANISOU 1394  CD  ARG A 199    16454  10598  11530  -1998   -669    653       C  
ATOM   1395  NE  ARG A 199      70.817  18.655 -14.207  1.00111.01           N  
ANISOU 1395  NE  ARG A 199    17870  11686  12623  -1802   -632    757       N  
ATOM   1396  CZ  ARG A 199      70.956  17.729 -15.151  1.00113.60           C  
ANISOU 1396  CZ  ARG A 199    17943  12309  12909  -1696   -503    762       C  
ATOM   1397  NH1 ARG A 199      71.888  16.792 -15.034  1.00117.45           N  
ANISOU 1397  NH1 ARG A 199    17953  13209  13463  -1743   -397    666       N  
ATOM   1398  NH2 ARG A 199      70.163  17.735 -16.215  1.00112.18           N  
ANISOU 1398  NH2 ARG A 199    17992  12018  12614  -1521   -494    851       N  
ATOM   1399  N   PRO A 200      69.484  15.832  -9.101  1.00 56.38           N  
ANISOU 1399  N   PRO A 200    10107   4990   6325   -770  -1026    209       N  
ATOM   1400  CA  PRO A 200      69.134  14.431  -8.838  1.00 51.35           C  
ANISOU 1400  CA  PRO A 200     9186   4541   5785   -460  -1015    146       C  
ATOM   1401  C   PRO A 200      69.386  13.546 -10.047  1.00 58.74           C  
ANISOU 1401  C   PRO A 200     9920   5690   6710   -393   -891    177       C  
ATOM   1402  O   PRO A 200      69.057  13.898 -11.182  1.00 59.39           O  
ANISOU 1402  O   PRO A 200    10167   5693   6706   -417   -831    249       O  
ATOM   1403  CB  PRO A 200      67.642  14.499  -8.494  1.00 49.63           C  
ANISOU 1403  CB  PRO A 200     9189   4079   5590   -170  -1092    112       C  
ATOM   1404  CG  PRO A 200      67.159  15.741  -9.177  1.00 56.15           C  
ANISOU 1404  CG  PRO A 200    10391   4625   6319   -247  -1116    180       C  
ATOM   1405  CD  PRO A 200      68.303  16.711  -9.101  1.00 53.84           C  
ANISOU 1405  CD  PRO A 200    10191   4301   5963   -639  -1110    226       C  
ATOM   1406  N   THR A 201      69.974  12.382  -9.787  1.00 56.48           N  
ANISOU 1406  N   THR A 201     9290   5670   6500   -290   -862    118       N  
ATOM   1407  CA  THR A 201      70.213  11.411 -10.840  1.00 50.12           C  
ANISOU 1407  CA  THR A 201     8280   5070   5692   -180   -749    111       C  
ATOM   1408  C   THR A 201      68.888  10.836 -11.337  1.00 51.82           C  
ANISOU 1408  C   THR A 201     8623   5140   5926    105   -753    103       C  
ATOM   1409  O   THR A 201      67.827  11.030 -10.736  1.00 52.04           O  
ANISOU 1409  O   THR A 201     8830   4959   5986    241   -840     90       O  
ATOM   1410  CB  THR A 201      71.118  10.288 -10.340  1.00 50.21           C  
ANISOU 1410  CB  THR A 201     7924   5365   5788    -85   -746     33       C  
ATOM   1411  OG1 THR A 201      70.412   9.505  -9.370  1.00 48.24           O  
ANISOU 1411  OG1 THR A 201     7678   5016   5633    175   -843     -8       O  
ATOM   1412  CG2 THR A 201      72.364  10.864  -9.701  1.00 52.42           C  
ANISOU 1412  CG2 THR A 201     8043   5822   6052   -355   -774     17       C  
ATOM   1413  N   ALA A 202      68.960  10.122 -12.461  1.00 56.62           N  
ANISOU 1413  N   ALA A 202     9122   5889   6503    188   -653     92       N  
ATOM   1414  CA  ALA A 202      67.752   9.537 -13.033  1.00 47.71           C  
ANISOU 1414  CA  ALA A 202     8091   4656   5382    430   -660     66       C  
ATOM   1415  C   ALA A 202      67.183   8.451 -12.129  1.00 44.69           C  
ANISOU 1415  C   ALA A 202     7605   4245   5131    660   -721    -13       C  
ATOM   1416  O   ALA A 202      65.963   8.369 -11.942  1.00 54.82           O  
ANISOU 1416  O   ALA A 202     9020   5372   6437    803   -775    -35       O  
ATOM   1417  CB  ALA A 202      68.044   8.985 -14.428  1.00 52.68           C  
ANISOU 1417  CB  ALA A 202     8626   5458   5932    453   -541     52       C  
ATOM   1418  N   ALA A 203      68.051   7.613 -11.557  1.00 45.15           N  
ANISOU 1418  N   ALA A 203     7428   4461   5264    697   -716    -56       N  
ATOM   1419  CA  ALA A 203      67.587   6.562 -10.655  1.00 50.72           C  
ANISOU 1419  CA  ALA A 203     8082   5116   6075    893   -776   -105       C  
ATOM   1420  C   ALA A 203      66.859   7.146  -9.450  1.00 55.59           C  
ANISOU 1420  C   ALA A 203     8854   5560   6706    878   -871    -85       C  
ATOM   1421  O   ALA A 203      65.863   6.581  -8.983  1.00 52.20           O  
ANISOU 1421  O   ALA A 203     8487   5026   6319   1015   -899   -114       O  
ATOM   1422  CB  ALA A 203      68.764   5.700 -10.201  1.00 44.55           C  
ANISOU 1422  CB  ALA A 203     7054   4522   5353    949   -783   -140       C  
ATOM   1423  N   PHE A 204      67.341   8.280  -8.935  1.00 49.43           N  
ANISOU 1423  N   PHE A 204     8140   4758   5882    695   -913    -48       N  
ATOM   1424  CA  PHE A 204      66.663   8.934  -7.821  1.00 43.14           C  
ANISOU 1424  CA  PHE A 204     7510   3801   5080    687   -999    -53       C  
ATOM   1425  C   PHE A 204      65.267   9.389  -8.226  1.00 47.71           C  
ANISOU 1425  C   PHE A 204     8296   4202   5631    784  -1002    -66       C  
ATOM   1426  O   PHE A 204      64.287   9.125  -7.518  1.00 47.10           O  
ANISOU 1426  O   PHE A 204     8267   4050   5577    911  -1034   -111       O  
ATOM   1427  CB  PHE A 204      67.495  10.118  -7.325  1.00 44.68           C  
ANISOU 1427  CB  PHE A 204     7762   3990   5224    452  -1046    -30       C  
ATOM   1428  CG  PHE A 204      66.875  10.863  -6.175  1.00 52.57           C  
ANISOU 1428  CG  PHE A 204     8948   4823   6202    445  -1136    -59       C  
ATOM   1429  CD1 PHE A 204      67.168  10.513  -4.868  1.00 44.57           C  
ANISOU 1429  CD1 PHE A 204     7856   3874   5203    461  -1207    -91       C  
ATOM   1430  CD2 PHE A 204      66.010  11.923  -6.403  1.00 45.03           C  
ANISOU 1430  CD2 PHE A 204     8259   3654   5197    443  -1158    -63       C  
ATOM   1431  CE1 PHE A 204      66.607  11.203  -3.811  1.00 48.09           C  
ANISOU 1431  CE1 PHE A 204     8476   4189   5606    455  -1279   -137       C  
ATOM   1432  CE2 PHE A 204      65.444  12.613  -5.351  1.00 44.96           C  
ANISOU 1432  CE2 PHE A 204     8419   3501   5162    465  -1236   -119       C  
ATOM   1433  CZ  PHE A 204      65.744  12.257  -4.055  1.00 49.00           C  
ANISOU 1433  CZ  PHE A 204     8841   4095   5681    460  -1287   -162       C  
ATOM   1434  N   ILE A 205      65.159  10.079  -9.366  1.00 43.41           N  
ANISOU 1434  N   ILE A 205     7868   3606   5018    729   -971    -28       N  
ATOM   1435  CA  ILE A 205      63.865  10.579  -9.822  1.00 46.94           C  
ANISOU 1435  CA  ILE A 205     8510   3901   5426    855  -1002    -43       C  
ATOM   1436  C   ILE A 205      62.919   9.419 -10.102  1.00 46.58           C  
ANISOU 1436  C   ILE A 205     8354   3913   5431   1053   -977   -109       C  
ATOM   1437  O   ILE A 205      61.745   9.440  -9.711  1.00 64.31           O  
ANISOU 1437  O   ILE A 205    10654   6091   7688   1186  -1016   -171       O  
ATOM   1438  CB  ILE A 205      64.043  11.473 -11.064  1.00 56.46           C  
ANISOU 1438  CB  ILE A 205     9884   5043   6523    759   -985     34       C  
ATOM   1439  CG1 ILE A 205      64.881  12.707 -10.715  1.00 51.45           C  
ANISOU 1439  CG1 ILE A 205     9408   4307   5834    516  -1012     98       C  
ATOM   1440  CG2 ILE A 205      62.688  11.866 -11.639  1.00 44.03           C  
ANISOU 1440  CG2 ILE A 205     8493   3338   4899    948  -1043     14       C  
ATOM   1441  CD1 ILE A 205      65.302  13.514 -11.925  1.00 53.38           C  
ANISOU 1441  CD1 ILE A 205     9829   4501   5953    349   -972    203       C  
ATOM   1442  N   SER A 206      63.423   8.385 -10.777  1.00 41.15           N  
ANISOU 1442  N   SER A 206     7502   3362   4771   1067   -907   -114       N  
ATOM   1443  CA  SER A 206      62.610   7.206 -11.055  1.00 45.73           C  
ANISOU 1443  CA  SER A 206     7994   3979   5401   1218   -883   -187       C  
ATOM   1444  C   SER A 206      62.119   6.554  -9.768  1.00 44.64           C  
ANISOU 1444  C   SER A 206     7809   3811   5340   1273   -907   -228       C  
ATOM   1445  O   SER A 206      60.947   6.173  -9.661  1.00 46.72           O  
ANISOU 1445  O   SER A 206     8083   4048   5620   1361   -912   -293       O  
ATOM   1446  CB  SER A 206      63.415   6.210 -11.887  1.00 43.57           C  
ANISOU 1446  CB  SER A 206     7573   3837   5143   1226   -808   -201       C  
ATOM   1447  OG  SER A 206      62.748   4.967 -11.950  1.00 61.66           O  
ANISOU 1447  OG  SER A 206     9799   6129   7498   1347   -794   -280       O  
ATOM   1448  N   GLN A 207      62.996   6.443  -8.770  1.00 45.19           N  
ANISOU 1448  N   GLN A 207     7827   3905   5440   1209   -924   -193       N  
ATOM   1449  CA  GLN A 207      62.594   5.881  -7.487  1.00 42.75           C  
ANISOU 1449  CA  GLN A 207     7509   3567   5167   1245   -948   -209       C  
ATOM   1450  C   GLN A 207      61.508   6.725  -6.827  1.00 43.45           C  
ANISOU 1450  C   GLN A 207     7717   3578   5213   1259   -980   -249       C  
ATOM   1451  O   GLN A 207      60.554   6.179  -6.262  1.00 45.64           O  
ANISOU 1451  O   GLN A 207     7987   3854   5501   1311   -961   -298       O  
ATOM   1452  CB  GLN A 207      63.821   5.752  -6.584  1.00 52.04           C  
ANISOU 1452  CB  GLN A 207     8618   4801   6354   1184   -987   -159       C  
ATOM   1453  CG  GLN A 207      63.583   5.077  -5.246  1.00 74.54           C  
ANISOU 1453  CG  GLN A 207    11481   7629   9210   1218  -1020   -150       C  
ATOM   1454  CD  GLN A 207      64.863   4.961  -4.437  1.00 82.68           C  
ANISOU 1454  CD  GLN A 207    12438   8742  10234   1185  -1089   -101       C  
ATOM   1455  OE1 GLN A 207      65.687   4.079  -4.683  1.00 85.06           O  
ANISOU 1455  OE1 GLN A 207    12624   9114  10579   1254  -1096    -83       O  
ATOM   1456  NE2 GLN A 207      65.046   5.869  -3.483  1.00 78.31           N  
ANISOU 1456  NE2 GLN A 207    11944   8189   9619   1094  -1151    -97       N  
ATOM   1457  N   GLN A 208      61.619   8.057  -6.906  1.00 39.57           N  
ANISOU 1457  N   GLN A 208     7344   3024   4666   1211  -1023   -239       N  
ATOM   1458  CA  GLN A 208      60.629   8.917  -6.262  1.00 39.83           C  
ANISOU 1458  CA  GLN A 208     7502   2977   4656   1268  -1063   -302       C  
ATOM   1459  C   GLN A 208      59.276   8.840  -6.958  1.00 48.99           C  
ANISOU 1459  C   GLN A 208     8662   4141   5810   1412  -1052   -377       C  
ATOM   1460  O   GLN A 208      58.235   8.771  -6.294  1.00 54.43           O  
ANISOU 1460  O   GLN A 208     9331   4859   6491   1492  -1046   -464       O  
ATOM   1461  CB  GLN A 208      61.125  10.363  -6.219  1.00 40.90           C  
ANISOU 1461  CB  GLN A 208     7810   2996   4734   1187  -1126   -277       C  
ATOM   1462  CG  GLN A 208      62.268  10.575  -5.251  1.00 41.41           C  
ANISOU 1462  CG  GLN A 208     7866   3078   4791   1033  -1157   -243       C  
ATOM   1463  CD  GLN A 208      62.082   9.775  -3.979  1.00 48.69           C  
ANISOU 1463  CD  GLN A 208     8700   4077   5721   1068  -1154   -274       C  
ATOM   1464  OE1 GLN A 208      61.101   9.950  -3.254  1.00 62.96           O  
ANISOU 1464  OE1 GLN A 208    10567   5859   7494   1151  -1155   -350       O  
ATOM   1465  NE2 GLN A 208      63.014   8.871  -3.712  1.00 50.99           N  
ANISOU 1465  NE2 GLN A 208     8853   4476   6046   1016  -1149   -218       N  
ATOM   1466  N   LEU A 209      59.266   8.860  -8.294  1.00 55.79           N  
ANISOU 1466  N   LEU A 209     9531   5006   6661   1442  -1050   -356       N  
ATOM   1467  CA  LEU A 209      58.005   8.770  -9.022  1.00 53.84           C  
ANISOU 1467  CA  LEU A 209     9266   4795   6397   1587  -1064   -437       C  
ATOM   1468  C   LEU A 209      57.320   7.426  -8.801  1.00 44.14           C  
ANISOU 1468  C   LEU A 209     7865   3680   5228   1602  -1002   -511       C  
ATOM   1469  O   LEU A 209      56.087   7.360  -8.760  1.00 58.60           O  
ANISOU 1469  O   LEU A 209     9637   5578   7050   1694  -1009   -616       O  
ATOM   1470  CB  LEU A 209      58.241   9.019 -10.512  1.00 54.94           C  
ANISOU 1470  CB  LEU A 209     9464   4925   6483   1603  -1081   -388       C  
ATOM   1471  CG  LEU A 209      58.760  10.415 -10.860  1.00 49.68           C  
ANISOU 1471  CG  LEU A 209     9022   4119   5734   1565  -1141   -302       C  
ATOM   1472  CD1 LEU A 209      59.068  10.519 -12.343  1.00 53.25           C  
ANISOU 1472  CD1 LEU A 209     9540   4588   6106   1548  -1135   -232       C  
ATOM   1473  CD2 LEU A 209      57.749  11.457 -10.459  1.00 46.51           C  
ANISOU 1473  CD2 LEU A 209     8771   3609   5292   1722  -1236   -366       C  
ATOM   1474  N   GLN A 210      58.094   6.349  -8.649  1.00 42.73           N  
ANISOU 1474  N   GLN A 210     7606   3524   5105   1511   -946   -464       N  
ATOM   1475  CA  GLN A 210      57.508   5.069  -8.262  1.00 45.44           C  
ANISOU 1475  CA  GLN A 210     7847   3918   5498   1490   -890   -517       C  
ATOM   1476  C   GLN A 210      56.889   5.152  -6.872  1.00 48.73           C  
ANISOU 1476  C   GLN A 210     8264   4352   5898   1466   -872   -549       C  
ATOM   1477  O   GLN A 210      55.749   4.724  -6.657  1.00 56.33           O  
ANISOU 1477  O   GLN A 210     9153   5391   6857   1467   -832   -640       O  
ATOM   1478  CB  GLN A 210      58.570   3.971  -8.311  1.00 45.71           C  
ANISOU 1478  CB  GLN A 210     7849   3931   5590   1433   -854   -452       C  
ATOM   1479  CG  GLN A 210      58.751   3.348  -9.675  1.00 54.85           C  
ANISOU 1479  CG  GLN A 210     8964   5112   6764   1465   -834   -482       C  
ATOM   1480  CD  GLN A 210      57.502   2.637 -10.152  1.00 65.12           C  
ANISOU 1480  CD  GLN A 210    10216   6449   8077   1478   -814   -594       C  
ATOM   1481  OE1 GLN A 210      56.861   3.056 -11.118  1.00 70.16           O  
ANISOU 1481  OE1 GLN A 210    10840   7148   8670   1535   -844   -658       O  
ATOM   1482  NE2 GLN A 210      57.149   1.551  -9.476  1.00 68.50           N  
ANISOU 1482  NE2 GLN A 210    10628   6843   8555   1412   -772   -616       N  
ATOM   1483  N   SER A 211      57.637   5.702  -5.913  1.00 43.90           N  
ANISOU 1483  N   SER A 211     7725   3694   5261   1426   -897   -486       N  
ATOM   1484  CA  SER A 211      57.129   5.846  -4.554  1.00 43.60           C  
ANISOU 1484  CA  SER A 211     7706   3685   5176   1402   -877   -519       C  
ATOM   1485  C   SER A 211      55.858   6.687  -4.532  1.00 40.46           C  
ANISOU 1485  C   SER A 211     7296   3347   4730   1505   -882   -649       C  
ATOM   1486  O   SER A 211      54.890   6.354  -3.841  1.00 49.57           O  
ANISOU 1486  O   SER A 211     8376   4606   5852   1495   -820   -732       O  
ATOM   1487  CB  SER A 211      58.207   6.465  -3.658  1.00 43.61           C  
ANISOU 1487  CB  SER A 211     7796   3633   5139   1349   -928   -447       C  
ATOM   1488  OG  SER A 211      57.648   7.017  -2.477  1.00 60.25           O  
ANISOU 1488  OG  SER A 211     9954   5769   7168   1354   -924   -509       O  
ATOM   1489  N   LEU A 212      55.843   7.781  -5.295  1.00 40.56           N  
ANISOU 1489  N   LEU A 212     7384   3301   4727   1610   -957   -669       N  
ATOM   1490  CA  LEU A 212      54.674   8.652  -5.318  1.00 44.95           C  
ANISOU 1490  CA  LEU A 212     7943   3900   5236   1771   -992   -800       C  
ATOM   1491  C   LEU A 212      53.453   7.917  -5.861  1.00 53.28           C  
ANISOU 1491  C   LEU A 212     8816   5119   6308   1824   -951   -909       C  
ATOM   1492  O   LEU A 212      52.368   7.968  -5.272  1.00 62.64           O  
ANISOU 1492  O   LEU A 212     9892   6447   7459   1884   -914  -1043       O  
ATOM   1493  CB  LEU A 212      54.972   9.896  -6.152  1.00 47.85           C  
ANISOU 1493  CB  LEU A 212     8480   4125   5574   1878  -1099   -772       C  
ATOM   1494  CG  LEU A 212      53.780  10.812  -6.419  1.00 50.95           C  
ANISOU 1494  CG  LEU A 212     8903   4537   5918   2112  -1172   -904       C  
ATOM   1495  CD1 LEU A 212      53.348  11.523  -5.144  1.00 50.73           C  
ANISOU 1495  CD1 LEU A 212     8924   4509   5843   2190  -1173  -1015       C  
ATOM   1496  CD2 LEU A 212      54.096  11.805  -7.533  1.00 52.75           C  
ANISOU 1496  CD2 LEU A 212     9337   4596   6108   2207  -1286   -835       C  
ATOM   1497  N   GLU A 213      53.618   7.219  -6.985  1.00 47.81           N  
ANISOU 1497  N   GLU A 213     8074   4433   5659   1792   -953   -872       N  
ATOM   1498  CA  GLU A 213      52.523   6.433  -7.540  1.00 46.39           C  
ANISOU 1498  CA  GLU A 213     7718   4413   5496   1802   -923   -985       C  
ATOM   1499  C   GLU A 213      52.047   5.384  -6.545  1.00 48.53           C  
ANISOU 1499  C   GLU A 213     7871   4785   5782   1643   -805  -1026       C  
ATOM   1500  O   GLU A 213      50.841   5.201  -6.347  1.00 54.07           O  
ANISOU 1500  O   GLU A 213     8411   5672   6462   1648   -763  -1168       O  
ATOM   1501  CB  GLU A 213      52.964   5.773  -8.846  1.00 47.28           C  
ANISOU 1501  CB  GLU A 213     7829   4494   5642   1769   -941   -938       C  
ATOM   1502  CG  GLU A 213      51.924   4.852  -9.454  1.00 65.75           C  
ANISOU 1502  CG  GLU A 213     9995   6989   7998   1739   -918  -1065       C  
ATOM   1503  CD  GLU A 213      52.364   4.254 -10.778  1.00 55.98           C  
ANISOU 1503  CD  GLU A 213     8776   5720   6773   1722   -943  -1041       C  
ATOM   1504  OE1 GLU A 213      52.002   3.089 -11.048  1.00 55.99           O  
ANISOU 1504  OE1 GLU A 213     8684   5775   6814   1607   -893  -1109       O  
ATOM   1505  OE2 GLU A 213      53.067   4.948 -11.545  1.00 52.61           O  
ANISOU 1505  OE2 GLU A 213     8471   5213   6305   1808  -1006   -959       O  
ATOM   1506  N   SER A 214      52.989   4.696  -5.897  1.00 42.59           N  
ANISOU 1506  N   SER A 214     7201   3926   5055   1496   -753   -902       N  
ATOM   1507  CA  SER A 214      52.627   3.663  -4.934  1.00 41.70           C  
ANISOU 1507  CA  SER A 214     7042   3868   4935   1326   -645   -903       C  
ATOM   1508  C   SER A 214      51.810   4.237  -3.783  1.00 53.11           C  
ANISOU 1508  C   SER A 214     8433   5452   6294   1336   -591   -993       C  
ATOM   1509  O   SER A 214      50.850   3.609  -3.321  1.00 62.41           O  
ANISOU 1509  O   SER A 214     9488   6785   7439   1217   -489  -1076       O  
ATOM   1510  CB  SER A 214      53.890   2.981  -4.412  1.00 49.88           C  
ANISOU 1510  CB  SER A 214     8213   4744   5994   1226   -636   -739       C  
ATOM   1511  OG  SER A 214      53.576   1.765  -3.762  1.00 70.61           O  
ANISOU 1511  OG  SER A 214    10846   7370   8613   1056   -546   -712       O  
ATOM   1512  N   LYS A 215      52.169   5.434  -3.314  1.00 46.47           N  
ANISOU 1512  N   LYS A 215     7684   4566   5405   1462   -652   -991       N  
ATOM   1513  CA  LYS A 215      51.467   6.014  -2.175  1.00 48.27           C  
ANISOU 1513  CA  LYS A 215     7878   4927   5538   1495   -599  -1097       C  
ATOM   1514  C   LYS A 215      50.095   6.544  -2.566  1.00 59.87           C  
ANISOU 1514  C   LYS A 215     9165   6598   6984   1652   -599  -1301       C  
ATOM   1515  O   LYS A 215      49.192   6.596  -1.724  1.00 53.70           O  
ANISOU 1515  O   LYS A 215     8259   6021   6124   1642   -506  -1431       O  
ATOM   1516  CB  LYS A 215      52.309   7.122  -1.542  1.00 49.12           C  
ANISOU 1516  CB  LYS A 215     8166   4901   5598   1578   -675  -1053       C  
ATOM   1517  CG  LYS A 215      53.545   6.605  -0.827  1.00 49.50           C  
ANISOU 1517  CG  LYS A 215     8344   4829   5636   1424   -674   -885       C  
ATOM   1518  CD  LYS A 215      54.539   7.719  -0.557  1.00 55.36           C  
ANISOU 1518  CD  LYS A 215     9250   5429   6355   1482   -779   -843       C  
ATOM   1519  CE  LYS A 215      55.778   7.179   0.140  1.00 64.64           C  
ANISOU 1519  CE  LYS A 215    10512   6534   7516   1343   -799   -692       C  
ATOM   1520  NZ  LYS A 215      56.882   8.179   0.194  1.00 67.80           N  
ANISOU 1520  NZ  LYS A 215    11039   6810   7912   1353   -911   -651       N  
ATOM   1521  N   LEU A 216      49.913   6.930  -3.832  1.00 52.76           N  
ANISOU 1521  N   LEU A 216     8238   5673   6137   1806   -703  -1337       N  
ATOM   1522  CA  LEU A 216      48.611   7.428  -4.266  1.00 47.02           C  
ANISOU 1522  CA  LEU A 216     7324   5157   5383   1998   -737  -1536       C  
ATOM   1523  C   LEU A 216      47.599   6.298  -4.416  1.00 59.91           C  
ANISOU 1523  C   LEU A 216     8693   7042   7028   1840   -633  -1643       C  
ATOM   1524  O   LEU A 216      46.405   6.500  -4.162  1.00 61.64           O  
ANISOU 1524  O   LEU A 216     8685   7537   7198   1919   -593  -1839       O  
ATOM   1525  CB  LEU A 216      48.749   8.200  -5.580  1.00 50.21           C  
ANISOU 1525  CB  LEU A 216     7816   5448   5812   2219   -902  -1524       C  
ATOM   1526  CG  LEU A 216      49.473   9.547  -5.507  1.00 54.77           C  
ANISOU 1526  CG  LEU A 216     8660   5789   6360   2389  -1015  -1458       C  
ATOM   1527  CD1 LEU A 216      49.756  10.081  -6.900  1.00 46.54           C  
ANISOU 1527  CD1 LEU A 216     7748   4608   5326   2528  -1159  -1390       C  
ATOM   1528  CD2 LEU A 216      48.670  10.562  -4.700  1.00 59.57           C  
ANISOU 1528  CD2 LEU A 216     9253   6485   6898   2611  -1037  -1632       C  
ATOM   1529  N   THR A 217      48.050   5.107  -4.814  1.00 49.67           N  
ANISOU 1529  N   THR A 217     7419   5663   5793   1612   -586  -1533       N  
ATOM   1530  CA  THR A 217      47.132   3.981  -4.954  1.00 58.64           C  
ANISOU 1530  CA  THR A 217     8342   7000   6940   1407   -486  -1632       C  
ATOM   1531  C   THR A 217      46.745   3.382  -3.612  1.00 61.40           C  
ANISOU 1531  C   THR A 217     8637   7470   7222   1171   -311  -1642       C  
ATOM   1532  O   THR A 217      45.733   2.679  -3.528  1.00 76.19           O  
ANISOU 1532  O   THR A 217    10298   9577   9075    989   -205  -1765       O  
ATOM   1533  CB  THR A 217      47.746   2.883  -5.826  1.00 61.41           C  
ANISOU 1533  CB  THR A 217     8779   7182   7373   1247   -500  -1524       C  
ATOM   1534  OG1 THR A 217      48.780   2.213  -5.093  1.00 63.77           O  
ANISOU 1534  OG1 THR A 217     9283   7261   7686   1078   -434  -1339       O  
ATOM   1535  CG2 THR A 217      48.332   3.472  -7.098  1.00 54.80           C  
ANISOU 1535  CG2 THR A 217     8035   6214   6571   1456   -654  -1482       C  
ATOM   1536  N   SER A 218      47.528   3.634  -2.568  1.00 58.35           N  
ANISOU 1536  N   SER A 218     8441   6944   6786   1148   -277  -1516       N  
ATOM   1537  CA  SER A 218      47.313   3.010  -1.273  1.00 65.17           C  
ANISOU 1537  CA  SER A 218     9313   7893   7554    908   -113  -1485       C  
ATOM   1538  C   SER A 218      46.854   3.984  -0.195  1.00 71.17           C  
ANISOU 1538  C   SER A 218    10017   8836   8189   1027    -59  -1600       C  
ATOM   1539  O   SER A 218      46.563   3.546   0.923  1.00 78.60           O  
ANISOU 1539  O   SER A 218    10951   9900   9014    829     93  -1593       O  
ATOM   1540  CB  SER A 218      48.596   2.305  -0.817  1.00 71.85           C  
ANISOU 1540  CB  SER A 218    10439   8449   8413    764   -116  -1242       C  
ATOM   1541  OG  SER A 218      49.678   3.219  -0.763  1.00 84.96           O  
ANISOU 1541  OG  SER A 218    12269   9927  10087    960   -241  -1152       O  
ATOM   1542  N   VAL A 219      46.774   5.283  -0.492  1.00 57.27           N  
ANISOU 1542  N   VAL A 219     8241   7087   6434   1345   -178  -1709       N  
ATOM   1543  CA  VAL A 219      46.364   6.252   0.519  1.00 57.42           C  
ANISOU 1543  CA  VAL A 219     8231   7253   6332   1494   -137  -1846       C  
ATOM   1544  C   VAL A 219      44.894   6.037   0.858  1.00 68.35           C  
ANISOU 1544  C   VAL A 219     9282   9052   7636   1446     11  -2076       C  
ATOM   1545  O   VAL A 219      44.040   5.909  -0.029  1.00 65.57           O  
ANISOU 1545  O   VAL A 219     8686   8886   7342   1509    -17  -2216       O  
ATOM   1546  CB  VAL A 219      46.645   7.690   0.046  1.00 60.54           C  
ANISOU 1546  CB  VAL A 219     8739   7506   6758   1854   -318  -1907       C  
ATOM   1547  CG1 VAL A 219      45.877   8.020  -1.230  1.00 57.54           C  
ANISOU 1547  CG1 VAL A 219     8187   7225   6452   2074   -429  -2039       C  
ATOM   1548  CG2 VAL A 219      46.336   8.698   1.152  1.00 63.00           C  
ANISOU 1548  CG2 VAL A 219     9077   7919   6943   2020   -286  -2057       C  
ATOM   1549  N   SER A 220      44.594   5.972   2.153  1.00 71.09           N  
ANISOU 1549  N   SER A 220     9603   9575   7833   1320    174  -2125       N  
ATOM   1550  CA  SER A 220      43.242   5.713   2.623  1.00 72.81           C  
ANISOU 1550  CA  SER A 220     9485  10233   7945   1220    358  -2344       C  
ATOM   1551  C   SER A 220      42.530   7.038   2.860  1.00 71.08           C  
ANISOU 1551  C   SER A 220     9108  10237   7661   1603    319  -2616       C  
ATOM   1552  O   SER A 220      43.015   7.884   3.619  1.00 90.24           O  
ANISOU 1552  O   SER A 220    11731  12549  10008   1767    288  -2622       O  
ATOM   1553  CB  SER A 220      43.262   4.874   3.901  1.00 85.29           C  
ANISOU 1553  CB  SER A 220    11131  11910   9365    852    578  -2247       C  
ATOM   1554  OG  SER A 220      43.788   5.614   4.989  1.00 86.85           O  
ANISOU 1554  OG  SER A 220    11524  12044   9429    963    585  -2231       O  
ATOM   1555  N   PHE A 221      41.383   7.214   2.211  1.00 70.95           N  
ANISOU 1555  N   PHE A 221     8742  10541   7676   1759    307  -2854       N  
ATOM   1556  CA  PHE A 221      40.584   8.417   2.375  1.00 74.46           C  
ANISOU 1556  CA  PHE A 221     9005  11228   8060   2172    259  -3143       C  
ATOM   1557  C   PHE A 221      39.115   8.038   2.270  1.00 83.00           C  
ANISOU 1557  C   PHE A 221     9583  12856   9095   2128    390  -3417       C  
ATOM   1558  O   PHE A 221      38.764   6.934   1.847  1.00 80.43           O  
ANISOU 1558  O   PHE A 221     9080  12668   8812   1789    477  -3374       O  
ATOM   1559  CB  PHE A 221      40.964   9.496   1.352  1.00 72.66           C  
ANISOU 1559  CB  PHE A 221     8950  10710   7949   2605    -23  -3144       C  
ATOM   1560  CG  PHE A 221      40.813   9.068  -0.081  1.00 64.85           C  
ANISOU 1560  CG  PHE A 221     7860   9685   7096   2614   -161  -3096       C  
ATOM   1561  CD1 PHE A 221      41.780   8.283  -0.690  1.00 69.44           C  
ANISOU 1561  CD1 PHE A 221     8663   9944   7776   2356   -203  -2822       C  
ATOM   1562  CD2 PHE A 221      39.719   9.469  -0.828  1.00 67.31           C  
ANISOU 1562  CD2 PHE A 221     7855  10296   7425   2909   -260  -3340       C  
ATOM   1563  CE1 PHE A 221      41.650   7.892  -2.008  1.00 67.61           C  
ANISOU 1563  CE1 PHE A 221     8353   9688   7649   2367   -325  -2795       C  
ATOM   1564  CE2 PHE A 221      39.585   9.083  -2.150  1.00 76.20           C  
ANISOU 1564  CE2 PHE A 221     8899  11400   8651   2918   -400  -3302       C  
ATOM   1565  CZ  PHE A 221      40.550   8.294  -2.740  1.00 73.19           C  
ANISOU 1565  CZ  PHE A 221     8756  10694   8359   2638   -426  -3031       C  
ATOM   1566  N   LEU A 222      38.252   8.973   2.661  1.00 92.41           N  
ANISOU 1566  N   LEU A 222    10542  14370  10198   2476    402  -3720       N  
ATOM   1567  CA  LEU A 222      36.830   8.693   2.808  1.00 95.77           C  
ANISOU 1567  CA  LEU A 222    10437  15406  10545   2438    561  -4024       C  
ATOM   1568  C   LEU A 222      36.011   9.046   1.573  1.00 95.65           C  
ANISOU 1568  C   LEU A 222    10111  15595  10637   2774    364  -4226       C  
ATOM   1569  O   LEU A 222      35.066   8.325   1.240  1.00107.99           O  
ANISOU 1569  O   LEU A 222    11250  17584  12199   2572    458  -4376       O  
ATOM   1570  CB  LEU A 222      36.276   9.438   4.026  1.00 96.71           C  
ANISOU 1570  CB  LEU A 222    10420  15846  10480   2632    713  -4280       C  
ATOM   1571  CG  LEU A 222      34.969   8.880   4.581  1.00 94.61           C  
ANISOU 1571  CG  LEU A 222     9617  16256  10074   2410    989  -4551       C  
ATOM   1572  CD1 LEU A 222      35.053   7.369   4.634  1.00 87.77           C  
ANISOU 1572  CD1 LEU A 222     8725  15422   9202   1749   1184  -4335       C  
ATOM   1573  CD2 LEU A 222      34.689   9.447   5.961  1.00 97.43           C  
ANISOU 1573  CD2 LEU A 222     9931  16875  10213   2502   1188  -4740       C  
ATOM   1574  N   GLY A 223      36.342  10.131   0.882  1.00 86.45           N  
ANISOU 1574  N   GLY A 223     9156  14140   9549   3267     87  -4233       N  
ATOM   1575  CA  GLY A 223      35.625  10.495  -0.320  1.00 97.35           C  
ANISOU 1575  CA  GLY A 223    10295  15683  11009   3618   -134  -4397       C  
ATOM   1576  C   GLY A 223      35.898   9.531  -1.467  1.00105.08           C  
ANISOU 1576  C   GLY A 223    11287  16528  12109   3327   -215  -4205       C  
ATOM   1577  O   GLY A 223      36.681   8.585  -1.367  1.00104.95           O  
ANISOU 1577  O   GLY A 223    11486  16260  12131   2876   -108  -3943       O  
ATOM   1578  N   ASP A 224      35.218   9.781  -2.586  1.00104.19           N  
ANISOU 1578  N   ASP A 224    10943  16598  12048   3618   -422  -4355       N  
ATOM   1579  CA  ASP A 224      35.506   9.039  -3.808  1.00 95.59           C  
ANISOU 1579  CA  ASP A 224     9905  15354  11059   3424   -545  -4194       C  
ATOM   1580  C   ASP A 224      36.736   9.569  -4.532  1.00 86.49           C  
ANISOU 1580  C   ASP A 224     9285  13597   9980   3600   -761  -3907       C  
ATOM   1581  O   ASP A 224      37.358   8.828  -5.298  1.00 77.48           O  
ANISOU 1581  O   ASP A 224     8305  12222   8912   3340   -799  -3700       O  
ATOM   1582  CB  ASP A 224      34.302   9.071  -4.753  1.00102.87           C  
ANISOU 1582  CB  ASP A 224    10367  16735  11983   3654   -697  -4468       C  
ATOM   1583  CG  ASP A 224      33.308   7.968  -4.464  1.00115.23           C  
ANISOU 1583  CG  ASP A 224    11413  18853  13516   3221   -473  -4665       C  
ATOM   1584  OD1 ASP A 224      33.731   6.923  -3.928  1.00116.69           O  
ANISOU 1584  OD1 ASP A 224    11696  18935  13707   2668   -241  -4499       O  
ATOM   1585  OD2 ASP A 224      32.111   8.142  -4.780  1.00121.17           O  
ANISOU 1585  OD2 ASP A 224    11666  20140  14232   3428   -536  -4984       O  
ATOM   1586  N   THR A 225      37.099  10.826  -4.301  1.00 89.88           N  
ANISOU 1586  N   THR A 225     9995  13772  10382   4019   -893  -3900       N  
ATOM   1587  CA  THR A 225      38.231  11.458  -4.961  1.00 80.33           C  
ANISOU 1587  CA  THR A 225     9290  12008   9223   4177  -1091  -3641       C  
ATOM   1588  C   THR A 225      39.065  12.207  -3.933  1.00 78.33           C  
ANISOU 1588  C   THR A 225     9404  11420   8936   4230  -1038  -3543       C  
ATOM   1589  O   THR A 225      38.522  12.839  -3.022  1.00 85.57           O  
ANISOU 1589  O   THR A 225    10215  12521   9777   4446   -976  -3754       O  
ATOM   1590  CB  THR A 225      37.766  12.428  -6.057  1.00 81.16           C  
ANISOU 1590  CB  THR A 225     9420  12097   9319   4703  -1394  -3738       C  
ATOM   1591  OG1 THR A 225      36.970  11.723  -7.019  1.00 95.50           O  
ANISOU 1591  OG1 THR A 225    10875  14261  11150   4652  -1462  -3848       O  
ATOM   1592  CG2 THR A 225      38.961  13.054  -6.759  1.00 78.43           C  
ANISOU 1592  CG2 THR A 225     9620  11176   9003   4802  -1575  -3449       C  
ATOM   1593  N   LEU A 226      40.385  12.132  -4.081  1.00 66.20           N  
ANISOU 1593  N   LEU A 226     8286   9417   7451   4032  -1062  -3241       N  
ATOM   1594  CA  LEU A 226      41.310  12.876  -3.236  1.00 74.13           C  
ANISOU 1594  CA  LEU A 226     9669  10070   8428   4062  -1048  -3132       C  
ATOM   1595  C   LEU A 226      42.320  13.573  -4.132  1.00 66.44           C  
ANISOU 1595  C   LEU A 226     9129   8614   7501   4189  -1259  -2909       C  
ATOM   1596  O   LEU A 226      42.988  12.922  -4.942  1.00 69.48           O  
ANISOU 1596  O   LEU A 226     9606   8844   7949   3958  -1281  -2698       O  
ATOM   1597  CB  LEU A 226      42.015  11.957  -2.234  1.00 65.30           C  
ANISOU 1597  CB  LEU A 226     8599   8912   7300   3595   -819  -2982       C  
ATOM   1598  CG  LEU A 226      42.877  12.675  -1.194  1.00 69.50           C  
ANISOU 1598  CG  LEU A 226     9465   9163   7778   3604   -796  -2912       C  
ATOM   1599  CD1 LEU A 226      42.033  13.662  -0.403  1.00 65.59           C  
ANISOU 1599  CD1 LEU A 226     8878   8862   7182   3956   -790  -3203       C  
ATOM   1600  CD2 LEU A 226      43.551  11.680  -0.264  1.00 73.73           C  
ANISOU 1600  CD2 LEU A 226    10040   9686   8287   3158   -595  -2752       C  
ATOM   1601  N   SER A 227      42.422  14.892  -3.995  1.00 64.74           N  
ANISOU 1601  N   SER A 227     9172   8178   7248   4474  -1402  -2912       N  
ATOM   1602  CA  SER A 227      43.338  15.696  -4.787  1.00 84.67           C  
ANISOU 1602  CA  SER A 227    12106  10275   9788   4469  -1581  -2638       C  
ATOM   1603  C   SER A 227      44.376  16.340  -3.880  1.00 71.00           C  
ANISOU 1603  C   SER A 227    10714   8220   8041   4319  -1541  -2507       C  
ATOM   1604  O   SER A 227      44.049  16.833  -2.796  1.00 67.31           O  
ANISOU 1604  O   SER A 227    10221   7832   7523   4403  -1480  -2651       O  
ATOM   1605  CB  SER A 227      42.592  16.780  -5.571  1.00 66.90           C  
ANISOU 1605  CB  SER A 227     9900   8039   7480   4797  -1804  -2671       C  
ATOM   1606  OG  SER A 227      41.697  16.215  -6.511  1.00 75.15           O  
ANISOU 1606  OG  SER A 227    10643   9384   8527   4934  -1875  -2785       O  
ATOM   1607  N   PHE A 228      45.627  16.325  -4.327  1.00 70.04           N  
ANISOU 1607  N   PHE A 228    10890   7764   7957   4091  -1573  -2248       N  
ATOM   1608  CA  PHE A 228      46.731  16.990  -3.642  1.00 71.92           C  
ANISOU 1608  CA  PHE A 228    11451   7692   8182   3922  -1564  -2109       C  
ATOM   1609  C   PHE A 228      47.187  18.137  -4.536  1.00 73.46           C  
ANISOU 1609  C   PHE A 228    11966   7599   8348   3969  -1740  -1937       C  
ATOM   1610  O   PHE A 228      47.960  17.936  -5.476  1.00 81.44           O  
ANISOU 1610  O   PHE A 228    13114   8450   9381   3806  -1777  -1737       O  
ATOM   1611  CB  PHE A 228      47.866  16.014  -3.353  1.00 69.79           C  
ANISOU 1611  CB  PHE A 228    11240   7313   7962   3590  -1444  -1970       C  
ATOM   1612  CG  PHE A 228      47.516  14.953  -2.348  1.00 66.81           C  
ANISOU 1612  CG  PHE A 228    10634   7181   7572   3514  -1263  -2135       C  
ATOM   1613  CD1 PHE A 228      46.941  13.758  -2.751  1.00 55.00           C  
ANISOU 1613  CD1 PHE A 228     8807   5977   6113   3381  -1165  -2142       C  
ATOM   1614  CD2 PHE A 228      47.770  15.147  -0.999  1.00 63.46           C  
ANISOU 1614  CD2 PHE A 228    10273   6761   7080   3428  -1171  -2199       C  
ATOM   1615  CE1 PHE A 228      46.623  12.779  -1.827  1.00 68.16           C  
ANISOU 1615  CE1 PHE A 228    10232   7914   7751   3151   -971  -2193       C  
ATOM   1616  CE2 PHE A 228      47.454  14.173  -0.070  1.00 61.33           C  
ANISOU 1616  CE2 PHE A 228     9752   6784   6765   3218   -979  -2247       C  
ATOM   1617  CZ  PHE A 228      46.881  12.987  -0.485  1.00 65.70           C  
ANISOU 1617  CZ  PHE A 228     9998   7607   7359   3070   -875  -2235       C  
ATOM   1618  N   GLU A 229      46.706  19.341  -4.237  1.00 71.95           N  
ANISOU 1618  N   GLU A 229    11902   7344   8091   4191  -1840  -2025       N  
ATOM   1619  CA  GLU A 229      46.912  20.511  -5.088  1.00 79.66           C  
ANISOU 1619  CA  GLU A 229    13199   8060   9008   4283  -2015  -1902       C  
ATOM   1620  C   GLU A 229      48.061  21.341  -4.528  1.00 81.34           C  
ANISOU 1620  C   GLU A 229    13765   7936   9206   4077  -2016  -1781       C  
ATOM   1621  O   GLU A 229      47.897  22.066  -3.543  1.00 84.99           O  
ANISOU 1621  O   GLU A 229    14311   8345   9636   4169  -2020  -1903       O  
ATOM   1622  CB  GLU A 229      45.628  21.326  -5.187  1.00 80.69           C  
ANISOU 1622  CB  GLU A 229    13271   8319   9068   4681  -2148  -2088       C  
ATOM   1623  CG  GLU A 229      44.544  20.646  -6.005  1.00 89.80           C  
ANISOU 1623  CG  GLU A 229    14100   9799  10221   4884  -2193  -2196       C  
ATOM   1624  CD  GLU A 229      43.149  21.040  -5.572  1.00 95.26           C  
ANISOU 1624  CD  GLU A 229    14548  10781  10865   5253  -2248  -2471       C  
ATOM   1625  OE1 GLU A 229      42.885  21.030  -4.351  1.00 97.02           O  
ANISOU 1625  OE1 GLU A 229    14629  11136  11097   5275  -2131  -2635       O  
ATOM   1626  OE2 GLU A 229      42.319  21.363  -6.450  1.00 91.25           O  
ANISOU 1626  OE2 GLU A 229    13986  10387  10297   5524  -2409  -2533       O  
ATOM   1627  N   GLU A 230      49.221  21.247  -5.170  1.00 63.75           N  
ANISOU 1627  N   GLU A 230    11733   5496   6994   3798  -2013  -1557       N  
ATOM   1628  CA  GLU A 230      50.400  22.001  -4.781  1.00 63.92           C  
ANISOU 1628  CA  GLU A 230    12075   5213   6999   3563  -2019  -1439       C  
ATOM   1629  C   GLU A 230      50.834  22.918  -5.916  1.00 74.27           C  
ANISOU 1629  C   GLU A 230    13717   6259   8242   3531  -2142  -1274       C  
ATOM   1630  O   GLU A 230      50.334  22.843  -7.043  1.00 79.87           O  
ANISOU 1630  O   GLU A 230    14410   7023   8915   3668  -2216  -1229       O  
ATOM   1631  CB  GLU A 230      51.556  21.071  -4.390  1.00 67.56           C  
ANISOU 1631  CB  GLU A 230    12472   5670   7529   3214  -1888  -1333       C  
ATOM   1632  CG  GLU A 230      51.244  20.174  -3.210  1.00 76.23           C  
ANISOU 1632  CG  GLU A 230    13307   6990   8666   3214  -1762  -1483       C  
ATOM   1633  CD  GLU A 230      50.755  20.951  -2.001  1.00 96.46           C  
ANISOU 1633  CD  GLU A 230    15922   9552  11177   3368  -1770  -1670       C  
ATOM   1634  OE1 GLU A 230      51.305  22.039  -1.717  1.00 96.90           O  
ANISOU 1634  OE1 GLU A 230    16268   9357  11192   3313  -1843  -1641       O  
ATOM   1635  OE2 GLU A 230      49.804  20.476  -1.347  1.00105.37           O  
ANISOU 1635  OE2 GLU A 230    16800  10939  12298   3541  -1696  -1860       O  
ATOM   1636  N   ASP A 231      51.772  23.801  -5.597  1.00 84.45           N  
ANISOU 1636  N   ASP A 231    15322   7261   9503   3341  -2167  -1192       N  
ATOM   1637  CA  ASP A 231      52.365  24.661  -6.610  1.00 94.34           C  
ANISOU 1637  CA  ASP A 231    16928   8235  10683   3239  -2259  -1022       C  
ATOM   1638  C   ASP A 231      53.143  23.813  -7.614  1.00 97.05           C  
ANISOU 1638  C   ASP A 231    17209   8616  11048   2992  -2189   -838       C  
ATOM   1639  O   ASP A 231      54.061  23.080  -7.233  1.00 94.11           O  
ANISOU 1639  O   ASP A 231    16727   8283  10747   2717  -2075   -780       O  
ATOM   1640  CB  ASP A 231      53.277  25.692  -5.944  1.00100.12           C  
ANISOU 1640  CB  ASP A 231    17992   8663  11388   3035  -2281   -989       C  
ATOM   1641  CG  ASP A 231      53.605  26.847  -6.856  1.00114.52           C  
ANISOU 1641  CG  ASP A 231    20233  10170  13109   2995  -2397   -857       C  
ATOM   1642  OD1 ASP A 231      54.756  27.328  -6.824  1.00117.22           O  
ANISOU 1642  OD1 ASP A 231    20828  10275  13436   2670  -2379   -739       O  
ATOM   1643  OD2 ASP A 231      52.705  27.275  -7.608  1.00127.32           O  
ANISOU 1643  OD2 ASP A 231    21936  11782  14658   3284  -2510   -875       O  
ATOM   1644  N   ARG A 232      52.752  23.893  -8.891  1.00 88.60           N  
ANISOU 1644  N   ARG A 232    16210   7543   9910   3111  -2264   -760       N  
ATOM   1645  CA  ARG A 232      53.398  23.203 -10.010  1.00 82.64           C  
ANISOU 1645  CA  ARG A 232    15437   6814   9149   2918  -2212   -591       C  
ATOM   1646  C   ARG A 232      53.284  21.684  -9.943  1.00 77.72           C  
ANISOU 1646  C   ARG A 232    14417   6485   8628   2888  -2098   -630       C  
ATOM   1647  O   ARG A 232      54.085  20.981 -10.567  1.00 72.59           O  
ANISOU 1647  O   ARG A 232    13732   5851   7998   2672  -2022   -500       O  
ATOM   1648  CB  ARG A 232      54.874  23.614 -10.146  1.00 71.57           C  
ANISOU 1648  CB  ARG A 232    14303   5163   7729   2535  -2161   -414       C  
ATOM   1649  CG  ARG A 232      55.054  24.847 -10.997  1.00 72.94           C  
ANISOU 1649  CG  ARG A 232    14900   5049   7767   2517  -2269   -295       C  
ATOM   1650  CD  ARG A 232      56.345  25.585 -10.714  1.00 71.87           C  
ANISOU 1650  CD  ARG A 232    15063   4637   7609   2151  -2236   -181       C  
ATOM   1651  NE  ARG A 232      56.200  27.001 -11.050  1.00 87.07           N  
ANISOU 1651  NE  ARG A 232    17416   6257   9411   2209  -2364   -139       N  
ATOM   1652  CZ  ARG A 232      55.887  27.952 -10.172  1.00104.46           C  
ANISOU 1652  CZ  ARG A 232    19791   8297  11603   2324  -2445   -252       C  
ATOM   1653  NH1 ARG A 232      55.760  29.216 -10.562  1.00100.73           N  
ANISOU 1653  NH1 ARG A 232    19737   7523  11012   2385  -2569   -206       N  
ATOM   1654  NH2 ARG A 232      55.706  27.644  -8.896  1.00 97.64           N  
ANISOU 1654  NH2 ARG A 232    18701   7560  10839   2381  -2404   -413       N  
ATOM   1655  N   VAL A 233      52.313  21.160  -9.197  1.00 63.27           N  
ANISOU 1655  N   VAL A 233    12300   4884   6857   3095  -2080   -811       N  
ATOM   1656  CA  VAL A 233      52.011  19.727  -9.207  1.00 59.36           C  
ANISOU 1656  CA  VAL A 233    11447   4661   6446   3095  -1985   -864       C  
ATOM   1657  C   VAL A 233      50.622  19.538  -8.600  1.00 58.91           C  
ANISOU 1657  C   VAL A 233    11137   4839   6407   3397  -2009  -1086       C  
ATOM   1658  O   VAL A 233      50.247  20.218  -7.639  1.00 84.48           O  
ANISOU 1658  O   VAL A 233    14415   8051   9633   3513  -2029  -1206       O  
ATOM   1659  CB  VAL A 233      53.098  18.896  -8.479  1.00 55.19           C  
ANISOU 1659  CB  VAL A 233    10823   4136   6011   2794  -1843   -808       C  
ATOM   1660  CG1 VAL A 233      52.995  19.037  -6.966  1.00 55.23           C  
ANISOU 1660  CG1 VAL A 233    10770   4163   6053   2800  -1798   -941       C  
ATOM   1661  CG2 VAL A 233      53.006  17.426  -8.877  1.00 57.78           C  
ANISOU 1661  CG2 VAL A 233    10869   4674   6410   2757  -1758   -809       C  
ATOM   1662  N   ASN A 234      49.855  18.617  -9.181  1.00 75.06           N  
ANISOU 1662  N   ASN A 234    12920   7126   8474   3526  -2007  -1155       N  
ATOM   1663  CA  ASN A 234      48.482  18.351  -8.756  1.00 60.95           C  
ANISOU 1663  CA  ASN A 234    10847   5613   6700   3808  -2027  -1384       C  
ATOM   1664  C   ASN A 234      48.202  16.876  -8.992  1.00 60.27           C  
ANISOU 1664  C   ASN A 234    10438   5772   6690   3756  -1936  -1442       C  
ATOM   1665  O   ASN A 234      48.024  16.457 -10.140  1.00 65.54           O  
ANISOU 1665  O   ASN A 234    11062   6503   7336   3798  -1996  -1398       O  
ATOM   1666  CB  ASN A 234      47.471  19.219  -9.514  1.00 65.30           C  
ANISOU 1666  CB  ASN A 234    11464   6198   7148   4137  -2207  -1456       C  
ATOM   1667  CG  ASN A 234      46.041  18.939  -9.105  1.00 77.53           C  
ANISOU 1667  CG  ASN A 234    12668   8084   8706   4435  -2230  -1716       C  
ATOM   1668  OD1 ASN A 234      45.795  18.326  -8.067  1.00 78.39           O  
ANISOU 1668  OD1 ASN A 234    12531   8367   8885   4396  -2099  -1853       O  
ATOM   1669  ND2 ASN A 234      45.087  19.393  -9.916  1.00 88.05           N  
ANISOU 1669  ND2 ASN A 234    13975   9525   9953   4732  -2394  -1797       N  
ATOM   1670  N   ALA A 235      48.163  16.099  -7.911  1.00 61.82           N  
ANISOU 1670  N   ALA A 235    10433   6095   6962   3666  -1795  -1548       N  
ATOM   1671  CA  ALA A 235      47.936  14.661  -7.956  1.00 63.67           C  
ANISOU 1671  CA  ALA A 235    10390   6533   7270   3589  -1688  -1625       C  
ATOM   1672  C   ALA A 235      46.533  14.346  -7.456  1.00 64.08           C  
ANISOU 1672  C   ALA A 235    10106   6921   7320   3815  -1660  -1906       C  
ATOM   1673  O   ALA A 235      46.135  14.811  -6.383  1.00 66.47           O  
ANISOU 1673  O   ALA A 235    10363   7295   7596   3899  -1613  -2038       O  
ATOM   1674  CB  ALA A 235      48.978  13.927  -7.111  1.00 55.37           C  
ANISOU 1674  CB  ALA A 235     9380   5377   6282   3297  -1537  -1545       C  
ATOM   1675  N   THR A 236      45.798  13.542  -8.224  1.00 67.06           N  
ANISOU 1675  N   THR A 236    10222   7544   7714   3876  -1676  -2005       N  
ATOM   1676  CA  THR A 236      44.402  13.234  -7.949  1.00 63.62           C  
ANISOU 1676  CA  THR A 236     9391   7518   7264   4029  -1648  -2268       C  
ATOM   1677  C   THR A 236      44.183  11.729  -8.020  1.00 65.37           C  
ANISOU 1677  C   THR A 236     9292   8008   7538   3686  -1489  -2280       C  
ATOM   1678  O   THR A 236      44.710  11.060  -8.913  1.00 58.90           O  
ANISOU 1678  O   THR A 236     8523   7106   6751   3505  -1502  -2137       O  
ATOM   1679  CB  THR A 236      43.479  13.946  -8.944  1.00 66.29           C  
ANISOU 1679  CB  THR A 236     9682   7965   7541   4416  -1868  -2374       C  
ATOM   1680  OG1 THR A 236      43.747  15.353  -8.916  1.00 80.63           O  
ANISOU 1680  OG1 THR A 236    11824   9530   9281   4536  -1993  -2250       O  
ATOM   1681  CG2 THR A 236      42.021  13.707  -8.591  1.00 73.76           C  
ANISOU 1681  CG2 THR A 236    10176   9377   8471   4626  -1847  -2697       C  
ATOM   1682  N   VAL A 237      43.403  11.204  -7.077  1.00 76.96           N  
ANISOU 1682  N   VAL A 237    10447   9792   9003   3587  -1334  -2456       N  
ATOM   1683  CA  VAL A 237      43.149   9.772  -6.954  1.00 67.64           C  
ANISOU 1683  CA  VAL A 237     8996   8841   7862   3217  -1163  -2472       C  
ATOM   1684  C   VAL A 237      41.651   9.535  -7.090  1.00 62.08           C  
ANISOU 1684  C   VAL A 237     7853   8606   7127   3325  -1160  -2753       C  
ATOM   1685  O   VAL A 237      40.856  10.089  -6.322  1.00 82.98           O  
ANISOU 1685  O   VAL A 237    10319  11490   9720   3517  -1124  -2957       O  
ATOM   1686  CB  VAL A 237      43.670   9.217  -5.617  1.00 63.86           C  
ANISOU 1686  CB  VAL A 237     8561   8317   7386   2904   -950  -2396       C  
ATOM   1687  CG1 VAL A 237      43.419   7.723  -5.529  1.00 55.71           C  
ANISOU 1687  CG1 VAL A 237     7316   7465   6387   2512   -784  -2390       C  
ATOM   1688  CG2 VAL A 237      45.149   9.533  -5.448  1.00 57.64           C  
ANISOU 1688  CG2 VAL A 237     8168   7109   6623   2824   -975  -2146       C  
ATOM   1689  N   TRP A 238      41.269   8.712  -8.061  1.00 72.81           N  
ANISOU 1689  N   TRP A 238     9028  10122   8515   3199  -1196  -2783       N  
ATOM   1690  CA  TRP A 238      39.884   8.302  -8.254  1.00 74.25           C  
ANISOU 1690  CA  TRP A 238     8751  10789   8673   3219  -1188  -3054       C  
ATOM   1691  C   TRP A 238      39.703   6.872  -7.765  1.00 77.49           C  
ANISOU 1691  C   TRP A 238     8958  11369   9117   2714   -956  -3066       C  
ATOM   1692  O   TRP A 238      40.442   5.976  -8.179  1.00 81.91           O  
ANISOU 1692  O   TRP A 238     9686  11702   9733   2418   -916  -2890       O  
ATOM   1693  CB  TRP A 238      39.487   8.379  -9.729  1.00 70.14           C  
ANISOU 1693  CB  TRP A 238     8156  10353   8139   3420  -1414  -3108       C  
ATOM   1694  CG  TRP A 238      39.191   9.746 -10.249  1.00 73.12           C  
ANISOU 1694  CG  TRP A 238     8637  10693   8453   3958  -1663  -3169       C  
ATOM   1695  CD1 TRP A 238      37.973  10.350 -10.306  1.00 87.58           C  
ANISOU 1695  CD1 TRP A 238    10154  12895  10226   4329  -1786  -3442       C  
ATOM   1696  CD2 TRP A 238      40.125  10.670 -10.819  1.00 74.85           C  
ANISOU 1696  CD2 TRP A 238     9316  10474   8649   4189  -1830  -2953       C  
ATOM   1697  NE1 TRP A 238      38.089  11.599 -10.863  1.00 97.51           N  
ANISOU 1697  NE1 TRP A 238    11686  13935  11427   4809  -2035  -3400       N  
ATOM   1698  CE2 TRP A 238      39.402  11.820 -11.187  1.00 88.70           C  
ANISOU 1698  CE2 TRP A 238    11062  12313  10327   4705  -2059  -3092       C  
ATOM   1699  CE3 TRP A 238      41.503  10.640 -11.045  1.00 75.37           C  
ANISOU 1699  CE3 TRP A 238     9797  10097   8744   4005  -1807  -2660       C  
ATOM   1700  CZ2 TRP A 238      40.010  12.930 -11.769  1.00 85.98           C  
ANISOU 1700  CZ2 TRP A 238    11158  11581   9929   5012  -2261  -2926       C  
ATOM   1701  CZ3 TRP A 238      42.103  11.740 -11.622  1.00 71.54           C  
ANISOU 1701  CZ3 TRP A 238     9701   9276   8205   4280  -1988  -2510       C  
ATOM   1702  CH2 TRP A 238      41.359  12.870 -11.979  1.00 80.79           C  
ANISOU 1702  CH2 TRP A 238    10904  10497   9295   4764  -2212  -2632       C  
ATOM   1703  N   LYS A 239      38.714   6.658  -6.902  1.00 78.44           N  
ANISOU 1703  N   LYS A 239     8727  11884   9191   2617   -801  -3278       N  
ATOM   1704  CA  LYS A 239      38.282   5.306  -6.562  1.00 74.80           C  
ANISOU 1704  CA  LYS A 239     8036  11644   8741   2124   -592  -3325       C  
ATOM   1705  C   LYS A 239      37.347   4.821  -7.663  1.00 80.30           C  
ANISOU 1705  C   LYS A 239     8394  12667   9452   2097   -698  -3518       C  
ATOM   1706  O   LYS A 239      36.231   5.330  -7.803  1.00 78.14           O  
ANISOU 1706  O   LYS A 239     7741  12821   9127   2347   -772  -3788       O  
ATOM   1707  CB  LYS A 239      37.584   5.285  -5.205  1.00 73.73           C  
ANISOU 1707  CB  LYS A 239     7656  11836   8524   1993   -365  -3476       C  
ATOM   1708  CG  LYS A 239      38.471   5.618  -4.018  1.00 68.87           C  
ANISOU 1708  CG  LYS A 239     7366  10933   7869   1958   -245  -3298       C  
ATOM   1709  CD  LYS A 239      38.003   4.849  -2.788  1.00 71.55           C  
ANISOU 1709  CD  LYS A 239     7532  11532   8121   1555     46  -3351       C  
ATOM   1710  CE  LYS A 239      38.290   5.601  -1.502  1.00 72.14           C  
ANISOU 1710  CE  LYS A 239     7747  11570   8093   1683    147  -3339       C  
ATOM   1711  NZ  LYS A 239      37.641   4.929  -0.343  1.00 73.08           N  
ANISOU 1711  NZ  LYS A 239     7651  12032   8086   1312    438  -3427       N  
ATOM   1712  N   LEU A 240      37.797   3.851  -8.453  1.00 78.34           N  
ANISOU 1712  N   LEU A 240     8270  12231   9263   1816   -717  -3399       N  
ATOM   1713  CA  LEU A 240      36.984   3.460  -9.596  1.00 83.09           C  
ANISOU 1713  CA  LEU A 240     8585  13120   9867   1811   -853  -3586       C  
ATOM   1714  C   LEU A 240      35.789   2.627  -9.144  1.00 86.77           C  
ANISOU 1714  C   LEU A 240     8590  14072  10309   1449   -682  -3833       C  
ATOM   1715  O   LEU A 240      35.925   1.763  -8.273  1.00 81.74           O  
ANISOU 1715  O   LEU A 240     7997  13383   9679   1007   -440  -3760       O  
ATOM   1716  CB  LEU A 240      37.803   2.667 -10.608  1.00 73.82           C  
ANISOU 1716  CB  LEU A 240     7687  11609   8750   1623   -924  -3417       C  
ATOM   1717  CG  LEU A 240      38.752   3.481 -11.483  1.00 69.62           C  
ANISOU 1717  CG  LEU A 240     7512  10723   8215   1986  -1134  -3234       C  
ATOM   1718  CD1 LEU A 240      39.565   2.559 -12.365  1.00 73.00           C  
ANISOU 1718  CD1 LEU A 240     8184  10864   8690   1754  -1153  -3090       C  
ATOM   1719  CD2 LEU A 240      37.972   4.478 -12.323  1.00 70.49           C  
ANISOU 1719  CD2 LEU A 240     7435  11096   8252   2445  -1385  -3405       C  
ATOM   1720  N   PRO A 241      34.614   2.879  -9.705  1.00 93.80           N  
ANISOU 1720  N   PRO A 241     9036  15447  11156   1622   -805  -4125       N  
ATOM   1721  CA  PRO A 241      33.461   2.034  -9.423  1.00103.41           C  
ANISOU 1721  CA  PRO A 241     9774  17170  12349   1228   -649  -4381       C  
ATOM   1722  C   PRO A 241      33.535   0.752 -10.229  1.00110.91           C  
ANISOU 1722  C   PRO A 241    10763  18027  13350    778   -649  -4361       C  
ATOM   1723  O   PRO A 241      34.267   0.682 -11.228  1.00114.94           O  
ANISOU 1723  O   PRO A 241    11578  18195  13899    893   -825  -4219       O  
ATOM   1724  CB  PRO A 241      32.277   2.903  -9.870  1.00102.74           C  
ANISOU 1724  CB  PRO A 241     9203  17632  12200   1670   -839  -4707       C  
ATOM   1725  CG  PRO A 241      32.845   3.751 -10.961  1.00 97.75           C  
ANISOU 1725  CG  PRO A 241     8863  16705  11572   2178  -1156  -4592       C  
ATOM   1726  CD  PRO A 241      34.269   4.029 -10.560  1.00 97.39           C  
ANISOU 1726  CD  PRO A 241     9406  16028  11570   2209  -1100  -4238       C  
ATOM   1727  N   PRO A 242      32.802  -0.289  -9.826  1.00114.15           N  
ANISOU 1727  N   PRO A 242    10891  18730  13752    244   -447  -4505       N  
ATOM   1728  CA  PRO A 242      32.668  -1.462 -10.704  1.00115.63           C  
ANISOU 1728  CA  PRO A 242    11068  18885  13981   -168   -481  -4559       C  
ATOM   1729  C   PRO A 242      32.085  -1.112 -12.065  1.00116.91           C  
ANISOU 1729  C   PRO A 242    10969  19331  14122    139   -783  -4774       C  
ATOM   1730  O   PRO A 242      32.420  -1.754 -13.070  1.00117.76           O  
ANISOU 1730  O   PRO A 242    11252  19232  14259      4   -903  -4742       O  
ATOM   1731  CB  PRO A 242      31.733  -2.388  -9.910  1.00120.45           C  
ANISOU 1731  CB  PRO A 242    11334  19873  14558   -762   -211  -4731       C  
ATOM   1732  CG  PRO A 242      31.844  -1.943  -8.505  1.00117.82           C  
ANISOU 1732  CG  PRO A 242    11036  19556  14173   -745     15  -4636       C  
ATOM   1733  CD  PRO A 242      32.077  -0.463  -8.557  1.00112.00           C  
ANISOU 1733  CD  PRO A 242    10319  18820  13417    -41   -170  -4628       C  
ATOM   1734  N   THR A 243      31.222  -0.098 -12.121  1.00125.77           N  
ANISOU 1734  N   THR A 243    11685  20925  15178    575   -918  -5001       N  
ATOM   1735  CA  THR A 243      30.571   0.333 -13.352  1.00127.27           C  
ANISOU 1735  CA  THR A 243    11597  21441  15320    927  -1232  -5219       C  
ATOM   1736  C   THR A 243      31.509   1.079 -14.294  1.00128.66           C  
ANISOU 1736  C   THR A 243    12218  21180  15487   1415  -1498  -5001       C  
ATOM   1737  O   THR A 243      31.134   1.326 -15.445  1.00136.84           O  
ANISOU 1737  O   THR A 243    13129  22400  16463   1678  -1775  -5129       O  
ATOM   1738  CB  THR A 243      29.374   1.227 -13.002  1.00128.00           C  
ANISOU 1738  CB  THR A 243    11125  22171  15338   1294  -1295  -5528       C  
ATOM   1739  OG1 THR A 243      28.778   0.768 -11.783  1.00137.64           O  
ANISOU 1739  OG1 THR A 243    12032  23711  16552    883   -974  -5651       O  
ATOM   1740  CG2 THR A 243      28.309   1.213 -14.116  1.00129.57           C  
ANISOU 1740  CG2 THR A 243    10841  22914  15477   1437  -1563  -5855       C  
ATOM   1741  N   ALA A 244      32.717   1.437 -13.847  1.00128.49           N  
ANISOU 1741  N   ALA A 244    12709  20605  15507   1523  -1423  -4679       N  
ATOM   1742  CA  ALA A 244      33.579   2.303 -14.652  1.00117.78           C  
ANISOU 1742  CA  ALA A 244    11755  18872  14123   1990  -1656  -4476       C  
ATOM   1743  C   ALA A 244      34.010   1.641 -15.949  1.00111.76           C  
ANISOU 1743  C   ALA A 244    11190  17924  13350   1864  -1799  -4420       C  
ATOM   1744  O   ALA A 244      34.301   2.334 -16.934  1.00117.85           O  
ANISOU 1744  O   ALA A 244    12142  18588  14048   2259  -2048  -4353       O  
ATOM   1745  CB  ALA A 244      34.826   2.706 -13.872  1.00108.35           C  
ANISOU 1745  CB  ALA A 244    11045  17143  12979   2043  -1523  -4154       C  
ATOM   1746  N   GLY A 245      34.087   0.310 -15.975  1.00100.43           N  
ANISOU 1746  N   GLY A 245     9761  16425  11974   1317  -1645  -4440       N  
ATOM   1747  CA  GLY A 245      34.480  -0.356 -17.207  1.00 97.99           C  
ANISOU 1747  CA  GLY A 245     9640  15947  11645   1200  -1776  -4422       C  
ATOM   1748  C   GLY A 245      33.433  -0.201 -18.293  1.00107.31           C  
ANISOU 1748  C   GLY A 245    10445  17607  12720   1378  -2041  -4707       C  
ATOM   1749  O   GLY A 245      33.709  -0.410 -19.483  1.00104.93           O  
ANISOU 1749  O   GLY A 245    10301  17214  12352   1439  -2222  -4703       O  
ATOM   1750  N   LEU A 246      32.219   0.178 -17.904  1.00104.31           N  
ANISOU 1750  N   LEU A 246     9553  17771  12308   1480  -2075  -4971       N  
ATOM   1751  CA  LEU A 246      31.126   0.192 -18.864  1.00103.11           C  
ANISOU 1751  CA  LEU A 246     8970  18149  12057   1602  -2327  -5283       C  
ATOM   1752  C   LEU A 246      31.173   1.421 -19.758  1.00109.70           C  
ANISOU 1752  C   LEU A 246     9911  19005  12766   2276  -2665  -5239       C  
ATOM   1753  O   LEU A 246      30.730   1.360 -20.911  1.00114.70           O  
ANISOU 1753  O   LEU A 246    10414  19878  13288   2403  -2926  -5389       O  
ATOM   1754  CB  LEU A 246      29.780   0.117 -18.142  1.00 95.09           C  
ANISOU 1754  CB  LEU A 246     7313  17771  11046   1462  -2241  -5610       C  
ATOM   1755  N   GLU A 247      31.731   2.529 -19.275  1.00111.60           N  
ANISOU 1755  N   GLU A 247    10424  18971  13006   2699  -2674  -5027       N  
ATOM   1756  CA  GLU A 247      31.650   3.786 -20.003  1.00118.08           C  
ANISOU 1756  CA  GLU A 247    11349  19817  13698   3352  -2995  -4991       C  
ATOM   1757  C   GLU A 247      32.991   4.506 -19.967  1.00106.88           C  
ANISOU 1757  C   GLU A 247    10560  17768  12282   3574  -2978  -4610       C  
ATOM   1758  O   GLU A 247      33.818   4.284 -19.081  1.00101.40           O  
ANISOU 1758  O   GLU A 247    10119  16708  11701   3324  -2717  -4414       O  
ATOM   1759  CB  GLU A 247      30.545   4.686 -19.432  1.00121.31           C  
ANISOU 1759  CB  GLU A 247    11314  20701  14078   3766  -3092  -5230       C  
ATOM   1760  N   ASP A 248      33.192   5.378 -20.955  1.00109.08           N  
ANISOU 1760  N   ASP A 248    11089  17938  12419   4037  -3267  -4508       N  
ATOM   1761  CA  ASP A 248      34.396   6.189 -21.044  1.00 99.03           C  
ANISOU 1761  CA  ASP A 248    10403  16106  11118   4262  -3281  -4159       C  
ATOM   1762  C   ASP A 248      34.455   7.199 -19.901  1.00 98.43           C  
ANISOU 1762  C   ASP A 248    10396  15897  11104   4538  -3205  -4092       C  
ATOM   1763  O   ASP A 248      33.450   7.515 -19.257  1.00 94.69           O  
ANISOU 1763  O   ASP A 248     9518  15809  10651   4716  -3220  -4333       O  
ATOM   1764  CB  ASP A 248      34.449   6.926 -22.386  1.00104.86           C  
ANISOU 1764  CB  ASP A 248    11385  16803  11655   4688  -3620  -4078       C  
ATOM   1765  CG  ASP A 248      34.847   6.021 -23.542  1.00113.38           C  
ANISOU 1765  CG  ASP A 248    12589  17842  12649   4407  -3661  -4048       C  
ATOM   1766  OD1 ASP A 248      34.588   4.802 -23.465  1.00118.82           O  
ANISOU 1766  OD1 ASP A 248    13012  18713  13423   3950  -3514  -4217       O  
ATOM   1767  OD2 ASP A 248      35.417   6.532 -24.530  1.00108.38           O  
ANISOU 1767  OD2 ASP A 248    12339  16987  11852   4635  -3836  -3859       O  
ATOM   1768  N   LEU A 249      35.658   7.723 -19.668  1.00101.12           N  
ANISOU 1768  N   LEU A 249    11251  15704  11467   4574  -3125  -3778       N  
ATOM   1769  CA  LEU A 249      35.918   8.693 -18.612  1.00 98.63           C  
ANISOU 1769  CA  LEU A 249    11099  15172  11204   4803  -3052  -3686       C  
ATOM   1770  C   LEU A 249      36.420   9.994 -19.223  1.00101.51           C  
ANISOU 1770  C   LEU A 249    11928  15196  11445   5271  -3289  -3478       C  
ATOM   1771  O   LEU A 249      37.371   9.986 -20.013  1.00 95.07           O  
ANISOU 1771  O   LEU A 249    11516  14044  10564   5187  -3324  -3232       O  
ATOM   1772  CB  LEU A 249      36.942   8.152 -17.609  1.00 97.47           C  
ANISOU 1772  CB  LEU A 249    11156  14680  11198   4372  -2727  -3500       C  
ATOM   1773  CG  LEU A 249      36.401   7.686 -16.255  1.00101.29           C  
ANISOU 1773  CG  LEU A 249    11288  15404  11794   4132  -2480  -3669       C  
ATOM   1774  CD1 LEU A 249      35.688   8.832 -15.550  1.00 98.01           C  
ANISOU 1774  CD1 LEU A 249    10729  15161  11350   4580  -2559  -3816       C  
ATOM   1775  CD2 LEU A 249      35.477   6.481 -16.415  1.00106.11           C  
ANISOU 1775  CD2 LEU A 249    11416  16470  12429   3783  -2410  -3924       C  
ATOM   1776  N   HIS A 250      35.785  11.103 -18.849  1.00104.14           N  
ANISOU 1776  N   HIS A 250    12228  15606  11735   5732  -3429  -3575       N  
ATOM   1777  CA  HIS A 250      36.137  12.435 -19.326  1.00100.69           C  
ANISOU 1777  CA  HIS A 250    12335  14769  11153   5995  -3547  -3358       C  
ATOM   1778  C   HIS A 250      36.641  13.277 -18.161  1.00 94.95           C  
ANISOU 1778  C   HIS A 250    11875  13712  10489   6024  -3410  -3244       C  
ATOM   1779  O   HIS A 250      35.977  13.369 -17.123  1.00104.91           O  
ANISOU 1779  O   HIS A 250    12836  15207  11818   6078  -3317  -3445       O  
ATOM   1780  CB  HIS A 250      34.935  13.112 -19.988  1.00109.09           C  
ANISOU 1780  CB  HIS A 250    13278  16108  12063   6335  -3751  -3537       C  
ATOM   1781  CG  HIS A 250      34.540  12.503 -21.296  1.00122.43           C  
ANISOU 1781  CG  HIS A 250    14823  18044  13651   6322  -3906  -3604       C  
ATOM   1782  ND1 HIS A 250      34.909  13.044 -22.509  1.00124.94           N  
ANISOU 1782  ND1 HIS A 250    15564  18106  13803   6458  -4063  -3405       N  
ATOM   1783  CD2 HIS A 250      33.806  11.401 -21.583  1.00123.29           C  
ANISOU 1783  CD2 HIS A 250    14413  18640  13790   6158  -3920  -3853       C  
ATOM   1784  CE1 HIS A 250      34.420  12.303 -23.487  1.00125.55           C  
ANISOU 1784  CE1 HIS A 250    15395  18499  13810   6405  -4171  -3526       C  
ATOM   1785  NE2 HIS A 250      33.747  11.299 -22.952  1.00122.12           N  
ANISOU 1785  NE2 HIS A 250    14392  18514  13495   6210  -4092  -3802       N  
ATOM   1786  N   ILE A 251      37.812  13.888 -18.338  1.00 84.08           N  
ANISOU 1786  N   ILE A 251    11051  11816   9077   5959  -3390  -2931       N  
ATOM   1787  CA  ILE A 251      38.463  14.695 -17.311  1.00 90.19           C  
ANISOU 1787  CA  ILE A 251    12130  12237   9901   5919  -3267  -2793       C  
ATOM   1788  C   ILE A 251      38.788  16.062 -17.900  1.00 99.98           C  
ANISOU 1788  C   ILE A 251    13894  13110  10985   6094  -3408  -2598       C  
ATOM   1789  O   ILE A 251      39.228  16.162 -19.051  1.00104.19           O  
ANISOU 1789  O   ILE A 251    14702  13478  11407   6082  -3506  -2430       O  
ATOM   1790  CB  ILE A 251      39.739  14.004 -16.775  1.00100.59           C  
ANISOU 1790  CB  ILE A 251    13588  13276  11357   5563  -3056  -2607       C  
ATOM   1791  CG1 ILE A 251      39.439  13.191 -15.510  1.00 96.55           C  
ANISOU 1791  CG1 ILE A 251    12666  13004  11013   5428  -2852  -2806       C  
ATOM   1792  CG2 ILE A 251      40.855  15.010 -16.515  1.00110.76           C  
ANISOU 1792  CG2 ILE A 251    15414  14058  12611   5471  -3007  -2326       C  
ATOM   1793  CD1 ILE A 251      38.716  11.886 -15.761  1.00 94.80           C  
ANISOU 1793  CD1 ILE A 251    11941  13236  10844   5237  -2794  -3017       C  
ATOM   1794  N   HIS A 252      38.568  17.117 -17.112  1.00102.71           N  
ANISOU 1794  N   HIS A 252    14377  13334  11314   6253  -3415  -2628       N  
ATOM   1795  CA  HIS A 252      38.825  18.486 -17.539  1.00108.28           C  
ANISOU 1795  CA  HIS A 252    15579  13683  11882   6424  -3548  -2470       C  
ATOM   1796  C   HIS A 252      39.584  19.229 -16.449  1.00 92.11           C  
ANISOU 1796  C   HIS A 252    13813  11291   9893   6301  -3429  -2350       C  
ATOM   1797  O   HIS A 252      39.491  18.892 -15.265  1.00 86.05           O  
ANISOU 1797  O   HIS A 252    12800  10648   9248   6215  -3283  -2465       O  
ATOM   1798  CB  HIS A 252      37.520  19.229 -17.870  1.00111.21           C  
ANISOU 1798  CB  HIS A 252    15842  14285  12128   6854  -3761  -2683       C  
ATOM   1799  CG  HIS A 252      36.481  18.367 -18.516  1.00121.79           C  
ANISOU 1799  CG  HIS A 252    16711  16118  13444   6977  -3850  -2913       C  
ATOM   1800  ND1 HIS A 252      35.524  17.689 -17.792  1.00127.14           N  
ANISOU 1800  ND1 HIS A 252    16821  17278  14211   7013  -3786  -3213       N  
ATOM   1801  CD2 HIS A 252      36.254  18.065 -19.816  1.00125.11           C  
ANISOU 1801  CD2 HIS A 252    17132  16644  13759   7046  -3990  -2895       C  
ATOM   1802  CE1 HIS A 252      34.749  17.011 -18.618  1.00131.16           C  
ANISOU 1802  CE1 HIS A 252    16988  18174  14674   7085  -3887  -3378       C  
ATOM   1803  NE2 HIS A 252      35.170  17.221 -19.852  1.00127.79           N  
ANISOU 1803  NE2 HIS A 252    16902  17524  14129   7117  -4019  -3189       N  
ATOM   1804  N   SER A 253      40.340  20.245 -16.859  1.00 91.43           N  
ANISOU 1804  N   SER A 253    14245  10781   9715   6278  -3487  -2124       N  
ATOM   1805  CA  SER A 253      41.174  21.002 -15.938  1.00107.69           C  
ANISOU 1805  CA  SER A 253    16609  12491  11819   6125  -3387  -1997       C  
ATOM   1806  C   SER A 253      41.024  22.491 -16.214  1.00117.47           C  
ANISOU 1806  C   SER A 253    18268  13449  12918   6372  -3560  -1948       C  
ATOM   1807  O   SER A 253      40.540  22.900 -17.272  1.00130.41           O  
ANISOU 1807  O   SER A 253    20043  15089  14418   6605  -3740  -1944       O  
ATOM   1808  CB  SER A 253      42.644  20.609 -16.065  1.00108.12           C  
ANISOU 1808  CB  SER A 253    16898  12254  11927   5707  -3230  -1729       C  
ATOM   1809  OG  SER A 253      43.200  21.172 -17.240  1.00 96.97           O  
ANISOU 1809  OG  SER A 253    15890  10575  10379   5676  -3324  -1521       O  
ATOM   1810  N   GLN A 254      41.477  23.303 -15.259  1.00115.54           N  
ANISOU 1810  N   GLN A 254    18249  12946  12705   6316  -3507  -1910       N  
ATOM   1811  CA  GLN A 254      41.413  24.754 -15.373  1.00127.99           C  
ANISOU 1811  CA  GLN A 254    20258  14210  14162   6531  -3663  -1868       C  
ATOM   1812  C   GLN A 254      42.721  25.371 -14.889  1.00134.98           C  
ANISOU 1812  C   GLN A 254    21546  14663  15076   6212  -3557  -1654       C  
ATOM   1813  O   GLN A 254      43.168  25.080 -13.776  1.00133.27           O  
ANISOU 1813  O   GLN A 254    21202  14453  14983   6008  -3396  -1678       O  
ATOM   1814  CB  GLN A 254      40.225  25.312 -14.582  1.00126.73           C  
ANISOU 1814  CB  GLN A 254    19910  14252  13990   6925  -3765  -2144       C  
ATOM   1815  CG  GLN A 254      39.818  26.690 -15.030  1.00129.79           C  
ANISOU 1815  CG  GLN A 254    20697  14394  14224   7269  -3992  -2147       C  
ATOM   1816  CD  GLN A 254      40.055  26.879 -16.516  1.00137.45           C  
ANISOU 1816  CD  GLN A 254    21974  15192  15059   7280  -4119  -1963       C  
ATOM   1817  OE1 GLN A 254      40.950  27.619 -16.924  1.00140.78           O  
ANISOU 1817  OE1 GLN A 254    22890  15188  15412   7121  -4137  -1733       O  
ATOM   1818  NE2 GLN A 254      39.261  26.198 -17.335  1.00137.54           N  
ANISOU 1818  NE2 GLN A 254    21687  15545  15025   7454  -4204  -2068       N  
ATOM   1819  N   LYS A 255      43.324  26.237 -15.721  1.00140.03           N  
ANISOU 1819  N   LYS A 255    22674  14936  15594   6163  -3648  -1452       N  
ATOM   1820  CA  LYS A 255      44.644  26.814 -15.457  1.00139.11           C  
ANISOU 1820  CA  LYS A 255    22951  14416  15489   5815  -3552  -1237       C  
ATOM   1821  C   LYS A 255      44.721  28.320 -15.673  1.00132.97           C  
ANISOU 1821  C   LYS A 255    22699  13243  14578   5961  -3712  -1166       C  
ATOM   1822  O   LYS A 255      45.805  28.895 -15.498  1.00135.62           O  
ANISOU 1822  O   LYS A 255    23388  13232  14910   5664  -3646   -993       O  
ATOM   1823  CB  LYS A 255      45.721  26.141 -16.327  1.00137.31           C  
ANISOU 1823  CB  LYS A 255    22807  14108  15257   5439  -3437  -1001       C  
ATOM   1824  N   GLU A 256      43.628  28.967 -16.083  1.00127.01           N  
ANISOU 1824  N   GLU A 256    22019  12529  13710   6403  -3925  -1293       N  
ATOM   1825  CA  GLU A 256      43.449  30.417 -15.991  1.00136.37           C  
ANISOU 1825  CA  GLU A 256    23660  13369  14784   6636  -4097  -1297       C  
ATOM   1826  C   GLU A 256      44.191  31.215 -17.060  1.00136.07           C  
ANISOU 1826  C   GLU A 256    24188  12913  14599   6499  -4177  -1037       C  
ATOM   1827  O   GLU A 256      44.302  32.454 -16.929  1.00137.20           O  
ANISOU 1827  O   GLU A 256    24789  12686  14656   6600  -4296   -999       O  
ATOM   1828  CB  GLU A 256      43.844  30.934 -14.606  1.00131.34           C  
ANISOU 1828  CB  GLU A 256    23092  12572  14241   6532  -4013  -1361       C  
ATOM   1829  N   GLU A 257      44.700  30.565 -18.106  1.00137.93           N  
ANISOU 1829  N   GLU A 257    24425  13185  14795   6272  -4116   -859       N  
ATOM   1830  CA  GLU A 257      45.048  31.221 -19.362  1.00148.23           C  
ANISOU 1830  CA  GLU A 257    26207  14191  15922   6247  -4227   -644       C  
ATOM   1831  C   GLU A 257      46.218  32.196 -19.233  1.00170.69           C  
ANISOU 1831  C   GLU A 257    29583  16551  18721   5917  -4180   -432       C  
ATOM   1832  O   GLU A 257      46.389  33.079 -20.075  1.00165.63           O  
ANISOU 1832  O   GLU A 257    29431  15588  17914   5949  -4306   -274       O  
ATOM   1833  CB  GLU A 257      43.815  31.937 -19.942  1.00143.42           C  
ANISOU 1833  CB  GLU A 257    25739  13589  15164   6785  -4501   -763       C  
ATOM   1834  CG  GLU A 257      43.858  32.394 -21.406  1.00138.60           C  
ANISOU 1834  CG  GLU A 257    25534  12777  14352   6856  -4647   -570       C  
ATOM   1835  CD  GLU A 257      44.003  33.909 -21.536  1.00150.46           C  
ANISOU 1835  CD  GLU A 257    27677  13783  15709   6974  -4812   -466       C  
ATOM   1836  OE1 GLU A 257      44.109  34.560 -20.477  1.00152.94           O  
ANISOU 1836  OE1 GLU A 257    28103  13918  16090   6985  -4805   -551       O  
ATOM   1837  OE2 GLU A 257      44.006  34.444 -22.674  1.00157.46           O  
ANISOU 1837  OE2 GLU A 257    28963  14453  16411   7056  -4951   -301       O  
ATOM   1838  N   GLU A 258      47.056  32.067 -18.207  1.00207.36           N  
ANISOU 1838  N   GLU A 258    34156  21132  23501   5582  -4004   -420       N  
ATOM   1839  CA  GLU A 258      48.233  32.932 -18.136  1.00211.41           C  
ANISOU 1839  CA  GLU A 258    35151  21209  23967   5219  -3952   -221       C  
ATOM   1840  C   GLU A 258      49.162  32.683 -19.330  1.00207.37           C  
ANISOU 1840  C   GLU A 258    34844  20588  23357   4865  -3871     50       C  
ATOM   1841  O   GLU A 258      48.928  31.761 -20.123  1.00207.79           O  
ANISOU 1841  O   GLU A 258    34640  20914  23395   4898  -3842     74       O  
ATOM   1842  CB  GLU A 258      48.989  32.742 -16.811  1.00207.20           C  
ANISOU 1842  CB  GLU A 258    34459  20670  23599   4913  -3776   -269       C  
ATOM   1843  N   GLN A 259      50.195  33.518 -19.495  1.00189.47           N  
ANISOU 1843  N   GLN A 259    33051  17928  21012   4526  -3837    250       N  
ATOM   1844  CA  GLN A 259      51.115  33.425 -20.639  1.00175.12           C  
ANISOU 1844  CA  GLN A 259    31479  15986  19074   4169  -3756    519       C  
ATOM   1845  C   GLN A 259      52.302  32.515 -20.320  1.00162.55           C  
ANISOU 1845  C   GLN A 259    29621  14535  17604   3673  -3499    605       C  
ATOM   1846  O   GLN A 259      53.473  32.907 -20.384  1.00156.03           O  
ANISOU 1846  O   GLN A 259    29072  13474  16740   3234  -3389    783       O  
ATOM   1847  CB  GLN A 259      51.589  34.815 -21.056  1.00168.94           C  
ANISOU 1847  CB  GLN A 259    31361  14710  18118   4044  -3854    696       C  
ATOM   1848  N   SER A 260      51.984  31.272 -19.970  1.00155.94           N  
ANISOU 1848  N   SER A 260    28240  14097  16912   3746  -3405    470       N  
ATOM   1849  CA  SER A 260      52.981  30.230 -19.783  1.00151.01           C  
ANISOU 1849  CA  SER A 260    27324  13655  16400   3347  -3179    539       C  
ATOM   1850  C   SER A 260      52.955  29.223 -20.922  1.00146.46           C  
ANISOU 1850  C   SER A 260    26558  13325  15763   3333  -3130    628       C  
ATOM   1851  O   SER A 260      53.577  28.160 -20.811  1.00151.61           O  
ANISOU 1851  O   SER A 260    26901  14190  16512   3091  -2959    652       O  
ATOM   1852  CB  SER A 260      52.769  29.522 -18.444  1.00139.06           C  
ANISOU 1852  CB  SER A 260    25356  12384  15097   3398  -3095    332       C  
ATOM   1853  N   GLU A 261      52.216  29.522 -21.993  1.00131.98           N  
ANISOU 1853  N   GLU A 261    24905  11472  13768   3609  -3287    668       N  
ATOM   1854  CA  GLU A 261      52.118  28.793 -23.251  1.00123.10           C  
ANISOU 1854  CA  GLU A 261    23704  10537  12533   3629  -3282    769       C  
ATOM   1855  C   GLU A 261      51.110  27.644 -23.206  1.00111.08           C  
ANISOU 1855  C   GLU A 261    21671   9430  11106   3944  -3316    564       C  
ATOM   1856  O   GLU A 261      50.821  27.070 -24.252  1.00118.98           O  
ANISOU 1856  O   GLU A 261    22599  10605  12003   4035  -3352    611       O  
ATOM   1857  CB  GLU A 261      53.474  28.252 -23.746  1.00118.22           C  
ANISOU 1857  CB  GLU A 261    23117   9922  11878   3136  -3070    986       C  
ATOM   1858  N   VAL A 262      50.572  27.279 -22.043  1.00 98.54           N  
ANISOU 1858  N   VAL A 262    19728   8014   9698   4098  -3303    339       N  
ATOM   1859  CA  VAL A 262      49.561  26.230 -21.952  1.00 98.43           C  
ANISOU 1859  CA  VAL A 262    19232   8397   9770   4380  -3338    133       C  
ATOM   1860  C   VAL A 262      48.438  26.720 -21.046  1.00108.44           C  
ANISOU 1860  C   VAL A 262    20376   9723  11103   4752  -3470   -106       C  
ATOM   1861  O   VAL A 262      48.697  27.322 -19.998  1.00127.17           O  
ANISOU 1861  O   VAL A 262    22835  11931  13555   4684  -3435   -149       O  
ATOM   1862  CB  VAL A 262      50.149  24.894 -21.449  1.00104.09           C  
ANISOU 1862  CB  VAL A 262    19542   9357  10651   4119  -3134    105       C  
ATOM   1863  CG1 VAL A 262      50.673  25.013 -20.019  1.00110.20           C  
ANISOU 1863  CG1 VAL A 262    20226  10052  11593   3934  -3013     43       C  
ATOM   1864  CG2 VAL A 262      49.117  23.762 -21.575  1.00 81.58           C  
ANISOU 1864  CG2 VAL A 262    16230   6909   7859   4382  -3177    -89       C  
ATOM   1865  N   GLN A 263      47.190  26.476 -21.453  1.00107.28           N  
ANISOU 1865  N   GLN A 263    20022   9826  10913   5147  -3624   -269       N  
ATOM   1866  CA  GLN A 263      46.049  27.098 -20.794  1.00112.44           C  
ANISOU 1866  CA  GLN A 263    20607  10535  11580   5549  -3779   -490       C  
ATOM   1867  C   GLN A 263      45.047  26.120 -20.191  1.00107.12           C  
ANISOU 1867  C   GLN A 263    19364  10304  11033   5761  -3770   -756       C  
ATOM   1868  O   GLN A 263      44.446  26.444 -19.163  1.00111.86           O  
ANISOU 1868  O   GLN A 263    19824  10970  11706   5949  -3799   -940       O  
ATOM   1869  CB  GLN A 263      45.320  28.031 -21.777  1.00108.67           C  
ANISOU 1869  CB  GLN A 263    20462   9923  10905   5900  -4021   -469       C  
ATOM   1870  CG  GLN A 263      46.171  29.210 -22.240  1.00116.12           C  
ANISOU 1870  CG  GLN A 263    22020  10388  11711   5727  -4056   -224       C  
ATOM   1871  CD  GLN A 263      45.506  30.045 -23.326  1.00132.02           C  
ANISOU 1871  CD  GLN A 263    24391  12258  13514   6061  -4296   -172       C  
ATOM   1872  OE1 GLN A 263      44.294  29.968 -23.538  1.00140.68           O  
ANISOU 1872  OE1 GLN A 263    25288  13592  14573   6492  -4468   -359       O  
ATOM   1873  NE2 GLN A 263      46.304  30.849 -24.022  1.00128.00           N  
ANISOU 1873  NE2 GLN A 263    24412  11364  12857   5857  -4311     83       N  
ATOM   1874  N   ALA A 264      44.846  24.946 -20.786  1.00106.90           N  
ANISOU 1874  N   ALA A 264    19010  10583  11024   5731  -3730   -785       N  
ATOM   1875  CA  ALA A 264      43.913  23.968 -20.236  1.00106.28           C  
ANISOU 1875  CA  ALA A 264    18387  10932  11063   5894  -3714  -1039       C  
ATOM   1876  C   ALA A 264      44.133  22.634 -20.937  1.00108.09           C  
ANISOU 1876  C   ALA A 264    18350  11404  11317   5725  -3632  -1004       C  
ATOM   1877  O   ALA A 264      44.795  22.559 -21.976  1.00107.63           O  
ANISOU 1877  O   ALA A 264    18527  11214  11152   5570  -3626   -806       O  
ATOM   1878  CB  ALA A 264      42.459  24.428 -20.384  1.00 92.93           C  
ANISOU 1878  CB  ALA A 264    16571   9444   9293   6380  -3933  -1264       C  
ATOM   1879  N   TYR A 265      43.568  21.577 -20.351  1.00 99.67           N  
ANISOU 1879  N   TYR A 265    16793  10695  10383   5753  -3569  -1202       N  
ATOM   1880  CA  TYR A 265      43.655  20.249 -20.941  1.00 87.65           C  
ANISOU 1880  CA  TYR A 265    14987   9424   8890   5622  -3510  -1211       C  
ATOM   1881  C   TYR A 265      42.375  19.472 -20.665  1.00 80.64           C  
ANISOU 1881  C   TYR A 265    13581   8990   8069   5857  -3573  -1506       C  
ATOM   1882  O   TYR A 265      41.612  19.790 -19.749  1.00 81.96           O  
ANISOU 1882  O   TYR A 265    13556   9288   8298   6041  -3595  -1698       O  
ATOM   1883  CB  TYR A 265      44.883  19.469 -20.435  1.00 81.36           C  
ANISOU 1883  CB  TYR A 265    14164   8527   8224   5213  -3283  -1075       C  
ATOM   1884  CG  TYR A 265      44.853  18.965 -19.002  1.00 82.39           C  
ANISOU 1884  CG  TYR A 265    13991   8766   8547   5114  -3140  -1207       C  
ATOM   1885  CD1 TYR A 265      44.087  17.862 -18.639  1.00 80.96           C  
ANISOU 1885  CD1 TYR A 265    13335   8955   8473   5183  -3115  -1421       C  
ATOM   1886  CD2 TYR A 265      45.644  19.558 -18.026  1.00 89.12           C  
ANISOU 1886  CD2 TYR A 265    15034   9355   9471   4924  -3023  -1115       C  
ATOM   1887  CE1 TYR A 265      44.074  17.396 -17.338  1.00 69.54           C  
ANISOU 1887  CE1 TYR A 265    11631   7599   7191   5080  -2971  -1532       C  
ATOM   1888  CE2 TYR A 265      45.641  19.095 -16.720  1.00 84.26           C  
ANISOU 1888  CE2 TYR A 265    14159   8840   9017   4830  -2888  -1227       C  
ATOM   1889  CZ  TYR A 265      44.854  18.014 -16.383  1.00 91.37           C  
ANISOU 1889  CZ  TYR A 265    14608  10095  10014   4910  -2857  -1429       C  
ATOM   1890  OH  TYR A 265      44.844  17.546 -15.087  1.00 95.64           O  
ANISOU 1890  OH  TYR A 265    14907  10728  10702   4810  -2711  -1536       O  
ATOM   1891  N   SER A 266      42.156  18.441 -21.479  1.00 81.62           N  
ANISOU 1891  N   SER A 266    13472   9371   8170   5835  -3601  -1551       N  
ATOM   1892  CA  SER A 266      41.053  17.508 -21.310  1.00 80.03           C  
ANISOU 1892  CA  SER A 266    12736   9633   8037   5978  -3644  -1833       C  
ATOM   1893  C   SER A 266      41.561  16.103 -21.595  1.00 82.92           C  
ANISOU 1893  C   SER A 266    12888  10143   8477   5714  -3541  -1810       C  
ATOM   1894  O   SER A 266      42.482  15.914 -22.393  1.00 85.59           O  
ANISOU 1894  O   SER A 266    13490  10292   8738   5532  -3511  -1597       O  
ATOM   1895  CB  SER A 266      39.874  17.832 -22.239  1.00 93.07           C  
ANISOU 1895  CB  SER A 266    14292  11530   9540   6333  -3875  -1983       C  
ATOM   1896  OG  SER A 266      39.767  19.224 -22.477  1.00110.34           O  
ANISOU 1896  OG  SER A 266    16878  13448  11599   6558  -4002  -1896       O  
ATOM   1897  N   LEU A 267      40.951  15.116 -20.944  1.00 83.31           N  
ANISOU 1897  N   LEU A 267    12452  10536   8665   5692  -3488  -2039       N  
ATOM   1898  CA  LEU A 267      41.341  13.723 -21.104  1.00 77.15           C  
ANISOU 1898  CA  LEU A 267    11438   9907   7970   5457  -3406  -2056       C  
ATOM   1899  C   LEU A 267      40.117  12.879 -21.422  1.00 78.91           C  
ANISOU 1899  C   LEU A 267    11144  10641   8196   5574  -3522  -2353       C  
ATOM   1900  O   LEU A 267      39.037  13.104 -20.871  1.00 83.15           O  
ANISOU 1900  O   LEU A 267    11368  11456   8771   5760  -3560  -2589       O  
ATOM   1901  CB  LEU A 267      42.025  13.175 -19.840  1.00 78.61           C  
ANISOU 1901  CB  LEU A 267    11535   9974   8360   5214  -3183  -2034       C  
ATOM   1902  CG  LEU A 267      43.275  13.894 -19.335  1.00 85.11           C  
ANISOU 1902  CG  LEU A 267    12796  10338   9205   5026  -3041  -1771       C  
ATOM   1903  CD1 LEU A 267      43.918  13.123 -18.193  1.00 74.86           C  
ANISOU 1903  CD1 LEU A 267    11369   8971   8105   4766  -2815  -1774       C  
ATOM   1904  CD2 LEU A 267      44.257  14.080 -20.464  1.00 88.59           C  
ANISOU 1904  CD2 LEU A 267    13626  10529   9505   4904  -3067  -1514       C  
ATOM   1905  N   LEU A 268      40.294  11.911 -22.317  1.00 80.46           N  
ANISOU 1905  N   LEU A 268    11244  10990   8338   5438  -3577  -2354       N  
ATOM   1906  CA  LEU A 268      39.283  10.902 -22.605  1.00 81.95           C  
ANISOU 1906  CA  LEU A 268    10926  11671   8542   5374  -3631  -2642       C  
ATOM   1907  C   LEU A 268      39.916   9.539 -22.377  1.00 82.48           C  
ANISOU 1907  C   LEU A 268    10873  11722   8743   4823  -3343  -2639       C  
ATOM   1908  O   LEU A 268      40.879   9.176 -23.061  1.00 79.20           O  
ANISOU 1908  O   LEU A 268    10733  11091   8268   4612  -3277  -2459       O  
ATOM   1909  CB  LEU A 268      38.753  11.036 -24.035  1.00 97.41           C  
ANISOU 1909  CB  LEU A 268    12921  13805  10286   5559  -3863  -2678       C  
ATOM   1910  CG  LEU A 268      37.663  10.089 -24.555  1.00100.73           C  
ANISOU 1910  CG  LEU A 268    12838  14755  10680   5511  -3972  -2987       C  
ATOM   1911  CD1 LEU A 268      38.241   8.836 -25.202  1.00 82.10           C  
ANISOU 1911  CD1 LEU A 268    10464  12431   8299   5104  -3886  -2979       C  
ATOM   1912  CD2 LEU A 268      36.693   9.716 -23.442  1.00114.60           C  
ANISOU 1912  CD2 LEU A 268    14053  16884  12605   5494  -3908  -3285       C  
ATOM   1913  N   LEU A 269      39.382   8.794 -21.417  1.00 81.39           N  
ANISOU 1913  N   LEU A 269    10341  11809   8773   4599  -3172  -2839       N  
ATOM   1914  CA  LEU A 269      39.929   7.490 -21.067  1.00 77.44           C  
ANISOU 1914  CA  LEU A 269     9756  11260   8409   4090  -2904  -2836       C  
ATOM   1915  C   LEU A 269      38.964   6.401 -21.505  1.00 90.11           C  
ANISOU 1915  C   LEU A 269    10939  13285  10014   3898  -2935  -3116       C  
ATOM   1916  O   LEU A 269      37.858   6.300 -20.949  1.00 84.27           O  
ANISOU 1916  O   LEU A 269     9785  12909   9326   3932  -2947  -3361       O  
ATOM   1917  CB  LEU A 269      40.194   7.409 -19.565  1.00 66.72           C  
ANISOU 1917  CB  LEU A 269     8346   9777   7228   3907  -2659  -2811       C  
ATOM   1918  CG  LEU A 269      41.212   8.443 -19.083  1.00 72.70           C  
ANISOU 1918  CG  LEU A 269     9521  10111   7990   4046  -2623  -2549       C  
ATOM   1919  CD1 LEU A 269      41.455   8.325 -17.588  1.00 70.35           C  
ANISOU 1919  CD1 LEU A 269     9164   9720   7846   3862  -2393  -2541       C  
ATOM   1920  CD2 LEU A 269      42.517   8.309 -19.857  1.00 74.41           C  
ANISOU 1920  CD2 LEU A 269    10127   9995   8151   3893  -2586  -2294       C  
ATOM   1921  N   PRO A 270      39.325   5.580 -22.491  1.00 91.38           N  
ANISOU 1921  N   PRO A 270    11180  13430  10112   3686  -2946  -3107       N  
ATOM   1922  CA  PRO A 270      38.385   4.580 -23.008  1.00 94.49           C  
ANISOU 1922  CA  PRO A 270    11197  14217  10487   3497  -3005  -3391       C  
ATOM   1923  C   PRO A 270      38.008   3.557 -21.948  1.00 86.40           C  
ANISOU 1923  C   PRO A 270     9863  13312   9651   3085  -2763  -3546       C  
ATOM   1924  O   PRO A 270      38.765   3.281 -21.015  1.00 83.48           O  
ANISOU 1924  O   PRO A 270     9650  12650   9418   2860  -2524  -3396       O  
ATOM   1925  CB  PRO A 270      39.157   3.930 -24.163  1.00 95.55           C  
ANISOU 1925  CB  PRO A 270    11592  14191  10520   3330  -3019  -3306       C  
ATOM   1926  CG  PRO A 270      40.194   4.937 -24.540  1.00 93.61           C  
ANISOU 1926  CG  PRO A 270    11808  13593  10166   3580  -3066  -3001       C  
ATOM   1927  CD  PRO A 270      40.574   5.618 -23.266  1.00 85.31           C  
ANISOU 1927  CD  PRO A 270    10850  12310   9256   3638  -2924  -2855       C  
ATOM   1928  N   ARG A 271      36.810   2.993 -22.113  1.00 83.08           N  
ANISOU 1928  N   ARG A 271     9001  13343   9222   2975  -2835  -3851       N  
ATOM   1929  CA  ARG A 271      36.289   2.038 -21.144  1.00 85.53           C  
ANISOU 1929  CA  ARG A 271     8995  13819   9683   2553  -2611  -4016       C  
ATOM   1930  C   ARG A 271      37.196   0.823 -21.012  1.00 81.82           C  
ANISOU 1930  C   ARG A 271     8770  13001   9317   2080  -2383  -3905       C  
ATOM   1931  O   ARG A 271      37.325   0.256 -19.921  1.00 77.85           O  
ANISOU 1931  O   ARG A 271     8238  12392   8951   1765  -2142  -3875       O  
ATOM   1932  CB  ARG A 271      34.875   1.622 -21.545  1.00100.24           C  
ANISOU 1932  CB  ARG A 271    10340  16253  11495   2484  -2748  -4375       C  
ATOM   1933  CG  ARG A 271      34.706   1.347 -23.031  1.00104.81           C  
ANISOU 1933  CG  ARG A 271    10935  16968  11920   2546  -2993  -4479       C  
ATOM   1934  CD  ARG A 271      33.279   0.926 -23.354  1.00105.92           C  
ANISOU 1934  CD  ARG A 271    10518  17715  12013   2452  -3134  -4860       C  
ATOM   1935  NE  ARG A 271      33.037   0.841 -24.792  1.00114.50           N  
ANISOU 1935  NE  ARG A 271    11607  18982  12918   2590  -3419  -4974       N  
ATOM   1936  CZ  ARG A 271      32.401   1.770 -25.499  1.00120.67           C  
ANISOU 1936  CZ  ARG A 271    12249  20073  13526   3086  -3743  -5059       C  
ATOM   1937  NH1 ARG A 271      31.938   2.861 -24.901  1.00120.38           N  
ANISOU 1937  NH1 ARG A 271    12062  20185  13492   3509  -3822  -5055       N  
ATOM   1938  NH2 ARG A 271      32.224   1.606 -26.803  1.00123.43           N  
ANISOU 1938  NH2 ARG A 271    12654  20531  13714   3160  -3942  -5114       N  
ATOM   1939  N   ALA A 272      37.839   0.411 -22.109  1.00 88.55           N  
ANISOU 1939  N   ALA A 272     9880  13673  10093   2043  -2460  -3844       N  
ATOM   1940  CA  ALA A 272      38.699  -0.768 -22.070  1.00 85.44           C  
ANISOU 1940  CA  ALA A 272     9723  12948   9791   1646  -2266  -3767       C  
ATOM   1941  C   ALA A 272      39.878  -0.581 -21.123  1.00 83.04           C  
ANISOU 1941  C   ALA A 272     9741  12212   9600   1622  -2061  -3478       C  
ATOM   1942  O   ALA A 272      40.393  -1.561 -20.573  1.00 75.75           O  
ANISOU 1942  O   ALA A 272     8936  11049   8795   1281  -1862  -3428       O  
ATOM   1943  CB  ALA A 272      39.196  -1.098 -23.477  1.00 79.22           C  
ANISOU 1943  CB  ALA A 272     9154  12073   8871   1684  -2397  -3770       C  
ATOM   1944  N   VAL A 273      40.316   0.664 -20.919  1.00 91.37           N  
ANISOU 1944  N   VAL A 273    10952  13153  10612   1980  -2118  -3289       N  
ATOM   1945  CA  VAL A 273      41.441   0.929 -20.027  1.00 92.05           C  
ANISOU 1945  CA  VAL A 273    11324  12859  10793   1964  -1944  -3028       C  
ATOM   1946  C   VAL A 273      41.114   0.521 -18.597  1.00 89.56           C  
ANISOU 1946  C   VAL A 273    10847  12565  10616   1718  -1745  -3060       C  
ATOM   1947  O   VAL A 273      41.988   0.046 -17.860  1.00 78.91           O  
ANISOU 1947  O   VAL A 273     9704  10913   9367   1521  -1563  -2900       O  
ATOM   1948  CB  VAL A 273      41.836   2.416 -20.120  1.00 92.52           C  
ANISOU 1948  CB  VAL A 273    11575  12815  10764   2377  -2066  -2851       C  
ATOM   1949  CG1 VAL A 273      42.863   2.764 -19.069  1.00 98.65           C  
ANISOU 1949  CG1 VAL A 273    12589  13255  11638   2344  -1898  -2619       C  
ATOM   1950  CG2 VAL A 273      42.372   2.728 -21.503  1.00 90.99           C  
ANISOU 1950  CG2 VAL A 273    11620  12540  10412   2555  -2222  -2764       C  
ATOM   1951  N   PHE A 274      39.858   0.677 -18.186  1.00 91.42           N  
ANISOU 1951  N   PHE A 274    10708  13180  10847   1727  -1774  -3272       N  
ATOM   1952  CA  PHE A 274      39.441   0.345 -16.832  1.00 92.26           C  
ANISOU 1952  CA  PHE A 274    10637  13368  11048   1486  -1573  -3316       C  
ATOM   1953  C   PHE A 274      38.997  -1.103 -16.672  1.00 86.66           C  
ANISOU 1953  C   PHE A 274     9783  12739  10404    989  -1432  -3459       C  
ATOM   1954  O   PHE A 274      38.724  -1.525 -15.542  1.00 97.99           O  
ANISOU 1954  O   PHE A 274    11119  14210  11902    718  -1238  -3469       O  
ATOM   1955  CB  PHE A 274      38.304   1.273 -16.394  1.00 81.40           C  
ANISOU 1955  CB  PHE A 274     8906  12397   9625   1746  -1650  -3491       C  
ATOM   1956  CG  PHE A 274      38.605   2.726 -16.594  1.00 77.26           C  
ANISOU 1956  CG  PHE A 274     8545  11781   9028   2253  -1818  -3376       C  
ATOM   1957  CD1 PHE A 274      39.452   3.390 -15.727  1.00 74.77           C  
ANISOU 1957  CD1 PHE A 274     8503  11154   8752   2358  -1721  -3161       C  
ATOM   1958  CD2 PHE A 274      38.049   3.425 -17.652  1.00 82.10           C  
ANISOU 1958  CD2 PHE A 274     9067  12605   9522   2617  -2085  -3480       C  
ATOM   1959  CE1 PHE A 274      39.737   4.726 -15.904  1.00 80.10           C  
ANISOU 1959  CE1 PHE A 274     9371  11703   9360   2789  -1874  -3057       C  
ATOM   1960  CE2 PHE A 274      38.331   4.765 -17.835  1.00 86.97           C  
ANISOU 1960  CE2 PHE A 274     9896  13086  10062   3075  -2246  -3357       C  
ATOM   1961  CZ  PHE A 274      39.176   5.416 -16.956  1.00 87.12           C  
ANISOU 1961  CZ  PHE A 274    10202  12768  10133   3147  -2134  -3147       C  
ATOM   1962  N   GLN A 275      38.928  -1.871 -17.755  1.00 80.34           N  
ANISOU 1962  N   GLN A 275     8997  11954   9576    848  -1521  -3567       N  
ATOM   1963  CA  GLN A 275      38.365  -3.209 -17.675  1.00 79.74           C  
ANISOU 1963  CA  GLN A 275     8779  11965   9552    362  -1412  -3739       C  
ATOM   1964  C   GLN A 275      39.343  -4.181 -17.028  1.00 76.08           C  
ANISOU 1964  C   GLN A 275     8669  11043   9194     44  -1205  -3550       C  
ATOM   1965  O   GLN A 275      40.541  -4.178 -17.319  1.00 74.39           O  
ANISOU 1965  O   GLN A 275     8815  10451   8998    176  -1209  -3350       O  
ATOM   1966  CB  GLN A 275      37.967  -3.706 -19.064  1.00 73.95           C  
ANISOU 1966  CB  GLN A 275     7963  11390   8743    320  -1592  -3942       C  
ATOM   1967  CG  GLN A 275      36.795  -2.945 -19.657  1.00 78.07           C  
ANISOU 1967  CG  GLN A 275     8076  12434   9152    582  -1811  -4175       C  
ATOM   1968  CD  GLN A 275      36.384  -3.454 -21.025  1.00 93.99           C  
ANISOU 1968  CD  GLN A 275    10006  14634  11072    529  -2006  -4386       C  
ATOM   1969  OE1 GLN A 275      37.162  -4.110 -21.719  1.00 88.73           O  
ANISOU 1969  OE1 GLN A 275     9654  13661  10397    421  -2007  -4324       O  
ATOM   1970  NE2 GLN A 275      35.149  -3.154 -21.421  1.00 97.18           N  
ANISOU 1970  NE2 GLN A 275     9968  15564  11390    621  -2179  -4657       N  
ATOM   1971  N   GLN A 276      38.813  -5.000 -16.126  1.00 77.12           N  
ANISOU 1971  N   GLN A 276     8691  11227   9385   -373  -1023  -3614       N  
ATOM   1972  CA  GLN A 276      39.574  -6.075 -15.509  1.00 80.54           C  
ANISOU 1972  CA  GLN A 276     9461  11234   9905   -709   -843  -3456       C  
ATOM   1973  C   GLN A 276      40.013  -7.078 -16.578  1.00 84.35           C  
ANISOU 1973  C   GLN A 276    10175  11469  10405   -852   -911  -3516       C  
ATOM   1974  O   GLN A 276      39.352  -7.239 -17.606  1.00 88.41           O  
ANISOU 1974  O   GLN A 276    10500  12230  10863   -876  -1052  -3745       O  
ATOM   1975  CB  GLN A 276      38.695  -6.735 -14.443  1.00 94.94           C  
ANISOU 1975  CB  GLN A 276    11097  13226  11750  -1163   -648  -3542       C  
ATOM   1976  CG  GLN A 276      39.401  -7.389 -13.282  1.00 99.22           C  
ANISOU 1976  CG  GLN A 276    11970  13379  12349  -1414   -442  -3309       C  
ATOM   1977  CD  GLN A 276      40.216  -6.433 -12.430  1.00104.32           C  
ANISOU 1977  CD  GLN A 276    12764  13880  12992  -1086   -402  -3064       C  
ATOM   1978  OE1 GLN A 276      40.040  -5.216 -12.485  1.00112.13           O  
ANISOU 1978  OE1 GLN A 276    13563  15106  13937   -717   -494  -3087       O  
ATOM   1979  NE2 GLN A 276      41.122  -6.989 -11.632  1.00 93.63           N  
ANISOU 1979  NE2 GLN A 276    11771  12122  11681  -1216   -280  -2832       N  
ATOM   1980  N   THR A 277      41.147  -7.748 -16.345  1.00 83.14           N  
ANISOU 1980  N   THR A 277    10431  10837  10322   -921   -824  -3323       N  
ATOM   1981  CA  THR A 277      41.673  -8.658 -17.360  1.00 67.67           C  
ANISOU 1981  CA  THR A 277     8719   8616   8375   -995   -887  -3387       C  
ATOM   1982  C   THR A 277      40.824  -9.929 -17.431  1.00 84.20           C  
ANISOU 1982  C   THR A 277    10765  10733  10496  -1499   -834  -3602       C  
ATOM   1983  O   THR A 277      39.982 -10.201 -16.570  1.00 81.03           O  
ANISOU 1983  O   THR A 277    10183  10495  10110  -1834   -712  -3655       O  
ATOM   1984  CB  THR A 277      43.145  -9.001 -17.099  1.00 78.51           C  
ANISOU 1984  CB  THR A 277    10525   9492   9814   -878   -820  -3141       C  
ATOM   1985  OG1 THR A 277      43.783  -9.325 -18.340  1.00 95.41           O  
ANISOU 1985  OG1 THR A 277    12841  11485  11925   -730   -927  -3208       O  
ATOM   1986  CG2 THR A 277      43.276 -10.192 -16.178  1.00 72.54           C  
ANISOU 1986  CG2 THR A 277    10009   8408   9144  -1259   -661  -3070       C  
ATOM   1987  N   ARG A 278      41.043 -10.701 -18.502  1.00 95.79           N  
ANISOU 1987  N   ARG A 278    12396  12044  11954  -1567   -923  -3741       N  
ATOM   1988  CA  ARG A 278      40.214 -11.875 -18.765  1.00104.68           C  
ANISOU 1988  CA  ARG A 278    13487  13192  13094  -2051   -905  -3985       C  
ATOM   1989  C   ARG A 278      40.337 -12.918 -17.658  1.00111.86           C  
ANISOU 1989  C   ARG A 278    14667  13736  14097  -2472   -707  -3869       C  
ATOM   1990  O   ARG A 278      39.345 -13.558 -17.289  1.00113.60           O  
ANISOU 1990  O   ARG A 278    14743  14097  14322  -2950   -625  -4016       O  
ATOM   1991  CB  ARG A 278      40.577 -12.483 -20.120  1.00107.37           C  
ANISOU 1991  CB  ARG A 278    14016  13382  13398  -2002  -1042  -4152       C  
ATOM   1992  CG  ARG A 278      39.573 -12.145 -21.204  1.00107.61           C  
ANISOU 1992  CG  ARG A 278    13676  13900  13312  -1981  -1227  -4447       C  
ATOM   1993  CD  ARG A 278      39.829 -12.894 -22.499  1.00109.18           C  
ANISOU 1993  CD  ARG A 278    14071  13959  13453  -2009  -1351  -4647       C  
ATOM   1994  NE  ARG A 278      40.958 -12.350 -23.249  1.00109.15           N  
ANISOU 1994  NE  ARG A 278    14285  13805  13383  -1533  -1430  -4517       N  
ATOM   1995  CZ  ARG A 278      40.927 -11.204 -23.924  1.00103.24           C  
ANISOU 1995  CZ  ARG A 278    13345  13378  12503  -1139  -1577  -4499       C  
ATOM   1996  NH1 ARG A 278      39.825 -10.463 -23.935  1.00106.41           N  
ANISOU 1996  NH1 ARG A 278    13331  14265  12836  -1107  -1682  -4611       N  
ATOM   1997  NH2 ARG A 278      42.002 -10.793 -24.584  1.00 87.60           N  
ANISOU 1997  NH2 ARG A 278    11594  11240  10450   -772  -1618  -4370       N  
ATOM   1998  N   GLY A 279      41.537 -13.101 -17.113  1.00123.53           N  
ANISOU 1998  N   GLY A 279    16540  14757  15638  -2314   -633  -3604       N  
ATOM   1999  CA  GLY A 279      41.743 -14.070 -16.052  1.00132.95           C  
ANISOU 1999  CA  GLY A 279    18053  15564  16900  -2663   -468  -3457       C  
ATOM   2000  C   GLY A 279      41.768 -13.467 -14.659  1.00134.62           C  
ANISOU 2000  C   GLY A 279    18200  15842  17107  -2647   -329  -3221       C  
ATOM   2001  O   GLY A 279      42.227 -14.100 -13.702  1.00135.47           O  
ANISOU 2001  O   GLY A 279    18635  15587  17250  -2821   -206  -3022       O  
ATOM   2002  N   ARG A 280      41.267 -12.246 -14.530  1.00145.85           N  
ANISOU 2002  N   ARG A 280    19221  17722  18472  -2427   -355  -3245       N  
ATOM   2003  CA  ARG A 280      41.294 -11.567 -13.247  1.00157.29           C  
ANISOU 2003  CA  ARG A 280    20598  19265  19902  -2370   -231  -3050       C  
ATOM   2004  C   ARG A 280      40.107 -11.972 -12.388  1.00179.73           C  
ANISOU 2004  C   ARG A 280    23226  22359  22704  -2866    -65  -3140       C  
ATOM   2005  O   ARG A 280      39.034 -12.339 -12.884  1.00178.10           O  
ANISOU 2005  O   ARG A 280    22744  22451  22475  -3174    -77  -3402       O  
ATOM   2006  CB  ARG A 280      41.291 -10.058 -13.433  1.00150.79           C  
ANISOU 2006  CB  ARG A 280    19474  18788  19031  -1902   -330  -3043       C  
ATOM   2007  N   ARG A 281      40.310 -11.882 -11.082  1.00207.79           N  
ANISOU 2007  N   ARG A 281    26895  25822  26234  -2950     92  -2927       N  
ATOM   2008  CA  ARG A 281      39.342 -12.354 -10.115  1.00209.21           C  
ANISOU 2008  CA  ARG A 281    26948  26190  26353  -3457    292  -2962       C  
ATOM   2009  C   ARG A 281      39.081 -11.278  -9.077  1.00205.36           C  
ANISOU 2009  C   ARG A 281    26200  26043  25786  -3290    393  -2883       C  
ATOM   2010  O   ARG A 281      39.876 -10.349  -8.894  1.00199.18           O  
ANISOU 2010  O   ARG A 281    25479  25193  25008  -2825    322  -2731       O  
ATOM   2011  CB  ARG A 281      39.825 -13.635  -9.422  1.00208.67           C  
ANISOU 2011  CB  ARG A 281    27396  25591  26298  -3846    418  -2764       C  
ATOM   2012  N   ARG A 282      37.913 -11.396  -8.452  1.00201.16           N  
ANISOU 2012  N   ARG A 282    25351  25907  25172  -3686    559  -3018       N  
ATOM   2013  CA  ARG A 282      37.467 -10.780  -7.203  1.00198.94           C  
ANISOU 2013  CA  ARG A 282    24865  25941  24784  -3733    738  -2962       C  
ATOM   2014  C   ARG A 282      36.881  -9.383  -7.369  1.00192.95           C  
ANISOU 2014  C   ARG A 282    23592  25730  23988  -3314    660  -3146       C  
ATOM   2015  O   ARG A 282      36.332  -8.848  -6.403  1.00199.33           O  
ANISOU 2015  O   ARG A 282    24158  26881  24698  -3352    812  -3171       O  
ATOM   2016  CB  ARG A 282      38.572 -10.731  -6.126  1.00194.00           C  
ANISOU 2016  CB  ARG A 282    24680  24902  24127  -3603    813  -2615       C  
ATOM   2017  N   ASP A 283      36.985  -8.774  -8.552  1.00164.20           N  
ANISOU 2017  N   ASP A 283    19805  22174  20410  -2906    427  -3276       N  
ATOM   2018  CA  ASP A 283      36.410  -7.457  -8.831  1.00141.95           C  
ANISOU 2018  CA  ASP A 283    16542  19838  17556  -2471    313  -3454       C  
ATOM   2019  C   ASP A 283      36.833  -6.438  -7.776  1.00133.51           C  
ANISOU 2019  C   ASP A 283    15518  18778  16433  -2151    382  -3292       C  
ATOM   2020  O   ASP A 283      36.022  -5.676  -7.249  1.00132.19           O  
ANISOU 2020  O   ASP A 283    14970  19070  16188  -2047    446  -3443       O  
ATOM   2021  CB  ASP A 283      34.884  -7.537  -8.943  1.00129.29           C  
ANISOU 2021  CB  ASP A 283    14372  18860  15893  -2746    369  -3791       C  
ATOM   2022  N   ASP A 284      38.123  -6.448  -7.449  1.00126.39           N  
ANISOU 2022  N   ASP A 284    15081  17373  15567  -1994    368  -2999       N  
ATOM   2023  CA  ASP A 284      38.639  -5.534  -6.443  1.00112.87           C  
ANISOU 2023  CA  ASP A 284    13461  15623  13801  -1716    420  -2839       C  
ATOM   2024  C   ASP A 284      38.627  -4.097  -6.961  1.00118.51           C  
ANISOU 2024  C   ASP A 284    13970  16538  14519  -1149    235  -2934       C  
ATOM   2025  O   ASP A 284      38.611  -3.842  -8.168  1.00113.73           O  
ANISOU 2025  O   ASP A 284    13289  15958  13964   -918     39  -3033       O  
ATOM   2026  CB  ASP A 284      40.058  -5.933  -6.032  1.00101.45           C  
ANISOU 2026  CB  ASP A 284    12546  13606  12393  -1689    423  -2515       C  
ATOM   2027  N   ALA A 285      38.631  -3.149  -6.026  1.00122.68           N  
ANISOU 2027  N   ALA A 285    14439  17199  14977   -927    295  -2902       N  
ATOM   2028  CA  ALA A 285      38.669  -1.742  -6.397  1.00120.07           C  
ANISOU 2028  CA  ALA A 285    13987  16992  14642   -384    120  -2973       C  
ATOM   2029  C   ALA A 285      39.990  -1.406  -7.076  1.00110.29           C  
ANISOU 2029  C   ALA A 285    13131  15297  13479    -89    -56  -2760       C  
ATOM   2030  O   ALA A 285      41.059  -1.854  -6.652  1.00112.69           O  
ANISOU 2030  O   ALA A 285    13799  15205  13812   -194     -5  -2519       O  
ATOM   2031  CB  ALA A 285      38.473  -0.857  -5.168  1.00117.28           C  
ANISOU 2031  CB  ALA A 285    13547  16823  14192   -229    232  -2986       C  
ATOM   2032  N   LYS A 286      39.908  -0.624  -8.147  1.00100.42           N  
ANISOU 2032  N   LYS A 286    11788  14120  12248    279   -267  -2851       N  
ATOM   2033  CA  LYS A 286      41.074  -0.088  -8.827  1.00 91.35           C  
ANISOU 2033  CA  LYS A 286    10958  12608  11142    581   -429  -2670       C  
ATOM   2034  C   LYS A 286      41.025   1.430  -8.755  1.00 87.28           C  
ANISOU 2034  C   LYS A 286    10401  12183  10580   1040   -551  -2700       C  
ATOM   2035  O   LYS A 286      39.956   2.022  -8.581  1.00 83.79           O  
ANISOU 2035  O   LYS A 286     9636  12118  10082   1192   -569  -2913       O  
ATOM   2036  CB  LYS A 286      41.136  -0.559 -10.283  1.00 80.00           C  
ANISOU 2036  CB  LYS A 286     9537  11116   9743    589   -578  -2721       C  
ATOM   2037  CG  LYS A 286      41.255  -2.064 -10.417  1.00 87.68           C  
ANISOU 2037  CG  LYS A 286    10610  11936  10768    155   -475  -2702       C  
ATOM   2038  CD  LYS A 286      42.598  -2.555  -9.905  1.00 87.24           C  
ANISOU 2038  CD  LYS A 286    10965  11420  10764     65   -398  -2431       C  
ATOM   2039  CE  LYS A 286      42.542  -4.037  -9.568  1.00 85.78           C  
ANISOU 2039  CE  LYS A 286    10895  11085  10614   -392   -255  -2409       C  
ATOM   2040  NZ  LYS A 286      43.877  -4.691  -9.669  1.00 81.57           N  
ANISOU 2040  NZ  LYS A 286    10764  10086  10144   -405   -263  -2194       N  
ATOM   2041  N   ARG A 287      42.187   2.061  -8.863  1.00 72.17           N  
ANISOU 2041  N   ARG A 287     8815   9922   8685   1257   -634  -2496       N  
ATOM   2042  CA  ARG A 287      42.272   3.504  -8.738  1.00 61.25           C  
ANISOU 2042  CA  ARG A 287     7480   8535   7256   1661   -749  -2497       C  
ATOM   2043  C   ARG A 287      42.841   4.123 -10.006  1.00 67.16           C  
ANISOU 2043  C   ARG A 287     8412   9098   8007   1938   -958  -2418       C  
ATOM   2044  O   ARG A 287      43.689   3.537 -10.686  1.00 65.50           O  
ANISOU 2044  O   ARG A 287     8400   8650   7837   1818   -977  -2278       O  
ATOM   2045  CB  ARG A 287      43.125   3.907  -7.530  1.00 58.79           C  
ANISOU 2045  CB  ARG A 287     7410   7993   6936   1652   -650  -2330       C  
ATOM   2046  CG  ARG A 287      42.424   3.707  -6.198  1.00 65.72           C  
ANISOU 2046  CG  ARG A 287     8102   9111   7756   1481   -461  -2432       C  
ATOM   2047  CD  ARG A 287      43.279   4.191  -5.045  1.00 65.84           C  
ANISOU 2047  CD  ARG A 287     8370   8908   7737   1503   -392  -2278       C  
ATOM   2048  NE  ARG A 287      42.575   4.096  -3.771  1.00 64.58           N  
ANISOU 2048  NE  ARG A 287     8041   9009   7487   1364   -209  -2387       N  
ATOM   2049  CZ  ARG A 287      43.038   4.585  -2.627  1.00 70.08           C  
ANISOU 2049  CZ  ARG A 287     8895   9617   8113   1394   -138  -2316       C  
ATOM   2050  NH1 ARG A 287      44.207   5.211  -2.598  1.00 60.84           N  
ANISOU 2050  NH1 ARG A 287     8043   8104   6969   1546   -244  -2143       N  
ATOM   2051  NH2 ARG A 287      42.331   4.453  -1.513  1.00 82.89           N  
ANISOU 2051  NH2 ARG A 287    10351  11516   9627   1253     43  -2429       N  
ATOM   2052  N   LEU A 288      42.346   5.314 -10.319  1.00 67.15           N  
ANISOU 2052  N   LEU A 288     8352   9215   7948   2318  -1114  -2514       N  
ATOM   2053  CA  LEU A 288      42.881   6.139 -11.388  1.00 65.69           C  
ANISOU 2053  CA  LEU A 288     8398   8833   7729   2608  -1314  -2412       C  
ATOM   2054  C   LEU A 288      43.795   7.197 -10.787  1.00 65.00           C  
ANISOU 2054  C   LEU A 288     8627   8438   7631   2772  -1329  -2245       C  
ATOM   2055  O   LEU A 288      43.461   7.816  -9.772  1.00 62.65           O  
ANISOU 2055  O   LEU A 288     8284   8206   7316   2882  -1283  -2319       O  
ATOM   2056  CB  LEU A 288      41.756   6.802 -12.186  1.00 64.44           C  
ANISOU 2056  CB  LEU A 288     8023   8964   7495   2946  -1512  -2612       C  
ATOM   2057  CG  LEU A 288      42.172   7.769 -13.296  1.00 63.14           C  
ANISOU 2057  CG  LEU A 288     8127   8606   7257   3277  -1740  -2503       C  
ATOM   2058  CD1 LEU A 288      43.027   7.063 -14.342  1.00 56.85           C  
ANISOU 2058  CD1 LEU A 288     7517   7623   6461   3084  -1752  -2348       C  
ATOM   2059  CD2 LEU A 288      40.953   8.398 -13.938  1.00 70.54           C  
ANISOU 2059  CD2 LEU A 288     8836   9858   8108   3645  -1951  -2714       C  
ATOM   2060  N   LEU A 289      44.957   7.387 -11.404  1.00 59.52           N  
ANISOU 2060  N   LEU A 289     8247   7426   6941   2767  -1384  -2034       N  
ATOM   2061  CA  LEU A 289      45.946   8.353 -10.946  1.00 57.92           C  
ANISOU 2061  CA  LEU A 289     8361   6917   6728   2862  -1402  -1866       C  
ATOM   2062  C   LEU A 289      46.241   9.327 -12.075  1.00 73.01           C  
ANISOU 2062  C   LEU A 289    10509   8668   8565   3118  -1594  -1779       C  
ATOM   2063  O   LEU A 289      46.724   8.920 -13.137  1.00 71.05           O  
ANISOU 2063  O   LEU A 289    10345   8356   8297   3042  -1632  -1684       O  
ATOM   2064  CB  LEU A 289      47.230   7.652 -10.498  1.00 56.80           C  
ANISOU 2064  CB  LEU A 289     8384   6545   6651   2560  -1263  -1675       C  
ATOM   2065  CG  LEU A 289      47.363   7.188  -9.047  1.00 74.04           C  
ANISOU 2065  CG  LEU A 289    10517   8741   8875   2359  -1096  -1671       C  
ATOM   2066  CD1 LEU A 289      46.297   6.174  -8.671  1.00 81.43           C  
ANISOU 2066  CD1 LEU A 289    11147   9967   9825   2190   -983  -1834       C  
ATOM   2067  CD2 LEU A 289      48.753   6.610  -8.837  1.00 75.93           C  
ANISOU 2067  CD2 LEU A 289    10952   8734   9165   2137  -1020  -1466       C  
ATOM   2068  N   VAL A 290      45.946  10.604 -11.852  1.00 68.24           N  
ANISOU 2068  N   VAL A 290    10032   7992   7904   3422  -1714  -1812       N  
ATOM   2069  CA  VAL A 290      46.344  11.673 -12.759  1.00 67.41           C  
ANISOU 2069  CA  VAL A 290    10248   7653   7711   3650  -1893  -1688       C  
ATOM   2070  C   VAL A 290      47.263  12.599 -11.976  1.00 66.55           C  
ANISOU 2070  C   VAL A 290    10459   7218   7608   3638  -1870  -1555       C  
ATOM   2071  O   VAL A 290      46.818  13.294 -11.053  1.00 69.82           O  
ANISOU 2071  O   VAL A 290    10878   7630   8023   3807  -1883  -1666       O  
ATOM   2072  CB  VAL A 290      45.146  12.438 -13.341  1.00 67.62           C  
ANISOU 2072  CB  VAL A 290    10204   7841   7649   4062  -2105  -1845       C  
ATOM   2073  CG1 VAL A 290      45.628  13.648 -14.124  1.00 65.79           C  
ANISOU 2073  CG1 VAL A 290    10382   7316   7302   4244  -2277  -1669       C  
ATOM   2074  CG2 VAL A 290      44.325  11.532 -14.247  1.00 58.00           C  
ANISOU 2074  CG2 VAL A 290     8674   6955   6408   4047  -2151  -1975       C  
ATOM   2075  N   VAL A 291      48.544  12.593 -12.327  1.00 59.15           N  
ANISOU 2075  N   VAL A 291     9773   6031   6671   3428  -1831  -1336       N  
ATOM   2076  CA  VAL A 291      49.538  13.469 -11.722  1.00 56.42           C  
ANISOU 2076  CA  VAL A 291     9718   5402   6318   3327  -1808  -1190       C  
ATOM   2077  C   VAL A 291      49.878  14.533 -12.755  1.00 65.22           C  
ANISOU 2077  C   VAL A 291    11127   6348   7308   3374  -1933  -1034       C  
ATOM   2078  O   VAL A 291      50.489  14.239 -13.791  1.00 68.75           O  
ANISOU 2078  O   VAL A 291    11681   6729   7710   3282  -1942   -905       O  
ATOM   2079  CB  VAL A 291      50.785  12.699 -11.268  1.00 50.68           C  
ANISOU 2079  CB  VAL A 291     9009   4577   5670   2997  -1652  -1065       C  
ATOM   2080  CG1 VAL A 291      51.843  13.660 -10.771  1.00 53.68           C  
ANISOU 2080  CG1 VAL A 291     9660   4709   6027   2861  -1644   -920       C  
ATOM   2081  CG2 VAL A 291      50.421  11.694 -10.180  1.00 48.29           C  
ANISOU 2081  CG2 VAL A 291     8416   4479   5452   2862  -1506  -1181       C  
ATOM   2082  N   ASP A 292      49.477  15.769 -12.474  1.00 54.89           N  
ANISOU 2082  N   ASP A 292     9966   4962   5929   3523  -2025  -1057       N  
ATOM   2083  CA  ASP A 292      49.581  16.878 -13.414  1.00 60.54           C  
ANISOU 2083  CA  ASP A 292    10988   5507   6506   3607  -2158   -941       C  
ATOM   2084  C   ASP A 292      50.766  17.753 -13.019  1.00 66.73           C  
ANISOU 2084  C   ASP A 292    12084   5995   7273   3376  -2111   -779       C  
ATOM   2085  O   ASP A 292      50.729  18.432 -11.988  1.00 65.67           O  
ANISOU 2085  O   ASP A 292    12007   5783   7163   3389  -2103   -837       O  
ATOM   2086  CB  ASP A 292      48.273  17.670 -13.428  1.00 60.32           C  
ANISOU 2086  CB  ASP A 292    10931   5583   6405   3956  -2312  -1097       C  
ATOM   2087  CG  ASP A 292      48.358  18.948 -14.243  1.00 63.24           C  
ANISOU 2087  CG  ASP A 292    11674   5731   6625   4056  -2456   -985       C  
ATOM   2088  OD1 ASP A 292      49.293  19.103 -15.058  1.00 71.22           O  
ANISOU 2088  OD1 ASP A 292    12939   6552   7571   3869  -2443   -788       O  
ATOM   2089  OD2 ASP A 292      47.470  19.808 -14.069  1.00 74.66           O  
ANISOU 2089  OD2 ASP A 292    13165   7192   8010   4331  -2581  -1100       O  
ATOM   2090  N   PHE A 293      51.810  17.744 -13.844  1.00 58.56           N  
ANISOU 2090  N   PHE A 293    11250   4810   6190   3168  -2081   -590       N  
ATOM   2091  CA  PHE A 293      52.996  18.558 -13.617  1.00 63.47           C  
ANISOU 2091  CA  PHE A 293    12165   5163   6786   2920  -2039   -437       C  
ATOM   2092  C   PHE A 293      52.920  19.847 -14.423  1.00 67.03           C  
ANISOU 2092  C   PHE A 293    12979   5405   7083   3000  -2167   -344       C  
ATOM   2093  O   PHE A 293      52.537  19.840 -15.596  1.00 73.34           O  
ANISOU 2093  O   PHE A 293    13855   6237   7775   3125  -2250   -298       O  
ATOM   2094  CB  PHE A 293      54.273  17.803 -13.996  1.00 64.00           C  
ANISOU 2094  CB  PHE A 293    12240   5193   6885   2623  -1918   -288       C  
ATOM   2095  CG  PHE A 293      54.718  16.804 -12.971  1.00 58.99           C  
ANISOU 2095  CG  PHE A 293    11352   4664   6399   2480  -1788   -348       C  
ATOM   2096  CD1 PHE A 293      55.395  17.213 -11.833  1.00 51.89           C  
ANISOU 2096  CD1 PHE A 293    10509   3653   5555   2315  -1738   -346       C  
ATOM   2097  CD2 PHE A 293      54.473  15.454 -13.149  1.00 59.73           C  
ANISOU 2097  CD2 PHE A 293    11172   4956   6566   2511  -1728   -410       C  
ATOM   2098  CE1 PHE A 293      55.811  16.293 -10.886  1.00 49.68           C  
ANISOU 2098  CE1 PHE A 293    10018   3466   5391   2196  -1634   -396       C  
ATOM   2099  CE2 PHE A 293      54.890  14.531 -12.206  1.00 55.83           C  
ANISOU 2099  CE2 PHE A 293    10480   4535   6197   2382  -1614   -458       C  
ATOM   2100  CZ  PHE A 293      55.556  14.951 -11.073  1.00 47.79           C  
ANISOU 2100  CZ  PHE A 293     9522   3414   5222   2232  -1570   -445       C  
ATOM   2101  N   SER A 294      53.290  20.952 -13.783  1.00 73.13           N  
ANISOU 2101  N   SER A 294    13995   5954   7837   2927  -2190   -320       N  
ATOM   2102  CA  SER A 294      53.537  22.221 -14.458  1.00 67.60           C  
ANISOU 2102  CA  SER A 294    13711   4980   6994   2910  -2288   -199       C  
ATOM   2103  C   SER A 294      55.033  22.520 -14.481  1.00 65.24           C  
ANISOU 2103  C   SER A 294    13644   4461   6682   2512  -2192    -18       C  
ATOM   2104  O   SER A 294      55.464  23.663 -14.325  1.00 77.53           O  
ANISOU 2104  O   SER A 294    15530   5753   8174   2402  -2235     46       O  
ATOM   2105  CB  SER A 294      52.758  23.352 -13.794  1.00 73.61           C  
ANISOU 2105  CB  SER A 294    14616   5628   7724   3147  -2410   -320       C  
ATOM   2106  OG  SER A 294      51.363  23.104 -13.848  1.00 76.04           O  
ANISOU 2106  OG  SER A 294    14701   6162   8029   3521  -2506   -493       O  
ATOM   2107  N   SER A 295      55.834  21.472 -14.671  1.00 62.46           N  
ANISOU 2107  N   SER A 295    13121   4222   6389   2292  -2063     56       N  
ATOM   2108  CA  SER A 295      57.287  21.546 -14.630  1.00 62.12           C  
ANISOU 2108  CA  SER A 295    13223   4032   6347   1902  -1957    209       C  
ATOM   2109  C   SER A 295      57.843  20.277 -15.258  1.00 64.94           C  
ANISOU 2109  C   SER A 295    13387   4559   6729   1783  -1849    285       C  
ATOM   2110  O   SER A 295      57.281  19.193 -15.084  1.00 62.65           O  
ANISOU 2110  O   SER A 295    12775   4498   6531   1946  -1824    172       O  
ATOM   2111  CB  SER A 295      57.802  21.698 -13.193  1.00 75.90           C  
ANISOU 2111  CB  SER A 295    14902   5726   8211   1753  -1908    129       C  
ATOM   2112  OG  SER A 295      59.190  21.427 -13.115  1.00 60.40           O  
ANISOU 2112  OG  SER A 295    12976   3699   6272   1381  -1801    248       O  
ATOM   2113  N   GLN A 296      58.942  20.418 -15.995  1.00 63.31           N  
ANISOU 2113  N   GLN A 296    13390   4239   6428   1489  -1781    476       N  
ATOM   2114  CA  GLN A 296      59.617  19.281 -16.609  1.00 60.81           C  
ANISOU 2114  CA  GLN A 296    12935   4065   6106   1359  -1671    565       C  
ATOM   2115  C   GLN A 296      60.951  18.996 -15.932  1.00 63.80           C  
ANISOU 2115  C   GLN A 296    13222   4452   6567   1000  -1536    609       C  
ATOM   2116  O   GLN A 296      61.867  18.429 -16.538  1.00 65.52           O  
ANISOU 2116  O   GLN A 296    13271   4879   6743    749  -1388    682       O  
ATOM   2117  CB  GLN A 296      59.808  19.509 -18.107  1.00 66.25           C  
ANISOU 2117  CB  GLN A 296    13872   4721   6580   1296  -1672    748       C  
ATOM   2118  CG  GLN A 296      60.795  20.610 -18.487  1.00 72.58           C  
ANISOU 2118  CG  GLN A 296    15048   5292   7236    937  -1629    941       C  
ATOM   2119  CD  GLN A 296      60.977  20.724 -19.998  1.00 75.00           C  
ANISOU 2119  CD  GLN A 296    15583   5616   7300    855  -1605   1129       C  
ATOM   2120  OE1 GLN A 296      60.117  21.255 -20.702  1.00 72.78           O  
ANISOU 2120  OE1 GLN A 296    15459   5286   6907   1084  -1727   1129       O  
ATOM   2121  NE2 GLN A 296      62.103  20.227 -20.499  1.00 65.88           N  
ANISOU 2121  NE2 GLN A 296    14354   4617   6061    513  -1424   1249       N  
ATOM   2122  N   ALA A 297      61.063  19.392 -14.663  1.00 69.25           N  
ANISOU 2122  N   ALA A 297    13924   5016   7371    961  -1568    520       N  
ATOM   2123  CA  ALA A 297      62.318  19.236 -13.938  1.00 66.78           C  
ANISOU 2123  CA  ALA A 297    13451   4790   7132    603  -1451    524       C  
ATOM   2124  C   ALA A 297      62.673  17.766 -13.764  1.00 53.96           C  
ANISOU 2124  C   ALA A 297    11329   3550   5623    590  -1321    442       C  
ATOM   2125  O   ALA A 297      63.849  17.391 -13.828  1.00 56.87           O  
ANISOU 2125  O   ALA A 297    11512   4097   5999    302  -1197    485       O  
ATOM   2126  CB  ALA A 297      62.238  19.944 -12.587  1.00 63.11           C  
ANISOU 2126  CB  ALA A 297    13117   4114   6748    605  -1537    424       C  
ATOM   2127  N   LEU A 298      61.669  16.914 -13.578  1.00 51.90           N  
ANISOU 2127  N   LEU A 298    10852   3424   5444    900  -1351    319       N  
ATOM   2128  CA  LEU A 298      61.889  15.483 -13.411  1.00 53.87           C  
ANISOU 2128  CA  LEU A 298    10687   3981   5799    913  -1245    241       C  
ATOM   2129  C   LEU A 298      61.929  14.727 -14.735  1.00 55.82           C  
ANISOU 2129  C   LEU A 298    10819   4414   5975    936  -1170    283       C  
ATOM   2130  O   LEU A 298      62.100  13.503 -14.732  1.00 50.56           O  
ANISOU 2130  O   LEU A 298     9843   3977   5390    963  -1087    212       O  
ATOM   2131  CB  LEU A 298      60.798  14.885 -12.514  1.00 50.31           C  
ANISOU 2131  CB  LEU A 298    10070   3583   5464   1180  -1296     85       C  
ATOM   2132  CG  LEU A 298      60.551  15.618 -11.194  1.00 59.64           C  
ANISOU 2132  CG  LEU A 298    11369   4600   6691   1213  -1371     12       C  
ATOM   2133  CD1 LEU A 298      59.457  14.927 -10.394  1.00 53.29           C  
ANISOU 2133  CD1 LEU A 298    10369   3908   5973   1454  -1387   -142       C  
ATOM   2134  CD2 LEU A 298      61.831  15.732 -10.378  1.00 56.48           C  
ANISOU 2134  CD2 LEU A 298    10919   4213   6328    922  -1320     42       C  
ATOM   2135  N   PHE A 299      61.777  15.423 -15.861  1.00 62.91           N  
ANISOU 2135  N   PHE A 299    11985   5207   6710    931  -1205    394       N  
ATOM   2136  CA  PHE A 299      61.668  14.796 -17.179  1.00 55.15           C  
ANISOU 2136  CA  PHE A 299    10936   4399   5621    981  -1152    423       C  
ATOM   2137  C   PHE A 299      62.576  15.526 -18.173  1.00 64.19           C  
ANISOU 2137  C   PHE A 299    12315   5501   6574    712  -1082    600       C  
ATOM   2138  O   PHE A 299      62.124  16.129 -19.147  1.00 66.98           O  
ANISOU 2138  O   PHE A 299    12957   5743   6750    779  -1150    702       O  
ATOM   2139  CB  PHE A 299      60.220  14.788 -17.667  1.00 51.49           C  
ANISOU 2139  CB  PHE A 299    10556   3896   5111   1319  -1292    363       C  
ATOM   2140  CG  PHE A 299      59.274  14.077 -16.746  1.00 57.63           C  
ANISOU 2140  CG  PHE A 299    11089   4750   6056   1544  -1339    184       C  
ATOM   2141  CD1 PHE A 299      58.662  14.756 -15.704  1.00 60.30           C  
ANISOU 2141  CD1 PHE A 299    11527   4920   6463   1671  -1439    123       C  
ATOM   2142  CD2 PHE A 299      58.994  12.732 -16.922  1.00 53.45           C  
ANISOU 2142  CD2 PHE A 299    10247   4459   5602   1613  -1275     69       C  
ATOM   2143  CE1 PHE A 299      57.792  14.109 -14.851  1.00 52.05           C  
ANISOU 2143  CE1 PHE A 299    10249   3979   5547   1847  -1458    -41       C  
ATOM   2144  CE2 PHE A 299      58.127  12.075 -16.073  1.00 55.51           C  
ANISOU 2144  CE2 PHE A 299    10301   4789   6000   1767  -1303    -82       C  
ATOM   2145  CZ  PHE A 299      57.523  12.766 -15.035  1.00 49.05           C  
ANISOU 2145  CZ  PHE A 299     9561   3838   5237   1877  -1386   -134       C  
ATOM   2146  N   GLN A 300      63.879  15.469 -17.909  1.00 66.02           N  
ANISOU 2146  N   GLN A 300    12416   5840   6829    397   -946    638       N  
ATOM   2147  CA  GLN A 300      64.895  16.061 -18.768  1.00 56.99           C  
ANISOU 2147  CA  GLN A 300    11425   4723   5504     67   -834    792       C  
ATOM   2148  C   GLN A 300      65.650  14.932 -19.453  1.00 66.69           C  
ANISOU 2148  C   GLN A 300    12303   6325   6710     -9   -657    742       C  
ATOM   2149  O   GLN A 300      66.405  14.203 -18.803  1.00 68.36           O  
ANISOU 2149  O   GLN A 300    12173   6738   7063    -81   -572    645       O  
ATOM   2150  CB  GLN A 300      65.854  16.937 -17.964  1.00 58.45           C  
ANISOU 2150  CB  GLN A 300    11707   4782   5718   -269   -808    851       C  
ATOM   2151  CG  GLN A 300      65.212  18.120 -17.260  1.00 59.39           C  
ANISOU 2151  CG  GLN A 300    12212   4503   5852   -209   -979    883       C  
ATOM   2152  CD  GLN A 300      65.146  19.363 -18.131  1.00 76.85           C  
ANISOU 2152  CD  GLN A 300    14935   6423   7843   -346  -1028   1076       C  
ATOM   2153  OE1 GLN A 300      64.653  19.326 -19.261  1.00 75.76           O  
ANISOU 2153  OE1 GLN A 300    14947   6294   7545   -217  -1043   1160       O  
ATOM   2154  NE2 GLN A 300      65.647  20.474 -17.605  1.00 84.06           N  
ANISOU 2154  NE2 GLN A 300    16144   7061   8733   -618  -1061   1148       N  
ATOM   2155  N   ASP A 301      65.443  14.785 -20.757  1.00 59.24           N  
ANISOU 2155  N   ASP A 301    11453   5476   5580     30   -615    799       N  
ATOM   2156  CA  ASP A 301      66.200  13.814 -21.526  1.00 63.68           C  
ANISOU 2156  CA  ASP A 301    11721   6391   6083    -46   -436    742       C  
ATOM   2157  C   ASP A 301      67.609  14.344 -21.779  1.00 67.75           C  
ANISOU 2157  C   ASP A 301    12219   7042   6481   -464   -261    845       C  
ATOM   2158  O   ASP A 301      67.970  15.453 -21.372  1.00 68.26           O  
ANISOU 2158  O   ASP A 301    12519   6905   6510   -719   -285    966       O  
ATOM   2159  CB  ASP A 301      65.475  13.492 -22.834  1.00 60.55           C  
ANISOU 2159  CB  ASP A 301    11439   6066   5501    133   -452    751       C  
ATOM   2160  CG  ASP A 301      65.191  14.731 -23.685  1.00 81.95           C  
ANISOU 2160  CG  ASP A 301    14622   8568   7948     33   -515    960       C  
ATOM   2161  OD1 ASP A 301      65.913  15.745 -23.570  1.00 74.95           O  
ANISOU 2161  OD1 ASP A 301    13955   7548   6975   -282   -465   1113       O  
ATOM   2162  OD2 ASP A 301      64.238  14.684 -24.489  1.00 94.71           O  
ANISOU 2162  OD2 ASP A 301    16406  10149   9432    265   -623    971       O  
ATOM   2163  N   LYS A 302      68.424  13.537 -22.450  1.00 65.01           N  
ANISOU 2163  N   LYS A 302    11580   7053   6069   -546    -78    778       N  
ATOM   2164  CA  LYS A 302      69.651  14.063 -23.025  1.00 83.54           C  
ANISOU 2164  CA  LYS A 302    13918   9591   8234   -953    113    879       C  
ATOM   2165  C   LYS A 302      69.290  15.103 -24.077  1.00109.74           C  
ANISOU 2165  C   LYS A 302    17713  12724  11259  -1101    104   1091       C  
ATOM   2166  O   LYS A 302      68.340  14.923 -24.844  1.00124.70           O  
ANISOU 2166  O   LYS A 302    19792  14550  13040   -847     19   1109       O  
ATOM   2167  CB  LYS A 302      70.486  12.939 -23.637  1.00 81.34           C  
ANISOU 2167  CB  LYS A 302    13223   9763   7920   -947    313    737       C  
ATOM   2168  N   ASN A 303      70.043  16.201 -24.094  1.00103.93           N  
ANISOU 2168  N   ASN A 303    17195  11900  10395  -1521    179   1255       N  
ATOM   2169  CA  ASN A 303      69.820  17.421 -24.875  1.00111.41           C  
ANISOU 2169  CA  ASN A 303    18688  12578  11066  -1734    153   1501       C  
ATOM   2170  C   ASN A 303      68.728  18.283 -24.246  1.00114.15           C  
ANISOU 2170  C   ASN A 303    19462  12418  11493  -1529   -114   1579       C  
ATOM   2171  O   ASN A 303      68.449  19.373 -24.769  1.00125.24           O  
ANISOU 2171  O   ASN A 303    21386  13513  12687  -1655   -183   1788       O  
ATOM   2172  CB  ASN A 303      69.471  17.157 -26.352  1.00104.52           C  
ANISOU 2172  CB  ASN A 303    17961  11849   9901  -1644    218   1573       C  
ATOM   2173  CG  ASN A 303      70.350  16.089 -26.976  1.00108.33           C  
ANISOU 2173  CG  ASN A 303    17982  12857  10323  -1718    466   1431       C  
ATOM   2174  OD1 ASN A 303      71.445  15.811 -26.490  1.00114.01           O  
ANISOU 2174  OD1 ASN A 303    18326  13843  11147  -1947    626   1336       O  
ATOM   2175  ND2 ASN A 303      69.869  15.482 -28.054  1.00105.93           N  
ANISOU 2175  ND2 ASN A 303    17695  12715   9840  -1504    490   1398       N  
ATOM   2176  N   SER A 304      68.104  17.838 -23.155  1.00100.56           N  
ANISOU 2176  N   SER A 304    17553  10601  10053  -1213   -263   1416       N  
ATOM   2177  CA  SER A 304      67.189  18.648 -22.347  1.00 92.57           C  
ANISOU 2177  CA  SER A 304    16874   9154   9144  -1027   -496   1443       C  
ATOM   2178  C   SER A 304      66.095  19.285 -23.205  1.00 88.89           C  
ANISOU 2178  C   SER A 304    16886   8408   8479   -795   -659   1581       C  
ATOM   2179  O   SER A 304      65.928  20.505 -23.253  1.00 82.04           O  
ANISOU 2179  O   SER A 304    16518   7163   7491   -901   -764   1748       O  
ATOM   2180  CB  SER A 304      67.962  19.712 -21.562  1.00 89.10           C  
ANISOU 2180  CB  SER A 304    16626   8491   8735  -1413   -487   1523       C  
ATOM   2181  OG  SER A 304      68.941  19.125 -20.722  1.00 82.17           O  
ANISOU 2181  OG  SER A 304    15285   7896   8038  -1597   -369   1382       O  
ATOM   2182  N   SER A 305      65.343  18.425 -23.886  1.00 89.69           N  
ANISOU 2182  N   SER A 305    16839   8696   8543   -463   -695   1499       N  
ATOM   2183  CA  SER A 305      64.302  18.887 -24.794  1.00 77.33           C  
ANISOU 2183  CA  SER A 305    15665   6946   6770   -206   -863   1610       C  
ATOM   2184  C   SER A 305      63.173  19.576 -24.035  1.00 76.72           C  
ANISOU 2184  C   SER A 305    15848   6491   6811    124  -1127   1585       C  
ATOM   2185  O   SER A 305      62.810  19.181 -22.923  1.00 73.15           O  
ANISOU 2185  O   SER A 305    15131   6039   6623    303  -1185   1405       O  
ATOM   2186  CB  SER A 305      63.753  17.713 -25.600  1.00 69.04           C  
ANISOU 2186  CB  SER A 305    14336   6222   5674     69   -850   1482       C  
ATOM   2187  OG  SER A 305      64.812  16.998 -26.213  1.00 72.46           O  
ANISOU 2187  OG  SER A 305    14491   7023   6017   -196   -598   1460       O  
ATOM   2188  N   GLN A 306      62.614  20.614 -24.650  1.00 87.01           N  
ANISOU 2188  N   GLN A 306    17684   7476   7899    218  -1289   1764       N  
ATOM   2189  CA  GLN A 306      61.565  21.404 -24.027  1.00 90.53           C  
ANISOU 2189  CA  GLN A 306    18248   7655   8494    538  -1511   1653       C  
ATOM   2190  C   GLN A 306      60.190  20.841 -24.358  1.00 86.96           C  
ANISOU 2190  C   GLN A 306    17627   7343   8071   1037  -1680   1499       C  
ATOM   2191  O   GLN A 306      59.975  20.232 -25.411  1.00 92.58           O  
ANISOU 2191  O   GLN A 306    18311   8260   8605   1130  -1675   1541       O  
ATOM   2192  CB  GLN A 306      61.652  22.866 -24.472  1.00 89.31           C  
ANISOU 2192  CB  GLN A 306    18522   7212   8199    387  -1567   1785       C  
ATOM   2193  CG  GLN A 306      62.929  23.570 -24.042  1.00 93.90           C  
ANISOU 2193  CG  GLN A 306    19274   7636   8769   -128  -1421   1907       C  
ATOM   2194  CD  GLN A 306      63.015  24.994 -24.556  1.00114.22           C  
ANISOU 2194  CD  GLN A 306    22303   9913  11185   -288  -1479   2042       C  
ATOM   2195  OE1 GLN A 306      62.120  25.473 -25.250  1.00109.03           O  
ANISOU 2195  OE1 GLN A 306    21854   9153  10418      5  -1635   2057       O  
ATOM   2196  NE2 GLN A 306      64.101  25.679 -24.217  1.00123.73           N  
ANISOU 2196  NE2 GLN A 306    23667  10978  12368   -764  -1360   2137       N  
ATOM   2197  N   VAL A 307      59.255  21.055 -23.436  1.00 81.18           N  
ANISOU 2197  N   VAL A 307    16767   6531   7546   1340  -1823   1306       N  
ATOM   2198  CA  VAL A 307      57.879  20.599 -23.570  1.00 70.47           C  
ANISOU 2198  CA  VAL A 307    15210   5326   6241   1790  -1983   1126       C  
ATOM   2199  C   VAL A 307      56.955  21.803 -23.447  1.00 73.43           C  
ANISOU 2199  C   VAL A 307    15795   5498   6608   2029  -2163   1064       C  
ATOM   2200  O   VAL A 307      57.239  22.745 -22.699  1.00 80.57           O  
ANISOU 2200  O   VAL A 307    16873   6165   7576   1912  -2169   1070       O  
ATOM   2201  CB  VAL A 307      57.532  19.529 -22.514  1.00 88.75           C  
ANISOU 2201  CB  VAL A 307    17097   7822   8802   1941  -1962    920       C  
ATOM   2202  CG1 VAL A 307      56.090  19.075 -22.654  1.00 89.16           C  
ANISOU 2202  CG1 VAL A 307    16923   8059   8896   2361  -2117    725       C  
ATOM   2203  CG2 VAL A 307      58.476  18.343 -22.627  1.00 82.00           C  
ANISOU 2203  CG2 VAL A 307    16056   7152   7948   1727  -1792    976       C  
ATOM   2204  N   LEU A 308      55.855  21.771 -24.200  1.00 83.91           N  
ANISOU 2204  N   LEU A 308    17115   6926   7840   2369  -2319    999       N  
ATOM   2205  CA  LEU A 308      54.903  22.875 -24.226  1.00 88.65           C  
ANISOU 2205  CA  LEU A 308    17927   7356   8398   2646  -2509    941       C  
ATOM   2206  C   LEU A 308      54.401  23.182 -22.820  1.00 85.58           C  
ANISOU 2206  C   LEU A 308    17380   6917   8218   2792  -2552    744       C  
ATOM   2207  O   LEU A 308      53.793  22.325 -22.172  1.00 81.51           O  
ANISOU 2207  O   LEU A 308    16476   6636   7859   2968  -2551    554       O  
ATOM   2208  CB  LEU A 308      53.735  22.520 -25.149  1.00 83.05           C  
ANISOU 2208  CB  LEU A 308    17124   6848   7582   3017  -2671    858       C  
ATOM   2209  CG  LEU A 308      52.663  23.565 -25.457  1.00 94.46           C  
ANISOU 2209  CG  LEU A 308    18792   8163   8935   3360  -2892    805       C  
ATOM   2210  CD1 LEU A 308      53.121  24.467 -26.592  1.00 98.29           C  
ANISOU 2210  CD1 LEU A 308    19759   8416   9172   3228  -2928   1050       C  
ATOM   2211  CD2 LEU A 308      51.337  22.892 -25.799  1.00 89.28           C  
ANISOU 2211  CD2 LEU A 308    17827   7811   8283   3766  -3044    607       C  
ATOM   2212  N   GLY A 309      54.654  24.402 -22.350  1.00 86.69           N  
ANISOU 2212  N   GLY A 309    17831   6761   8346   2707  -2587    789       N  
ATOM   2213  CA  GLY A 309      54.239  24.789 -21.014  1.00 82.35           C  
ANISOU 2213  CA  GLY A 309    17171   6159   7959   2832  -2625    612       C  
ATOM   2214  C   GLY A 309      54.800  23.942 -19.889  1.00 80.19           C  
ANISOU 2214  C   GLY A 309    16557   6024   7888   2645  -2470    528       C  
ATOM   2215  O   GLY A 309      54.233  23.928 -18.797  1.00 79.17           O  
ANISOU 2215  O   GLY A 309    16225   5961   7895   2807  -2496    347       O  
ATOM   2216  N   GLU A 310      55.906  23.240 -20.127  1.00 89.29           N  
ANISOU 2216  N   GLU A 310    17651   7228   9048   2313  -2307    659       N  
ATOM   2217  CA  GLU A 310      56.490  22.306 -19.158  1.00 79.36           C  
ANISOU 2217  CA  GLU A 310    16070   6110   7975   2146  -2165    591       C  
ATOM   2218  C   GLU A 310      55.478  21.267 -18.673  1.00 73.58           C  
ANISOU 2218  C   GLU A 310    14911   5667   7380   2442  -2191    379       C  
ATOM   2219  O   GLU A 310      55.665  20.653 -17.615  1.00 78.62           O  
ANISOU 2219  O   GLU A 310    15284   6404   8186   2380  -2105    277       O  
ATOM   2220  CB  GLU A 310      57.105  23.048 -17.967  1.00 87.67           C  
ANISOU 2220  CB  GLU A 310    17223   6967   9120   1946  -2127    570       C  
ATOM   2221  CG  GLU A 310      58.229  23.992 -18.334  1.00102.15           C  
ANISOU 2221  CG  GLU A 310    19452   8527  10834   1576  -2080    769       C  
ATOM   2222  CD  GLU A 310      58.740  24.783 -17.148  1.00120.80           C  
ANISOU 2222  CD  GLU A 310    21925  10695  13279   1397  -2071    723       C  
ATOM   2223  OE1 GLU A 310      58.212  24.586 -16.035  1.00117.80           O  
ANISOU 2223  OE1 GLU A 310    21316  10402  13042   1577  -2099    540       O  
ATOM   2224  OE2 GLU A 310      59.667  25.600 -17.332  1.00127.85           O  
ANISOU 2224  OE2 GLU A 310    23137  11359  14082   1060  -2034    867       O  
ATOM   2225  N   LYS A 311      54.407  21.060 -19.437  1.00 84.63           N  
ANISOU 2225  N   LYS A 311    16245   7209   8702   2749  -2310    311       N  
ATOM   2226  CA  LYS A 311      53.338  20.159 -19.028  1.00 65.10           C  
ANISOU 2226  CA  LYS A 311    13377   5017   6342   3019  -2348     99       C  
ATOM   2227  C   LYS A 311      53.776  18.710 -19.186  1.00 65.61           C  
ANISOU 2227  C   LYS A 311    13162   5286   6480   2900  -2228    100       C  
ATOM   2228  O   LYS A 311      54.140  18.280 -20.285  1.00 68.34           O  
ANISOU 2228  O   LYS A 311    13587   5677   6704   2839  -2214    217       O  
ATOM   2229  CB  LYS A 311      52.085  20.429 -19.857  1.00 67.67           C  
ANISOU 2229  CB  LYS A 311    13725   5440   6547   3375  -2530     19       C  
ATOM   2230  CG  LYS A 311      51.135  21.437 -19.237  1.00 90.67           C  
ANISOU 2230  CG  LYS A 311    16702   8283   9464   3642  -2664   -117       C  
ATOM   2231  CD  LYS A 311      50.528  20.889 -17.955  1.00 83.68           C  
ANISOU 2231  CD  LYS A 311    15441   7596   8756   3746  -2622   -330       C  
ATOM   2232  CE  LYS A 311      49.686  21.937 -17.246  1.00 77.41           C  
ANISOU 2232  CE  LYS A 311    14725   6734   7955   4001  -2741   -465       C  
ATOM   2233  NZ  LYS A 311      49.065  21.394 -16.008  1.00 72.69           N  
ANISOU 2233  NZ  LYS A 311    13755   6355   7506   4099  -2688   -671       N  
ATOM   2234  N   VAL A 312      53.757  17.963 -18.086  1.00 59.09           N  
ANISOU 2234  N   VAL A 312    12032   4580   5839   2868  -2140    -28       N  
ATOM   2235  CA  VAL A 312      53.952  16.519 -18.102  1.00 56.23           C  
ANISOU 2235  CA  VAL A 312    11380   4414   5572   2815  -2045    -75       C  
ATOM   2236  C   VAL A 312      52.791  15.905 -17.331  1.00 55.22           C  
ANISOU 2236  C   VAL A 312    10905   4503   5574   3030  -2076   -306       C  
ATOM   2237  O   VAL A 312      52.632  16.163 -16.133  1.00 74.56           O  
ANISOU 2237  O   VAL A 312    13262   6936   8130   3020  -2039   -395       O  
ATOM   2238  CB  VAL A 312      55.303  16.105 -17.493  1.00 61.62           C  
ANISOU 2238  CB  VAL A 312    12053   5009   6352   2500  -1881     18       C  
ATOM   2239  CG1 VAL A 312      55.535  14.615 -17.670  1.00 57.59           C  
ANISOU 2239  CG1 VAL A 312    11210   4748   5922   2409  -1757    -46       C  
ATOM   2240  CG2 VAL A 312      56.437  16.898 -18.126  1.00 55.80           C  
ANISOU 2240  CG2 VAL A 312    11671   4056   5475   2255  -1847    243       C  
ATOM   2241  N   LEU A 313      51.982  15.103 -18.014  1.00 69.81           N  
ANISOU 2241  N   LEU A 313    12565   6562   7398   3217  -2145   -406       N  
ATOM   2242  CA  LEU A 313      50.724  14.603 -17.472  1.00 55.08           C  
ANISOU 2242  CA  LEU A 313    10376   4928   5624   3437  -2196   -637       C  
ATOM   2243  C   LEU A 313      50.832  13.096 -17.280  1.00 58.49           C  
ANISOU 2243  C   LEU A 313    10481   5560   6182   3286  -2062   -730       C  
ATOM   2244  O   LEU A 313      50.917  12.347 -18.260  1.00 67.16           O  
ANISOU 2244  O   LEU A 313    11495   6802   7222   3209  -2043   -722       O  
ATOM   2245  CB  LEU A 313      49.570  14.956 -18.406  1.00 70.79           C  
ANISOU 2245  CB  LEU A 313    12361   7058   7477   3741  -2391   -719       C  
ATOM   2246  CG  LEU A 313      48.218  15.275 -17.778  1.00 80.95           C  
ANISOU 2246  CG  LEU A 313    13432   8525   8801   4015  -2489   -939       C  
ATOM   2247  CD1 LEU A 313      48.317  16.496 -16.873  1.00 82.29           C  
ANISOU 2247  CD1 LEU A 313    13788   8503   8977   4018  -2481   -916       C  
ATOM   2248  CD2 LEU A 313      47.189  15.500 -18.870  1.00 73.21           C  
ANISOU 2248  CD2 LEU A 313    12431   7712   7673   4308  -2690  -1018       C  
ATOM   2249  N   GLY A 314      50.811  12.650 -16.026  1.00 54.83           N  
ANISOU 2249  N   GLY A 314     9817   5143   5871   3183  -1943   -825       N  
ATOM   2250  CA  GLY A 314      50.886  11.235 -15.704  1.00 54.42           C  
ANISOU 2250  CA  GLY A 314     9454   5287   5935   2969  -1788   -908       C  
ATOM   2251  C   GLY A 314      49.505  10.639 -15.503  1.00 52.18           C  
ANISOU 2251  C   GLY A 314     8850   5283   5694   3099  -1821  -1134       C  
ATOM   2252  O   GLY A 314      48.698  11.161 -14.731  1.00 55.39           O  
ANISOU 2252  O   GLY A 314     9181   5744   6122   3275  -1869  -1254       O  
ATOM   2253  N   ILE A 315      49.241   9.544 -16.218  1.00 51.32           N  
ANISOU 2253  N   ILE A 315     8549   5365   5587   3001  -1792  -1207       N  
ATOM   2254  CA  ILE A 315      47.979   8.820 -16.142  1.00 54.96           C  
ANISOU 2254  CA  ILE A 315     8677   6121   6083   3045  -1810  -1429       C  
ATOM   2255  C   ILE A 315      48.296   7.368 -15.825  1.00 58.29           C  
ANISOU 2255  C   ILE A 315     8927   6605   6616   2732  -1635  -1463       C  
ATOM   2256  O   ILE A 315      49.113   6.741 -16.510  1.00 55.10           O  
ANISOU 2256  O   ILE A 315     8607   6124   6203   2584  -1583  -1378       O  
ATOM   2257  CB  ILE A 315      47.161   8.929 -17.443  1.00 61.92           C  
ANISOU 2257  CB  ILE A 315     9508   7182   6835   3248  -1991  -1517       C  
ATOM   2258  CG1 ILE A 315      47.101  10.383 -17.919  1.00 71.01           C  
ANISOU 2258  CG1 ILE A 315    10943   8188   7850   3563  -2182  -1421       C  
ATOM   2259  CG2 ILE A 315      45.758   8.376 -17.230  1.00 58.35           C  
ANISOU 2259  CG2 ILE A 315     8676   7074   6419   3306  -2026  -1777       C  
ATOM   2260  CD1 ILE A 315      46.391  10.563 -19.266  1.00 61.45           C  
ANISOU 2260  CD1 ILE A 315     9736   7137   6474   3791  -2390  -1474       C  
ATOM   2261  N   VAL A 316      47.666   6.843 -14.778  1.00 56.05           N  
ANISOU 2261  N   VAL A 316     8420   6451   6424   2636  -1541  -1588       N  
ATOM   2262  CA  VAL A 316      47.949   5.504 -14.280  1.00 61.92           C  
ANISOU 2262  CA  VAL A 316     9055   7200   7269   2334  -1375  -1601       C  
ATOM   2263  C   VAL A 316      46.646   4.856 -13.839  1.00 56.25           C  
ANISOU 2263  C   VAL A 316     8025   6762   6585   2258  -1337  -1814       C  
ATOM   2264  O   VAL A 316      45.913   5.411 -13.013  1.00 60.28           O  
ANISOU 2264  O   VAL A 316     8409   7403   7091   2360  -1334  -1907       O  
ATOM   2265  CB  VAL A 316      48.953   5.519 -13.105  1.00 57.18           C  
ANISOU 2265  CB  VAL A 316     8592   6391   6741   2198  -1247  -1455       C  
ATOM   2266  CG1 VAL A 316      48.912   4.201 -12.361  1.00 53.47           C  
ANISOU 2266  CG1 VAL A 316     8004   5952   6362   1930  -1097  -1490       C  
ATOM   2267  CG2 VAL A 316      50.359   5.808 -13.585  1.00 50.03           C  
ANISOU 2267  CG2 VAL A 316     7936   5253   5819   2178  -1250  -1262       C  
ATOM   2268  N   VAL A 317      46.358   3.687 -14.393  1.00 58.92           N  
ANISOU 2268  N   VAL A 317     8239   7200   6947   2067  -1303  -1906       N  
ATOM   2269  CA  VAL A 317      45.396   2.770 -13.802  1.00 51.11           C  
ANISOU 2269  CA  VAL A 317     6988   6422   6009   1850  -1206  -2073       C  
ATOM   2270  C   VAL A 317      46.176   1.802 -12.929  1.00 61.30           C  
ANISOU 2270  C   VAL A 317     8399   7502   7389   1560  -1029  -1955       C  
ATOM   2271  O   VAL A 317      47.150   1.193 -13.387  1.00 58.70           O  
ANISOU 2271  O   VAL A 317     8254   6956   7092   1473  -1006  -1845       O  
ATOM   2272  CB  VAL A 317      44.596   2.026 -14.881  1.00 68.61           C  
ANISOU 2272  CB  VAL A 317     9019   8853   8196   1775  -1281  -2256       C  
ATOM   2273  CG1 VAL A 317      43.776   0.917 -14.253  1.00 63.89           C  
ANISOU 2273  CG1 VAL A 317     8191   8426   7659   1450  -1149  -2408       C  
ATOM   2274  CG2 VAL A 317      43.704   2.999 -15.626  1.00 61.16           C  
ANISOU 2274  CG2 VAL A 317     7928   8160   7148   2093  -1478  -2384       C  
ATOM   2275  N   GLN A 318      45.750   1.668 -11.672  1.00 55.28           N  
ANISOU 2275  N   GLN A 318     7538   6815   6653   1431   -908  -1982       N  
ATOM   2276  CA  GLN A 318      46.498   0.974 -10.629  1.00 55.11           C  
ANISOU 2276  CA  GLN A 318     7669   6584   6685   1206   -758  -1839       C  
ATOM   2277  C   GLN A 318      47.069  -0.366 -11.078  1.00 49.83           C  
ANISOU 2277  C   GLN A 318     7128   5728   6078    980   -710  -1790       C  
ATOM   2278  O   GLN A 318      46.321  -1.310 -11.352  1.00 65.29           O  
ANISOU 2278  O   GLN A 318     8963   7792   8051    767   -673  -1923       O  
ATOM   2279  CB  GLN A 318      45.603   0.775  -9.404  1.00 66.04           C  
ANISOU 2279  CB  GLN A 318     8878   8162   8052   1039   -626  -1927       C  
ATOM   2280  CG  GLN A 318      46.274   0.053  -8.250  1.00 63.92           C  
ANISOU 2280  CG  GLN A 318     8788   7692   7806    804   -480  -1771       C  
ATOM   2281  CD  GLN A 318      45.397  -0.001  -7.016  1.00 70.12           C  
ANISOU 2281  CD  GLN A 318     9415   8693   8532    642   -337  -1847       C  
ATOM   2282  OE1 GLN A 318      44.332   0.615  -6.970  1.00 70.19           O  
ANISOU 2282  OE1 GLN A 318     9159   9019   8492    741   -344  -2031       O  
ATOM   2283  NE2 GLN A 318      45.840  -0.741  -6.006  1.00 71.74           N  
ANISOU 2283  NE2 GLN A 318     9785   8745   8728    405   -209  -1711       N  
ATOM   2284  N   ASN A 319      48.400  -0.441 -11.164  1.00 47.00           N  
ANISOU 2284  N   ASN A 319     7011   5095   5751   1029   -715  -1613       N  
ATOM   2285  CA  ASN A 319      49.120  -1.691 -11.415  1.00 59.26           C  
ANISOU 2285  CA  ASN A 319     8721   6430   7366    867   -668  -1555       C  
ATOM   2286  C   ASN A 319      48.676  -2.353 -12.717  1.00 56.81           C  
ANISOU 2286  C   ASN A 319     8349   6184   7054    821   -725  -1708       C  
ATOM   2287  O   ASN A 319      48.552  -3.576 -12.798  1.00 55.33           O  
ANISOU 2287  O   ASN A 319     8212   5900   6911    603   -671  -1763       O  
ATOM   2288  CB  ASN A 319      48.960  -2.659 -10.242  1.00 59.78           C  
ANISOU 2288  CB  ASN A 319     8842   6406   7465    602   -538  -1513       C  
ATOM   2289  CG  ASN A 319      49.551  -2.122  -8.957  1.00 59.59           C  
ANISOU 2289  CG  ASN A 319     8915   6303   7423    644   -489  -1353       C  
ATOM   2290  OD1 ASN A 319      50.621  -1.510  -8.954  1.00 50.76           O  
ANISOU 2290  OD1 ASN A 319     7918   5060   6309    819   -542  -1226       O  
ATOM   2291  ND2 ASN A 319      48.856  -2.353  -7.851  1.00 63.17           N  
ANISOU 2291  ND2 ASN A 319     9312   6848   7841    461   -383  -1366       N  
ATOM   2292  N   THR A 320      48.443  -1.544 -13.748  1.00 54.70           N  
ANISOU 2292  N   THR A 320     7999   6063   6719   1025   -844  -1777       N  
ATOM   2293  CA  THR A 320      47.930  -2.053 -15.011  1.00 52.53           C  
ANISOU 2293  CA  THR A 320     7649   5899   6410   1000   -920  -1940       C  
ATOM   2294  C   THR A 320      48.635  -1.376 -16.174  1.00 52.10           C  
ANISOU 2294  C   THR A 320     7699   5819   6277   1238  -1026  -1887       C  
ATOM   2295  O   THR A 320      48.901  -0.171 -16.137  1.00 53.46           O  
ANISOU 2295  O   THR A 320     7908   6011   6395   1444  -1083  -1786       O  
ATOM   2296  CB  THR A 320      46.415  -1.839 -15.125  1.00 56.69           C  
ANISOU 2296  CB  THR A 320     7888   6758   6892    968   -975  -2145       C  
ATOM   2297  OG1 THR A 320      45.759  -2.507 -14.041  1.00 62.77           O  
ANISOU 2297  OG1 THR A 320     8553   7579   7718    697   -847  -2197       O  
ATOM   2298  CG2 THR A 320      45.889  -2.396 -16.443  1.00 57.05           C  
ANISOU 2298  CG2 THR A 320     7850   6936   6889    929  -1073  -2329       C  
ATOM   2299  N   LYS A 321      48.946  -2.167 -17.198  1.00 53.72           N  
ANISOU 2299  N   LYS A 321     7976   5971   6464   1192  -1045  -1957       N  
ATOM   2300  CA  LYS A 321      49.430  -1.668 -18.476  1.00 50.16           C  
ANISOU 2300  CA  LYS A 321     7604   5556   5899   1378  -1138  -1944       C  
ATOM   2301  C   LYS A 321      48.502  -2.157 -19.577  1.00 56.54           C  
ANISOU 2301  C   LYS A 321     8295   6559   6629   1339  -1235  -2163       C  
ATOM   2302  O   LYS A 321      48.252  -3.362 -19.694  1.00 56.56           O  
ANISOU 2302  O   LYS A 321     8285   6517   6686   1132  -1192  -2300       O  
ATOM   2303  CB  LYS A 321      50.862  -2.124 -18.743  1.00 54.30           C  
ANISOU 2303  CB  LYS A 321     8329   5857   6444   1389  -1062  -1834       C  
ATOM   2304  CG  LYS A 321      51.857  -0.988 -18.776  1.00 72.33           C  
ANISOU 2304  CG  LYS A 321    10720   8091   8669   1561  -1066  -1642       C  
ATOM   2305  CD  LYS A 321      51.988  -0.391 -20.160  1.00 60.38           C  
ANISOU 2305  CD  LYS A 321     9260   6694   6989   1703  -1153  -1652       C  
ATOM   2306  CE  LYS A 321      53.031   0.720 -20.165  1.00 64.72           C  
ANISOU 2306  CE  LYS A 321     9943   7174   7474   1812  -1137  -1448       C  
ATOM   2307  NZ  LYS A 321      54.367   0.254 -19.690  1.00 47.72           N  
ANISOU 2307  NZ  LYS A 321     7862   4863   5408   1749  -1010  -1348       N  
ATOM   2308  N   VAL A 322      47.989  -1.223 -20.371  1.00 56.98           N  
ANISOU 2308  N   VAL A 322     8283   6819   6546   1535  -1379  -2199       N  
ATOM   2309  CA  VAL A 322      47.098  -1.527 -21.482  1.00 66.85           C  
ANISOU 2309  CA  VAL A 322     9410   8300   7688   1538  -1510  -2407       C  
ATOM   2310  C   VAL A 322      47.791  -1.114 -22.771  1.00 58.99           C  
ANISOU 2310  C   VAL A 322     8589   7301   6524   1713  -1588  -2348       C  
ATOM   2311  O   VAL A 322      48.466  -0.079 -22.818  1.00 52.91           O  
ANISOU 2311  O   VAL A 322     7961   6458   5686   1891  -1600  -2156       O  
ATOM   2312  CB  VAL A 322      45.736  -0.815 -21.337  1.00 55.61           C  
ANISOU 2312  CB  VAL A 322     7731   7179   6218   1643  -1643  -2525       C  
ATOM   2313  CG1 VAL A 322      44.736  -1.413 -22.296  1.00 73.65           C  
ANISOU 2313  CG1 VAL A 322     9834   9729   8419   1572  -1769  -2782       C  
ATOM   2314  CG2 VAL A 322      45.224  -0.914 -19.909  1.00 69.99           C  
ANISOU 2314  CG2 VAL A 322     9398   9015   8182   1504  -1533  -2535       C  
ATOM   2315  N   THR A 323      47.629  -1.926 -23.813  1.00 59.98           N  
ANISOU 2315  N   THR A 323     8716   7506   6568   1641  -1633  -2518       N  
ATOM   2316  CA  THR A 323      48.261  -1.658 -25.095  1.00 68.22           C  
ANISOU 2316  CA  THR A 323     9925   8577   7419   1781  -1690  -2484       C  
ATOM   2317  C   THR A 323      47.332  -2.119 -26.208  1.00 67.41           C  
ANISOU 2317  C   THR A 323     9716   8723   7174   1763  -1843  -2729       C  
ATOM   2318  O   THR A 323      46.402  -2.900 -25.985  1.00 62.24           O  
ANISOU 2318  O   THR A 323     8874   8172   6602   1584  -1869  -2938       O  
ATOM   2319  CB  THR A 323      49.624  -2.355 -25.209  1.00 73.41           C  
ANISOU 2319  CB  THR A 323    10774   9001   8119   1709  -1527  -2416       C  
ATOM   2320  OG1 THR A 323      50.384  -1.754 -26.264  1.00 86.34           O  
ANISOU 2320  OG1 THR A 323    12571  10682   9552   1861  -1547  -2321       O  
ATOM   2321  CG2 THR A 323      49.442  -3.832 -25.510  1.00 62.72           C  
ANISOU 2321  CG2 THR A 323     9407   7599   6825   1515  -1488  -2646       C  
ATOM   2322  N   ASN A 324      47.594  -1.615 -27.415  1.00 73.90           N  
ANISOU 2322  N   ASN A 324    10663   9652   7763   1931  -1944  -2701       N  
ATOM   2323  CA  ASN A 324      46.828  -1.976 -28.609  1.00 78.16           C  
ANISOU 2323  CA  ASN A 324    11134  10445   8117   1944  -2110  -2925       C  
ATOM   2324  C   ASN A 324      45.339  -1.682 -28.417  1.00 81.58           C  
ANISOU 2324  C   ASN A 324    11286  11159   8553   1983  -2295  -3077       C  
ATOM   2325  O   ASN A 324      44.473  -2.526 -28.660  1.00 87.21           O  
ANISOU 2325  O   ASN A 324    11809  12046   9282   1816  -2363  -3341       O  
ATOM   2326  CB  ASN A 324      47.062  -3.442 -28.986  1.00 78.87           C  
ANISOU 2326  CB  ASN A 324    11254  10456   8256   1714  -2020  -3140       C  
ATOM   2327  CG  ASN A 324      46.579  -3.769 -30.385  1.00 98.93           C  
ANISOU 2327  CG  ASN A 324    13795  13236  10559   1738  -2179  -3357       C  
ATOM   2328  OD1 ASN A 324      46.614  -2.924 -31.281  1.00105.09           O  
ANISOU 2328  OD1 ASN A 324    14661  14178  11090   1951  -2306  -3278       O  
ATOM   2329  ND2 ASN A 324      46.118  -4.998 -30.577  1.00108.66           N  
ANISOU 2329  ND2 ASN A 324    14952  14483  11852   1508  -2180  -3632       N  
ATOM   2330  N   LEU A 325      45.046  -0.462 -27.975  1.00 73.65           N  
ANISOU 2330  N   LEU A 325    10249  10206   7530   2206  -2379  -2923       N  
ATOM   2331  CA  LEU A 325      43.667  -0.055 -27.746  1.00 73.21           C  
ANISOU 2331  CA  LEU A 325     9901  10444   7471   2308  -2558  -3069       C  
ATOM   2332  C   LEU A 325      42.944   0.181 -29.066  1.00 81.72           C  
ANISOU 2332  C   LEU A 325    10928  11834   8288   2485  -2820  -3211       C  
ATOM   2333  O   LEU A 325      43.507   0.746 -30.009  1.00 77.85           O  
ANISOU 2333  O   LEU A 325    10695  11309   7575   2668  -2899  -3074       O  
ATOM   2334  CB  LEU A 325      43.625   1.216 -26.898  1.00 66.52           C  
ANISOU 2334  CB  LEU A 325     9070   9532   6671   2543  -2579  -2873       C  
ATOM   2335  CG  LEU A 325      44.005   1.087 -25.424  1.00 62.40           C  
ANISOU 2335  CG  LEU A 325     8520   8791   6399   2388  -2362  -2774       C  
ATOM   2336  CD1 LEU A 325      44.392   2.439 -24.870  1.00 61.15           C  
ANISOU 2336  CD1 LEU A 325     8519   8485   6231   2639  -2377  -2537       C  
ATOM   2337  CD2 LEU A 325      42.846   0.508 -24.634  1.00 63.67           C  
ANISOU 2337  CD2 LEU A 325     8320   9170   6704   2219  -2347  -3000       C  
ATOM   2338  N   SER A 326      41.685  -0.259 -29.131  1.00 85.90           N  
ANISOU 2338  N   SER A 326    11120  12690   8829   2415  -2957  -3490       N  
ATOM   2339  CA  SER A 326      40.843   0.026 -30.287  1.00 89.00           C  
ANISOU 2339  CA  SER A 326    11407  13437   8971   2614  -3247  -3648       C  
ATOM   2340  C   SER A 326      40.541   1.517 -30.337  1.00 92.20           C  
ANISOU 2340  C   SER A 326    11865  13923   9242   3047  -3444  -3480       C  
ATOM   2341  O   SER A 326      41.035   2.227 -31.217  1.00 95.05           O  
ANISOU 2341  O   SER A 326    12528  14220   9368   3281  -3558  -3305       O  
ATOM   2342  CB  SER A 326      39.546  -0.787 -30.238  1.00 87.74           C  
ANISOU 2342  CB  SER A 326    10824  13641   8874   2412  -3345  -4006       C  
ATOM   2343  OG  SER A 326      39.805  -2.179 -30.313  1.00 86.09           O  
ANISOU 2343  OG  SER A 326    10627  13319   8763   2005  -3188  -4169       O  
ATOM   2344  N   ASP A 327      39.737   1.999 -29.398  1.00 82.89           N  
ANISOU 2344  N   ASP A 327    10417  12877   8199   3157  -3483  -3532       N  
ATOM   2345  CA  ASP A 327      39.542   3.433 -29.241  1.00 85.53           C  
ANISOU 2345  CA  ASP A 327    10846  13205   8448   3585  -3644  -3363       C  
ATOM   2346  C   ASP A 327      40.670   3.992 -28.385  1.00 85.02           C  
ANISOU 2346  C   ASP A 327    11089  12703   8510   3575  -3424  -3058       C  
ATOM   2347  O   ASP A 327      40.895   3.495 -27.275  1.00 76.56           O  
ANISOU 2347  O   ASP A 327     9910  11498   7679   3327  -3192  -3065       O  
ATOM   2348  CB  ASP A 327      38.191   3.728 -28.606  1.00 89.85           C  
ANISOU 2348  CB  ASP A 327    10952  14110   9077   3742  -3781  -3584       C  
ATOM   2349  CG  ASP A 327      37.029   3.273 -29.470  1.00115.18           C  
ANISOU 2349  CG  ASP A 327    13814  17806  12144   3772  -4032  -3902       C  
ATOM   2350  OD1 ASP A 327      37.195   3.187 -30.706  1.00121.56           O  
ANISOU 2350  OD1 ASP A 327    14801  18645  12740   3827  -4161  -3879       O  
ATOM   2351  OD2 ASP A 327      35.946   2.996 -28.914  1.00120.79           O  
ANISOU 2351  OD2 ASP A 327    14060  18869  12965   3711  -4064  -4164       O  
ATOM   2352  N   PRO A 328      41.402   4.995 -28.853  1.00 83.04           N  
ANISOU 2352  N   PRO A 328    11229  12226   8097   3812  -3487  -2787       N  
ATOM   2353  CA  PRO A 328      42.582   5.456 -28.120  1.00 73.04           C  
ANISOU 2353  CA  PRO A 328    10260  10552   6941   3744  -3270  -2507       C  
ATOM   2354  C   PRO A 328      42.220   6.383 -26.970  1.00 83.84           C  
ANISOU 2354  C   PRO A 328    11568  11843   8443   3942  -3282  -2451       C  
ATOM   2355  O   PRO A 328      41.169   7.029 -26.956  1.00 89.92           O  
ANISOU 2355  O   PRO A 328    12172  12836   9157   4254  -3503  -2565       O  
ATOM   2356  CB  PRO A 328      43.374   6.212 -29.191  1.00 76.50           C  
ANISOU 2356  CB  PRO A 328    11130  10826   7110   3900  -3357  -2262       C  
ATOM   2357  CG  PRO A 328      42.313   6.775 -30.080  1.00 79.54           C  
ANISOU 2357  CG  PRO A 328    11464  11498   7260   4245  -3695  -2359       C  
ATOM   2358  CD  PRO A 328      41.207   5.740 -30.108  1.00 79.97           C  
ANISOU 2358  CD  PRO A 328    11049  11945   7392   4129  -3763  -2717       C  
ATOM   2359  N   VAL A 329      43.120   6.435 -25.988  1.00 83.39           N  
ANISOU 2359  N   VAL A 329    11645  11479   8561   3772  -3046  -2290       N  
ATOM   2360  CA  VAL A 329      43.090   7.536 -25.039  1.00 88.95           C  
ANISOU 2360  CA  VAL A 329    12437  12021   9339   3982  -3057  -2174       C  
ATOM   2361  C   VAL A 329      43.507   8.797 -25.780  1.00 88.22           C  
ANISOU 2361  C   VAL A 329    12763  11731   9028   4274  -3227  -1939       C  
ATOM   2362  O   VAL A 329      44.426   8.776 -26.613  1.00 81.07           O  
ANISOU 2362  O   VAL A 329    12152  10672   7979   4168  -3185  -1764       O  
ATOM   2363  CB  VAL A 329      43.991   7.251 -23.819  1.00 81.83           C  
ANISOU 2363  CB  VAL A 329    11584  10850   8657   3709  -2774  -2064       C  
ATOM   2364  CG1 VAL A 329      44.053   5.762 -23.534  1.00 89.01           C  
ANISOU 2364  CG1 VAL A 329    12254  11851   9717   3335  -2583  -2211       C  
ATOM   2365  CG2 VAL A 329      45.397   7.815 -23.997  1.00 71.83           C  
ANISOU 2365  CG2 VAL A 329    10739   9221   7332   3654  -2679  -1767       C  
ATOM   2366  N   VAL A 330      42.787   9.889 -25.549  1.00 84.31           N  
ANISOU 2366  N   VAL A 330    12298  11252   8482   4651  -3428  -1945       N  
ATOM   2367  CA  VAL A 330      43.062  11.140 -26.240  1.00 87.43           C  
ANISOU 2367  CA  VAL A 330    13134  11429   8656   4952  -3621  -1719       C  
ATOM   2368  C   VAL A 330      43.333  12.220 -25.202  1.00 76.55           C  
ANISOU 2368  C   VAL A 330    11961   9733   7391   5063  -3560  -1592       C  
ATOM   2369  O   VAL A 330      42.640  12.306 -24.181  1.00 81.23           O  
ANISOU 2369  O   VAL A 330    12284  10433   8146   5168  -3546  -1762       O  
ATOM   2370  CB  VAL A 330      41.927  11.537 -27.214  1.00 86.73           C  
ANISOU 2370  CB  VAL A 330    12962  11590   8402   5247  -3858  -1844       C  
ATOM   2371  CG1 VAL A 330      41.393  10.306 -27.956  1.00 87.74           C  
ANISOU 2371  CG1 VAL A 330    12750  12126   8460   5136  -3940  -2071       C  
ATOM   2372  CG2 VAL A 330      40.806  12.287 -26.523  1.00 91.95           C  
ANISOU 2372  CG2 VAL A 330    13424  12353   9160   5536  -3937  -2009       C  
ATOM   2373  N   LEU A 331      44.382  13.001 -25.443  1.00 70.75           N  
ANISOU 2373  N   LEU A 331    11686   8620   6575   4965  -3476  -1310       N  
ATOM   2374  CA  LEU A 331      44.760  14.128 -24.601  1.00 80.86           C  
ANISOU 2374  CA  LEU A 331    13223   9565   7936   4972  -3389  -1185       C  
ATOM   2375  C   LEU A 331      44.736  15.380 -25.465  1.00 85.39           C  
ANISOU 2375  C   LEU A 331    14193   9938   8313   5112  -3498  -1032       C  
ATOM   2376  O   LEU A 331      45.488  15.473 -26.441  1.00 85.23           O  
ANISOU 2376  O   LEU A 331    14469   9789   8126   4983  -3484   -830       O  
ATOM   2377  CB  LEU A 331      46.148  13.926 -23.986  1.00 69.09           C  
ANISOU 2377  CB  LEU A 331    11913   7795   6543   4656  -3175   -992       C  
ATOM   2378  CG  LEU A 331      46.376  12.764 -23.012  1.00 73.68           C  
ANISOU 2378  CG  LEU A 331    12151   8491   7353   4427  -2989  -1114       C  
ATOM   2379  CD1 LEU A 331      46.615  11.431 -23.732  1.00 74.74           C  
ANISOU 2379  CD1 LEU A 331    12078   8846   7474   4156  -2876  -1183       C  
ATOM   2380  CD2 LEU A 331      47.524  13.090 -22.058  1.00 80.26           C  
ANISOU 2380  CD2 LEU A 331    13179   9005   8313   4189  -2787   -949       C  
ATOM   2381  N   THR A 332      43.878  16.333 -25.108  1.00 86.88           N  
ANISOU 2381  N   THR A 332    14395  10107   8508   5375  -3607  -1132       N  
ATOM   2382  CA  THR A 332      43.703  17.572 -25.854  1.00 96.45           C  
ANISOU 2382  CA  THR A 332    15986  11122   9541   5559  -3744  -1013       C  
ATOM   2383  C   THR A 332      44.166  18.740 -24.996  1.00 92.99           C  
ANISOU 2383  C   THR A 332    15855  10321   9156   5520  -3680   -906       C  
ATOM   2384  O   THR A 332      43.747  18.868 -23.841  1.00 80.67           O  
ANISOU 2384  O   THR A 332    14099   8807   7744   5592  -3646  -1060       O  
ATOM   2385  CB  THR A 332      42.240  17.756 -26.268  1.00108.73           C  
ANISOU 2385  CB  THR A 332    17316  12970  11025   5945  -3966  -1240       C  
ATOM   2386  OG1 THR A 332      41.396  17.565 -25.125  1.00125.62           O  
ANISOU 2386  OG1 THR A 332    19065  15330  13333   6078  -3958  -1500       O  
ATOM   2387  CG2 THR A 332      41.862  16.745 -27.328  1.00 85.17           C  
ANISOU 2387  CG2 THR A 332    14096  10321   7943   5956  -4052  -1320       C  
ATOM   2388  N   PHE A 333      45.023  19.590 -25.563  1.00 89.40           N  
ANISOU 2388  N   PHE A 333    15876   9522   8569   5392  -3664   -649       N  
ATOM   2389  CA  PHE A 333      45.644  20.694 -24.841  1.00 86.59           C  
ANISOU 2389  CA  PHE A 333    15853   8797   8249   5286  -3599   -526       C  
ATOM   2390  C   PHE A 333      45.396  22.003 -25.578  1.00 99.95           C  
ANISOU 2390  C   PHE A 333    17977  10248   9752   5482  -3769   -416       C  
ATOM   2391  O   PHE A 333      45.708  22.117 -26.768  1.00105.59           O  
ANISOU 2391  O   PHE A 333    18943  10893  10285   5437  -3818   -244       O  
ATOM   2392  CB  PHE A 333      47.154  20.464 -24.681  1.00 94.64           C  
ANISOU 2392  CB  PHE A 333    17054   9599   9307   4852  -3383   -303       C  
ATOM   2393  CG  PHE A 333      47.507  19.145 -24.047  1.00101.80           C  
ANISOU 2393  CG  PHE A 333    17585  10711  10384   4660  -3223   -384       C  
ATOM   2394  CD1 PHE A 333      46.859  18.719 -22.906  1.00 95.95           C  
ANISOU 2394  CD1 PHE A 333    16479  10148   9828   4759  -3199   -605       C  
ATOM   2395  CD2 PHE A 333      48.482  18.330 -24.598  1.00 99.58           C  
ANISOU 2395  CD2 PHE A 333    17326  10448  10064   4386  -3097   -239       C  
ATOM   2396  CE1 PHE A 333      47.173  17.508 -22.314  1.00 97.23           C  
ANISOU 2396  CE1 PHE A 333    16321  10474  10146   4585  -3059   -673       C  
ATOM   2397  CE2 PHE A 333      48.805  17.115 -24.012  1.00104.44           C  
ANISOU 2397  CE2 PHE A 333    17622  11227  10831   4236  -2966   -317       C  
ATOM   2398  CZ  PHE A 333      48.148  16.705 -22.867  1.00 98.16           C  
ANISOU 2398  CZ  PHE A 333    16482  10579  10235   4334  -2950   -530       C  
ATOM   2399  N   GLN A 334      44.837  22.985 -24.871  1.00105.36           N  
ANISOU 2399  N   GLN A 334    18760  10805  10466   5701  -3862   -515       N  
ATOM   2400  CA  GLN A 334      44.721  24.344 -25.382  1.00100.91           C  
ANISOU 2400  CA  GLN A 334    18670   9935   9737   5872  -4019   -402       C  
ATOM   2401  C   GLN A 334      45.981  25.128 -25.037  1.00100.29           C  
ANISOU 2401  C   GLN A 334    19014   9435   9658   5532  -3889   -173       C  
ATOM   2402  O   GLN A 334      46.486  25.049 -23.913  1.00101.26           O  
ANISOU 2402  O   GLN A 334    19036   9498   9942   5334  -3743   -208       O  
ATOM   2403  CB  GLN A 334      43.492  25.047 -24.802  1.00102.60           C  
ANISOU 2403  CB  GLN A 334    18801  10218   9966   6301  -4199   -634       C  
ATOM   2404  CG  GLN A 334      42.156  24.471 -25.251  1.00111.61           C  
ANISOU 2404  CG  GLN A 334    19552  11781  11074   6671  -4361   -870       C  
ATOM   2405  CD  GLN A 334      41.762  23.217 -24.490  1.00120.12           C  
ANISOU 2405  CD  GLN A 334    20040  13263  12337   6614  -4246  -1093       C  
ATOM   2406  OE1 GLN A 334      42.385  22.164 -24.633  1.00114.99           O  
ANISOU 2406  OE1 GLN A 334    19215  12724  11753   6322  -4096  -1030       O  
ATOM   2407  NE2 GLN A 334      40.720  23.327 -23.674  1.00124.48           N  
ANISOU 2407  NE2 GLN A 334    20289  14042  12965   6897  -4317  -1360       N  
ATOM   2408  N   HIS A 335      46.483  25.889 -26.007  1.00 98.51           N  
ANISOU 2408  N   HIS A 335    19259   8929   9243   5453  -3945     60       N  
ATOM   2409  CA  HIS A 335      47.769  26.556 -25.850  1.00 98.53           C  
ANISOU 2409  CA  HIS A 335    19660   8556   9223   5068  -3811    294       C  
ATOM   2410  C   HIS A 335      47.824  27.768 -26.771  1.00106.58           C  
ANISOU 2410  C   HIS A 335    21238   9243  10015   5142  -3959    483       C  
ATOM   2411  O   HIS A 335      47.005  27.922 -27.680  1.00107.59           O  
ANISOU 2411  O   HIS A 335    21435   9451   9992   5456  -4147    468       O  
ATOM   2412  CB  HIS A 335      48.924  25.592 -26.144  1.00 94.47           C  
ANISOU 2412  CB  HIS A 335    19039   8124   8733   4637  -3587    450       C  
ATOM   2413  CG  HIS A 335      48.856  24.959 -27.500  1.00103.14           C  
ANISOU 2413  CG  HIS A 335    20121   9406   9661   4652  -3621    547       C  
ATOM   2414  ND1 HIS A 335      49.335  25.578 -28.634  1.00114.48           N  
ANISOU 2414  ND1 HIS A 335    21992  10641  10864   4538  -3655    794       N  
ATOM   2415  CD2 HIS A 335      48.367  23.762 -27.903  1.00 99.93           C  
ANISOU 2415  CD2 HIS A 335    19323   9375   9271   4759  -3628    429       C  
ATOM   2416  CE1 HIS A 335      49.141  24.792 -29.678  1.00 98.47           C  
ANISOU 2416  CE1 HIS A 335    19835   8871   8709   4583  -3681    825       C  
ATOM   2417  NE2 HIS A 335      48.554  23.684 -29.262  1.00 94.97           N  
ANISOU 2417  NE2 HIS A 335    18893   8776   8416   4719  -3670    599       N  
ATOM   2418  N   GLN A 336      48.827  28.643 -26.520  1.00113.94           N  
ANISOU 2418  N   GLN A 336    22580   9793  10917   4832  -3876    667       N  
ATOM   2419  CA  GLN A 336      49.049  29.757 -27.436  1.00129.87           C  
ANISOU 2419  CA  GLN A 336    25172  11466  12706   4821  -3990    885       C  
ATOM   2420  C   GLN A 336      50.106  29.368 -28.458  1.00126.91           C  
ANISOU 2420  C   GLN A 336    24953  11078  12191   4417  -3840   1155       C  
ATOM   2421  O   GLN A 336      51.164  28.843 -28.082  1.00135.31           O  
ANISOU 2421  O   GLN A 336    25895  12170  13345   4002  -3612   1231       O  
ATOM   2422  CB  GLN A 336      49.466  31.024 -26.682  1.00137.56           C  
ANISOU 2422  CB  GLN A 336    26554  12020  13693   4720  -4010    930       C  
ATOM   2423  CG  GLN A 336      50.866  31.040 -26.074  1.00137.40           C  
ANISOU 2423  CG  GLN A 336    26613  11834  13760   4181  -3772   1063       C  
ATOM   2424  CD  GLN A 336      51.133  32.304 -25.268  1.00143.52           C  
ANISOU 2424  CD  GLN A 336    27770  12212  14548   4123  -3822   1067       C  
ATOM   2425  OE1 GLN A 336      50.239  32.830 -24.602  1.00143.28           O  
ANISOU 2425  OE1 GLN A 336    27734  12136  14568   4496  -3979    876       O  
ATOM   2426  NE2 GLN A 336      52.364  32.800 -25.332  1.00146.41           N  
ANISOU 2426  NE2 GLN A 336    28472  12301  14858   3650  -3689   1278       N  
ATOM   2427  N   PRO A 337      49.844  29.567 -29.748  1.00123.65           N  
ANISOU 2427  N   PRO A 337    24784  10652  11546   4532  -3959   1298       N  
ATOM   2428  CA  PRO A 337      50.754  29.045 -30.777  1.00127.15           C  
ANISOU 2428  CA  PRO A 337    25311  11171  11831   4169  -3808   1537       C  
ATOM   2429  C   PRO A 337      52.088  29.782 -30.816  1.00129.70           C  
ANISOU 2429  C   PRO A 337    26061  11153  12069   3673  -3646   1796       C  
ATOM   2430  O   PRO A 337      52.158  30.996 -30.613  1.00137.24           O  
ANISOU 2430  O   PRO A 337    27449  11729  12968   3670  -3734   1868       O  
ATOM   2431  CB  PRO A 337      49.969  29.249 -32.079  1.00131.58           C  
ANISOU 2431  CB  PRO A 337    26059  11787  12146   4479  -4018   1608       C  
ATOM   2432  CG  PRO A 337      48.952  30.316 -31.758  1.00125.88           C  
ANISOU 2432  CG  PRO A 337    25560  10847  11420   4919  -4276   1487       C  
ATOM   2433  CD  PRO A 337      48.606  30.128 -30.317  1.00121.73           C  
ANISOU 2433  CD  PRO A 337    24682  10397  11172   5035  -4243   1220       C  
ATOM   2434  N   GLN A 338      53.155  29.024 -31.081  1.00113.85           N  
ANISOU 2434  N   GLN A 338    23924   9294  10040   3243  -3407   1929       N  
ATOM   2435  CA  GLN A 338      54.482  29.584 -31.356  1.00117.88           C  
ANISOU 2435  CA  GLN A 338    24801   9565  10422   2719  -3227   2193       C  
ATOM   2436  C   GLN A 338      55.127  28.817 -32.509  1.00121.33           C  
ANISOU 2436  C   GLN A 338    25191  10255  10655   2450  -3073   2378       C  
ATOM   2437  O   GLN A 338      56.249  28.318 -32.394  1.00132.44           O  
ANISOU 2437  O   GLN A 338    26482  11765  12074   2011  -2824   2467       O  
ATOM   2438  CB  GLN A 338      55.365  29.546 -30.105  1.00127.70           C  
ANISOU 2438  CB  GLN A 338    25906  10729  11886   2383  -3043   2137       C  
ATOM   2439  CG  GLN A 338      55.613  28.148 -29.494  1.00131.31           C  
ANISOU 2439  CG  GLN A 338    25794  11553  12544   2309  -2879   1989       C  
ATOM   2440  CD  GLN A 338      54.411  27.612 -28.718  1.00121.26           C  
ANISOU 2440  CD  GLN A 338    24120  10470  11483   2777  -3019   1691       C  
ATOM   2441  OE1 GLN A 338      53.616  26.841 -29.257  1.00119.03           O  
ANISOU 2441  OE1 GLN A 338    23585  10471  11171   3067  -3104   1595       O  
ATOM   2442  NE2 GLN A 338      54.276  28.020 -27.450  1.00114.08           N  
ANISOU 2442  NE2 GLN A 338    23145   9425  10773   2835  -3040   1538       N  
ATOM   2443  N   PRO A 339      54.453  28.735 -33.657  1.00128.28           N  
ANISOU 2443  N   PRO A 339    26166  11252  11321   2702  -3217   2437       N  
ATOM   2444  CA  PRO A 339      54.799  27.722 -34.666  1.00141.30           C  
ANISOU 2444  CA  PRO A 339    27634  13260  12794   2556  -3094   2528       C  
ATOM   2445  C   PRO A 339      55.771  28.166 -35.750  1.00151.91           C  
ANISOU 2445  C   PRO A 339    29373  14521  13823   2140  -2954   2843       C  
ATOM   2446  O   PRO A 339      55.917  27.445 -36.742  1.00142.12           O  
ANISOU 2446  O   PRO A 339    28034  13589  12377   2074  -2883   2920       O  
ATOM   2447  CB  PRO A 339      53.428  27.426 -35.284  1.00144.19           C  
ANISOU 2447  CB  PRO A 339    27872  13820  13094   3085  -3353   2393       C  
ATOM   2448  CG  PRO A 339      52.768  28.773 -35.304  1.00147.04           C  
ANISOU 2448  CG  PRO A 339    28666  13806  13396   3353  -3589   2432       C  
ATOM   2449  CD  PRO A 339      53.310  29.552 -34.104  1.00139.07           C  
ANISOU 2449  CD  PRO A 339    27807  12452  12579   3156  -3512   2412       C  
ATOM   2450  N   LYS A 340      56.432  29.316 -35.598  1.00171.56           N  
ANISOU 2450  N   LYS A 340    32303  16627  16253   1848  -2907   3018       N  
ATOM   2451  CA  LYS A 340      57.307  29.799 -36.659  1.00178.06           C  
ANISOU 2451  CA  LYS A 340    33520  17377  16758   1439  -2773   3322       C  
ATOM   2452  C   LYS A 340      58.470  28.844 -36.887  1.00166.65           C  
ANISOU 2452  C   LYS A 340    31797  16276  15248    971  -2447   3392       C  
ATOM   2453  O   LYS A 340      58.826  28.552 -38.034  1.00178.58           O  
ANISOU 2453  O   LYS A 340    33382  18006  16466    799  -2344   3556       O  
ATOM   2454  CB  LYS A 340      57.817  31.201 -36.326  1.00187.75           C  
ANISOU 2454  CB  LYS A 340    35260  18118  17958   1182  -2780   3470       C  
ATOM   2455  N   ASN A 341      59.055  28.321 -35.808  1.00139.80           N  
ANISOU 2455  N   ASN A 341    28062  12954  12103    778  -2283   3259       N  
ATOM   2456  CA  ASN A 341      60.227  27.463 -35.919  1.00130.13           C  
ANISOU 2456  CA  ASN A 341    26574  12050  10821    328  -1965   3312       C  
ATOM   2457  C   ASN A 341      60.078  26.163 -35.135  1.00125.19           C  
ANISOU 2457  C   ASN A 341    25390  11734  10441    488  -1911   3067       C  
ATOM   2458  O   ASN A 341      61.085  25.523 -34.825  1.00117.83           O  
ANISOU 2458  O   ASN A 341    24220  11009   9540    129  -1655   3067       O  
ATOM   2459  CB  ASN A 341      61.474  28.215 -35.451  1.00136.94           C  
ANISOU 2459  CB  ASN A 341    27644  12693  11694   -233  -1757   3450       C  
ATOM   2460  CG  ASN A 341      61.328  28.752 -34.037  1.00134.71           C  
ANISOU 2460  CG  ASN A 341    27352  12100  11732   -159  -1853   3301       C  
ATOM   2461  OD1 ASN A 341      60.263  29.244 -33.655  1.00138.91           O  
ANISOU 2461  OD1 ASN A 341    27994  12402  12384    282  -2116   3185       O  
ATOM   2462  ND2 ASN A 341      62.396  28.659 -33.254  1.00129.28           N  
ANISOU 2462  ND2 ASN A 341    26518  11432  11169   -587  -1638   3291       N  
ATOM   2463  N   VAL A 342      58.853  25.750 -34.809  1.00113.72           N  
ANISOU 2463  N   VAL A 342    23721  10333   9153   1009  -2141   2854       N  
ATOM   2464  CA  VAL A 342      58.652  24.574 -33.970  1.00109.43           C  
ANISOU 2464  CA  VAL A 342    22677  10043   8858   1165  -2105   2616       C  
ATOM   2465  C   VAL A 342      57.365  23.870 -34.380  1.00105.76           C  
ANISOU 2465  C   VAL A 342    21982   9807   8395   1669  -2318   2439       C  
ATOM   2466  O   VAL A 342      56.412  24.493 -34.858  1.00104.51           O  
ANISOU 2466  O   VAL A 342    22027   9525   8159   1993  -2551   2441       O  
ATOM   2467  CB  VAL A 342      58.639  24.944 -32.462  1.00111.34           C  
ANISOU 2467  CB  VAL A 342    22830  10041   9433   1189  -2135   2478       C  
ATOM   2468  CG1 VAL A 342      57.266  25.417 -32.020  1.00103.40           C  
ANISOU 2468  CG1 VAL A 342    21838   8870   8577   1702  -2424   2304       C  
ATOM   2469  CG2 VAL A 342      59.096  23.772 -31.605  1.00 94.45           C  
ANISOU 2469  CG2 VAL A 342    20239   8151   7497   1096  -1976   2330       C  
ATOM   2470  N   THR A 343      57.356  22.551 -34.198  1.00 96.90           N  
ANISOU 2470  N   THR A 343    20435   9031   7352   1726  -2238   2277       N  
ATOM   2471  CA  THR A 343      56.187  21.709 -34.387  1.00 95.13           C  
ANISOU 2471  CA  THR A 343    19906   9062   7176   2161  -2420   2058       C  
ATOM   2472  C   THR A 343      55.895  21.003 -33.069  1.00 90.15           C  
ANISOU 2472  C   THR A 343    18880   8489   6885   2304  -2422   1817       C  
ATOM   2473  O   THR A 343      56.792  20.807 -32.244  1.00 90.25           O  
ANISOU 2473  O   THR A 343    18804   8453   7033   2026  -2238   1833       O  
ATOM   2474  CB  THR A 343      56.412  20.683 -35.517  1.00100.04           C  
ANISOU 2474  CB  THR A 343    20394  10083   7535   2091  -2328   2066       C  
ATOM   2475  OG1 THR A 343      56.913  21.355 -36.679  1.00111.43           O  
ANISOU 2475  OG1 THR A 343    22213  11482   8645   1868  -2268   2319       O  
ATOM   2476  CG2 THR A 343      55.116  19.965 -35.884  1.00 94.41           C  
ANISOU 2476  CG2 THR A 343    19419   9620   6834   2532  -2554   1844       C  
ATOM   2477  N   LEU A 344      54.632  20.646 -32.858  1.00 89.15           N  
ANISOU 2477  N   LEU A 344    18511   8475   6888   2728  -2632   1593       N  
ATOM   2478  CA  LEU A 344      54.203  19.978 -31.638  1.00 84.93           C  
ANISOU 2478  CA  LEU A 344    17590   8017   6662   2886  -2647   1354       C  
ATOM   2479  C   LEU A 344      54.027  18.490 -31.903  1.00 88.00           C  
ANISOU 2479  C   LEU A 344    17600   8800   7037   2953  -2614   1191       C  
ATOM   2480  O   LEU A 344      53.326  18.103 -32.844  1.00 89.39           O  
ANISOU 2480  O   LEU A 344    17712   9198   7053   3151  -2741   1123       O  
ATOM   2481  CB  LEU A 344      52.900  20.583 -31.116  1.00 86.10           C  
ANISOU 2481  CB  LEU A 344    17689   8058   6965   3290  -2883   1184       C  
ATOM   2482  CG  LEU A 344      52.963  22.070 -30.767  1.00 89.30           C  
ANISOU 2482  CG  LEU A 344    18478   8068   7383   3275  -2942   1296       C  
ATOM   2483  CD1 LEU A 344      51.700  22.493 -30.039  1.00 89.89           C  
ANISOU 2483  CD1 LEU A 344    18425   8102   7625   3684  -3145   1072       C  
ATOM   2484  CD2 LEU A 344      54.201  22.385 -29.940  1.00 87.73           C  
ANISOU 2484  CD2 LEU A 344    18391   7654   7290   2874  -2734   1412       C  
ATOM   2485  N   GLN A 345      54.662  17.660 -31.077  1.00 78.07           N  
ANISOU 2485  N   GLN A 345    16101   7625   5936   2789  -2454   1120       N  
ATOM   2486  CA  GLN A 345      54.601  16.211 -31.228  1.00 75.34           C  
ANISOU 2486  CA  GLN A 345    15419   7631   5578   2828  -2412    950       C  
ATOM   2487  C   GLN A 345      54.227  15.568 -29.903  1.00 83.16           C  
ANISOU 2487  C   GLN A 345    16063   8646   6888   2950  -2429    745       C  
ATOM   2488  O   GLN A 345      54.943  15.723 -28.907  1.00 70.71           O  
ANISOU 2488  O   GLN A 345    14461   6904   5502   2755  -2285    786       O  
ATOM   2489  CB  GLN A 345      55.929  15.643 -31.727  1.00 74.80           C  
ANISOU 2489  CB  GLN A 345    15415   7702   5305   2473  -2163   1070       C  
ATOM   2490  CG  GLN A 345      55.935  14.125 -31.757  1.00 99.64           C  
ANISOU 2490  CG  GLN A 345    18048  11207   8602   2438  -2026    789       C  
ATOM   2491  CD  GLN A 345      57.214  13.554 -32.325  1.00108.53           C  
ANISOU 2491  CD  GLN A 345    19099  12523   9613   2086  -1726    822       C  
ATOM   2492  OE1 GLN A 345      58.272  14.180 -32.259  1.00111.00           O  
ANISOU 2492  OE1 GLN A 345    19608  12712   9855   1792  -1555   1021       O  
ATOM   2493  NE2 GLN A 345      57.123  12.360 -32.899  1.00114.17           N  
ANISOU 2493  NE2 GLN A 345    19523  13553  10302   2110  -1658    609       N  
ATOM   2494  N   CYS A 346      53.120  14.831 -29.900  1.00 81.71           N  
ANISOU 2494  N   CYS A 346    15575   8694   6779   3231  -2583    507       N  
ATOM   2495  CA  CYS A 346      52.729  14.062 -28.728  1.00 67.57           C  
ANISOU 2495  CA  CYS A 346    13345   6991   5336   3264  -2530    265       C  
ATOM   2496  C   CYS A 346      53.735  12.953 -28.452  1.00 64.66           C  
ANISOU 2496  C   CYS A 346    12685   6759   5123   2925  -2234    186       C  
ATOM   2497  O   CYS A 346      54.071  12.167 -29.342  1.00 93.40           O  
ANISOU 2497  O   CYS A 346    16238  10617   8632   2812  -2139    137       O  
ATOM   2498  CB  CYS A 346      51.343  13.469 -28.944  1.00 68.03           C  
ANISOU 2498  CB  CYS A 346    13118   7313   5416   3573  -2735     17       C  
ATOM   2499  SG  CYS A 346      50.090  14.715 -29.194  1.00 75.04           S  
ANISOU 2499  SG  CYS A 346    14172   8102   6237   3947  -3011     16       S  
ATOM   2500  N   VAL A 347      54.208  12.886 -27.205  1.00 71.91           N  
ANISOU 2500  N   VAL A 347    13458   7551   6312   2786  -2098    163       N  
ATOM   2501  CA  VAL A 347      55.169  11.876 -26.779  1.00 66.52           C  
ANISOU 2501  CA  VAL A 347    12502   6973   5800   2509  -1842     89       C  
ATOM   2502  C   VAL A 347      54.813  11.407 -25.374  1.00 60.16           C  
ANISOU 2502  C   VAL A 347    11402   6140   5316   2540  -1816    -68       C  
ATOM   2503  O   VAL A 347      54.047  12.049 -24.653  1.00 65.04           O  
ANISOU 2503  O   VAL A 347    12059   6635   6019   2724  -1955    -90       O  
ATOM   2504  CB  VAL A 347      56.627  12.397 -26.804  1.00 68.30           C  
ANISOU 2504  CB  VAL A 347    12923   7072   5955   2199  -1649    300       C  
ATOM   2505  CG1 VAL A 347      57.088  12.664 -28.229  1.00 62.69           C  
ANISOU 2505  CG1 VAL A 347    12468   6446   4906   2105  -1617    446       C  
ATOM   2506  CG2 VAL A 347      56.769  13.647 -25.935  1.00 60.40           C  
ANISOU 2506  CG2 VAL A 347    12178   5754   5017   2181  -1708    452       C  
ATOM   2507  N   PHE A 348      55.385  10.269 -24.986  1.00 54.99           N  
ANISOU 2507  N   PHE A 348    10465   5604   4826   2367  -1635   -181       N  
ATOM   2508  CA  PHE A 348      55.266   9.767 -23.624  1.00 56.87           C  
ANISOU 2508  CA  PHE A 348    10459   5804   5345   2340  -1577   -293       C  
ATOM   2509  C   PHE A 348      56.647   9.391 -23.112  1.00 56.10           C  
ANISOU 2509  C   PHE A 348    10291   5670   5353   2084  -1366   -231       C  
ATOM   2510  O   PHE A 348      57.512   8.954 -23.875  1.00 56.93           O  
ANISOU 2510  O   PHE A 348    10390   5882   5360   1948  -1241   -203       O  
ATOM   2511  CB  PHE A 348      54.315   8.564 -23.522  1.00 56.15           C  
ANISOU 2511  CB  PHE A 348    10061   5902   5372   2427  -1608   -533       C  
ATOM   2512  CG  PHE A 348      54.784   7.346 -24.259  1.00 55.33           C  
ANISOU 2512  CG  PHE A 348     9823   5958   5241   2308  -1490   -631       C  
ATOM   2513  CD1 PHE A 348      54.485   7.178 -25.598  1.00 53.09           C  
ANISOU 2513  CD1 PHE A 348     9605   5827   4739   2375  -1560   -672       C  
ATOM   2514  CD2 PHE A 348      55.502   6.356 -23.609  1.00 57.26           C  
ANISOU 2514  CD2 PHE A 348     9891   6199   5667   2154  -1324   -693       C  
ATOM   2515  CE1 PHE A 348      54.909   6.052 -26.281  1.00 53.12           C  
ANISOU 2515  CE1 PHE A 348     9499   5974   4710   2280  -1451   -790       C  
ATOM   2516  CE2 PHE A 348      55.928   5.226 -24.289  1.00 49.57           C  
ANISOU 2516  CE2 PHE A 348     8816   5348   4671   2083  -1225   -804       C  
ATOM   2517  CZ  PHE A 348      55.628   5.074 -25.624  1.00 51.39           C  
ANISOU 2517  CZ  PHE A 348     9110   5728   4687   2141  -1283   -863       C  
ATOM   2518  N   TRP A 349      56.850   9.578 -21.812  1.00 51.46           N  
ANISOU 2518  N   TRP A 349     9642   4956   4953   2033  -1332   -222       N  
ATOM   2519  CA  TRP A 349      58.160   9.354 -21.223  1.00 48.95           C  
ANISOU 2519  CA  TRP A 349     9256   4612   4732   1812  -1166   -160       C  
ATOM   2520  C   TRP A 349      58.451   7.863 -21.119  1.00 57.12           C  
ANISOU 2520  C   TRP A 349    10013   5798   5893   1769  -1051   -304       C  
ATOM   2521  O   TRP A 349      57.648   7.099 -20.576  1.00 61.54           O  
ANISOU 2521  O   TRP A 349    10410   6385   6587   1857  -1088   -444       O  
ATOM   2522  CB  TRP A 349      58.229  10.005 -19.847  1.00 53.61           C  
ANISOU 2522  CB  TRP A 349     9878   5028   5465   1785  -1189   -119       C  
ATOM   2523  CG  TRP A 349      59.579   9.974 -19.210  1.00 55.40           C  
ANISOU 2523  CG  TRP A 349    10049   5232   5767   1560  -1053    -47       C  
ATOM   2524  CD1 TRP A 349      60.002   9.126 -18.227  1.00 50.76           C  
ANISOU 2524  CD1 TRP A 349     9237   4691   5359   1505   -976   -121       C  
ATOM   2525  CD2 TRP A 349      60.682  10.841 -19.495  1.00 63.29           C  
ANISOU 2525  CD2 TRP A 349    11218   6171   6657   1353   -988    112       C  
ATOM   2526  NE1 TRP A 349      61.302   9.411 -17.882  1.00 49.88           N  
ANISOU 2526  NE1 TRP A 349     9117   4576   5259   1306   -884    -31       N  
ATOM   2527  CE2 TRP A 349      61.741  10.464 -18.641  1.00 52.85           C  
ANISOU 2527  CE2 TRP A 349     9719   4897   5465   1188   -880    106       C  
ATOM   2528  CE3 TRP A 349      60.877  11.900 -20.387  1.00 55.31           C  
ANISOU 2528  CE3 TRP A 349    10505   5073   5439   1276  -1015    265       C  
ATOM   2529  CZ2 TRP A 349      62.976  11.108 -18.654  1.00 49.58           C  
ANISOU 2529  CZ2 TRP A 349     9367   4483   4990    935   -792    223       C  
ATOM   2530  CZ3 TRP A 349      62.103  12.540 -20.398  1.00 60.80           C  
ANISOU 2530  CZ3 TRP A 349    11298   5736   6068    995   -911    399       C  
ATOM   2531  CH2 TRP A 349      63.139  12.138 -19.540  1.00 59.66           C  
ANISOU 2531  CH2 TRP A 349    10924   5678   6066    820   -798    366       C  
ATOM   2532  N   VAL A 350      59.595   7.447 -21.648  1.00 49.05           N  
ANISOU 2532  N   VAL A 350     8945   4875   4818   1633   -911   -275       N  
ATOM   2533  CA  VAL A 350      60.063   6.075 -21.532  1.00 57.76           C  
ANISOU 2533  CA  VAL A 350     9820   6087   6039   1615   -803   -406       C  
ATOM   2534  C   VAL A 350      61.419   6.089 -20.841  1.00 60.15           C  
ANISOU 2534  C   VAL A 350    10036   6390   6427   1469   -683   -337       C  
ATOM   2535  O   VAL A 350      62.239   6.984 -21.076  1.00 60.21           O  
ANISOU 2535  O   VAL A 350    10144   6407   6327   1328   -630   -203       O  
ATOM   2536  CB  VAL A 350      60.146   5.380 -22.908  1.00 58.77           C  
ANISOU 2536  CB  VAL A 350     9928   6387   6015   1644   -753   -497       C  
ATOM   2537  CG1 VAL A 350      61.041   6.162 -23.845  1.00 61.99           C  
ANISOU 2537  CG1 VAL A 350    10475   6878   6201   1525   -670   -360       C  
ATOM   2538  CG2 VAL A 350      60.653   3.956 -22.754  1.00 64.97           C  
ANISOU 2538  CG2 VAL A 350    10512   7243   6932   1654   -652   -649       C  
ATOM   2539  N   GLU A 351      61.647   5.106 -19.974  1.00 57.66           N  
ANISOU 2539  N   GLU A 351     9544   6068   6297   1494   -648   -425       N  
ATOM   2540  CA  GLU A 351      62.939   4.912 -19.337  1.00 65.96           C  
ANISOU 2540  CA  GLU A 351    10469   7162   7431   1401   -554   -391       C  
ATOM   2541  C   GLU A 351      63.400   3.480 -19.570  1.00 73.16           C  
ANISOU 2541  C   GLU A 351    11211   8173   8414   1485   -479   -532       C  
ATOM   2542  O   GLU A 351      62.607   2.594 -19.892  1.00 76.12           O  
ANISOU 2542  O   GLU A 351    11580   8522   8818   1591   -510   -656       O  
ATOM   2543  CB  GLU A 351      62.879   5.212 -17.834  1.00 79.40           C  
ANISOU 2543  CB  GLU A 351    12158   8727   9283   1375   -613   -342       C  
ATOM   2544  CG  GLU A 351      61.920   4.324 -17.059  1.00 85.87           C  
ANISOU 2544  CG  GLU A 351    12925   9457  10244   1488   -673   -440       C  
ATOM   2545  CD  GLU A 351      61.779   4.745 -15.610  1.00 80.73           C  
ANISOU 2545  CD  GLU A 351    12287   8690   9695   1457   -726   -387       C  
ATOM   2546  OE1 GLU A 351      61.466   5.927 -15.361  1.00 82.89           O  
ANISOU 2546  OE1 GLU A 351    12688   8890   9917   1421   -783   -314       O  
ATOM   2547  OE2 GLU A 351      61.988   3.895 -14.719  1.00 86.10           O  
ANISOU 2547  OE2 GLU A 351    12875   9345  10493   1478   -716   -419       O  
ATOM   2548  N   ASP A 352      64.697   3.256 -19.405  1.00 93.90           N  
ANISOU 2548  N   ASP A 352    13697  10914  11065   1440   -385   -526       N  
ATOM   2549  CA  ASP A 352      65.252   1.914 -19.539  1.00102.58           C  
ANISOU 2549  CA  ASP A 352    14644  12092  12240   1565   -325   -667       C  
ATOM   2550  C   ASP A 352      65.580   1.353 -18.164  1.00106.10           C  
ANISOU 2550  C   ASP A 352    15002  12438  12874   1621   -373   -665       C  
ATOM   2551  O   ASP A 352      66.527   1.832 -17.519  1.00108.43           O  
ANISOU 2551  O   ASP A 352    15200  12805  13195   1547   -358   -589       O  
ATOM   2552  CB  ASP A 352      66.505   1.927 -20.419  1.00101.43           C  
ANISOU 2552  CB  ASP A 352    14369  12199  11973   1526   -186   -697       C  
ATOM   2553  CG  ASP A 352      67.084   0.535 -20.637  1.00110.40           C  
ANISOU 2553  CG  ASP A 352    15352  13417  13176   1710   -130   -874       C  
ATOM   2554  OD1 ASP A 352      67.879   0.082 -19.792  1.00105.08           O  
ANISOU 2554  OD1 ASP A 352    14533  12760  12631   1782   -135   -891       O  
ATOM   2555  OD2 ASP A 352      66.751  -0.103 -21.657  1.00116.61           O  
ANISOU 2555  OD2 ASP A 352    16177  14249  13880   1800    -92  -1005       O  
ATOM   2556  N   PRO A 353      64.839   0.361 -17.666  1.00113.32           N  
ANISOU 2556  N   PRO A 353    15956  13193  13908   1731   -434   -741       N  
ATOM   2557  CA  PRO A 353      65.293  -0.357 -16.471  1.00116.50           C  
ANISOU 2557  CA  PRO A 353    16299  13506  14459   1805   -473   -735       C  
ATOM   2558  C   PRO A 353      66.601  -1.070 -16.769  1.00126.30           C  
ANISOU 2558  C   PRO A 353    17382  14893  15714   1929   -410   -815       C  
ATOM   2559  O   PRO A 353      66.785  -1.626 -17.853  1.00135.48           O  
ANISOU 2559  O   PRO A 353    18515  16148  16815   2014   -341   -939       O  
ATOM   2560  CB  PRO A 353      64.153  -1.344 -16.190  1.00101.88           C  
ANISOU 2560  CB  PRO A 353    14563  11455  12693   1865   -528   -810       C  
ATOM   2561  CG  PRO A 353      63.470  -1.516 -17.503  1.00104.01           C  
ANISOU 2561  CG  PRO A 353    14882  11769  12869   1872   -499   -920       C  
ATOM   2562  CD  PRO A 353      63.585  -0.191 -18.203  1.00111.08           C  
ANISOU 2562  CD  PRO A 353    15777  12814  13614   1775   -472   -838       C  
ATOM   2563  N   ALA A 354      67.515  -1.022 -15.800  1.00132.97           N  
ANISOU 2563  N   ALA A 354    18113  15780  16628   1952   -442   -757       N  
ATOM   2564  CA  ALA A 354      68.897  -1.513 -15.867  1.00139.91           C  
ANISOU 2564  CA  ALA A 354    18784  16853  17524   2084   -403   -826       C  
ATOM   2565  C   ALA A 354      69.820  -0.553 -16.605  1.00139.79           C  
ANISOU 2565  C   ALA A 354    18595  17138  17379   1942   -293   -811       C  
ATOM   2566  O   ALA A 354      70.979  -0.909 -16.864  1.00147.23           O  
ANISOU 2566  O   ALA A 354    19313  18317  18311   2041   -233   -899       O  
ATOM   2567  CB  ALA A 354      69.021  -2.902 -16.507  1.00139.78           C  
ANISOU 2567  CB  ALA A 354    18767  16802  17543   2325   -378   -998       C  
ATOM   2568  N   SER A 355      69.358   0.649 -16.951  1.00132.12           N  
ANISOU 2568  N   SER A 355    17725  16171  16303   1714   -264   -707       N  
ATOM   2569  CA  SER A 355      70.241   1.645 -17.545  1.00123.99           C  
ANISOU 2569  CA  SER A 355    16576  15396  15138   1517   -158   -660       C  
ATOM   2570  C   SER A 355      70.830   2.589 -16.505  1.00128.91           C  
ANISOU 2570  C   SER A 355    17134  16053  15792   1335   -209   -544       C  
ATOM   2571  O   SER A 355      71.995   2.983 -16.626  1.00133.44           O  
ANISOU 2571  O   SER A 355    17495  16893  16312   1214   -133   -550       O  
ATOM   2572  CB  SER A 355      69.493   2.464 -18.599  1.00128.54           C  
ANISOU 2572  CB  SER A 355    17346  15941  15552   1365   -104   -600       C  
ATOM   2573  OG  SER A 355      68.416   3.174 -18.011  1.00132.51           O  
ANISOU 2573  OG  SER A 355    18072  16194  16084   1289   -215   -487       O  
ATOM   2574  N   SER A 356      70.044   2.957 -15.488  1.00113.75           N  
ANISOU 2574  N   SER A 356    15383  13889  13949   1302   -331   -453       N  
ATOM   2575  CA  SER A 356      70.419   3.996 -14.522  1.00109.30           C  
ANISOU 2575  CA  SER A 356    14821  13316  13393   1107   -391   -349       C  
ATOM   2576  C   SER A 356      70.782   5.299 -15.230  1.00105.76           C  
ANISOU 2576  C   SER A 356    14421  12966  12796    820   -305   -268       C  
ATOM   2577  O   SER A 356      71.540   6.121 -14.711  1.00108.50           O  
ANISOU 2577  O   SER A 356    14700  13401  13125    608   -313   -214       O  
ATOM   2578  CB  SER A 356      71.565   3.537 -13.616  1.00115.22           C  
ANISOU 2578  CB  SER A 356    15317  14235  14225   1173   -439   -390       C  
ATOM   2579  OG  SER A 356      72.776   3.430 -14.344  1.00123.80           O  
ANISOU 2579  OG  SER A 356    16134  15653  15251   1141   -327   -466       O  
ATOM   2580  N   SER A 357      70.237   5.485 -16.428  1.00 97.96           N  
ANISOU 2580  N   SER A 357    13573  11958  11690    797   -229   -258       N  
ATOM   2581  CA  SER A 357      70.506   6.640 -17.264  1.00 87.20           C  
ANISOU 2581  CA  SER A 357    12318  10661  10152    531   -140   -162       C  
ATOM   2582  C   SER A 357      69.220   7.425 -17.477  1.00 79.12           C  
ANISOU 2582  C   SER A 357    11643   9353   9067    513   -220    -64       C  
ATOM   2583  O   SER A 357      68.116   6.919 -17.251  1.00 68.71           O  
ANISOU 2583  O   SER A 357    10421   7860   7825    719   -311   -105       O  
ATOM   2584  CB  SER A 357      71.092   6.218 -18.616  1.00 83.84           C  
ANISOU 2584  CB  SER A 357    11761  10507   9588    526     24   -230       C  
ATOM   2585  OG  SER A 357      71.186   7.326 -19.492  1.00 98.23           O  
ANISOU 2585  OG  SER A 357    13756  12360  11208    258    111   -111       O  
ATOM   2586  N   THR A 358      69.377   8.671 -17.918  1.00 73.56           N  
ANISOU 2586  N   THR A 358    11127   8608   8217    262   -189     62       N  
ATOM   2587  CA  THR A 358      68.228   9.533 -18.156  1.00 71.43           C  
ANISOU 2587  CA  THR A 358    11207   8062   7870    272   -283    159       C  
ATOM   2588  C   THR A 358      67.309   8.931 -19.215  1.00 66.36           C  
ANISOU 2588  C   THR A 358    10642   7422   7150    478   -283    110       C  
ATOM   2589  O   THR A 358      67.746   8.211 -20.117  1.00 61.23           O  
ANISOU 2589  O   THR A 358     9847   6992   6424    510   -168     40       O  
ATOM   2590  CB  THR A 358      68.685  10.927 -18.588  1.00 69.51           C  
ANISOU 2590  CB  THR A 358    11193   7761   7456    -42   -242    314       C  
ATOM   2591  OG1 THR A 358      67.540  11.720 -18.924  1.00 74.39           O  
ANISOU 2591  OG1 THR A 358    12179   8100   7986     30   -354    405       O  
ATOM   2592  CG2 THR A 358      69.612  10.841 -19.795  1.00 78.27           C  
ANISOU 2592  CG2 THR A 358    12198   9156   8386   -222    -57    333       C  
ATOM   2593  N   GLY A 359      66.017   9.225 -19.090  1.00 59.42           N  
ANISOU 2593  N   GLY A 359     9977   6316   6283    627   -417    127       N  
ATOM   2594  CA  GLY A 359      65.023   8.724 -20.013  1.00 52.04           C  
ANISOU 2594  CA  GLY A 359     9113   5385   5276    819   -452     68       C  
ATOM   2595  C   GLY A 359      64.960   9.539 -21.292  1.00 58.27           C  
ANISOU 2595  C   GLY A 359    10142   6185   5813    723   -427    182       C  
ATOM   2596  O   GLY A 359      65.808  10.386 -21.576  1.00 64.91           O  
ANISOU 2596  O   GLY A 359    11085   7052   6527    476   -347    309       O  
ATOM   2597  N   SER A 360      63.923   9.267 -22.079  1.00 53.30           N  
ANISOU 2597  N   SER A 360     9612   5543   5098    909   -502    137       N  
ATOM   2598  CA  SER A 360      63.732   9.952 -23.350  1.00 54.90           C  
ANISOU 2598  CA  SER A 360    10069   5758   5032    864   -506    246       C  
ATOM   2599  C   SER A 360      62.251   9.943 -23.695  1.00 60.82           C  
ANISOU 2599  C   SER A 360    10955   6408   5745   1121   -686    200       C  
ATOM   2600  O   SER A 360      61.455   9.232 -23.080  1.00 57.51           O  
ANISOU 2600  O   SER A 360    10382   5967   5502   1302   -766     57       O  
ATOM   2601  CB  SER A 360      64.547   9.298 -24.467  1.00 54.96           C  
ANISOU 2601  CB  SER A 360     9949   6051   4882    778   -332    200       C  
ATOM   2602  OG  SER A 360      64.049   8.003 -24.747  1.00 63.81           O  
ANISOU 2602  OG  SER A 360    10879   7292   6073    990   -340      3       O  
ATOM   2603  N   TRP A 361      61.896  10.739 -24.698  1.00 55.18           N  
ANISOU 2603  N   TRP A 361    10531   5650   4784   1127   -750    322       N  
ATOM   2604  CA  TRP A 361      60.518  10.840 -25.151  1.00 63.50           C  
ANISOU 2604  CA  TRP A 361    11718   6647   5764   1387   -944    281       C  
ATOM   2605  C   TRP A 361      60.282   9.923 -26.341  1.00 67.41           C  
ANISOU 2605  C   TRP A 361    12120   7382   6111   1471   -915    166       C  
ATOM   2606  O   TRP A 361      61.130   9.806 -27.231  1.00 66.66           O  
ANISOU 2606  O   TRP A 361    12050   7447   5829   1317   -768    212       O  
ATOM   2607  CB  TRP A 361      60.177  12.280 -25.531  1.00 66.71           C  
ANISOU 2607  CB  TRP A 361    12539   6836   5973   1398  -1077    484       C  
ATOM   2608  CG  TRP A 361      60.286  13.250 -24.393  1.00 63.48           C  
ANISOU 2608  CG  TRP A 361    12271   6153   5695   1340  -1131    575       C  
ATOM   2609  CD1 TRP A 361      61.251  14.199 -24.216  1.00 59.01           C  
ANISOU 2609  CD1 TRP A 361    11920   5437   5063   1064  -1052    752       C  
ATOM   2610  CD2 TRP A 361      59.400  13.365 -23.273  1.00 55.89           C  
ANISOU 2610  CD2 TRP A 361    11247   5046   4942   1544  -1271    476       C  
ATOM   2611  NE1 TRP A 361      61.018  14.902 -23.058  1.00 58.46           N  
ANISOU 2611  NE1 TRP A 361    11946   5116   5151   1096  -1148    763       N  
ATOM   2612  CE2 TRP A 361      59.887  14.410 -22.461  1.00 56.46           C  
ANISOU 2612  CE2 TRP A 361    11522   4869   5061   1402  -1278    594       C  
ATOM   2613  CE3 TRP A 361      58.243  12.686 -22.878  1.00 54.31           C  
ANISOU 2613  CE3 TRP A 361    10834   4919   4882   1812  -1381    288       C  
ATOM   2614  CZ2 TRP A 361      59.258  14.793 -21.282  1.00 55.45           C  
ANISOU 2614  CZ2 TRP A 361    11397   4565   5105   1551  -1392    522       C  
ATOM   2615  CZ3 TRP A 361      57.619  13.070 -21.707  1.00 69.90           C  
ANISOU 2615  CZ3 TRP A 361    12791   6743   7024   1942  -1478    227       C  
ATOM   2616  CH2 TRP A 361      58.127  14.114 -20.923  1.00 57.29           C  
ANISOU 2616  CH2 TRP A 361    11406   4900   5462   1827  -1484    340       C  
ATOM   2617  N   SER A 362      59.122   9.274 -26.351  1.00 68.92           N  
ANISOU 2617  N   SER A 362    12196   7616   6376   1700  -1050      0       N  
ATOM   2618  CA  SER A 362      58.747   8.363 -27.419  1.00 61.44           C  
ANISOU 2618  CA  SER A 362    11161   6884   5299   1788  -1055   -147       C  
ATOM   2619  C   SER A 362      57.346   8.694 -27.909  1.00 61.33           C  
ANISOU 2619  C   SER A 362    11267   6866   5172   2024  -1294   -183       C  
ATOM   2620  O   SER A 362      56.454   8.999 -27.112  1.00 57.86           O  
ANISOU 2620  O   SER A 362    10795   6309   4880   2171  -1439   -218       O  
ATOM   2621  CB  SER A 362      58.807   6.901 -26.958  1.00 60.42           C  
ANISOU 2621  CB  SER A 362    10703   6859   5394   1802   -968   -375       C  
ATOM   2622  OG  SER A 362      58.404   6.025 -27.997  1.00 60.60           O  
ANISOU 2622  OG  SER A 362    10666   7067   5290   1880   -984   -541       O  
ATOM   2623  N   SER A 363      57.158   8.623 -29.226  1.00 59.39           N  
ANISOU 2623  N   SER A 363    11142   6776   4649   2071  -1336   -187       N  
ATOM   2624  CA  SER A 363      55.865   8.865 -29.853  1.00 60.99           C  
ANISOU 2624  CA  SER A 363    11439   7031   4704   2311  -1582   -237       C  
ATOM   2625  C   SER A 363      55.203   7.581 -30.335  1.00 67.26           C  
ANISOU 2625  C   SER A 363    11982   8055   5518   2393  -1619   -510       C  
ATOM   2626  O   SER A 363      54.206   7.646 -31.064  1.00 62.62           O  
ANISOU 2626  O   SER A 363    11440   7585   4765   2572  -1819   -582       O  
ATOM   2627  CB  SER A 363      56.017   9.844 -31.021  1.00 64.23           C  
ANISOU 2627  CB  SER A 363    12228   7437   4740   2321  -1651    -26       C  
ATOM   2628  OG  SER A 363      56.883   9.324 -32.017  1.00 91.00           O  
ANISOU 2628  OG  SER A 363    15632  11023   7921   2152  -1471    -30       O  
ATOM   2629  N   ALA A 364      55.728   6.422 -29.940  1.00 68.52           N  
ANISOU 2629  N   ALA A 364    11890   8273   5871   2269  -1446   -670       N  
ATOM   2630  CA  ALA A 364      55.216   5.151 -30.434  1.00 74.06           C  
ANISOU 2630  CA  ALA A 364    12397   9155   6587   2305  -1465   -936       C  
ATOM   2631  C   ALA A 364      53.754   4.973 -30.053  1.00 64.86           C  
ANISOU 2631  C   ALA A 364    11088   8019   5538   2460  -1676  -1090       C  
ATOM   2632  O   ALA A 364      53.376   5.145 -28.892  1.00 66.43           O  
ANISOU 2632  O   ALA A 364    11176   8092   5973   2481  -1702  -1086       O  
ATOM   2633  CB  ALA A 364      56.050   3.996 -29.880  1.00 74.20           C  
ANISOU 2633  CB  ALA A 364    12210   9155   6826   2167  -1255  -1064       C  
ATOM   2634  N   GLY A 365      52.933   4.630 -31.040  1.00 66.12           N  
ANISOU 2634  N   GLY A 365    11231   8375   5515   2561  -1826  -1240       N  
ATOM   2635  CA  GLY A 365      51.519   4.441 -30.792  1.00 61.66           C  
ANISOU 2635  CA  GLY A 365    10487   7907   5035   2695  -2033  -1415       C  
ATOM   2636  C   GLY A 365      50.775   5.695 -30.399  1.00 66.30           C  
ANISOU 2636  C   GLY A 365    11162   8430   5599   2899  -2226  -1281       C  
ATOM   2637  O   GLY A 365      49.672   5.603 -29.860  1.00 75.70           O  
ANISOU 2637  O   GLY A 365    12145   9697   6922   3007  -2363  -1426       O  
ATOM   2638  N   CYS A 366      51.346   6.870 -30.657  1.00 63.02           N  
ANISOU 2638  N   CYS A 366    11055   7876   5013   2952  -2238  -1016       N  
ATOM   2639  CA  CYS A 366      50.728   8.143 -30.308  1.00 64.07           C  
ANISOU 2639  CA  CYS A 366    11343   7889   5111   3173  -2429   -876       C  
ATOM   2640  C   CYS A 366      50.679   9.020 -31.550  1.00 73.53           C  
ANISOU 2640  C   CYS A 366    12888   9113   5935   3320  -2591   -708       C  
ATOM   2641  O   CYS A 366      51.727   9.391 -32.090  1.00 81.04           O  
ANISOU 2641  O   CYS A 366    14110   9973   6707   3170  -2458   -506       O  
ATOM   2642  CB  CYS A 366      51.501   8.847 -29.187  1.00 62.14           C  
ANISOU 2642  CB  CYS A 366    11208   7359   5046   3077  -2293   -689       C  
ATOM   2643  SG  CYS A 366      51.285   8.169 -27.515  1.00 75.68           S  
ANISOU 2643  SG  CYS A 366    12571   9015   7171   2988  -2176   -848       S  
ATOM   2644  N   GLU A 367      49.471   9.354 -31.993  1.00 69.73           N  
ANISOU 2644  N   GLU A 367    12397   8773   5325   3607  -2877   -791       N  
ATOM   2645  CA  GLU A 367      49.264  10.218 -33.147  1.00 73.31           C  
ANISOU 2645  CA  GLU A 367    13203   9249   5404   3802  -3085   -627       C  
ATOM   2646  C   GLU A 367      48.995  11.645 -32.688  1.00 74.65           C  
ANISOU 2646  C   GLU A 367    13638   9144   5582   4015  -3225   -421       C  
ATOM   2647  O   GLU A 367      48.311  11.867 -31.685  1.00 73.78           O  
ANISOU 2647  O   GLU A 367    13341   8980   5710   4170  -3302   -523       O  
ATOM   2648  CB  GLU A 367      48.097   9.719 -34.000  1.00 75.77           C  
ANISOU 2648  CB  GLU A 367    13338   9898   5554   4010  -3338   -855       C  
ATOM   2649  CG  GLU A 367      47.847  10.546 -35.255  1.00 88.71           C  
ANISOU 2649  CG  GLU A 367    15240  11540   6926   4134  -3457   -692       C  
ATOM   2650  CD  GLU A 367      46.504  10.250 -35.895  1.00 99.01           C  
ANISOU 2650  CD  GLU A 367    16284  13144   8189   4350  -3693   -920       C  
ATOM   2651  OE1 GLU A 367      45.787   9.369 -35.373  1.00105.29           O  
ANISOU 2651  OE1 GLU A 367    16680  14157   9166   4367  -3746  -1212       O  
ATOM   2652  OE2 GLU A 367      46.167  10.900 -36.912  1.00 95.48           O  
ANISOU 2652  OE2 GLU A 367    16033  12723   7524   4486  -3824   -808       O  
ATOM   2653  N   THR A 368      49.519  12.608 -33.438  1.00 77.13           N  
ANISOU 2653  N   THR A 368    14340   9273   5692   3967  -3198   -157       N  
ATOM   2654  CA  THR A 368      49.403  14.020 -33.108  1.00 78.95           C  
ANISOU 2654  CA  THR A 368    14843   9179   5976   4075  -3254     31       C  
ATOM   2655  C   THR A 368      48.540  14.727 -34.143  1.00 94.22           C  
ANISOU 2655  C   THR A 368    16923  11155   7722   4315  -3465     62       C  
ATOM   2656  O   THR A 368      48.728  14.537 -35.350  1.00 92.31           O  
ANISOU 2656  O   THR A 368    16810  11054   7210   4253  -3476    131       O  
ATOM   2657  CB  THR A 368      50.784  14.676 -33.049  1.00 78.68           C  
ANISOU 2657  CB  THR A 368    15181   8852   5862   3777  -3047    325       C  
ATOM   2658  OG1 THR A 368      51.609  13.979 -32.106  1.00 84.40           O  
ANISOU 2658  OG1 THR A 368    15759   9561   6748   3566  -2858    293       O  
ATOM   2659  CG2 THR A 368      50.668  16.138 -32.648  1.00 80.79           C  
ANISOU 2659  CG2 THR A 368    15741   8759   6196   3855  -3107    484       C  
ATOM   2660  N   VAL A 369      47.595  15.534 -33.671  1.00 92.74           N  
ANISOU 2660  N   VAL A 369    16716  10859   7661   4598  -3630     -1       N  
ATOM   2661  CA  VAL A 369      46.897  16.501 -34.508  1.00 90.56           C  
ANISOU 2661  CA  VAL A 369    16674  10525   7210   4843  -3830     74       C  
ATOM   2662  C   VAL A 369      47.097  17.869 -33.864  1.00 93.51           C  
ANISOU 2662  C   VAL A 369    17378  10488   7664   4884  -3826    232       C  
ATOM   2663  O   VAL A 369      46.623  18.124 -32.749  1.00 90.07           O  
ANISOU 2663  O   VAL A 369    16783   9977   7463   5021  -3849     92       O  
ATOM   2664  CB  VAL A 369      45.411  16.154 -34.698  1.00 98.90           C  
ANISOU 2664  CB  VAL A 369    17375  11902   8302   5191  -4068   -207       C  
ATOM   2665  CG1 VAL A 369      45.281  14.840 -35.442  1.00101.41           C  
ANISOU 2665  CG1 VAL A 369    17407  12612   8514   5099  -4073   -364       C  
ATOM   2666  CG2 VAL A 369      44.685  16.041 -33.385  1.00 91.06           C  
ANISOU 2666  CG2 VAL A 369    16035  10955   7607   5348  -4092   -441       C  
ATOM   2667  N   SER A 370      47.826  18.742 -34.551  1.00100.93           N  
ANISOU 2667  N   SER A 370    18781  11170   8396   4738  -3787    516       N  
ATOM   2668  CA  SER A 370      48.310  19.989 -33.964  1.00103.96           C  
ANISOU 2668  CA  SER A 370    19528  11134   8838   4664  -3740    689       C  
ATOM   2669  C   SER A 370      47.790  21.170 -34.776  1.00107.55           C  
ANISOU 2669  C   SER A 370    20368  11408   9088   4886  -3942    816       C  
ATOM   2670  O   SER A 370      48.462  21.658 -35.688  1.00113.55           O  
ANISOU 2670  O   SER A 370    21513  12027   9602   4701  -3902   1074       O  
ATOM   2671  CB  SER A 370      49.838  19.988 -33.892  1.00 96.10           C  
ANISOU 2671  CB  SER A 370    18756   9960   7797   4207  -3475    923       C  
ATOM   2672  OG  SER A 370      50.321  21.153 -33.246  1.00 94.35           O  
ANISOU 2672  OG  SER A 370    18858   9343   7649   4096  -3428   1064       O  
ATOM   2673  N   ARG A 371      46.589  21.631 -34.437  1.00112.51           N  
ANISOU 2673  N   ARG A 371    20893  12052   9805   5285  -4156    632       N  
ATOM   2674  CA  ARG A 371      46.110  22.890 -34.975  1.00116.23           C  
ANISOU 2674  CA  ARG A 371    21765  12286  10110   5529  -4356    743       C  
ATOM   2675  C   ARG A 371      46.823  24.043 -34.275  1.00116.84           C  
ANISOU 2675  C   ARG A 371    22242  11903  10250   5366  -4270    905       C  
ATOM   2676  O   ARG A 371      47.585  23.850 -33.322  1.00122.08           O  
ANISOU 2676  O   ARG A 371    22822  12464  11099   5092  -4068    905       O  
ATOM   2677  CB  ARG A 371      44.592  22.986 -34.834  1.00115.84           C  
ANISOU 2677  CB  ARG A 371    21456  12438  10121   6024  -4615    470       C  
ATOM   2678  CG  ARG A 371      43.878  21.931 -35.665  1.00129.52           C  
ANISOU 2678  CG  ARG A 371    22823  14628  11759   6165  -4723    317       C  
ATOM   2679  CD  ARG A 371      42.413  21.763 -35.304  1.00134.31           C  
ANISOU 2679  CD  ARG A 371    23027  15526  12481   6593  -4931    -12       C  
ATOM   2680  NE  ARG A 371      41.889  20.511 -35.846  1.00129.75           N  
ANISOU 2680  NE  ARG A 371    22005  15419  11876   6615  -4976   -197       N  
ATOM   2681  CZ  ARG A 371      40.620  20.124 -35.761  1.00127.40           C  
ANISOU 2681  CZ  ARG A 371    21285  15479  11643   6931  -5150   -496       C  
ATOM   2682  NH1 ARG A 371      39.727  20.897 -35.157  1.00134.15           N  
ANISOU 2682  NH1 ARG A 371    22097  16291  12583   7281  -5295   -645       N  
ATOM   2683  NH2 ARG A 371      40.246  18.963 -36.282  1.00112.77           N  
ANISOU 2683  NH2 ARG A 371    19046  14043   9758   6886  -5179   -659       N  
ATOM   2684  N   ASP A 372      46.577  25.257 -34.767  1.00114.69           N  
ANISOU 2684  N   ASP A 372    22420  11348   9810   5533  -4434   1043       N  
ATOM   2685  CA  ASP A 372      47.369  26.401 -34.331  1.00118.71           C  
ANISOU 2685  CA  ASP A 372    23389  11396  10318   5321  -4357   1234       C  
ATOM   2686  C   ASP A 372      47.280  26.597 -32.820  1.00118.61           C  
ANISOU 2686  C   ASP A 372    23199  11275  10594   5352  -4299   1046       C  
ATOM   2687  O   ASP A 372      48.306  26.684 -32.137  1.00110.94           O  
ANISOU 2687  O   ASP A 372    22304  10119   9730   4984  -4092   1138       O  
ATOM   2688  CB  ASP A 372      46.924  27.658 -35.080  1.00123.21           C  
ANISOU 2688  CB  ASP A 372    24469  11686  10661   5566  -4587   1376       C  
ATOM   2689  CG  ASP A 372      48.025  28.697 -35.187  1.00133.32           C  
ANISOU 2689  CG  ASP A 372    26318  12512  11824   5210  -4480   1674       C  
ATOM   2690  OD1 ASP A 372      49.213  28.310 -35.231  1.00133.62           O  
ANISOU 2690  OD1 ASP A 372    26379  12539  11851   4734  -4227   1837       O  
ATOM   2691  OD2 ASP A 372      47.700  29.903 -35.232  1.00139.98           O  
ANISOU 2691  OD2 ASP A 372    27590  13018  12577   5404  -4651   1739       O  
ATOM   2692  N   THR A 373      46.065  26.630 -32.271  1.00129.47           N  
ANISOU 2692  N   THR A 373    24308  12799  12087   5778  -4472    773       N  
ATOM   2693  CA  THR A 373      45.867  26.918 -30.856  1.00112.32           C  
ANISOU 2693  CA  THR A 373    21987  10541  10150   5845  -4436    588       C  
ATOM   2694  C   THR A 373      45.501  25.691 -30.027  1.00123.12           C  
ANISOU 2694  C   THR A 373    22740  12293  11748   5860  -4336    329       C  
ATOM   2695  O   THR A 373      45.302  25.816 -28.813  1.00105.37           O  
ANISOU 2695  O   THR A 373    20318  10027   9689   5908  -4295    165       O  
ATOM   2696  CB  THR A 373      44.787  27.996 -30.686  1.00117.48           C  
ANISOU 2696  CB  THR A 373    22820  11060  10756   6312  -4695    461       C  
ATOM   2697  OG1 THR A 373      44.931  28.622 -29.406  1.00127.61           O  
ANISOU 2697  OG1 THR A 373    24157  12128  12201   6286  -4641    373       O  
ATOM   2698  CG2 THR A 373      43.386  27.396 -30.797  1.00118.11           C  
ANISOU 2698  CG2 THR A 373    22447  11567  10865   6756  -4873    175       C  
ATOM   2699  N   GLN A 374      45.420  24.512 -30.639  1.00112.08           N  
ANISOU 2699  N   GLN A 374    21020  11239  10325   5808  -4297    290       N  
ATOM   2700  CA  GLN A 374      44.973  23.321 -29.931  1.00109.33           C  
ANISOU 2700  CA  GLN A 374    20099  11262  10179   5839  -4227     37       C  
ATOM   2701  C   GLN A 374      45.634  22.092 -30.537  1.00104.91           C  
ANISOU 2701  C   GLN A 374    19356  10920   9584   5554  -4084    112       C  
ATOM   2702  O   GLN A 374      45.747  21.976 -31.760  1.00101.47           O  
ANISOU 2702  O   GLN A 374    19076  10545   8932   5535  -4142    246       O  
ATOM   2703  CB  GLN A 374      43.445  23.195 -29.979  1.00106.77           C  
ANISOU 2703  CB  GLN A 374    19451  11254   9863   6303  -4450   -244       C  
ATOM   2704  CG  GLN A 374      42.904  21.835 -29.570  1.00106.80           C  
ANISOU 2704  CG  GLN A 374    18854  11702  10024   6317  -4398   -498       C  
ATOM   2705  CD  GLN A 374      41.415  21.863 -29.300  1.00103.70           C  
ANISOU 2705  CD  GLN A 374    18115  11614   9674   6743  -4590   -804       C  
ATOM   2706  OE1 GLN A 374      40.894  22.824 -28.734  1.00107.11           O  
ANISOU 2706  OE1 GLN A 374    18662  11911  10123   6991  -4688   -883       O  
ATOM   2707  NE2 GLN A 374      40.720  20.807 -29.703  1.00104.99           N  
ANISOU 2707  NE2 GLN A 374    17842  12207   9843   6825  -4647   -990       N  
ATOM   2708  N   THR A 375      46.069  21.180 -29.668  1.00 93.82           N  
ANISOU 2708  N   THR A 375    17632   9638   8378   5340  -3903     23       N  
ATOM   2709  CA  THR A 375      46.749  19.956 -30.068  1.00 88.80           C  
ANISOU 2709  CA  THR A 375    16811   9202   7726   5071  -3757     68       C  
ATOM   2710  C   THR A 375      46.165  18.773 -29.306  1.00 90.43           C  
ANISOU 2710  C   THR A 375    16478   9745   8137   5136  -3730   -206       C  
ATOM   2711  O   THR A 375      45.928  18.860 -28.097  1.00 89.20           O  
ANISOU 2711  O   THR A 375    16146   9560   8186   5176  -3686   -340       O  
ATOM   2712  CB  THR A 375      48.257  20.048 -29.806  1.00 86.49           C  
ANISOU 2712  CB  THR A 375    16764   8651   7445   4645  -3523    302       C  
ATOM   2713  OG1 THR A 375      48.790  21.186 -30.493  1.00 90.15           O  
ANISOU 2713  OG1 THR A 375    17733   8805   7714   4550  -3543    555       O  
ATOM   2714  CG2 THR A 375      48.968  18.791 -30.299  1.00 83.55           C  
ANISOU 2714  CG2 THR A 375    16224   8505   7017   4395  -3381    343       C  
ATOM   2715  N   SER A 376      45.944  17.666 -30.015  1.00 84.51           N  
ANISOU 2715  N   SER A 376    15473   9320   7316   5127  -3756   -291       N  
ATOM   2716  CA  SER A 376      45.340  16.465 -29.456  1.00 81.87           C  
ANISOU 2716  CA  SER A 376    14629   9330   7147   5170  -3751   -558       C  
ATOM   2717  C   SER A 376      46.240  15.263 -29.694  1.00 89.06           C  
ANISOU 2717  C   SER A 376    15442  10358   8039   4866  -3599   -514       C  
ATOM   2718  O   SER A 376      46.783  15.083 -30.791  1.00 79.47           O  
ANISOU 2718  O   SER A 376    14421   9169   6607   4742  -3582   -374       O  
ATOM   2719  CB  SER A 376      43.961  16.193 -30.063  1.00 84.78           C  
ANISOU 2719  CB  SER A 376    14711  10053   7449   5484  -3972   -788       C  
ATOM   2720  OG  SER A 376      43.234  17.396 -30.203  1.00110.63           O  
ANISOU 2720  OG  SER A 376    18174  13207  10655   5787  -4137   -786       O  
ATOM   2721  N   CYS A 377      46.369  14.433 -28.664  1.00 79.39           N  
ANISOU 2721  N   CYS A 377    13917   9221   7025   4757  -3491   -644       N  
ATOM   2722  CA  CYS A 377      47.244  13.268 -28.659  1.00 75.25           C  
ANISOU 2722  CA  CYS A 377    13295   8788   6507   4482  -3346   -629       C  
ATOM   2723  C   CYS A 377      46.385  12.014 -28.640  1.00 78.92           C  
ANISOU 2723  C   CYS A 377    13303   9651   7032   4543  -3433   -926       C  
ATOM   2724  O   CYS A 377      45.571  11.836 -27.733  1.00 81.50           O  
ANISOU 2724  O   CYS A 377    13307  10098   7561   4654  -3468  -1125       O  
ATOM   2725  CB  CYS A 377      48.167  13.301 -27.442  1.00 72.24           C  
ANISOU 2725  CB  CYS A 377    12962   8162   6323   4282  -3156   -532       C  
ATOM   2726  SG  CYS A 377      49.202  14.768 -27.379  1.00 77.19           S  
ANISOU 2726  SG  CYS A 377    14096   8341   6893   4133  -3046   -220       S  
ATOM   2727  N   LEU A 378      46.573  11.144 -29.628  1.00 88.02           N  
ANISOU 2727  N   LEU A 378    14393  11009   8043   4390  -3401   -984       N  
ATOM   2728  CA  LEU A 378      45.799   9.914 -29.751  1.00 77.82           C  
ANISOU 2728  CA  LEU A 378    12660  10072   6838   4326  -3414  -1292       C  
ATOM   2729  C   LEU A 378      46.757   8.745 -29.580  1.00 69.87           C  
ANISOU 2729  C   LEU A 378    11538   9037   5971   3920  -3108  -1330       C  
ATOM   2730  O   LEU A 378      47.523   8.423 -30.494  1.00 72.54           O  
ANISOU 2730  O   LEU A 378    12050   9378   6134   3773  -3025  -1250       O  
ATOM   2731  CB  LEU A 378      45.070   9.849 -31.093  1.00 77.71           C  
ANISOU 2731  CB  LEU A 378    12662  10336   6528   4526  -3673  -1379       C  
ATOM   2732  CG  LEU A 378      43.887  10.805 -31.286  1.00 86.79           C  
ANISOU 2732  CG  LEU A 378    13764  11543   7670   4867  -3876  -1418       C  
ATOM   2733  CD1 LEU A 378      44.351  12.212 -31.653  1.00 87.05           C  
ANISOU 2733  CD1 LEU A 378    14271  11228   7577   4978  -3881  -1114       C  
ATOM   2734  CD2 LEU A 378      42.910  10.269 -32.326  1.00 84.66           C  
ANISOU 2734  CD2 LEU A 378    13255  11646   7267   4960  -4047  -1628       C  
ATOM   2735  N   CYS A 379      46.718   8.117 -28.408  1.00 74.84           N  
ANISOU 2735  N   CYS A 379    11889   9646   6902   3756  -2945  -1453       N  
ATOM   2736  CA  CYS A 379      47.621   7.028 -28.065  1.00 76.48           C  
ANISOU 2736  CA  CYS A 379    12003   9786   7271   3412  -2670  -1483       C  
ATOM   2737  C   CYS A 379      46.835   5.747 -27.825  1.00 69.91           C  
ANISOU 2737  C   CYS A 379    10787   9183   6592   3281  -2648  -1781       C  
ATOM   2738  O   CYS A 379      45.777   5.769 -27.190  1.00 76.94           O  
ANISOU 2738  O   CYS A 379    11420  10217   7598   3376  -2743  -1936       O  
ATOM   2739  CB  CYS A 379      48.442   7.362 -26.817  1.00 81.79           C  
ANISOU 2739  CB  CYS A 379    12742  10181   8155   3287  -2479  -1333       C  
ATOM   2740  SG  CYS A 379      49.462   8.850 -26.929  1.00 74.86           S  
ANISOU 2740  SG  CYS A 379    12320   8993   7129   3350  -2473   -989       S  
ATOM   2741  N   ASN A 380      47.368   4.627 -28.318  1.00 68.47           N  
ANISOU 2741  N   ASN A 380    10573   9033   6409   3052  -2515  -1869       N  
ATOM   2742  CA  ASN A 380      46.734   3.323 -28.164  1.00 76.46           C  
ANISOU 2742  CA  ASN A 380    11284  10209   7557   2873  -2481  -2146       C  
ATOM   2743  C   ASN A 380      47.229   2.565 -26.936  1.00 78.78           C  
ANISOU 2743  C   ASN A 380    11477  10319   8137   2629  -2247  -2154       C  
ATOM   2744  O   ASN A 380      47.276   1.326 -26.959  1.00 85.99           O  
ANISOU 2744  O   ASN A 380    12284  11244   9143   2412  -2148  -2316       O  
ATOM   2745  CB  ASN A 380      46.946   2.485 -29.428  1.00 71.11           C  
ANISOU 2745  CB  ASN A 380    10659   9656   6705   2781  -2492  -2272       C  
ATOM   2746  CG  ASN A 380      48.412   2.356 -29.814  1.00 62.18           C  
ANISOU 2746  CG  ASN A 380     9786   8332   5507   2676  -2299  -2107       C  
ATOM   2747  OD1 ASN A 380      49.309   2.621 -29.018  1.00 72.15           O  
ANISOU 2747  OD1 ASN A 380    11139   9369   6907   2608  -2131  -1931       O  
ATOM   2748  ND2 ASN A 380      48.657   1.943 -31.052  1.00 63.87           N  
ANISOU 2748  ND2 ASN A 380    10103   8668   5496   2662  -2324  -2182       N  
ATOM   2749  N   HIS A 381      47.598   3.270 -25.867  1.00 80.44           N  
ANISOU 2749  N   HIS A 381    11743  10344   8476   2664  -2168  -1984       N  
ATOM   2750  CA  HIS A 381      48.171   2.634 -24.686  1.00 75.44           C  
ANISOU 2750  CA  HIS A 381    11054   9529   8083   2452  -1958  -1958       C  
ATOM   2751  C   HIS A 381      48.304   3.666 -23.577  1.00 74.05           C  
ANISOU 2751  C   HIS A 381    10928   9211   7997   2548  -1936  -1796       C  
ATOM   2752  O   HIS A 381      48.432   4.864 -23.844  1.00 74.54           O  
ANISOU 2752  O   HIS A 381    11170   9219   7933   2746  -2038  -1648       O  
ATOM   2753  CB  HIS A 381      49.546   2.027 -24.994  1.00 72.71           C  
ANISOU 2753  CB  HIS A 381    10878   9009   7740   2305  -1786  -1866       C  
ATOM   2754  CG  HIS A 381      50.572   3.047 -25.374  1.00 70.97           C  
ANISOU 2754  CG  HIS A 381    10913   8668   7383   2398  -1762  -1627       C  
ATOM   2755  ND1 HIS A 381      50.638   3.594 -26.636  1.00 81.92           N  
ANISOU 2755  ND1 HIS A 381    12463  10150   8511   2517  -1867  -1574       N  
ATOM   2756  CD2 HIS A 381      51.557   3.635 -24.655  1.00 61.65           C  
ANISOU 2756  CD2 HIS A 381     9860   7290   6276   2363  -1647  -1425       C  
ATOM   2757  CE1 HIS A 381      51.626   4.470 -26.681  1.00 80.27           C  
ANISOU 2757  CE1 HIS A 381    12481   9796   8222   2529  -1801  -1342       C  
ATOM   2758  NE2 HIS A 381      52.199   4.514 -25.492  1.00 69.77           N  
ANISOU 2758  NE2 HIS A 381    11120   8293   7096   2432  -1671  -1258       N  
ATOM   2759  N   LEU A 382      48.263   3.188 -22.336  1.00 62.31           N  
ANISOU 2759  N   LEU A 382     9309   7652   6714   2401  -1809  -1827       N  
ATOM   2760  CA  LEU A 382      48.710   3.977 -21.189  1.00 68.48           C  
ANISOU 2760  CA  LEU A 382    10171   8257   7590   2435  -1740  -1668       C  
ATOM   2761  C   LEU A 382      49.317   3.044 -20.146  1.00 63.95           C  
ANISOU 2761  C   LEU A 382     9551   7543   7203   2196  -1547  -1652       C  
ATOM   2762  O   LEU A 382      50.278   3.389 -19.462  1.00 66.59           O  
ANISOU 2762  O   LEU A 382    10017   7687   7597   2160  -1453  -1489       O  
ATOM   2763  CB  LEU A 382      47.570   4.820 -20.583  1.00 70.32           C  
ANISOU 2763  CB  LEU A 382    10270   8618   7831   2626  -1860  -1741       C  
ATOM   2764  CG  LEU A 382      46.284   4.265 -19.961  1.00 71.64           C  
ANISOU 2764  CG  LEU A 382    10105   9026   8090   2575  -1867  -1969       C  
ATOM   2765  CD1 LEU A 382      46.512   3.611 -18.612  1.00 82.79           C  
ANISOU 2765  CD1 LEU A 382    11435  10343   9679   2339  -1673  -1962       C  
ATOM   2766  CD2 LEU A 382      45.286   5.397 -19.812  1.00 72.02           C  
ANISOU 2766  CD2 LEU A 382    10062   9231   8071   2880  -2036  -2034       C  
ATOM   2767  OXT LEU A 382      48.868   1.912 -19.977  1.00 63.73           O  
ANISOU 2767  OXT LEU A 382     9370   7583   7260   2028  -1491  -1801       O  
TER    2768      LEU A 382                                                      
ATOM   2769  N   THR B 383      51.895   6.254 -16.857  1.00 55.63           N  
ANISOU 2769  N   THR B 383     7281   4835   9020   2103  -3125    -10       N  
ATOM   2770  CA  THR B 383      52.594   6.781 -18.024  1.00 63.56           C  
ANISOU 2770  CA  THR B 383     8547   5780   9824   2101  -3108   -215       C  
ATOM   2771  C   THR B 383      52.477   8.300 -18.071  1.00 54.56           C  
ANISOU 2771  C   THR B 383     7907   4678   8145   2194  -3092   -228       C  
ATOM   2772  O   THR B 383      51.398   8.854 -17.869  1.00 57.74           O  
ANISOU 2772  O   THR B 383     8442   5159   8337   2403  -3116   -236       O  
ATOM   2773  CB  THR B 383      52.047   6.176 -19.332  1.00 55.66           C  
ANISOU 2773  CB  THR B 383     7415   4764   8969   2215  -3147   -524       C  
ATOM   2774  OG1 THR B 383      52.263   4.760 -19.329  1.00 62.30           O  
ANISOU 2774  OG1 THR B 383     7853   5477  10341   2101  -3115   -548       O  
ATOM   2775  CG2 THR B 383      52.740   6.786 -20.544  1.00 55.80           C  
ANISOU 2775  CG2 THR B 383     7731   4764   8707   2237  -3110   -711       C  
ATOM   2776  N   TYR B 384      53.595   8.970 -18.334  1.00 54.44           N  
ANISOU 2776  N   TYR B 384     8168   4595   7923   2040  -3025   -220       N  
ATOM   2777  CA  TYR B 384      53.651  10.427 -18.360  1.00 54.85           C  
ANISOU 2777  CA  TYR B 384     8753   4592   7495   2068  -2962   -224       C  
ATOM   2778  C   TYR B 384      53.644  10.904 -19.807  1.00 60.09           C  
ANISOU 2778  C   TYR B 384     9676   5206   7951   2216  -2924   -406       C  
ATOM   2779  O   TYR B 384      54.612  10.692 -20.545  1.00 62.57           O  
ANISOU 2779  O   TYR B 384     9962   5488   8325   2068  -2870   -469       O  
ATOM   2780  CB  TYR B 384      54.883  10.929 -17.613  1.00 55.04           C  
ANISOU 2780  CB  TYR B 384     8924   4587   7403   1731  -2903    -86       C  
ATOM   2781  CG  TYR B 384      54.708  10.863 -16.117  1.00 71.52           C  
ANISOU 2781  CG  TYR B 384    10908   6773   9492   1631  -2942     96       C  
ATOM   2782  CD1 TYR B 384      55.059   9.724 -15.402  1.00 71.67           C  
ANISOU 2782  CD1 TYR B 384    10444   6921   9868   1513  -3005    273       C  
ATOM   2783  CD2 TYR B 384      54.172  11.935 -15.422  1.00 62.40           C  
ANISOU 2783  CD2 TYR B 384    10160   5580   7968   1684  -2892    101       C  
ATOM   2784  CE1 TYR B 384      54.887   9.665 -14.031  1.00 73.76           C  
ANISOU 2784  CE1 TYR B 384    10618   7326  10083   1436  -3038    470       C  
ATOM   2785  CE2 TYR B 384      53.995  11.884 -14.060  1.00 70.50           C  
ANISOU 2785  CE2 TYR B 384    11111   6734   8941   1598  -2913    245       C  
ATOM   2786  CZ  TYR B 384      54.354  10.750 -13.368  1.00 71.23           C  
ANISOU 2786  CZ  TYR B 384    10705   7007   9353   1467  -2997    439       C  
ATOM   2787  OH  TYR B 384      54.177  10.709 -12.008  1.00 83.10           O  
ANISOU 2787  OH  TYR B 384    12139   8684  10750   1391  -3015    611       O  
ATOM   2788  N   PHE B 385      52.549  11.550 -20.203  1.00 56.34           N  
ANISOU 2788  N   PHE B 385     9435   4759   7212   2535  -2941   -464       N  
ATOM   2789  CA  PHE B 385      52.378  12.081 -21.547  1.00 57.58           C  
ANISOU 2789  CA  PHE B 385     9858   4924   7097   2744  -2917   -586       C  
ATOM   2790  C   PHE B 385      52.728  13.561 -21.571  1.00 60.18           C  
ANISOU 2790  C   PHE B 385    10806   5055   7005   2761  -2760   -487       C  
ATOM   2791  O   PHE B 385      52.398  14.304 -20.642  1.00 65.46           O  
ANISOU 2791  O   PHE B 385    11736   5615   7520   2800  -2700   -383       O  
ATOM   2792  CB  PHE B 385      50.942  11.890 -22.041  1.00 58.62           C  
ANISOU 2792  CB  PHE B 385     9838   5262   7174   3120  -3042   -678       C  
ATOM   2793  CG  PHE B 385      50.482  10.463 -22.037  1.00 70.00           C  
ANISOU 2793  CG  PHE B 385    10698   6862   9037   3059  -3180   -809       C  
ATOM   2794  CD1 PHE B 385      49.895   9.916 -20.907  1.00 63.90           C  
ANISOU 2794  CD1 PHE B 385     9617   6131   8531   3020  -3222   -707       C  
ATOM   2795  CD2 PHE B 385      50.633   9.670 -23.163  1.00 61.91           C  
ANISOU 2795  CD2 PHE B 385     9461   5926   8136   3025  -3240  -1042       C  
ATOM   2796  CE1 PHE B 385      49.469   8.602 -20.899  1.00 73.45           C  
ANISOU 2796  CE1 PHE B 385    10320   7426  10160   2929  -3313   -813       C  
ATOM   2797  CE2 PHE B 385      50.208   8.356 -23.164  1.00 59.20           C  
ANISOU 2797  CE2 PHE B 385     8630   5659   8205   2931  -3337  -1198       C  
ATOM   2798  CZ  PHE B 385      49.625   7.820 -22.030  1.00 65.10           C  
ANISOU 2798  CZ  PHE B 385     9077   6404   9253   2873  -3369  -1072       C  
ATOM   2799  N   ALA B 386      53.390  13.982 -22.645  1.00 64.59           N  
ANISOU 2799  N   ALA B 386    11618   5548   7373   2727  -2666   -528       N  
ATOM   2800  CA  ALA B 386      53.740  15.379 -22.841  1.00 61.65           C  
ANISOU 2800  CA  ALA B 386    11870   4935   6618   2728  -2479   -426       C  
ATOM   2801  C   ALA B 386      53.776  15.657 -24.336  1.00 70.22           C  
ANISOU 2801  C   ALA B 386    13151   6070   7457   2928  -2424   -462       C  
ATOM   2802  O   ALA B 386      53.781  14.737 -25.159  1.00 71.24           O  
ANISOU 2802  O   ALA B 386    12925   6427   7714   2970  -2525   -605       O  
ATOM   2803  CB  ALA B 386      55.077  15.719 -22.176  1.00 61.51           C  
ANISOU 2803  CB  ALA B 386    11990   4742   6640   2233  -2355   -367       C  
ATOM   2804  N   VAL B 387      53.792  16.937 -24.683  1.00 70.63           N  
ANISOU 2804  N   VAL B 387    13800   5896   7140   3053  -2243   -331       N  
ATOM   2805  CA  VAL B 387      53.810  17.367 -26.075  1.00 68.16           C  
ANISOU 2805  CA  VAL B 387    13752   5628   6517   3276  -2159   -294       C  
ATOM   2806  C   VAL B 387      55.162  18.016 -26.350  1.00 69.40           C  
ANISOU 2806  C   VAL B 387    14266   5534   6571   2883  -1911   -214       C  
ATOM   2807  O   VAL B 387      55.430  19.142 -25.912  1.00 72.02           O  
ANISOU 2807  O   VAL B 387    15123   5510   6733   2765  -1710    -79       O  
ATOM   2808  CB  VAL B 387      52.646  18.313 -26.390  1.00 70.85           C  
ANISOU 2808  CB  VAL B 387    14489   5928   6502   3820  -2127   -141       C  
ATOM   2809  CG1 VAL B 387      51.377  17.507 -26.599  1.00 84.96           C  
ANISOU 2809  CG1 VAL B 387    15800   8129   8353   4206  -2398   -242       C  
ATOM   2810  CG2 VAL B 387      52.430  19.288 -25.255  1.00 83.90           C  
ANISOU 2810  CG2 VAL B 387    16512   7263   8105   3783  -1958    -31       C  
ATOM   2811  N   LEU B 388      56.020  17.294 -27.066  1.00 68.97           N  
ANISOU 2811  N   LEU B 388    13920   5657   6629   2662  -1902   -314       N  
ATOM   2812  CA  LEU B 388      57.366  17.770 -27.343  1.00 70.36           C  
ANISOU 2812  CA  LEU B 388    14314   5675   6745   2251  -1663   -240       C  
ATOM   2813  C   LEU B 388      57.339  18.945 -28.317  1.00 90.70           C  
ANISOU 2813  C   LEU B 388    17511   8070   8882   2433  -1430    -58       C  
ATOM   2814  O   LEU B 388      56.473  19.042 -29.192  1.00 75.49           O  
ANISOU 2814  O   LEU B 388    15697   6294   6693   2905  -1485    -21       O  
ATOM   2815  CB  LEU B 388      58.217  16.633 -27.910  1.00 69.41           C  
ANISOU 2815  CB  LEU B 388    13685   5829   6860   2051  -1687   -389       C  
ATOM   2816  CG  LEU B 388      59.738  16.769 -27.856  1.00 70.29           C  
ANISOU 2816  CG  LEU B 388    13760   5883   7064   1544  -1482   -332       C  
ATOM   2817  CD1 LEU B 388      60.221  16.884 -26.418  1.00 85.78           C  
ANISOU 2817  CD1 LEU B 388    15615   7720   9255   1151  -1524   -284       C  
ATOM   2818  CD2 LEU B 388      60.405  15.590 -28.553  1.00 69.91           C  
ANISOU 2818  CD2 LEU B 388    13203   6126   7233   1494  -1481   -483       C  
ATOM   2819  N   MET B 389      58.301  19.850 -28.151  1.00 83.29           N  
ANISOU 2819  N   MET B 389    16971   6819   7857   2041  -1166     71       N  
ATOM   2820  CA  MET B 389      58.470  20.997 -29.042  1.00 81.61           C  
ANISOU 2820  CA  MET B 389    17386   6359   7261   2129   -877    289       C  
ATOM   2821  C   MET B 389      59.658  20.699 -29.950  1.00 86.95           C  
ANISOU 2821  C   MET B 389    17906   7209   7920   1814   -711    289       C  
ATOM   2822  O   MET B 389      60.815  20.842 -29.543  1.00 96.48           O  
ANISOU 2822  O   MET B 389    19062   8314   9281   1259   -562    293       O  
ATOM   2823  CB  MET B 389      58.674  22.288 -28.256  1.00 82.48           C  
ANISOU 2823  CB  MET B 389    18117   5936   7286   1881   -645    425       C  
ATOM   2824  CG  MET B 389      57.553  22.615 -27.283  1.00 91.28           C  
ANISOU 2824  CG  MET B 389    19405   6864   8412   2195   -758    408       C  
ATOM   2825  SD  MET B 389      57.617  24.323 -26.708  1.00103.17           S  
ANISOU 2825  SD  MET B 389    21840   7649   9710   2053   -394    564       S  
ATOM   2826  CE  MET B 389      59.381  24.633 -26.757  1.00111.10           C  
ANISOU 2826  CE  MET B 389    22924   8499  10790   1183   -152    549       C  
ATOM   2827  N   VAL B 390      59.369  20.280 -31.180  1.00 88.23           N  
ANISOU 2827  N   VAL B 390    17968   7682   7874   2164   -736    277       N  
ATOM   2828  CA  VAL B 390      60.388  19.911 -32.154  1.00 85.93           C  
ANISOU 2828  CA  VAL B 390    17510   7617   7524   1954   -563    255       C  
ATOM   2829  C   VAL B 390      60.495  21.022 -33.192  1.00 91.73           C  
ANISOU 2829  C   VAL B 390    18868   8193   7792   2086   -254    544       C  
ATOM   2830  O   VAL B 390      59.481  21.483 -33.730  1.00 90.34           O  
ANISOU 2830  O   VAL B 390    19025   8021   7279   2604   -297    684       O  
ATOM   2831  CB  VAL B 390      60.076  18.552 -32.812  1.00 91.12           C  
ANISOU 2831  CB  VAL B 390    17604   8754   8265   2211   -785    -14       C  
ATOM   2832  CG1 VAL B 390      60.184  17.428 -31.789  1.00 80.89           C  
ANISOU 2832  CG1 VAL B 390    15702   7549   7483   2017  -1016   -250       C  
ATOM   2833  CG2 VAL B 390      58.689  18.551 -33.452  1.00 86.68           C  
ANISOU 2833  CG2 VAL B 390    17158   8388   7389   2810   -984    -27       C  
ATOM   2834  N   SER B 391      61.723  21.455 -33.465  1.00101.89           N  
ANISOU 2834  N   SER B 391    20294   9364   9057   1625     67    665       N  
ATOM   2835  CA  SER B 391      61.963  22.547 -34.404  1.00116.52           C  
ANISOU 2835  CA  SER B 391    22764  11016  10491   1671    423    986       C  
ATOM   2836  C   SER B 391      62.125  22.032 -35.831  1.00109.67           C  
ANISOU 2836  C   SER B 391    21745  10605   9318   1920    498    983       C  
ATOM   2837  O   SER B 391      62.846  21.064 -36.071  1.00109.58           O  
ANISOU 2837  O   SER B 391    21204  10941   9488   1714    482    762       O  
ATOM   2838  CB  SER B 391      63.203  23.346 -33.991  1.00125.81           C  
ANISOU 2838  CB  SER B 391    24188  11831  11783    989    768   1128       C  
ATOM   2839  OG  SER B 391      64.382  22.573 -34.121  1.00128.24           O  
ANISOU 2839  OG  SER B 391    23939  12472  12313    557    830    987       O  
TER    2840      SER B 391                                                      
CONECT   74  535                                                                
CONECT  106 3658                                                                
CONECT  535   74                                                                
CONECT  787 1214                                                                
CONECT  999 3580                                                                
CONECT 1214  787                                                                
CONECT 1669 3630                                                                
CONECT 2499 2726                                                                
CONECT 2643 2740                                                                
CONECT 2726 2499                                                                
CONECT 2740 2643                                                                
CONECT 3580  999 3581 3591                                                      
CONECT 3581 3580 3582 3588                                                      
CONECT 3582 3581 3583 3589                                                      
CONECT 3583 3582 3584 3590                                                      
CONECT 3584 3583 3585 3591                                                      
CONECT 3585 3584 3592                                                           
CONECT 3586 3587 3588 3593                                                      
CONECT 3587 3586                                                                
CONECT 3588 3581 3586                                                           
CONECT 3589 3582                                                                
CONECT 3590 3583 3594                                                           
CONECT 3591 3580 3584                                                           
CONECT 3592 3585                                                                
CONECT 3593 3586                                                                
CONECT 3594 3590 3595 3605                                                      
CONECT 3595 3594 3596 3602                                                      
CONECT 3596 3595 3597 3603                                                      
CONECT 3597 3596 3598 3604                                                      
CONECT 3598 3597 3599 3605                                                      
CONECT 3599 3598 3606                                                           
CONECT 3600 3601 3602 3607                                                      
CONECT 3601 3600                                                                
CONECT 3602 3595 3600                                                           
CONECT 3603 3596                                                                
CONECT 3604 3597 3608                                                           
CONECT 3605 3594 3598                                                           
CONECT 3606 3599                                                                
CONECT 3607 3600                                                                
CONECT 3608 3604 3609 3617                                                      
CONECT 3609 3608 3610 3614                                                      
CONECT 3610 3609 3611 3615                                                      
CONECT 3611 3610 3612 3616                                                      
CONECT 3612 3611 3613 3617                                                      
CONECT 3613 3612 3618                                                           
CONECT 3614 3609                                                                
CONECT 3615 3610                                                                
CONECT 3616 3611                                                                
CONECT 3617 3608 3612                                                           
CONECT 3618 3613 3619                                                           
CONECT 3619 3618 3620 3628                                                      
CONECT 3620 3619 3621 3625                                                      
CONECT 3621 3620 3622 3626                                                      
CONECT 3622 3621 3623 3627                                                      
CONECT 3623 3622 3624 3628                                                      
CONECT 3624 3623 3629                                                           
CONECT 3625 3620                                                                
CONECT 3626 3621                                                                
CONECT 3627 3622                                                                
CONECT 3628 3619 3623                                                           
CONECT 3629 3624                                                                
CONECT 3630 1669 3631 3641                                                      
CONECT 3631 3630 3632 3638                                                      
CONECT 3632 3631 3633 3639                                                      
CONECT 3633 3632 3634 3640                                                      
CONECT 3634 3633 3635 3641                                                      
CONECT 3635 3634 3642                                                           
CONECT 3636 3637 3638 3643                                                      
CONECT 3637 3636                                                                
CONECT 3638 3631 3636                                                           
CONECT 3639 3632                                                                
CONECT 3640 3633 3644                                                           
CONECT 3641 3630 3634                                                           
CONECT 3642 3635                                                                
CONECT 3643 3636                                                                
CONECT 3644 3640 3645 3655                                                      
CONECT 3645 3644 3646 3652                                                      
CONECT 3646 3645 3647 3653                                                      
CONECT 3647 3646 3648 3654                                                      
CONECT 3648 3647 3649 3655                                                      
CONECT 3649 3648 3656                                                           
CONECT 3650 3651 3652 3657                                                      
CONECT 3651 3650                                                                
CONECT 3652 3645 3650                                                           
CONECT 3653 3646                                                                
CONECT 3654 3647                                                                
CONECT 3655 3644 3648                                                           
CONECT 3656 3649                                                                
CONECT 3657 3650                                                                
CONECT 3658  106 3659 3669                                                      
CONECT 3659 3658 3660 3666                                                      
CONECT 3660 3659 3661 3667                                                      
CONECT 3661 3660 3662 3668                                                      
CONECT 3662 3661 3663 3669                                                      
CONECT 3663 3662 3670                                                           
CONECT 3664 3665 3666 3671                                                      
CONECT 3665 3664                                                                
CONECT 3666 3659 3664                                                           
CONECT 3667 3660                                                                
CONECT 3668 3661                                                                
CONECT 3669 3658 3662                                                           
CONECT 3670 3663                                                                
CONECT 3671 3664                                                                
CONECT 3672 3673 3674                                                           
CONECT 3673 3672                                                                
CONECT 3674 3672 3675 3676                                                      
CONECT 3675 3674                                                                
CONECT 3676 3674 3677                                                           
CONECT 3677 3676                                                                
MASTER      388    0    8    7   30    0    0    6 3698    3  109   37          
END                                                                             



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