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***  soumi_IgG4_400_Rev_00  ***

elNémo ID: 2011020404578303

Job options:

ID        	=	 2011020404578303
JOBID     	=	 soumi_IgG4_400_Rev_00
USERID    	=	 unknown
PRIVAT    	=	 0

NMODES    	=	 10
DQMIN     	=	 -600
DQMAX     	=	 600
DQSTEP    	=	 20
DOGRAPHS  	=	 on

DOPROJMODS	=	 0
DORMSD    	=	 0

NRBL      	=	 0
CUTOFF    	=	 0
CAONLY    	=	 0


Input data for this run:

HEADER soumi_IgG4_400_Rev_00

HEADER    IMMUNE SYSTEM                           02-SEP-15   5DK3              
TITLE     CRYSTAL STRUCTURE OF PEMBROLIZUMAB, A FULL LENGTH IGG4 ANTIBODY       
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: LIGHT CHAIN;                                               
COMPND   3 CHAIN: A, F;                                                         
COMPND   4 ENGINEERED: YES;                                                     
COMPND   5 MOL_ID: 2;                                                           
COMPND   6 MOLECULE: HEAVY CHAIN;                                               
COMPND   7 CHAIN: B, G;                                                         
COMPND   8 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_TAXID: 9606;                                                
SOURCE   4 EXPRESSION_SYSTEM: MAMMALIA;                                         
SOURCE   5 EXPRESSION_SYSTEM_TAXID: 40674;                                      
SOURCE   6 MOL_ID: 2;                                                           
SOURCE   7 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   8 ORGANISM_TAXID: 9606;                                                
SOURCE   9 EXPRESSION_SYSTEM: MAMMALIA;                                         
SOURCE  10 EXPRESSION_SYSTEM_TAXID: 40674                                       
KEYWDS    CANCER, ANTIBODY, SUBCLASSES, IGG4, MELANOMA, IMMUNE SYSTEM           
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    G.SCAPIN,W.PROSISE,P.REICHERT                                         
REVDAT   4   29-JUL-20 5DK3    1       COMPND REMARK HET    HETNAM              
REVDAT   4 2                   1       FORMUL LINK   SITE   ATOM                
REVDAT   3   03-AUG-16 5DK3    1       JRNL                                     
REVDAT   2   06-JUL-16 5DK3    1       JRNL                                     
REVDAT   1   18-NOV-15 5DK3    0                                                
JRNL        AUTH   G.SCAPIN,X.YANG,W.W.PROSISE,M.MCCOY,P.REICHERT,J.M.JOHNSTON, 
JRNL        AUTH 2 R.S.KASHI,C.STRICKLAND                                       
JRNL        TITL   STRUCTURE OF FULL-LENGTH HUMAN ANTI-PD1 THERAPEUTIC IGG4     
JRNL        TITL 2 ANTIBODY PEMBROLIZUMAB.                                      
JRNL        REF    NAT.STRUCT.MOL.BIOL.          V.  22   953 2015              
JRNL        REFN                   ESSN 1545-9985                               
JRNL        PMID   26595420                                                     
JRNL        DOI    10.1038/NSMB.3129                                            
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.28 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : BUSTER 2.11.5                                        
REMARK   3   AUTHORS     : BRICOGNE,BLANC,BRANDL,FLENSBURG,KELLER,              
REMARK   3               : PACIOREK,ROVERSI,SHARFF,SMART,VONRHEIN,              
REMARK   3               : WOMACK,MATTHEWS,TEN EYCK,TRONRUD                     
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.28                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 33.38                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 100.0                          
REMARK   3   NUMBER OF REFLECTIONS             : 86694                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD           : THROUGHOUT                     
REMARK   3   FREE R VALUE TEST SET SELECTION   : RANDOM                         
REMARK   3   R VALUE     (WORKING + TEST SET)  : 0.186                          
REMARK   3   R VALUE            (WORKING SET)  : 0.184                          
REMARK   3   FREE R VALUE                      : 0.224                          
REMARK   3   FREE R VALUE TEST SET SIZE   (%)  : 5.060                          
REMARK   3   FREE R VALUE TEST SET COUNT       : 4386                           
REMARK   3   ESTIMATED ERROR OF FREE R VALUE   : NULL                           
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED               : 20                       
REMARK   3   BIN RESOLUTION RANGE HIGH   (ANGSTROMS) : 2.28                     
REMARK   3   BIN RESOLUTION RANGE LOW    (ANGSTROMS) : 2.34                     
REMARK   3   BIN COMPLETENESS (WORKING+TEST)     (%) : 99.99                    
REMARK   3   REFLECTIONS IN BIN (WORKING + TEST SET) : 6245                     
REMARK   3   BIN R VALUE        (WORKING + TEST SET) : 0.2071                   
REMARK   3   REFLECTIONS IN BIN        (WORKING SET) : 5945                     
REMARK   3   BIN R VALUE               (WORKING SET) : 0.2055                   
REMARK   3   BIN FREE R VALUE                        : 0.2375                   
REMARK   3   BIN FREE R VALUE TEST SET SIZE      (%) : 4.80                     
REMARK   3   BIN FREE R VALUE TEST SET COUNT         : 300                      
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE     : NULL                     
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 10000                                   
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 268                                     
REMARK   3   SOLVENT ATOMS            : 481                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 53.08                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 64.17                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.25900                                              
REMARK   3    B22 (A**2) : 6.95850                                              
REMARK   3    B33 (A**2) : -7.21750                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT                    (A) : 0.308               
REMARK   3   DPI (BLOW EQ-10) BASED ON R VALUE        (A) : 0.207               
REMARK   3   DPI (BLOW EQ-9) BASED ON FREE R VALUE    (A) : 0.177               
REMARK   3   DPI (CRUICKSHANK) BASED ON R VALUE       (A) : 0.627               
REMARK   3   DPI (CRUICKSHANK) BASED ON FREE R VALUE  (A) : 0.179               
REMARK   3                                                                      
REMARK   3   REFERENCES: BLOW, D. (2002) ACTA CRYST D58, 792-797                
REMARK   3               CRUICKSHANK, D.W.J. (1999) ACTA CRYST D55, 583-601     
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.942                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.923                         
REMARK   3                                                                      
REMARK   3   NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15                    
REMARK   3   TERM                          COUNT    WEIGHT   FUNCTION.          
REMARK   3    BOND LENGTHS              : 20259  ; 2.000  ; HARMONIC            
REMARK   3    BOND ANGLES               : 36518  ; 2.000  ; HARMONIC            
REMARK   3    TORSION ANGLES            : 4320   ; 2.000  ; SINUSOIDAL          
REMARK   3    TRIGONAL CARBON PLANES    : 221    ; 2.000  ; HARMONIC            
REMARK   3    GENERAL PLANES            : 2940   ; 5.000  ; HARMONIC            
REMARK   3    ISOTROPIC THERMAL FACTORS : 20259  ; 20.000 ; HARMONIC            
REMARK   3    BAD NON-BONDED CONTACTS   : 6      ; 5.000  ; SEMIHARMONIC        
REMARK   3    IMPROPER TORSIONS         : NULL   ; NULL   ; NULL                
REMARK   3    PSEUDOROTATION ANGLES     : NULL   ; NULL   ; NULL                
REMARK   3    CHIRAL IMPROPER TORSION   : 1455   ; 5.000  ; SEMIHARMONIC        
REMARK   3    SUM OF OCCUPANCIES        : NULL   ; NULL   ; NULL                
REMARK   3    UTILITY DISTANCES         : NULL   ; NULL   ; NULL                
REMARK   3    UTILITY ANGLES            : NULL   ; NULL   ; NULL                
REMARK   3    UTILITY TORSION           : NULL   ; NULL   ; NULL                
REMARK   3    IDEAL-DIST CONTACT TERM   : 21020  ; 4.000  ; SEMIHARMONIC        
REMARK   3                                                                      
REMARK   3   RMS DEVIATIONS FROM IDEAL VALUES.                                  
REMARK   3    BOND LENGTHS                       (A) : 0.010                    
REMARK   3    BOND ANGLES                  (DEGREES) : 1.18                     
REMARK   3    PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 4.08                     
REMARK   3    OTHER TORSION ANGLES         (DEGREES) : 15.77                    
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 6                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: { A|1 - A|218 }                                        
REMARK   3    ORIGIN FOR THE GROUP (A):   10.9073  -19.7359  -68.1115           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.0795 T22:   -0.1176                                    
REMARK   3     T33:   -0.0389 T12:    0.0133                                    
REMARK   3     T13:    0.0682 T23:   -0.0563                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    0.9392 L22:    1.2899                                    
REMARK   3     L33:    0.7865 L12:    0.3592                                    
REMARK   3     L13:   -0.2495 L23:   -0.6265                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:    0.0189 S12:   -0.0025 S13:   -0.0745                     
REMARK   3     S21:    0.1406 S22:   -0.0772 S23:   -0.0400                     
REMARK   3     S31:   -0.0440 S32:    0.1007 S33:    0.0583                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: { B|1 - B|444 }                                        
REMARK   3    ORIGIN FOR THE GROUP (A):   11.8349  -28.8997  -54.1121           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.0500 T22:   -0.0913                                    
REMARK   3     T33:   -0.0487 T12:   -0.0076                                    
REMARK   3     T13:    0.0715 T23:   -0.0395                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    0.2033 L22:    1.0620                                    
REMARK   3     L33:    0.2826 L12:   -0.0133                                    
REMARK   3     L13:    0.0456 L23:   -0.5312                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:   -0.0173 S12:   -0.0802 S13:   -0.0018                     
REMARK   3     S21:    0.2327 S22:   -0.0236 S23:   -0.1109                     
REMARK   3     S31:   -0.1200 S32:    0.0354 S33:    0.0409                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: { G|501 - G|507 }                                      
REMARK   3    ORIGIN FOR THE GROUP (A):    4.5010  -48.5158  -28.3024           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.0633 T22:    0.0323                                    
REMARK   3     T33:   -0.0201 T12:   -0.0006                                    
REMARK   3     T13:    0.3022 T23:    0.0591                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    0.3193 L22:    0.3711                                    
REMARK   3     L33:    0.1979 L12:    1.1402                                    
REMARK   3     L13:   -1.8965 L23:    1.3190                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:    0.0137 S12:    0.0046 S13:    0.0085                     
REMARK   3     S21:   -0.0711 S22:    0.0158 S23:    0.0140                     
REMARK   3     S31:   -0.0146 S32:   -0.0453 S33:   -0.0294                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: { F|1 - F|218 }                                        
REMARK   3    ORIGIN FOR THE GROUP (A):    7.2615   -2.3914    5.9137           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.1925 T22:   -0.0718                                    
REMARK   3     T33:   -0.3832 T12:    0.1108                                    
REMARK   3     T13:   -0.0840 T23:    0.0896                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    2.8746 L22:    3.3484                                    
REMARK   3     L33:    4.6285 L12:   -2.2086                                    
REMARK   3     L13:   -0.1273 L23:    1.1430                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:   -0.3306 S12:   -0.7365 S13:   -0.2251                     
REMARK   3     S21:    0.4649 S22:    0.6004 S23:   -0.1486                     
REMARK   3     S31:    0.8538 S32:    0.2923 S33:   -0.2698                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION: { B|505 - B|511 }                                      
REMARK   3    ORIGIN FOR THE GROUP (A):   27.4109  -30.0513  -38.4026           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:    0.0389 T22:   -0.1789                                    
REMARK   3     T33:    0.0972 T12:   -0.1415                                    
REMARK   3     T13:    0.1461 T23:    0.0473                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    0.3244 L22:    1.1945                                    
REMARK   3     L33:    0.3098 L12:    0.3638                                    
REMARK   3     L13:   -1.0668 L23:   -0.4528                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:   -0.0032 S12:    0.0258 S13:   -0.0012                     
REMARK   3     S21:   -0.0230 S22:   -0.0064 S23:    0.0168                     
REMARK   3     S31:    0.0315 S32:   -0.0246 S33:    0.0096                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    SELECTION: { G|1 - G|444 }                                        
REMARK   3    ORIGIN FOR THE GROUP (A):    2.7046  -26.5963  -16.4152           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.0723 T22:    0.0215                                    
REMARK   3     T33:   -0.1429 T12:   -0.0145                                    
REMARK   3     T13:    0.0367 T23:    0.0249                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    0.0950 L22:    2.3699                                    
REMARK   3     L33:    0.5940 L12:    0.0182                                    
REMARK   3     L13:    0.1079 L23:    1.2830                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:   -0.0113 S12:   -0.1770 S13:    0.0450                     
REMARK   3     S21:    0.1256 S22:    0.0091 S23:   -0.0590                     
REMARK   3     S31:    0.0123 S32:   -0.0068 S33:    0.0022                     
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 5DK3 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 03-SEP-15.                  
REMARK 100 THE DEPOSITION ID IS D_1000213319.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 21-MAY-14                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 8.0 - 8.5                          
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : CLSI                               
REMARK 200  BEAMLINE                       : 08ID-1                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.00                               
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 : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : AIMLESS 0.1.27                     
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 654220                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.280                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 110.830                            
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY                : 3.800                              
REMARK 200  R MERGE                    (I) : 0.07200                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 18.5000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.28                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.55                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 7.50                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.72300                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : 3.000                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: RODS                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 61.75                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.22                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.8-2.2 M NH4H2PO4, 100 MM TRIS, PH      
REMARK 280  8.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 303K                
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000       31.91500            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000      132.48000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       55.41500            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000      132.48000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       31.91500            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       55.41500            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
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: TETRAMERIC                        
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC                 
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 19280 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 59230 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -102.0 KCAL/MOL                       
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, F, G, C, D, E, H, I             
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     PRO B   230                                                      
REMARK 465     ALA B   231                                                      
REMARK 465     PRO B   232                                                      
REMARK 465     PRO G   230                                                      
REMARK 465     ALA G   231                                                      
REMARK 465     PRO G   232                                                      
REMARK 465     GLU G   233                                                      
REMARK 465     PHE G   234                                                      
REMARK 465     LEU G   235                                                      
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     GLU A 147    CG   CD   OE1  OE2                                  
REMARK 470     GLU B  62    CG   CD   OE1  OE2                                  
REMARK 470     LYS B  65    CG   CD   CE   NZ                                   
REMARK 470     LYS B  84    CG   CD   CE   NZ                                   
REMARK 470     ARG B 102    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG B 136    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU B 233    CG   CD   OE1  OE2                                  
REMARK 470     PHE B 234    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     LYS B 246    CG   CD   CE   NZ                                   
REMARK 470     MET B 252    CG   SD   CE                                        
REMARK 470     ILE B 253    CG1  CG2  CD1                                       
REMARK 470     ARG B 255    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLN B 268    CG   CD   OE1  NE2                                  
REMARK 470     GLU B 272    CG   CD   OE1  OE2                                  
REMARK 470     LYS B 288    CG   CD   CE   NZ                                   
REMARK 470     ARG B 292    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLN B 311    CG   CD   OE1  NE2                                  
REMARK 470     LYS B 322    CG   CD   CE   NZ                                   
REMARK 470     LYS B 326    CG   CD   CE   NZ                                   
REMARK 470     SER B 330    OG                                                  
REMARK 470     LYS B 334    CG   CD   CE   NZ                                   
REMARK 470     LYS B 340    CG   CD   CE   NZ                                   
REMARK 470     GLN B 342    CG   CD   OE1  NE2                                  
REMARK 470     ARG F  96    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS F 111    CG   CD   CE   NZ                                   
REMARK 470     LYS F 130    CG   CD   CE   NZ                                   
REMARK 470     LYS F 149    CG   CD   CE   NZ                                   
REMARK 470     LYS F 173    CG   CD   CE   NZ                                   
REMARK 470     GLU F 191    CG   CD   OE1  OE2                                  
REMARK 470     LYS F 194    CG   CD   CE   NZ                                   
REMARK 470     GLU F 217    CG   CD   OE1  OE2                                  
REMARK 470     LYS G  65    CG   CD   CE   NZ                                   
REMARK 470     LYS G  84    CG   CD   CE   NZ                                   
REMARK 470     ARG G 102    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG G 136    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS G 246    CD   CE   NZ                                        
REMARK 470     GLN G 268    CG   CD   OE1  NE2                                  
REMARK 470     GLN G 274    CG   CD   OE1  NE2                                  
REMARK 470     ARG G 292    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLN G 311    CG   CD   OE1  NE2                                  
REMARK 470     LYS G 322    CG   CD   CE   NZ                                   
REMARK 470     LYS G 334    CG   CD   CE   NZ                                   
REMARK 470     GLN G 386    CG   CD   OE1  NE2                                  
REMARK 470     ARG G 416    CG   CD   NE   CZ   NH1  NH2                        
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   ND2  ASN B   297     O5   NAG C     1              1.91            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    SER G 122   C   -  N   -  CA  ANGL. DEV. =  15.7 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ALA A  55      -40.39     73.71                                   
REMARK 500    ALA A  88      174.69    178.00                                   
REMARK 500    SER A  95       42.75   -142.04                                   
REMARK 500    ASN B  66      -22.14     98.99                                   
REMARK 500    SER B 135       86.16     57.26                                   
REMARK 500    SER B 139       68.52   -109.08                                   
REMARK 500    ASP B 151       68.99     67.44                                   
REMARK 500    LEU B 235       -1.58     78.78                                   
REMARK 500    LYS B 246     -108.62   -160.57                                   
REMARK 500    PRO B 247      -77.01    -90.78                                   
REMARK 500    ASP B 249      -81.68     69.40                                   
REMARK 500    LEU B 251     -170.45    -66.42                                   
REMARK 500    MET B 252      -82.58   -128.56                                   
REMARK 500    ARG B 255     -177.80     63.11                                   
REMARK 500    THR B 256       84.17     88.27                                   
REMARK 500    GLN B 295      105.66    -25.59                                   
REMARK 500    PHE B 296      -52.41   -152.51                                   
REMARK 500    ASN B 297      -56.07    -20.00                                   
REMARK 500    SER B 298      -33.50    172.76                                   
REMARK 500    HIS B 310     -120.69     55.40                                   
REMARK 500    SER B 330     -168.78   -110.60                                   
REMARK 500    ALA F  55       -3.00     60.24                                   
REMARK 500    SER F  56      -48.81   -145.51                                   
REMARK 500    SER F  80      -48.93    -28.01                                   
REMARK 500    SER F  95       31.16   -153.13                                   
REMARK 500    ASN F 142       71.46     35.67                                   
REMARK 500    LYS F 173      -70.31    -69.91                                   
REMARK 500    ASN G  66      -38.18     91.95                                   
REMARK 500    THR G  77       53.78     35.01                                   
REMARK 500    SER G 122       88.65     92.59                                   
REMARK 500    SER G 137      -70.03   -102.23                                   
REMARK 500    THR G 138     -175.97     43.44                                   
REMARK 500    GLN G 295       61.77   -105.39                                   
REMARK 500    PHE G 296       12.63     45.86                                   
REMARK 500    SER G 298       42.94    -92.22                                   
REMARK 500    LYS G 317      117.72     62.75                                   
REMARK 500    SER G 330     -124.57   -129.14                                   
REMARK 500    PRO G 374     -173.45    -66.50                                   
REMARK 500    ASN G 384      -74.37     58.96                                   
REMARK 500    ASN G 389      -46.29   -130.96                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 610                                                                      
REMARK 610 MISSING HETEROATOM                                                   
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 610 I=INSERTION CODE):                                                   
REMARK 610   M RES C SSEQI                                                      
REMARK 610     NAG C    1                                                       
DBREF  5DK3 A    1   218  PDB    5DK3     5DK3             1    218             
DBREF  5DK3 B    1   444  PDB    5DK3     5DK3             1    444             
DBREF  5DK3 F    1   218  PDB    5DK3     5DK3             1    218             
DBREF  5DK3 G    1   444  PDB    5DK3     5DK3             1    444             
SEQRES   1 A  218  GLU ILE VAL LEU THR GLN SER PRO ALA THR LEU SER LEU          
SEQRES   2 A  218  SER PRO GLY GLU ARG ALA THR LEU SER CYS ARG ALA SER          
SEQRES   3 A  218  LYS GLY VAL SER THR SER GLY TYR SER TYR LEU HIS TRP          
SEQRES   4 A  218  TYR GLN GLN LYS PRO GLY GLN ALA PRO ARG LEU LEU ILE          
SEQRES   5 A  218  TYR LEU ALA SER TYR LEU GLU SER GLY VAL PRO ALA ARG          
SEQRES   6 A  218  PHE SER GLY SER GLY SER GLY THR ASP PHE THR LEU THR          
SEQRES   7 A  218  ILE SER SER LEU GLU PRO GLU ASP PHE ALA VAL TYR TYR          
SEQRES   8 A  218  CYS GLN HIS SER ARG ASP LEU PRO LEU THR PHE GLY GLY          
SEQRES   9 A  218  GLY THR LYS VAL GLU ILE LYS ARG THR VAL ALA ALA PRO          
SEQRES  10 A  218  SER VAL PHE ILE PHE PRO PRO SER ASP GLU GLN LEU LYS          
SEQRES  11 A  218  SER GLY THR ALA SER VAL VAL CYS LEU LEU ASN ASN PHE          
SEQRES  12 A  218  TYR PRO ARG GLU ALA LYS VAL GLN TRP LYS VAL ASP ASN          
SEQRES  13 A  218  ALA LEU GLN SER GLY ASN SER GLN GLU SER VAL THR GLU          
SEQRES  14 A  218  GLN ASP SER LYS ASP SER THR TYR SER LEU SER SER THR          
SEQRES  15 A  218  LEU THR LEU SER LYS ALA ASP TYR GLU LYS HIS LYS VAL          
SEQRES  16 A  218  TYR ALA CYS GLU VAL THR HIS GLN GLY LEU SER SER PRO          
SEQRES  17 A  218  VAL THR LYS SER PHE ASN ARG GLY GLU CYS                      
SEQRES   1 B  444  GLN VAL GLN LEU VAL GLN SER GLY VAL GLU VAL LYS LYS          
SEQRES   2 B  444  PRO GLY ALA SER VAL LYS VAL SER CYS LYS ALA SER GLY          
SEQRES   3 B  444  TYR THR PHE THR ASN TYR TYR MET TYR TRP VAL ARG GLN          
SEQRES   4 B  444  ALA PRO GLY GLN GLY LEU GLU TRP MET GLY GLY ILE ASN          
SEQRES   5 B  444  PRO SER ASN GLY GLY THR ASN PHE ASN GLU LYS PHE LYS          
SEQRES   6 B  444  ASN ARG VAL THR LEU THR THR ASP SER SER THR THR THR          
SEQRES   7 B  444  ALA TYR MET GLU LEU LYS SER LEU GLN PHE ASP ASP THR          
SEQRES   8 B  444  ALA VAL TYR TYR CYS ALA ARG ARG ASP TYR ARG PHE ASP          
SEQRES   9 B  444  MET GLY PHE ASP TYR TRP GLY GLN GLY THR THR VAL THR          
SEQRES  10 B  444  VAL SER SER ALA SER THR LYS GLY PRO SER VAL PHE PRO          
SEQRES  11 B  444  LEU ALA PRO CYS SER ARG SER THR SER GLU SER THR ALA          
SEQRES  12 B  444  ALA LEU GLY CYS LEU VAL LYS ASP TYR PHE PRO GLU PRO          
SEQRES  13 B  444  VAL THR VAL SER TRP ASN SER GLY ALA LEU THR SER GLY          
SEQRES  14 B  444  VAL HIS THR PHE PRO ALA VAL LEU GLN SER SER GLY LEU          
SEQRES  15 B  444  TYR SER LEU SER SER VAL VAL THR VAL PRO SER SER SER          
SEQRES  16 B  444  LEU GLY THR LYS THR TYR THR CYS ASN VAL ASP HIS LYS          
SEQRES  17 B  444  PRO SER ASN THR LYS VAL ASP LYS ARG VAL GLU SER LYS          
SEQRES  18 B  444  TYR GLY PRO PRO CYS PRO PRO CYS PRO ALA PRO GLU PHE          
SEQRES  19 B  444  LEU GLY GLY PRO SER VAL PHE LEU PHE PRO PRO LYS PRO          
SEQRES  20 B  444  LYS ASP THR LEU MET ILE SER ARG THR PRO GLU VAL THR          
SEQRES  21 B  444  CYS VAL VAL VAL ASP VAL SER GLN GLU ASP PRO GLU VAL          
SEQRES  22 B  444  GLN PHE ASN TRP TYR VAL ASP GLY VAL GLU VAL HIS ASN          
SEQRES  23 B  444  ALA LYS THR LYS PRO ARG GLU GLU GLN PHE ASN SER THR          
SEQRES  24 B  444  TYR ARG VAL VAL SER VAL LEU THR VAL LEU HIS GLN ASP          
SEQRES  25 B  444  TRP LEU ASN GLY LYS GLU TYR LYS CYS LYS VAL SER ASN          
SEQRES  26 B  444  LYS GLY LEU PRO SER SER ILE GLU LYS THR ILE SER LYS          
SEQRES  27 B  444  ALA LYS GLY GLN PRO ARG GLU PRO GLN VAL TYR THR LEU          
SEQRES  28 B  444  PRO PRO SER GLN GLU GLU MET THR LYS ASN GLN VAL SER          
SEQRES  29 B  444  LEU THR CYS LEU VAL LYS GLY PHE TYR PRO SER ASP ILE          
SEQRES  30 B  444  ALA VAL GLU TRP GLU SER ASN GLY GLN PRO GLU ASN ASN          
SEQRES  31 B  444  TYR LYS THR THR PRO PRO VAL LEU ASP SER ASP GLY SER          
SEQRES  32 B  444  PHE PHE LEU TYR SER ARG LEU THR VAL ASP LYS SER ARG          
SEQRES  33 B  444  TRP GLN GLN GLY ASN VAL PHE SER CYS SER VAL MET HIS          
SEQRES  34 B  444  GLU ALA LEU HIS ASN HIS TYR THR GLN LYS SER LEU SER          
SEQRES  35 B  444  LEU SER                                                      
SEQRES   1 F  218  GLU ILE VAL LEU THR GLN SER PRO ALA THR LEU SER LEU          
SEQRES   2 F  218  SER PRO GLY GLU ARG ALA THR LEU SER CYS ARG ALA SER          
SEQRES   3 F  218  LYS GLY VAL SER THR SER GLY TYR SER TYR LEU HIS TRP          
SEQRES   4 F  218  TYR GLN GLN LYS PRO GLY GLN ALA PRO ARG LEU LEU ILE          
SEQRES   5 F  218  TYR LEU ALA SER TYR LEU GLU SER GLY VAL PRO ALA ARG          
SEQRES   6 F  218  PHE SER GLY SER GLY SER GLY THR ASP PHE THR LEU THR          
SEQRES   7 F  218  ILE SER SER LEU GLU PRO GLU ASP PHE ALA VAL TYR TYR          
SEQRES   8 F  218  CYS GLN HIS SER ARG ASP LEU PRO LEU THR PHE GLY GLY          
SEQRES   9 F  218  GLY THR LYS VAL GLU ILE LYS ARG THR VAL ALA ALA PRO          
SEQRES  10 F  218  SER VAL PHE ILE PHE PRO PRO SER ASP GLU GLN LEU LYS          
SEQRES  11 F  218  SER GLY THR ALA SER VAL VAL CYS LEU LEU ASN ASN PHE          
SEQRES  12 F  218  TYR PRO ARG GLU ALA LYS VAL GLN TRP LYS VAL ASP ASN          
SEQRES  13 F  218  ALA LEU GLN SER GLY ASN SER GLN GLU SER VAL THR GLU          
SEQRES  14 F  218  GLN ASP SER LYS ASP SER THR TYR SER LEU SER SER THR          
SEQRES  15 F  218  LEU THR LEU SER LYS ALA ASP TYR GLU LYS HIS LYS VAL          
SEQRES  16 F  218  TYR ALA CYS GLU VAL THR HIS GLN GLY LEU SER SER PRO          
SEQRES  17 F  218  VAL THR LYS SER PHE ASN ARG GLY GLU CYS                      
SEQRES   1 G  444  GLN VAL GLN LEU VAL GLN SER GLY VAL GLU VAL LYS LYS          
SEQRES   2 G  444  PRO GLY ALA SER VAL LYS VAL SER CYS LYS ALA SER GLY          
SEQRES   3 G  444  TYR THR PHE THR ASN TYR TYR MET TYR TRP VAL ARG GLN          
SEQRES   4 G  444  ALA PRO GLY GLN GLY LEU GLU TRP MET GLY GLY ILE ASN          
SEQRES   5 G  444  PRO SER ASN GLY GLY THR ASN PHE ASN GLU LYS PHE LYS          
SEQRES   6 G  444  ASN ARG VAL THR LEU THR THR ASP SER SER THR THR THR          
SEQRES   7 G  444  ALA TYR MET GLU LEU LYS SER LEU GLN PHE ASP ASP THR          
SEQRES   8 G  444  ALA VAL TYR TYR CYS ALA ARG ARG ASP TYR ARG PHE ASP          
SEQRES   9 G  444  MET GLY PHE ASP TYR TRP GLY GLN GLY THR THR VAL THR          
SEQRES  10 G  444  VAL SER SER ALA SER THR LYS GLY PRO SER VAL PHE PRO          
SEQRES  11 G  444  LEU ALA PRO CYS SER ARG SER THR SER GLU SER THR ALA          
SEQRES  12 G  444  ALA LEU GLY CYS LEU VAL LYS ASP TYR PHE PRO GLU PRO          
SEQRES  13 G  444  VAL THR VAL SER TRP ASN SER GLY ALA LEU THR SER GLY          
SEQRES  14 G  444  VAL HIS THR PHE PRO ALA VAL LEU GLN SER SER GLY LEU          
SEQRES  15 G  444  TYR SER LEU SER SER VAL VAL THR VAL PRO SER SER SER          
SEQRES  16 G  444  LEU GLY THR LYS THR TYR THR CYS ASN VAL ASP HIS LYS          
SEQRES  17 G  444  PRO SER ASN THR LYS VAL ASP LYS ARG VAL GLU SER LYS          
SEQRES  18 G  444  TYR GLY PRO PRO CYS PRO PRO CYS PRO ALA PRO GLU PHE          
SEQRES  19 G  444  LEU GLY GLY PRO SER VAL PHE LEU PHE PRO PRO LYS PRO          
SEQRES  20 G  444  LYS ASP THR LEU MET ILE SER ARG THR PRO GLU VAL THR          
SEQRES  21 G  444  CYS VAL VAL VAL ASP VAL SER GLN GLU ASP PRO GLU VAL          
SEQRES  22 G  444  GLN PHE ASN TRP TYR VAL ASP GLY VAL GLU VAL HIS ASN          
SEQRES  23 G  444  ALA LYS THR LYS PRO ARG GLU GLU GLN PHE ASN SER THR          
SEQRES  24 G  444  TYR ARG VAL VAL SER VAL LEU THR VAL LEU HIS GLN ASP          
SEQRES  25 G  444  TRP LEU ASN GLY LYS GLU TYR LYS CYS LYS VAL SER ASN          
SEQRES  26 G  444  LYS GLY LEU PRO SER SER ILE GLU LYS THR ILE SER LYS          
SEQRES  27 G  444  ALA LYS GLY GLN PRO ARG GLU PRO GLN VAL TYR THR LEU          
SEQRES  28 G  444  PRO PRO SER GLN GLU GLU MET THR LYS ASN GLN VAL SER          
SEQRES  29 G  444  LEU THR CYS LEU VAL LYS GLY PHE TYR PRO SER ASP ILE          
SEQRES  30 G  444  ALA VAL GLU TRP GLU SER ASN GLY GLN PRO GLU ASN ASN          
SEQRES  31 G  444  TYR LYS THR THR PRO PRO VAL LEU ASP SER ASP GLY SER          
SEQRES  32 G  444  PHE PHE LEU TYR SER ARG LEU THR VAL ASP LYS SER ARG          
SEQRES  33 G  444  TRP GLN GLN GLY ASN VAL PHE SER CYS SER VAL MET HIS          
SEQRES  34 G  444  GLU ALA LEU HIS ASN HIS TYR THR GLN LYS SER LEU SER          
SEQRES  35 G  444  LEU SER                                                      
HET    NAG  C   1      14                                                       
HET    NAG  C   2      14                                                       
HET    BMA  C   3      11                                                       
HET    MAN  C   4      11                                                       
HET    NAG  C   5      14                                                       
HET    MAN  C   6      11                                                       
HET    NAG  C   7      14                                                       
HET    NAG  D   1      14                                                       
HET    NAG  D   2      14                                                       
HET    BMA  D   3      11                                                       
HET    MAN  D   4      11                                                       
HET    NAG  D   5      14                                                       
HET    MAN  D   6      11                                                       
HET    FUC  D   7      10                                                       
HET    GLC  E   1      11                                                       
HET    FRU  E   2      12                                                       
HET    GLC  H   1      11                                                       
HET    FRU  H   2      12                                                       
HET    GLC  I   1      11                                                       
HET    FRU  I   2      12                                                       
HET    SO4  A 301       5                                                       
HET    SO4  B 501       5                                                       
HET    SO4  B 502       5                                                       
HET    SO4  B 503       5                                                       
HET    SO4  B 504       5                                                       
HETNAM     NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE                         
HETNAM     BMA BETA-D-MANNOPYRANOSE                                             
HETNAM     MAN ALPHA-D-MANNOPYRANOSE                                            
HETNAM     FUC ALPHA-L-FUCOPYRANOSE                                             
HETNAM     GLC ALPHA-D-GLUCOPYRANOSE                                            
HETNAM     FRU BETA-D-FRUCTOFURANOSE                                            
HETNAM     SO4 SULFATE ION                                                      
FORMUL   5  NAG    7(C8 H15 N O6)                                               
FORMUL   5  BMA    2(C6 H12 O6)                                                 
FORMUL   5  MAN    4(C6 H12 O6)                                                 
FORMUL   6  FUC    C6 H12 O5                                                    
FORMUL   7  GLC    3(C6 H12 O6)                                                 
FORMUL   7  FRU    3(C6 H12 O6)                                                 
FORMUL  10  SO4    5(O4 S 2-)                                                   
FORMUL  15  HOH   *481(H2 O)                                                    
HELIX    1 AA1 GLU A   83  PHE A   87  5                                   5    
HELIX    2 AA2 SER A  125  SER A  131  1                                   7    
HELIX    3 AA3 LYS A  187  LYS A  192  1                                   6    
HELIX    4 AA4 THR B   28  THR B   30  5                                   3    
HELIX    5 AA5 GLN B   87  THR B   91  5                                   5    
HELIX    6 AA6 SER B  163  ALA B  165  5                                   3    
HELIX    7 AA7 SER B  194  LEU B  196  5                                   3    
HELIX    8 AA8 LYS B  208  ASN B  211  5                                   4    
HELIX    9 AA9 GLN B  311  GLY B  316  1                                   6    
HELIX   10 AB1 SER B  354  LYS B  360  5                                   7    
HELIX   11 AB2 LYS B  414  GLN B  419  1                                   6    
HELIX   12 AB3 LEU B  432  TYR B  436  5                                   5    
HELIX   13 AB4 GLU F   83  PHE F   87  5                                   5    
HELIX   14 AB5 SER F  125  LYS F  130  1                                   6    
HELIX   15 AB6 LYS F  187  HIS F  193  1                                   7    
HELIX   16 AB7 THR G   28  THR G   30  5                                   3    
HELIX   17 AB8 GLN G   87  THR G   91  5                                   5    
HELIX   18 AB9 SER G  163  ALA G  165  5                                   3    
HELIX   19 AC1 SER G  194  LEU G  196  5                                   3    
HELIX   20 AC2 LYS G  208  ASN G  211  5                                   4    
HELIX   21 AC3 LYS G  246  MET G  252  1                                   7    
HELIX   22 AC4 LEU G  309  ASN G  315  1                                   7    
HELIX   23 AC5 SER G  354  LYS G  360  5                                   7    
HELIX   24 AC6 LYS G  414  GLN G  419  1                                   6    
HELIX   25 AC7 LEU G  432  TYR G  436  5                                   5    
SHEET    1 AA1 4 LEU A   4  SER A   7  0                                        
SHEET    2 AA1 4 ALA A  19  ALA A  25 -1  O  ARG A  24   N  THR A   5           
SHEET    3 AA1 4 ASP A  74  ILE A  79 -1  O  PHE A  75   N  CYS A  23           
SHEET    4 AA1 4 PHE A  66  SER A  71 -1  N  SER A  67   O  THR A  78           
SHEET    1 AA2 6 THR A  10  LEU A  13  0                                        
SHEET    2 AA2 6 THR A 106  ILE A 110  1  O  GLU A 109   N  LEU A  11           
SHEET    3 AA2 6 ALA A  88  HIS A  94 -1  N  ALA A  88   O  VAL A 108           
SHEET    4 AA2 6 LEU A  37  GLN A  42 -1  N  GLN A  42   O  VAL A  89           
SHEET    5 AA2 6 ARG A  49  TYR A  53 -1  O  LEU A  51   N  TRP A  39           
SHEET    6 AA2 6 TYR A  57  LEU A  58 -1  O  TYR A  57   N  TYR A  53           
SHEET    1 AA3 4 THR A  10  LEU A  13  0                                        
SHEET    2 AA3 4 THR A 106  ILE A 110  1  O  GLU A 109   N  LEU A  11           
SHEET    3 AA3 4 ALA A  88  HIS A  94 -1  N  ALA A  88   O  VAL A 108           
SHEET    4 AA3 4 THR A 101  PHE A 102 -1  O  THR A 101   N  HIS A  94           
SHEET    1 AA4 2 SER A  30  THR A  31  0                                        
SHEET    2 AA4 2 TYR A  34  SER A  35 -1  O  TYR A  34   N  THR A  31           
SHEET    1 AA5 4 SER A 118  PHE A 122  0                                        
SHEET    2 AA5 4 THR A 133  PHE A 143 -1  O  LEU A 139   N  PHE A 120           
SHEET    3 AA5 4 TYR A 177  SER A 186 -1  O  LEU A 185   N  ALA A 134           
SHEET    4 AA5 4 SER A 163  VAL A 167 -1  N  GLN A 164   O  THR A 182           
SHEET    1 AA6 4 ALA A 157  LEU A 158  0                                        
SHEET    2 AA6 4 LYS A 149  VAL A 154 -1  N  VAL A 154   O  ALA A 157           
SHEET    3 AA6 4 VAL A 195  THR A 201 -1  O  GLU A 199   N  GLN A 151           
SHEET    4 AA6 4 VAL A 209  ASN A 214 -1  O  LYS A 211   N  CYS A 198           
SHEET    1 AA7 4 GLN B   3  GLN B   6  0                                        
SHEET    2 AA7 4 VAL B  18  SER B  25 -1  O  LYS B  23   N  VAL B   5           
SHEET    3 AA7 4 THR B  78  LEU B  83 -1  O  MET B  81   N  VAL B  20           
SHEET    4 AA7 4 VAL B  68  ASP B  73 -1  N  THR B  69   O  GLU B  82           
SHEET    1 AA8 6 GLU B  10  LYS B  12  0                                        
SHEET    2 AA8 6 THR B 114  VAL B 118  1  O  THR B 117   N  GLU B  10           
SHEET    3 AA8 6 ALA B  92  ASP B 100 -1  N  TYR B  94   O  THR B 114           
SHEET    4 AA8 6 TYR B  32  GLN B  39 -1  N  VAL B  37   O  TYR B  95           
SHEET    5 AA8 6 LEU B  45  ILE B  51 -1  O  MET B  48   N  TRP B  36           
SHEET    6 AA8 6 THR B  58  PHE B  60 -1  O  ASN B  59   N  GLY B  50           
SHEET    1 AA9 4 GLU B  10  LYS B  12  0                                        
SHEET    2 AA9 4 THR B 114  VAL B 118  1  O  THR B 117   N  GLU B  10           
SHEET    3 AA9 4 ALA B  92  ASP B 100 -1  N  TYR B  94   O  THR B 114           
SHEET    4 AA9 4 PHE B 107  TRP B 110 -1  O  TYR B 109   N  ARG B  98           
SHEET    1 AB1 4 SER B 127  LEU B 131  0                                        
SHEET    2 AB1 4 THR B 142  TYR B 152 -1  O  LEU B 148   N  PHE B 129           
SHEET    3 AB1 4 TYR B 183  PRO B 192 -1  O  LEU B 185   N  VAL B 149           
SHEET    4 AB1 4 VAL B 170  THR B 172 -1  N  HIS B 171   O  VAL B 188           
SHEET    1 AB2 4 SER B 127  LEU B 131  0                                        
SHEET    2 AB2 4 THR B 142  TYR B 152 -1  O  LEU B 148   N  PHE B 129           
SHEET    3 AB2 4 TYR B 183  PRO B 192 -1  O  LEU B 185   N  VAL B 149           
SHEET    4 AB2 4 VAL B 176  LEU B 177 -1  N  VAL B 176   O  SER B 184           
SHEET    1 AB3 3 THR B 158  TRP B 161  0                                        
SHEET    2 AB3 3 TYR B 201  HIS B 207 -1  O  ASN B 204   N  SER B 160           
SHEET    3 AB3 3 THR B 212  GLU B 219 -1  O  VAL B 214   N  VAL B 205           
SHEET    1 AB4 4 SER B 239  PHE B 243  0                                        
SHEET    2 AB4 4 GLU B 258  VAL B 266 -1  O  THR B 260   N  PHE B 243           
SHEET    3 AB4 4 TYR B 300  THR B 307 -1  O  SER B 304   N  CYS B 261           
SHEET    4 AB4 4 LYS B 288  THR B 289 -1  N  LYS B 288   O  VAL B 305           
SHEET    1 AB5 4 VAL B 282  VAL B 284  0                                        
SHEET    2 AB5 4 VAL B 273  VAL B 279 -1  N  TRP B 277   O  VAL B 284           
SHEET    3 AB5 4 TYR B 319  ASN B 325 -1  O  LYS B 322   N  ASN B 276           
SHEET    4 AB5 4 ILE B 332  ILE B 336 -1  O  ILE B 332   N  VAL B 323           
SHEET    1 AB6 4 GLN B 347  LEU B 351  0                                        
SHEET    2 AB6 4 GLN B 362  PHE B 372 -1  O  LEU B 368   N  TYR B 349           
SHEET    3 AB6 4 PHE B 404  ASP B 413 -1  O  LEU B 410   N  LEU B 365           
SHEET    4 AB6 4 TYR B 391  THR B 393 -1  N  LYS B 392   O  ARG B 409           
SHEET    1 AB7 4 GLN B 347  LEU B 351  0                                        
SHEET    2 AB7 4 GLN B 362  PHE B 372 -1  O  LEU B 368   N  TYR B 349           
SHEET    3 AB7 4 PHE B 404  ASP B 413 -1  O  LEU B 410   N  LEU B 365           
SHEET    4 AB7 4 VAL B 397  LEU B 398 -1  N  VAL B 397   O  PHE B 405           
SHEET    1 AB8 4 GLN B 386  PRO B 387  0                                        
SHEET    2 AB8 4 ALA B 378  SER B 383 -1  N  SER B 383   O  GLN B 386           
SHEET    3 AB8 4 PHE B 423  MET B 428 -1  O  SER B 426   N  GLU B 380           
SHEET    4 AB8 4 THR B 437  LEU B 441 -1  O  THR B 437   N  VAL B 427           
SHEET    1 AB9 4 LEU F   4  SER F   7  0                                        
SHEET    2 AB9 4 ALA F  19  ALA F  25 -1  O  SER F  22   N  SER F   7           
SHEET    3 AB9 4 ASP F  74  ILE F  79 -1  O  LEU F  77   N  LEU F  21           
SHEET    4 AB9 4 PHE F  66  SER F  71 -1  N  SER F  67   O  THR F  78           
SHEET    1 AC1 6 THR F  10  LEU F  13  0                                        
SHEET    2 AC1 6 THR F 106  ILE F 110  1  O  GLU F 109   N  LEU F  11           
SHEET    3 AC1 6 VAL F  89  HIS F  94 -1  N  TYR F  90   O  THR F 106           
SHEET    4 AC1 6 LEU F  37  GLN F  42 -1  N  GLN F  42   O  VAL F  89           
SHEET    5 AC1 6 ARG F  49  TYR F  53 -1  O  ARG F  49   N  GLN F  41           
SHEET    6 AC1 6 TYR F  57  LEU F  58 -1  O  TYR F  57   N  TYR F  53           
SHEET    1 AC2 4 THR F  10  LEU F  13  0                                        
SHEET    2 AC2 4 THR F 106  ILE F 110  1  O  GLU F 109   N  LEU F  11           
SHEET    3 AC2 4 VAL F  89  HIS F  94 -1  N  TYR F  90   O  THR F 106           
SHEET    4 AC2 4 THR F 101  PHE F 102 -1  O  THR F 101   N  HIS F  94           
SHEET    1 AC3 2 SER F  30  THR F  31  0                                        
SHEET    2 AC3 2 TYR F  34  SER F  35 -1  O  TYR F  34   N  THR F  31           
SHEET    1 AC4 4 SER F 118  PHE F 122  0                                        
SHEET    2 AC4 4 THR F 133  PHE F 143 -1  O  LEU F 139   N  PHE F 120           
SHEET    3 AC4 4 TYR F 177  SER F 186 -1  O  LEU F 179   N  LEU F 140           
SHEET    4 AC4 4 SER F 163  VAL F 167 -1  N  GLN F 164   O  THR F 182           
SHEET    1 AC5 4 ALA F 157  LEU F 158  0                                        
SHEET    2 AC5 4 LYS F 149  VAL F 154 -1  N  VAL F 154   O  ALA F 157           
SHEET    3 AC5 4 VAL F 195  THR F 201 -1  O  ALA F 197   N  LYS F 153           
SHEET    4 AC5 4 VAL F 209  ASN F 214 -1  O  VAL F 209   N  VAL F 200           
SHEET    1 AC6 4 GLN G   3  GLN G   6  0                                        
SHEET    2 AC6 4 VAL G  18  SER G  25 -1  O  LYS G  23   N  VAL G   5           
SHEET    3 AC6 4 THR G  78  LEU G  83 -1  O  LEU G  83   N  VAL G  18           
SHEET    4 AC6 4 VAL G  68  ASP G  73 -1  N  THR G  69   O  GLU G  82           
SHEET    1 AC7 6 GLU G  10  LYS G  12  0                                        
SHEET    2 AC7 6 THR G 114  VAL G 118  1  O  THR G 117   N  LYS G  12           
SHEET    3 AC7 6 ALA G  92  ASP G 100 -1  N  TYR G  94   O  THR G 114           
SHEET    4 AC7 6 TYR G  32  GLN G  39 -1  N  VAL G  37   O  TYR G  95           
SHEET    5 AC7 6 LEU G  45  ILE G  51 -1  O  MET G  48   N  TRP G  36           
SHEET    6 AC7 6 THR G  58  PHE G  60 -1  O  ASN G  59   N  GLY G  50           
SHEET    1 AC8 4 SER G 127  LEU G 131  0                                        
SHEET    2 AC8 4 THR G 142  TYR G 152 -1  O  LEU G 148   N  PHE G 129           
SHEET    3 AC8 4 TYR G 183  PRO G 192 -1  O  LEU G 185   N  VAL G 149           
SHEET    4 AC8 4 VAL G 170  THR G 172 -1  N  HIS G 171   O  VAL G 188           
SHEET    1 AC9 4 SER G 127  LEU G 131  0                                        
SHEET    2 AC9 4 THR G 142  TYR G 152 -1  O  LEU G 148   N  PHE G 129           
SHEET    3 AC9 4 TYR G 183  PRO G 192 -1  O  LEU G 185   N  VAL G 149           
SHEET    4 AC9 4 VAL G 176  LEU G 177 -1  N  VAL G 176   O  SER G 184           
SHEET    1 AD1 3 THR G 158  TRP G 161  0                                        
SHEET    2 AD1 3 TYR G 201  HIS G 207 -1  O  ASN G 204   N  SER G 160           
SHEET    3 AD1 3 THR G 212  GLU G 219 -1  O  VAL G 214   N  VAL G 205           
SHEET    1 AD2 4 SER G 239  PHE G 243  0                                        
SHEET    2 AD2 4 GLU G 258  VAL G 266 -1  O  THR G 260   N  PHE G 243           
SHEET    3 AD2 4 TYR G 300  THR G 307 -1  O  SER G 304   N  CYS G 261           
SHEET    4 AD2 4 LYS G 288  THR G 289 -1  N  LYS G 288   O  VAL G 305           
SHEET    1 AD3 4 SER G 239  PHE G 243  0                                        
SHEET    2 AD3 4 GLU G 258  VAL G 266 -1  O  THR G 260   N  PHE G 243           
SHEET    3 AD3 4 TYR G 300  THR G 307 -1  O  SER G 304   N  CYS G 261           
SHEET    4 AD3 4 GLU G 293  GLU G 294 -1  N  GLU G 293   O  ARG G 301           
SHEET    1 AD4 4 VAL G 282  VAL G 284  0                                        
SHEET    2 AD4 4 GLN G 274  VAL G 279 -1  N  TRP G 277   O  VAL G 284           
SHEET    3 AD4 4 TYR G 319  SER G 324 -1  O  LYS G 322   N  ASN G 276           
SHEET    4 AD4 4 ILE G 332  ILE G 336 -1  O  ILE G 332   N  VAL G 323           
SHEET    1 AD5 4 GLN G 347  LEU G 351  0                                        
SHEET    2 AD5 4 GLN G 362  PHE G 372 -1  O  LYS G 370   N  GLN G 347           
SHEET    3 AD5 4 PHE G 404  ASP G 413 -1  O  VAL G 412   N  VAL G 363           
SHEET    4 AD5 4 TYR G 391  THR G 393 -1  N  LYS G 392   O  ARG G 409           
SHEET    1 AD6 4 GLN G 347  LEU G 351  0                                        
SHEET    2 AD6 4 GLN G 362  PHE G 372 -1  O  LYS G 370   N  GLN G 347           
SHEET    3 AD6 4 PHE G 404  ASP G 413 -1  O  VAL G 412   N  VAL G 363           
SHEET    4 AD6 4 VAL G 397  LEU G 398 -1  N  VAL G 397   O  PHE G 405           
SHEET    1 AD7 4 GLN G 386  PRO G 387  0                                        
SHEET    2 AD7 4 ALA G 378  SER G 383 -1  N  SER G 383   O  GLN G 386           
SHEET    3 AD7 4 PHE G 423  MET G 428 -1  O  SER G 426   N  GLU G 380           
SHEET    4 AD7 4 THR G 437  LEU G 441 -1  O  LEU G 441   N  PHE G 423           
SSBOND   1 CYS A   23    CYS A   92                          1555   1555  2.51  
SSBOND   2 CYS A  138    CYS A  198                          1555   1555  2.02  
SSBOND   3 CYS A  218    CYS B  134                          1555   1555  2.04  
SSBOND   4 CYS B   22    CYS B   96                          1555   1555  2.08  
SSBOND   5 CYS B  147    CYS B  203                          1555   1555  2.06  
SSBOND   6 CYS B  226    CYS G  226                          1555   1555  2.03  
SSBOND   7 CYS B  229    CYS G  229                          1555   1555  2.03  
SSBOND   8 CYS B  261    CYS B  321                          1555   1555  2.04  
SSBOND   9 CYS B  367    CYS B  425                          1555   1555  2.02  
SSBOND  10 CYS F   23    CYS F   92                          1555   1555  2.55  
SSBOND  11 CYS F  138    CYS F  198                          1555   1555  2.04  
SSBOND  12 CYS F  218    CYS G  134                          1555   1555  2.04  
SSBOND  13 CYS G   22    CYS G   96                          1555   1555  2.04  
SSBOND  14 CYS G  147    CYS G  203                          1555   1555  2.04  
SSBOND  15 CYS G  261    CYS G  321                          1555   1555  2.05  
SSBOND  16 CYS G  367    CYS G  425                          1555   1555  2.04  
LINK         ND2 ASN G 297                 C1  NAG D   1     1555   1555  1.44  
LINK         O4  NAG C   1                 C1  NAG C   2     1555   1555  1.42  
LINK         O4  NAG C   2                 C1  BMA C   3     1555   1555  1.40  
LINK         O3  BMA C   3                 C1  MAN C   4     1555   1555  1.43  
LINK         O6  BMA C   3                 C1  MAN C   6     1555   1555  1.41  
LINK         O2  MAN C   4                 C1  NAG C   5     1555   1555  1.43  
LINK         O2  MAN C   6                 C1  NAG C   7     1555   1555  1.42  
LINK         O4  NAG D   1                 C1  NAG D   2     1555   1555  1.43  
LINK         O6  NAG D   1                 C1  FUC D   7     1555   1555  1.41  
LINK         O4  NAG D   2                 C1  BMA D   3     1555   1555  1.42  
LINK         O6  BMA D   3                 C1  MAN D   4     1555   1555  1.40  
LINK         O3  BMA D   3                 C1  MAN D   6     1555   1555  1.42  
LINK         O2  MAN D   4                 C1  NAG D   5     1555   1555  1.41  
LINK         C1  GLC E   1                 O2  FRU E   2     1555   1555  1.41  
LINK         C1  GLC H   1                 O2  FRU H   2     1555   1555  1.42  
LINK         C1  GLC I   1                 O2  FRU I   2     1555   1555  1.42  
CISPEP   1 SER A    7    PRO A    8          0        -8.51                     
CISPEP   2 LEU A   98    PRO A   99          0        -4.08                     
CISPEP   3 TYR A  144    PRO A  145          0         2.87                     
CISPEP   4 THR B  138    SER B  139          0         1.78                     
CISPEP   5 PHE B  153    PRO B  154          0        -4.63                     
CISPEP   6 GLU B  155    PRO B  156          0        -2.99                     
CISPEP   7 TYR B  222    GLY B  223          0        20.68                     
CISPEP   8 PRO B  224    PRO B  225          0        16.98                     
CISPEP   9 LYS B  246    PRO B  247          0        -7.46                     
CISPEP  10 LEU B  251    MET B  252          0        -0.44                     
CISPEP  11 SER B  254    ARG B  255          0         1.38                     
CISPEP  12 GLN B  295    PHE B  296          0         0.78                     
CISPEP  13 TYR B  373    PRO B  374          0         3.31                     
CISPEP  14 SER F    7    PRO F    8          0        -7.73                     
CISPEP  15 LEU F   98    PRO F   99          0         8.30                     
CISPEP  16 TYR F  144    PRO F  145          0        -0.64                     
CISPEP  17 ALA G  121    SER G  122          0        12.36                     
CISPEP  18 PHE G  153    PRO G  154          0        -6.76                     
CISPEP  19 GLU G  155    PRO G  156          0         3.11                     
CISPEP  20 PRO G  224    PRO G  225          0         4.35                     
CISPEP  21 TYR G  373    PRO G  374          0        -7.80                     
CRYST1   63.830  110.830  264.960  90.00  90.00  90.00 P 21 21 21    8          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.015667  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.009023  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.003774        0.00000                         
ATOM      1  N   GLU A   1       9.227  -4.698 -95.607  1.00 46.98           N  
ANISOU    1  N   GLU A   1     5668   6628   5556   -198    398    291       N  
ATOM      2  CA  GLU A   1      10.294  -4.659 -94.606  1.00 46.14           C  
ANISOU    2  CA  GLU A   1     5556   6454   5523   -157    468    239       C  
ATOM      3  C   GLU A   1      11.184  -5.906 -94.675  1.00 52.57           C  
ANISOU    3  C   GLU A   1     6415   7291   6266   -155    531    131       C  
ATOM      4  O   GLU A   1      10.782  -6.919 -95.254  1.00 52.79           O  
ANISOU    4  O   GLU A   1     6488   7366   6207   -181    520     75       O  
ATOM      5  CB  GLU A   1       9.699  -4.556 -93.188  1.00 46.05           C  
ANISOU    5  CB  GLU A   1     5514   6345   5640   -117    457    214       C  
ATOM      6  CG  GLU A   1       8.758  -5.683 -92.809  1.00 50.46           C  
ANISOU    6  CG  GLU A   1     6084   6894   6194   -116    430    141       C  
ATOM      7  CD  GLU A   1       8.122  -5.620 -91.431  1.00 68.80           C  
ANISOU    7  CD  GLU A   1     8380   9124   8637    -78    427    120       C  
ATOM      8  OE1 GLU A   1       7.614  -6.669 -90.977  1.00 73.07           O  
ANISOU    8  OE1 GLU A   1     8934   9652   9178    -74    421     47       O  
ATOM      9  OE2 GLU A   1       8.111  -4.538 -90.807  1.00 62.48           O  
ANISOU    9  OE2 GLU A   1     7551   8261   7927    -53    434    173       O  
ATOM     10  N   ILE A   2      12.375  -5.860 -94.028  1.00 47.00           N  
ANISOU   10  N   ILE A   2     5700   6548   5610   -126    595    104       N  
ATOM     11  CA  ILE A   2      13.229  -7.042 -94.009  1.00 44.38           C  
ANISOU   11  CA  ILE A   2     5401   6228   5235   -114    661     12       C  
ATOM     12  C   ILE A   2      12.662  -7.978 -92.956  1.00 45.09           C  
ANISOU   12  C   ILE A   2     5495   6258   5379    -90    649    -72       C  
ATOM     13  O   ILE A   2      12.320  -7.522 -91.893  1.00 44.68           O  
ANISOU   13  O   ILE A   2     5411   6140   5425    -69    624    -60       O  
ATOM     14  CB  ILE A   2      14.692  -6.637 -93.717  1.00 46.77           C  
ANISOU   14  CB  ILE A   2     5675   6515   5580    -93    727     30       C  
ATOM     15  CG1 ILE A   2      15.244  -5.817 -94.919  1.00 46.18           C  
ANISOU   15  CG1 ILE A   2     5600   6510   5438   -121    747    114       C  
ATOM     16  CG2 ILE A   2      15.561  -7.879 -93.359  1.00 45.90           C  
ANISOU   16  CG2 ILE A   2     5579   6394   5466    -66    798    -60       C  
ATOM     17  CD1 ILE A   2      16.487  -5.282 -94.758  1.00 41.86           C  
ANISOU   17  CD1 ILE A   2     5017   5955   4934   -111    800    153       C  
ATOM     18  N   VAL A   3      12.535  -9.260 -93.250  1.00 39.54           N  
ANISOU   18  N   VAL A   3     4836   5575   4611    -96    669   -156       N  
ATOM     19  CA  VAL A   3      12.059 -10.255 -92.296  1.00 37.07           C  
ANISOU   19  CA  VAL A   3     4532   5207   4348    -76    664   -235       C  
ATOM     20  C   VAL A   3      13.283 -11.032 -91.866  1.00 39.63           C  
ANISOU   20  C   VAL A   3     4861   5507   4689    -42    744   -295       C  
ATOM     21  O   VAL A   3      14.044 -11.507 -92.692  1.00 40.04           O  
ANISOU   21  O   VAL A   3     4942   5601   4669    -46    804   -319       O  
ATOM     22  CB  VAL A   3      10.939 -11.168 -92.858  1.00 40.23           C  
ANISOU   22  CB  VAL A   3     4975   5634   4677   -111    621   -283       C  
ATOM     23  CG1 VAL A   3      10.614 -12.326 -91.895  1.00 39.49           C  
ANISOU   23  CG1 VAL A   3     4891   5480   4634    -90    630   -369       C  
ATOM     24  CG2 VAL A   3       9.696 -10.359 -93.147  1.00 39.52           C  
ANISOU   24  CG2 VAL A   3     4858   5563   4594   -141    534   -206       C  
ATOM     25  N   LEU A   4      13.474 -11.148 -90.576  1.00 37.26           N  
ANISOU   25  N   LEU A   4     4531   5140   4485     -9    747   -314       N  
ATOM     26  CA  LEU A   4      14.599 -11.851 -89.988  1.00 36.56           C  
ANISOU   26  CA  LEU A   4     4433   5023   4435     25    811   -355       C  
ATOM     27  C   LEU A   4      14.073 -13.129 -89.406  1.00 38.67           C  
ANISOU   27  C   LEU A   4     4726   5251   4717     39    812   -436       C  
ATOM     28  O   LEU A   4      13.339 -13.103 -88.427  1.00 39.65           O  
ANISOU   28  O   LEU A   4     4837   5326   4901     45    768   -442       O  
ATOM     29  CB  LEU A   4      15.256 -11.023 -88.890  1.00 35.53           C  
ANISOU   29  CB  LEU A   4     4253   4848   4400     42    803   -308       C  
ATOM     30  CG  LEU A   4      15.934  -9.721 -89.260  1.00 38.97           C  
ANISOU   30  CG  LEU A   4     4656   5306   4843     27    804   -224       C  
ATOM     31  CD1 LEU A   4      16.652  -9.135 -88.010  1.00 39.21           C  
ANISOU   31  CD1 LEU A   4     4646   5281   4969     35    795   -196       C  
ATOM     32  CD2 LEU A   4      16.941  -9.903 -90.367  1.00 40.19           C  
ANISOU   32  CD2 LEU A   4     4812   5523   4935     25    870   -211       C  
ATOM     33  N   THR A   5      14.423 -14.248 -90.033  1.00 35.24           N  
ANISOU   33  N   THR A   5     4331   4832   4225     43    869   -499       N  
ATOM     34  CA  THR A   5      13.980 -15.592 -89.642  1.00 33.91           C  
ANISOU   34  CA  THR A   5     4196   4623   4066     54    880   -581       C  
ATOM     35  C   THR A   5      15.006 -16.230 -88.687  1.00 36.83           C  
ANISOU   35  C   THR A   5     4535   4942   4516    103    936   -600       C  
ATOM     36  O   THR A   5      16.114 -16.564 -89.104  1.00 36.96           O  
ANISOU   36  O   THR A   5     4548   4971   4523    127   1012   -605       O  
ATOM     37  CB  THR A   5      13.740 -16.419 -90.926  1.00 35.28           C  
ANISOU   37  CB  THR A   5     4441   4836   4128     24    911   -641       C  
ATOM     38  OG1 THR A   5      12.654 -15.836 -91.634  1.00 37.33           O  
ANISOU   38  OG1 THR A   5     4720   5142   4323    -28    837   -612       O  
ATOM     39  CG2 THR A   5      13.417 -17.811 -90.664  1.00 29.97           C  
ANISOU   39  CG2 THR A   5     3810   4117   3461     31    934   -728       C  
ATOM     40  N   GLN A   6      14.607 -16.447 -87.436  1.00 32.84           N  
ANISOU   40  N   GLN A   6     4010   4382   4087    118    900   -608       N  
ATOM     41  CA  GLN A   6      15.454 -17.071 -86.417  1.00 32.37           C  
ANISOU   41  CA  GLN A   6     3920   4275   4105    158    936   -616       C  
ATOM     42  C   GLN A   6      15.108 -18.533 -86.276  1.00 39.23           C  
ANISOU   42  C   GLN A   6     4825   5102   4977    173    965   -692       C  
ATOM     43  O   GLN A   6      13.949 -18.921 -86.475  1.00 38.75           O  
ANISOU   43  O   GLN A   6     4804   5036   4884    146    929   -733       O  
ATOM     44  CB  GLN A   6      15.325 -16.372 -85.045  1.00 31.33           C  
ANISOU   44  CB  GLN A   6     3749   4105   4049    160    881   -574       C  
ATOM     45  CG  GLN A   6      16.161 -15.085 -85.041  1.00 27.03           C  
ANISOU   45  CG  GLN A   6     3164   3585   3521    152    872   -499       C  
ATOM     46  CD  GLN A   6      16.224 -14.455 -83.693  1.00 34.44           C  
ANISOU   46  CD  GLN A   6     4077   4482   4526    148    827   -465       C  
ATOM     47  OE1 GLN A   6      15.512 -13.505 -83.422  1.00 35.50           O  
ANISOU   47  OE1 GLN A   6     4219   4606   4664    126    780   -442       O  
ATOM     48  NE2 GLN A   6      17.124 -14.908 -82.844  1.00 24.28           N  
ANISOU   48  NE2 GLN A   6     2761   3171   3292    166    841   -456       N  
ATOM     49  N   SER A   7      16.139 -19.357 -86.018  1.00 36.55           N  
ANISOU   49  N   SER A   7     4470   4737   4682    215   1033   -705       N  
ATOM     50  CA  SER A   7      15.961 -20.791 -85.813  1.00 36.83           C  
ANISOU   50  CA  SER A   7     4538   4720   4736    236   1072   -772       C  
ATOM     51  C   SER A   7      17.106 -21.344 -85.013  1.00 41.76           C  
ANISOU   51  C   SER A   7     5112   5305   5448    287   1121   -747       C  
ATOM     52  O   SER A   7      18.204 -20.817 -85.076  1.00 44.39           O  
ANISOU   52  O   SER A   7     5395   5664   5806    307   1152   -692       O  
ATOM     53  CB  SER A   7      15.832 -21.537 -87.133  1.00 38.47           C  
ANISOU   53  CB  SER A   7     4814   4942   4861    224   1132   -841       C  
ATOM     54  OG  SER A   7      16.932 -21.262 -87.984  1.00 47.22           O  
ANISOU   54  OG  SER A   7     5915   6089   5939    242   1207   -820       O  
ATOM     55  N   PRO A   8      16.885 -22.379 -84.216  1.00 39.00           N  
ANISOU   55  N   PRO A   8     4768   4896   5153    309   1126   -777       N  
ATOM     56  CA  PRO A   8      15.586 -22.976 -83.872  1.00 38.30           C  
ANISOU   56  CA  PRO A   8     4725   4772   5056    284   1082   -830       C  
ATOM     57  C   PRO A   8      14.791 -22.039 -82.948  1.00 40.35           C  
ANISOU   57  C   PRO A   8     4962   5038   5331    257    991   -789       C  
ATOM     58  O   PRO A   8      15.313 -21.062 -82.441  1.00 41.83           O  
ANISOU   58  O   PRO A   8     5106   5246   5541    257    964   -727       O  
ATOM     59  CB  PRO A   8      16.005 -24.273 -83.173  1.00 40.17           C  
ANISOU   59  CB  PRO A   8     4953   4940   5368    328   1129   -849       C  
ATOM     60  CG  PRO A   8      17.231 -23.883 -82.438  1.00 45.80           C  
ANISOU   60  CG  PRO A   8     5592   5658   6150    363   1139   -771       C  
ATOM     61  CD  PRO A   8      17.961 -22.927 -83.367  1.00 40.75           C  
ANISOU   61  CD  PRO A   8     4934   5081   5468    358   1164   -739       C  
ATOM     62  N   ALA A   9      13.533 -22.304 -82.746  1.00 37.34           N  
ANISOU   62  N   ALA A   9     4612   4638   4939    230    947   -822       N  
ATOM     63  CA  ALA A   9      12.701 -21.518 -81.817  1.00 36.88           C  
ANISOU   63  CA  ALA A   9     4536   4575   4903    210    878   -787       C  
ATOM     64  C   ALA A   9      13.208 -21.694 -80.373  1.00 40.93           C  
ANISOU   64  C   ALA A   9     5017   5047   5488    237    873   -753       C  
ATOM     65  O   ALA A   9      13.102 -20.784 -79.549  1.00 38.19           O  
ANISOU   65  O   ALA A   9     4652   4701   5158    227    832   -710       O  
ATOM     66  CB  ALA A   9      11.262 -22.012 -81.870  1.00 36.58           C  
ANISOU   66  CB  ALA A   9     4530   4518   4851    181    844   -827       C  
ATOM     67  N   THR A  10      13.611 -22.930 -80.061  1.00 38.37           N  
ANISOU   67  N   THR A  10     4695   4680   5203    265    914   -777       N  
ATOM     68  CA  THR A  10      14.053 -23.336 -78.733  1.00 38.92           C  
ANISOU   68  CA  THR A  10     4738   4711   5338    288    909   -744       C  
ATOM     69  C   THR A  10      15.275 -24.198 -78.857  1.00 39.30           C  
ANISOU   69  C   THR A  10     4762   4741   5431    331    970   -735       C  
ATOM     70  O   THR A  10      15.442 -24.922 -79.820  1.00 38.94           O  
ANISOU   70  O   THR A  10     4739   4687   5371    347   1029   -781       O  
ATOM     71  CB  THR A  10      12.901 -24.064 -77.940  1.00 45.97           C  
ANISOU   71  CB  THR A  10     5658   5556   6254    278    886   -771       C  
ATOM     72  OG1 THR A  10      11.794 -23.165 -77.859  1.00 52.09           O  
ANISOU   72  OG1 THR A  10     6446   6350   6998    244    838   -769       O  
ATOM     73  CG2 THR A  10      13.296 -24.399 -76.505  1.00 47.82           C  
ANISOU   73  CG2 THR A  10     5870   5756   6545    295    874   -729       C  
ATOM     74  N   LEU A  11      16.121 -24.121 -77.876  1.00 37.10           N  
ANISOU   74  N   LEU A  11     4438   4455   5205    349    958   -674       N  
ATOM     75  CA  LEU A  11      17.352 -24.873 -77.851  1.00 38.60           C  
ANISOU   75  CA  LEU A  11     4584   4626   5454    394   1012   -643       C  
ATOM     76  C   LEU A  11      17.602 -25.253 -76.407  1.00 43.02           C  
ANISOU   76  C   LEU A  11     5116   5156   6076    402    976   -589       C  
ATOM     77  O   LEU A  11      17.637 -24.381 -75.553  1.00 42.66           O  
ANISOU   77  O   LEU A  11     5057   5132   6020    371    911   -543       O  
ATOM     78  CB  LEU A  11      18.420 -23.932 -78.422  1.00 39.62           C  
ANISOU   78  CB  LEU A  11     4669   4810   5576    396   1024   -595       C  
ATOM     79  CG  LEU A  11      19.770 -24.434 -78.723  1.00 46.57           C  
ANISOU   79  CG  LEU A  11     5492   5687   6514    443   1091   -554       C  
ATOM     80  CD1 LEU A  11      19.733 -25.767 -79.572  1.00 46.16           C  
ANISOU   80  CD1 LEU A  11     5474   5590   6475    487   1189   -620       C  
ATOM     81  CD2 LEU A  11      20.569 -23.329 -79.452  1.00 48.32           C  
ANISOU   81  CD2 LEU A  11     5677   5970   6710    432   1100   -513       C  
ATOM     82  N   SER A  12      17.657 -26.554 -76.122  1.00 41.61           N  
ANISOU   82  N   SER A  12     4936   4921   5951    437   1015   -598       N  
ATOM     83  CA  SER A  12      17.850 -27.084 -74.777  1.00 42.16           C  
ANISOU   83  CA  SER A  12     4980   4959   6078    445    983   -543       C  
ATOM     84  C   SER A  12      19.192 -27.786 -74.763  1.00 46.31           C  
ANISOU   84  C   SER A  12     5440   5468   6689    498   1032   -482       C  
ATOM     85  O   SER A  12      19.394 -28.730 -75.509  1.00 46.80           O  
ANISOU   85  O   SER A  12     5507   5489   6785    542   1114   -518       O  
ATOM     86  CB  SER A  12      16.740 -28.060 -74.402  1.00 44.83           C  
ANISOU   86  CB  SER A  12     5368   5241   6424    443    987   -592       C  
ATOM     87  OG  SER A  12      16.872 -28.391 -73.028  1.00 55.09           O  
ANISOU   87  OG  SER A  12     6648   6519   7766    442    947   -530       O  
ATOM     88  N   LEU A  13      20.129 -27.281 -73.968  1.00 42.42           N  
ANISOU   88  N   LEU A  13     4884   5005   6227    491    985   -389       N  
ATOM     89  CA  LEU A  13      21.486 -27.798 -73.941  1.00 41.77           C  
ANISOU   89  CA  LEU A  13     4719   4917   6235    540   1025   -309       C  
ATOM     90  C   LEU A  13      22.050 -27.823 -72.527  1.00 41.24           C  
ANISOU   90  C   LEU A  13     4599   4855   6214    525    950   -204       C  
ATOM     91  O   LEU A  13      21.694 -26.995 -71.677  1.00 38.87           O  
ANISOU   91  O   LEU A  13     4323   4586   5859    465    862   -186       O  
ATOM     92  CB  LEU A  13      22.365 -26.877 -74.821  1.00 42.39           C  
ANISOU   92  CB  LEU A  13     4753   5052   6302    540   1046   -285       C  
ATOM     93  CG  LEU A  13      22.175 -26.941 -76.350  1.00 47.02           C  
ANISOU   93  CG  LEU A  13     5377   5639   6849    563   1136   -368       C  
ATOM     94  CD1 LEU A  13      22.821 -25.727 -77.025  1.00 47.33           C  
ANISOU   94  CD1 LEU A  13     5383   5747   6855    542   1132   -339       C  
ATOM     95  CD2 LEU A  13      22.776 -28.201 -76.917  1.00 47.30           C  
ANISOU   95  CD2 LEU A  13     5391   5620   6960    636   1248   -376       C  
ATOM     96  N   SER A  14      23.032 -28.689 -72.327  1.00 38.63           N  
ANISOU   96  N   SER A  14     4194   4499   5985    577    986   -129       N  
ATOM     97  CA  SER A  14      23.744 -28.771 -71.048  1.00 39.56           C  
ANISOU   97  CA  SER A  14     4248   4630   6154    562    911     -9       C  
ATOM     98  C   SER A  14      24.826 -27.711 -70.961  1.00 44.04           C  
ANISOU   98  C   SER A  14     4742   5266   6726    529    856     78       C  
ATOM     99  O   SER A  14      25.432 -27.330 -71.977  1.00 43.57           O  
ANISOU   99  O   SER A  14     4643   5230   6681    552    912     74       O  
ATOM    100  CB  SER A  14      24.394 -30.142 -70.859  1.00 40.42           C  
ANISOU  100  CB  SER A  14     4292   4680   6385    635    969     56       C  
ATOM    101  OG  SER A  14      23.420 -31.094 -70.472  1.00 53.12           O  
ANISOU  101  OG  SER A  14     5964   6224   7993    647    985      5       O  
ATOM    102  N   PRO A  15      25.180 -27.312 -69.732  1.00 39.78           N  
ANISOU  102  N   PRO A  15     4177   4758   6181    474    750    167       N  
ATOM    103  CA  PRO A  15      26.301 -26.379 -69.580  1.00 39.57           C  
ANISOU  103  CA  PRO A  15     4073   4794   6170    434    689    262       C  
ATOM    104  C   PRO A  15      27.617 -26.990 -70.111  1.00 43.51           C  
ANISOU  104  C   PRO A  15     4445   5291   6796    504    754    356       C  
ATOM    105  O   PRO A  15      27.880 -28.188 -69.956  1.00 43.66           O  
ANISOU  105  O   PRO A  15     4420   5262   6908    569    805    397       O  
ATOM    106  CB  PRO A  15      26.334 -26.122 -68.059  1.00 40.83           C  
ANISOU  106  CB  PRO A  15     4242   4974   6296    360    563    336       C  
ATOM    107  CG  PRO A  15      24.976 -26.433 -67.598  1.00 42.76           C  
ANISOU  107  CG  PRO A  15     4599   5181   6469    348    561    246       C  
ATOM    108  CD  PRO A  15      24.552 -27.599 -68.428  1.00 39.15           C  
ANISOU  108  CD  PRO A  15     4145   4662   6067    435    675    184       C  
ATOM    109  N   GLY A  16      28.396 -26.170 -70.808  1.00 40.52           N  
ANISOU  109  N   GLY A  16     4008   4958   6428    495    766    386       N  
ATOM    110  CA  GLY A  16      29.641 -26.590 -71.426  1.00 40.54           C  
ANISOU  110  CA  GLY A  16     3887   4964   6551    561    842    474       C  
ATOM    111  C   GLY A  16      29.489 -26.910 -72.896  1.00 45.17           C  
ANISOU  111  C   GLY A  16     4497   5522   7144    634    989    381       C  
ATOM    112  O   GLY A  16      30.496 -27.029 -73.589  1.00 45.15           O  
ANISOU  112  O   GLY A  16     4401   5528   7225    686   1068    441       O  
ATOM    113  N   GLU A  17      28.240 -27.058 -73.392  1.00 42.20           N  
ANISOU  113  N   GLU A  17     4243   5113   6678    636   1029    240       N  
ATOM    114  CA  GLU A  17      27.985 -27.319 -74.803  1.00 42.03           C  
ANISOU  114  CA  GLU A  17     4265   5068   6637    688   1157    142       C  
ATOM    115  C   GLU A  17      28.020 -26.022 -75.609  1.00 46.24           C  
ANISOU  115  C   GLU A  17     4814   5664   7090    643   1149    112       C  
ATOM    116  O   GLU A  17      27.790 -24.930 -75.112  1.00 46.50           O  
ANISOU  116  O   GLU A  17     4866   5742   7058    566   1045    124       O  
ATOM    117  CB  GLU A  17      26.629 -28.019 -75.031  1.00 41.84           C  
ANISOU  117  CB  GLU A  17     4362   4987   6551    697   1193     10       C  
ATOM    118  CG  GLU A  17      26.553 -29.463 -74.539  1.00 54.31           C  
ANISOU  118  CG  GLU A  17     5934   6486   8214    755   1236     22       C  
ATOM    119  CD  GLU A  17      25.313 -30.209 -75.008  1.00 70.84           C  
ANISOU  119  CD  GLU A  17     8142   8518  10255    766   1289   -112       C  
ATOM    120  OE1 GLU A  17      25.266 -30.582 -76.203  1.00 83.75           O  
ANISOU  120  OE1 GLU A  17     9814  10125  11881    806   1400   -190       O  
ATOM    121  OE2 GLU A  17      24.360 -30.360 -74.211  1.00 64.66           O  
ANISOU  121  OE2 GLU A  17     7418   7719   9432    727   1219   -141       O  
ATOM    122  N   ARG A  18      28.295 -26.158 -76.872  1.00 43.97           N  
ANISOU  122  N   ARG A  18     4526   5374   6806    691   1266     71       N  
ATOM    123  CA  ARG A  18      28.261 -25.039 -77.807  1.00 42.42           C  
ANISOU  123  CA  ARG A  18     4355   5234   6530    655   1275     37       C  
ATOM    124  C   ARG A  18      26.810 -24.809 -78.287  1.00 44.81           C  
ANISOU  124  C   ARG A  18     4792   5529   6706    620   1264    -99       C  
ATOM    125  O   ARG A  18      26.196 -25.742 -78.786  1.00 46.60           O  
ANISOU  125  O   ARG A  18     5084   5705   6918    658   1337   -185       O  
ATOM    126  CB  ARG A  18      29.145 -25.375 -79.000  1.00 40.95           C  
ANISOU  126  CB  ARG A  18     4118   5048   6393    723   1417     49       C  
ATOM    127  CG  ARG A  18      29.144 -24.353 -80.136  1.00 58.66           C  
ANISOU  127  CG  ARG A  18     6389   7346   8552    695   1450     14       C  
ATOM    128  CD  ARG A  18      30.259 -24.665 -81.118  1.00 69.14           C  
ANISOU  128  CD  ARG A  18     7645   8678   9946    764   1592     56       C  
ATOM    129  NE  ARG A  18      31.400 -23.784 -80.856  1.00 87.66           N  
ANISOU  129  NE  ARG A  18     9867  11082  12356    741   1550    189       N  
ATOM    130  CZ  ARG A  18      32.097 -23.100 -81.765  1.00102.17           C  
ANISOU  130  CZ  ARG A  18    11662  12970  14190    742   1613    225       C  
ATOM    131  NH1 ARG A  18      31.796 -23.192 -83.063  1.00 88.18           N  
ANISOU  131  NH1 ARG A  18     9965  11197  12341    769   1729    136       N  
ATOM    132  NH2 ARG A  18      33.098 -22.317 -81.387  1.00 83.65           N  
ANISOU  132  NH2 ARG A  18     9198  10674  11912    711   1558    353       N  
ATOM    133  N   ALA A  19      26.277 -23.585 -78.190  1.00 39.14           N  
ANISOU  133  N   ALA A  19     4113   4855   5904    548   1177   -114       N  
ATOM    134  CA  ALA A  19      24.946 -23.264 -78.741  1.00 37.52           C  
ANISOU  134  CA  ALA A  19     4019   4649   5589    517   1168   -225       C  
ATOM    135  C   ALA A  19      25.092 -22.503 -80.055  1.00 42.90           C  
ANISOU  135  C   ALA A  19     4714   5377   6211    509   1219   -248       C  
ATOM    136  O   ALA A  19      25.864 -21.555 -80.111  1.00 43.82           O  
ANISOU  136  O   ALA A  19     4771   5539   6339    484   1194   -177       O  
ATOM    137  CB  ALA A  19      24.141 -22.456 -77.749  1.00 37.26           C  
ANISOU  137  CB  ALA A  19     4025   4624   5506    449   1048   -228       C  
ATOM    138  N   THR A  20      24.353 -22.901 -81.109  1.00 41.00           N  
ANISOU  138  N   THR A  20     4552   5124   5901    523   1285   -345       N  
ATOM    139  CA  THR A  20      24.427 -22.270 -82.458  1.00 40.13           C  
ANISOU  139  CA  THR A  20     4467   5061   5720    514   1340   -371       C  
ATOM    140  C   THR A  20      23.036 -21.752 -82.856  1.00 40.74           C  
ANISOU  140  C   THR A  20     4640   5152   5688    462   1286   -449       C  
ATOM    141  O   THR A  20      22.116 -22.536 -83.106  1.00 39.34           O  
ANISOU  141  O   THR A  20     4536   4941   5472    465   1303   -532       O  
ATOM    142  CB  THR A  20      24.955 -23.244 -83.497  1.00 42.70           C  
ANISOU  142  CB  THR A  20     4801   5365   6056    575   1481   -407       C  
ATOM    143  OG1 THR A  20      26.256 -23.637 -83.109  1.00 45.35           O  
ANISOU  143  OG1 THR A  20     5034   5688   6508    627   1531   -318       O  
ATOM    144  CG2 THR A  20      25.017 -22.621 -84.883  1.00 44.97           C  
ANISOU  144  CG2 THR A  20     5124   5705   6256    561   1539   -432       C  
ATOM    145  N   LEU A  21      22.904 -20.435 -82.928  1.00 36.25           N  
ANISOU  145  N   LEU A  21     4066   4631   5077    413   1222   -415       N  
ATOM    146  CA  LEU A  21      21.623 -19.756 -83.223  1.00 34.21           C  
ANISOU  146  CA  LEU A  21     3879   4388   4730    364   1162   -465       C  
ATOM    147  C   LEU A  21      21.728 -19.138 -84.588  1.00 38.35           C  
ANISOU  147  C   LEU A  21     4425   4965   5182    351   1205   -470       C  
ATOM    148  O   LEU A  21      22.745 -18.517 -84.888  1.00 38.24           O  
ANISOU  148  O   LEU A  21     4353   4986   5189    354   1232   -404       O  
ATOM    149  CB  LEU A  21      21.386 -18.668 -82.193  1.00 32.53           C  
ANISOU  149  CB  LEU A  21     3647   4179   4532    319   1059   -416       C  
ATOM    150  CG  LEU A  21      20.988 -19.127 -80.819  1.00 34.16           C  
ANISOU  150  CG  LEU A  21     3858   4339   4784    317   1003   -419       C  
ATOM    151  CD1 LEU A  21      22.147 -19.697 -80.078  1.00 35.83           C  
ANISOU  151  CD1 LEU A  21     3997   4535   5080    346   1017   -358       C  
ATOM    152  CD2 LEU A  21      20.435 -18.017 -80.045  1.00 32.26           C  
ANISOU  152  CD2 LEU A  21     3632   4099   4527    267    915   -399       C  
ATOM    153  N   SER A  22      20.719 -19.312 -85.435  1.00 35.23           N  
ANISOU  153  N   SER A  22     4106   4578   4700    332   1211   -541       N  
ATOM    154  CA  SER A  22      20.848 -18.779 -86.787  1.00 36.44           C  
ANISOU  154  CA  SER A  22     4285   4787   4772    316   1254   -542       C  
ATOM    155  C   SER A  22      19.818 -17.693 -87.063  1.00 40.72           C  
ANISOU  155  C   SER A  22     4861   5363   5247    261   1171   -536       C  
ATOM    156  O   SER A  22      18.755 -17.676 -86.468  1.00 38.90           O  
ANISOU  156  O   SER A  22     4657   5107   5016    240   1100   -562       O  
ATOM    157  CB  SER A  22      20.848 -19.910 -87.822  1.00 37.74           C  
ANISOU  157  CB  SER A  22     4512   4944   4884    340   1354   -619       C  
ATOM    158  OG  SER A  22      19.628 -19.937 -88.536  1.00 58.53           O  
ANISOU  158  OG  SER A  22     7230   7593   7417    297   1320   -683       O  
ATOM    159  N   CYS A  23      20.213 -16.715 -87.870  1.00 40.06           N  
ANISOU  159  N   CYS A  23     4765   5334   5122    241   1181   -488       N  
ATOM    160  CA  CYS A  23      19.370 -15.602 -88.278  1.00 40.28           C  
ANISOU  160  CA  CYS A  23     4816   5396   5092    193   1112   -465       C  
ATOM    161  C   CYS A  23      19.545 -15.449 -89.761  1.00 44.95           C  
ANISOU  161  C   CYS A  23     5444   6048   5588    180   1168   -467       C  
ATOM    162  O   CYS A  23      20.654 -15.191 -90.194  1.00 45.26           O  
ANISOU  162  O   CYS A  23     5446   6115   5636    196   1233   -423       O  
ATOM    163  CB  CYS A  23      19.758 -14.312 -87.568  1.00 41.40           C  
ANISOU  163  CB  CYS A  23     4900   5538   5291    175   1055   -383       C  
ATOM    164  SG  CYS A  23      18.870 -12.856 -88.189  1.00 45.52           S  
ANISOU  164  SG  CYS A  23     5443   6096   5755    125    988   -339       S  
ATOM    165  N   ARG A  24      18.461 -15.539 -90.518  1.00 42.17           N  
ANISOU  165  N   ARG A  24     5159   5719   5146    146   1139   -509       N  
ATOM    166  CA  ARG A  24      18.449 -15.385 -91.964  1.00 41.33           C  
ANISOU  166  CA  ARG A  24     5103   5676   4926    119   1178   -513       C  
ATOM    167  C   ARG A  24      17.611 -14.163 -92.339  1.00 40.99           C  
ANISOU  167  C   ARG A  24     5062   5673   4838     70   1091   -456       C  
ATOM    168  O   ARG A  24      16.428 -14.100 -92.000  1.00 39.81           O  
ANISOU  168  O   ARG A  24     4929   5508   4689     47   1010   -470       O  
ATOM    169  CB  ARG A  24      17.861 -16.637 -92.626  1.00 41.18           C  
ANISOU  169  CB  ARG A  24     5171   5650   4825    110   1214   -612       C  
ATOM    170  CG  ARG A  24      18.095 -16.643 -94.138  1.00 48.96           C  
ANISOU  170  CG  ARG A  24     6221   6700   5681     84   1278   -626       C  
ATOM    171  CD  ARG A  24      17.545 -17.877 -94.824  1.00 49.70           C  
ANISOU  171  CD  ARG A  24     6417   6783   5683     63   1314   -732       C  
ATOM    172  NE  ARG A  24      16.066 -17.954 -94.785  1.00 45.56           N  
ANISOU  172  NE  ARG A  24     5933   6260   5118      7   1203   -760       N  
ATOM    173  CZ  ARG A  24      15.335 -18.805 -94.073  1.00 51.11           C  
ANISOU  173  CZ  ARG A  24     6650   6904   5865      8   1166   -819       C  
ATOM    174  NH1 ARG A  24      15.917 -19.669 -93.247  1.00 53.15           N  
ANISOU  174  NH1 ARG A  24     6887   7092   6215     64   1226   -857       N  
ATOM    175  NH2 ARG A  24      14.009 -18.781 -94.158  1.00 53.32           N  
ANISOU  175  NH2 ARG A  24     6958   7195   6107    -47   1067   -830       N  
ATOM    176  N   ALA A  25      18.214 -13.196 -93.015  1.00 37.20           N  
ANISOU  176  N   ALA A  25     4560   5244   4329     57   1110   -385       N  
ATOM    177  CA  ALA A  25      17.505 -11.988 -93.433  1.00 36.76           C  
ANISOU  177  CA  ALA A  25     4503   5226   4239     14   1033   -317       C  
ATOM    178  C   ALA A  25      16.847 -12.220 -94.792  1.00 42.43           C  
ANISOU  178  C   ALA A  25     5295   6007   4818    -29   1032   -339       C  
ATOM    179  O   ALA A  25      17.384 -12.933 -95.619  1.00 44.01           O  
ANISOU  179  O   ALA A  25     5545   6238   4941    -26   1115   -384       O  
ATOM    180  CB  ALA A  25      18.467 -10.812 -93.497  1.00 36.99           C  
ANISOU  180  CB  ALA A  25     4473   5275   4307     15   1050   -222       C  
ATOM    181  N   SER A  26      15.684 -11.637 -95.027  1.00 40.60           N  
ANISOU  181  N   SER A  26     5075   5795   4555    -69    940   -307       N  
ATOM    182  CA  SER A  26      15.006 -11.841 -96.298  1.00 41.77           C  
ANISOU  182  CA  SER A  26     5295   6011   4566   -122    920   -319       C  
ATOM    183  C   SER A  26      15.696 -11.132 -97.487  1.00 49.16           C  
ANISOU  183  C   SER A  26     6245   7022   5411   -145    964   -255       C  
ATOM    184  O   SER A  26      15.508 -11.546 -98.612  1.00 50.38           O  
ANISOU  184  O   SER A  26     6474   7235   5432   -185    984   -283       O  
ATOM    185  CB  SER A  26      13.534 -11.462 -96.189  1.00 40.89           C  
ANISOU  185  CB  SER A  26     5178   5901   4457   -159    803   -290       C  
ATOM    186  OG  SER A  26      13.380 -10.133 -95.733  1.00 41.36           O  
ANISOU  186  OG  SER A  26     5171   5947   4599   -151    751   -191       O  
ATOM    187  N   LYS A  27      16.512 -10.111 -97.212  1.00 46.67           N  
ANISOU  187  N   LYS A  27     5863   6703   5167   -123    984   -172       N  
ATOM    188  CA  LYS A  27      17.239  -9.236 -98.150  1.00 46.32           C  
ANISOU  188  CA  LYS A  27     5811   6721   5066   -140   1024    -89       C  
ATOM    189  C   LYS A  27      18.630  -9.112 -97.523  1.00 47.42           C  
ANISOU  189  C   LYS A  27     5886   6827   5305    -92   1105    -71       C  
ATOM    190  O   LYS A  27      18.727  -9.177 -96.311  1.00 42.57           O  
ANISOU  190  O   LYS A  27     5222   6144   4807    -61   1082    -86       O  
ATOM    191  CB  LYS A  27      16.585  -7.813 -98.075  1.00 48.96           C  
ANISOU  191  CB  LYS A  27     6099   7062   5442   -166    927     22       C  
ATOM    192  CG  LYS A  27      16.225  -7.128 -99.350  1.00 60.25           C  
ANISOU  192  CG  LYS A  27     7561   8574   6759   -218    898     98       C  
ATOM    193  CD  LYS A  27      15.821  -5.643 -99.080  1.00 73.48           C  
ANISOU  193  CD  LYS A  27     9172  10232   8516   -226    820    219       C  
ATOM    194  CE  LYS A  27      17.003  -4.682 -99.190  1.00 90.18           C  
ANISOU  194  CE  LYS A  27    11239  12351  10673   -217    876    302       C  
ATOM    195  NZ  LYS A  27      16.613  -3.239 -99.085  1.00 91.77           N  
ANISOU  195  NZ  LYS A  27    11392  12534  10944   -231    808    420       N  
ATOM    196  N   GLY A  28      19.659  -8.844 -98.316  1.00 47.58           N  
ANISOU  196  N   GLY A  28     5902   6896   5281    -91   1190    -28       N  
ATOM    197  CA  GLY A  28      20.994  -8.618 -97.796  1.00 46.86           C  
ANISOU  197  CA  GLY A  28     5735   6779   5289    -53   1260     10       C  
ATOM    198  C   GLY A  28      21.065  -7.401 -96.888  1.00 48.25           C  
ANISOU  198  C   GLY A  28     5832   6914   5586    -58   1185     95       C  
ATOM    199  O   GLY A  28      20.387  -6.398 -97.147  1.00 46.03           O  
ANISOU  199  O   GLY A  28     5552   6647   5289    -93   1112    160       O  
ATOM    200  N   VAL A  29      21.869  -7.491 -95.796  1.00 42.88           N  
ANISOU  200  N   VAL A  29     5086   6179   5028    -26   1201     96       N  
ATOM    201  CA  VAL A  29      22.029  -6.400 -94.817  1.00 40.83           C  
ANISOU  201  CA  VAL A  29     4761   5869   4882    -37   1133    164       C  
ATOM    202  C   VAL A  29      23.476  -5.884 -94.770  1.00 45.63           C  
ANISOU  202  C   VAL A  29     5294   6487   5557    -35   1190    240       C  
ATOM    203  O   VAL A  29      23.838  -5.150 -93.851  1.00 42.76           O  
ANISOU  203  O   VAL A  29     4875   6076   5295    -48   1143    287       O  
ATOM    204  CB  VAL A  29      21.481  -6.739 -93.414  1.00 42.81           C  
ANISOU  204  CB  VAL A  29     5004   6042   5218    -22   1067    109       C  
ATOM    205  CG1 VAL A  29      19.964  -6.968 -93.463  1.00 42.74           C  
ANISOU  205  CG1 VAL A  29     5056   6025   5159    -32   1000     59       C  
ATOM    206  CG2 VAL A  29      22.201  -7.925 -92.775  1.00 41.87           C  
ANISOU  206  CG2 VAL A  29     4865   5898   5145     20   1123     48       C  
ATOM    207  N   SER A  30      24.271  -6.215 -95.801  1.00 46.16           N  
ANISOU  207  N   SER A  30     5362   6615   5562    -24   1293    257       N  
ATOM    208  CA  SER A  30      25.676  -5.808 -95.935  1.00 47.69           C  
ANISOU  208  CA  SER A  30     5477   6828   5814    -20   1364    337       C  
ATOM    209  C   SER A  30      25.876  -4.732 -96.969  1.00 54.52           C  
ANISOU  209  C   SER A  30     6340   7750   6625    -58   1379    432       C  
ATOM    210  O   SER A  30      25.267  -4.775 -98.021  1.00 55.35           O  
ANISOU  210  O   SER A  30     6515   7908   6607    -72   1394    421       O  
ATOM    211  CB  SER A  30      26.560  -6.997 -96.256  1.00 48.79           C  
ANISOU  211  CB  SER A  30     5607   6988   5944     29   1488    296       C  
ATOM    212  OG  SER A  30      26.266  -8.069 -95.375  1.00 57.79           O  
ANISOU  212  OG  SER A  30     6758   8075   7126     65   1475    207       O  
ATOM    213  N   THR A  31      26.702  -3.747 -96.650  1.00 55.44           N  
ANISOU  213  N   THR A  31     6378   7855   6832    -80   1369    529       N  
ATOM    214  CA  THR A  31      26.987  -2.624 -97.551  1.00 58.36           C  
ANISOU  214  CA  THR A  31     6734   8270   7169   -119   1382    635       C  
ATOM    215  C   THR A  31      28.289  -1.970 -97.190  1.00 62.36           C  
ANISOU  215  C   THR A  31     7139   8766   7787   -133   1408    729       C  
ATOM    216  O   THR A  31      28.485  -1.629 -96.016  1.00 59.97           O  
ANISOU  216  O   THR A  31     6788   8398   7599   -147   1337    739       O  
ATOM    217  CB  THR A  31      25.889  -1.545 -97.449  1.00 75.79           C  
ANISOU  217  CB  THR A  31     8974  10450   9371   -160   1269    669       C  
ATOM    218  OG1 THR A  31      24.605  -2.138 -97.606  1.00 82.47           O  
ANISOU  218  OG1 THR A  31     9901  11299  10133   -151   1227    588       O  
ATOM    219  CG2 THR A  31      26.067  -0.450 -98.473  1.00 78.25           C  
ANISOU  219  CG2 THR A  31     9281  10811   9640   -199   1283    780       C  
ATOM    220  N   SER A  32      29.163  -1.758 -98.201  1.00 62.14           N  
ANISOU  220  N   SER A  32     7082   8804   7725   -136   1506    803       N  
ATOM    221  CA  SER A  32      30.438  -1.050 -98.054  1.00 62.83           C  
ANISOU  221  CA  SER A  32     7064   8893   7915   -158   1538    913       C  
ATOM    222  C   SER A  32      31.305  -1.583 -96.892  1.00 64.79           C  
ANISOU  222  C   SER A  32     7226   9095   8296   -136   1537    902       C  
ATOM    223  O   SER A  32      31.818  -0.800 -96.091  1.00 65.55           O  
ANISOU  223  O   SER A  32     7252   9149   8505   -177   1470    968       O  
ATOM    224  CB  SER A  32      30.176   0.444 -97.865  1.00 67.89           C  
ANISOU  224  CB  SER A  32     7692   9500   8603   -221   1441   1000       C  
ATOM    225  OG  SER A  32      29.313   0.996 -98.851  1.00 78.12           O  
ANISOU  225  OG  SER A  32     9059  10832   9789   -241   1425   1023       O  
ATOM    226  N   GLY A  33      31.444  -2.900 -96.813  1.00 58.47           N  
ANISOU  226  N   GLY A  33     6434   8301   7480    -77   1606    822       N  
ATOM    227  CA  GLY A  33      32.247  -3.541 -95.780  1.00 57.63           C  
ANISOU  227  CA  GLY A  33     6245   8158   7495    -50   1610    818       C  
ATOM    228  C   GLY A  33      31.606  -3.722 -94.413  1.00 61.11           C  
ANISOU  228  C   GLY A  33     6702   8524   7992    -59   1488    753       C  
ATOM    229  O   GLY A  33      32.279  -4.171 -93.484  1.00 61.67           O  
ANISOU  229  O   GLY A  33     6702   8566   8165    -46   1476    761       O  
ATOM    230  N   TYR A  34      30.310  -3.418 -94.268  1.00 55.54           N  
ANISOU  230  N   TYR A  34     6088   7790   7224    -79   1402    692       N  
ATOM    231  CA  TYR A  34      29.618  -3.570 -92.991  1.00 53.65           C  
ANISOU  231  CA  TYR A  34     5873   7480   7030    -86   1296    628       C  
ATOM    232  C   TYR A  34      28.346  -4.380 -93.129  1.00 51.00           C  
ANISOU  232  C   TYR A  34     5637   7137   6603    -53   1286    515       C  
ATOM    233  O   TYR A  34      27.614  -4.174 -94.085  1.00 49.55           O  
ANISOU  233  O   TYR A  34     5519   6989   6320    -59   1298    504       O  
ATOM    234  CB  TYR A  34      29.290  -2.179 -92.415  1.00 55.61           C  
ANISOU  234  CB  TYR A  34     6124   7680   7324   -152   1187    679       C  
ATOM    235  CG  TYR A  34      30.542  -1.460 -91.969  1.00 60.06           C  
ANISOU  235  CG  TYR A  34     6589   8235   7996   -196   1174    781       C  
ATOM    236  CD1 TYR A  34      31.300  -1.939 -90.905  1.00 62.18           C  
ANISOU  236  CD1 TYR A  34     6791   8476   8357   -197   1149    784       C  
ATOM    237  CD2 TYR A  34      31.022  -0.357 -92.666  1.00 62.02           C  
ANISOU  237  CD2 TYR A  34     6804   8508   8252   -240   1189    881       C  
ATOM    238  CE1 TYR A  34      32.470  -1.302 -90.506  1.00 63.76           C  
ANISOU  238  CE1 TYR A  34     6894   8673   8657   -247   1128    885       C  
ATOM    239  CE2 TYR A  34      32.207   0.273 -92.293  1.00 63.80           C  
ANISOU  239  CE2 TYR A  34     6933   8727   8581   -287   1177    980       C  
ATOM    240  CZ  TYR A  34      32.927  -0.197 -91.206  1.00 71.82           C  
ANISOU  240  CZ  TYR A  34     7883   9716   9689   -293   1142    981       C  
ATOM    241  OH  TYR A  34      34.087   0.428 -90.810  1.00 72.20           O  
ANISOU  241  OH  TYR A  34     7832   9761   9841   -350   1117   1085       O  
ATOM    242  N   SER A  35      28.060  -5.258 -92.146  1.00 43.62           N  
ANISOU  242  N   SER A  35     4712   6157   5705    -26   1254    441       N  
ATOM    243  CA  SER A  35      26.799  -6.007 -92.080  1.00 41.97           C  
ANISOU  243  CA  SER A  35     4590   5929   5426     -3   1229    336       C  
ATOM    244  C   SER A  35      26.002  -5.418 -90.939  1.00 42.20           C  
ANISOU  244  C   SER A  35     4640   5892   5501    -34   1113    319       C  
ATOM    245  O   SER A  35      26.458  -5.474 -89.807  1.00 41.77           O  
ANISOU  245  O   SER A  35     4544   5795   5532    -41   1073    325       O  
ATOM    246  CB  SER A  35      27.054  -7.492 -91.897  1.00 45.39           C  
ANISOU  246  CB  SER A  35     5024   6358   5864     54   1295    264       C  
ATOM    247  OG  SER A  35      27.549  -7.996 -93.124  1.00 54.51           O  
ANISOU  247  OG  SER A  35     6187   7570   6954     83   1415    265       O  
ATOM    248  N   TYR A  36      24.846  -4.810 -91.231  1.00 37.58           N  
ANISOU  248  N   TYR A  36     4117   5299   4862    -55   1060    306       N  
ATOM    249  CA  TYR A  36      24.037  -4.096 -90.227  1.00 36.29           C  
ANISOU  249  CA  TYR A  36     3978   5067   4745    -82    963    298       C  
ATOM    250  C   TYR A  36      23.081  -5.038 -89.534  1.00 39.89           C  
ANISOU  250  C   TYR A  36     4481   5487   5190    -54    935    202       C  
ATOM    251  O   TYR A  36      21.890  -5.002 -89.773  1.00 39.65           O  
ANISOU  251  O   TYR A  36     4504   5451   5112    -52    904    168       O  
ATOM    252  CB  TYR A  36      23.321  -2.927 -90.885  1.00 38.40           C  
ANISOU  252  CB  TYR A  36     4274   5339   4979   -113    929    348       C  
ATOM    253  CG  TYR A  36      24.284  -1.865 -91.360  1.00 41.72           C  
ANISOU  253  CG  TYR A  36     4644   5778   5428   -149    947    451       C  
ATOM    254  CD1 TYR A  36      24.802  -0.925 -90.478  1.00 44.39           C  
ANISOU  254  CD1 TYR A  36     4948   6059   5859   -190    899    499       C  
ATOM    255  CD2 TYR A  36      24.778  -1.875 -92.661  1.00 43.56           C  
ANISOU  255  CD2 TYR A  36     4864   6088   5597   -146   1018    498       C  
ATOM    256  CE1 TYR A  36      25.741   0.014 -90.889  1.00 46.62           C  
ANISOU  256  CE1 TYR A  36     5180   6356   6177   -229    914    597       C  
ATOM    257  CE2 TYR A  36      25.789  -0.997 -93.058  1.00 45.15           C  
ANISOU  257  CE2 TYR A  36     5009   6311   5835   -178   1044    598       C  
ATOM    258  CZ  TYR A  36      26.223  -0.013 -92.185  1.00 54.89           C  
ANISOU  258  CZ  TYR A  36     6205   7483   7167   -221    987    650       C  
ATOM    259  OH  TYR A  36      27.142   0.939 -92.558  1.00 63.15           O  
ANISOU  259  OH  TYR A  36     7196   8542   8255   -262   1003    753       O  
ATOM    260  N   LEU A  37      23.641  -5.891 -88.673  1.00 35.41           N  
ANISOU  260  N   LEU A  37     3886   4897   4672    -32    945    168       N  
ATOM    261  CA  LEU A  37      22.946  -6.980 -88.033  1.00 34.56           C  
ANISOU  261  CA  LEU A  37     3814   4759   4557     -1    933     81       C  
ATOM    262  C   LEU A  37      23.528  -7.143 -86.633  1.00 36.10           C  
ANISOU  262  C   LEU A  37     3973   4906   4838     -8    896     84       C  
ATOM    263  O   LEU A  37      24.708  -7.350 -86.512  1.00 35.93           O  
ANISOU  263  O   LEU A  37     3889   4901   4863     -4    926    126       O  
ATOM    264  CB  LEU A  37      23.152  -8.276 -88.898  1.00 33.97           C  
ANISOU  264  CB  LEU A  37     3750   4731   4427     44   1019     34       C  
ATOM    265  CG  LEU A  37      22.259  -9.522 -88.640  1.00 36.75           C  
ANISOU  265  CG  LEU A  37     4154   5060   4749     75   1021    -63       C  
ATOM    266  CD1 LEU A  37      22.543 -10.173 -87.280  1.00 36.28           C  
ANISOU  266  CD1 LEU A  37     4068   4947   4769     93    998    -87       C  
ATOM    267  CD2 LEU A  37      20.842  -9.216 -88.755  1.00 36.10           C  
ANISOU  267  CD2 LEU A  37     4131   4967   4620     57    963    -95       C  
ATOM    268  N   HIS A  38      22.708  -6.957 -85.588  1.00 32.84           N  
ANISOU  268  N   HIS A  38     3598   4434   4444    -22    829     48       N  
ATOM    269  CA  HIS A  38      23.123  -7.031 -84.189  1.00 31.96           C  
ANISOU  269  CA  HIS A  38     3472   4276   4398    -40    782     48       C  
ATOM    270  C   HIS A  38      22.313  -8.099 -83.430  1.00 35.14           C  
ANISOU  270  C   HIS A  38     3914   4646   4792     -9    770    -31       C  
ATOM    271  O   HIS A  38      21.230  -8.490 -83.872  1.00 33.57           O  
ANISOU  271  O   HIS A  38     3763   4448   4545     15    781    -85       O  
ATOM    272  CB  HIS A  38      22.919  -5.662 -83.544  1.00 33.06           C  
ANISOU  272  CB  HIS A  38     3632   4365   4563    -95    717     80       C  
ATOM    273  CG  HIS A  38      23.216  -4.512 -84.456  1.00 36.62           C  
ANISOU  273  CG  HIS A  38     4065   4838   5009   -124    726    148       C  
ATOM    274  ND1 HIS A  38      24.508  -4.151 -84.771  1.00 38.84           N  
ANISOU  274  ND1 HIS A  38     4279   5152   5325   -148    744    222       N  
ATOM    275  CD2 HIS A  38      22.368  -3.735 -85.163  1.00 38.19           C  
ANISOU  275  CD2 HIS A  38     4301   5034   5175   -128    724    158       C  
ATOM    276  CE1 HIS A  38      24.402  -3.140 -85.617  1.00 38.17           C  
ANISOU  276  CE1 HIS A  38     4198   5080   5224   -170    751    272       C  
ATOM    277  NE2 HIS A  38      23.138  -2.860 -85.880  1.00 38.00           N  
ANISOU  277  NE2 HIS A  38     4239   5038   5162   -158    738    237       N  
ATOM    278  N   TRP A  39      22.895  -8.605 -82.333  1.00 32.18           N  
ANISOU  278  N   TRP A  39     3514   4246   4465    -12    747    -30       N  
ATOM    279  CA  TRP A  39      22.336  -9.656 -81.516  1.00 31.61           C  
ANISOU  279  CA  TRP A  39     3470   4143   4395     15    737    -91       C  
ATOM    280  C   TRP A  39      22.151  -9.172 -80.113  1.00 34.93           C  
ANISOU  280  C   TRP A  39     3919   4510   4841    -27    667    -92       C  
ATOM    281  O   TRP A  39      23.045  -8.531 -79.579  1.00 32.63           O  
ANISOU  281  O   TRP A  39     3597   4214   4585    -72    629    -37       O  
ATOM    282  CB  TRP A  39      23.272 -10.851 -81.451  1.00 30.31           C  
ANISOU  282  CB  TRP A  39     3250   3999   4266     52    779    -81       C  
ATOM    283  CG  TRP A  39      23.345 -11.667 -82.699  1.00 31.81           C  
ANISOU  283  CG  TRP A  39     3432   4228   4426    102    865   -105       C  
ATOM    284  CD1 TRP A  39      24.275 -11.567 -83.692  1.00 35.32           C  
ANISOU  284  CD1 TRP A  39     3828   4721   4874    115    928    -59       C  
ATOM    285  CD2 TRP A  39      22.457 -12.723 -83.084  1.00 31.43           C  
ANISOU  285  CD2 TRP A  39     3434   4173   4336    142    902   -184       C  
ATOM    286  NE1 TRP A  39      24.016 -12.488 -84.669  1.00 34.79           N  
ANISOU  286  NE1 TRP A  39     3786   4673   4760    160   1006   -110       N  
ATOM    287  CE2 TRP A  39      22.918 -13.226 -84.315  1.00 34.89           C  
ANISOU  287  CE2 TRP A  39     3859   4652   4745    175    988   -188       C  
ATOM    288  CE3 TRP A  39      21.346 -13.338 -82.473  1.00 32.45           C  
ANISOU  288  CE3 TRP A  39     3616   4262   4450    151    874   -250       C  
ATOM    289  CZ2 TRP A  39      22.311 -14.303 -84.958  1.00 34.11           C  
ANISOU  289  CZ2 TRP A  39     3808   4552   4599    209   1041   -262       C  
ATOM    290  CZ3 TRP A  39      20.757 -14.428 -83.106  1.00 33.00           C  
ANISOU  290  CZ3 TRP A  39     3722   4333   4482    186    923   -316       C  
ATOM    291  CH2 TRP A  39      21.269 -14.921 -84.315  1.00 33.97           C  
ANISOU  291  CH2 TRP A  39     3839   4493   4575    213   1004   -324       C  
ATOM    292  N   TYR A  40      21.013  -9.538 -79.489  1.00 32.28           N  
ANISOU  292  N   TYR A  40     3644   4135   4486    -15    650   -154       N  
ATOM    293  CA  TYR A  40      20.721  -9.163 -78.103  1.00 30.70           C  
ANISOU  293  CA  TYR A  40     3487   3880   4296    -52    595   -166       C  
ATOM    294  C   TYR A  40      20.341 -10.367 -77.320  1.00 34.21           C  
ANISOU  294  C   TYR A  40     3947   4308   4743    -24    595   -209       C  
ATOM    295  O   TYR A  40      19.816 -11.326 -77.884  1.00 31.33           O  
ANISOU  295  O   TYR A  40     3584   3957   4364     24    636   -249       O  
ATOM    296  CB  TYR A  40      19.571  -8.173 -78.015  1.00 29.49           C  
ANISOU  296  CB  TYR A  40     3399   3684   4123    -68    581   -192       C  
ATOM    297  CG  TYR A  40      19.812  -6.928 -78.827  1.00 28.72           C  
ANISOU  297  CG  TYR A  40     3290   3594   4027    -94    582   -145       C  
ATOM    298  CD1 TYR A  40      19.494  -6.880 -80.179  1.00 30.17           C  
ANISOU  298  CD1 TYR A  40     3456   3820   4187    -65    619   -136       C  
ATOM    299  CD2 TYR A  40      20.356  -5.799 -78.248  1.00 28.69           C  
ANISOU  299  CD2 TYR A  40     3298   3556   4045   -153    543   -108       C  
ATOM    300  CE1 TYR A  40      19.760  -5.752 -80.936  1.00 31.01           C  
ANISOU  300  CE1 TYR A  40     3549   3938   4295    -90    620    -83       C  
ATOM    301  CE2 TYR A  40      20.651  -4.673 -79.000  1.00 30.22           C  
ANISOU  301  CE2 TYR A  40     3479   3755   4249   -179    545    -59       C  
ATOM    302  CZ  TYR A  40      20.360  -4.650 -80.344  1.00 34.10           C  
ANISOU  302  CZ  TYR A  40     3945   4292   4720   -144    585    -42       C  
ATOM    303  OH  TYR A  40      20.578  -3.478 -81.019  1.00 32.41           O  
ANISOU  303  OH  TYR A  40     3722   4077   4516   -172    585     13       O  
ATOM    304  N   GLN A  41      20.522 -10.257 -75.999  1.00 32.27           N  
ANISOU  304  N   GLN A  41     3726   4027   4507    -61    546   -204       N  
ATOM    305  CA  GLN A  41      20.164 -11.273 -75.030  1.00 33.03           C  
ANISOU  305  CA  GLN A  41     3845   4101   4603    -45    537   -236       C  
ATOM    306  C   GLN A  41      19.127 -10.646 -74.126  1.00 34.51           C  
ANISOU  306  C   GLN A  41     4116   4232   4762    -73    514   -276       C  
ATOM    307  O   GLN A  41      19.386  -9.584 -73.582  1.00 32.92           O  
ANISOU  307  O   GLN A  41     3947   4006   4556   -128    477   -258       O  
ATOM    308  CB  GLN A  41      21.395 -11.677 -74.187  1.00 34.93           C  
ANISOU  308  CB  GLN A  41     4040   4356   4877    -72    497   -182       C  
ATOM    309  CG  GLN A  41      21.093 -12.666 -73.054  1.00 37.43           C  
ANISOU  309  CG  GLN A  41     4382   4649   5191    -64    478   -201       C  
ATOM    310  CD  GLN A  41      22.280 -12.808 -72.167  1.00 31.87           C  
ANISOU  310  CD  GLN A  41     3637   3959   4515   -106    420   -133       C  
ATOM    311  OE1 GLN A  41      22.707 -11.852 -71.533  1.00 33.04           O  
ANISOU  311  OE1 GLN A  41     3808   4099   4649   -178    361   -104       O  
ATOM    312  NE2 GLN A  41      22.929 -13.956 -72.187  1.00 34.01           N  
ANISOU  312  NE2 GLN A  41     3839   4252   4829    -66    435    -98       N  
ATOM    313  N   GLN A  42      17.959 -11.276 -73.974  1.00 30.36           N  
ANISOU  313  N   GLN A  42     3628   3685   4222    -36    540   -330       N  
ATOM    314  CA  GLN A  42      16.937 -10.772 -73.045  1.00 29.61           C  
ANISOU  314  CA  GLN A  42     3611   3534   4107    -54    533   -367       C  
ATOM    315  C   GLN A  42      16.592 -11.818 -71.994  1.00 33.81           C  
ANISOU  315  C   GLN A  42     4168   4047   4632    -44    530   -392       C  
ATOM    316  O   GLN A  42      16.041 -12.845 -72.321  1.00 33.40           O  
ANISOU  316  O   GLN A  42     4100   4004   4588      2    560   -417       O  
ATOM    317  CB  GLN A  42      15.667 -10.302 -73.743  1.00 29.71           C  
ANISOU  317  CB  GLN A  42     3646   3528   4114    -26    569   -396       C  
ATOM    318  CG  GLN A  42      14.768  -9.531 -72.762  1.00 31.90           C  
ANISOU  318  CG  GLN A  42     4000   3739   4383    -46    573   -422       C  
ATOM    319  CD  GLN A  42      13.523  -8.977 -73.416  1.00 40.02           C  
ANISOU  319  CD  GLN A  42     5037   4745   5422    -16    608   -435       C  
ATOM    320  OE1 GLN A  42      13.002  -9.523 -74.360  1.00 37.09           O  
ANISOU  320  OE1 GLN A  42     4628   4407   5056     22    624   -440       O  
ATOM    321  NE2 GLN A  42      13.005  -7.903 -72.900  1.00 36.78           N  
ANISOU  321  NE2 GLN A  42     4682   4275   5017    -33    619   -440       N  
ATOM    322  N   LYS A  43      16.893 -11.528 -70.743  1.00 35.73           N  
ANISOU  322  N   LYS A  43     4457   4263   4856    -92    493   -384       N  
ATOM    323  CA  LYS A  43      16.616 -12.396 -69.593  1.00 36.49           C  
ANISOU  323  CA  LYS A  43     4588   4341   4936    -94    484   -399       C  
ATOM    324  C   LYS A  43      15.312 -11.969 -68.942  1.00 41.43           C  
ANISOU  324  C   LYS A  43     5297   4911   5534    -95    514   -448       C  
ATOM    325  O   LYS A  43      14.947 -10.809 -69.057  1.00 40.07           O  
ANISOU  325  O   LYS A  43     5165   4707   5354   -114    526   -460       O  
ATOM    326  CB  LYS A  43      17.753 -12.321 -68.550  1.00 36.61           C  
ANISOU  326  CB  LYS A  43     4610   4365   4936   -157    419   -353       C  
ATOM    327  CG  LYS A  43      19.016 -13.011 -69.023  1.00 36.81           C  
ANISOU  327  CG  LYS A  43     4539   4444   5004   -146    396   -293       C  
ATOM    328  CD  LYS A  43      20.169 -12.951 -68.008  1.00 38.79           C  
ANISOU  328  CD  LYS A  43     4780   4709   5247   -213    319   -231       C  
ATOM    329  CE  LYS A  43      21.470 -13.382 -68.674  1.00 40.85           C  
ANISOU  329  CE  LYS A  43     4929   5023   5569   -198    305   -158       C  
ATOM    330  NZ  LYS A  43      22.617 -13.549 -67.718  1.00 48.17           N  
ANISOU  330  NZ  LYS A  43     5824   5974   6505   -257    225    -79       N  
ATOM    331  N   PRO A  44      14.604 -12.889 -68.245  1.00 42.65           N  
ANISOU  331  N   PRO A  44     5477   5050   5680    -73    534   -472       N  
ATOM    332  CA  PRO A  44      13.365 -12.504 -67.544  1.00 43.71           C  
ANISOU  332  CA  PRO A  44     5687   5128   5791    -72    573   -513       C  
ATOM    333  C   PRO A  44      13.446 -11.224 -66.717  1.00 46.74           C  
ANISOU  333  C   PRO A  44     6156   5466   6135   -130    564   -523       C  
ATOM    334  O   PRO A  44      14.378 -11.071 -65.932  1.00 47.09           O  
ANISOU  334  O   PRO A  44     6230   5516   6144   -189    513   -502       O  
ATOM    335  CB  PRO A  44      13.139 -13.700 -66.605  1.00 45.72           C  
ANISOU  335  CB  PRO A  44     5957   5382   6033    -64    574   -517       C  
ATOM    336  CG  PRO A  44      13.643 -14.824 -67.335  1.00 48.66           C  
ANISOU  336  CG  PRO A  44     6248   5798   6444    -28    565   -495       C  
ATOM    337  CD  PRO A  44      14.889 -14.328 -68.027  1.00 44.15           C  
ANISOU  337  CD  PRO A  44     5626   5264   5886    -47    527   -458       C  
ATOM    338  N   GLY A  45      12.509 -10.304 -66.950  1.00 43.09           N  
ANISOU  338  N   GLY A  45     5731   4958   5682   -115    613   -550       N  
ATOM    339  CA  GLY A  45      12.420  -9.062 -66.189  1.00 43.31           C  
ANISOU  339  CA  GLY A  45     5854   4924   5679   -163    625   -571       C  
ATOM    340  C   GLY A  45      13.424  -7.985 -66.527  1.00 48.96           C  
ANISOU  340  C   GLY A  45     6572   5638   6391   -216    582   -548       C  
ATOM    341  O   GLY A  45      13.516  -6.994 -65.796  1.00 50.16           O  
ANISOU  341  O   GLY A  45     6814   5734   6510   -270    583   -567       O  
ATOM    342  N   GLN A  46      14.195  -8.149 -67.622  1.00 43.38           N  
ANISOU  342  N   GLN A  46     5773   4990   5719   -204    547   -507       N  
ATOM    343  CA  GLN A  46      15.187  -7.157 -67.989  1.00 39.04           C  
ANISOU  343  CA  GLN A  46     5214   4444   5174   -255    507   -476       C  
ATOM    344  C   GLN A  46      15.026  -6.662 -69.389  1.00 38.03           C  
ANISOU  344  C   GLN A  46     5023   4332   5093   -216    530   -455       C  
ATOM    345  O   GLN A  46      14.446  -7.329 -70.264  1.00 37.10           O  
ANISOU  345  O   GLN A  46     4846   4249   5002   -152    559   -454       O  
ATOM    346  CB  GLN A  46      16.573  -7.771 -67.849  1.00 40.03           C  
ANISOU  346  CB  GLN A  46     5284   4630   5293   -293    436   -429       C  
ATOM    347  CG  GLN A  46      16.923  -8.266 -66.449  1.00 48.96           C  
ANISOU  347  CG  GLN A  46     6472   5758   6375   -345    394   -431       C  
ATOM    348  CD  GLN A  46      18.333  -8.850 -66.382  1.00 63.26           C  
ANISOU  348  CD  GLN A  46     8209   7632   8195   -381    319   -366       C  
ATOM    349  OE1 GLN A  46      19.088  -8.887 -67.369  1.00 55.85           O  
ANISOU  349  OE1 GLN A  46     7179   6739   7304   -365    307   -321       O  
ATOM    350  NE2 GLN A  46      18.725  -9.332 -65.218  1.00 54.83           N  
ANISOU  350  NE2 GLN A  46     7178   6571   7086   -429    270   -352       N  
ATOM    351  N   ALA A  47      15.664  -5.526 -69.642  1.00 33.88           N  
ANISOU  351  N   ALA A  47     4508   3789   4576   -262    508   -431       N  
ATOM    352  CA  ALA A  47      15.779  -4.977 -70.971  1.00 34.31           C  
ANISOU  352  CA  ALA A  47     4499   3867   4669   -239    518   -396       C  
ATOM    353  C   ALA A  47      16.718  -5.881 -71.797  1.00 35.59           C  
ANISOU  353  C   ALA A  47     4561   4118   4843   -222    491   -354       C  
ATOM    354  O   ALA A  47      17.610  -6.547 -71.235  1.00 34.33           O  
ANISOU  354  O   ALA A  47     4382   3991   4672   -250    449   -338       O  
ATOM    355  CB  ALA A  47      16.385  -3.562 -70.891  1.00 37.11           C  
ANISOU  355  CB  ALA A  47     4895   4177   5031   -305    496   -375       C  
ATOM    356  N   PRO A  48      16.561  -5.906 -73.133  1.00 31.55           N  
ANISOU  356  N   PRO A  48     3986   3647   4354   -178    515   -332       N  
ATOM    357  CA  PRO A  48      17.529  -6.615 -73.960  1.00 31.34           C  
ANISOU  357  CA  PRO A  48     3873   3696   4337   -164    504   -294       C  
ATOM    358  C   PRO A  48      18.933  -6.055 -73.752  1.00 37.43           C  
ANISOU  358  C   PRO A  48     4621   4483   5120   -228    457   -242       C  
ATOM    359  O   PRO A  48      19.090  -4.881 -73.457  1.00 39.54           O  
ANISOU  359  O   PRO A  48     4930   4705   5389   -280    437   -231       O  
ATOM    360  CB  PRO A  48      17.054  -6.328 -75.388  1.00 33.52           C  
ANISOU  360  CB  PRO A  48     4112   4000   4622   -124    538   -278       C  
ATOM    361  CG  PRO A  48      15.667  -5.900 -75.260  1.00 37.42           C  
ANISOU  361  CG  PRO A  48     4656   4442   5118   -101    565   -311       C  
ATOM    362  CD  PRO A  48      15.534  -5.244 -73.955  1.00 34.17           C  
ANISOU  362  CD  PRO A  48     4323   3958   4705   -142    555   -334       C  
ATOM    363  N   ARG A  49      19.937  -6.909 -73.859  1.00 33.12           N  
ANISOU  363  N   ARG A  49     4006   3992   4585   -224    440   -208       N  
ATOM    364  CA  ARG A  49      21.341  -6.576 -73.710  1.00 32.10           C  
ANISOU  364  CA  ARG A  49     3830   3888   4477   -281    393   -145       C  
ATOM    365  C   ARG A  49      22.077  -6.788 -75.018  1.00 33.87           C  
ANISOU  365  C   ARG A  49     3960   4177   4731   -248    424    -95       C  
ATOM    366  O   ARG A  49      22.081  -7.893 -75.510  1.00 34.48           O  
ANISOU  366  O   ARG A  49     3993   4294   4814   -190    462   -103       O  
ATOM    367  CB  ARG A  49      21.921  -7.529 -72.666  1.00 31.70           C  
ANISOU  367  CB  ARG A  49     3766   3852   4426   -297    353   -134       C  
ATOM    368  CG  ARG A  49      23.410  -7.343 -72.347  1.00 33.93           C  
ANISOU  368  CG  ARG A  49     3988   4167   4739   -360    291    -55       C  
ATOM    369  CD  ARG A  49      23.909  -8.631 -71.725  1.00 38.25           C  
ANISOU  369  CD  ARG A  49     4489   4745   5301   -342    271    -31       C  
ATOM    370  NE  ARG A  49      25.292  -8.580 -71.249  1.00 46.62           N  
ANISOU  370  NE  ARG A  49     5481   5837   6394   -404    202     55       N  
ATOM    371  CZ  ARG A  49      25.962  -9.610 -70.727  1.00 53.58           C  
ANISOU  371  CZ  ARG A  49     6301   6751   7305   -395    174    104       C  
ATOM    372  NH1 ARG A  49      25.383 -10.810 -70.609  1.00 46.18           N  
ANISOU  372  NH1 ARG A  49     5367   5812   6366   -324    214     69       N  
ATOM    373  NH2 ARG A  49      27.206  -9.450 -70.311  1.00 42.79           N  
ANISOU  373  NH2 ARG A  49     4867   5416   5975   -458    103    194       N  
ATOM    374  N   LEU A  50      22.732  -5.779 -75.568  1.00 31.12           N  
ANISOU  374  N   LEU A  50     3585   3837   4402   -287    414    -44       N  
ATOM    375  CA  LEU A  50      23.573  -5.964 -76.781  1.00 31.19           C  
ANISOU  375  CA  LEU A  50     3502   3911   4438   -261    449     12       C  
ATOM    376  C   LEU A  50      24.753  -6.906 -76.532  1.00 34.46           C  
ANISOU  376  C   LEU A  50     3832   4372   4889   -257    439     61       C  
ATOM    377  O   LEU A  50      25.554  -6.667 -75.615  1.00 33.81           O  
ANISOU  377  O   LEU A  50     3735   4282   4829   -320    374    104       O  
ATOM    378  CB  LEU A  50      24.144  -4.597 -77.249  1.00 31.17           C  
ANISOU  378  CB  LEU A  50     3485   3903   4454   -317    433     70       C  
ATOM    379  CG  LEU A  50      24.959  -4.565 -78.563  1.00 32.50           C  
ANISOU  379  CG  LEU A  50     3566   4137   4646   -296    478    134       C  
ATOM    380  CD1 LEU A  50      24.125  -4.933 -79.727  1.00 29.94           C  
ANISOU  380  CD1 LEU A  50     3251   3840   4285   -227    545    100       C  
ATOM    381  CD2 LEU A  50      25.533  -3.172 -78.810  1.00 35.49           C  
ANISOU  381  CD2 LEU A  50     3935   4501   5049   -364    451    196       C  
ATOM    382  N   LEU A  51      24.858  -7.966 -77.353  1.00 32.37           N  
ANISOU  382  N   LEU A  51     3515   4151   4631   -185    503     58       N  
ATOM    383  CA  LEU A  51      25.989  -8.902 -77.308  1.00 32.47           C  
ANISOU  383  CA  LEU A  51     3437   4206   4695   -163    515    112       C  
ATOM    384  C   LEU A  51      27.001  -8.605 -78.397  1.00 38.01           C  
ANISOU  384  C   LEU A  51     4052   4958   5432   -156    560    183       C  
ATOM    385  O   LEU A  51      28.202  -8.499 -78.125  1.00 37.80           O  
ANISOU  385  O   LEU A  51     3945   4955   5463   -189    532    266       O  
ATOM    386  CB  LEU A  51      25.511 -10.349 -77.488  1.00 31.88           C  
ANISOU  386  CB  LEU A  51     3363   4137   4614    -84    572     61       C  
ATOM    387  CG  LEU A  51      24.518 -10.906 -76.464  1.00 36.28           C  
ANISOU  387  CG  LEU A  51     3994   4649   5142    -78    542     -5       C  
ATOM    388  CD1 LEU A  51      24.075 -12.283 -76.897  1.00 36.34           C  
ANISOU  388  CD1 LEU A  51     3997   4662   5149     -1    607    -52       C  
ATOM    389  CD2 LEU A  51      25.108 -10.921 -75.048  1.00 33.51           C  
ANISOU  389  CD2 LEU A  51     3635   4282   4814   -133    462     35       C  
ATOM    390  N   ILE A  52      26.503  -8.555 -79.646  1.00 34.70           N  
ANISOU  390  N   ILE A  52     3648   4560   4977   -112    631    154       N  
ATOM    391  CA  ILE A  52      27.281  -8.422 -80.885  1.00 33.87           C  
ANISOU  391  CA  ILE A  52     3476   4507   4887    -91    699    208       C  
ATOM    392  C   ILE A  52      26.675  -7.337 -81.738  1.00 37.47           C  
ANISOU  392  C   ILE A  52     3977   4964   5295   -111    708    201       C  
ATOM    393  O   ILE A  52      25.463  -7.325 -81.941  1.00 34.90           O  
ANISOU  393  O   ILE A  52     3728   4618   4914    -93    711    133       O  
ATOM    394  CB  ILE A  52      27.278  -9.749 -81.724  1.00 35.77           C  
ANISOU  394  CB  ILE A  52     3696   4778   5117     -6    797    175       C  
ATOM    395  CG1 ILE A  52      27.784 -10.976 -80.925  1.00 35.50           C  
ANISOU  395  CG1 ILE A  52     3616   4734   5138     28    800    181       C  
ATOM    396  CG2 ILE A  52      28.040  -9.605 -83.057  1.00 34.75           C  
ANISOU  396  CG2 ILE A  52     3510   4703   4989     17    883    224       C  
ATOM    397  CD1 ILE A  52      29.269 -10.967 -80.525  1.00 34.76           C  
ANISOU  397  CD1 ILE A  52     3408   4664   5135      9    785    289       C  
ATOM    398  N   TYR A  53      27.532  -6.486 -82.311  1.00 35.94           N  
ANISOU  398  N   TYR A  53     3729   4798   5127   -145    716    279       N  
ATOM    399  CA  TYR A  53      27.095  -5.461 -83.227  1.00 34.52           C  
ANISOU  399  CA  TYR A  53     3581   4626   4909   -162    731    291       C  
ATOM    400  C   TYR A  53      27.836  -5.621 -84.535  1.00 36.81           C  
ANISOU  400  C   TYR A  53     3810   4982   5195   -131    818    342       C  
ATOM    401  O   TYR A  53      28.915  -6.207 -84.591  1.00 34.00           O  
ANISOU  401  O   TYR A  53     3372   4658   4887   -112    858    389       O  
ATOM    402  CB  TYR A  53      27.219  -4.057 -82.631  1.00 35.31           C  
ANISOU  402  CB  TYR A  53     3698   4681   5035   -243    656    332       C  
ATOM    403  CG  TYR A  53      28.626  -3.588 -82.380  1.00 35.38           C  
ANISOU  403  CG  TYR A  53     3621   4708   5114   -299    629    427       C  
ATOM    404  CD1 TYR A  53      29.384  -3.018 -83.399  1.00 38.69           C  
ANISOU  404  CD1 TYR A  53     3978   5171   5552   -309    674    506       C  
ATOM    405  CD2 TYR A  53      29.208  -3.721 -81.131  1.00 35.13           C  
ANISOU  405  CD2 TYR A  53     3568   4652   5128   -346    558    445       C  
ATOM    406  CE1 TYR A  53      30.709  -2.658 -83.198  1.00 38.27           C  
ANISOU  406  CE1 TYR A  53     3831   5138   5572   -359    653    603       C  
ATOM    407  CE2 TYR A  53      30.526  -3.336 -80.907  1.00 36.13           C  
ANISOU  407  CE2 TYR A  53     3605   4800   5324   -403    525    543       C  
ATOM    408  CZ  TYR A  53      31.265  -2.780 -81.938  1.00 43.36           C  
ANISOU  408  CZ  TYR A  53     4450   5758   6267   -410    573    622       C  
ATOM    409  OH  TYR A  53      32.551  -2.350 -81.730  1.00 39.60           O  
ANISOU  409  OH  TYR A  53     3876   5302   5866   -472    538    727       O  
ATOM    410  N   LEU A  54      27.174  -5.195 -85.615  1.00 36.64           N  
ANISOU  410  N   LEU A  54     3832   4981   5110   -120    854    329       N  
ATOM    411  CA  LEU A  54      27.695  -5.262 -86.980  1.00 36.21           C  
ANISOU  411  CA  LEU A  54     3742   4992   5026    -94    943    370       C  
ATOM    412  C   LEU A  54      28.204  -6.656 -87.316  1.00 40.71           C  
ANISOU  412  C   LEU A  54     4278   5596   5596    -29   1030    344       C  
ATOM    413  O   LEU A  54      29.355  -6.854 -87.695  1.00 40.75           O  
ANISOU  413  O   LEU A  54     4202   5637   5644    -15   1093    408       O  
ATOM    414  CB  LEU A  54      28.736  -4.162 -87.236  1.00 36.28           C  
ANISOU  414  CB  LEU A  54     3682   5018   5085   -146    939    477       C  
ATOM    415  CG  LEU A  54      28.226  -2.740 -87.217  1.00 39.49           C  
ANISOU  415  CG  LEU A  54     4130   5390   5485   -205    876    506       C  
ATOM    416  CD1 LEU A  54      29.388  -1.765 -87.255  1.00 38.23           C  
ANISOU  416  CD1 LEU A  54     3895   5238   5392   -264    864    613       C  
ATOM    417  CD2 LEU A  54      27.238  -2.482 -88.358  1.00 47.17           C  
ANISOU  417  CD2 LEU A  54     5165   6387   6371   -184    909    484       C  
ATOM    418  N   ALA A  55      27.350  -7.643 -87.016  1.00 38.49           N  
ANISOU  418  N   ALA A  55     4054   5292   5280     11   1030    253       N  
ATOM    419  CA  ALA A  55      27.498  -9.064 -87.312  1.00 36.89           C  
ANISOU  419  CA  ALA A  55     3848   5103   5067     76   1112    203       C  
ATOM    420  C   ALA A  55      28.511  -9.819 -86.465  1.00 39.67           C  
ANISOU  420  C   ALA A  55     4119   5440   5513     99   1122    236       C  
ATOM    421  O   ALA A  55      28.283 -10.991 -86.159  1.00 35.46           O  
ANISOU  421  O   ALA A  55     3602   4886   4987    146   1149    178       O  
ATOM    422  CB  ALA A  55      27.826  -9.257 -88.795  1.00 37.35           C  
ANISOU  422  CB  ALA A  55     3908   5219   5065    105   1222    212       C  
ATOM    423  N   SER A  56      29.660  -9.215 -86.179  1.00 39.77           N  
ANISOU  423  N   SER A  56     4040   5467   5604     68   1107    335       N  
ATOM    424  CA  SER A  56      30.725  -9.947 -85.510  1.00 40.32           C  
ANISOU  424  CA  SER A  56     4016   5534   5771     92   1121    387       C  
ATOM    425  C   SER A  56      31.562  -9.186 -84.500  1.00 42.35           C  
ANISOU  425  C   SER A  56     4195   5783   6113     25   1027    481       C  
ATOM    426  O   SER A  56      32.518  -9.785 -84.033  1.00 41.24           O  
ANISOU  426  O   SER A  56     3962   5648   6058     43   1039    541       O  
ATOM    427  CB  SER A  56      31.641 -10.559 -86.574  1.00 44.18           C  
ANISOU  427  CB  SER A  56     4440   6066   6280    153   1259    424       C  
ATOM    428  OG  SER A  56      32.198  -9.579 -87.435  1.00 48.60           O  
ANISOU  428  OG  SER A  56     4965   6670   6832    122   1291    496       O  
ATOM    429  N   TYR A  57      31.234  -7.926 -84.114  1.00 39.45           N  
ANISOU  429  N   TYR A  57     3864   5397   5728    -54    933    495       N  
ATOM    430  CA  TYR A  57      32.051  -7.230 -83.122  1.00 39.45           C  
ANISOU  430  CA  TYR A  57     3801   5385   5804   -130    838    578       C  
ATOM    431  C   TYR A  57      31.428  -7.430 -81.754  1.00 42.17           C  
ANISOU  431  C   TYR A  57     4205   5677   6140   -159    739    525       C  
ATOM    432  O   TYR A  57      30.238  -7.152 -81.562  1.00 39.01           O  
ANISOU  432  O   TYR A  57     3911   5239   5671   -167    708    442       O  
ATOM    433  CB  TYR A  57      32.170  -5.758 -83.432  1.00 41.50           C  
ANISOU  433  CB  TYR A  57     4067   5645   6056   -204    798    628       C  
ATOM    434  CG  TYR A  57      32.827  -5.490 -84.760  1.00 44.28           C  
ANISOU  434  CG  TYR A  57     4359   6052   6414   -182    895    692       C  
ATOM    435  CD1 TYR A  57      34.210  -5.503 -84.893  1.00 46.19           C  
ANISOU  435  CD1 TYR A  57     4471   6332   6745   -190    925    804       C  
ATOM    436  CD2 TYR A  57      32.068  -5.301 -85.904  1.00 45.81           C  
ANISOU  436  CD2 TYR A  57     4620   6263   6522   -149    962    645       C  
ATOM    437  CE1 TYR A  57      34.821  -5.204 -86.113  1.00 42.45           C  
ANISOU  437  CE1 TYR A  57     3942   5910   6276   -171   1024    867       C  
ATOM    438  CE2 TYR A  57      32.662  -5.016 -87.127  1.00 47.98           C  
ANISOU  438  CE2 TYR A  57     4848   6591   6790   -134   1053    706       C  
ATOM    439  CZ  TYR A  57      34.045  -4.993 -87.233  1.00 51.66           C  
ANISOU  439  CZ  TYR A  57     5190   7093   7346   -142   1091    814       C  
ATOM    440  OH  TYR A  57      34.637  -4.809 -88.450  1.00 55.36           O  
ANISOU  440  OH  TYR A  57     5612   7616   7805   -120   1197    873       O  
ATOM    441  N   LEU A  58      32.256  -7.853 -80.795  1.00 39.38           N  
ANISOU  441  N   LEU A  58     3780   5324   5859   -180    687    584       N  
ATOM    442  CA  LEU A  58      31.831  -8.124 -79.444  1.00 38.35           C  
ANISOU  442  CA  LEU A  58     3699   5152   5721   -213    594    547       C  
ATOM    443  C   LEU A  58      31.685  -6.839 -78.685  1.00 42.48           C  
ANISOU  443  C   LEU A  58     4276   5640   6226   -318    486    555       C  
ATOM    444  O   LEU A  58      32.613  -6.051 -78.644  1.00 41.65           O  
ANISOU  444  O   LEU A  58     4107   5551   6169   -385    445    643       O  
ATOM    445  CB  LEU A  58      32.842  -9.045 -78.761  1.00 38.29           C  
ANISOU  445  CB  LEU A  58     3586   5163   5798   -199    577    622       C  
ATOM    446  CG  LEU A  58      32.549  -9.509 -77.317  1.00 42.21           C  
ANISOU  446  CG  LEU A  58     4122   5627   6290   -230    482    602       C  
ATOM    447  CD1 LEU A  58      31.357 -10.419 -77.242  1.00 41.43           C  
ANISOU  447  CD1 LEU A  58     4114   5495   6132   -162    523    490       C  
ATOM    448  CD2 LEU A  58      33.756 -10.283 -76.784  1.00 42.55           C  
ANISOU  448  CD2 LEU A  58     4036   5700   6433   -222    462    710       C  
ATOM    449  N   GLU A  59      30.535  -6.654 -78.033  1.00 40.33           N  
ANISOU  449  N   GLU A  59     4122   5316   5887   -334    443    465       N  
ATOM    450  CA  GLU A  59      30.273  -5.457 -77.255  1.00 40.51           C  
ANISOU  450  CA  GLU A  59     4217   5289   5885   -431    353    455       C  
ATOM    451  C   GLU A  59      31.123  -5.474 -75.988  1.00 42.90           C  
ANISOU  451  C   GLU A  59     4486   5589   6225   -511    250    514       C  
ATOM    452  O   GLU A  59      31.291  -6.532 -75.408  1.00 41.82           O  
ANISOU  452  O   GLU A  59     4319   5466   6104   -480    240    519       O  
ATOM    453  CB  GLU A  59      28.747  -5.376 -76.928  1.00 40.18           C  
ANISOU  453  CB  GLU A  59     4309   5190   5766   -412    354    341       C  
ATOM    454  CG  GLU A  59      28.325  -4.255 -75.997  1.00 42.00           C  
ANISOU  454  CG  GLU A  59     4637   5354   5968   -500    277    313       C  
ATOM    455  CD  GLU A  59      28.547  -2.823 -76.445  1.00 47.60           C  
ANISOU  455  CD  GLU A  59     5359   6041   6688   -563    263    348       C  
ATOM    456  OE1 GLU A  59      28.382  -1.918 -75.594  1.00 39.58           O  
ANISOU  456  OE1 GLU A  59     4421   4963   5656   -645    199    329       O  
ATOM    457  OE2 GLU A  59      28.885  -2.599 -77.630  1.00 36.53           O  
ANISOU  457  OE2 GLU A  59     3894   4678   5308   -533    319    393       O  
ATOM    458  N   SER A  60      31.724  -4.327 -75.609  1.00 41.44           N  
ANISOU  458  N   SER A  60     4300   5389   6058   -617    173    568       N  
ATOM    459  CA  SER A  60      32.484  -4.230 -74.352  1.00 42.17           C  
ANISOU  459  CA  SER A  60     4374   5478   6172   -715     57    623       C  
ATOM    460  C   SER A  60      31.659  -4.706 -73.165  1.00 45.62           C  
ANISOU  460  C   SER A  60     4918   5874   6544   -724     10    543       C  
ATOM    461  O   SER A  60      30.476  -4.406 -73.056  1.00 44.65           O  
ANISOU  461  O   SER A  60     4915   5696   6354   -708     34    443       O  
ATOM    462  CB  SER A  60      32.958  -2.808 -74.091  1.00 47.87           C  
ANISOU  462  CB  SER A  60     5119   6170   6900   -839    -21    664       C  
ATOM    463  OG  SER A  60      34.108  -2.598 -74.894  1.00 69.99           O  
ANISOU  463  OG  SER A  60     7784   9025   9784   -848     -2    776       O  
ATOM    464  N   GLY A  61      32.293  -5.510 -72.338  1.00 42.84           N  
ANISOU  464  N   GLY A  61     4510   5550   6218   -742    -49    597       N  
ATOM    465  CA  GLY A  61      31.702  -6.085 -71.148  1.00 41.76           C  
ANISOU  465  CA  GLY A  61     4457   5386   6024   -755    -99    543       C  
ATOM    466  C   GLY A  61      31.063  -7.429 -71.357  1.00 45.52           C  
ANISOU  466  C   GLY A  61     4925   5872   6497   -635    -20    496       C  
ATOM    467  O   GLY A  61      30.761  -8.110 -70.375  1.00 46.90           O  
ANISOU  467  O   GLY A  61     5141   6036   6641   -640    -60    475       O  
ATOM    468  N   VAL A  62      30.795  -7.816 -72.619  1.00 41.54           N  
ANISOU  468  N   VAL A  62     4380   5386   6018   -533     92    474       N  
ATOM    469  CA  VAL A  62      30.185  -9.115 -72.899  1.00 40.14           C  
ANISOU  469  CA  VAL A  62     4199   5213   5838   -423    171    424       C  
ATOM    470  C   VAL A  62      31.276 -10.225 -72.876  1.00 43.20           C  
ANISOU  470  C   VAL A  62     4452   5649   6314   -380    181    520       C  
ATOM    471  O   VAL A  62      32.346 -10.026 -73.441  1.00 41.61           O  
ANISOU  471  O   VAL A  62     4139   5488   6184   -385    194    612       O  
ATOM    472  CB  VAL A  62      29.382  -9.079 -74.214  1.00 41.82           C  
ANISOU  472  CB  VAL A  62     4440   5422   6028   -342    281    354       C  
ATOM    473  CG1 VAL A  62      28.755 -10.444 -74.506  1.00 40.34           C  
ANISOU  473  CG1 VAL A  62     4257   5235   5837   -239    358    299       C  
ATOM    474  CG2 VAL A  62      28.303  -8.016 -74.121  1.00 40.64           C  
ANISOU  474  CG2 VAL A  62     4414   5222   5807   -381    266    274       C  
ATOM    475  N   PRO A  63      31.035 -11.394 -72.245  1.00 41.07           N  
ANISOU  475  N   PRO A  63     4184   5372   6049   -335    182    508       N  
ATOM    476  CA  PRO A  63      32.068 -12.455 -72.238  1.00 41.62           C  
ANISOU  476  CA  PRO A  63     4119   5478   6215   -287    199    608       C  
ATOM    477  C   PRO A  63      32.431 -12.953 -73.640  1.00 48.35           C  
ANISOU  477  C   PRO A  63     4887   6355   7129   -186    329    621       C  
ATOM    478  O   PRO A  63      31.608 -12.960 -74.561  1.00 48.00           O  
ANISOU  478  O   PRO A  63     4906   6295   7038   -130    417    529       O  
ATOM    479  CB  PRO A  63      31.442 -13.574 -71.395  1.00 42.76           C  
ANISOU  479  CB  PRO A  63     4310   5597   6341   -249    189    569       C  
ATOM    480  CG  PRO A  63      30.293 -12.968 -70.714  1.00 46.55           C  
ANISOU  480  CG  PRO A  63     4939   6034   6714   -304    142    471       C  
ATOM    481  CD  PRO A  63      29.829 -11.815 -71.513  1.00 41.39           C  
ANISOU  481  CD  PRO A  63     4342   5369   6016   -323    172    412       C  
ATOM    482  N   ALA A  64      33.680 -13.367 -73.786  1.00 47.34           N  
ANISOU  482  N   ALA A  64     4617   6264   7106   -168    342    740       N  
ATOM    483  CA  ALA A  64      34.269 -13.851 -75.035  1.00 47.11           C  
ANISOU  483  CA  ALA A  64     4493   6260   7148    -76    472    773       C  
ATOM    484  C   ALA A  64      33.622 -15.146 -75.570  1.00 45.88           C  
ANISOU  484  C   ALA A  64     4369   6075   6989     41    591    693       C  
ATOM    485  O   ALA A  64      33.789 -15.488 -76.726  1.00 44.81           O  
ANISOU  485  O   ALA A  64     4204   5948   6875    117    714    677       O  
ATOM    486  CB  ALA A  64      35.747 -14.095 -74.808  1.00 49.79           C  
ANISOU  486  CB  ALA A  64     4665   6639   7614    -83    450    932       C  
ATOM    487  N   ARG A  65      32.909 -15.877 -74.725  1.00 43.00           N  
ANISOU  487  N   ARG A  65     4069   5675   6595     53    555    643       N  
ATOM    488  CA  ARG A  65      32.237 -17.085 -75.151  1.00 41.37           C  
ANISOU  488  CA  ARG A  65     3901   5432   6385    152    657    563       C  
ATOM    489  C   ARG A  65      31.125 -16.793 -76.189  1.00 43.22           C  
ANISOU  489  C   ARG A  65     4245   5651   6523    177    731    433       C  
ATOM    490  O   ARG A  65      30.740 -17.724 -76.893  1.00 41.64           O  
ANISOU  490  O   ARG A  65     4068   5430   6324    258    835    372       O  
ATOM    491  CB  ARG A  65      31.743 -17.888 -73.934  1.00 42.34           C  
ANISOU  491  CB  ARG A  65     4065   5521   6502    148    593    551       C  
ATOM    492  CG  ARG A  65      30.584 -17.283 -73.195  1.00 47.30           C  
ANISOU  492  CG  ARG A  65     4826   6125   7019     80    509    464       C  
ATOM    493  CD  ARG A  65      30.110 -18.267 -72.186  1.00 47.38           C  
ANISOU  493  CD  ARG A  65     4870   6103   7030     96    478    452       C  
ATOM    494  NE  ARG A  65      29.040 -17.726 -71.368  1.00 39.63           N  
ANISOU  494  NE  ARG A  65     4013   5098   5947     32    404    377       N  
ATOM    495  CZ  ARG A  65      29.199 -16.892 -70.348  1.00 44.85           C  
ANISOU  495  CZ  ARG A  65     4704   5770   6567    -67    290    412       C  
ATOM    496  NH1 ARG A  65      28.147 -16.445 -69.680  1.00 43.38           N  
ANISOU  496  NH1 ARG A  65     4642   5554   6288   -114    248    332       N  
ATOM    497  NH2 ARG A  65      30.408 -16.472 -70.004  1.00 57.43           N  
ANISOU  497  NH2 ARG A  65     6207   7402   8212   -124    219    527       N  
ATOM    498  N   PHE A  66      30.640 -15.506 -76.306  1.00 38.54           N  
ANISOU  498  N   PHE A  66     3721   5069   5854    106    678    398       N  
ATOM    499  CA  PHE A  66      29.672 -15.102 -77.312  1.00 37.17           C  
ANISOU  499  CA  PHE A  66     3636   4890   5598    122    736    298       C  
ATOM    500  C   PHE A  66      30.419 -14.655 -78.550  1.00 40.37           C  
ANISOU  500  C   PHE A  66     3978   5336   6025    141    814    341       C  
ATOM    501  O   PHE A  66      31.354 -13.889 -78.434  1.00 41.47           O  
ANISOU  501  O   PHE A  66     4043   5505   6209     92    774    433       O  
ATOM    502  CB  PHE A  66      28.751 -13.956 -76.800  1.00 37.35           C  
ANISOU  502  CB  PHE A  66     3759   4894   5538     44    648    247       C  
ATOM    503  CG  PHE A  66      27.863 -14.363 -75.645  1.00 36.73           C  
ANISOU  503  CG  PHE A  66     3758   4774   5423     28    587    193       C  
ATOM    504  CD1 PHE A  66      26.638 -14.962 -75.873  1.00 37.26           C  
ANISOU  504  CD1 PHE A  66     3908   4810   5439     73    631     93       C  
ATOM    505  CD2 PHE A  66      28.294 -14.223 -74.329  1.00 38.93           C  
ANISOU  505  CD2 PHE A  66     4025   5047   5721    -33    488    249       C  
ATOM    506  CE1 PHE A  66      25.849 -15.398 -74.819  1.00 37.99           C  
ANISOU  506  CE1 PHE A  66     4064   4865   5506     63    585     51       C  
ATOM    507  CE2 PHE A  66      27.498 -14.658 -73.268  1.00 40.74           C  
ANISOU  507  CE2 PHE A  66     4327   5239   5912    -45    442    202       C  
ATOM    508  CZ  PHE A  66      26.292 -15.264 -73.522  1.00 38.35           C  
ANISOU  508  CZ  PHE A  66     4099   4905   5566      7    496    106       C  
ATOM    509  N   SER A  67      30.005 -15.100 -79.739  1.00 38.63           N  
ANISOU  509  N   SER A  67     3792   5118   5767    204    924    275       N  
ATOM    510  CA  SER A  67      30.611 -14.637 -81.000  1.00 39.16           C  
ANISOU  510  CA  SER A  67     3817   5227   5835    220   1008    308       C  
ATOM    511  C   SER A  67      29.593 -14.657 -82.121  1.00 40.83           C  
ANISOU  511  C   SER A  67     4127   5439   5948    247   1076    205       C  
ATOM    512  O   SER A  67      28.738 -15.515 -82.157  1.00 40.83           O  
ANISOU  512  O   SER A  67     4196   5408   5910    284   1103    119       O  
ATOM    513  CB  SER A  67      31.846 -15.453 -81.390  1.00 43.58           C  
ANISOU  513  CB  SER A  67     4262   5804   6494    285   1105    385       C  
ATOM    514  OG  SER A  67      31.515 -16.743 -81.866  1.00 56.92           O  
ANISOU  514  OG  SER A  67     5984   7464   8179    370   1210    315       O  
ATOM    515  N   GLY A  68      29.733 -13.740 -83.053  1.00 36.62           N  
ANISOU  515  N   GLY A  68     3595   4942   5375    224   1102    224       N  
ATOM    516  CA  GLY A  68      28.857 -13.645 -84.192  1.00 36.02           C  
ANISOU  516  CA  GLY A  68     3606   4880   5201    238   1159    145       C  
ATOM    517  C   GLY A  68      29.622 -13.787 -85.481  1.00 41.32           C  
ANISOU  517  C   GLY A  68     4238   5593   5868    278   1282    174       C  
ATOM    518  O   GLY A  68      30.789 -13.398 -85.575  1.00 40.89           O  
ANISOU  518  O   GLY A  68     4086   5567   5883    273   1306    272       O  
ATOM    519  N   SER A  69      28.946 -14.298 -86.504  1.00 38.85           N  
ANISOU  519  N   SER A  69     4005   5286   5470    311   1360     91       N  
ATOM    520  CA  SER A  69      29.545 -14.434 -87.824  1.00 38.57           C  
ANISOU  520  CA  SER A  69     3957   5291   5406    346   1488    104       C  
ATOM    521  C   SER A  69      28.502 -14.359 -88.918  1.00 43.94           C  
ANISOU  521  C   SER A  69     4753   5992   5952    335   1517     19       C  
ATOM    522  O   SER A  69      27.310 -14.492 -88.680  1.00 43.58           O  
ANISOU  522  O   SER A  69     4789   5922   5848    316   1452    -57       O  
ATOM    523  CB  SER A  69      30.314 -15.743 -87.926  1.00 41.72           C  
ANISOU  523  CB  SER A  69     4311   5669   5873    425   1605    102       C  
ATOM    524  OG  SER A  69      29.447 -16.860 -87.843  1.00 56.99           O  
ANISOU  524  OG  SER A  69     6328   7555   7769    458   1625     -4       O  
ATOM    525  N   GLY A  70      28.978 -14.170 -90.120  1.00 43.47           N  
ANISOU  525  N   GLY A  70     4694   5979   5844    346   1615     38       N  
ATOM    526  CA  GLY A  70      28.138 -14.118 -91.295  1.00 43.44           C  
ANISOU  526  CA  GLY A  70     4797   6005   5704    332   1649    -31       C  
ATOM    527  C   GLY A  70      28.191 -12.800 -92.008  1.00 46.63           C  
ANISOU  527  C   GLY A  70     5199   6466   6054    281   1626     33       C  
ATOM    528  O   GLY A  70      28.758 -11.808 -91.523  1.00 43.47           O  
ANISOU  528  O   GLY A  70     4720   6073   5721    249   1569    125       O  
ATOM    529  N   SER A  71      27.514 -12.803 -93.150  1.00 46.59           N  
ANISOU  529  N   SER A  71     5287   6496   5919    267   1662    -19       N  
ATOM    530  CA  SER A  71      27.405 -11.652 -94.047  1.00 48.41           C  
ANISOU  530  CA  SER A  71     5534   6785   6073    219   1649     35       C  
ATOM    531  C   SER A  71      26.249 -11.886 -95.022  1.00 52.11           C  
ANISOU  531  C   SER A  71     6126   7282   6392    196   1647    -44       C  
ATOM    532  O   SER A  71      25.839 -13.026 -95.268  1.00 52.15           O  
ANISOU  532  O   SER A  71     6202   7268   6346    221   1696   -140       O  
ATOM    533  CB  SER A  71      28.693 -11.483 -94.847  1.00 55.10           C  
ANISOU  533  CB  SER A  71     6323   7679   6935    241   1773    109       C  
ATOM    534  OG  SER A  71      28.885 -12.650 -95.633  1.00 66.71           O  
ANISOU  534  OG  SER A  71     7848   9154   8347    291   1909     37       O  
ATOM    535  N   GLY A  72      25.755 -10.800 -95.569  1.00 48.12           N  
ANISOU  535  N   GLY A  72     5644   6819   5822    144   1588      2       N  
ATOM    536  CA  GLY A  72      24.706 -10.845 -96.569  1.00 48.00           C  
ANISOU  536  CA  GLY A  72     5734   6843   5660    110   1573    -47       C  
ATOM    537  C   GLY A  72      23.367 -11.135 -95.986  1.00 47.67           C  
ANISOU  537  C   GLY A  72     5743   6763   5606     91   1466   -114       C  
ATOM    538  O   GLY A  72      22.739 -10.227 -95.443  1.00 47.48           O  
ANISOU  538  O   GLY A  72     5699   6726   5617     60   1357    -72       O  
ATOM    539  N   THR A  73      22.946 -12.401 -96.064  1.00 42.44           N  
ANISOU  539  N   THR A  73     5146   6077   4901    112   1502   -218       N  
ATOM    540  CA  THR A  73      21.670 -12.852 -95.536  1.00 41.49           C  
ANISOU  540  CA  THR A  73     5073   5919   4771     95   1410   -286       C  
ATOM    541  C   THR A  73      21.745 -13.881 -94.425  1.00 43.11           C  
ANISOU  541  C   THR A  73     5258   6051   5070    139   1416   -347       C  
ATOM    542  O   THR A  73      20.730 -14.076 -93.793  1.00 42.32           O  
ANISOU  542  O   THR A  73     5178   5916   4985    125   1331   -384       O  
ATOM    543  CB  THR A  73      20.793 -13.405 -96.675  1.00 51.64           C  
ANISOU  543  CB  THR A  73     6471   7244   5904     58   1418   -356       C  
ATOM    544  OG1 THR A  73      21.415 -14.565 -97.250  1.00 50.28           O  
ANISOU  544  OG1 THR A  73     6351   7068   5685     89   1546   -430       O  
ATOM    545  CG2 THR A  73      20.497 -12.362 -97.742  1.00 51.31           C  
ANISOU  545  CG2 THR A  73     6455   7280   5759      5   1387   -289       C  
ATOM    546  N   ASP A  74      22.875 -14.543 -94.175  1.00 39.87           N  
ANISOU  546  N   ASP A  74     4805   5616   4728    193   1514   -349       N  
ATOM    547  CA  ASP A  74      22.955 -15.657 -93.190  1.00 38.99           C  
ANISOU  547  CA  ASP A  74     4677   5433   4703    238   1528   -405       C  
ATOM    548  C   ASP A  74      23.861 -15.326 -92.051  1.00 38.55           C  
ANISOU  548  C   ASP A  74     4513   5349   4786    265   1509   -331       C  
ATOM    549  O   ASP A  74      25.018 -15.099 -92.260  1.00 40.69           O  
ANISOU  549  O   ASP A  74     4720   5640   5101    288   1579   -268       O  
ATOM    550  CB  ASP A  74      23.452 -16.955 -93.894  1.00 41.88           C  
ANISOU  550  CB  ASP A  74     5095   5785   5033    281   1667   -478       C  
ATOM    551  CG  ASP A  74      22.717 -17.200 -95.201  1.00 60.30           C  
ANISOU  551  CG  ASP A  74     7547   8158   7205    240   1694   -548       C  
ATOM    552  OD1 ASP A  74      21.467 -17.227 -95.180  1.00 61.76           O  
ANISOU  552  OD1 ASP A  74     7793   8341   7332    194   1600   -595       O  
ATOM    553  OD2 ASP A  74      23.395 -17.281 -96.268  1.00 66.96           O  
ANISOU  553  OD2 ASP A  74     8423   9041   7979    249   1808   -548       O  
ATOM    554  N   PHE A  75      23.347 -15.313 -90.848  1.00 36.24           N  
ANISOU  554  N   PHE A  75     4199   5009   4560    259   1416   -335       N  
ATOM    555  CA  PHE A  75      24.094 -14.920 -89.649  1.00 34.29           C  
ANISOU  555  CA  PHE A  75     3859   4735   4435    269   1374   -264       C  
ATOM    556  C   PHE A  75      23.953 -15.940 -88.515  1.00 37.56           C  
ANISOU  556  C   PHE A  75     4263   5085   4922    301   1356   -304       C  
ATOM    557  O   PHE A  75      22.931 -16.619 -88.368  1.00 35.78           O  
ANISOU  557  O   PHE A  75     4104   4830   4662    299   1330   -382       O  
ATOM    558  CB  PHE A  75      23.668 -13.517 -89.199  1.00 34.24           C  
ANISOU  558  CB  PHE A  75     3836   4739   4436    216   1265   -207       C  
ATOM    559  CG  PHE A  75      23.853 -12.478 -90.279  1.00 35.04           C  
ANISOU  559  CG  PHE A  75     3940   4899   4475    185   1281   -154       C  
ATOM    560  CD1 PHE A  75      22.834 -12.208 -91.190  1.00 36.88           C  
ANISOU  560  CD1 PHE A  75     4248   5164   4601    156   1262   -186       C  
ATOM    561  CD2 PHE A  75      25.033 -11.764 -90.379  1.00 32.75           C  
ANISOU  561  CD2 PHE A  75     3573   4634   4235    181   1311    -63       C  
ATOM    562  CE1 PHE A  75      23.047 -11.331 -92.248  1.00 37.81           C  
ANISOU  562  CE1 PHE A  75     4370   5340   4656    128   1283   -131       C  
ATOM    563  CE2 PHE A  75      25.227 -10.856 -91.401  1.00 36.33           C  
ANISOU  563  CE2 PHE A  75     4028   5142   4631    153   1334    -10       C  
ATOM    564  CZ  PHE A  75      24.224 -10.628 -92.328  1.00 36.14           C  
ANISOU  564  CZ  PHE A  75     4085   5151   4496    128   1319    -43       C  
ATOM    565  N   THR A  76      25.011 -16.039 -87.717  1.00 35.55           N  
ANISOU  565  N   THR A  76     3921   4813   4772    325   1365   -242       N  
ATOM    566  CA  THR A  76      25.090 -17.000 -86.624  1.00 36.07           C  
ANISOU  566  CA  THR A  76     3963   4823   4918    358   1352   -258       C  
ATOM    567  C   THR A  76      25.626 -16.370 -85.341  1.00 39.83           C  
ANISOU  567  C   THR A  76     4363   5289   5483    334   1265   -177       C  
ATOM    568  O   THR A  76      26.591 -15.631 -85.390  1.00 40.75           O  
ANISOU  568  O   THR A  76     4406   5435   5640    320   1267    -92       O  
ATOM    569  CB  THR A  76      26.023 -18.148 -87.054  1.00 43.13           C  
ANISOU  569  CB  THR A  76     4826   5703   5858    426   1481   -262       C  
ATOM    570  OG1 THR A  76      25.547 -18.679 -88.277  1.00 50.05           O  
ANISOU  570  OG1 THR A  76     5790   6588   6638    438   1564   -345       O  
ATOM    571  CG2 THR A  76      26.110 -19.264 -86.039  1.00 40.54           C  
ANISOU  571  CG2 THR A  76     4474   5313   5615    466   1479   -275       C  
ATOM    572  N   LEU A  77      24.971 -16.640 -84.219  1.00 35.60           N  
ANISOU  572  N   LEU A  77     3848   4710   4970    322   1188   -202       N  
ATOM    573  CA  LEU A  77      25.430 -16.309 -82.886  1.00 34.70           C  
ANISOU  573  CA  LEU A  77     3678   4578   4930    299   1107   -139       C  
ATOM    574  C   LEU A  77      25.866 -17.656 -82.299  1.00 39.29           C  
ANISOU  574  C   LEU A  77     4223   5121   5583    352   1145   -139       C  
ATOM    575  O   LEU A  77      25.116 -18.625 -82.330  1.00 36.81           O  
ANISOU  575  O   LEU A  77     3966   4771   5248    381   1173   -215       O  
ATOM    576  CB  LEU A  77      24.322 -15.737 -82.000  1.00 33.74           C  
ANISOU  576  CB  LEU A  77     3615   4429   4775    250   1003   -171       C  
ATOM    577  CG  LEU A  77      24.671 -15.502 -80.519  1.00 36.31           C  
ANISOU  577  CG  LEU A  77     3907   4730   5159    218    918   -120       C  
ATOM    578  CD1 LEU A  77      25.758 -14.497 -80.375  1.00 36.87           C  
ANISOU  578  CD1 LEU A  77     3908   4830   5269    178    885    -28       C  
ATOM    579  CD2 LEU A  77      23.452 -15.036 -79.768  1.00 38.22           C  
ANISOU  579  CD2 LEU A  77     4224   4939   5357    180    842   -168       C  
ATOM    580  N   THR A  78      27.058 -17.692 -81.731  1.00 38.93           N  
ANISOU  580  N   THR A  78     4081   5082   5628    360   1141    -47       N  
ATOM    581  CA  THR A  78      27.596 -18.877 -81.090  1.00 39.02           C  
ANISOU  581  CA  THR A  78     4041   5058   5725    410   1169    -22       C  
ATOM    582  C   THR A  78      27.884 -18.571 -79.636  1.00 42.72           C  
ANISOU  582  C   THR A  78     4466   5519   6245    366   1055     47       C  
ATOM    583  O   THR A  78      28.413 -17.504 -79.327  1.00 38.79           O  
ANISOU  583  O   THR A  78     3928   5053   5757    309    988    115       O  
ATOM    584  CB  THR A  78      28.880 -19.376 -81.792  1.00 44.26           C  
ANISOU  584  CB  THR A  78     4614   5738   6466    470   1283     40       C  
ATOM    585  OG1 THR A  78      28.615 -19.558 -83.184  1.00 43.93           O  
ANISOU  585  OG1 THR A  78     4628   5706   6355    501   1391    -29       O  
ATOM    586  CG2 THR A  78      29.366 -20.711 -81.227  1.00 41.88           C  
ANISOU  586  CG2 THR A  78     4261   5390   6262    535   1328     66       C  
ATOM    587  N   ILE A  79      27.454 -19.482 -78.742  1.00 41.55           N  
ANISOU  587  N   ILE A  79     4340   5327   6120    383   1029     24       N  
ATOM    588  CA  ILE A  79      27.811 -19.473 -77.323  1.00 41.46           C  
ANISOU  588  CA  ILE A  79     4288   5307   6159    348    931     95       C  
ATOM    589  C   ILE A  79      28.680 -20.758 -77.187  1.00 45.23           C  
ANISOU  589  C   ILE A  79     4679   5762   6743    420    996    153       C  
ATOM    590  O   ILE A  79      28.150 -21.853 -77.110  1.00 41.85           O  
ANISOU  590  O   ILE A  79     4289   5288   6325    469   1040    100       O  
ATOM    591  CB  ILE A  79      26.606 -19.461 -76.360  1.00 42.77           C  
ANISOU  591  CB  ILE A  79     4546   5440   6265    310    851     33       C  
ATOM    592  CG1 ILE A  79      25.499 -18.484 -76.831  1.00 42.67           C  
ANISOU  592  CG1 ILE A  79     4626   5433   6153    269    831    -48       C  
ATOM    593  CG2 ILE A  79      27.084 -19.118 -74.943  1.00 42.49           C  
ANISOU  593  CG2 ILE A  79     4477   5410   6259    252    740    114       C  
ATOM    594  CD1 ILE A  79      24.212 -18.640 -76.030  1.00 46.88           C  
ANISOU  594  CD1 ILE A  79     5249   5927   6634    248    781   -116       C  
ATOM    595  N   SER A  80      29.997 -20.618 -77.254  1.00 47.59           N  
ANISOU  595  N   SER A  80     4862   6092   7129    430   1011    264       N  
ATOM    596  CA  SER A  80      30.958 -21.756 -77.296  1.00 49.56           C  
ANISOU  596  CA  SER A  80     5012   6322   7499    510   1092    336       C  
ATOM    597  C   SER A  80      30.927 -22.735 -76.100  1.00 58.27           C  
ANISOU  597  C   SER A  80     6093   7383   8662    526   1043    375       C  
ATOM    598  O   SER A  80      31.144 -23.950 -76.292  1.00 60.19           O  
ANISOU  598  O   SER A  80     6307   7581   8980    609   1135    378       O  
ATOM    599  CB  SER A  80      32.368 -21.233 -77.477  1.00 49.65           C  
ANISOU  599  CB  SER A  80     4887   6380   7596    505   1100    466       C  
ATOM    600  OG  SER A  80      32.761 -20.454 -76.359  1.00 58.14           O  
ANISOU  600  OG  SER A  80     5919   7488   8684    419    954    555       O  
ATOM    601  N   SER A  81      30.677 -22.216 -74.885  1.00 53.32           N  
ANISOU  601  N   SER A  81     5487   6770   8004    448    904    406       N  
ATOM    602  CA  SER A  81      30.652 -23.050 -73.692  1.00 52.28           C  
ANISOU  602  CA  SER A  81     5338   6607   7917    452    845    453       C  
ATOM    603  C   SER A  81      29.562 -22.517 -72.750  1.00 53.22           C  
ANISOU  603  C   SER A  81     5569   6722   7929    372    735    391       C  
ATOM    604  O   SER A  81      29.835 -21.696 -71.875  1.00 51.76           O  
ANISOU  604  O   SER A  81     5377   6570   7719    288    619    449       O  
ATOM    605  CB  SER A  81      32.020 -23.047 -73.022  1.00 57.66           C  
ANISOU  605  CB  SER A  81     5877   7322   8708    437    788    618       C  
ATOM    606  OG  SER A  81      32.006 -23.928 -71.911  1.00 78.63           O  
ANISOU  606  OG  SER A  81     8516   9950  11408    445    734    671       O  
ATOM    607  N   LEU A  82      28.313 -22.974 -72.988  1.00 47.74           N  
ANISOU  607  N   LEU A  82     4983   5985   7170    397    777    270       N  
ATOM    608  CA  LEU A  82      27.124 -22.548 -72.275  1.00 45.95           C  
ANISOU  608  CA  LEU A  82     4867   5746   6845    338    703    197       C  
ATOM    609  C   LEU A  82      27.265 -22.575 -70.791  1.00 47.52           C  
ANISOU  609  C   LEU A  82     5062   5948   7045    283    594    267       C  
ATOM    610  O   LEU A  82      27.741 -23.560 -70.241  1.00 48.76           O  
ANISOU  610  O   LEU A  82     5160   6088   7277    317    593    338       O  
ATOM    611  CB  LEU A  82      25.924 -23.445 -72.598  1.00 45.64           C  
ANISOU  611  CB  LEU A  82     4914   5654   6775    385    770     87       C  
ATOM    612  CG  LEU A  82      24.850 -23.020 -73.586  1.00 49.83           C  
ANISOU  612  CG  LEU A  82     5533   6180   7221    384    816    -32       C  
ATOM    613  CD1 LEU A  82      23.636 -23.879 -73.374  1.00 50.75           C  
ANISOU  613  CD1 LEU A  82     5728   6244   7310    404    836   -115       C  
ATOM    614  CD2 LEU A  82      24.405 -21.615 -73.405  1.00 46.49           C  
ANISOU  614  CD2 LEU A  82     5159   5788   6716    310    743    -51       C  
ATOM    615  N   GLU A  83      26.706 -21.569 -70.138  1.00 41.08           N  
ANISOU  615  N   GLU A  83     4323   5146   6140    201    509    238       N  
ATOM    616  CA  GLU A  83      26.641 -21.504 -68.680  1.00 40.38           C  
ANISOU  616  CA  GLU A  83     4264   5058   6020    135    404    283       C  
ATOM    617  C   GLU A  83      25.210 -21.462 -68.262  1.00 41.29           C  
ANISOU  617  C   GLU A  83     4505   5138   6046    118    402    180       C  
ATOM    618  O   GLU A  83      24.361 -21.043 -69.066  1.00 39.24           O  
ANISOU  618  O   GLU A  83     4304   4866   5740    133    454     84       O  
ATOM    619  CB  GLU A  83      27.354 -20.257 -68.182  1.00 42.45           C  
ANISOU  619  CB  GLU A  83     4512   5366   6253     39    304    346       C  
ATOM    620  CG  GLU A  83      28.864 -20.414 -68.215  1.00 49.79           C  
ANISOU  620  CG  GLU A  83     5301   6335   7284     41    278    483       C  
ATOM    621  CD  GLU A  83      29.655 -19.240 -67.681  1.00 71.34           C  
ANISOU  621  CD  GLU A  83     8006   9109   9992    -65    167    557       C  
ATOM    622  OE1 GLU A  83      30.895 -19.243 -67.854  1.00 85.75           O  
ANISOU  622  OE1 GLU A  83     9706  10971  11905    -67    148    673       O  
ATOM    623  OE2 GLU A  83      29.044 -18.316 -67.099  1.00 60.97           O  
ANISOU  623  OE2 GLU A  83     6799   7790   8577   -147    103    502       O  
ATOM    624  N   PRO A  84      24.887 -21.831 -67.005  1.00 38.35           N  
ANISOU  624  N   PRO A  84     4175   4753   5645     84    342    201       N  
ATOM    625  CA  PRO A  84      23.481 -21.731 -66.548  1.00 36.83           C  
ANISOU  625  CA  PRO A  84     4101   4525   5367     67    347    106       C  
ATOM    626  C   PRO A  84      22.833 -20.348 -66.666  1.00 38.23           C  
ANISOU  626  C   PRO A  84     4362   4707   5458     10    329     36       C  
ATOM    627  O   PRO A  84      21.646 -20.227 -66.975  1.00 37.38           O  
ANISOU  627  O   PRO A  84     4326   4570   5307     28    376    -55       O  
ATOM    628  CB  PRO A  84      23.559 -22.170 -65.081  1.00 39.21           C  
ANISOU  628  CB  PRO A  84     4424   4825   5649     23    272    168       C  
ATOM    629  CG  PRO A  84      24.744 -23.023 -65.011  1.00 44.19           C  
ANISOU  629  CG  PRO A  84     4939   5472   6379     56    259    282       C  
ATOM    630  CD  PRO A  84      25.743 -22.404 -65.947  1.00 40.29           C  
ANISOU  630  CD  PRO A  84     4360   5013   5934     62    270    318       C  
ATOM    631  N   GLU A  85      23.623 -19.303 -66.487  1.00 36.36           N  
ANISOU  631  N   GLU A  85     4110   4503   5204    -56    265     83       N  
ATOM    632  CA  GLU A  85      23.138 -17.920 -66.577  1.00 36.47           C  
ANISOU  632  CA  GLU A  85     4199   4512   5145   -113    248     26       C  
ATOM    633  C   GLU A  85      22.810 -17.479 -68.047  1.00 37.93           C  
ANISOU  633  C   GLU A  85     4370   4697   5345    -66    324    -31       C  
ATOM    634  O   GLU A  85      22.280 -16.385 -68.227  1.00 35.78           O  
ANISOU  634  O   GLU A  85     4158   4414   5022   -100    322    -80       O  
ATOM    635  CB  GLU A  85      24.135 -16.922 -65.892  1.00 38.22           C  
ANISOU  635  CB  GLU A  85     4414   4764   5345   -211    149     97       C  
ATOM    636  CG  GLU A  85      25.399 -16.617 -66.689  1.00 57.35           C  
ANISOU  636  CG  GLU A  85     6724   7227   7838   -210    141    172       C  
ATOM    637  CD  GLU A  85      26.407 -15.692 -66.027  1.00100.60           C  
ANISOU  637  CD  GLU A  85    12185  12735  13302   -315     35    250       C  
ATOM    638  OE1 GLU A  85      25.985 -14.659 -65.455  1.00115.60           O  
ANISOU  638  OE1 GLU A  85    14188  14615  15121   -395    -10    206       O  
ATOM    639  OE2 GLU A  85      27.624 -15.969 -66.137  1.00 94.37           O  
ANISOU  639  OE2 GLU A  85    11281  11987  12589   -319      2    356       O  
ATOM    640  N   ASP A  86      23.142 -18.309 -69.067  1.00 33.87           N  
ANISOU  640  N   ASP A  86     3779   4193   4896     10    391    -23       N  
ATOM    641  CA  ASP A  86      22.864 -18.052 -70.476  1.00 33.51           C  
ANISOU  641  CA  ASP A  86     3723   4153   4855     53    464    -74       C  
ATOM    642  C   ASP A  86      21.416 -18.365 -70.857  1.00 37.49           C  
ANISOU  642  C   ASP A  86     4302   4624   5320     89    517   -172       C  
ATOM    643  O   ASP A  86      21.009 -18.092 -71.990  1.00 36.40           O  
ANISOU  643  O   ASP A  86     4169   4492   5169    114    567   -218       O  
ATOM    644  CB  ASP A  86      23.876 -18.786 -71.381  1.00 35.77           C  
ANISOU  644  CB  ASP A  86     3908   4463   5220    113    521    -26       C  
ATOM    645  CG  ASP A  86      25.296 -18.317 -71.117  1.00 42.09           C  
ANISOU  645  CG  ASP A  86     4623   5303   6068     75    469     81       C  
ATOM    646  OD1 ASP A  86      25.455 -17.251 -70.515  1.00 41.41           O  
ANISOU  646  OD1 ASP A  86     4564   5228   5944     -4    392    104       O  
ATOM    647  OD2 ASP A  86      26.248 -19.068 -71.442  1.00 46.80           O  
ANISOU  647  OD2 ASP A  86     5123   5913   6746    122    504    147       O  
ATOM    648  N   PHE A  87      20.607 -18.824 -69.889  1.00 34.09           N  
ANISOU  648  N   PHE A  87     3929   4160   4863     81    500   -199       N  
ATOM    649  CA  PHE A  87      19.174 -18.970 -70.069  1.00 32.12           C  
ANISOU  649  CA  PHE A  87     3747   3879   4578    101    538   -281       C  
ATOM    650  C   PHE A  87      18.611 -17.554 -70.439  1.00 32.96           C  
ANISOU  650  C   PHE A  87     3901   3986   4635     66    530   -317       C  
ATOM    651  O   PHE A  87      18.787 -16.605 -69.682  1.00 32.57           O  
ANISOU  651  O   PHE A  87     3888   3934   4554      9    481   -298       O  
ATOM    652  CB  PHE A  87      18.549 -19.523 -68.760  1.00 34.21           C  
ANISOU  652  CB  PHE A  87     4064   4112   4824     86    514   -286       C  
ATOM    653  CG  PHE A  87      17.070 -19.409 -68.775  1.00 37.32           C  
ANISOU  653  CG  PHE A  87     4526   4473   5180     93    545   -359       C  
ATOM    654  CD1 PHE A  87      16.307 -20.248 -69.571  1.00 43.27           C  
ANISOU  654  CD1 PHE A  87     5273   5212   5956    143    601   -407       C  
ATOM    655  CD2 PHE A  87      16.436 -18.354 -68.135  1.00 39.72           C  
ANISOU  655  CD2 PHE A  87     4900   4761   5430     48    525   -381       C  
ATOM    656  CE1 PHE A  87      14.950 -20.026 -69.742  1.00 43.72           C  
ANISOU  656  CE1 PHE A  87     5379   5247   5987    146    625   -465       C  
ATOM    657  CE2 PHE A  87      15.066 -18.165 -68.266  1.00 42.77           C  
ANISOU  657  CE2 PHE A  87     5335   5119   5797     61    562   -440       C  
ATOM    658  CZ  PHE A  87      14.336 -18.986 -69.082  1.00 41.00           C  
ANISOU  658  CZ  PHE A  87     5090   4889   5600    109    608   -476       C  
ATOM    659  N   ALA A  88      17.956 -17.427 -71.597  1.00 29.41           N  
ANISOU  659  N   ALA A  88     3456   3541   4179     97    578   -364       N  
ATOM    660  CA  ALA A  88      17.438 -16.151 -72.110  1.00 29.83           C  
ANISOU  660  CA  ALA A  88     3541   3596   4199     73    577   -386       C  
ATOM    661  C   ALA A  88      16.803 -16.374 -73.456  1.00 32.44           C  
ANISOU  661  C   ALA A  88     3861   3939   4526    113    626   -427       C  
ATOM    662  O   ALA A  88      16.996 -17.420 -74.055  1.00 31.88           O  
ANISOU  662  O   ALA A  88     3759   3878   4476    152    662   -438       O  
ATOM    663  CB  ALA A  88      18.593 -15.154 -72.308  1.00 32.04           C  
ANISOU  663  CB  ALA A  88     3786   3903   4484     36    546   -332       C  
ATOM    664  N   VAL A  89      16.197 -15.327 -73.987  1.00 28.86           N  
ANISOU  664  N   VAL A  89     3432   3487   4048     98    627   -441       N  
ATOM    665  CA  VAL A  89      15.724 -15.256 -75.374  1.00 29.11           C  
ANISOU  665  CA  VAL A  89     3452   3543   4066    121    660   -463       C  
ATOM    666  C   VAL A  89      16.782 -14.392 -76.121  1.00 33.16           C  
ANISOU  666  C   VAL A  89     3926   4093   4578    105    657   -418       C  
ATOM    667  O   VAL A  89      17.206 -13.342 -75.629  1.00 33.99           O  
ANISOU  667  O   VAL A  89     4039   4192   4685     66    624   -384       O  
ATOM    668  CB  VAL A  89      14.278 -14.701 -75.519  1.00 33.36           C  
ANISOU  668  CB  VAL A  89     4031   4060   4585    118    661   -494       C  
ATOM    669  CG1 VAL A  89      13.843 -14.703 -76.970  1.00 32.85           C  
ANISOU  669  CG1 VAL A  89     3951   4030   4499    132    682   -507       C  
ATOM    670  CG2 VAL A  89      13.313 -15.547 -74.711  1.00 33.55           C  
ANISOU  670  CG2 VAL A  89     4084   4047   4617    131    667   -529       C  
ATOM    671  N   TYR A  90      17.227 -14.854 -77.285  1.00 30.62           N  
ANISOU  671  N   TYR A  90     3571   3811   4254    131    696   -418       N  
ATOM    672  CA  TYR A  90      18.235 -14.166 -78.081  1.00 29.70           C  
ANISOU  672  CA  TYR A  90     3414   3734   4138    121    706   -372       C  
ATOM    673  C   TYR A  90      17.604 -13.649 -79.336  1.00 32.96           C  
ANISOU  673  C   TYR A  90     3841   4173   4509    122    725   -386       C  
ATOM    674  O   TYR A  90      16.939 -14.403 -80.002  1.00 33.04           O  
ANISOU  674  O   TYR A  90     3869   4192   4494    145    753   -429       O  
ATOM    675  CB  TYR A  90      19.400 -15.115 -78.396  1.00 30.53           C  
ANISOU  675  CB  TYR A  90     3464   3863   4275    152    746   -350       C  
ATOM    676  CG  TYR A  90      20.184 -15.494 -77.165  1.00 30.00           C  
ANISOU  676  CG  TYR A  90     3366   3776   4255    144    715   -311       C  
ATOM    677  CD1 TYR A  90      19.726 -16.474 -76.303  1.00 29.02           C  
ANISOU  677  CD1 TYR A  90     3263   3618   4145    161    708   -339       C  
ATOM    678  CD2 TYR A  90      21.353 -14.815 -76.820  1.00 33.06           C  
ANISOU  678  CD2 TYR A  90     3705   4183   4674    112    684   -239       C  
ATOM    679  CE1 TYR A  90      20.426 -16.800 -75.150  1.00 31.56           C  
ANISOU  679  CE1 TYR A  90     3559   3927   4505    148    671   -293       C  
ATOM    680  CE2 TYR A  90      22.048 -15.119 -75.650  1.00 32.84           C  
ANISOU  680  CE2 TYR A  90     3650   4144   4685     94    640   -194       C  
ATOM    681  CZ  TYR A  90      21.599 -16.137 -74.838  1.00 34.12           C  
ANISOU  681  CZ  TYR A  90     3834   4275   4856    114    634   -220       C  
ATOM    682  OH  TYR A  90      22.278 -16.411 -73.678  1.00 35.51           O  
ANISOU  682  OH  TYR A  90     3984   4445   5063     90    584   -166       O  
ATOM    683  N   TYR A  91      17.770 -12.362 -79.648  1.00 31.91           N  
ANISOU  683  N   TYR A  91     3704   4052   4368     93    706   -346       N  
ATOM    684  CA  TYR A  91      17.170 -11.743 -80.844  1.00 30.11           C  
ANISOU  684  CA  TYR A  91     3487   3852   4100     90    717   -343       C  
ATOM    685  C   TYR A  91      18.229 -11.167 -81.722  1.00 34.04           C  
ANISOU  685  C   TYR A  91     3946   4395   4592     80    739   -292       C  
ATOM    686  O   TYR A  91      19.178 -10.581 -81.218  1.00 34.38           O  
ANISOU  686  O   TYR A  91     3959   4433   4670     56    721   -244       O  
ATOM    687  CB  TYR A  91      16.239 -10.572 -80.469  1.00 29.35           C  
ANISOU  687  CB  TYR A  91     3424   3721   4007     66    680   -333       C  
ATOM    688  CG  TYR A  91      15.066 -10.918 -79.594  1.00 31.30           C  
ANISOU  688  CG  TYR A  91     3708   3920   4263     74    666   -376       C  
ATOM    689  CD1 TYR A  91      13.855 -11.331 -80.148  1.00 34.57           C  
ANISOU  689  CD1 TYR A  91     4138   4341   4657     91    671   -405       C  
ATOM    690  CD2 TYR A  91      15.133 -10.780 -78.215  1.00 31.69           C  
ANISOU  690  CD2 TYR A  91     3781   3920   4340     60    645   -381       C  
ATOM    691  CE1 TYR A  91      12.760 -11.652 -79.346  1.00 33.46           C  
ANISOU  691  CE1 TYR A  91     4023   4156   4533     99    663   -437       C  
ATOM    692  CE2 TYR A  91      14.015 -11.022 -77.407  1.00 31.96           C  
ANISOU  692  CE2 TYR A  91     3852   3909   4381     69    642   -416       C  
ATOM    693  CZ  TYR A  91      12.832 -11.470 -77.979  1.00 36.94           C  
ANISOU  693  CZ  TYR A  91     4487   4547   5003     92    654   -442       C  
ATOM    694  OH  TYR A  91      11.695 -11.706 -77.234  1.00 40.28           O  
ANISOU  694  OH  TYR A  91     4937   4928   5441    101    656   -469       O  
ATOM    695  N   CYS A  92      18.028 -11.254 -83.032  1.00 31.58           N  
ANISOU  695  N   CYS A  92     3637   4128   4232     90    771   -296       N  
ATOM    696  CA  CYS A  92      18.845 -10.557 -84.003  1.00 32.66           C  
ANISOU  696  CA  CYS A  92     3745   4312   4353     78    796   -242       C  
ATOM    697  C   CYS A  92      18.041  -9.335 -84.449  1.00 34.70           C  
ANISOU  697  C   CYS A  92     4025   4571   4589     51    762   -212       C  
ATOM    698  O   CYS A  92      16.827  -9.283 -84.253  1.00 31.75           O  
ANISOU  698  O   CYS A  92     3685   4172   4206     51    733   -240       O  
ATOM    699  CB  CYS A  92      19.210 -11.455 -85.175  1.00 34.36           C  
ANISOU  699  CB  CYS A  92     3957   4576   4521    104    863   -264       C  
ATOM    700  SG  CYS A  92      17.784 -12.071 -86.063  1.00 38.70           S  
ANISOU  700  SG  CYS A  92     4569   5144   4992    107    865   -329       S  
ATOM    701  N   GLN A  93      18.729  -8.340 -85.019  1.00 34.19           N  
ANISOU  701  N   GLN A  93     3934   4533   4525     28    767   -148       N  
ATOM    702  CA  GLN A  93      18.101  -7.085 -85.446  1.00 33.75           C  
ANISOU  702  CA  GLN A  93     3892   4472   4460      4    738   -104       C  
ATOM    703  C   GLN A  93      18.936  -6.432 -86.554  1.00 36.82           C  
ANISOU  703  C   GLN A  93     4250   4915   4824    -13    766    -37       C  
ATOM    704  O   GLN A  93      20.159  -6.356 -86.436  1.00 36.76           O  
ANISOU  704  O   GLN A  93     4202   4920   4847    -20    789     -4       O  
ATOM    705  CB  GLN A  93      18.027  -6.130 -84.250  1.00 33.93           C  
ANISOU  705  CB  GLN A  93     3924   4425   4545    -21    694    -85       C  
ATOM    706  CG  GLN A  93      17.503  -4.714 -84.540  1.00 34.61           C  
ANISOU  706  CG  GLN A  93     4020   4485   4643    -45    670    -33       C  
ATOM    707  CD  GLN A  93      18.529  -3.623 -84.348  1.00 38.53           C  
ANISOU  707  CD  GLN A  93     4496   4963   5181    -84    660     29       C  
ATOM    708  OE1 GLN A  93      19.275  -3.615 -83.362  1.00 38.05           O  
ANISOU  708  OE1 GLN A  93     4429   4871   5158   -106    645     24       O  
ATOM    709  NE2 GLN A  93      18.589  -2.654 -85.272  1.00 34.37           N  
ANISOU  709  NE2 GLN A  93     3956   4456   4647   -101    664     95       N  
ATOM    710  N   HIS A  94      18.282  -5.887 -87.576  1.00 32.51           N  
ANISOU  710  N   HIS A  94     3720   4401   4230    -21    762     -8       N  
ATOM    711  CA  HIS A  94      19.026  -5.241 -88.641  1.00 33.67           C  
ANISOU  711  CA  HIS A  94     3843   4601   4348    -39    791     61       C  
ATOM    712  C   HIS A  94      18.801  -3.776 -88.589  1.00 39.69           C  
ANISOU  712  C   HIS A  94     4601   5332   5148    -69    752    131       C  
ATOM    713  O   HIS A  94      17.803  -3.294 -88.025  1.00 37.21           O  
ANISOU  713  O   HIS A  94     4311   4963   4866    -70    709    125       O  
ATOM    714  CB  HIS A  94      18.660  -5.773 -90.036  1.00 34.00           C  
ANISOU  714  CB  HIS A  94     3910   4718   4292    -33    824     51       C  
ATOM    715  CG  HIS A  94      17.412  -5.151 -90.557  1.00 37.36           C  
ANISOU  715  CG  HIS A  94     4361   5149   4683    -48    775     78       C  
ATOM    716  ND1 HIS A  94      17.445  -3.962 -91.257  1.00 39.65           N  
ANISOU  716  ND1 HIS A  94     4639   5459   4967    -74    762    166       N  
ATOM    717  CD2 HIS A  94      16.126  -5.457 -90.289  1.00 38.03           C  
ANISOU  717  CD2 HIS A  94     4474   5210   4764    -42    732     40       C  
ATOM    718  CE1 HIS A  94      16.185  -3.607 -91.417  1.00 38.03           C  
ANISOU  718  CE1 HIS A  94     4452   5243   4753    -78    712    181       C  
ATOM    719  NE2 HIS A  94      15.363  -4.478 -90.857  1.00 37.79           N  
ANISOU  719  NE2 HIS A  94     4444   5190   4726    -60    692    108       N  
ATOM    720  N   SER A  95      19.712  -3.073 -89.270  1.00 37.52           N  
ANISOU  720  N   SER A  95     4294   5091   4871    -91    777    204       N  
ATOM    721  CA  SER A  95      19.608  -1.638 -89.518  1.00 37.33           C  
ANISOU  721  CA  SER A  95     4263   5044   4875   -122    750    285       C  
ATOM    722  C   SER A  95      20.115  -1.315 -90.921  1.00 43.64           C  
ANISOU  722  C   SER A  95     5044   5923   5615   -135    789    354       C  
ATOM    723  O   SER A  95      20.807  -0.331 -91.155  1.00 42.38           O  
ANISOU  723  O   SER A  95     4854   5761   5487   -164    794    433       O  
ATOM    724  CB  SER A  95      20.322  -0.842 -88.436  1.00 41.01           C  
ANISOU  724  CB  SER A  95     4711   5441   5431   -152    727    310       C  
ATOM    725  OG  SER A  95      21.544  -1.474 -88.110  1.00 52.24           O  
ANISOU  725  OG  SER A  95     6094   6885   6871   -154    754    301       O  
ATOM    726  N   ARG A  96      19.728  -2.150 -91.875  1.00 43.49           N  
ANISOU  726  N   ARG A  96     5049   5972   5502   -117    816    325       N  
ATOM    727  CA  ARG A  96      20.069  -1.917 -93.270  1.00 45.45           C  
ANISOU  727  CA  ARG A  96     5297   6302   5672   -132    855    384       C  
ATOM    728  C   ARG A  96      19.118  -0.880 -93.894  1.00 49.83           C  
ANISOU  728  C   ARG A  96     5866   6860   6207   -154    805    457       C  
ATOM    729  O   ARG A  96      19.502  -0.103 -94.754  1.00 51.37           O  
ANISOU  729  O   ARG A  96     6048   7095   6376   -178    820    543       O  
ATOM    730  CB  ARG A  96      19.961  -3.240 -94.049  1.00 42.91           C  
ANISOU  730  CB  ARG A  96     5012   6048   5245   -112    904    316       C  
ATOM    731  CG  ARG A  96      20.234  -3.108 -95.550  1.00 51.20           C  
ANISOU  731  CG  ARG A  96     6078   7187   6187   -131    951    367       C  
ATOM    732  CD  ARG A  96      21.671  -2.680 -95.886  1.00 49.51           C  
ANISOU  732  CD  ARG A  96     5816   7000   5995   -137   1022    432       C  
ATOM    733  NE  ARG A  96      21.865  -2.602 -97.337  1.00 60.64           N  
ANISOU  733  NE  ARG A  96     7252   8498   7290   -155   1075    477       N  
ATOM    734  CZ  ARG A  96      21.493  -1.583 -98.111  1.00 82.88           C  
ANISOU  734  CZ  ARG A  96    10076  11347  10067   -189   1043    567       C  
ATOM    735  NH1 ARG A  96      20.895  -0.517 -97.584  1.00 73.70           N  
ANISOU  735  NH1 ARG A  96     8892  10129   8982   -205    962    624       N  
ATOM    736  NH2 ARG A  96      21.719  -1.620 -99.419  1.00 76.88           N  
ANISOU  736  NH2 ARG A  96     9347  10674   9189   -208   1096    604       N  
ATOM    737  N   ASP A  97      17.896  -0.885 -93.408  1.00 45.74           N  
ANISOU  737  N   ASP A  97     5371   6299   5711   -144    749    428       N  
ATOM    738  CA  ASP A  97      16.686  -0.264 -93.923  1.00 44.31           C  
ANISOU  738  CA  ASP A  97     5203   6121   5513   -153    696    481       C  
ATOM    739  C   ASP A  97      15.813   0.223 -92.832  1.00 42.98           C  
ANISOU  739  C   ASP A  97     5032   5857   5441   -138    650    471       C  
ATOM    740  O   ASP A  97      15.868  -0.318 -91.739  1.00 40.52           O  
ANISOU  740  O   ASP A  97     4727   5492   5177   -119    653    395       O  
ATOM    741  CB  ASP A  97      15.805  -1.459 -94.471  1.00 46.68           C  
ANISOU  741  CB  ASP A  97     5542   6480   5716   -146    683    415       C  
ATOM    742  CG  ASP A  97      15.423  -1.355 -95.884  1.00 65.84           C  
ANISOU  742  CG  ASP A  97     7988   8995   8034   -174    671    472       C  
ATOM    743  OD1 ASP A  97      16.131  -0.654 -96.628  1.00 71.11           O  
ANISOU  743  OD1 ASP A  97     8644   9702   8675   -195    698    550       O  
ATOM    744  OD2 ASP A  97      14.427  -2.004 -96.268  1.00 73.09           O  
ANISOU  744  OD2 ASP A  97     8936   9947   8888   -182    633    442       O  
ATOM    745  N   LEU A  98      14.810   0.985 -93.232  1.00 39.32           N  
ANISOU  745  N   LEU A  98     4564   5384   4990   -141    607    541       N  
ATOM    746  CA  LEU A  98      13.677   1.355 -92.436  1.00 38.71           C  
ANISOU  746  CA  LEU A  98     4486   5228   4994   -120    569    540       C  
ATOM    747  C   LEU A  98      12.489   0.557 -92.989  1.00 41.88           C  
ANISOU  747  C   LEU A  98     4896   5684   5331   -114    532    522       C  
ATOM    748  O   LEU A  98      12.326   0.440 -94.201  1.00 40.87           O  
ANISOU  748  O   LEU A  98     4772   5644   5112   -138    515    568       O  
ATOM    749  CB  LEU A  98      13.402   2.863 -92.527  1.00 39.25           C  
ANISOU  749  CB  LEU A  98     4534   5238   5140   -126    552    648       C  
ATOM    750  CG  LEU A  98      14.411   3.780 -91.836  1.00 44.18           C  
ANISOU  750  CG  LEU A  98     5156   5788   5844   -140    579    666       C  
ATOM    751  CD1 LEU A  98      13.925   5.209 -91.888  1.00 45.99           C  
ANISOU  751  CD1 LEU A  98     5373   5945   6158   -142    565    767       C  
ATOM    752  CD2 LEU A  98      14.645   3.390 -90.407  1.00 41.57           C  
ANISOU  752  CD2 LEU A  98     4846   5378   5571   -129    592    570       C  
ATOM    753  N   PRO A  99      11.632   0.000 -92.137  1.00 39.71           N  
ANISOU  753  N   PRO A  99     4628   5362   5100    -89    515    460       N  
ATOM    754  CA  PRO A  99      11.722  -0.018 -90.676  1.00 39.41           C  
ANISOU  754  CA  PRO A  99     4597   5225   5152    -64    534    396       C  
ATOM    755  C   PRO A  99      12.782  -0.962 -90.125  1.00 43.13           C  
ANISOU  755  C   PRO A  99     5086   5704   5596    -64    571    304       C  
ATOM    756  O   PRO A  99      13.008  -2.058 -90.654  1.00 42.57           O  
ANISOU  756  O   PRO A  99     5027   5703   5443    -68    583    254       O  
ATOM    757  CB  PRO A  99      10.326  -0.498 -90.256  1.00 41.45           C  
ANISOU  757  CB  PRO A  99     4853   5459   5439    -40    505    369       C  
ATOM    758  CG  PRO A  99       9.862  -1.366 -91.388  1.00 45.40           C  
ANISOU  758  CG  PRO A  99     5354   6061   5834    -60    474    368       C  
ATOM    759  CD  PRO A  99      10.492  -0.797 -92.631  1.00 41.58           C  
ANISOU  759  CD  PRO A  99     4867   5649   5282    -91    473    445       C  
ATOM    760  N   LEU A 100      13.390  -0.552 -89.002  1.00 39.79           N  
ANISOU  760  N   LEU A 100     4668   5204   5246    -61    589    281       N  
ATOM    761  CA  LEU A 100      14.279  -1.410 -88.234  1.00 37.51           C  
ANISOU  761  CA  LEU A 100     4389   4910   4954    -59    614    202       C  
ATOM    762  C   LEU A 100      13.375  -2.541 -87.718  1.00 37.96           C  
ANISOU  762  C   LEU A 100     4464   4959   5000    -33    605    123       C  
ATOM    763  O   LEU A 100      12.223  -2.320 -87.319  1.00 37.49           O  
ANISOU  763  O   LEU A 100     4410   4855   4981    -17    584    125       O  
ATOM    764  CB  LEU A 100      14.905  -0.712 -87.037  1.00 36.77           C  
ANISOU  764  CB  LEU A 100     4302   4729   4938    -71    619    197       C  
ATOM    765  CG  LEU A 100      15.717   0.549 -87.248  1.00 42.39           C  
ANISOU  765  CG  LEU A 100     5001   5419   5685   -104    622    272       C  
ATOM    766  CD1 LEU A 100      16.300   0.985 -85.944  1.00 42.42           C  
ANISOU  766  CD1 LEU A 100     5024   5339   5754   -125    618    245       C  
ATOM    767  CD2 LEU A 100      16.858   0.316 -88.222  1.00 47.22           C  
ANISOU  767  CD2 LEU A 100     5581   6117   6242   -122    645    306       C  
ATOM    768  N   THR A 101      13.890  -3.727 -87.713  1.00 34.01           N  
ANISOU  768  N   THR A 101     3970   4498   4455    -28    626     59       N  
ATOM    769  CA  THR A 101      13.081  -4.895 -87.362  1.00 34.25           C  
ANISOU  769  CA  THR A 101     4017   4527   4468     -8    619    -13       C  
ATOM    770  C   THR A 101      13.951  -5.948 -86.649  1.00 35.90           C  
ANISOU  770  C   THR A 101     4232   4730   4678      3    649    -83       C  
ATOM    771  O   THR A 101      15.184  -5.956 -86.769  1.00 31.57           O  
ANISOU  771  O   THR A 101     3669   4203   4125     -4    677    -72       O  
ATOM    772  CB  THR A 101      12.370  -5.307 -88.690  1.00 41.25           C  
ANISOU  772  CB  THR A 101     4908   5490   5275    -18    602      2       C  
ATOM    773  OG1 THR A 101      10.983  -5.524 -88.473  1.00 56.44           O  
ANISOU  773  OG1 THR A 101     6834   7394   7219     -9    566     -8       O  
ATOM    774  CG2 THR A 101      13.001  -6.416 -89.364  1.00 33.31           C  
ANISOU  774  CG2 THR A 101     3918   4547   4190    -22    634    -48       C  
ATOM    775  N   PHE A 102      13.290  -6.749 -85.807  1.00 33.15           N  
ANISOU  775  N   PHE A 102     3901   4345   4351     21    641   -144       N  
ATOM    776  CA  PHE A 102      13.901  -7.754 -84.976  1.00 31.21           C  
ANISOU  776  CA  PHE A 102     3660   4082   4117     35    662   -204       C  
ATOM    777  C   PHE A 102      13.438  -9.125 -85.450  1.00 35.79           C  
ANISOU  777  C   PHE A 102     4255   4696   4648     48    674   -264       C  
ATOM    778  O   PHE A 102      12.355  -9.224 -85.999  1.00 33.09           O  
ANISOU  778  O   PHE A 102     3924   4371   4279     43    650   -264       O  
ATOM    779  CB  PHE A 102      13.462  -7.562 -83.515  1.00 32.18           C  
ANISOU  779  CB  PHE A 102     3798   4126   4302     41    646   -226       C  
ATOM    780  CG  PHE A 102      14.037  -6.364 -82.798  1.00 33.29           C  
ANISOU  780  CG  PHE A 102     3941   4217   4490     20    638   -188       C  
ATOM    781  CD1 PHE A 102      13.453  -5.109 -82.925  1.00 34.34           C  
ANISOU  781  CD1 PHE A 102     4080   4316   4652     12    625   -140       C  
ATOM    782  CD2 PHE A 102      15.174  -6.488 -82.014  1.00 34.56           C  
ANISOU  782  CD2 PHE A 102     4097   4363   4670      6    641   -195       C  
ATOM    783  CE1 PHE A 102      14.006  -4.002 -82.285  1.00 34.14           C  
ANISOU  783  CE1 PHE A 102     4068   4237   4669    -13    621   -110       C  
ATOM    784  CE2 PHE A 102      15.750  -5.375 -81.423  1.00 36.55           C  
ANISOU  784  CE2 PHE A 102     4357   4571   4959    -26    626   -160       C  
ATOM    785  CZ  PHE A 102      15.140  -4.153 -81.519  1.00 34.26           C  
ANISOU  785  CZ  PHE A 102     4085   4240   4693    -37    618   -125       C  
ATOM    786  N   GLY A 103      14.253 -10.164 -85.209  1.00 32.36           N  
ANISOU  786  N   GLY A 103     3821   4267   4209     62    708   -308       N  
ATOM    787  CA  GLY A 103      13.854 -11.537 -85.461  1.00 31.86           C  
ANISOU  787  CA  GLY A 103     3779   4215   4111     75    725   -374       C  
ATOM    788  C   GLY A 103      12.927 -11.924 -84.344  1.00 36.88           C  
ANISOU  788  C   GLY A 103     4427   4795   4793     85    699   -407       C  
ATOM    789  O   GLY A 103      12.792 -11.187 -83.367  1.00 36.00           O  
ANISOU  789  O   GLY A 103     4309   4637   4733     85    679   -385       O  
ATOM    790  N   GLY A 104      12.297 -13.075 -84.486  1.00 33.35           N  
ANISOU  790  N   GLY A 104     4000   4349   4324     90    703   -463       N  
ATOM    791  CA  GLY A 104      11.354 -13.580 -83.512  1.00 31.47           C  
ANISOU  791  CA  GLY A 104     3771   4061   4126     98    683   -494       C  
ATOM    792  C   GLY A 104      11.879 -14.226 -82.250  1.00 34.34           C  
ANISOU  792  C   GLY A 104     4134   4377   4537    119    701   -521       C  
ATOM    793  O   GLY A 104      11.088 -14.612 -81.386  1.00 35.18           O  
ANISOU  793  O   GLY A 104     4250   4441   4675    125    688   -543       O  
ATOM    794  N   GLY A 105      13.170 -14.396 -82.157  1.00 30.11           N  
ANISOU  794  N   GLY A 105     3584   3848   4007    130    729   -515       N  
ATOM    795  CA  GLY A 105      13.816 -14.934 -80.967  1.00 31.11           C  
ANISOU  795  CA  GLY A 105     3702   3936   4180    145    738   -523       C  
ATOM    796  C   GLY A 105      14.075 -16.426 -80.946  1.00 37.58           C  
ANISOU  796  C   GLY A 105     4526   4746   5005    170    773   -569       C  
ATOM    797  O   GLY A 105      13.317 -17.208 -81.523  1.00 37.32           O  
ANISOU  797  O   GLY A 105     4518   4716   4946    171    782   -614       O  
ATOM    798  N   THR A 106      15.203 -16.819 -80.312  1.00 34.95           N  
ANISOU  798  N   THR A 106     4168   4402   4711    187    791   -552       N  
ATOM    799  CA  THR A 106      15.522 -18.190 -79.985  1.00 33.73           C  
ANISOU  799  CA  THR A 106     4010   4221   4583    216    825   -582       C  
ATOM    800  C   THR A 106      15.653 -18.252 -78.441  1.00 36.77           C  
ANISOU  800  C   THR A 106     4387   4566   5017    215    792   -558       C  
ATOM    801  O   THR A 106      16.463 -17.530 -77.844  1.00 32.70           O  
ANISOU  801  O   THR A 106     3846   4056   4522    201    768   -508       O  
ATOM    802  CB  THR A 106      16.790 -18.712 -80.652  1.00 34.81           C  
ANISOU  802  CB  THR A 106     4115   4379   4730    244    883   -570       C  
ATOM    803  OG1 THR A 106      16.591 -18.802 -82.046  1.00 31.26           O  
ANISOU  803  OG1 THR A 106     3691   3964   4223    242    921   -602       O  
ATOM    804  CG2 THR A 106      17.169 -20.129 -80.143  1.00 30.54           C  
ANISOU  804  CG2 THR A 106     3566   3798   4238    281    921   -591       C  
ATOM    805  N   LYS A 107      14.872 -19.132 -77.809  1.00 33.77           N  
ANISOU  805  N   LYS A 107     4032   4148   4653    223    789   -593       N  
ATOM    806  CA  LYS A 107      14.924 -19.295 -76.351  1.00 33.00           C  
ANISOU  806  CA  LYS A 107     3935   4015   4590    220    761   -572       C  
ATOM    807  C   LYS A 107      15.918 -20.392 -76.009  1.00 37.56           C  
ANISOU  807  C   LYS A 107     4480   4579   5212    249    787   -555       C  
ATOM    808  O   LYS A 107      15.791 -21.486 -76.542  1.00 35.99           O  
ANISOU  808  O   LYS A 107     4286   4365   5024    277    830   -592       O  
ATOM    809  CB  LYS A 107      13.539 -19.642 -75.823  1.00 33.76           C  
ANISOU  809  CB  LYS A 107     4069   4076   4682    214    749   -609       C  
ATOM    810  CG  LYS A 107      13.473 -19.918 -74.328  1.00 52.58           C  
ANISOU  810  CG  LYS A 107     6465   6423   7090    209    729   -591       C  
ATOM    811  CD  LYS A 107      12.003 -20.073 -73.928  1.00 58.20           C  
ANISOU  811  CD  LYS A 107     7212   7104   7797    202    726   -623       C  
ATOM    812  CE  LYS A 107      11.764 -20.248 -72.451  1.00 68.53           C  
ANISOU  812  CE  LYS A 107     8544   8376   9117    194    713   -608       C  
ATOM    813  NZ  LYS A 107      10.747 -19.280 -71.929  1.00 67.73           N  
ANISOU  813  NZ  LYS A 107     8476   8258   8998    174    706   -611       N  
ATOM    814  N   VAL A 108      16.962 -20.072 -75.206  1.00 34.28           N  
ANISOU  814  N   VAL A 108     4032   4170   4825    241    761   -495       N  
ATOM    815  CA  VAL A 108      17.973 -21.043 -74.814  1.00 33.74           C  
ANISOU  815  CA  VAL A 108     3918   4090   4812    270    779   -458       C  
ATOM    816  C   VAL A 108      17.622 -21.529 -73.411  1.00 40.21           C  
ANISOU  816  C   VAL A 108     4756   4873   5648    260    742   -444       C  
ATOM    817  O   VAL A 108      17.498 -20.726 -72.490  1.00 38.06           O  
ANISOU  817  O   VAL A 108     4506   4603   5352    219    689   -420       O  
ATOM    818  CB  VAL A 108      19.436 -20.550 -74.937  1.00 36.66           C  
ANISOU  818  CB  VAL A 108     4222   4496   5212    269    775   -386       C  
ATOM    819  CG1 VAL A 108      20.402 -21.593 -74.376  1.00 37.30           C  
ANISOU  819  CG1 VAL A 108     4247   4561   5365    301    788   -332       C  
ATOM    820  CG2 VAL A 108      19.772 -20.255 -76.391  1.00 35.91           C  
ANISOU  820  CG2 VAL A 108     4110   4434   5100    285    828   -400       C  
ATOM    821  N   GLU A 109      17.386 -22.841 -73.287  1.00 39.42           N  
ANISOU  821  N   GLU A 109     4657   4738   5582    295    776   -463       N  
ATOM    822  CA  GLU A 109      17.052 -23.505 -72.044  1.00 38.95           C  
ANISOU  822  CA  GLU A 109     4614   4643   5542    291    751   -447       C  
ATOM    823  C   GLU A 109      18.243 -24.379 -71.629  1.00 38.15           C  
ANISOU  823  C   GLU A 109     4452   4532   5510    321    759   -380       C  
ATOM    824  O   GLU A 109      18.985 -24.901 -72.472  1.00 36.48           O  
ANISOU  824  O   GLU A 109     4196   4321   5341    363    813   -373       O  
ATOM    825  CB  GLU A 109      15.784 -24.330 -72.226  1.00 41.17           C  
ANISOU  825  CB  GLU A 109     4940   4885   5819    304    781   -513       C  
ATOM    826  CG  GLU A 109      14.642 -23.537 -72.848  1.00 58.03           C  
ANISOU  826  CG  GLU A 109     7117   7033   7900    280    777   -568       C  
ATOM    827  CD  GLU A 109      13.379 -24.332 -73.124  1.00 88.57           C  
ANISOU  827  CD  GLU A 109    11019  10867  11768    284    800   -627       C  
ATOM    828  OE1 GLU A 109      12.290 -23.711 -73.177  1.00 79.92           O  
ANISOU  828  OE1 GLU A 109     9951   9775  10639    260    783   -652       O  
ATOM    829  OE2 GLU A 109      13.487 -25.561 -73.354  1.00 77.62           O  
ANISOU  829  OE2 GLU A 109     9628   9448  10418    312    836   -646       O  
ATOM    830  N   ILE A 110      18.486 -24.424 -70.326  1.00 34.08           N  
ANISOU  830  N   ILE A 110     3934   4013   5003    298    706   -322       N  
ATOM    831  CA  ILE A 110      19.589 -25.179 -69.731  1.00 34.52           C  
ANISOU  831  CA  ILE A 110     3926   4063   5126    319    695   -237       C  
ATOM    832  C   ILE A 110      19.146 -26.545 -69.237  1.00 39.38           C  
ANISOU  832  C   ILE A 110     4551   4625   5785    353    722   -240       C  
ATOM    833  O   ILE A 110      18.191 -26.649 -68.471  1.00 40.58           O  
ANISOU  833  O   ILE A 110     4760   4758   5902    328    699   -262       O  
ATOM    834  CB  ILE A 110      20.307 -24.344 -68.622  1.00 37.17           C  
ANISOU  834  CB  ILE A 110     4246   4435   5441    261    607   -156       C  
ATOM    835  CG1 ILE A 110      20.624 -22.897 -69.133  1.00 36.24           C  
ANISOU  835  CG1 ILE A 110     4129   4361   5278    220    581   -161       C  
ATOM    836  CG2 ILE A 110      21.568 -25.039 -68.164  1.00 39.07           C  
ANISOU  836  CG2 ILE A 110     4401   4682   5760    281    590    -51       C  
ATOM    837  CD1 ILE A 110      21.560 -22.817 -70.392  1.00 40.67           C  
ANISOU  837  CD1 ILE A 110     4617   4948   5886    257    631   -144       C  
ATOM    838  N   LYS A 111      19.868 -27.583 -69.643  1.00 37.46           N  
ANISOU  838  N   LYS A 111     4252   4356   5626    410    775   -210       N  
ATOM    839  CA  LYS A 111      19.603 -28.955 -69.223  1.00 38.98           C  
ANISOU  839  CA  LYS A 111     4445   4488   5877    448    806   -202       C  
ATOM    840  C   LYS A 111      20.344 -29.226 -67.958  1.00 42.40           C  
ANISOU  840  C   LYS A 111     4832   4928   6349    437    747    -89       C  
ATOM    841  O   LYS A 111      21.460 -28.783 -67.789  1.00 42.14           O  
ANISOU  841  O   LYS A 111     4735   4936   6341    429    710     -8       O  
ATOM    842  CB  LYS A 111      20.062 -29.990 -70.255  1.00 43.60           C  
ANISOU  842  CB  LYS A 111     4996   5028   6541    519    903   -223       C  
ATOM    843  CG  LYS A 111      19.216 -30.049 -71.493  1.00 54.08           C  
ANISOU  843  CG  LYS A 111     6382   6337   7826    526    966   -340       C  
ATOM    844  CD  LYS A 111      19.739 -31.146 -72.444  1.00 59.76           C  
ANISOU  844  CD  LYS A 111     7082   7003   8620    594   1070   -364       C  
ATOM    845  CE  LYS A 111      18.710 -31.494 -73.506  1.00 82.21           C  
ANISOU  845  CE  LYS A 111    10003   9815  11416    590   1124   -486       C  
ATOM    846  NZ  LYS A 111      19.284 -32.309 -74.618  1.00 91.53           N  
ANISOU  846  NZ  LYS A 111    11181  10950  12644    646   1233   -524       N  
ATOM    847  N   ARG A 112      19.727 -29.960 -67.071  1.00 41.81           N  
ANISOU  847  N   ARG A 112     4790   4816   6279    433    732    -78       N  
ATOM    848  CA  ARG A 112      20.346 -30.397 -65.824  1.00 40.87           C  
ANISOU  848  CA  ARG A 112     4633   4699   6196    422    675     35       C  
ATOM    849  C   ARG A 112      19.788 -31.762 -65.467  1.00 43.05           C  
ANISOU  849  C   ARG A 112     4924   4905   6527    459    715     36       C  
ATOM    850  O   ARG A 112      18.926 -32.277 -66.178  1.00 42.94           O  
ANISOU  850  O   ARG A 112     4953   4843   6519    485    782    -57       O  
ATOM    851  CB  ARG A 112      20.126 -29.374 -64.700  1.00 34.15           C  
ANISOU  851  CB  ARG A 112     3830   3898   5247    339    579     62       C  
ATOM    852  CG  ARG A 112      18.710 -29.090 -64.348  1.00 39.85           C  
ANISOU  852  CG  ARG A 112     4650   4606   5886    304    581    -21       C  
ATOM    853  CD  ARG A 112      18.578 -28.645 -62.904  1.00 32.19           C  
ANISOU  853  CD  ARG A 112     3728   3662   4842    236    502     30       C  
ATOM    854  NE  ARG A 112      18.863 -29.757 -61.992  1.00 38.93           N  
ANISOU  854  NE  ARG A 112     4556   4492   5744    249    484    119       N  
ATOM    855  CZ  ARG A 112      19.395 -29.661 -60.780  1.00 46.06           C  
ANISOU  855  CZ  ARG A 112     5460   5428   6615    199    403    215       C  
ATOM    856  NH1 ARG A 112      19.707 -28.477 -60.273  1.00 35.62           N  
ANISOU  856  NH1 ARG A 112     4171   4159   5205    125    331    228       N  
ATOM    857  NH2 ARG A 112      19.596 -30.747 -60.052  1.00 46.49           N  
ANISOU  857  NH2 ARG A 112     5486   5458   6720    216    391    299       N  
ATOM    858  N   THR A 113      20.273 -32.335 -64.387  1.00 40.04           N  
ANISOU  858  N   THR A 113     4510   4519   6186    456    670    142       N  
ATOM    859  CA  THR A 113      19.790 -33.609 -63.889  1.00 40.71           C  
ANISOU  859  CA  THR A 113     4606   4536   6325    486    700    161       C  
ATOM    860  C   THR A 113      18.401 -33.408 -63.226  1.00 43.97           C  
ANISOU  860  C   THR A 113     5116   4945   6646    434    679    100       C  
ATOM    861  O   THR A 113      18.053 -32.315 -62.763  1.00 43.63           O  
ANISOU  861  O   THR A 113     5122   4956   6501    371    624     82       O  
ATOM    862  CB  THR A 113      20.799 -34.208 -62.884  1.00 43.62           C  
ANISOU  862  CB  THR A 113     4901   4909   6763    495    649    313       C  
ATOM    863  OG1 THR A 113      20.898 -33.311 -61.797  1.00 43.24           O  
ANISOU  863  OG1 THR A 113     4879   4931   6621    415    544    369       O  
ATOM    864  CG2 THR A 113      22.182 -34.466 -63.502  1.00 37.64           C  
ANISOU  864  CG2 THR A 113     4033   4153   6117    554    678    389       C  
ATOM    865  N   VAL A 114      17.627 -34.489 -63.195  1.00 39.91           N  
ANISOU  865  N   VAL A 114     4628   4361   6174    461    730     71       N  
ATOM    866  CA  VAL A 114      16.300 -34.511 -62.608  1.00 37.25           C  
ANISOU  866  CA  VAL A 114     4370   4010   5774    422    726     23       C  
ATOM    867  C   VAL A 114      16.361 -34.103 -61.112  1.00 41.00           C  
ANISOU  867  C   VAL A 114     4869   4529   6178    364    645    108       C  
ATOM    868  O   VAL A 114      17.223 -34.561 -60.352  1.00 40.89           O  
ANISOU  868  O   VAL A 114     4811   4524   6203    367    602    223       O  
ATOM    869  CB  VAL A 114      15.633 -35.920 -62.822  1.00 39.61           C  
ANISOU  869  CB  VAL A 114     4678   4218   6154    462    794     -2       C  
ATOM    870  CG1 VAL A 114      14.318 -36.055 -62.024  1.00 38.21           C  
ANISOU  870  CG1 VAL A 114     4568   4025   5923    420    787    -25       C  
ATOM    871  CG2 VAL A 114      15.374 -36.178 -64.308  1.00 38.42           C  
ANISOU  871  CG2 VAL A 114     4532   4027   6040    499    870   -109       C  
ATOM    872  N   ALA A 115      15.456 -33.203 -60.721  1.00 37.48           N  
ANISOU  872  N   ALA A 115     4499   4116   5628    309    626     54       N  
ATOM    873  CA  ALA A 115      15.331 -32.705 -59.359  1.00 35.67           C  
ANISOU  873  CA  ALA A 115     4320   3926   5307    246    563    109       C  
ATOM    874  C   ALA A 115      13.875 -32.796 -58.963  1.00 37.08           C  
ANISOU  874  C   ALA A 115     4574   4077   5438    226    602     49       C  
ATOM    875  O   ALA A 115      13.022 -32.208 -59.607  1.00 36.26           O  
ANISOU  875  O   ALA A 115     4503   3970   5305    223    639    -46       O  
ATOM    876  CB  ALA A 115      15.820 -31.268 -59.289  1.00 36.26           C  
ANISOU  876  CB  ALA A 115     4414   4068   5296    195    507    100       C  
ATOM    877  N   ALA A 116      13.566 -33.604 -57.974  1.00 35.27           N  
ANISOU  877  N   ALA A 116     4363   3824   5213    217    599    111       N  
ATOM    878  CA  ALA A 116      12.184 -33.717 -57.492  1.00 35.32           C  
ANISOU  878  CA  ALA A 116     4437   3806   5178    197    640     67       C  
ATOM    879  C   ALA A 116      11.757 -32.432 -56.776  1.00 38.00           C  
ANISOU  879  C   ALA A 116     4856   4195   5388    135    618     42       C  
ATOM    880  O   ALA A 116      12.580 -31.818 -56.106  1.00 38.00           O  
ANISOU  880  O   ALA A 116     4872   4243   5322     93    553     95       O  
ATOM    881  CB  ALA A 116      12.075 -34.873 -56.517  1.00 36.16           C  
ANISOU  881  CB  ALA A 116     4545   3879   5317    198    640    155       C  
ATOM    882  N   PRO A 117      10.496 -31.992 -56.881  1.00 36.21           N  
ANISOU  882  N   PRO A 117     4679   3955   5124    126    670    -37       N  
ATOM    883  CA  PRO A 117      10.082 -30.817 -56.088  1.00 36.27           C  
ANISOU  883  CA  PRO A 117     4771   3998   5014     72    664    -57       C  
ATOM    884  C   PRO A 117       9.934 -31.150 -54.604  1.00 39.96           C  
ANISOU  884  C   PRO A 117     5299   4472   5413     30    651     14       C  
ATOM    885  O   PRO A 117       9.623 -32.282 -54.244  1.00 41.18           O  
ANISOU  885  O   PRO A 117     5436   4593   5616     48    672     61       O  
ATOM    886  CB  PRO A 117       8.711 -30.464 -56.662  1.00 36.81           C  
ANISOU  886  CB  PRO A 117     4858   4039   5089     87    737   -147       C  
ATOM    887  CG  PRO A 117       8.204 -31.737 -57.228  1.00 40.55           C  
ANISOU  887  CG  PRO A 117     5279   4462   5667    130    775   -150       C  
ATOM    888  CD  PRO A 117       9.369 -32.547 -57.659  1.00 36.91           C  
ANISOU  888  CD  PRO A 117     4753   3993   5279    160    739   -103       C  
ATOM    889  N   SER A 118      10.201 -30.161 -53.776  1.00 36.25           N  
ANISOU  889  N   SER A 118     4904   4044   4827    -29    616     23       N  
ATOM    890  CA  SER A 118       9.909 -30.115 -52.339  1.00 36.49           C  
ANISOU  890  CA  SER A 118     5025   4088   4752    -84    613     68       C  
ATOM    891  C   SER A 118       8.544 -29.425 -52.304  1.00 37.27           C  
ANISOU  891  C   SER A 118     5190   4162   4807    -85    703    -18       C  
ATOM    892  O   SER A 118       8.376 -28.363 -52.889  1.00 35.03           O  
ANISOU  892  O   SER A 118     4922   3883   4506    -84    720    -92       O  
ATOM    893  CB  SER A 118      10.926 -29.252 -51.592  1.00 38.27           C  
ANISOU  893  CB  SER A 118     5306   4368   4866   -157    528    107       C  
ATOM    894  OG  SER A 118      12.208 -29.812 -51.806  1.00 47.36           O  
ANISOU  894  OG  SER A 118     6374   5543   6078   -149    445    191       O  
ATOM    895  N   VAL A 119       7.591 -30.041 -51.659  1.00 36.32           N  
ANISOU  895  N   VAL A 119     5102   4016   4681    -82    764     -2       N  
ATOM    896  CA  VAL A 119       6.216 -29.593 -51.626  1.00 35.59           C  
ANISOU  896  CA  VAL A 119     5053   3895   4574    -72    862    -68       C  
ATOM    897  C   VAL A 119       5.822 -29.025 -50.269  1.00 38.54           C  
ANISOU  897  C   VAL A 119     5550   4282   4812   -127    897    -59       C  
ATOM    898  O   VAL A 119       6.211 -29.543 -49.230  1.00 38.76           O  
ANISOU  898  O   VAL A 119     5622   4329   4776   -167    864     16       O  
ATOM    899  CB  VAL A 119       5.293 -30.741 -52.078  1.00 38.02           C  
ANISOU  899  CB  VAL A 119     5292   4157   4996    -23    918    -63       C  
ATOM    900  CG1 VAL A 119       3.852 -30.271 -52.276  1.00 36.54           C  
ANISOU  900  CG1 VAL A 119     5121   3942   4822     -6   1016   -126       C  
ATOM    901  CG2 VAL A 119       5.851 -31.377 -53.345  1.00 36.65           C  
ANISOU  901  CG2 VAL A 119     5014   3969   4941     22    879    -71       C  
ATOM    902  N   PHE A 120       5.065 -27.931 -50.307  1.00 34.65           N  
ANISOU  902  N   PHE A 120     5115   3776   4275   -130    967   -134       N  
ATOM    903  CA  PHE A 120       4.556 -27.263 -49.128  1.00 35.13           C  
ANISOU  903  CA  PHE A 120     5304   3837   4208   -175   1027   -146       C  
ATOM    904  C   PHE A 120       3.130 -26.840 -49.402  1.00 39.21           C  
ANISOU  904  C   PHE A 120     5822   4310   4766   -134   1151   -206       C  
ATOM    905  O   PHE A 120       2.852 -26.311 -50.465  1.00 36.47           O  
ANISOU  905  O   PHE A 120     5416   3948   4493    -94   1165   -261       O  
ATOM    906  CB  PHE A 120       5.370 -25.998 -48.799  1.00 35.77           C  
ANISOU  906  CB  PHE A 120     5475   3943   4171   -234    978   -179       C  
ATOM    907  CG  PHE A 120       6.849 -26.212 -48.621  1.00 36.69           C  
ANISOU  907  CG  PHE A 120     5579   4109   4254   -282    845   -117       C  
ATOM    908  CD1 PHE A 120       7.702 -26.221 -49.715  1.00 36.69           C  
ANISOU  908  CD1 PHE A 120     5476   4122   4341   -255    771   -116       C  
ATOM    909  CD2 PHE A 120       7.386 -26.458 -47.361  1.00 36.79           C  
ANISOU  909  CD2 PHE A 120     5675   4156   4149   -353    794    -48       C  
ATOM    910  CE1 PHE A 120       9.078 -26.429 -49.547  1.00 38.33           C  
ANISOU  910  CE1 PHE A 120     5659   4376   4530   -295    652    -47       C  
ATOM    911  CE2 PHE A 120       8.764 -26.676 -47.199  1.00 39.13           C  
ANISOU  911  CE2 PHE A 120     5945   4501   4424   -398    662     25       C  
ATOM    912  CZ  PHE A 120       9.600 -26.643 -48.289  1.00 36.47           C  
ANISOU  912  CZ  PHE A 120     5497   4174   4185   -367    594     27       C  
ATOM    913  N   ILE A 121       2.256 -27.007 -48.415  1.00 38.31           N  
ANISOU  913  N   ILE A 121     5777   4179   4598   -145   1241   -191       N  
ATOM    914  CA  ILE A 121       0.842 -26.581 -48.498  1.00 37.77           C  
ANISOU  914  CA  ILE A 121     5714   4070   4569   -106   1373   -235       C  
ATOM    915  C   ILE A 121       0.625 -25.447 -47.439  1.00 40.17           C  
ANISOU  915  C   ILE A 121     6170   4365   4728   -148   1449   -273       C  
ATOM    916  O   ILE A 121       1.279 -25.426 -46.389  1.00 38.66           O  
ANISOU  916  O   ILE A 121     6085   4200   4404   -212   1413   -246       O  
ATOM    917  CB  ILE A 121      -0.157 -27.790 -48.362  1.00 40.34           C  
ANISOU  917  CB  ILE A 121     5974   4372   4980    -74   1436   -183       C  
ATOM    918  CG1 ILE A 121      -1.625 -27.350 -48.655  1.00 39.72           C  
ANISOU  918  CG1 ILE A 121     5867   4252   4973    -28   1565   -220       C  
ATOM    919  CG2 ILE A 121      -0.057 -28.461 -47.000  1.00 40.84           C  
ANISOU  919  CG2 ILE A 121     6119   4449   4947   -119   1448   -114       C  
ATOM    920  CD1 ILE A 121      -2.651 -28.532 -48.900  1.00 43.55           C  
ANISOU  920  CD1 ILE A 121     6251   4713   5583      6   1611   -172       C  
ATOM    921  N   PHE A 122      -0.217 -24.472 -47.781  1.00 37.62           N  
ANISOU  921  N   PHE A 122     5859   4004   4433   -113   1546   -336       N  
ATOM    922  CA  PHE A 122      -0.531 -23.344 -46.915  1.00 38.77           C  
ANISOU  922  CA  PHE A 122     6148   4124   4460   -141   1640   -385       C  
ATOM    923  C   PHE A 122      -2.021 -23.194 -46.806  1.00 44.34           C  
ANISOU  923  C   PHE A 122     6840   4780   5226    -87   1800   -396       C  
ATOM    924  O   PHE A 122      -2.705 -23.048 -47.831  1.00 43.04           O  
ANISOU  924  O   PHE A 122     6564   4593   5198    -25   1831   -410       O  
ATOM    925  CB  PHE A 122       0.025 -22.013 -47.453  1.00 39.54           C  
ANISOU  925  CB  PHE A 122     6282   4210   4532   -152   1609   -455       C  
ATOM    926  CG  PHE A 122       1.512 -21.991 -47.632  1.00 40.08           C  
ANISOU  926  CG  PHE A 122     6355   4326   4549   -207   1455   -444       C  
ATOM    927  CD1 PHE A 122       2.356 -21.874 -46.536  1.00 41.35           C  
ANISOU  927  CD1 PHE A 122     6642   4516   4555   -292   1400   -428       C  
ATOM    928  CD2 PHE A 122       2.075 -22.022 -48.903  1.00 40.28           C  
ANISOU  928  CD2 PHE A 122     6260   4368   4678   -177   1365   -448       C  
ATOM    929  CE1 PHE A 122       3.736 -21.855 -46.696  1.00 40.77           C  
ANISOU  929  CE1 PHE A 122     6559   4488   4444   -345   1252   -405       C  
ATOM    930  CE2 PHE A 122       3.454 -22.071 -49.060  1.00 41.69           C  
ANISOU  930  CE2 PHE A 122     6429   4590   4820   -223   1228   -426       C  
ATOM    931  CZ  PHE A 122       4.281 -21.930 -47.958  1.00 40.35           C  
ANISOU  931  CZ  PHE A 122     6376   4450   4507   -307   1172   -404       C  
ATOM    932  N   PRO A 123      -2.551 -23.156 -45.575  1.00 42.72           N  
ANISOU  932  N   PRO A 123     6752   4560   4921   -110   1907   -388       N  
ATOM    933  CA  PRO A 123      -3.977 -22.886 -45.417  1.00 42.71           C  
ANISOU  933  CA  PRO A 123     6742   4508   4979    -55   2078   -397       C  
ATOM    934  C   PRO A 123      -4.296 -21.404 -45.665  1.00 46.84           C  
ANISOU  934  C   PRO A 123     7319   4980   5497    -30   2164   -475       C  
ATOM    935  O   PRO A 123      -3.411 -20.514 -45.635  1.00 46.90           O  
ANISOU  935  O   PRO A 123     7417   4989   5415    -73   2107   -528       O  
ATOM    936  CB  PRO A 123      -4.213 -23.247 -43.950  1.00 45.14           C  
ANISOU  936  CB  PRO A 123     7180   4819   5153    -99   2160   -366       C  
ATOM    937  CG  PRO A 123      -2.998 -22.872 -43.296  1.00 50.08           C  
ANISOU  937  CG  PRO A 123     7940   5477   5611   -182   2067   -387       C  
ATOM    938  CD  PRO A 123      -1.909 -23.316 -44.253  1.00 44.80           C  
ANISOU  938  CD  PRO A 123     7162   4851   5007   -190   1886   -366       C  
ATOM    939  N   PRO A 124      -5.578 -21.104 -45.865  1.00 44.06           N  
ANISOU  939  N   PRO A 124     6915   4579   5246     37   2307   -476       N  
ATOM    940  CA  PRO A 124      -5.989 -19.703 -45.963  1.00 44.51           C  
ANISOU  940  CA  PRO A 124     7031   4575   5304     68   2414   -541       C  
ATOM    941  C   PRO A 124      -5.724 -18.943 -44.652  1.00 46.73           C  
ANISOU  941  C   PRO A 124     7528   4828   5399     12   2500   -594       C  
ATOM    942  O   PRO A 124      -5.773 -19.537 -43.582  1.00 44.66           O  
ANISOU  942  O   PRO A 124     7354   4584   5032    -28   2538   -567       O  
ATOM    943  CB  PRO A 124      -7.494 -19.805 -46.268  1.00 46.45           C  
ANISOU  943  CB  PRO A 124     7164   4781   5703    152   2557   -505       C  
ATOM    944  CG  PRO A 124      -7.890 -21.071 -45.817  1.00 50.88           C  
ANISOU  944  CG  PRO A 124     7680   5373   6281    145   2564   -435       C  
ATOM    945  CD  PRO A 124      -6.740 -21.997 -45.953  1.00 46.27           C  
ANISOU  945  CD  PRO A 124     7081   4853   5648     88   2385   -412       C  
ATOM    946  N   SER A 125      -5.402 -17.652 -44.729  1.00 43.91           N  
ANISOU  946  N   SER A 125     7264   4427   4994      2   2525   -669       N  
ATOM    947  CA  SER A 125      -5.223 -16.852 -43.484  1.00 46.66           C  
ANISOU  947  CA  SER A 125     7835   4734   5159    -56   2621   -732       C  
ATOM    948  C   SER A 125      -6.557 -16.464 -42.890  1.00 53.72           C  
ANISOU  948  C   SER A 125     8778   5556   6078      4   2851   -743       C  
ATOM    949  O   SER A 125      -7.465 -16.146 -43.644  1.00 53.33           O  
ANISOU  949  O   SER A 125     8606   5464   6194     94   2936   -730       O  
ATOM    950  CB  SER A 125      -4.467 -15.555 -43.758  1.00 48.28           C  
ANISOU  950  CB  SER A 125     8132   4903   5310    -90   2580   -813       C  
ATOM    951  OG  SER A 125      -5.099 -14.804 -44.782  1.00 52.88           O  
ANISOU  951  OG  SER A 125     8608   5430   6052     -4   2641   -830       O  
ATOM    952  N   ASP A 126      -6.652 -16.380 -41.546  1.00 55.04           N  
ANISOU  952  N   ASP A 126     9130   5706   6077    -46   2957   -767       N  
ATOM    953  CA  ASP A 126      -7.845 -15.855 -40.863  1.00 57.01           C  
ANISOU  953  CA  ASP A 126     9457   5875   6328      8   3200   -790       C  
ATOM    954  C   ASP A 126      -8.215 -14.465 -41.369  1.00 60.24           C  
ANISOU  954  C   ASP A 126     9884   6190   6814     66   3307   -858       C  
ATOM    955  O   ASP A 126      -9.397 -14.121 -41.425  1.00 59.67           O  
ANISOU  955  O   ASP A 126     9764   6051   6857    156   3491   -847       O  
ATOM    956  CB  ASP A 126      -7.621 -15.763 -39.356  1.00 61.89           C  
ANISOU  956  CB  ASP A 126    10313   6487   6716    -76   3282   -828       C  
ATOM    957  CG  ASP A 126      -7.724 -17.089 -38.619  1.00 81.88           C  
ANISOU  957  CG  ASP A 126    12837   9089   9184   -110   3261   -746       C  
ATOM    958  OD1 ASP A 126      -8.379 -18.014 -39.148  1.00 84.36           O  
ANISOU  958  OD1 ASP A 126    12964   9431   9657    -46   3256   -662       O  
ATOM    959  OD2 ASP A 126      -7.210 -17.177 -37.481  1.00 91.51           O  
ANISOU  959  OD2 ASP A 126    14243  10333  10194   -203   3257   -764       O  
ATOM    960  N   GLU A 127      -7.202 -13.663 -41.735  1.00 57.73           N  
ANISOU  960  N   GLU A 127     9630   5864   6439     15   3192   -923       N  
ATOM    961  CA  GLU A 127      -7.395 -12.349 -42.318  1.00 57.35           C  
ANISOU  961  CA  GLU A 127     9595   5729   6469     63   3265   -984       C  
ATOM    962  C   GLU A 127      -8.201 -12.460 -43.623  1.00 59.51           C  
ANISOU  962  C   GLU A 127     9626   5996   6989    175   3270   -919       C  
ATOM    963  O   GLU A 127      -9.116 -11.689 -43.834  1.00 62.41           O  
ANISOU  963  O   GLU A 127     9967   6279   7466    258   3430   -928       O  
ATOM    964  CB  GLU A 127      -6.027 -11.701 -42.556  1.00 58.86           C  
ANISOU  964  CB  GLU A 127     9872   5933   6559    -26   3099  -1045       C  
ATOM    965  CG  GLU A 127      -6.069 -10.250 -42.999  1.00 76.03           C  
ANISOU  965  CG  GLU A 127    12099   8008   8782      3   3171  -1118       C  
ATOM    966  CD  GLU A 127      -4.741  -9.725 -43.521  1.00103.72           C  
ANISOU  966  CD  GLU A 127    15633  11539  12236    -75   2983  -1157       C  
ATOM    967  OE1 GLU A 127      -3.687 -10.270 -43.116  1.00102.20           O  
ANISOU  967  OE1 GLU A 127    15501  11426  11907   -177   2825  -1152       O  
ATOM    968  OE2 GLU A 127      -4.752  -8.764 -44.327  1.00 93.46           O  
ANISOU  968  OE2 GLU A 127    14293  10180  11038    -33   2994  -1184       O  
ATOM    969  N   GLN A 128      -7.870 -13.400 -44.494  1.00 54.40           N  
ANISOU  969  N   GLN A 128     8805   5435   6429    176   3099   -853       N  
ATOM    970  CA  GLN A 128      -8.605 -13.565 -45.764  1.00 51.93           C  
ANISOU  970  CA  GLN A 128     8268   5126   6338    268   3086   -791       C  
ATOM    971  C   GLN A 128     -10.021 -14.102 -45.522  1.00 54.82           C  
ANISOU  971  C   GLN A 128     8542   5472   6816    345   3246   -723       C  
ATOM    972  O   GLN A 128     -10.965 -13.735 -46.229  1.00 51.56           O  
ANISOU  972  O   GLN A 128     7997   5018   6575    432   3328   -686       O  
ATOM    973  CB  GLN A 128      -7.866 -14.510 -46.694  1.00 49.85           C  
ANISOU  973  CB  GLN A 128     7862   4958   6120    241   2868   -744       C  
ATOM    974  CG  GLN A 128      -8.491 -14.563 -48.082  1.00 51.37           C  
ANISOU  974  CG  GLN A 128     7843   5157   6519    318   2835   -691       C  
ATOM    975  CD  GLN A 128      -7.908 -15.596 -48.983  1.00 53.71           C  
ANISOU  975  CD  GLN A 128     8003   5540   6864    296   2644   -647       C  
ATOM    976  OE1 GLN A 128      -7.264 -16.562 -48.538  1.00 48.05           O  
ANISOU  976  OE1 GLN A 128     7315   4882   6060    238   2553   -633       O  
ATOM    977  NE2 GLN A 128      -8.246 -15.475 -50.263  1.00 46.00           N  
ANISOU  977  NE2 GLN A 128     6867   4571   6038    346   2594   -616       N  
ATOM    978  N   LEU A 129     -10.162 -14.957 -44.517  1.00 53.15           N  
ANISOU  978  N   LEU A 129     8396   5290   6508    310   3289   -700       N  
ATOM    979  CA  LEU A 129     -11.465 -15.501 -44.176  1.00 55.11           C  
ANISOU  979  CA  LEU A 129     8565   5521   6853    373   3445   -632       C  
ATOM    980  C   LEU A 129     -12.443 -14.447 -43.659  1.00 64.68           C  
ANISOU  980  C   LEU A 129     9852   6629   8096    442   3691   -660       C  
ATOM    981  O   LEU A 129     -13.631 -14.746 -43.662  1.00 67.88           O  
ANISOU  981  O   LEU A 129    10145   7012   8633    515   3823   -591       O  
ATOM    982  CB  LEU A 129     -11.337 -16.689 -43.216  1.00 55.26           C  
ANISOU  982  CB  LEU A 129     8640   5599   6759    315   3429   -594       C  
ATOM    983  CG  LEU A 129     -10.595 -17.909 -43.786  1.00 58.31           C  
ANISOU  983  CG  LEU A 129     8915   6079   7160    269   3210   -544       C  
ATOM    984  CD1 LEU A 129     -10.295 -18.920 -42.708  1.00 59.99           C  
ANISOU  984  CD1 LEU A 129     9217   6341   7236    202   3192   -513       C  
ATOM    985  CD2 LEU A 129     -11.380 -18.589 -44.867  1.00 56.51           C  
ANISOU  985  CD2 LEU A 129     8455   5872   7145    332   3175   -465       C  
ATOM    986  N   LYS A 130     -11.996 -13.217 -43.265  1.00 62.00           N  
ANISOU  986  N   LYS A 130     9690   6218   7651    422   3757   -756       N  
ATOM    987  CA  LYS A 130     -12.917 -12.124 -42.895  1.00 63.05           C  
ANISOU  987  CA  LYS A 130     9888   6233   7833    498   4000   -787       C  
ATOM    988  C   LYS A 130     -13.713 -11.684 -44.134  1.00 67.28           C  
ANISOU  988  C   LYS A 130    10213   6736   8616    604   4023   -728       C  
ATOM    989  O   LYS A 130     -14.895 -11.356 -44.011  1.00 69.83           O  
ANISOU  989  O   LYS A 130    10478   6991   9065    695   4220   -686       O  
ATOM    990  CB  LYS A 130     -12.187 -10.940 -42.261  1.00 66.25           C  
ANISOU  990  CB  LYS A 130    10536   6566   8071    444   4049   -908       C  
ATOM    991  CG  LYS A 130     -11.734 -11.223 -40.835  1.00 82.47           C  
ANISOU  991  CG  LYS A 130    12821   8634   9881    349   4092   -963       C  
ATOM    992  CD  LYS A 130     -10.976 -10.041 -40.245  1.00 94.93           C  
ANISOU  992  CD  LYS A 130    14646  10138  11286    280   4126  -1088       C  
ATOM    993  CE  LYS A 130     -10.491 -10.274 -38.834  1.00107.90           C  
ANISOU  993  CE  LYS A 130    16530  11797  12668    171   4156  -1143       C  
ATOM    994  NZ  LYS A 130     -11.578 -10.159 -37.823  1.00125.05           N  
ANISOU  994  NZ  LYS A 130    18808  13898  14806    220   4430  -1152       N  
ATOM    995  N   SER A 131     -13.084 -11.709 -45.332  1.00 60.59           N  
ANISOU  995  N   SER A 131     9243   5939   7840    591   3821   -714       N  
ATOM    996  CA  SER A 131     -13.800 -11.539 -46.600  1.00 59.29           C  
ANISOU  996  CA  SER A 131     8856   5769   7903    676   3801   -639       C  
ATOM    997  C   SER A 131     -14.475 -12.919 -46.846  1.00 64.24           C  
ANISOU  997  C   SER A 131     9303   6474   8630    691   3756   -535       C  
ATOM    998  O   SER A 131     -14.347 -13.836 -46.018  1.00 65.75           O  
ANISOU  998  O   SER A 131     9558   6709   8714    641   3755   -529       O  
ATOM    999  CB  SER A 131     -12.861 -11.164 -47.743  1.00 62.46           C  
ANISOU  999  CB  SER A 131     9203   6204   8325    648   3603   -661       C  
ATOM   1000  OG  SER A 131     -12.169 -12.262 -48.351  1.00 72.41           O  
ANISOU 1000  OG  SER A 131    10369   7575   9569    590   3384   -631       O  
ATOM   1001  N   GLY A 132     -15.192 -13.084 -47.946  1.00 57.94           N  
ANISOU 1001  N   GLY A 132     8288   5694   8032    751   3716   -449       N  
ATOM   1002  CA  GLY A 132     -15.897 -14.353 -48.166  1.00 55.87           C  
ANISOU 1002  CA  GLY A 132     7861   5497   7869    758   3680   -352       C  
ATOM   1003  C   GLY A 132     -15.214 -15.364 -49.051  1.00 57.87           C  
ANISOU 1003  C   GLY A 132     8009   5849   8128    699   3440   -329       C  
ATOM   1004  O   GLY A 132     -15.906 -16.193 -49.646  1.00 58.16           O  
ANISOU 1004  O   GLY A 132     7870   5928   8300    716   3395   -243       O  
ATOM   1005  N   THR A 133     -13.871 -15.329 -49.143  1.00 53.86           N  
ANISOU 1005  N   THR A 133     7607   5378   7480    628   3289   -403       N  
ATOM   1006  CA  THR A 133     -13.074 -16.243 -49.994  1.00 51.41           C  
ANISOU 1006  CA  THR A 133     7212   5156   7166    574   3066   -392       C  
ATOM   1007  C   THR A 133     -11.974 -16.914 -49.191  1.00 51.35           C  
ANISOU 1007  C   THR A 133     7343   5193   6976    490   2981   -438       C  
ATOM   1008  O   THR A 133     -11.501 -16.372 -48.192  1.00 52.69           O  
ANISOU 1008  O   THR A 133     7692   5329   6997    458   3049   -500       O  
ATOM   1009  CB  THR A 133     -12.477 -15.469 -51.180  1.00 60.22           C  
ANISOU 1009  CB  THR A 133     8280   6276   8323    579   2948   -419       C  
ATOM   1010  OG1 THR A 133     -13.547 -14.885 -51.901  1.00 67.27           O  
ANISOU 1010  OG1 THR A 133     9038   7132   9391    656   3025   -361       O  
ATOM   1011  CG2 THR A 133     -11.686 -16.348 -52.147  1.00 60.65           C  
ANISOU 1011  CG2 THR A 133     8246   6416   8382    530   2734   -409       C  
ATOM   1012  N   ALA A 134     -11.630 -18.125 -49.595  1.00 44.94           N  
ANISOU 1012  N   ALA A 134     6446   4452   6178    452   2838   -401       N  
ATOM   1013  CA  ALA A 134     -10.554 -18.906 -49.019  1.00 44.19           C  
ANISOU 1013  CA  ALA A 134     6446   4406   5937    376   2732   -424       C  
ATOM   1014  C   ALA A 134      -9.578 -19.326 -50.125  1.00 46.34           C  
ANISOU 1014  C   ALA A 134     6642   4737   6229    345   2529   -431       C  
ATOM   1015  O   ALA A 134      -9.972 -20.030 -51.060  1.00 46.43           O  
ANISOU 1015  O   ALA A 134     6499   4777   6364    362   2460   -383       O  
ATOM   1016  CB  ALA A 134     -11.124 -20.130 -48.347  1.00 45.40           C  
ANISOU 1016  CB  ALA A 134     6571   4581   6098    365   2773   -362       C  
ATOM   1017  N   SER A 135      -8.292 -18.940 -50.000  1.00 42.14           N  
ANISOU 1017  N   SER A 135     6217   4222   5571    292   2434   -489       N  
ATOM   1018  CA  SER A 135      -7.242 -19.358 -50.942  1.00 40.15           C  
ANISOU 1018  CA  SER A 135     5904   4026   5324    261   2251   -495       C  
ATOM   1019  C   SER A 135      -6.323 -20.350 -50.252  1.00 41.72           C  
ANISOU 1019  C   SER A 135     6168   4272   5412    197   2163   -485       C  
ATOM   1020  O   SER A 135      -5.741 -20.042 -49.212  1.00 41.38           O  
ANISOU 1020  O   SER A 135     6273   4224   5226    150   2183   -514       O  
ATOM   1021  CB  SER A 135      -6.441 -18.174 -51.478  1.00 40.88           C  
ANISOU 1021  CB  SER A 135     6043   4107   5382    252   2198   -553       C  
ATOM   1022  OG  SER A 135      -7.307 -17.274 -52.151  1.00 43.93           O  
ANISOU 1022  OG  SER A 135     6360   4448   5881    315   2277   -551       O  
ATOM   1023  N   VAL A 136      -6.199 -21.539 -50.848  1.00 37.28           N  
ANISOU 1023  N   VAL A 136     5495   3752   4919    193   2064   -442       N  
ATOM   1024  CA  VAL A 136      -5.331 -22.599 -50.372  1.00 35.52           C  
ANISOU 1024  CA  VAL A 136     5302   3570   4624    142   1970   -417       C  
ATOM   1025  C   VAL A 136      -4.188 -22.632 -51.363  1.00 39.16           C  
ANISOU 1025  C   VAL A 136     5715   4068   5095    126   1819   -437       C  
ATOM   1026  O   VAL A 136      -4.430 -22.637 -52.568  1.00 38.37           O  
ANISOU 1026  O   VAL A 136     5503   3972   5105    159   1779   -440       O  
ATOM   1027  CB  VAL A 136      -6.044 -23.965 -50.305  1.00 37.11           C  
ANISOU 1027  CB  VAL A 136     5414   3779   4906    153   1983   -352       C  
ATOM   1028  CG1 VAL A 136      -5.196 -24.972 -49.537  1.00 37.71           C  
ANISOU 1028  CG1 VAL A 136     5546   3887   4895    102   1912   -318       C  
ATOM   1029  CG2 VAL A 136      -7.434 -23.848 -49.700  1.00 35.63           C  
ANISOU 1029  CG2 VAL A 136     5223   3552   4761    187   2145   -324       C  
ATOM   1030  N   VAL A 137      -2.948 -22.632 -50.881  1.00 36.51           N  
ANISOU 1030  N   VAL A 137     5464   3760   4646     73   1735   -448       N  
ATOM   1031  CA  VAL A 137      -1.802 -22.564 -51.779  1.00 35.57           C  
ANISOU 1031  CA  VAL A 137     5303   3675   4536     59   1602   -464       C  
ATOM   1032  C   VAL A 137      -0.882 -23.785 -51.638  1.00 38.90           C  
ANISOU 1032  C   VAL A 137     5702   4138   4941     28   1496   -419       C  
ATOM   1033  O   VAL A 137      -0.657 -24.289 -50.546  1.00 36.62           O  
ANISOU 1033  O   VAL A 137     5485   3859   4569     -9   1501   -385       O  
ATOM   1034  CB  VAL A 137      -1.083 -21.200 -51.560  1.00 38.87           C  
ANISOU 1034  CB  VAL A 137     5825   4085   4857     28   1593   -518       C  
ATOM   1035  CG1 VAL A 137       0.164 -21.070 -52.411  1.00 38.06           C  
ANISOU 1035  CG1 VAL A 137     5682   4020   4758      9   1460   -528       C  
ATOM   1036  CG2 VAL A 137      -2.047 -20.037 -51.841  1.00 38.23           C  
ANISOU 1036  CG2 VAL A 137     5753   3953   4821     71   1705   -557       C  
ATOM   1037  N   CYS A 138      -0.386 -24.263 -52.768  1.00 37.53           N  
ANISOU 1037  N   CYS A 138     5427   3986   4849     45   1406   -415       N  
ATOM   1038  CA  CYS A 138       0.576 -25.337 -52.814  1.00 40.19           C  
ANISOU 1038  CA  CYS A 138     5731   4352   5188     26   1308   -374       C  
ATOM   1039  C   CYS A 138       1.810 -24.870 -53.534  1.00 42.20           C  
ANISOU 1039  C   CYS A 138     5968   4635   5430     14   1209   -395       C  
ATOM   1040  O   CYS A 138       1.678 -24.406 -54.656  1.00 41.95           O  
ANISOU 1040  O   CYS A 138     5874   4601   5463     43   1201   -431       O  
ATOM   1041  CB  CYS A 138       0.004 -26.566 -53.503  1.00 41.95           C  
ANISOU 1041  CB  CYS A 138     5844   4563   5531     59   1305   -347       C  
ATOM   1042  SG  CYS A 138       1.062 -28.015 -53.336  1.00 46.74           S  
ANISOU 1042  SG  CYS A 138     6420   5189   6150     42   1212   -287       S  
ATOM   1043  N   LEU A 139       3.006 -25.071 -52.937  1.00 36.74           N  
ANISOU 1043  N   LEU A 139     5321   3975   4663    -30   1131   -363       N  
ATOM   1044  CA  LEU A 139       4.302 -24.722 -53.531  1.00 34.58           C  
ANISOU 1044  CA  LEU A 139     5024   3733   4382    -46   1032   -367       C  
ATOM   1045  C   LEU A 139       5.086 -25.969 -53.894  1.00 38.82           C  
ANISOU 1045  C   LEU A 139     5479   4289   4980    -34    957   -313       C  
ATOM   1046  O   LEU A 139       5.243 -26.854 -53.059  1.00 37.85           O  
ANISOU 1046  O   LEU A 139     5374   4170   4838    -51    945   -255       O  
ATOM   1047  CB  LEU A 139       5.119 -23.861 -52.540  1.00 34.42           C  
ANISOU 1047  CB  LEU A 139     5116   3733   4227   -113    995   -365       C  
ATOM   1048  CG  LEU A 139       6.581 -23.538 -52.889  1.00 38.26           C  
ANISOU 1048  CG  LEU A 139     5584   4259   4694   -146    884   -350       C  
ATOM   1049  CD1 LEU A 139       6.671 -22.729 -54.205  1.00 38.40           C  
ANISOU 1049  CD1 LEU A 139     5544   4272   4776   -114    879   -403       C  
ATOM   1050  CD2 LEU A 139       7.236 -22.798 -51.737  1.00 39.71           C  
ANISOU 1050  CD2 LEU A 139     5890   4461   4738   -227    847   -341       C  
ATOM   1051  N   LEU A 140       5.592 -26.023 -55.149  1.00 35.43           N  
ANISOU 1051  N   LEU A 140     4965   3869   4628     -4    913   -331       N  
ATOM   1052  CA  LEU A 140       6.480 -27.081 -55.670  1.00 33.73           C  
ANISOU 1052  CA  LEU A 140     4672   3665   4480     14    850   -289       C  
ATOM   1053  C   LEU A 140       7.776 -26.337 -55.905  1.00 36.79           C  
ANISOU 1053  C   LEU A 140     5059   4090   4831    -11    775   -284       C  
ATOM   1054  O   LEU A 140       7.855 -25.517 -56.807  1.00 35.91           O  
ANISOU 1054  O   LEU A 140     4926   3984   4734      1    774   -332       O  
ATOM   1055  CB  LEU A 140       5.964 -27.679 -57.008  1.00 33.05           C  
ANISOU 1055  CB  LEU A 140     4495   3555   4507     67    873   -323       C  
ATOM   1056  CG  LEU A 140       4.757 -28.636 -56.955  1.00 36.86           C  
ANISOU 1056  CG  LEU A 140     4955   4000   5052     88    933   -320       C  
ATOM   1057  CD1 LEU A 140       3.488 -27.970 -56.281  1.00 35.53           C  
ANISOU 1057  CD1 LEU A 140     4843   3816   4841     78   1011   -340       C  
ATOM   1058  CD2 LEU A 140       4.367 -29.073 -58.341  1.00 38.93           C  
ANISOU 1058  CD2 LEU A 140     5140   4244   5408    123    940   -361       C  
ATOM   1059  N   ASN A 141       8.765 -26.549 -55.052  1.00 34.64           N  
ANISOU 1059  N   ASN A 141     4812   3845   4505    -51    711   -219       N  
ATOM   1060  CA  ASN A 141      10.007 -25.786 -55.106  1.00 33.48           C  
ANISOU 1060  CA  ASN A 141     4668   3737   4316    -89    633   -203       C  
ATOM   1061  C   ASN A 141      11.222 -26.473 -55.688  1.00 36.25           C  
ANISOU 1061  C   ASN A 141     4923   4109   4741    -68    566   -146       C  
ATOM   1062  O   ASN A 141      11.559 -27.544 -55.249  1.00 36.40           O  
ANISOU 1062  O   ASN A 141     4911   4127   4792    -59    544    -76       O  
ATOM   1063  CB  ASN A 141      10.350 -25.324 -53.690  1.00 36.08           C  
ANISOU 1063  CB  ASN A 141     5100   4089   4520   -165    595   -167       C  
ATOM   1064  CG  ASN A 141      11.109 -24.032 -53.666  1.00 43.56           C  
ANISOU 1064  CG  ASN A 141     6093   5062   5397   -221    542   -187       C  
ATOM   1065  OD1 ASN A 141      10.764 -23.084 -54.351  1.00 41.85           O  
ANISOU 1065  OD1 ASN A 141     5885   4830   5187   -208    578   -257       O  
ATOM   1066  ND2 ASN A 141      12.150 -23.966 -52.895  1.00 49.28           N  
ANISOU 1066  ND2 ASN A 141     6845   5825   6056   -286    454   -123       N  
ATOM   1067  N   ASN A 142      11.934 -25.792 -56.619  1.00 34.41           N  
ANISOU 1067  N   ASN A 142     4645   3896   4533    -61    536   -168       N  
ATOM   1068  CA  ASN A 142      13.218 -26.189 -57.186  1.00 34.22           C  
ANISOU 1068  CA  ASN A 142     4532   3897   4574    -45    478   -113       C  
ATOM   1069  C   ASN A 142      13.261 -27.589 -57.771  1.00 37.76           C  
ANISOU 1069  C   ASN A 142     4896   4317   5132     22    504    -86       C  
ATOM   1070  O   ASN A 142      14.002 -28.455 -57.307  1.00 38.67           O  
ANISOU 1070  O   ASN A 142     4971   4438   5283     25    466     -1       O  
ATOM   1071  CB  ASN A 142      14.329 -25.997 -56.135  1.00 32.56           C  
ANISOU 1071  CB  ASN A 142     4341   3729   4300   -111    385    -26       C  
ATOM   1072  CG  ASN A 142      14.503 -24.560 -55.716  1.00 39.27           C  
ANISOU 1072  CG  ASN A 142     5273   4602   5045   -184    351    -57       C  
ATOM   1073  OD1 ASN A 142      14.097 -23.622 -56.394  1.00 38.53           O  
ANISOU 1073  OD1 ASN A 142     5198   4497   4943   -177    387   -134       O  
ATOM   1074  ND2 ASN A 142      15.064 -24.369 -54.579  1.00 38.72           N  
ANISOU 1074  ND2 ASN A 142     5259   4563   4891   -259    281      2       N  
ATOM   1075  N   PHE A 143      12.571 -27.751 -58.873  1.00 33.66           N  
ANISOU 1075  N   PHE A 143     4348   3770   4672     71    565   -156       N  
ATOM   1076  CA  PHE A 143      12.468 -29.041 -59.577  1.00 32.59           C  
ANISOU 1076  CA  PHE A 143     4147   3596   4639    131    603   -154       C  
ATOM   1077  C   PHE A 143      12.881 -28.919 -61.068  1.00 36.51           C  
ANISOU 1077  C   PHE A 143     4582   4094   5196    172    621   -200       C  
ATOM   1078  O   PHE A 143      12.888 -27.829 -61.644  1.00 35.79           O  
ANISOU 1078  O   PHE A 143     4501   4030   5068    159    616   -245       O  
ATOM   1079  CB  PHE A 143      11.009 -29.595 -59.441  1.00 33.10           C  
ANISOU 1079  CB  PHE A 143     4246   3616   4714    143    666   -198       C  
ATOM   1080  CG  PHE A 143       9.914 -28.775 -60.070  1.00 32.60           C  
ANISOU 1080  CG  PHE A 143     4211   3549   4628    142    710   -284       C  
ATOM   1081  CD1 PHE A 143       9.623 -28.898 -61.415  1.00 35.25           C  
ANISOU 1081  CD1 PHE A 143     4504   3871   5020    177    738   -342       C  
ATOM   1082  CD2 PHE A 143       9.186 -27.862 -59.323  1.00 32.83           C  
ANISOU 1082  CD2 PHE A 143     4310   3585   4578    106    724   -303       C  
ATOM   1083  CE1 PHE A 143       8.652 -28.111 -62.008  1.00 33.89           C  
ANISOU 1083  CE1 PHE A 143     4347   3700   4828    174    768   -407       C  
ATOM   1084  CE2 PHE A 143       8.216 -27.073 -59.922  1.00 33.79           C  
ANISOU 1084  CE2 PHE A 143     4446   3701   4692    112    766   -371       C  
ATOM   1085  CZ  PHE A 143       7.957 -27.198 -61.258  1.00 30.98           C  
ANISOU 1085  CZ  PHE A 143     4037   3338   4396    145    782   -417       C  
ATOM   1086  N   TYR A 144      13.216 -30.049 -61.661  1.00 33.84           N  
ANISOU 1086  N   TYR A 144     4187   3725   4948    222    647   -186       N  
ATOM   1087  CA  TYR A 144      13.604 -30.146 -63.061  1.00 33.99           C  
ANISOU 1087  CA  TYR A 144     4156   3738   5022    263    677   -229       C  
ATOM   1088  C   TYR A 144      13.300 -31.537 -63.512  1.00 35.93           C  
ANISOU 1088  C   TYR A 144     4378   3922   5352    309    730   -242       C  
ATOM   1089  O   TYR A 144      13.644 -32.463 -62.794  1.00 36.42           O  
ANISOU 1089  O   TYR A 144     4422   3956   5460    322    724   -173       O  
ATOM   1090  CB  TYR A 144      15.100 -29.865 -63.268  1.00 36.05           C  
ANISOU 1090  CB  TYR A 144     4357   4034   5307    272    641   -169       C  
ATOM   1091  CG  TYR A 144      15.464 -29.799 -64.731  1.00 36.08           C  
ANISOU 1091  CG  TYR A 144     4319   4038   5353    312    683   -219       C  
ATOM   1092  CD1 TYR A 144      15.317 -28.620 -65.447  1.00 37.09           C  
ANISOU 1092  CD1 TYR A 144     4462   4202   5427    292    680   -273       C  
ATOM   1093  CD2 TYR A 144      15.803 -30.947 -65.437  1.00 36.88           C  
ANISOU 1093  CD2 TYR A 144     4377   4094   5543    369    737   -220       C  
ATOM   1094  CE1 TYR A 144      15.546 -28.572 -66.820  1.00 36.89           C  
ANISOU 1094  CE1 TYR A 144     4408   4179   5429    324    722   -322       C  
ATOM   1095  CE2 TYR A 144      15.977 -30.923 -66.821  1.00 37.15           C  
ANISOU 1095  CE2 TYR A 144     4391   4123   5599    401    788   -281       C  
ATOM   1096  CZ  TYR A 144      15.878 -29.726 -67.504  1.00 41.13           C  
ANISOU 1096  CZ  TYR A 144     4909   4674   6042    377    777   -328       C  
ATOM   1097  OH  TYR A 144      16.059 -29.658 -68.865  1.00 39.57           O  
ANISOU 1097  OH  TYR A 144     4699   4480   5856    404    825   -383       O  
ATOM   1098  N   PRO A 145      12.678 -31.769 -64.661  1.00 33.48           N  
ANISOU 1098  N   PRO A 145     4069   3584   5066    331    779   -323       N  
ATOM   1099  CA  PRO A 145      12.230 -30.833 -65.704  1.00 33.80           C  
ANISOU 1099  CA  PRO A 145     4123   3653   5064    320    789   -401       C  
ATOM   1100  C   PRO A 145      10.946 -30.068 -65.351  1.00 37.74           C  
ANISOU 1100  C   PRO A 145     4674   4165   5502    282    783   -440       C  
ATOM   1101  O   PRO A 145      10.410 -30.227 -64.276  1.00 35.67           O  
ANISOU 1101  O   PRO A 145     4440   3890   5221    262    777   -411       O  
ATOM   1102  CB  PRO A 145      12.117 -31.752 -66.935  1.00 34.92           C  
ANISOU 1102  CB  PRO A 145     4251   3752   5266    356    843   -458       C  
ATOM   1103  CG  PRO A 145      11.672 -33.039 -66.367  1.00 39.08           C  
ANISOU 1103  CG  PRO A 145     4785   4216   5849    367    866   -440       C  
ATOM   1104  CD  PRO A 145      12.429 -33.169 -65.066  1.00 35.45           C  
ANISOU 1104  CD  PRO A 145     4307   3765   5397    367    829   -340       C  
ATOM   1105  N   ARG A 146      10.491 -29.203 -66.253  1.00 36.79           N  
ANISOU 1105  N   ARG A 146     4561   4069   5349    273    789   -498       N  
ATOM   1106  CA  ARG A 146       9.338 -28.328 -66.035  1.00 38.05           C  
ANISOU 1106  CA  ARG A 146     4757   4240   5460    244    789   -528       C  
ATOM   1107  C   ARG A 146       8.006 -29.030 -65.762  1.00 39.11           C  
ANISOU 1107  C   ARG A 146     4907   4334   5617    238    818   -547       C  
ATOM   1108  O   ARG A 146       7.205 -28.516 -64.971  1.00 36.01           O  
ANISOU 1108  O   ARG A 146     4546   3943   5194    217    824   -539       O  
ATOM   1109  CB  ARG A 146       9.151 -27.347 -67.223  1.00 38.22           C  
ANISOU 1109  CB  ARG A 146     4771   4293   5456    240    789   -577       C  
ATOM   1110  CG  ARG A 146       8.343 -26.099 -66.882  1.00 45.74           C  
ANISOU 1110  CG  ARG A 146     5755   5264   6360    215    784   -586       C  
ATOM   1111  CD  ARG A 146       8.415 -25.097 -68.027  1.00 57.19           C  
ANISOU 1111  CD  ARG A 146     7191   6748   7790    213    776   -616       C  
ATOM   1112  NE  ARG A 146       7.796 -23.791 -67.738  1.00 64.82           N  
ANISOU 1112  NE  ARG A 146     8184   7726   8719    194    775   -618       N  
ATOM   1113  CZ  ARG A 146       6.514 -23.462 -67.893  1.00 73.64           C  
ANISOU 1113  CZ  ARG A 146     9305   8831   9842    191    796   -637       C  
ATOM   1114  NH1 ARG A 146       5.624 -24.370 -68.282  1.00 59.93           N  
ANISOU 1114  NH1 ARG A 146     7550   7077   8145    196    812   -655       N  
ATOM   1115  NH2 ARG A 146       6.103 -22.227 -67.624  1.00 77.67           N  
ANISOU 1115  NH2 ARG A 146     9839   9345  10327    181    804   -634       N  
ATOM   1116  N   GLU A 147       7.765 -30.157 -66.450  1.00 35.37           N  
ANISOU 1116  N   GLU A 147     4416   3823   5201    254    841   -574       N  
ATOM   1117  CA  GLU A 147       6.514 -30.886 -66.368  1.00 34.79           C  
ANISOU 1117  CA  GLU A 147     4350   3709   5159    242    864   -593       C  
ATOM   1118  C   GLU A 147       6.206 -31.329 -64.919  1.00 41.33           C  
ANISOU 1118  C   GLU A 147     5198   4514   5992    234    872   -538       C  
ATOM   1119  O   GLU A 147       6.996 -31.997 -64.282  1.00 42.25           O  
ANISOU 1119  O   GLU A 147     5311   4613   6128    247    866   -490       O  
ATOM   1120  CB  GLU A 147       6.523 -32.103 -67.315  1.00 35.83           C  
ANISOU 1120  CB  GLU A 147     4469   3797   5349    254    885   -631       C  
ATOM   1121  N   ALA A 148       5.094 -30.907 -64.398  1.00 39.24           N  
ANISOU 1121  N   ALA A 148     4950   4250   5708    213    886   -537       N  
ATOM   1122  CA  ALA A 148       4.659 -31.264 -63.067  1.00 38.44           C  
ANISOU 1122  CA  ALA A 148     4874   4129   5602    203    903   -489       C  
ATOM   1123  C   ALA A 148       3.158 -31.157 -63.066  1.00 43.36           C  
ANISOU 1123  C   ALA A 148     5495   4738   6240    187    937   -506       C  
ATOM   1124  O   ALA A 148       2.607 -30.327 -63.786  1.00 43.03           O  
ANISOU 1124  O   ALA A 148     5441   4719   6189    182    937   -542       O  
ATOM   1125  CB  ALA A 148       5.269 -30.315 -62.037  1.00 38.25           C  
ANISOU 1125  CB  ALA A 148     4889   4141   5503    191    887   -451       C  
ATOM   1126  N   LYS A 149       2.492 -32.014 -62.287  1.00 39.48           N  
ANISOU 1126  N   LYS A 149     5009   4210   5781    179    964   -474       N  
ATOM   1127  CA  LYS A 149       1.049 -31.993 -62.169  1.00 37.39           C  
ANISOU 1127  CA  LYS A 149     4733   3931   5543    163   1001   -476       C  
ATOM   1128  C   LYS A 149       0.715 -31.833 -60.713  1.00 39.36           C  
ANISOU 1128  C   LYS A 149     5022   4178   5756    156   1038   -425       C  
ATOM   1129  O   LYS A 149       1.338 -32.462 -59.854  1.00 36.51           O  
ANISOU 1129  O   LYS A 149     4685   3804   5381    155   1033   -380       O  
ATOM   1130  CB  LYS A 149       0.427 -33.284 -62.705  1.00 38.95           C  
ANISOU 1130  CB  LYS A 149     4897   4080   5823    152   1006   -486       C  
ATOM   1131  CG  LYS A 149      -1.102 -33.257 -62.793  1.00 56.97           C  
ANISOU 1131  CG  LYS A 149     7149   6351   8145    130   1034   -485       C  
ATOM   1132  CD  LYS A 149      -1.681 -34.518 -63.480  1.00 70.86           C  
ANISOU 1132  CD  LYS A 149     8877   8062   9985    105   1026   -501       C  
ATOM   1133  CE  LYS A 149      -1.765 -35.729 -62.571  1.00 81.77           C  
ANISOU 1133  CE  LYS A 149    10268   9390  11410    100   1051   -455       C  
ATOM   1134  NZ  LYS A 149      -2.313 -36.935 -63.267  1.00 95.04           N  
ANISOU 1134  NZ  LYS A 149    11925  11015  13172     70   1043   -477       N  
ATOM   1135  N   VAL A 150      -0.271 -30.993 -60.446  1.00 37.55           N  
ANISOU 1135  N   VAL A 150     4797   3959   5510    151   1079   -427       N  
ATOM   1136  CA  VAL A 150      -0.867 -30.778 -59.133  1.00 37.46           C  
ANISOU 1136  CA  VAL A 150     4828   3941   5464    144   1136   -386       C  
ATOM   1137  C   VAL A 150      -2.315 -31.197 -59.232  1.00 40.49           C  
ANISOU 1137  C   VAL A 150     5166   4298   5921    139   1184   -374       C  
ATOM   1138  O   VAL A 150      -3.027 -30.817 -60.178  1.00 38.47           O  
ANISOU 1138  O   VAL A 150     4860   4048   5711    140   1182   -401       O  
ATOM   1139  CB  VAL A 150      -0.809 -29.313 -58.664  1.00 39.47           C  
ANISOU 1139  CB  VAL A 150     5134   4223   5639    146   1161   -399       C  
ATOM   1140  CG1 VAL A 150      -1.411 -29.152 -57.277  1.00 39.22           C  
ANISOU 1140  CG1 VAL A 150     5160   4179   5562    137   1233   -362       C  
ATOM   1141  CG2 VAL A 150       0.600 -28.831 -58.652  1.00 39.48           C  
ANISOU 1141  CG2 VAL A 150     5173   4254   5574    142   1105   -409       C  
ATOM   1142  N   GLN A 151      -2.759 -31.937 -58.231  1.00 37.80           N  
ANISOU 1142  N   GLN A 151     4841   3932   5591    129   1226   -326       N  
ATOM   1143  CA  GLN A 151      -4.172 -32.287 -58.070  1.00 37.20           C  
ANISOU 1143  CA  GLN A 151     4722   3830   5582    121   1284   -299       C  
ATOM   1144  C   GLN A 151      -4.616 -31.863 -56.696  1.00 38.16           C  
ANISOU 1144  C   GLN A 151     4898   3952   5648    123   1364   -258       C  
ATOM   1145  O   GLN A 151      -3.913 -32.103 -55.724  1.00 36.30           O  
ANISOU 1145  O   GLN A 151     4728   3720   5346    116   1365   -230       O  
ATOM   1146  CB  GLN A 151      -4.388 -33.760 -58.262  1.00 38.50           C  
ANISOU 1146  CB  GLN A 151     4849   3955   5826    104   1266   -277       C  
ATOM   1147  CG  GLN A 151      -4.292 -34.146 -59.707  1.00 46.94           C  
ANISOU 1147  CG  GLN A 151     5866   5015   6953     95   1205   -326       C  
ATOM   1148  CD  GLN A 151      -4.519 -35.628 -59.838  1.00 61.94           C  
ANISOU 1148  CD  GLN A 151     7741   6862   8932     73   1194   -310       C  
ATOM   1149  OE1 GLN A 151      -5.532 -36.049 -60.412  1.00 55.35           O  
ANISOU 1149  OE1 GLN A 151     6853   6007   8171     46   1195   -312       O  
ATOM   1150  NE2 GLN A 151      -3.582 -36.442 -59.287  1.00 44.12           N  
ANISOU 1150  NE2 GLN A 151     5520   4580   6663     80   1182   -286       N  
ATOM   1151  N   TRP A 152      -5.763 -31.175 -56.625  1.00 36.35           N  
ANISOU 1151  N   TRP A 152     4644   3721   5446    133   1434   -251       N  
ATOM   1152  CA  TRP A 152      -6.354 -30.705 -55.379  1.00 35.02           C  
ANISOU 1152  CA  TRP A 152     4529   3547   5231    139   1533   -217       C  
ATOM   1153  C   TRP A 152      -7.475 -31.651 -54.987  1.00 36.94           C  
ANISOU 1153  C   TRP A 152     4722   3760   5554    129   1590   -160       C  
ATOM   1154  O   TRP A 152      -8.303 -32.024 -55.823  1.00 34.21           O  
ANISOU 1154  O   TRP A 152     4283   3401   5312    124   1579   -154       O  
ATOM   1155  CB  TRP A 152      -6.892 -29.268 -55.535  1.00 34.24           C  
ANISOU 1155  CB  TRP A 152     4434   3456   5120    164   1591   -243       C  
ATOM   1156  CG  TRP A 152      -5.835 -28.210 -55.481  1.00 34.82           C  
ANISOU 1156  CG  TRP A 152     4584   3552   5093    169   1561   -289       C  
ATOM   1157  CD1 TRP A 152      -5.324 -27.508 -56.528  1.00 36.13           C  
ANISOU 1157  CD1 TRP A 152     4727   3737   5263    178   1499   -334       C  
ATOM   1158  CD2 TRP A 152      -5.163 -27.725 -54.309  1.00 35.72           C  
ANISOU 1158  CD2 TRP A 152     4815   3672   5086    156   1590   -292       C  
ATOM   1159  NE1 TRP A 152      -4.423 -26.574 -56.077  1.00 34.17           N  
ANISOU 1159  NE1 TRP A 152     4567   3502   4912    173   1492   -364       N  
ATOM   1160  CE2 TRP A 152      -4.279 -26.706 -54.725  1.00 37.14           C  
ANISOU 1160  CE2 TRP A 152     5033   3871   5207    156   1542   -341       C  
ATOM   1161  CE3 TRP A 152      -5.230 -28.043 -52.940  1.00 38.04           C  
ANISOU 1161  CE3 TRP A 152     5189   3958   5307    138   1651   -256       C  
ATOM   1162  CZ2 TRP A 152      -3.495 -25.983 -53.821  1.00 37.26           C  
ANISOU 1162  CZ2 TRP A 152     5163   3895   5099    135   1548   -357       C  
ATOM   1163  CZ3 TRP A 152      -4.390 -27.378 -52.068  1.00 39.15           C  
ANISOU 1163  CZ3 TRP A 152     5448   4113   5316    115   1651   -273       C  
ATOM   1164  CH2 TRP A 152      -3.580 -26.324 -52.503  1.00 38.73           C  
ANISOU 1164  CH2 TRP A 152     5429   4075   5210    112   1601   -325       C  
ATOM   1165  N   LYS A 153      -7.508 -32.038 -53.712  1.00 36.37           N  
ANISOU 1165  N   LYS A 153     4711   3678   5430    120   1649   -114       N  
ATOM   1166  CA  LYS A 153      -8.599 -32.873 -53.144  1.00 36.02           C  
ANISOU 1166  CA  LYS A 153     4627   3606   5454    110   1721    -50       C  
ATOM   1167  C   LYS A 153      -9.104 -32.219 -51.890  1.00 40.85           C  
ANISOU 1167  C   LYS A 153     5309   4218   5993    120   1842    -22       C  
ATOM   1168  O   LYS A 153      -8.320 -31.695 -51.097  1.00 42.69           O  
ANISOU 1168  O   LYS A 153     5650   4469   6101    116   1850    -37       O  
ATOM   1169  CB  LYS A 153      -8.179 -34.346 -52.853  1.00 36.31           C  
ANISOU 1169  CB  LYS A 153     4662   3620   5514     82   1675     -7       C  
ATOM   1170  CG  LYS A 153      -7.885 -35.202 -54.076  1.00 36.68           C  
ANISOU 1170  CG  LYS A 153     4639   3648   5651     70   1578    -33       C  
ATOM   1171  CD  LYS A 153      -6.389 -35.303 -54.472  1.00 43.25           C  
ANISOU 1171  CD  LYS A 153     5511   4493   6430     73   1484    -73       C  
ATOM   1172  CE  LYS A 153      -5.766 -36.700 -54.366  1.00 59.80           C  
ANISOU 1172  CE  LYS A 153     7605   6553   8561     58   1437    -40       C  
ATOM   1173  NZ  LYS A 153      -5.560 -37.340 -55.709  1.00 71.60           N  
ANISOU 1173  NZ  LYS A 153     9042   8020  10142     53   1367    -86       N  
ATOM   1174  N   VAL A 154     -10.419 -32.140 -51.764  1.00 39.10           N  
ANISOU 1174  N   VAL A 154     5028   3979   5850    133   1937     16       N  
ATOM   1175  CA  VAL A 154     -11.093 -31.539 -50.614  1.00 39.29           C  
ANISOU 1175  CA  VAL A 154     5111   3995   5822    150   2078     45       C  
ATOM   1176  C   VAL A 154     -11.965 -32.656 -50.106  1.00 45.30           C  
ANISOU 1176  C   VAL A 154     5820   4734   6657    133   2134    124       C  
ATOM   1177  O   VAL A 154     -12.897 -33.028 -50.797  1.00 44.88           O  
ANISOU 1177  O   VAL A 154     5649   4666   6739    134   2135    153       O  
ATOM   1178  CB  VAL A 154     -11.911 -30.280 -50.979  1.00 41.87           C  
ANISOU 1178  CB  VAL A 154     5402   4317   6191    191   2159     24       C  
ATOM   1179  CG1 VAL A 154     -12.718 -29.777 -49.763  1.00 43.06           C  
ANISOU 1179  CG1 VAL A 154     5611   4448   6302    213   2329     58       C  
ATOM   1180  CG2 VAL A 154     -11.009 -29.177 -51.510  1.00 41.20           C  
ANISOU 1180  CG2 VAL A 154     5369   4250   6035    204   2100    -52       C  
ATOM   1181  N   ASP A 155     -11.621 -33.237 -48.944  1.00 42.65           N  
ANISOU 1181  N   ASP A 155     5570   4398   6237    111   2166    164       N  
ATOM   1182  CA  ASP A 155     -12.285 -34.401 -48.364  1.00 41.38           C  
ANISOU 1182  CA  ASP A 155     5373   4215   6134     90   2212    247       C  
ATOM   1183  C   ASP A 155     -12.346 -35.509 -49.379  1.00 41.96           C  
ANISOU 1183  C   ASP A 155     5337   4267   6338     67   2108    259       C  
ATOM   1184  O   ASP A 155     -13.402 -36.095 -49.570  1.00 42.18           O  
ANISOU 1184  O   ASP A 155     5270   4271   6487     58   2145    309       O  
ATOM   1185  CB  ASP A 155     -13.686 -34.078 -47.836  1.00 43.53           C  
ANISOU 1185  CB  ASP A 155     5605   4471   6461    111   2368    297       C  
ATOM   1186  CG  ASP A 155     -13.687 -33.403 -46.489  1.00 47.14           C  
ANISOU 1186  CG  ASP A 155     6194   4937   6780    122   2496    304       C  
ATOM   1187  OD1 ASP A 155     -12.656 -33.492 -45.778  1.00 44.39           O  
ANISOU 1187  OD1 ASP A 155     5967   4608   6290     96   2456    292       O  
ATOM   1188  OD2 ASP A 155     -14.710 -32.763 -46.150  1.00 48.28           O  
ANISOU 1188  OD2 ASP A 155     6322   5068   6955    154   2637    323       O  
ATOM   1189  N   ASN A 156     -11.229 -35.752 -50.073  1.00 37.56           N  
ANISOU 1189  N   ASN A 156     4793   3717   5759     58   1981    210       N  
ATOM   1190  CA  ASN A 156     -11.093 -36.793 -51.118  1.00 36.53           C  
ANISOU 1190  CA  ASN A 156     4581   3560   5738     35   1878    203       C  
ATOM   1191  C   ASN A 156     -11.869 -36.536 -52.416  1.00 39.19           C  
ANISOU 1191  C   ASN A 156     4807   3893   6190     36   1848    172       C  
ATOM   1192  O   ASN A 156     -11.865 -37.394 -53.291  1.00 38.50           O  
ANISOU 1192  O   ASN A 156     4659   3781   6188      9   1769    162       O  
ATOM   1193  CB  ASN A 156     -11.444 -38.188 -50.550  1.00 36.66           C  
ANISOU 1193  CB  ASN A 156     4576   3537   5815      4   1895    282       C  
ATOM   1194  CG  ASN A 156     -10.498 -38.593 -49.451  1.00 45.29           C  
ANISOU 1194  CG  ASN A 156     5771   4637   6800     -3   1892    318       C  
ATOM   1195  OD1 ASN A 156      -9.267 -38.478 -49.575  1.00 38.67           O  
ANISOU 1195  OD1 ASN A 156     4987   3815   5890      2   1811    283       O  
ATOM   1196  ND2 ASN A 156     -11.021 -39.173 -48.398  1.00 38.48           N  
ANISOU 1196  ND2 ASN A 156     4928   3761   5933    -18   1970    400       N  
ATOM   1197  N   ALA A 157     -12.460 -35.352 -52.597  1.00 36.52           N  
ANISOU 1197  N   ALA A 157     4447   3577   5851     65   1904    154       N  
ATOM   1198  CA  ALA A 157     -13.177 -35.016 -53.810  1.00 35.95           C  
ANISOU 1198  CA  ALA A 157     4269   3509   5883     64   1869    136       C  
ATOM   1199  C   ALA A 157     -12.237 -34.256 -54.689  1.00 39.64           C  
ANISOU 1199  C   ALA A 157     4765   4003   6293     79   1783     55       C  
ATOM   1200  O   ALA A 157     -11.712 -33.240 -54.260  1.00 40.58           O  
ANISOU 1200  O   ALA A 157     4959   4144   6315    109   1816     25       O  
ATOM   1201  CB  ALA A 157     -14.409 -34.182 -53.487  1.00 36.74           C  
ANISOU 1201  CB  ALA A 157     4317   3613   6030     92   1985    179       C  
ATOM   1202  N   LEU A 158     -11.984 -34.749 -55.911  1.00 37.44           N  
ANISOU 1202  N   LEU A 158     4435   3722   6070     53   1675     18       N  
ATOM   1203  CA  LEU A 158     -11.077 -34.103 -56.867  1.00 35.80           C  
ANISOU 1203  CA  LEU A 158     4248   3541   5812     65   1591    -57       C  
ATOM   1204  C   LEU A 158     -11.662 -32.765 -57.293  1.00 40.96           C  
ANISOU 1204  C   LEU A 158     4864   4223   6477     94   1624    -66       C  
ATOM   1205  O   LEU A 158     -12.829 -32.709 -57.678  1.00 41.27           O  
ANISOU 1205  O   LEU A 158     4808   4259   6613     87   1647    -26       O  
ATOM   1206  CB  LEU A 158     -10.882 -34.986 -58.103  1.00 36.51           C  
ANISOU 1206  CB  LEU A 158     4289   3617   5965     27   1485    -90       C  
ATOM   1207  CG  LEU A 158      -9.883 -34.504 -59.196  1.00 41.42           C  
ANISOU 1207  CG  LEU A 158     4932   4265   6539     33   1396   -167       C  
ATOM   1208  CD1 LEU A 158      -8.403 -34.438 -58.671  1.00 42.88           C  
ANISOU 1208  CD1 LEU A 158     5214   4457   6619     57   1378   -197       C  
ATOM   1209  CD2 LEU A 158      -9.950 -35.412 -60.418  1.00 39.93           C  
ANISOU 1209  CD2 LEU A 158     4696   4057   6417    -11   1310   -198       C  
ATOM   1210  N   GLN A 159     -10.840 -31.697 -57.258  1.00 36.89           N  
ANISOU 1210  N   GLN A 159     4416   3731   5867    125   1621   -113       N  
ATOM   1211  CA  GLN A 159     -11.283 -30.374 -57.630  1.00 37.21           C  
ANISOU 1211  CA  GLN A 159     4431   3791   5917    157   1655   -122       C  
ATOM   1212  C   GLN A 159     -10.993 -30.077 -59.076  1.00 41.56           C  
ANISOU 1212  C   GLN A 159     4934   4367   6492    148   1553   -165       C  
ATOM   1213  O   GLN A 159      -9.951 -30.475 -59.559  1.00 41.69           O  
ANISOU 1213  O   GLN A 159     4988   4392   6461    132   1470   -214       O  
ATOM   1214  CB  GLN A 159     -10.592 -29.303 -56.750  1.00 37.41           C  
ANISOU 1214  CB  GLN A 159     4566   3821   5826    190   1715   -150       C  
ATOM   1215  CG  GLN A 159     -10.760 -29.523 -55.286  1.00 33.96           C  
ANISOU 1215  CG  GLN A 159     4201   3366   5337    194   1815   -115       C  
ATOM   1216  CD  GLN A 159     -12.207 -29.431 -54.919  1.00 40.65           C  
ANISOU 1216  CD  GLN A 159     4980   4192   6273    211   1927    -53       C  
ATOM   1217  OE1 GLN A 159     -12.809 -28.395 -55.089  1.00 40.26           O  
ANISOU 1217  OE1 GLN A 159     4902   4140   6256    246   1988    -49       O  
ATOM   1218  NE2 GLN A 159     -12.827 -30.515 -54.502  1.00 36.68           N  
ANISOU 1218  NE2 GLN A 159     4437   3673   5829    188   1953      4       N  
ATOM   1219  N   SER A 160     -11.899 -29.359 -59.764  1.00 41.57           N  
ANISOU 1219  N   SER A 160     4850   4379   6564    159   1562   -143       N  
ATOM   1220  CA  SER A 160     -11.667 -28.895 -61.141  1.00 42.97           C  
ANISOU 1220  CA  SER A 160     4986   4588   6754    150   1468   -177       C  
ATOM   1221  C   SER A 160     -12.362 -27.544 -61.380  1.00 44.84           C  
ANISOU 1221  C   SER A 160     5174   4835   7028    189   1518   -149       C  
ATOM   1222  O   SER A 160     -13.402 -27.267 -60.788  1.00 43.35           O  
ANISOU 1222  O   SER A 160     4938   4628   6905    213   1612    -88       O  
ATOM   1223  CB  SER A 160     -12.079 -29.940 -62.174  1.00 47.50           C  
ANISOU 1223  CB  SER A 160     5482   5165   7400     95   1377   -172       C  
ATOM   1224  OG  SER A 160     -13.484 -30.051 -62.257  1.00 62.40           O  
ANISOU 1224  OG  SER A 160     7265   7047   9399     82   1409    -99       O  
ATOM   1225  N   GLY A 161     -11.727 -26.696 -62.178  1.00 40.82           N  
ANISOU 1225  N   GLY A 161     4681   4351   6477    201   1464   -189       N  
ATOM   1226  CA  GLY A 161     -12.242 -25.365 -62.493  1.00 40.32           C  
ANISOU 1226  CA  GLY A 161     4578   4295   6449    241   1503   -163       C  
ATOM   1227  C   GLY A 161     -12.043 -24.254 -61.477  1.00 42.87           C  
ANISOU 1227  C   GLY A 161     4980   4590   6720    294   1614   -172       C  
ATOM   1228  O   GLY A 161     -12.494 -23.144 -61.724  1.00 46.83           O  
ANISOU 1228  O   GLY A 161     5448   5085   7260    331   1656   -149       O  
ATOM   1229  N   ASN A 162     -11.355 -24.500 -60.369  1.00 36.91           N  
ANISOU 1229  N   ASN A 162     4332   3816   5875    295   1660   -205       N  
ATOM   1230  CA  ASN A 162     -11.203 -23.542 -59.260  1.00 35.25           C  
ANISOU 1230  CA  ASN A 162     4217   3574   5601    333   1772   -218       C  
ATOM   1231  C   ASN A 162      -9.764 -23.458 -58.748  1.00 38.18           C  
ANISOU 1231  C   ASN A 162     4719   3952   5836    315   1736   -284       C  
ATOM   1232  O   ASN A 162      -9.520 -22.998 -57.622  1.00 38.17           O  
ANISOU 1232  O   ASN A 162     4820   3926   5758    326   1819   -300       O  
ATOM   1233  CB  ASN A 162     -12.144 -23.961 -58.130  1.00 33.18           C  
ANISOU 1233  CB  ASN A 162     3952   3279   5374    345   1893   -168       C  
ATOM   1234  CG  ASN A 162     -11.910 -25.375 -57.613  1.00 42.63           C  
ANISOU 1234  CG  ASN A 162     5170   4482   6547    304   1863   -161       C  
ATOM   1235  OD1 ASN A 162     -11.115 -26.128 -58.167  1.00 39.80           O  
ANISOU 1235  OD1 ASN A 162     4814   4146   6161    268   1751   -191       O  
ATOM   1236  ND2 ASN A 162     -12.699 -25.818 -56.647  1.00 35.66           N  
ANISOU 1236  ND2 ASN A 162     4284   3574   5692    310   1965   -112       N  
ATOM   1237  N   SER A 163      -8.812 -23.765 -59.637  1.00 32.60           N  
ANISOU 1237  N   SER A 163     4009   3280   5100    289   1615   -321       N  
ATOM   1238  CA  SER A 163      -7.382 -23.797 -59.370  1.00 31.58           C  
ANISOU 1238  CA  SER A 163     3975   3164   4859    268   1558   -372       C  
ATOM   1239  C   SER A 163      -6.688 -22.954 -60.480  1.00 36.31           C  
ANISOU 1239  C   SER A 163     4563   3789   5444    272   1484   -408       C  
ATOM   1240  O   SER A 163      -7.205 -22.846 -61.595  1.00 36.31           O  
ANISOU 1240  O   SER A 163     4474   3805   5517    276   1445   -393       O  
ATOM   1241  CB  SER A 163      -6.891 -25.257 -59.426  1.00 35.87           C  
ANISOU 1241  CB  SER A 163     4510   3722   5399    234   1487   -371       C  
ATOM   1242  OG  SER A 163      -5.503 -25.382 -59.243  1.00 61.15           O  
ANISOU 1242  OG  SER A 163     7784   6939   8510    217   1426   -406       O  
ATOM   1243  N   GLN A 164      -5.565 -22.316 -60.145  1.00 31.72           N  
ANISOU 1243  N   GLN A 164     4072   3212   4769    265   1466   -448       N  
ATOM   1244  CA  GLN A 164      -4.710 -21.612 -61.103  1.00 30.70           C  
ANISOU 1244  CA  GLN A 164     3940   3109   4615    263   1392   -480       C  
ATOM   1245  C   GLN A 164      -3.270 -21.858 -60.677  1.00 32.36           C  
ANISOU 1245  C   GLN A 164     4229   3336   4730    235   1336   -511       C  
ATOM   1246  O   GLN A 164      -3.013 -21.978 -59.479  1.00 31.72           O  
ANISOU 1246  O   GLN A 164     4227   3239   4585    222   1374   -509       O  
ATOM   1247  CB  GLN A 164      -4.978 -20.116 -61.168  1.00 32.40           C  
ANISOU 1247  CB  GLN A 164     4175   3302   4834    290   1445   -485       C  
ATOM   1248  CG  GLN A 164      -6.337 -19.738 -61.658  1.00 40.16           C  
ANISOU 1248  CG  GLN A 164     5069   4269   5922    323   1498   -441       C  
ATOM   1249  CD  GLN A 164      -6.384 -18.269 -62.016  1.00 47.79           C  
ANISOU 1249  CD  GLN A 164     6043   5215   6899    352   1528   -445       C  
ATOM   1250  OE1 GLN A 164      -6.144 -17.388 -61.187  1.00 45.90           O  
ANISOU 1250  OE1 GLN A 164     5896   4936   6608    362   1597   -469       O  
ATOM   1251  NE2 GLN A 164      -6.791 -17.968 -63.220  1.00 35.22           N  
ANISOU 1251  NE2 GLN A 164     4359   3645   5378    363   1483   -417       N  
ATOM   1252  N   GLU A 165      -2.356 -21.957 -61.642  1.00 31.06           N  
ANISOU 1252  N   GLU A 165     4040   3205   4556    223   1247   -531       N  
ATOM   1253  CA  GLU A 165      -0.912 -22.181 -61.422  1.00 31.67           C  
ANISOU 1253  CA  GLU A 165     4170   3303   4559    199   1185   -550       C  
ATOM   1254  C   GLU A 165      -0.082 -21.125 -62.085  1.00 33.82           C  
ANISOU 1254  C   GLU A 165     4454   3595   4800    197   1143   -574       C  
ATOM   1255  O   GLU A 165      -0.410 -20.792 -63.217  1.00 32.21           O  
ANISOU 1255  O   GLU A 165     4189   3405   4644    211   1123   -577       O  
ATOM   1256  CB  GLU A 165      -0.396 -23.434 -62.149  1.00 32.29           C  
ANISOU 1256  CB  GLU A 165     4197   3405   4667    191   1115   -550       C  
ATOM   1257  CG  GLU A 165      -0.921 -24.713 -61.669  1.00 49.48           C  
ANISOU 1257  CG  GLU A 165     6357   5564   6879    186   1133   -527       C  
ATOM   1258  CD  GLU A 165      -0.235 -25.908 -62.283  1.00 55.60           C  
ANISOU 1258  CD  GLU A 165     7099   6349   7678    178   1071   -532       C  
ATOM   1259  OE1 GLU A 165      -0.322 -26.990 -61.667  1.00 70.36           O  
ANISOU 1259  OE1 GLU A 165     8973   8198   9563    171   1080   -509       O  
ATOM   1260  OE2 GLU A 165       0.400 -25.772 -63.357  1.00 47.06           O  
ANISOU 1260  OE2 GLU A 165     5991   5291   6599    180   1020   -558       O  
ATOM   1261  N   SER A 166       1.141 -20.891 -61.535  1.00 30.23           N  
ANISOU 1261  N   SER A 166     4064   3152   4269    172   1107   -583       N  
ATOM   1262  CA  SER A 166       2.213 -20.063 -62.106  1.00 30.85           C  
ANISOU 1262  CA  SER A 166     4154   3254   4315    159   1053   -600       C  
ATOM   1263  C   SER A 166       3.534 -20.811 -61.948  1.00 33.19           C  
ANISOU 1263  C   SER A 166     4457   3580   4575    136    984   -590       C  
ATOM   1264  O   SER A 166       3.803 -21.342 -60.904  1.00 32.24           O  
ANISOU 1264  O   SER A 166     4381   3454   4416    117    986   -572       O  
ATOM   1265  CB  SER A 166       2.287 -18.673 -61.443  1.00 30.77           C  
ANISOU 1265  CB  SER A 166     4224   3216   4250    146   1091   -615       C  
ATOM   1266  OG  SER A 166       3.360 -17.959 -61.994  0.60 31.86           O  
ANISOU 1266  OG  SER A 166     4368   3377   4362    128   1034   -626       O  
ATOM   1267  N   VAL A 167       4.331 -20.828 -62.980  1.00 32.78           N  
ANISOU 1267  N   VAL A 167     4358   3558   4538    139    929   -596       N  
ATOM   1268  CA  VAL A 167       5.650 -21.449 -63.038  1.00 33.10           C  
ANISOU 1268  CA  VAL A 167     4386   3627   4563    126    868   -579       C  
ATOM   1269  C   VAL A 167       6.699 -20.356 -63.199  1.00 35.98           C  
ANISOU 1269  C   VAL A 167     4772   4012   4885    103    829   -581       C  
ATOM   1270  O   VAL A 167       6.571 -19.510 -64.075  1.00 33.97           O  
ANISOU 1270  O   VAL A 167     4498   3764   4644    111    831   -599       O  
ATOM   1271  CB  VAL A 167       5.746 -22.473 -64.206  1.00 36.25           C  
ANISOU 1271  CB  VAL A 167     4709   4040   5022    151    847   -585       C  
ATOM   1272  CG1 VAL A 167       6.985 -23.327 -64.065  1.00 36.75           C  
ANISOU 1272  CG1 VAL A 167     4758   4120   5086    148    804   -559       C  
ATOM   1273  CG2 VAL A 167       4.507 -23.368 -64.241  1.00 36.81           C  
ANISOU 1273  CG2 VAL A 167     4757   4086   5144    166    885   -589       C  
ATOM   1274  N   THR A 168       7.776 -20.417 -62.416  1.00 33.27           N  
ANISOU 1274  N   THR A 168     4462   3682   4495     69    786   -554       N  
ATOM   1275  CA  THR A 168       8.834 -19.445 -62.558  1.00 33.84           C  
ANISOU 1275  CA  THR A 168     4549   3776   4532     39    741   -549       C  
ATOM   1276  C   THR A 168       9.617 -19.733 -63.847  1.00 38.19           C  
ANISOU 1276  C   THR A 168     5018   4362   5132     62    706   -541       C  
ATOM   1277  O   THR A 168       9.586 -20.845 -64.398  1.00 38.66           O  
ANISOU 1277  O   THR A 168     5022   4427   5239     94    710   -537       O  
ATOM   1278  CB  THR A 168       9.815 -19.483 -61.346  1.00 39.11           C  
ANISOU 1278  CB  THR A 168     5269   4455   5136    -14    692   -512       C  
ATOM   1279  OG1 THR A 168      10.357 -20.791 -61.212  1.00 45.67           O  
ANISOU 1279  OG1 THR A 168     6053   5305   5996     -1    662   -469       O  
ATOM   1280  CG2 THR A 168       9.169 -19.087 -60.057  1.00 40.53           C  
ANISOU 1280  CG2 THR A 168     5549   4604   5248    -46    728   -524       C  
ATOM   1281  N   GLU A 169      10.370 -18.752 -64.295  1.00 37.88           N  
ANISOU 1281  N   GLU A 169     4975   4341   5077     42    676   -539       N  
ATOM   1282  CA  GLU A 169      11.284 -18.956 -65.424  1.00 39.00           C  
ANISOU 1282  CA  GLU A 169     5044   4519   5254     59    647   -525       C  
ATOM   1283  C   GLU A 169      12.464 -19.745 -64.818  1.00 40.63           C  
ANISOU 1283  C   GLU A 169     5229   4746   5463     44    601   -474       C  
ATOM   1284  O   GLU A 169      12.691 -19.710 -63.602  1.00 38.99           O  
ANISOU 1284  O   GLU A 169     5070   4532   5211      5    575   -448       O  
ATOM   1285  CB  GLU A 169      11.754 -17.607 -66.055  1.00 40.72           C  
ANISOU 1285  CB  GLU A 169     5262   4752   5459     39    631   -528       C  
ATOM   1286  CG  GLU A 169      10.657 -16.857 -66.811  1.00 54.35           C  
ANISOU 1286  CG  GLU A 169     6993   6460   7197     60    673   -564       C  
ATOM   1287  CD  GLU A 169      10.423 -17.170 -68.286  1.00 77.27           C  
ANISOU 1287  CD  GLU A 169     9831   9388  10140     97    684   -575       C  
ATOM   1288  OE1 GLU A 169       9.863 -16.283 -68.974  1.00 89.32           O  
ANISOU 1288  OE1 GLU A 169    11355  10911  11672    103    700   -587       O  
ATOM   1289  OE2 GLU A 169      10.725 -18.299 -68.744  1.00 59.46           O  
ANISOU 1289  OE2 GLU A 169     7532   7151   7910    120    682   -573       O  
ATOM   1290  N   GLN A 170      13.170 -20.465 -65.651  1.00 37.40           N  
ANISOU 1290  N   GLN A 170     4748   4359   5102     75    595   -455       N  
ATOM   1291  CA  GLN A 170      14.312 -21.251 -65.202  1.00 39.91           C  
ANISOU 1291  CA  GLN A 170     5027   4694   5442     72    557   -395       C  
ATOM   1292  C   GLN A 170      15.301 -20.419 -64.399  1.00 44.61           C  
ANISOU 1292  C   GLN A 170     5644   5313   5994     11    493   -347       C  
ATOM   1293  O   GLN A 170      15.607 -19.310 -64.787  1.00 45.78           O  
ANISOU 1293  O   GLN A 170     5798   5475   6122    -15    477   -355       O  
ATOM   1294  CB  GLN A 170      14.984 -21.891 -66.403  1.00 41.24           C  
ANISOU 1294  CB  GLN A 170     5116   4879   5673    118    574   -387       C  
ATOM   1295  CG  GLN A 170      16.138 -22.757 -66.064  1.00 49.20           C  
ANISOU 1295  CG  GLN A 170     6070   5899   6726    128    548   -318       C  
ATOM   1296  CD  GLN A 170      16.455 -23.704 -67.208  1.00 53.75           C  
ANISOU 1296  CD  GLN A 170     6581   6469   7371    189    597   -327       C  
ATOM   1297  OE1 GLN A 170      16.388 -23.344 -68.388  1.00 46.50           O  
ANISOU 1297  OE1 GLN A 170     5649   5563   6457    208    629   -368       O  
ATOM   1298  NE2 GLN A 170      16.723 -24.949 -66.895  1.00 41.77           N  
ANISOU 1298  NE2 GLN A 170     5034   4928   5907    221    611   -294       N  
ATOM   1299  N   ASP A 171      15.743 -20.933 -63.254  1.00 38.81           N  
ANISOU 1299  N   ASP A 171     4923   4581   5241    -18    451   -294       N  
ATOM   1300  CA  ASP A 171      16.657 -20.225 -62.378  1.00 37.81           C  
ANISOU 1300  CA  ASP A 171     4822   4478   5064    -89    377   -243       C  
ATOM   1301  C   ASP A 171      18.035 -20.064 -63.024  1.00 45.39           C  
ANISOU 1301  C   ASP A 171     5695   5479   6073    -93    334   -185       C  
ATOM   1302  O   ASP A 171      18.556 -21.023 -63.601  1.00 45.62           O  
ANISOU 1302  O   ASP A 171     5639   5518   6177    -40    350   -149       O  
ATOM   1303  CB  ASP A 171      16.781 -20.989 -61.059  1.00 39.00           C  
ANISOU 1303  CB  ASP A 171     5003   4630   5187   -118    340   -190       C  
ATOM   1304  CG  ASP A 171      17.578 -20.270 -60.010  1.00 45.92           C  
ANISOU 1304  CG  ASP A 171     5926   5532   5991   -208    256   -141       C  
ATOM   1305  OD1 ASP A 171      17.001 -19.404 -59.332  1.00 50.64           O  
ANISOU 1305  OD1 ASP A 171     6628   6110   6503   -261    258   -186       O  
ATOM   1306  OD2 ASP A 171      18.788 -20.572 -59.865  1.00 48.83           O  
ANISOU 1306  OD2 ASP A 171     6227   5938   6390   -229    187    -55       O  
ATOM   1307  N   SER A 172      18.642 -18.865 -62.896  1.00 42.80           N  
ANISOU 1307  N   SER A 172     5387   5170   5705   -156    284   -172       N  
ATOM   1308  CA  SER A 172      19.928 -18.563 -63.530  1.00 42.63           C  
ANISOU 1308  CA  SER A 172     5278   5187   5731   -165    245   -114       C  
ATOM   1309  C   SER A 172      21.117 -19.252 -62.909  1.00 45.76           C  
ANISOU 1309  C   SER A 172     5606   5618   6162   -186    177     -8       C  
ATOM   1310  O   SER A 172      22.132 -19.349 -63.589  1.00 46.90           O  
ANISOU 1310  O   SER A 172     5652   5793   6376   -167    167     49       O  
ATOM   1311  CB  SER A 172      20.176 -17.059 -63.581  1.00 46.83           C  
ANISOU 1311  CB  SER A 172     5854   5724   6216   -233    211   -130       C  
ATOM   1312  OG  SER A 172      20.497 -16.536 -62.301  1.00 59.80           O  
ANISOU 1312  OG  SER A 172     7568   7369   7786   -325    135   -102       O  
ATOM   1313  N   LYS A 173      21.022 -19.727 -61.660  1.00 41.59           N  
ANISOU 1313  N   LYS A 173     5123   5087   5591   -224    132     27       N  
ATOM   1314  CA  LYS A 173      22.135 -20.439 -61.021  1.00 43.27           C  
ANISOU 1314  CA  LYS A 173     5264   5334   5842   -244     59    143       C  
ATOM   1315  C   LYS A 173      21.939 -21.960 -61.034  1.00 44.42           C  
ANISOU 1315  C   LYS A 173     5356   5462   6060   -164    104    173       C  
ATOM   1316  O   LYS A 173      22.818 -22.667 -61.514  1.00 44.14           O  
ANISOU 1316  O   LYS A 173     5209   5441   6121   -116    108    244       O  
ATOM   1317  CB  LYS A 173      22.364 -19.961 -59.562  1.00 47.61           C  
ANISOU 1317  CB  LYS A 173     5895   5902   6293   -354    -40    185       C  
ATOM   1318  CG  LYS A 173      22.432 -18.441 -59.422  1.00 68.80           C  
ANISOU 1318  CG  LYS A 173     8659   8587   8895   -443    -79    141       C  
ATOM   1319  CD  LYS A 173      22.811 -18.005 -58.016  1.00 81.69           C  
ANISOU 1319  CD  LYS A 173    10374  10238  10425   -562   -183    185       C  
ATOM   1320  CE  LYS A 173      22.932 -16.498 -57.893  1.00 86.16           C  
ANISOU 1320  CE  LYS A 173    11026  10796  10915   -655   -219    139       C  
ATOM   1321  NZ  LYS A 173      23.520 -16.085 -56.576  1.00 91.58           N  
ANISOU 1321  NZ  LYS A 173    11788  11506  11500   -788   -336    191       N  
ATOM   1322  N   ASP A 174      20.815 -22.473 -60.505  1.00 40.49           N  
ANISOU 1322  N   ASP A 174     4935   4928   5521   -149    143    122       N  
ATOM   1323  CA  ASP A 174      20.612 -23.935 -60.414  1.00 40.23           C  
ANISOU 1323  CA  ASP A 174     4859   4870   5555    -82    182    154       C  
ATOM   1324  C   ASP A 174      19.819 -24.551 -61.562  1.00 42.54           C  
ANISOU 1324  C   ASP A 174     5132   5121   5909      8    287     73       C  
ATOM   1325  O   ASP A 174      19.790 -25.772 -61.629  1.00 41.99           O  
ANISOU 1325  O   ASP A 174     5019   5024   5909     64    322    100       O  
ATOM   1326  CB  ASP A 174      20.019 -24.378 -59.068  1.00 42.15           C  
ANISOU 1326  CB  ASP A 174     5182   5102   5730   -121    155    173       C  
ATOM   1327  CG  ASP A 174      18.660 -23.844 -58.709  1.00 51.19           C  
ANISOU 1327  CG  ASP A 174     6449   6217   6784   -143    199     74       C  
ATOM   1328  OD1 ASP A 174      17.863 -23.591 -59.634  1.00 47.39           O  
ANISOU 1328  OD1 ASP A 174     5977   5708   6320    -98    274    -16       O  
ATOM   1329  OD2 ASP A 174      18.364 -23.744 -57.486  1.00 60.29           O  
ANISOU 1329  OD2 ASP A 174     7686   7373   7849   -204    163     91       O  
ATOM   1330  N   SER A 175      19.206 -23.745 -62.453  1.00 36.73           N  
ANISOU 1330  N   SER A 175     4428   4378   5150     17    333    -18       N  
ATOM   1331  CA  SER A 175      18.449 -24.226 -63.624  1.00 34.95           C  
ANISOU 1331  CA  SER A 175     4189   4120   4970     88    422    -95       C  
ATOM   1332  C   SER A 175      17.135 -24.963 -63.282  1.00 38.01           C  
ANISOU 1332  C   SER A 175     4632   4462   5346    110    469   -147       C  
ATOM   1333  O   SER A 175      16.536 -25.569 -64.169  1.00 35.28           O  
ANISOU 1333  O   SER A 175     4272   4088   5043    163    533   -201       O  
ATOM   1334  CB  SER A 175      19.325 -25.090 -64.541  1.00 38.94           C  
ANISOU 1334  CB  SER A 175     4593   4625   5577    154    456    -58       C  
ATOM   1335  OG  SER A 175      20.603 -24.534 -64.772  1.00 40.95           O  
ANISOU 1335  OG  SER A 175     4780   4922   5855    136    415      8       O  
ATOM   1336  N   THR A 176      16.611 -24.786 -62.063  1.00 37.82           N  
ANISOU 1336  N   THR A 176     4682   4434   5254     62    440   -138       N  
ATOM   1337  CA  THR A 176      15.351 -25.397 -61.662  1.00 37.02           C  
ANISOU 1337  CA  THR A 176     4632   4292   5141     78    487   -179       C  
ATOM   1338  C   THR A 176      14.161 -24.490 -61.943  1.00 39.32           C  
ANISOU 1338  C   THR A 176     4989   4571   5382     67    528   -266       C  
ATOM   1339  O   THR A 176      14.318 -23.334 -62.318  1.00 38.74           O  
ANISOU 1339  O   THR A 176     4930   4516   5275     43    516   -293       O  
ATOM   1340  CB  THR A 176      15.357 -25.725 -60.176  1.00 39.08           C  
ANISOU 1340  CB  THR A 176     4941   4555   5353     34    446   -120       C  
ATOM   1341  OG1 THR A 176      15.380 -24.515 -59.434  1.00 35.39           O  
ANISOU 1341  OG1 THR A 176     4549   4110   4787    -37    405   -127       O  
ATOM   1342  CG2 THR A 176      16.462 -26.630 -59.783  1.00 34.65           C  
ANISOU 1342  CG2 THR A 176     4313   4007   4846     42    400    -18       C  
ATOM   1343  N   TYR A 177      12.959 -25.050 -61.760  1.00 37.33           N  
ANISOU 1343  N   TYR A 177     4767   4282   5134     86    578   -303       N  
ATOM   1344  CA  TYR A 177      11.692 -24.340 -61.822  1.00 36.27           C  
ANISOU 1344  CA  TYR A 177     4689   4129   4963     80    623   -369       C  
ATOM   1345  C   TYR A 177      11.032 -24.498 -60.466  1.00 36.13           C  
ANISOU 1345  C   TYR A 177     4742   4093   4892     50    633   -353       C  
ATOM   1346  O   TYR A 177      11.377 -25.395 -59.694  1.00 34.35           O  
ANISOU 1346  O   TYR A 177     4513   3865   4672     45    613   -297       O  
ATOM   1347  CB  TYR A 177      10.741 -24.945 -62.864  1.00 37.47           C  
ANISOU 1347  CB  TYR A 177     4807   4255   5175    127    678   -420       C  
ATOM   1348  CG  TYR A 177      11.296 -24.979 -64.250  1.00 38.15           C  
ANISOU 1348  CG  TYR A 177     4832   4357   5307    158    679   -440       C  
ATOM   1349  CD1 TYR A 177      11.204 -23.874 -65.080  1.00 39.96           C  
ANISOU 1349  CD1 TYR A 177     5061   4606   5516    153    680   -477       C  
ATOM   1350  CD2 TYR A 177      12.013 -26.082 -64.706  1.00 38.70           C  
ANISOU 1350  CD2 TYR A 177     4847   4420   5439    192    681   -417       C  
ATOM   1351  CE1 TYR A 177      11.744 -23.887 -66.367  1.00 41.49           C  
ANISOU 1351  CE1 TYR A 177     5204   4819   5742    178    684   -493       C  
ATOM   1352  CE2 TYR A 177      12.644 -26.068 -65.948  1.00 39.61           C  
ANISOU 1352  CE2 TYR A 177     4913   4550   5587    219    690   -434       C  
ATOM   1353  CZ  TYR A 177      12.466 -24.987 -66.797  1.00 46.75           C  
ANISOU 1353  CZ  TYR A 177     5821   5479   6461    210    692   -475       C  
ATOM   1354  OH  TYR A 177      12.998 -24.972 -68.056  1.00 50.06           O  
ANISOU 1354  OH  TYR A 177     6201   5917   6905    234    708   -494       O  
ATOM   1355  N   SER A 178      10.053 -23.633 -60.218  1.00 33.29           N  
ANISOU 1355  N   SER A 178     4444   3718   4487     35    673   -400       N  
ATOM   1356  CA  SER A 178       9.187 -23.655 -59.050  1.00 32.60           C  
ANISOU 1356  CA  SER A 178     4431   3607   4347     13    709   -399       C  
ATOM   1357  C   SER A 178       7.797 -23.335 -59.544  1.00 36.82           C  
ANISOU 1357  C   SER A 178     4970   4112   4909     43    783   -455       C  
ATOM   1358  O   SER A 178       7.639 -22.734 -60.616  1.00 34.41           O  
ANISOU 1358  O   SER A 178     4629   3810   4634     63    791   -491       O  
ATOM   1359  CB  SER A 178       9.678 -22.726 -57.954  1.00 31.46           C  
ANISOU 1359  CB  SER A 178     4375   3476   4101    -51    678   -386       C  
ATOM   1360  OG  SER A 178      10.958 -23.145 -57.516  1.00 41.58           O  
ANISOU 1360  OG  SER A 178     5640   4792   5368    -82    598   -319       O  
ATOM   1361  N   LEU A 179       6.781 -23.873 -58.845  1.00 34.64           N  
ANISOU 1361  N   LEU A 179     4721   3808   4632     49    836   -451       N  
ATOM   1362  CA  LEU A 179       5.395 -23.757 -59.275  1.00 33.29           C  
ANISOU 1362  CA  LEU A 179     4536   3609   4504     78    906   -487       C  
ATOM   1363  C   LEU A 179       4.547 -23.494 -58.067  1.00 35.93           C  
ANISOU 1363  C   LEU A 179     4948   3918   4787     62    969   -484       C  
ATOM   1364  O   LEU A 179       4.725 -24.160 -57.047  1.00 34.77           O  
ANISOU 1364  O   LEU A 179     4839   3771   4602     40    965   -446       O  
ATOM   1365  CB  LEU A 179       4.973 -25.072 -59.992  1.00 33.24           C  
ANISOU 1365  CB  LEU A 179     4452   3591   4586    112    911   -481       C  
ATOM   1366  CG  LEU A 179       3.594 -25.145 -60.595  1.00 36.80           C  
ANISOU 1366  CG  LEU A 179     4867   4019   5096    137    965   -508       C  
ATOM   1367  CD1 LEU A 179       3.582 -26.135 -61.732  1.00 37.00           C  
ANISOU 1367  CD1 LEU A 179     4818   4042   5197    158    942   -518       C  
ATOM   1368  CD2 LEU A 179       2.495 -25.528 -59.541  1.00 39.40           C  
ANISOU 1368  CD2 LEU A 179     5228   4317   5423    133   1030   -487       C  
ATOM   1369  N   SER A 180       3.607 -22.532 -58.186  1.00 32.20           N  
ANISOU 1369  N   SER A 180     4497   3422   4315     74   1033   -519       N  
ATOM   1370  CA  SER A 180       2.662 -22.226 -57.122  1.00 32.64           C  
ANISOU 1370  CA  SER A 180     4623   3446   4332     67   1117   -521       C  
ATOM   1371  C   SER A 180       1.258 -22.459 -57.683  1.00 37.78           C  
ANISOU 1371  C   SER A 180     5209   4072   5073    111   1185   -526       C  
ATOM   1372  O   SER A 180       0.944 -21.925 -58.730  1.00 36.62           O  
ANISOU 1372  O   SER A 180     5008   3926   4981    135   1183   -547       O  
ATOM   1373  CB  SER A 180       2.790 -20.782 -56.631  1.00 35.62           C  
ANISOU 1373  CB  SER A 180     5093   3807   4633     43   1146   -554       C  
ATOM   1374  OG  SER A 180       2.372 -20.716 -55.273  1.00 52.03           O  
ANISOU 1374  OG  SER A 180     7270   5862   6636     18   1211   -549       O  
ATOM   1375  N   SER A 181       0.431 -23.262 -57.003  1.00 35.55           N  
ANISOU 1375  N   SER A 181     4928   3771   4809    117   1239   -499       N  
ATOM   1376  CA  SER A 181      -0.942 -23.528 -57.415  1.00 34.58           C  
ANISOU 1376  CA  SER A 181     4739   3625   4776    151   1303   -492       C  
ATOM   1377  C   SER A 181      -1.851 -22.977 -56.321  1.00 38.43           C  
ANISOU 1377  C   SER A 181     5294   4078   5230    155   1414   -486       C  
ATOM   1378  O   SER A 181      -1.534 -23.123 -55.150  1.00 38.97           O  
ANISOU 1378  O   SER A 181     5449   4144   5214    126   1435   -475       O  
ATOM   1379  CB  SER A 181      -1.183 -25.022 -57.579  1.00 34.71           C  
ANISOU 1379  CB  SER A 181     4691   3642   4854    152   1280   -460       C  
ATOM   1380  OG  SER A 181      -2.562 -25.258 -57.821  1.00 37.93           O  
ANISOU 1380  OG  SER A 181     5039   4027   5344    174   1343   -445       O  
ATOM   1381  N   THR A 182      -2.956 -22.341 -56.689  1.00 34.71           N  
ANISOU 1381  N   THR A 182     4783   3581   4822    189   1487   -490       N  
ATOM   1382  CA  THR A 182      -3.891 -21.796 -55.708  1.00 35.42           C  
ANISOU 1382  CA  THR A 182     4931   3631   4894    202   1612   -484       C  
ATOM   1383  C   THR A 182      -5.238 -22.375 -55.951  1.00 37.10           C  
ANISOU 1383  C   THR A 182     5050   3828   5217    234   1672   -444       C  
ATOM   1384  O   THR A 182      -5.739 -22.213 -57.046  1.00 36.65           O  
ANISOU 1384  O   THR A 182     4896   3777   5253    258   1650   -438       O  
ATOM   1385  CB  THR A 182      -3.964 -20.239 -55.819  1.00 40.75           C  
ANISOU 1385  CB  THR A 182     5654   4278   5552    219   1663   -521       C  
ATOM   1386  OG1 THR A 182      -2.675 -19.706 -55.594  1.00 41.27           O  
ANISOU 1386  OG1 THR A 182     5806   4359   5515    180   1597   -557       O  
ATOM   1387  CG2 THR A 182      -4.903 -19.600 -54.807  1.00 33.41           C  
ANISOU 1387  CG2 THR A 182     4795   3296   4603    240   1810   -521       C  
ATOM   1388  N   LEU A 183      -5.846 -22.986 -54.936  1.00 34.53           N  
ANISOU 1388  N   LEU A 183     4753   3486   4881    231   1749   -412       N  
ATOM   1389  CA  LEU A 183      -7.225 -23.474 -54.966  1.00 34.99           C  
ANISOU 1389  CA  LEU A 183     4724   3524   5045    258   1826   -364       C  
ATOM   1390  C   LEU A 183      -8.085 -22.362 -54.377  1.00 41.20           C  
ANISOU 1390  C   LEU A 183     5552   4268   5834    293   1967   -365       C  
ATOM   1391  O   LEU A 183      -7.841 -21.941 -53.226  1.00 41.10           O  
ANISOU 1391  O   LEU A 183     5665   4235   5716    281   2039   -385       O  
ATOM   1392  CB  LEU A 183      -7.392 -24.746 -54.105  1.00 34.59           C  
ANISOU 1392  CB  LEU A 183     4686   3475   4981    234   1843   -322       C  
ATOM   1393  CG  LEU A 183      -8.783 -25.344 -54.002  1.00 37.90           C  
ANISOU 1393  CG  LEU A 183     5020   3874   5508    254   1924   -265       C  
ATOM   1394  CD1 LEU A 183      -9.272 -25.832 -55.323  1.00 36.08           C  
ANISOU 1394  CD1 LEU A 183     4651   3655   5403    258   1852   -247       C  
ATOM   1395  CD2 LEU A 183      -8.807 -26.464 -52.994  1.00 41.95           C  
ANISOU 1395  CD2 LEU A 183     5569   4383   5985    227   1948   -224       C  
ATOM   1396  N   THR A 184      -9.082 -21.870 -55.140  1.00 37.69           N  
ANISOU 1396  N   THR A 184     5006   3807   5507    336   2008   -341       N  
ATOM   1397  CA  THR A 184      -9.921 -20.796 -54.609  1.00 38.85           C  
ANISOU 1397  CA  THR A 184     5183   3903   5673    380   2155   -336       C  
ATOM   1398  C   THR A 184     -11.327 -21.275 -54.335  1.00 43.72           C  
ANISOU 1398  C   THR A 184     5713   4499   6398    410   2260   -267       C  
ATOM   1399  O   THR A 184     -11.990 -21.771 -55.229  1.00 43.11           O  
ANISOU 1399  O   THR A 184     5498   4441   6442    417   2213   -219       O  
ATOM   1400  CB  THR A 184      -9.895 -19.545 -55.481  1.00 46.87           C  
ANISOU 1400  CB  THR A 184     6172   4904   6732    412   2147   -357       C  
ATOM   1401  OG1 THR A 184      -8.549 -19.185 -55.689  1.00 47.53           O  
ANISOU 1401  OG1 THR A 184     6335   5009   6714    377   2048   -416       O  
ATOM   1402  CG2 THR A 184     -10.587 -18.352 -54.808  1.00 49.44           C  
ANISOU 1402  CG2 THR A 184     6555   5164   7067    460   2310   -360       C  
ATOM   1403  N   LEU A 185     -11.788 -21.065 -53.102  1.00 41.45           N  
ANISOU 1403  N   LEU A 185     5509   4173   6065    425   2405   -260       N  
ATOM   1404  CA  LEU A 185     -13.100 -21.473 -52.661  1.00 44.03           C  
ANISOU 1404  CA  LEU A 185     5764   4477   6487    455   2527   -191       C  
ATOM   1405  C   LEU A 185     -13.833 -20.346 -51.978  1.00 48.39           C  
ANISOU 1405  C   LEU A 185     6369   4967   7049    511   2711   -191       C  
ATOM   1406  O   LEU A 185     -13.225 -19.427 -51.439  1.00 48.26           O  
ANISOU 1406  O   LEU A 185     6493   4921   6923    510   2757   -256       O  
ATOM   1407  CB  LEU A 185     -12.938 -22.609 -51.635  1.00 45.21           C  
ANISOU 1407  CB  LEU A 185     5976   4642   6561    414   2540   -173       C  
ATOM   1408  CG  LEU A 185     -12.064 -23.808 -52.021  1.00 48.99           C  
ANISOU 1408  CG  LEU A 185     6435   5169   7008    358   2376   -177       C  
ATOM   1409  CD1 LEU A 185     -11.932 -24.756 -50.863  1.00 49.43           C  
ANISOU 1409  CD1 LEU A 185     6566   5230   6986    324   2410   -152       C  
ATOM   1410  CD2 LEU A 185     -12.663 -24.561 -53.177  1.00 51.22           C  
ANISOU 1410  CD2 LEU A 185     6550   5472   7438    358   2295   -129       C  
ATOM   1411  N   SER A 186     -15.141 -20.456 -51.889  1.00 46.67           N  
ANISOU 1411  N   SER A 186     6048   4725   6959    556   2826   -117       N  
ATOM   1412  CA  SER A 186     -15.886 -19.500 -51.041  1.00 46.50           C  
ANISOU 1412  CA  SER A 186     6087   4634   6945    614   3033   -112       C  
ATOM   1413  C   SER A 186     -15.599 -19.953 -49.601  1.00 50.06           C  
ANISOU 1413  C   SER A 186     6695   5079   7249    580   3119   -138       C  
ATOM   1414  O   SER A 186     -15.331 -21.148 -49.372  1.00 48.27           O  
ANISOU 1414  O   SER A 186     6458   4896   6984    530   3040   -116       O  
ATOM   1415  CB  SER A 186     -17.384 -19.587 -51.301  1.00 47.39           C  
ANISOU 1415  CB  SER A 186     6032   4727   7247    672   3138    -11       C  
ATOM   1416  OG  SER A 186     -17.858 -20.902 -51.068  1.00 47.78           O  
ANISOU 1416  OG  SER A 186     6007   4810   7337    641   3119     53       O  
ATOM   1417  N   LYS A 187     -15.597 -19.009 -48.659  1.00 47.29           N  
ANISOU 1417  N   LYS A 187     6492   4670   6806    603   3272   -187       N  
ATOM   1418  CA  LYS A 187     -15.407 -19.312 -47.230  1.00 48.49           C  
ANISOU 1418  CA  LYS A 187     6808   4812   6804    569   3371   -211       C  
ATOM   1419  C   LYS A 187     -16.427 -20.366 -46.770  1.00 52.54           C  
ANISOU 1419  C   LYS A 187     7231   5337   7395    580   3454   -119       C  
ATOM   1420  O   LYS A 187     -16.072 -21.251 -45.995  1.00 51.06           O  
ANISOU 1420  O   LYS A 187     7117   5182   7102    526   3432   -112       O  
ATOM   1421  CB  LYS A 187     -15.556 -18.036 -46.372  1.00 51.45           C  
ANISOU 1421  CB  LYS A 187     7344   5108   7097    602   3559   -272       C  
ATOM   1422  CG  LYS A 187     -15.485 -18.280 -44.854  1.00 54.83           C  
ANISOU 1422  CG  LYS A 187     7953   5524   7357    566   3683   -295       C  
ATOM   1423  CD  LYS A 187     -15.965 -17.127 -44.040  1.00 60.72           C  
ANISOU 1423  CD  LYS A 187     8834   6180   8055    610   3906   -343       C  
ATOM   1424  CE  LYS A 187     -15.857 -17.371 -42.547  1.00 77.45           C  
ANISOU 1424  CE  LYS A 187    11149   8292   9987    564   4024   -371       C  
ATOM   1425  NZ  LYS A 187     -15.389 -16.151 -41.816  1.00 98.36           N  
ANISOU 1425  NZ  LYS A 187    14023  10871  12476    548   4129   -480       N  
ATOM   1426  N   ALA A 188     -17.704 -20.231 -47.217  1.00 51.74           N  
ANISOU 1426  N   ALA A 188     6969   5207   7481    648   3554    -41       N  
ATOM   1427  CA  ALA A 188     -18.796 -21.172 -46.887  1.00 52.64           C  
ANISOU 1427  CA  ALA A 188     6972   5330   7701    661   3638     59       C  
ATOM   1428  C   ALA A 188     -18.407 -22.605 -47.240  1.00 56.47           C  
ANISOU 1428  C   ALA A 188     7386   5883   8189    593   3461     94       C  
ATOM   1429  O   ALA A 188     -18.502 -23.490 -46.398  1.00 55.91           O  
ANISOU 1429  O   ALA A 188     7357   5826   8062    560   3499    126       O  
ATOM   1430  CB  ALA A 188     -20.069 -20.786 -47.631  1.00 53.59           C  
ANISOU 1430  CB  ALA A 188     6898   5421   8042    735   3716    145       C  
ATOM   1431  N   ASP A 189     -17.903 -22.812 -48.463  1.00 54.08           N  
ANISOU 1431  N   ASP A 189     6989   5618   7941    570   3270     82       N  
ATOM   1432  CA  ASP A 189     -17.451 -24.136 -48.915  1.00 53.88           C  
ANISOU 1432  CA  ASP A 189     6903   5648   7923    507   3099    103       C  
ATOM   1433  C   ASP A 189     -16.211 -24.584 -48.171  1.00 52.05           C  
ANISOU 1433  C   ASP A 189     6834   5439   7502    447   3029     45       C  
ATOM   1434  O   ASP A 189     -16.140 -25.738 -47.776  1.00 49.01           O  
ANISOU 1434  O   ASP A 189     6445   5078   7099    406   2992     84       O  
ATOM   1435  CB  ASP A 189     -17.219 -24.163 -50.434  1.00 56.85           C  
ANISOU 1435  CB  ASP A 189     7151   6053   8395    498   2926     98       C  
ATOM   1436  CG  ASP A 189     -18.489 -23.971 -51.259  1.00 82.67           C  
ANISOU 1436  CG  ASP A 189    10233   9314  11865    541   2960    179       C  
ATOM   1437  OD1 ASP A 189     -19.606 -24.074 -50.680  1.00 88.01           O  
ANISOU 1437  OD1 ASP A 189    10849   9963  12627    573   3108    255       O  
ATOM   1438  OD2 ASP A 189     -18.371 -23.720 -52.480  1.00 92.46           O  
ANISOU 1438  OD2 ASP A 189    11382  10575  13175    539   2839    174       O  
ATOM   1439  N   TYR A 190     -15.253 -23.669 -47.939  1.00 47.36           N  
ANISOU 1439  N   TYR A 190     6384   4839   6771    440   3013    -41       N  
ATOM   1440  CA  TYR A 190     -14.061 -23.980 -47.147  1.00 45.92           C  
ANISOU 1440  CA  TYR A 190     6362   4682   6404    379   2949    -88       C  
ATOM   1441  C   TYR A 190     -14.429 -24.522 -45.744  1.00 50.14           C  
ANISOU 1441  C   TYR A 190     6991   5209   6853    361   3077    -50       C  
ATOM   1442  O   TYR A 190     -13.862 -25.521 -45.301  1.00 49.29           O  
ANISOU 1442  O   TYR A 190     6921   5136   6672    307   2999    -29       O  
ATOM   1443  CB  TYR A 190     -13.169 -22.731 -47.009  1.00 47.01           C  
ANISOU 1443  CB  TYR A 190     6642   4803   6416    374   2944   -180       C  
ATOM   1444  CG  TYR A 190     -11.939 -22.988 -46.176  1.00 46.36           C  
ANISOU 1444  CG  TYR A 190     6722   4751   6142    303   2870   -221       C  
ATOM   1445  CD1 TYR A 190     -10.933 -23.832 -46.631  1.00 45.30           C  
ANISOU 1445  CD1 TYR A 190     6559   4669   5985    255   2686   -218       C  
ATOM   1446  CD2 TYR A 190     -11.798 -22.422 -44.908  1.00 47.56           C  
ANISOU 1446  CD2 TYR A 190     7056   4879   6136    283   2988   -258       C  
ATOM   1447  CE1 TYR A 190      -9.812 -24.103 -45.856  1.00 45.56           C  
ANISOU 1447  CE1 TYR A 190     6724   4732   5852    190   2613   -238       C  
ATOM   1448  CE2 TYR A 190     -10.663 -22.653 -44.141  1.00 48.19           C  
ANISOU 1448  CE2 TYR A 190     7282   4993   6035    208   2907   -286       C  
ATOM   1449  CZ  TYR A 190      -9.686 -23.524 -44.604  1.00 54.24           C  
ANISOU 1449  CZ  TYR A 190     8000   5815   6793    163   2717   -268       C  
ATOM   1450  OH  TYR A 190      -8.570 -23.801 -43.853  1.00 52.86           O  
ANISOU 1450  OH  TYR A 190     7952   5678   6453     90   2629   -278       O  
ATOM   1451  N   GLU A 191     -15.399 -23.867 -45.065  1.00 47.49           N  
ANISOU 1451  N   GLU A 191     6688   4826   6532    408   3279    -37       N  
ATOM   1452  CA  GLU A 191     -15.797 -24.229 -43.709  1.00 48.77           C  
ANISOU 1452  CA  GLU A 191     6952   4977   6601    395   3425     -5       C  
ATOM   1453  C   GLU A 191     -16.658 -25.492 -43.634  1.00 51.74           C  
ANISOU 1453  C   GLU A 191     7197   5368   7092    393   3447    100       C  
ATOM   1454  O   GLU A 191     -16.759 -26.048 -42.557  1.00 52.61           O  
ANISOU 1454  O   GLU A 191     7392   5485   7111    366   3524    134       O  
ATOM   1455  CB  GLU A 191     -16.487 -23.033 -43.003  1.00 51.58           C  
ANISOU 1455  CB  GLU A 191     7404   5268   6926    449   3650    -35       C  
ATOM   1456  CG  GLU A 191     -15.591 -21.813 -42.805  1.00 59.28           C  
ANISOU 1456  CG  GLU A 191     8550   6219   7756    435   3645   -145       C  
ATOM   1457  CD  GLU A 191     -14.527 -21.867 -41.728  1.00 76.50           C  
ANISOU 1457  CD  GLU A 191    10947   8424   9697    354   3610   -200       C  
ATOM   1458  OE1 GLU A 191     -14.540 -22.807 -40.903  1.00 71.50           O  
ANISOU 1458  OE1 GLU A 191    10355   7823   8989    312   3621   -152       O  
ATOM   1459  OE2 GLU A 191     -13.686 -20.940 -41.696  1.00 76.94           O  
ANISOU 1459  OE2 GLU A 191    11131   8465   9639    328   3571   -289       O  
ATOM   1460  N   LYS A 192     -17.225 -25.974 -44.751  1.00 49.72           N  
ANISOU 1460  N   LYS A 192     6745   5121   7025    414   3370    153       N  
ATOM   1461  CA  LYS A 192     -18.009 -27.234 -44.814  1.00 51.00           C  
ANISOU 1461  CA  LYS A 192     6772   5296   7311    400   3366    253       C  
ATOM   1462  C   LYS A 192     -17.120 -28.502 -44.981  1.00 51.57           C  
ANISOU 1462  C   LYS A 192     6844   5411   7341    331   3184    262       C  
ATOM   1463  O   LYS A 192     -17.647 -29.614 -44.981  1.00 50.13           O  
ANISOU 1463  O   LYS A 192     6567   5233   7247    310   3171    339       O  
ATOM   1464  CB  LYS A 192     -18.995 -27.197 -46.020  1.00 55.28           C  
ANISOU 1464  CB  LYS A 192     7100   5829   8075    440   3346    306       C  
ATOM   1465  CG  LYS A 192     -20.252 -26.385 -45.778  1.00 80.68           C  
ANISOU 1465  CG  LYS A 192    10257   9001  11395    513   3548    352       C  
ATOM   1466  CD  LYS A 192     -20.874 -25.840 -47.069  1.00101.11           C  
ANISOU 1466  CD  LYS A 192    12671  11582  14164    556   3504    377       C  
ATOM   1467  CE  LYS A 192     -21.180 -26.880 -48.126  1.00114.83           C  
ANISOU 1467  CE  LYS A 192    14230  13355  16046    516   3345    438       C  
ATOM   1468  NZ  LYS A 192     -21.810 -26.268 -49.327  1.00124.92           N  
ANISOU 1468  NZ  LYS A 192    15348  14630  17485    552   3305    469       N  
ATOM   1469  N   HIS A 193     -15.806 -28.342 -45.187  1.00 46.70           N  
ANISOU 1469  N   HIS A 193     6320   4819   6606    297   3045    188       N  
ATOM   1470  CA  HIS A 193     -14.921 -29.455 -45.470  1.00 44.83           C  
ANISOU 1470  CA  HIS A 193     6071   4615   6349    243   2875    197       C  
ATOM   1471  C   HIS A 193     -13.728 -29.464 -44.539  1.00 47.56           C  
ANISOU 1471  C   HIS A 193     6593   4984   6496    198   2835    161       C  
ATOM   1472  O   HIS A 193     -13.410 -28.441 -43.939  1.00 48.12           O  
ANISOU 1472  O   HIS A 193     6795   5048   6439    202   2903    106       O  
ATOM   1473  CB  HIS A 193     -14.555 -29.451 -46.948  1.00 44.45           C  
ANISOU 1473  CB  HIS A 193     5911   4578   6401    246   2718    162       C  
ATOM   1474  CG  HIS A 193     -15.742 -29.635 -47.845  1.00 48.37           C  
ANISOU 1474  CG  HIS A 193     6230   5060   7091    273   2737    213       C  
ATOM   1475  ND1 HIS A 193     -16.523 -30.800 -47.796  1.00 51.04           N  
ANISOU 1475  ND1 HIS A 193     6466   5390   7536    252   2748    296       N  
ATOM   1476  CD2 HIS A 193     -16.235 -28.823 -48.810  1.00 49.33           C  
ANISOU 1476  CD2 HIS A 193     6257   5173   7313    311   2735    197       C  
ATOM   1477  CE1 HIS A 193     -17.493 -30.618 -48.680  1.00 50.45           C  
ANISOU 1477  CE1 HIS A 193     6241   5306   7620    276   2756    329       C  
ATOM   1478  NE2 HIS A 193     -17.356 -29.445 -49.323  1.00 50.09           N  
ANISOU 1478  NE2 HIS A 193     6193   5261   7576    313   2747    274       N  
ATOM   1479  N   LYS A 194     -13.154 -30.658 -44.313  1.00 43.02           N  
ANISOU 1479  N   LYS A 194     6020   4431   5895    151   2736    204       N  
ATOM   1480  CA  LYS A 194     -12.086 -30.871 -43.325  1.00 42.96           C  
ANISOU 1480  CA  LYS A 194     6165   4452   5708    101   2693    200       C  
ATOM   1481  C   LYS A 194     -10.650 -31.016 -43.901  1.00 46.51           C  
ANISOU 1481  C   LYS A 194     6634   4931   6108     70   2505    159       C  
ATOM   1482  O   LYS A 194      -9.775 -30.254 -43.474  1.00 43.85           O  
ANISOU 1482  O   LYS A 194     6424   4614   5624     47   2478    107       O  
ATOM   1483  CB  LYS A 194     -12.451 -32.094 -42.442  1.00 44.58           C  
ANISOU 1483  CB  LYS A 194     6373   4659   5908     71   2735    296       C  
ATOM   1484  CG  LYS A 194     -11.496 -32.400 -41.277  1.00 77.59           C  
ANISOU 1484  CG  LYS A 194    10708   8872   9901     15   2702    318       C  
ATOM   1485  CD  LYS A 194     -11.325 -31.236 -40.307  1.00102.02           C  
ANISOU 1485  CD  LYS A 194    13978  11974  12812      3   2804    265       C  
ATOM   1486  CE  LYS A 194     -10.935 -31.702 -38.922  1.00130.23           C  
ANISOU 1486  CE  LYS A 194    17694  15576  16213    -55   2830    318       C  
ATOM   1487  NZ  LYS A 194     -10.494 -30.573 -38.056  1.00146.36           N  
ANISOU 1487  NZ  LYS A 194    19930  17630  18051    -86   2890    252       N  
ATOM   1488  N   VAL A 195     -10.369 -31.971 -44.815  1.00 45.81           N  
ANISOU 1488  N   VAL A 195     6429   4845   6134     65   2379    181       N  
ATOM   1489  CA  VAL A 195      -8.956 -32.146 -45.221  1.00 45.47           C  
ANISOU 1489  CA  VAL A 195     6411   4828   6037     39   2218    151       C  
ATOM   1490  C   VAL A 195      -8.713 -31.633 -46.658  1.00 44.61           C  
ANISOU 1490  C   VAL A 195     6214   4717   6019     67   2133     84       C  
ATOM   1491  O   VAL A 195      -9.464 -31.886 -47.607  1.00 44.27           O  
ANISOU 1491  O   VAL A 195     6045   4654   6120     92   2132     87       O  
ATOM   1492  CB  VAL A 195      -8.351 -33.554 -44.917  1.00 50.81           C  
ANISOU 1492  CB  VAL A 195     7076   5512   6718      4   2131    223       C  
ATOM   1493  CG1 VAL A 195      -9.311 -34.456 -44.162  1.00 51.65           C  
ANISOU 1493  CG1 VAL A 195     7162   5598   6866     -4   2227    309       C  
ATOM   1494  CG2 VAL A 195      -7.662 -34.246 -46.087  1.00 49.78           C  
ANISOU 1494  CG2 VAL A 195     6847   5375   6690      8   1988    211       C  
ATOM   1495  N   TYR A 196      -7.656 -30.832 -46.748  1.00 38.23           N  
ANISOU 1495  N   TYR A 196     5480   3933   5111     56   2064     26       N  
ATOM   1496  CA  TYR A 196      -7.207 -30.140 -47.942  1.00 36.70           C  
ANISOU 1496  CA  TYR A 196     5237   3745   4963     77   1987    -41       C  
ATOM   1497  C   TYR A 196      -5.892 -30.706 -48.290  1.00 41.13           C  
ANISOU 1497  C   TYR A 196     5797   4331   5500     52   1842    -42       C  
ATOM   1498  O   TYR A 196      -4.987 -30.684 -47.453  1.00 41.08           O  
ANISOU 1498  O   TYR A 196     5890   4350   5370     16   1806    -28       O  
ATOM   1499  CB  TYR A 196      -7.088 -28.636 -47.672  1.00 37.69           C  
ANISOU 1499  CB  TYR A 196     5458   3871   4991     84   2043   -105       C  
ATOM   1500  CG  TYR A 196      -8.458 -28.044 -47.451  1.00 37.60           C  
ANISOU 1500  CG  TYR A 196     5432   3826   5029    122   2201   -102       C  
ATOM   1501  CD1 TYR A 196      -9.091 -28.149 -46.213  1.00 39.90           C  
ANISOU 1501  CD1 TYR A 196     5800   4103   5256    115   2330    -64       C  
ATOM   1502  CD2 TYR A 196      -9.194 -27.541 -48.515  1.00 37.13           C  
ANISOU 1502  CD2 TYR A 196     5263   3747   5097    167   2220   -122       C  
ATOM   1503  CE1 TYR A 196     -10.432 -27.807 -46.053  1.00 37.85           C  
ANISOU 1503  CE1 TYR A 196     5501   3810   5072    157   2483    -45       C  
ATOM   1504  CE2 TYR A 196     -10.518 -27.143 -48.353  1.00 38.72           C  
ANISOU 1504  CE2 TYR A 196     5422   3915   5373    207   2364    -99       C  
ATOM   1505  CZ  TYR A 196     -11.146 -27.320 -47.138  1.00 42.68           C  
ANISOU 1505  CZ  TYR A 196     5991   4401   5824    205   2497    -58       C  
ATOM   1506  OH  TYR A 196     -12.444 -26.906 -47.047  1.00 43.61           O  
ANISOU 1506  OH  TYR A 196     6054   4485   6031    251   2645    -31       O  
ATOM   1507  N   ALA A 197      -5.800 -31.265 -49.505  1.00 36.72           N  
ANISOU 1507  N   ALA A 197     5126   3765   5061     68   1762    -52       N  
ATOM   1508  CA  ALA A 197      -4.636 -31.979 -49.978  1.00 35.95           C  
ANISOU 1508  CA  ALA A 197     5007   3681   4972     54   1637    -47       C  
ATOM   1509  C   ALA A 197      -4.177 -31.505 -51.349  1.00 40.02           C  
ANISOU 1509  C   ALA A 197     5461   4204   5540     74   1561   -110       C  
ATOM   1510  O   ALA A 197      -4.964 -31.304 -52.262  1.00 38.70           O  
ANISOU 1510  O   ALA A 197     5217   4023   5465     97   1580   -137       O  
ATOM   1511  CB  ALA A 197      -4.938 -33.461 -50.040  1.00 36.31           C  
ANISOU 1511  CB  ALA A 197     4985   3699   5113     49   1622     13       C  
ATOM   1512  N   CYS A 198      -2.881 -31.432 -51.489  1.00 37.66           N  
ANISOU 1512  N   CYS A 198     5191   3930   5187     62   1469   -122       N  
ATOM   1513  CA  CYS A 198      -2.207 -31.073 -52.693  1.00 37.91           C  
ANISOU 1513  CA  CYS A 198     5176   3975   5254     76   1392   -174       C  
ATOM   1514  C   CYS A 198      -1.403 -32.319 -53.105  1.00 37.76           C  
ANISOU 1514  C   CYS A 198     5108   3947   5291     75   1310   -144       C  
ATOM   1515  O   CYS A 198      -0.559 -32.736 -52.333  1.00 37.50           O  
ANISOU 1515  O   CYS A 198     5120   3926   5202     56   1273    -97       O  
ATOM   1516  CB  CYS A 198      -1.288 -29.880 -52.404  1.00 40.83           C  
ANISOU 1516  CB  CYS A 198     5625   4377   5510     61   1362   -207       C  
ATOM   1517  SG  CYS A 198      -0.238 -29.492 -53.770  1.00 47.01           S  
ANISOU 1517  SG  CYS A 198     6354   5181   6326     75   1262   -256       S  
ATOM   1518  N   GLU A 199      -1.685 -32.939 -54.259  1.00 34.31           N  
ANISOU 1518  N   GLU A 199     4586   3487   4965     92   1286   -166       N  
ATOM   1519  CA  GLU A 199      -0.941 -34.113 -54.748  1.00 33.26           C  
ANISOU 1519  CA  GLU A 199     4410   3332   4896     97   1222   -148       C  
ATOM   1520  C   GLU A 199      -0.080 -33.753 -55.928  1.00 34.11           C  
ANISOU 1520  C   GLU A 199     4487   3456   5018    113   1158   -203       C  
ATOM   1521  O   GLU A 199      -0.563 -33.196 -56.892  1.00 32.17           O  
ANISOU 1521  O   GLU A 199     4206   3215   4803    122   1161   -258       O  
ATOM   1522  CB  GLU A 199      -1.830 -35.284 -55.111  1.00 35.31           C  
ANISOU 1522  CB  GLU A 199     4609   3541   5266     96   1247   -132       C  
ATOM   1523  CG  GLU A 199      -1.002 -36.507 -55.504  1.00 41.48           C  
ANISOU 1523  CG  GLU A 199     5362   4287   6110    102   1193   -114       C  
ATOM   1524  CD  GLU A 199      -1.783 -37.773 -55.719  1.00 52.09           C  
ANISOU 1524  CD  GLU A 199     6661   5569   7561     93   1215    -93       C  
ATOM   1525  OE1 GLU A 199      -2.954 -37.795 -55.312  1.00 37.40           O  
ANISOU 1525  OE1 GLU A 199     4792   3700   5720     77   1272    -73       O  
ATOM   1526  OE2 GLU A 199      -1.239 -38.746 -56.281  1.00 51.87           O  
ANISOU 1526  OE2 GLU A 199     6608   5500   7602    100   1181    -96       O  
ATOM   1527  N   VAL A 200       1.187 -34.128 -55.863  1.00 32.18           N  
ANISOU 1527  N   VAL A 200     4249   3219   4758    117   1100   -179       N  
ATOM   1528  CA  VAL A 200       2.195 -33.748 -56.831  1.00 32.33           C  
ANISOU 1528  CA  VAL A 200     4245   3258   4781    132   1043   -220       C  
ATOM   1529  C   VAL A 200       2.775 -34.933 -57.547  1.00 34.69           C  
ANISOU 1529  C   VAL A 200     4494   3519   5168    153   1014   -214       C  
ATOM   1530  O   VAL A 200       3.177 -35.897 -56.910  1.00 36.49           O  
ANISOU 1530  O   VAL A 200     4723   3721   5420    154   1007   -151       O  
ATOM   1531  CB  VAL A 200       3.288 -32.883 -56.137  1.00 34.99           C  
ANISOU 1531  CB  VAL A 200     4634   3643   5016    118   1003   -197       C  
ATOM   1532  CG1 VAL A 200       4.458 -32.615 -57.075  1.00 35.50           C  
ANISOU 1532  CG1 VAL A 200     4665   3730   5095    135    944   -222       C  
ATOM   1533  CG2 VAL A 200       2.679 -31.576 -55.649  1.00 33.51           C  
ANISOU 1533  CG2 VAL A 200     4504   3483   4744     99   1041   -225       C  
ATOM   1534  N   THR A 201       2.844 -34.841 -58.880  1.00 32.04           N  
ANISOU 1534  N   THR A 201     4119   3179   4876    168   1001   -278       N  
ATOM   1535  CA  THR A 201       3.429 -35.874 -59.725  1.00 33.86           C  
ANISOU 1535  CA  THR A 201     4312   3368   5186    189    984   -290       C  
ATOM   1536  C   THR A 201       4.547 -35.215 -60.552  1.00 34.78           C  
ANISOU 1536  C   THR A 201     4416   3520   5279    209    947   -324       C  
ATOM   1537  O   THR A 201       4.393 -34.103 -61.036  1.00 35.91           O  
ANISOU 1537  O   THR A 201     4565   3706   5375    203    940   -369       O  
ATOM   1538  CB  THR A 201       2.381 -36.682 -60.565  1.00 43.56           C  
ANISOU 1538  CB  THR A 201     5512   4543   6496    181   1011   -335       C  
ATOM   1539  OG1 THR A 201       1.787 -35.878 -61.540  1.00 54.59           O  
ANISOU 1539  OG1 THR A 201     6895   5967   7879    171   1008   -402       O  
ATOM   1540  CG2 THR A 201       1.311 -37.254 -59.771  1.00 37.21           C  
ANISOU 1540  CG2 THR A 201     4712   3708   5720    159   1047   -296       C  
ATOM   1541  N   HIS A 202       5.705 -35.853 -60.575  1.00 31.80           N  
ANISOU 1541  N   HIS A 202     4021   3127   4935    233    927   -289       N  
ATOM   1542  CA  HIS A 202       6.896 -35.357 -61.246  1.00 31.09           C  
ANISOU 1542  CA  HIS A 202     3911   3069   4833    255    897   -302       C  
ATOM   1543  C   HIS A 202       7.779 -36.498 -61.513  1.00 37.49           C  
ANISOU 1543  C   HIS A 202     4688   3831   5725    291    902   -271       C  
ATOM   1544  O   HIS A 202       7.761 -37.439 -60.753  1.00 40.76           O  
ANISOU 1544  O   HIS A 202     5102   4204   6182    295    910   -210       O  
ATOM   1545  CB  HIS A 202       7.626 -34.326 -60.367  1.00 31.79           C  
ANISOU 1545  CB  HIS A 202     4022   3220   4837    238    856   -254       C  
ATOM   1546  CG  HIS A 202       8.736 -33.612 -61.064  1.00 33.19           C  
ANISOU 1546  CG  HIS A 202     4174   3437   4998    252    824   -267       C  
ATOM   1547  ND1 HIS A 202      10.047 -34.024 -60.931  1.00 34.68           N  
ANISOU 1547  ND1 HIS A 202     4327   3628   5220    274    795   -205       N  
ATOM   1548  CD2 HIS A 202       8.705 -32.497 -61.827  1.00 33.90           C  
ANISOU 1548  CD2 HIS A 202     4268   3567   5047    245    817   -326       C  
ATOM   1549  CE1 HIS A 202      10.761 -33.197 -61.679  1.00 33.15           C  
ANISOU 1549  CE1 HIS A 202     4114   3475   5007    280    777   -232       C  
ATOM   1550  NE2 HIS A 202       9.981 -32.296 -62.281  1.00 33.18           N  
ANISOU 1550  NE2 HIS A 202     4143   3500   4966    263    789   -307       N  
ATOM   1551  N   GLN A 203       8.606 -36.404 -62.548  1.00 36.35           N  
ANISOU 1551  N   GLN A 203     4516   3691   5604    319    901   -306       N  
ATOM   1552  CA  GLN A 203       9.572 -37.431 -62.931  1.00 35.94           C  
ANISOU 1552  CA  GLN A 203     4428   3587   5638    364    920   -280       C  
ATOM   1553  C   GLN A 203      10.551 -37.788 -61.792  1.00 39.51           C  
ANISOU 1553  C   GLN A 203     4856   4044   6110    378    890   -163       C  
ATOM   1554  O   GLN A 203      10.936 -38.933 -61.675  1.00 39.88           O  
ANISOU 1554  O   GLN A 203     4880   4029   6245    411    914   -117       O  
ATOM   1555  CB  GLN A 203      10.370 -36.953 -64.155  1.00 36.77           C  
ANISOU 1555  CB  GLN A 203     4511   3715   5744    389    928   -331       C  
ATOM   1556  CG  GLN A 203      11.107 -38.083 -64.854  1.00 45.46           C  
ANISOU 1556  CG  GLN A 203     5584   4745   6943    440    976   -334       C  
ATOM   1557  CD  GLN A 203      11.983 -37.592 -65.972  1.00 61.31           C  
ANISOU 1557  CD  GLN A 203     7570   6780   8947    468    992   -374       C  
ATOM   1558  OE1 GLN A 203      11.780 -36.509 -66.546  1.00 61.68           O  
ANISOU 1558  OE1 GLN A 203     7629   6886   8921    444    974   -427       O  
ATOM   1559  NE2 GLN A 203      12.968 -38.396 -66.315  1.00 58.71           N  
ANISOU 1559  NE2 GLN A 203     7204   6401   8701    522   1035   -346       N  
ATOM   1560  N   GLY A 204      10.936 -36.823 -60.970  1.00 36.53           N  
ANISOU 1560  N   GLY A 204     4489   3739   5653    350    838   -113       N  
ATOM   1561  CA  GLY A 204      11.832 -37.070 -59.845  1.00 36.33           C  
ANISOU 1561  CA  GLY A 204     4443   3730   5629    349    793      5       C  
ATOM   1562  C   GLY A 204      11.197 -37.822 -58.687  1.00 39.04           C  
ANISOU 1562  C   GLY A 204     4815   4044   5976    330    795     69       C  
ATOM   1563  O   GLY A 204      11.895 -38.158 -57.732  1.00 38.92           O  
ANISOU 1563  O   GLY A 204     4784   4040   5965    326    756    177       O  
ATOM   1564  N   LEU A 205       9.866 -38.022 -58.718  1.00 35.14           N  
ANISOU 1564  N   LEU A 205     4360   3518   5474    312    836     11       N  
ATOM   1565  CA  LEU A 205       9.115 -38.693 -57.667  1.00 36.22           C  
ANISOU 1565  CA  LEU A 205     4526   3627   5611    290    849     65       C  
ATOM   1566  C   LEU A 205       8.545 -40.037 -58.169  1.00 39.51           C  
ANISOU 1566  C   LEU A 205     4924   3947   6140    316    904     45       C  
ATOM   1567  O   LEU A 205       7.628 -40.038 -58.980  1.00 41.14           O  
ANISOU 1567  O   LEU A 205     5142   4128   6363    309    940    -46       O  
ATOM   1568  CB  LEU A 205       7.958 -37.794 -57.222  1.00 36.01           C  
ANISOU 1568  CB  LEU A 205     4556   3638   5488    243    860     20       C  
ATOM   1569  CG  LEU A 205       8.284 -36.482 -56.633  1.00 38.43           C  
ANISOU 1569  CG  LEU A 205     4901   4023   5677    209    819     28       C  
ATOM   1570  CD1 LEU A 205       7.030 -35.672 -56.467  1.00 38.32           C  
ANISOU 1570  CD1 LEU A 205     4938   4026   5594    178    856    -34       C  
ATOM   1571  CD2 LEU A 205       8.985 -36.646 -55.349  1.00 40.87           C  
ANISOU 1571  CD2 LEU A 205     5228   4360   5941    185    773    138       C  
ATOM   1572  N   SER A 206       9.106 -41.162 -57.730  1.00 35.27           N  
ANISOU 1572  N   SER A 206     4360   3357   5685    343    907    131       N  
ATOM   1573  CA  SER A 206       8.604 -42.515 -58.115  1.00 36.74           C  
ANISOU 1573  CA  SER A 206     4535   3438   5985    365    962    119       C  
ATOM   1574  C   SER A 206       7.122 -42.671 -57.852  1.00 39.11           C  
ANISOU 1574  C   SER A 206     4874   3718   6269    323    991     82       C  
ATOM   1575  O   SER A 206       6.397 -43.171 -58.689  1.00 38.13           O  
ANISOU 1575  O   SER A 206     4752   3533   6201    320   1030      6       O  
ATOM   1576  CB  SER A 206       9.333 -43.580 -57.320  1.00 41.86           C  
ANISOU 1576  CB  SER A 206     5154   4039   6712    393    956    244       C  
ATOM   1577  OG  SER A 206      10.732 -43.404 -57.479  1.00 53.80           O  
ANISOU 1577  OG  SER A 206     6619   5576   8248    433    925    296       O  
ATOM   1578  N   SER A 207       6.687 -42.207 -56.681  1.00 35.61           N  
ANISOU 1578  N   SER A 207     4461   3326   5742    286    972    139       N  
ATOM   1579  CA  SER A 207       5.310 -42.216 -56.269  1.00 34.22           C  
ANISOU 1579  CA  SER A 207     4317   3143   5542    246   1005    121       C  
ATOM   1580  C   SER A 207       4.964 -40.777 -55.999  1.00 36.38           C  
ANISOU 1580  C   SER A 207     4626   3505   5692    216    990     85       C  
ATOM   1581  O   SER A 207       5.828 -40.003 -55.581  1.00 36.52           O  
ANISOU 1581  O   SER A 207     4656   3586   5635    214    947    116       O  
ATOM   1582  CB  SER A 207       5.103 -43.104 -55.031  1.00 33.97           C  
ANISOU 1582  CB  SER A 207     4297   3081   5530    234   1014    232       C  
ATOM   1583  OG  SER A 207       4.883 -44.443 -55.421  1.00 43.90           O  
ANISOU 1583  OG  SER A 207     5528   4236   6914    252   1049    240       O  
ATOM   1584  N   PRO A 208       3.725 -40.376 -56.251  1.00 34.39           N  
ANISOU 1584  N   PRO A 208     4388   3257   5423    191   1026     22       N  
ATOM   1585  CA  PRO A 208       3.339 -38.975 -55.971  1.00 33.57           C  
ANISOU 1585  CA  PRO A 208     4318   3226   5210    168   1024    -10       C  
ATOM   1586  C   PRO A 208       3.503 -38.576 -54.506  1.00 37.70           C  
ANISOU 1586  C   PRO A 208     4894   3795   5634    143   1018     68       C  
ATOM   1587  O   PRO A 208       3.348 -39.393 -53.609  1.00 37.86           O  
ANISOU 1587  O   PRO A 208     4926   3790   5669    133   1031    146       O  
ATOM   1588  CB  PRO A 208       1.862 -38.927 -56.349  1.00 36.13           C  
ANISOU 1588  CB  PRO A 208     4635   3530   5562    150   1074    -63       C  
ATOM   1589  CG  PRO A 208       1.566 -40.175 -57.080  1.00 40.90           C  
ANISOU 1589  CG  PRO A 208     5202   4056   6283    156   1086    -79       C  
ATOM   1590  CD  PRO A 208       2.606 -41.168 -56.798  1.00 37.30           C  
ANISOU 1590  CD  PRO A 208     4737   3559   5876    181   1068    -17       C  
ATOM   1591  N   VAL A 209       3.681 -37.301 -54.276  1.00 36.00           N  
ANISOU 1591  N   VAL A 209     4718   3643   5317    127   1003     42       N  
ATOM   1592  CA  VAL A 209       3.793 -36.719 -52.937  1.00 37.31           C  
ANISOU 1592  CA  VAL A 209     4954   3856   5366     92    999     97       C  
ATOM   1593  C   VAL A 209       2.511 -35.950 -52.630  1.00 38.41           C  
ANISOU 1593  C   VAL A 209     5136   4006   5453     73   1068     53       C  
ATOM   1594  O   VAL A 209       2.101 -35.134 -53.427  1.00 37.07           O  
ANISOU 1594  O   VAL A 209     4953   3844   5287     82   1084    -24       O  
ATOM   1595  CB  VAL A 209       5.039 -35.798 -52.810  1.00 41.20           C  
ANISOU 1595  CB  VAL A 209     5471   4409   5776     79    930    103       C  
ATOM   1596  CG1 VAL A 209       5.001 -34.994 -51.530  1.00 41.43           C  
ANISOU 1596  CG1 VAL A 209     5591   4486   5665     30    929    134       C  
ATOM   1597  CG2 VAL A 209       6.313 -36.628 -52.874  1.00 42.17           C  
ANISOU 1597  CG2 VAL A 209     5546   4523   5954     98    867    175       C  
ATOM   1598  N   THR A 210       1.919 -36.196 -51.464  1.00 36.04           N  
ANISOU 1598  N   THR A 210     4885   3705   5105     48   1112    110       N  
ATOM   1599  CA  THR A 210       0.729 -35.486 -50.995  1.00 35.29           C  
ANISOU 1599  CA  THR A 210     4834   3616   4958     33   1194     82       C  
ATOM   1600  C   THR A 210       1.062 -34.728 -49.708  1.00 38.20           C  
ANISOU 1600  C   THR A 210     5306   4031   5176     -6   1198    114       C  
ATOM   1601  O   THR A 210       1.701 -35.279 -48.810  1.00 36.14           O  
ANISOU 1601  O   THR A 210     5080   3784   4866    -31   1161    194       O  
ATOM   1602  CB  THR A 210      -0.451 -36.435 -50.771  1.00 41.83           C  
ANISOU 1602  CB  THR A 210     5633   4398   5865     35   1262    116       C  
ATOM   1603  OG1 THR A 210      -0.734 -37.131 -51.988  1.00 43.22           O  
ANISOU 1603  OG1 THR A 210     5721   4528   6171     59   1249     81       O  
ATOM   1604  CG2 THR A 210      -1.705 -35.696 -50.316  1.00 40.47           C  
ANISOU 1604  CG2 THR A 210     5493   4231   5652     27   1358     94       C  
ATOM   1605  N   LYS A 211       0.748 -33.417 -49.698  1.00 36.11           N  
ANISOU 1605  N   LYS A 211     5093   3790   4836    -13   1234     49       N  
ATOM   1606  CA  LYS A 211       0.833 -32.569 -48.531  1.00 36.17           C  
ANISOU 1606  CA  LYS A 211     5215   3831   4695    -55   1260     58       C  
ATOM   1607  C   LYS A 211      -0.617 -32.179 -48.240  1.00 41.84           C  
ANISOU 1607  C   LYS A 211     5958   4526   5414    -44   1385     30       C  
ATOM   1608  O   LYS A 211      -1.374 -31.825 -49.163  1.00 41.05           O  
ANISOU 1608  O   LYS A 211     5796   4403   5399     -9   1426    -26       O  
ATOM   1609  CB  LYS A 211       1.759 -31.350 -48.730  1.00 36.49           C  
ANISOU 1609  CB  LYS A 211     5304   3910   4652    -74   1202      7       C  
ATOM   1610  CG  LYS A 211       3.214 -31.683 -49.000  1.00 38.85           C  
ANISOU 1610  CG  LYS A 211     5568   4236   4956    -85   1081     44       C  
ATOM   1611  CD  LYS A 211       3.847 -32.520 -47.932  1.00 40.81           C  
ANISOU 1611  CD  LYS A 211     5849   4504   5153   -121   1032    146       C  
ATOM   1612  CE  LYS A 211       5.285 -32.794 -48.247  1.00 48.14           C  
ANISOU 1612  CE  LYS A 211     6728   5458   6103   -125    916    192       C  
ATOM   1613  NZ  LYS A 211       6.044 -33.199 -47.039  1.00 59.30           N  
ANISOU 1613  NZ  LYS A 211     8195   6909   7427   -179    852    296       N  
ATOM   1614  N   SER A 212      -0.996 -32.312 -46.964  1.00 39.33           N  
ANISOU 1614  N   SER A 212     5725   4214   5006    -76   1446     78       N  
ATOM   1615  CA  SER A 212      -2.328 -32.032 -46.441  1.00 39.86           C  
ANISOU 1615  CA  SER A 212     5824   4258   5063    -67   1580     71       C  
ATOM   1616  C   SER A 212      -2.304 -31.230 -45.175  1.00 44.03           C  
ANISOU 1616  C   SER A 212     6499   4808   5422   -110   1638     68       C  
ATOM   1617  O   SER A 212      -1.317 -31.228 -44.466  1.00 43.50           O  
ANISOU 1617  O   SER A 212     6510   4777   5240   -159   1567    101       O  
ATOM   1618  CB  SER A 212      -3.031 -33.346 -46.083  1.00 43.00           C  
ANISOU 1618  CB  SER A 212     6172   4629   5537    -63   1621    148       C  
ATOM   1619  OG  SER A 212      -3.659 -33.909 -47.217  1.00 65.47           O  
ANISOU 1619  OG  SER A 212     8892   7438   8546    -24   1621    133       O  
ATOM   1620  N   PHE A 213      -3.472 -30.699 -44.815  1.00 42.02           N  
ANISOU 1620  N   PHE A 213     6279   4530   5158    -94   1775     44       N  
ATOM   1621  CA  PHE A 213      -3.779 -30.103 -43.496  1.00 41.61           C  
ANISOU 1621  CA  PHE A 213     6374   4485   4952   -130   1875     45       C  
ATOM   1622  C   PHE A 213      -5.283 -30.274 -43.215  1.00 47.55           C  
ANISOU 1622  C   PHE A 213     7100   5199   5767    -94   2034     62       C  
ATOM   1623  O   PHE A 213      -6.076 -30.439 -44.142  1.00 44.62           O  
ANISOU 1623  O   PHE A 213     6606   4798   5549    -43   2065     51       O  
ATOM   1624  CB  PHE A 213      -3.328 -28.644 -43.325  1.00 42.49           C  
ANISOU 1624  CB  PHE A 213     6599   4604   4942   -152   1883    -38       C  
ATOM   1625  CG  PHE A 213      -4.120 -27.615 -44.087  1.00 41.87           C  
ANISOU 1625  CG  PHE A 213     6483   4486   4938    -99   1971   -115       C  
ATOM   1626  CD1 PHE A 213      -5.330 -27.147 -43.599  1.00 43.84           C  
ANISOU 1626  CD1 PHE A 213     6773   4699   5186    -72   2138   -129       C  
ATOM   1627  CD2 PHE A 213      -3.718 -27.205 -45.348  1.00 41.14           C  
ANISOU 1627  CD2 PHE A 213     6303   4393   4936    -70   1890   -163       C  
ATOM   1628  CE1 PHE A 213      -6.137 -26.320 -44.364  1.00 44.56           C  
ANISOU 1628  CE1 PHE A 213     6803   4750   5375    -14   2219   -181       C  
ATOM   1629  CE2 PHE A 213      -4.558 -26.424 -46.140  1.00 42.88           C  
ANISOU 1629  CE2 PHE A 213     6464   4577   5251    -16   1966   -214       C  
ATOM   1630  CZ  PHE A 213      -5.731 -25.931 -45.621  1.00 41.96           C  
ANISOU 1630  CZ  PHE A 213     6385   4424   5136     12   2127   -222       C  
ATOM   1631  N   ASN A 214      -5.663 -30.323 -41.932  1.00 48.98           N  
ANISOU 1631  N   ASN A 214     7393   5385   5832   -125   2131     99       N  
ATOM   1632  CA  ASN A 214      -7.059 -30.365 -41.540  1.00 49.87           C  
ANISOU 1632  CA  ASN A 214     7493   5463   5991    -93   2299    118       C  
ATOM   1633  C   ASN A 214      -7.441 -28.976 -41.084  1.00 55.04           C  
ANISOU 1633  C   ASN A 214     8266   6100   6547    -87   2424     44       C  
ATOM   1634  O   ASN A 214      -6.752 -28.415 -40.236  1.00 55.72           O  
ANISOU 1634  O   ASN A 214     8508   6207   6454   -141   2416     19       O  
ATOM   1635  CB  ASN A 214      -7.286 -31.359 -40.412  1.00 59.11           C  
ANISOU 1635  CB  ASN A 214     8711   6646   7100   -128   2343    212       C  
ATOM   1636  CG  ASN A 214      -6.985 -32.786 -40.817  1.00 78.03           C  
ANISOU 1636  CG  ASN A 214    10993   9048   9609   -130   2235    292       C  
ATOM   1637  OD1 ASN A 214      -7.249 -33.190 -41.944  1.00 63.89           O  
ANISOU 1637  OD1 ASN A 214     9059   7231   7985    -90   2194    285       O  
ATOM   1638  ND2 ASN A 214      -6.352 -33.570 -39.953  1.00 71.69           N  
ANISOU 1638  ND2 ASN A 214    10250   8273   8715   -180   2178    370       N  
ATOM   1639  N   ARG A 215      -8.486 -28.382 -41.685  1.00 53.23           N  
ANISOU 1639  N   ARG A 215     7963   5828   6433    -24   2533      9       N  
ATOM   1640  CA  ARG A 215      -9.003 -27.070 -41.263  1.00 54.73           C  
ANISOU 1640  CA  ARG A 215     8258   5984   6553     -5   2681    -58       C  
ATOM   1641  C   ARG A 215      -9.406 -27.170 -39.784  1.00 65.42           C  
ANISOU 1641  C   ARG A 215     9757   7337   7761    -38   2819    -27       C  
ATOM   1642  O   ARG A 215     -10.080 -28.130 -39.390  1.00 64.33           O  
ANISOU 1642  O   ARG A 215     9569   7202   7673    -32   2877     54       O  
ATOM   1643  CB  ARG A 215     -10.244 -26.685 -42.080  1.00 51.21           C  
ANISOU 1643  CB  ARG A 215     7679   5492   6286     75   2790    -65       C  
ATOM   1644  CG  ARG A 215     -10.898 -25.336 -41.673  1.00 55.90           C  
ANISOU 1644  CG  ARG A 215     8367   6036   6836    110   2966   -125       C  
ATOM   1645  CD  ARG A 215     -12.260 -25.109 -42.317  1.00 53.29           C  
ANISOU 1645  CD  ARG A 215     7892   5661   6695    192   3090   -101       C  
ATOM   1646  NE  ARG A 215     -13.116 -26.291 -42.211  1.00 56.95           N  
ANISOU 1646  NE  ARG A 215     8241   6132   7267    203   3129     -5       N  
ATOM   1647  CZ  ARG A 215     -13.724 -26.719 -41.110  1.00 68.95           C  
ANISOU 1647  CZ  ARG A 215     9820   7645   8731    194   3264     47       C  
ATOM   1648  NH1 ARG A 215     -14.457 -27.828 -41.138  1.00 66.25           N  
ANISOU 1648  NH1 ARG A 215     9359   7310   8506    201   3281    139       N  
ATOM   1649  NH2 ARG A 215     -13.605 -26.046 -39.969  1.00 58.62           N  
ANISOU 1649  NH2 ARG A 215     8700   6324   7250    174   3383      8       N  
ATOM   1650  N   GLY A 216      -8.984 -26.193 -38.990  1.00 68.27           N  
ANISOU 1650  N   GLY A 216    10302   7694   7944    -77   2869    -91       N  
ATOM   1651  CA  GLY A 216      -9.284 -26.178 -37.557  1.00 72.63           C  
ANISOU 1651  CA  GLY A 216    11021   8248   8329   -118   3001    -74       C  
ATOM   1652  C   GLY A 216      -8.147 -26.657 -36.673  1.00 80.37           C  
ANISOU 1652  C   GLY A 216    12130   9288   9119   -216   2878    -42       C  
ATOM   1653  O   GLY A 216      -8.150 -26.381 -35.469  1.00 82.14           O  
ANISOU 1653  O   GLY A 216    12534   9519   9157   -270   2966    -49       O  
ATOM   1654  N   GLU A 217      -7.152 -27.356 -37.268  1.00 76.83           N  
ANISOU 1654  N   GLU A 217    11593   8884   8716   -241   2675     -5       N  
ATOM   1655  CA  GLU A 217      -5.948 -27.826 -36.593  1.00 76.95           C  
ANISOU 1655  CA  GLU A 217    11700   8959   8577   -330   2529     38       C  
ATOM   1656  C   GLU A 217      -4.774 -26.903 -36.950  1.00 81.01           C  
ANISOU 1656  C   GLU A 217    12276   9490   9013   -373   2399    -38       C  
ATOM   1657  O   GLU A 217      -3.632 -27.349 -36.903  1.00 82.04           O  
ANISOU 1657  O   GLU A 217    12404   9672   9094   -428   2228      4       O  
ATOM   1658  CB  GLU A 217      -5.659 -29.276 -37.007  1.00 77.70           C  
ANISOU 1658  CB  GLU A 217    11646   9084   8794   -323   2405    142       C  
ATOM   1659  CG  GLU A 217      -6.794 -30.216 -36.635  1.00 89.44           C  
ANISOU 1659  CG  GLU A 217    13071  10551  10359   -290   2527    223       C  
ATOM   1660  CD  GLU A 217      -6.519 -31.691 -36.842  1.00108.58           C  
ANISOU 1660  CD  GLU A 217    15375  12996  12886   -293   2417    331       C  
ATOM   1661  OE1 GLU A 217      -5.407 -32.034 -37.309  1.00 96.54           O  
ANISOU 1661  OE1 GLU A 217    13805  11498  11376   -314   2245    346       O  
ATOM   1662  OE2 GLU A 217      -7.438 -32.503 -36.583  1.00101.60           O  
ANISOU 1662  OE2 GLU A 217    14432  12092  12077   -270   2509    402       O  
ATOM   1663  N   CYS A 218      -5.053 -25.605 -37.269  1.00 77.15           N  
ANISOU 1663  N   CYS A 218    11841   8955   8517   -348   2483   -143       N  
ATOM   1664  CA  CYS A 218      -4.060 -24.599 -37.656  1.00 93.00           C  
ANISOU 1664  CA  CYS A 218    13908  10968  10462   -385   2379   -222       C  
ATOM   1665  C   CYS A 218      -4.098 -23.451 -36.644  1.00131.40           C  
ANISOU 1665  C   CYS A 218    18997  15804  15123   -443   2486   -303       C  
ATOM   1666  O   CYS A 218      -3.287 -22.528 -36.721  1.00 99.36           O  
ANISOU 1666  O   CYS A 218    15027  11745  10978   -494   2413   -372       O  
ATOM   1667  CB  CYS A 218      -4.340 -24.092 -39.074  1.00 91.68           C  
ANISOU 1667  CB  CYS A 218    13591  10760  10483   -302   2372   -274       C  
ATOM   1668  SG  CYS A 218      -4.486 -25.397 -40.335  1.00 93.71           S  
ANISOU 1668  SG  CYS A 218    13594  11035  10977   -234   2271   -196       S  
TER    1669      CYS A 218                                                      
ATOM   1670  N   GLN B   1      29.748   5.028 -66.741  1.00 65.32           N  
ANISOU 1670  N   GLN B   1     7824   7201   9793   -857   -506    205       N  
ATOM   1671  CA  GLN B   1      28.594   5.273 -65.876  1.00 62.58           C  
ANISOU 1671  CA  GLN B   1     7623   6842   9313   -849   -519    102       C  
ATOM   1672  C   GLN B   1      27.382   5.712 -66.755  1.00 56.85           C  
ANISOU 1672  C   GLN B   1     6922   6153   8526   -801   -407     35       C  
ATOM   1673  O   GLN B   1      26.628   6.600 -66.367  1.00 53.72           O  
ANISOU 1673  O   GLN B   1     6624   5727   8062   -805   -430    -27       O  
ATOM   1674  CB  GLN B   1      28.988   6.345 -64.829  1.00 65.16           C  
ANISOU 1674  CB  GLN B   1     8036   7087   9637   -912   -672    102       C  
ATOM   1675  CG  GLN B   1      28.271   6.219 -63.494  1.00 86.97           C  
ANISOU 1675  CG  GLN B   1    10951   9820  12274   -916   -720     23       C  
ATOM   1676  CD  GLN B   1      28.208   7.570 -62.799  1.00113.61           C  
ANISOU 1676  CD  GLN B   1    14437  13115  15615   -959   -830     -6       C  
ATOM   1677  OE1 GLN B   1      27.129   8.143 -62.589  1.00111.99           O  
ANISOU 1677  OE1 GLN B   1    14339  12899  15312   -934   -793    -88       O  
ATOM   1678  NE2 GLN B   1      29.366   8.151 -62.498  1.00102.59           N  
ANISOU 1678  NE2 GLN B   1    13015  11659  14306  -1025   -965     67       N  
ATOM   1679  N   VAL B   2      27.181   5.047 -67.921  1.00 50.58           N  
ANISOU 1679  N   VAL B   2     6044   5421   7755   -755   -284     50       N  
ATOM   1680  CA  VAL B   2      26.067   5.346 -68.832  1.00 48.18           C  
ANISOU 1680  CA  VAL B   2     5754   5154   7400   -711   -179     -3       C  
ATOM   1681  C   VAL B   2      24.791   4.813 -68.230  1.00 46.46           C  
ANISOU 1681  C   VAL B   2     5635   4957   7062   -678   -134    -92       C  
ATOM   1682  O   VAL B   2      24.705   3.631 -67.934  1.00 44.35           O  
ANISOU 1682  O   VAL B   2     5365   4720   6767   -659   -102    -99       O  
ATOM   1683  CB  VAL B   2      26.253   4.786 -70.264  1.00 51.25           C  
ANISOU 1683  CB  VAL B   2     6036   5595   7841   -675    -68     40       C  
ATOM   1684  CG1 VAL B   2      25.007   5.043 -71.125  1.00 50.05           C  
ANISOU 1684  CG1 VAL B   2     5913   5478   7626   -634     29    -18       C  
ATOM   1685  CG2 VAL B   2      27.493   5.375 -70.909  1.00 51.22           C  
ANISOU 1685  CG2 VAL B   2     5932   5569   7962   -702   -101    134       C  
ATOM   1686  N   GLN B   3      23.818   5.692 -68.044  1.00 41.03           N  
ANISOU 1686  N   GLN B   3     5031   4250   6309   -671   -131   -154       N  
ATOM   1687  CA  GLN B   3      22.523   5.328 -67.506  1.00 41.33           C  
ANISOU 1687  CA  GLN B   3     5161   4303   6239   -636    -80   -233       C  
ATOM   1688  C   GLN B   3      21.375   5.966 -68.269  1.00 41.19           C  
ANISOU 1688  C   GLN B   3     5161   4302   6187   -604     -3   -276       C  
ATOM   1689  O   GLN B   3      21.417   7.149 -68.616  1.00 38.74           O  
ANISOU 1689  O   GLN B   3     4854   3961   5904   -620    -28   -271       O  
ATOM   1690  CB  GLN B   3      22.424   5.782 -66.047  1.00 44.74           C  
ANISOU 1690  CB  GLN B   3     5713   4676   6611   -662   -172   -272       C  
ATOM   1691  CG  GLN B   3      23.415   5.108 -65.114  1.00 58.42           C  
ANISOU 1691  CG  GLN B   3     7447   6388   8362   -697   -258   -236       C  
ATOM   1692  CD  GLN B   3      23.081   5.469 -63.684  1.00 86.86           C  
ANISOU 1692  CD  GLN B   3    11189   9933  11879   -714   -334   -286       C  
ATOM   1693  OE1 GLN B   3      22.047   5.060 -63.141  1.00 88.94           O  
ANISOU 1693  OE1 GLN B   3    11535  10209  12049   -679   -281   -348       O  
ATOM   1694  NE2 GLN B   3      23.866   6.332 -63.078  1.00 83.42           N  
ANISOU 1694  NE2 GLN B   3    10794   9430  11470   -767   -455   -263       N  
ATOM   1695  N   LEU B   4      20.332   5.181 -68.493  1.00 37.99           N  
ANISOU 1695  N   LEU B   4     4769   3941   5724   -560     88   -316       N  
ATOM   1696  CA  LEU B   4      19.092   5.638 -69.077  1.00 36.06           C  
ANISOU 1696  CA  LEU B   4     4550   3711   5441   -528    160   -358       C  
ATOM   1697  C   LEU B   4      17.987   5.284 -68.044  1.00 38.57           C  
ANISOU 1697  C   LEU B   4     4967   4023   5667   -502    181   -420       C  
ATOM   1698  O   LEU B   4      17.739   4.125 -67.815  1.00 37.97           O  
ANISOU 1698  O   LEU B   4     4887   3979   5560   -481    217   -429       O  
ATOM   1699  CB  LEU B   4      18.835   4.974 -70.432  1.00 35.57           C  
ANISOU 1699  CB  LEU B   4     4406   3707   5402   -499    251   -337       C  
ATOM   1700  CG  LEU B   4      19.819   5.265 -71.569  1.00 39.12           C  
ANISOU 1700  CG  LEU B   4     4761   4166   5938   -515    253   -274       C  
ATOM   1701  CD1 LEU B   4      19.359   4.569 -72.835  1.00 38.04           C  
ANISOU 1701  CD1 LEU B   4     4572   4081   5801   -482    350   -265       C  
ATOM   1702  CD2 LEU B   4      19.946   6.752 -71.833  1.00 42.62           C  
ANISOU 1702  CD2 LEU B   4     5207   4570   6416   -538    213   -265       C  
ATOM   1703  N   VAL B   5      17.368   6.295 -67.384  1.00 34.84           N  
ANISOU 1703  N   VAL B   5     4584   3503   5151   -501    159   -461       N  
ATOM   1704  CA  VAL B   5      16.343   6.087 -66.362  1.00 32.59           C  
ANISOU 1704  CA  VAL B   5     4400   3203   4780   -473    184   -516       C  
ATOM   1705  C   VAL B   5      14.996   6.534 -66.851  1.00 33.90           C  
ANISOU 1705  C   VAL B   5     4582   3378   4920   -435    266   -547       C  
ATOM   1706  O   VAL B   5      14.777   7.699 -67.114  1.00 33.63           O  
ANISOU 1706  O   VAL B   5     4566   3311   4899   -440    258   -554       O  
ATOM   1707  CB  VAL B   5      16.770   6.813 -65.056  1.00 36.85           C  
ANISOU 1707  CB  VAL B   5     5046   3670   5283   -502     91   -535       C  
ATOM   1708  CG1 VAL B   5      15.716   6.658 -63.956  1.00 36.88           C  
ANISOU 1708  CG1 VAL B   5     5167   3652   5193   -468    125   -590       C  
ATOM   1709  CG2 VAL B   5      18.102   6.257 -64.603  1.00 36.63           C  
ANISOU 1709  CG2 VAL B   5     4992   3636   5290   -543      5   -495       C  
ATOM   1710  N   GLN B   6      14.089   5.600 -66.969  1.00 33.14           N  
ANISOU 1710  N   GLN B   6     4478   3322   4791   -397    342   -562       N  
ATOM   1711  CA  GLN B   6      12.734   5.860 -67.425  1.00 31.93           C  
ANISOU 1711  CA  GLN B   6     4331   3180   4619   -360    422   -583       C  
ATOM   1712  C   GLN B   6      11.738   6.138 -66.290  1.00 38.07           C  
ANISOU 1712  C   GLN B   6     5216   3919   5329   -329    447   -627       C  
ATOM   1713  O   GLN B   6      11.855   5.591 -65.186  1.00 39.59           O  
ANISOU 1713  O   GLN B   6     5473   4096   5471   -326    428   -645       O  
ATOM   1714  CB  GLN B   6      12.238   4.652 -68.215  1.00 30.46           C  
ANISOU 1714  CB  GLN B   6     4076   3057   4441   -336    490   -570       C  
ATOM   1715  CG  GLN B   6      13.066   4.359 -69.433  1.00 33.62           C  
ANISOU 1715  CG  GLN B   6     4379   3493   4901   -357    485   -528       C  
ATOM   1716  CD  GLN B   6      12.517   3.267 -70.316  1.00 32.23           C  
ANISOU 1716  CD  GLN B   6     4148   3371   4727   -334    552   -516       C  
ATOM   1717  OE1 GLN B   6      13.268   2.469 -70.834  1.00 31.97           O  
ANISOU 1717  OE1 GLN B   6     4061   3369   4719   -343    551   -488       O  
ATOM   1718  NE2 GLN B   6      11.234   3.287 -70.652  1.00 38.44           N  
ANISOU 1718  NE2 GLN B   6     4943   4168   5495   -306    609   -531       N  
ATOM   1719  N   SER B   7      10.658   6.832 -66.642  1.00 34.28           N  
ANISOU 1719  N   SER B   7     4749   3428   4849   -302    504   -640       N  
ATOM   1720  CA  SER B   7       9.545   7.122 -65.744  1.00 34.42           C  
ANISOU 1720  CA  SER B   7     4858   3409   4810   -263    551   -674       C  
ATOM   1721  C   SER B   7       8.809   5.818 -65.384  1.00 38.13           C  
ANISOU 1721  C   SER B   7     5325   3916   5246   -229    612   -678       C  
ATOM   1722  O   SER B   7       9.039   4.745 -65.959  1.00 39.93           O  
ANISOU 1722  O   SER B   7     5479   4198   5495   -234    621   -657       O  
ATOM   1723  CB  SER B   7       8.610   8.159 -66.387  1.00 38.50           C  
ANISOU 1723  CB  SER B   7     5367   3909   5353   -242    600   -674       C  
ATOM   1724  OG  SER B   7       8.260   7.857 -67.733  1.00 39.33           O  
ANISOU 1724  OG  SER B   7     5368   4065   5510   -241    638   -644       O  
ATOM   1725  N   GLY B   8       7.972   5.916 -64.398  1.00 36.65           N  
ANISOU 1725  N   GLY B   8     5226   3695   5005   -193    653   -704       N  
ATOM   1726  CA  GLY B   8       7.259   4.785 -63.811  1.00 37.36           C  
ANISOU 1726  CA  GLY B   8     5332   3807   5056   -158    708   -709       C  
ATOM   1727  C   GLY B   8       6.015   4.288 -64.519  1.00 44.87           C  
ANISOU 1727  C   GLY B   8     6218   4796   6035   -123    793   -689       C  
ATOM   1728  O   GLY B   8       5.587   4.842 -65.536  1.00 43.41           O  
ANISOU 1728  O   GLY B   8     5975   4619   5898   -123    815   -672       O  
ATOM   1729  N   VAL B   9       5.441   3.205 -63.954  1.00 43.83           N  
ANISOU 1729  N   VAL B   9     6097   4684   5872    -95    837   -689       N  
ATOM   1730  CA  VAL B   9       4.246   2.502 -64.451  1.00 42.75           C  
ANISOU 1730  CA  VAL B   9     5903   4581   5760    -62    912   -666       C  
ATOM   1731  C   VAL B   9       3.159   3.508 -64.825  1.00 42.62           C  
ANISOU 1731  C   VAL B   9     5885   4536   5773    -35    968   -656       C  
ATOM   1732  O   VAL B   9       2.960   4.468 -64.125  1.00 43.45           O  
ANISOU 1732  O   VAL B   9     6070   4586   5851    -16    981   -676       O  
ATOM   1733  CB  VAL B   9       3.654   1.483 -63.414  1.00 46.92           C  
ANISOU 1733  CB  VAL B   9     6474   5113   6242    -27    958   -670       C  
ATOM   1734  CG1 VAL B   9       2.412   0.785 -63.976  1.00 44.84           C  
ANISOU 1734  CG1 VAL B   9     6144   4881   6015      3   1029   -638       C  
ATOM   1735  CG2 VAL B   9       4.667   0.430 -63.023  1.00 48.90           C  
ANISOU 1735  CG2 VAL B   9     6724   5392   6466    -53    906   -676       C  
ATOM   1736  N   GLU B  10       2.430   3.248 -65.885  1.00 38.31           N  
ANISOU 1736  N   GLU B  10     5254   4023   5280    -30   1001   -624       N  
ATOM   1737  CA  GLU B  10       1.300   4.069 -66.296  1.00 37.57           C  
ANISOU 1737  CA  GLU B  10     5145   3904   5225     -4   1056   -604       C  
ATOM   1738  C   GLU B  10       0.120   3.182 -66.656  1.00 40.52           C  
ANISOU 1738  C   GLU B  10     5459   4307   5630     21   1114   -567       C  
ATOM   1739  O   GLU B  10       0.288   2.097 -67.238  1.00 39.08           O  
ANISOU 1739  O   GLU B  10     5216   4172   5459      2   1095   -552       O  
ATOM   1740  CB  GLU B  10       1.644   4.871 -67.551  1.00 38.56           C  
ANISOU 1740  CB  GLU B  10     5210   4038   5401    -37   1020   -591       C  
ATOM   1741  CG  GLU B  10       2.849   5.777 -67.414  1.00 43.57           C  
ANISOU 1741  CG  GLU B  10     5885   4648   6023    -69    955   -618       C  
ATOM   1742  CD  GLU B  10       2.628   6.984 -66.530  1.00 65.12           C  
ANISOU 1742  CD  GLU B  10     8707   7310   8727    -47    969   -642       C  
ATOM   1743  OE1 GLU B  10       1.462   7.265 -66.172  1.00 52.75           O  
ANISOU 1743  OE1 GLU B  10     7166   5715   7161     -3   1041   -635       O  
ATOM   1744  OE2 GLU B  10       3.621   7.688 -66.249  1.00 67.62           O  
ANISOU 1744  OE2 GLU B  10     9069   7598   9025    -75    908   -665       O  
ATOM   1745  N   VAL B  11      -1.073   3.673 -66.342  1.00 37.17           N  
ANISOU 1745  N   VAL B  11     5050   3848   5225     64   1184   -549       N  
ATOM   1746  CA  VAL B  11      -2.322   3.086 -66.756  1.00 36.81           C  
ANISOU 1746  CA  VAL B  11     4941   3818   5228     87   1238   -502       C  
ATOM   1747  C   VAL B  11      -3.165   4.224 -67.301  1.00 38.33           C  
ANISOU 1747  C   VAL B  11     5109   3978   5477    102   1272   -474       C  
ATOM   1748  O   VAL B  11      -3.285   5.257 -66.674  1.00 37.50           O  
ANISOU 1748  O   VAL B  11     5069   3822   5358    128   1302   -491       O  
ATOM   1749  CB  VAL B  11      -3.008   2.160 -65.721  1.00 40.35           C  
ANISOU 1749  CB  VAL B  11     5417   4263   5650    129   1296   -492       C  
ATOM   1750  CG1 VAL B  11      -3.312   2.863 -64.433  1.00 39.15           C  
ANISOU 1750  CG1 VAL B  11     5367   4053   5456    176   1353   -513       C  
ATOM   1751  CG2 VAL B  11      -4.261   1.516 -66.288  1.00 40.29           C  
ANISOU 1751  CG2 VAL B  11     5328   4273   5707    146   1340   -433       C  
ATOM   1752  N   LYS B  12      -3.660   4.053 -68.515  1.00 35.95           N  
ANISOU 1752  N   LYS B  12     4718   3703   5238     82   1261   -433       N  
ATOM   1753  CA  LYS B  12      -4.424   5.064 -69.245  1.00 35.46           C  
ANISOU 1753  CA  LYS B  12     4617   3616   5239     87   1282   -399       C  
ATOM   1754  C   LYS B  12      -5.640   4.475 -69.879  1.00 39.15           C  
ANISOU 1754  C   LYS B  12     5005   4097   5772     95   1310   -336       C  
ATOM   1755  O   LYS B  12      -5.694   3.282 -70.177  1.00 37.36           O  
ANISOU 1755  O   LYS B  12     4739   3909   5545     79   1290   -321       O  
ATOM   1756  CB  LYS B  12      -3.572   5.681 -70.380  1.00 37.13           C  
ANISOU 1756  CB  LYS B  12     4797   3845   5465     37   1213   -409       C  
ATOM   1757  CG  LYS B  12      -2.317   6.376 -69.905  1.00 34.25           C  
ANISOU 1757  CG  LYS B  12     4499   3465   5051     21   1172   -463       C  
ATOM   1758  CD  LYS B  12      -2.612   7.610 -69.069  1.00 39.49           C  
ANISOU 1758  CD  LYS B  12     5234   4065   5704     55   1212   -480       C  
ATOM   1759  CE  LYS B  12      -1.326   8.170 -68.532  1.00 45.72           C  
ANISOU 1759  CE  LYS B  12     6096   4836   6441     33   1158   -531       C  
ATOM   1760  NZ  LYS B  12      -1.572   9.324 -67.641  1.00 51.91           N  
ANISOU 1760  NZ  LYS B  12     6969   5551   7205     66   1193   -553       N  
ATOM   1761  N   LYS B  13      -6.577   5.340 -70.176  1.00 37.37           N  
ANISOU 1761  N   LYS B  13     4752   3837   5608    114   1349   -297       N  
ATOM   1762  CA  LYS B  13      -7.811   4.939 -70.828  1.00 38.04           C  
ANISOU 1762  CA  LYS B  13     4756   3927   5771    119   1370   -226       C  
ATOM   1763  C   LYS B  13      -7.617   4.912 -72.334  1.00 38.96           C  
ANISOU 1763  C   LYS B  13     4807   4075   5922     63   1299   -205       C  
ATOM   1764  O   LYS B  13      -6.838   5.704 -72.866  1.00 37.21           O  
ANISOU 1764  O   LYS B  13     4598   3854   5687     36   1258   -234       O  
ATOM   1765  CB  LYS B  13      -8.946   5.907 -70.473  1.00 42.97           C  
ANISOU 1765  CB  LYS B  13     5376   4496   6454    167   1448   -185       C  
ATOM   1766  CG  LYS B  13      -9.499   5.675 -69.062  1.00 55.40           C  
ANISOU 1766  CG  LYS B  13     7004   6037   8008    230   1536   -183       C  
ATOM   1767  CD  LYS B  13     -10.319   6.844 -68.527  1.00 68.39           C  
ANISOU 1767  CD  LYS B  13     8676   7617   9691    285   1622   -160       C  
ATOM   1768  CE  LYS B  13     -11.695   6.964 -69.150  1.00 94.24           C  
ANISOU 1768  CE  LYS B  13    11856  10874  13078    300   1662    -69       C  
ATOM   1769  NZ  LYS B  13     -12.716   6.144 -68.435  1.00106.48           N  
ANISOU 1769  NZ  LYS B  13    13383  12412  14662    348   1738    -15       N  
ATOM   1770  N   PRO B  14      -8.348   4.032 -73.048  1.00 36.79           N  
ANISOU 1770  N   PRO B  14     4465   3822   5694     46   1281   -152       N  
ATOM   1771  CA  PRO B  14      -8.317   4.079 -74.519  1.00 36.16           C  
ANISOU 1771  CA  PRO B  14     4331   3761   5647     -5   1215   -125       C  
ATOM   1772  C   PRO B  14      -8.725   5.477 -75.022  1.00 38.80           C  
ANISOU 1772  C   PRO B  14     4646   4061   6036     -4   1224   -101       C  
ATOM   1773  O   PRO B  14      -9.517   6.145 -74.377  1.00 38.98           O  
ANISOU 1773  O   PRO B  14     4670   4043   6100     39   1288    -76       O  
ATOM   1774  CB  PRO B  14      -9.334   3.029 -74.937  1.00 37.61           C  
ANISOU 1774  CB  PRO B  14     4455   3955   5880    -13   1207    -62       C  
ATOM   1775  CG  PRO B  14      -9.697   2.320 -73.761  1.00 42.11           C  
ANISOU 1775  CG  PRO B  14     5043   4520   6438     29   1262    -61       C  
ATOM   1776  CD  PRO B  14      -9.314   3.031 -72.555  1.00 37.48           C  
ANISOU 1776  CD  PRO B  14     4524   3908   5809     73   1320   -107       C  
ATOM   1777  N   GLY B  15      -8.106   5.934 -76.104  1.00 34.79           N  
ANISOU 1777  N   GLY B  15     4127   3569   5524    -48   1165   -111       N  
ATOM   1778  CA  GLY B  15      -8.314   7.268 -76.640  1.00 33.57           C  
ANISOU 1778  CA  GLY B  15     3956   3385   5414    -52   1164    -94       C  
ATOM   1779  C   GLY B  15      -7.453   8.327 -75.956  1.00 37.48           C  
ANISOU 1779  C   GLY B  15     4513   3858   5868    -35   1182   -152       C  
ATOM   1780  O   GLY B  15      -7.358   9.457 -76.457  1.00 35.75           O  
ANISOU 1780  O   GLY B  15     4287   3619   5676    -46   1172   -148       O  
ATOM   1781  N   ALA B  16      -6.832   7.997 -74.792  1.00 33.71           N  
ANISOU 1781  N   ALA B  16     4099   3381   5327    -11   1206   -204       N  
ATOM   1782  CA  ALA B  16      -5.993   8.936 -74.060  1.00 32.74           C  
ANISOU 1782  CA  ALA B  16     4045   3232   5161      2   1214   -259       C  
ATOM   1783  C   ALA B  16      -4.551   8.847 -74.561  1.00 36.42           C  
ANISOU 1783  C   ALA B  16     4526   3733   5579    -43   1143   -302       C  
ATOM   1784  O   ALA B  16      -4.312   8.306 -75.643  1.00 35.40           O  
ANISOU 1784  O   ALA B  16     4351   3642   5458    -82   1098   -285       O  
ATOM   1785  CB  ALA B  16      -6.072   8.696 -72.564  1.00 32.83           C  
ANISOU 1785  CB  ALA B  16     4125   3219   5129     50   1270   -288       C  
ATOM   1786  N   SER B  17      -3.597   9.445 -73.833  1.00 34.58           N  
ANISOU 1786  N   SER B  17     4357   3481   5300    -40   1133   -353       N  
ATOM   1787  CA  SER B  17      -2.191   9.436 -74.234  1.00 32.47           C  
ANISOU 1787  CA  SER B  17     4099   3241   4997    -82   1069   -386       C  
ATOM   1788  C   SER B  17      -1.295   9.063 -73.076  1.00 33.63           C  
ANISOU 1788  C   SER B  17     4313   3385   5079    -74   1060   -435       C  
ATOM   1789  O   SER B  17      -1.647   9.219 -71.921  1.00 31.46           O  
ANISOU 1789  O   SER B  17     4098   3076   4780    -37   1100   -453       O  
ATOM   1790  CB  SER B  17      -1.778  10.798 -74.792  1.00 37.07           C  
ANISOU 1790  CB  SER B  17     4681   3800   5606   -100   1043   -389       C  
ATOM   1791  OG  SER B  17      -1.804  11.817 -73.808  1.00 40.49           O  
ANISOU 1791  OG  SER B  17     5178   4178   6028    -72   1069   -415       O  
ATOM   1792  N   VAL B  18      -0.091   8.631 -73.403  1.00 33.20           N  
ANISOU 1792  N   VAL B  18     4253   3364   4998   -109   1005   -454       N  
ATOM   1793  CA  VAL B  18       0.931   8.340 -72.394  1.00 32.75           C  
ANISOU 1793  CA  VAL B  18     4255   3302   4885   -112    981   -496       C  
ATOM   1794  C   VAL B  18       2.201   8.996 -72.849  1.00 35.63           C  
ANISOU 1794  C   VAL B  18     4617   3668   5253   -150    920   -508       C  
ATOM   1795  O   VAL B  18       2.493   9.004 -74.040  1.00 33.39           O  
ANISOU 1795  O   VAL B  18     4275   3412   4999   -178    897   -485       O  
ATOM   1796  CB  VAL B  18       1.138   6.820 -72.165  1.00 36.18           C  
ANISOU 1796  CB  VAL B  18     4680   3779   5288   -113    979   -498       C  
ATOM   1797  CG1 VAL B  18       1.506   6.119 -73.460  1.00 32.71           C  
ANISOU 1797  CG1 VAL B  18     4172   3388   4868   -145    950   -474       C  
ATOM   1798  CG2 VAL B  18       2.197   6.583 -71.067  1.00 36.59           C  
ANISOU 1798  CG2 VAL B  18     4794   3823   5287   -117    949   -537       C  
ATOM   1799  N   LYS B  19       2.948   9.569 -71.906  1.00 37.22           N  
ANISOU 1799  N   LYS B  19     4885   3835   5424   -152    893   -542       N  
ATOM   1800  CA  LYS B  19       4.232  10.199 -72.196  1.00 37.34           C  
ANISOU 1800  CA  LYS B  19     4897   3844   5446   -190    829   -549       C  
ATOM   1801  C   LYS B  19       5.293   9.519 -71.336  1.00 41.80           C  
ANISOU 1801  C   LYS B  19     5500   4414   5968   -203    788   -573       C  
ATOM   1802  O   LYS B  19       5.256   9.657 -70.123  1.00 44.38           O  
ANISOU 1802  O   LYS B  19     5905   4704   6253   -186    789   -601       O  
ATOM   1803  CB  LYS B  19       4.217  11.709 -71.973  1.00 38.08           C  
ANISOU 1803  CB  LYS B  19     5033   3881   5555   -190    818   -561       C  
ATOM   1804  CG  LYS B  19       5.551  12.336 -72.419  1.00 40.03           C  
ANISOU 1804  CG  LYS B  19     5263   4125   5821   -233    747   -558       C  
ATOM   1805  CD  LYS B  19       5.469  13.810 -72.682  1.00 43.79           C  
ANISOU 1805  CD  LYS B  19     5752   4556   6330   -240    736   -557       C  
ATOM   1806  CE  LYS B  19       5.212  14.599 -71.402  1.00 58.68           C  
ANISOU 1806  CE  LYS B  19     7741   6373   8180   -217    740   -592       C  
ATOM   1807  NZ  LYS B  19       4.806  16.002 -71.671  1.00 65.87           N  
ANISOU 1807  NZ  LYS B  19     8666   7237   9124   -212    748   -589       N  
ATOM   1808  N   VAL B  20       6.211   8.784 -71.964  1.00 36.17           N  
ANISOU 1808  N   VAL B  20     4734   3743   5264   -232    755   -558       N  
ATOM   1809  CA  VAL B  20       7.281   8.078 -71.276  1.00 36.37           C  
ANISOU 1809  CA  VAL B  20     4780   3777   5262   -248    712   -570       C  
ATOM   1810  C   VAL B  20       8.568   8.910 -71.377  1.00 40.81           C  
ANISOU 1810  C   VAL B  20     5340   4317   5848   -286    643   -565       C  
ATOM   1811  O   VAL B  20       8.944   9.317 -72.474  1.00 40.27           O  
ANISOU 1811  O   VAL B  20     5213   4264   5824   -306    632   -538       O  
ATOM   1812  CB  VAL B  20       7.464   6.643 -71.855  1.00 37.99           C  
ANISOU 1812  CB  VAL B  20     4927   4040   5467   -251    726   -551       C  
ATOM   1813  CG1 VAL B  20       8.555   5.891 -71.115  1.00 38.84           C  
ANISOU 1813  CG1 VAL B  20     5051   4155   5551   -266    684   -559       C  
ATOM   1814  CG2 VAL B  20       6.157   5.865 -71.774  1.00 36.72           C  
ANISOU 1814  CG2 VAL B  20     4766   3897   5289   -217    786   -551       C  
ATOM   1815  N   SER B  21       9.222   9.179 -70.232  1.00 36.40           N  
ANISOU 1815  N   SER B  21     4850   3720   5261   -296    595   -588       N  
ATOM   1816  CA  SER B  21      10.471   9.931 -70.220  1.00 35.54           C  
ANISOU 1816  CA  SER B  21     4741   3584   5179   -336    518   -578       C  
ATOM   1817  C   SER B  21      11.656   8.992 -70.086  1.00 37.82           C  
ANISOU 1817  C   SER B  21     4997   3899   5474   -361    473   -559       C  
ATOM   1818  O   SER B  21      11.532   7.883 -69.582  1.00 35.01           O  
ANISOU 1818  O   SER B  21     4651   3566   5084   -347    491   -568       O  
ATOM   1819  CB  SER B  21      10.464  10.981 -69.115  1.00 38.23           C  
ANISOU 1819  CB  SER B  21     5183   3854   5490   -337    482   -609       C  
ATOM   1820  OG  SER B  21      10.698  10.398 -67.847  1.00 47.46           O  
ANISOU 1820  OG  SER B  21     6426   5003   6602   -334    457   -633       O  
ATOM   1821  N   CYS B  22      12.791   9.424 -70.613  1.00 37.25           N  
ANISOU 1821  N   CYS B  22     4876   3823   5453   -398    420   -528       N  
ATOM   1822  CA  CYS B  22      14.042   8.700 -70.552  1.00 38.70           C  
ANISOU 1822  CA  CYS B  22     5020   4025   5661   -424    373   -498       C  
ATOM   1823  C   CYS B  22      15.143   9.685 -70.202  1.00 39.36           C  
ANISOU 1823  C   CYS B  22     5115   4058   5780   -466    284   -481       C  
ATOM   1824  O   CYS B  22      15.578  10.433 -71.078  1.00 38.73           O  
ANISOU 1824  O   CYS B  22     4983   3976   5758   -484    271   -450       O  
ATOM   1825  CB  CYS B  22      14.307   8.019 -71.893  1.00 41.05           C  
ANISOU 1825  CB  CYS B  22     5219   4378   6001   -422    415   -459       C  
ATOM   1826  SG  CYS B  22      15.885   7.140 -71.977  1.00 45.59           S  
ANISOU 1826  SG  CYS B  22     5729   4973   6620   -449    374   -412       S  
ATOM   1827  N   LYS B  23      15.601   9.686 -68.941  1.00 35.88           N  
ANISOU 1827  N   LYS B  23     4748   3576   5308   -482    219   -498       N  
ATOM   1828  CA  LYS B  23      16.648  10.603 -68.451  1.00 36.10           C  
ANISOU 1828  CA  LYS B  23     4802   3548   5367   -528    118   -481       C  
ATOM   1829  C   LYS B  23      18.031  10.010 -68.698  1.00 40.01           C  
ANISOU 1829  C   LYS B  23     5217   4061   5925   -562     66   -425       C  
ATOM   1830  O   LYS B  23      18.353   8.948 -68.164  1.00 39.22           O  
ANISOU 1830  O   LYS B  23     5116   3980   5806   -561     58   -421       O  
ATOM   1831  CB  LYS B  23      16.406  10.921 -66.951  1.00 39.26           C  
ANISOU 1831  CB  LYS B  23     5335   3886   5695   -530     69   -527       C  
ATOM   1832  CG  LYS B  23      17.515  11.657 -66.190  1.00 48.98           C  
ANISOU 1832  CG  LYS B  23     6615   5051   6944   -582    -53   -513       C  
ATOM   1833  CD  LYS B  23      17.906  12.966 -66.779  1.00 61.95           C  
ANISOU 1833  CD  LYS B  23     8234   6658   8645   -609    -96   -491       C  
ATOM   1834  CE  LYS B  23      18.867  13.735 -65.893  1.00 70.12           C  
ANISOU 1834  CE  LYS B  23     9337   7616   9689   -662   -225   -481       C  
ATOM   1835  NZ  LYS B  23      20.077  14.198 -66.638  1.00 79.42           N  
ANISOU 1835  NZ  LYS B  23    10414   8790  10971   -708   -292   -412       N  
ATOM   1836  N   ALA B  24      18.841  10.670 -69.532  1.00 38.90           N  
ANISOU 1836  N   ALA B  24     5002   3915   5863   -589     35   -376       N  
ATOM   1837  CA  ALA B  24      20.163  10.144 -69.878  1.00 40.07           C  
ANISOU 1837  CA  ALA B  24     5060   4080   6086   -617     -3   -310       C  
ATOM   1838  C   ALA B  24      21.218  10.741 -69.022  1.00 44.57           C  
ANISOU 1838  C   ALA B  24     5658   4587   6688   -668   -123   -284       C  
ATOM   1839  O   ALA B  24      21.140  11.914 -68.738  1.00 44.23           O  
ANISOU 1839  O   ALA B  24     5670   4492   6644   -688   -175   -299       O  
ATOM   1840  CB  ALA B  24      20.487  10.447 -71.311  1.00 41.28           C  
ANISOU 1840  CB  ALA B  24     5111   4261   6311   -616     40   -261       C  
ATOM   1841  N   SER B  25      22.194   9.941 -68.588  1.00 43.75           N  
ANISOU 1841  N   SER B  25     5521   4486   6615   -690   -173   -244       N  
ATOM   1842  CA  SER B  25      23.326  10.455 -67.815  1.00 45.01           C  
ANISOU 1842  CA  SER B  25     5697   4585   6821   -747   -302   -205       C  
ATOM   1843  C   SER B  25      24.585   9.615 -68.073  1.00 48.02           C  
ANISOU 1843  C   SER B  25     5970   4987   7290   -767   -327   -124       C  
ATOM   1844  O   SER B  25      24.495   8.537 -68.632  1.00 46.82           O  
ANISOU 1844  O   SER B  25     5755   4893   7140   -734   -243   -113       O  
ATOM   1845  CB  SER B  25      22.976  10.562 -66.338  1.00 46.96           C  
ANISOU 1845  CB  SER B  25     6083   4780   6980   -759   -369   -260       C  
ATOM   1846  OG  SER B  25      23.106   9.330 -65.656  1.00 56.39           O  
ANISOU 1846  OG  SER B  25     7289   5996   8141   -752   -369   -264       O  
ATOM   1847  N   GLY B  26      25.741  10.211 -67.820  1.00 46.30           N  
ANISOU 1847  N   GLY B  26     5722   4718   7150   -821   -436    -63       N  
ATOM   1848  CA  GLY B  26      27.039   9.568 -67.963  1.00 45.18           C  
ANISOU 1848  CA  GLY B  26     5476   4583   7108   -846   -474     26       C  
ATOM   1849  C   GLY B  26      27.639   9.584 -69.349  1.00 46.19           C  
ANISOU 1849  C   GLY B  26     5467   4745   7339   -834   -410    100       C  
ATOM   1850  O   GLY B  26      28.585   8.842 -69.610  1.00 44.68           O  
ANISOU 1850  O   GLY B  26     5180   4570   7225   -839   -406    174       O  
ATOM   1851  N   TYR B  27      27.129  10.446 -70.236  1.00 42.12           N  
ANISOU 1851  N   TYR B  27     4940   4236   6825   -818   -359     86       N  
ATOM   1852  CA  TYR B  27      27.610  10.524 -71.614  1.00 41.09           C  
ANISOU 1852  CA  TYR B  27     4692   4138   6782   -803   -288    152       C  
ATOM   1853  C   TYR B  27      27.165  11.828 -72.237  1.00 46.22           C  
ANISOU 1853  C   TYR B  27     5354   4770   7436   -806   -282    136       C  
ATOM   1854  O   TYR B  27      26.388  12.538 -71.630  1.00 45.26           O  
ANISOU 1854  O   TYR B  27     5334   4619   7246   -812   -317     68       O  
ATOM   1855  CB  TYR B  27      27.136   9.305 -72.438  1.00 41.13           C  
ANISOU 1855  CB  TYR B  27     4656   4217   6756   -745   -153    140       C  
ATOM   1856  CG  TYR B  27      25.673   9.270 -72.843  1.00 41.72           C  
ANISOU 1856  CG  TYR B  27     4794   4328   6729   -701    -61     56       C  
ATOM   1857  CD1 TYR B  27      24.728   8.628 -72.057  1.00 43.48           C  
ANISOU 1857  CD1 TYR B  27     5104   4565   6851   -681    -45    -19       C  
ATOM   1858  CD2 TYR B  27      25.268   9.724 -74.089  1.00 43.47           C  
ANISOU 1858  CD2 TYR B  27     4980   4575   6962   -678     16     61       C  
ATOM   1859  CE1 TYR B  27      23.404   8.480 -72.482  1.00 43.03           C  
ANISOU 1859  CE1 TYR B  27     5091   4543   6715   -639     43    -84       C  
ATOM   1860  CE2 TYR B  27      23.928   9.682 -74.480  1.00 43.79           C  
ANISOU 1860  CE2 TYR B  27     5073   4648   6919   -641     93     -8       C  
ATOM   1861  CZ  TYR B  27      22.994   9.057 -73.672  1.00 48.15           C  
ANISOU 1861  CZ  TYR B  27     5706   5211   7379   -622    106    -79       C  
ATOM   1862  OH  TYR B  27      21.686   8.961 -74.073  1.00 44.72           O  
ANISOU 1862  OH  TYR B  27     5313   4806   6873   -586    181   -136       O  
ATOM   1863  N   THR B  28      27.651  12.138 -73.444  1.00 46.29           N  
ANISOU 1863  N   THR B  28     5264   4797   7527   -798   -232    200       N  
ATOM   1864  CA  THR B  28      27.312  13.359 -74.159  1.00 45.88           C  
ANISOU 1864  CA  THR B  28     5210   4731   7491   -801   -222    196       C  
ATOM   1865  C   THR B  28      26.005  13.087 -74.853  1.00 49.80           C  
ANISOU 1865  C   THR B  28     5742   5279   7901   -749   -106    128       C  
ATOM   1866  O   THR B  28      25.990  12.415 -75.875  1.00 50.35           O  
ANISOU 1866  O   THR B  28     5750   5400   7982   -714     -8    153       O  
ATOM   1867  CB  THR B  28      28.431  13.772 -75.141  1.00 49.62           C  
ANISOU 1867  CB  THR B  28     5562   5200   8092   -816   -219    301       C  
ATOM   1868  OG1 THR B  28      29.641  13.958 -74.415  1.00 52.36           O  
ANISOU 1868  OG1 THR B  28     5872   5495   8527   -867   -335    371       O  
ATOM   1869  CG2 THR B  28      28.106  15.073 -75.884  1.00 41.61           C  
ANISOU 1869  CG2 THR B  28     4545   4169   7098   -821   -213    300       C  
ATOM   1870  N   PHE B  29      24.901  13.566 -74.255  1.00 45.24           N  
ANISOU 1870  N   PHE B  29     5268   4685   7235   -744   -119     44       N  
ATOM   1871  CA  PHE B  29      23.513  13.409 -74.732  1.00 41.81           C  
ANISOU 1871  CA  PHE B  29     4879   4290   6716   -699    -23    -24       C  
ATOM   1872  C   PHE B  29      23.318  13.601 -76.219  1.00 43.94           C  
ANISOU 1872  C   PHE B  29     5081   4598   7016   -675     64      5       C  
ATOM   1873  O   PHE B  29      22.612  12.856 -76.858  1.00 41.69           O  
ANISOU 1873  O   PHE B  29     4793   4362   6685   -636    155    -18       O  
ATOM   1874  CB  PHE B  29      22.575  14.386 -73.976  1.00 42.76           C  
ANISOU 1874  CB  PHE B  29     5108   4367   6773   -705    -64    -95       C  
ATOM   1875  CG  PHE B  29      21.094  14.207 -74.270  1.00 42.14           C  
ANISOU 1875  CG  PHE B  29     5078   4321   6611   -660     26   -161       C  
ATOM   1876  CD1 PHE B  29      20.451  13.008 -73.988  1.00 41.13           C  
ANISOU 1876  CD1 PHE B  29     4976   4234   6418   -627     84   -199       C  
ATOM   1877  CD2 PHE B  29      20.348  15.243 -74.803  1.00 41.14           C  
ANISOU 1877  CD2 PHE B  29     4969   4183   6480   -652     50   -182       C  
ATOM   1878  CE1 PHE B  29      19.091  12.852 -74.229  1.00 40.70           C  
ANISOU 1878  CE1 PHE B  29     4963   4206   6297   -589    159   -252       C  
ATOM   1879  CE2 PHE B  29      18.993  15.080 -75.057  1.00 42.92           C  
ANISOU 1879  CE2 PHE B  29     5234   4435   6639   -613    127   -235       C  
ATOM   1880  CZ  PHE B  29      18.378  13.869 -74.807  1.00 39.40           C  
ANISOU 1880  CZ  PHE B  29     4808   4029   6134   -582    182   -266       C  
ATOM   1881  N   THR B  30      23.935  14.589 -76.757  1.00 46.17           N  
ANISOU 1881  N   THR B  30     5314   4854   7373   -699     33     56       N  
ATOM   1882  CA  THR B  30      23.775  14.957 -78.157  1.00 46.00           C  
ANISOU 1882  CA  THR B  30     5237   4861   7381   -680    108     85       C  
ATOM   1883  C   THR B  30      24.584  14.061 -79.137  1.00 50.28           C  
ANISOU 1883  C   THR B  30     5685   5443   7975   -660    179    156       C  
ATOM   1884  O   THR B  30      24.342  14.146 -80.334  1.00 51.37           O  
ANISOU 1884  O   THR B  30     5790   5610   8117   -637    256    174       O  
ATOM   1885  CB  THR B  30      24.059  16.474 -78.258  1.00 56.63           C  
ANISOU 1885  CB  THR B  30     6576   6157   8783   -714     41    108       C  
ATOM   1886  OG1 THR B  30      23.457  17.000 -79.417  1.00 67.96           O  
ANISOU 1886  OG1 THR B  30     7992   7615  10216   -694    109    108       O  
ATOM   1887  CG2 THR B  30      25.479  16.831 -78.172  1.00 50.57           C  
ANISOU 1887  CG2 THR B  30     5737   5355   8123   -753    -31    192       C  
ATOM   1888  N   ASN B  31      25.469  13.162 -78.667  1.00 45.20           N  
ANISOU 1888  N   ASN B  31     5007   4802   7365   -666    161    195       N  
ATOM   1889  CA  ASN B  31      26.202  12.274 -79.581  1.00 45.14           C  
ANISOU 1889  CA  ASN B  31     4917   4829   7405   -640    240    262       C  
ATOM   1890  C   ASN B  31      25.516  10.922 -79.860  1.00 48.09           C  
ANISOU 1890  C   ASN B  31     5318   5254   7698   -595    333    220       C  
ATOM   1891  O   ASN B  31      26.123  10.039 -80.499  1.00 46.87           O  
ANISOU 1891  O   ASN B  31     5109   5125   7574   -570    400    271       O  
ATOM   1892  CB  ASN B  31      27.606  12.038 -79.036  1.00 49.96           C  
ANISOU 1892  CB  ASN B  31     5461   5412   8112   -668    177    341       C  
ATOM   1893  CG  ASN B  31      28.500  13.247 -79.104  1.00 58.41           C  
ANISOU 1893  CG  ASN B  31     6474   6433   9284   -710    101    410       C  
ATOM   1894  OD1 ASN B  31      28.233  14.231 -79.821  1.00 53.44           O  
ANISOU 1894  OD1 ASN B  31     5840   5798   8669   -712    115    414       O  
ATOM   1895  ND2 ASN B  31      29.605  13.178 -78.367  1.00 52.59           N  
ANISOU 1895  ND2 ASN B  31     5694   5660   8629   -746     15    472       N  
ATOM   1896  N   TYR B  32      24.264  10.738 -79.372  1.00 42.91           N  
ANISOU 1896  N   TYR B  32     4748   4612   6944   -583    338    133       N  
ATOM   1897  CA  TYR B  32      23.568   9.480 -79.533  1.00 41.08           C  
ANISOU 1897  CA  TYR B  32     4547   4424   6639   -545    412     93       C  
ATOM   1898  C   TYR B  32      22.175   9.713 -79.895  1.00 42.30           C  
ANISOU 1898  C   TYR B  32     4761   4596   6716   -527    452     28       C  
ATOM   1899  O   TYR B  32      21.522  10.555 -79.291  1.00 39.54           O  
ANISOU 1899  O   TYR B  32     4462   4221   6339   -542    403    -17       O  
ATOM   1900  CB  TYR B  32      23.609   8.643 -78.229  1.00 40.68           C  
ANISOU 1900  CB  TYR B  32     4532   4369   6555   -551    367     61       C  
ATOM   1901  CG  TYR B  32      24.992   8.136 -77.875  1.00 41.67           C  
ANISOU 1901  CG  TYR B  32     4592   4481   6758   -567    333    132       C  
ATOM   1902  CD1 TYR B  32      25.970   8.996 -77.394  1.00 43.87           C  
ANISOU 1902  CD1 TYR B  32     4836   4714   7120   -610    242    183       C  
ATOM   1903  CD2 TYR B  32      25.340   6.803 -78.073  1.00 43.03           C  
ANISOU 1903  CD2 TYR B  32     4735   4684   6930   -540    393    153       C  
ATOM   1904  CE1 TYR B  32      27.277   8.564 -77.186  1.00 43.42           C  
ANISOU 1904  CE1 TYR B  32     4705   4643   7151   -625    212    262       C  
ATOM   1905  CE2 TYR B  32      26.647   6.365 -77.900  1.00 44.81           C  
ANISOU 1905  CE2 TYR B  32     4887   4897   7241   -551    373    231       C  
ATOM   1906  CZ  TYR B  32      27.611   7.242 -77.434  1.00 50.32           C  
ANISOU 1906  CZ  TYR B  32     5543   5549   8027   -594    280    287       C  
ATOM   1907  OH  TYR B  32      28.875   6.755 -77.205  1.00 49.48           O  
ANISOU 1907  OH  TYR B  32     5360   5428   8013   -607    256    370       O  
ATOM   1908  N   TYR B  33      21.668   8.884 -80.808  1.00 41.86           N  
ANISOU 1908  N   TYR B  33     4706   4580   6618   -492    539     21       N  
ATOM   1909  CA  TYR B  33      20.256   8.891 -81.131  1.00 42.42           C  
ANISOU 1909  CA  TYR B  33     4834   4670   6614   -474    576    -38       C  
ATOM   1910  C   TYR B  33      19.560   8.192 -79.950  1.00 42.21           C  
ANISOU 1910  C   TYR B  33     4865   4647   6524   -468    555    -98       C  
ATOM   1911  O   TYR B  33      20.162   7.329 -79.290  1.00 38.99           O  
ANISOU 1911  O   TYR B  33     4450   4244   6121   -468    541    -90       O  
ATOM   1912  CB  TYR B  33      19.969   8.023 -82.352  1.00 44.84           C  
ANISOU 1912  CB  TYR B  33     5135   5014   6889   -443    666    -26       C  
ATOM   1913  CG  TYR B  33      20.530   8.500 -83.663  1.00 50.22           C  
ANISOU 1913  CG  TYR B  33     5771   5696   7615   -439    710     32       C  
ATOM   1914  CD1 TYR B  33      20.132   9.704 -84.207  1.00 54.92           C  
ANISOU 1914  CD1 TYR B  33     6367   6278   8223   -452    698     33       C  
ATOM   1915  CD2 TYR B  33      21.322   7.672 -84.448  1.00 51.10           C  
ANISOU 1915  CD2 TYR B  33     5847   5823   7746   -417    774     82       C  
ATOM   1916  CE1 TYR B  33      20.647  10.159 -85.414  1.00 59.95           C  
ANISOU 1916  CE1 TYR B  33     6965   6915   8899   -448    739     89       C  
ATOM   1917  CE2 TYR B  33      21.817   8.100 -85.679  1.00 52.25           C  
ANISOU 1917  CE2 TYR B  33     5959   5967   7927   -409    824    137       C  
ATOM   1918  CZ  TYR B  33      21.456   9.340 -86.170  1.00 64.94           C  
ANISOU 1918  CZ  TYR B  33     7565   7561   9547   -425    805    140       C  
ATOM   1919  OH  TYR B  33      21.961   9.849 -87.346  1.00 69.49           O  
ANISOU 1919  OH  TYR B  33     8108   8133  10160   -419    851    197       O  
ATOM   1920  N   MET B  34      18.292   8.522 -79.732  1.00 36.63           N  
ANISOU 1920  N   MET B  34     4216   3940   5764   -461    557   -153       N  
ATOM   1921  CA  MET B  34      17.467   7.815 -78.771  1.00 33.86           C  
ANISOU 1921  CA  MET B  34     3921   3596   5350   -448    555   -208       C  
ATOM   1922  C   MET B  34      16.386   7.135 -79.531  1.00 34.40           C  
ANISOU 1922  C   MET B  34     4005   3698   5367   -421    622   -229       C  
ATOM   1923  O   MET B  34      15.676   7.762 -80.304  1.00 31.60           O  
ANISOU 1923  O   MET B  34     3655   3344   5007   -418    644   -232       O  
ATOM   1924  CB  MET B  34      16.884   8.712 -77.700  1.00 36.35           C  
ANISOU 1924  CB  MET B  34     4292   3875   5645   -460    502   -251       C  
ATOM   1925  CG  MET B  34      16.344   7.901 -76.517  1.00 39.41           C  
ANISOU 1925  CG  MET B  34     4736   4265   5975   -447    495   -296       C  
ATOM   1926  SD  MET B  34      17.733   7.215 -75.536  1.00 43.50           S  
ANISOU 1926  SD  MET B  34     5238   4772   6518   -467    438   -271       S  
ATOM   1927  CE  MET B  34      18.256   8.730 -74.664  1.00 42.27           C  
ANISOU 1927  CE  MET B  34     5115   4551   6394   -505    341   -272       C  
ATOM   1928  N   TYR B  35      16.259   5.835 -79.290  1.00 33.21           N  
ANISOU 1928  N   TYR B  35     3865   3573   5181   -403    650   -241       N  
ATOM   1929  CA  TYR B  35      15.308   4.950 -79.907  1.00 34.23           C  
ANISOU 1929  CA  TYR B  35     4013   3732   5261   -380    705   -258       C  
ATOM   1930  C   TYR B  35      14.333   4.456 -78.921  1.00 36.63           C  
ANISOU 1930  C   TYR B  35     4364   4038   5515   -369    700   -306       C  
ATOM   1931  O   TYR B  35      14.659   4.383 -77.749  1.00 34.40           O  
ANISOU 1931  O   TYR B  35     4099   3741   5230   -374    662   -321       O  
ATOM   1932  CB  TYR B  35      16.054   3.767 -80.473  1.00 39.94           C  
ANISOU 1932  CB  TYR B  35     4710   4480   5987   -367    746   -228       C  
ATOM   1933  CG  TYR B  35      16.707   4.097 -81.787  1.00 48.22           C  
ANISOU 1933  CG  TYR B  35     5720   5530   7070   -368    780   -180       C  
ATOM   1934  CD1 TYR B  35      17.893   4.817 -81.842  1.00 52.94           C  
ANISOU 1934  CD1 TYR B  35     6271   6110   7735   -383    756   -135       C  
ATOM   1935  CD2 TYR B  35      16.105   3.765 -82.973  1.00 51.30           C  
ANISOU 1935  CD2 TYR B  35     6127   5938   7428   -353    832   -176       C  
ATOM   1936  CE1 TYR B  35      18.497   5.113 -83.061  1.00 55.21           C  
ANISOU 1936  CE1 TYR B  35     6523   6398   8056   -380    796    -85       C  
ATOM   1937  CE2 TYR B  35      16.704   4.045 -84.198  1.00 53.92           C  
ANISOU 1937  CE2 TYR B  35     6433   6268   7784   -350    869   -131       C  
ATOM   1938  CZ  TYR B  35      17.918   4.687 -84.234  1.00 56.22           C  
ANISOU 1938  CZ  TYR B  35     6673   6544   8142   -361    857    -85       C  
ATOM   1939  OH  TYR B  35      18.533   4.889 -85.430  1.00 59.23           O  
ANISOU 1939  OH  TYR B  35     7030   6924   8548   -353    903    -36       O  
ATOM   1940  N   TRP B  36      13.125   4.069 -79.410  1.00 33.86           N  
ANISOU 1940  N   TRP B  36     4035   3703   5126   -353    737   -324       N  
ATOM   1941  CA  TRP B  36      12.044   3.559 -78.587  1.00 32.55           C  
ANISOU 1941  CA  TRP B  36     3909   3541   4917   -338    742   -362       C  
ATOM   1942  C   TRP B  36      11.615   2.257 -79.150  1.00 34.63           C  
ANISOU 1942  C   TRP B  36     4175   3834   5149   -322    782   -360       C  
ATOM   1943  O   TRP B  36      11.410   2.148 -80.344  1.00 33.67           O  
ANISOU 1943  O   TRP B  36     4044   3724   5027   -322    809   -341       O  
ATOM   1944  CB  TRP B  36      10.896   4.567 -78.538  1.00 31.00           C  
ANISOU 1944  CB  TRP B  36     3736   3325   4718   -336    740   -380       C  
ATOM   1945  CG  TRP B  36      11.364   5.844 -77.920  1.00 31.70           C  
ANISOU 1945  CG  TRP B  36     3833   3378   4835   -351    698   -385       C  
ATOM   1946  CD1 TRP B  36      11.927   6.914 -78.543  1.00 34.51           C  
ANISOU 1946  CD1 TRP B  36     4163   3718   5232   -369    680   -361       C  
ATOM   1947  CD2 TRP B  36      11.376   6.133 -76.527  1.00 31.63           C  
ANISOU 1947  CD2 TRP B  36     3867   3342   4811   -350    666   -414       C  
ATOM   1948  NE1 TRP B  36      12.258   7.879 -77.620  1.00 34.25           N  
ANISOU 1948  NE1 TRP B  36     4153   3647   5213   -381    634   -375       N  
ATOM   1949  CE2 TRP B  36      11.885   7.442 -76.376  1.00 35.00           C  
ANISOU 1949  CE2 TRP B  36     4296   3731   5270   -369    625   -409       C  
ATOM   1950  CE3 TRP B  36      10.845   5.482 -75.405  1.00 33.17           C  
ANISOU 1950  CE3 TRP B  36     4105   3533   4964   -332    670   -445       C  
ATOM   1951  CZ2 TRP B  36      11.979   8.059 -75.140  1.00 34.23           C  
ANISOU 1951  CZ2 TRP B  36     4251   3594   5161   -374    584   -436       C  
ATOM   1952  CZ3 TRP B  36      10.932   6.111 -74.173  1.00 35.18           C  
ANISOU 1952  CZ3 TRP B  36     4412   3750   5205   -335    635   -471       C  
ATOM   1953  CH2 TRP B  36      11.458   7.399 -74.059  1.00 35.51           C  
ANISOU 1953  CH2 TRP B  36     4464   3754   5276   -355    592   -468       C  
ATOM   1954  N   VAL B  37      11.576   1.251 -78.295  1.00 32.61           N  
ANISOU 1954  N   VAL B  37     3934   3588   4867   -311    783   -378       N  
ATOM   1955  CA  VAL B  37      11.247  -0.110 -78.633  1.00 31.63           C  
ANISOU 1955  CA  VAL B  37     3816   3489   4712   -297    815   -378       C  
ATOM   1956  C   VAL B  37      10.221  -0.613 -77.627  1.00 35.01           C  
ANISOU 1956  C   VAL B  37     4276   3919   5109   -283    815   -409       C  
ATOM   1957  O   VAL B  37      10.387  -0.391 -76.431  1.00 33.49           O  
ANISOU 1957  O   VAL B  37     4100   3713   4913   -282    791   -428       O  
ATOM   1958  CB  VAL B  37      12.560  -0.985 -78.644  1.00 34.06           C  
ANISOU 1958  CB  VAL B  37     4100   3809   5031   -296    821   -358       C  
ATOM   1959  CG1 VAL B  37      12.271  -2.465 -78.814  1.00 33.95           C  
ANISOU 1959  CG1 VAL B  37     4099   3818   4983   -280    852   -362       C  
ATOM   1960  CG2 VAL B  37      13.527  -0.516 -79.716  1.00 33.49           C  
ANISOU 1960  CG2 VAL B  37     3995   3734   4995   -304    834   -319       C  
ATOM   1961  N   ARG B  38       9.179  -1.319 -78.100  1.00 31.19           N  
ANISOU 1961  N   ARG B  38     3802   3447   4601   -273    841   -411       N  
ATOM   1962  CA  ARG B  38       8.220  -1.909 -77.182  1.00 31.29           C  
ANISOU 1962  CA  ARG B  38     3838   3461   4588   -258    846   -432       C  
ATOM   1963  C   ARG B  38       8.159  -3.431 -77.274  1.00 31.54           C  
ANISOU 1963  C   ARG B  38     3873   3516   4595   -248    864   -430       C  
ATOM   1964  O   ARG B  38       8.588  -4.031 -78.244  1.00 30.01           O  
ANISOU 1964  O   ARG B  38     3671   3335   4398   -252    877   -413       O  
ATOM   1965  CB  ARG B  38       6.836  -1.307 -77.348  1.00 32.31           C  
ANISOU 1965  CB  ARG B  38     3976   3579   4723   -253    855   -432       C  
ATOM   1966  CG  ARG B  38       6.065  -1.790 -78.577  1.00 32.08           C  
ANISOU 1966  CG  ARG B  38     3940   3559   4691   -257    869   -411       C  
ATOM   1967  CD  ARG B  38       4.731  -1.118 -78.564  1.00 34.71           C  
ANISOU 1967  CD  ARG B  38     4273   3875   5040   -253    872   -404       C  
ATOM   1968  NE  ARG B  38       3.824  -1.684 -79.534  1.00 40.61           N  
ANISOU 1968  NE  ARG B  38     5016   4627   5786   -260    875   -381       N  
ATOM   1969  CZ  ARG B  38       2.597  -1.249 -79.768  1.00 48.37           C  
ANISOU 1969  CZ  ARG B  38     5991   5595   6791   -261    875   -362       C  
ATOM   1970  NH1 ARG B  38       2.113  -0.199 -79.104  1.00 37.58           N  
ANISOU 1970  NH1 ARG B  38     4621   4208   5451   -249    882   -366       N  
ATOM   1971  NH2 ARG B  38       1.848  -1.841 -80.678  1.00 38.86           N  
ANISOU 1971  NH2 ARG B  38     4787   4393   5587   -273    867   -337       N  
ATOM   1972  N   GLN B  39       7.636  -4.025 -76.233  1.00 29.88           N  
ANISOU 1972  N   GLN B  39     3679   3307   4366   -234    866   -447       N  
ATOM   1973  CA  GLN B  39       7.390  -5.464 -76.115  1.00 30.36           C  
ANISOU 1973  CA  GLN B  39     3745   3386   4402   -224    880   -448       C  
ATOM   1974  C   GLN B  39       6.004  -5.705 -75.576  1.00 34.81           C  
ANISOU 1974  C   GLN B  39     4323   3946   4957   -210    891   -453       C  
ATOM   1975  O   GLN B  39       5.755  -5.567 -74.381  1.00 33.82           O  
ANISOU 1975  O   GLN B  39     4214   3812   4824   -197    892   -469       O  
ATOM   1976  CB  GLN B  39       8.434  -6.164 -75.239  1.00 30.83           C  
ANISOU 1976  CB  GLN B  39     3805   3454   4453   -220    871   -456       C  
ATOM   1977  CG  GLN B  39       8.379  -7.671 -75.410  1.00 41.11           C  
ANISOU 1977  CG  GLN B  39     5109   4777   5735   -212    888   -452       C  
ATOM   1978  CD  GLN B  39       9.561  -8.388 -74.829  1.00 44.67           C  
ANISOU 1978  CD  GLN B  39     5551   5235   6185   -210    882   -452       C  
ATOM   1979  OE1 GLN B  39      10.115  -7.983 -73.830  1.00 40.19           O  
ANISOU 1979  OE1 GLN B  39     4987   4661   5624   -213    859   -460       O  
ATOM   1980  NE2 GLN B  39       9.918  -9.511 -75.404  1.00 41.61           N  
ANISOU 1980  NE2 GLN B  39     5159   4862   5790   -205    901   -440       N  
ATOM   1981  N   ALA B  40       5.081  -6.025 -76.476  1.00 33.97           N  
ANISOU 1981  N   ALA B  40     4211   3841   4853   -214    899   -436       N  
ATOM   1982  CA  ALA B  40       3.689  -6.306 -76.076  1.00 33.63           C  
ANISOU 1982  CA  ALA B  40     4172   3793   4814   -201    910   -428       C  
ATOM   1983  C   ALA B  40       3.581  -7.701 -75.478  1.00 35.26           C  
ANISOU 1983  C   ALA B  40     4385   4014   4999   -190    917   -433       C  
ATOM   1984  O   ALA B  40       4.453  -8.530 -75.715  1.00 32.26           O  
ANISOU 1984  O   ALA B  40     4007   3648   4601   -194    914   -437       O  
ATOM   1985  CB  ALA B  40       2.739  -6.143 -77.259  1.00 34.07           C  
ANISOU 1985  CB  ALA B  40     4218   3841   4888   -215    905   -401       C  
ATOM   1986  N   PRO B  41       2.541  -7.965 -74.661  1.00 35.12           N  
ANISOU 1986  N   PRO B  41     4369   3989   4985   -172    931   -428       N  
ATOM   1987  CA  PRO B  41       2.418  -9.295 -74.011  1.00 36.32           C  
ANISOU 1987  CA  PRO B  41     4526   4155   5118   -160    939   -430       C  
ATOM   1988  C   PRO B  41       2.375 -10.474 -74.998  1.00 40.14           C  
ANISOU 1988  C   PRO B  41     5007   4651   5594   -174    928   -416       C  
ATOM   1989  O   PRO B  41       1.650 -10.448 -75.972  1.00 38.42           O  
ANISOU 1989  O   PRO B  41     4783   4425   5390   -188    917   -393       O  
ATOM   1990  CB  PRO B  41       1.107  -9.198 -73.206  1.00 37.12           C  
ANISOU 1990  CB  PRO B  41     4625   4243   5236   -139    961   -416       C  
ATOM   1991  CG  PRO B  41       0.679  -7.848 -73.257  1.00 40.43           C  
ANISOU 1991  CG  PRO B  41     5043   4641   5679   -136    969   -412       C  
ATOM   1992  CD  PRO B  41       1.457  -7.062 -74.256  1.00 36.55           C  
ANISOU 1992  CD  PRO B  41     4547   4149   5191   -159    947   -418       C  
ATOM   1993  N   GLY B  42       3.172 -11.476 -74.732  1.00 41.17           N  
ANISOU 1993  N   GLY B  42     5146   4797   5702   -171    928   -428       N  
ATOM   1994  CA  GLY B  42       3.345 -12.622 -75.624  1.00 43.77           C  
ANISOU 1994  CA  GLY B  42     5482   5133   6015   -182    921   -419       C  
ATOM   1995  C   GLY B  42       4.019 -12.322 -76.960  1.00 50.59           C  
ANISOU 1995  C   GLY B  42     6354   5993   6873   -199    915   -415       C  
ATOM   1996  O   GLY B  42       3.843 -13.080 -77.917  1.00 51.75           O  
ANISOU 1996  O   GLY B  42     6521   6136   7006   -209    909   -403       O  
ATOM   1997  N   GLN B  43       4.769 -11.189 -77.065  1.00 43.80           N  
ANISOU 1997  N   GLN B  43     5486   5131   6024   -202    917   -422       N  
ATOM   1998  CA  GLN B  43       5.366 -10.751 -78.317  1.00 39.77           C  
ANISOU 1998  CA  GLN B  43     4982   4616   5512   -216    917   -413       C  
ATOM   1999  C   GLN B  43       6.834 -10.559 -78.191  1.00 39.03           C  
ANISOU 1999  C   GLN B  43     4879   4529   5421   -212    928   -420       C  
ATOM   2000  O   GLN B  43       7.402 -10.536 -77.092  1.00 38.06           O  
ANISOU 2000  O   GLN B  43     4744   4413   5304   -203    926   -432       O  
ATOM   2001  CB  GLN B  43       4.757  -9.396 -78.775  1.00 41.08           C  
ANISOU 2001  CB  GLN B  43     5140   4768   5701   -227    907   -403       C  
ATOM   2002  CG  GLN B  43       3.242  -9.323 -78.821  1.00 48.21           C  
ANISOU 2002  CG  GLN B  43     6040   5659   6618   -231    895   -387       C  
ATOM   2003  CD  GLN B  43       2.709 -10.529 -79.574  1.00 63.34           C  
ANISOU 2003  CD  GLN B  43     7979   7573   8516   -241    884   -372       C  
ATOM   2004  OE1 GLN B  43       3.178 -10.845 -80.672  1.00 55.16           O  
ANISOU 2004  OE1 GLN B  43     6968   6532   7456   -252    881   -367       O  
ATOM   2005  NE2 GLN B  43       1.769 -11.258 -79.000  1.00 50.08           N  
ANISOU 2005  NE2 GLN B  43     6293   5892   6843   -235    878   -363       N  
ATOM   2006  N   GLY B  44       7.429 -10.303 -79.338  1.00 34.38           N  
ANISOU 2006  N   GLY B  44     4297   3935   4830   -220    937   -407       N  
ATOM   2007  CA  GLY B  44       8.835  -9.947 -79.430  1.00 33.91           C  
ANISOU 2007  CA  GLY B  44     4221   3878   4785   -217    950   -402       C  
ATOM   2008  C   GLY B  44       9.012  -8.457 -79.306  1.00 36.26           C  
ANISOU 2008  C   GLY B  44     4497   4167   5111   -227    936   -401       C  
ATOM   2009  O   GLY B  44       8.118  -7.742 -78.835  1.00 37.41           O  
ANISOU 2009  O   GLY B  44     4641   4307   5265   -231    919   -410       O  
ATOM   2010  N   LEU B  45      10.115  -7.975 -79.831  1.00 32.50           N  
ANISOU 2010  N   LEU B  45     4006   3689   4655   -230    946   -385       N  
ATOM   2011  CA  LEU B  45      10.493  -6.558 -79.826  1.00 31.12           C  
ANISOU 2011  CA  LEU B  45     3809   3504   4511   -241    931   -378       C  
ATOM   2012  C   LEU B  45      10.021  -5.823 -81.063  1.00 35.73           C  
ANISOU 2012  C   LEU B  45     4403   4079   5095   -251    937   -365       C  
ATOM   2013  O   LEU B  45      10.235  -6.284 -82.179  1.00 37.26           O  
ANISOU 2013  O   LEU B  45     4614   4271   5271   -249    962   -349       O  
ATOM   2014  CB  LEU B  45      12.013  -6.449 -79.703  1.00 30.73           C  
ANISOU 2014  CB  LEU B  45     3730   3454   4493   -240    937   -359       C  
ATOM   2015  CG  LEU B  45      12.608  -7.102 -78.467  1.00 34.21           C  
ANISOU 2015  CG  LEU B  45     4158   3901   4940   -234    923   -367       C  
ATOM   2016  CD1 LEU B  45      14.099  -7.199 -78.590  1.00 35.17           C  
ANISOU 2016  CD1 LEU B  45     4244   4019   5098   -233    932   -335       C  
ATOM   2017  CD2 LEU B  45      12.181  -6.343 -77.202  1.00 35.68           C  
ANISOU 2017  CD2 LEU B  45     4348   4079   5130   -242    883   -390       C  
ATOM   2018  N   GLU B  46       9.517  -4.603 -80.870  1.00 32.98           N  
ANISOU 2018  N   GLU B  46     4045   3720   4766   -261    915   -369       N  
ATOM   2019  CA  GLU B  46       9.031  -3.767 -81.961  1.00 31.89           C  
ANISOU 2019  CA  GLU B  46     3912   3572   4633   -273    915   -355       C  
ATOM   2020  C   GLU B  46       9.630  -2.376 -81.944  1.00 34.59           C  
ANISOU 2020  C   GLU B  46     4228   3903   5013   -283    902   -346       C  
ATOM   2021  O   GLU B  46       9.457  -1.654 -80.969  1.00 34.59           O  
ANISOU 2021  O   GLU B  46     4218   3893   5030   -285    880   -362       O  
ATOM   2022  CB  GLU B  46       7.521  -3.718 -81.866  1.00 33.27           C  
ANISOU 2022  CB  GLU B  46     4101   3741   4799   -277    900   -362       C  
ATOM   2023  CG  GLU B  46       6.823  -3.023 -83.008  1.00 45.15           C  
ANISOU 2023  CG  GLU B  46     5614   5234   6307   -292    894   -344       C  
ATOM   2024  CD  GLU B  46       5.313  -3.117 -82.902  1.00 64.82           C  
ANISOU 2024  CD  GLU B  46     8112   7717   8799   -296    878   -342       C  
ATOM   2025  OE1 GLU B  46       4.791  -3.509 -81.830  1.00 71.78           O  
ANISOU 2025  OE1 GLU B  46     8988   8602   9683   -283    877   -356       O  
ATOM   2026  OE2 GLU B  46       4.645  -2.756 -83.894  1.00 62.37           O  
ANISOU 2026  OE2 GLU B  46     7811   7396   8490   -311    866   -321       O  
ATOM   2027  N   TRP B  47      10.302  -1.971 -83.040  1.00 32.14           N  
ANISOU 2027  N   TRP B  47     3911   3589   4712   -289    918   -320       N  
ATOM   2028  CA  TRP B  47      10.854  -0.629 -83.132  1.00 34.70           C  
ANISOU 2028  CA  TRP B  47     4207   3900   5076   -300    905   -307       C  
ATOM   2029  C   TRP B  47       9.749   0.376 -83.357  1.00 39.03           C  
ANISOU 2029  C   TRP B  47     4763   4437   5631   -311    886   -312       C  
ATOM   2030  O   TRP B  47       8.902   0.163 -84.220  1.00 40.36           O  
ANISOU 2030  O   TRP B  47     4953   4605   5778   -315    892   -305       O  
ATOM   2031  CB  TRP B  47      11.900  -0.548 -84.268  1.00 34.98           C  
ANISOU 2031  CB  TRP B  47     4233   3935   5124   -300    935   -272       C  
ATOM   2032  CG  TRP B  47      12.376   0.831 -84.523  1.00 36.63           C  
ANISOU 2032  CG  TRP B  47     4413   4130   5375   -313    921   -252       C  
ATOM   2033  CD1 TRP B  47      13.183   1.575 -83.722  1.00 39.67           C  
ANISOU 2033  CD1 TRP B  47     4763   4506   5806   -321    894   -248       C  
ATOM   2034  CD2 TRP B  47      12.131   1.621 -85.691  1.00 37.43           C  
ANISOU 2034  CD2 TRP B  47     4518   4223   5479   -322    929   -231       C  
ATOM   2035  NE1 TRP B  47      13.414   2.802 -84.300  1.00 40.39           N  
ANISOU 2035  NE1 TRP B  47     4834   4583   5930   -334    886   -226       N  
ATOM   2036  CE2 TRP B  47      12.835   2.832 -85.532  1.00 41.38           C  
ANISOU 2036  CE2 TRP B  47     4982   4711   6031   -334    911   -214       C  
ATOM   2037  CE3 TRP B  47      11.427   1.411 -86.879  1.00 38.87           C  
ANISOU 2037  CE3 TRP B  47     4737   4405   5626   -324    948   -222       C  
ATOM   2038  CZ2 TRP B  47      12.831   3.832 -86.491  1.00 39.69           C  
ANISOU 2038  CZ2 TRP B  47     4760   4487   5835   -344    915   -189       C  
ATOM   2039  CZ3 TRP B  47      11.450   2.408 -87.841  1.00 39.84           C  
ANISOU 2039  CZ3 TRP B  47     4857   4517   5763   -336    950   -197       C  
ATOM   2040  CH2 TRP B  47      12.063   3.631 -87.597  1.00 39.86           C  
ANISOU 2040  CH2 TRP B  47     4817   4510   5819   -345    933   -183       C  
ATOM   2041  N   MET B  48       9.742   1.471 -82.581  1.00 34.49           N  
ANISOU 2041  N   MET B  48     4172   3847   5086   -317    860   -322       N  
ATOM   2042  CA  MET B  48       8.718   2.519 -82.725  1.00 33.91           C  
ANISOU 2042  CA  MET B  48     4101   3758   5027   -325    846   -324       C  
ATOM   2043  C   MET B  48       9.229   3.706 -83.482  1.00 38.95           C  
ANISOU 2043  C   MET B  48     4720   4384   5697   -339    839   -302       C  
ATOM   2044  O   MET B  48       8.579   4.176 -84.402  1.00 40.51           O  
ANISOU 2044  O   MET B  48     4920   4575   5895   -348    842   -286       O  
ATOM   2045  CB  MET B  48       8.190   2.944 -81.364  1.00 35.50           C  
ANISOU 2045  CB  MET B  48     4309   3944   5235   -318    828   -352       C  
ATOM   2046  CG  MET B  48       7.388   1.814 -80.663  1.00 39.62           C  
ANISOU 2046  CG  MET B  48     4851   4477   5726   -302    839   -371       C  
ATOM   2047  SD  MET B  48       7.066   2.367 -79.035  1.00 45.86           S  
ANISOU 2047  SD  MET B  48     5659   5245   6519   -289    826   -401       S  
ATOM   2048  CE  MET B  48       5.554   3.574 -79.402  1.00 42.04           C  
ANISOU 2048  CE  MET B  48     5175   4736   6062   -287    833   -391       C  
ATOM   2049  N   GLY B  49      10.390   4.180 -83.109  1.00 34.32           N  
ANISOU 2049  N   GLY B  49     4111   3790   5139   -344    828   -295       N  
ATOM   2050  CA  GLY B  49      10.984   5.345 -83.763  1.00 32.65           C  
ANISOU 2050  CA  GLY B  49     3874   3565   4965   -358    820   -269       C  
ATOM   2051  C   GLY B  49      12.274   5.761 -83.109  1.00 36.02           C  
ANISOU 2051  C   GLY B  49     4275   3981   5430   -366    797   -260       C  
ATOM   2052  O   GLY B  49      12.747   5.115 -82.180  1.00 35.69           O  
ANISOU 2052  O   GLY B  49     4235   3943   5383   -360    787   -272       O  
ATOM   2053  N   GLY B  50      12.860   6.818 -83.628  1.00 36.03           N  
ANISOU 2053  N   GLY B  50     4250   3968   5472   -379    786   -233       N  
ATOM   2054  CA  GLY B  50      14.110   7.377 -83.124  1.00 33.87           C  
ANISOU 2054  CA  GLY B  50     3945   3678   5248   -392    756   -213       C  
ATOM   2055  C   GLY B  50      14.203   8.855 -83.376  1.00 35.93           C  
ANISOU 2055  C   GLY B  50     4189   3913   5550   -410    728   -199       C  
ATOM   2056  O   GLY B  50      13.556   9.375 -84.289  1.00 35.68           O  
ANISOU 2056  O   GLY B  50     4160   3883   5515   -412    745   -190       O  
ATOM   2057  N   ILE B  51      14.977   9.532 -82.545  1.00 32.22           N  
ANISOU 2057  N   ILE B  51     3705   3417   5120   -427    680   -194       N  
ATOM   2058  CA  ILE B  51      15.207  10.962 -82.630  1.00 32.40           C  
ANISOU 2058  CA  ILE B  51     3713   3409   5189   -447    644   -180       C  
ATOM   2059  C   ILE B  51      16.710  11.268 -82.499  1.00 37.52           C  
ANISOU 2059  C   ILE B  51     4314   4042   5899   -466    612   -135       C  
ATOM   2060  O   ILE B  51      17.444  10.583 -81.793  1.00 37.33           O  
ANISOU 2060  O   ILE B  51     4282   4019   5882   -467    594   -129       O  
ATOM   2061  CB  ILE B  51      14.375  11.740 -81.551  1.00 35.31           C  
ANISOU 2061  CB  ILE B  51     4127   3746   5542   -451    605   -227       C  
ATOM   2062  CG1 ILE B  51      14.498  13.275 -81.783  1.00 34.47           C  
ANISOU 2062  CG1 ILE B  51     4010   3605   5481   -471    571   -212       C  
ATOM   2063  CG2 ILE B  51      14.788  11.335 -80.088  1.00 33.14           C  
ANISOU 2063  CG2 ILE B  51     3882   3456   5255   -454    563   -253       C  
ATOM   2064  CD1 ILE B  51      13.493  14.108 -81.130  1.00 38.59           C  
ANISOU 2064  CD1 ILE B  51     4579   4096   5988   -468    554   -252       C  
ATOM   2065  N   ASN B  52      17.126  12.338 -83.142  1.00 36.45           N  
ANISOU 2065  N   ASN B  52     4146   3889   5813   -481    599   -100       N  
ATOM   2066  CA  ASN B  52      18.470  12.854 -83.086  1.00 37.76           C  
ANISOU 2066  CA  ASN B  52     4261   4033   6052   -503    563    -48       C  
ATOM   2067  C   ASN B  52      18.417  14.050 -82.161  1.00 41.83           C  
ANISOU 2067  C   ASN B  52     4800   4503   6590   -529    487    -69       C  
ATOM   2068  O   ASN B  52      17.873  15.048 -82.559  1.00 40.33           O  
ANISOU 2068  O   ASN B  52     4618   4299   6407   -534    483    -75       O  
ATOM   2069  CB  ASN B  52      18.925  13.263 -84.479  1.00 36.23           C  
ANISOU 2069  CB  ASN B  52     4020   3849   5898   -501    605      9       C  
ATOM   2070  CG  ASN B  52      20.361  13.698 -84.549  1.00 50.37           C  
ANISOU 2070  CG  ASN B  52     5746   5619   7774   -520    578     76       C  
ATOM   2071  OD1 ASN B  52      21.026  13.949 -83.540  1.00 44.22           O  
ANISOU 2071  OD1 ASN B  52     4957   4812   7034   -542    510     81       O  
ATOM   2072  ND2 ASN B  52      20.883  13.771 -85.754  1.00 46.83           N  
ANISOU 2072  ND2 ASN B  52     5253   5181   7358   -511    630    132       N  
ATOM   2073  N   PRO B  53      18.965  13.969 -80.922  1.00 40.87           N  
ANISOU 2073  N   PRO B  53     4695   4355   6478   -545    424    -80       N  
ATOM   2074  CA  PRO B  53      18.912  15.123 -80.007  1.00 40.41           C  
ANISOU 2074  CA  PRO B  53     4676   4245   6432   -571    347   -103       C  
ATOM   2075  C   PRO B  53      19.653  16.372 -80.439  1.00 47.58           C  
ANISOU 2075  C   PRO B  53     5542   5120   7417   -600    304    -55       C  
ATOM   2076  O   PRO B  53      19.349  17.441 -79.897  1.00 47.13           O  
ANISOU 2076  O   PRO B  53     5526   5019   7362   -617    252    -81       O  
ATOM   2077  CB  PRO B  53      19.500  14.566 -78.699  1.00 41.50           C  
ANISOU 2077  CB  PRO B  53     4840   4364   6562   -584    290   -115       C  
ATOM   2078  CG  PRO B  53      19.313  13.044 -78.811  1.00 45.05           C  
ANISOU 2078  CG  PRO B  53     5285   4863   6970   -555    351   -123       C  
ATOM   2079  CD  PRO B  53      19.577  12.798 -80.262  1.00 41.15           C  
ANISOU 2079  CD  PRO B  53     4726   4405   6506   -541    419    -75       C  
ATOM   2080  N   SER B  54      20.656  16.265 -81.343  1.00 46.22           N  
ANISOU 2080  N   SER B  54     5290   4962   7308   -605    324     15       N  
ATOM   2081  CA  SER B  54      21.385  17.466 -81.784  1.00 46.09           C  
ANISOU 2081  CA  SER B  54     5228   4913   7373   -633    284     68       C  
ATOM   2082  C   SER B  54      20.499  18.336 -82.670  1.00 46.40           C  
ANISOU 2082  C   SER B  54     5276   4956   7399   -624    319     55       C  
ATOM   2083  O   SER B  54      20.516  19.537 -82.506  1.00 46.22           O  
ANISOU 2083  O   SER B  54     5260   4893   7410   -648    267     57       O  
ATOM   2084  CB  SER B  54      22.694  17.110 -82.496  1.00 49.96           C  
ANISOU 2084  CB  SER B  54     5627   5415   7940   -637    303    155       C  
ATOM   2085  OG  SER B  54      22.384  16.505 -83.739  1.00 64.77           O  
ANISOU 2085  OG  SER B  54     7480   7338   9793   -603    403    171       O  
ATOM   2086  N   ASN B  55      19.684  17.763 -83.537  1.00 41.55           N  
ANISOU 2086  N   ASN B  55     4668   4384   6735   -594    400     40       N  
ATOM   2087  CA  ASN B  55      18.849  18.604 -84.409  1.00 41.01           C  
ANISOU 2087  CA  ASN B  55     4605   4317   6659   -589    427     34       C  
ATOM   2088  C   ASN B  55      17.339  18.282 -84.443  1.00 41.95           C  
ANISOU 2088  C   ASN B  55     4781   4455   6701   -565    468    -26       C  
ATOM   2089  O   ASN B  55      16.628  18.885 -85.240  1.00 42.95           O  
ANISOU 2089  O   ASN B  55     4909   4585   6824   -561    493    -24       O  
ATOM   2090  CB  ASN B  55      19.416  18.549 -85.825  1.00 41.19           C  
ANISOU 2090  CB  ASN B  55     4567   4365   6719   -582    483    100       C  
ATOM   2091  CG  ASN B  55      19.308  17.188 -86.477  1.00 48.79           C  
ANISOU 2091  CG  ASN B  55     5530   5375   7635   -552    560    104       C  
ATOM   2092  OD1 ASN B  55      18.449  16.369 -86.181  1.00 49.96           O  
ANISOU 2092  OD1 ASN B  55     5725   5544   7715   -534    583     54       O  
ATOM   2093  ND2 ASN B  55      20.256  16.857 -87.271  1.00 47.27           N  
ANISOU 2093  ND2 ASN B  55     5286   5195   7479   -545    601    167       N  
ATOM   2094  N   GLY B  56      16.881  17.282 -83.698  1.00 36.55           N  
ANISOU 2094  N   GLY B  56     4138   3787   5962   -548    479    -69       N  
ATOM   2095  CA  GLY B  56      15.476  16.917 -83.679  1.00 34.69           C  
ANISOU 2095  CA  GLY B  56     3950   3567   5662   -525    516   -118       C  
ATOM   2096  C   GLY B  56      14.953  16.119 -84.842  1.00 39.20           C  
ANISOU 2096  C   GLY B  56     4511   4183   6201   -505    584   -105       C  
ATOM   2097  O   GLY B  56      13.740  15.919 -84.937  1.00 37.43           O  
ANISOU 2097  O   GLY B  56     4319   3969   5934   -491    608   -136       O  
ATOM   2098  N   GLY B  57      15.834  15.607 -85.700  1.00 37.24           N  
ANISOU 2098  N   GLY B  57     4222   3958   5971   -504    615    -58       N  
ATOM   2099  CA  GLY B  57      15.377  14.787 -86.811  1.00 36.43           C  
ANISOU 2099  CA  GLY B  57     4123   3890   5827   -485    678    -47       C  
ATOM   2100  C   GLY B  57      14.841  13.458 -86.311  1.00 38.08           C  
ANISOU 2100  C   GLY B  57     4368   4123   5977   -466    699    -84       C  
ATOM   2101  O   GLY B  57      15.356  12.918 -85.340  1.00 34.37           O  
ANISOU 2101  O   GLY B  57     3900   3652   5508   -465    679    -98       O  
ATOM   2102  N   THR B  58      13.768  12.947 -86.928  1.00 37.84           N  
ANISOU 2102  N   THR B  58     4368   4113   5897   -453    734   -100       N  
ATOM   2103  CA  THR B  58      13.142  11.713 -86.483  1.00 38.82           C  
ANISOU 2103  CA  THR B  58     4526   4257   5967   -436    751   -134       C  
ATOM   2104  C   THR B  58      12.885  10.721 -87.601  1.00 43.77           C  
ANISOU 2104  C   THR B  58     5169   4911   6551   -424    800   -119       C  
ATOM   2105  O   THR B  58      12.816  11.077 -88.778  1.00 42.51           O  
ANISOU 2105  O   THR B  58     5008   4753   6392   -428    821    -89       O  
ATOM   2106  CB  THR B  58      11.774  11.998 -85.811  1.00 43.38           C  
ANISOU 2106  CB  THR B  58     5136   4822   6522   -433    734   -176       C  
ATOM   2107  OG1 THR B  58      10.947  12.692 -86.742  1.00 49.57           O  
ANISOU 2107  OG1 THR B  58     5921   5602   7310   -439    741   -163       O  
ATOM   2108  CG2 THR B  58      11.894  12.767 -84.515  1.00 41.68           C  
ANISOU 2108  CG2 THR B  58     4928   4576   6331   -439    690   -203       C  
ATOM   2109  N   ASN B  59      12.687   9.467 -87.191  1.00 39.48           N  
ANISOU 2109  N   ASN B  59     4649   4386   5966   -409    816   -141       N  
ATOM   2110  CA  ASN B  59      12.233   8.391 -88.064  1.00 39.15           C  
ANISOU 2110  CA  ASN B  59     4638   4364   5872   -398    855   -137       C  
ATOM   2111  C   ASN B  59      11.246   7.592 -87.257  1.00 43.66           C  
ANISOU 2111  C   ASN B  59     5239   4943   6407   -389    846   -178       C  
ATOM   2112  O   ASN B  59      11.382   7.486 -86.053  1.00 43.40           O  
ANISOU 2112  O   ASN B  59     5200   4906   6382   -386    825   -203       O  
ATOM   2113  CB  ASN B  59      13.366   7.505 -88.599  1.00 38.60           C  
ANISOU 2113  CB  ASN B  59     4564   4308   5796   -384    898   -108       C  
ATOM   2114  CG  ASN B  59      14.047   8.109 -89.816  1.00 61.38           C  
ANISOU 2114  CG  ASN B  59     7433   7186   8702   -386    927    -60       C  
ATOM   2115  OD1 ASN B  59      13.431   8.376 -90.864  1.00 56.63           O  
ANISOU 2115  OD1 ASN B  59     6859   6584   8075   -391    939    -48       O  
ATOM   2116  ND2 ASN B  59      15.316   8.396 -89.703  1.00 54.42           N  
ANISOU 2116  ND2 ASN B  59     6507   6299   7871   -385    935    -26       N  
ATOM   2117  N   PHE B  60      10.221   7.097 -87.915  1.00 41.92           N  
ANISOU 2117  N   PHE B  60     5050   4729   6147   -388    856   -181       N  
ATOM   2118  CA  PHE B  60       9.150   6.365 -87.298  1.00 41.14           C  
ANISOU 2118  CA  PHE B  60     4975   4635   6019   -382    848   -211       C  
ATOM   2119  C   PHE B  60       8.855   5.137 -88.068  1.00 45.37           C  
ANISOU 2119  C   PHE B  60     5547   5185   6506   -377    870   -205       C  
ATOM   2120  O   PHE B  60       9.012   5.103 -89.286  1.00 45.38           O  
ANISOU 2120  O   PHE B  60     5568   5186   6489   -382    887   -179       O  
ATOM   2121  CB  PHE B  60       7.880   7.211 -87.311  1.00 42.23           C  
ANISOU 2121  CB  PHE B  60     5115   4758   6173   -391    825   -214       C  
ATOM   2122  CG  PHE B  60       7.950   8.345 -86.362  1.00 44.01           C  
ANISOU 2122  CG  PHE B  60     5319   4964   6441   -392    804   -228       C  
ATOM   2123  CD1 PHE B  60       8.040   8.116 -85.005  1.00 48.01           C  
ANISOU 2123  CD1 PHE B  60     5828   5466   6946   -380    795   -259       C  
ATOM   2124  CD2 PHE B  60       8.137   9.637 -86.818  1.00 46.87           C  
ANISOU 2124  CD2 PHE B  60     5661   5309   6840   -405    791   -209       C  
ATOM   2125  CE1 PHE B  60       8.251   9.158 -84.120  1.00 48.51           C  
ANISOU 2125  CE1 PHE B  60     5885   5505   7041   -382    773   -273       C  
ATOM   2126  CE2 PHE B  60       8.294  10.692 -85.911  1.00 48.70           C  
ANISOU 2126  CE2 PHE B  60     5879   5516   7108   -407    768   -224       C  
ATOM   2127  CZ  PHE B  60       8.328  10.443 -84.569  1.00 44.70           C  
ANISOU 2127  CZ  PHE B  60     5386   5002   6595   -395    759   -257       C  
ATOM   2128  N   ASN B  61       8.337   4.168 -87.348  1.00 41.75           N  
ANISOU 2128  N   ASN B  61     5104   4735   6024   -367    868   -229       N  
ATOM   2129  CA  ASN B  61       7.770   2.966 -87.889  1.00 42.70           C  
ANISOU 2129  CA  ASN B  61     5263   4863   6097   -365    878   -229       C  
ATOM   2130  C   ASN B  61       6.359   3.427 -88.371  1.00 47.32           C  
ANISOU 2130  C   ASN B  61     5859   5436   6685   -381    852   -219       C  
ATOM   2131  O   ASN B  61       5.622   4.031 -87.596  1.00 44.99           O  
ANISOU 2131  O   ASN B  61     5541   5132   6421   -381    833   -229       O  
ATOM   2132  CB  ASN B  61       7.700   1.916 -86.797  1.00 39.59           C  
ANISOU 2132  CB  ASN B  61     4872   4481   5688   -350    881   -256       C  
ATOM   2133  CG  ASN B  61       7.089   0.603 -87.225  1.00 49.34           C  
ANISOU 2133  CG  ASN B  61     6147   5722   6877   -348    886   -257       C  
ATOM   2134  OD1 ASN B  61       6.220   0.543 -88.081  1.00 49.28           O  
ANISOU 2134  OD1 ASN B  61     6167   5705   6852   -362    872   -242       O  
ATOM   2135  ND2 ASN B  61       7.387  -0.449 -86.508  1.00 41.96           N  
ANISOU 2135  ND2 ASN B  61     5218   4800   5926   -333    897   -275       N  
ATOM   2136  N   GLU B  62       6.026   3.171 -89.659  1.00 46.08           N  
ANISOU 2136  N   GLU B  62     5739   5273   6497   -394    850   -195       N  
ATOM   2137  CA  GLU B  62       4.770   3.596 -90.316  1.00 45.10           C  
ANISOU 2137  CA  GLU B  62     5625   5132   6379   -416    818   -175       C  
ATOM   2138  C   GLU B  62       3.532   3.158 -89.539  1.00 46.83           C  
ANISOU 2138  C   GLU B  62     5836   5348   6610   -415    795   -183       C  
ATOM   2139  O   GLU B  62       2.523   3.849 -89.563  1.00 46.15           O  
ANISOU 2139  O   GLU B  62     5731   5247   6558   -427    770   -166       O  
ATOM   2140  CB  GLU B  62       4.680   3.083 -91.778  1.00 46.27           C  
ANISOU 2140  CB  GLU B  62     5831   5271   6476   -431    815   -150       C  
ATOM   2141  N   LYS B  63       3.611   2.038 -88.844  1.00 42.93           N  
ANISOU 2141  N   LYS B  63     5352   4867   6094   -400    805   -204       N  
ATOM   2142  CA  LYS B  63       2.508   1.542 -88.022  1.00 44.17           C  
ANISOU 2142  CA  LYS B  63     5498   5021   6264   -396    790   -210       C  
ATOM   2143  C   LYS B  63       2.080   2.560 -86.912  1.00 50.62           C  
ANISOU 2143  C   LYS B  63     6269   5830   7134   -383    792   -219       C  
ATOM   2144  O   LYS B  63       0.917   2.555 -86.517  1.00 49.56           O  
ANISOU 2144  O   LYS B  63     6121   5684   7026   -382    781   -206       O  
ATOM   2145  CB  LYS B  63       2.919   0.193 -87.388  1.00 47.03           C  
ANISOU 2145  CB  LYS B  63     5877   5400   6592   -379    807   -233       C  
ATOM   2146  CG  LYS B  63       1.960  -0.342 -86.358  1.00 63.45           C  
ANISOU 2146  CG  LYS B  63     7941   7479   8687   -369    800   -241       C  
ATOM   2147  CD  LYS B  63       2.322  -1.752 -85.933  1.00 67.90           C  
ANISOU 2147  CD  LYS B  63     8526   8058   9214   -356    813   -259       C  
ATOM   2148  CE  LYS B  63       1.711  -2.050 -84.566  1.00 70.75           C  
ANISOU 2148  CE  LYS B  63     8863   8423   9596   -337    818   -273       C  
ATOM   2149  NZ  LYS B  63       1.875  -3.465 -84.174  1.00 74.55           N  
ANISOU 2149  NZ  LYS B  63     9363   8917  10045   -328    826   -286       N  
ATOM   2150  N   PHE B  64       3.027   3.370 -86.389  1.00 49.19           N  
ANISOU 2150  N   PHE B  64     6071   5652   6969   -373    808   -237       N  
ATOM   2151  CA  PHE B  64       2.792   4.369 -85.339  1.00 50.11           C  
ANISOU 2151  CA  PHE B  64     6161   5755   7125   -361    811   -251       C  
ATOM   2152  C   PHE B  64       2.885   5.794 -85.846  1.00 64.07           C  
ANISOU 2152  C   PHE B  64     7911   7505   8927   -372    802   -235       C  
ATOM   2153  O   PHE B  64       2.515   6.710 -85.092  1.00 65.42           O  
ANISOU 2153  O   PHE B  64     8066   7657   9132   -363    803   -243       O  
ATOM   2154  CB  PHE B  64       3.835   4.257 -84.232  1.00 50.18           C  
ANISOU 2154  CB  PHE B  64     6169   5772   7125   -344    824   -284       C  
ATOM   2155  CG  PHE B  64       3.937   2.902 -83.618  1.00 49.53           C  
ANISOU 2155  CG  PHE B  64     6101   5707   7010   -331    834   -301       C  
ATOM   2156  CD1 PHE B  64       2.967   2.451 -82.738  1.00 52.38           C  
ANISOU 2156  CD1 PHE B  64     6465   6064   7374   -315    839   -309       C  
ATOM   2157  CD2 PHE B  64       4.968   2.053 -83.960  1.00 48.19           C  
ANISOU 2157  CD2 PHE B  64     5944   5556   6810   -332    843   -305       C  
ATOM   2158  CE1 PHE B  64       3.041   1.182 -82.207  1.00 54.11           C  
ANISOU 2158  CE1 PHE B  64     6696   6299   7563   -304    848   -323       C  
ATOM   2159  CE2 PHE B  64       5.056   0.794 -83.415  1.00 52.61           C  
ANISOU 2159  CE2 PHE B  64     6517   6131   7342   -319    852   -320       C  
ATOM   2160  CZ  PHE B  64       4.079   0.351 -82.560  1.00 52.45           C  
ANISOU 2160  CZ  PHE B  64     6498   6108   7321   -308    852   -329       C  
ATOM   2161  N   LYS B  65       3.456   6.026 -87.066  1.00 63.50           N  
ANISOU 2161  N   LYS B  65     7846   7438   8845   -391    796   -215       N  
ATOM   2162  CA  LYS B  65       3.496   7.376 -87.611  1.00 63.55           C  
ANISOU 2162  CA  LYS B  65     7833   7427   8886   -404    786   -196       C  
ATOM   2163  C   LYS B  65       2.043   7.889 -87.503  1.00 67.71           C  
ANISOU 2163  C   LYS B  65     8345   7933   9448   -406    772   -179       C  
ATOM   2164  O   LYS B  65       1.098   7.108 -87.716  1.00 71.45           O  
ANISOU 2164  O   LYS B  65     8828   8407   9913   -410    763   -163       O  
ATOM   2165  CB  LYS B  65       4.007   7.402 -89.065  1.00 65.24           C  
ANISOU 2165  CB  LYS B  65     8063   7646   9078   -423    784   -169       C  
ATOM   2166  N   ASN B  66       1.886   9.112 -87.001  1.00 59.28           N  
ANISOU 2166  N   ASN B  66     7256   6845   8424   -400    773   -182       N  
ATOM   2167  CA  ASN B  66       0.608   9.802 -86.732  1.00 58.42           C  
ANISOU 2167  CA  ASN B  66     7126   6709   8361   -395    771   -164       C  
ATOM   2168  C   ASN B  66       0.175   9.736 -85.276  1.00 56.53           C  
ANISOU 2168  C   ASN B  66     6888   6458   8134   -364    794   -189       C  
ATOM   2169  O   ASN B  66      -0.662  10.538 -84.902  1.00 57.84           O  
ANISOU 2169  O   ASN B  66     7038   6596   8343   -353    804   -177       O  
ATOM   2170  CB  ASN B  66      -0.561   9.386 -87.639  1.00 61.21           C  
ANISOU 2170  CB  ASN B  66     7475   7058   8725   -413    751   -121       C  
ATOM   2171  CG  ASN B  66      -0.289   9.612 -89.121  1.00 87.60           C  
ANISOU 2171  CG  ASN B  66    10827  10403  12053   -444    726    -92       C  
ATOM   2172  OD1 ASN B  66       0.409  10.577 -89.516  1.00 70.31           O  
ANISOU 2172  OD1 ASN B  66     8632   8211   9874   -451    725    -91       O  
ATOM   2173  ND2 ASN B  66      -0.833   8.722 -89.973  1.00 78.19           N  
ANISOU 2173  ND2 ASN B  66     9657   9215  10835   -464    702    -66       N  
ATOM   2174  N   ARG B  67       0.653   8.763 -84.483  1.00 46.37           N  
ANISOU 2174  N   ARG B  67     5620   5189   6810   -350    807   -220       N  
ATOM   2175  CA  ARG B  67       0.307   8.658 -83.068  1.00 43.43           C  
ANISOU 2175  CA  ARG B  67     5258   4804   6440   -319    831   -246       C  
ATOM   2176  C   ARG B  67       1.470   8.886 -82.135  1.00 40.57           C  
ANISOU 2176  C   ARG B  67     4918   4441   6056   -310    834   -287       C  
ATOM   2177  O   ARG B  67       1.212   9.078 -80.961  1.00 35.59           O  
ANISOU 2177  O   ARG B  67     4307   3791   5426   -285    852   -309       O  
ATOM   2178  CB  ARG B  67      -0.333   7.303 -82.760  1.00 41.46           C  
ANISOU 2178  CB  ARG B  67     5013   4570   6170   -309    841   -242       C  
ATOM   2179  CG  ARG B  67      -1.648   7.118 -83.448  1.00 40.82           C  
ANISOU 2179  CG  ARG B  67     4908   4479   6121   -318    834   -196       C  
ATOM   2180  CD  ARG B  67      -2.486   6.107 -82.742  1.00 39.56           C  
ANISOU 2180  CD  ARG B  67     4747   4322   5961   -299    851   -189       C  
ATOM   2181  NE  ARG B  67      -1.866   4.786 -82.740  1.00 33.40           N  
ANISOU 2181  NE  ARG B  67     3989   3573   5130   -304    843   -209       N  
ATOM   2182  CZ  ARG B  67      -1.678   3.987 -81.680  1.00 43.34           C  
ANISOU 2182  CZ  ARG B  67     5263   4841   6362   -281    864   -236       C  
ATOM   2183  NH1 ARG B  67      -1.995   4.397 -80.458  1.00 31.97           N  
ANISOU 2183  NH1 ARG B  67     3827   3383   4936   -250    897   -252       N  
ATOM   2184  NH2 ARG B  67      -1.121   2.800 -81.832  1.00 36.64           N  
ANISOU 2184  NH2 ARG B  67     4431   4019   5471   -288    855   -250       N  
ATOM   2185  N   VAL B  68       2.741   8.862 -82.624  1.00 39.15           N  
ANISOU 2185  N   VAL B  68     4739   4278   5859   -328    815   -293       N  
ATOM   2186  CA  VAL B  68       3.909   9.026 -81.774  1.00 38.85           C  
ANISOU 2186  CA  VAL B  68     4717   4238   5808   -325    807   -324       C  
ATOM   2187  C   VAL B  68       4.560  10.366 -82.010  1.00 41.91           C  
ANISOU 2187  C   VAL B  68     5096   4604   6226   -339    788   -320       C  
ATOM   2188  O   VAL B  68       4.769  10.787 -83.151  1.00 40.54           O  
ANISOU 2188  O   VAL B  68     4898   4435   6068   -358    779   -293       O  
ATOM   2189  CB  VAL B  68       4.933   7.882 -81.936  1.00 43.35           C  
ANISOU 2189  CB  VAL B  68     5288   4840   6343   -331    804   -329       C  
ATOM   2190  CG1 VAL B  68       6.152   8.099 -81.044  1.00 43.72           C  
ANISOU 2190  CG1 VAL B  68     5346   4880   6387   -332    787   -352       C  
ATOM   2191  CG2 VAL B  68       4.319   6.569 -81.553  1.00 44.54           C  
ANISOU 2191  CG2 VAL B  68     5451   5009   6464   -317    820   -337       C  
ATOM   2192  N   THR B  69       4.941  11.010 -80.904  1.00 37.67           N  
ANISOU 2192  N   THR B  69     4582   4039   5691   -330    778   -347       N  
ATOM   2193  CA  THR B  69       5.707  12.244 -80.931  1.00 36.50           C  
ANISOU 2193  CA  THR B  69     4432   3866   5572   -345    751   -347       C  
ATOM   2194  C   THR B  69       6.964  12.019 -80.097  1.00 39.38           C  
ANISOU 2194  C   THR B  69     4814   4228   5921   -352    724   -368       C  
ATOM   2195  O   THR B  69       6.867  11.609 -78.950  1.00 40.73           O  
ANISOU 2195  O   THR B  69     5023   4390   6065   -336    726   -396       O  
ATOM   2196  CB  THR B  69       4.872  13.402 -80.393  1.00 43.81           C  
ANISOU 2196  CB  THR B  69     5378   4747   6521   -332    758   -356       C  
ATOM   2197  OG1 THR B  69       3.774  13.592 -81.268  1.00 44.52           O  
ANISOU 2197  OG1 THR B  69     5441   4839   6635   -330    779   -327       O  
ATOM   2198  CG2 THR B  69       5.653  14.687 -80.293  1.00 46.12           C  
ANISOU 2198  CG2 THR B  69     5676   5007   6841   -348    725   -359       C  
ATOM   2199  N   LEU B  70       8.130  12.307 -80.663  1.00 35.72           N  
ANISOU 2199  N   LEU B  70     4323   3770   5478   -375    698   -348       N  
ATOM   2200  CA  LEU B  70       9.417  12.235 -79.968  1.00 34.91           C  
ANISOU 2200  CA  LEU B  70     4226   3660   5377   -387    663   -355       C  
ATOM   2201  C   LEU B  70       9.914  13.634 -79.765  1.00 35.90           C  
ANISOU 2201  C   LEU B  70     4356   3745   5540   -405    623   -353       C  
ATOM   2202  O   LEU B  70       9.838  14.468 -80.665  1.00 36.03           O  
ANISOU 2202  O   LEU B  70     4345   3755   5589   -415    624   -328       O  
ATOM   2203  CB  LEU B  70      10.442  11.403 -80.732  1.00 34.90           C  
ANISOU 2203  CB  LEU B  70     4185   3695   5382   -399    666   -326       C  
ATOM   2204  CG  LEU B  70       9.986  10.063 -81.187  1.00 39.19           C  
ANISOU 2204  CG  LEU B  70     4725   4276   5889   -384    705   -324       C  
ATOM   2205  CD1 LEU B  70      11.090   9.371 -81.927  1.00 40.26           C  
ANISOU 2205  CD1 LEU B  70     4827   4438   6031   -392    714   -293       C  
ATOM   2206  CD2 LEU B  70       9.474   9.202 -80.018  1.00 39.07           C  
ANISOU 2206  CD2 LEU B  70     4747   4264   5835   -365    711   -358       C  
ATOM   2207  N   THR B  71      10.357  13.922 -78.555  1.00 31.34           N  
ANISOU 2207  N   THR B  71     3821   3134   4954   -408    587   -378       N  
ATOM   2208  CA  THR B  71      10.815  15.252 -78.187  1.00 29.63           C  
ANISOU 2208  CA  THR B  71     3622   2868   4767   -426    540   -380       C  
ATOM   2209  C   THR B  71      12.045  15.126 -77.297  1.00 35.33           C  
ANISOU 2209  C   THR B  71     4361   3571   5490   -447    481   -383       C  
ATOM   2210  O   THR B  71      12.278  14.076 -76.716  1.00 34.96           O  
ANISOU 2210  O   THR B  71     4327   3543   5412   -441    482   -394       O  
ATOM   2211  CB  THR B  71       9.714  16.048 -77.439  1.00 36.79           C  
ANISOU 2211  CB  THR B  71     4591   3731   5655   -405    552   -415       C  
ATOM   2212  OG1 THR B  71       9.412  15.370 -76.258  1.00 48.89           O  
ANISOU 2212  OG1 THR B  71     6181   5255   7138   -385    560   -450       O  
ATOM   2213  CG2 THR B  71       8.439  16.203 -78.215  1.00 30.63           C  
ANISOU 2213  CG2 THR B  71     3791   2964   4884   -385    606   -406       C  
ATOM   2214  N   THR B  72      12.848  16.180 -77.210  1.00 35.50           N  
ANISOU 2214  N   THR B  72     4381   3554   5552   -475    425   -369       N  
ATOM   2215  CA  THR B  72      14.012  16.185 -76.325  1.00 37.26           C  
ANISOU 2215  CA  THR B  72     4623   3749   5784   -501    355   -366       C  
ATOM   2216  C   THR B  72      14.033  17.452 -75.515  1.00 39.44           C  
ANISOU 2216  C   THR B  72     4966   3956   6063   -516    298   -389       C  
ATOM   2217  O   THR B  72      13.494  18.474 -75.919  1.00 36.75           O  
ANISOU 2217  O   THR B  72     4630   3592   5741   -513    308   -391       O  
ATOM   2218  CB  THR B  72      15.369  16.048 -77.074  1.00 40.21           C  
ANISOU 2218  CB  THR B  72     4917   4141   6219   -530    326   -308       C  
ATOM   2219  OG1 THR B  72      15.450  17.043 -78.071  1.00 46.50           O  
ANISOU 2219  OG1 THR B  72     5670   4932   7066   -542    329   -276       O  
ATOM   2220  CG2 THR B  72      15.550  14.739 -77.676  1.00 37.94           C  
ANISOU 2220  CG2 THR B  72     4581   3912   5925   -516    374   -287       C  
ATOM   2221  N   ASP B  73      14.663  17.354 -74.363  1.00 38.56           N  
ANISOU 2221  N   ASP B  73     4908   3810   5932   -532    236   -404       N  
ATOM   2222  CA  ASP B  73      14.928  18.470 -73.472  1.00 40.56           C  
ANISOU 2222  CA  ASP B  73     5238   3989   6184   -554    165   -424       C  
ATOM   2223  C   ASP B  73      16.439  18.433 -73.181  1.00 44.99           C  
ANISOU 2223  C   ASP B  73     5773   4532   6789   -600     73   -385       C  
ATOM   2224  O   ASP B  73      16.890  17.643 -72.365  1.00 42.19           O  
ANISOU 2224  O   ASP B  73     5447   4178   6407   -607     41   -393       O  
ATOM   2225  CB  ASP B  73      14.072  18.389 -72.189  1.00 42.26           C  
ANISOU 2225  CB  ASP B  73     5570   4167   6319   -526    177   -485       C  
ATOM   2226  CG  ASP B  73      14.146  19.647 -71.329  1.00 54.53           C  
ANISOU 2226  CG  ASP B  73     7223   5636   7860   -541    116   -512       C  
ATOM   2227  OD1 ASP B  73      15.046  20.470 -71.558  1.00 54.26           O  
ANISOU 2227  OD1 ASP B  73     7168   5569   7879   -582     43   -483       O  
ATOM   2228  OD2 ASP B  73      13.354  19.764 -70.389  1.00 62.04           O  
ANISOU 2228  OD2 ASP B  73     8276   6549   8746   -513    139   -560       O  
ATOM   2229  N   SER B  74      17.208  19.284 -73.890  1.00 46.85           N  
ANISOU 2229  N   SER B  74     5949   4753   7099   -632     31   -339       N  
ATOM   2230  CA  SER B  74      18.673  19.382 -73.783  1.00 48.79           C  
ANISOU 2230  CA  SER B  74     6150   4979   7409   -679    -57   -285       C  
ATOM   2231  C   SER B  74      19.192  19.763 -72.403  1.00 54.22           C  
ANISOU 2231  C   SER B  74     6930   5594   8075   -711   -161   -306       C  
ATOM   2232  O   SER B  74      20.254  19.273 -72.016  1.00 56.27           O  
ANISOU 2232  O   SER B  74     7166   5850   8365   -742   -226   -270       O  
ATOM   2233  CB  SER B  74      19.200  20.374 -74.807  1.00 53.60           C  
ANISOU 2233  CB  SER B  74     6685   5580   8102   -702    -74   -233       C  
ATOM   2234  OG  SER B  74      18.641  21.641 -74.516  1.00 72.21           O  
ANISOU 2234  OG  SER B  74     9111   7880  10447   -706    -99   -266       O  
ATOM   2235  N   SER B  75      18.460  20.600 -71.657  1.00 50.25           N  
ANISOU 2235  N   SER B  75     6539   5034   7520   -704   -177   -360       N  
ATOM   2236  CA  SER B  75      18.885  21.047 -70.320  1.00 50.59           C  
ANISOU 2236  CA  SER B  75     6695   4999   7529   -734   -278   -385       C  
ATOM   2237  C   SER B  75      18.818  19.954 -69.260  1.00 54.55           C  
ANISOU 2237  C   SER B  75     7261   5506   7958   -723   -282   -417       C  
ATOM   2238  O   SER B  75      19.641  19.956 -68.347  1.00 55.88           O  
ANISOU 2238  O   SER B  75     7483   5627   8123   -762   -383   -409       O  
ATOM   2239  CB  SER B  75      18.054  22.238 -69.866  1.00 54.54           C  
ANISOU 2239  CB  SER B  75     7305   5432   7985   -722   -280   -437       C  
ATOM   2240  OG  SER B  75      16.671  22.007 -70.077  1.00 68.91           O  
ANISOU 2240  OG  SER B  75     9150   7284   9751   -663   -165   -482       O  
ATOM   2241  N   THR B  76      17.866  19.023 -69.385  1.00 48.42           N  
ANISOU 2241  N   THR B  76     6481   4787   7130   -673   -180   -447       N  
ATOM   2242  CA  THR B  76      17.708  17.898 -68.462  1.00 46.67           C  
ANISOU 2242  CA  THR B  76     6314   4580   6841   -657   -170   -476       C  
ATOM   2243  C   THR B  76      18.178  16.594 -69.095  1.00 48.81           C  
ANISOU 2243  C   THR B  76     6472   4927   7145   -653   -133   -435       C  
ATOM   2244  O   THR B  76      17.951  15.535 -68.499  1.00 50.16           O  
ANISOU 2244  O   THR B  76     6672   5124   7264   -634   -107   -456       O  
ATOM   2245  CB  THR B  76      16.226  17.792 -68.035  1.00 51.48           C  
ANISOU 2245  CB  THR B  76     7008   5188   7365   -601    -78   -540       C  
ATOM   2246  OG1 THR B  76      15.423  17.604 -69.200  1.00 54.21           O  
ANISOU 2246  OG1 THR B  76     7268   5595   7735   -566     23   -530       O  
ATOM   2247  CG2 THR B  76      15.731  19.038 -67.306  1.00 48.95           C  
ANISOU 2247  CG2 THR B  76     6813   4784   7003   -598   -104   -583       C  
ATOM   2248  N   THR B  77      18.764  16.642 -70.313  1.00 42.85           N  
ANISOU 2248  N   THR B  77     5596   4211   6474   -667   -121   -377       N  
ATOM   2249  CA  THR B  77      19.218  15.482 -71.104  1.00 41.36           C  
ANISOU 2249  CA  THR B  77     5298   4093   6323   -658    -74   -333       C  
ATOM   2250  C   THR B  77      18.220  14.312 -71.027  1.00 42.92           C  
ANISOU 2250  C   THR B  77     5512   4343   6452   -611     17   -373       C  
ATOM   2251  O   THR B  77      18.563  13.142 -70.720  1.00 38.91           O  
ANISOU 2251  O   THR B  77     4986   3866   5931   -607     23   -364       O  
ATOM   2252  CB  THR B  77      20.650  15.094 -70.752  1.00 48.33           C  
ANISOU 2252  CB  THR B  77     6138   4963   7261   -701   -160   -279       C  
ATOM   2253  OG1 THR B  77      20.724  14.581 -69.421  1.00 50.41           O  
ANISOU 2253  OG1 THR B  77     6488   5198   7466   -709   -212   -310       O  
ATOM   2254  CG2 THR B  77      21.596  16.269 -70.910  1.00 48.50           C  
ANISOU 2254  CG2 THR B  77     6134   4932   7361   -749   -251   -232       C  
ATOM   2255  N   THR B  78      16.977  14.664 -71.345  1.00 39.75           N  
ANISOU 2255  N   THR B  78     5141   3950   6014   -576     88   -411       N  
ATOM   2256  CA  THR B  78      15.849  13.739 -71.302  1.00 40.06           C  
ANISOU 2256  CA  THR B  78     5199   4031   5992   -530    175   -446       C  
ATOM   2257  C   THR B  78      15.194  13.661 -72.658  1.00 41.16           C  
ANISOU 2257  C   THR B  78     5264   4219   6156   -507    256   -430       C  
ATOM   2258  O   THR B  78      14.956  14.682 -73.285  1.00 39.48           O  
ANISOU 2258  O   THR B  78     5037   3990   5974   -512    259   -422       O  
ATOM   2259  CB  THR B  78      14.778  14.188 -70.231  1.00 39.55           C  
ANISOU 2259  CB  THR B  78     5254   3920   5853   -505    188   -507       C  
ATOM   2260  OG1 THR B  78      15.396  14.222 -68.963  1.00 40.85           O  
ANISOU 2260  OG1 THR B  78     5501   4035   5986   -527    110   -524       O  
ATOM   2261  CG2 THR B  78      13.575  13.239 -70.149  1.00 35.91           C  
ANISOU 2261  CG2 THR B  78     4807   3499   5338   -457    279   -537       C  
ATOM   2262  N   ALA B  79      14.797  12.452 -73.023  1.00 38.02           N  
ANISOU 2262  N   ALA B  79     4833   3877   5736   -482    318   -429       N  
ATOM   2263  CA  ALA B  79      14.047  12.153 -74.246  1.00 36.87           C  
ANISOU 2263  CA  ALA B  79     4631   3778   5599   -458    395   -418       C  
ATOM   2264  C   ALA B  79      12.664  11.681 -73.818  1.00 38.39           C  
ANISOU 2264  C   ALA B  79     4874   3980   5733   -420    453   -459       C  
ATOM   2265  O   ALA B  79      12.521  11.035 -72.786  1.00 36.82           O  
ANISOU 2265  O   ALA B  79     4727   3776   5488   -409    449   -486       O  
ATOM   2266  CB  ALA B  79      14.753  11.053 -75.060  1.00 36.15           C  
ANISOU 2266  CB  ALA B  79     4464   3739   5532   -461    418   -378       C  
ATOM   2267  N   TYR B  80      11.644  12.027 -74.605  1.00 35.34           N  
ANISOU 2267  N   TYR B  80     4471   3605   5351   -401    505   -459       N  
ATOM   2268  CA  TYR B  80      10.272  11.668 -74.329  1.00 33.47           C  
ANISOU 2268  CA  TYR B  80     4268   3374   5074   -366    563   -486       C  
ATOM   2269  C   TYR B  80       9.657  10.998 -75.525  1.00 35.44           C  
ANISOU 2269  C   TYR B  80     4459   3673   5335   -354    616   -463       C  
ATOM   2270  O   TYR B  80       9.863  11.399 -76.663  1.00 32.82           O  
ANISOU 2270  O   TYR B  80     4076   3355   5040   -368    618   -433       O  
ATOM   2271  CB  TYR B  80       9.421  12.895 -73.980  1.00 34.66           C  
ANISOU 2271  CB  TYR B  80     4469   3476   5224   -352    573   -506       C  
ATOM   2272  CG  TYR B  80       9.949  13.716 -72.833  1.00 37.46           C  
ANISOU 2272  CG  TYR B  80     4900   3770   5562   -364    517   -532       C  
ATOM   2273  CD1 TYR B  80      10.858  14.754 -73.049  1.00 40.47           C  
ANISOU 2273  CD1 TYR B  80     5273   4120   5984   -398    456   -517       C  
ATOM   2274  CD2 TYR B  80       9.494  13.508 -71.534  1.00 38.24           C  
ANISOU 2274  CD2 TYR B  80     5087   3838   5605   -341    526   -570       C  
ATOM   2275  CE1 TYR B  80      11.371  15.496 -71.984  1.00 39.84           C  
ANISOU 2275  CE1 TYR B  80     5272   3978   5887   -414    394   -539       C  
ATOM   2276  CE2 TYR B  80       9.941  14.294 -70.476  1.00 39.14           C  
ANISOU 2276  CE2 TYR B  80     5288   3888   5694   -352    472   -596       C  
ATOM   2277  CZ  TYR B  80      10.915  15.252 -70.694  1.00 44.72           C  
ANISOU 2277  CZ  TYR B  80     5986   4563   6441   -391    401   -581       C  
ATOM   2278  OH  TYR B  80      11.351  16.011 -69.642  1.00 48.26           O  
ANISOU 2278  OH  TYR B  80     6529   4944   6864   -407    338   -606       O  
ATOM   2279  N   MET B  81       8.839   9.999 -75.237  1.00 34.00           N  
ANISOU 2279  N   MET B  81     4289   3513   5117   -329    657   -476       N  
ATOM   2280  CA  MET B  81       8.043   9.292 -76.201  1.00 32.95           C  
ANISOU 2280  CA  MET B  81     4115   3418   4985   -317    704   -458       C  
ATOM   2281  C   MET B  81       6.590   9.530 -75.787  1.00 34.14           C  
ANISOU 2281  C   MET B  81     4298   3551   5125   -287    744   -472       C  
ATOM   2282  O   MET B  81       6.201   9.099 -74.711  1.00 31.58           O  
ANISOU 2282  O   MET B  81     4018   3215   4766   -265    759   -496       O  
ATOM   2283  CB  MET B  81       8.370   7.798 -76.121  1.00 34.49           C  
ANISOU 2283  CB  MET B  81     4298   3652   5153   -312    714   -456       C  
ATOM   2284  CG  MET B  81       7.835   6.970 -77.268  1.00 39.82           C  
ANISOU 2284  CG  MET B  81     4933   4367   5829   -309    749   -433       C  
ATOM   2285  SD  MET B  81       6.059   6.640 -77.291  1.00 47.48           S  
ANISOU 2285  SD  MET B  81     5913   5338   6787   -282    794   -435       S  
ATOM   2286  CE  MET B  81       5.786   5.793 -75.707  1.00 43.25           C  
ANISOU 2286  CE  MET B  81     5425   4797   6209   -256    806   -467       C  
ATOM   2287  N   GLU B  82       5.796  10.160 -76.650  1.00 31.24           N  
ANISOU 2287  N   GLU B  82     3904   3180   4788   -285    765   -452       N  
ATOM   2288  CA  GLU B  82       4.375  10.344 -76.391  1.00 31.41           C  
ANISOU 2288  CA  GLU B  82     3939   3183   4812   -256    808   -452       C  
ATOM   2289  C   GLU B  82       3.569   9.591 -77.410  1.00 34.91           C  
ANISOU 2289  C   GLU B  82     4336   3661   5267   -255    833   -421       C  
ATOM   2290  O   GLU B  82       3.691   9.855 -78.607  1.00 33.37           O  
ANISOU 2290  O   GLU B  82     4102   3480   5098   -277    822   -394       O  
ATOM   2291  CB  GLU B  82       3.996  11.813 -76.333  1.00 32.14           C  
ANISOU 2291  CB  GLU B  82     4048   3229   4934   -252    810   -452       C  
ATOM   2292  CG  GLU B  82       2.596  12.024 -75.828  1.00 36.50           C  
ANISOU 2292  CG  GLU B  82     4622   3755   5492   -215    861   -451       C  
ATOM   2293  CD  GLU B  82       2.267  13.492 -75.640  1.00 49.33           C  
ANISOU 2293  CD  GLU B  82     6273   5327   7144   -206    868   -455       C  
ATOM   2294  OE1 GLU B  82       1.785  13.846 -74.542  1.00 43.52           O  
ANISOU 2294  OE1 GLU B  82     5597   4548   6389   -174    898   -477       O  
ATOM   2295  OE2 GLU B  82       2.490  14.287 -76.582  1.00 49.24           O  
ANISOU 2295  OE2 GLU B  82     6225   5314   7171   -229    845   -435       O  
ATOM   2296  N   LEU B  83       2.725   8.649 -76.914  1.00 32.98           N  
ANISOU 2296  N   LEU B  83     4101   3427   5005   -232    865   -422       N  
ATOM   2297  CA  LEU B  83       1.846   7.846 -77.736  1.00 32.49           C  
ANISOU 2297  CA  LEU B  83     4001   3390   4954   -232    883   -391       C  
ATOM   2298  C   LEU B  83       0.435   8.256 -77.422  1.00 36.43           C  
ANISOU 2298  C   LEU B  83     4500   3861   5482   -205    921   -374       C  
ATOM   2299  O   LEU B  83      -0.034   8.132 -76.287  1.00 35.45           O  
ANISOU 2299  O   LEU B  83     4409   3718   5344   -174    953   -390       O  
ATOM   2300  CB  LEU B  83       2.072   6.367 -77.493  1.00 32.35           C  
ANISOU 2300  CB  LEU B  83     3986   3406   4900   -229    885   -399       C  
ATOM   2301  CG  LEU B  83       1.257   5.354 -78.353  1.00 37.05           C  
ANISOU 2301  CG  LEU B  83     4550   4026   5500   -234    893   -367       C  
ATOM   2302  CD1 LEU B  83       1.641   5.385 -79.818  1.00 37.76           C  
ANISOU 2302  CD1 LEU B  83     4613   4135   5600   -265    869   -344       C  
ATOM   2303  CD2 LEU B  83       1.456   4.001 -77.841  1.00 33.04           C  
ANISOU 2303  CD2 LEU B  83     4054   3544   4957   -226    899   -380       C  
ATOM   2304  N   LYS B  84      -0.215   8.815 -78.438  1.00 34.68           N  
ANISOU 2304  N   LYS B  84     4240   3633   5302   -217    919   -339       N  
ATOM   2305  CA  LYS B  84      -1.585   9.370 -78.366  1.00 36.01           C  
ANISOU 2305  CA  LYS B  84     4394   3772   5517   -194    953   -308       C  
ATOM   2306  C   LYS B  84      -2.637   8.402 -78.947  1.00 37.17           C  
ANISOU 2306  C   LYS B  84     4502   3937   5686   -197    960   -265       C  
ATOM   2307  O   LYS B  84      -2.262   7.421 -79.600  1.00 33.28           O  
ANISOU 2307  O   LYS B  84     3998   3478   5168   -220    932   -261       O  
ATOM   2308  CB  LYS B  84      -1.608  10.746 -79.102  1.00 35.54           C  
ANISOU 2308  CB  LYS B  84     4316   3688   5499   -209    940   -292       C  
ATOM   2309  N   SER B  85      -3.945   8.691 -78.693  1.00 35.66           N  
ANISOU 2309  N   SER B  85     4291   3717   5543   -171    996   -230       N  
ATOM   2310  CA  SER B  85      -5.107   7.887 -79.172  1.00 35.98           C  
ANISOU 2310  CA  SER B  85     4288   3763   5619   -174    999   -178       C  
ATOM   2311  C   SER B  85      -4.921   6.411 -78.852  1.00 37.17           C  
ANISOU 2311  C   SER B  85     4450   3946   5728   -174    995   -190       C  
ATOM   2312  O   SER B  85      -4.998   5.541 -79.707  1.00 36.71           O  
ANISOU 2312  O   SER B  85     4371   3912   5663   -202    960   -169       O  
ATOM   2313  CB  SER B  85      -5.334   8.097 -80.665  1.00 38.58           C  
ANISOU 2313  CB  SER B  85     4579   4100   5979   -214    954   -137       C  
ATOM   2314  OG  SER B  85      -5.472   9.482 -80.933  1.00 49.36           O  
ANISOU 2314  OG  SER B  85     5934   5437   7386   -214    958   -125       O  
ATOM   2315  N   LEU B  86      -4.621   6.156 -77.591  1.00 35.96           N  
ANISOU 2315  N   LEU B  86     4335   3789   5540   -143   1028   -227       N  
ATOM   2316  CA  LEU B  86      -4.302   4.837 -77.094  1.00 34.48           C  
ANISOU 2316  CA  LEU B  86     4163   3629   5306   -139   1027   -246       C  
ATOM   2317  C   LEU B  86      -5.349   3.792 -77.407  1.00 37.98           C  
ANISOU 2317  C   LEU B  86     4570   4083   5779   -140   1028   -199       C  
ATOM   2318  O   LEU B  86      -6.555   4.023 -77.305  1.00 37.88           O  
ANISOU 2318  O   LEU B  86     4526   4044   5823   -122   1057   -152       O  
ATOM   2319  CB  LEU B  86      -3.995   4.874 -75.580  1.00 33.79           C  
ANISOU 2319  CB  LEU B  86     4128   3528   5183   -101   1067   -287       C  
ATOM   2320  CG  LEU B  86      -2.623   5.508 -75.209  1.00 36.21           C  
ANISOU 2320  CG  LEU B  86     4481   3832   5444   -111   1044   -340       C  
ATOM   2321  CD1 LEU B  86      -2.512   5.762 -73.726  1.00 33.74           C  
ANISOU 2321  CD1 LEU B  86     4231   3491   5098    -74   1080   -375       C  
ATOM   2322  CD2 LEU B  86      -1.469   4.653 -75.691  1.00 36.55           C  
ANISOU 2322  CD2 LEU B  86     4522   3917   5447   -143    999   -360       C  
ATOM   2323  N   GLN B  87      -4.858   2.626 -77.748  1.00 34.79           N  
ANISOU 2323  N   GLN B  87     4169   3712   5337   -161    998   -209       N  
ATOM   2324  CA  GLN B  87      -5.646   1.442 -78.067  1.00 33.84           C  
ANISOU 2324  CA  GLN B  87     4023   3603   5232   -170    986   -171       C  
ATOM   2325  C   GLN B  87      -5.375   0.400 -77.009  1.00 37.19           C  
ANISOU 2325  C   GLN B  87     4472   4043   5616   -147   1009   -198       C  
ATOM   2326  O   GLN B  87      -4.278   0.359 -76.462  1.00 35.95           O  
ANISOU 2326  O   GLN B  87     4353   3900   5407   -142   1011   -249       O  
ATOM   2327  CB  GLN B  87      -5.172   0.912 -79.409  1.00 34.83           C  
ANISOU 2327  CB  GLN B  87     4145   3751   5337   -215    928   -165       C  
ATOM   2328  CG  GLN B  87      -5.427   1.883 -80.546  1.00 36.40           C  
ANISOU 2328  CG  GLN B  87     4324   3935   5572   -241    900   -135       C  
ATOM   2329  CD  GLN B  87      -4.680   1.537 -81.809  1.00 49.79           C  
ANISOU 2329  CD  GLN B  87     6037   5651   7231   -281    852   -141       C  
ATOM   2330  OE1 GLN B  87      -4.090   0.446 -81.972  1.00 47.88           O  
ANISOU 2330  OE1 GLN B  87     5819   5432   6940   -291    837   -160       O  
ATOM   2331  NE2 GLN B  87      -4.782   2.429 -82.768  1.00 47.59           N  
ANISOU 2331  NE2 GLN B  87     5748   5360   6975   -304    829   -119       N  
ATOM   2332  N   PHE B  88      -6.321  -0.492 -76.777  1.00 36.74           N  
ANISOU 2332  N   PHE B  88     4391   3984   5584   -137   1020   -161       N  
ATOM   2333  CA  PHE B  88      -6.164  -1.601 -75.841  1.00 37.07           C  
ANISOU 2333  CA  PHE B  88     4452   4043   5592   -117   1040   -180       C  
ATOM   2334  C   PHE B  88      -4.851  -2.401 -76.150  1.00 37.30           C  
ANISOU 2334  C   PHE B  88     4511   4107   5554   -142   1002   -225       C  
ATOM   2335  O   PHE B  88      -4.134  -2.793 -75.240  1.00 34.81           O  
ANISOU 2335  O   PHE B  88     4228   3805   5195   -125   1018   -265       O  
ATOM   2336  CB  PHE B  88      -7.401  -2.560 -75.896  1.00 39.54           C  
ANISOU 2336  CB  PHE B  88     4723   4349   5950   -114   1041   -121       C  
ATOM   2337  CG  PHE B  88      -8.620  -2.079 -75.164  1.00 40.78           C  
ANISOU 2337  CG  PHE B  88     4851   4472   6170    -75   1098    -75       C  
ATOM   2338  CD1 PHE B  88      -8.650  -2.056 -73.782  1.00 46.00           C  
ANISOU 2338  CD1 PHE B  88     5541   5123   6813    -27   1163    -94       C  
ATOM   2339  CD2 PHE B  88      -9.777  -1.746 -75.852  1.00 40.88           C  
ANISOU 2339  CD2 PHE B  88     4810   4460   6264    -85   1089     -5       C  
ATOM   2340  CE1 PHE B  88      -9.800  -1.647 -73.102  1.00 47.27           C  
ANISOU 2340  CE1 PHE B  88     5679   5249   7033     15   1227    -47       C  
ATOM   2341  CE2 PHE B  88     -10.893  -1.271 -75.176  1.00 43.91           C  
ANISOU 2341  CE2 PHE B  88     5161   4808   6714    -44   1150     45       C  
ATOM   2342  CZ  PHE B  88     -10.907  -1.225 -73.810  1.00 43.43           C  
ANISOU 2342  CZ  PHE B  88     5132   4738   6634      8   1224     24       C  
ATOM   2343  N   ASP B  89      -4.539  -2.578 -77.429  1.00 34.81           N  
ANISOU 2343  N   ASP B  89     4188   3803   5233   -180    955   -217       N  
ATOM   2344  CA  ASP B  89      -3.337  -3.302 -77.864  1.00 35.41           C  
ANISOU 2344  CA  ASP B  89     4291   3908   5254   -201    927   -252       C  
ATOM   2345  C   ASP B  89      -2.029  -2.492 -77.805  1.00 38.47           C  
ANISOU 2345  C   ASP B  89     4703   4303   5612   -203    927   -294       C  
ATOM   2346  O   ASP B  89      -1.031  -2.935 -78.362  1.00 36.74           O  
ANISOU 2346  O   ASP B  89     4498   4104   5359   -221    906   -313       O  
ATOM   2347  CB  ASP B  89      -3.524  -3.914 -79.276  1.00 36.97           C  
ANISOU 2347  CB  ASP B  89     4485   4111   5452   -238    881   -224       C  
ATOM   2348  CG  ASP B  89      -3.682  -2.936 -80.418  1.00 46.14           C  
ANISOU 2348  CG  ASP B  89     5637   5258   6636   -263    856   -202       C  
ATOM   2349  OD1 ASP B  89      -3.528  -1.691 -80.177  1.00 45.34           O  
ANISOU 2349  OD1 ASP B  89     5528   5145   6553   -253    874   -211       O  
ATOM   2350  OD2 ASP B  89      -3.938  -3.398 -81.562  1.00 48.73           O  
ANISOU 2350  OD2 ASP B  89     5971   5584   6961   -294    816   -176       O  
ATOM   2351  N   ASP B  90      -2.035  -1.302 -77.190  1.00 35.00           N  
ANISOU 2351  N   ASP B  90     4266   3843   5188   -186    949   -306       N  
ATOM   2352  CA  ASP B  90      -0.824  -0.538 -76.951  1.00 32.96           C  
ANISOU 2352  CA  ASP B  90     4031   3586   4906   -189    943   -344       C  
ATOM   2353  C   ASP B  90      -0.241  -0.942 -75.566  1.00 35.42           C  
ANISOU 2353  C   ASP B  90     4375   3901   5181   -165    961   -380       C  
ATOM   2354  O   ASP B  90       0.801  -0.409 -75.160  1.00 35.07           O  
ANISOU 2354  O   ASP B  90     4354   3854   5117   -168    950   -410       O  
ATOM   2355  CB  ASP B  90      -1.094   0.980 -77.038  1.00 34.86           C  
ANISOU 2355  CB  ASP B  90     4267   3798   5181   -185    950   -338       C  
ATOM   2356  CG  ASP B  90      -1.312   1.516 -78.441  1.00 37.71           C  
ANISOU 2356  CG  ASP B  90     4601   4156   5570   -214    925   -308       C  
ATOM   2357  OD1 ASP B  90      -0.631   1.048 -79.376  1.00 36.89           O  
ANISOU 2357  OD1 ASP B  90     4498   4074   5446   -240    898   -308       O  
ATOM   2358  OD2 ASP B  90      -2.075   2.476 -78.590  1.00 38.86           O  
ANISOU 2358  OD2 ASP B  90     4731   4277   5759   -209    934   -285       O  
ATOM   2359  N   THR B  91      -0.934  -1.816 -74.818  1.00 31.30           N  
ANISOU 2359  N   THR B  91     3856   3382   4655   -144    984   -373       N  
ATOM   2360  CA  THR B  91      -0.431  -2.365 -73.556  1.00 32.58           C  
ANISOU 2360  CA  THR B  91     4052   3548   4777   -124    998   -403       C  
ATOM   2361  C   THR B  91       0.895  -3.067 -73.811  1.00 33.97           C  
ANISOU 2361  C   THR B  91     4234   3753   4919   -145    966   -426       C  
ATOM   2362  O   THR B  91       0.930  -3.949 -74.625  1.00 35.43           O  
ANISOU 2362  O   THR B  91     4400   3959   5103   -161    952   -412       O  
ATOM   2363  CB  THR B  91      -1.465  -3.308 -72.931  1.00 30.88           C  
ANISOU 2363  CB  THR B  91     3831   3334   4568    -99   1029   -382       C  
ATOM   2364  OG1 THR B  91      -2.561  -2.496 -72.548  1.00 32.98           O  
ANISOU 2364  OG1 THR B  91     4092   3568   4870    -73   1068   -359       O  
ATOM   2365  CG2 THR B  91      -0.955  -4.072 -71.694  1.00 24.67           C  
ANISOU 2365  CG2 THR B  91     3080   2557   3738    -81   1041   -411       C  
ATOM   2366  N   ALA B  92       1.992  -2.595 -73.214  1.00 28.71           N  
ANISOU 2366  N   ALA B  92     3596   3083   4231   -148    952   -456       N  
ATOM   2367  CA  ALA B  92       3.304  -3.167 -73.453  1.00 28.38           C  
ANISOU 2367  CA  ALA B  92     3551   3063   4168   -167    924   -469       C  
ATOM   2368  C   ALA B  92       4.310  -2.623 -72.486  1.00 33.13           C  
ANISOU 2368  C   ALA B  92     4185   3651   4752   -167    906   -496       C  
ATOM   2369  O   ALA B  92       4.035  -1.663 -71.761  1.00 33.18           O  
ANISOU 2369  O   ALA B  92     4223   3628   4757   -156    912   -509       O  
ATOM   2370  CB  ALA B  92       3.763  -2.844 -74.891  1.00 29.11           C  
ANISOU 2370  CB  ALA B  92     3616   3165   4281   -193    906   -453       C  
ATOM   2371  N   VAL B  93       5.524  -3.164 -72.547  1.00 30.40           N  
ANISOU 2371  N   VAL B  93     3832   3322   4395   -183    880   -502       N  
ATOM   2372  CA  VAL B  93       6.649  -2.552 -71.836  1.00 30.17           C  
ANISOU 2372  CA  VAL B  93     3826   3278   4360   -194    847   -518       C  
ATOM   2373  C   VAL B  93       7.339  -1.698 -72.909  1.00 31.62           C  
ANISOU 2373  C   VAL B  93     3979   3459   4576   -217    828   -504       C  
ATOM   2374  O   VAL B  93       7.644  -2.180 -74.008  1.00 29.28           O  
ANISOU 2374  O   VAL B  93     3647   3185   4293   -228    833   -484       O  
ATOM   2375  CB  VAL B  93       7.631  -3.537 -71.157  1.00 32.10           C  
ANISOU 2375  CB  VAL B  93     4076   3537   4585   -198    827   -525       C  
ATOM   2376  CG1 VAL B  93       8.873  -2.811 -70.631  1.00 30.58           C  
ANISOU 2376  CG1 VAL B  93     3898   3324   4398   -219    780   -531       C  
ATOM   2377  CG2 VAL B  93       6.941  -4.301 -70.047  1.00 31.21           C  
ANISOU 2377  CG2 VAL B  93     3997   3424   4438   -175    847   -538       C  
ATOM   2378  N   TYR B  94       7.561  -0.429 -72.593  1.00 29.23           N  
ANISOU 2378  N   TYR B  94     3695   3126   4284   -224    807   -513       N  
ATOM   2379  CA  TYR B  94       8.231   0.505 -73.488  1.00 27.69           C  
ANISOU 2379  CA  TYR B  94     3473   2924   4124   -247    786   -498       C  
ATOM   2380  C   TYR B  94       9.630   0.797 -73.006  1.00 32.44           C  
ANISOU 2380  C   TYR B  94     4077   3514   4734   -267    740   -498       C  
ATOM   2381  O   TYR B  94       9.799   1.138 -71.852  1.00 30.29           O  
ANISOU 2381  O   TYR B  94     3849   3215   4444   -267    714   -518       O  
ATOM   2382  CB  TYR B  94       7.436   1.798 -73.567  1.00 28.40           C  
ANISOU 2382  CB  TYR B  94     3579   2985   4228   -242    794   -502       C  
ATOM   2383  CG  TYR B  94       6.141   1.610 -74.314  1.00 30.36           C  
ANISOU 2383  CG  TYR B  94     3809   3244   4484   -229    832   -488       C  
ATOM   2384  CD1 TYR B  94       4.999   1.145 -73.669  1.00 29.55           C  
ANISOU 2384  CD1 TYR B  94     3725   3137   4364   -202    864   -494       C  
ATOM   2385  CD2 TYR B  94       6.041   1.938 -75.660  1.00 32.67           C  
ANISOU 2385  CD2 TYR B  94     4063   3545   4803   -243    834   -463       C  
ATOM   2386  CE1 TYR B  94       3.832   0.892 -74.381  1.00 29.48           C  
ANISOU 2386  CE1 TYR B  94     3691   3136   4372   -195    892   -471       C  
ATOM   2387  CE2 TYR B  94       4.832   1.852 -76.327  1.00 34.59           C  
ANISOU 2387  CE2 TYR B  94     4293   3793   5058   -236    859   -446       C  
ATOM   2388  CZ  TYR B  94       3.771   1.203 -75.733  1.00 37.63           C  
ANISOU 2388  CZ  TYR B  94     4689   4177   5432   -214    885   -447       C  
ATOM   2389  OH  TYR B  94       2.654   1.023 -76.504  1.00 35.57           O  
ANISOU 2389  OH  TYR B  94     4406   3919   5190   -213    900   -420       O  
ATOM   2390  N   TYR B  95      10.622   0.748 -73.921  1.00 31.87           N  
ANISOU 2390  N   TYR B  95     3959   3456   4694   -286    729   -470       N  
ATOM   2391  CA  TYR B  95      12.027   1.034 -73.632  1.00 31.63           C  
ANISOU 2391  CA  TYR B  95     3915   3413   4690   -308    683   -456       C  
ATOM   2392  C   TYR B  95      12.559   2.156 -74.454  1.00 34.95           C  
ANISOU 2392  C   TYR B  95     4305   3819   5154   -327    667   -433       C  
ATOM   2393  O   TYR B  95      12.220   2.225 -75.636  1.00 31.36           O  
ANISOU 2393  O   TYR B  95     3823   3381   4712   -324    700   -417       O  
ATOM   2394  CB  TYR B  95      12.917  -0.152 -74.039  1.00 31.94           C  
ANISOU 2394  CB  TYR B  95     3914   3481   4741   -310    692   -430       C  
ATOM   2395  CG  TYR B  95      12.646  -1.418 -73.276  1.00 31.91           C  
ANISOU 2395  CG  TYR B  95     3930   3494   4700   -294    704   -446       C  
ATOM   2396  CD1 TYR B  95      13.217  -1.635 -72.027  1.00 33.07           C  
ANISOU 2396  CD1 TYR B  95     4102   3627   4837   -301    664   -455       C  
ATOM   2397  CD2 TYR B  95      11.851  -2.421 -73.813  1.00 32.80           C  
ANISOU 2397  CD2 TYR B  95     4039   3635   4790   -275    751   -449       C  
ATOM   2398  CE1 TYR B  95      12.963  -2.795 -71.309  1.00 31.82           C  
ANISOU 2398  CE1 TYR B  95     3962   3484   4644   -286    675   -469       C  
ATOM   2399  CE2 TYR B  95      11.600  -3.596 -73.107  1.00 34.33           C  
ANISOU 2399  CE2 TYR B  95     4249   3843   4953   -261    761   -461       C  
ATOM   2400  CZ  TYR B  95      12.184  -3.790 -71.865  1.00 40.86           C  
ANISOU 2400  CZ  TYR B  95     5096   4658   5769   -266    726   -471       C  
ATOM   2401  OH  TYR B  95      11.945  -4.943 -71.164  1.00 42.07           O  
ANISOU 2401  OH  TYR B  95     5266   4827   5893   -252    736   -481       O  
ATOM   2402  N   CYS B  96      13.539   2.913 -73.887  1.00 34.13           N  
ANISOU 2402  N   CYS B  96     4204   3686   5077   -350    612   -425       N  
ATOM   2403  CA  CYS B  96      14.389   3.828 -74.652  1.00 35.04           C  
ANISOU 2403  CA  CYS B  96     4279   3790   5247   -373    589   -391       C  
ATOM   2404  C   CYS B  96      15.708   3.074 -74.790  1.00 34.53           C  
ANISOU 2404  C   CYS B  96     4165   3737   5216   -383    577   -352       C  
ATOM   2405  O   CYS B  96      16.007   2.199 -73.992  1.00 32.77           O  
ANISOU 2405  O   CYS B  96     3954   3521   4976   -381    564   -358       O  
ATOM   2406  CB  CYS B  96      14.585   5.209 -74.011  1.00 38.52           C  
ANISOU 2406  CB  CYS B  96     4751   4183   5703   -393    533   -400       C  
ATOM   2407  SG  CYS B  96      15.244   5.188 -72.322  1.00 43.93           S  
ANISOU 2407  SG  CYS B  96     5492   4830   6368   -410    459   -418       S  
ATOM   2408  N   ALA B  97      16.439   3.323 -75.834  1.00 34.13           N  
ANISOU 2408  N   ALA B  97     4061   3694   5214   -392    589   -309       N  
ATOM   2409  CA  ALA B  97      17.782   2.755 -75.997  1.00 35.01           C  
ANISOU 2409  CA  ALA B  97     4119   3811   5373   -400    581   -261       C  
ATOM   2410  C   ALA B  97      18.600   3.674 -76.855  1.00 37.30           C  
ANISOU 2410  C   ALA B  97     4358   4088   5728   -417    574   -213       C  
ATOM   2411  O   ALA B  97      18.055   4.364 -77.695  1.00 36.00           O  
ANISOU 2411  O   ALA B  97     4193   3924   5562   -413    599   -216       O  
ATOM   2412  CB  ALA B  97      17.733   1.343 -76.574  1.00 35.89           C  
ANISOU 2412  CB  ALA B  97     4212   3959   5464   -375    643   -253       C  
ATOM   2413  N   ARG B  98      19.877   3.812 -76.552  1.00 37.04           N  
ANISOU 2413  N   ARG B  98     4282   4035   5757   -438    530   -167       N  
ATOM   2414  CA  ARG B  98      20.708   4.711 -77.323  1.00 37.76           C  
ANISOU 2414  CA  ARG B  98     4319   4111   5919   -454    521   -113       C  
ATOM   2415  C   ARG B  98      21.453   4.022 -78.470  1.00 39.69           C  
ANISOU 2415  C   ARG B  98     4500   4378   6203   -435    589    -56       C  
ATOM   2416  O   ARG B  98      21.670   2.822 -78.457  1.00 36.09           O  
ANISOU 2416  O   ARG B  98     4035   3943   5735   -416    626    -49       O  
ATOM   2417  CB  ARG B  98      21.661   5.498 -76.438  1.00 39.21           C  
ANISOU 2417  CB  ARG B  98     4488   4251   6159   -492    428    -86       C  
ATOM   2418  CG  ARG B  98      22.791   4.681 -75.965  1.00 40.52           C  
ANISOU 2418  CG  ARG B  98     4612   4415   6371   -501    404    -40       C  
ATOM   2419  CD  ARG B  98      23.825   5.529 -75.291  1.00 38.07           C  
ANISOU 2419  CD  ARG B  98     4277   4057   6131   -544    307      2       C  
ATOM   2420  NE  ARG B  98      25.086   4.816 -75.347  1.00 41.67           N  
ANISOU 2420  NE  ARG B  98     4657   4514   6661   -549    304     75       N  
ATOM   2421  CZ  ARG B  98      26.250   5.277 -74.929  1.00 46.52           C  
ANISOU 2421  CZ  ARG B  98     5224   5091   7362   -586    226    139       C  
ATOM   2422  NH1 ARG B  98      26.340   6.490 -74.401  1.00 41.85           N  
ANISOU 2422  NH1 ARG B  98     4659   4454   6787   -625    136    134       N  
ATOM   2423  NH2 ARG B  98      27.339   4.529 -75.036  1.00 40.29           N  
ANISOU 2423  NH2 ARG B  98     4358   4303   6645   -585    235    211       N  
ATOM   2424  N   ARG B  99      21.901   4.835 -79.431  1.00 37.65           N  
ANISOU 2424  N   ARG B  99     4199   4110   5994   -440    605    -12       N  
ATOM   2425  CA  ARG B  99      22.646   4.360 -80.594  1.00 36.67           C  
ANISOU 2425  CA  ARG B  99     4021   4002   5911   -419    677     48       C  
ATOM   2426  C   ARG B  99      23.618   5.437 -80.930  1.00 40.18           C  
ANISOU 2426  C   ARG B  99     4406   4419   6444   -441    648    112       C  
ATOM   2427  O   ARG B  99      23.239   6.614 -81.008  1.00 40.07           O  
ANISOU 2427  O   ARG B  99     4405   4388   6434   -460    613     98       O  
ATOM   2428  CB  ARG B  99      21.685   4.095 -81.776  1.00 38.06           C  
ANISOU 2428  CB  ARG B  99     4231   4205   6026   -391    757     23       C  
ATOM   2429  CG  ARG B  99      22.227   3.154 -82.854  1.00 38.39           C  
ANISOU 2429  CG  ARG B  99     4249   4264   6073   -358    846     67       C  
ATOM   2430  CD  ARG B  99      23.035   3.952 -83.859  1.00 53.39           C  
ANISOU 2430  CD  ARG B  99     6098   6150   8038   -358    875    134       C  
ATOM   2431  NE  ARG B  99      22.413   3.976 -85.167  1.00 58.41           N  
ANISOU 2431  NE  ARG B  99     6767   6799   8626   -337    944    128       N  
ATOM   2432  CZ  ARG B  99      22.811   4.719 -86.188  1.00 59.64           C  
ANISOU 2432  CZ  ARG B  99     6897   6945   8818   -335    977    175       C  
ATOM   2433  NH1 ARG B  99      23.857   5.532 -86.063  1.00 45.72           N  
ANISOU 2433  NH1 ARG B  99     5066   5160   7147   -352    948    235       N  
ATOM   2434  NH2 ARG B  99      22.158   4.672 -87.338  1.00 63.15           N  
ANISOU 2434  NH2 ARG B  99     7386   7401   9208   -317   1035    165       N  
ATOM   2435  N   ASP B 100      24.881   5.060 -81.150  1.00 37.97           N  
ANISOU 2435  N   ASP B 100     4055   4131   6240   -438    665    187       N  
ATOM   2436  CA  ASP B 100      25.918   6.022 -81.509  1.00 37.33           C  
ANISOU 2436  CA  ASP B 100     3904   4022   6258   -458    640    263       C  
ATOM   2437  C   ASP B 100      25.558   6.745 -82.817  1.00 42.74           C  
ANISOU 2437  C   ASP B 100     4588   4713   6936   -445    699    273       C  
ATOM   2438  O   ASP B 100      25.253   6.086 -83.803  1.00 40.27           O  
ANISOU 2438  O   ASP B 100     4291   4426   6582   -409    791    272       O  
ATOM   2439  CB  ASP B 100      27.270   5.302 -81.607  1.00 40.24           C  
ANISOU 2439  CB  ASP B 100     4194   4384   6712   -448    667    349       C  
ATOM   2440  CG  ASP B 100      28.465   6.245 -81.731  1.00 50.28           C  
ANISOU 2440  CG  ASP B 100     5381   5620   8104   -475    626    439       C  
ATOM   2441  OD1 ASP B 100      28.920   6.749 -80.704  1.00 60.38           O  
ANISOU 2441  OD1 ASP B 100     6644   6866   9430   -517    520    452       O  
ATOM   2442  OD2 ASP B 100      28.842   6.577 -82.863  1.00 50.56           O  
ANISOU 2442  OD2 ASP B 100     5375   5657   8181   -456    694    494       O  
ATOM   2443  N   TYR B 101      25.565   8.092 -82.820  1.00 45.13           N  
ANISOU 2443  N   TYR B 101     4882   4991   7276   -474    644    281       N  
ATOM   2444  CA  TYR B 101      25.252   8.870 -84.022  1.00 48.02           C  
ANISOU 2444  CA  TYR B 101     5245   5361   7641   -465    691    295       C  
ATOM   2445  C   TYR B 101      26.153   8.577 -85.234  1.00 52.45           C  
ANISOU 2445  C   TYR B 101     5745   5928   8255   -437    781    378       C  
ATOM   2446  O   TYR B 101      25.631   8.389 -86.337  1.00 53.10           O  
ANISOU 2446  O   TYR B 101     5857   6031   8288   -408    861    369       O  
ATOM   2447  CB  TYR B 101      25.294  10.383 -83.731  1.00 53.33           C  
ANISOU 2447  CB  TYR B 101     5906   5999   8358   -504    610    300       C  
ATOM   2448  CG  TYR B 101      25.287  11.219 -84.994  1.00 61.22           C  
ANISOU 2448  CG  TYR B 101     6881   6998   9381   -498    657    336       C  
ATOM   2449  CD1 TYR B 101      24.120  11.391 -85.732  1.00 63.99           C  
ANISOU 2449  CD1 TYR B 101     7288   7370   9656   -482    701    286       C  
ATOM   2450  CD2 TYR B 101      26.473  11.704 -85.537  1.00 64.31           C  
ANISOU 2450  CD2 TYR B 101     7191   7370   9874   -504    666    429       C  
ATOM   2451  CE1 TYR B 101      24.112  12.123 -86.919  1.00 66.39           C  
ANISOU 2451  CE1 TYR B 101     7574   7674   9978   -476    744    321       C  
ATOM   2452  CE2 TYR B 101      26.493  12.349 -86.775  1.00 66.59           C  
ANISOU 2452  CE2 TYR B 101     7459   7660  10180   -492    722    467       C  
ATOM   2453  CZ  TYR B 101      25.307  12.573 -87.455  1.00 77.51           C  
ANISOU 2453  CZ  TYR B 101     8905   9064  11480   -479    758    411       C  
ATOM   2454  OH  TYR B 101      25.321  13.232 -88.663  1.00 83.01           O  
ANISOU 2454  OH  TYR B 101     9587   9761  12192   -470    808    449       O  
ATOM   2455  N   ARG B 102      27.484   8.584 -85.043  1.00 49.36           N  
ANISOU 2455  N   ARG B 102     5273   5515   7968   -446    766    461       N  
ATOM   2456  CA  ARG B 102      28.445   8.446 -86.149  1.00 50.11           C  
ANISOU 2456  CA  ARG B 102     5302   5607   8130   -417    854    554       C  
ATOM   2457  C   ARG B 102      28.561   7.039 -86.729  1.00 50.44           C  
ANISOU 2457  C   ARG B 102     5358   5674   8134   -367    962    563       C  
ATOM   2458  O   ARG B 102      28.775   6.893 -87.922  1.00 49.30           O  
ANISOU 2458  O   ARG B 102     5209   5535   7988   -332   1061    604       O  
ATOM   2459  CB  ARG B 102      29.839   8.973 -85.737  1.00 52.50           C  
ANISOU 2459  CB  ARG B 102     5504   5873   8571   -444    800    651       C  
ATOM   2460  N   PHE B 103      28.474   6.017 -85.897  1.00 47.46           N  
ANISOU 2460  N   PHE B 103     5000   5306   7725   -363    946    530       N  
ATOM   2461  CA  PHE B 103      28.586   4.628 -86.324  1.00 47.18           C  
ANISOU 2461  CA  PHE B 103     4982   5291   7654   -317   1042    536       C  
ATOM   2462  C   PHE B 103      27.430   3.870 -85.737  1.00 48.58           C  
ANISOU 2462  C   PHE B 103     5242   5492   7722   -316   1022    437       C  
ATOM   2463  O   PHE B 103      27.151   4.010 -84.564  1.00 48.61           O  
ANISOU 2463  O   PHE B 103     5257   5492   7719   -348    932    395       O  
ATOM   2464  CB  PHE B 103      29.913   3.994 -85.818  1.00 50.75           C  
ANISOU 2464  CB  PHE B 103     5350   5725   8207   -312   1044    618       C  
ATOM   2465  CG  PHE B 103      31.132   4.743 -86.265  1.00 54.33           C  
ANISOU 2465  CG  PHE B 103     5706   6148   8787   -316   1055    728       C  
ATOM   2466  CD1 PHE B 103      31.659   4.544 -87.526  1.00 57.65           C  
ANISOU 2466  CD1 PHE B 103     6102   6567   9234   -270   1177    795       C  
ATOM   2467  CD2 PHE B 103      31.688   5.731 -85.469  1.00 58.54           C  
ANISOU 2467  CD2 PHE B 103     6180   6652   9410   -367    942    764       C  
ATOM   2468  CE1 PHE B 103      32.712   5.325 -87.989  1.00 59.72           C  
ANISOU 2468  CE1 PHE B 103     6274   6802   9616   -273   1191    900       C  
ATOM   2469  CE2 PHE B 103      32.756   6.493 -85.926  1.00 62.56           C  
ANISOU 2469  CE2 PHE B 103     6596   7132  10041   -374    948    869       C  
ATOM   2470  CZ  PHE B 103      33.247   6.299 -87.191  1.00 60.54           C  
ANISOU 2470  CZ  PHE B 103     6310   6878   9814   -326   1075    938       C  
ATOM   2471  N   ASP B 104      26.800   3.027 -86.519  1.00 43.28           N  
ANISOU 2471  N   ASP B 104     4632   4843   6967   -279   1107    405       N  
ATOM   2472  CA  ASP B 104      25.777   2.166 -86.020  1.00 41.68           C  
ANISOU 2472  CA  ASP B 104     4502   4663   6670   -274   1095    323       C  
ATOM   2473  C   ASP B 104      26.418   0.937 -85.349  1.00 45.23           C  
ANISOU 2473  C   ASP B 104     4928   5115   7142   -259   1108    341       C  
ATOM   2474  O   ASP B 104      26.741  -0.036 -86.020  1.00 46.23           O  
ANISOU 2474  O   ASP B 104     5062   5247   7257   -219   1198    367       O  
ATOM   2475  CB  ASP B 104      24.869   1.746 -87.149  1.00 43.51           C  
ANISOU 2475  CB  ASP B 104     4811   4913   6809   -246   1171    286       C  
ATOM   2476  CG  ASP B 104      23.689   0.874 -86.758  1.00 48.64           C  
ANISOU 2476  CG  ASP B 104     5537   5584   7361   -242   1159    204       C  
ATOM   2477  OD1 ASP B 104      23.487   0.627 -85.530  1.00 46.50           O  
ANISOU 2477  OD1 ASP B 104     5263   5317   7089   -261   1094    169       O  
ATOM   2478  OD2 ASP B 104      22.926   0.531 -87.639  1.00 57.55           O  
ANISOU 2478  OD2 ASP B 104     6730   6722   8415   -225   1208    176       O  
ATOM   2479  N   MET B 105      26.543   0.962 -84.029  1.00 39.98           N  
ANISOU 2479  N   MET B 105     4243   4444   6501   -290   1018    324       N  
ATOM   2480  CA  MET B 105      27.113  -0.162 -83.297  1.00 39.91           C  
ANISOU 2480  CA  MET B 105     4213   4438   6515   -280   1019    340       C  
ATOM   2481  C   MET B 105      26.067  -0.755 -82.359  1.00 40.33           C  
ANISOU 2481  C   MET B 105     4332   4509   6481   -289    972    253       C  
ATOM   2482  O   MET B 105      26.409  -1.250 -81.297  1.00 39.27           O  
ANISOU 2482  O   MET B 105     4181   4371   6367   -303    923    254       O  
ATOM   2483  CB  MET B 105      28.385   0.276 -82.565  1.00 42.77           C  
ANISOU 2483  CB  MET B 105     4484   4770   6995   -308    955    416       C  
ATOM   2484  CG  MET B 105      29.514   0.708 -83.526  1.00 46.11           C  
ANISOU 2484  CG  MET B 105     4828   5173   7517   -292   1015    518       C  
ATOM   2485  SD  MET B 105      30.792   1.716 -82.743  1.00 51.51           S  
ANISOU 2485  SD  MET B 105     5407   5816   8347   -341    911    607       S  
ATOM   2486  CE  MET B 105      31.529   0.648 -81.843  1.00 49.80           C  
ANISOU 2486  CE  MET B 105     5150   5593   8177   -340    890    642       C  
ATOM   2487  N   GLY B 106      24.802  -0.712 -82.779  1.00 34.72           N  
ANISOU 2487  N   GLY B 106     3697   3818   5679   -282    991    185       N  
ATOM   2488  CA  GLY B 106      23.695  -1.257 -82.012  1.00 34.95           C  
ANISOU 2488  CA  GLY B 106     3790   3865   5626   -287    958    106       C  
ATOM   2489  C   GLY B 106      23.197  -0.414 -80.871  1.00 34.95           C  
ANISOU 2489  C   GLY B 106     3806   3855   5619   -324    861     63       C  
ATOM   2490  O   GLY B 106      23.736   0.653 -80.575  1.00 33.86           O  
ANISOU 2490  O   GLY B 106     3632   3693   5539   -352    804     91       O  
ATOM   2491  N   PHE B 107      22.141  -0.914 -80.238  1.00 34.31           N  
ANISOU 2491  N   PHE B 107     3784   3789   5463   -323    843     -4       N  
ATOM   2492  CA  PHE B 107      21.506  -0.268 -79.080  1.00 35.29           C  
ANISOU 2492  CA  PHE B 107     3942   3902   5563   -350    763    -53       C  
ATOM   2493  C   PHE B 107      22.283  -0.761 -77.859  1.00 37.41           C  
ANISOU 2493  C   PHE B 107     4190   4160   5863   -364    709    -38       C  
ATOM   2494  O   PHE B 107      21.986  -1.794 -77.291  1.00 34.44           O  
ANISOU 2494  O   PHE B 107     3839   3799   5448   -352    716    -65       O  
ATOM   2495  CB  PHE B 107      20.015  -0.595 -79.010  1.00 37.54           C  
ANISOU 2495  CB  PHE B 107     4296   4208   5761   -337    779   -123       C  
ATOM   2496  CG  PHE B 107      19.211  -0.266 -80.249  1.00 41.39           C  
ANISOU 2496  CG  PHE B 107     4805   4705   6216   -325    829   -133       C  
ATOM   2497  CD1 PHE B 107      19.441   0.909 -80.962  1.00 50.60           C  
ANISOU 2497  CD1 PHE B 107     5949   5857   7419   -337    826   -107       C  
ATOM   2498  CD2 PHE B 107      18.100  -1.010 -80.586  1.00 42.63           C  
ANISOU 2498  CD2 PHE B 107     5010   4881   6305   -307    866   -172       C  
ATOM   2499  CE1 PHE B 107      18.699   1.192 -82.120  1.00 52.41           C  
ANISOU 2499  CE1 PHE B 107     6203   6095   7617   -327    869   -114       C  
ATOM   2500  CE2 PHE B 107      17.364  -0.727 -81.736  1.00 46.01           C  
ANISOU 2500  CE2 PHE B 107     5462   5316   6705   -300    902   -177       C  
ATOM   2501  CZ  PHE B 107      17.715   0.308 -82.535  1.00 46.78           C  
ANISOU 2501  CZ  PHE B 107     5536   5400   6836   -308    908   -147       C  
ATOM   2502  N   ASP B 108      23.355  -0.065 -77.544  1.00 36.23           N  
ANISOU 2502  N   ASP B 108     3991   3983   5792   -391    655     13       N  
ATOM   2503  CA  ASP B 108      24.281  -0.533 -76.526  1.00 35.82           C  
ANISOU 2503  CA  ASP B 108     3909   3916   5785   -408    600     45       C  
ATOM   2504  C   ASP B 108      23.785  -0.341 -75.088  1.00 37.15           C  
ANISOU 2504  C   ASP B 108     4137   4070   5910   -433    515     -8       C  
ATOM   2505  O   ASP B 108      24.120  -1.168 -74.261  1.00 34.76           O  
ANISOU 2505  O   ASP B 108     3835   3767   5605   -437    489     -5       O  
ATOM   2506  CB  ASP B 108      25.685   0.051 -76.736  1.00 35.31           C  
ANISOU 2506  CB  ASP B 108     3762   3823   5832   -428    572    132       C  
ATOM   2507  CG  ASP B 108      25.865   1.567 -76.686  1.00 36.54           C  
ANISOU 2507  CG  ASP B 108     3909   3946   6028   -464    505    145       C  
ATOM   2508  OD1 ASP B 108      24.861   2.286 -76.715  1.00 34.38           O  
ANISOU 2508  OD1 ASP B 108     3694   3674   5696   -467    495     87       O  
ATOM   2509  OD2 ASP B 108      27.032   2.035 -76.714  1.00 40.05           O  
ANISOU 2509  OD2 ASP B 108     4284   4363   6570   -486    468    221       O  
ATOM   2510  N   TYR B 109      22.979   0.687 -74.795  1.00 34.37           N  
ANISOU 2510  N   TYR B 109     3839   3703   5518   -448    478    -56       N  
ATOM   2511  CA  TYR B 109      22.446   0.905 -73.433  1.00 34.19           C  
ANISOU 2511  CA  TYR B 109     3887   3661   5443   -467    407   -109       C  
ATOM   2512  C   TYR B 109      20.985   1.163 -73.552  1.00 37.46           C  
ANISOU 2512  C   TYR B 109     4367   4088   5778   -447    443   -177       C  
ATOM   2513  O   TYR B 109      20.552   1.877 -74.468  1.00 35.60           O  
ANISOU 2513  O   TYR B 109     4124   3856   5545   -440    477   -179       O  
ATOM   2514  CB  TYR B 109      23.142   2.082 -72.676  1.00 35.84           C  
ANISOU 2514  CB  TYR B 109     4101   3820   5698   -512    303    -88       C  
ATOM   2515  CG  TYR B 109      24.549   1.742 -72.241  1.00 38.64           C  
ANISOU 2515  CG  TYR B 109     4396   4154   6132   -538    246    -18       C  
ATOM   2516  CD1 TYR B 109      24.790   1.110 -71.033  1.00 40.97           C  
ANISOU 2516  CD1 TYR B 109     4721   4436   6408   -553    187    -27       C  
ATOM   2517  CD2 TYR B 109      25.639   2.043 -73.045  1.00 40.27           C  
ANISOU 2517  CD2 TYR B 109     4512   4352   6437   -547    252     61       C  
ATOM   2518  CE1 TYR B 109      26.087   0.859 -70.598  1.00 41.29           C  
ANISOU 2518  CE1 TYR B 109     4706   4454   6530   -582    124     44       C  
ATOM   2519  CE2 TYR B 109      26.930   1.710 -72.666  1.00 41.60           C  
ANISOU 2519  CE2 TYR B 109     4616   4499   6691   -571    201    136       C  
ATOM   2520  CZ  TYR B 109      27.156   1.108 -71.443  1.00 49.40           C  
ANISOU 2520  CZ  TYR B 109     5634   5473   7661   -589    135    128       C  
ATOM   2521  OH  TYR B 109      28.437   0.737 -71.072  1.00 51.15           O  
ANISOU 2521  OH  TYR B 109     5787   5674   7976   -614     81    208       O  
ATOM   2522  N   TRP B 110      20.216   0.549 -72.636  1.00 34.79           N  
ANISOU 2522  N   TRP B 110     4089   3757   5372   -436    439   -227       N  
ATOM   2523  CA  TRP B 110      18.761   0.612 -72.614  1.00 33.72           C  
ANISOU 2523  CA  TRP B 110     4014   3634   5164   -414    478   -287       C  
ATOM   2524  C   TRP B 110      18.271   1.097 -71.274  1.00 37.82           C  
ANISOU 2524  C   TRP B 110     4611   4122   5637   -424    422   -331       C  
ATOM   2525  O   TRP B 110      18.920   0.868 -70.273  1.00 37.49           O  
ANISOU 2525  O   TRP B 110     4587   4060   5598   -443    363   -325       O  
ATOM   2526  CB  TRP B 110      18.171  -0.782 -72.827  1.00 31.60           C  
ANISOU 2526  CB  TRP B 110     3748   3405   4853   -382    542   -304       C  
ATOM   2527  CG  TRP B 110      18.462  -1.407 -74.144  1.00 31.78           C  
ANISOU 2527  CG  TRP B 110     3717   3457   4902   -365    607   -270       C  
ATOM   2528  CD1 TRP B 110      19.674  -1.778 -74.623  1.00 34.13           C  
ANISOU 2528  CD1 TRP B 110     3953   3756   5259   -368    615   -214       C  
ATOM   2529  CD2 TRP B 110      17.491  -1.906 -75.079  1.00 31.49           C  
ANISOU 2529  CD2 TRP B 110     3691   3448   4827   -338    676   -288       C  
ATOM   2530  NE1 TRP B 110      19.537  -2.314 -75.875  1.00 34.05           N  
ANISOU 2530  NE1 TRP B 110     3920   3770   5246   -344    690   -199       N  
ATOM   2531  CE2 TRP B 110      18.208  -2.467 -76.158  1.00 34.65           C  
ANISOU 2531  CE2 TRP B 110     4043   3862   5259   -327    723   -245       C  
ATOM   2532  CE3 TRP B 110      16.082  -1.941 -75.105  1.00 31.51           C  
ANISOU 2532  CE3 TRP B 110     3739   3460   4773   -323    701   -333       C  
ATOM   2533  CZ2 TRP B 110      17.578  -3.003 -77.283  1.00 32.61           C  
ANISOU 2533  CZ2 TRP B 110     3793   3625   4971   -305    788   -250       C  
ATOM   2534  CZ3 TRP B 110      15.452  -2.450 -76.236  1.00 32.41           C  
ANISOU 2534  CZ3 TRP B 110     3851   3597   4867   -305    759   -332       C  
ATOM   2535  CH2 TRP B 110      16.208  -2.927 -77.333  1.00 33.06           C  
ANISOU 2535  CH2 TRP B 110     3896   3690   4975   -298    799   -293       C  
ATOM   2536  N   GLY B 111      17.102   1.717 -71.265  1.00 34.64           N  
ANISOU 2536  N   GLY B 111     4259   3713   5191   -410    445   -374       N  
ATOM   2537  CA  GLY B 111      16.423   2.065 -70.024  1.00 35.34           C  
ANISOU 2537  CA  GLY B 111     4433   3772   5223   -408    415   -421       C  
ATOM   2538  C   GLY B 111      15.849   0.786 -69.411  1.00 35.09           C  
ANISOU 2538  C   GLY B 111     4428   3765   5138   -383    448   -444       C  
ATOM   2539  O   GLY B 111      15.902  -0.283 -70.020  1.00 32.88           O  
ANISOU 2539  O   GLY B 111     4102   3525   4867   -369    493   -428       O  
ATOM   2540  N   GLN B 112      15.311   0.874 -68.207  1.00 32.23           N  
ANISOU 2540  N   GLN B 112     4147   3379   4721   -377    429   -482       N  
ATOM   2541  CA  GLN B 112      14.810  -0.301 -67.480  1.00 31.33           C  
ANISOU 2541  CA  GLN B 112     4063   3285   4558   -355    456   -502       C  
ATOM   2542  C   GLN B 112      13.424  -0.777 -67.934  1.00 34.29           C  
ANISOU 2542  C   GLN B 112     4439   3689   4901   -317    537   -524       C  
ATOM   2543  O   GLN B 112      13.007  -1.896 -67.620  1.00 34.47           O  
ANISOU 2543  O   GLN B 112     4466   3737   4895   -297    568   -531       O  
ATOM   2544  CB  GLN B 112      14.861  -0.068 -65.959  1.00 32.92           C  
ANISOU 2544  CB  GLN B 112     4356   3444   4709   -363    402   -529       C  
ATOM   2545  CG  GLN B 112      13.704   0.777 -65.332  1.00 35.87           C  
ANISOU 2545  CG  GLN B 112     4820   3783   5027   -341    424   -573       C  
ATOM   2546  CD  GLN B 112      13.784   2.248 -65.590  1.00 45.82           C  
ANISOU 2546  CD  GLN B 112     6099   5002   6308   -357    396   -576       C  
ATOM   2547  OE1 GLN B 112      14.606   2.724 -66.374  1.00 40.51           O  
ANISOU 2547  OE1 GLN B 112     5365   4331   5695   -384    364   -545       O  
ATOM   2548  NE2 GLN B 112      12.920   3.017 -64.924  1.00 41.70           N  
ANISOU 2548  NE2 GLN B 112     5665   4441   5739   -338    410   -613       N  
ATOM   2549  N   GLY B 113      12.748   0.049 -68.695  1.00 30.67           N  
ANISOU 2549  N   GLY B 113     3972   3227   4454   -309    567   -528       N  
ATOM   2550  CA  GLY B 113      11.440  -0.260 -69.234  1.00 29.91           C  
ANISOU 2550  CA  GLY B 113     3871   3154   4342   -279    636   -539       C  
ATOM   2551  C   GLY B 113      10.342   0.380 -68.402  1.00 34.93           C  
ANISOU 2551  C   GLY B 113     4577   3758   4938   -257    655   -571       C  
ATOM   2552  O   GLY B 113      10.536   0.652 -67.202  1.00 33.35           O  
ANISOU 2552  O   GLY B 113     4445   3523   4703   -258    623   -592       O  
ATOM   2553  N   THR B 114       9.241   0.756 -69.081  1.00 32.84           N  
ANISOU 2553  N   THR B 114     4299   3497   4681   -238    704   -571       N  
ATOM   2554  CA  THR B 114       8.041   1.345 -68.459  1.00 32.66           C  
ANISOU 2554  CA  THR B 114     4332   3444   4632   -209    740   -592       C  
ATOM   2555  C   THR B 114       6.885   0.444 -68.821  1.00 34.73           C  
ANISOU 2555  C   THR B 114     4567   3737   4892   -181    800   -583       C  
ATOM   2556  O   THR B 114       6.604   0.281 -69.995  1.00 32.60           O  
ANISOU 2556  O   THR B 114     4240   3493   4654   -186    817   -561       O  
ATOM   2557  CB  THR B 114       7.767   2.782 -68.939  1.00 37.47           C  
ANISOU 2557  CB  THR B 114     4946   4023   5267   -213    739   -592       C  
ATOM   2558  OG1 THR B 114       8.892   3.617 -68.649  1.00 35.09           O  
ANISOU 2558  OG1 THR B 114     4667   3692   4975   -243    675   -597       O  
ATOM   2559  CG2 THR B 114       6.565   3.394 -68.276  1.00 33.02           C  
ANISOU 2559  CG2 THR B 114     4441   3425   4682   -179    783   -610       C  
ATOM   2560  N   THR B 115       6.186  -0.090 -67.828  1.00 32.21           N  
ANISOU 2560  N   THR B 115     4292   3411   4535   -153    831   -596       N  
ATOM   2561  CA  THR B 115       4.999  -0.904 -68.091  1.00 32.99           C  
ANISOU 2561  CA  THR B 115     4364   3532   4638   -127    886   -581       C  
ATOM   2562  C   THR B 115       3.846   0.040 -68.318  1.00 34.92           C  
ANISOU 2562  C   THR B 115     4613   3750   4903   -105    928   -574       C  
ATOM   2563  O   THR B 115       3.628   0.942 -67.517  1.00 31.81           O  
ANISOU 2563  O   THR B 115     4280   3314   4491    -89    938   -592       O  
ATOM   2564  CB  THR B 115       4.708  -1.841 -66.924  1.00 38.67           C  
ANISOU 2564  CB  THR B 115     5124   4253   5314   -103    907   -592       C  
ATOM   2565  OG1 THR B 115       5.868  -2.659 -66.738  1.00 43.58           O  
ANISOU 2565  OG1 THR B 115     5739   4897   5923   -126    863   -596       O  
ATOM   2566  CG2 THR B 115       3.521  -2.681 -67.182  1.00 34.26           C  
ANISOU 2566  CG2 THR B 115     4534   3716   4768    -78    959   -571       C  
ATOM   2567  N   VAL B 116       3.185  -0.100 -69.477  1.00 32.96           N  
ANISOU 2567  N   VAL B 116     4304   3523   4695   -108    947   -546       N  
ATOM   2568  CA  VAL B 116       2.044   0.741 -69.821  1.00 33.42           C  
ANISOU 2568  CA  VAL B 116     4353   3558   4785    -90    985   -529       C  
ATOM   2569  C   VAL B 116       0.844  -0.158 -70.079  1.00 34.89           C  
ANISOU 2569  C   VAL B 116     4503   3762   4991    -71   1026   -498       C  
ATOM   2570  O   VAL B 116       0.935  -1.042 -70.899  1.00 31.48           O  
ANISOU 2570  O   VAL B 116     4026   3364   4569    -90   1010   -481       O  
ATOM   2571  CB  VAL B 116       2.280   1.700 -71.017  1.00 36.23           C  
ANISOU 2571  CB  VAL B 116     4672   3913   5182   -116    961   -516       C  
ATOM   2572  CG1 VAL B 116       0.972   2.454 -71.369  1.00 35.77           C  
ANISOU 2572  CG1 VAL B 116     4598   3830   5162    -96   1002   -491       C  
ATOM   2573  CG2 VAL B 116       3.411   2.664 -70.700  1.00 36.72           C  
ANISOU 2573  CG2 VAL B 116     4768   3951   5231   -135    919   -541       C  
ATOM   2574  N   THR B 117      -0.270   0.092 -69.380  1.00 33.85           N  
ANISOU 2574  N   THR B 117     4394   3603   4866    -34   1079   -487       N  
ATOM   2575  CA  THR B 117      -1.504  -0.661 -69.578  1.00 33.11           C  
ANISOU 2575  CA  THR B 117     4260   3519   4803    -15   1118   -448       C  
ATOM   2576  C   THR B 117      -2.551   0.298 -70.078  1.00 35.37           C  
ANISOU 2576  C   THR B 117     4519   3777   5144     -2   1149   -415       C  
ATOM   2577  O   THR B 117      -2.704   1.379 -69.524  1.00 33.61           O  
ANISOU 2577  O   THR B 117     4336   3515   4919     20   1175   -427       O  
ATOM   2578  CB  THR B 117      -1.969  -1.371 -68.282  1.00 38.04           C  
ANISOU 2578  CB  THR B 117     4922   4134   5396     23   1163   -451       C  
ATOM   2579  OG1 THR B 117      -0.941  -2.275 -67.863  1.00 39.30           O  
ANISOU 2579  OG1 THR B 117     5103   4321   5509      8   1128   -480       O  
ATOM   2580  CG2 THR B 117      -3.295  -2.143 -68.484  1.00 35.78           C  
ANISOU 2580  CG2 THR B 117     4586   3855   5153     43   1203   -401       C  
ATOM   2581  N   VAL B 118      -3.267  -0.101 -71.129  1.00 34.10           N  
ANISOU 2581  N   VAL B 118     4293   3632   5030    -17   1142   -372       N  
ATOM   2582  CA  VAL B 118      -4.366   0.664 -71.675  1.00 34.72           C  
ANISOU 2582  CA  VAL B 118     4335   3686   5171     -8   1167   -329       C  
ATOM   2583  C   VAL B 118      -5.640  -0.061 -71.265  1.00 38.40           C  
ANISOU 2583  C   VAL B 118     4773   4144   5671     23   1214   -283       C  
ATOM   2584  O   VAL B 118      -5.840  -1.202 -71.624  1.00 36.65           O  
ANISOU 2584  O   VAL B 118     4520   3951   5456      8   1194   -262       O  
ATOM   2585  CB  VAL B 118      -4.252   0.879 -73.204  1.00 38.11           C  
ANISOU 2585  CB  VAL B 118     4714   4132   5634    -51   1117   -307       C  
ATOM   2586  CG1 VAL B 118      -5.449   1.699 -73.717  1.00 37.76           C  
ANISOU 2586  CG1 VAL B 118     4630   4058   5660    -42   1139   -257       C  
ATOM   2587  CG2 VAL B 118      -2.929   1.572 -73.536  1.00 37.51           C  
ANISOU 2587  CG2 VAL B 118     4663   4062   5526    -77   1076   -349       C  
ATOM   2588  N   SER B 119      -6.465   0.570 -70.457  1.00 38.70           N  
ANISOU 2588  N   SER B 119     4830   4144   5733     67   1279   -266       N  
ATOM   2589  CA  SER B 119      -7.698  -0.053 -69.985  1.00 39.53           C  
ANISOU 2589  CA  SER B 119     4905   4236   5878    102   1334   -214       C  
ATOM   2590  C   SER B 119      -8.703   0.982 -69.453  1.00 45.50           C  
ANISOU 2590  C   SER B 119     5667   4940   6681    151   1411   -181       C  
ATOM   2591  O   SER B 119      -8.319   1.959 -68.832  1.00 44.56           O  
ANISOU 2591  O   SER B 119     5611   4791   6529    173   1438   -219       O  
ATOM   2592  CB  SER B 119      -7.393  -1.064 -68.878  1.00 40.57           C  
ANISOU 2592  CB  SER B 119     5080   4381   5954    124   1355   -239       C  
ATOM   2593  OG  SER B 119      -8.575  -1.714 -68.457  1.00 48.93           O  
ANISOU 2593  OG  SER B 119     6104   5429   7057    157   1409   -183       O  
ATOM   2594  N   SER B 120      -9.986   0.714 -69.665  1.00 45.64           N  
ANISOU 2594  N   SER B 120     5621   4944   6777    168   1446   -108       N  
ATOM   2595  CA  SER B 120     -11.084   1.488 -69.100  1.00 46.59           C  
ANISOU 2595  CA  SER B 120     5736   5013   6953    222   1533    -62       C  
ATOM   2596  C   SER B 120     -11.507   0.809 -67.784  1.00 52.03           C  
ANISOU 2596  C   SER B 120     6460   5688   7620    276   1609    -54       C  
ATOM   2597  O   SER B 120     -12.292   1.405 -67.068  1.00 53.51           O  
ANISOU 2597  O   SER B 120     6664   5830   7839    332   1698    -23       O  
ATOM   2598  CB  SER B 120     -12.251   1.602 -70.076  1.00 48.15           C  
ANISOU 2598  CB  SER B 120     5837   5199   7260    210   1528     24       C  
ATOM   2599  OG  SER B 120     -12.373   0.427 -70.851  1.00 62.57           O  
ANISOU 2599  OG  SER B 120     7606   7063   9106    167   1462     53       O  
ATOM   2600  N   ALA B 121     -10.892  -0.369 -67.395  1.00 46.39           N  
ANISOU 2600  N   ALA B 121     5769   5012   6844    263   1580    -87       N  
ATOM   2601  CA  ALA B 121     -11.192  -0.991 -66.107  1.00 44.38           C  
ANISOU 2601  CA  ALA B 121     5557   4745   6559    313   1651    -84       C  
ATOM   2602  C   ALA B 121     -10.571  -0.182 -64.986  1.00 49.20           C  
ANISOU 2602  C   ALA B 121     6282   5324   7090    349   1695   -147       C  
ATOM   2603  O   ALA B 121      -9.573   0.500 -65.186  1.00 49.60           O  
ANISOU 2603  O   ALA B 121     6378   5376   7090    321   1644   -205       O  
ATOM   2604  CB  ALA B 121     -10.696  -2.425 -66.049  1.00 43.62           C  
ANISOU 2604  CB  ALA B 121     5453   4697   6423    286   1603   -100       C  
ATOM   2605  N   SER B 122     -11.151  -0.270 -63.796  1.00 47.55           N  
ANISOU 2605  N   SER B 122     6122   5080   6865    411   1787   -132       N  
ATOM   2606  CA  SER B 122     -10.662   0.512 -62.673  1.00 48.46           C  
ANISOU 2606  CA  SER B 122     6360   5153   6898    449   1833   -188       C  
ATOM   2607  C   SER B 122      -9.429  -0.074 -62.008  1.00 50.46           C  
ANISOU 2607  C   SER B 122     6694   5432   7046    427   1782   -260       C  
ATOM   2608  O   SER B 122      -9.254  -1.302 -61.886  1.00 49.56           O  
ANISOU 2608  O   SER B 122     6556   5358   6917    413   1757   -256       O  
ATOM   2609  CB  SER B 122     -11.774   0.724 -61.642  1.00 53.47           C  
ANISOU 2609  CB  SER B 122     7030   5734   7553    530   1963   -142       C  
ATOM   2610  OG  SER B 122     -12.227  -0.524 -61.156  1.00 61.53           O  
ANISOU 2610  OG  SER B 122     8025   6775   8579    548   1993   -107       O  
ATOM   2611  N   THR B 123      -8.576   0.841 -61.564  1.00 45.45           N  
ANISOU 2611  N   THR B 123     6157   4769   6342    424   1762   -323       N  
ATOM   2612  CA  THR B 123      -7.376   0.512 -60.815  1.00 44.50           C  
ANISOU 2612  CA  THR B 123     6128   4660   6122    405   1712   -390       C  
ATOM   2613  C   THR B 123      -7.775  -0.012 -59.433  1.00 47.90           C  
ANISOU 2613  C   THR B 123     6639   5064   6498    461   1791   -387       C  
ATOM   2614  O   THR B 123      -8.631   0.594 -58.799  1.00 47.93           O  
ANISOU 2614  O   THR B 123     6690   5013   6509    522   1889   -364       O  
ATOM   2615  CB  THR B 123      -6.492   1.741 -60.719  1.00 40.33           C  
ANISOU 2615  CB  THR B 123     5680   4097   5545    387   1671   -447       C  
ATOM   2616  OG1 THR B 123      -5.924   1.930 -62.000  1.00 46.36           O  
ANISOU 2616  OG1 THR B 123     6365   4899   6351    328   1587   -450       O  
ATOM   2617  CG2 THR B 123      -5.405   1.595 -59.722  1.00 43.20           C  
ANISOU 2617  CG2 THR B 123     6156   4452   5807    377   1630   -508       C  
ATOM   2618  N   LYS B 124      -7.162  -1.132 -58.973  1.00 43.46           N  
ANISOU 2618  N   LYS B 124     6093   4537   5883    443   1752   -409       N  
ATOM   2619  CA  LYS B 124      -7.469  -1.738 -57.672  1.00 41.25           C  
ANISOU 2619  CA  LYS B 124     5891   4237   5547    492   1820   -407       C  
ATOM   2620  C   LYS B 124      -6.186  -2.207 -56.992  1.00 43.98           C  
ANISOU 2620  C   LYS B 124     6319   4597   5794    460   1746   -468       C  
ATOM   2621  O   LYS B 124      -5.397  -2.919 -57.596  1.00 41.73           O  
ANISOU 2621  O   LYS B 124     5976   4366   5515    405   1659   -482       O  
ATOM   2622  CB  LYS B 124      -8.448  -2.915 -57.872  1.00 41.92           C  
ANISOU 2622  CB  LYS B 124     5876   4354   5698    510   1864   -339       C  
ATOM   2623  CG  LYS B 124      -9.054  -3.421 -56.587  1.00 59.62           C  
ANISOU 2623  CG  LYS B 124     8184   6567   7901    573   1959   -319       C  
ATOM   2624  CD  LYS B 124      -9.799  -4.753 -56.769  1.00 68.16           C  
ANISOU 2624  CD  LYS B 124     9165   7688   9044    579   1981   -256       C  
ATOM   2625  CE  LYS B 124     -10.443  -5.221 -55.481  1.00 71.98           C  
ANISOU 2625  CE  LYS B 124     9713   8141   9493    646   2084   -229       C  
ATOM   2626  NZ  LYS B 124      -9.432  -5.584 -54.436  1.00 88.58           N  
ANISOU 2626  NZ  LYS B 124    11936  10245  11476    641   2053   -294       N  
ATOM   2627  N   GLY B 125      -5.989  -1.811 -55.739  1.00 41.64           N  
ANISOU 2627  N   GLY B 125     6162   4250   5410    495   1783   -502       N  
ATOM   2628  CA  GLY B 125      -4.825  -2.212 -54.965  1.00 40.53           C  
ANISOU 2628  CA  GLY B 125     6112   4114   5175    466   1713   -556       C  
ATOM   2629  C   GLY B 125      -5.016  -3.625 -54.432  1.00 45.48           C  
ANISOU 2629  C   GLY B 125     6718   4775   5786    478   1732   -534       C  
ATOM   2630  O   GLY B 125      -6.152  -4.074 -54.238  1.00 43.30           O  
ANISOU 2630  O   GLY B 125     6407   4496   5549    528   1826   -482       O  
ATOM   2631  N   PRO B 126      -3.911  -4.362 -54.211  1.00 42.31           N  
ANISOU 2631  N   PRO B 126     6333   4406   5335    432   1644   -567       N  
ATOM   2632  CA  PRO B 126      -4.034  -5.757 -53.737  1.00 42.08           C  
ANISOU 2632  CA  PRO B 126     6282   4413   5293    440   1656   -546       C  
ATOM   2633  C   PRO B 126      -4.324  -5.904 -52.259  1.00 48.51           C  
ANISOU 2633  C   PRO B 126     7226   5183   6023    493   1724   -553       C  
ATOM   2634  O   PRO B 126      -3.992  -5.018 -51.482  1.00 48.34           O  
ANISOU 2634  O   PRO B 126     7338   5104   5925    506   1728   -592       O  
ATOM   2635  CB  PRO B 126      -2.632  -6.314 -53.971  1.00 42.18           C  
ANISOU 2635  CB  PRO B 126     6281   4466   5278    372   1535   -583       C  
ATOM   2636  CG  PRO B 126      -1.740  -5.114 -53.838  1.00 46.15           C  
ANISOU 2636  CG  PRO B 126     6870   4930   5736    346   1475   -631       C  
ATOM   2637  CD  PRO B 126      -2.498  -3.989 -54.434  1.00 42.05           C  
ANISOU 2637  CD  PRO B 126     6330   4381   5266    370   1527   -618       C  
ATOM   2638  N   SER B 127      -4.831  -7.086 -51.877  1.00 45.44           N  
ANISOU 2638  N   SER B 127     6803   4820   5641    516   1768   -517       N  
ATOM   2639  CA  SER B 127      -4.945  -7.508 -50.484  1.00 45.74           C  
ANISOU 2639  CA  SER B 127     6958   4827   5593    559   1820   -522       C  
ATOM   2640  C   SER B 127      -3.729  -8.398 -50.311  1.00 46.35           C  
ANISOU 2640  C   SER B 127     7039   4946   5626    501   1711   -554       C  
ATOM   2641  O   SER B 127      -3.410  -9.131 -51.246  1.00 46.78           O  
ANISOU 2641  O   SER B 127     6971   5060   5743    457   1650   -542       O  
ATOM   2642  CB  SER B 127      -6.224  -8.293 -50.227  1.00 49.68           C  
ANISOU 2642  CB  SER B 127     7403   5333   6139    617   1931   -456       C  
ATOM   2643  OG  SER B 127      -7.363  -7.456 -50.331  1.00 51.01           O  
ANISOU 2643  OG  SER B 127     7566   5459   6356    674   2038   -418       O  
ATOM   2644  N   VAL B 128      -3.001  -8.280 -49.189  1.00 42.00           N  
ANISOU 2644  N   VAL B 128     6629   4359   4968    498   1680   -596       N  
ATOM   2645  CA  VAL B 128      -1.778  -9.054 -48.941  1.00 42.62           C  
ANISOU 2645  CA  VAL B 128     6718   4469   5004    443   1572   -623       C  
ATOM   2646  C   VAL B 128      -2.033 -10.017 -47.802  1.00 46.46           C  
ANISOU 2646  C   VAL B 128     7269   4951   5430    476   1617   -609       C  
ATOM   2647  O   VAL B 128      -2.417  -9.593 -46.715  1.00 46.01           O  
ANISOU 2647  O   VAL B 128     7350   4837   5296    525   1684   -617       O  
ATOM   2648  CB  VAL B 128      -0.530  -8.171 -48.733  1.00 46.16           C  
ANISOU 2648  CB  VAL B 128     7262   4885   5393    394   1468   -677       C  
ATOM   2649  CG1 VAL B 128       0.732  -9.039 -48.549  1.00 45.15           C  
ANISOU 2649  CG1 VAL B 128     7124   4791   5239    334   1354   -694       C  
ATOM   2650  CG2 VAL B 128      -0.359  -7.229 -49.928  1.00 45.46           C  
ANISOU 2650  CG2 VAL B 128     7099   4802   5373    365   1433   -685       C  
ATOM   2651  N   PHE B 129      -1.923 -11.340 -48.088  1.00 41.87           N  
ANISOU 2651  N   PHE B 129     6587   4431   4889    455   1590   -583       N  
ATOM   2652  CA  PHE B 129      -2.240 -12.376 -47.113  1.00 40.52           C  
ANISOU 2652  CA  PHE B 129     6455   4264   4675    487   1635   -562       C  
ATOM   2653  C   PHE B 129      -1.049 -13.197 -46.859  1.00 44.16           C  
ANISOU 2653  C   PHE B 129     6921   4756   5101    432   1529   -584       C  
ATOM   2654  O   PHE B 129      -0.398 -13.593 -47.811  1.00 45.48           O  
ANISOU 2654  O   PHE B 129     6980   4972   5328    380   1450   -586       O  
ATOM   2655  CB  PHE B 129      -3.395 -13.238 -47.633  1.00 41.51           C  
ANISOU 2655  CB  PHE B 129     6453   4428   4891    520   1716   -501       C  
ATOM   2656  CG  PHE B 129      -4.689 -12.467 -47.824  1.00 41.90           C  
ANISOU 2656  CG  PHE B 129     6491   4444   4987    580   1831   -465       C  
ATOM   2657  CD1 PHE B 129      -5.261 -11.770 -46.777  1.00 46.22           C  
ANISOU 2657  CD1 PHE B 129     7171   4925   5467    643   1927   -465       C  
ATOM   2658  CD2 PHE B 129      -5.343 -12.466 -49.043  1.00 42.75           C  
ANISOU 2658  CD2 PHE B 129     6456   4581   5206    573   1845   -427       C  
ATOM   2659  CE1 PHE B 129      -6.443 -11.057 -46.960  1.00 47.32           C  
ANISOU 2659  CE1 PHE B 129     7293   5028   5657    701   2039   -427       C  
ATOM   2660  CE2 PHE B 129      -6.550 -11.801 -49.204  1.00 44.95           C  
ANISOU 2660  CE2 PHE B 129     6715   4826   5537    627   1949   -385       C  
ATOM   2661  CZ  PHE B 129      -7.079 -11.083 -48.172  1.00 44.20           C  
ANISOU 2661  CZ  PHE B 129     6745   4666   5381    692   2048   -385       C  
ATOM   2662  N   PRO B 130      -0.713 -13.466 -45.587  1.00 41.99           N  
ANISOU 2662  N   PRO B 130     6775   4451   4729    443   1523   -599       N  
ATOM   2663  CA  PRO B 130       0.491 -14.281 -45.299  1.00 41.33           C  
ANISOU 2663  CA  PRO B 130     6694   4394   4614    387   1413   -615       C  
ATOM   2664  C   PRO B 130       0.326 -15.776 -45.568  1.00 45.76           C  
ANISOU 2664  C   PRO B 130     7138   5018   5230    382   1418   -578       C  
ATOM   2665  O   PRO B 130      -0.750 -16.341 -45.333  1.00 45.82           O  
ANISOU 2665  O   PRO B 130     7121   5032   5255    434   1515   -539       O  
ATOM   2666  CB  PRO B 130       0.705 -14.039 -43.804  1.00 42.74           C  
ANISOU 2666  CB  PRO B 130     7058   4512   4667    408   1418   -638       C  
ATOM   2667  CG  PRO B 130      -0.707 -13.859 -43.286  1.00 46.96           C  
ANISOU 2667  CG  PRO B 130     7643   5014   5185    491   1568   -610       C  
ATOM   2668  CD  PRO B 130      -1.378 -13.038 -44.331  1.00 42.63           C  
ANISOU 2668  CD  PRO B 130     7012   4468   4720    507   1616   -600       C  
ATOM   2669  N   LEU B 131       1.421 -16.427 -46.024  1.00 41.60           N  
ANISOU 2669  N   LEU B 131     6543   4533   4730    321   1312   -586       N  
ATOM   2670  CA  LEU B 131       1.471 -17.870 -46.250  1.00 39.94           C  
ANISOU 2670  CA  LEU B 131     6232   4379   4565    310   1300   -556       C  
ATOM   2671  C   LEU B 131       2.361 -18.516 -45.198  1.00 45.87           C  
ANISOU 2671  C   LEU B 131     7062   5123   5242    286   1236   -567       C  
ATOM   2672  O   LEU B 131       3.581 -18.399 -45.269  1.00 44.36           O  
ANISOU 2672  O   LEU B 131     6880   4933   5042    231   1130   -589       O  
ATOM   2673  CB  LEU B 131       1.925 -18.221 -47.660  1.00 38.59           C  
ANISOU 2673  CB  LEU B 131     5914   4260   4489    265   1244   -550       C  
ATOM   2674  CG  LEU B 131       1.123 -17.651 -48.804  1.00 40.61           C  
ANISOU 2674  CG  LEU B 131     6086   4525   4820    278   1292   -537       C  
ATOM   2675  CD1 LEU B 131       1.874 -17.837 -50.115  1.00 39.73           C  
ANISOU 2675  CD1 LEU B 131     5861   4454   4780    226   1218   -542       C  
ATOM   2676  CD2 LEU B 131      -0.195 -18.323 -48.914  1.00 42.59           C  
ANISOU 2676  CD2 LEU B 131     6275   4790   5115    324   1386   -492       C  
ATOM   2677  N   ALA B 132       1.747 -19.176 -44.190  1.00 47.26           N  
ANISOU 2677  N   ALA B 132     7299   5290   5370    328   1299   -546       N  
ATOM   2678  CA  ALA B 132       2.513 -19.811 -43.108  1.00 49.05           C  
ANISOU 2678  CA  ALA B 132     7610   5508   5521    309   1241   -553       C  
ATOM   2679  C   ALA B 132       2.069 -21.238 -42.901  1.00 56.29           C  
ANISOU 2679  C   ALA B 132     8460   6464   6463    328   1280   -514       C  
ATOM   2680  O   ALA B 132       0.909 -21.533 -43.123  1.00 55.67           O  
ANISOU 2680  O   ALA B 132     8327   6398   6426    375   1379   -481       O  
ATOM   2681  CB  ALA B 132       2.378 -19.006 -41.819  1.00 50.07           C  
ANISOU 2681  CB  ALA B 132     7928   5566   5532    339   1269   -575       C  
ATOM   2682  N   PRO B 133       2.981 -22.164 -42.562  1.00 58.29           N  
ANISOU 2682  N   PRO B 133     8703   6740   6703    288   1200   -511       N  
ATOM   2683  CA  PRO B 133       2.568 -23.572 -42.421  1.00 60.31           C  
ANISOU 2683  CA  PRO B 133     8889   7037   6991    305   1235   -472       C  
ATOM   2684  C   PRO B 133       1.577 -23.840 -41.281  1.00 69.75           C  
ANISOU 2684  C   PRO B 133    10175   8206   8122    367   1336   -449       C  
ATOM   2685  O   PRO B 133       1.628 -23.183 -40.251  1.00 66.95           O  
ANISOU 2685  O   PRO B 133     9971   7798   7668    385   1347   -468       O  
ATOM   2686  CB  PRO B 133       3.895 -24.322 -42.241  1.00 61.49           C  
ANISOU 2686  CB  PRO B 133     9023   7206   7134    246   1119   -478       C  
ATOM   2687  CG  PRO B 133       4.860 -23.323 -41.774  1.00 65.23           C  
ANISOU 2687  CG  PRO B 133     9607   7635   7542    211   1037   -514       C  
ATOM   2688  CD  PRO B 133       4.427 -21.991 -42.314  1.00 60.37           C  
ANISOU 2688  CD  PRO B 133     9011   6992   6933    226   1073   -537       C  
ATOM   2689  N   CYS B 134       0.652 -24.791 -41.505  1.00 74.58           N  
ANISOU 2689  N   CYS B 134    10695   8851   8793    401   1410   -405       N  
ATOM   2690  CA  CYS B 134      -0.363 -25.198 -40.528  1.00 79.34           C  
ANISOU 2690  CA  CYS B 134    11358   9434   9354    463   1515   -370       C  
ATOM   2691  C   CYS B 134       0.335 -26.100 -39.509  1.00 91.81           C  
ANISOU 2691  C   CYS B 134    13003  11016  10866    446   1463   -368       C  
ATOM   2692  O   CYS B 134       0.378 -27.319 -39.692  1.00 92.99           O  
ANISOU 2692  O   CYS B 134    13059  11209  11065    433   1447   -339       O  
ATOM   2693  CB  CYS B 134      -1.537 -25.910 -41.212  1.00 80.07           C  
ANISOU 2693  CB  CYS B 134    11316   9561   9547    497   1598   -316       C  
ATOM   2694  SG  CYS B 134      -2.812 -26.536 -40.075  1.00 85.63           S  
ANISOU 2694  SG  CYS B 134    12070  10244  10220    576   1733   -258       S  
ATOM   2695  N   SER B 135       0.933 -25.496 -38.471  1.00 93.94           N  
ANISOU 2695  N   SER B 135    13433  11237  11023    440   1429   -399       N  
ATOM   2696  CA  SER B 135       1.653 -26.217 -37.409  1.00 96.84           C  
ANISOU 2696  CA  SER B 135    13883  11598  11315    419   1370   -399       C  
ATOM   2697  C   SER B 135       2.794 -27.092 -37.967  1.00103.10           C  
ANISOU 2697  C   SER B 135    14568  12440  12167    350   1249   -399       C  
ATOM   2698  O   SER B 135       2.596 -28.278 -38.240  1.00101.17           O  
ANISOU 2698  O   SER B 135    14215  12241  11985    351   1260   -366       O  
ATOM   2699  CB  SER B 135       0.687 -27.032 -36.549  1.00102.12           C  
ANISOU 2699  CB  SER B 135    14583  12265  11955    479   1475   -355       C  
ATOM   2700  OG  SER B 135      -0.332 -26.199 -36.012  1.00112.54           O  
ANISOU 2700  OG  SER B 135    16005  13534  13222    548   1595   -350       O  
ATOM   2701  N   ARG B 136       3.981 -26.472 -38.145  1.00103.33           N  
ANISOU 2701  N   ARG B 136    14627  12454  12179    292   1134   -434       N  
ATOM   2702  CA  ARG B 136       5.184 -27.109 -38.696  1.00103.99           C  
ANISOU 2702  CA  ARG B 136    14615  12575  12322    225   1018   -433       C  
ATOM   2703  C   ARG B 136       5.639 -28.314 -37.869  1.00112.07           C  
ANISOU 2703  C   ARG B 136    15652  13612  13319    211    977   -408       C  
ATOM   2704  O   ARG B 136       5.593 -28.281 -36.639  1.00112.18           O  
ANISOU 2704  O   ARG B 136    15803  13587  13232    227    985   -407       O  
ATOM   2705  CB  ARG B 136       6.341 -26.105 -38.846  1.00103.76           C  
ANISOU 2705  CB  ARG B 136    14635  12516  12274    170    907   -468       C  
ATOM   2706  N   SER B 137       6.096 -29.369 -38.574  1.00111.00           N  
ANISOU 2706  N   SER B 137    15375  13528  13272    181    935   -387       N  
ATOM   2707  CA  SER B 137       6.509 -30.652 -38.003  1.00111.77           C  
ANISOU 2707  CA  SER B 137    15452  13647  13368    166    900   -357       C  
ATOM   2708  C   SER B 137       8.026 -30.854 -37.993  1.00115.96           C  
ANISOU 2708  C   SER B 137    15967  14179  13914     97    764   -359       C  
ATOM   2709  O   SER B 137       8.764 -30.108 -38.643  1.00115.73           O  
ANISOU 2709  O   SER B 137    15914  14142  13917     60    700   -379       O  
ATOM   2710  CB  SER B 137       5.886 -31.790 -38.812  1.00115.17           C  
ANISOU 2710  CB  SER B 137    15733  14132  13895    186    957   -326       C  
ATOM   2711  OG  SER B 137       6.629 -32.064 -39.992  1.00122.87           O  
ANISOU 2711  OG  SER B 137    16580  15141  14965    144    897   -328       O  
ATOM   2712  N   THR B 138       8.461 -31.927 -37.295  1.00111.67           N  
ANISOU 2712  N   THR B 138    15426  13647  13358     83    725   -332       N  
ATOM   2713  CA  THR B 138       9.853 -32.369 -37.206  1.00110.75           C  
ANISOU 2713  CA  THR B 138    15280  13533  13267     20    601   -318       C  
ATOM   2714  C   THR B 138       9.972 -33.697 -37.992  1.00111.90           C  
ANISOU 2714  C   THR B 138    15264  13735  13518     16    609   -288       C  
ATOM   2715  O   THR B 138       8.985 -34.428 -38.067  1.00111.70           O  
ANISOU 2715  O   THR B 138    15196  13735  13509     59    697   -273       O  
ATOM   2716  CB  THR B 138      10.304 -32.541 -35.735  1.00120.10           C  
ANISOU 2716  CB  THR B 138    16604  14679  14349      3    540   -308       C  
ATOM   2717  OG1 THR B 138       9.230 -33.043 -34.935  1.00118.81           O  
ANISOU 2717  OG1 THR B 138    16508  14514  14122     58    635   -297       O  
ATOM   2718  CG2 THR B 138      10.840 -31.250 -35.134  1.00118.85           C  
ANISOU 2718  CG2 THR B 138    16590  14459  14108    -25    468   -337       C  
ATOM   2719  N   SER B 139      11.130 -34.029 -38.594  1.00105.67           N  
ANISOU 2719  N   SER B 139    14384  12961  12803    -33    523   -275       N  
ATOM   2720  CA  SER B 139      12.376 -33.264 -38.570  1.00104.44           C  
ANISOU 2720  CA  SER B 139    14258  12776  12649    -89    412   -281       C  
ATOM   2721  C   SER B 139      12.603 -32.665 -39.964  1.00103.84           C  
ANISOU 2721  C   SER B 139    14082  12715  12656    -99    417   -297       C  
ATOM   2722  O   SER B 139      13.497 -33.084 -40.712  1.00103.85           O  
ANISOU 2722  O   SER B 139    13980  12736  12745   -132    366   -277       O  
ATOM   2723  CB  SER B 139      13.528 -34.163 -38.147  1.00108.18           C  
ANISOU 2723  CB  SER B 139    14697  13252  13153   -134    316   -243       C  
ATOM   2724  OG  SER B 139      13.246 -34.771 -36.894  1.00115.34           O  
ANISOU 2724  OG  SER B 139    15695  14146  13981   -122    317   -228       O  
ATOM   2725  N   GLU B 140      11.728 -31.700 -40.316  1.00 94.84           N  
ANISOU 2725  N   GLU B 140    12977  11565  11490    -67    486   -329       N  
ATOM   2726  CA  GLU B 140      11.778 -30.960 -41.574  1.00 90.63           C  
ANISOU 2726  CA  GLU B 140    12370  11042  11022    -72    498   -347       C  
ATOM   2727  C   GLU B 140      12.884 -29.913 -41.381  1.00 84.29           C  
ANISOU 2727  C   GLU B 140    11623  10200  10204   -121    395   -356       C  
ATOM   2728  O   GLU B 140      12.778 -29.106 -40.466  1.00 84.92           O  
ANISOU 2728  O   GLU B 140    11837  10235  10194   -123    373   -375       O  
ATOM   2729  CB  GLU B 140      10.407 -30.283 -41.844  1.00 92.17           C  
ANISOU 2729  CB  GLU B 140    12597  11236  11189    -20    603   -374       C  
ATOM   2730  CG  GLU B 140      10.064 -30.105 -43.318  1.00107.64           C  
ANISOU 2730  CG  GLU B 140    14441  13225  13234    -11    649   -381       C  
ATOM   2731  CD  GLU B 140       8.952 -30.990 -43.856  1.00131.83           C  
ANISOU 2731  CD  GLU B 140    17428  16324  16337     31    741   -367       C  
ATOM   2732  OE1 GLU B 140       9.064 -32.234 -43.743  1.00115.45           O  
ANISOU 2732  OE1 GLU B 140    15303  14275  14289     30    739   -340       O  
ATOM   2733  OE2 GLU B 140       7.981 -30.437 -44.422  1.00129.70           O  
ANISOU 2733  OE2 GLU B 140    17147  16056  16077     62    812   -379       O  
ATOM   2734  N   SER B 141      13.976 -29.982 -42.151  1.00 71.94           N  
ANISOU 2734  N   SER B 141     9963   8647   8724   -162    329   -338       N  
ATOM   2735  CA  SER B 141      15.079 -29.022 -42.004  1.00 68.96           C  
ANISOU 2735  CA  SER B 141     9624   8230   8348   -214    224   -337       C  
ATOM   2736  C   SER B 141      14.791 -27.688 -42.732  1.00 65.25           C  
ANISOU 2736  C   SER B 141     9166   7746   7881   -208    247   -371       C  
ATOM   2737  O   SER B 141      15.391 -26.672 -42.385  1.00 62.89           O  
ANISOU 2737  O   SER B 141     8941   7403   7552   -242    171   -379       O  
ATOM   2738  CB  SER B 141      16.398 -29.629 -42.487  1.00 72.15           C  
ANISOU 2738  CB  SER B 141     9916   8649   8850   -258    147   -294       C  
ATOM   2739  OG  SER B 141      16.250 -30.345 -43.700  1.00 82.80           O  
ANISOU 2739  OG  SER B 141    11128  10044  10287   -236    212   -284       O  
ATOM   2740  N   THR B 142      13.905 -27.700 -43.753  1.00 58.25           N  
ANISOU 2740  N   THR B 142     8207   6892   7032   -169    344   -387       N  
ATOM   2741  CA  THR B 142      13.546 -26.516 -44.522  1.00 56.72           C  
ANISOU 2741  CA  THR B 142     8014   6689   6849   -160    374   -416       C  
ATOM   2742  C   THR B 142      12.067 -26.181 -44.339  1.00 57.72           C  
ANISOU 2742  C   THR B 142     8200   6813   6916   -105    478   -444       C  
ATOM   2743  O   THR B 142      11.222 -27.067 -44.307  1.00 58.14           O  
ANISOU 2743  O   THR B 142     8224   6894   6971    -68    551   -435       O  
ATOM   2744  CB  THR B 142      13.924 -26.689 -45.977  1.00 56.70           C  
ANISOU 2744  CB  THR B 142     7871   6721   6950   -169    386   -404       C  
ATOM   2745  OG1 THR B 142      15.344 -26.748 -46.049  1.00 57.24           O  
ANISOU 2745  OG1 THR B 142     7897   6780   7072   -219    289   -375       O  
ATOM   2746  CG2 THR B 142      13.479 -25.529 -46.835  1.00 56.47           C  
ANISOU 2746  CG2 THR B 142     7836   6685   6933   -158    423   -432       C  
ATOM   2747  N   ALA B 143      11.773 -24.896 -44.212  1.00 49.98           N  
ANISOU 2747  N   ALA B 143     7304   5797   5891    -99    483   -473       N  
ATOM   2748  CA  ALA B 143      10.417 -24.398 -44.072  1.00 48.35           C  
ANISOU 2748  CA  ALA B 143     7155   5580   5635    -46    584   -496       C  
ATOM   2749  C   ALA B 143      10.164 -23.434 -45.204  1.00 48.46           C  
ANISOU 2749  C   ALA B 143     7117   5597   5698    -43    611   -514       C  
ATOM   2750  O   ALA B 143      11.100 -22.790 -45.667  1.00 47.48           O  
ANISOU 2750  O   ALA B 143     6972   5461   5606    -84    539   -518       O  
ATOM   2751  CB  ALA B 143      10.273 -23.677 -42.747  1.00 49.41           C  
ANISOU 2751  CB  ALA B 143     7459   5657   5657    -39    569   -516       C  
ATOM   2752  N   ALA B 144       8.910 -23.299 -45.625  1.00 42.92           N  
ANISOU 2752  N   ALA B 144     6397   4908   5003      5    713   -521       N  
ATOM   2753  CA  ALA B 144       8.547 -22.293 -46.615  1.00 42.26           C  
ANISOU 2753  CA  ALA B 144     6278   4821   4956     12    743   -538       C  
ATOM   2754  C   ALA B 144       7.531 -21.329 -46.014  1.00 43.51           C  
ANISOU 2754  C   ALA B 144     6547   4939   5047     54    811   -558       C  
ATOM   2755  O   ALA B 144       6.742 -21.685 -45.134  1.00 40.67           O  
ANISOU 2755  O   ALA B 144     6255   4568   4632     94    871   -552       O  
ATOM   2756  CB  ALA B 144       7.999 -22.926 -47.880  1.00 42.59           C  
ANISOU 2756  CB  ALA B 144     6187   4912   5083     26    797   -522       C  
ATOM   2757  N   LEU B 145       7.637 -20.082 -46.416  1.00 42.23           N  
ANISOU 2757  N   LEU B 145     6410   4750   4885     45    797   -581       N  
ATOM   2758  CA  LEU B 145       6.671 -19.063 -46.040  1.00 45.67           C  
ANISOU 2758  CA  LEU B 145     6939   5145   5269     87    869   -600       C  
ATOM   2759  C   LEU B 145       6.498 -18.125 -47.208  1.00 48.34           C  
ANISOU 2759  C   LEU B 145     7214   5486   5667     83    881   -610       C  
ATOM   2760  O   LEU B 145       7.243 -18.201 -48.187  1.00 49.48           O  
ANISOU 2760  O   LEU B 145     7261   5659   5879     44    827   -606       O  
ATOM   2761  CB  LEU B 145       6.976 -18.375 -44.691  1.00 49.30           C  
ANISOU 2761  CB  LEU B 145     7570   5540   5620     86    834   -623       C  
ATOM   2762  CG  LEU B 145       8.415 -17.974 -44.413  1.00 56.86           C  
ANISOU 2762  CG  LEU B 145     8573   6472   6560     22    702   -634       C  
ATOM   2763  CD1 LEU B 145       8.648 -16.531 -44.832  1.00 59.96           C  
ANISOU 2763  CD1 LEU B 145     9002   6825   6954      6    673   -660       C  
ATOM   2764  CD2 LEU B 145       8.739 -18.128 -42.941  1.00 58.15           C  
ANISOU 2764  CD2 LEU B 145     8886   6590   6620     17    660   -640       C  
ATOM   2765  N   GLY B 146       5.432 -17.373 -47.210  1.00 43.64           N  
ANISOU 2765  N   GLY B 146     6658   4868   5056    128    965   -618       N  
ATOM   2766  CA  GLY B 146       5.188 -16.519 -48.355  1.00 41.98           C  
ANISOU 2766  CA  GLY B 146     6382   4662   4906    125    981   -624       C  
ATOM   2767  C   GLY B 146       4.134 -15.474 -48.142  1.00 45.39           C  
ANISOU 2767  C   GLY B 146     6884   5053   5310    172   1064   -634       C  
ATOM   2768  O   GLY B 146       3.659 -15.277 -47.020  1.00 43.73           O  
ANISOU 2768  O   GLY B 146     6793   4801   5022    209   1109   -641       O  
ATOM   2769  N   CYS B 147       3.710 -14.874 -49.244  1.00 45.74           N  
ANISOU 2769  N   CYS B 147     6852   5108   5418    175   1091   -631       N  
ATOM   2770  CA  CYS B 147       2.659 -13.855 -49.278  1.00 48.41           C  
ANISOU 2770  CA  CYS B 147     7231   5410   5751    220   1174   -634       C  
ATOM   2771  C   CYS B 147       1.806 -14.046 -50.518  1.00 46.70           C  
ANISOU 2771  C   CYS B 147     6883   5232   5629    233   1227   -604       C  
ATOM   2772  O   CYS B 147       2.349 -14.140 -51.605  1.00 43.37           O  
ANISOU 2772  O   CYS B 147     6366   4844   5267    193   1173   -603       O  
ATOM   2773  CB  CYS B 147       3.260 -12.447 -49.240  1.00 51.74           C  
ANISOU 2773  CB  CYS B 147     7733   5785   6143    198   1124   -669       C  
ATOM   2774  SG  CYS B 147       3.662 -11.892 -47.568  1.00 59.28           S  
ANISOU 2774  SG  CYS B 147     8890   6666   6968    207   1101   -701       S  
ATOM   2775  N   LEU B 148       0.486 -14.016 -50.361  1.00 43.48           N  
ANISOU 2775  N   LEU B 148     6474   4813   5234    288   1330   -578       N  
ATOM   2776  CA  LEU B 148      -0.459 -14.033 -51.487  1.00 42.23           C  
ANISOU 2776  CA  LEU B 148     6201   4679   5166    302   1380   -544       C  
ATOM   2777  C   LEU B 148      -0.893 -12.552 -51.690  1.00 45.30           C  
ANISOU 2777  C   LEU B 148     6632   5024   5558    322   1417   -556       C  
ATOM   2778  O   LEU B 148      -1.429 -11.950 -50.774  1.00 45.40           O  
ANISOU 2778  O   LEU B 148     6745   4986   5517    367   1482   -560       O  
ATOM   2779  CB  LEU B 148      -1.673 -14.906 -51.137  1.00 41.58           C  
ANISOU 2779  CB  LEU B 148     6087   4605   5105    351   1471   -497       C  
ATOM   2780  CG  LEU B 148      -2.821 -14.991 -52.143  1.00 44.32           C  
ANISOU 2780  CG  LEU B 148     6323   4969   5547    369   1526   -451       C  
ATOM   2781  CD1 LEU B 148      -2.334 -15.506 -53.517  1.00 44.48           C  
ANISOU 2781  CD1 LEU B 148     6227   5039   5636    316   1452   -448       C  
ATOM   2782  CD2 LEU B 148      -3.929 -15.869 -51.587  1.00 43.69           C  
ANISOU 2782  CD2 LEU B 148     6222   4891   5486    417   1610   -399       C  
ATOM   2783  N   VAL B 149      -0.612 -11.985 -52.863  1.00 41.64           N  
ANISOU 2783  N   VAL B 149     6096   4575   5150    288   1375   -562       N  
ATOM   2784  CA  VAL B 149      -0.931 -10.602 -53.263  1.00 40.75           C  
ANISOU 2784  CA  VAL B 149     6004   4426   5052    298   1397   -572       C  
ATOM   2785  C   VAL B 149      -2.110 -10.749 -54.215  1.00 42.19           C  
ANISOU 2785  C   VAL B 149     6079   4629   5324    320   1458   -526       C  
ATOM   2786  O   VAL B 149      -1.928 -11.076 -55.379  1.00 39.04           O  
ANISOU 2786  O   VAL B 149     5578   4269   4988    284   1415   -514       O  
ATOM   2787  CB  VAL B 149       0.305  -9.942 -53.894  1.00 43.05           C  
ANISOU 2787  CB  VAL B 149     6291   4722   5346    241   1298   -608       C  
ATOM   2788  CG1 VAL B 149       0.030  -8.472 -54.225  1.00 43.68           C  
ANISOU 2788  CG1 VAL B 149     6401   4761   5436    250   1317   -621       C  
ATOM   2789  CG2 VAL B 149       1.499 -10.068 -52.955  1.00 42.20           C  
ANISOU 2789  CG2 VAL B 149     6275   4599   5162    213   1225   -642       C  
ATOM   2790  N   LYS B 150      -3.325 -10.613 -53.687  1.00 40.32           N  
ANISOU 2790  N   LYS B 150     5864   4361   5092    378   1559   -493       N  
ATOM   2791  CA  LYS B 150      -4.529 -10.961 -54.424  1.00 39.28           C  
ANISOU 2791  CA  LYS B 150     5626   4246   5051    400   1618   -435       C  
ATOM   2792  C   LYS B 150      -5.380  -9.822 -54.886  1.00 41.41           C  
ANISOU 2792  C   LYS B 150     5881   4482   5369    427   1674   -414       C  
ATOM   2793  O   LYS B 150      -5.645  -8.901 -54.134  1.00 43.02           O  
ANISOU 2793  O   LYS B 150     6179   4634   5532    467   1731   -426       O  
ATOM   2794  CB  LYS B 150      -5.378 -11.929 -53.558  1.00 41.36           C  
ANISOU 2794  CB  LYS B 150     5897   4509   5310    448   1694   -393       C  
ATOM   2795  CG  LYS B 150      -6.726 -12.355 -54.120  1.00 43.37           C  
ANISOU 2795  CG  LYS B 150     6046   4772   5661    475   1759   -321       C  
ATOM   2796  CD  LYS B 150      -7.265 -13.560 -53.410  1.00 42.01           C  
ANISOU 2796  CD  LYS B 150     5862   4611   5488    504   1806   -281       C  
ATOM   2797  CE  LYS B 150      -8.716 -13.860 -53.723  1.00 45.85           C  
ANISOU 2797  CE  LYS B 150     6259   5092   6071    541   1884   -200       C  
ATOM   2798  NZ  LYS B 150      -8.912 -14.308 -55.132  1.00 49.50           N  
ANISOU 2798  NZ  LYS B 150     6591   5592   6625    494   1822   -170       N  
ATOM   2799  N   ASP B 151      -5.888  -9.940 -56.126  1.00 37.87           N  
ANISOU 2799  N   ASP B 151     5316   4061   5013    407   1661   -377       N  
ATOM   2800  CA  ASP B 151      -6.915  -9.072 -56.672  1.00 38.81           C  
ANISOU 2800  CA  ASP B 151     5394   4153   5201    433   1718   -338       C  
ATOM   2801  C   ASP B 151      -6.460  -7.629 -56.896  1.00 44.22           C  
ANISOU 2801  C   ASP B 151     6131   4805   5865    424   1701   -378       C  
ATOM   2802  O   ASP B 151      -6.844  -6.733 -56.152  1.00 45.50           O  
ANISOU 2802  O   ASP B 151     6376   4914   5997    470   1769   -383       O  
ATOM   2803  CB  ASP B 151      -8.196  -9.104 -55.763  1.00 39.35           C  
ANISOU 2803  CB  ASP B 151     5486   4182   5284    507   1841   -285       C  
ATOM   2804  CG  ASP B 151      -9.017 -10.372 -55.806  1.00 43.01           C  
ANISOU 2804  CG  ASP B 151     5864   4671   5805    519   1871   -222       C  
ATOM   2805  OD1 ASP B 151      -8.719 -11.236 -56.624  1.00 44.13           O  
ANISOU 2805  OD1 ASP B 151     5926   4861   5981    471   1798   -216       O  
ATOM   2806  OD2 ASP B 151      -9.975 -10.484 -55.020  1.00 56.00           O  
ANISOU 2806  OD2 ASP B 151     7528   6286   7462    580   1971   -175       O  
ATOM   2807  N   TYR B 152      -5.575  -7.436 -57.860  1.00 40.54           N  
ANISOU 2807  N   TYR B 152     5626   4367   5410    366   1610   -407       N  
ATOM   2808  CA  TYR B 152      -5.125  -6.107 -58.221  1.00 40.55           C  
ANISOU 2808  CA  TYR B 152     5661   4342   5403    351   1584   -440       C  
ATOM   2809  C   TYR B 152      -5.152  -5.910 -59.726  1.00 44.47           C  
ANISOU 2809  C   TYR B 152     6053   4868   5976    309   1535   -421       C  
ATOM   2810  O   TYR B 152      -5.166  -6.863 -60.528  1.00 42.24           O  
ANISOU 2810  O   TYR B 152     5685   4631   5735    279   1497   -398       O  
ATOM   2811  CB  TYR B 152      -3.752  -5.782 -57.615  1.00 40.62           C  
ANISOU 2811  CB  TYR B 152     5765   4341   5326    323   1517   -504       C  
ATOM   2812  CG  TYR B 152      -2.642  -6.635 -58.165  1.00 40.18           C  
ANISOU 2812  CG  TYR B 152     5661   4339   5268    265   1422   -523       C  
ATOM   2813  CD1 TYR B 152      -1.937  -6.247 -59.302  1.00 40.67           C  
ANISOU 2813  CD1 TYR B 152     5666   4423   5363    216   1352   -535       C  
ATOM   2814  CD2 TYR B 152      -2.325  -7.861 -57.590  1.00 40.54           C  
ANISOU 2814  CD2 TYR B 152     5712   4412   5281    262   1408   -524       C  
ATOM   2815  CE1 TYR B 152      -0.993  -7.074 -59.884  1.00 38.41           C  
ANISOU 2815  CE1 TYR B 152     5329   4182   5081    169   1279   -544       C  
ATOM   2816  CE2 TYR B 152      -1.336  -8.686 -58.144  1.00 39.73           C  
ANISOU 2816  CE2 TYR B 152     5558   4355   5182    212   1328   -535       C  
ATOM   2817  CZ  TYR B 152      -0.683  -8.294 -59.295  1.00 39.55           C  
ANISOU 2817  CZ  TYR B 152     5479   4351   5195    168   1267   -545       C  
ATOM   2818  OH  TYR B 152       0.301  -9.088 -59.828  1.00 42.59           O  
ANISOU 2818  OH  TYR B 152     5820   4778   5586    125   1199   -553       O  
ATOM   2819  N   PHE B 153      -5.220  -4.639 -60.098  1.00 40.68           N  
ANISOU 2819  N   PHE B 153     5587   4358   5514    310   1541   -429       N  
ATOM   2820  CA  PHE B 153      -5.247  -4.241 -61.477  1.00 38.07           C  
ANISOU 2820  CA  PHE B 153     5172   4045   5248    274   1498   -414       C  
ATOM   2821  C   PHE B 153      -4.766  -2.809 -61.584  1.00 41.92           C  
ANISOU 2821  C   PHE B 153     5710   4498   5719    266   1482   -448       C  
ATOM   2822  O   PHE B 153      -5.185  -1.971 -60.809  1.00 39.72           O  
ANISOU 2822  O   PHE B 153     5504   4168   5419    309   1542   -454       O  
ATOM   2823  CB  PHE B 153      -6.651  -4.385 -62.074  1.00 39.56           C  
ANISOU 2823  CB  PHE B 153     5274   4231   5525    296   1552   -344       C  
ATOM   2824  CG  PHE B 153      -6.612  -4.126 -63.557  1.00 40.21           C  
ANISOU 2824  CG  PHE B 153     5272   4337   5669    250   1495   -328       C  
ATOM   2825  CD1 PHE B 153      -6.246  -5.131 -64.444  1.00 40.40           C  
ANISOU 2825  CD1 PHE B 153     5232   4408   5709    205   1430   -321       C  
ATOM   2826  CD2 PHE B 153      -6.769  -2.841 -64.054  1.00 41.31           C  
ANISOU 2826  CD2 PHE B 153     5410   4447   5838    250   1501   -327       C  
ATOM   2827  CE1 PHE B 153      -6.124  -4.869 -65.794  1.00 40.02           C  
ANISOU 2827  CE1 PHE B 153     5123   4378   5704    163   1377   -310       C  
ATOM   2828  CE2 PHE B 153      -6.669  -2.589 -65.407  1.00 42.35           C  
ANISOU 2828  CE2 PHE B 153     5473   4600   6019    206   1446   -313       C  
ATOM   2829  CZ  PHE B 153      -6.352  -3.597 -66.269  1.00 39.27           C  
ANISOU 2829  CZ  PHE B 153     5025   4256   5641    164   1385   -305       C  
ATOM   2830  N   PRO B 154      -3.887  -2.487 -62.543  1.00 41.54           N  
ANISOU 2830  N   PRO B 154     5629   4474   5682    214   1404   -470       N  
ATOM   2831  CA  PRO B 154      -3.204  -3.351 -63.512  1.00 40.59           C  
ANISOU 2831  CA  PRO B 154     5437   4408   5578    164   1332   -470       C  
ATOM   2832  C   PRO B 154      -1.912  -3.890 -62.930  1.00 42.06           C  
ANISOU 2832  C   PRO B 154     5672   4611   5699    140   1276   -513       C  
ATOM   2833  O   PRO B 154      -1.561  -3.655 -61.784  1.00 39.88           O  
ANISOU 2833  O   PRO B 154     5484   4306   5363    157   1285   -543       O  
ATOM   2834  CB  PRO B 154      -2.912  -2.360 -64.638  1.00 42.13           C  
ANISOU 2834  CB  PRO B 154     5596   4600   5810    132   1293   -472       C  
ATOM   2835  CG  PRO B 154      -2.572  -1.131 -63.917  1.00 46.87           C  
ANISOU 2835  CG  PRO B 154     6282   5154   6374    147   1302   -506       C  
ATOM   2836  CD  PRO B 154      -3.391  -1.111 -62.664  1.00 43.53           C  
ANISOU 2836  CD  PRO B 154     5926   4692   5923    204   1383   -500       C  
ATOM   2837  N   GLU B 155      -1.150  -4.532 -63.762  1.00 40.85           N  
ANISOU 2837  N   GLU B 155     5464   4500   5557     97   1215   -516       N  
ATOM   2838  CA  GLU B 155       0.204  -4.910 -63.388  1.00 40.23           C  
ANISOU 2838  CA  GLU B 155     5418   4436   5431     68   1155   -552       C  
ATOM   2839  C   GLU B 155       1.127  -3.679 -63.427  1.00 43.90           C  
ANISOU 2839  C   GLU B 155     5924   4874   5881     45   1110   -582       C  
ATOM   2840  O   GLU B 155       0.813  -2.699 -64.097  1.00 43.72           O  
ANISOU 2840  O   GLU B 155     5883   4837   5894     42   1116   -575       O  
ATOM   2841  CB  GLU B 155       0.730  -5.894 -64.393  1.00 39.73           C  
ANISOU 2841  CB  GLU B 155     5280   4421   5393     32   1111   -540       C  
ATOM   2842  CG  GLU B 155      -0.024  -7.204 -64.384  1.00 45.35           C  
ANISOU 2842  CG  GLU B 155     5953   5158   6118     47   1141   -511       C  
ATOM   2843  CD  GLU B 155       0.846  -8.304 -63.844  1.00 69.48           C  
ANISOU 2843  CD  GLU B 155     9024   8240   9137     36   1110   -527       C  
ATOM   2844  OE1 GLU B 155       1.270  -9.119 -64.686  1.00 42.76           O  
ANISOU 2844  OE1 GLU B 155     5586   4888   5771      9   1079   -518       O  
ATOM   2845  OE2 GLU B 155       1.243  -8.255 -62.653  1.00 60.18           O  
ANISOU 2845  OE2 GLU B 155     7913   7043   7908     48   1110   -550       O  
ATOM   2846  N   PRO B 156       2.297  -3.736 -62.794  1.00 40.94           N  
ANISOU 2846  N   PRO B 156     5598   4496   5462     23   1056   -612       N  
ATOM   2847  CA  PRO B 156       2.836  -4.827 -61.981  1.00 42.33           C  
ANISOU 2847  CA  PRO B 156     5799   4688   5597     20   1037   -621       C  
ATOM   2848  C   PRO B 156       2.774  -4.542 -60.495  1.00 45.82           C  
ANISOU 2848  C   PRO B 156     6352   5087   5972     47   1053   -644       C  
ATOM   2849  O   PRO B 156       2.456  -3.423 -60.092  1.00 46.13           O  
ANISOU 2849  O   PRO B 156     6455   5079   5994     65   1074   -658       O  
ATOM   2850  CB  PRO B 156       4.303  -4.850 -62.446  1.00 43.05           C  
ANISOU 2850  CB  PRO B 156     5866   4797   5695    -28    956   -631       C  
ATOM   2851  CG  PRO B 156       4.631  -3.372 -62.618  1.00 46.50           C  
ANISOU 2851  CG  PRO B 156     6334   5196   6137    -41    931   -646       C  
ATOM   2852  CD  PRO B 156       3.295  -2.657 -62.892  1.00 42.22           C  
ANISOU 2852  CD  PRO B 156     5791   4634   5618     -7    999   -635       C  
ATOM   2853  N   VAL B 157       3.176  -5.534 -59.690  1.00 42.83           N  
ANISOU 2853  N   VAL B 157     6000   4720   5553     46   1038   -650       N  
ATOM   2854  CA  VAL B 157       3.391  -5.367 -58.253  1.00 43.59           C  
ANISOU 2854  CA  VAL B 157     6213   4775   5575     62   1034   -674       C  
ATOM   2855  C   VAL B 157       4.825  -5.774 -58.011  1.00 48.80           C  
ANISOU 2855  C   VAL B 157     6881   5446   6214     16    943   -688       C  
ATOM   2856  O   VAL B 157       5.306  -6.683 -58.676  1.00 46.75           O  
ANISOU 2856  O   VAL B 157     6538   5234   5992     -8    916   -671       O  
ATOM   2857  CB  VAL B 157       2.454  -6.116 -57.281  1.00 47.01           C  
ANISOU 2857  CB  VAL B 157     6689   5202   5970    110   1106   -665       C  
ATOM   2858  CG1 VAL B 157       1.016  -5.701 -57.466  1.00 47.12           C  
ANISOU 2858  CG1 VAL B 157     6691   5200   6014    158   1201   -642       C  
ATOM   2859  CG2 VAL B 157       2.634  -7.610 -57.340  1.00 47.28           C  
ANISOU 2859  CG2 VAL B 157     6664   5287   6014    100   1095   -647       C  
ATOM   2860  N   THR B 158       5.507  -5.120 -57.063  1.00 47.07           N  
ANISOU 2860  N   THR B 158     6765   5180   5940      3    895   -714       N  
ATOM   2861  CA  THR B 158       6.858  -5.531 -56.706  1.00 47.28           C  
ANISOU 2861  CA  THR B 158     6801   5211   5951    -42    803   -718       C  
ATOM   2862  C   THR B 158       6.806  -6.144 -55.330  1.00 47.67           C  
ANISOU 2862  C   THR B 158     6945   5240   5926    -25    806   -729       C  
ATOM   2863  O   THR B 158       5.996  -5.735 -54.499  1.00 45.31           O  
ANISOU 2863  O   THR B 158     6743   4901   5572     15    861   -744       O  
ATOM   2864  CB  THR B 158       7.847  -4.368 -56.748  1.00 60.37           C  
ANISOU 2864  CB  THR B 158     8497   6831   7611    -82    722   -733       C  
ATOM   2865  OG1 THR B 158       7.566  -3.477 -55.683  1.00 59.80           O  
ANISOU 2865  OG1 THR B 158     8560   6693   7469    -64    727   -761       O  
ATOM   2866  CG2 THR B 158       7.840  -3.642 -58.079  1.00 61.25           C  
ANISOU 2866  CG2 THR B 158     8523   6957   7791    -96    725   -722       C  
ATOM   2867  N   VAL B 159       7.654  -7.139 -55.091  1.00 45.33           N  
ANISOU 2867  N   VAL B 159     6624   4971   5628    -53    752   -719       N  
ATOM   2868  CA  VAL B 159       7.744  -7.779 -53.774  1.00 45.85           C  
ANISOU 2868  CA  VAL B 159     6779   5018   5622    -43    742   -726       C  
ATOM   2869  C   VAL B 159       9.190  -7.934 -53.373  1.00 47.74           C  
ANISOU 2869  C   VAL B 159     7037   5249   5854    -98    630   -724       C  
ATOM   2870  O   VAL B 159      10.031  -8.349 -54.179  1.00 47.98           O  
ANISOU 2870  O   VAL B 159     6965   5316   5949   -133    582   -702       O  
ATOM   2871  CB  VAL B 159       7.037  -9.171 -53.678  1.00 48.51           C  
ANISOU 2871  CB  VAL B 159     7066   5401   5963    -12    806   -707       C  
ATOM   2872  CG1 VAL B 159       6.964  -9.653 -52.220  1.00 47.77           C  
ANISOU 2872  CG1 VAL B 159     7083   5280   5786      6    809   -716       C  
ATOM   2873  CG2 VAL B 159       5.640  -9.126 -54.293  1.00 48.53           C  
ANISOU 2873  CG2 VAL B 159     7021   5420   5999     35    909   -695       C  
ATOM   2874  N   SER B 160       9.449  -7.666 -52.111  1.00 43.13           N  
ANISOU 2874  N   SER B 160     6584   4614   5192   -102    591   -743       N  
ATOM   2875  CA  SER B 160      10.726  -7.890 -51.480  1.00 44.05           C  
ANISOU 2875  CA  SER B 160     6735   4712   5291   -152    479   -737       C  
ATOM   2876  C   SER B 160      10.457  -8.486 -50.081  1.00 48.39           C  
ANISOU 2876  C   SER B 160     7401   5236   5748   -132    488   -747       C  
ATOM   2877  O   SER B 160       9.337  -8.470 -49.585  1.00 46.64           O  
ANISOU 2877  O   SER B 160     7246   5001   5474    -79    579   -762       O  
ATOM   2878  CB  SER B 160      11.547  -6.597 -51.422  1.00 46.89           C  
ANISOU 2878  CB  SER B 160     7153   5016   5648   -195    389   -748       C  
ATOM   2879  OG  SER B 160      11.023  -5.697 -50.469  1.00 55.98           O  
ANISOU 2879  OG  SER B 160     8460   6099   6711   -173    404   -782       O  
ATOM   2880  N   TRP B 161      11.487  -9.045 -49.484  1.00 47.00           N  
ANISOU 2880  N   TRP B 161     7242   5055   5559   -174    396   -733       N  
ATOM   2881  CA  TRP B 161      11.432  -9.670 -48.182  1.00 46.92           C  
ANISOU 2881  CA  TRP B 161     7340   5022   5466   -165    386   -738       C  
ATOM   2882  C   TRP B 161      12.420  -8.961 -47.247  1.00 52.29           C  
ANISOU 2882  C   TRP B 161     8147   5632   6088   -214    263   -748       C  
ATOM   2883  O   TRP B 161      13.559  -8.693 -47.643  1.00 51.00           O  
ANISOU 2883  O   TRP B 161     7930   5464   5981   -272    160   -728       O  
ATOM   2884  CB  TRP B 161      11.777 -11.153 -48.309  1.00 44.43           C  
ANISOU 2884  CB  TRP B 161     6924   4766   5190   -173    380   -706       C  
ATOM   2885  CG  TRP B 161      10.667 -11.924 -48.918  1.00 44.13           C  
ANISOU 2885  CG  TRP B 161     6799   4783   5184   -122    498   -699       C  
ATOM   2886  CD1 TRP B 161      10.415 -12.122 -50.241  1.00 45.30           C  
ANISOU 2886  CD1 TRP B 161     6811   4983   5419   -115    542   -685       C  
ATOM   2887  CD2 TRP B 161       9.567 -12.467 -48.213  1.00 44.41           C  
ANISOU 2887  CD2 TRP B 161     6893   4821   5162    -68    588   -705       C  
ATOM   2888  NE1 TRP B 161       9.260 -12.833 -50.400  1.00 43.63           N  
ANISOU 2888  NE1 TRP B 161     6562   4804   5209    -65    644   -680       N  
ATOM   2889  CE2 TRP B 161       8.704 -13.050 -49.168  1.00 47.18           C  
ANISOU 2889  CE2 TRP B 161     7125   5225   5575    -34    678   -690       C  
ATOM   2890  CE3 TRP B 161       9.266 -12.596 -46.856  1.00 46.51           C  
ANISOU 2890  CE3 TRP B 161     7298   5046   5329    -46    600   -718       C  
ATOM   2891  CZ2 TRP B 161       7.522 -13.703 -48.804  1.00 46.68           C  
ANISOU 2891  CZ2 TRP B 161     7073   5176   5488     21    778   -683       C  
ATOM   2892  CZ3 TRP B 161       8.102 -13.259 -46.491  1.00 48.92           C  
ANISOU 2892  CZ3 TRP B 161     7615   5367   5607     13    708   -712       C  
ATOM   2893  CH2 TRP B 161       7.247 -13.804 -47.459  1.00 48.67           C  
ANISOU 2893  CH2 TRP B 161     7455   5389   5648     45    795   -693       C  
ATOM   2894  N   ASN B 162      11.971  -8.644 -46.027  1.00 51.21           N  
ANISOU 2894  N   ASN B 162     8180   5436   5840   -191    275   -776       N  
ATOM   2895  CA  ASN B 162      12.796  -7.963 -45.008  1.00 52.71           C  
ANISOU 2895  CA  ASN B 162     8522   5547   5956   -237    158   -789       C  
ATOM   2896  C   ASN B 162      13.548  -6.739 -45.581  1.00 57.79           C  
ANISOU 2896  C   ASN B 162     9156   6155   6646   -285     71   -791       C  
ATOM   2897  O   ASN B 162      14.747  -6.570 -45.383  1.00 58.12           O  
ANISOU 2897  O   ASN B 162     9206   6170   6708   -351    -64   -771       O  
ATOM   2898  CB  ASN B 162      13.723  -9.004 -44.350  1.00 49.10           C  
ANISOU 2898  CB  ASN B 162     8064   5100   5493   -280     64   -759       C  
ATOM   2899  CG  ASN B 162      12.928 -10.006 -43.565  1.00 60.21           C  
ANISOU 2899  CG  ASN B 162     9522   6524   6831   -231    146   -763       C  
ATOM   2900  OD1 ASN B 162      11.715  -9.869 -43.411  1.00 60.27           O  
ANISOU 2900  OD1 ASN B 162     9578   6530   6794   -165    269   -786       O  
ATOM   2901  ND2 ASN B 162      13.573 -11.035 -43.050  1.00 52.00           N  
ANISOU 2901  ND2 ASN B 162     8467   5502   5789   -260     84   -736       N  
ATOM   2902  N   SER B 163      12.814  -5.948 -46.375  1.00 54.48           N  
ANISOU 2902  N   SER B 163     8702   5742   6257   -251    151   -809       N  
ATOM   2903  CA  SER B 163      13.266  -4.723 -47.027  1.00 54.10           C  
ANISOU 2903  CA  SER B 163     8639   5664   6255   -283     98   -814       C  
ATOM   2904  C   SER B 163      14.458  -4.889 -47.957  1.00 59.79           C  
ANISOU 2904  C   SER B 163     9208   6422   7088   -344      5   -772       C  
ATOM   2905  O   SER B 163      15.290  -3.985 -48.061  1.00 62.19           O  
ANISOU 2905  O   SER B 163     9533   6682   7416   -394    -95   -766       O  
ATOM   2906  CB  SER B 163      13.555  -3.657 -45.976  1.00 56.93           C  
ANISOU 2906  CB  SER B 163     9192   5922   6517   -305     20   -844       C  
ATOM   2907  OG  SER B 163      12.512  -3.616 -45.015  1.00 65.37           O  
ANISOU 2907  OG  SER B 163    10412   6951   7473   -245    110   -879       O  
ATOM   2908  N   GLY B 164      14.527  -6.026 -48.640  1.00 55.00           N  
ANISOU 2908  N   GLY B 164     8453   5892   6553   -338     42   -741       N  
ATOM   2909  CA  GLY B 164      15.600  -6.320 -49.577  1.00 53.29           C  
ANISOU 2909  CA  GLY B 164     8086   5716   6447   -385    -23   -697       C  
ATOM   2910  C   GLY B 164      16.773  -7.051 -48.965  1.00 57.06           C  
ANISOU 2910  C   GLY B 164     8557   6185   6936   -437   -135   -660       C  
ATOM   2911  O   GLY B 164      17.663  -7.498 -49.700  1.00 58.09           O  
ANISOU 2911  O   GLY B 164     8554   6353   7165   -470   -177   -615       O  
ATOM   2912  N   ALA B 165      16.781  -7.202 -47.626  1.00 52.89           N  
ANISOU 2912  N   ALA B 165     8174   5610   6312   -444   -181   -675       N  
ATOM   2913  CA  ALA B 165      17.840  -7.902 -46.911  1.00 54.10           C  
ANISOU 2913  CA  ALA B 165     8337   5750   6468   -495   -293   -639       C  
ATOM   2914  C   ALA B 165      17.770  -9.409 -47.182  1.00 61.89           C  
ANISOU 2914  C   ALA B 165     9207   6811   7496   -474   -237   -612       C  
ATOM   2915  O   ALA B 165      18.810 -10.076 -47.144  1.00 63.92           O  
ANISOU 2915  O   ALA B 165     9396   7081   7812   -517   -319   -565       O  
ATOM   2916  CB  ALA B 165      17.720  -7.643 -45.411  1.00 55.32           C  
ANISOU 2916  CB  ALA B 165     8695   5831   6495   -502   -347   -667       C  
ATOM   2917  N   LEU B 166      16.554  -9.958 -47.382  1.00 57.03           N  
ANISOU 2917  N   LEU B 166     8577   6240   6853   -408   -102   -637       N  
ATOM   2918  CA  LEU B 166      16.384 -11.387 -47.667  1.00 55.56           C  
ANISOU 2918  CA  LEU B 166     8284   6121   6704   -385    -44   -614       C  
ATOM   2919  C   LEU B 166      16.135 -11.574 -49.169  1.00 57.42           C  
ANISOU 2919  C   LEU B 166     8360   6421   7038   -364     34   -602       C  
ATOM   2920  O   LEU B 166      15.157 -11.062 -49.710  1.00 56.21           O  
ANISOU 2920  O   LEU B 166     8205   6278   6876   -323    123   -629       O  
ATOM   2921  CB  LEU B 166      15.242 -11.972 -46.823  1.00 55.10           C  
ANISOU 2921  CB  LEU B 166     8318   6067   6552   -330     45   -642       C  
ATOM   2922  CG  LEU B 166      15.013 -13.473 -46.917  1.00 57.79           C  
ANISOU 2922  CG  LEU B 166     8570   6470   6918   -307     99   -620       C  
ATOM   2923  CD1 LEU B 166      16.258 -14.254 -46.524  1.00 56.07           C  
ANISOU 2923  CD1 LEU B 166     8317   6254   6733   -360     -8   -578       C  
ATOM   2924  CD2 LEU B 166      13.871 -13.860 -46.064  1.00 62.88           C  
ANISOU 2924  CD2 LEU B 166     9312   7109   7471   -254    185   -645       C  
ATOM   2925  N   THR B 167      17.097 -12.191 -49.847  1.00 53.76           N  
ANISOU 2925  N   THR B 167     7767   5991   6666   -395     -8   -557       N  
ATOM   2926  CA  THR B 167      17.031 -12.469 -51.286  1.00 52.93           C  
ANISOU 2926  CA  THR B 167     7515   5943   6654   -380     57   -540       C  
ATOM   2927  C   THR B 167      17.209 -13.954 -51.617  1.00 56.29           C  
ANISOU 2927  C   THR B 167     7837   6424   7125   -369     91   -509       C  
ATOM   2928  O   THR B 167      16.608 -14.420 -52.589  1.00 56.74           O  
ANISOU 2928  O   THR B 167     7810   6528   7219   -335    179   -511       O  
ATOM   2929  CB  THR B 167      18.074 -11.649 -52.013  1.00 59.69           C  
ANISOU 2929  CB  THR B 167     8307   6782   7589   -424    -13   -511       C  
ATOM   2930  OG1 THR B 167      19.331 -11.874 -51.375  1.00 63.63           O  
ANISOU 2930  OG1 THR B 167     8809   7253   8113   -477   -130   -470       O  
ATOM   2931  CG2 THR B 167      17.723 -10.175 -52.038  1.00 55.91           C  
ANISOU 2931  CG2 THR B 167     7905   6258   7079   -426    -23   -544       C  
ATOM   2932  N   SER B 168      18.057 -14.674 -50.863  1.00 52.08           N  
ANISOU 2932  N   SER B 168     7311   5883   6596   -400     16   -478       N  
ATOM   2933  CA  SER B 168      18.324 -16.089 -51.096  1.00 52.80           C  
ANISOU 2933  CA  SER B 168     7309   6020   6733   -392     41   -446       C  
ATOM   2934  C   SER B 168      17.103 -16.939 -50.762  1.00 56.75           C  
ANISOU 2934  C   SER B 168     7841   6550   7171   -341    134   -474       C  
ATOM   2935  O   SER B 168      16.483 -16.754 -49.717  1.00 57.51           O  
ANISOU 2935  O   SER B 168     8055   6619   7178   -327    137   -503       O  
ATOM   2936  CB  SER B 168      19.506 -16.568 -50.261  1.00 57.87           C  
ANISOU 2936  CB  SER B 168     7959   6638   7392   -439    -68   -403       C  
ATOM   2937  OG  SER B 168      20.652 -15.790 -50.565  1.00 77.74           O  
ANISOU 2937  OG  SER B 168    10439   9124   9976   -489   -159   -367       O  
ATOM   2938  N   GLY B 169      16.786 -17.860 -51.661  1.00 51.06           N  
ANISOU 2938  N   GLY B 169     7017   5882   6500   -313    208   -463       N  
ATOM   2939  CA  GLY B 169      15.653 -18.757 -51.529  1.00 48.12           C  
ANISOU 2939  CA  GLY B 169     6651   5541   6089   -267    297   -481       C  
ATOM   2940  C   GLY B 169      14.322 -18.119 -51.863  1.00 46.65           C  
ANISOU 2940  C   GLY B 169     6500   5358   5867   -226    382   -519       C  
ATOM   2941  O   GLY B 169      13.299 -18.733 -51.609  1.00 43.97           O  
ANISOU 2941  O   GLY B 169     6177   5036   5492   -187    452   -531       O  
ATOM   2942  N   VAL B 170      14.306 -16.878 -52.391  1.00 44.20           N  
ANISOU 2942  N   VAL B 170     6200   5026   5567   -233    376   -534       N  
ATOM   2943  CA  VAL B 170      13.072 -16.164 -52.724  1.00 42.16           C  
ANISOU 2943  CA  VAL B 170     5972   4766   5282   -196    454   -566       C  
ATOM   2944  C   VAL B 170      12.620 -16.516 -54.161  1.00 44.38           C  
ANISOU 2944  C   VAL B 170     6141   5091   5629   -177    521   -557       C  
ATOM   2945  O   VAL B 170      13.423 -16.413 -55.093  1.00 45.18           O  
ANISOU 2945  O   VAL B 170     6165   5206   5796   -202    494   -538       O  
ATOM   2946  CB  VAL B 170      13.247 -14.617 -52.577  1.00 45.43           C  
ANISOU 2946  CB  VAL B 170     6458   5131   5673   -213    414   -587       C  
ATOM   2947  CG1 VAL B 170      11.982 -13.868 -53.013  1.00 44.78           C  
ANISOU 2947  CG1 VAL B 170     6396   5045   5573   -173    499   -614       C  
ATOM   2948  CG2 VAL B 170      13.624 -14.232 -51.154  1.00 45.55           C  
ANISOU 2948  CG2 VAL B 170     6603   5093   5613   -232    345   -598       C  
ATOM   2949  N   HIS B 171      11.330 -16.827 -54.344  1.00 38.78           N  
ANISOU 2949  N   HIS B 171     5431   4401   4903   -135    606   -569       N  
ATOM   2950  CA  HIS B 171      10.713 -16.996 -55.665  1.00 38.00           C  
ANISOU 2950  CA  HIS B 171     5246   4335   4856   -118    666   -564       C  
ATOM   2951  C   HIS B 171       9.482 -16.121 -55.670  1.00 41.69           C  
ANISOU 2951  C   HIS B 171     5759   4786   5296    -87    726   -584       C  
ATOM   2952  O   HIS B 171       8.558 -16.365 -54.894  1.00 40.23           O  
ANISOU 2952  O   HIS B 171     5627   4593   5066    -54    772   -590       O  
ATOM   2953  CB  HIS B 171      10.275 -18.431 -56.003  1.00 37.72           C  
ANISOU 2953  CB  HIS B 171     5150   4341   4843    -99    711   -546       C  
ATOM   2954  CG  HIS B 171      11.399 -19.379 -56.137  1.00 40.63           C  
ANISOU 2954  CG  HIS B 171     5464   4727   5246   -124    667   -523       C  
ATOM   2955  ND1 HIS B 171      12.337 -19.239 -57.138  1.00 42.89           N  
ANISOU 2955  ND1 HIS B 171     5682   5022   5593   -148    640   -507       N  
ATOM   2956  CD2 HIS B 171      11.777 -20.381 -55.322  1.00 40.41           C  
ANISOU 2956  CD2 HIS B 171     5446   4706   5203   -127    645   -509       C  
ATOM   2957  CE1 HIS B 171      13.209 -20.214 -56.949  1.00 41.33           C  
ANISOU 2957  CE1 HIS B 171     5449   4837   5419   -162    610   -482       C  
ATOM   2958  NE2 HIS B 171      12.890 -20.940 -55.883  1.00 40.97           N  
ANISOU 2958  NE2 HIS B 171     5446   4792   5330   -151    610   -484       N  
ATOM   2959  N   THR B 172       9.486 -15.088 -56.514  1.00 38.03           N  
ANISOU 2959  N   THR B 172     5275   4313   4862    -95    725   -591       N  
ATOM   2960  CA  THR B 172       8.332 -14.246 -56.724  1.00 37.24           C  
ANISOU 2960  CA  THR B 172     5200   4198   4751    -66    784   -605       C  
ATOM   2961  C   THR B 172       7.791 -14.759 -57.998  1.00 38.41           C  
ANISOU 2961  C   THR B 172     5256   4383   4956    -57    827   -588       C  
ATOM   2962  O   THR B 172       8.487 -14.704 -59.003  1.00 37.45           O  
ANISOU 2962  O   THR B 172     5072   4277   4879    -82    800   -579       O  
ATOM   2963  CB  THR B 172       8.676 -12.756 -56.738  1.00 42.83           C  
ANISOU 2963  CB  THR B 172     5955   4867   5452    -82    751   -623       C  
ATOM   2964  OG1 THR B 172       9.040 -12.393 -55.398  1.00 50.76           O  
ANISOU 2964  OG1 THR B 172     7065   5830   6391    -87    711   -639       O  
ATOM   2965  CG2 THR B 172       7.476 -11.894 -57.152  1.00 41.37           C  
ANISOU 2965  CG2 THR B 172     5779   4668   5270    -51    817   -632       C  
ATOM   2966  N   PHE B 173       6.559 -15.262 -57.980  1.00 37.03           N  
ANISOU 2966  N   PHE B 173     5073   4219   4778    -23    892   -580       N  
ATOM   2967  CA  PHE B 173       5.964 -15.879 -59.166  1.00 36.14           C  
ANISOU 2967  CA  PHE B 173     4879   4138   4716    -18    926   -561       C  
ATOM   2968  C   PHE B 173       5.364 -14.913 -60.144  1.00 38.61           C  
ANISOU 2968  C   PHE B 173     5167   4444   5061    -16    949   -560       C  
ATOM   2969  O   PHE B 173       4.708 -13.992 -59.722  1.00 38.87           O  
ANISOU 2969  O   PHE B 173     5245   4448   5075      4    977   -568       O  
ATOM   2970  CB  PHE B 173       4.863 -16.876 -58.745  1.00 36.95           C  
ANISOU 2970  CB  PHE B 173     4976   4253   4811     14    979   -543       C  
ATOM   2971  CG  PHE B 173       5.413 -18.142 -58.147  1.00 37.64           C  
ANISOU 2971  CG  PHE B 173     5060   4359   4883      9    958   -537       C  
ATOM   2972  CD1 PHE B 173       5.775 -18.197 -56.808  1.00 40.01           C  
ANISOU 2972  CD1 PHE B 173     5431   4641   5129     14    942   -547       C  
ATOM   2973  CD2 PHE B 173       5.711 -19.235 -58.953  1.00 36.66           C  
ANISOU 2973  CD2 PHE B 173     4868   4266   4796     -5    948   -521       C  
ATOM   2974  CE1 PHE B 173       6.357 -19.344 -56.277  1.00 40.47           C  
ANISOU 2974  CE1 PHE B 173     5484   4717   5177      5    917   -538       C  
ATOM   2975  CE2 PHE B 173       6.249 -20.387 -58.409  1.00 38.62           C  
ANISOU 2975  CE2 PHE B 173     5112   4529   5033     -9    929   -513       C  
ATOM   2976  CZ  PHE B 173       6.635 -20.420 -57.094  1.00 37.43           C  
ANISOU 2976  CZ  PHE B 173     5023   4364   4835     -6    910   -521       C  
ATOM   2977  N   PRO B 174       5.421 -15.178 -61.459  1.00 34.88           N  
ANISOU 2977  N   PRO B 174     4624   3993   4634    -31    946   -547       N  
ATOM   2978  CA  PRO B 174       4.613 -14.375 -62.398  1.00 33.86           C  
ANISOU 2978  CA  PRO B 174     4470   3858   4536    -26    973   -541       C  
ATOM   2979  C   PRO B 174       3.143 -14.337 -61.956  1.00 37.25           C  
ANISOU 2979  C   PRO B 174     4915   4275   4963     10   1031   -527       C  
ATOM   2980  O   PRO B 174       2.628 -15.326 -61.448  1.00 34.01           O  
ANISOU 2980  O   PRO B 174     4503   3875   4546     28   1055   -512       O  
ATOM   2981  CB  PRO B 174       4.713 -15.162 -63.712  1.00 34.60           C  
ANISOU 2981  CB  PRO B 174     4497   3980   4669    -42    967   -523       C  
ATOM   2982  CG  PRO B 174       5.955 -15.921 -63.609  1.00 39.32           C  
ANISOU 2982  CG  PRO B 174     5084   4593   5261    -61    930   -527       C  
ATOM   2983  CD  PRO B 174       6.142 -16.257 -62.152  1.00 35.68           C  
ANISOU 2983  CD  PRO B 174     4672   4124   4760    -50    924   -535       C  
ATOM   2984  N   ALA B 175       2.447 -13.238 -62.202  1.00 35.78           N  
ANISOU 2984  N   ALA B 175     4738   4066   4791     21   1057   -525       N  
ATOM   2985  CA  ALA B 175       1.055 -13.144 -61.790  1.00 35.13           C  
ANISOU 2985  CA  ALA B 175     4664   3967   4716     59   1119   -504       C  
ATOM   2986  C   ALA B 175       0.133 -14.064 -62.595  1.00 36.83           C  
ANISOU 2986  C   ALA B 175     4811   4204   4980     61   1138   -466       C  
ATOM   2987  O   ALA B 175       0.465 -14.463 -63.693  1.00 35.68           O  
ANISOU 2987  O   ALA B 175     4618   4079   4860     33   1105   -461       O  
ATOM   2988  CB  ALA B 175       0.588 -11.688 -61.889  1.00 35.75           C  
ANISOU 2988  CB  ALA B 175     4766   4013   4804     71   1142   -508       C  
ATOM   2989  N   VAL B 176      -1.021 -14.395 -62.025  1.00 34.20           N  
ANISOU 2989  N   VAL B 176     4477   3860   4656     95   1191   -437       N  
ATOM   2990  CA  VAL B 176      -2.091 -15.140 -62.696  1.00 31.97           C  
ANISOU 2990  CA  VAL B 176     4133   3588   4428     98   1209   -392       C  
ATOM   2991  C   VAL B 176      -3.227 -14.160 -62.914  1.00 36.23           C  
ANISOU 2991  C   VAL B 176     4658   4098   5008    120   1253   -363       C  
ATOM   2992  O   VAL B 176      -3.416 -13.221 -62.129  1.00 34.03           O  
ANISOU 2992  O   VAL B 176     4429   3791   4708    149   1292   -373       O  
ATOM   2993  CB  VAL B 176      -2.617 -16.408 -61.988  1.00 33.17           C  
ANISOU 2993  CB  VAL B 176     4276   3750   4579    118   1234   -366       C  
ATOM   2994  CG1 VAL B 176      -1.578 -17.536 -62.005  1.00 31.94           C  
ANISOU 2994  CG1 VAL B 176     4117   3623   4395     93   1187   -387       C  
ATOM   2995  CG2 VAL B 176      -3.097 -16.112 -60.558  1.00 33.25           C  
ANISOU 2995  CG2 VAL B 176     4343   3735   4556    164   1295   -363       C  
ATOM   2996  N   LEU B 177      -3.963 -14.359 -63.984  1.00 34.25           N  
ANISOU 2996  N   LEU B 177     4344   3851   4816    105   1244   -325       N  
ATOM   2997  CA  LEU B 177      -5.088 -13.491 -64.301  1.00 35.22           C  
ANISOU 2997  CA  LEU B 177     4442   3948   4993    122   1281   -287       C  
ATOM   2998  C   LEU B 177      -6.347 -14.253 -63.995  1.00 37.87           C  
ANISOU 2998  C   LEU B 177     4738   4276   5375    148   1322   -228       C  
ATOM   2999  O   LEU B 177      -6.585 -15.290 -64.577  1.00 36.39           O  
ANISOU 2999  O   LEU B 177     4505   4105   5216    126   1289   -202       O  
ATOM   3000  CB  LEU B 177      -5.001 -13.066 -65.760  1.00 35.03           C  
ANISOU 3000  CB  LEU B 177     4378   3929   5004     84   1233   -282       C  
ATOM   3001  CG  LEU B 177      -6.062 -12.100 -66.339  1.00 39.71           C  
ANISOU 3001  CG  LEU B 177     4935   4494   5659     91   1256   -241       C  
ATOM   3002  CD1 LEU B 177      -6.337 -10.862 -65.447  1.00 35.44           C  
ANISOU 3002  CD1 LEU B 177     4436   3919   5109    131   1316   -249       C  
ATOM   3003  CD2 LEU B 177      -5.618 -11.643 -67.706  1.00 41.92           C  
ANISOU 3003  CD2 LEU B 177     5195   4782   5952     48   1200   -251       C  
ATOM   3004  N   GLN B 178      -7.126 -13.767 -63.039  1.00 37.03           N  
ANISOU 3004  N   GLN B 178     4653   4141   5277    195   1394   -204       N  
ATOM   3005  CA  GLN B 178      -8.381 -14.391 -62.641  1.00 38.03           C  
ANISOU 3005  CA  GLN B 178     4738   4255   5457    226   1446   -138       C  
ATOM   3006  C   GLN B 178      -9.499 -14.073 -63.649  1.00 40.65           C  
ANISOU 3006  C   GLN B 178     4994   4569   5882    217   1444    -74       C  
ATOM   3007  O   GLN B 178      -9.369 -13.157 -64.459  1.00 37.90           O  
ANISOU 3007  O   GLN B 178     4638   4214   5550    196   1419    -84       O  
ATOM   3008  CB  GLN B 178      -8.747 -13.962 -61.209  1.00 40.29           C  
ANISOU 3008  CB  GLN B 178     5083   4511   5713    286   1535   -136       C  
ATOM   3009  CG  GLN B 178      -7.625 -14.302 -60.208  1.00 43.77           C  
ANISOU 3009  CG  GLN B 178     5606   4966   6059    290   1525   -197       C  
ATOM   3010  CD  GLN B 178      -7.836 -13.627 -58.882  1.00 54.63           C  
ANISOU 3010  CD  GLN B 178     7065   6305   7388    345   1604   -206       C  
ATOM   3011  OE1 GLN B 178      -8.411 -14.199 -57.952  1.00 52.97           O  
ANISOU 3011  OE1 GLN B 178     6871   6086   7172    385   1664   -176       O  
ATOM   3012  NE2 GLN B 178      -7.396 -12.379 -58.776  1.00 39.37           N  
ANISOU 3012  NE2 GLN B 178     5191   4347   5419    349   1608   -246       N  
ATOM   3013  N   SER B 179     -10.577 -14.848 -63.613  1.00 39.52           N  
ANISOU 3013  N   SER B 179     4793   4419   5805    229   1465     -4       N  
ATOM   3014  CA  SER B 179     -11.731 -14.664 -64.515  1.00 41.19           C  
ANISOU 3014  CA  SER B 179     4925   4610   6115    217   1456     71       C  
ATOM   3015  C   SER B 179     -12.464 -13.342 -64.324  1.00 45.52           C  
ANISOU 3015  C   SER B 179     5469   5120   6707    254   1523    102       C  
ATOM   3016  O   SER B 179     -13.166 -12.869 -65.221  1.00 44.20           O  
ANISOU 3016  O   SER B 179     5244   4935   6614    237   1504    150       O  
ATOM   3017  CB  SER B 179     -12.692 -15.842 -64.391  1.00 45.75           C  
ANISOU 3017  CB  SER B 179     5442   5185   6756    221   1461    144       C  
ATOM   3018  OG  SER B 179     -13.059 -16.012 -63.033  1.00 60.32           O  
ANISOU 3018  OG  SER B 179     7312   7019   8590    279   1549    161       O  
ATOM   3019  N   SER B 180     -12.255 -12.715 -63.166  1.00 44.63           N  
ANISOU 3019  N   SER B 180     5424   4991   6543    304   1599     71       N  
ATOM   3020  CA  SER B 180     -12.745 -11.377 -62.866  1.00 42.75           C  
ANISOU 3020  CA  SER B 180     5205   4713   6326    345   1669     84       C  
ATOM   3021  C   SER B 180     -11.981 -10.275 -63.625  1.00 50.95           C  
ANISOU 3021  C   SER B 180     6269   5752   7337    312   1621     30       C  
ATOM   3022  O   SER B 180     -12.403  -9.110 -63.587  1.00 54.20           O  
ANISOU 3022  O   SER B 180     6689   6130   7776    338   1668     43       O  
ATOM   3023  CB  SER B 180     -12.553 -11.107 -61.386  1.00 41.97           C  
ANISOU 3023  CB  SER B 180     5195   4594   6158    404   1755     54       C  
ATOM   3024  OG  SER B 180     -11.169 -11.142 -61.073  1.00 46.66           O  
ANISOU 3024  OG  SER B 180     5870   5212   6648    381   1708    -35       O  
ATOM   3025  N   GLY B 181     -10.826 -10.607 -64.224  1.00 45.26           N  
ANISOU 3025  N   GLY B 181     5567   5068   6562    261   1535    -31       N  
ATOM   3026  CA  GLY B 181      -9.979  -9.631 -64.889  1.00 42.91           C  
ANISOU 3026  CA  GLY B 181     5296   4774   6233    231   1490    -83       C  
ATOM   3027  C   GLY B 181      -8.949  -9.017 -63.965  1.00 43.78           C  
ANISOU 3027  C   GLY B 181     5502   4879   6254    248   1507   -156       C  
ATOM   3028  O   GLY B 181      -8.166  -8.175 -64.406  1.00 44.00           O  
ANISOU 3028  O   GLY B 181     5556   4907   6255    224   1469   -200       O  
ATOM   3029  N   LEU B 182      -8.907  -9.453 -62.687  1.00 38.36           N  
ANISOU 3029  N   LEU B 182     4870   4185   5519    287   1557   -167       N  
ATOM   3030  CA  LEU B 182      -7.926  -9.005 -61.694  1.00 36.59           C  
ANISOU 3030  CA  LEU B 182     4747   3951   5203    301   1565   -234       C  
ATOM   3031  C   LEU B 182      -6.807 -10.007 -61.596  1.00 39.83           C  
ANISOU 3031  C   LEU B 182     5174   4402   5556    266   1500   -277       C  
ATOM   3032  O   LEU B 182      -7.013 -11.211 -61.746  1.00 40.75           O  
ANISOU 3032  O   LEU B 182     5246   4546   5692    256   1485   -251       O  
ATOM   3033  CB  LEU B 182      -8.550  -8.836 -60.298  1.00 36.42           C  
ANISOU 3033  CB  LEU B 182     4790   3892   5155    366   1662   -220       C  
ATOM   3034  CG  LEU B 182      -9.795  -7.941 -60.170  1.00 40.93           C  
ANISOU 3034  CG  LEU B 182     5349   4416   5788    417   1752   -166       C  
ATOM   3035  CD1 LEU B 182     -10.354  -8.011 -58.791  1.00 41.17           C  
ANISOU 3035  CD1 LEU B 182     5446   4411   5786    484   1853   -150       C  
ATOM   3036  CD2 LEU B 182      -9.479  -6.498 -60.499  1.00 36.29           C  
ANISOU 3036  CD2 LEU B 182     4797   3800   5192    412   1745   -199       C  
ATOM   3037  N   TYR B 183      -5.633  -9.514 -61.258  1.00 36.92           N  
ANISOU 3037  N   TYR B 183     4875   4033   5119    250   1463   -338       N  
ATOM   3038  CA  TYR B 183      -4.423 -10.314 -61.074  1.00 35.45           C  
ANISOU 3038  CA  TYR B 183     4711   3880   4878    218   1401   -379       C  
ATOM   3039  C   TYR B 183      -4.202 -10.740 -59.620  1.00 37.40           C  
ANISOU 3039  C   TYR B 183     5037   4116   5058    249   1432   -398       C  
ATOM   3040  O   TYR B 183      -4.719 -10.121 -58.682  1.00 35.98           O  
ANISOU 3040  O   TYR B 183     4922   3896   4853    294   1498   -396       O  
ATOM   3041  CB  TYR B 183      -3.182  -9.507 -61.471  1.00 36.03           C  
ANISOU 3041  CB  TYR B 183     4814   3955   4921    181   1337   -430       C  
ATOM   3042  CG  TYR B 183      -3.105  -9.258 -62.941  1.00 36.62           C  
ANISOU 3042  CG  TYR B 183     4818   4049   5049    143   1294   -419       C  
ATOM   3043  CD1 TYR B 183      -2.627 -10.237 -63.805  1.00 39.92           C  
ANISOU 3043  CD1 TYR B 183     5181   4505   5480    106   1242   -415       C  
ATOM   3044  CD2 TYR B 183      -3.563  -8.061 -63.490  1.00 35.37           C  
ANISOU 3044  CD2 TYR B 183     4649   3865   4926    147   1310   -409       C  
ATOM   3045  CE1 TYR B 183      -2.598 -10.034 -65.179  1.00 39.45           C  
ANISOU 3045  CE1 TYR B 183     5068   4459   5464     74   1207   -403       C  
ATOM   3046  CE2 TYR B 183      -3.553  -7.849 -64.866  1.00 34.95           C  
ANISOU 3046  CE2 TYR B 183     4533   3827   4919    112   1271   -395       C  
ATOM   3047  CZ  TYR B 183      -3.042  -8.830 -65.705  1.00 41.33           C  
ANISOU 3047  CZ  TYR B 183     5296   4674   5734     75   1218   -394       C  
ATOM   3048  OH  TYR B 183      -3.026  -8.671 -67.055  1.00 45.25           O  
ANISOU 3048  OH  TYR B 183     5743   5182   6268     43   1182   -380       O  
ATOM   3049  N   SER B 184      -3.404 -11.802 -59.469  1.00 34.96           N  
ANISOU 3049  N   SER B 184     4725   3840   4719    224   1384   -415       N  
ATOM   3050  CA  SER B 184      -2.907 -12.312 -58.194  1.00 34.64           C  
ANISOU 3050  CA  SER B 184     4759   3795   4609    239   1389   -438       C  
ATOM   3051  C   SER B 184      -1.472 -12.748 -58.358  1.00 40.09           C  
ANISOU 3051  C   SER B 184     5453   4512   5265    192   1305   -476       C  
ATOM   3052  O   SER B 184      -1.100 -13.291 -59.403  1.00 38.35           O  
ANISOU 3052  O   SER B 184     5162   4326   5083    157   1259   -470       O  
ATOM   3053  CB  SER B 184      -3.700 -13.524 -57.720  1.00 36.09           C  
ANISOU 3053  CB  SER B 184     4915   3992   4807    266   1434   -397       C  
ATOM   3054  OG  SER B 184      -4.858 -13.164 -57.006  1.00 47.27           O  
ANISOU 3054  OG  SER B 184     6357   5372   6230    321   1525   -364       O  
ATOM   3055  N   LEU B 185      -0.658 -12.559 -57.325  1.00 40.18           N  
ANISOU 3055  N   LEU B 185     5552   4508   5208    192   1284   -511       N  
ATOM   3056  CA  LEU B 185       0.670 -13.135 -57.383  1.00 39.95           C  
ANISOU 3056  CA  LEU B 185     5520   4504   5156    150   1206   -535       C  
ATOM   3057  C   LEU B 185       1.099 -13.605 -56.015  1.00 40.97           C  
ANISOU 3057  C   LEU B 185     5729   4621   5216    161   1201   -550       C  
ATOM   3058  O   LEU B 185       0.613 -13.134 -54.991  1.00 41.27           O  
ANISOU 3058  O   LEU B 185     5853   4622   5207    197   1248   -555       O  
ATOM   3059  CB  LEU B 185       1.733 -12.315 -58.128  1.00 40.14           C  
ANISOU 3059  CB  LEU B 185     5534   4528   5189    108   1139   -561       C  
ATOM   3060  CG  LEU B 185       2.647 -11.261 -57.560  1.00 44.31           C  
ANISOU 3060  CG  LEU B 185     6142   5021   5672     92   1095   -596       C  
ATOM   3061  CD1 LEU B 185       3.489 -11.701 -56.330  1.00 41.88           C  
ANISOU 3061  CD1 LEU B 185     5911   4703   5299     84   1055   -615       C  
ATOM   3062  CD2 LEU B 185       3.647 -10.901 -58.617  1.00 48.21           C  
ANISOU 3062  CD2 LEU B 185     6583   5533   6203     46   1029   -604       C  
ATOM   3063  N   SER B 186       1.982 -14.588 -56.037  1.00 35.57           N  
ANISOU 3063  N   SER B 186     5019   3969   4528    131   1146   -553       N  
ATOM   3064  CA  SER B 186       2.522 -15.241 -54.872  1.00 36.18           C  
ANISOU 3064  CA  SER B 186     5157   4042   4547    132   1127   -563       C  
ATOM   3065  C   SER B 186       4.030 -15.047 -54.857  1.00 40.64           C  
ANISOU 3065  C   SER B 186     5740   4607   5095     85   1036   -588       C  
ATOM   3066  O   SER B 186       4.676 -15.092 -55.897  1.00 39.75           O  
ANISOU 3066  O   SER B 186     5556   4518   5030     52    993   -586       O  
ATOM   3067  CB  SER B 186       2.164 -16.722 -54.904  1.00 42.12           C  
ANISOU 3067  CB  SER B 186     5850   4831   5323    140   1145   -534       C  
ATOM   3068  OG  SER B 186       0.770 -16.835 -54.674  1.00 56.41           O  
ANISOU 3068  OG  SER B 186     7656   6632   7146    186   1228   -505       O  
ATOM   3069  N   SER B 187       4.561 -14.746 -53.688  1.00 39.00           N  
ANISOU 3069  N   SER B 187     5631   4366   4820     83   1007   -607       N  
ATOM   3070  CA  SER B 187       5.976 -14.673 -53.426  1.00 39.02           C  
ANISOU 3070  CA  SER B 187     5658   4363   4805     38    915   -622       C  
ATOM   3071  C   SER B 187       6.254 -15.613 -52.267  1.00 40.58           C  
ANISOU 3071  C   SER B 187     5908   4560   4951     41    899   -618       C  
ATOM   3072  O   SER B 187       5.516 -15.627 -51.276  1.00 38.26           O  
ANISOU 3072  O   SER B 187     5695   4241   4600     79    950   -621       O  
ATOM   3073  CB  SER B 187       6.421 -13.249 -53.098  1.00 43.69           C  
ANISOU 3073  CB  SER B 187     6334   4906   5362     24    876   -649       C  
ATOM   3074  OG  SER B 187       7.837 -13.190 -53.001  1.00 50.05           O  
ANISOU 3074  OG  SER B 187     7144   5706   6169    -27    777   -653       O  
ATOM   3075  N   VAL B 188       7.296 -16.429 -52.402  1.00 39.01           N  
ANISOU 3075  N   VAL B 188     5661   4387   4774      5    834   -608       N  
ATOM   3076  CA  VAL B 188       7.676 -17.379 -51.357  1.00 38.74           C  
ANISOU 3076  CA  VAL B 188     5668   4355   4698      2    809   -600       C  
ATOM   3077  C   VAL B 188       9.153 -17.305 -51.022  1.00 43.41           C  
ANISOU 3077  C   VAL B 188     6278   4933   5283    -49    704   -601       C  
ATOM   3078  O   VAL B 188       9.978 -16.808 -51.789  1.00 40.45           O  
ANISOU 3078  O   VAL B 188     5853   4559   4956    -83    652   -600       O  
ATOM   3079  CB  VAL B 188       7.266 -18.852 -51.679  1.00 41.13           C  
ANISOU 3079  CB  VAL B 188     5885   4705   5037     16    847   -574       C  
ATOM   3080  CG1 VAL B 188       5.771 -18.977 -51.931  1.00 39.12           C  
ANISOU 3080  CG1 VAL B 188     5612   4459   4795     64    944   -563       C  
ATOM   3081  CG2 VAL B 188       8.071 -19.421 -52.851  1.00 41.47           C  
ANISOU 3081  CG2 VAL B 188     5816   4786   5155    -16    808   -559       C  
ATOM   3082  N   VAL B 189       9.486 -17.829 -49.855  1.00 44.55           N  
ANISOU 3082  N   VAL B 189     6492   5062   5372    -54    671   -599       N  
ATOM   3083  CA  VAL B 189      10.879 -17.930 -49.456  1.00 44.55           C  
ANISOU 3083  CA  VAL B 189     6505   5049   5374   -104    565   -590       C  
ATOM   3084  C   VAL B 189      11.080 -19.220 -48.659  1.00 43.74           C  
ANISOU 3084  C   VAL B 189     6407   4962   5249   -104    552   -570       C  
ATOM   3085  O   VAL B 189      10.215 -19.580 -47.885  1.00 39.92           O  
ANISOU 3085  O   VAL B 189     5987   4474   4709    -67    608   -575       O  
ATOM   3086  CB  VAL B 189      11.377 -16.624 -48.760  1.00 49.03           C  
ANISOU 3086  CB  VAL B 189     7189   5555   5886   -129    499   -612       C  
ATOM   3087  CG1 VAL B 189      10.607 -16.323 -47.484  1.00 49.71           C  
ANISOU 3087  CG1 VAL B 189     7423   5598   5869    -95    535   -634       C  
ATOM   3088  CG2 VAL B 189      12.874 -16.679 -48.497  1.00 49.67           C  
ANISOU 3088  CG2 VAL B 189     7265   5620   5986   -189    377   -592       C  
ATOM   3089  N   THR B 190      12.171 -19.955 -48.929  1.00 42.65           N  
ANISOU 3089  N   THR B 190     6195   4846   5164   -142    487   -543       N  
ATOM   3090  CA  THR B 190      12.510 -21.171 -48.170  1.00 43.64           C  
ANISOU 3090  CA  THR B 190     6323   4985   5275   -147    462   -521       C  
ATOM   3091  C   THR B 190      13.626 -20.787 -47.221  1.00 49.29           C  
ANISOU 3091  C   THR B 190     7117   5657   5956   -194    351   -514       C  
ATOM   3092  O   THR B 190      14.523 -20.039 -47.580  1.00 50.06           O  
ANISOU 3092  O   THR B 190     7198   5735   6089   -233    280   -509       O  
ATOM   3093  CB  THR B 190      12.845 -22.403 -49.044  1.00 46.03           C  
ANISOU 3093  CB  THR B 190     6492   5339   5660   -151    475   -491       C  
ATOM   3094  OG1 THR B 190      13.803 -22.033 -50.034  1.00 50.39           O  
ANISOU 3094  OG1 THR B 190     6963   5896   6287   -184    432   -478       O  
ATOM   3095  CG2 THR B 190      11.603 -23.008 -49.681  1.00 43.09           C  
ANISOU 3095  CG2 THR B 190     6067   5002   5303   -105    578   -495       C  
ATOM   3096  N   VAL B 191      13.510 -21.218 -45.992  1.00 47.30           N  
ANISOU 3096  N   VAL B 191     6957   5385   5630   -189    336   -514       N  
ATOM   3097  CA  VAL B 191      14.453 -20.877 -44.947  1.00 48.13           C  
ANISOU 3097  CA  VAL B 191     7160   5441   5688   -234    226   -508       C  
ATOM   3098  C   VAL B 191      14.703 -22.124 -44.114  1.00 53.49           C  
ANISOU 3098  C   VAL B 191     7847   6132   6345   -238    203   -482       C  
ATOM   3099  O   VAL B 191      13.871 -23.040 -44.107  1.00 51.30           O  
ANISOU 3099  O   VAL B 191     7540   5890   6061   -197    287   -480       O  
ATOM   3100  CB  VAL B 191      13.905 -19.703 -44.060  1.00 51.31           C  
ANISOU 3100  CB  VAL B 191     7729   5783   5984   -220    229   -546       C  
ATOM   3101  CG1 VAL B 191      13.684 -18.442 -44.884  1.00 50.33           C  
ANISOU 3101  CG1 VAL B 191     7595   5645   5884   -217    249   -570       C  
ATOM   3102  CG2 VAL B 191      12.627 -20.091 -43.319  1.00 50.67           C  
ANISOU 3102  CG2 VAL B 191     7730   5701   5821   -161    330   -564       C  
ATOM   3103  N   PRO B 192      15.794 -22.167 -43.333  1.00 53.71           N  
ANISOU 3103  N   PRO B 192     7922   6127   6358   -289     87   -459       N  
ATOM   3104  CA  PRO B 192      15.974 -23.319 -42.442  1.00 54.19           C  
ANISOU 3104  CA  PRO B 192     8004   6195   6391   -293     63   -435       C  
ATOM   3105  C   PRO B 192      14.893 -23.288 -41.375  1.00 61.35           C  
ANISOU 3105  C   PRO B 192     9053   7079   7179   -250    126   -464       C  
ATOM   3106  O   PRO B 192      14.531 -22.210 -40.897  1.00 61.88           O  
ANISOU 3106  O   PRO B 192     9246   7097   7168   -242    127   -496       O  
ATOM   3107  CB  PRO B 192      17.370 -23.104 -41.853  1.00 56.52           C  
ANISOU 3107  CB  PRO B 192     8333   6448   6695   -362    -85   -403       C  
ATOM   3108  CG  PRO B 192      17.981 -21.983 -42.610  1.00 60.23           C  
ANISOU 3108  CG  PRO B 192     8767   6897   7220   -394   -135   -404       C  
ATOM   3109  CD  PRO B 192      16.868 -21.172 -43.153  1.00 55.64           C  
ANISOU 3109  CD  PRO B 192     8211   6321   6609   -347    -33   -452       C  
ATOM   3110  N   SER B 193      14.366 -24.449 -41.004  1.00 60.64           N  
ANISOU 3110  N   SER B 193     8945   7021   7075   -219    182   -450       N  
ATOM   3111  CA  SER B 193      13.348 -24.542 -39.935  1.00 61.56           C  
ANISOU 3111  CA  SER B 193     9193   7116   7082   -174    249   -469       C  
ATOM   3112  C   SER B 193      13.864 -23.957 -38.622  1.00 67.25           C  
ANISOU 3112  C   SER B 193    10087   7768   7697   -205    158   -477       C  
ATOM   3113  O   SER B 193      13.088 -23.410 -37.843  1.00 67.94           O  
ANISOU 3113  O   SER B 193    10319   7815   7680   -170    208   -505       O  
ATOM   3114  CB  SER B 193      12.951 -25.995 -39.698  1.00 63.09           C  
ANISOU 3114  CB  SER B 193     9330   7354   7288   -148    300   -443       C  
ATOM   3115  OG  SER B 193      12.193 -26.481 -40.789  1.00 74.30           O  
ANISOU 3115  OG  SER B 193    10620   8828   8784   -110    398   -440       O  
ATOM   3116  N   SER B 194      15.176 -24.102 -38.378  1.00 65.29           N  
ANISOU 3116  N   SER B 194     9828   7502   7476   -271     23   -448       N  
ATOM   3117  CA  SER B 194      15.857 -23.602 -37.180  1.00 66.38           C  
ANISOU 3117  CA  SER B 194    10126   7571   7525   -316    -93   -448       C  
ATOM   3118  C   SER B 194      15.735 -22.092 -37.047  1.00 70.28           C  
ANISOU 3118  C   SER B 194    10744   8003   7956   -321   -113   -487       C  
ATOM   3119  O   SER B 194      15.759 -21.599 -35.917  1.00 72.31           O  
ANISOU 3119  O   SER B 194    11181   8195   8097   -332   -162   -504       O  
ATOM   3120  CB  SER B 194      17.333 -23.997 -37.198  1.00 69.72           C  
ANISOU 3120  CB  SER B 194    10477   7990   8022   -390   -237   -399       C  
ATOM   3121  OG  SER B 194      17.992 -23.507 -38.356  1.00 78.40           O  
ANISOU 3121  OG  SER B 194    11450   9106   9234   -419   -269   -387       O  
ATOM   3122  N   SER B 195      15.622 -21.366 -38.189  1.00 64.39           N  
ANISOU 3122  N   SER B 195     9908   7275   7281   -314    -78   -503       N  
ATOM   3123  CA  SER B 195      15.488 -19.900 -38.227  1.00 64.18           C  
ANISOU 3123  CA  SER B 195     9981   7195   7211   -317    -90   -540       C  
ATOM   3124  C   SER B 195      14.108 -19.368 -37.851  1.00 67.33           C  
ANISOU 3124  C   SER B 195    10498   7571   7513   -246     38   -584       C  
ATOM   3125  O   SER B 195      14.005 -18.184 -37.558  1.00 68.55           O  
ANISOU 3125  O   SER B 195    10778   7666   7603   -248     20   -616       O  
ATOM   3126  CB  SER B 195      15.850 -19.353 -39.607  1.00 66.91           C  
ANISOU 3126  CB  SER B 195    10181   7568   7672   -334    -94   -536       C  
ATOM   3127  OG  SER B 195      17.194 -19.645 -39.944  1.00 79.53           O  
ANISOU 3127  OG  SER B 195    11679   9175   9362   -399   -213   -491       O  
ATOM   3128  N   LEU B 196      13.051 -20.189 -37.877  1.00 63.17           N  
ANISOU 3128  N   LEU B 196     9932   7089   6981   -184    165   -583       N  
ATOM   3129  CA  LEU B 196      11.715 -19.697 -37.528  1.00 63.09           C  
ANISOU 3129  CA  LEU B 196    10024   7056   6891   -112    295   -615       C  
ATOM   3130  C   LEU B 196      11.679 -19.387 -36.040  1.00 68.61           C  
ANISOU 3130  C   LEU B 196    10944   7682   7445   -109    266   -631       C  
ATOM   3131  O   LEU B 196      12.034 -20.240 -35.224  1.00 68.31           O  
ANISOU 3131  O   LEU B 196    10948   7642   7366   -126    219   -609       O  
ATOM   3132  CB  LEU B 196      10.613 -20.697 -37.872  1.00 62.32           C  
ANISOU 3132  CB  LEU B 196     9829   7020   6830    -49    432   -599       C  
ATOM   3133  CG  LEU B 196      10.511 -21.146 -39.319  1.00 65.93           C  
ANISOU 3133  CG  LEU B 196    10080   7550   7421    -47    470   -583       C  
ATOM   3134  CD1 LEU B 196       9.424 -22.159 -39.458  1.00 65.72           C  
ANISOU 3134  CD1 LEU B 196     9981   7571   7417     11    591   -565       C  
ATOM   3135  CD2 LEU B 196      10.279 -19.978 -40.257  1.00 68.24           C  
ANISOU 3135  CD2 LEU B 196    10341   7834   7755    -42    495   -607       C  
ATOM   3136  N   GLY B 197      11.290 -18.154 -35.716  1.00 66.19           N  
ANISOU 3136  N   GLY B 197    10779   7309   7059    -89    289   -668       N  
ATOM   3137  CA  GLY B 197      11.269 -17.635 -34.353  1.00 66.83           C  
ANISOU 3137  CA  GLY B 197    11096   7306   6990    -85    260   -691       C  
ATOM   3138  C   GLY B 197      12.540 -16.948 -33.889  1.00 70.33           C  
ANISOU 3138  C   GLY B 197    11642   7683   7395   -167     83   -696       C  
ATOM   3139  O   GLY B 197      12.558 -16.375 -32.802  1.00 72.50           O  
ANISOU 3139  O   GLY B 197    12130   7878   7540   -169     47   -719       O  
ATOM   3140  N   THR B 198      13.599 -16.978 -34.702  1.00 66.73           N  
ANISOU 3140  N   THR B 198    11044   7258   7053   -234    -28   -673       N  
ATOM   3141  CA  THR B 198      14.895 -16.336 -34.459  1.00 67.87           C  
ANISOU 3141  CA  THR B 198    11246   7345   7194   -319   -206   -665       C  
ATOM   3142  C   THR B 198      14.904 -14.946 -35.088  1.00 72.30           C  
ANISOU 3142  C   THR B 198    11824   7872   7776   -327   -215   -695       C  
ATOM   3143  O   THR B 198      15.450 -14.008 -34.519  1.00 73.54           O  
ANISOU 3143  O   THR B 198    12129   7947   7864   -369   -320   -712       O  
ATOM   3144  CB  THR B 198      16.015 -17.179 -35.117  1.00 82.96           C  
ANISOU 3144  CB  THR B 198    12967   9314   9240   -381   -306   -612       C  
ATOM   3145  OG1 THR B 198      15.974 -18.502 -34.593  1.00 89.14           O  
ANISOU 3145  OG1 THR B 198    13725  10133  10012   -372   -291   -583       O  
ATOM   3146  CG2 THR B 198      17.388 -16.606 -34.904  1.00 87.88           C  
ANISOU 3146  CG2 THR B 198    13626   9882   9882   -472   -493   -590       C  
ATOM   3147  N   LYS B 199      14.377 -14.859 -36.310  1.00 67.84           N  
ANISOU 3147  N   LYS B 199    11098   7368   7310   -291   -117   -699       N  
ATOM   3148  CA  LYS B 199      14.319 -13.666 -37.147  1.00 66.32           C  
ANISOU 3148  CA  LYS B 199    10876   7159   7161   -293   -109   -722       C  
ATOM   3149  C   LYS B 199      12.863 -13.433 -37.546  1.00 67.38           C  
ANISOU 3149  C   LYS B 199    11001   7316   7283   -205     71   -750       C  
ATOM   3150  O   LYS B 199      12.112 -14.402 -37.692  1.00 65.98           O  
ANISOU 3150  O   LYS B 199    10743   7198   7128   -156    179   -736       O  
ATOM   3151  CB  LYS B 199      15.151 -13.954 -38.435  1.00 67.36           C  
ANISOU 3151  CB  LYS B 199    10786   7357   7452   -339   -163   -685       C  
ATOM   3152  CG  LYS B 199      15.476 -12.726 -39.273  1.00 90.35           C  
ANISOU 3152  CG  LYS B 199    13664  10247  10420   -364   -200   -697       C  
ATOM   3153  CD  LYS B 199      15.827 -13.070 -40.725  1.00 95.80           C  
ANISOU 3153  CD  LYS B 199    14125  11014  11262   -376   -185   -667       C  
ATOM   3154  CE  LYS B 199      17.150 -13.780 -40.857  1.00101.40           C  
ANISOU 3154  CE  LYS B 199    14731  11744  12054   -443   -308   -613       C  
ATOM   3155  NZ  LYS B 199      17.596 -13.831 -42.280  1.00107.78           N  
ANISOU 3155  NZ  LYS B 199    15340  12608  13003   -457   -301   -585       N  
ATOM   3156  N   THR B 200      12.477 -12.178 -37.790  1.00 62.58           N  
ANISOU 3156  N   THR B 200    10461   6665   6653   -188    102   -784       N  
ATOM   3157  CA  THR B 200      11.142 -11.892 -38.308  1.00 61.18           C  
ANISOU 3157  CA  THR B 200    10252   6509   6485   -108    268   -803       C  
ATOM   3158  C   THR B 200      11.162 -12.016 -39.837  1.00 61.59           C  
ANISOU 3158  C   THR B 200    10081   6638   6683   -115    294   -784       C  
ATOM   3159  O   THR B 200      12.209 -11.831 -40.481  1.00 61.08           O  
ANISOU 3159  O   THR B 200     9925   6586   6697   -178    185   -768       O  
ATOM   3160  CB  THR B 200      10.656 -10.499 -37.918  1.00 72.35           C  
ANISOU 3160  CB  THR B 200    11835   7841   7814    -81    301   -845       C  
ATOM   3161  OG1 THR B 200      11.580  -9.533 -38.415  1.00 73.46           O  
ANISOU 3161  OG1 THR B 200    11964   7952   7997   -144    182   -853       O  
ATOM   3162  CG2 THR B 200      10.449 -10.357 -36.425  1.00 70.65           C  
ANISOU 3162  CG2 THR B 200    11859   7544   7441    -60    301   -867       C  
ATOM   3163  N   TYR B 201       9.998 -12.321 -40.416  1.00 55.39           N  
ANISOU 3163  N   TYR B 201     9212   5900   5936    -49    439   -782       N  
ATOM   3164  CA  TYR B 201       9.854 -12.455 -41.870  1.00 51.96           C  
ANISOU 3164  CA  TYR B 201     8579   5534   5629    -48    477   -766       C  
ATOM   3165  C   TYR B 201       8.659 -11.641 -42.305  1.00 51.04           C  
ANISOU 3165  C   TYR B 201     8473   5407   5515     13    601   -785       C  
ATOM   3166  O   TYR B 201       7.557 -11.851 -41.830  1.00 47.49           O  
ANISOU 3166  O   TYR B 201     8076   4950   5017     78    717   -786       O  
ATOM   3167  CB  TYR B 201       9.732 -13.933 -42.248  1.00 51.47           C  
ANISOU 3167  CB  TYR B 201     8374   5551   5632    -39    512   -731       C  
ATOM   3168  CG  TYR B 201      11.027 -14.695 -42.064  1.00 51.09           C  
ANISOU 3168  CG  TYR B 201     8283   5519   5610   -105    385   -706       C  
ATOM   3169  CD1 TYR B 201      12.069 -14.571 -42.981  1.00 51.66           C  
ANISOU 3169  CD1 TYR B 201     8236   5614   5777   -161    295   -688       C  
ATOM   3170  CD2 TYR B 201      11.168 -15.632 -41.047  1.00 52.28           C  
ANISOU 3170  CD2 TYR B 201     8496   5666   5701   -106    365   -692       C  
ATOM   3171  CE1 TYR B 201      13.266 -15.263 -42.811  1.00 53.71           C  
ANISOU 3171  CE1 TYR B 201     8450   5886   6072   -219    184   -657       C  
ATOM   3172  CE2 TYR B 201      12.342 -16.371 -40.898  1.00 53.23           C  
ANISOU 3172  CE2 TYR B 201     8567   5802   5855   -165    250   -662       C  
ATOM   3173  CZ  TYR B 201      13.401 -16.168 -41.763  1.00 60.65           C  
ANISOU 3173  CZ  TYR B 201     9394   6759   6891   -221    159   -644       C  
ATOM   3174  OH  TYR B 201      14.563 -16.889 -41.568  1.00 58.16           O  
ANISOU 3174  OH  TYR B 201     9030   6453   6614   -277     49   -607       O  
ATOM   3175  N   THR B 202       8.906 -10.678 -43.176  1.00 50.52           N  
ANISOU 3175  N   THR B 202     8357   5334   5503     -8    573   -796       N  
ATOM   3176  CA  THR B 202       7.922  -9.703 -43.647  1.00 50.79           C  
ANISOU 3176  CA  THR B 202     8402   5350   5546     40    671   -813       C  
ATOM   3177  C   THR B 202       8.092  -9.524 -45.155  1.00 54.13           C  
ANISOU 3177  C   THR B 202     8648   5827   6092     17    664   -799       C  
ATOM   3178  O   THR B 202       9.226  -9.355 -45.611  1.00 52.48           O  
ANISOU 3178  O   THR B 202     8385   5626   5930    -45    553   -793       O  
ATOM   3179  CB  THR B 202       8.192  -8.316 -42.981  1.00 55.12           C  
ANISOU 3179  CB  THR B 202     9127   5806   6011     28    623   -850       C  
ATOM   3180  OG1 THR B 202       8.340  -8.466 -41.570  1.00 55.13           O  
ANISOU 3180  OG1 THR B 202     9308   5749   5891     31    594   -864       O  
ATOM   3181  CG2 THR B 202       7.102  -7.260 -43.298  1.00 47.60           C  
ANISOU 3181  CG2 THR B 202     8209   4822   5055     86    735   -869       C  
ATOM   3182  N   CYS B 203       6.988  -9.514 -45.911  1.00 50.84           N  
ANISOU 3182  N   CYS B 203     8146   5442   5727     67    778   -790       N  
ATOM   3183  CA  CYS B 203       7.050  -9.239 -47.341  1.00 51.31           C  
ANISOU 3183  CA  CYS B 203     8057   5546   5893     49    777   -779       C  
ATOM   3184  C   CYS B 203       6.636  -7.777 -47.549  1.00 52.13           C  
ANISOU 3184  C   CYS B 203     8224   5599   5986     66    805   -803       C  
ATOM   3185  O   CYS B 203       5.713  -7.286 -46.911  1.00 51.94           O  
ANISOU 3185  O   CYS B 203     8305   5529   5900    120    890   -817       O  
ATOM   3186  CB  CYS B 203       6.174 -10.206 -48.137  1.00 53.03           C  
ANISOU 3186  CB  CYS B 203     8134   5832   6182     84    867   -749       C  
ATOM   3187  SG  CYS B 203       4.403  -9.994 -47.854  1.00 59.00           S  
ANISOU 3187  SG  CYS B 203     8931   6569   6916    171   1027   -743       S  
ATOM   3188  N   ASN B 204       7.336  -7.080 -48.416  1.00 47.27           N  
ANISOU 3188  N   ASN B 204     7545   4987   5428     22    737   -806       N  
ATOM   3189  CA  ASN B 204       7.078  -5.669 -48.690  1.00 45.57           C  
ANISOU 3189  CA  ASN B 204     7379   4723   5211     30    750   -828       C  
ATOM   3190  C   ASN B 204       6.517  -5.584 -50.072  1.00 47.56           C  
ANISOU 3190  C   ASN B 204     7482   5026   5562     42    807   -809       C  
ATOM   3191  O   ASN B 204       7.212  -5.889 -51.035  1.00 47.08           O  
ANISOU 3191  O   ASN B 204     7298   5013   5576      0    751   -792       O  
ATOM   3192  CB  ASN B 204       8.366  -4.847 -48.538  1.00 41.51           C  
ANISOU 3192  CB  ASN B 204     6923   4165   4684    -35    616   -844       C  
ATOM   3193  CG  ASN B 204       9.270  -5.377 -47.459  1.00 56.12           C  
ANISOU 3193  CG  ASN B 204     8864   5991   6470    -71    521   -845       C  
ATOM   3194  OD1 ASN B 204      10.274  -6.018 -47.741  1.00 51.73           O  
ANISOU 3194  OD1 ASN B 204     8225   5470   5961   -123    434   -822       O  
ATOM   3195  ND2 ASN B 204       8.891  -5.183 -46.193  1.00 51.41           N  
ANISOU 3195  ND2 ASN B 204     8439   5332   5761    -43    543   -869       N  
ATOM   3196  N   VAL B 205       5.232  -5.253 -50.171  1.00 44.81           N  
ANISOU 3196  N   VAL B 205     7143   4669   5216    102    922   -807       N  
ATOM   3197  CA  VAL B 205       4.509  -5.220 -51.442  1.00 43.95           C  
ANISOU 3197  CA  VAL B 205     6897   4605   5199    118    984   -784       C  
ATOM   3198  C   VAL B 205       4.221  -3.784 -51.874  1.00 48.23           C  
ANISOU 3198  C   VAL B 205     7465   5104   5755    126   1000   -799       C  
ATOM   3199  O   VAL B 205       3.735  -2.994 -51.076  1.00 49.33           O  
ANISOU 3199  O   VAL B 205     7732   5179   5832    162   1045   -819       O  
ATOM   3200  CB  VAL B 205       3.199  -6.052 -51.331  1.00 47.47           C  
ANISOU 3200  CB  VAL B 205     7305   5076   5655    179   1102   -756       C  
ATOM   3201  CG1 VAL B 205       2.435  -6.022 -52.647  1.00 47.54           C  
ANISOU 3201  CG1 VAL B 205     7176   5127   5760    190   1154   -728       C  
ATOM   3202  CG2 VAL B 205       3.487  -7.495 -50.890  1.00 46.74           C  
ANISOU 3202  CG2 VAL B 205     7186   5025   5548    171   1084   -742       C  
ATOM   3203  N   ASP B 206       4.476  -3.476 -53.147  1.00 45.01           N  
ANISOU 3203  N   ASP B 206     6941   4731   5431     96    972   -787       N  
ATOM   3204  CA  ASP B 206       4.246  -2.173 -53.728  1.00 45.47           C  
ANISOU 3204  CA  ASP B 206     7002   4757   5516     98    982   -796       C  
ATOM   3205  C   ASP B 206       3.413  -2.325 -55.006  1.00 46.13           C  
ANISOU 3205  C   ASP B 206     6946   4889   5690    115   1045   -764       C  
ATOM   3206  O   ASP B 206       3.777  -3.114 -55.866  1.00 44.00           O  
ANISOU 3206  O   ASP B 206     6562   4680   5478     85   1014   -744       O  
ATOM   3207  CB  ASP B 206       5.603  -1.487 -54.046  1.00 49.29           C  
ANISOU 3207  CB  ASP B 206     7487   5227   6012     33    862   -811       C  
ATOM   3208  CG  ASP B 206       5.617   0.026 -54.053  1.00 72.28           C  
ANISOU 3208  CG  ASP B 206    10473   8076   8913     31    849   -834       C  
ATOM   3209  OD1 ASP B 206       4.519   0.643 -54.005  1.00 73.86           O  
ANISOU 3209  OD1 ASP B 206    10709   8248   9109     83    941   -836       O  
ATOM   3210  OD2 ASP B 206       6.718   0.599 -54.153  1.00 85.77           O  
ANISOU 3210  OD2 ASP B 206    12198   9765  10627    -21    747   -844       O  
ATOM   3211  N   HIS B 207       2.266  -1.611 -55.096  1.00 42.85           N  
ANISOU 3211  N   HIS B 207     6548   4444   5287    163   1135   -757       N  
ATOM   3212  CA  HIS B 207       1.411  -1.560 -56.284  1.00 40.48           C  
ANISOU 3212  CA  HIS B 207     6127   4178   5074    177   1189   -724       C  
ATOM   3213  C   HIS B 207       1.290  -0.072 -56.594  1.00 46.18           C  
ANISOU 3213  C   HIS B 207     6885   4854   5810    179   1193   -737       C  
ATOM   3214  O   HIS B 207       0.400   0.620 -56.086  1.00 45.36           O  
ANISOU 3214  O   HIS B 207     6851   4698   5685    230   1272   -738       O  
ATOM   3215  CB  HIS B 207       0.034  -2.186 -56.069  1.00 39.47           C  
ANISOU 3215  CB  HIS B 207     5975   4059   4963    236   1299   -690       C  
ATOM   3216  CG  HIS B 207      -0.776  -2.216 -57.330  1.00 40.89           C  
ANISOU 3216  CG  HIS B 207     6026   4274   5237    240   1337   -650       C  
ATOM   3217  ND1 HIS B 207      -1.990  -1.583 -57.417  1.00 41.94           N  
ANISOU 3217  ND1 HIS B 207     6155   4376   5403    288   1427   -623       N  
ATOM   3218  CD2 HIS B 207      -0.486  -2.763 -58.529  1.00 41.60           C  
ANISOU 3218  CD2 HIS B 207     5996   4421   5389    200   1291   -631       C  
ATOM   3219  CE1 HIS B 207      -2.410  -1.776 -58.651  1.00 40.72           C  
ANISOU 3219  CE1 HIS B 207     5878   4262   5333    272   1425   -588       C  
ATOM   3220  NE2 HIS B 207      -1.529  -2.483 -59.350  1.00 40.92           N  
ANISOU 3220  NE2 HIS B 207     5836   4340   5373    219   1345   -594       N  
ATOM   3221  N   LYS B 208       2.232   0.417 -57.395  1.00 43.94           N  
ANISOU 3221  N   LYS B 208     6554   4582   5559    126   1109   -746       N  
ATOM   3222  CA  LYS B 208       2.360   1.828 -57.694  1.00 45.38           C  
ANISOU 3222  CA  LYS B 208     6769   4720   5752    117   1091   -762       C  
ATOM   3223  C   LYS B 208       1.094   2.427 -58.371  1.00 48.44           C  
ANISOU 3223  C   LYS B 208     7106   5101   6199    158   1181   -735       C  
ATOM   3224  O   LYS B 208       0.626   3.473 -57.912  1.00 47.00           O  
ANISOU 3224  O   LYS B 208     7007   4857   5993    190   1223   -749       O  
ATOM   3225  CB  LYS B 208       3.665   2.085 -58.481  1.00 49.25           C  
ANISOU 3225  CB  LYS B 208     7203   5233   6276     51    983   -767       C  
ATOM   3226  CG  LYS B 208       4.918   1.856 -57.607  1.00 65.16           C  
ANISOU 3226  CG  LYS B 208     9295   7230   8233     12    890   -791       C  
ATOM   3227  CD  LYS B 208       6.242   1.838 -58.388  1.00 73.79           C  
ANISOU 3227  CD  LYS B 208    10312   8354   9373    -52    788   -783       C  
ATOM   3228  CE  LYS B 208       7.436   1.577 -57.485  1.00 85.83           C  
ANISOU 3228  CE  LYS B 208    11906   9857  10849    -91    694   -797       C  
ATOM   3229  NZ  LYS B 208       7.810   0.127 -57.428  1.00 96.56           N  
ANISOU 3229  NZ  LYS B 208    13205  11270  12212   -102    680   -779       N  
ATOM   3230  N   PRO B 209       0.392   1.719 -59.290  1.00 44.61           N  
ANISOU 3230  N   PRO B 209     6498   4669   5782    165   1220   -695       N  
ATOM   3231  CA  PRO B 209      -0.838   2.310 -59.849  1.00 43.89           C  
ANISOU 3231  CA  PRO B 209     6363   4564   5748    202   1300   -664       C  
ATOM   3232  C   PRO B 209      -1.895   2.752 -58.837  1.00 50.72           C  
ANISOU 3232  C   PRO B 209     7320   5370   6583    270   1402   -660       C  
ATOM   3233  O   PRO B 209      -2.580   3.738 -59.083  1.00 50.44           O  
ANISOU 3233  O   PRO B 209     7288   5297   6580    297   1452   -648       O  
ATOM   3234  CB  PRO B 209      -1.359   1.232 -60.789  1.00 44.53           C  
ANISOU 3234  CB  PRO B 209     6315   4710   5896    195   1314   -620       C  
ATOM   3235  CG  PRO B 209      -0.137   0.435 -61.173  1.00 47.80           C  
ANISOU 3235  CG  PRO B 209     6688   5174   6300    140   1223   -635       C  
ATOM   3236  CD  PRO B 209       0.767   0.466 -59.983  1.00 43.92           C  
ANISOU 3236  CD  PRO B 209     6307   4654   5728    133   1182   -676       C  
ATOM   3237  N   SER B 210      -2.020   2.065 -57.696  1.00 48.36           N  
ANISOU 3237  N   SER B 210     7097   5057   6219    301   1437   -668       N  
ATOM   3238  CA  SER B 210      -2.999   2.444 -56.666  1.00 47.42           C  
ANISOU 3238  CA  SER B 210     7076   4878   6063    372   1545   -662       C  
ATOM   3239  C   SER B 210      -2.320   3.070 -55.404  1.00 51.32           C  
ANISOU 3239  C   SER B 210     7746   5304   6449    379   1523   -716       C  
ATOM   3240  O   SER B 210      -2.980   3.232 -54.369  1.00 50.33           O  
ANISOU 3240  O   SER B 210     7728   5125   6270    439   1610   -718       O  
ATOM   3241  CB  SER B 210      -3.760   1.190 -56.249  1.00 49.69           C  
ANISOU 3241  CB  SER B 210     7330   5194   6355    408   1612   -626       C  
ATOM   3242  OG  SER B 210      -2.855   0.294 -55.629  1.00 45.63           O  
ANISOU 3242  OG  SER B 210     6858   4703   5775    379   1548   -654       O  
ATOM   3243  N   ASN B 211      -0.990   3.295 -55.451  1.00 48.65           N  
ANISOU 3243  N   ASN B 211     7440   4970   6077    317   1405   -756       N  
ATOM   3244  CA  ASN B 211      -0.197   3.807 -54.326  1.00 50.82           C  
ANISOU 3244  CA  ASN B 211     7876   5181   6250    308   1356   -805       C  
ATOM   3245  C   ASN B 211      -0.350   2.950 -53.075  1.00 57.06           C  
ANISOU 3245  C   ASN B 211     8762   5958   6958    341   1393   -811       C  
ATOM   3246  O   ASN B 211      -0.491   3.462 -51.968  1.00 58.64           O  
ANISOU 3246  O   ASN B 211     9121   6086   7074    377   1429   -837       O  
ATOM   3247  CB  ASN B 211      -0.480   5.317 -54.058  1.00 52.55           C  
ANISOU 3247  CB  ASN B 211     8203   5318   6447    335   1389   -827       C  
ATOM   3248  CG  ASN B 211      -0.229   6.151 -55.310  1.00 80.41           C  
ANISOU 3248  CG  ASN B 211    11635   8862  10057    297   1341   -820       C  
ATOM   3249  OD1 ASN B 211       0.926   6.316 -55.739  1.00 76.83           O  
ANISOU 3249  OD1 ASN B 211    11157   8426   9610    232   1227   -838       O  
ATOM   3250  ND2 ASN B 211      -1.302   6.533 -56.031  1.00 66.83           N  
ANISOU 3250  ND2 ASN B 211     9833   7146   8411    333   1426   -784       N  
ATOM   3251  N   THR B 212      -0.276   1.627 -53.262  1.00 54.48           N  
ANISOU 3251  N   THR B 212     8345   5700   6655    326   1381   -788       N  
ATOM   3252  CA  THR B 212      -0.368   0.660 -52.185  1.00 53.78           C  
ANISOU 3252  CA  THR B 212     8325   5610   6497    351   1408   -789       C  
ATOM   3253  C   THR B 212       1.046   0.258 -51.842  1.00 57.75           C  
ANISOU 3253  C   THR B 212     8866   6125   6952    287   1280   -820       C  
ATOM   3254  O   THR B 212       1.838  -0.050 -52.737  1.00 54.28           O  
ANISOU 3254  O   THR B 212     8317   5738   6568    229   1194   -814       O  
ATOM   3255  CB  THR B 212      -1.229  -0.529 -52.573  1.00 58.55           C  
ANISOU 3255  CB  THR B 212     8808   6276   7162    378   1479   -741       C  
ATOM   3256  OG1 THR B 212      -2.444  -0.045 -53.116  1.00 57.65           O  
ANISOU 3256  OG1 THR B 212     8636   6151   7116    426   1578   -704       O  
ATOM   3257  CG2 THR B 212      -1.551  -1.422 -51.391  1.00 59.64           C  
ANISOU 3257  CG2 THR B 212     9026   6404   7232    418   1532   -736       C  
ATOM   3258  N   LYS B 213       1.390   0.372 -50.548  1.00 57.48           N  
ANISOU 3258  N   LYS B 213     8995   6033   6812    296   1265   -850       N  
ATOM   3259  CA  LYS B 213       2.701  -0.006 -50.020  1.00 56.79           C  
ANISOU 3259  CA  LYS B 213     8962   5945   6670    237   1140   -875       C  
ATOM   3260  C   LYS B 213       2.400  -0.718 -48.706  1.00 59.83           C  
ANISOU 3260  C   LYS B 213     9464   6305   6962    275   1186   -879       C  
ATOM   3261  O   LYS B 213       1.982  -0.064 -47.764  1.00 59.20           O  
ANISOU 3261  O   LYS B 213     9543   6151   6801    318   1238   -901       O  
ATOM   3262  CB  LYS B 213       3.592   1.236 -49.874  1.00 58.36           C  
ANISOU 3262  CB  LYS B 213     9258   6081   6834    195   1046   -911       C  
ATOM   3263  CG  LYS B 213       5.083   0.966 -49.956  1.00 73.92           C  
ANISOU 3263  CG  LYS B 213    11208   8070   8809    114    894   -918       C  
ATOM   3264  CD  LYS B 213       5.888   2.222 -50.223  1.00 87.65           C  
ANISOU 3264  CD  LYS B 213    12988   9761  10554     67    800   -939       C  
ATOM   3265  CE  LYS B 213       7.343   1.912 -50.486  1.00104.04           C  
ANISOU 3265  CE  LYS B 213    15007  11863  12662    -14    655   -931       C  
ATOM   3266  NZ  LYS B 213       8.210   3.105 -50.265  1.00116.49           N  
ANISOU 3266  NZ  LYS B 213    16677  13370  14215    -62    548   -953       N  
ATOM   3267  N   VAL B 214       2.443  -2.077 -48.710  1.00 55.98           N  
ANISOU 3267  N   VAL B 214     8894   5881   6493    269   1185   -855       N  
ATOM   3268  CA  VAL B 214       2.099  -2.928 -47.551  1.00 55.42           C  
ANISOU 3268  CA  VAL B 214     8913   5798   6345    307   1235   -851       C  
ATOM   3269  C   VAL B 214       3.314  -3.719 -47.075  1.00 58.83           C  
ANISOU 3269  C   VAL B 214     9366   6250   6738    248   1115   -861       C  
ATOM   3270  O   VAL B 214       4.025  -4.292 -47.887  1.00 57.67           O  
ANISOU 3270  O   VAL B 214     9087   6164   6661    196   1041   -846       O  
ATOM   3271  CB  VAL B 214       0.941  -3.898 -47.904  1.00 58.14           C  
ANISOU 3271  CB  VAL B 214     9143   6198   6751    358   1350   -805       C  
ATOM   3272  CG1 VAL B 214       0.639  -4.862 -46.750  1.00 58.58           C  
ANISOU 3272  CG1 VAL B 214     9277   6246   6733    394   1398   -796       C  
ATOM   3273  CG2 VAL B 214      -0.301  -3.129 -48.266  1.00 58.16           C  
ANISOU 3273  CG2 VAL B 214     9130   6175   6795    419   1470   -786       C  
ATOM   3274  N   ASP B 215       3.513  -3.791 -45.761  1.00 56.72           N  
ANISOU 3274  N   ASP B 215     9264   5927   6359    259   1103   -882       N  
ATOM   3275  CA  ASP B 215       4.597  -4.554 -45.140  1.00 56.67           C  
ANISOU 3275  CA  ASP B 215     9293   5930   6307    206    992   -887       C  
ATOM   3276  C   ASP B 215       3.873  -5.593 -44.287  1.00 61.51           C  
ANISOU 3276  C   ASP B 215     9949   6554   6870    258   1080   -870       C  
ATOM   3277  O   ASP B 215       3.391  -5.262 -43.208  1.00 62.97           O  
ANISOU 3277  O   ASP B 215    10297   6672   6956    305   1141   -886       O  
ATOM   3278  CB  ASP B 215       5.516  -3.628 -44.301  1.00 58.35           C  
ANISOU 3278  CB  ASP B 215     9683   6059   6428    166    886   -926       C  
ATOM   3279  CG  ASP B 215       6.179  -2.535 -45.114  1.00 65.82           C  
ANISOU 3279  CG  ASP B 215    10591   6989   7427    117    803   -939       C  
ATOM   3280  OD1 ASP B 215       6.667  -2.829 -46.224  1.00 65.58           O  
ANISOU 3280  OD1 ASP B 215    10393   7025   7500     76    755   -917       O  
ATOM   3281  OD2 ASP B 215       6.203  -1.380 -44.645  1.00 77.94           O  
ANISOU 3281  OD2 ASP B 215    12270   8444   8901    122    790   -970       O  
ATOM   3282  N   LYS B 216       3.661  -6.799 -44.839  1.00 56.56           N  
ANISOU 3282  N   LYS B 216     9169   6006   6315    259   1104   -835       N  
ATOM   3283  CA  LYS B 216       2.869  -7.837 -44.176  1.00 55.67           C  
ANISOU 3283  CA  LYS B 216     9069   5911   6173    311   1196   -810       C  
ATOM   3284  C   LYS B 216       3.756  -8.770 -43.407  1.00 59.27           C  
ANISOU 3284  C   LYS B 216     9568   6377   6575    272   1109   -811       C  
ATOM   3285  O   LYS B 216       4.622  -9.395 -44.010  1.00 59.19           O  
ANISOU 3285  O   LYS B 216     9443   6421   6625    214   1017   -800       O  
ATOM   3286  CB  LYS B 216       2.037  -8.625 -45.211  1.00 56.40           C  
ANISOU 3286  CB  LYS B 216     8973   6078   6377    335   1274   -767       C  
ATOM   3287  CG  LYS B 216       1.155  -9.764 -44.650  1.00 57.73           C  
ANISOU 3287  CG  LYS B 216     9130   6270   6535    388   1371   -732       C  
ATOM   3288  CD  LYS B 216       0.210  -9.310 -43.505  1.00 59.39           C  
ANISOU 3288  CD  LYS B 216     9499   6410   6656    464   1489   -734       C  
ATOM   3289  CE  LYS B 216      -0.751  -8.230 -43.950  1.00 61.50           C  
ANISOU 3289  CE  LYS B 216     9764   6643   6960    513   1587   -728       C  
ATOM   3290  NZ  LYS B 216      -1.869  -8.022 -42.981  1.00 80.57           N  
ANISOU 3290  NZ  LYS B 216    12298   9002   9315    601   1731   -712       N  
ATOM   3291  N   ARG B 217       3.527  -8.901 -42.086  1.00 56.06           N  
ANISOU 3291  N   ARG B 217     9326   5919   6057    305   1143   -821       N  
ATOM   3292  CA  ARG B 217       4.313  -9.798 -41.254  1.00 54.66           C  
ANISOU 3292  CA  ARG B 217     9202   5746   5821    271   1062   -820       C  
ATOM   3293  C   ARG B 217       3.781 -11.193 -41.435  1.00 57.91           C  
ANISOU 3293  C   ARG B 217     9489   6228   6284    295   1125   -779       C  
ATOM   3294  O   ARG B 217       2.600 -11.453 -41.184  1.00 58.98           O  
ANISOU 3294  O   ARG B 217     9632   6364   6414    366   1258   -758       O  
ATOM   3295  CB  ARG B 217       4.265  -9.408 -39.763  1.00 51.05           C  
ANISOU 3295  CB  ARG B 217     8979   5202   5216    297   1073   -845       C  
ATOM   3296  CG  ARG B 217       5.094 -10.376 -38.894  1.00 64.08           C  
ANISOU 3296  CG  ARG B 217    10685   6857   6806    257    981   -840       C  
ATOM   3297  CD  ARG B 217       5.805  -9.728 -37.736  1.00 92.10           C  
ANISOU 3297  CD  ARG B 217    14454  10316  10223    228    891   -874       C  
ATOM   3298  NE  ARG B 217       6.828  -8.772 -38.160  1.00105.74           N  
ANISOU 3298  NE  ARG B 217    16192  12014  11971    158    757   -897       N  
ATOM   3299  CZ  ARG B 217       7.597  -8.081 -37.322  1.00124.20           C  
ANISOU 3299  CZ  ARG B 217    18709  14270  14210    117    649   -926       C  
ATOM   3300  NH1 ARG B 217       7.474  -8.241 -36.006  1.00112.85           N  
ANISOU 3300  NH1 ARG B 217    17466  12772  12640    139    658   -938       N  
ATOM   3301  NH2 ARG B 217       8.500  -7.226 -37.791  1.00111.74           N  
ANISOU 3301  NH2 ARG B 217    17121  12667  12666     53    528   -940       N  
ATOM   3302  N   VAL B 218       4.662 -12.101 -41.833  1.00 51.84           N  
ANISOU 3302  N   VAL B 218     8612   5517   5569    238   1030   -765       N  
ATOM   3303  CA  VAL B 218       4.319 -13.501 -42.058  1.00 47.91           C  
ANISOU 3303  CA  VAL B 218     7991   5087   5124    251   1070   -727       C  
ATOM   3304  C   VAL B 218       4.735 -14.313 -40.833  1.00 52.42           C  
ANISOU 3304  C   VAL B 218     8665   5645   5610    244   1033   -724       C  
ATOM   3305  O   VAL B 218       3.952 -15.133 -40.348  1.00 52.07           O  
ANISOU 3305  O   VAL B 218     8623   5615   5548    292   1121   -700       O  
ATOM   3306  CB  VAL B 218       4.998 -14.006 -43.364  1.00 47.22           C  
ANISOU 3306  CB  VAL B 218     7715   5072   5155    197    998   -712       C  
ATOM   3307  CG1 VAL B 218       4.562 -15.428 -43.694  1.00 44.23           C  
ANISOU 3307  CG1 VAL B 218     7209   4760   4835    213   1044   -674       C  
ATOM   3308  CG2 VAL B 218       4.707 -13.058 -44.524  1.00 46.18           C  
ANISOU 3308  CG2 VAL B 218     7505   4945   5096    198   1021   -719       C  
ATOM   3309  N   GLU B 219       5.977 -14.149 -40.367  1.00 50.74           N  
ANISOU 3309  N   GLU B 219     8524   5404   5351    181    898   -742       N  
ATOM   3310  CA  GLU B 219       6.441 -14.921 -39.190  1.00 52.69           C  
ANISOU 3310  CA  GLU B 219     8872   5634   5515    168    850   -736       C  
ATOM   3311  C   GLU B 219       7.172 -14.031 -38.134  1.00 58.28           C  
ANISOU 3311  C   GLU B 219     9785   6254   6105    136    757   -769       C  
ATOM   3312  O   GLU B 219       8.051 -13.248 -38.507  1.00 56.30           O  
ANISOU 3312  O   GLU B 219     9536   5981   5874     80    651   -786       O  
ATOM   3313  CB  GLU B 219       7.314 -16.122 -39.649  1.00 52.94           C  
ANISOU 3313  CB  GLU B 219     8758   5734   5625    114    764   -707       C  
ATOM   3314  CG  GLU B 219       7.308 -17.277 -38.676  1.00 66.27           C  
ANISOU 3314  CG  GLU B 219    10490   7430   7258    124    768   -686       C  
ATOM   3315  CD  GLU B 219       6.140 -18.227 -38.837  1.00 86.63           C  
ANISOU 3315  CD  GLU B 219    12985  10057   9872    187    901   -657       C  
ATOM   3316  OE1 GLU B 219       5.040 -17.775 -39.225  1.00 77.05           O  
ANISOU 3316  OE1 GLU B 219    11754   8842   8679    243   1017   -657       O  
ATOM   3317  OE2 GLU B 219       6.324 -19.432 -38.559  1.00 91.44           O  
ANISOU 3317  OE2 GLU B 219    13547  10704  10492    179    886   -631       O  
ATOM   3318  N   SER B 220       6.785 -14.155 -36.825  1.00 57.40           N  
ANISOU 3318  N   SER B 220     9851   6090   5869    173    798   -777       N  
ATOM   3319  CA  SER B 220       7.371 -13.362 -35.715  1.00 59.64           C  
ANISOU 3319  CA  SER B 220    10357   6280   6023    148    716   -808       C  
ATOM   3320  C   SER B 220       8.442 -14.161 -34.922  1.00 64.37           C  
ANISOU 3320  C   SER B 220    11007   6875   6577     86    582   -795       C  
ATOM   3321  O   SER B 220       8.689 -15.313 -35.256  1.00 60.62           O  
ANISOU 3321  O   SER B 220    10389   6470   6174     69    567   -761       O  
ATOM   3322  CB  SER B 220       6.254 -12.907 -34.765  1.00 63.54           C  
ANISOU 3322  CB  SER B 220    11035   6709   6400    231    851   -825       C  
ATOM   3323  OG  SER B 220       5.279 -12.136 -35.449  1.00 71.85           O  
ANISOU 3323  OG  SER B 220    12044   7760   7497    288    973   -832       O  
ATOM   3324  N   LYS B 221       9.041 -13.561 -33.844  1.00 65.99           N  
ANISOU 3324  N   LYS B 221    11423   6993   6659     54    488   -819       N  
ATOM   3325  CA  LYS B 221      10.011 -14.242 -32.959  1.00 66.55           C  
ANISOU 3325  CA  LYS B 221    11566   7045   6673     -4    357   -803       C  
ATOM   3326  C   LYS B 221       9.268 -15.070 -31.863  1.00 75.47           C  
ANISOU 3326  C   LYS B 221    12809   8166   7701     54    452   -793       C  
ATOM   3327  O   LYS B 221       8.038 -15.052 -31.856  1.00 75.47           O  
ANISOU 3327  O   LYS B 221    12820   8171   7683    139    617   -796       O  
ATOM   3328  CB  LYS B 221      11.057 -13.276 -32.417  1.00 69.42           C  
ANISOU 3328  CB  LYS B 221    12088   7322   6966    -76    194   -826       C  
ATOM   3329  CG  LYS B 221      11.860 -12.589 -33.509  1.00 74.65           C  
ANISOU 3329  CG  LYS B 221    12620   8000   7742   -137     96   -825       C  
ATOM   3330  CD  LYS B 221      13.018 -11.760 -32.919  1.00 86.23           C  
ANISOU 3330  CD  LYS B 221    14234   9380   9148   -219    -87   -836       C  
ATOM   3331  CE  LYS B 221      13.110 -10.345 -33.452  1.00102.11           C  
ANISOU 3331  CE  LYS B 221    16278  11344  11175   -232   -112   -867       C  
ATOM   3332  NZ  LYS B 221      13.801  -9.426 -32.497  1.00108.88           N  
ANISOU 3332  NZ  LYS B 221    17363  12088  11917   -285   -250   -890       N  
ATOM   3333  N   TYR B 222       9.990 -15.746 -30.919  1.00 76.57           N  
ANISOU 3333  N   TYR B 222    13034   8285   7773     11    349   -778       N  
ATOM   3334  CA  TYR B 222       9.438 -16.771 -29.995  1.00 78.35           C  
ANISOU 3334  CA  TYR B 222    13326   8518   7924     56    424   -758       C  
ATOM   3335  C   TYR B 222       8.856 -16.468 -28.526  1.00 85.42           C  
ANISOU 3335  C   TYR B 222    14501   9322   8632    107    486   -779       C  
ATOM   3336  O   TYR B 222       8.516 -17.450 -27.852  1.00 87.07           O  
ANISOU 3336  O   TYR B 222    14738   9548   8797    137    536   -755       O  
ATOM   3337  CB  TYR B 222      10.540 -17.856 -29.766  1.00 79.50           C  
ANISOU 3337  CB  TYR B 222    13402   8700   8106    -19    281   -721       C  
ATOM   3338  CG  TYR B 222      10.438 -19.051 -30.683  1.00 81.09           C  
ANISOU 3338  CG  TYR B 222    13353   9009   8451    -14    323   -682       C  
ATOM   3339  CD1 TYR B 222       9.266 -19.793 -30.761  1.00 83.13           C  
ANISOU 3339  CD1 TYR B 222    13547   9315   8725     65    486   -666       C  
ATOM   3340  CD2 TYR B 222      11.554 -19.535 -31.352  1.00 81.96           C  
ANISOU 3340  CD2 TYR B 222    13303   9165   8673    -89    195   -654       C  
ATOM   3341  CE1 TYR B 222       9.170 -20.912 -31.583  1.00 83.46           C  
ANISOU 3341  CE1 TYR B 222    13370   9449   8893     67    518   -630       C  
ATOM   3342  CE2 TYR B 222      11.473 -20.649 -32.184  1.00 82.67           C  
ANISOU 3342  CE2 TYR B 222    13176   9347   8887    -83    235   -620       C  
ATOM   3343  CZ  TYR B 222      10.275 -21.336 -32.304  1.00 91.86           C  
ANISOU 3343  CZ  TYR B 222    14282  10557  10063     -6    394   -610       C  
ATOM   3344  OH  TYR B 222      10.176 -22.449 -33.114  1.00 93.99           O  
ANISOU 3344  OH  TYR B 222    14349  10912  10451     -1    429   -577       O  
ATOM   3345  N   GLY B 223       8.853 -15.290 -27.935  1.00 80.97           N  
ANISOU 3345  N   GLY B 223    14150   8661   7953    113    469   -820       N  
ATOM   3346  CA  GLY B 223       8.954 -13.954 -28.454  1.00 79.36           C  
ANISOU 3346  CA  GLY B 223    13979   8413   7761    101    447   -856       C  
ATOM   3347  C   GLY B 223       7.659 -13.265 -28.029  1.00 80.08           C  
ANISOU 3347  C   GLY B 223    14220   8448   7760    204    629   -882       C  
ATOM   3348  O   GLY B 223       6.771 -13.125 -28.878  1.00 78.85           O  
ANISOU 3348  O   GLY B 223    13928   8338   7693    263    765   -876       O  
ATOM   3349  N   PRO B 224       7.456 -12.897 -26.715  1.00 75.30           N  
ANISOU 3349  N   PRO B 224    13892   7743   6977    233    649   -905       N  
ATOM   3350  CA  PRO B 224       6.203 -12.189 -26.299  1.00 73.98           C  
ANISOU 3350  CA  PRO B 224    13874   7514   6720    339    837   -927       C  
ATOM   3351  C   PRO B 224       5.857 -11.058 -27.260  1.00 71.01           C  
ANISOU 3351  C   PRO B 224    13431   7132   6419    357    885   -951       C  
ATOM   3352  O   PRO B 224       6.785 -10.382 -27.695  1.00 68.71           O  
ANISOU 3352  O   PRO B 224    13124   6822   6159    279    736   -972       O  
ATOM   3353  CB  PRO B 224       6.514 -11.659 -24.882  1.00 77.63           C  
ANISOU 3353  CB  PRO B 224    14663   7852   6980    333    780   -960       C  
ATOM   3354  CG  PRO B 224       7.991 -11.821 -24.707  1.00 83.08           C  
ANISOU 3354  CG  PRO B 224    15367   8532   7666    212    539   -960       C  
ATOM   3355  CD  PRO B 224       8.384 -13.003 -25.573  1.00 78.17           C  
ANISOU 3355  CD  PRO B 224    14455   8036   7210    170    496   -913       C  
ATOM   3356  N   PRO B 225       4.609 -10.933 -27.754  1.00 66.36           N  
ANISOU 3356  N   PRO B 225    12758   6569   5885    450   1077   -939       N  
ATOM   3357  CA  PRO B 225       3.361 -11.542 -27.262  1.00 67.27           C  
ANISOU 3357  CA  PRO B 225    12897   6694   5969    554   1276   -909       C  
ATOM   3358  C   PRO B 225       3.003 -12.960 -27.739  1.00 72.32           C  
ANISOU 3358  C   PRO B 225    13307   7446   6726    566   1329   -854       C  
ATOM   3359  O   PRO B 225       1.887 -13.412 -27.473  1.00 70.70           O  
ANISOU 3359  O   PRO B 225    13094   7251   6516    655   1501   -822       O  
ATOM   3360  CB  PRO B 225       2.302 -10.520 -27.697  1.00 68.82           C  
ANISOU 3360  CB  PRO B 225    13103   6856   6188    636   1435   -919       C  
ATOM   3361  CG  PRO B 225       2.850  -9.986 -28.988  1.00 71.32           C  
ANISOU 3361  CG  PRO B 225    13241   7220   6639    571   1337   -931       C  
ATOM   3362  CD  PRO B 225       4.324  -9.870 -28.739  1.00 67.11           C  
ANISOU 3362  CD  PRO B 225    12774   6662   6062    461   1113   -958       C  
ATOM   3363  N   CYS B 226       3.932 -13.685 -28.354  1.00 71.54           N  
ANISOU 3363  N   CYS B 226    13035   7423   6724    481   1187   -839       N  
ATOM   3364  CA  CYS B 226       3.657 -15.055 -28.770  1.00 73.40           C  
ANISOU 3364  CA  CYS B 226    13067   7759   7064    489   1227   -789       C  
ATOM   3365  C   CYS B 226       3.754 -15.957 -27.544  1.00 79.88           C  
ANISOU 3365  C   CYS B 226    14018   8560   7774    498   1223   -772       C  
ATOM   3366  O   CYS B 226       4.788 -15.910 -26.880  1.00 79.79           O  
ANISOU 3366  O   CYS B 226    14136   8505   7677    430   1073   -791       O  
ATOM   3367  CB  CYS B 226       4.643 -15.479 -29.851  1.00 74.00           C  
ANISOU 3367  CB  CYS B 226    12926   7915   7277    399   1082   -780       C  
ATOM   3368  SG  CYS B 226       4.483 -14.537 -31.388  1.00 78.16           S  
ANISOU 3368  SG  CYS B 226    13279   8474   7942    391   1095   -794       S  
ATOM   3369  N   PRO B 227       2.733 -16.777 -27.190  1.00 78.65           N  
ANISOU 3369  N   PRO B 227    13836   8430   7616    577   1377   -732       N  
ATOM   3370  CA  PRO B 227       2.879 -17.637 -25.994  1.00 80.13           C  
ANISOU 3370  CA  PRO B 227    14154   8597   7694    582   1367   -715       C  
ATOM   3371  C   PRO B 227       4.144 -18.514 -26.019  1.00 84.68           C  
ANISOU 3371  C   PRO B 227    14651   9221   8303    482   1180   -706       C  
ATOM   3372  O   PRO B 227       4.664 -18.804 -27.104  1.00 83.15           O  
ANISOU 3372  O   PRO B 227    14245   9101   8249    426   1100   -696       O  
ATOM   3373  CB  PRO B 227       1.585 -18.453 -25.970  1.00 81.66           C  
ANISOU 3373  CB  PRO B 227    14258   8835   7934    676   1560   -663       C  
ATOM   3374  CG  PRO B 227       0.600 -17.607 -26.729  1.00 85.39           C  
ANISOU 3374  CG  PRO B 227    14663   9303   8477    740   1697   -663       C  
ATOM   3375  CD  PRO B 227       1.404 -16.950 -27.812  1.00 79.55           C  
ANISOU 3375  CD  PRO B 227    13810   8588   7827    663   1564   -696       C  
ATOM   3376  N   PRO B 228       4.712 -18.893 -24.851  1.00 83.06           N  
ANISOU 3376  N   PRO B 228    14620   8969   7970    454   1100   -707       N  
ATOM   3377  CA  PRO B 228       5.975 -19.662 -24.872  1.00 82.91           C  
ANISOU 3377  CA  PRO B 228    14525   8989   7989    354    912   -694       C  
ATOM   3378  C   PRO B 228       5.894 -21.100 -25.407  1.00 85.55           C  
ANISOU 3378  C   PRO B 228    14625   9430   8451    349    930   -643       C  
ATOM   3379  O   PRO B 228       6.941 -21.645 -25.747  1.00 83.52           O  
ANISOU 3379  O   PRO B 228    14257   9215   8264    267    782   -631       O  
ATOM   3380  CB  PRO B 228       6.428 -19.640 -23.396  1.00 85.93           C  
ANISOU 3380  CB  PRO B 228    15177   9283   8189    336    840   -705       C  
ATOM   3381  CG  PRO B 228       5.539 -18.638 -22.718  1.00 90.79           C  
ANISOU 3381  CG  PRO B 228    16021   9805   8669    418    974   -736       C  
ATOM   3382  CD  PRO B 228       4.265 -18.659 -23.464  1.00 85.30           C  
ANISOU 3382  CD  PRO B 228    15178   9160   8071    510   1173   -717       C  
ATOM   3383  N   CYS B 229       4.661 -21.685 -25.475  1.00 83.80           N  
ANISOU 3383  N   CYS B 229    14331   9246   8263    438   1111   -611       N  
ATOM   3384  CA  CYS B 229       4.260 -23.059 -25.881  1.00130.77           C  
ANISOU 3384  CA  CYS B 229    20079  15288  14321    456   1169   -560       C  
ATOM   3385  C   CYS B 229       4.119 -23.944 -24.638  1.00175.36           C  
ANISOU 3385  C   CYS B 229    25852  20915  19862    480   1197   -532       C  
ATOM   3386  O   CYS B 229       3.228 -23.716 -23.817  1.00142.89           O  
ANISOU 3386  O   CYS B 229    21892  16751  15648    561   1335   -528       O  
ATOM   3387  CB  CYS B 229       5.157 -23.707 -26.943  1.00129.87           C  
ANISOU 3387  CB  CYS B 229    19736  15255  14353    375   1040   -547       C  
ATOM   3388  SG  CYS B 229       4.594 -23.464 -28.651  1.00132.38           S  
ANISOU 3388  SG  CYS B 229    19800  15647  14852    392   1111   -542       S  
ATOM   3389  N   GLU B 233      10.238 -25.563 -23.534  1.00120.58           N  
ANISOU 3389  N   GLU B 233    18934  13966  12913     39    315   -508       N  
ATOM   3390  CA  GLU B 233      11.683 -25.393 -23.642  1.00120.68           C  
ANISOU 3390  CA  GLU B 233    18929  13963  12961    -67    105   -502       C  
ATOM   3391  C   GLU B 233      12.035 -24.319 -24.669  1.00124.73           C  
ANISOU 3391  C   GLU B 233    19364  14472  13555    -97     61   -531       C  
ATOM   3392  O   GLU B 233      11.260 -24.063 -25.592  1.00124.18           O  
ANISOU 3392  O   GLU B 233    19173  14446  13564    -44    185   -545       O  
ATOM   3393  CB  GLU B 233      12.356 -26.717 -24.009  1.00121.33           C  
ANISOU 3393  CB  GLU B 233    18814  14122  13165   -114     32   -451       C  
ATOM   3394  N   PHE B 234      13.227 -23.720 -24.516  1.00121.00           N  
ANISOU 3394  N   PHE B 234    18956  13948  13069   -185   -122   -535       N  
ATOM   3395  CA  PHE B 234      13.717 -22.613 -25.346  1.00119.84           C  
ANISOU 3395  CA  PHE B 234    18763  13783  12986   -224   -188   -560       C  
ATOM   3396  C   PHE B 234      14.803 -23.032 -26.379  1.00121.13           C  
ANISOU 3396  C   PHE B 234    18690  14009  13324   -298   -306   -523       C  
ATOM   3397  O   PHE B 234      15.001 -24.233 -26.594  1.00119.64           O  
ANISOU 3397  O   PHE B 234    18350  13888  13218   -304   -304   -481       O  
ATOM   3398  CB  PHE B 234      14.238 -21.517 -24.406  1.00122.92           C  
ANISOU 3398  CB  PHE B 234    19412  14058  13234   -268   -308   -589       C  
ATOM   3399  N   LEU B 235      15.441 -22.028 -27.075  1.00116.22           N  
ANISOU 3399  N   LEU B 235    18031  13366  12762   -347   -394   -537       N  
ATOM   3400  CA  LEU B 235      16.523 -22.190 -28.071  1.00114.36           C  
ANISOU 3400  CA  LEU B 235    17590  13175  12688   -417   -507   -501       C  
ATOM   3401  C   LEU B 235      16.040 -22.634 -29.483  1.00114.70           C  
ANISOU 3401  C   LEU B 235    17384  13316  12882   -374   -386   -495       C  
ATOM   3402  O   LEU B 235      16.871 -22.778 -30.380  1.00114.16           O  
ANISOU 3402  O   LEU B 235    17144  13286  12947   -422   -460   -467       O  
ATOM   3403  CB  LEU B 235      17.623 -23.162 -27.546  1.00114.69           C  
ANISOU 3403  CB  LEU B 235    17598  13221  12760   -489   -655   -444       C  
ATOM   3404  CG  LEU B 235      19.087 -22.708 -27.618  1.00119.68           C  
ANISOU 3404  CG  LEU B 235    18211  13810  13452   -593   -862   -410       C  
ATOM   3405  CD1 LEU B 235      19.994 -23.740 -26.966  1.00119.85           C  
ANISOU 3405  CD1 LEU B 235    18213  13832  13493   -654   -989   -349       C  
ATOM   3406  CD2 LEU B 235      19.541 -22.441 -29.047  1.00121.08           C  
ANISOU 3406  CD2 LEU B 235    18167  14039  13798   -612   -867   -396       C  
ATOM   3407  N   GLY B 236      14.735 -22.859 -29.672  1.00108.09           N  
ANISOU 3407  N   GLY B 236    16530  12516  12024   -286   -207   -517       N  
ATOM   3408  CA  GLY B 236      14.194 -23.371 -30.929  1.00104.90           C  
ANISOU 3408  CA  GLY B 236    15906  12200  11751   -245    -94   -509       C  
ATOM   3409  C   GLY B 236      14.028 -24.882 -30.895  1.00104.32           C  
ANISOU 3409  C   GLY B 236    15718  12193  11727   -227    -49   -470       C  
ATOM   3410  O   GLY B 236      13.034 -25.414 -31.399  1.00103.58           O  
ANISOU 3410  O   GLY B 236    15530  12153  11672   -163     92   -471       O  
ATOM   3411  N   GLY B 237      15.005 -25.565 -30.297  1.00 97.43           N  
ANISOU 3411  N   GLY B 237    14854  11311  10853   -286   -174   -433       N  
ATOM   3412  CA  GLY B 237      15.021 -27.010 -30.136  1.00 94.78           C  
ANISOU 3412  CA  GLY B 237    14424  11029  10559   -279   -156   -392       C  
ATOM   3413  C   GLY B 237      16.402 -27.581 -30.403  1.00 93.60           C  
ANISOU 3413  C   GLY B 237    14155  10897  10512   -358   -304   -344       C  
ATOM   3414  O   GLY B 237      17.172 -26.978 -31.160  1.00 91.56           O  
ANISOU 3414  O   GLY B 237    13817  10636  10337   -404   -380   -340       O  
ATOM   3415  N   PRO B 238      16.764 -28.748 -29.815  1.00 88.24           N  
ANISOU 3415  N   PRO B 238    13455  10235   9836   -376   -345   -302       N  
ATOM   3416  CA  PRO B 238      18.083 -29.335 -30.128  1.00 86.88           C  
ANISOU 3416  CA  PRO B 238    13153  10080   9777   -448   -478   -248       C  
ATOM   3417  C   PRO B 238      18.193 -29.770 -31.592  1.00 85.98           C  
ANISOU 3417  C   PRO B 238    12804  10039   9824   -437   -424   -234       C  
ATOM   3418  O   PRO B 238      17.185 -30.135 -32.197  1.00 84.19           O  
ANISOU 3418  O   PRO B 238    12504   9864   9622   -372   -282   -253       O  
ATOM   3419  CB  PRO B 238      18.207 -30.530 -29.157  1.00 89.00           C  
ANISOU 3419  CB  PRO B 238    13457  10354  10006   -455   -507   -210       C  
ATOM   3420  CG  PRO B 238      17.036 -30.467 -28.251  1.00 94.01           C  
ANISOU 3420  CG  PRO B 238    14260  10966  10495   -392   -401   -245       C  
ATOM   3421  CD  PRO B 238      15.992 -29.608 -28.894  1.00 89.58           C  
ANISOU 3421  CD  PRO B 238    13706  10411   9918   -329   -268   -296       C  
ATOM   3422  N   SER B 239      19.407 -29.696 -32.165  1.00 81.02           N  
ANISOU 3422  N   SER B 239    12066   9411   9307   -500   -537   -196       N  
ATOM   3423  CA  SER B 239      19.656 -30.101 -33.558  1.00 79.47           C  
ANISOU 3423  CA  SER B 239    11655   9276   9262   -493   -492   -178       C  
ATOM   3424  C   SER B 239      20.407 -31.438 -33.635  1.00 78.47           C  
ANISOU 3424  C   SER B 239    11397   9186   9232   -517   -535   -116       C  
ATOM   3425  O   SER B 239      21.398 -31.645 -32.931  1.00 75.45           O  
ANISOU 3425  O   SER B 239    11046   8768   8853   -577   -667    -71       O  
ATOM   3426  CB  SER B 239      20.421 -29.016 -34.311  1.00 84.53           C  
ANISOU 3426  CB  SER B 239    12251   9894   9971   -535   -564   -177       C  
ATOM   3427  OG  SER B 239      19.535 -27.977 -34.691  1.00 98.46           O  
ANISOU 3427  OG  SER B 239    14075  11650  11685   -494   -479   -236       O  
ATOM   3428  N   VAL B 240      19.927 -32.333 -34.515  1.00 74.25           N  
ANISOU 3428  N   VAL B 240    10716   8718   8778   -472   -425   -113       N  
ATOM   3429  CA  VAL B 240      20.496 -33.670 -34.706  1.00 72.17           C  
ANISOU 3429  CA  VAL B 240    10319   8493   8609   -483   -440    -59       C  
ATOM   3430  C   VAL B 240      21.203 -33.751 -36.055  1.00 72.88           C  
ANISOU 3430  C   VAL B 240    10230   8613   8848   -495   -439    -33       C  
ATOM   3431  O   VAL B 240      20.629 -33.377 -37.089  1.00 69.30           O  
ANISOU 3431  O   VAL B 240     9714   8188   8428   -458   -346    -68       O  
ATOM   3432  CB  VAL B 240      19.408 -34.766 -34.592  1.00 74.67           C  
ANISOU 3432  CB  VAL B 240    10617   8856   8898   -421   -318    -70       C  
ATOM   3433  CG1 VAL B 240      20.026 -36.169 -34.725  1.00 73.84           C  
ANISOU 3433  CG1 VAL B 240    10384   8785   8888   -434   -338    -14       C  
ATOM   3434  CG2 VAL B 240      18.636 -34.633 -33.274  1.00 75.12           C  
ANISOU 3434  CG2 VAL B 240    10857   8881   8804   -400   -302    -94       C  
ATOM   3435  N   PHE B 241      22.431 -34.296 -36.032  1.00 70.35           N  
ANISOU 3435  N   PHE B 241     9825   8285   8619   -545   -538     31       N  
ATOM   3436  CA  PHE B 241      23.256 -34.530 -37.215  1.00 70.58           C  
ANISOU 3436  CA  PHE B 241     9682   8338   8797   -557   -540     71       C  
ATOM   3437  C   PHE B 241      23.725 -35.996 -37.249  1.00 70.96           C  
ANISOU 3437  C   PHE B 241     9617   8416   8928   -556   -537    126       C  
ATOM   3438  O   PHE B 241      24.464 -36.463 -36.364  1.00 70.10           O  
ANISOU 3438  O   PHE B 241     9530   8281   8823   -600   -639    177       O  
ATOM   3439  CB  PHE B 241      24.434 -33.551 -37.242  1.00 74.08           C  
ANISOU 3439  CB  PHE B 241    10125   8732   9289   -622   -669    105       C  
ATOM   3440  CG  PHE B 241      23.951 -32.122 -37.379  1.00 77.12           C  
ANISOU 3440  CG  PHE B 241    10608   9091   9604   -618   -660     48       C  
ATOM   3441  CD1 PHE B 241      23.426 -31.659 -38.585  1.00 80.55           C  
ANISOU 3441  CD1 PHE B 241    10972   9558  10077   -578   -558     10       C  
ATOM   3442  CD2 PHE B 241      23.937 -31.266 -36.283  1.00 80.56           C  
ANISOU 3442  CD2 PHE B 241    11215   9467   9926   -651   -748     30       C  
ATOM   3443  CE1 PHE B 241      22.980 -30.340 -38.714  1.00 81.75           C  
ANISOU 3443  CE1 PHE B 241    11209   9683  10169   -574   -550    -40       C  
ATOM   3444  CE2 PHE B 241      23.484 -29.950 -36.411  1.00 83.97           C  
ANISOU 3444  CE2 PHE B 241    11739   9871  10294   -645   -737    -23       C  
ATOM   3445  CZ  PHE B 241      23.010 -29.495 -37.626  1.00 81.63           C  
ANISOU 3445  CZ  PHE B 241    11359   9609  10047   -607   -637    -56       C  
ATOM   3446  N   LEU B 242      23.263 -36.711 -38.280  1.00 65.08           N  
ANISOU 3446  N   LEU B 242     8757   7724   8248   -507   -421    116       N  
ATOM   3447  CA  LEU B 242      23.515 -38.132 -38.496  1.00 64.19           C  
ANISOU 3447  CA  LEU B 242     8534   7643   8213   -493   -390    158       C  
ATOM   3448  C   LEU B 242      24.545 -38.304 -39.628  1.00 68.81           C  
ANISOU 3448  C   LEU B 242     8964   8234   8946   -505   -396    206       C  
ATOM   3449  O   LEU B 242      24.277 -37.951 -40.779  1.00 66.33           O  
ANISOU 3449  O   LEU B 242     8590   7941   8673   -476   -318    179       O  
ATOM   3450  CB  LEU B 242      22.166 -38.796 -38.837  1.00 62.84           C  
ANISOU 3450  CB  LEU B 242     8360   7518   8000   -427   -253    110       C  
ATOM   3451  CG  LEU B 242      22.092 -40.304 -38.907  1.00 65.08           C  
ANISOU 3451  CG  LEU B 242     8561   7834   8333   -403   -207    140       C  
ATOM   3452  CD1 LEU B 242      22.576 -40.950 -37.632  1.00 64.13           C  
ANISOU 3452  CD1 LEU B 242     8490   7694   8184   -436   -293    184       C  
ATOM   3453  CD2 LEU B 242      20.661 -40.747 -39.190  1.00 65.69           C  
ANISOU 3453  CD2 LEU B 242     8651   7948   8359   -342    -82     90       C  
ATOM   3454  N   PHE B 243      25.742 -38.813 -39.274  1.00 68.25           N  
ANISOU 3454  N   PHE B 243     8834   8143   8956   -549   -489    281       N  
ATOM   3455  CA  PHE B 243      26.868 -38.993 -40.194  1.00 69.21           C  
ANISOU 3455  CA  PHE B 243     8810   8262   9226   -563   -503    343       C  
ATOM   3456  C   PHE B 243      27.032 -40.461 -40.729  1.00 72.69           C  
ANISOU 3456  C   PHE B 243     9129   8734   9756   -529   -430    378       C  
ATOM   3457  O   PHE B 243      26.906 -41.414 -39.951  1.00 71.18           O  
ANISOU 3457  O   PHE B 243     8956   8549   9540   -529   -444    396       O  
ATOM   3458  CB  PHE B 243      28.168 -38.552 -39.504  1.00 72.35           C  
ANISOU 3458  CB  PHE B 243     9210   8607   9673   -635   -657    416       C  
ATOM   3459  CG  PHE B 243      28.136 -37.097 -39.110  1.00 75.28           C  
ANISOU 3459  CG  PHE B 243     9693   8939   9970   -672   -734    385       C  
ATOM   3460  CD1 PHE B 243      28.326 -36.101 -40.058  1.00 79.11           C  
ANISOU 3460  CD1 PHE B 243    10138   9419  10502   -671   -715    373       C  
ATOM   3461  CD2 PHE B 243      27.783 -36.719 -37.823  1.00 78.62           C  
ANISOU 3461  CD2 PHE B 243    10274   9331  10266   -699   -811    361       C  
ATOM   3462  CE1 PHE B 243      28.225 -34.755 -39.710  1.00 80.59           C  
ANISOU 3462  CE1 PHE B 243    10433   9569  10618   -702   -781    341       C  
ATOM   3463  CE2 PHE B 243      27.690 -35.370 -37.474  1.00 82.22           C  
ANISOU 3463  CE2 PHE B 243    10847   9747  10646   -729   -875    328       C  
ATOM   3464  CZ  PHE B 243      27.913 -34.398 -38.418  1.00 80.25           C  
ANISOU 3464  CZ  PHE B 243    10549   9492  10450   -730   -861    318       C  
ATOM   3465  N   PRO B 244      27.374 -40.634 -42.033  1.00 67.99           N  
ANISOU 3465  N   PRO B 244     8413   8154   9264   -503   -357    393       N  
ATOM   3466  CA  PRO B 244      27.630 -41.982 -42.555  1.00 67.62           C  
ANISOU 3466  CA  PRO B 244     8258   8129   9306   -472   -292    430       C  
ATOM   3467  C   PRO B 244      29.019 -42.531 -42.184  1.00 72.00           C  
ANISOU 3467  C   PRO B 244     8728   8654   9974   -511   -379    530       C  
ATOM   3468  O   PRO B 244      29.829 -41.816 -41.585  1.00 71.00           O  
ANISOU 3468  O   PRO B 244     8621   8490   9867   -567   -497    574       O  
ATOM   3469  CB  PRO B 244      27.479 -41.810 -44.069  1.00 68.68           C  
ANISOU 3469  CB  PRO B 244     8317   8282   9497   -429   -184    406       C  
ATOM   3470  CG  PRO B 244      27.697 -40.371 -44.340  1.00 73.18           C  
ANISOU 3470  CG  PRO B 244     8917   8832  10057   -454   -223    391       C  
ATOM   3471  CD  PRO B 244      27.624 -39.604 -43.062  1.00 69.41           C  
ANISOU 3471  CD  PRO B 244     8555   8328   9489   -501   -334    382       C  
ATOM   3472  N   PRO B 245      29.316 -43.813 -42.502  1.00 69.64           N  
ANISOU 3472  N   PRO B 245     8336   8369   9755   -485   -327    571       N  
ATOM   3473  CA  PRO B 245      30.645 -44.344 -42.171  1.00 71.49           C  
ANISOU 3473  CA  PRO B 245     8482   8573  10110   -521   -405    673       C  
ATOM   3474  C   PRO B 245      31.760 -43.734 -43.032  1.00 81.28           C  
ANISOU 3474  C   PRO B 245     9619   9786  11478   -534   -418    734       C  
ATOM   3475  O   PRO B 245      31.580 -43.540 -44.232  1.00 79.94           O  
ANISOU 3475  O   PRO B 245     9401   9631  11341   -492   -316    709       O  
ATOM   3476  CB  PRO B 245      30.492 -45.864 -42.367  1.00 72.30           C  
ANISOU 3476  CB  PRO B 245     8519   8698  10252   -479   -326    689       C  
ATOM   3477  CG  PRO B 245      29.064 -46.097 -42.704  1.00 74.77           C  
ANISOU 3477  CG  PRO B 245     8897   9051  10461   -428   -221    596       C  
ATOM   3478  CD  PRO B 245      28.487 -44.829 -43.180  1.00 69.50           C  
ANISOU 3478  CD  PRO B 245     8290   8389   9728   -424   -199    531       C  
ATOM   3479  N   LYS B 246      32.887 -43.371 -42.387  1.00 84.45           N  
ANISOU 3479  N   LYS B 246     9994  10145  11948   -595   -548    817       N  
ATOM   3480  CA  LYS B 246      34.088 -42.795 -43.023  1.00 87.09           C  
ANISOU 3480  CA  LYS B 246    10224  10446  12420   -618   -581    896       C  
ATOM   3481  C   LYS B 246      35.260 -43.009 -42.013  1.00 99.50           C  
ANISOU 3481  C   LYS B 246    11758  11973  14073   -684   -731   1005       C  
ATOM   3482  O   LYS B 246      35.555 -44.192 -41.822  1.00 98.37           O  
ANISOU 3482  O   LYS B 246    11553  11834  13989   -671   -713   1053       O  
ATOM   3483  CB  LYS B 246      33.851 -41.355 -43.515  1.00 87.88           C  
ANISOU 3483  CB  LYS B 246    10371  10541  12478   -626   -584    848       C  
ATOM   3484  N   PRO B 247      35.889 -42.047 -41.266  1.00104.02           N  
ANISOU 3484  N   PRO B 247    12373  12502  14648   -757   -883   1047       N  
ATOM   3485  CA  PRO B 247      35.786 -40.574 -41.272  1.00105.82           C  
ANISOU 3485  CA  PRO B 247    12677  12709  14821   -791   -944   1011       C  
ATOM   3486  C   PRO B 247      36.818 -39.954 -42.240  1.00113.21           C  
ANISOU 3486  C   PRO B 247    13486  13619  15908   -799   -942   1085       C  
ATOM   3487  O   PRO B 247      36.459 -39.573 -43.353  1.00112.24           O  
ANISOU 3487  O   PRO B 247    13334  13520  15792   -751   -828   1040       O  
ATOM   3488  CB  PRO B 247      36.023 -40.215 -39.789  1.00108.61           C  
ANISOU 3488  CB  PRO B 247    13140  13021  15105   -867  -1119   1034       C  
ATOM   3489  CG  PRO B 247      36.810 -41.406 -39.191  1.00113.36           C  
ANISOU 3489  CG  PRO B 247    13663  13608  15799   -889  -1176   1131       C  
ATOM   3490  CD  PRO B 247      36.928 -42.452 -40.295  1.00107.84           C  
ANISOU 3490  CD  PRO B 247    12821  12944  15211   -819  -1024   1154       C  
ATOM   3491  N   LYS B 248      38.102 -39.891 -41.829  1.00113.02           N  
ANISOU 3491  N   LYS B 248    13384  13545  16012   -858  -1066   1205       N  
ATOM   3492  CA  LYS B 248      39.215 -39.367 -42.625  1.00113.99           C  
ANISOU 3492  CA  LYS B 248    13376  13636  16299   -871  -1077   1297       C  
ATOM   3493  C   LYS B 248      40.539 -39.962 -42.048  1.00120.72           C  
ANISOU 3493  C   LYS B 248    14121  14442  17306   -921  -1190   1443       C  
ATOM   3494  O   LYS B 248      40.499 -40.906 -41.254  1.00120.23           O  
ANISOU 3494  O   LYS B 248    14077  14383  17223   -931  -1226   1461       O  
ATOM   3495  CB  LYS B 248      39.191 -37.814 -42.581  1.00116.18           C  
ANISOU 3495  CB  LYS B 248    13729  13886  16527   -915  -1161   1268       C  
ATOM   3496  CG  LYS B 248      38.660 -37.145 -43.857  1.00123.65           C  
ANISOU 3496  CG  LYS B 248    14662  14863  17457   -860  -1027   1199       C  
ATOM   3497  CD  LYS B 248      39.601 -37.274 -45.070  1.00129.29           C  
ANISOU 3497  CD  LYS B 248    15204  15568  18351   -828   -945   1288       C  
ATOM   3498  CE  LYS B 248      40.369 -36.015 -45.394  1.00135.16           C  
ANISOU 3498  CE  LYS B 248    15906  16270  19177   -872  -1020   1344       C  
ATOM   3499  NZ  LYS B 248      41.222 -35.553 -44.265  1.00143.49           N  
ANISOU 3499  NZ  LYS B 248    16978  17266  20276   -966  -1224   1429       N  
ATOM   3500  N   ASP B 249      41.688 -39.445 -42.493  1.00119.77           N  
ANISOU 3500  N   ASP B 249    13882  14280  17346   -950  -1238   1551       N  
ATOM   3501  CA  ASP B 249      43.046 -39.755 -42.022  1.00121.64           C  
ANISOU 3501  CA  ASP B 249    14003  14462  17751  -1007  -1360   1706       C  
ATOM   3502  C   ASP B 249      43.617 -41.172 -42.345  1.00125.87           C  
ANISOU 3502  C   ASP B 249    14396  15004  18423   -962  -1273   1791       C  
ATOM   3503  O   ASP B 249      44.460 -41.245 -43.248  1.00125.47           O  
ANISOU 3503  O   ASP B 249    14197  14937  18539   -935  -1205   1882       O  
ATOM   3504  CB  ASP B 249      43.214 -39.468 -40.506  1.00124.58           C  
ANISOU 3504  CB  ASP B 249    14485  14793  18056  -1100  -1570   1729       C  
ATOM   3505  CG  ASP B 249      43.684 -38.054 -40.191  1.00136.26           C  
ANISOU 3505  CG  ASP B 249    16012  16219  19542  -1178  -1725   1758       C  
ATOM   3506  OD1 ASP B 249      43.243 -37.107 -40.890  1.00136.33           O  
ANISOU 3506  OD1 ASP B 249    16056  16241  19501  -1156  -1666   1688       O  
ATOM   3507  OD2 ASP B 249      44.487 -37.894 -39.243  1.00143.46           O  
ANISOU 3507  OD2 ASP B 249    16927  17073  20507  -1263  -1909   1852       O  
ATOM   3508  N   THR B 250      43.292 -42.250 -41.575  1.00122.53           N  
ANISOU 3508  N   THR B 250    14011  14597  17946   -959  -1284   1779       N  
ATOM   3509  CA  THR B 250      44.032 -43.516 -41.756  1.00122.71           C  
ANISOU 3509  CA  THR B 250    13890  14612  18120   -931  -1232   1882       C  
ATOM   3510  C   THR B 250      43.304 -44.886 -41.580  1.00125.14           C  
ANISOU 3510  C   THR B 250    14225  14963  18358   -876  -1133   1826       C  
ATOM   3511  O   THR B 250      42.110 -44.971 -41.307  1.00123.54           O  
ANISOU 3511  O   THR B 250    14155  14805  17981   -853  -1090   1699       O  
ATOM   3512  CB  THR B 250      45.232 -43.490 -40.754  1.00131.37           C  
ANISOU 3512  CB  THR B 250    14929  15645  19340  -1022  -1429   2028       C  
ATOM   3513  OG1 THR B 250      45.071 -42.412 -39.823  1.00127.30           O  
ANISOU 3513  OG1 THR B 250    14548  15103  18717  -1105  -1602   1997       O  
ATOM   3514  CG2 THR B 250      46.580 -43.344 -41.459  1.00132.02           C  
ANISOU 3514  CG2 THR B 250    14823  15681  19657  -1026  -1427   2181       C  
ATOM   3515  N   LEU B 251      44.118 -45.956 -41.791  1.00122.05           N  
ANISOU 3515  N   LEU B 251    13694  14556  18125   -853  -1090   1934       N  
ATOM   3516  CA  LEU B 251      43.839 -47.412 -41.701  1.00121.67           C  
ANISOU 3516  CA  LEU B 251    13619  14533  18077   -804  -1002   1928       C  
ATOM   3517  C   LEU B 251      43.522 -47.886 -40.223  1.00126.03           C  
ANISOU 3517  C   LEU B 251    14272  15086  18530   -860  -1138   1916       C  
ATOM   3518  O   LEU B 251      43.356 -47.015 -39.368  1.00126.11           O  
ANISOU 3518  O   LEU B 251    14392  15080  18443   -929  -1280   1890       O  
ATOM   3519  CB  LEU B 251      45.091 -48.156 -42.274  1.00122.40           C  
ANISOU 3519  CB  LEU B 251    13520  14589  18398   -778   -950   2078       C  
ATOM   3520  CG  LEU B 251      44.917 -48.881 -43.623  1.00126.44           C  
ANISOU 3520  CG  LEU B 251    13956  15123  18961   -674   -729   2054       C  
ATOM   3521  CD1 LEU B 251      45.341 -47.987 -44.796  1.00126.72           C  
ANISOU 3521  CD1 LEU B 251    13924  15145  19079   -645   -651   2078       C  
ATOM   3522  CD2 LEU B 251      45.698 -50.203 -43.647  1.00129.26           C  
ANISOU 3522  CD2 LEU B 251    14184  15458  19473   -643   -679   2166       C  
ATOM   3523  N   MET B 252      43.425 -49.223 -39.881  1.00121.91           N  
ANISOU 3523  N   MET B 252    13723  14578  18021   -834  -1098   1934       N  
ATOM   3524  CA  MET B 252      43.557 -50.468 -40.671  1.00120.77           C  
ANISOU 3524  CA  MET B 252    13468  14447  17973   -755   -940   1962       C  
ATOM   3525  C   MET B 252      42.330 -51.361 -40.421  1.00122.31           C  
ANISOU 3525  C   MET B 252    13763  14693  18017   -712   -861   1848       C  
ATOM   3526  O   MET B 252      41.408 -51.316 -41.231  1.00121.35           O  
ANISOU 3526  O   MET B 252    13693  14611  17802   -651   -727   1739       O  
ATOM   3527  CB  MET B 252      44.876 -51.209 -40.335  1.00124.00           C  
ANISOU 3527  CB  MET B 252    13727  14806  18580   -782  -1004   2128       C  
ATOM   3528  N   ILE B 253      42.303 -52.151 -39.318  1.00117.49           N  
ANISOU 3528  N   ILE B 253    13181  14080  17381   -745   -946   1876       N  
ATOM   3529  CA  ILE B 253      41.148 -52.959 -38.915  1.00115.75           C  
ANISOU 3529  CA  ILE B 253    13059  13904  17015   -713   -891   1777       C  
ATOM   3530  C   ILE B 253      40.477 -52.271 -37.712  1.00118.86           C  
ANISOU 3530  C   ILE B 253    13616  14306  17239   -775  -1025   1712       C  
ATOM   3531  O   ILE B 253      39.600 -52.864 -37.085  1.00118.09           O  
ANISOU 3531  O   ILE B 253    13611  14239  17017   -764  -1012   1644       O  
ATOM   3532  CB  ILE B 253      41.567 -54.399 -38.561  1.00 20.00           C  
ATOM   3533  N   SER B 254      40.897 -51.010 -37.404  1.00114.81           N  
ANISOU 3533  N   SER B 254    13142  13762  16719   -839  -1149   1733       N  
ATOM   3534  CA  SER B 254      40.337 -50.163 -36.355  1.00113.87           C  
ANISOU 3534  CA  SER B 254    13188  13640  16438   -897  -1274   1672       C  
ATOM   3535  C   SER B 254      40.280 -48.683 -36.863  1.00115.01           C  
ANISOU 3535  C   SER B 254    13374  13774  16550   -912  -1289   1629       C  
ATOM   3536  O   SER B 254      41.062 -47.860 -36.375  1.00115.87           O  
ANISOU 3536  O   SER B 254    13486  13835  16704   -985  -1437   1697       O  
ATOM   3537  CB  SER B 254      41.163 -50.258 -35.070  1.00 20.00           C  
ATOM   3538  OG  SER B 254      42.481 -49.780 -35.275  1.00 20.00           O  
ATOM   3539  N   ARG B 255      39.416 -48.311 -37.855  1.00107.10           N  
ANISOU 3539  N   ARG B 255    12401  12814  15480   -848  -1145   1525       N  
ATOM   3540  CA  ARG B 255      38.409 -49.088 -38.604  1.00103.79           C  
ANISOU 3540  CA  ARG B 255    11985  12447  15003   -762   -967   1435       C  
ATOM   3541  C   ARG B 255      37.278 -49.644 -37.723  1.00102.07           C  
ANISOU 3541  C   ARG B 255    11896  12263  14623   -754   -965   1353       C  
ATOM   3542  O   ARG B 255      37.238 -49.353 -36.533  1.00102.80           O  
ANISOU 3542  O   ARG B 255    12089  12337  14633   -813  -1095   1357       O  
ATOM   3543  CB  ARG B 255      39.089 -50.240 -39.346  1.00 20.00           C  
ATOM   3544  N   THR B 256      36.347 -50.405 -38.344  1.00 92.61           N  
ANISOU 3544  N   THR B 256    10700  11110  13377   -682   -814   1279       N  
ATOM   3545  CA  THR B 256      35.058 -50.886 -37.841  1.00 89.22           C  
ANISOU 3545  CA  THR B 256    10383  10720  12796   -655   -768   1186       C  
ATOM   3546  C   THR B 256      34.101 -49.745 -38.202  1.00 85.86           C  
ANISOU 3546  C   THR B 256    10062  10316  12246   -640   -728   1081       C  
ATOM   3547  O   THR B 256      33.963 -48.787 -37.453  1.00 84.02           O  
ANISOU 3547  O   THR B 256     9935  10066  11923   -687   -827   1058       O  
ATOM   3548  CB  THR B 256      35.035 -51.469 -36.385  1.00 97.94           C  
ANISOU 3548  CB  THR B 256    11556  11815  13840   -699   -879   1216       C  
ATOM   3549  OG1 THR B 256      33.962 -52.415 -36.330  1.00 92.80           O  
ANISOU 3549  OG1 THR B 256    10946  11206  13108   -647   -780   1151       O  
ATOM   3550  CG2 THR B 256      34.764 -50.436 -35.265  1.00 99.27           C  
ANISOU 3550  CG2 THR B 256    11877  11964  13876   -760  -1010   1186       C  
ATOM   3551  N   PRO B 257      33.585 -49.731 -39.446  1.00 79.36           N  
ANISOU 3551  N   PRO B 257     9202   9520  11433   -579   -588   1024       N  
ATOM   3552  CA  PRO B 257      32.721 -48.616 -39.866  1.00 77.36           C  
ANISOU 3552  CA  PRO B 257     9035   9284  11074   -565   -548    931       C  
ATOM   3553  C   PRO B 257      31.489 -48.437 -38.984  1.00 76.04           C  
ANISOU 3553  C   PRO B 257     9016   9139  10735   -566   -560    847       C  
ATOM   3554  O   PRO B 257      30.895 -49.404 -38.500  1.00 72.68           O  
ANISOU 3554  O   PRO B 257     8617   8734  10262   -545   -529    831       O  
ATOM   3555  CB  PRO B 257      32.380 -48.939 -41.324  1.00 78.71           C  
ANISOU 3555  CB  PRO B 257     9135   9481  11292   -496   -393    894       C  
ATOM   3556  CG  PRO B 257      33.354 -49.976 -41.734  1.00 84.06           C  
ANISOU 3556  CG  PRO B 257     9680  10142  12118   -481   -365    982       C  
ATOM   3557  CD  PRO B 257      33.709 -50.739 -40.516  1.00 80.70           C  
ANISOU 3557  CD  PRO B 257     9259   9703  11699   -518   -459   1040       C  
ATOM   3558  N   GLU B 258      31.166 -47.171 -38.722  1.00 72.05           N  
ANISOU 3558  N   GLU B 258     8610   8624  10142   -591   -609    800       N  
ATOM   3559  CA  GLU B 258      30.115 -46.791 -37.796  1.00 70.68           C  
ANISOU 3559  CA  GLU B 258     8589   8461   9806   -597   -630    730       C  
ATOM   3560  C   GLU B 258      29.273 -45.656 -38.337  1.00 71.23           C  
ANISOU 3560  C   GLU B 258     8730   8542   9791   -575   -574    644       C  
ATOM   3561  O   GLU B 258      29.775 -44.791 -39.038  1.00 68.47           O  
ANISOU 3561  O   GLU B 258     8342   8177   9495   -587   -585    652       O  
ATOM   3562  CB  GLU B 258      30.784 -46.339 -36.485  1.00 72.82           C  
ANISOU 3562  CB  GLU B 258     8937   8687  10045   -670   -795    780       C  
ATOM   3563  CG  GLU B 258      31.241 -47.490 -35.601  1.00 82.03           C  
ANISOU 3563  CG  GLU B 258    10080   9845  11243   -692   -855    847       C  
ATOM   3564  CD  GLU B 258      32.385 -47.206 -34.642  1.00 98.85           C  
ANISOU 3564  CD  GLU B 258    12224  11922  13413   -772  -1029    934       C  
ATOM   3565  OE1 GLU B 258      32.922 -46.072 -34.651  1.00 83.44           O  
ANISOU 3565  OE1 GLU B 258    10296   9935  11473   -816  -1113    949       O  
ATOM   3566  OE2 GLU B 258      32.727 -48.123 -33.858  1.00 80.02           O  
ANISOU 3566  OE2 GLU B 258     9830   9529  11046   -793  -1085    989       O  
ATOM   3567  N   VAL B 259      27.990 -45.664 -38.004  1.00 68.79           N  
ANISOU 3567  N   VAL B 259     8522   8259   9354   -543   -514    567       N  
ATOM   3568  CA  VAL B 259      27.070 -44.575 -38.322  1.00 68.38           C  
ANISOU 3568  CA  VAL B 259     8555   8217   9209   -523   -466    486       C  
ATOM   3569  C   VAL B 259      27.087 -43.745 -37.025  1.00 71.99           C  
ANISOU 3569  C   VAL B 259     9156   8639   9560   -572   -582    481       C  
ATOM   3570  O   VAL B 259      27.024 -44.329 -35.941  1.00 72.64           O  
ANISOU 3570  O   VAL B 259     9298   8712   9589   -589   -633    500       O  
ATOM   3571  CB  VAL B 259      25.671 -45.112 -38.710  1.00 72.12           C  
ANISOU 3571  CB  VAL B 259     9051   8735   9617   -459   -333    417       C  
ATOM   3572  CG1 VAL B 259      24.657 -43.980 -38.842  1.00 71.84           C  
ANISOU 3572  CG1 VAL B 259     9114   8705   9477   -441   -291    339       C  
ATOM   3573  CG2 VAL B 259      25.759 -45.895 -40.020  1.00 71.88           C  
ANISOU 3573  CG2 VAL B 259     8890   8730   9692   -417   -233    425       C  
ATOM   3574  N   THR B 260      27.289 -42.427 -37.120  1.00 68.31           N  
ANISOU 3574  N   THR B 260     8741   8145   9069   -600   -632    462       N  
ATOM   3575  CA  THR B 260      27.397 -41.558 -35.931  1.00 69.28           C  
ANISOU 3575  CA  THR B 260     9009   8223   9092   -650   -751    459       C  
ATOM   3576  C   THR B 260      26.226 -40.565 -35.841  1.00 71.11           C  
ANISOU 3576  C   THR B 260     9372   8458   9189   -623   -695    369       C  
ATOM   3577  O   THR B 260      25.946 -39.866 -36.804  1.00 69.84           O  
ANISOU 3577  O   THR B 260     9179   8309   9047   -599   -632    331       O  
ATOM   3578  CB  THR B 260      28.767 -40.842 -35.893  1.00 79.47           C  
ANISOU 3578  CB  THR B 260    10262   9464  10468   -719   -887    527       C  
ATOM   3579  OG1 THR B 260      29.814 -41.808 -36.041  1.00 80.00           O  
ANISOU 3579  OG1 THR B 260    10195   9529  10673   -738   -924    616       O  
ATOM   3580  CG2 THR B 260      28.977 -40.065 -34.602  1.00 80.82           C  
ANISOU 3580  CG2 THR B 260    10590   9581  10537   -779  -1027    531       C  
ATOM   3581  N   CYS B 261      25.554 -40.512 -34.680  1.00 67.36           N  
ANISOU 3581  N   CYS B 261     9046   7969   8579   -623   -716    339       N  
ATOM   3582  CA  CYS B 261      24.467 -39.568 -34.413  1.00 66.81           C  
ANISOU 3582  CA  CYS B 261     9116   7893   8375   -596   -666    262       C  
ATOM   3583  C   CYS B 261      24.998 -38.558 -33.412  1.00 70.96           C  
ANISOU 3583  C   CYS B 261     9783   8354   8824   -656   -803    270       C  
ATOM   3584  O   CYS B 261      25.457 -38.957 -32.339  1.00 69.90           O  
ANISOU 3584  O   CYS B 261     9715   8191   8654   -696   -901    310       O  
ATOM   3585  CB  CYS B 261      23.236 -40.278 -33.868  1.00 66.13           C  
ANISOU 3585  CB  CYS B 261     9099   7835   8191   -544   -571    224       C  
ATOM   3586  SG  CYS B 261      21.701 -39.342 -34.055  1.00 69.26           S  
ANISOU 3586  SG  CYS B 261     9602   8242   8470   -484   -449    133       S  
ATOM   3587  N   VAL B 262      24.985 -37.269 -33.776  1.00 69.40           N  
ANISOU 3587  N   VAL B 262     9632   8133   8605   -667   -818    235       N  
ATOM   3588  CA  VAL B 262      25.455 -36.204 -32.885  1.00 71.99           C  
ANISOU 3588  CA  VAL B 262    10104   8392   8855   -725   -951    238       C  
ATOM   3589  C   VAL B 262      24.342 -35.169 -32.684  1.00 77.15           C  
ANISOU 3589  C   VAL B 262    10909   9032   9372   -689   -885    155       C  
ATOM   3590  O   VAL B 262      23.698 -34.732 -33.644  1.00 74.22           O  
ANISOU 3590  O   VAL B 262    10489   8691   9019   -644   -779    109       O  
ATOM   3591  CB  VAL B 262      26.757 -35.548 -33.395  1.00 76.64           C  
ANISOU 3591  CB  VAL B 262    10611   8949   9561   -787  -1065    292       C  
ATOM   3592  CG1 VAL B 262      27.294 -34.549 -32.371  1.00 78.00           C  
ANISOU 3592  CG1 VAL B 262    10940   9043   9653   -855  -1222    302       C  
ATOM   3593  CG2 VAL B 262      27.803 -36.604 -33.733  1.00 76.33           C  
ANISOU 3593  CG2 VAL B 262    10403   8926   9673   -811  -1106    378       C  
ATOM   3594  N   VAL B 263      24.122 -34.784 -31.422  1.00 77.51           N  
ANISOU 3594  N   VAL B 263    11143   9028   9279   -708   -948    138       N  
ATOM   3595  CA  VAL B 263      23.085 -33.822 -31.069  1.00 78.40           C  
ANISOU 3595  CA  VAL B 263    11419   9118   9253   -672   -886     64       C  
ATOM   3596  C   VAL B 263      23.702 -32.660 -30.371  1.00 82.78           C  
ANISOU 3596  C   VAL B 263    12120   9593   9739   -734  -1026     64       C  
ATOM   3597  O   VAL B 263      24.505 -32.844 -29.455  1.00 82.97           O  
ANISOU 3597  O   VAL B 263    12214   9572   9741   -795  -1165    111       O  
ATOM   3598  CB  VAL B 263      22.001 -34.451 -30.188  1.00 83.48           C  
ANISOU 3598  CB  VAL B 263    12174   9773   9774   -621   -799     36       C  
ATOM   3599  CG1 VAL B 263      20.812 -33.506 -30.037  1.00 83.14           C  
ANISOU 3599  CG1 VAL B 263    12269   9713   9607   -568   -700    -38       C  
ATOM   3600  CG2 VAL B 263      21.558 -35.772 -30.785  1.00 83.33           C  
ANISOU 3600  CG2 VAL B 263    12000   9827   9835   -572   -687     51       C  
ATOM   3601  N   VAL B 264      23.280 -31.466 -30.777  1.00 79.61           N  
ANISOU 3601  N   VAL B 264    11777   9173   9299   -718   -991     11       N  
ATOM   3602  CA  VAL B 264      23.732 -30.188 -30.218  1.00 80.38           C  
ANISOU 3602  CA  VAL B 264    12027   9191   9324   -771  -1112     -1       C  
ATOM   3603  C   VAL B 264      22.499 -29.315 -29.873  1.00 83.72           C  
ANISOU 3603  C   VAL B 264    12623   9590   9596   -715  -1012    -83       C  
ATOM   3604  O   VAL B 264      21.360 -29.686 -30.202  1.00 80.74           O  
ANISOU 3604  O   VAL B 264    12220   9264   9196   -638   -851   -121       O  
ATOM   3605  CB  VAL B 264      24.722 -29.463 -31.178  1.00 83.34           C  
ANISOU 3605  CB  VAL B 264    12280   9556   9830   -820  -1191     29       C  
ATOM   3606  CG1 VAL B 264      26.033 -30.240 -31.295  1.00 83.22           C  
ANISOU 3606  CG1 VAL B 264    12121   9544   9953   -881  -1306    120       C  
ATOM   3607  CG2 VAL B 264      24.102 -29.229 -32.549  1.00 81.57           C  
ANISOU 3607  CG2 VAL B 264    11923   9391   9680   -761  -1047     -9       C  
ATOM   3608  N   ASP B 265      22.746 -28.168 -29.183  1.00 81.65           N  
ANISOU 3608  N   ASP B 265    12541   9246   9236   -755  -1112   -104       N  
ATOM   3609  CA  ASP B 265      21.726 -27.216 -28.735  1.00 81.21           C  
ANISOU 3609  CA  ASP B 265    12674   9150   9032   -709  -1037   -176       C  
ATOM   3610  C   ASP B 265      20.760 -27.873 -27.728  1.00 86.14           C  
ANISOU 3610  C   ASP B 265    13433   9775   9522   -655   -947   -197       C  
ATOM   3611  O   ASP B 265      19.552 -27.600 -27.717  1.00 83.46           O  
ANISOU 3611  O   ASP B 265    13164   9444   9102   -580   -800   -250       O  
ATOM   3612  CB  ASP B 265      21.020 -26.532 -29.925  1.00 81.53           C  
ANISOU 3612  CB  ASP B 265    12626   9229   9123   -656   -908   -223       C  
ATOM   3613  CG  ASP B 265      21.949 -25.679 -30.786  1.00 90.96           C  
ANISOU 3613  CG  ASP B 265    13729  10408  10425   -710  -1001   -206       C  
ATOM   3614  OD1 ASP B 265      23.002 -25.231 -30.267  1.00 92.50           O  
ANISOU 3614  OD1 ASP B 265    13991  10538  10616   -789  -1171   -172       O  
ATOM   3615  OD2 ASP B 265      21.617 -25.450 -31.975  1.00 93.80           O  
ANISOU 3615  OD2 ASP B 265    13952  10816  10871   -675   -907   -224       O  
ATOM   3616  N   VAL B 266      21.356 -28.714 -26.843  1.00 85.82           N  
ANISOU 3616  N   VAL B 266    13430   9719   9459   -697  -1044   -149       N  
ATOM   3617  CA  VAL B 266      20.688 -29.430 -25.755  1.00 86.99           C  
ANISOU 3617  CA  VAL B 266    13708   9860   9483   -660   -991   -154       C  
ATOM   3618  C   VAL B 266      20.979 -28.545 -24.557  1.00 94.36           C  
ANISOU 3618  C   VAL B 266    14900  10691  10263   -704  -1111   -170       C  
ATOM   3619  O   VAL B 266      22.146 -28.270 -24.290  1.00 94.11           O  
ANISOU 3619  O   VAL B 266    14889  10610  10260   -792  -1293   -130       O  
ATOM   3620  CB  VAL B 266      21.252 -30.870 -25.570  1.00 90.73           C  
ANISOU 3620  CB  VAL B 266    14061  10377  10034   -685  -1037    -88       C  
ATOM   3621  CG1 VAL B 266      20.730 -31.521 -24.289  1.00 91.16           C  
ANISOU 3621  CG1 VAL B 266    14276  10409   9949   -662  -1015    -87       C  
ATOM   3622  CG2 VAL B 266      20.939 -31.742 -26.787  1.00 88.90           C  
ANISOU 3622  CG2 VAL B 266    13585  10241   9951   -639   -916    -76       C  
ATOM   3623  N   SER B 267      19.932 -28.056 -23.876  1.00 93.86           N  
ANISOU 3623  N   SER B 267    15032  10589  10040   -645  -1011   -225       N  
ATOM   3624  CA  SER B 267      20.074 -27.125 -22.751  1.00 95.84           C  
ANISOU 3624  CA  SER B 267    15556  10734  10125   -676  -1107   -251       C  
ATOM   3625  C   SER B 267      20.645 -27.748 -21.472  1.00102.77           C  
ANISOU 3625  C   SER B 267    16574  11562  10913   -728  -1235   -210       C  
ATOM   3626  O   SER B 267      20.690 -28.972 -21.326  1.00101.35           O  
ANISOU 3626  O   SER B 267    16297  11434  10777   -722  -1217   -168       O  
ATOM   3627  CB  SER B 267      18.731 -26.463 -22.449  1.00 98.97           C  
ANISOU 3627  CB  SER B 267    16117  11105  10383   -586   -940   -319       C  
ATOM   3628  OG  SER B 267      17.733 -27.422 -22.148  1.00105.68           O  
ANISOU 3628  OG  SER B 267    16956  12003  11193   -508   -785   -319       O  
ATOM   3629  N   GLN B 268      21.075 -26.871 -20.548  1.00103.31           N  
ANISOU 3629  N   GLN B 268    16878  11525  10849   -781  -1367   -223       N  
ATOM   3630  CA  GLN B 268      21.618 -27.251 -19.236  1.00105.59           C  
ANISOU 3630  CA  GLN B 268    17346  11746  11025   -838  -1507   -190       C  
ATOM   3631  C   GLN B 268      20.487 -27.591 -18.247  1.00112.56           C  
ANISOU 3631  C   GLN B 268    18422  12613  11733   -757  -1369   -224       C  
ATOM   3632  O   GLN B 268      20.706 -28.393 -17.336  1.00112.83           O  
ANISOU 3632  O   GLN B 268    18533  12632  11704   -779  -1426   -188       O  
ATOM   3633  CB  GLN B 268      22.513 -26.138 -18.660  1.00108.35           C  
ANISOU 3633  CB  GLN B 268    17884  11982  11301   -928  -1710   -190       C  
ATOM   3634  N   GLU B 269      19.296 -26.958 -18.403  1.00110.70           N  
ANISOU 3634  N   GLU B 269    18267  12376  11418   -665  -1188   -289       N  
ATOM   3635  CA  GLU B 269      18.117 -27.252 -17.564  1.00111.69           C  
ANISOU 3635  CA  GLU B 269    18559  12489  11389   -575  -1027   -317       C  
ATOM   3636  C   GLU B 269      17.437 -28.568 -17.978  1.00114.89           C  
ANISOU 3636  C   GLU B 269    18766  13002  11887   -509   -874   -290       C  
ATOM   3637  O   GLU B 269      16.759 -29.181 -17.150  1.00114.71           O  
ANISOU 3637  O   GLU B 269    18851  12974  11758   -457   -784   -286       O  
ATOM   3638  CB  GLU B 269      17.096 -26.089 -17.523  1.00113.45           C  
ANISOU 3638  CB  GLU B 269    18946  12662  11497   -499   -887   -388       C  
ATOM   3639  CG  GLU B 269      16.622 -25.544 -18.863  1.00121.65           C  
ANISOU 3639  CG  GLU B 269    19800  13759  12662   -455   -774   -418       C  
ATOM   3640  CD  GLU B 269      17.099 -24.129 -19.146  1.00138.18           C  
ANISOU 3640  CD  GLU B 269    21978  15783  14742   -501   -871   -454       C  
ATOM   3641  OE1 GLU B 269      16.421 -23.174 -18.702  1.00128.41           O  
ANISOU 3641  OE1 GLU B 269    20948  14473  13366   -453   -797   -507       O  
ATOM   3642  OE2 GLU B 269      18.173 -23.976 -19.772  1.00128.10           O  
ANISOU 3642  OE2 GLU B 269    20566  14517  13589   -584  -1023   -426       O  
ATOM   3643  N   ASP B 270      17.639 -29.011 -19.239  1.00110.45           N  
ANISOU 3643  N   ASP B 270    17918  12530  11516   -513   -849   -269       N  
ATOM   3644  CA  ASP B 270      17.129 -30.286 -19.764  1.00109.27           C  
ANISOU 3644  CA  ASP B 270    17560  12482  11475   -463   -727   -239       C  
ATOM   3645  C   ASP B 270      18.313 -31.037 -20.419  1.00110.14           C  
ANISOU 3645  C   ASP B 270    17445  12643  11758   -541   -861   -180       C  
ATOM   3646  O   ASP B 270      18.402 -31.104 -21.650  1.00107.82           O  
ANISOU 3646  O   ASP B 270    16933  12415  11618   -535   -822   -177       O  
ATOM   3647  CB  ASP B 270      15.976 -30.047 -20.769  1.00110.43           C  
ANISOU 3647  CB  ASP B 270    17586  12689  11683   -372   -525   -277       C  
ATOM   3648  CG  ASP B 270      14.782 -29.331 -20.156  1.00122.81           C  
ANISOU 3648  CG  ASP B 270    19362  14207  13095   -288   -380   -326       C  
ATOM   3649  OD1 ASP B 270      14.135 -29.917 -19.256  1.00124.52           O  
ANISOU 3649  OD1 ASP B 270    19694  14412  13207   -240   -299   -317       O  
ATOM   3650  OD2 ASP B 270      14.502 -28.179 -20.565  1.00126.61           O  
ANISOU 3650  OD2 ASP B 270    19892  14656  13558   -270   -344   -371       O  
ATOM   3651  N   PRO B 271      19.247 -31.586 -19.603  1.00106.23           N  
ANISOU 3651  N   PRO B 271    17006  12115  11240   -614  -1020   -130       N  
ATOM   3652  CA  PRO B 271      20.417 -32.275 -20.175  1.00105.19           C  
ANISOU 3652  CA  PRO B 271    16666  12025  11277   -688  -1149    -66       C  
ATOM   3653  C   PRO B 271      20.189 -33.732 -20.607  1.00107.43           C  
ANISOU 3653  C   PRO B 271    16743  12402  11673   -653  -1062    -27       C  
ATOM   3654  O   PRO B 271      20.804 -34.171 -21.578  1.00105.61           O  
ANISOU 3654  O   PRO B 271    16289  12226  11612   -679  -1091      8       O  
ATOM   3655  CB  PRO B 271      21.439 -32.196 -19.037  1.00108.08           C  
ANISOU 3655  CB  PRO B 271    17197  12307  11562   -779  -1357    -27       C  
ATOM   3656  CG  PRO B 271      20.622 -32.246 -17.812  1.00113.14           C  
ANISOU 3656  CG  PRO B 271    18082  12901  12005   -733  -1292    -55       C  
ATOM   3657  CD  PRO B 271      19.309 -31.575 -18.126  1.00108.53           C  
ANISOU 3657  CD  PRO B 271    17559  12326  11352   -634  -1094   -126       C  
ATOM   3658  N   GLU B 272      19.359 -34.495 -19.864  1.00104.05           N  
ANISOU 3658  N   GLU B 272    16394  11987  11152   -596   -960    -27       N  
ATOM   3659  CA  GLU B 272      19.132 -35.920 -20.140  1.00102.56           C  
ANISOU 3659  CA  GLU B 272    16029  11879  11059   -566   -884     12       C  
ATOM   3660  C   GLU B 272      18.604 -36.175 -21.557  1.00102.69           C  
ANISOU 3660  C   GLU B 272    15812  11982  11223   -512   -747     -2       C  
ATOM   3661  O   GLU B 272      17.539 -35.679 -21.926  1.00102.44           O  
ANISOU 3661  O   GLU B 272    15801  11964  11157   -440   -600    -51       O  
ATOM   3662  CB  GLU B 272      18.213 -36.559 -19.077  1.00104.49           C  
ANISOU 3662  CB  GLU B 272    16416  12118  11168   -508   -786     11       C  
ATOM   3663  N   VAL B 273      19.386 -36.930 -22.352  1.00 95.67           N  
ANISOU 3663  N   VAL B 273    14706  11146  10500   -549   -801     44       N  
ATOM   3664  CA  VAL B 273      19.054 -37.295 -23.729  1.00 92.61           C  
ANISOU 3664  CA  VAL B 273    14092  10837  10260   -509   -692     38       C  
ATOM   3665  C   VAL B 273      19.029 -38.830 -23.851  1.00 91.06           C  
ANISOU 3665  C   VAL B 273    13746  10704  10151   -493   -652     85       C  
ATOM   3666  O   VAL B 273      19.837 -39.528 -23.216  1.00 91.80           O  
ANISOU 3666  O   VAL B 273    13839  10783  10256   -545   -765    138       O  
ATOM   3667  CB  VAL B 273      20.062 -36.641 -24.727  1.00 96.43           C  
ANISOU 3667  CB  VAL B 273    14453  11318  10868   -565   -787     47       C  
ATOM   3668  CG1 VAL B 273      20.015 -37.297 -26.110  1.00 95.03           C  
ANISOU 3668  CG1 VAL B 273    14028  11220  10859   -538   -704     58       C  
ATOM   3669  CG2 VAL B 273      19.804 -35.142 -24.852  1.00 96.53           C  
ANISOU 3669  CG2 VAL B 273    14585  11282  10808   -561   -782    -10       C  
ATOM   3670  N   GLN B 274      18.079 -39.339 -24.664  1.00 81.41           N  
ANISOU 3670  N   GLN B 274    12397   9546   8988   -423   -495     67       N  
ATOM   3671  CA  GLN B 274      17.934 -40.753 -24.990  1.00 78.22           C  
ANISOU 3671  CA  GLN B 274    11836   9205   8679   -401   -440    105       C  
ATOM   3672  C   GLN B 274      18.087 -40.904 -26.514  1.00 77.56           C  
ANISOU 3672  C   GLN B 274    11537   9176   8754   -393   -395    103       C  
ATOM   3673  O   GLN B 274      17.578 -40.069 -27.270  1.00 77.23           O  
ANISOU 3673  O   GLN B 274    11482   9142   8722   -363   -325     58       O  
ATOM   3674  CB  GLN B 274      16.562 -41.282 -24.528  1.00 78.84           C  
ANISOU 3674  CB  GLN B 274    11972   9306   8677   -322   -289     90       C  
ATOM   3675  CG  GLN B 274      16.265 -42.709 -24.987  1.00 80.38           C  
ANISOU 3675  CG  GLN B 274    11999   9568   8975   -293   -218    124       C  
ATOM   3676  CD  GLN B 274      15.136 -43.361 -24.231  1.00 98.39           C  
ANISOU 3676  CD  GLN B 274    14352  11859  11171   -231   -104    128       C  
ATOM   3677  OE1 GLN B 274      14.052 -43.591 -24.785  1.00 89.66           O  
ANISOU 3677  OE1 GLN B 274    13183  10793  10092   -165     36    112       O  
ATOM   3678  NE2 GLN B 274      15.391 -43.753 -22.974  1.00 87.69           N  
ANISOU 3678  NE2 GLN B 274    13126  10471   9721   -251   -166    158       N  
ATOM   3679  N   PHE B 275      18.782 -41.969 -26.955  1.00 70.15           N  
ANISOU 3679  N   PHE B 275    10439   8275   7940   -416   -433    152       N  
ATOM   3680  CA  PHE B 275      18.991 -42.280 -28.377  1.00 66.73           C  
ANISOU 3680  CA  PHE B 275     9804   7891   7659   -407   -389    156       C  
ATOM   3681  C   PHE B 275      18.304 -43.594 -28.723  1.00 67.37           C  
ANISOU 3681  C   PHE B 275     9773   8029   7796   -358   -283    170       C  
ATOM   3682  O   PHE B 275      18.465 -44.574 -27.999  1.00 66.34           O  
ANISOU 3682  O   PHE B 275     9648   7902   7655   -366   -311    210       O  
ATOM   3683  CB  PHE B 275      20.487 -42.413 -28.690  1.00 67.91           C  
ANISOU 3683  CB  PHE B 275     9854   8028   7921   -478   -525    208       C  
ATOM   3684  CG  PHE B 275      21.234 -41.113 -28.839  1.00 69.29           C  
ANISOU 3684  CG  PHE B 275    10077   8156   8093   -527   -623    197       C  
ATOM   3685  CD1 PHE B 275      21.185 -40.403 -30.023  1.00 70.58           C  
ANISOU 3685  CD1 PHE B 275    10156   8336   8325   -513   -576    167       C  
ATOM   3686  CD2 PHE B 275      22.059 -40.650 -27.829  1.00 72.98           C  
ANISOU 3686  CD2 PHE B 275    10667   8562   8499   -592   -771    225       C  
ATOM   3687  CE1 PHE B 275      21.901 -39.223 -30.178  1.00 71.66           C  
ANISOU 3687  CE1 PHE B 275    10331   8430   8468   -560   -668    162       C  
ATOM   3688  CE2 PHE B 275      22.804 -39.487 -27.998  1.00 75.90           C  
ANISOU 3688  CE2 PHE B 275    11072   8886   8880   -643   -871    222       C  
ATOM   3689  CZ  PHE B 275      22.722 -38.781 -29.176  1.00 72.65           C  
ANISOU 3689  CZ  PHE B 275    10572   8493   8537   -625   -817    191       C  
ATOM   3690  N   ASN B 276      17.536 -43.610 -29.816  1.00 62.10           N  
ANISOU 3690  N   ASN B 276     9007   7403   7186   -309   -166    139       N  
ATOM   3691  CA  ASN B 276      16.880 -44.812 -30.317  1.00 61.42           C  
ANISOU 3691  CA  ASN B 276     8804   7368   7165   -264    -68    152       C  
ATOM   3692  C   ASN B 276      17.346 -45.015 -31.763  1.00 63.34           C  
ANISOU 3692  C   ASN B 276     8874   7642   7549   -269    -54    154       C  
ATOM   3693  O   ASN B 276      17.292 -44.078 -32.569  1.00 61.51           O  
ANISOU 3693  O   ASN B 276     8625   7409   7337   -265    -34    120       O  
ATOM   3694  CB  ASN B 276      15.351 -44.725 -30.225  1.00 64.42           C  
ANISOU 3694  CB  ASN B 276     9240   7764   7474   -195     69    117       C  
ATOM   3695  CG  ASN B 276      14.838 -44.864 -28.809  1.00 85.03           C  
ANISOU 3695  CG  ASN B 276    12003  10348   9955   -180     77    125       C  
ATOM   3696  OD1 ASN B 276      14.977 -43.957 -27.995  1.00 75.51           O  
ANISOU 3696  OD1 ASN B 276    10951   9096   8643   -196     30    108       O  
ATOM   3697  ND2 ASN B 276      14.239 -45.998 -28.468  1.00 79.89           N  
ANISOU 3697  ND2 ASN B 276    11323   9725   9309   -147    138    152       N  
ATOM   3698  N   TRP B 277      17.828 -46.235 -32.073  1.00 58.99           N  
ANISOU 3698  N   TRP B 277     8202   7117   7094   -276    -65    197       N  
ATOM   3699  CA  TRP B 277      18.399 -46.578 -33.372  1.00 57.70           C  
ANISOU 3699  CA  TRP B 277     7881   6977   7064   -281    -55    207       C  
ATOM   3700  C   TRP B 277      17.555 -47.610 -34.099  1.00 58.61           C  
ANISOU 3700  C   TRP B 277     7901   7135   7233   -231     54    202       C  
ATOM   3701  O   TRP B 277      17.221 -48.626 -33.508  1.00 59.27           O  
ANISOU 3701  O   TRP B 277     7985   7231   7304   -217     73    227       O  
ATOM   3702  CB  TRP B 277      19.812 -47.135 -33.165  1.00 56.89           C  
ANISOU 3702  CB  TRP B 277     7715   6860   7041   -333   -165    268       C  
ATOM   3703  CG  TRP B 277      20.849 -46.104 -32.884  1.00 58.22           C  
ANISOU 3703  CG  TRP B 277     7931   6986   7204   -390   -281    282       C  
ATOM   3704  CD1 TRP B 277      21.327 -45.729 -31.665  1.00 62.45           C  
ANISOU 3704  CD1 TRP B 277     8586   7480   7662   -434   -389    303       C  
ATOM   3705  CD2 TRP B 277      21.610 -45.380 -33.855  1.00 57.71           C  
ANISOU 3705  CD2 TRP B 277     7793   6913   7223   -412   -311    282       C  
ATOM   3706  NE1 TRP B 277      22.344 -44.807 -31.815  1.00 62.48           N  
ANISOU 3706  NE1 TRP B 277     8592   7448   7700   -486   -490    318       N  
ATOM   3707  CE2 TRP B 277      22.540 -44.582 -33.153  1.00 62.74           C  
ANISOU 3707  CE2 TRP B 277     8502   7502   7835   -472   -441    308       C  
ATOM   3708  CE3 TRP B 277      21.592 -45.317 -35.256  1.00 57.75           C  
ANISOU 3708  CE3 TRP B 277     7680   6942   7319   -387   -240    266       C  
ATOM   3709  CZ2 TRP B 277      23.488 -43.801 -33.806  1.00 61.64           C  
ANISOU 3709  CZ2 TRP B 277     8306   7342   7772   -508   -503    324       C  
ATOM   3710  CZ3 TRP B 277      22.519 -44.518 -35.899  1.00 58.58           C  
ANISOU 3710  CZ3 TRP B 277     7738   7028   7492   -420   -294    278       C  
ATOM   3711  CH2 TRP B 277      23.453 -43.775 -35.179  1.00 59.73           C  
ANISOU 3711  CH2 TRP B 277     7944   7128   7622   -479   -423    309       C  
ATOM   3712  N   TYR B 278      17.222 -47.368 -35.375  1.00 52.31           N  
ANISOU 3712  N   TYR B 278     7023   6357   6495   -207    122    173       N  
ATOM   3713  CA  TYR B 278      16.460 -48.323 -36.179  1.00 51.33           C  
ANISOU 3713  CA  TYR B 278     6809   6268   6427   -165    215    169       C  
ATOM   3714  C   TYR B 278      17.221 -48.614 -37.496  1.00 53.79           C  
ANISOU 3714  C   TYR B 278     6991   6589   6859   -173    216    178       C  
ATOM   3715  O   TYR B 278      17.805 -47.713 -38.095  1.00 52.73           O  
ANISOU 3715  O   TYR B 278     6842   6442   6751   -192    189    165       O  
ATOM   3716  CB  TYR B 278      15.007 -47.841 -36.452  1.00 53.72           C  
ANISOU 3716  CB  TYR B 278     7154   6584   6675   -117    316    124       C  
ATOM   3717  CG  TYR B 278      14.284 -47.319 -35.229  1.00 58.35           C  
ANISOU 3717  CG  TYR B 278     7877   7154   7140   -104    327    113       C  
ATOM   3718  CD1 TYR B 278      14.552 -46.050 -34.728  1.00 61.03           C  
ANISOU 3718  CD1 TYR B 278     8323   7461   7404   -124    280     91       C  
ATOM   3719  CD2 TYR B 278      13.403 -48.128 -34.515  1.00 59.89           C  
ANISOU 3719  CD2 TYR B 278     8102   7360   7294    -72    380    129       C  
ATOM   3720  CE1 TYR B 278      13.982 -45.606 -33.537  1.00 64.08           C  
ANISOU 3720  CE1 TYR B 278     8851   7825   7673   -111    289     83       C  
ATOM   3721  CE2 TYR B 278      12.801 -47.684 -33.338  1.00 61.21           C  
ANISOU 3721  CE2 TYR B 278     8403   7508   7347    -56    395    125       C  
ATOM   3722  CZ  TYR B 278      13.085 -46.415 -32.855  1.00 71.01           C  
ANISOU 3722  CZ  TYR B 278     9758   8715   8509    -75    352    100       C  
ATOM   3723  OH  TYR B 278      12.509 -45.940 -31.694  1.00 73.35           O  
ANISOU 3723  OH  TYR B 278    10200   8984   8684    -56    371     93       O  
ATOM   3724  N   VAL B 279      17.288 -49.897 -37.889  1.00 50.91           N  
ANISOU 3724  N   VAL B 279     6535   6241   6566   -159    244    205       N  
ATOM   3725  CA  VAL B 279      17.903 -50.325 -39.153  1.00 49.59           C  
ANISOU 3725  CA  VAL B 279     6254   6080   6508   -157    263    214       C  
ATOM   3726  C   VAL B 279      16.727 -50.859 -39.936  1.00 52.21           C  
ANISOU 3726  C   VAL B 279     6554   6435   6848   -113    360    185       C  
ATOM   3727  O   VAL B 279      16.147 -51.855 -39.530  1.00 52.64           O  
ANISOU 3727  O   VAL B 279     6603   6501   6895    -95    388    200       O  
ATOM   3728  CB  VAL B 279      19.025 -51.353 -38.972  1.00 52.26           C  
ANISOU 3728  CB  VAL B 279     6520   6411   6927   -179    211    272       C  
ATOM   3729  CG1 VAL B 279      19.602 -51.788 -40.329  1.00 52.01           C  
ANISOU 3729  CG1 VAL B 279     6377   6380   7004   -168    247    281       C  
ATOM   3730  CG2 VAL B 279      20.119 -50.780 -38.094  1.00 52.29           C  
ANISOU 3730  CG2 VAL B 279     6561   6387   6919   -228    102    307       C  
ATOM   3731  N   ASP B 280      16.325 -50.168 -40.994  1.00 48.14           N  
ANISOU 3731  N   ASP B 280     6024   5924   6344    -98    407    147       N  
ATOM   3732  CA  ASP B 280      15.124 -50.498 -41.763  1.00 49.24           C  
ANISOU 3732  CA  ASP B 280     6144   6080   6486    -60    491    119       C  
ATOM   3733  C   ASP B 280      13.856 -50.522 -40.869  1.00 57.61           C  
ANISOU 3733  C   ASP B 280     7275   7149   7466    -37    527    111       C  
ATOM   3734  O   ASP B 280      13.010 -51.400 -40.986  1.00 56.83           O  
ANISOU 3734  O   ASP B 280     7151   7063   7379    -12    577    117       O  
ATOM   3735  CB  ASP B 280      15.321 -51.795 -42.574  1.00 50.93           C  
ANISOU 3735  CB  ASP B 280     6269   6299   6784    -48    519    139       C  
ATOM   3736  CG  ASP B 280      16.077 -51.609 -43.872  1.00 50.44           C  
ANISOU 3736  CG  ASP B 280     6143   6227   6794    -51    528    132       C  
ATOM   3737  OD1 ASP B 280      16.397 -50.451 -44.218  1.00 46.29           O  
ANISOU 3737  OD1 ASP B 280     5635   5694   6259    -63    513    111       O  
ATOM   3738  OD2 ASP B 280      16.324 -52.611 -44.549  1.00 54.41           O  
ANISOU 3738  OD2 ASP B 280     6584   6727   7361    -40    552    147       O  
ATOM   3739  N   GLY B 281      13.774 -49.561 -39.953  1.00 58.87           N  
ANISOU 3739  N   GLY B 281     7525   7298   7546    -47    501    101       N  
ATOM   3740  CA  GLY B 281      12.641 -49.424 -39.045  1.00 60.78           C  
ANISOU 3740  CA  GLY B 281     7846   7542   7705    -21    541     96       C  
ATOM   3741  C   GLY B 281      12.508 -50.479 -37.971  1.00 66.61           C  
ANISOU 3741  C   GLY B 281     8603   8286   8422    -17    532    133       C  
ATOM   3742  O   GLY B 281      11.445 -50.596 -37.360  1.00 67.71           O  
ANISOU 3742  O   GLY B 281     8790   8429   8507     13    584    136       O  
ATOM   3743  N   VAL B 282      13.574 -51.235 -37.723  1.00 62.66           N  
ANISOU 3743  N   VAL B 282     8062   7781   7963    -45    470    167       N  
ATOM   3744  CA  VAL B 282      13.609 -52.308 -36.739  1.00 62.26           C  
ANISOU 3744  CA  VAL B 282     8021   7735   7901    -46    452    208       C  
ATOM   3745  C   VAL B 282      14.557 -51.808 -35.694  1.00 64.74           C  
ANISOU 3745  C   VAL B 282     8407   8026   8164    -84    363    224       C  
ATOM   3746  O   VAL B 282      15.727 -51.571 -36.008  1.00 62.35           O  
ANISOU 3746  O   VAL B 282     8067   7710   7911   -119    297    235       O  
ATOM   3747  CB  VAL B 282      14.110 -53.645 -37.362  1.00 66.16           C  
ANISOU 3747  CB  VAL B 282     8405   8239   8495    -48    449    238       C  
ATOM   3748  CG1 VAL B 282      14.337 -54.702 -36.296  1.00 65.79           C  
ANISOU 3748  CG1 VAL B 282     8364   8192   8439    -56    417    284       C  
ATOM   3749  CG2 VAL B 282      13.141 -54.153 -38.422  1.00 65.97           C  
ANISOU 3749  CG2 VAL B 282     8319   8230   8517    -14    529    220       C  
ATOM   3750  N   GLU B 283      14.081 -51.654 -34.459  1.00 63.45           N  
ANISOU 3750  N   GLU B 283     8349   7855   7906    -78    360    231       N  
ATOM   3751  CA  GLU B 283      14.927 -51.129 -33.393  1.00 65.05           C  
ANISOU 3751  CA  GLU B 283     8641   8028   8045   -117    268    246       C  
ATOM   3752  C   GLU B 283      16.092 -52.084 -33.081  1.00 68.35           C  
ANISOU 3752  C   GLU B 283     9001   8442   8526   -155    185    298       C  
ATOM   3753  O   GLU B 283      15.907 -53.294 -33.001  1.00 68.24           O  
ANISOU 3753  O   GLU B 283     8932   8445   8550   -141    208    328       O  
ATOM   3754  CB  GLU B 283      14.118 -50.798 -32.127  1.00 67.12           C  
ANISOU 3754  CB  GLU B 283     9043   8277   8182    -98    290    242       C  
ATOM   3755  CG  GLU B 283      14.809 -49.778 -31.240  1.00 77.70           C  
ANISOU 3755  CG  GLU B 283    10507   9579   9438   -136    202    236       C  
ATOM   3756  CD  GLU B 283      14.110 -49.436 -29.938  1.00 89.61           C  
ANISOU 3756  CD  GLU B 283    12171  11065  10811   -117    223    232       C  
ATOM   3757  OE1 GLU B 283      14.803 -48.941 -29.019  1.00 77.83           O  
ANISOU 3757  OE1 GLU B 283    10788   9538   9248   -154    133    241       O  
ATOM   3758  OE2 GLU B 283      12.878 -49.639 -29.838  1.00 80.30           O  
ANISOU 3758  OE2 GLU B 283    11010   9901   9599    -64    328    224       O  
ATOM   3759  N   VAL B 284      17.285 -51.514 -32.934  1.00 64.71           N  
ANISOU 3759  N   VAL B 284     8551   7956   8079   -202     87    312       N  
ATOM   3760  CA  VAL B 284      18.539 -52.223 -32.651  1.00 64.26           C  
ANISOU 3760  CA  VAL B 284     8437   7887   8090   -244     -4    369       C  
ATOM   3761  C   VAL B 284      19.086 -51.637 -31.344  1.00 71.95           C  
ANISOU 3761  C   VAL B 284     9535   8826   8977   -288   -107    388       C  
ATOM   3762  O   VAL B 284      18.767 -50.492 -31.013  1.00 71.06           O  
ANISOU 3762  O   VAL B 284     9532   8693   8773   -290   -114    351       O  
ATOM   3763  CB  VAL B 284      19.546 -52.134 -33.840  1.00 65.93           C  
ANISOU 3763  CB  VAL B 284     8528   8097   8424   -263    -26    380       C  
ATOM   3764  CG1 VAL B 284      18.973 -52.821 -35.080  1.00 63.83           C  
ANISOU 3764  CG1 VAL B 284     8158   7861   8233   -220     75    361       C  
ATOM   3765  CG2 VAL B 284      19.952 -50.679 -34.161  1.00 65.61           C  
ANISOU 3765  CG2 VAL B 284     8529   8035   8365   -287    -66    352       C  
ATOM   3766  N   HIS B 285      19.873 -52.429 -30.597  1.00 72.10           N  
ANISOU 3766  N   HIS B 285     9542   8833   9019   -322   -188    445       N  
ATOM   3767  CA  HIS B 285      20.338 -52.072 -29.253  1.00 74.01           C  
ANISOU 3767  CA  HIS B 285     9910   9039   9172   -365   -292    470       C  
ATOM   3768  C   HIS B 285      21.849 -52.159 -29.040  1.00 82.23           C  
ANISOU 3768  C   HIS B 285    10905  10050  10288   -430   -427    532       C  
ATOM   3769  O   HIS B 285      22.296 -51.980 -27.907  1.00 83.87           O  
ANISOU 3769  O   HIS B 285    11214  10225  10429   -472   -528    561       O  
ATOM   3770  CB  HIS B 285      19.620 -52.987 -28.227  1.00 74.50           C  
ANISOU 3770  CB  HIS B 285    10034   9111   9162   -342   -261    488       C  
ATOM   3771  CG  HIS B 285      18.141 -53.086 -28.445  1.00 76.81           C  
ANISOU 3771  CG  HIS B 285    10349   9432   9403   -276   -125    443       C  
ATOM   3772  ND1 HIS B 285      17.282 -52.078 -28.038  1.00 78.71           N  
ANISOU 3772  ND1 HIS B 285    10721   9660   9526   -252    -81    398       N  
ATOM   3773  CD2 HIS B 285      17.424 -54.050 -29.069  1.00 77.79           C  
ANISOU 3773  CD2 HIS B 285    10375   9594   9587   -232    -29    443       C  
ATOM   3774  CE1 HIS B 285      16.071 -52.458 -28.422  1.00 77.68           C  
ANISOU 3774  CE1 HIS B 285    10562   9561   9394   -194     42    376       C  
ATOM   3775  NE2 HIS B 285      16.110 -53.640 -29.053  1.00 77.45           N  
ANISOU 3775  NE2 HIS B 285    10396   9562   9470   -182     73    401       N  
ATOM   3776  N   ASN B 286      22.638 -52.356 -30.103  1.00 79.67           N  
ANISOU 3776  N   ASN B 286    10438   9733  10098   -440   -433    554       N  
ATOM   3777  CA  ASN B 286      24.103 -52.484 -29.983  1.00 80.59           C  
ANISOU 3777  CA  ASN B 286    10491   9820  10309   -499   -555    624       C  
ATOM   3778  C   ASN B 286      24.862 -51.120 -29.961  1.00 85.53           C  
ANISOU 3778  C   ASN B 286    11168  10406  10925   -548   -652    624       C  
ATOM   3779  O   ASN B 286      26.087 -51.124 -29.810  1.00 85.20           O  
ANISOU 3779  O   ASN B 286    11076  10334  10963   -602   -763    689       O  
ATOM   3780  CB  ASN B 286      24.662 -53.428 -31.104  1.00 80.41           C  
ANISOU 3780  CB  ASN B 286    10287   9818  10446   -482   -509    659       C  
ATOM   3781  CG  ASN B 286      24.350 -53.033 -32.555  1.00 91.89           C  
ANISOU 3781  CG  ASN B 286    11663  11294  11957   -442   -410    613       C  
ATOM   3782  OD1 ASN B 286      23.192 -53.086 -33.008  1.00 81.00           O  
ANISOU 3782  OD1 ASN B 286    10300   9944  10531   -392   -301    554       O  
ATOM   3783  ND2 ASN B 286      25.372 -52.690 -33.342  1.00 77.36           N  
ANISOU 3783  ND2 ASN B 286     9731   9438  10225   -464   -443    643       N  
ATOM   3784  N   ALA B 287      24.150 -49.967 -30.057  1.00 82.88           N  
ANISOU 3784  N   ALA B 287    10931  10065  10494   -533   -617    557       N  
ATOM   3785  CA  ALA B 287      24.793 -48.646 -30.124  1.00 83.20           C  
ANISOU 3785  CA  ALA B 287    11020  10067  10525   -576   -702    551       C  
ATOM   3786  C   ALA B 287      25.620 -48.262 -28.900  1.00 89.33           C  
ANISOU 3786  C   ALA B 287    11902  10789  11249   -647   -861    597       C  
ATOM   3787  O   ALA B 287      25.335 -48.707 -27.789  1.00 89.14           O  
ANISOU 3787  O   ALA B 287    11980  10755  11135   -654   -891    607       O  
ATOM   3788  CB  ALA B 287      23.761 -47.563 -30.410  1.00 83.47           C  
ANISOU 3788  CB  ALA B 287    11147  10107  10462   -540   -624    469       C  
ATOM   3789  N   LYS B 288      26.644 -47.414 -29.134  1.00 87.38           N  
ANISOU 3789  N   LYS B 288    11634  10506  11062   -700   -963    626       N  
ATOM   3790  CA  LYS B 288      27.560 -46.897 -28.120  1.00 88.70           C  
ANISOU 3790  CA  LYS B 288    11893  10612  11196   -777  -1134    675       C  
ATOM   3791  C   LYS B 288      27.253 -45.434 -27.867  1.00 94.86           C  
ANISOU 3791  C   LYS B 288    12823  11356  11863   -793  -1168    619       C  
ATOM   3792  O   LYS B 288      27.690 -44.566 -28.628  1.00 93.96           O  
ANISOU 3792  O   LYS B 288    12661  11230  11810   -808  -1186    613       O  
ATOM   3793  CB  LYS B 288      29.027 -47.057 -28.555  1.00 91.19           C  
ANISOU 3793  CB  LYS B 288    12063  10906  11680   -831  -1236    764       C  
ATOM   3794  N   THR B 289      26.475 -45.162 -26.807  1.00 93.72           N  
ANISOU 3794  N   THR B 289    12864  11192  11553   -785  -1170    578       N  
ATOM   3795  CA  THR B 289      26.121 -43.797 -26.425  1.00 94.53           C  
ANISOU 3795  CA  THR B 289    13135  11252  11529   -796  -1200    523       C  
ATOM   3796  C   THR B 289      27.250 -43.290 -25.540  1.00 99.93           C  
ANISOU 3796  C   THR B 289    13907  11865  12197   -887  -1396    579       C  
ATOM   3797  O   THR B 289      27.487 -43.847 -24.457  1.00100.55           O  
ANISOU 3797  O   THR B 289    14067  11918  12220   -919  -1479    619       O  
ATOM   3798  CB  THR B 289      24.746 -43.741 -25.740  1.00104.06           C  
ANISOU 3798  CB  THR B 289    14501  12467  12569   -739  -1097    456       C  
ATOM   3799  OG1 THR B 289      23.775 -44.397 -26.564  1.00103.56           O  
ANISOU 3799  OG1 THR B 289    14333  12471  12545   -662   -928    421       O  
ATOM   3800  CG2 THR B 289      24.297 -42.320 -25.483  1.00101.83           C  
ANISOU 3800  CG2 THR B 289    14385  12143  12163   -739  -1102    393       C  
ATOM   3801  N   LYS B 290      27.976 -42.270 -26.027  1.00 96.42           N  
ANISOU 3801  N   LYS B 290    13439  11387  11810   -930  -1475    588       N  
ATOM   3802  CA  LYS B 290      29.111 -41.684 -25.313  1.00 97.78           C  
ANISOU 3802  CA  LYS B 290    13682  11485  11985  -1022  -1674    647       C  
ATOM   3803  C   LYS B 290      28.589 -40.804 -24.158  1.00104.00           C  
ANISOU 3803  C   LYS B 290    14728  12214  12573  -1039  -1731    596       C  
ATOM   3804  O   LYS B 290      27.486 -40.259 -24.265  1.00102.74           O  
ANISOU 3804  O   LYS B 290    14664  12068  12304   -980  -1611    512       O  
ATOM   3805  CB  LYS B 290      29.980 -40.852 -26.286  1.00 99.80           C  
ANISOU 3805  CB  LYS B 290    13824  11725  12371  -1057  -1728    673       C  
ATOM   3806  CG  LYS B 290      30.522 -41.654 -27.473  1.00108.62           C  
ANISOU 3806  CG  LYS B 290    14694  12894  13684  -1036  -1663    724       C  
ATOM   3807  CD  LYS B 290      31.644 -40.935 -28.214  1.00117.79           C  
ANISOU 3807  CD  LYS B 290    15744  14026  14986  -1085  -1750    778       C  
ATOM   3808  CE  LYS B 290      32.354 -41.847 -29.186  1.00129.63           C  
ANISOU 3808  CE  LYS B 290    17011  15562  16679  -1071  -1705    848       C  
ATOM   3809  NZ  LYS B 290      33.510 -41.177 -29.839  1.00141.92           N  
ANISOU 3809  NZ  LYS B 290    18458  17086  18380  -1120  -1792    915       N  
ATOM   3810  N   PRO B 291      29.335 -40.658 -23.039  1.00103.68           N  
ANISOU 3810  N   PRO B 291    14811  12104  12478  -1118  -1908    647       N  
ATOM   3811  CA  PRO B 291      28.847 -39.787 -21.950  1.00104.82           C  
ANISOU 3811  CA  PRO B 291    15220  12184  12423  -1132  -1961    596       C  
ATOM   3812  C   PRO B 291      28.746 -38.321 -22.393  1.00108.74           C  
ANISOU 3812  C   PRO B 291    15788  12647  12884  -1138  -1968    541       C  
ATOM   3813  O   PRO B 291      29.643 -37.826 -23.085  1.00107.56           O  
ANISOU 3813  O   PRO B 291    15523  12483  12862  -1184  -2048    580       O  
ATOM   3814  CB  PRO B 291      29.886 -39.987 -20.838  1.00107.98           C  
ANISOU 3814  CB  PRO B 291    15705  12515  12807  -1227  -2171    677       C  
ATOM   3815  CG  PRO B 291      31.124 -40.415 -21.545  1.00112.27           C  
ANISOU 3815  CG  PRO B 291    16024  13070  13565  -1278  -2258    771       C  
ATOM   3816  CD  PRO B 291      30.663 -41.225 -22.726  1.00106.34           C  
ANISOU 3816  CD  PRO B 291    15060  12411  12933  -1198  -2074    756       C  
ATOM   3817  N   ARG B 292      27.640 -37.643 -22.014  1.00106.14           N  
ANISOU 3817  N   ARG B 292    15641  12302  12384  -1087  -1877    453       N  
ATOM   3818  CA  ARG B 292      27.372 -36.237 -22.381  1.00106.51           C  
ANISOU 3818  CA  ARG B 292    15775  12316  12379  -1082  -1865    391       C  
ATOM   3819  C   ARG B 292      28.517 -35.293 -21.993  1.00111.03           C  
ANISOU 3819  C   ARG B 292    16428  12800  12959  -1183  -2079    433       C  
ATOM   3820  O   ARG B 292      29.184 -35.526 -20.982  1.00110.95           O  
ANISOU 3820  O   ARG B 292    16515  12733  12907  -1252  -2236    488       O  
ATOM   3821  CB  ARG B 292      26.058 -35.740 -21.743  1.00107.40           C  
ANISOU 3821  CB  ARG B 292    16105  12412  12291  -1017  -1750    303       C  
ATOM   3822  N   GLU B 293      28.746 -34.241 -22.814  1.00108.01           N  
ANISOU 3822  N   GLU B 293    16000  12406  12634  -1193  -2087    412       N  
ATOM   3823  CA  GLU B 293      29.805 -33.247 -22.583  1.00109.01           C  
ANISOU 3823  CA  GLU B 293    16188  12448  12781  -1288  -2285    451       C  
ATOM   3824  C   GLU B 293      29.284 -31.795 -22.706  1.00113.29           C  
ANISOU 3824  C   GLU B 293    16877  12946  13220  -1273  -2261    371       C  
ATOM   3825  O   GLU B 293      28.527 -31.475 -23.627  1.00110.53           O  
ANISOU 3825  O   GLU B 293    16455  12650  12891  -1202  -2101    311       O  
ATOM   3826  CB  GLU B 293      31.001 -33.498 -23.528  1.00109.84           C  
ANISOU 3826  CB  GLU B 293    16044  12575  13114  -1336  -2360    540       C  
ATOM   3827  CG  GLU B 293      31.867 -34.691 -23.133  1.00117.67           C  
ANISOU 3827  CG  GLU B 293    16932  13573  14205  -1384  -2458    640       C  
ATOM   3828  CD  GLU B 293      32.631 -34.564 -21.823  1.00140.62           C  
ANISOU 3828  CD  GLU B 293    20003  16387  17039  -1480  -2677    698       C  
ATOM   3829  OE1 GLU B 293      32.991 -33.424 -21.443  1.00140.80           O  
ANISOU 3829  OE1 GLU B 293    20168  16329  17001  -1541  -2811    692       O  
ATOM   3830  OE2 GLU B 293      32.870 -35.610 -21.176  1.00126.04           O  
ANISOU 3830  OE2 GLU B 293    18144  14546  15197  -1497  -2720    751       O  
ATOM   3831  N   GLU B 294      29.708 -30.930 -21.753  1.00112.52           N  
ANISOU 3831  N   GLU B 294    16993  12748  13011  -1344  -2427    373       N  
ATOM   3832  CA  GLU B 294      29.328 -29.512 -21.657  1.00113.16           C  
ANISOU 3832  CA  GLU B 294    17252  12767  12978  -1343  -2436    303       C  
ATOM   3833  C   GLU B 294      29.960 -28.685 -22.784  1.00118.77           C  
ANISOU 3833  C   GLU B 294    17810  13480  13837  -1372  -2474    320       C  
ATOM   3834  O   GLU B 294      29.280 -27.824 -23.339  1.00117.80           O  
ANISOU 3834  O   GLU B 294    17718  13364  13675  -1323  -2370    248       O  
ATOM   3835  CB  GLU B 294      29.745 -28.956 -20.266  1.00116.11           C  
ANISOU 3835  CB  GLU B 294    17897  13023  13194  -1421  -2626    313       C  
ATOM   3836  CG  GLU B 294      29.485 -27.476 -19.996  1.00124.37           C  
ANISOU 3836  CG  GLU B 294    19160  13986  14110  -1433  -2668    247       C  
ATOM   3837  CD  GLU B 294      28.031 -27.064 -19.891  1.00133.51           C  
ANISOU 3837  CD  GLU B 294    20466  15155  15105  -1330  -2469    139       C  
ATOM   3838  OE1 GLU B 294      27.393 -27.407 -18.870  1.00113.03           O  
ANISOU 3838  OE1 GLU B 294    18064  12536  12346  -1299  -2429    110       O  
ATOM   3839  OE2 GLU B 294      27.552 -26.335 -20.791  1.00123.52           O  
ANISOU 3839  OE2 GLU B 294    19140  13917  13874  -1283  -2360     87       O  
ATOM   3840  N   GLN B 295      31.259 -28.929 -23.096  1.00117.45           N  
ANISOU 3840  N   GLN B 295    17484  13303  13840  -1452  -2623    420       N  
ATOM   3841  CA  GLN B 295      32.044 -28.222 -24.139  1.00118.10           C  
ANISOU 3841  CA  GLN B 295    17404  13383  14085  -1489  -2676    457       C  
ATOM   3842  C   GLN B 295      31.192 -27.597 -25.311  1.00122.31           C  
ANISOU 3842  C   GLN B 295    17862  13974  14636  -1405  -2488    377       C  
ATOM   3843  O   GLN B 295      30.695 -28.353 -26.162  1.00120.71           O  
ANISOU 3843  O   GLN B 295    17490  13864  14511  -1332  -2320    363       O  
ATOM   3844  CB  GLN B 295      33.145 -29.149 -24.718  1.00119.26           C  
ANISOU 3844  CB  GLN B 295    17293  13569  14450  -1528  -2735    570       C  
ATOM   3845  CG  GLN B 295      34.528 -28.939 -24.102  1.00131.65           C  
ANISOU 3845  CG  GLN B 295    18879  15052  16090  -1648  -2989    676       C  
ATOM   3846  CD  GLN B 295      34.580 -29.327 -22.645  1.00151.37           C  
ANISOU 3846  CD  GLN B 295    21578  17488  18446  -1695  -3113    691       C  
ATOM   3847  OE1 GLN B 295      34.158 -30.428 -22.258  1.00145.47           O  
ANISOU 3847  OE1 GLN B 295    20824  16787  17662  -1655  -3036    689       O  
ATOM   3848  NE2 GLN B 295      35.108 -28.443 -21.800  1.00144.68           N  
ANISOU 3848  NE2 GLN B 295    20920  16534  17518  -1783  -3311    709       N  
ATOM   3849  N   PHE B 296      30.998 -26.244 -25.364  1.00119.51           N  
ANISOU 3849  N   PHE B 296    17635  13564  14210  -1416  -2515    323       N  
ATOM   3850  CA  PHE B 296      31.530 -25.238 -24.415  1.00120.95           C  
ANISOU 3850  CA  PHE B 296    18033  13630  14292  -1501  -2712    331       C  
ATOM   3851  C   PHE B 296      30.652 -23.974 -24.318  1.00124.78           C  
ANISOU 3851  C   PHE B 296    18713  14072  14626  -1464  -2650    229       C  
ATOM   3852  O   PHE B 296      30.324 -23.552 -23.207  1.00125.45           O  
ANISOU 3852  O   PHE B 296    19056  14079  14530  -1478  -2709    189       O  
ATOM   3853  CB  PHE B 296      32.975 -24.852 -24.786  1.00123.35           C  
ANISOU 3853  CB  PHE B 296    18208  13891  14769  -1601  -2903    431       C  
ATOM   3854  CG  PHE B 296      33.687 -24.070 -23.708  1.00126.48           C  
ANISOU 3854  CG  PHE B 296    18812  14163  15081  -1704  -3139    462       C  
ATOM   3855  CD1 PHE B 296      34.068 -24.680 -22.521  1.00130.49           C  
ANISOU 3855  CD1 PHE B 296    19442  14621  15517  -1760  -3274    508       C  
ATOM   3856  CD2 PHE B 296      33.959 -22.719 -23.871  1.00129.18           C  
ANISOU 3856  CD2 PHE B 296    19237  14436  15412  -1747  -3230    445       C  
ATOM   3857  CE1 PHE B 296      34.713 -23.956 -21.521  1.00133.09           C  
ANISOU 3857  CE1 PHE B 296    19978  14831  15762  -1859  -3500    536       C  
ATOM   3858  CE2 PHE B 296      34.612 -21.996 -22.873  1.00133.67           C  
ANISOU 3858  CE2 PHE B 296    20006  14882  15898  -1847  -3456    473       C  
ATOM   3859  CZ  PHE B 296      34.986 -22.619 -21.704  1.00132.84           C  
ANISOU 3859  CZ  PHE B 296    20025  14726  15720  -1903  -3593    519       C  
ATOM   3860  N   ASN B 297      30.335 -23.351 -25.475  1.00119.78           N  
ANISOU 3860  N   ASN B 297    17960  13481  14069  -1419  -2538    192       N  
ATOM   3861  CA  ASN B 297      29.451 -22.178 -25.639  1.00119.18           C  
ANISOU 3861  CA  ASN B 297    18024  13380  13881  -1371  -2449     98       C  
ATOM   3862  C   ASN B 297      28.492 -21.948 -24.456  1.00122.90           C  
ANISOU 3862  C   ASN B 297    18781  13796  14118  -1335  -2407     22       C  
ATOM   3863  O   ASN B 297      28.529 -20.890 -23.834  1.00125.07           O  
ANISOU 3863  O   ASN B 297    19269  13976  14275  -1370  -2501    -11       O  
ATOM   3864  CB  ASN B 297      28.579 -22.321 -26.914  1.00118.47           C  
ANISOU 3864  CB  ASN B 297    17758  13392  13863  -1274  -2223     49       C  
ATOM   3865  CG  ASN B 297      29.301 -22.523 -28.233  1.00138.88           C  
ANISOU 3865  CG  ASN B 297    20064  16038  16665  -1287  -2215    109       C  
ATOM   3866  OD1 ASN B 297      29.632 -21.559 -28.937  1.00133.36           O  
ANISOU 3866  OD1 ASN B 297    19317  15321  16035  -1308  -2248    109       O  
ATOM   3867  ND2 ASN B 297      29.570 -23.790 -28.597  1.00126.18           N  
ANISOU 3867  ND2 ASN B 297    18271  14502  15171  -1272  -2171    163       N  
ATOM   3868  N   SER B 298      27.687 -22.983 -24.130  1.00116.55           N  
ANISOU 3868  N   SER B 298    17982  13050  13252  -1266  -2271      0       N  
ATOM   3869  CA  SER B 298      26.637 -23.002 -23.091  1.00115.60           C  
ANISOU 3869  CA  SER B 298    18103  12897  12922  -1210  -2186    -67       C  
ATOM   3870  C   SER B 298      25.794 -24.308 -23.121  1.00116.34           C  
ANISOU 3870  C   SER B 298    18108  13082  13012  -1127  -2011    -74       C  
ATOM   3871  O   SER B 298      25.319 -24.744 -22.072  1.00116.09           O  
ANISOU 3871  O   SER B 298    18246  13025  12838  -1106  -1991    -90       O  
ATOM   3872  CB  SER B 298      25.677 -21.823 -23.265  1.00118.64           C  
ANISOU 3872  CB  SER B 298    18625  13253  13199  -1149  -2071   -158       C  
ATOM   3873  OG  SER B 298      25.256 -21.682 -24.612  1.00123.25           O  
ANISOU 3873  OG  SER B 298    19003  13919  13907  -1092  -1927   -179       O  
ATOM   3874  N   THR B 299      25.573 -24.890 -24.328  1.00109.75           N  
ANISOU 3874  N   THR B 299    17020  12351  12330  -1078  -1880    -65       N  
ATOM   3875  CA  THR B 299      24.754 -26.087 -24.552  1.00107.44           C  
ANISOU 3875  CA  THR B 299    16618  12149  12056   -998  -1709    -72       C  
ATOM   3876  C   THR B 299      25.513 -27.385 -24.230  1.00109.11           C  
ANISOU 3876  C   THR B 299    16723  12388  12345  -1041  -1792      8       C  
ATOM   3877  O   THR B 299      26.632 -27.341 -23.727  1.00108.02           O  
ANISOU 3877  O   THR B 299    16613  12194  12235  -1132  -1984     69       O  
ATOM   3878  CB  THR B 299      24.247 -26.094 -26.026  1.00113.29           C  
ANISOU 3878  CB  THR B 299    17140  12979  12926   -935  -1550    -95       C  
ATOM   3879  OG1 THR B 299      25.350 -26.320 -26.915  1.00108.84           O  
ANISOU 3879  OG1 THR B 299    16359  12445  12549   -990  -1637    -28       O  
ATOM   3880  CG2 THR B 299      23.478 -24.808 -26.400  1.00113.10           C  
ANISOU 3880  CG2 THR B 299    17207  12929  12835   -891  -1464   -170       C  
ATOM   3881  N   TYR B 300      24.875 -28.542 -24.508  1.00105.10           N  
ANISOU 3881  N   TYR B 300    16094  11964  11874   -975  -1648      9       N  
ATOM   3882  CA  TYR B 300      25.457 -29.874 -24.334  1.00104.37           C  
ANISOU 3882  CA  TYR B 300    15879  11910  11866  -1001  -1695     81       C  
ATOM   3883  C   TYR B 300      25.626 -30.554 -25.695  1.00104.31           C  
ANISOU 3883  C   TYR B 300    15589  11995  12050   -974  -1608    110       C  
ATOM   3884  O   TYR B 300      24.932 -30.209 -26.657  1.00102.48           O  
ANISOU 3884  O   TYR B 300    15276  11809  11852   -913  -1469     62       O  
ATOM   3885  CB  TYR B 300      24.581 -30.738 -23.403  1.00105.79           C  
ANISOU 3885  CB  TYR B 300    16173  12104  11918   -947  -1605     62       C  
ATOM   3886  CG  TYR B 300      25.005 -30.648 -21.955  1.00109.18           C  
ANISOU 3886  CG  TYR B 300    16828  12446  12209  -1007  -1755     82       C  
ATOM   3887  CD1 TYR B 300      26.026 -31.449 -21.457  1.00111.80           C  
ANISOU 3887  CD1 TYR B 300    17115  12765  12600  -1079  -1905    164       C  
ATOM   3888  CD2 TYR B 300      24.419 -29.729 -21.092  1.00110.88           C  
ANISOU 3888  CD2 TYR B 300    17309  12586  12235   -992  -1752     23       C  
ATOM   3889  CE1 TYR B 300      26.439 -31.353 -20.130  1.00114.32           C  
ANISOU 3889  CE1 TYR B 300    17648  12999  12790  -1140  -2055    185       C  
ATOM   3890  CE2 TYR B 300      24.817 -29.631 -19.761  1.00113.27           C  
ANISOU 3890  CE2 TYR B 300    17836  12801  12400  -1049  -1894     40       C  
ATOM   3891  CZ  TYR B 300      25.821 -30.453 -19.279  1.00121.38           C  
ANISOU 3891  CZ  TYR B 300    18814  13818  13485  -1124  -2049    122       C  
ATOM   3892  OH  TYR B 300      26.232 -30.358 -17.970  1.00124.66           O  
ANISOU 3892  OH  TYR B 300    19456  14144  13765  -1185  -2200    142       O  
ATOM   3893  N   ARG B 301      26.587 -31.491 -25.773  1.00 99.62           N  
ANISOU 3893  N   ARG B 301    14849  11421  11581  -1021  -1695    191       N  
ATOM   3894  CA  ARG B 301      26.849 -32.299 -26.970  1.00 97.29           C  
ANISOU 3894  CA  ARG B 301    14294  11207  11466   -997  -1618    228       C  
ATOM   3895  C   ARG B 301      26.891 -33.770 -26.552  1.00 98.70           C  
ANISOU 3895  C   ARG B 301    14408  11425  11670   -987  -1601    273       C  
ATOM   3896  O   ARG B 301      27.735 -34.150 -25.725  1.00 98.66           O  
ANISOU 3896  O   ARG B 301    14443  11377  11667  -1053  -1749    337       O  
ATOM   3897  CB  ARG B 301      28.160 -31.905 -27.665  1.00 95.60           C  
ANISOU 3897  CB  ARG B 301    13938  10974  11413  -1067  -1744    295       C  
ATOM   3898  CG  ARG B 301      28.353 -32.613 -29.008  1.00 99.82           C  
ANISOU 3898  CG  ARG B 301    14216  11587  12125  -1032  -1644    324       C  
ATOM   3899  CD  ARG B 301      29.517 -32.027 -29.776  1.00103.12           C  
ANISOU 3899  CD  ARG B 301    14503  11983  12693  -1089  -1744    383       C  
ATOM   3900  NE  ARG B 301      29.921 -32.844 -30.925  1.00 97.59           N  
ANISOU 3900  NE  ARG B 301    13564  11347  12168  -1064  -1669    430       N  
ATOM   3901  CZ  ARG B 301      30.731 -33.902 -30.882  1.00101.58           C  
ANISOU 3901  CZ  ARG B 301    13943  11866  12787  -1089  -1717    514       C  
ATOM   3902  NH1 ARG B 301      31.233 -34.324 -29.725  1.00 82.53           N  
ANISOU 3902  NH1 ARG B 301    11614   9410  10335  -1144  -1849    564       N  
ATOM   3903  NH2 ARG B 301      31.040 -34.552 -31.997  1.00 88.33           N  
ANISOU 3903  NH2 ARG B 301    12060  10242  11260  -1058  -1634    549       N  
ATOM   3904  N   VAL B 302      25.968 -34.584 -27.109  1.00 92.32           N  
ANISOU 3904  N   VAL B 302    13502  10693  10882   -906  -1427    243       N  
ATOM   3905  CA  VAL B 302      25.884 -36.024 -26.814  1.00 91.20           C  
ANISOU 3905  CA  VAL B 302    13289  10595  10769   -887  -1390    281       C  
ATOM   3906  C   VAL B 302      26.054 -36.786 -28.143  1.00 91.45           C  
ANISOU 3906  C   VAL B 302    13073  10700  10973   -855  -1299    307       C  
ATOM   3907  O   VAL B 302      25.427 -36.425 -29.150  1.00 90.20           O  
ANISOU 3907  O   VAL B 302    12845  10581  10845   -803  -1176    258       O  
ATOM   3908  CB  VAL B 302      24.583 -36.433 -26.063  1.00 94.54           C  
ANISOU 3908  CB  VAL B 302    13848  11033  11040   -820  -1270    229       C  
ATOM   3909  CG1 VAL B 302      24.815 -37.699 -25.236  1.00 94.64           C  
ANISOU 3909  CG1 VAL B 302    13859  11054  11046   -834  -1310    282       C  
ATOM   3910  CG2 VAL B 302      24.078 -35.305 -25.168  1.00 95.09           C  
ANISOU 3910  CG2 VAL B 302    14164  11034  10932   -822  -1296    174       C  
ATOM   3911  N   VAL B 303      26.941 -37.806 -28.142  1.00 85.81           N  
ANISOU 3911  N   VAL B 303    12232   9999  10374   -889  -1364    386       N  
ATOM   3912  CA  VAL B 303      27.272 -38.588 -29.333  1.00 84.45           C  
ANISOU 3912  CA  VAL B 303    11833   9886  10369   -865  -1293    420       C  
ATOM   3913  C   VAL B 303      26.928 -40.070 -29.168  1.00 83.80           C  
ANISOU 3913  C   VAL B 303    11679   9852  10308   -828  -1219    441       C  
ATOM   3914  O   VAL B 303      27.312 -40.692 -28.182  1.00 82.99           O  
ANISOU 3914  O   VAL B 303    11627   9726  10178   -863  -1306    488       O  
ATOM   3915  CB  VAL B 303      28.767 -38.405 -29.698  1.00 89.55           C  
ANISOU 3915  CB  VAL B 303    12360  10500  11164   -937  -1429    505       C  
ATOM   3916  CG1 VAL B 303      29.170 -39.324 -30.855  1.00 88.89           C  
ANISOU 3916  CG1 VAL B 303    12049  10472  11253   -909  -1351    548       C  
ATOM   3917  CG2 VAL B 303      29.059 -36.949 -30.044  1.00 89.73           C  
ANISOU 3917  CG2 VAL B 303    12430  10482  11183   -968  -1487    483       C  
ATOM   3918  N   SER B 304      26.255 -40.635 -30.177  1.00 77.22           N  
ANISOU 3918  N   SER B 304    10725   9083   9533   -760  -1066    412       N  
ATOM   3919  CA  SER B 304      25.916 -42.054 -30.225  1.00 75.30           C  
ANISOU 3919  CA  SER B 304    10394   8887   9328   -721   -986    431       C  
ATOM   3920  C   SER B 304      26.490 -42.624 -31.521  1.00 75.57           C  
ANISOU 3920  C   SER B 304    10219   8959   9534   -708   -938    467       C  
ATOM   3921  O   SER B 304      26.310 -42.040 -32.593  1.00 72.83           O  
ANISOU 3921  O   SER B 304     9811   8630   9233   -682   -869    434       O  
ATOM   3922  CB  SER B 304      24.408 -42.272 -30.158  1.00 78.03           C  
ANISOU 3922  CB  SER B 304    10809   9270   9567   -647   -838    360       C  
ATOM   3923  OG  SER B 304      24.077 -43.634 -29.924  1.00 85.40           O  
ANISOU 3923  OG  SER B 304    11690  10241  10518   -618   -783    383       O  
ATOM   3924  N   VAL B 305      27.229 -43.735 -31.397  1.00 71.11           N  
ANISOU 3924  N   VAL B 305     9553   8401   9064   -727   -978    539       N  
ATOM   3925  CA  VAL B 305      27.888 -44.422 -32.499  1.00 69.11           C  
ANISOU 3925  CA  VAL B 305     9108   8175   8976   -714   -937    585       C  
ATOM   3926  C   VAL B 305      27.259 -45.803 -32.672  1.00 68.90           C  
ANISOU 3926  C   VAL B 305     9016   8197   8967   -660   -828    581       C  
ATOM   3927  O   VAL B 305      27.255 -46.564 -31.710  1.00 68.93           O  
ANISOU 3927  O   VAL B 305     9064   8196   8932   -673   -870    610       O  
ATOM   3928  CB  VAL B 305      29.408 -44.494 -32.177  1.00 73.87           C  
ANISOU 3928  CB  VAL B 305     9646   8734   9689   -787  -1088    685       C  
ATOM   3929  CG1 VAL B 305      30.054 -45.768 -32.705  1.00 74.04           C  
ANISOU 3929  CG1 VAL B 305     9497   8778   9859   -774  -1057    754       C  
ATOM   3930  CG2 VAL B 305      30.133 -43.269 -32.711  1.00 73.83           C  
ANISOU 3930  CG2 VAL B 305     9618   8694   9739   -825  -1154    698       C  
ATOM   3931  N   LEU B 306      26.727 -46.131 -33.876  1.00 62.40           N  
ANISOU 3931  N   LEU B 306     8092   7416   8199   -602   -694    547       N  
ATOM   3932  CA  LEU B 306      26.207 -47.477 -34.165  1.00 61.00           C  
ANISOU 3932  CA  LEU B 306     7841   7281   8055   -553   -595    548       C  
ATOM   3933  C   LEU B 306      27.134 -48.167 -35.172  1.00 65.95           C  
ANISOU 3933  C   LEU B 306     8296   7915   8846   -549   -574    604       C  
ATOM   3934  O   LEU B 306      27.300 -47.675 -36.283  1.00 66.77           O  
ANISOU 3934  O   LEU B 306     8331   8025   9013   -532   -523    589       O  
ATOM   3935  CB  LEU B 306      24.774 -47.458 -34.715  1.00 59.51           C  
ANISOU 3935  CB  LEU B 306     7682   7133   7797   -487   -454    466       C  
ATOM   3936  CG  LEU B 306      24.169 -48.852 -35.009  1.00 62.69           C  
ANISOU 3936  CG  LEU B 306     8014   7574   8231   -439   -357    467       C  
ATOM   3937  CD1 LEU B 306      23.705 -49.556 -33.741  1.00 64.14           C  
ANISOU 3937  CD1 LEU B 306     8282   7760   8331   -441   -379    479       C  
ATOM   3938  CD2 LEU B 306      23.046 -48.756 -35.946  1.00 62.70           C  
ANISOU 3938  CD2 LEU B 306     8002   7609   8212   -382   -229    402       C  
ATOM   3939  N   THR B 307      27.668 -49.333 -34.818  1.00 62.37           N  
ANISOU 3939  N   THR B 307     7777   7462   8459   -558   -601    667       N  
ATOM   3940  CA  THR B 307      28.527 -50.119 -35.718  1.00 61.93           C  
ANISOU 3940  CA  THR B 307     7562   7409   8561   -547   -570    726       C  
ATOM   3941  C   THR B 307      27.702 -50.733 -36.847  1.00 62.37           C  
ANISOU 3941  C   THR B 307     7556   7505   8635   -477   -418    675       C  
ATOM   3942  O   THR B 307      26.677 -51.357 -36.573  1.00 60.59           O  
ANISOU 3942  O   THR B 307     7376   7307   8337   -443   -356    635       O  
ATOM   3943  CB  THR B 307      29.193 -51.281 -34.949  1.00 74.30           C  
ANISOU 3943  CB  THR B 307     9082   8964  10184   -570   -633    805       C  
ATOM   3944  OG1 THR B 307      29.824 -50.763 -33.782  1.00 83.93           O  
ANISOU 3944  OG1 THR B 307    10379  10144  11366   -638   -782    848       O  
ATOM   3945  CG2 THR B 307      30.213 -52.041 -35.793  1.00 71.79           C  
ANISOU 3945  CG2 THR B 307     8601   8639  10036   -561   -609    877       C  
ATOM   3946  N   VAL B 308      28.179 -50.635 -38.095  1.00 59.33           N  
ANISOU 3946  N   VAL B 308     7068   7121   8355   -457   -362    686       N  
ATOM   3947  CA  VAL B 308      27.485 -51.296 -39.216  1.00 60.30           C  
ANISOU 3947  CA  VAL B 308     7135   7275   8502   -394   -225    644       C  
ATOM   3948  C   VAL B 308      27.710 -52.830 -39.077  1.00 68.75           C  
ANISOU 3948  C   VAL B 308     8134   8351   9638   -377   -200    691       C  
ATOM   3949  O   VAL B 308      28.763 -53.242 -38.578  1.00 70.23           O  
ANISOU 3949  O   VAL B 308     8268   8514   9904   -410   -277    771       O  
ATOM   3950  CB  VAL B 308      27.958 -50.815 -40.611  1.00 62.43           C  
ANISOU 3950  CB  VAL B 308     7323   7539   8860   -375   -166    643       C  
ATOM   3951  CG1 VAL B 308      27.911 -49.302 -40.724  1.00 60.34           C  
ANISOU 3951  CG1 VAL B 308     7117   7264   8546   -398   -203    609       C  
ATOM   3952  CG2 VAL B 308      29.343 -51.361 -40.934  1.00 63.54           C  
ANISOU 3952  CG2 VAL B 308     7340   7653   9151   -387   -191    736       C  
ATOM   3953  N   LEU B 309      26.733 -53.654 -39.496  1.00 65.85           N  
ANISOU 3953  N   LEU B 309     7767   8012   9243   -327   -100    647       N  
ATOM   3954  CA  LEU B 309      26.845 -55.120 -39.439  1.00 65.92           C  
ANISOU 3954  CA  LEU B 309     7712   8025   9309   -306    -68    684       C  
ATOM   3955  C   LEU B 309      26.661 -55.687 -40.821  1.00 65.79           C  
ANISOU 3955  C   LEU B 309     7624   8016   9357   -254     48    664       C  
ATOM   3956  O   LEU B 309      26.021 -55.059 -41.659  1.00 63.40           O  
ANISOU 3956  O   LEU B 309     7346   7725   9019   -230    111    603       O  
ATOM   3957  CB  LEU B 309      25.749 -55.712 -38.548  1.00 66.87           C  
ANISOU 3957  CB  LEU B 309     7910   8168   9327   -296    -59    653       C  
ATOM   3958  CG  LEU B 309      25.680 -55.242 -37.097  1.00 73.36           C  
ANISOU 3958  CG  LEU B 309     8833   8984  10057   -339   -160    662       C  
ATOM   3959  CD1 LEU B 309      24.445 -55.778 -36.446  1.00 74.29           C  
ANISOU 3959  CD1 LEU B 309     9026   9127  10074   -315   -120    623       C  
ATOM   3960  CD2 LEU B 309      26.861 -55.711 -36.306  1.00 76.88           C  
ANISOU 3960  CD2 LEU B 309     9239   9403  10570   -384   -262    749       C  
ATOM   3961  N   HIS B 310      27.182 -56.892 -41.051  1.00 62.62           N  
ANISOU 3961  N   HIS B 310     7141   7605   9047   -237     76    713       N  
ATOM   3962  CA  HIS B 310      26.980 -57.646 -42.312  1.00 61.84           C  
ANISOU 3962  CA  HIS B 310     6987   7507   9004   -184    189    694       C  
ATOM   3963  C   HIS B 310      27.409 -56.833 -43.565  1.00 61.86           C  
ANISOU 3963  C   HIS B 310     6953   7495   9054   -169    238    682       C  
ATOM   3964  O   HIS B 310      28.568 -56.496 -43.647  1.00 62.63           O  
ANISOU 3964  O   HIS B 310     6991   7567   9237   -189    199    743       O  
ATOM   3965  CB  HIS B 310      25.507 -58.142 -42.360  1.00 61.86           C  
ANISOU 3965  CB  HIS B 310     7052   7538   8914   -152    252    624       C  
ATOM   3966  CG  HIS B 310      25.071 -58.742 -41.061  1.00 65.27           C  
ANISOU 3966  CG  HIS B 310     7527   7984   9290   -169    200    638       C  
ATOM   3967  ND1 HIS B 310      25.724 -59.842 -40.521  1.00 67.10           N  
ANISOU 3967  ND1 HIS B 310     7705   8203   9588   -177    171    703       N  
ATOM   3968  CD2 HIS B 310      24.101 -58.337 -40.201  1.00 66.95           C  
ANISOU 3968  CD2 HIS B 310     7831   8218   9388   -180    175    599       C  
ATOM   3969  CE1 HIS B 310      25.137 -60.067 -39.354  1.00 66.86           C  
ANISOU 3969  CE1 HIS B 310     7737   8189   9479   -194    125    701       C  
ATOM   3970  NE2 HIS B 310      24.148 -59.192 -39.124  1.00 66.86           N  
ANISOU 3970  NE2 HIS B 310     7827   8209   9368   -194    130    639       N  
ATOM   3971  N   GLN B 311      26.538 -56.555 -44.533  1.00 56.20           N  
ANISOU 3971  N   GLN B 311     6269   6793   8292   -134    320    612       N  
ATOM   3972  CA  GLN B 311      26.871 -55.691 -45.685  1.00 55.50           C  
ANISOU 3972  CA  GLN B 311     6159   6692   8235   -121    364    596       C  
ATOM   3973  C   GLN B 311      25.741 -54.620 -45.792  1.00 50.34           C  
ANISOU 3973  C   GLN B 311     5594   6064   7469   -123    372    515       C  
ATOM   3974  O   GLN B 311      25.391 -54.157 -46.872  1.00 46.01           O  
ANISOU 3974  O   GLN B 311     5053   5516   6911    -99    436    472       O  
ATOM   3975  CB  GLN B 311      26.989 -56.550 -46.963  1.00 57.23           C  
ANISOU 3975  CB  GLN B 311     6328   6896   8522    -70    471    596       C  
ATOM   3976  N   ASP B 312      25.222 -54.207 -44.628  1.00 47.51           N  
ANISOU 3976  N   ASP B 312     5304   5721   7025   -154    303    499       N  
ATOM   3977  CA  ASP B 312      24.046 -53.338 -44.483  1.00 46.13           C  
ANISOU 3977  CA  ASP B 312     5220   5569   6738   -153    310    428       C  
ATOM   3978  C   ASP B 312      24.145 -51.977 -45.130  1.00 49.01           C  
ANISOU 3978  C   ASP B 312     5600   5929   7090   -160    312    398       C  
ATOM   3979  O   ASP B 312      23.191 -51.563 -45.775  1.00 46.42           O  
ANISOU 3979  O   ASP B 312     5311   5616   6710   -137    370    338       O  
ATOM   3980  CB  ASP B 312      23.661 -53.169 -43.008  1.00 46.95           C  
ANISOU 3980  CB  ASP B 312     5398   5683   6759   -183    235    429       C  
ATOM   3981  CG  ASP B 312      23.114 -54.428 -42.368  1.00 46.82           C  
ANISOU 3981  CG  ASP B 312     5387   5679   6724   -169    249    438       C  
ATOM   3982  OD1 ASP B 312      23.012 -55.454 -43.070  1.00 45.56           O  
ANISOU 3982  OD1 ASP B 312     5174   5520   6617   -137    313    442       O  
ATOM   3983  OD2 ASP B 312      22.841 -54.400 -41.152  1.00 47.37           O  
ANISOU 3983  OD2 ASP B 312     5517   5754   6727   -191    193    445       O  
ATOM   3984  N   TRP B 313      25.276 -51.282 -44.977  1.00 48.12           N  
ANISOU 3984  N   TRP B 313     5458   5795   7031   -194    248    444       N  
ATOM   3985  CA  TRP B 313      25.438 -49.967 -45.582  1.00 47.34           C  
ANISOU 3985  CA  TRP B 313     5370   5690   6927   -203    245    421       C  
ATOM   3986  C   TRP B 313      25.441 -50.073 -47.102  1.00 48.91           C  
ANISOU 3986  C   TRP B 313     5518   5886   7178   -162    343    404       C  
ATOM   3987  O   TRP B 313      24.704 -49.359 -47.779  1.00 47.67           O  
ANISOU 3987  O   TRP B 313     5401   5740   6970   -148    387    346       O  
ATOM   3988  CB  TRP B 313      26.700 -49.271 -45.059  1.00 47.74           C  
ANISOU 3988  CB  TRP B 313     5392   5712   7033   -250    147    484       C  
ATOM   3989  CG  TRP B 313      26.864 -47.889 -45.592  1.00 49.45           C  
ANISOU 3989  CG  TRP B 313     5624   5921   7243   -263    137    463       C  
ATOM   3990  CD1 TRP B 313      27.585 -47.518 -46.684  1.00 52.52           C  
ANISOU 3990  CD1 TRP B 313     5942   6294   7717   -252    174    486       C  
ATOM   3991  CD2 TRP B 313      26.109 -46.739 -45.198  1.00 50.00           C  
ANISOU 3991  CD2 TRP B 313     5789   5998   7209   -280    106    405       C  
ATOM   3992  NE1 TRP B 313      27.378 -46.183 -46.956  1.00 52.32           N  
ANISOU 3992  NE1 TRP B 313     5960   6268   7651   -266    160    449       N  
ATOM   3993  CE2 TRP B 313      26.445 -45.692 -46.081  1.00 54.06           C  
ANISOU 3993  CE2 TRP B 313     6283   6503   7754   -282    120    397       C  
ATOM   3994  CE3 TRP B 313      25.147 -46.502 -44.202  1.00 52.06           C  
ANISOU 3994  CE3 TRP B 313     6155   6273   7353   -288     78    360       C  
ATOM   3995  CZ2 TRP B 313      25.859 -44.428 -45.992  1.00 53.98           C  
ANISOU 3995  CZ2 TRP B 313     6351   6495   7663   -294    102    344       C  
ATOM   3996  CZ3 TRP B 313      24.597 -45.237 -44.086  1.00 53.85           C  
ANISOU 3996  CZ3 TRP B 313     6461   6499   7500   -299     62    311       C  
ATOM   3997  CH2 TRP B 313      24.930 -44.226 -44.992  1.00 54.84           C  
ANISOU 3997  CH2 TRP B 313     6563   6616   7659   -302     74    300       C  
ATOM   3998  N   LEU B 314      26.192 -51.014 -47.621  1.00 47.50           N  
ANISOU 3998  N   LEU B 314     5262   5692   7095   -142    381    452       N  
ATOM   3999  CA  LEU B 314      26.307 -51.225 -49.055  1.00 48.79           C  
ANISOU 3999  CA  LEU B 314     5384   5845   7309   -101    478    442       C  
ATOM   4000  C   LEU B 314      25.025 -51.730 -49.663  1.00 49.82           C  
ANISOU 4000  C   LEU B 314     5562   5993   7373    -65    554    374       C  
ATOM   4001  O   LEU B 314      24.748 -51.374 -50.798  1.00 45.69           O  
ANISOU 4001  O   LEU B 314     5046   5467   6846    -40    619    340       O  
ATOM   4002  CB  LEU B 314      27.450 -52.190 -49.344  1.00 51.35           C  
ANISOU 4002  CB  LEU B 314     5617   6141   7752    -86    502    517       C  
ATOM   4003  CG  LEU B 314      28.819 -51.717 -48.864  1.00 59.74           C  
ANISOU 4003  CG  LEU B 314     6616   7180   8905   -122    427    600       C  
ATOM   4004  CD1 LEU B 314      29.819 -52.802 -48.977  1.00 61.53           C  
ANISOU 4004  CD1 LEU B 314     6753   7379   9246   -106    450    679       C  
ATOM   4005  CD2 LEU B 314      29.272 -50.480 -49.615  1.00 61.92           C  
ANISOU 4005  CD2 LEU B 314     6877   7444   9206   -128    433    601       C  
ATOM   4006  N   ASN B 315      24.210 -52.528 -48.906  1.00 47.95           N  
ANISOU 4006  N   ASN B 315     5362   5775   7083    -63    543    357       N  
ATOM   4007  CA  ASN B 315      22.892 -52.993 -49.378  1.00 47.16           C  
ANISOU 4007  CA  ASN B 315     5308   5691   6920    -34    604    297       C  
ATOM   4008  C   ASN B 315      21.909 -51.898 -49.534  1.00 49.68           C  
ANISOU 4008  C   ASN B 315     5692   6029   7156    -39    607    237       C  
ATOM   4009  O   ASN B 315      20.951 -52.056 -50.285  1.00 48.41           O  
ANISOU 4009  O   ASN B 315     5559   5874   6961    -14    664    191       O  
ATOM   4010  CB  ASN B 315      22.285 -54.024 -48.436  1.00 52.95           C  
ANISOU 4010  CB  ASN B 315     6059   6437   7621    -34    586    302       C  
ATOM   4011  CG  ASN B 315      22.954 -55.364 -48.393  1.00 65.78           C  
ANISOU 4011  CG  ASN B 315     7626   8045   9322    -21    600    353       C  
ATOM   4012  OD1 ASN B 315      22.873 -56.036 -47.376  1.00 70.53           O  
ANISOU 4012  OD1 ASN B 315     8229   8654   9915    -33    560    377       O  
ATOM   4013  ND2 ASN B 315      23.570 -55.843 -49.469  1.00 55.75           N  
ANISOU 4013  ND2 ASN B 315     6309   6750   8125      7    661    370       N  
ATOM   4014  N   GLY B 316      22.131 -50.796 -48.830  1.00 47.04           N  
ANISOU 4014  N   GLY B 316     5384   5699   6791    -71    544    238       N  
ATOM   4015  CA  GLY B 316      21.258 -49.637 -48.897  1.00 46.61           C  
ANISOU 4015  CA  GLY B 316     5393   5659   6658    -76    544    184       C  
ATOM   4016  C   GLY B 316      20.292 -49.572 -47.725  1.00 50.49           C  
ANISOU 4016  C   GLY B 316     5952   6169   7062    -86    512    162       C  
ATOM   4017  O   GLY B 316      19.272 -48.902 -47.827  1.00 52.08           O  
ANISOU 4017  O   GLY B 316     6207   6383   7197    -79    533    115       O  
ATOM   4018  N   LYS B 317      20.609 -50.224 -46.592  1.00 43.21           N  
ANISOU 4018  N   LYS B 317     5031   5247   6139   -102    462    199       N  
ATOM   4019  CA  LYS B 317      19.748 -50.183 -45.433  1.00 42.19           C  
ANISOU 4019  CA  LYS B 317     4972   5132   5925   -108    437    184       C  
ATOM   4020  C   LYS B 317      19.673 -48.754 -44.836  1.00 48.83           C  
ANISOU 4020  C   LYS B 317     5884   5970   6700   -133    388    162       C  
ATOM   4021  O   LYS B 317      20.639 -47.991 -44.915  1.00 47.48           O  
ANISOU 4021  O   LYS B 317     5698   5781   6560   -160    339    182       O  
ATOM   4022  CB  LYS B 317      20.217 -51.189 -44.366  1.00 41.04           C  
ANISOU 4022  CB  LYS B 317     4813   4984   5795   -122    390    233       C  
ATOM   4023  CG  LYS B 317      20.163 -52.611 -44.859  1.00 35.13           C  
ANISOU 4023  CG  LYS B 317     4007   4238   5104    -96    439    251       C  
ATOM   4024  CD  LYS B 317      19.821 -53.551 -43.743  1.00 35.58           C  
ANISOU 4024  CD  LYS B 317     4082   4303   5133    -98    416    274       C  
ATOM   4025  CE  LYS B 317      19.866 -54.987 -44.222  1.00 42.03           C  
ANISOU 4025  CE  LYS B 317     4838   5118   6014    -74    460    295       C  
ATOM   4026  NZ  LYS B 317      19.397 -55.934 -43.161  1.00 52.63           N  
ANISOU 4026  NZ  LYS B 317     6199   6471   7327    -73    444    316       N  
ATOM   4027  N   GLU B 318      18.515 -48.420 -44.240  1.00 47.06           N  
ANISOU 4027  N   GLU B 318     5736   5759   6387   -123    404    127       N  
ATOM   4028  CA  GLU B 318      18.269 -47.104 -43.649  1.00 47.49           C  
ANISOU 4028  CA  GLU B 318     5872   5806   6366   -140    369    101       C  
ATOM   4029  C   GLU B 318      18.610 -47.101 -42.193  1.00 50.95           C  
ANISOU 4029  C   GLU B 318     6372   6233   6755   -167    295    128       C  
ATOM   4030  O   GLU B 318      18.059 -47.881 -41.429  1.00 51.46           O  
ANISOU 4030  O   GLU B 318     6464   6307   6783   -156    305    137       O  
ATOM   4031  CB  GLU B 318      16.799 -46.672 -43.828  1.00 49.21           C  
ANISOU 4031  CB  GLU B 318     6144   6039   6515   -109    436     51       C  
ATOM   4032  CG  GLU B 318      16.477 -46.095 -45.200  1.00 68.95           C  
ANISOU 4032  CG  GLU B 318     8612   8543   9043    -93    489     17       C  
ATOM   4033  CD  GLU B 318      14.999 -45.785 -45.407  1.00 93.87           C  
ANISOU 4033  CD  GLU B 318    11809  11711  12144    -63    553    -22       C  
ATOM   4034  OE1 GLU B 318      14.427 -45.044 -44.573  1.00 83.11           O  
ANISOU 4034  OE1 GLU B 318    10524  10346  10708    -63    546    -38       O  
ATOM   4035  OE2 GLU B 318      14.413 -46.283 -46.397  1.00 82.92           O  
ANISOU 4035  OE2 GLU B 318    10381  10334  10791    -41    609    -34       O  
ATOM   4036  N   TYR B 319      19.490 -46.198 -41.801  1.00 47.71           N  
ANISOU 4036  N   TYR B 319     5989   5799   6340   -205    218    141       N  
ATOM   4037  CA  TYR B 319      19.877 -46.013 -40.422  1.00 47.72           C  
ANISOU 4037  CA  TYR B 319     6065   5781   6285   -238    133    165       C  
ATOM   4038  C   TYR B 319      19.091 -44.806 -39.924  1.00 55.42           C  
ANISOU 4038  C   TYR B 319     7156   6747   7153   -235    135    118       C  
ATOM   4039  O   TYR B 319      19.173 -43.745 -40.525  1.00 54.91           O  
ANISOU 4039  O   TYR B 319     7098   6673   7090   -240    137     92       O  
ATOM   4040  CB  TYR B 319      21.371 -45.790 -40.312  1.00 47.91           C  
ANISOU 4040  CB  TYR B 319     6048   5778   6378   -285     37    216       C  
ATOM   4041  CG  TYR B 319      22.129 -47.055 -40.625  1.00 48.17           C  
ANISOU 4041  CG  TYR B 319     5973   5815   6513   -284     37    270       C  
ATOM   4042  CD1 TYR B 319      22.365 -47.445 -41.939  1.00 48.99           C  
ANISOU 4042  CD1 TYR B 319     5977   5930   6709   -260    102    273       C  
ATOM   4043  CD2 TYR B 319      22.569 -47.893 -39.609  1.00 48.52           C  
ANISOU 4043  CD2 TYR B 319     6022   5852   6560   -305    -21    318       C  
ATOM   4044  CE1 TYR B 319      23.066 -48.608 -42.229  1.00 49.42           C  
ANISOU 4044  CE1 TYR B 319     5938   5982   6856   -254    111    323       C  
ATOM   4045  CE2 TYR B 319      23.273 -49.057 -39.888  1.00 48.66           C  
ANISOU 4045  CE2 TYR B 319     5940   5872   6677   -303    -18    370       C  
ATOM   4046  CZ  TYR B 319      23.544 -49.394 -41.202  1.00 53.71           C  
ANISOU 4046  CZ  TYR B 319     6480   6518   7409   -276     49    373       C  
ATOM   4047  OH  TYR B 319      24.201 -50.546 -41.529  1.00 55.10           O  
ANISOU 4047  OH  TYR B 319     6563   6692   7681   -267     65    423       O  
ATOM   4048  N   LYS B 320      18.262 -45.001 -38.897  1.00 54.64           N  
ANISOU 4048  N   LYS B 320     7146   6650   6964   -221    148    108       N  
ATOM   4049  CA  LYS B 320      17.414 -43.967 -38.334  1.00 55.53           C  
ANISOU 4049  CA  LYS B 320     7379   6751   6970   -210    165     66       C  
ATOM   4050  C   LYS B 320      17.808 -43.753 -36.903  1.00 61.26           C  
ANISOU 4050  C   LYS B 320     8214   7446   7617   -241     81     85       C  
ATOM   4051  O   LYS B 320      17.810 -44.707 -36.123  1.00 60.88           O  
ANISOU 4051  O   LYS B 320     8177   7402   7554   -242     67    115       O  
ATOM   4052  CB  LYS B 320      15.933 -44.389 -38.404  1.00 59.23           C  
ANISOU 4052  CB  LYS B 320     7863   7245   7398   -156    273     39       C  
ATOM   4053  CG  LYS B 320      14.939 -43.396 -37.778  1.00 78.53           C  
ANISOU 4053  CG  LYS B 320    10430   9675   9733   -134    309      2       C  
ATOM   4054  CD  LYS B 320      13.504 -43.780 -38.097  1.00 90.52           C  
ANISOU 4054  CD  LYS B 320    11935  11218  11240    -81    421    -16       C  
ATOM   4055  CE  LYS B 320      12.515 -42.893 -37.396  1.00111.02           C  
ANISOU 4055  CE  LYS B 320    14650  13797  13734    -53    467    -43       C  
ATOM   4056  NZ  LYS B 320      11.149 -43.483 -37.378  1.00126.43           N  
ANISOU 4056  NZ  LYS B 320    16593  15770  15675     -2    568    -40       N  
ATOM   4057  N   CYS B 321      18.113 -42.502 -36.553  1.00 60.23           N  
ANISOU 4057  N   CYS B 321     8171   7282   7432   -268     24     67       N  
ATOM   4058  CA  CYS B 321      18.462 -42.100 -35.205  1.00 63.00           C  
ANISOU 4058  CA  CYS B 321     8651   7593   7691   -301    -64     79       C  
ATOM   4059  C   CYS B 321      17.366 -41.171 -34.688  1.00 69.44           C  
ANISOU 4059  C   CYS B 321     9606   8393   8386   -270    -10     28       C  
ATOM   4060  O   CYS B 321      17.071 -40.160 -35.325  1.00 68.68           O  
ANISOU 4060  O   CYS B 321     9519   8291   8285   -260     21    -10       O  
ATOM   4061  CB  CYS B 321      19.818 -41.414 -35.197  1.00 64.25           C  
ANISOU 4061  CB  CYS B 321     8804   7716   7892   -363   -187    105       C  
ATOM   4062  SG  CYS B 321      20.291 -40.746 -33.590  1.00 69.13           S  
ANISOU 4062  SG  CYS B 321     9600   8274   8393   -413   -315    118       S  
ATOM   4063  N   LYS B 322      16.776 -41.513 -33.536  1.00 68.24           N  
ANISOU 4063  N   LYS B 322     9561   8230   8136   -254      4     31       N  
ATOM   4064  CA  LYS B 322      15.698 -40.741 -32.917  1.00 68.53           C  
ANISOU 4064  CA  LYS B 322     9738   8247   8052   -217     67    -10       C  
ATOM   4065  C   LYS B 322      16.210 -40.217 -31.596  1.00 72.03           C  
ANISOU 4065  C   LYS B 322    10343   8637   8389   -254    -30     -3       C  
ATOM   4066  O   LYS B 322      16.721 -40.994 -30.792  1.00 72.38           O  
ANISOU 4066  O   LYS B 322    10408   8673   8421   -280    -94     37       O  
ATOM   4067  CB  LYS B 322      14.437 -41.600 -32.720  1.00 71.25           C  
ANISOU 4067  CB  LYS B 322    10076   8622   8372   -156    185     -9       C  
ATOM   4068  N   VAL B 323      16.131 -38.901 -31.390  1.00 68.32           N  
ANISOU 4068  N   VAL B 323     9989   8126   7845   -260    -49    -39       N  
ATOM   4069  CA  VAL B 323      16.613 -38.275 -30.165  1.00 69.97           C  
ANISOU 4069  CA  VAL B 323    10370   8273   7942   -298   -148    -38       C  
ATOM   4070  C   VAL B 323      15.445 -37.659 -29.379  1.00 74.02           C  
ANISOU 4070  C   VAL B 323    11055   8757   8314   -247    -61    -77       C  
ATOM   4071  O   VAL B 323      14.671 -36.848 -29.907  1.00 72.36           O  
ANISOU 4071  O   VAL B 323    10857   8547   8088   -207     26   -118       O  
ATOM   4072  CB  VAL B 323      17.725 -37.238 -30.425  1.00 74.25           C  
ANISOU 4072  CB  VAL B 323    10925   8775   8511   -362   -272    -39       C  
ATOM   4073  CG1 VAL B 323      18.461 -36.922 -29.122  1.00 74.99           C  
ANISOU 4073  CG1 VAL B 323    11178   8804   8509   -417   -407    -19       C  
ATOM   4074  CG2 VAL B 323      18.701 -37.743 -31.498  1.00 73.38           C  
ANISOU 4074  CG2 VAL B 323    10621   8699   8560   -396   -319     -2       C  
ATOM   4075  N   SER B 324      15.359 -38.047 -28.101  1.00 70.99           N  
ANISOU 4075  N   SER B 324    10803   8345   7826   -248    -86    -60       N  
ATOM   4076  CA  SER B 324      14.334 -37.614 -27.172  1.00 71.57           C  
ANISOU 4076  CA  SER B 324    11054   8384   7756   -197     -4    -87       C  
ATOM   4077  C   SER B 324      15.032 -36.922 -26.037  1.00 81.02           C  
ANISOU 4077  C   SER B 324    12444   9507   8835   -246   -126    -90       C  
ATOM   4078  O   SER B 324      15.889 -37.530 -25.394  1.00 81.47           O  
ANISOU 4078  O   SER B 324    12519   9550   8887   -298   -238    -50       O  
ATOM   4079  CB  SER B 324      13.552 -38.814 -26.653  1.00 72.22           C  
ANISOU 4079  CB  SER B 324    11124   8497   7819   -149     87    -60       C  
ATOM   4080  OG  SER B 324      12.939 -39.507 -27.727  1.00 75.68           O  
ANISOU 4080  OG  SER B 324    11382   9001   8373   -109    188    -54       O  
ATOM   4081  N   ASN B 325      14.719 -35.631 -25.824  1.00 81.18           N  
ANISOU 4081  N   ASN B 325    12608   9475   8763   -235   -113   -134       N  
ATOM   4082  CA  ASN B 325      15.322 -34.856 -24.750  1.00 83.73           C  
ANISOU 4082  CA  ASN B 325    13137   9717   8960   -281   -231   -142       C  
ATOM   4083  C   ASN B 325      14.340 -34.836 -23.574  1.00 91.36           C  
ANISOU 4083  C   ASN B 325    14301  10645   9766   -224   -139   -157       C  
ATOM   4084  O   ASN B 325      13.155 -34.554 -23.775  1.00 90.63           O  
ANISOU 4084  O   ASN B 325    14226  10565   9645   -147     16   -185       O  
ATOM   4085  CB  ASN B 325      15.672 -33.440 -25.236  1.00 83.48           C  
ANISOU 4085  CB  ASN B 325    13149   9644   8926   -308   -282   -181       C  
ATOM   4086  CG  ASN B 325      16.314 -32.532 -24.207  1.00105.19           C  
ANISOU 4086  CG  ASN B 325    16117  12301  11549   -361   -414   -192       C  
ATOM   4087  OD1 ASN B 325      16.137 -31.310 -24.260  1.00107.52           O  
ANISOU 4087  OD1 ASN B 325    16517  12548  11785   -357   -411   -235       O  
ATOM   4088  ND2 ASN B 325      17.124 -33.065 -23.276  1.00 89.26           N  
ANISOU 4088  ND2 ASN B 325    14174  10252   9489   -419   -544   -152       N  
ATOM   4089  N   LYS B 326      14.820 -35.188 -22.364  1.00 91.21           N  
ANISOU 4089  N   LYS B 326    14426  10581   9647   -258   -231   -132       N  
ATOM   4090  CA  LYS B 326      13.966 -35.241 -21.167  1.00 92.77           C  
ANISOU 4090  CA  LYS B 326    14826  10739   9685   -204   -147   -140       C  
ATOM   4091  C   LYS B 326      13.536 -33.822 -20.762  1.00 98.40           C  
ANISOU 4091  C   LYS B 326    15747  11375  10264   -180   -117   -194       C  
ATOM   4092  O   LYS B 326      14.336 -33.062 -20.207  1.00 98.25           O  
ANISOU 4092  O   LYS B 326    15878  11284  10167   -241   -256   -205       O  
ATOM   4093  CB  LYS B 326      14.661 -35.976 -20.002  1.00 96.25           C  
ANISOU 4093  CB  LYS B 326    15371  11148  10053   -253   -264    -98       C  
ATOM   4094  N   GLY B 327      12.280 -33.493 -21.079  1.00 95.72           N  
ANISOU 4094  N   GLY B 327    15410  11051   9909    -92     63   -222       N  
ATOM   4095  CA  GLY B 327      11.689 -32.183 -20.834  1.00 97.21           C  
ANISOU 4095  CA  GLY B 327    15773  11174   9987    -52    128   -272       C  
ATOM   4096  C   GLY B 327      10.964 -31.586 -22.027  1.00102.66           C  
ANISOU 4096  C   GLY B 327    16333  11903  10771     -3    245   -301       C  
ATOM   4097  O   GLY B 327      10.231 -30.608 -21.852  1.00102.18           O  
ANISOU 4097  O   GLY B 327    16402  11795  10626     49    337   -338       O  
ATOM   4098  N   LEU B 328      11.164 -32.146 -23.250  1.00100.37           N  
ANISOU 4098  N   LEU B 328    15790  11693  10652    -19    244   -283       N  
ATOM   4099  CA  LEU B 328      10.542 -31.642 -24.478  1.00100.70           C  
ANISOU 4099  CA  LEU B 328    15693  11775  10794     19    342   -307       C  
ATOM   4100  C   LEU B 328       9.370 -32.546 -24.953  1.00105.57           C  
ANISOU 4100  C   LEU B 328    16167  12461  11485     95    508   -283       C  
ATOM   4101  O   LEU B 328       9.402 -33.752 -24.683  1.00104.87           O  
ANISOU 4101  O   LEU B 328    16010  12409  11425     94    508   -243       O  
ATOM   4102  CB  LEU B 328      11.606 -31.478 -25.582  1.00100.34           C  
ANISOU 4102  CB  LEU B 328    15481  11760  10882    -53    220   -307       C  
ATOM   4103  CG  LEU B 328      12.219 -30.077 -25.670  1.00105.91           C  
ANISOU 4103  CG  LEU B 328    16288  12404  11547    -97    127   -345       C  
ATOM   4104  CD1 LEU B 328      13.549 -30.104 -26.368  1.00105.84           C  
ANISOU 4104  CD1 LEU B 328    16148  12413  11652   -183    -29   -327       C  
ATOM   4105  CD2 LEU B 328      11.286 -29.107 -26.402  1.00109.35           C  
ANISOU 4105  CD2 LEU B 328    16711  12840  11997    -38    252   -385       C  
ATOM   4106  N   PRO B 329       8.349 -32.000 -25.680  1.00102.66           N  
ANISOU 4106  N   PRO B 329    15744  12106  11154    157    643   -302       N  
ATOM   4107  CA  PRO B 329       7.188 -32.827 -26.070  1.00102.15           C  
ANISOU 4107  CA  PRO B 329    15555  12098  11158    227    795   -272       C  
ATOM   4108  C   PRO B 329       7.366 -33.891 -27.158  1.00105.05           C  
ANISOU 4108  C   PRO B 329    15678  12549  11687    206    782   -243       C  
ATOM   4109  O   PRO B 329       6.640 -34.888 -27.115  1.00104.37           O  
ANISOU 4109  O   PRO B 329    15516  12502  11638    249    871   -208       O  
ATOM   4110  CB  PRO B 329       6.148 -31.790 -26.536  1.00103.78           C  
ANISOU 4110  CB  PRO B 329    15784  12287  11361    291    925   -299       C  
ATOM   4111  CG  PRO B 329       6.638 -30.486 -26.076  1.00108.88           C  
ANISOU 4111  CG  PRO B 329    16611  12857  11901    267    859   -344       C  
ATOM   4112  CD  PRO B 329       8.120 -30.589 -26.053  1.00104.50           C  
ANISOU 4112  CD  PRO B 329    16047  12298  11360    171    669   -348       C  
ATOM   4113  N   SER B 330       8.249 -33.668 -28.146  1.00100.86           N  
ANISOU 4113  N   SER B 330    15028  12042  11252    147    682   -257       N  
ATOM   4114  CA  SER B 330       8.420 -34.584 -29.287  1.00 99.81           C  
ANISOU 4114  CA  SER B 330    14671  11982  11271    130    675   -234       C  
ATOM   4115  C   SER B 330       9.782 -35.332 -29.258  1.00103.48           C  
ANISOU 4115  C   SER B 330    15072  12463  11782     54    527   -211       C  
ATOM   4116  O   SER B 330      10.460 -35.350 -28.220  1.00104.45           O  
ANISOU 4116  O   SER B 330    15323  12546  11819     19    438   -203       O  
ATOM   4117  CB  SER B 330       8.257 -33.799 -30.594  1.00102.08           C  
ANISOU 4117  CB  SER B 330    14854  12288  11645    131    700   -262       C  
ATOM   4118  N   SER B 331      10.128 -36.013 -30.379  1.00 97.12           N  
ANISOU 4118  N   SER B 331    14073  11715  11115     32    508   -195       N  
ATOM   4119  CA  SER B 331      11.405 -36.695 -30.582  1.00 95.30           C  
ANISOU 4119  CA  SER B 331    13752  11503  10956    -34    382   -169       C  
ATOM   4120  C   SER B 331      11.922 -36.289 -31.980  1.00 96.05           C  
ANISOU 4120  C   SER B 331    13704  11623  11167    -62    352   -183       C  
ATOM   4121  O   SER B 331      11.126 -36.219 -32.925  1.00 94.49           O  
ANISOU 4121  O   SER B 331    13416  11457  11028    -22    447   -196       O  
ATOM   4122  CB  SER B 331      11.258 -38.214 -30.470  1.00 20.00           C  
ATOM   4123  OG  SER B 331      10.388 -38.717 -31.468  1.00 20.00           O  
ATOM   4124  N   ILE B 332      13.233 -35.981 -32.095  1.00 90.79           N  
ANISOU 4124  N   ILE B 332    13024  10939  10534   -129    220   -176       N  
ATOM   4125  CA  ILE B 332      13.854 -35.558 -33.357  1.00 89.13           C  
ANISOU 4125  CA  ILE B 332    12687  10747  10431   -157    185   -184       C  
ATOM   4126  C   ILE B 332      14.436 -36.786 -34.064  1.00 89.50           C  
ANISOU 4126  C   ILE B 332    12562  10842  10599   -176    164   -146       C  
ATOM   4127  O   ILE B 332      15.373 -37.391 -33.547  1.00 88.58           O  
ANISOU 4127  O   ILE B 332    12440  10718  10497   -219     69   -109       O  
ATOM   4128  CB  ILE B 332      14.960 -34.499 -33.125  1.00 93.17           C  
ANISOU 4128  CB  ILE B 332    13274  11208  10919   -219     56   -192       C  
ATOM   4129  CG1 ILE B 332      14.509 -33.366 -32.173  1.00 94.67           C  
ANISOU 4129  CG1 ILE B 332    13666  11336  10968   -207     58   -228       C  
ATOM   4130  CG2 ILE B 332      15.424 -33.913 -34.459  1.00 93.73           C  
ANISOU 4130  CG2 ILE B 332    13222  11296  11095   -238     41   -202       C  
ATOM   4131  CD1 ILE B 332      15.558 -33.037 -31.076  1.00103.12           C  
ANISOU 4131  CD1 ILE B 332    14871  12345  11964   -271    -91   -212       C  
ATOM   4132  N   GLU B 333      13.889 -37.139 -35.243  1.00 83.86           N  
ANISOU 4132  N   GLU B 333    11715  10174   9973   -144    249   -152       N  
ATOM   4133  CA  GLU B 333      14.301 -38.291 -36.053  1.00 82.02           C  
ANISOU 4133  CA  GLU B 333    11323   9986   9855   -152    249   -121       C  
ATOM   4134  C   GLU B 333      15.104 -37.888 -37.309  1.00 83.75           C  
ANISOU 4134  C   GLU B 333    11430  10215  10175   -180    213   -123       C  
ATOM   4135  O   GLU B 333      14.647 -37.043 -38.072  1.00 82.68           O  
ANISOU 4135  O   GLU B 333    11283  10081  10049   -162    262   -156       O  
ATOM   4136  CB  GLU B 333      13.057 -39.083 -36.486  1.00 82.71           C  
ANISOU 4136  CB  GLU B 333    11348  10113   9965    -94    371   -122       C  
ATOM   4137  CG  GLU B 333      12.306 -39.737 -35.340  1.00 94.34           C  
ANISOU 4137  CG  GLU B 333    12901  11583  11361    -63    414   -107       C  
ATOM   4138  CD  GLU B 333      10.824 -39.925 -35.607  1.00124.57           C  
ANISOU 4138  CD  GLU B 333    16715  15434  15184     -1    543   -116       C  
ATOM   4139  OE1 GLU B 333      10.459 -40.924 -36.269  1.00121.28           O  
ANISOU 4139  OE1 GLU B 333    16183  15053  14843     16    588    -97       O  
ATOM   4140  OE2 GLU B 333      10.027 -39.064 -35.167  1.00122.33           O  
ANISOU 4140  OE2 GLU B 333    16533  15125  14822     31    599   -139       O  
ATOM   4141  N   LYS B 334      16.268 -38.534 -37.549  1.00 79.08           N  
ANISOU 4141  N   LYS B 334    10751   9630   9666   -220    138    -84       N  
ATOM   4142  CA  LYS B 334      17.117 -38.306 -38.738  1.00 76.93           C  
ANISOU 4142  CA  LYS B 334    10363   9366   9500   -244    110    -75       C  
ATOM   4143  C   LYS B 334      17.405 -39.656 -39.395  1.00 77.48           C  
ANISOU 4143  C   LYS B 334    10298   9471   9668   -236    136    -41       C  
ATOM   4144  O   LYS B 334      17.584 -40.639 -38.683  1.00 77.52           O  
ANISOU 4144  O   LYS B 334    10304   9481   9669   -241    114     -9       O  
ATOM   4145  CB  LYS B 334      18.432 -37.599 -38.356  1.00 79.94           C  
ANISOU 4145  CB  LYS B 334    10774   9707   9892   -305    -18    -51       C  
ATOM   4146  N   THR B 335      17.401 -39.723 -40.739  1.00 70.98           N  
ANISOU 4146  N   THR B 335     9369   8672   8928   -221    186    -49       N  
ATOM   4147  CA  THR B 335      17.645 -40.968 -41.474  1.00 68.98           C  
ANISOU 4147  CA  THR B 335     8996   8446   8766   -210    219    -21       C  
ATOM   4148  C   THR B 335      18.684 -40.786 -42.569  1.00 69.75           C  
ANISOU 4148  C   THR B 335     8995   8542   8965   -230    196     -2       C  
ATOM   4149  O   THR B 335      18.627 -39.800 -43.312  1.00 67.90           O  
ANISOU 4149  O   THR B 335     8757   8303   8738   -229    212    -29       O  
ATOM   4150  CB  THR B 335      16.364 -41.517 -42.112  1.00 74.29           C  
ANISOU 4150  CB  THR B 335     9639   9150   9436   -160    328    -47       C  
ATOM   4151  OG1 THR B 335      15.864 -40.592 -43.076  1.00 82.37           O  
ANISOU 4151  OG1 THR B 335    10655  10177  10463   -144    375    -85       O  
ATOM   4152  CG2 THR B 335      15.313 -41.812 -41.109  1.00 70.46           C  
ANISOU 4152  CG2 THR B 335     9235   8670   8868   -134    363    -56       C  
ATOM   4153  N   ILE B 336      19.590 -41.783 -42.708  1.00 64.73           N  
ANISOU 4153  N   ILE B 336     8274   7910   8411   -243    169     47       N  
ATOM   4154  CA  ILE B 336      20.622 -41.810 -43.744  1.00 63.17           C  
ANISOU 4154  CA  ILE B 336     7974   7708   8320   -255    160     76       C  
ATOM   4155  C   ILE B 336      20.775 -43.207 -44.296  1.00 67.04           C  
ANISOU 4155  C   ILE B 336     8372   8217   8884   -233    208    103       C  
ATOM   4156  O   ILE B 336      20.505 -44.205 -43.616  1.00 65.96           O  
ANISOU 4156  O   ILE B 336     8244   8090   8730   -225    210    118       O  
ATOM   4157  CB  ILE B 336      22.003 -41.248 -43.281  1.00 66.14           C  
ANISOU 4157  CB  ILE B 336     8343   8050   8737   -308     49    124       C  
ATOM   4158  CG1 ILE B 336      22.653 -42.126 -42.192  1.00 66.43           C  
ANISOU 4158  CG1 ILE B 336     8382   8075   8783   -335    -24    177       C  
ATOM   4159  CG2 ILE B 336      21.868 -39.796 -42.824  1.00 67.82           C  
ANISOU 4159  CG2 ILE B 336     8653   8238   8876   -332     -1     93       C  
ATOM   4160  CD1 ILE B 336      24.078 -41.841 -41.975  1.00 72.76           C  
ANISOU 4160  CD1 ILE B 336     9144   8844   9658   -385   -127    239       C  
ATOM   4161  N   SER B 337      21.308 -43.263 -45.507  1.00 63.71           N  
ANISOU 4161  N   SER B 337     7865   7796   8547   -224    243    114       N  
ATOM   4162  CA  SER B 337      21.550 -44.496 -46.217  1.00 63.00           C  
ANISOU 4162  CA  SER B 337     7690   7716   8533   -200    294    139       C  
ATOM   4163  C   SER B 337      22.453 -44.231 -47.405  1.00 67.50           C  
ANISOU 4163  C   SER B 337     8181   8274   9193   -198    314    161       C  
ATOM   4164  O   SER B 337      22.566 -43.086 -47.860  1.00 66.32           O  
ANISOU 4164  O   SER B 337     8043   8116   9038   -208    308    143       O  
ATOM   4165  CB  SER B 337      20.229 -45.077 -46.716  1.00 64.97           C  
ANISOU 4165  CB  SER B 337     7953   7990   8742   -158    382     95       C  
ATOM   4166  OG  SER B 337      19.533 -44.167 -47.546  1.00 68.78           O  
ANISOU 4166  OG  SER B 337     8458   8479   9197   -143    428     47       O  
ATOM   4167  N   LYS B 338      23.055 -45.298 -47.943  1.00 64.36           N  
ANISOU 4167  N   LYS B 338     7703   7872   8878   -182    347    200       N  
ATOM   4168  CA  LYS B 338      23.846 -45.193 -49.163  1.00 64.44           C  
ANISOU 4168  CA  LYS B 338     7638   7869   8976   -170    387    223       C  
ATOM   4169  C   LYS B 338      22.852 -44.854 -50.288  1.00 70.81           C  
ANISOU 4169  C   LYS B 338     8470   8691   9744   -137    470    161       C  
ATOM   4170  O   LYS B 338      21.718 -45.336 -50.268  1.00 69.93           O  
ANISOU 4170  O   LYS B 338     8398   8598   9574   -115    511    120       O  
ATOM   4171  CB  LYS B 338      24.594 -46.496 -49.457  1.00 66.37           C  
ANISOU 4171  CB  LYS B 338     7804   8104   9310   -153    416    276       C  
ATOM   4172  CG  LYS B 338      25.544 -46.392 -50.619  1.00 64.26           C  
ANISOU 4172  CG  LYS B 338     7461   7815   9138   -138    461    312       C  
ATOM   4173  CD  LYS B 338      26.377 -47.650 -50.794  1.00 70.78           C  
ANISOU 4173  CD  LYS B 338     8210   8624  10057   -120    489    373       C  
ATOM   4174  CE  LYS B 338      27.487 -47.478 -51.809  1.00 73.96           C  
ANISOU 4174  CE  LYS B 338     8535   9000  10565   -105    531    423       C  
ATOM   4175  NZ  LYS B 338      27.032 -46.778 -53.045  1.00 89.80           N  
ANISOU 4175  NZ  LYS B 338    10565  11010  12546    -80    602    373       N  
ATOM   4176  N   ALA B 339      23.247 -43.963 -51.204  1.00 70.31           N  
ANISOU 4176  N   ALA B 339     8386   8617   9711   -136    489    157       N  
ATOM   4177  CA  ALA B 339      22.387 -43.509 -52.300  1.00 70.33           C  
ANISOU 4177  CA  ALA B 339     8413   8630   9680   -110    558    103       C  
ATOM   4178  C   ALA B 339      21.882 -44.662 -53.149  1.00 72.50           C  
ANISOU 4178  C   ALA B 339     8671   8909   9966    -71    639     89       C  
ATOM   4179  O   ALA B 339      20.680 -44.905 -53.205  1.00 73.15           O  
ANISOU 4179  O   ALA B 339     8800   9007   9986    -57    668     44       O  
ATOM   4180  CB  ALA B 339      23.157 -42.520 -53.171  1.00 71.74           C  
ANISOU 4180  CB  ALA B 339     8557   8792   9909   -116    565    117       C  
ATOM   4181  N   LYS B 340      22.808 -45.400 -53.753  1.00 67.96           N  
ANISOU 4181  N   LYS B 340     8033   8315   9472    -55    672    132       N  
ATOM   4182  CA  LYS B 340      22.506 -46.546 -54.614  1.00 67.02           C  
ANISOU 4182  CA  LYS B 340     7905   8192   9370    -18    748    124       C  
ATOM   4183  C   LYS B 340      23.007 -47.799 -53.883  1.00 67.00           C  
ANISOU 4183  C   LYS B 340     7864   8182   9409    -16    732    170       C  
ATOM   4184  O   LYS B 340      24.215 -47.980 -53.738  1.00 65.93           O  
ANISOU 4184  O   LYS B 340     7669   8029   9353    -23    715    230       O  
ATOM   4185  CB  LYS B 340      23.196 -46.402 -55.993  1.00 69.51           C  
ANISOU 4185  CB  LYS B 340     8185   8483   9744      7    815    138       C  
ATOM   4186  N   GLY B 341      22.069 -48.598 -53.368  1.00 60.31           N  
ANISOU 4186  N   GLY B 341     7051   7350   8512    -10    733    146       N  
ATOM   4187  CA  GLY B 341      22.377 -49.832 -52.659  1.00 57.98           C  
ANISOU 4187  CA  GLY B 341     6729   7053   8249     -8    719    184       C  
ATOM   4188  C   GLY B 341      22.642 -51.010 -53.578  1.00 56.43           C  
ANISOU 4188  C   GLY B 341     6500   6834   8106     29    791    199       C  
ATOM   4189  O   GLY B 341      22.170 -51.056 -54.716  1.00 55.96           O  
ANISOU 4189  O   GLY B 341     6465   6767   8033     54    854    164       O  
ATOM   4190  N   GLN B 342      23.414 -51.956 -53.086  1.00 51.00           N  
ANISOU 4190  N   GLN B 342     5764   6134   7480     30    779    252       N  
ATOM   4191  CA  GLN B 342      23.781 -53.185 -53.786  1.00 50.11           C  
ANISOU 4191  CA  GLN B 342     5621   5995   7424     66    845    275       C  
ATOM   4192  C   GLN B 342      22.811 -54.289 -53.301  1.00 51.55           C  
ANISOU 4192  C   GLN B 342     5834   6189   7563     73    845    253       C  
ATOM   4193  O   GLN B 342      22.945 -54.779 -52.187  1.00 49.60           O  
ANISOU 4193  O   GLN B 342     5570   5952   7323     56    794    283       O  
ATOM   4194  CB  GLN B 342      25.219 -53.592 -53.436  1.00 51.95           C  
ANISOU 4194  CB  GLN B 342     5774   6205   7760     63    830    355       C  
ATOM   4195  N   PRO B 343      21.808 -54.698 -54.075  1.00 48.18           N  
ANISOU 4195  N   PRO B 343     5455   5760   7092     95    894    204       N  
ATOM   4196  CA  PRO B 343      20.911 -55.757 -53.573  1.00 47.28           C  
ANISOU 4196  CA  PRO B 343     5364   5654   6945     99    888    191       C  
ATOM   4197  C   PRO B 343      21.572 -57.139 -53.444  1.00 46.89           C  
ANISOU 4197  C   PRO B 343     5274   5582   6962    118    907    236       C  
ATOM   4198  O   PRO B 343      22.688 -57.341 -53.928  1.00 44.57           O  
ANISOU 4198  O   PRO B 343     4935   5259   6741    134    941    276       O  
ATOM   4199  CB  PRO B 343      19.783 -55.733 -54.593  1.00 48.97           C  
ANISOU 4199  CB  PRO B 343     5635   5863   7107    116    931    134       C  
ATOM   4200  CG  PRO B 343      20.492 -55.377 -55.867  1.00 53.41           C  
ANISOU 4200  CG  PRO B 343     6193   6396   7704    137    987    133       C  
ATOM   4201  CD  PRO B 343      21.428 -54.275 -55.440  1.00 48.30           C  
ANISOU 4201  CD  PRO B 343     5506   5760   7085    116    953    162       C  
ATOM   4202  N   ARG B 344      20.938 -58.058 -52.690  1.00 42.67           N  
ANISOU 4202  N   ARG B 344     4748   5058   6408    114    885    238       N  
ATOM   4203  CA  ARG B 344      21.422 -59.438 -52.536  1.00 43.34           C  
ANISOU 4203  CA  ARG B 344     4798   5121   6550    131    902    278       C  
ATOM   4204  C   ARG B 344      20.458 -60.357 -53.305  1.00 47.48           C  
ANISOU 4204  C   ARG B 344     5367   5626   7046    156    948    240       C  
ATOM   4205  O   ARG B 344      19.238 -60.215 -53.234  1.00 47.30           O  
ANISOU 4205  O   ARG B 344     5391   5623   6960    147    934    200       O  
ATOM   4206  CB  ARG B 344      21.511 -59.886 -51.076  1.00 45.01           C  
ANISOU 4206  CB  ARG B 344     4984   5354   6765    108    838    315       C  
ATOM   4207  CG  ARG B 344      22.396 -59.028 -50.183  1.00 50.88           C  
ANISOU 4207  CG  ARG B 344     5695   6111   7528     76    775    354       C  
ATOM   4208  CD  ARG B 344      22.593 -59.723 -48.824  1.00 65.13           C  
ANISOU 4208  CD  ARG B 344     7477   7927   9343     55    716    399       C  
ATOM   4209  NE  ARG B 344      22.666 -58.794 -47.688  1.00 69.63           N  
ANISOU 4209  NE  ARG B 344     8063   8520   9871     16    637    408       N  
ATOM   4210  CZ  ARG B 344      23.029 -59.119 -46.442  1.00 83.40           C  
ANISOU 4210  CZ  ARG B 344     9795  10272  11621     -9    571    452       C  
ATOM   4211  NH1 ARG B 344      23.347 -60.374 -46.138  1.00 63.31           N  
ANISOU 4211  NH1 ARG B 344     7212   7717   9128      0    574    493       N  
ATOM   4212  NH2 ARG B 344      23.095 -58.184 -45.494  1.00 74.59           N  
ANISOU 4212  NH2 ARG B 344     8711   9172  10459    -45    499    456       N  
ATOM   4213  N   GLU B 345      21.012 -61.240 -54.081  1.00 45.42           N  
ANISOU 4213  N   GLU B 345     5096   5325   6836    187   1004    256       N  
ATOM   4214  CA  GLU B 345      20.256 -62.146 -54.935  1.00 46.03           C  
ANISOU 4214  CA  GLU B 345     5224   5373   6893    210   1047    224       C  
ATOM   4215  C   GLU B 345      19.560 -63.284 -54.167  1.00 48.47           C  
ANISOU 4215  C   GLU B 345     5535   5688   7193    204   1018    231       C  
ATOM   4216  O   GLU B 345      20.218 -64.015 -53.413  1.00 50.32           O  
ANISOU 4216  O   GLU B 345     5721   5921   7478    205   1004    278       O  
ATOM   4217  CB  GLU B 345      21.215 -62.774 -55.966  1.00 47.74           C  
ANISOU 4217  CB  GLU B 345     5434   5535   7169    249   1122    244       C  
ATOM   4218  CG  GLU B 345      20.526 -63.577 -57.042  1.00 60.54           C  
ANISOU 4218  CG  GLU B 345     7126   7116   8762    275   1169    206       C  
ATOM   4219  CD  GLU B 345      21.400 -63.827 -58.258  1.00 79.28           C  
ANISOU 4219  CD  GLU B 345     9517   9432  11173    317   1254    213       C  
ATOM   4220  OE1 GLU B 345      21.624 -62.874 -59.040  1.00 79.99           O  
ANISOU 4220  OE1 GLU B 345     9626   9518  11248    323   1284    196       O  
ATOM   4221  OE2 GLU B 345      21.895 -64.967 -58.406  1.00 63.76           O  
ANISOU 4221  OE2 GLU B 345     7546   7426   9253    345   1295    240       O  
ATOM   4222  N   PRO B 346      18.266 -63.535 -54.427  1.00 43.39           N  
ANISOU 4222  N   PRO B 346     4944   5046   6494    200   1011    191       N  
ATOM   4223  CA  PRO B 346      17.637 -64.716 -53.842  1.00 42.38           C  
ANISOU 4223  CA  PRO B 346     4817   4917   6370    199    991    203       C  
ATOM   4224  C   PRO B 346      18.232 -66.035 -54.333  1.00 44.03           C  
ANISOU 4224  C   PRO B 346     5021   5076   6632    228   1033    225       C  
ATOM   4225  O   PRO B 346      18.541 -66.195 -55.510  1.00 42.28           O  
ANISOU 4225  O   PRO B 346     4834   4810   6419    253   1088    208       O  
ATOM   4226  CB  PRO B 346      16.182 -64.630 -54.301  1.00 43.82           C  
ANISOU 4226  CB  PRO B 346     5057   5100   6491    190    981    159       C  
ATOM   4227  CG  PRO B 346      16.060 -63.463 -55.106  1.00 48.55           C  
ANISOU 4227  CG  PRO B 346     5687   5701   7057    188    996    123       C  
ATOM   4228  CD  PRO B 346      17.333 -62.791 -55.286  1.00 44.53           C  
ANISOU 4228  CD  PRO B 346     5148   5191   6582    196   1019    139       C  
ATOM   4229  N   GLN B 347      18.358 -66.976 -53.415  1.00 43.01           N  
ANISOU 4229  N   GLN B 347     4855   4952   6535    225   1010    262       N  
ATOM   4230  CA  GLN B 347      18.715 -68.382 -53.653  1.00 43.10           C  
ANISOU 4230  CA  GLN B 347     4861   4919   6595    250   1041    285       C  
ATOM   4231  C   GLN B 347      17.367 -69.118 -53.529  1.00 46.27           C  
ANISOU 4231  C   GLN B 347     5302   5320   6958    239   1013    263       C  
ATOM   4232  O   GLN B 347      16.643 -68.838 -52.573  1.00 45.39           O  
ANISOU 4232  O   GLN B 347     5177   5253   6817    214    963    267       O  
ATOM   4233  CB  GLN B 347      19.654 -68.876 -52.555  1.00 45.39           C  
ANISOU 4233  CB  GLN B 347     5077   5221   6946    246   1020    346       C  
ATOM   4234  CG  GLN B 347      21.012 -68.146 -52.497  1.00 58.03           C  
ANISOU 4234  CG  GLN B 347     6625   6824   8599    250   1033    383       C  
ATOM   4235  CD  GLN B 347      21.615 -68.331 -51.119  1.00 80.40           C  
ANISOU 4235  CD  GLN B 347     9391   9685  11472    228    978    441       C  
ATOM   4236  OE1 GLN B 347      21.618 -69.443 -50.561  1.00 82.13           O  
ANISOU 4236  OE1 GLN B 347     9589   9897  11722    232    968    471       O  
ATOM   4237  NE2 GLN B 347      22.089 -67.250 -50.512  1.00 63.70           N  
ANISOU 4237  NE2 GLN B 347     7247   7602   9353    203    937    457       N  
ATOM   4238  N   VAL B 348      16.994 -69.956 -54.518  1.00 41.33           N  
ANISOU 4238  N   VAL B 348     4732   4642   6331    258   1045    241       N  
ATOM   4239  CA  VAL B 348      15.717 -70.661 -54.562  1.00 40.81           C  
ANISOU 4239  CA  VAL B 348     4705   4565   6235    246   1015    223       C  
ATOM   4240  C   VAL B 348      15.909 -72.173 -54.468  1.00 45.10           C  
ANISOU 4240  C   VAL B 348     5245   5067   6822    263   1025    249       C  
ATOM   4241  O   VAL B 348      16.619 -72.735 -55.268  1.00 45.19           O  
ANISOU 4241  O   VAL B 348     5282   5026   6863    293   1076    249       O  
ATOM   4242  CB  VAL B 348      14.944 -70.272 -55.857  1.00 44.01           C  
ANISOU 4242  CB  VAL B 348     5193   4939   6591    246   1027    172       C  
ATOM   4243  CG1 VAL B 348      13.570 -70.933 -55.906  1.00 43.14           C  
ANISOU 4243  CG1 VAL B 348     5120   4816   6457    228    985    160       C  
ATOM   4244  CG2 VAL B 348      14.816 -68.749 -55.985  1.00 42.91           C  
ANISOU 4244  CG2 VAL B 348     5054   4839   6412    232   1021    148       C  
ATOM   4245  N   TYR B 349      15.242 -72.827 -53.517  1.00 41.82           N  
ANISOU 4245  N   TYR B 349     4805   4675   6412    245    979    272       N  
ATOM   4246  CA  TYR B 349      15.299 -74.290 -53.338  1.00 41.86           C  
ANISOU 4246  CA  TYR B 349     4804   4643   6459    257    981    298       C  
ATOM   4247  C   TYR B 349      13.881 -74.874 -53.214  1.00 43.43           C  
ANISOU 4247  C   TYR B 349     5032   4838   6632    236    935    291       C  
ATOM   4248  O   TYR B 349      13.083 -74.344 -52.472  1.00 42.99           O  
ANISOU 4248  O   TYR B 349     4955   4831   6548    212    895    295       O  
ATOM   4249  CB  TYR B 349      16.066 -74.669 -52.077  1.00 42.60           C  
ANISOU 4249  CB  TYR B 349     4819   4768   6601    256    966    353       C  
ATOM   4250  CG  TYR B 349      17.435 -74.049 -51.993  1.00 45.49           C  
ANISOU 4250  CG  TYR B 349     5141   5142   7001    269    996    375       C  
ATOM   4251  CD1 TYR B 349      18.516 -74.606 -52.664  1.00 47.11           C  
ANISOU 4251  CD1 TYR B 349     5342   5296   7262    303   1055    390       C  
ATOM   4252  CD2 TYR B 349      17.653 -72.901 -51.247  1.00 46.24           C  
ANISOU 4252  CD2 TYR B 349     5199   5293   7078    247    966    383       C  
ATOM   4253  CE1 TYR B 349      19.765 -74.017 -52.620  1.00 47.96           C  
ANISOU 4253  CE1 TYR B 349     5402   5408   7413    315   1082    419       C  
ATOM   4254  CE2 TYR B 349      18.901 -72.304 -51.194  1.00 46.87           C  
ANISOU 4254  CE2 TYR B 349     5236   5376   7195    254    985    408       C  
ATOM   4255  CZ  TYR B 349      19.953 -72.851 -51.899  1.00 55.00           C  
ANISOU 4255  CZ  TYR B 349     6254   6356   8287    288   1043    428       C  
ATOM   4256  OH  TYR B 349      21.195 -72.254 -51.886  1.00 58.56           O  
ANISOU 4256  OH  TYR B 349     6656   6808   8786    296   1063    462       O  
ATOM   4257  N   THR B 350      13.602 -75.961 -53.913  1.00 41.90           N  
ANISOU 4257  N   THR B 350     4886   4583   6452    247    943    283       N  
ATOM   4258  CA  THR B 350      12.336 -76.682 -53.888  1.00 41.40           C  
ANISOU 4258  CA  THR B 350     4850   4503   6378    227    897    283       C  
ATOM   4259  C   THR B 350      12.489 -77.928 -53.070  1.00 43.45           C  
ANISOU 4259  C   THR B 350     5067   4754   6686    232    884    327       C  
ATOM   4260  O   THR B 350      13.512 -78.591 -53.168  1.00 42.99           O  
ANISOU 4260  O   THR B 350     5001   4665   6670    258    922    341       O  
ATOM   4261  CB  THR B 350      11.878 -76.984 -55.311  1.00 50.18           C  
ANISOU 4261  CB  THR B 350     6059   5544   7465    231    904    242       C  
ATOM   4262  OG1 THR B 350      12.858 -77.768 -55.988  1.00 44.21           O  
ANISOU 4262  OG1 THR B 350     5338   4725   6736    266    957    238       O  
ATOM   4263  CG2 THR B 350      11.603 -75.721 -56.105  1.00 47.69           C  
ANISOU 4263  CG2 THR B 350     5785   5238   7099    223    911    201       C  
ATOM   4264  N   LEU B 351      11.521 -78.199 -52.195  1.00 41.09           N  
ANISOU 4264  N   LEU B 351     4736   4487   6387    208    834    353       N  
ATOM   4265  CA  LEU B 351      11.506 -79.360 -51.321  1.00 40.22           C  
ANISOU 4265  CA  LEU B 351     4584   4377   6321    208    815    398       C  
ATOM   4266  C   LEU B 351      10.257 -80.191 -51.584  1.00 43.03           C  
ANISOU 4266  C   LEU B 351     4974   4697   6680    190    772    402       C  
ATOM   4267  O   LEU B 351       9.143 -79.660 -51.553  1.00 42.50           O  
ANISOU 4267  O   LEU B 351     4913   4651   6585    167    738    398       O  
ATOM   4268  CB  LEU B 351      11.547 -78.947 -49.828  1.00 40.17           C  
ANISOU 4268  CB  LEU B 351     4502   4444   6316    195    793    439       C  
ATOM   4269  CG  LEU B 351      12.447 -77.768 -49.442  1.00 47.16           C  
ANISOU 4269  CG  LEU B 351     5358   5376   7184    198    812    435       C  
ATOM   4270  CD1 LEU B 351      12.409 -77.526 -47.958  1.00 47.60           C  
ANISOU 4270  CD1 LEU B 351     5358   5494   7234    184    784    476       C  
ATOM   4271  CD2 LEU B 351      13.890 -78.000 -49.826  1.00 53.05           C  
ANISOU 4271  CD2 LEU B 351     6093   6092   7970    224    855    439       C  
ATOM   4272  N   PRO B 352      10.406 -81.506 -51.835  1.00 40.30           N  
ANISOU 4272  N   PRO B 352     4647   4294   6372    201    772    414       N  
ATOM   4273  CA  PRO B 352       9.216 -82.361 -52.015  1.00 38.76           C  
ANISOU 4273  CA  PRO B 352     4479   4060   6186    180    722    424       C  
ATOM   4274  C   PRO B 352       8.408 -82.553 -50.719  1.00 41.32           C  
ANISOU 4274  C   PRO B 352     4732   4438   6528    159    681    476       C  
ATOM   4275  O   PRO B 352       8.795 -82.083 -49.643  1.00 36.43           O  
ANISOU 4275  O   PRO B 352     4050   3884   5909    162    691    502       O  
ATOM   4276  CB  PRO B 352       9.814 -83.698 -52.501  1.00 40.29           C  
ANISOU 4276  CB  PRO B 352     4710   4180   6418    201    740    426       C  
ATOM   4277  CG  PRO B 352      11.143 -83.737 -51.913  1.00 45.32           C  
ANISOU 4277  CG  PRO B 352     5293   4841   7085    228    788    446       C  
ATOM   4278  CD  PRO B 352      11.648 -82.308 -51.894  1.00 41.70           C  
ANISOU 4278  CD  PRO B 352     4816   4435   6592    231    816    426       C  
ATOM   4279  N   PRO B 353       7.226 -83.198 -50.811  1.00 41.81           N  
ANISOU 4279  N   PRO B 353     4808   4472   6605    137    631    495       N  
ATOM   4280  CA  PRO B 353       6.456 -83.440 -49.597  1.00 43.13           C  
ANISOU 4280  CA  PRO B 353     4907   4686   6794    122    600    550       C  
ATOM   4281  C   PRO B 353       7.178 -84.361 -48.610  1.00 49.81           C  
ANISOU 4281  C   PRO B 353     5699   5545   7681    136    611    591       C  
ATOM   4282  O   PRO B 353       7.803 -85.325 -49.023  1.00 48.55           O  
ANISOU 4282  O   PRO B 353     5563   5333   7553    150    621    587       O  
ATOM   4283  CB  PRO B 353       5.196 -84.156 -50.099  1.00 43.85           C  
ANISOU 4283  CB  PRO B 353     5027   4726   6907     97    545    566       C  
ATOM   4284  CG  PRO B 353       5.181 -84.012 -51.546  1.00 47.53           C  
ANISOU 4284  CG  PRO B 353     5583   5128   7349     94    541    513       C  
ATOM   4285  CD  PRO B 353       6.583 -83.820 -51.983  1.00 44.20           C  
ANISOU 4285  CD  PRO B 353     5190   4695   6910    125    600    473       C  
ATOM   4286  N   SER B 354       7.053 -84.089 -47.316  1.00 48.76           N  
ANISOU 4286  N   SER B 354     5501   5479   7548    133    608    633       N  
ATOM   4287  CA  SER B 354       7.528 -85.001 -46.278  1.00 50.20           C  
ANISOU 4287  CA  SER B 354     5630   5674   7768    141    607    681       C  
ATOM   4288  C   SER B 354       6.958 -86.410 -46.557  1.00 55.85           C  
ANISOU 4288  C   SER B 354     6356   6330   8534    134    574    705       C  
ATOM   4289  O   SER B 354       5.828 -86.541 -47.065  1.00 55.10           O  
ANISOU 4289  O   SER B 354     6285   6207   8442    114    539    707       O  
ATOM   4290  CB  SER B 354       7.021 -84.542 -44.908  1.00 55.91           C  
ANISOU 4290  CB  SER B 354     6299   6470   8476    132    598    726       C  
ATOM   4291  OG  SER B 354       7.115 -85.540 -43.905  1.00 71.39           O  
ANISOU 4291  OG  SER B 354     8212   8440  10474    133    585    781       O  
ATOM   4292  N   GLN B 355       7.719 -87.452 -46.208  1.00 54.12           N  
ANISOU 4292  N   GLN B 355     6115   6089   8358    147    581    729       N  
ATOM   4293  CA  GLN B 355       7.260 -88.841 -46.368  1.00 55.24           C  
ANISOU 4293  CA  GLN B 355     6264   6173   8550    141    550    756       C  
ATOM   4294  C   GLN B 355       5.967 -89.075 -45.576  1.00 54.88           C  
ANISOU 4294  C   GLN B 355     6177   6156   8520    118    507    809       C  
ATOM   4295  O   GLN B 355       5.060 -89.718 -46.095  1.00 54.21           O  
ANISOU 4295  O   GLN B 355     6117   6021   8460    101    467    818       O  
ATOM   4296  CB  GLN B 355       8.378 -89.799 -45.915  1.00 58.40           C  
ANISOU 4296  CB  GLN B 355     6634   6559   8996    162    571    780       C  
ATOM   4297  CG  GLN B 355       8.192 -91.281 -46.237  1.00 89.13           C  
ANISOU 4297  CG  GLN B 355    10545  10378  12941    162    548    798       C  
ATOM   4298  CD  GLN B 355       9.059 -92.192 -45.366  1.00108.26           C  
ANISOU 4298  CD  GLN B 355    12913  12806  15414    178    561    843       C  
ATOM   4299  OE1 GLN B 355       8.589 -93.221 -44.846  1.00103.01           O  
ANISOU 4299  OE1 GLN B 355    12221  12127  14793    169    530    887       O  
ATOM   4300  NE2 GLN B 355      10.356 -91.885 -45.236  1.00 91.00           N  
ANISOU 4300  NE2 GLN B 355    10708  10636  13231    201    606    836       N  
ATOM   4301  N   GLU B 356       5.842 -88.478 -44.377  1.00 50.64           N  
ANISOU 4301  N   GLU B 356     5583   5694   7965    117    516    844       N  
ATOM   4302  CA  GLU B 356       4.641 -88.625 -43.535  1.00 51.99           C  
ANISOU 4302  CA  GLU B 356     5711   5894   8149    102    490    901       C  
ATOM   4303  C   GLU B 356       3.413 -87.934 -44.090  1.00 55.43           C  
ANISOU 4303  C   GLU B 356     6167   6325   8568     85    471    893       C  
ATOM   4304  O   GLU B 356       2.291 -88.356 -43.780  1.00 54.93           O  
ANISOU 4304  O   GLU B 356     6077   6257   8539     70    441    943       O  
ATOM   4305  CB  GLU B 356       4.899 -88.154 -42.079  1.00 54.13           C  
ANISOU 4305  CB  GLU B 356     5929   6243   8396    110    511    940       C  
ATOM   4306  CG  GLU B 356       6.158 -88.739 -41.431  1.00 71.69           C  
ANISOU 4306  CG  GLU B 356     8127   8475  10636    124    524    955       C  
ATOM   4307  CD  GLU B 356       6.479 -90.192 -41.770  1.00105.70           C  
ANISOU 4307  CD  GLU B 356    12431  12722  15008    127    507    970       C  
ATOM   4308  OE1 GLU B 356       5.655 -91.070 -41.420  1.00117.06           O  
ANISOU 4308  OE1 GLU B 356    13845  14146  16486    117    479   1017       O  
ATOM   4309  OE2 GLU B 356       7.528 -90.452 -42.410  1.00 88.07           O  
ANISOU 4309  OE2 GLU B 356    10221  10452  12789    141    525    937       O  
ATOM   4310  N   GLU B 357       3.600 -86.870 -44.897  1.00 50.63           N  
ANISOU 4310  N   GLU B 357     5603   5719   7914     86    487    836       N  
ATOM   4311  CA  GLU B 357       2.466 -86.177 -45.514  1.00 49.66           C  
ANISOU 4311  CA  GLU B 357     5501   5588   7778     68    467    828       C  
ATOM   4312  C   GLU B 357       1.944 -87.005 -46.711  1.00 52.32           C  
ANISOU 4312  C   GLU B 357     5888   5840   8150     48    419    816       C  
ATOM   4313  O   GLU B 357       0.778 -86.901 -47.034  1.00 51.61           O  
ANISOU 4313  O   GLU B 357     5800   5732   8077     26    381    839       O  
ATOM   4314  CB  GLU B 357       2.880 -84.752 -45.944  1.00 50.27           C  
ANISOU 4314  CB  GLU B 357     5609   5696   7794     75    500    773       C  
ATOM   4315  CG  GLU B 357       1.714 -83.833 -46.280  1.00 53.13           C  
ANISOU 4315  CG  GLU B 357     5978   6068   8141     59    487    775       C  
ATOM   4316  CD  GLU B 357       2.100 -82.484 -46.857  1.00 56.75           C  
ANISOU 4316  CD  GLU B 357     6473   6548   8542     65    515    717       C  
ATOM   4317  OE1 GLU B 357       3.075 -82.408 -47.642  1.00 49.19           O  
ANISOU 4317  OE1 GLU B 357     5561   5565   7564     73    530    663       O  
ATOM   4318  OE2 GLU B 357       1.334 -81.523 -46.633  1.00 42.65           O  
ANISOU 4318  OE2 GLU B 357     4673   4797   6736     60    522    728       O  
ATOM   4319  N   MET B 358       2.764 -87.898 -47.292  1.00 49.68           N  
ANISOU 4319  N   MET B 358     5594   5449   7831     57    417    790       N  
ATOM   4320  CA  MET B 358       2.357 -88.749 -48.425  1.00 49.95           C  
ANISOU 4320  CA  MET B 358     5695   5394   7892     39    370    775       C  
ATOM   4321  C   MET B 358       1.258 -89.777 -48.098  1.00 56.46           C  
ANISOU 4321  C   MET B 358     6487   6188   8778     15    310    839       C  
ATOM   4322  O   MET B 358       0.765 -90.417 -49.017  1.00 56.89           O  
ANISOU 4322  O   MET B 358     6598   6164   8853     -7    258    832       O  
ATOM   4323  CB  MET B 358       3.571 -89.444 -49.064  1.00 51.96           C  
ANISOU 4323  CB  MET B 358     6004   5593   8144     61    396    732       C  
ATOM   4324  CG  MET B 358       4.568 -88.461 -49.694  1.00 54.61           C  
ANISOU 4324  CG  MET B 358     6383   5941   8426     83    451    668       C  
ATOM   4325  SD  MET B 358       3.991 -87.811 -51.280  1.00 57.71           S  
ANISOU 4325  SD  MET B 358     6877   6275   8774     65    426    610       S  
ATOM   4326  CE  MET B 358       4.041 -89.289 -52.286  1.00 54.81           C  
ANISOU 4326  CE  MET B 358     6602   5790   8433     61    392    595       C  
ATOM   4327  N   THR B 359       0.823 -89.887 -46.823  1.00 52.98           N  
ANISOU 4327  N   THR B 359     5962   5804   8364     16    315    905       N  
ATOM   4328  CA  THR B 359      -0.314 -90.722 -46.435  1.00 53.15           C  
ANISOU 4328  CA  THR B 359     5941   5804   8449     -7    263    977       C  
ATOM   4329  C   THR B 359      -1.635 -89.938 -46.636  1.00 56.89           C  
ANISOU 4329  C   THR B 359     6399   6286   8929    -31    233   1005       C  
ATOM   4330  O   THR B 359      -2.711 -90.532 -46.635  1.00 56.60           O  
ANISOU 4330  O   THR B 359     6337   6216   8951    -56    179   1063       O  
ATOM   4331  CB  THR B 359      -0.134 -91.202 -44.962  1.00 62.28           C  
ANISOU 4331  CB  THR B 359     7015   7016   9631      9    289   1038       C  
ATOM   4332  OG1 THR B 359      -0.226 -90.088 -44.052  1.00 62.17           O  
ANISOU 4332  OG1 THR B 359     6957   7086   9578     24    335   1052       O  
ATOM   4333  CG2 THR B 359       1.197 -91.990 -44.747  1.00 54.10           C  
ANISOU 4333  CG2 THR B 359     5988   5969   8598     32    314   1018       C  
ATOM   4334  N   LYS B 360      -1.557 -88.606 -46.840  1.00 53.35           N  
ANISOU 4334  N   LYS B 360     5964   5879   8425    -23    268    967       N  
ATOM   4335  CA  LYS B 360      -2.735 -87.781 -47.037  1.00 52.19           C  
ANISOU 4335  CA  LYS B 360     5801   5742   8285    -42    248    992       C  
ATOM   4336  C   LYS B 360      -3.194 -87.717 -48.512  1.00 51.86           C  
ANISOU 4336  C   LYS B 360     5835   5625   8244    -73    189    957       C  
ATOM   4337  O   LYS B 360      -2.504 -88.214 -49.397  1.00 49.19           O  
ANISOU 4337  O   LYS B 360     5573   5230   7887    -75    173    902       O  
ATOM   4338  CB  LYS B 360      -2.465 -86.383 -46.474  1.00 56.26           C  
ANISOU 4338  CB  LYS B 360     6296   6337   8741    -19    313    972       C  
ATOM   4339  CG  LYS B 360      -2.235 -86.388 -44.951  1.00 77.46           C  
ANISOU 4339  CG  LYS B 360     8914   9093  11423      6    363   1018       C  
ATOM   4340  CD  LYS B 360      -3.360 -85.655 -44.212  1.00 91.35           C  
ANISOU 4340  CD  LYS B 360    10619  10898  13193      9    383   1079       C  
ATOM   4341  CE  LYS B 360      -3.400 -85.950 -42.732  1.00106.08           C  
ANISOU 4341  CE  LYS B 360    12424  12815  15067     31    421   1141       C  
ATOM   4342  NZ  LYS B 360      -4.612 -85.367 -42.090  1.00118.39           N  
ANISOU 4342  NZ  LYS B 360    13934  14404  16644     36    445   1209       N  
ATOM   4343  N   ASN B 361      -4.396 -87.140 -48.747  1.00 49.21           N  
ANISOU 4343  N   ASN B 361     5479   5287   7933    -97    155    994       N  
ATOM   4344  CA  ASN B 361      -5.004 -86.937 -50.079  1.00 50.43           C  
ANISOU 4344  CA  ASN B 361     5700   5374   8090   -132     90    972       C  
ATOM   4345  C   ASN B 361      -4.357 -85.740 -50.788  1.00 53.31           C  
ANISOU 4345  C   ASN B 361     6123   5757   8375   -120    129    891       C  
ATOM   4346  O   ASN B 361      -4.353 -85.691 -52.020  1.00 52.20           O  
ANISOU 4346  O   ASN B 361     6067   5555   8213   -141     87    846       O  
ATOM   4347  CB  ASN B 361      -6.513 -86.691 -49.951  1.00 58.52           C  
ANISOU 4347  CB  ASN B 361     6664   6392   9177   -161     43   1053       C  
ATOM   4348  CG  ASN B 361      -7.253 -86.472 -51.267  1.00122.51           C  
ANISOU 4348  CG  ASN B 361    14830  14426  17293   -204    -37   1043       C  
ATOM   4349  OD1 ASN B 361      -6.991 -87.142 -52.276  1.00126.96           O  
ANISOU 4349  OD1 ASN B 361    15483  14911  17846   -226    -94   1002       O  
ATOM   4350  ND2 ASN B 361      -8.209 -85.536 -51.291  1.00120.69           N  
ANISOU 4350  ND2 ASN B 361    14558  14217  17083   -217    -44   1082       N  
ATOM   4351  N   GLN B 362      -3.905 -84.734 -50.000  1.00 48.91           N  
ANISOU 4351  N   GLN B 362     5524   5284   7777    -89    205    879       N  
ATOM   4352  CA  GLN B 362      -3.249 -83.532 -50.497  1.00 47.25           C  
ANISOU 4352  CA  GLN B 362     5358   5101   7495    -74    249    808       C  
ATOM   4353  C   GLN B 362      -1.885 -83.411 -49.864  1.00 47.27           C  
ANISOU 4353  C   GLN B 362     5356   5153   7453    -37    318    769       C  
ATOM   4354  O   GLN B 362      -1.718 -83.685 -48.668  1.00 46.44           O  
ANISOU 4354  O   GLN B 362     5187   5095   7362    -19    349    809       O  
ATOM   4355  CB  GLN B 362      -4.073 -82.293 -50.180  1.00 48.46           C  
ANISOU 4355  CB  GLN B 362     5465   5303   7642    -75    268    834       C  
ATOM   4356  CG  GLN B 362      -5.364 -82.240 -50.961  1.00 73.01           C  
ANISOU 4356  CG  GLN B 362     8582   8362  10797   -114    197    871       C  
ATOM   4357  CD  GLN B 362      -6.270 -81.237 -50.351  1.00 96.12           C  
ANISOU 4357  CD  GLN B 362    11442  11340  13740   -110    223    922       C  
ATOM   4358  OE1 GLN B 362      -6.391 -80.117 -50.854  1.00 99.32           O  
ANISOU 4358  OE1 GLN B 362    11867  11758  14110   -111    236    891       O  
ATOM   4359  NE2 GLN B 362      -6.861 -81.595 -49.211  1.00 81.31           N  
ANISOU 4359  NE2 GLN B 362     9484   9495  11914    -99    241   1000       N  
ATOM   4360  N   VAL B 363      -0.907 -83.029 -50.683  1.00 42.19           N  
ANISOU 4360  N   VAL B 363     4779   4493   6758    -27    342    695       N  
ATOM   4361  CA  VAL B 363       0.493 -82.863 -50.282  1.00 41.40           C  
ANISOU 4361  CA  VAL B 363     4680   4430   6621      6    403    657       C  
ATOM   4362  C   VAL B 363       0.953 -81.420 -50.533  1.00 42.99           C  
ANISOU 4362  C   VAL B 363     4899   4674   6763     18    447    608       C  
ATOM   4363  O   VAL B 363       0.379 -80.709 -51.349  1.00 41.12           O  
ANISOU 4363  O   VAL B 363     4696   4420   6508      2    428    587       O  
ATOM   4364  CB  VAL B 363       1.433 -83.920 -50.920  1.00 45.55           C  
ANISOU 4364  CB  VAL B 363     5261   4893   7152     16    402    624       C  
ATOM   4365  CG1 VAL B 363       1.071 -85.345 -50.462  1.00 45.89           C  
ANISOU 4365  CG1 VAL B 363     5278   4902   7256      7    365    676       C  
ATOM   4366  CG2 VAL B 363       1.458 -83.829 -52.440  1.00 45.23           C  
ANISOU 4366  CG2 VAL B 363     5320   4781   7085      4    380    568       C  
ATOM   4367  N   SER B 364       2.023 -81.028 -49.844  1.00 39.63           N  
ANISOU 4367  N   SER B 364     4449   4299   6310     44    499    592       N  
ATOM   4368  CA  SER B 364       2.615 -79.709 -49.899  1.00 37.11           C  
ANISOU 4368  CA  SER B 364     4138   4023   5937     57    541    550       C  
ATOM   4369  C   SER B 364       3.915 -79.728 -50.657  1.00 39.40           C  
ANISOU 4369  C   SER B 364     4477   4286   6205     74    571    495       C  
ATOM   4370  O   SER B 364       4.814 -80.507 -50.339  1.00 37.37           O  
ANISOU 4370  O   SER B 364     4210   4021   5969     91    588    501       O  
ATOM   4371  CB  SER B 364       2.923 -79.190 -48.506  1.00 36.47           C  
ANISOU 4371  CB  SER B 364     3997   4017   5841     73    575    578       C  
ATOM   4372  OG  SER B 364       1.774 -79.078 -47.688  1.00 39.32           O  
ANISOU 4372  OG  SER B 364     4313   4409   6219     65    564    632       O  
ATOM   4373  N   LEU B 365       4.047 -78.811 -51.612  1.00 37.34           N  
ANISOU 4373  N   LEU B 365     4267   4015   5907     73    583    447       N  
ATOM   4374  CA  LEU B 365       5.301 -78.592 -52.329  1.00 37.26           C  
ANISOU 4374  CA  LEU B 365     4300   3985   5872     93    623    397       C  
ATOM   4375  C   LEU B 365       5.815 -77.314 -51.740  1.00 37.28           C  
ANISOU 4375  C   LEU B 365     4268   4056   5842    103    659    386       C  
ATOM   4376  O   LEU B 365       5.052 -76.395 -51.581  1.00 35.42           O  
ANISOU 4376  O   LEU B 365     4021   3854   5584     91    649    388       O  
ATOM   4377  CB  LEU B 365       5.096 -78.466 -53.832  1.00 37.97           C  
ANISOU 4377  CB  LEU B 365     4476   4011   5939     85    612    351       C  
ATOM   4378  CG  LEU B 365       4.303 -79.604 -54.483  1.00 43.24           C  
ANISOU 4378  CG  LEU B 365     5193   4604   6632     65    558    363       C  
ATOM   4379  CD1 LEU B 365       4.457 -79.568 -55.990  1.00 43.77           C  
ANISOU 4379  CD1 LEU B 365     5365   4599   6666     63    555    311       C  
ATOM   4380  CD2 LEU B 365       4.735 -80.948 -53.964  1.00 45.83           C  
ANISOU 4380  CD2 LEU B 365     5501   4909   7004     77    558    391       C  
ATOM   4381  N   THR B 366       7.072 -77.297 -51.309  1.00 38.09           N  
ANISOU 4381  N   THR B 366     4347   4178   5946    125    696    383       N  
ATOM   4382  CA  THR B 366       7.692 -76.155 -50.633  1.00 37.30           C  
ANISOU 4382  CA  THR B 366     4214   4140   5818    132    722    378       C  
ATOM   4383  C   THR B 366       8.781 -75.513 -51.455  1.00 40.15           C  
ANISOU 4383  C   THR B 366     4606   4488   6162    147    760    336       C  
ATOM   4384  O   THR B 366       9.546 -76.196 -52.141  1.00 37.63           O  
ANISOU 4384  O   THR B 366     4314   4120   5864    163    782    323       O  
ATOM   4385  CB  THR B 366       8.286 -76.631 -49.316  1.00 39.01           C  
ANISOU 4385  CB  THR B 366     4371   4393   6057    139    725    421       C  
ATOM   4386  OG1 THR B 366       7.245 -77.241 -48.584  1.00 36.49           O  
ANISOU 4386  OG1 THR B 366     4025   4085   5755    127    694    463       O  
ATOM   4387  CG2 THR B 366       8.930 -75.503 -48.512  1.00 34.97           C  
ANISOU 4387  CG2 THR B 366     3831   3941   5515    142    740    421       C  
ATOM   4388  N   CYS B 367       8.864 -74.192 -51.336  1.00 39.34           N  
ANISOU 4388  N   CYS B 367     4497   4428   6022    144    771    317       N  
ATOM   4389  CA  CYS B 367       9.880 -73.392 -51.948  1.00 39.70           C  
ANISOU 4389  CA  CYS B 367     4560   4471   6052    156    806    284       C  
ATOM   4390  C   CYS B 367      10.523 -72.539 -50.883  1.00 42.15           C  
ANISOU 4390  C   CYS B 367     4822   4841   6350    156    811    300       C  
ATOM   4391  O   CYS B 367       9.854 -71.685 -50.295  1.00 40.07           O  
ANISOU 4391  O   CYS B 367     4549   4621   6054    143    795    302       O  
ATOM   4392  CB  CYS B 367       9.310 -72.527 -53.052  1.00 41.68           C  
ANISOU 4392  CB  CYS B 367     4865   4707   6266    149    808    242       C  
ATOM   4393  SG  CYS B 367      10.570 -71.755 -54.098  1.00 47.22           S  
ANISOU 4393  SG  CYS B 367     5600   5388   6954    169    858    201       S  
ATOM   4394  N   LEU B 368      11.814 -72.781 -50.620  1.00 39.24           N  
ANISOU 4394  N   LEU B 368     4425   4471   6011    170    831    315       N  
ATOM   4395  CA  LEU B 368      12.589 -71.958 -49.719  1.00 38.23           C  
ANISOU 4395  CA  LEU B 368     4260   4391   5877    167    828    331       C  
ATOM   4396  C   LEU B 368      13.322 -70.892 -50.592  1.00 39.84           C  
ANISOU 4396  C   LEU B 368     4482   4588   6067    174    858    297       C  
ATOM   4397  O   LEU B 368      14.002 -71.242 -51.537  1.00 36.82           O  
ANISOU 4397  O   LEU B 368     4117   4162   5711    193    893    285       O  
ATOM   4398  CB  LEU B 368      13.577 -72.814 -48.945  1.00 38.73           C  
ANISOU 4398  CB  LEU B 368     4275   4452   5989    174    826    375       C  
ATOM   4399  CG  LEU B 368      14.674 -72.071 -48.170  1.00 44.00           C  
ANISOU 4399  CG  LEU B 368     4903   5153   6661    169    818    397       C  
ATOM   4400  CD1 LEU B 368      14.072 -71.059 -47.159  1.00 41.82           C  
ANISOU 4400  CD1 LEU B 368     4630   4932   6329    148    785    398       C  
ATOM   4401  CD2 LEU B 368      15.628 -73.053 -47.533  1.00 46.47           C  
ANISOU 4401  CD2 LEU B 368     5168   5455   7033    176    813    446       C  
ATOM   4402  N   VAL B 369      13.099 -69.599 -50.297  1.00 37.96           N  
ANISOU 4402  N   VAL B 369     4247   4390   5786    160    847    281       N  
ATOM   4403  CA  VAL B 369      13.757 -68.483 -50.957  1.00 37.95           C  
ANISOU 4403  CA  VAL B 369     4258   4390   5771    164    868    254       C  
ATOM   4404  C   VAL B 369      14.549 -67.783 -49.850  1.00 40.86           C  
ANISOU 4404  C   VAL B 369     4586   4799   6139    153    847    280       C  
ATOM   4405  O   VAL B 369      13.971 -67.416 -48.838  1.00 39.95           O  
ANISOU 4405  O   VAL B 369     4467   4722   5989    137    816    291       O  
ATOM   4406  CB  VAL B 369      12.763 -67.517 -51.649  1.00 40.74           C  
ANISOU 4406  CB  VAL B 369     4655   4749   6074    155    869    212       C  
ATOM   4407  CG1 VAL B 369      13.507 -66.446 -52.439  1.00 41.13           C  
ANISOU 4407  CG1 VAL B 369     4718   4794   6114    160    895    184       C  
ATOM   4408  CG2 VAL B 369      11.811 -68.287 -52.546  1.00 40.05           C  
ANISOU 4408  CG2 VAL B 369     4610   4621   5987    157    871    195       C  
ATOM   4409  N   LYS B 370      15.858 -67.631 -50.014  1.00 39.42           N  
ANISOU 4409  N   LYS B 370     4377   4606   5996    161    862    296       N  
ATOM   4410  CA  LYS B 370      16.681 -67.023 -48.969  1.00 38.54           C  
ANISOU 4410  CA  LYS B 370     4227   4525   5890    145    830    327       C  
ATOM   4411  C   LYS B 370      17.804 -66.203 -49.539  1.00 41.80           C  
ANISOU 4411  C   LYS B 370     4625   4928   6330    149    848    327       C  
ATOM   4412  O   LYS B 370      18.058 -66.241 -50.735  1.00 41.13           O  
ANISOU 4412  O   LYS B 370     4555   4809   6264    170    895    306       O  
ATOM   4413  CB  LYS B 370      17.204 -68.099 -47.981  1.00 40.77           C  
ANISOU 4413  CB  LYS B 370     4466   4807   6217    143    807    381       C  
ATOM   4414  CG  LYS B 370      18.160 -69.127 -48.563  1.00 44.57           C  
ANISOU 4414  CG  LYS B 370     4916   5244   6775    167    841    407       C  
ATOM   4415  CD  LYS B 370      18.870 -69.966 -47.473  1.00 54.98           C  
ANISOU 4415  CD  LYS B 370     6181   6566   8142    160    811    468       C  
ATOM   4416  CE  LYS B 370      20.290 -70.356 -47.868  1.00 73.26           C  
ANISOU 4416  CE  LYS B 370     8448   8847  10543    178    840    507       C  
ATOM   4417  NZ  LYS B 370      20.969 -71.190 -46.838  1.00 86.04           N  
ANISOU 4417  NZ  LYS B 370    10011  10466  12216    171    807    571       N  
ATOM   4418  N   GLY B 371      18.429 -65.437 -48.666  1.00 39.10           N  
ANISOU 4418  N   GLY B 371     4259   4613   5985    129    809    351       N  
ATOM   4419  CA  GLY B 371      19.571 -64.623 -49.008  1.00 40.06           C  
ANISOU 4419  CA  GLY B 371     4355   4726   6141    127    814    363       C  
ATOM   4420  C   GLY B 371      19.304 -63.373 -49.821  1.00 43.45           C  
ANISOU 4420  C   GLY B 371     4819   5160   6530    126    832    317       C  
ATOM   4421  O   GLY B 371      20.225 -62.865 -50.460  1.00 44.09           O  
ANISOU 4421  O   GLY B 371     4879   5224   6649    133    855    326       O  
ATOM   4422  N   PHE B 372      18.101 -62.810 -49.727  1.00 37.83           N  
ANISOU 4422  N   PHE B 372     4154   4473   5746    116    821    276       N  
ATOM   4423  CA  PHE B 372      17.700 -61.647 -50.543  1.00 34.64           C  
ANISOU 4423  CA  PHE B 372     3787   4073   5303    116    839    231       C  
ATOM   4424  C   PHE B 372      17.558 -60.352 -49.789  1.00 37.58           C  
ANISOU 4424  C   PHE B 372     4174   4480   5627     91    797    222       C  
ATOM   4425  O   PHE B 372      17.302 -60.325 -48.590  1.00 38.02           O  
ANISOU 4425  O   PHE B 372     4233   4559   5653     74    755    239       O  
ATOM   4426  CB  PHE B 372      16.400 -61.924 -51.335  1.00 34.65           C  
ANISOU 4426  CB  PHE B 372     3835   4066   5267    126    866    188       C  
ATOM   4427  CG  PHE B 372      15.146 -62.253 -50.554  1.00 33.59           C  
ANISOU 4427  CG  PHE B 372     3718   3953   5090    117    841    185       C  
ATOM   4428  CD1 PHE B 372      14.222 -61.265 -50.235  1.00 33.09           C  
ANISOU 4428  CD1 PHE B 372     3685   3918   4968    105    826    162       C  
ATOM   4429  CD2 PHE B 372      14.836 -63.567 -50.237  1.00 33.02           C  
ANISOU 4429  CD2 PHE B 372     3636   3871   5041    124    839    208       C  
ATOM   4430  CE1 PHE B 372      13.069 -61.575 -49.537  1.00 34.16           C  
ANISOU 4430  CE1 PHE B 372     3835   4072   5073    101    813    167       C  
ATOM   4431  CE2 PHE B 372      13.683 -63.877 -49.537  1.00 34.07           C  
ANISOU 4431  CE2 PHE B 372     3780   4022   5141    117    820    212       C  
ATOM   4432  CZ  PHE B 372      12.774 -62.895 -49.239  1.00 33.26           C  
ANISOU 4432  CZ  PHE B 372     3706   3947   4985    107    811    192       C  
ATOM   4433  N   TYR B 373      17.797 -59.266 -50.517  1.00 34.61           N  
ANISOU 4433  N   TYR B 373     3808   4100   5241     90    811    197       N  
ATOM   4434  CA  TYR B 373      17.684 -57.901 -50.028  1.00 33.85           C  
ANISOU 4434  CA  TYR B 373     3734   4030   5099     68    778    182       C  
ATOM   4435  C   TYR B 373      17.529 -57.026 -51.269  1.00 36.94           C  
ANISOU 4435  C   TYR B 373     4147   4411   5479     76    814    142       C  
ATOM   4436  O   TYR B 373      18.287 -57.239 -52.201  1.00 35.68           O  
ANISOU 4436  O   TYR B 373     3966   4224   5368     92    850    150       O  
ATOM   4437  CB  TYR B 373      18.889 -57.461 -49.213  1.00 34.46           C  
ANISOU 4437  CB  TYR B 373     3779   4110   5204     47    730    223       C  
ATOM   4438  CG  TYR B 373      18.611 -56.135 -48.540  1.00 33.66           C  
ANISOU 4438  CG  TYR B 373     3716   4031   5041     22    688    205       C  
ATOM   4439  CD1 TYR B 373      17.877 -56.074 -47.360  1.00 33.70           C  
ANISOU 4439  CD1 TYR B 373     3760   4060   4986     10    653    203       C  
ATOM   4440  CD2 TYR B 373      18.854 -54.938 -49.204  1.00 34.25           C  
ANISOU 4440  CD2 TYR B 373     3801   4104   5110     17    694    182       C  
ATOM   4441  CE1 TYR B 373      17.457 -54.856 -46.829  1.00 30.77           C  
ANISOU 4441  CE1 TYR B 373     3439   3704   4549     -6    627    180       C  
ATOM   4442  CE2 TYR B 373      18.387 -53.723 -48.710  1.00 32.71           C  
ANISOU 4442  CE2 TYR B 373     3652   3926   4850      0    665    156       C  
ATOM   4443  CZ  TYR B 373      17.695 -53.686 -47.520  1.00 34.26           C  
ANISOU 4443  CZ  TYR B 373     3889   4141   4986    -11    632    154       C  
ATOM   4444  OH  TYR B 373      17.347 -52.465 -46.987  1.00 34.69           O  
ANISOU 4444  OH  TYR B 373     3996   4207   4978    -26    605    132       O  
ATOM   4445  N   PRO B 374      16.525 -56.132 -51.380  1.00 36.21           N  
ANISOU 4445  N   PRO B 374     4097   4335   5326     70    813    103       N  
ATOM   4446  CA  PRO B 374      15.497 -55.795 -50.373  1.00 36.58           C  
ANISOU 4446  CA  PRO B 374     4177   4411   5313     59    785     93       C  
ATOM   4447  C   PRO B 374      14.488 -56.911 -50.142  1.00 36.55           C  
ANISOU 4447  C   PRO B 374     4180   4408   5301     69    796     97       C  
ATOM   4448  O   PRO B 374      14.510 -57.915 -50.822  1.00 35.87           O  
ANISOU 4448  O   PRO B 374     4079   4299   5250     84    821    101       O  
ATOM   4449  CB  PRO B 374      14.886 -54.495 -50.939  1.00 37.69           C  
ANISOU 4449  CB  PRO B 374     4352   4558   5410     56    797     53       C  
ATOM   4450  CG  PRO B 374      15.013 -54.630 -52.403  1.00 42.06           C  
ANISOU 4450  CG  PRO B 374     4901   5086   5992     70    838     33       C  
ATOM   4451  CD  PRO B 374      16.334 -55.340 -52.618  1.00 38.60           C  
ANISOU 4451  CD  PRO B 374     4420   4627   5618     78    847     66       C  
ATOM   4452  N   SER B 375      13.658 -56.746 -49.137  1.00 35.98           N  
ANISOU 4452  N   SER B 375     4131   4359   5183     63    778    100       N  
ATOM   4453  CA  SER B 375      12.583 -57.689 -48.776  1.00 35.00           C  
ANISOU 4453  CA  SER B 375     4011   4237   5049     72    786    111       C  
ATOM   4454  C   SER B 375      11.478 -57.786 -49.835  1.00 39.41           C  
ANISOU 4454  C   SER B 375     4585   4784   5606     83    817     85       C  
ATOM   4455  O   SER B 375      10.796 -58.806 -49.879  1.00 41.02           O  
ANISOU 4455  O   SER B 375     4782   4979   5825     90    824     98       O  
ATOM   4456  CB  SER B 375      11.959 -57.318 -47.442  1.00 35.26           C  
ANISOU 4456  CB  SER B 375     4071   4296   5030     67    768    123       C  
ATOM   4457  OG  SER B 375      11.230 -56.108 -47.565  1.00 48.87           O  
ANISOU 4457  OG  SER B 375     5832   6031   6708     67    780     94       O  
ATOM   4458  N   ASP B 376      11.288 -56.740 -50.657  1.00 35.03           N  
ANISOU 4458  N   ASP B 376     4050   4227   5034     81    831     52       N  
ATOM   4459  CA  ASP B 376      10.307 -56.714 -51.759  1.00 33.57           C  
ANISOU 4459  CA  ASP B 376     3883   4026   4847     86    852     28       C  
ATOM   4460  C   ASP B 376      10.534 -57.872 -52.752  1.00 36.05           C  
ANISOU 4460  C   ASP B 376     4191   4305   5203     94    865     28       C  
ATOM   4461  O   ASP B 376      11.496 -57.887 -53.496  1.00 35.80           O  
ANISOU 4461  O   ASP B 376     4156   4254   5193     99    880     19       O  
ATOM   4462  CB  ASP B 376      10.363 -55.363 -52.510  1.00 34.21           C  
ANISOU 4462  CB  ASP B 376     3984   4106   4906     81    861     -6       C  
ATOM   4463  CG  ASP B 376       9.341 -55.176 -53.627  1.00 40.54           C  
ANISOU 4463  CG  ASP B 376     4808   4892   5702     82    876    -28       C  
ATOM   4464  OD1 ASP B 376       8.345 -55.906 -53.642  1.00 42.45           O  
ANISOU 4464  OD1 ASP B 376     5052   5126   5951     83    874    -16       O  
ATOM   4465  OD2 ASP B 376       9.519 -54.259 -54.454  1.00 45.36           O  
ANISOU 4465  OD2 ASP B 376     5436   5497   6304     79    886    -55       O  
ATOM   4466  N   ILE B 377       9.624 -58.829 -52.766  1.00 32.83           N  
ANISOU 4466  N   ILE B 377     3784   3886   4805     96    862     41       N  
ATOM   4467  CA  ILE B 377       9.746 -59.991 -53.618  1.00 33.41           C  
ANISOU 4467  CA  ILE B 377     3862   3920   4911    103    870     42       C  
ATOM   4468  C   ILE B 377       8.364 -60.573 -53.883  1.00 37.18           C  
ANISOU 4468  C   ILE B 377     4354   4383   5390     98    859     48       C  
ATOM   4469  O   ILE B 377       7.404 -60.261 -53.172  1.00 33.11           O  
ANISOU 4469  O   ILE B 377     3831   3891   4860     93    848     64       O  
ATOM   4470  CB  ILE B 377      10.643 -61.012 -52.842  1.00 36.73           C  
ANISOU 4470  CB  ILE B 377     4250   4342   5365    110    866     74       C  
ATOM   4471  CG1 ILE B 377      11.220 -62.091 -53.755  1.00 36.69           C  
ANISOU 4471  CG1 ILE B 377     4251   4291   5397    123    885     73       C  
ATOM   4472  CG2 ILE B 377       9.903 -61.627 -51.638  1.00 36.63           C  
ANISOU 4472  CG2 ILE B 377     4218   4349   5348    106    845    107       C  
ATOM   4473  CD1 ILE B 377      12.402 -62.786 -53.149  1.00 47.17           C  
ANISOU 4473  CD1 ILE B 377     5541   5617   6763    132    888    104       C  
ATOM   4474  N   ALA B 378       8.267 -61.390 -54.921  1.00 35.13           N  
ANISOU 4474  N   ALA B 378     4119   4081   5150    100    861     39       N  
ATOM   4475  CA  ALA B 378       7.051 -62.128 -55.189  1.00 34.35           C  
ANISOU 4475  CA  ALA B 378     4032   3958   5061     91    839     52       C  
ATOM   4476  C   ALA B 378       7.381 -63.508 -55.613  1.00 35.72           C  
ANISOU 4476  C   ALA B 378     4219   4090   5265     97    837     59       C  
ATOM   4477  O   ALA B 378       8.356 -63.723 -56.322  1.00 35.26           O  
ANISOU 4477  O   ALA B 378     4181   4004   5211    109    860     41       O  
ATOM   4478  CB  ALA B 378       6.210 -61.458 -56.240  1.00 35.31           C  
ANISOU 4478  CB  ALA B 378     4190   4060   5165     78    830     30       C  
ATOM   4479  N   VAL B 379       6.541 -64.441 -55.200  1.00 31.50           N  
ANISOU 4479  N   VAL B 379     3672   3546   4751     90    812     89       N  
ATOM   4480  CA  VAL B 379       6.648 -65.827 -55.570  1.00 30.53           C  
ANISOU 4480  CA  VAL B 379     3564   3378   4657     93    803     99       C  
ATOM   4481  C   VAL B 379       5.327 -66.267 -56.229  1.00 32.08           C  
ANISOU 4481  C   VAL B 379     3790   3537   4861     73    764    107       C  
ATOM   4482  O   VAL B 379       4.264 -65.917 -55.757  1.00 30.15           O  
ANISOU 4482  O   VAL B 379     3521   3314   4620     60    744    131       O  
ATOM   4483  CB  VAL B 379       6.987 -66.712 -54.337  1.00 33.59           C  
ANISOU 4483  CB  VAL B 379     3903   3787   5072    101    801    137       C  
ATOM   4484  CG1 VAL B 379       7.267 -68.157 -54.754  1.00 32.44           C  
ANISOU 4484  CG1 VAL B 379     3775   3592   4960    108    797    145       C  
ATOM   4485  CG2 VAL B 379       8.174 -66.154 -53.586  1.00 33.81           C  
ANISOU 4485  CG2 VAL B 379     3900   3854   5094    114    825    138       C  
ATOM   4486  N   GLU B 380       5.416 -67.077 -57.270  1.00 30.38           N  
ANISOU 4486  N   GLU B 380     3629   3262   4652     71    755     91       N  
ATOM   4487  CA  GLU B 380       4.265 -67.682 -57.942  1.00 30.87           C  
ANISOU 4487  CA  GLU B 380     3727   3276   4725     48    707    102       C  
ATOM   4488  C   GLU B 380       4.625 -69.147 -58.167  1.00 33.09           C  
ANISOU 4488  C   GLU B 380     4036   3506   5030     55    699    108       C  
ATOM   4489  O   GLU B 380       5.802 -69.472 -58.133  1.00 33.36           O  
ANISOU 4489  O   GLU B 380     4074   3537   5065     79    740     94       O  
ATOM   4490  CB  GLU B 380       4.042 -67.078 -59.333  1.00 32.13           C  
ANISOU 4490  CB  GLU B 380     3958   3396   4853     36    696     64       C  
ATOM   4491  CG  GLU B 380       3.437 -65.719 -59.492  1.00 53.71           C  
ANISOU 4491  CG  GLU B 380     6682   6159   7565     23    691     57       C  
ATOM   4492  CD  GLU B 380       3.297 -65.390 -60.974  1.00 81.24           C  
ANISOU 4492  CD  GLU B 380    10252   9595  11021      9    676     22       C  
ATOM   4493  OE1 GLU B 380       2.150 -65.433 -61.478  1.00 84.15           O  
ANISOU 4493  OE1 GLU B 380    10643   9933  11397    -20    622     37       O  
ATOM   4494  OE2 GLU B 380       4.338 -65.255 -61.662  1.00 68.64           O  
ANISOU 4494  OE2 GLU B 380     8702   7980   9397     28    715    -16       O  
ATOM   4495  N   TRP B 381       3.646 -69.980 -58.536  1.00 30.75           N  
ANISOU 4495  N   TRP B 381     3766   3163   4753     32    647    127       N  
ATOM   4496  CA  TRP B 381       3.857 -71.382 -58.851  1.00 31.10           C  
ANISOU 4496  CA  TRP B 381     3850   3150   4818     35    633    132       C  
ATOM   4497  C   TRP B 381       3.216 -71.723 -60.177  1.00 32.81           C  
ANISOU 4497  C   TRP B 381     4158   3289   5019     11    586    114       C  
ATOM   4498  O   TRP B 381       2.215 -71.140 -60.559  1.00 32.31           O  
ANISOU 4498  O   TRP B 381     4104   3221   4950    -17    542    121       O  
ATOM   4499  CB  TRP B 381       3.254 -72.308 -57.783  1.00 30.98           C  
ANISOU 4499  CB  TRP B 381     3773   3148   4851     27    603    185       C  
ATOM   4500  CG  TRP B 381       4.001 -72.369 -56.490  1.00 32.00           C  
ANISOU 4500  CG  TRP B 381     3827   3336   4995     51    643    206       C  
ATOM   4501  CD1 TRP B 381       3.787 -71.598 -55.388  1.00 33.92           C  
ANISOU 4501  CD1 TRP B 381     4002   3649   5238     53    655    230       C  
ATOM   4502  CD2 TRP B 381       4.954 -73.369 -56.102  1.00 31.77           C  
ANISOU 4502  CD2 TRP B 381     3787   3296   4988     72    667    213       C  
ATOM   4503  NE1 TRP B 381       4.598 -72.006 -54.365  1.00 33.38           N  
ANISOU 4503  NE1 TRP B 381     3886   3613   5183     72    682    248       N  
ATOM   4504  CE2 TRP B 381       5.281 -73.129 -54.752  1.00 35.01           C  
ANISOU 4504  CE2 TRP B 381     4120   3772   5409     83    687    242       C  
ATOM   4505  CE3 TRP B 381       5.456 -74.526 -56.720  1.00 33.55           C  
ANISOU 4505  CE3 TRP B 381     4064   3457   5227     82    669    203       C  
ATOM   4506  CZ2 TRP B 381       6.109 -73.986 -54.016  1.00 34.18           C  
ANISOU 4506  CZ2 TRP B 381     3981   3673   5332    101    705    263       C  
ATOM   4507  CZ3 TRP B 381       6.284 -75.362 -55.990  1.00 35.12           C  
ANISOU 4507  CZ3 TRP B 381     4224   3662   5456    103    694    223       C  
ATOM   4508  CH2 TRP B 381       6.676 -75.030 -54.683  1.00 35.21           C  
ANISOU 4508  CH2 TRP B 381     4153   3743   5480    112    712    252       C  
ATOM   4509  N   GLU B 382       3.747 -72.740 -60.826  1.00 31.03           N  
ANISOU 4509  N   GLU B 382     4001   2998   4789     21    590     96       N  
ATOM   4510  CA  GLU B 382       3.203 -73.260 -62.071  1.00 31.13           C  
ANISOU 4510  CA  GLU B 382     4120   2925   4781     -1    540     78       C  
ATOM   4511  C   GLU B 382       3.213 -74.780 -62.039  1.00 31.20           C  
ANISOU 4511  C   GLU B 382     4160   2876   4818     -1    516     95       C  
ATOM   4512  O   GLU B 382       3.953 -75.383 -61.277  1.00 29.83           O  
ANISOU 4512  O   GLU B 382     3939   2724   4672     26    556    108       O  
ATOM   4513  CB  GLU B 382       4.018 -72.807 -63.281  1.00 32.55           C  
ANISOU 4513  CB  GLU B 382     4397   3065   4905     17    584     23       C  
ATOM   4514  CG  GLU B 382       4.167 -71.290 -63.469  1.00 32.19           C  
ANISOU 4514  CG  GLU B 382     4334   3071   4828     19    614      1       C  
ATOM   4515  CD  GLU B 382       5.223 -70.605 -62.623  1.00 39.07           C  
ANISOU 4515  CD  GLU B 382     5124   4016   5706     53    687     -1       C  
ATOM   4516  OE1 GLU B 382       6.332 -71.163 -62.546  1.00 38.17           O  
ANISOU 4516  OE1 GLU B 382     5015   3889   5599     87    741    -10       O  
ATOM   4517  OE2 GLU B 382       4.963 -69.516 -62.055  1.00 35.52           O  
ANISOU 4517  OE2 GLU B 382     4608   3631   5257     46    689      7       O  
ATOM   4518  N   SER B 383       2.354 -75.382 -62.854  1.00 28.79           N  
ANISOU 4518  N   SER B 383     3934   2495   4509    -34    443     98       N  
ATOM   4519  CA  SER B 383       2.257 -76.821 -63.053  1.00 30.03           C  
ANISOU 4519  CA  SER B 383     4146   2580   4686    -40    407    108       C  
ATOM   4520  C   SER B 383       2.396 -77.051 -64.555  1.00 34.33           C  
ANISOU 4520  C   SER B 383     4844   3027   5172    -46    392     61       C  
ATOM   4521  O   SER B 383       1.532 -76.619 -65.303  1.00 33.98           O  
ANISOU 4521  O   SER B 383     4855   2951   5106    -84    327     58       O  
ATOM   4522  CB  SER B 383       0.927 -77.360 -62.538  1.00 30.78           C  
ANISOU 4522  CB  SER B 383     4192   2669   4836    -83    317    167       C  
ATOM   4523  OG  SER B 383       0.793 -78.723 -62.874  1.00 45.14           O  
ANISOU 4523  OG  SER B 383     6077   4406   6669    -94    273    174       O  
ATOM   4524  N   ASN B 384       3.501 -77.670 -65.004  1.00 34.45           N  
ANISOU 4524  N   ASN B 384     4932   2995   5160     -6    456     26       N  
ATOM   4525  CA  ASN B 384       3.783 -77.916 -66.428  1.00 35.39           C  
ANISOU 4525  CA  ASN B 384     5213   3018   5215     -1    460    -22       C  
ATOM   4526  C   ASN B 384       3.811 -76.598 -67.210  1.00 36.73           C  
ANISOU 4526  C   ASN B 384     5423   3202   5330     -4    478    -56       C  
ATOM   4527  O   ASN B 384       3.446 -76.553 -68.371  1.00 38.72           O  
ANISOU 4527  O   ASN B 384     5802   3381   5529    -25    439    -83       O  
ATOM   4528  CB  ASN B 384       2.799 -78.927 -67.035  1.00 36.24           C  
ANISOU 4528  CB  ASN B 384     5417   3030   5321    -45    357    -11       C  
ATOM   4529  CG  ASN B 384       2.831 -80.252 -66.345  1.00 42.37           C  
ANISOU 4529  CG  ASN B 384     6162   3785   6150    -40    342     21       C  
ATOM   4530  OD1 ASN B 384       3.873 -80.694 -65.845  1.00 43.31           O  
ANISOU 4530  OD1 ASN B 384     6247   3921   6286      7    424     16       O  
ATOM   4531  ND2 ASN B 384       1.676 -80.863 -66.162  1.00 40.08           N  
ANISOU 4531  ND2 ASN B 384     5861   3467   5900    -89    237     62       N  
ATOM   4532  N   GLY B 385       4.225 -75.543 -66.524  1.00 30.00           N  
ANISOU 4532  N   GLY B 385     4463   2444   4491     14    532    -51       N  
ATOM   4533  CA  GLY B 385       4.292 -74.187 -67.049  1.00 29.30           C  
ANISOU 4533  CA  GLY B 385     4386   2386   4361     12    555    -78       C  
ATOM   4534  C   GLY B 385       3.058 -73.351 -66.825  1.00 31.83           C  
ANISOU 4534  C   GLY B 385     4649   2748   4696    -35    479    -52       C  
ATOM   4535  O   GLY B 385       3.121 -72.152 -66.992  1.00 30.17           O  
ANISOU 4535  O   GLY B 385     4419   2581   4464    -34    502    -66       O  
ATOM   4536  N   GLN B 386       1.920 -73.943 -66.443  1.00 31.91           N  
ANISOU 4536  N   GLN B 386     4629   2745   4749    -75    391     -8       N  
ATOM   4537  CA  GLN B 386       0.706 -73.151 -66.273  1.00 32.44           C  
ANISOU 4537  CA  GLN B 386     4641   2846   4840   -118    323     25       C  
ATOM   4538  C   GLN B 386       0.585 -72.533 -64.851  1.00 37.39           C  
ANISOU 4538  C   GLN B 386     5112   3578   5517   -107    354     64       C  
ATOM   4539  O   GLN B 386       0.592 -73.298 -63.885  1.00 37.13           O  
ANISOU 4539  O   GLN B 386     5011   3567   5531    -99    357     98       O  
ATOM   4540  CB  GLN B 386      -0.521 -74.033 -66.549  1.00 33.37           C  
ANISOU 4540  CB  GLN B 386     4794   2895   4989   -169    211     64       C  
ATOM   4541  CG  GLN B 386      -1.793 -73.184 -66.642  1.00 33.30           C  
ANISOU 4541  CG  GLN B 386     4745   2904   5004   -216    136    101       C  
ATOM   4542  CD  GLN B 386      -3.025 -74.031 -66.720  1.00 34.71           C  
ANISOU 4542  CD  GLN B 386     4931   3023   5233   -267     23    156       C  
ATOM   4543  OE1 GLN B 386      -2.988 -75.200 -67.077  1.00 33.61           O  
ANISOU 4543  OE1 GLN B 386     4870   2810   5092   -277    -17    153       O  
ATOM   4544  NE2 GLN B 386      -4.175 -73.415 -66.492  1.00 37.12           N  
ANISOU 4544  NE2 GLN B 386     5165   3352   5585   -304    -36    208       N  
ATOM   4545  N   PRO B 387       0.439 -71.191 -64.725  1.00 32.29           N  
ANISOU 4545  N   PRO B 387     4417   2991   4860   -108    375     59       N  
ATOM   4546  CA  PRO B 387       0.161 -70.573 -63.414  1.00 32.17           C  
ANISOU 4546  CA  PRO B 387     4271   3065   4886   -101    397     97       C  
ATOM   4547  C   PRO B 387      -0.887 -71.310 -62.564  1.00 38.51           C  
ANISOU 4547  C   PRO B 387     5003   3873   5755   -124    341    163       C  
ATOM   4548  O   PRO B 387      -1.980 -71.656 -63.035  1.00 37.80           O  
ANISOU 4548  O   PRO B 387     4938   3734   5691   -164    259    195       O  
ATOM   4549  CB  PRO B 387      -0.312 -69.159 -63.806  1.00 33.01           C  
ANISOU 4549  CB  PRO B 387     4371   3200   4971   -116    391     89       C  
ATOM   4550  CG  PRO B 387       0.459 -68.887 -65.076  1.00 37.73           C  
ANISOU 4550  CG  PRO B 387     5079   3752   5505   -106    416     29       C  
ATOM   4551  CD  PRO B 387       0.432 -70.172 -65.797  1.00 34.42           C  
ANISOU 4551  CD  PRO B 387     4757   3245   5078   -117    375     22       C  
ATOM   4552  N   GLU B 388      -0.490 -71.605 -61.308  1.00 35.42           N  
ANISOU 4552  N   GLU B 388     4526   3538   5394    -98    384    186       N  
ATOM   4553  CA  GLU B 388      -1.287 -72.333 -60.338  1.00 35.09           C  
ANISOU 4553  CA  GLU B 388     4409   3509   5414   -110    350    250       C  
ATOM   4554  C   GLU B 388      -2.359 -71.471 -59.632  1.00 41.29           C  
ANISOU 4554  C   GLU B 388     5107   4347   6233   -123    338    300       C  
ATOM   4555  O   GLU B 388      -2.386 -70.234 -59.742  1.00 37.57           O  
ANISOU 4555  O   GLU B 388     4626   3912   5737   -119    364    283       O  
ATOM   4556  CB  GLU B 388      -0.363 -73.040 -59.329  1.00 36.33           C  
ANISOU 4556  CB  GLU B 388     4521   3700   5583    -75    402    254       C  
ATOM   4557  CG  GLU B 388       0.077 -74.414 -59.809  1.00 40.37           C  
ANISOU 4557  CG  GLU B 388     5098   4142   6100    -74    384    243       C  
ATOM   4558  CD  GLU B 388      -0.918 -75.535 -59.592  1.00 43.08           C  
ANISOU 4558  CD  GLU B 388     5427   4444   6499   -103    312    297       C  
ATOM   4559  OE1 GLU B 388      -2.086 -75.251 -59.242  1.00 51.28           O  
ANISOU 4559  OE1 GLU B 388     6408   5498   7577   -129    267    349       O  
ATOM   4560  OE2 GLU B 388      -0.516 -76.712 -59.729  1.00 43.74           O  
ANISOU 4560  OE2 GLU B 388     5550   4478   6592    -98    302    293       O  
ATOM   4561  N   ASN B 389      -3.225 -72.143 -58.878  1.00 44.27           N  
ANISOU 4561  N   ASN B 389     5422   4727   6672   -135    304    366       N  
ATOM   4562  CA  ASN B 389      -4.370 -71.511 -58.192  1.00 47.10           C  
ANISOU 4562  CA  ASN B 389     5696   5124   7076   -145    294    428       C  
ATOM   4563  C   ASN B 389      -4.324 -71.439 -56.674  1.00 56.67           C  
ANISOU 4563  C   ASN B 389     6815   6407   8309   -115    351    467       C  
ATOM   4564  O   ASN B 389      -4.964 -70.524 -56.164  1.00 64.94           O  
ANISOU 4564  O   ASN B 389     7809   7496   9371   -110    372    498       O  
ATOM   4565  CB  ASN B 389      -5.688 -72.221 -58.567  1.00 50.78           C  
ANISOU 4565  CB  ASN B 389     6156   5530   7608   -188    203    492       C  
ATOM   4566  CG  ASN B 389      -5.721 -73.688 -58.202  1.00 81.04           C  
ANISOU 4566  CG  ASN B 389     9982   9328  11482   -194    171    525       C  
ATOM   4567  OD1 ASN B 389      -4.883 -74.480 -58.668  1.00 83.70           O  
ANISOU 4567  OD1 ASN B 389    10389   9625  11788   -189    168    480       O  
ATOM   4568  ND2 ASN B 389      -6.642 -74.081 -57.324  1.00 75.94           N  
ANISOU 4568  ND2 ASN B 389     9251   8696  10907   -200    154    605       N  
ATOM   4569  N   ASN B 390      -3.710 -72.385 -55.944  1.00 46.98           N  
ANISOU 4569  N   ASN B 390     5570   5189   7090    -96    372    472       N  
ATOM   4570  CA  ASN B 390      -3.901 -72.451 -54.479  1.00 45.77           C  
ANISOU 4570  CA  ASN B 390     5332   5095   6964    -74    412    523       C  
ATOM   4571  C   ASN B 390      -2.550 -72.631 -53.755  1.00 48.04           C  
ANISOU 4571  C   ASN B 390     5617   5423   7213    -40    470    487       C  
ATOM   4572  O   ASN B 390      -2.173 -73.753 -53.249  1.00 48.38           O  
ANISOU 4572  O   ASN B 390     5647   5458   7278    -33    467    505       O  
ATOM   4573  CB  ASN B 390      -4.892 -73.656 -54.164  1.00 52.49           C  
ANISOU 4573  CB  ASN B 390     6143   5910   7891    -94    357    598       C  
ATOM   4574  CG  ASN B 390      -5.309 -73.979 -52.710  1.00 75.45           C  
ANISOU 4574  CG  ASN B 390     8965   8864  10838    -75    389    666       C  
ATOM   4575  OD1 ASN B 390      -5.699 -73.108 -51.924  1.00 68.71           O  
ANISOU 4575  OD1 ASN B 390     8063   8062   9982    -56    436    694       O  
ATOM   4576  ND2 ASN B 390      -5.453 -75.275 -52.381  1.00 58.77           N  
ANISOU 4576  ND2 ASN B 390     6834   6724   8771    -82    359    706       N  
ATOM   4577  N   TYR B 391      -1.876 -71.472 -53.617  1.00 35.65           N  
ANISOU 4577  N   TYR B 391     4055   3900   5592    -20    521    445       N  
ATOM   4578  CA  TYR B 391      -0.604 -71.409 -52.950  1.00 31.88           C  
ANISOU 4578  CA  TYR B 391     3572   3462   5079      8    572    415       C  
ATOM   4579  C   TYR B 391      -0.550 -70.201 -52.071  1.00 35.77           C  
ANISOU 4579  C   TYR B 391     4031   4019   5540     26    619    417       C  
ATOM   4580  O   TYR B 391      -1.287 -69.254 -52.264  1.00 32.67           O  
ANISOU 4580  O   TYR B 391     3634   3637   5142     20    620    422       O  
ATOM   4581  CB  TYR B 391       0.553 -71.412 -53.950  1.00 30.72           C  
ANISOU 4581  CB  TYR B 391     3490   3286   4897     12    581    350       C  
ATOM   4582  CG  TYR B 391       0.483 -70.317 -54.991  1.00 30.97           C  
ANISOU 4582  CG  TYR B 391     3566   3306   4893      3    581    307       C  
ATOM   4583  CD1 TYR B 391       1.052 -69.070 -54.755  1.00 30.98           C  
ANISOU 4583  CD1 TYR B 391     3561   3356   4854     18    625    278       C  
ATOM   4584  CD2 TYR B 391      -0.037 -70.566 -56.258  1.00 30.95           C  
ANISOU 4584  CD2 TYR B 391     3622   3241   4895    -22    534    294       C  
ATOM   4585  CE1 TYR B 391       1.069 -68.098 -55.728  1.00 31.61           C  
ANISOU 4585  CE1 TYR B 391     3683   3425   4902     11    626    238       C  
ATOM   4586  CE2 TYR B 391       0.092 -69.634 -57.277  1.00 32.61           C  
ANISOU 4586  CE2 TYR B 391     3884   3438   5067    -28    537    250       C  
ATOM   4587  CZ  TYR B 391       0.665 -68.406 -57.010  1.00 32.48           C  
ANISOU 4587  CZ  TYR B 391     3853   3474   5014    -11    586    222       C  
ATOM   4588  OH  TYR B 391       0.639 -67.386 -57.917  1.00 34.21           O  
ANISOU 4588  OH  TYR B 391     4113   3686   5200    -18    587    187       O  
ATOM   4589  N   LYS B 392       0.306 -70.265 -51.064  1.00 35.49           N  
ANISOU 4589  N   LYS B 392     3974   4025   5486     47    654    416       N  
ATOM   4590  CA  LYS B 392       0.490 -69.200 -50.087  1.00 34.19           C  
ANISOU 4590  CA  LYS B 392     3789   3918   5283     65    696    417       C  
ATOM   4591  C   LYS B 392       1.957 -69.060 -49.769  1.00 34.89           C  
ANISOU 4591  C   LYS B 392     3890   4029   5337     79    720    380       C  
ATOM   4592  O   LYS B 392       2.692 -70.054 -49.660  1.00 35.98           O  
ANISOU 4592  O   LYS B 392     4025   4152   5493     82    713    382       O  
ATOM   4593  CB  LYS B 392      -0.258 -69.522 -48.783  1.00 36.68           C  
ANISOU 4593  CB  LYS B 392     4057   4262   5619     75    709    480       C  
ATOM   4594  CG  LYS B 392      -1.780 -69.651 -48.865  1.00 36.25           C  
ANISOU 4594  CG  LYS B 392     3972   4189   5611     65    692    536       C  
ATOM   4595  CD  LYS B 392      -2.489 -68.319 -49.154  1.00 33.30           C  
ANISOU 4595  CD  LYS B 392     3603   3828   5222     65    709    531       C  
ATOM   4596  CE  LYS B 392      -3.984 -68.467 -49.467  1.00 34.47           C  
ANISOU 4596  CE  LYS B 392     3719   3947   5432     50    684    590       C  
ATOM   4597  NZ  LYS B 392      -4.221 -69.017 -50.852  1.00 46.07           N  
ANISOU 4597  NZ  LYS B 392     5215   5357   6934     17    620    576       N  
ATOM   4598  N   THR B 393       2.359 -67.844 -49.557  1.00 30.00           N  
ANISOU 4598  N   THR B 393     3281   3444   4675     87    746    353       N  
ATOM   4599  CA  THR B 393       3.707 -67.479 -49.225  1.00 30.54           C  
ANISOU 4599  CA  THR B 393     3357   3534   4711     97    764    324       C  
ATOM   4600  C   THR B 393       3.743 -66.734 -47.914  1.00 34.53           C  
ANISOU 4600  C   THR B 393     3851   4089   5182    107    785    341       C  
ATOM   4601  O   THR B 393       2.938 -65.851 -47.683  1.00 33.30           O  
ANISOU 4601  O   THR B 393     3698   3950   5004    110    800    347       O  
ATOM   4602  CB  THR B 393       4.275 -66.704 -50.406  1.00 37.97           C  
ANISOU 4602  CB  THR B 393     4334   4459   5633     93    769    270       C  
ATOM   4603  OG1 THR B 393       4.112 -67.513 -51.571  1.00 39.45           O  
ANISOU 4603  OG1 THR B 393     4546   4594   5849     84    749    259       O  
ATOM   4604  CG2 THR B 393       5.723 -66.343 -50.221  1.00 35.08           C  
ANISOU 4604  CG2 THR B 393     3972   4109   5248    101    786    245       C  
ATOM   4605  N   THR B 394       4.753 -67.005 -47.102  1.00 34.52           N  
ANISOU 4605  N   THR B 394     3840   4106   5169    113    787    347       N  
ATOM   4606  CA  THR B 394       4.905 -66.322 -45.818  1.00 33.87           C  
ANISOU 4606  CA  THR B 394     3762   4065   5044    121    800    362       C  
ATOM   4607  C   THR B 394       5.467 -64.927 -46.045  1.00 36.03           C  
ANISOU 4607  C   THR B 394     4064   4354   5273    119    810    320       C  
ATOM   4608  O   THR B 394       6.169 -64.704 -47.035  1.00 35.25           O  
ANISOU 4608  O   THR B 394     3973   4237   5183    113    805    283       O  
ATOM   4609  CB  THR B 394       5.898 -67.095 -44.894  1.00 36.88           C  
ANISOU 4609  CB  THR B 394     4127   4457   5430    122    787    384       C  
ATOM   4610  OG1 THR B 394       7.222 -67.020 -45.391  1.00 37.43           O  
ANISOU 4610  OG1 THR B 394     4199   4516   5508    117    778    356       O  
ATOM   4611  CG2 THR B 394       5.547 -68.558 -44.707  1.00 42.06           C  
ANISOU 4611  CG2 THR B 394     4753   5095   6133    123    776    424       C  
ATOM   4612  N   PRO B 395       5.341 -63.998 -45.089  1.00 32.43           N  
ANISOU 4612  N   PRO B 395     3627   3928   4767    125    823    324       N  
ATOM   4613  CA  PRO B 395       6.089 -62.761 -45.240  1.00 33.51           C  
ANISOU 4613  CA  PRO B 395     3792   4076   4865    121    823    286       C  
ATOM   4614  C   PRO B 395       7.612 -63.023 -45.124  1.00 38.10           C  
ANISOU 4614  C   PRO B 395     4365   4656   5455    112    799    278       C  
ATOM   4615  O   PRO B 395       8.061 -64.056 -44.579  1.00 36.66           O  
ANISOU 4615  O   PRO B 395     4161   4471   5297    111    784    308       O  
ATOM   4616  CB  PRO B 395       5.558 -61.864 -44.109  1.00 34.94           C  
ANISOU 4616  CB  PRO B 395     4004   4284   4989    130    842    298       C  
ATOM   4617  CG  PRO B 395       4.396 -62.540 -43.553  1.00 36.34           C  
ANISOU 4617  CG  PRO B 395     4167   4462   5180    143    861    343       C  
ATOM   4618  CD  PRO B 395       4.588 -64.004 -43.826  1.00 33.11           C  
ANISOU 4618  CD  PRO B 395     3718   4035   4827    137    840    365       C  
ATOM   4619  N   PRO B 396       8.424 -62.117 -45.678  1.00 36.02           N  
ANISOU 4619  N   PRO B 396     4115   4391   5180    105    795    243       N  
ATOM   4620  CA  PRO B 396       9.891 -62.240 -45.523  1.00 35.84           C  
ANISOU 4620  CA  PRO B 396     4079   4366   5173     96    772    245       C  
ATOM   4621  C   PRO B 396      10.302 -62.165 -44.051  1.00 39.81           C  
ANISOU 4621  C   PRO B 396     4592   4890   5643     90    747    275       C  
ATOM   4622  O   PRO B 396       9.693 -61.420 -43.297  1.00 38.65           O  
ANISOU 4622  O   PRO B 396     4482   4761   5441     92    752    275       O  
ATOM   4623  CB  PRO B 396      10.436 -61.019 -46.275  1.00 37.56           C  
ANISOU 4623  CB  PRO B 396     4312   4581   5377     90    776    207       C  
ATOM   4624  CG  PRO B 396       9.310 -60.551 -47.150  1.00 41.77           C  
ANISOU 4624  CG  PRO B 396     4863   5108   5900     96    801    180       C  
ATOM   4625  CD  PRO B 396       8.062 -60.889 -46.401  1.00 38.28           C  
ANISOU 4625  CD  PRO B 396     4426   4678   5441    104    810    206       C  
ATOM   4626  N   VAL B 397      11.296 -62.956 -43.639  1.00 38.27           N  
ANISOU 4626  N   VAL B 397     4370   4690   5481     83    722    303       N  
ATOM   4627  CA  VAL B 397      11.787 -62.959 -42.255  1.00 38.41           C  
ANISOU 4627  CA  VAL B 397     4401   4724   5470     72    687    335       C  
ATOM   4628  C   VAL B 397      13.249 -62.537 -42.282  1.00 40.88           C  
ANISOU 4628  C   VAL B 397     4701   5030   5803     54    652    338       C  
ATOM   4629  O   VAL B 397      14.020 -63.017 -43.112  1.00 39.78           O  
ANISOU 4629  O   VAL B 397     4519   4870   5725     55    656    339       O  
ATOM   4630  CB  VAL B 397      11.607 -64.364 -41.590  1.00 42.74           C  
ANISOU 4630  CB  VAL B 397     4922   5271   6044     77    681    379       C  
ATOM   4631  CG1 VAL B 397      12.117 -64.369 -40.146  1.00 42.91           C  
ANISOU 4631  CG1 VAL B 397     4966   5307   6031     63    642    414       C  
ATOM   4632  CG2 VAL B 397      10.152 -64.835 -41.648  1.00 41.70           C  
ANISOU 4632  CG2 VAL B 397     4794   5142   5907     94    715    384       C  
ATOM   4633  N   LEU B 398      13.621 -61.609 -41.420  1.00 38.27           N  
ANISOU 4633  N   LEU B 398     4409   4711   5421     38    618    340       N  
ATOM   4634  CA  LEU B 398      14.991 -61.141 -41.354  1.00 38.99           C  
ANISOU 4634  CA  LEU B 398     4488   4793   5535     15    574    351       C  
ATOM   4635  C   LEU B 398      15.870 -62.233 -40.752  1.00 44.76           C  
ANISOU 4635  C   LEU B 398     5176   5515   6315      5    538    402       C  
ATOM   4636  O   LEU B 398      15.594 -62.774 -39.677  1.00 42.61           O  
ANISOU 4636  O   LEU B 398     4922   5253   6015      1    517    431       O  
ATOM   4637  CB  LEU B 398      15.081 -59.842 -40.544  1.00 39.52           C  
ANISOU 4637  CB  LEU B 398     4618   4869   5528     -3    539    340       C  
ATOM   4638  CG  LEU B 398      16.484 -59.197 -40.398  1.00 44.70           C  
ANISOU 4638  CG  LEU B 398     5266   5513   6206    -33    479    356       C  
ATOM   4639  CD1 LEU B 398      17.045 -58.717 -41.734  1.00 44.36           C  
ANISOU 4639  CD1 LEU B 398     5181   5456   6217    -30    501    333       C  
ATOM   4640  CD2 LEU B 398      16.446 -58.049 -39.445  1.00 41.27           C  
ANISOU 4640  CD2 LEU B 398     4909   5082   5689    -53    438    347       C  
ATOM   4641  N   ASP B 399      16.890 -62.598 -41.504  1.00 45.90           N  
ANISOU 4641  N   ASP B 399     5263   5639   6536      4    537    415       N  
ATOM   4642  CA  ASP B 399      17.861 -63.595 -41.110  1.00 47.18           C  
ANISOU 4642  CA  ASP B 399     5375   5788   6763     -4    506    468       C  
ATOM   4643  C   ASP B 399      19.014 -62.980 -40.291  1.00 50.66           C  
ANISOU 4643  C   ASP B 399     5817   6226   7207    -38    434    504       C  
ATOM   4644  O   ASP B 399      19.178 -61.763 -40.234  1.00 51.01           O  
ANISOU 4644  O   ASP B 399     5898   6274   7212    -54    411    484       O  
ATOM   4645  CB  ASP B 399      18.418 -64.289 -42.370  1.00 49.44           C  
ANISOU 4645  CB  ASP B 399     5601   6048   7138     15    549    470       C  
ATOM   4646  CG  ASP B 399      18.601 -65.769 -42.202  1.00 57.94           C  
ANISOU 4646  CG  ASP B 399     6632   7111   8271     26    555    509       C  
ATOM   4647  OD1 ASP B 399      18.490 -66.252 -41.061  1.00 61.95           O  
ANISOU 4647  OD1 ASP B 399     7147   7631   8759     14    518    542       O  
ATOM   4648  OD2 ASP B 399      18.744 -66.459 -43.217  1.00 62.38           O  
ANISOU 4648  OD2 ASP B 399     7162   7649   8891     49    601    504       O  
ATOM   4649  N   SER B 400      19.811 -63.844 -39.677  1.00 48.34           N  
ANISOU 4649  N   SER B 400     5482   5922   6963    -51    396    560       N  
ATOM   4650  CA  SER B 400      21.010 -63.473 -38.878  1.00 48.93           C  
ANISOU 4650  CA  SER B 400     5546   5986   7058    -88    315    609       C  
ATOM   4651  C   SER B 400      22.098 -62.702 -39.659  1.00 51.63           C  
ANISOU 4651  C   SER B 400     5847   6308   7462    -98    304    616       C  
ATOM   4652  O   SER B 400      22.800 -61.874 -39.078  1.00 52.09           O  
ANISOU 4652  O   SER B 400     5922   6360   7511   -133    234    639       O  
ATOM   4653  CB  SER B 400      21.646 -64.728 -38.287  1.00 51.87           C  
ANISOU 4653  CB  SER B 400     5866   6347   7494    -94    285    673       C  
ATOM   4654  OG  SER B 400      20.846 -65.188 -37.214  1.00 68.38           O  
ANISOU 4654  OG  SER B 400     8006   8456   9517    -97    269    679       O  
ATOM   4655  N   ASP B 401      22.243 -62.979 -40.953  1.00 45.22           N  
ANISOU 4655  N   ASP B 401     4985   5482   6713    -69    371    601       N  
ATOM   4656  CA  ASP B 401      23.235 -62.306 -41.790  1.00 44.58           C  
ANISOU 4656  CA  ASP B 401     4862   5381   6697    -72    376    611       C  
ATOM   4657  C   ASP B 401      22.744 -60.994 -42.451  1.00 46.05           C  
ANISOU 4657  C   ASP B 401     5095   5576   6827    -70    399    551       C  
ATOM   4658  O   ASP B 401      23.383 -60.526 -43.397  1.00 46.13           O  
ANISOU 4658  O   ASP B 401     5069   5569   6889    -62    425    551       O  
ATOM   4659  CB  ASP B 401      23.745 -63.276 -42.878  1.00 46.06           C  
ANISOU 4659  CB  ASP B 401     4978   5541   6983    -38    444    630       C  
ATOM   4660  CG  ASP B 401      22.746 -63.626 -43.954  1.00 55.82           C  
ANISOU 4660  CG  ASP B 401     6237   6778   8195      1    529    570       C  
ATOM   4661  OD1 ASP B 401      21.542 -63.285 -43.791  1.00 55.31           O  
ANISOU 4661  OD1 ASP B 401     6235   6738   8043      2    536    520       O  
ATOM   4662  OD2 ASP B 401      23.143 -64.287 -44.929  1.00 62.07           O  
ANISOU 4662  OD2 ASP B 401     6988   7542   9055     31    588    578       O  
ATOM   4663  N   GLY B 402      21.604 -60.460 -42.025  1.00 40.13           N  
ANISOU 4663  N   GLY B 402     4420   4851   5976    -71    399    503       N  
ATOM   4664  CA  GLY B 402      21.071 -59.225 -42.589  1.00 39.32           C  
ANISOU 4664  CA  GLY B 402     4363   4756   5819    -69    420    448       C  
ATOM   4665  C   GLY B 402      20.237 -59.375 -43.848  1.00 41.41           C  
ANISOU 4665  C   GLY B 402     4627   5022   6082    -33    503    398       C  
ATOM   4666  O   GLY B 402      19.684 -58.389 -44.335  1.00 42.37           O  
ANISOU 4666  O   GLY B 402     4788   5152   6158    -30    524    351       O  
ATOM   4667  N   SER B 403      20.096 -60.585 -44.376  1.00 38.33           N  
ANISOU 4667  N   SER B 403     4202   4623   5740     -7    549    406       N  
ATOM   4668  CA  SER B 403      19.276 -60.833 -45.558  1.00 37.62           C  
ANISOU 4668  CA  SER B 403     4121   4527   5646     23    619    361       C  
ATOM   4669  C   SER B 403      17.929 -61.402 -45.105  1.00 41.99           C  
ANISOU 4669  C   SER B 403     4712   5099   6145     32    631    343       C  
ATOM   4670  O   SER B 403      17.699 -61.559 -43.906  1.00 41.50           O  
ANISOU 4670  O   SER B 403     4668   5053   6047     18    593    364       O  
ATOM   4671  CB  SER B 403      19.985 -61.792 -46.501  1.00 42.54           C  
ANISOU 4671  CB  SER B 403     4690   5118   6354     46    664    382       C  
ATOM   4672  OG  SER B 403      19.977 -63.118 -45.986  1.00 47.52           O  
ANISOU 4672  OG  SER B 403     5296   5742   7015     53    660    416       O  
ATOM   4673  N   PHE B 404      17.012 -61.645 -46.050  1.00 38.20           N  
ANISOU 4673  N   PHE B 404     4247   4613   5656     54    682    305       N  
ATOM   4674  CA  PHE B 404      15.700 -62.174 -45.706  1.00 36.28           C  
ANISOU 4674  CA  PHE B 404     4030   4382   5372     62    694    295       C  
ATOM   4675  C   PHE B 404      15.526 -63.532 -46.277  1.00 38.44           C  
ANISOU 4675  C   PHE B 404     4278   4633   5693     80    723    304       C  
ATOM   4676  O   PHE B 404      16.135 -63.876 -47.281  1.00 35.70           O  
ANISOU 4676  O   PHE B 404     3911   4258   5397     93    751    300       O  
ATOM   4677  CB  PHE B 404      14.570 -61.271 -46.243  1.00 36.90           C  
ANISOU 4677  CB  PHE B 404     4153   4471   5397     67    719    248       C  
ATOM   4678  CG  PHE B 404      14.382 -59.965 -45.508  1.00 36.82           C  
ANISOU 4678  CG  PHE B 404     4182   4484   5323     52    694    235       C  
ATOM   4679  CD1 PHE B 404      15.080 -58.830 -45.890  1.00 39.93           C  
ANISOU 4679  CD1 PHE B 404     4582   4876   5714     41    684    218       C  
ATOM   4680  CD2 PHE B 404      13.430 -59.845 -44.516  1.00 35.37           C  
ANISOU 4680  CD2 PHE B 404     4035   4321   5083     52    688    239       C  
ATOM   4681  CE1 PHE B 404      14.903 -57.623 -45.208  1.00 41.18           C  
ANISOU 4681  CE1 PHE B 404     4786   5051   5811     27    660    204       C  
ATOM   4682  CE2 PHE B 404      13.253 -58.640 -43.824  1.00 37.69           C  
ANISOU 4682  CE2 PHE B 404     4377   4630   5312     41    671    227       C  
ATOM   4683  CZ  PHE B 404      13.986 -57.536 -44.173  1.00 37.00           C  
ANISOU 4683  CZ  PHE B 404     4299   4538   5220     28    654    207       C  
ATOM   4684  N   PHE B 405      14.599 -64.273 -45.700  1.00 37.73           N  
ANISOU 4684  N   PHE B 405     4196   4552   5586     84    720    316       N  
ATOM   4685  CA  PHE B 405      14.177 -65.547 -46.270  1.00 37.14           C  
ANISOU 4685  CA  PHE B 405     4108   4454   5551    100    745    321       C  
ATOM   4686  C   PHE B 405      12.656 -65.655 -46.188  1.00 37.77           C  
ANISOU 4686  C   PHE B 405     4215   4544   5593    103    753    308       C  
ATOM   4687  O   PHE B 405      12.018 -64.938 -45.419  1.00 36.91           O  
ANISOU 4687  O   PHE B 405     4129   4463   5431     96    743    307       O  
ATOM   4688  CB  PHE B 405      14.898 -66.753 -45.619  1.00 39.47           C  
ANISOU 4688  CB  PHE B 405     4363   4740   5896    101    728    369       C  
ATOM   4689  CG  PHE B 405      14.350 -67.158 -44.287  1.00 40.27           C  
ANISOU 4689  CG  PHE B 405     4466   4866   5969     92    699    400       C  
ATOM   4690  CD1 PHE B 405      14.825 -66.582 -43.122  1.00 42.58           C  
ANISOU 4690  CD1 PHE B 405     4765   5183   6230     74    659    423       C  
ATOM   4691  CD2 PHE B 405      13.345 -68.111 -44.195  1.00 41.13           C  
ANISOU 4691  CD2 PHE B 405     4575   4971   6080    101    709    409       C  
ATOM   4692  CE1 PHE B 405      14.257 -66.912 -41.886  1.00 44.93           C  
ANISOU 4692  CE1 PHE B 405     5078   5502   6491     68    637    451       C  
ATOM   4693  CE2 PHE B 405      12.789 -68.441 -42.965  1.00 42.37           C  
ANISOU 4693  CE2 PHE B 405     4737   5152   6210     96    689    441       C  
ATOM   4694  CZ  PHE B 405      13.249 -67.841 -41.818  1.00 41.69           C  
ANISOU 4694  CZ  PHE B 405     4664   5091   6086     81    657    461       C  
ATOM   4695  N   LEU B 406      12.077 -66.535 -47.002  1.00 34.03           N  
ANISOU 4695  N   LEU B 406     3741   4043   5146    114    773    301       N  
ATOM   4696  CA  LEU B 406      10.659 -66.886 -46.867  1.00 33.29           C  
ANISOU 4696  CA  LEU B 406     3660   3953   5035    115    774    305       C  
ATOM   4697  C   LEU B 406      10.404 -68.293 -47.366  1.00 36.90           C  
ANISOU 4697  C   LEU B 406     4105   4375   5540    122    778    318       C  
ATOM   4698  O   LEU B 406      11.308 -68.937 -47.897  1.00 37.51           O  
ANISOU 4698  O   LEU B 406     4171   4423   5657    130    786    319       O  
ATOM   4699  CB  LEU B 406       9.703 -65.871 -47.522  1.00 32.72           C  
ANISOU 4699  CB  LEU B 406     3620   3885   4927    113    787    270       C  
ATOM   4700  CG  LEU B 406       9.892 -65.540 -48.994  1.00 36.12           C  
ANISOU 4700  CG  LEU B 406     4071   4285   5367    115    805    230       C  
ATOM   4701  CD1 LEU B 406       9.481 -66.703 -49.879  1.00 36.48           C  
ANISOU 4701  CD1 LEU B 406     4124   4288   5449    120    809    229       C  
ATOM   4702  CD2 LEU B 406       9.076 -64.293 -49.318  1.00 34.98           C  
ANISOU 4702  CD2 LEU B 406     3954   4155   5180    110    811    202       C  
ATOM   4703  N   TYR B 407       9.163 -68.771 -47.183  1.00 33.62           N  
ANISOU 4703  N   TYR B 407     3693   3959   5122    121    772    333       N  
ATOM   4704  CA  TYR B 407       8.717 -70.025 -47.740  1.00 33.07           C  
ANISOU 4704  CA  TYR B 407     3619   3851   5093    124    768    344       C  
ATOM   4705  C   TYR B 407       7.424 -69.796 -48.511  1.00 36.17           C  
ANISOU 4705  C   TYR B 407     4037   4228   5477    117    766    329       C  
ATOM   4706  O   TYR B 407       6.593 -69.026 -48.102  1.00 34.85           O  
ANISOU 4706  O   TYR B 407     3873   4088   5282    113    767    334       O  
ATOM   4707  CB  TYR B 407       8.483 -71.078 -46.640  1.00 35.15           C  
ANISOU 4707  CB  TYR B 407     3851   4125   5379    124    753    394       C  
ATOM   4708  CG  TYR B 407       9.733 -71.703 -46.054  1.00 34.88           C  
ANISOU 4708  CG  TYR B 407     3790   4092   5372    129    748    417       C  
ATOM   4709  CD1 TYR B 407      10.258 -72.875 -46.578  1.00 36.06           C  
ANISOU 4709  CD1 TYR B 407     3928   4200   5573    137    751    424       C  
ATOM   4710  CD2 TYR B 407      10.291 -71.217 -44.885  1.00 36.56           C  
ANISOU 4710  CD2 TYR B 407     3988   4342   5560    124    736    438       C  
ATOM   4711  CE1 TYR B 407      11.352 -73.502 -45.993  1.00 36.98           C  
ANISOU 4711  CE1 TYR B 407     4011   4317   5723    141    746    454       C  
ATOM   4712  CE2 TYR B 407      11.423 -71.802 -44.323  1.00 37.02           C  
ANISOU 4712  CE2 TYR B 407     4017   4400   5650    124    724    467       C  
ATOM   4713  CZ  TYR B 407      11.902 -72.988 -44.831  1.00 43.61           C  
ANISOU 4713  CZ  TYR B 407     4830   5196   6542    133    730    478       C  
ATOM   4714  OH  TYR B 407      13.038 -73.535 -44.287  1.00 46.95           O  
ANISOU 4714  OH  TYR B 407     5218   5616   7003    134    719    512       O  
ATOM   4715  N   SER B 408       7.237 -70.541 -49.580  1.00 35.17           N  
ANISOU 4715  N   SER B 408     3932   4053   5379    116    761    316       N  
ATOM   4716  CA  SER B 408       6.010 -70.567 -50.359  1.00 33.89           C  
ANISOU 4716  CA  SER B 408     3793   3864   5218    105    745    310       C  
ATOM   4717  C   SER B 408       5.591 -72.053 -50.414  1.00 37.27           C  
ANISOU 4717  C   SER B 408     4215   4253   5691    101    722    340       C  
ATOM   4718  O   SER B 408       6.415 -72.961 -50.478  1.00 33.60           O  
ANISOU 4718  O   SER B 408     3750   3765   5252    111    726    342       O  
ATOM   4719  CB  SER B 408       6.204 -69.971 -51.747  1.00 35.21           C  
ANISOU 4719  CB  SER B 408     4009   4000   5369    102    753    261       C  
ATOM   4720  OG  SER B 408       4.987 -69.945 -52.474  1.00 40.91           O  
ANISOU 4720  OG  SER B 408     4756   4695   6093     86    728    260       O  
ATOM   4721  N   ARG B 409       4.321 -72.269 -50.268  1.00 35.78           N  
ANISOU 4721  N   ARG B 409     4016   4061   5517     89    698    370       N  
ATOM   4722  CA  ARG B 409       3.755 -73.579 -50.183  1.00 35.28           C  
ANISOU 4722  CA  ARG B 409     3941   3965   5498     82    669    406       C  
ATOM   4723  C   ARG B 409       2.643 -73.747 -51.196  1.00 37.67           C  
ANISOU 4723  C   ARG B 409     4274   4221   5818     61    633    406       C  
ATOM   4724  O   ARG B 409       1.669 -73.006 -51.150  1.00 36.63           O  
ANISOU 4724  O   ARG B 409     4132   4106   5682     51    625    421       O  
ATOM   4725  CB  ARG B 409       3.165 -73.713 -48.787  1.00 35.47           C  
ANISOU 4725  CB  ARG B 409     3912   4033   5533     85    670    462       C  
ATOM   4726  CG  ARG B 409       2.685 -75.101 -48.507  1.00 37.41           C  
ANISOU 4726  CG  ARG B 409     4134   4250   5828     79    643    507       C  
ATOM   4727  CD  ARG B 409       2.329 -75.258 -47.042  1.00 47.81           C  
ANISOU 4727  CD  ARG B 409     5401   5613   7151     88    654    562       C  
ATOM   4728  NE  ARG B 409       1.353 -76.317 -46.965  1.00 52.00           N  
ANISOU 4728  NE  ARG B 409     5907   6114   7734     77    623    613       N  
ATOM   4729  CZ  ARG B 409       0.066 -76.163 -46.747  1.00 55.95           C  
ANISOU 4729  CZ  ARG B 409     6384   6618   8257     70    614    657       C  
ATOM   4730  NH1 ARG B 409      -0.423 -74.977 -46.446  1.00 47.28           N  
ANISOU 4730  NH1 ARG B 409     5280   5555   7128     76    642    658       N  
ATOM   4731  NH2 ARG B 409      -0.740 -77.216 -46.763  1.00 60.67           N  
ANISOU 4731  NH2 ARG B 409     6958   7182   8913     57    580    706       N  
ATOM   4732  N   LEU B 410       2.735 -74.784 -52.020  1.00 34.55           N  
ANISOU 4732  N   LEU B 410     3915   3764   5447     54    607    398       N  
ATOM   4733  CA  LEU B 410       1.715 -75.142 -52.970  1.00 32.24           C  
ANISOU 4733  CA  LEU B 410     3660   3416   5174     29    559    402       C  
ATOM   4734  C   LEU B 410       1.107 -76.474 -52.554  1.00 35.03           C  
ANISOU 4734  C   LEU B 410     3988   3742   5581     19    520    454       C  
ATOM   4735  O   LEU B 410       1.791 -77.508 -52.491  1.00 36.12           O  
ANISOU 4735  O   LEU B 410     4134   3853   5736     28    523    453       O  
ATOM   4736  CB  LEU B 410       2.308 -75.232 -54.389  1.00 31.46           C  
ANISOU 4736  CB  LEU B 410     3645   3258   5051     28    556    346       C  
ATOM   4737  CG  LEU B 410       1.366 -75.777 -55.474  1.00 33.76           C  
ANISOU 4737  CG  LEU B 410     3995   3476   5358     -2    495    348       C  
ATOM   4738  CD1 LEU B 410       0.296 -74.770 -55.820  1.00 33.12           C  
ANISOU 4738  CD1 LEU B 410     3911   3405   5269    -25    467    356       C  
ATOM   4739  CD2 LEU B 410       2.113 -76.190 -56.662  1.00 31.10           C  
ANISOU 4739  CD2 LEU B 410     3749   3074   4995      4    500    298       C  
ATOM   4740  N   THR B 411      -0.190 -76.470 -52.395  1.00 35.04           N  
ANISOU 4740  N   THR B 411     3960   3739   5613     -2    483    501       N  
ATOM   4741  CA  THR B 411      -0.989 -77.671 -52.097  1.00 36.67           C  
ANISOU 4741  CA  THR B 411     4140   3912   5879    -18    437    559       C  
ATOM   4742  C   THR B 411      -1.508 -78.245 -53.402  1.00 41.55           C  
ANISOU 4742  C   THR B 411     4824   4448   6514    -49    373    547       C  
ATOM   4743  O   THR B 411      -2.171 -77.533 -54.175  1.00 39.56           O  
ANISOU 4743  O   THR B 411     4600   4177   6253    -69    345    538       O  
ATOM   4744  CB  THR B 411      -2.185 -77.339 -51.192  1.00 47.92           C  
ANISOU 4744  CB  THR B 411     5492   5375   7339    -24    433    628       C  
ATOM   4745  OG1 THR B 411      -1.659 -77.008 -49.911  1.00 51.63           O  
ANISOU 4745  OG1 THR B 411     5914   5914   7789      5    490    640       O  
ATOM   4746  CG2 THR B 411      -3.179 -78.514 -51.071  1.00 50.61           C  
ANISOU 4746  CG2 THR B 411     5803   5673   7751    -46    376    695       C  
ATOM   4747  N   VAL B 412      -1.261 -79.545 -53.603  1.00 41.02           N  
ANISOU 4747  N   VAL B 412     4783   4327   6474    -53    344    553       N  
ATOM   4748  CA  VAL B 412      -1.705 -80.274 -54.781  1.00 42.63           C  
ANISOU 4748  CA  VAL B 412     5064   4442   6691    -83    277    543       C  
ATOM   4749  C   VAL B 412      -2.273 -81.610 -54.371  1.00 48.55           C  
ANISOU 4749  C   VAL B 412     5786   5155   7505    -98    227    601       C  
ATOM   4750  O   VAL B 412      -1.892 -82.151 -53.340  1.00 49.80           O  
ANISOU 4750  O   VAL B 412     5888   5349   7685    -78    258    628       O  
ATOM   4751  CB  VAL B 412      -0.536 -80.451 -55.804  1.00 46.54           C  
ANISOU 4751  CB  VAL B 412     5658   4890   7135    -67    301    468       C  
ATOM   4752  CG1 VAL B 412       0.027 -79.100 -56.202  1.00 45.69           C  
ANISOU 4752  CG1 VAL B 412     5571   4820   6969    -51    351    416       C  
ATOM   4753  CG2 VAL B 412       0.586 -81.356 -55.274  1.00 46.51           C  
ANISOU 4753  CG2 VAL B 412     5645   4888   7139    -35    345    461       C  
ATOM   4754  N   ASP B 413      -3.114 -82.193 -55.212  1.00 45.81           N  
ANISOU 4754  N   ASP B 413     5488   4732   7187   -136    145    618       N  
ATOM   4755  CA  ASP B 413      -3.615 -83.550 -54.959  1.00 45.14           C  
ANISOU 4755  CA  ASP B 413     5388   4598   7163   -155     88    670       C  
ATOM   4756  C   ASP B 413      -2.437 -84.475 -55.079  1.00 46.82           C  
ANISOU 4756  C   ASP B 413     5653   4780   7356   -130    118    628       C  
ATOM   4757  O   ASP B 413      -1.623 -84.292 -55.973  1.00 46.67           O  
ANISOU 4757  O   ASP B 413     5722   4728   7281   -117    143    560       O  
ATOM   4758  CB  ASP B 413      -4.659 -83.962 -56.000  1.00 47.68           C  
ANISOU 4758  CB  ASP B 413     5771   4831   7514   -206    -15    690       C  
ATOM   4759  CG  ASP B 413      -5.959 -83.198 -55.906  1.00 62.70           C  
ANISOU 4759  CG  ASP B 413     7613   6753   9458   -235    -57    749       C  
ATOM   4760  OD1 ASP B 413      -6.194 -82.545 -54.851  1.00 64.08           O  
ANISOU 4760  OD1 ASP B 413     7689   7009   9651   -215     -3    789       O  
ATOM   4761  OD2 ASP B 413      -6.751 -83.249 -56.887  1.00 65.74           O  
ANISOU 4761  OD2 ASP B 413     8052   7067   9857   -280   -143    760       O  
ATOM   4762  N   LYS B 414      -2.331 -85.464 -54.197  1.00 43.69           N  
ANISOU 4762  N   LYS B 414     5203   4391   7006   -121    121    670       N  
ATOM   4763  CA  LYS B 414      -1.246 -86.439 -54.230  1.00 43.08           C  
ANISOU 4763  CA  LYS B 414     5165   4282   6921    -96    149    640       C  
ATOM   4764  C   LYS B 414      -1.138 -87.153 -55.600  1.00 48.02           C  
ANISOU 4764  C   LYS B 414     5920   4798   7527   -112    102    597       C  
ATOM   4765  O   LYS B 414      -0.026 -87.455 -56.039  1.00 48.52           O  
ANISOU 4765  O   LYS B 414     6048   4832   7554    -83    150    544       O  
ATOM   4766  CB  LYS B 414      -1.451 -87.469 -53.122  1.00 45.64           C  
ANISOU 4766  CB  LYS B 414     5411   4622   7310    -94    139    706       C  
ATOM   4767  CG  LYS B 414      -0.402 -88.578 -53.130  1.00 52.33           C  
ANISOU 4767  CG  LYS B 414     6293   5429   8160    -69    164    683       C  
ATOM   4768  CD  LYS B 414      -0.378 -89.373 -51.858  1.00 66.25           C  
ANISOU 4768  CD  LYS B 414     7965   7231   9978    -58    174    744       C  
ATOM   4769  CE  LYS B 414      -1.631 -90.191 -51.662  1.00 66.79           C  
ANISOU 4769  CE  LYS B 414     8002   7262  10113    -95     93    814       C  
ATOM   4770  NZ  LYS B 414      -1.708 -90.699 -50.283  1.00 70.70           N  
ANISOU 4770  NZ  LYS B 414     8394   7812  10657    -83    112    880       N  
ATOM   4771  N   SER B 415      -2.290 -87.469 -56.225  1.00 44.12           N  
ANISOU 4771  N   SER B 415     5463   4240   7061   -159      8    625       N  
ATOM   4772  CA  SER B 415      -2.378 -88.110 -57.537  1.00 44.50           C  
ANISOU 4772  CA  SER B 415     5646   4176   7086   -183    -55    589       C  
ATOM   4773  C   SER B 415      -1.597 -87.305 -58.589  1.00 47.64           C  
ANISOU 4773  C   SER B 415     6146   4556   7399   -164     -8    507       C  
ATOM   4774  O   SER B 415      -0.878 -87.886 -59.392  1.00 47.12           O  
ANISOU 4774  O   SER B 415     6192   4418   7295   -150      5    456       O  
ATOM   4775  CB  SER B 415      -3.843 -88.253 -57.960  1.00 47.90           C  
ANISOU 4775  CB  SER B 415     6084   4555   7561   -243   -170    642       C  
ATOM   4776  OG  SER B 415      -4.505 -86.997 -58.005  1.00 60.04           O  
ANISOU 4776  OG  SER B 415     7578   6142   9093   -258   -175    655       O  
ATOM   4777  N   ARG B 416      -1.718 -85.979 -58.555  1.00 44.12           N  
ANISOU 4777  N   ARG B 416     5664   4176   6926   -162     22    495       N  
ATOM   4778  CA  ARG B 416      -1.005 -85.083 -59.490  1.00 44.07           C  
ANISOU 4778  CA  ARG B 416     5742   4162   6842   -143     70    422       C  
ATOM   4779  C   ARG B 416       0.500 -85.059 -59.287  1.00 46.48           C  
ANISOU 4779  C   ARG B 416     6052   4496   7113    -87    176    376       C  
ATOM   4780  O   ARG B 416       1.246 -84.981 -60.262  1.00 45.36           O  
ANISOU 4780  O   ARG B 416     6016   4304   6916    -68    211    316       O  
ATOM   4781  CB  ARG B 416      -1.588 -83.666 -59.444  1.00 42.36           C  
ANISOU 4781  CB  ARG B 416     5475   4008   6611   -157     70    429       C  
ATOM   4782  CG  ARG B 416      -2.949 -83.588 -60.185  1.00 48.62           C  
ANISOU 4782  CG  ARG B 416     6308   4743   7423   -215    -40    459       C  
ATOM   4783  CD  ARG B 416      -2.974 -82.450 -61.177  1.00 66.87           C  
ANISOU 4783  CD  ARG B 416     8688   7047   9674   -224    -39    412       C  
ATOM   4784  NE  ARG B 416      -2.979 -81.148 -60.477  1.00 84.88           N  
ANISOU 4784  NE  ARG B 416    10868   9429  11952   -207     20    420       N  
ATOM   4785  CZ  ARG B 416      -2.202 -80.091 -60.748  1.00 78.22           C  
ANISOU 4785  CZ  ARG B 416    10043   8627  11050   -179     91    366       C  
ATOM   4786  NH1 ARG B 416      -1.286 -80.151 -61.722  1.00 55.92           N  
ANISOU 4786  NH1 ARG B 416     7331   5753   8161   -160    123    299       N  
ATOM   4787  NH2 ARG B 416      -2.322 -78.971 -60.038  1.00 39.49           N  
ANISOU 4787  NH2 ARG B 416     5046   3809   6148   -167    134    380       N  
ATOM   4788  N   TRP B 417       0.944 -85.128 -58.030  1.00 41.88           N  
ANISOU 4788  N   TRP B 417     5358   3989   6565    -61    227    407       N  
ATOM   4789  CA  TRP B 417       2.353 -85.223 -57.700  1.00 40.88           C  
ANISOU 4789  CA  TRP B 417     5219   3889   6424    -11    318    378       C  
ATOM   4790  C   TRP B 417       2.853 -86.592 -58.153  1.00 47.94           C  
ANISOU 4790  C   TRP B 417     6190   4695   7329      1    316    367       C  
ATOM   4791  O   TRP B 417       3.865 -86.677 -58.859  1.00 48.29           O  
ANISOU 4791  O   TRP B 417     6313   4699   7336     35    375    318       O  
ATOM   4792  CB  TRP B 417       2.556 -85.010 -56.191  1.00 39.08           C  
ANISOU 4792  CB  TRP B 417     4856   3759   6234      4    355    424       C  
ATOM   4793  CG  TRP B 417       3.939 -85.275 -55.684  1.00 40.22           C  
ANISOU 4793  CG  TRP B 417     4973   3929   6381     49    433    412       C  
ATOM   4794  CD1 TRP B 417       4.334 -86.337 -54.928  1.00 43.68           C  
ANISOU 4794  CD1 TRP B 417     5367   4365   6865     63    441    446       C  
ATOM   4795  CD2 TRP B 417       5.136 -84.567 -56.036  1.00 39.78           C  
ANISOU 4795  CD2 TRP B 417     4940   3889   6285     84    509    366       C  
ATOM   4796  NE1 TRP B 417       5.683 -86.250 -54.662  1.00 43.13           N  
ANISOU 4796  NE1 TRP B 417     5278   4319   6790    103    518    429       N  
ATOM   4797  CE2 TRP B 417       6.205 -85.188 -55.347  1.00 43.14           C  
ANISOU 4797  CE2 TRP B 417     5320   4330   6742    117    561    381       C  
ATOM   4798  CE3 TRP B 417       5.393 -83.381 -56.759  1.00 40.35           C  
ANISOU 4798  CE3 TRP B 417     5054   3974   6305     89    539    320       C  
ATOM   4799  CZ2 TRP B 417       7.513 -84.715 -55.412  1.00 42.16           C  
ANISOU 4799  CZ2 TRP B 417     5191   4226   6603    154    638    356       C  
ATOM   4800  CZ3 TRP B 417       6.689 -82.897 -56.803  1.00 41.39           C  
ANISOU 4800  CZ3 TRP B 417     5180   4128   6419    127    619    293       C  
ATOM   4801  CH2 TRP B 417       7.727 -83.543 -56.103  1.00 42.47           C  
ANISOU 4801  CH2 TRP B 417     5267   4277   6593    159    666    314       C  
ATOM   4802  N   GLN B 418       2.115 -87.665 -57.785  1.00 46.19           N  
ANISOU 4802  N   GLN B 418     5950   4439   7160    -24    249    414       N  
ATOM   4803  CA  GLN B 418       2.469 -89.040 -58.152  1.00 45.99           C  
ANISOU 4803  CA  GLN B 418     5998   4326   7151    -15    238    408       C  
ATOM   4804  C   GLN B 418       2.502 -89.311 -59.625  1.00 50.68           C  
ANISOU 4804  C   GLN B 418     6753   4810   7691    -22    215    355       C  
ATOM   4805  O   GLN B 418       3.319 -90.115 -60.039  1.00 49.00           O  
ANISOU 4805  O   GLN B 418     6617   4534   7468      8    254    327       O  
ATOM   4806  CB  GLN B 418       1.566 -90.057 -57.466  1.00 47.68           C  
ANISOU 4806  CB  GLN B 418     6157   4525   7434    -47    162    474       C  
ATOM   4807  CG  GLN B 418       1.946 -90.235 -56.012  1.00 68.42           C  
ANISOU 4807  CG  GLN B 418     8650   7238  10110    -24    206    521       C  
ATOM   4808  CD  GLN B 418       1.062 -91.199 -55.268  1.00 84.85           C  
ANISOU 4808  CD  GLN B 418    10667   9310  12261    -52    139    591       C  
ATOM   4809  OE1 GLN B 418      -0.143 -91.345 -55.540  1.00 79.90           O  
ANISOU 4809  OE1 GLN B 418    10052   8648  11659    -97     52    623       O  
ATOM   4810  NE2 GLN B 418       1.634 -91.826 -54.257  1.00 75.53           N  
ANISOU 4810  NE2 GLN B 418     9412   8165  11119    -27    177    623       N  
ATOM   4811  N   GLN B 419       1.713 -88.592 -60.452  1.00 50.43           N  
ANISOU 4811  N   GLN B 419     6784   4756   7623    -58    160    337       N  
ATOM   4812  CA  GLN B 419       1.764 -88.868 -61.889  1.00 50.65           C  
ANISOU 4812  CA  GLN B 419     6981   4672   7590    -65    135    284       C  
ATOM   4813  C   GLN B 419       2.862 -88.073 -62.642  1.00 54.65           C  
ANISOU 4813  C   GLN B 419     7560   5180   8024    -21    232    218       C  
ATOM   4814  O   GLN B 419       2.871 -88.085 -63.879  1.00 55.83           O  
ANISOU 4814  O   GLN B 419     7858   5243   8112    -26    218    171       O  
ATOM   4815  CB  GLN B 419       0.391 -88.776 -62.556  1.00 52.43           C  
ANISOU 4815  CB  GLN B 419     7264   4844   7813   -130     11    302       C  
ATOM   4816  CG  GLN B 419      -0.421 -87.503 -62.461  1.00 68.67           C  
ANISOU 4816  CG  GLN B 419     9255   6968   9869   -161    -21    320       C  
ATOM   4817  CD  GLN B 419      -1.902 -87.825 -62.303  1.00 74.28           C  
ANISOU 4817  CD  GLN B 419     9930   7654  10639   -224   -147    386       C  
ATOM   4818  OE1 GLN B 419      -2.325 -88.989 -62.257  1.00 64.91           O  
ANISOU 4818  OE1 GLN B 419     8768   6401   9493   -248   -214    418       O  
ATOM   4819  NE2 GLN B 419      -2.738 -86.818 -62.296  1.00 65.19           N  
ANISOU 4819  NE2 GLN B 419     8727   6545   9496   -255   -184    411       N  
ATOM   4820  N   GLY B 420       3.834 -87.512 -61.903  1.00 48.93           N  
ANISOU 4820  N   GLY B 420     6739   4542   7309     24    330    216       N  
ATOM   4821  CA  GLY B 420       5.034 -86.908 -62.462  1.00 48.12           C  
ANISOU 4821  CA  GLY B 420     6686   4442   7157     73    433    165       C  
ATOM   4822  C   GLY B 420       4.931 -85.565 -63.143  1.00 52.25           C  
ANISOU 4822  C   GLY B 420     7242   4990   7622     66    444    130       C  
ATOM   4823  O   GLY B 420       5.761 -85.252 -64.001  1.00 50.90           O  
ANISOU 4823  O   GLY B 420     7159   4783   7399    100    514     82       O  
ATOM   4824  N   ASN B 421       3.934 -84.751 -62.757  1.00 47.39           N  
ANISOU 4824  N   ASN B 421     6553   4434   7018     24    382    156       N  
ATOM   4825  CA  ASN B 421       3.777 -83.405 -63.282  1.00 43.33           C  
ANISOU 4825  CA  ASN B 421     6053   3953   6456     15    390    128       C  
ATOM   4826  C   ASN B 421       4.904 -82.552 -62.765  1.00 43.82           C  
ANISOU 4826  C   ASN B 421     6038   4097   6514     61    494    115       C  
ATOM   4827  O   ASN B 421       5.369 -82.758 -61.635  1.00 43.28           O  
ANISOU 4827  O   ASN B 421     5860   4090   6493     81    530    147       O  
ATOM   4828  CB  ASN B 421       2.435 -82.802 -62.862  1.00 43.17           C  
ANISOU 4828  CB  ASN B 421     5959   3980   6463    -37    304    169       C  
ATOM   4829  CG  ASN B 421       1.276 -83.446 -63.575  1.00 58.69           C  
ANISOU 4829  CG  ASN B 421     8010   5858   8432    -90    191    184       C  
ATOM   4830  OD1 ASN B 421       1.131 -83.342 -64.794  1.00 46.47           O  
ANISOU 4830  OD1 ASN B 421     6594   4236   6828   -106    160    145       O  
ATOM   4831  ND2 ASN B 421       0.452 -84.157 -62.860  1.00 57.20           N  
ANISOU 4831  ND2 ASN B 421     7754   5672   8308   -119    123    241       N  
ATOM   4832  N   VAL B 422       5.345 -81.579 -63.572  1.00 39.11           N  
ANISOU 4832  N   VAL B 422     5499   3500   5861     75    539     71       N  
ATOM   4833  CA  VAL B 422       6.442 -80.701 -63.161  1.00 37.81           C  
ANISOU 4833  CA  VAL B 422     5264   3407   5693    116    633     60       C  
ATOM   4834  C   VAL B 422       5.887 -79.417 -62.565  1.00 41.15           C  
ANISOU 4834  C   VAL B 422     5593   3923   6120     92    612     75       C  
ATOM   4835  O   VAL B 422       5.193 -78.680 -63.243  1.00 41.49           O  
ANISOU 4835  O   VAL B 422     5682   3957   6126     65    573     57       O  
ATOM   4836  CB  VAL B 422       7.429 -80.419 -64.331  1.00 38.84           C  
ANISOU 4836  CB  VAL B 422     5507   3484   5769    155    712      8       C  
ATOM   4837  CG1 VAL B 422       8.555 -79.506 -63.880  1.00 36.43           C  
ANISOU 4837  CG1 VAL B 422     5118   3252   5471    194    803      6       C  
ATOM   4838  CG2 VAL B 422       7.976 -81.724 -64.883  1.00 38.07           C  
ANISOU 4838  CG2 VAL B 422     5508   3289   5668    184    741     -4       C  
ATOM   4839  N   PHE B 423       6.210 -79.153 -61.302  1.00 36.32           N  
ANISOU 4839  N   PHE B 423     4854   3397   5549    104    639    108       N  
ATOM   4840  CA  PHE B 423       5.796 -77.963 -60.606  1.00 34.33           C  
ANISOU 4840  CA  PHE B 423     4512   3233   5299     88    630    123       C  
ATOM   4841  C   PHE B 423       6.998 -77.027 -60.540  1.00 38.39           C  
ANISOU 4841  C   PHE B 423     4999   3794   5795    124    713    100       C  
ATOM   4842  O   PHE B 423       8.122 -77.485 -60.423  1.00 37.61           O  
ANISOU 4842  O   PHE B 423     4894   3684   5711    160    773     98       O  
ATOM   4843  CB  PHE B 423       5.268 -78.331 -59.198  1.00 35.27           C  
ANISOU 4843  CB  PHE B 423     4519   3410   5472     75    599    179       C  
ATOM   4844  CG  PHE B 423       4.037 -79.182 -59.295  1.00 35.46           C  
ANISOU 4844  CG  PHE B 423     4564   3388   5522     38    515    209       C  
ATOM   4845  CD1 PHE B 423       2.792 -78.603 -59.489  1.00 36.13           C  
ANISOU 4845  CD1 PHE B 423     4645   3479   5604     -1    452    224       C  
ATOM   4846  CD2 PHE B 423       4.129 -80.577 -59.297  1.00 37.73           C  
ANISOU 4846  CD2 PHE B 423     4880   3617   5839     41    498    224       C  
ATOM   4847  CE1 PHE B 423       1.658 -79.391 -59.684  1.00 36.78           C  
ANISOU 4847  CE1 PHE B 423     4748   3509   5717    -38    368    258       C  
ATOM   4848  CE2 PHE B 423       3.005 -81.362 -59.499  1.00 40.48           C  
ANISOU 4848  CE2 PHE B 423     5257   3913   6213      4    413    251       C  
ATOM   4849  CZ  PHE B 423       1.761 -80.763 -59.651  1.00 39.01           C  
ANISOU 4849  CZ  PHE B 423     5059   3735   6029    -37    347    272       C  
ATOM   4850  N   SER B 424       6.764 -75.708 -60.662  1.00 35.35           N  
ANISOU 4850  N   SER B 424     4598   3454   5380    113    715     84       N  
ATOM   4851  CA  SER B 424       7.828 -74.717 -60.618  1.00 33.67           C  
ANISOU 4851  CA  SER B 424     4357   3284   5150    141    784     65       C  
ATOM   4852  C   SER B 424       7.464 -73.626 -59.640  1.00 36.89           C  
ANISOU 4852  C   SER B 424     4673   3781   5563    126    771     84       C  
ATOM   4853  O   SER B 424       6.346 -73.145 -59.633  1.00 32.43           O  
ANISOU 4853  O   SER B 424     4102   3231   4989     96    721     91       O  
ATOM   4854  CB  SER B 424       8.052 -74.068 -61.993  1.00 34.97           C  
ANISOU 4854  CB  SER B 424     4620   3406   5263    148    809     17       C  
ATOM   4855  OG  SER B 424       8.184 -75.043 -63.009  1.00 49.15           O  
ANISOU 4855  OG  SER B 424     6526   5108   7041    158    814     -4       O  
ATOM   4856  N   CYS B 425       8.470 -73.177 -58.912  1.00 37.96           N  
ANISOU 4856  N   CYS B 425     4743   3968   5711    150    820     92       N  
ATOM   4857  CA  CYS B 425       8.449 -72.066 -57.989  1.00 37.47           C  
ANISOU 4857  CA  CYS B 425     4604   3985   5646    143    821    104       C  
ATOM   4858  C   CYS B 425       9.151 -70.934 -58.786  1.00 39.98           C  
ANISOU 4858  C   CYS B 425     4954   4306   5930    156    865     67       C  
ATOM   4859  O   CYS B 425      10.268 -71.137 -59.271  1.00 37.79           O  
ANISOU 4859  O   CYS B 425     4699   4000   5658    185    918     55       O  
ATOM   4860  CB  CYS B 425       9.221 -72.429 -56.728  1.00 40.19           C  
ANISOU 4860  CB  CYS B 425     4869   4372   6028    158    840    140       C  
ATOM   4861  SG  CYS B 425       9.369 -71.062 -55.570  1.00 47.06           S  
ANISOU 4861  SG  CYS B 425     5663   5333   6885    151    842    153       S  
ATOM   4862  N   SER B 426       8.469 -69.777 -58.965  1.00 35.67           N  
ANISOU 4862  N   SER B 426     4411   3790   5352    136    845     51       N  
ATOM   4863  CA  SER B 426       8.954 -68.633 -59.721  1.00 34.39           C  
ANISOU 4863  CA  SER B 426     4278   3633   5157    144    878     17       C  
ATOM   4864  C   SER B 426       9.083 -67.424 -58.824  1.00 37.79           C  
ANISOU 4864  C   SER B 426     4639   4136   5582    139    882     26       C  
ATOM   4865  O   SER B 426       8.214 -67.156 -58.002  1.00 33.96           O  
ANISOU 4865  O   SER B 426     4114   3692   5099    120    846     46       O  
ATOM   4866  CB  SER B 426       8.030 -68.344 -60.889  1.00 36.85           C  
ANISOU 4866  CB  SER B 426     4668   3902   5431    123    848    -10       C  
ATOM   4867  OG  SER B 426       8.231 -69.375 -61.846  1.00 50.80           O  
ANISOU 4867  OG  SER B 426     6518   5591   7193    133    856    -25       O  
ATOM   4868  N   VAL B 427      10.216 -66.732 -58.926  1.00 37.36           N  
ANISOU 4868  N   VAL B 427     4572   4098   5526    158    927     14       N  
ATOM   4869  CA  VAL B 427      10.537 -65.600 -58.050  1.00 36.53           C  
ANISOU 4869  CA  VAL B 427     4407   4057   5416    154    930     22       C  
ATOM   4870  C   VAL B 427      10.825 -64.351 -58.878  1.00 39.19           C  
ANISOU 4870  C   VAL B 427     4772   4397   5723    155    953    -10       C  
ATOM   4871  O   VAL B 427      11.485 -64.431 -59.890  1.00 36.66           O  
ANISOU 4871  O   VAL B 427     4495   4035   5399    173    991    -29       O  
ATOM   4872  CB  VAL B 427      11.698 -65.996 -57.088  1.00 39.88           C  
ANISOU 4872  CB  VAL B 427     4770   4503   5879    170    949     54       C  
ATOM   4873  CG1 VAL B 427      11.990 -64.894 -56.076  1.00 39.78           C  
ANISOU 4873  CG1 VAL B 427     4704   4551   5859    161    939     65       C  
ATOM   4874  CG2 VAL B 427      11.363 -67.287 -56.347  1.00 39.03           C  
ANISOU 4874  CG2 VAL B 427     4640   4389   5801    168    926     86       C  
ATOM   4875  N   MET B 428      10.305 -63.201 -58.444  1.00 39.81           N  
ANISOU 4875  N   MET B 428     4827   4520   5778    138    933    -15       N  
ATOM   4876  CA  MET B 428      10.498 -61.890 -59.068  1.00 39.14           C  
ANISOU 4876  CA  MET B 428     4760   4446   5665    136    949    -42       C  
ATOM   4877  C   MET B 428      11.170 -61.009 -58.008  1.00 39.66           C  
ANISOU 4877  C   MET B 428     4766   4565   5736    136    952    -28       C  
ATOM   4878  O   MET B 428      10.711 -60.947 -56.876  1.00 37.43           O  
ANISOU 4878  O   MET B 428     4449   4321   5453    125    925     -8       O  
ATOM   4879  CB  MET B 428       9.160 -61.311 -59.560  1.00 43.23           C  
ANISOU 4879  CB  MET B 428     5311   4962   6151    114    918    -60       C  
ATOM   4880  CG  MET B 428       8.383 -62.252 -60.550  1.00 51.22           C  
ANISOU 4880  CG  MET B 428     6387   5915   7159    106    897    -68       C  
ATOM   4881  SD  MET B 428       7.143 -63.338 -59.741  1.00 61.67           S  
ANISOU 4881  SD  MET B 428     7685   7238   8507     88    845    -31       S  
ATOM   4882  CE  MET B 428       7.097 -64.721 -60.994  1.00 60.86           C  
ANISOU 4882  CE  MET B 428     7669   7048   8406     90    836    -43       C  
ATOM   4883  N   HIS B 429      12.295 -60.371 -58.361  1.00 37.54           N  
ANISOU 4883  N   HIS B 429     4491   4297   5475    149    985    -35       N  
ATOM   4884  CA  HIS B 429      13.078 -59.587 -57.419  1.00 37.36           C  
ANISOU 4884  CA  HIS B 429     4417   4316   5463    145    980    -18       C  
ATOM   4885  C   HIS B 429      14.012 -58.653 -58.177  1.00 42.18           C  
ANISOU 4885  C   HIS B 429     5031   4918   6076    154   1013    -31       C  
ATOM   4886  O   HIS B 429      14.379 -58.947 -59.317  1.00 41.50           O  
ANISOU 4886  O   HIS B 429     4981   4791   5997    172   1052    -44       O  
ATOM   4887  CB  HIS B 429      13.923 -60.552 -56.553  1.00 38.01           C  
ANISOU 4887  CB  HIS B 429     4453   4399   5589    155    980     21       C  
ATOM   4888  CG  HIS B 429      14.600 -59.909 -55.390  1.00 40.78           C  
ANISOU 4888  CG  HIS B 429     4755   4791   5950    144    957     46       C  
ATOM   4889  ND1 HIS B 429      15.914 -59.510 -55.458  1.00 41.84           N  
ANISOU 4889  ND1 HIS B 429     4858   4921   6119    152    974     63       N  
ATOM   4890  CD2 HIS B 429      14.102 -59.594 -54.169  1.00 42.21           C  
ANISOU 4890  CD2 HIS B 429     4919   5010   6108    127    918     57       C  
ATOM   4891  CE1 HIS B 429      16.170 -58.966 -54.278  1.00 41.61           C  
ANISOU 4891  CE1 HIS B 429     4796   4927   6085    133    935     84       C  
ATOM   4892  NE2 HIS B 429      15.081 -58.934 -53.500  1.00 41.61           N  
ANISOU 4892  NE2 HIS B 429     4811   4954   6044    119    903     77       N  
ATOM   4893  N   GLU B 430      14.447 -57.564 -57.542  1.00 41.86           N  
ANISOU 4893  N   GLU B 430     4959   4914   6032    143    998    -26       N  
ATOM   4894  CA  GLU B 430      15.381 -56.651 -58.222  1.00 43.93           C  
ANISOU 4894  CA  GLU B 430     5217   5168   6305    151   1027    -32       C  
ATOM   4895  C   GLU B 430      16.749 -57.284 -58.591  1.00 49.04           C  
ANISOU 4895  C   GLU B 430     5839   5784   7009    176   1070     -2       C  
ATOM   4896  O   GLU B 430      17.288 -56.947 -59.642  1.00 50.34           O  
ANISOU 4896  O   GLU B 430     6024   5922   7183    193   1115    -11       O  
ATOM   4897  CB  GLU B 430      15.579 -55.338 -57.456  1.00 45.65           C  
ANISOU 4897  CB  GLU B 430     5409   5427   6510    131    996    -29       C  
ATOM   4898  CG  GLU B 430      16.875 -55.171 -56.692  1.00 63.97           C  
ANISOU 4898  CG  GLU B 430     7675   7757   8874    128    984     10       C  
ATOM   4899  CD  GLU B 430      17.061 -53.750 -56.202  1.00 72.38           C  
ANISOU 4899  CD  GLU B 430     8731   8851   9920    107    953      5       C  
ATOM   4900  OE1 GLU B 430      17.990 -53.071 -56.697  1.00 66.81           O  
ANISOU 4900  OE1 GLU B 430     8007   8135   9243    110    969     14       O  
ATOM   4901  OE2 GLU B 430      16.244 -53.297 -55.367  1.00 51.74           O  
ANISOU 4901  OE2 GLU B 430     6132   6265   7262     90    916     -7       O  
ATOM   4902  N   ALA B 431      17.305 -58.177 -57.755  1.00 44.22           N  
ANISOU 4902  N   ALA B 431     5186   5175   6441    180   1061     36       N  
ATOM   4903  CA  ALA B 431      18.646 -58.734 -57.968  1.00 43.54           C  
ANISOU 4903  CA  ALA B 431     5063   5059   6420    204   1101     74       C  
ATOM   4904  C   ALA B 431      18.725 -59.995 -58.802  1.00 52.26           C  
ANISOU 4904  C   ALA B 431     6201   6113   7543    235   1152     74       C  
ATOM   4905  O   ALA B 431      19.661 -60.767 -58.617  1.00 55.98           O  
ANISOU 4905  O   ALA B 431     6634   6563   8073    254   1178    114       O  
ATOM   4906  CB  ALA B 431      19.299 -58.976 -56.625  1.00 44.01           C  
ANISOU 4906  CB  ALA B 431     5057   5143   6521    191   1061    122       C  
ATOM   4907  N   LEU B 432      17.784 -60.238 -59.713  1.00 47.86           N  
ANISOU 4907  N   LEU B 432     5715   5530   6938    239   1166     32       N  
ATOM   4908  CA  LEU B 432      17.830 -61.443 -60.536  1.00 46.54           C  
ANISOU 4908  CA  LEU B 432     5595   5307   6780    268   1211     29       C  
ATOM   4909  C   LEU B 432      17.972 -60.995 -61.964  1.00 52.24           C  
ANISOU 4909  C   LEU B 432     6382   5989   7477    288   1265      0       C  
ATOM   4910  O   LEU B 432      17.480 -59.909 -62.330  1.00 47.57           O  
ANISOU 4910  O   LEU B 432     5814   5417   6845    271   1249    -29       O  
ATOM   4911  CB  LEU B 432      16.546 -62.259 -60.394  1.00 45.43           C  
ANISOU 4911  CB  LEU B 432     5495   5160   6604    252   1171      8       C  
ATOM   4912  CG  LEU B 432      16.279 -62.927 -59.049  1.00 48.06           C  
ANISOU 4912  CG  LEU B 432     5776   5525   6959    237   1124     37       C  
ATOM   4913  CD1 LEU B 432      14.843 -63.345 -58.965  1.00 46.50           C  
ANISOU 4913  CD1 LEU B 432     5616   5329   6722    216   1080     16       C  
ATOM   4914  CD2 LEU B 432      17.186 -64.154 -58.840  1.00 47.83           C  
ANISOU 4914  CD2 LEU B 432     5720   5466   6989    263   1155     75       C  
ATOM   4915  N   HIS B 433      18.572 -61.880 -62.794  1.00 53.66           N  
ANISOU 4915  N   HIS B 433     6601   6110   7679    325   1330      7       N  
ATOM   4916  CA  HIS B 433      18.728 -61.656 -64.221  1.00 54.81           C  
ANISOU 4916  CA  HIS B 433     6826   6206   7794    350   1391    -19       C  
ATOM   4917  C   HIS B 433      17.353 -61.666 -64.819  1.00 55.61           C  
ANISOU 4917  C   HIS B 433     7013   6294   7821    327   1351    -69       C  
ATOM   4918  O   HIS B 433      16.618 -62.625 -64.612  1.00 54.38           O  
ANISOU 4918  O   HIS B 433     6884   6124   7654    317   1317    -75       O  
ATOM   4919  CB  HIS B 433      19.563 -62.772 -64.846  1.00 58.85           C  
ANISOU 4919  CB  HIS B 433     7369   6651   8340    398   1471      1       C  
ATOM   4920  CG  HIS B 433      19.789 -62.553 -66.302  1.00 64.41           C  
ANISOU 4920  CG  HIS B 433     8165   7300   9009    429   1543    -23       C  
ATOM   4921  ND1 HIS B 433      19.352 -63.463 -67.240  1.00 67.55           N  
ANISOU 4921  ND1 HIS B 433     8673   7629   9363    448   1571    -52       N  
ATOM   4922  CD2 HIS B 433      20.292 -61.468 -66.935  1.00 67.35           C  
ANISOU 4922  CD2 HIS B 433     8539   7676   9376    439   1582    -25       C  
ATOM   4923  CE1 HIS B 433      19.671 -62.938 -68.416  1.00 68.26           C  
ANISOU 4923  CE1 HIS B 433     8833   7681   9421    473   1633    -69       C  
ATOM   4924  NE2 HIS B 433      20.201 -61.719 -68.277  1.00 68.30           N  
ANISOU 4924  NE2 HIS B 433     8773   7730   9448    468   1641    -54       N  
ATOM   4925  N   ASN B 434      16.981 -60.574 -65.490  1.00 52.02           N  
ANISOU 4925  N   ASN B 434     6594   5848   7323    315   1347    -98       N  
ATOM   4926  CA  ASN B 434      15.642 -60.329 -66.035  1.00 52.08           C  
ANISOU 4926  CA  ASN B 434     6674   5850   7266    286   1298   -140       C  
ATOM   4927  C   ASN B 434      14.590 -60.272 -64.911  1.00 55.77           C  
ANISOU 4927  C   ASN B 434     7092   6368   7729    246   1216   -137       C  
ATOM   4928  O   ASN B 434      13.412 -60.495 -65.184  1.00 57.10           O  
ANISOU 4928  O   ASN B 434     7310   6525   7862    223   1170   -158       O  
ATOM   4929  CB  ASN B 434      15.227 -61.352 -67.096  1.00 57.52           C  
ANISOU 4929  CB  ASN B 434     7474   6465   7918    299   1315   -163       C  
ATOM   4930  CG  ASN B 434      16.238 -61.596 -68.199  1.00 86.30           C  
ANISOU 4930  CG  ASN B 434    11182  10047  11561    346   1407   -164       C  
ATOM   4931  OD1 ASN B 434      16.644 -62.742 -68.465  1.00 88.97           O  
ANISOU 4931  OD1 ASN B 434    11561  10333  11913    376   1449   -155       O  
ATOM   4932  ND2 ASN B 434      16.568 -60.554 -68.942  1.00 68.88           N  
ANISOU 4932  ND2 ASN B 434     8998   7840   9332    353   1442   -176       N  
ATOM   4933  N   HIS B 435      15.003 -59.973 -63.655  1.00 50.40           N  
ANISOU 4933  N   HIS B 435     6319   5743   7089    239   1197   -108       N  
ATOM   4934  CA  HIS B 435      14.100 -59.930 -62.490  1.00 50.86           C  
ANISOU 4934  CA  HIS B 435     6333   5849   7143    208   1131   -100       C  
ATOM   4935  C   HIS B 435      13.217 -61.182 -62.405  1.00 52.25           C  
ANISOU 4935  C   HIS B 435     6540   5999   7315    201   1101    -99       C  
ATOM   4936  O   HIS B 435      12.044 -61.096 -62.049  1.00 53.58           O  
ANISOU 4936  O   HIS B 435     6709   6187   7464    174   1049   -103       O  
ATOM   4937  CB  HIS B 435      13.262 -58.649 -62.523  1.00 51.53           C  
ANISOU 4937  CB  HIS B 435     6423   5969   7189    181   1096   -123       C  
ATOM   4938  CG  HIS B 435      14.094 -57.461 -62.870  1.00 55.14           C  
ANISOU 4938  CG  HIS B 435     6864   6439   7647    188   1128   -128       C  
ATOM   4939  ND1 HIS B 435      14.127 -56.963 -64.166  1.00 57.02           N  
ANISOU 4939  ND1 HIS B 435     7164   6645   7857    197   1160   -154       N  
ATOM   4940  CD2 HIS B 435      15.033 -56.830 -62.136  1.00 55.78           C  
ANISOU 4940  CD2 HIS B 435     6880   6554   7760    191   1134   -105       C  
ATOM   4941  CE1 HIS B 435      15.035 -56.015 -64.158  1.00 55.71           C  
ANISOU 4941  CE1 HIS B 435     6962   6497   7708    205   1186   -146       C  
ATOM   4942  NE2 HIS B 435      15.580 -55.871 -62.946  1.00 55.76           N  
ANISOU 4942  NE2 HIS B 435     6891   6543   7751    199   1168   -116       N  
ATOM   4943  N   TYR B 436      13.778 -62.329 -62.790  1.00 46.65           N  
ANISOU 4943  N   TYR B 436     5857   5241   6627    226   1136    -90       N  
ATOM   4944  CA  TYR B 436      13.036 -63.572 -62.855  1.00 44.96           C  
ANISOU 4944  CA  TYR B 436     5682   4991   6410    221   1109    -90       C  
ATOM   4945  C   TYR B 436      13.899 -64.810 -62.786  1.00 49.58           C  
ANISOU 4945  C   TYR B 436     6264   5538   7035    251   1149    -68       C  
ATOM   4946  O   TYR B 436      14.907 -64.913 -63.456  1.00 50.66           O  
ANISOU 4946  O   TYR B 436     6425   5639   7185    284   1214    -67       O  
ATOM   4947  CB  TYR B 436      12.222 -63.628 -64.150  1.00 43.70           C  
ANISOU 4947  CB  TYR B 436     5625   4778   6200    212   1099   -125       C  
ATOM   4948  CG  TYR B 436      11.345 -64.856 -64.236  1.00 42.38           C  
ANISOU 4948  CG  TYR B 436     5503   4569   6029    199   1057   -123       C  
ATOM   4949  CD1 TYR B 436      10.095 -64.892 -63.614  1.00 42.24           C  
ANISOU 4949  CD1 TYR B 436     5460   4578   6010    164    986   -113       C  
ATOM   4950  CD2 TYR B 436      11.825 -66.039 -64.794  1.00 41.99           C  
ANISOU 4950  CD2 TYR B 436     5513   4454   5986    225   1090   -125       C  
ATOM   4951  CE1 TYR B 436       9.318 -66.045 -63.626  1.00 41.21           C  
ANISOU 4951  CE1 TYR B 436     5361   4410   5887    150    943   -103       C  
ATOM   4952  CE2 TYR B 436      11.035 -67.177 -64.861  1.00 41.98           C  
ANISOU 4952  CE2 TYR B 436     5556   4411   5983    211   1046   -122       C  
ATOM   4953  CZ  TYR B 436       9.802 -67.195 -64.238  1.00 47.78           C  
ANISOU 4953  CZ  TYR B 436     6259   5175   6722    172    970   -109       C  
ATOM   4954  OH  TYR B 436       9.073 -68.364 -64.308  1.00 46.12           O  
ANISOU 4954  OH  TYR B 436     6088   4919   6518    157    925   -100       O  
ATOM   4955  N   THR B 437      13.456 -65.774 -62.003  1.00 46.00           N  
ANISOU 4955  N   THR B 437     5785   5089   6603    242   1113    -47       N  
ATOM   4956  CA  THR B 437      14.056 -67.082 -61.946  1.00 44.77           C  
ANISOU 4956  CA  THR B 437     5634   4891   6484    267   1143    -27       C  
ATOM   4957  C   THR B 437      13.012 -68.098 -61.529  1.00 44.86           C  
ANISOU 4957  C   THR B 437     5657   4892   6496    246   1086    -20       C  
ATOM   4958  O   THR B 437      12.097 -67.764 -60.779  1.00 41.62           O  
ANISOU 4958  O   THR B 437     5208   4526   6077    215   1029    -12       O  
ATOM   4959  CB  THR B 437      15.295 -67.129 -61.035  1.00 47.91           C  
ANISOU 4959  CB  THR B 437     5942   5319   6941    287   1174     15       C  
ATOM   4960  OG1 THR B 437      16.033 -68.318 -61.347  1.00 52.71           O  
ANISOU 4960  OG1 THR B 437     6570   5871   7585    321   1223     31       O  
ATOM   4961  CG2 THR B 437      14.948 -67.088 -59.577  1.00 47.81           C  
ANISOU 4961  CG2 THR B 437     5849   5369   6948    261   1118     43       C  
ATOM   4962  N   GLN B 438      13.179 -69.339 -61.982  1.00 42.07           N  
ANISOU 4962  N   GLN B 438     5355   4476   6155    265   1105    -18       N  
ATOM   4963  CA  GLN B 438      12.324 -70.425 -61.547  1.00 42.92           C  
ANISOU 4963  CA  GLN B 438     5467   4568   6273    247   1053     -4       C  
ATOM   4964  C   GLN B 438      13.122 -71.651 -61.173  1.00 46.27           C  
ANISOU 4964  C   GLN B 438     5870   4964   6746    275   1085     24       C  
ATOM   4965  O   GLN B 438      14.242 -71.801 -61.607  1.00 43.64           O  
ANISOU 4965  O   GLN B 438     5548   4601   6432    312   1154     27       O  
ATOM   4966  CB  GLN B 438      11.242 -70.757 -62.578  1.00 44.99           C  
ANISOU 4966  CB  GLN B 438     5831   4771   6490    227   1014    -34       C  
ATOM   4967  CG  GLN B 438      11.707 -71.200 -63.927  1.00 48.69           C  
ANISOU 4967  CG  GLN B 438     6414   5157   6931    254   1061    -64       C  
ATOM   4968  CD  GLN B 438      10.558 -71.734 -64.751  1.00 57.50           C  
ANISOU 4968  CD  GLN B 438     7631   6209   8006    226   1002    -86       C  
ATOM   4969  OE1 GLN B 438      10.511 -72.910 -65.136  1.00 60.76           O  
ANISOU 4969  OE1 GLN B 438     8112   6554   8420    235    999    -88       O  
ATOM   4970  NE2 GLN B 438       9.611 -70.893 -65.066  1.00 49.76           N  
ANISOU 4970  NE2 GLN B 438     6669   5246   6991    191    950   -101       N  
ATOM   4971  N   LYS B 439      12.574 -72.467 -60.270  1.00 43.58           N  
ANISOU 4971  N   LYS B 439     5488   4638   6432    258   1038     51       N  
ATOM   4972  CA  LYS B 439      13.135 -73.759 -59.875  1.00 42.99           C  
ANISOU 4972  CA  LYS B 439     5396   4533   6405    280   1057     80       C  
ATOM   4973  C   LYS B 439      11.995 -74.777 -59.932  1.00 45.13           C  
ANISOU 4973  C   LYS B 439     5709   4766   6670    257    998     81       C  
ATOM   4974  O   LYS B 439      10.898 -74.530 -59.415  1.00 43.49           O  
ANISOU 4974  O   LYS B 439     5475   4596   6454    221    934     89       O  
ATOM   4975  CB  LYS B 439      13.733 -73.726 -58.458  1.00 47.03           C  
ANISOU 4975  CB  LYS B 439     5794   5109   6968    280   1054    126       C  
ATOM   4976  CG  LYS B 439      15.048 -72.992 -58.371  1.00 63.80           C  
ANISOU 4976  CG  LYS B 439     7871   7255   9115    305   1110    138       C  
ATOM   4977  CD  LYS B 439      16.241 -73.855 -58.771  1.00 75.92           C  
ANISOU 4977  CD  LYS B 439     9414   8734  10698    349   1180    157       C  
ATOM   4978  CE  LYS B 439      17.542 -73.075 -58.728  1.00 87.82           C  
ANISOU 4978  CE  LYS B 439    10867  10261  12239    372   1235    178       C  
ATOM   4979  NZ  LYS B 439      17.517 -71.866 -59.604  1.00 99.90           N  
ANISOU 4979  NZ  LYS B 439    12440  11793  13723    371   1257    142       N  
ATOM   4980  N   SER B 440      12.279 -75.919 -60.536  1.00 42.41           N  
ANISOU 4980  N   SER B 440     5430   4348   6336    278   1022     76       N  
ATOM   4981  CA  SER B 440      11.346 -76.991 -60.755  1.00 41.73           C  
ANISOU 4981  CA  SER B 440     5399   4209   6246    259    969     76       C  
ATOM   4982  C   SER B 440      11.502 -78.125 -59.756  1.00 48.20           C  
ANISOU 4982  C   SER B 440     6157   5034   7123    264    957    119       C  
ATOM   4983  O   SER B 440      12.525 -78.253 -59.081  1.00 50.08           O  
ANISOU 4983  O   SER B 440     6326   5299   7405    290   1002    146       O  
ATOM   4984  CB  SER B 440      11.438 -77.478 -62.193  1.00 43.70           C  
ANISOU 4984  CB  SER B 440     5786   4361   6457    277    995     38       C  
ATOM   4985  OG  SER B 440      11.067 -76.406 -63.053  1.00 50.37           O  
ANISOU 4985  OG  SER B 440     6688   5206   7246    263    989      1       O  
ATOM   4986  N   LEU B 441      10.439 -78.908 -59.640  1.00 43.26           N  
ANISOU 4986  N   LEU B 441     5552   4384   6502    235    890    129       N  
ATOM   4987  CA  LEU B 441      10.293 -80.001 -58.692  1.00 44.17           C  
ANISOU 4987  CA  LEU B 441     5611   4504   6668    231    862    171       C  
ATOM   4988  C   LEU B 441       9.328 -81.006 -59.353  1.00 45.68           C  
ANISOU 4988  C   LEU B 441     5889   4616   6849    210    805    163       C  
ATOM   4989  O   LEU B 441       8.285 -80.615 -59.867  1.00 41.77           O  
ANISOU 4989  O   LEU B 441     5440   4109   6322    176    749    148       O  
ATOM   4990  CB  LEU B 441       9.666 -79.393 -57.406  1.00 45.74           C  
ANISOU 4990  CB  LEU B 441     5703   4795   6882    203    818    206       C  
ATOM   4991  CG  LEU B 441       9.446 -80.271 -56.197  1.00 51.11           C  
ANISOU 4991  CG  LEU B 441     6307   5502   7612    195    788    256       C  
ATOM   4992  CD1 LEU B 441      10.696 -80.709 -55.612  1.00 52.14           C  
ANISOU 4992  CD1 LEU B 441     6386   5642   7782    227    839    279       C  
ATOM   4993  CD2 LEU B 441       8.649 -79.542 -55.163  1.00 53.15           C  
ANISOU 4993  CD2 LEU B 441     6488   5838   7867    168    748    283       C  
ATOM   4994  N   SER B 442       9.716 -82.272 -59.385  1.00 46.05           N  
ANISOU 4994  N   SER B 442     5964   4606   6928    229    819    175       N  
ATOM   4995  CA  SER B 442       8.973 -83.376 -60.004  1.00 46.32           C  
ANISOU 4995  CA  SER B 442     6089   4554   6958    212    766    169       C  
ATOM   4996  C   SER B 442       9.192 -84.622 -59.162  1.00 52.47           C  
ANISOU 4996  C   SER B 442     6815   5325   7797    221    762    210       C  
ATOM   4997  O   SER B 442      10.223 -84.707 -58.490  1.00 51.47           O  
ANISOU 4997  O   SER B 442     6616   5233   7707    253    821    232       O  
ATOM   4998  CB  SER B 442       9.527 -83.635 -61.397  1.00 49.30           C  
ANISOU 4998  CB  SER B 442     6606   4837   7291    240    814    121       C  
ATOM   4999  OG  SER B 442       8.534 -84.243 -62.193  1.00 66.40           O  
ANISOU 4999  OG  SER B 442     8880   6923   9427    208    741    105       O  
ATOM   5000  N   LEU B 443       8.261 -85.590 -59.194  1.00 51.96           N  
ANISOU 5000  N   LEU B 443     6783   5211   7747    192    689    226       N  
ATOM   5001  CA  LEU B 443       8.477 -86.849 -58.465  1.00 53.80           C  
ANISOU 5001  CA  LEU B 443     6975   5429   8039    202    685    265       C  
ATOM   5002  C   LEU B 443       9.594 -87.583 -59.172  1.00 60.02           C  
ANISOU 5002  C   LEU B 443     7842   6138   8826    250    759    242       C  
ATOM   5003  O   LEU B 443       9.472 -87.868 -60.373  1.00 58.63           O  
ANISOU 5003  O   LEU B 443     7800   5872   8606    254    759    201       O  
ATOM   5004  CB  LEU B 443       7.235 -87.740 -58.398  1.00 54.75           C  
ANISOU 5004  CB  LEU B 443     7115   5507   8179    160    589    290       C  
ATOM   5005  CG  LEU B 443       7.386 -89.082 -57.646  1.00 60.95           C  
ANISOU 5005  CG  LEU B 443     7858   6273   9027    167    579    333       C  
ATOM   5006  CD1 LEU B 443       7.990 -88.896 -56.263  1.00 62.49           C  
ANISOU 5006  CD1 LEU B 443     7914   6563   9268    184    617    376       C  
ATOM   5007  CD2 LEU B 443       6.066 -89.725 -57.468  1.00 61.77           C  
ANISOU 5007  CD2 LEU B 443     7962   6353   9156    120    479    366       C  
ATOM   5008  N   SER B 444      10.727 -87.780 -58.436  1.00 58.54           N  
ANISOU 5008  N   SER B 444     7573   5985   8686    288    828    268       N  
ATOM   5009  CA  SER B 444      11.956 -88.434 -58.902  1.00 98.81           C  
ANISOU 5009  CA  SER B 444    12718  11022  13803    342    916    261       C  
ATOM   5010  C   SER B 444      11.707 -89.774 -59.626  1.00119.64           C  
ANISOU 5010  C   SER B 444    15472  13546  16439    349    901    247       C  
ATOM   5011  O   SER B 444      11.355 -90.775 -59.004  1.00 79.13           O  
ANISOU 5011  O   SER B 444    10307   8404  11354    336    858    281       O  
ATOM   5012  CB  SER B 444      12.906 -88.639 -57.723  1.00102.72           C  
ANISOU 5012  CB  SER B 444    13084  11577  14368    366    959    312       C  
ATOM   5013  OG  SER B 444      14.155 -89.168 -58.140  1.00115.88           O  
ANISOU 5013  OG  SER B 444    14778  13187  16063    422   1052    313       O  
TER    5014      SER B 444                                                      
ATOM   5015  N   GLU F   1      15.755  20.582  22.516  1.00111.78           N  
ANISOU 5015  N   GLU F   1    11587  18031  12855   3351  -5330  -7316       N  
ATOM   5016  CA  GLU F   1      15.565  19.581  21.458  1.00106.89           C  
ANISOU 5016  CA  GLU F   1    10973  17347  12292   3122  -4945  -6753       C  
ATOM   5017  C   GLU F   1      15.340  18.200  22.107  1.00107.32           C  
ANISOU 5017  C   GLU F   1    11133  17822  11822   3638  -4969  -6434       C  
ATOM   5018  O   GLU F   1      16.293  17.591  22.608  1.00110.99           O  
ANISOU 5018  O   GLU F   1    11367  18590  12212   3873  -5215  -6675       O  
ATOM   5019  CB  GLU F   1      16.772  19.586  20.490  1.00108.83           C  
ANISOU 5019  CB  GLU F   1    10826  17433  13091   2613  -4879  -6937       C  
ATOM   5020  CG  GLU F   1      16.396  19.406  19.032  1.00109.34           C  
ANISOU 5020  CG  GLU F   1    10968  17160  13415   2147  -4422  -6455       C  
ATOM   5021  CD  GLU F   1      15.806  18.060  18.668  1.00121.20           C  
ANISOU 5021  CD  GLU F   1    12634  18813  14604   2320  -4177  -5867       C  
ATOM   5022  OE1 GLU F   1      16.136  17.059  19.343  1.00122.14           O  
ANISOU 5022  OE1 GLU F   1    12692  19298  14417   2712  -4337  -5850       O  
ATOM   5023  OE2 GLU F   1      15.055  17.995  17.669  1.00103.26           O  
ANISOU 5023  OE2 GLU F   1    10552  16275  12407   2056  -3826  -5434       O  
ATOM   5024  N   ILE F   2      14.069  17.744  22.144  1.00 95.33           N  
ANISOU 5024  N   ILE F   2     9963  16320   9936   3827  -4717  -5906       N  
ATOM   5025  CA  ILE F   2      13.660  16.472  22.756  1.00 91.52           C  
ANISOU 5025  CA  ILE F   2     9652  16175   8945   4292  -4673  -5533       C  
ATOM   5026  C   ILE F   2      13.435  15.460  21.649  1.00 87.77           C  
ANISOU 5026  C   ILE F   2     9201  15567   8580   4013  -4311  -5005       C  
ATOM   5027  O   ILE F   2      12.814  15.802  20.650  1.00 84.57           O  
ANISOU 5027  O   ILE F   2     8868  14846   8418   3613  -4024  -4752       O  
ATOM   5028  CB  ILE F   2      12.396  16.668  23.646  1.00 93.49           C  
ANISOU 5028  CB  ILE F   2    10252  16564   8707   4704  -4640  -5338       C  
ATOM   5029  CG1 ILE F   2      12.765  17.492  24.874  1.00 98.03           C  
ANISOU 5029  CG1 ILE F   2    10808  17340   9098   5091  -5057  -5903       C  
ATOM   5030  CG2 ILE F   2      11.754  15.320  24.058  1.00 91.23           C  
ANISOU 5030  CG2 ILE F   2    10188  16537   7936   5074  -4457  -4811       C  
ATOM   5031  CD1 ILE F   2      11.611  17.958  25.759  1.00 96.08           C  
ANISOU 5031  CD1 ILE F   2    10881  17217   8409   5490  -5052  -5816       C  
ATOM   5032  N   VAL F   3      13.882  14.210  21.851  1.00 82.99           N  
ANISOU 5032  N   VAL F   3     8567  15198   7766   4261  -4334  -4838       N  
ATOM   5033  CA  VAL F   3      13.742  13.130  20.859  1.00 78.88           C  
ANISOU 5033  CA  VAL F   3     8085  14559   7325   4043  -4023  -4362       C  
ATOM   5034  C   VAL F   3      12.934  11.972  21.429  1.00 83.02           C  
ANISOU 5034  C   VAL F   3     8916  15272   7355   4435  -3890  -3889       C  
ATOM   5035  O   VAL F   3      12.965  11.729  22.634  1.00 84.73           O  
ANISOU 5035  O   VAL F   3     9243  15789   7160   4943  -4092  -3983       O  
ATOM   5036  CB  VAL F   3      15.094  12.672  20.252  1.00 83.01           C  
ANISOU 5036  CB  VAL F   3     8281  15095   8166   3864  -4107  -4571       C  
ATOM   5037  CG1 VAL F   3      15.743  13.804  19.475  1.00 83.90           C  
ANISOU 5037  CG1 VAL F   3     8103  14955   8821   3366  -4122  -4940       C  
ATOM   5038  CG2 VAL F   3      16.059  12.141  21.316  1.00 86.05           C  
ANISOU 5038  CG2 VAL F   3     8536  15866   8293   4360  -4468  -4891       C  
ATOM   5039  N   LEU F   4      12.176  11.292  20.549  1.00 78.97           N  
ANISOU 5039  N   LEU F   4     8553  14569   6885   4190  -3539  -3381       N  
ATOM   5040  CA  LEU F   4      11.267  10.199  20.894  1.00 77.90           C  
ANISOU 5040  CA  LEU F   4     8712  14527   6360   4434  -3332  -2872       C  
ATOM   5041  C   LEU F   4      11.612   8.899  20.169  1.00 82.20           C  
ANISOU 5041  C   LEU F   4     9273  14985   6975   4327  -3179  -2568       C  
ATOM   5042  O   LEU F   4      11.693   8.878  18.938  1.00 80.74           O  
ANISOU 5042  O   LEU F   4     8983  14545   7151   3892  -3012  -2478       O  
ATOM   5043  CB  LEU F   4       9.833  10.586  20.536  1.00 74.42           C  
ANISOU 5043  CB  LEU F   4     8445  13929   5903   4232  -3045  -2539       C  
ATOM   5044  CG  LEU F   4       9.337  11.933  21.062  1.00 79.37           C  
ANISOU 5044  CG  LEU F   4     9085  14581   6491   4298  -3152  -2805       C  
ATOM   5045  CD1 LEU F   4       7.926  12.220  20.559  1.00 75.50           C  
ANISOU 5045  CD1 LEU F   4     8744  13947   5995   4102  -2853  -2454       C  
ATOM   5046  CD2 LEU F   4       9.430  12.001  22.605  1.00 87.05           C  
ANISOU 5046  CD2 LEU F   4    10160  15903   7012   4873  -3398  -3003       C  
ATOM   5047  N   THR F   5      11.762   7.811  20.944  1.00 79.93           N  
ANISOU 5047  N   THR F   5     9155  14901   6314   4750  -3227  -2397       N  
ATOM   5048  CA  THR F   5      12.061   6.468  20.465  1.00 78.12           C  
ANISOU 5048  CA  THR F   5     9018  14599   6067   4756  -3103  -2096       C  
ATOM   5049  C   THR F   5      10.813   5.606  20.646  1.00 81.46           C  
ANISOU 5049  C   THR F   5     9788  14961   6203   4822  -2799  -1531       C  
ATOM   5050  O   THR F   5      10.309   5.514  21.765  1.00 82.78           O  
ANISOU 5050  O   THR F   5    10157  15332   5963   5209  -2812  -1425       O  
ATOM   5051  CB  THR F   5      13.215   5.867  21.293  1.00 84.67           C  
ANISOU 5051  CB  THR F   5     9813  15698   6659   5243  -3401  -2336       C  
ATOM   5052  OG1 THR F   5      14.369   6.704  21.163  1.00 82.45           O  
ANISOU 5052  OG1 THR F   5     9154  15502   6671   5160  -3691  -2898       O  
ATOM   5053  CG2 THR F   5      13.537   4.431  20.882  1.00 84.32           C  
ANISOU 5053  CG2 THR F   5     9914  15572   6552   5321  -3288  -2024       C  
ATOM   5054  N   GLN F   6      10.325   4.967  19.562  1.00 76.32           N  
ANISOU 5054  N   GLN F   6     9200  14038   5760   4449  -2523  -1180       N  
ATOM   5055  CA  GLN F   6       9.189   4.052  19.639  1.00 75.13           C  
ANISOU 5055  CA  GLN F   6     9345  13800   5401   4446  -2226   -655       C  
ATOM   5056  C   GLN F   6       9.644   2.601  19.563  1.00 82.66           C  
ANISOU 5056  C   GLN F   6    10487  14678   6243   4599  -2179   -411       C  
ATOM   5057  O   GLN F   6      10.693   2.298  18.979  1.00 81.41           O  
ANISOU 5057  O   GLN F   6    10195  14460   6279   4558  -2313   -601       O  
ATOM   5058  CB  GLN F   6       8.159   4.342  18.573  1.00 72.06           C  
ANISOU 5058  CB  GLN F   6     8921  13167   5290   3953  -1962   -434       C  
ATOM   5059  CG  GLN F   6       7.324   5.539  18.920  1.00 74.42           C  
ANISOU 5059  CG  GLN F   6     9163  13560   5554   3919  -1943   -530       C  
ATOM   5060  CD  GLN F   6       6.299   5.795  17.863  1.00 78.77           C  
ANISOU 5060  CD  GLN F   6     9681  13896   6351   3482  -1701   -319       C  
ATOM   5061  OE1 GLN F   6       6.490   6.629  16.975  1.00 68.10           O  
ANISOU 5061  OE1 GLN F   6     8159  12394   5322   3182  -1736   -525       O  
ATOM   5062  NE2 GLN F   6       5.230   5.024  17.890  1.00 73.03           N  
ANISOU 5062  NE2 GLN F   6     9119  13139   5489   3433  -1446    100       N  
ATOM   5063  N   SER F   7       8.863   1.709  20.199  1.00 82.86           N  
ANISOU 5063  N   SER F   7    10833  14708   5942   4794  -1981     10       N  
ATOM   5064  CA  SER F   7       9.180   0.287  20.266  1.00 85.37           C  
ANISOU 5064  CA  SER F   7    11416  14919   6103   4982  -1915    288       C  
ATOM   5065  C   SER F   7       7.910  -0.571  20.327  1.00 89.76           C  
ANISOU 5065  C   SER F   7    12273  15303   6530   4854  -1552    836       C  
ATOM   5066  O   SER F   7       6.943  -0.196  20.994  1.00 90.38           O  
ANISOU 5066  O   SER F   7    12418  15508   6416   4900  -1401    997       O  
ATOM   5067  CB  SER F   7      10.076  -0.001  21.469  1.00 95.45           C  
ANISOU 5067  CB  SER F   7    12813  16469   6984   5603  -2168    123       C  
ATOM   5068  OG  SER F   7      11.437   0.126  21.085  1.00109.71           O  
ANISOU 5068  OG  SER F   7    14370  18338   8978   5673  -2465   -296       O  
ATOM   5069  N   PRO F   8       7.910  -1.757  19.685  1.00 86.24           N  
ANISOU 5069  N   PRO F   8    12014  14574   6179   4708  -1404   1120       N  
ATOM   5070  CA  PRO F   8       8.939  -2.289  18.782  1.00 84.17           C  
ANISOU 5070  CA  PRO F   8    11688  14141   6151   4632  -1540    968       C  
ATOM   5071  C   PRO F   8       8.740  -1.591  17.442  1.00 79.13           C  
ANISOU 5071  C   PRO F   8    10752  13346   5967   4096  -1499    820       C  
ATOM   5072  O   PRO F   8       7.681  -1.018  17.242  1.00 74.52           O  
ANISOU 5072  O   PRO F   8    10104  12733   5476   3807  -1331    936       O  
ATOM   5073  CB  PRO F   8       8.590  -3.775  18.720  1.00 87.74           C  
ANISOU 5073  CB  PRO F   8    12526  14319   6491   4654  -1326   1412       C  
ATOM   5074  CG  PRO F   8       7.094  -3.789  18.782  1.00 92.36           C  
ANISOU 5074  CG  PRO F   8    13209  14807   7078   4355  -1001   1779       C  
ATOM   5075  CD  PRO F   8       6.701  -2.605  19.658  1.00 88.88           C  
ANISOU 5075  CD  PRO F   8    12611  14702   6458   4509  -1049   1626       C  
ATOM   5076  N   ALA F   9       9.736  -1.590  16.555  1.00 74.48           N  
ANISOU 5076  N   ALA F   9     9983  12680   5638   3990  -1644    564       N  
ATOM   5077  CA  ALA F   9       9.578  -0.938  15.253  1.00 71.69           C  
ANISOU 5077  CA  ALA F   9     9382  12171   5687   3509  -1585    442       C  
ATOM   5078  C   ALA F   9       8.415  -1.547  14.479  1.00 75.13           C  
ANISOU 5078  C   ALA F   9     9976  12323   6246   3142  -1310    816       C  
ATOM   5079  O   ALA F   9       7.715  -0.853  13.730  1.00 72.48           O  
ANISOU 5079  O   ALA F   9     9493  11912   6135   2778  -1210    808       O  
ATOM   5080  CB  ALA F   9      10.855  -1.086  14.437  1.00 72.27           C  
ANISOU 5080  CB  ALA F   9     9279  12201   5980   3488  -1737    170       C  
ATOM   5081  N   THR F  10       8.233  -2.859  14.639  1.00 73.87           N  
ANISOU 5081  N   THR F  10    10126  11997   5945   3245  -1200   1129       N  
ATOM   5082  CA  THR F  10       7.184  -3.591  13.943  1.00 72.78           C  
ANISOU 5082  CA  THR F  10    10147  11569   5937   2897   -957   1467       C  
ATOM   5083  C   THR F  10       6.549  -4.581  14.919  1.00 79.10           C  
ANISOU 5083  C   THR F  10    11296  12312   6447   3085   -786   1854       C  
ATOM   5084  O   THR F  10       7.255  -5.259  15.665  1.00 80.55           O  
ANISOU 5084  O   THR F  10    11700  12531   6373   3488   -870   1894       O  
ATOM   5085  CB  THR F  10       7.767  -4.205  12.650  1.00 76.97           C  
ANISOU 5085  CB  THR F  10    10676  11842   6729   2704   -990   1402       C  
ATOM   5086  OG1 THR F  10       6.711  -4.779  11.889  1.00 76.34           O  
ANISOU 5086  OG1 THR F  10    10711  11487   6808   2333   -787   1669       O  
ATOM   5087  CG2 THR F  10       8.863  -5.241  12.917  1.00 83.63           C  
ANISOU 5087  CG2 THR F  10    11724  12630   7421   3070  -1114   1388       C  
ATOM   5088  N   LEU F  11       5.213  -4.602  14.951  1.00 76.00           N  
ANISOU 5088  N   LEU F  11    10940  11854   6082   2811   -543   2131       N  
ATOM   5089  CA  LEU F  11       4.422  -5.445  15.847  1.00 78.39           C  
ANISOU 5089  CA  LEU F  11    11544  12098   6141   2908   -309   2535       C  
ATOM   5090  C   LEU F  11       3.509  -6.309  14.969  1.00 81.94           C  
ANISOU 5090  C   LEU F  11    12093  12198   6840   2459    -87   2810       C  
ATOM   5091  O   LEU F  11       2.763  -5.788  14.144  1.00 78.52           O  
ANISOU 5091  O   LEU F  11    11423  11740   6669   2069    -29   2757       O  
ATOM   5092  CB  LEU F  11       3.622  -4.533  16.781  1.00 78.75           C  
ANISOU 5092  CB  LEU F  11    11473  12458   5992   2997   -216   2572       C  
ATOM   5093  CG  LEU F  11       2.909  -5.172  17.951  1.00 86.79           C  
ANISOU 5093  CG  LEU F  11    12773  13522   6680   3192     35   2963       C  
ATOM   5094  CD1 LEU F  11       3.860  -5.979  18.821  1.00 88.76           C  
ANISOU 5094  CD1 LEU F  11    13367  13765   6592   3697    -54   3038       C  
ATOM   5095  CD2 LEU F  11       2.216  -4.107  18.788  1.00 88.95           C  
ANISOU 5095  CD2 LEU F  11    12881  14155   6762   3312     96   2928       C  
ATOM   5096  N   SER F  12       3.656  -7.627  15.085  1.00 81.58           N  
ANISOU 5096  N   SER F  12    12406  11869   6723   2530      8   3069       N  
ATOM   5097  CA  SER F  12       2.960  -8.619  14.269  1.00 81.66           C  
ANISOU 5097  CA  SER F  12    12560  11488   6977   2128    183   3301       C  
ATOM   5098  C   SER F  12       1.974  -9.386  15.157  1.00 88.45           C  
ANISOU 5098  C   SER F  12    13689  12243   7675   2086    505   3744       C  
ATOM   5099  O   SER F  12       2.392 -10.126  16.047  1.00 90.95           O  
ANISOU 5099  O   SER F  12    14363  12493   7700   2442    559   3948       O  
ATOM   5100  CB  SER F  12       3.978  -9.559  13.631  1.00 85.33           C  
ANISOU 5100  CB  SER F  12    13252  11659   7512   2239     34   3227       C  
ATOM   5101  OG  SER F  12       3.347 -10.370  12.659  1.00 97.15           O  
ANISOU 5101  OG  SER F  12    14847  12774   9291   1823    151   3363       O  
ATOM   5102  N   LEU F  13       0.668  -9.151  14.942  1.00 84.77           N  
ANISOU 5102  N   LEU F  13    13034  11792   7383   1672    723   3887       N  
ATOM   5103  CA  LEU F  13      -0.420  -9.692  15.745  1.00 88.17           C  
ANISOU 5103  CA  LEU F  13    13617  12181   7703   1557   1074   4296       C  
ATOM   5104  C   LEU F  13      -1.599 -10.151  14.911  1.00 93.45           C  
ANISOU 5104  C   LEU F  13    14168  12606   8732    970   1273   4441       C  
ATOM   5105  O   LEU F  13      -1.744  -9.738  13.780  1.00 91.02           O  
ANISOU 5105  O   LEU F  13    13589  12271   8722    678   1128   4193       O  
ATOM   5106  CB  LEU F  13      -0.908  -8.581  16.685  1.00 88.20           C  
ANISOU 5106  CB  LEU F  13    13395  12647   7469   1744   1145   4278       C  
ATOM   5107  CG  LEU F  13       0.086  -8.072  17.722  1.00 93.56           C  
ANISOU 5107  CG  LEU F  13    14180  13617   7750   2342    965   4142       C  
ATOM   5108  CD1 LEU F  13      -0.415  -6.785  18.349  1.00 92.91           C  
ANISOU 5108  CD1 LEU F  13    13808  13980   7514   2463    973   4018       C  
ATOM   5109  CD2 LEU F  13       0.375  -9.148  18.791  1.00100.51           C  
ANISOU 5109  CD2 LEU F  13    15545  14367   8277   2704   1124   4491       C  
ATOM   5110  N   SER F  14      -2.473 -10.968  15.488  1.00 95.56           N  
ANISOU 5110  N   SER F  14    14625  12714   8967    799   1614   4837       N  
ATOM   5111  CA  SER F  14      -3.670 -11.483  14.819  1.00 96.27           C  
ANISOU 5111  CA  SER F  14    14586  12579   9413    216   1828   4984       C  
ATOM   5112  C   SER F  14      -4.876 -10.614  15.214  1.00100.80           C  
ANISOU 5112  C   SER F  14    14767  13545   9986     43   2030   5040       C  
ATOM   5113  O   SER F  14      -4.924 -10.166  16.360  1.00101.05           O  
ANISOU 5113  O   SER F  14    14831  13887   9678    374   2158   5171       O  
ATOM   5114  CB  SER F  14      -3.934 -12.923  15.269  1.00103.26           C  
ANISOU 5114  CB  SER F  14    15911  13036  10288     98   2122   5403       C  
ATOM   5115  OG  SER F  14      -2.741 -13.686  15.360  1.00105.78           O  
ANISOU 5115  OG  SER F  14    16680  13064  10449    448   1971   5417       O  
ATOM   5116  N   PRO F  15      -5.883 -10.408  14.332  1.00 98.20           N  
ANISOU 5116  N   PRO F  15    14080  13224  10009   -442   2069   4949       N  
ATOM   5117  CA  PRO F  15      -7.069  -9.627  14.744  1.00 99.33           C  
ANISOU 5117  CA  PRO F  15    13840  13765  10138   -577   2272   5006       C  
ATOM   5118  C   PRO F  15      -7.784 -10.279  15.938  1.00110.01           C  
ANISOU 5118  C   PRO F  15    15357  15131  11311   -595   2712   5462       C  
ATOM   5119  O   PRO F  15      -8.202 -11.432  15.847  1.00113.76           O  
ANISOU 5119  O   PRO F  15    16018  15232  11972   -932   2943   5729       O  
ATOM   5120  CB  PRO F  15      -7.940  -9.593  13.483  1.00100.24           C  
ANISOU 5120  CB  PRO F  15    13601  13800  10685  -1098   2215   4833       C  
ATOM   5121  CG  PRO F  15      -7.426 -10.678  12.610  1.00104.79           C  
ANISOU 5121  CG  PRO F  15    14450  13864  11501  -1306   2094   4807       C  
ATOM   5122  CD  PRO F  15      -5.981 -10.842  12.924  1.00 98.58           C  
ANISOU 5122  CD  PRO F  15    14046  12954  10457   -843   1906   4761       C  
ATOM   5123  N   GLY F  16      -7.848  -9.547  17.052  1.00106.63           N  
ANISOU 5123  N   GLY F  16    14890  15111  10511   -213   2821   5542       N  
ATOM   5124  CA  GLY F  16      -8.397  -9.996  18.321  1.00111.14           C  
ANISOU 5124  CA  GLY F  16    15644  15773  10810   -105   3242   5973       C  
ATOM   5125  C   GLY F  16      -7.398  -9.785  19.445  1.00115.56           C  
ANISOU 5125  C   GLY F  16    16556  16488  10865    550   3172   6026       C  
ATOM   5126  O   GLY F  16      -7.785  -9.584  20.600  1.00118.33           O  
ANISOU 5126  O   GLY F  16    16965  17126  10869    815   3438   6266       O  
ATOM   5127  N   GLU F  17      -6.094  -9.839  19.114  1.00109.32           N  
ANISOU 5127  N   GLU F  17    15994  15526  10016    836   2808   5789       N  
ATOM   5128  CA  GLU F  17      -5.010  -9.639  20.082  1.00109.23           C  
ANISOU 5128  CA  GLU F  17    16291  15668   9546   1482   2660   5760       C  
ATOM   5129  C   GLU F  17      -4.884  -8.176  20.528  1.00109.62           C  
ANISOU 5129  C   GLU F  17    16042  16242   9367   1829   2465   5454       C  
ATOM   5130  O   GLU F  17      -5.420  -7.260  19.894  1.00105.22           O  
ANISOU 5130  O   GLU F  17    15060  15885   9035   1591   2369   5204       O  
ATOM   5131  CB  GLU F  17      -3.652 -10.074  19.482  1.00108.40           C  
ANISOU 5131  CB  GLU F  17    16433  15260   9494   1660   2302   5537       C  
ATOM   5132  CG  GLU F  17      -3.510 -11.560  19.212  1.00120.83           C  
ANISOU 5132  CG  GLU F  17    18422  16291  11196   1477   2444   5823       C  
ATOM   5133  CD  GLU F  17      -2.067 -11.999  19.052  1.00132.33           C  
ANISOU 5133  CD  GLU F  17    20204  17542  12532   1864   2125   5657       C  
ATOM   5134  OE1 GLU F  17      -1.374 -12.152  20.085  1.00133.81           O  
ANISOU 5134  OE1 GLU F  17    20715  17833  12292   2412   2106   5762       O  
ATOM   5135  OE2 GLU F  17      -1.618 -12.157  17.894  1.00111.34           O  
ANISOU 5135  OE2 GLU F  17    17462  14651  10190   1649   1883   5402       O  
ATOM   5136  N   ARG F  18      -4.110  -7.974  21.601  1.00107.59           N  
ANISOU 5136  N   ARG F  18    16037  16185   8655   2421   2377   5451       N  
ATOM   5137  CA  ARG F  18      -3.805  -6.663  22.155  1.00105.69           C  
ANISOU 5137  CA  ARG F  18    15596  16405   8157   2825   2152   5136       C  
ATOM   5138  C   ARG F  18      -2.501  -6.148  21.558  1.00105.95           C  
ANISOU 5138  C   ARG F  18    15571  16407   8278   3009   1671   4672       C  
ATOM   5139  O   ARG F  18      -1.579  -6.933  21.317  1.00106.38           O  
ANISOU 5139  O   ARG F  18    15894  16179   8347   3113   1531   4668       O  
ATOM   5140  CB  ARG F  18      -3.654  -6.759  23.670  1.00110.01           C  
ANISOU 5140  CB  ARG F  18    16457  17198   8145   3393   2303   5362       C  
ATOM   5141  CG  ARG F  18      -3.472  -5.427  24.396  1.00116.53           C  
ANISOU 5141  CG  ARG F  18    17097  18515   8662   3834   2101   5054       C  
ATOM   5142  CD  ARG F  18      -3.778  -5.643  25.865  1.00121.20           C  
ANISOU 5142  CD  ARG F  18    17981  19359   8713   4298   2385   5385       C  
ATOM   5143  NE  ARG F  18      -3.432  -4.521  26.742  1.00130.64           N  
ANISOU 5143  NE  ARG F  18    19110  21008   9520   4845   2160   5090       N  
ATOM   5144  CZ  ARG F  18      -2.362  -4.437  27.541  1.00153.15           C  
ANISOU 5144  CZ  ARG F  18    22225  23992  11973   5452   1890   4926       C  
ATOM   5145  NH1 ARG F  18      -1.454  -5.412  27.564  1.00144.34           N  
ANISOU 5145  NH1 ARG F  18    21464  22597  10780   5628   1796   5025       N  
ATOM   5146  NH2 ARG F  18      -2.178  -3.365  28.303  1.00141.74           N  
ANISOU 5146  NH2 ARG F  18    20684  22962  10206   5904   1687   4631       N  
ATOM   5147  N   ALA F  19      -2.419  -4.827  21.351  1.00 97.80           N  
ANISOU 5147  N   ALA F  19    14196  15667   7295   3064   1431   4285       N  
ATOM   5148  CA  ALA F  19      -1.225  -4.160  20.845  1.00 92.88           C  
ANISOU 5148  CA  ALA F  19    13463  15060   6768   3217   1003   3825       C  
ATOM   5149  C   ALA F  19      -0.809  -3.111  21.868  1.00 95.91           C  
ANISOU 5149  C   ALA F  19    13801  15846   6793   3721    819   3578       C  
ATOM   5150  O   ALA F  19      -1.597  -2.213  22.152  1.00 97.31           O  
ANISOU 5150  O   ALA F  19    13764  16294   6914   3712    896   3524       O  
ATOM   5151  CB  ALA F  19      -1.527  -3.493  19.515  1.00 88.82           C  
ANISOU 5151  CB  ALA F  19    12586  14466   6695   2763    887   3570       C  
ATOM   5152  N   THR F  20       0.391  -3.239  22.456  1.00 89.92           N  
ANISOU 5152  N   THR F  20    13245  15141   5781   4183    571   3419       N  
ATOM   5153  CA  THR F  20       0.895  -2.253  23.410  1.00 90.18           C  
ANISOU 5153  CA  THR F  20    13233  15549   5483   4678    338   3121       C  
ATOM   5154  C   THR F  20       2.109  -1.634  22.765  1.00 90.06           C  
ANISOU 5154  C   THR F  20    13023  15507   5687   4699    -81   2624       C  
ATOM   5155  O   THR F  20       3.120  -2.324  22.614  1.00 91.03           O  
ANISOU 5155  O   THR F  20    13295  15484   5808   4848   -245   2563       O  
ATOM   5156  CB  THR F  20       1.211  -2.886  24.774  1.00102.21           C  
ANISOU 5156  CB  THR F  20    15144  17218   6474   5253    404   3341       C  
ATOM   5157  OG1 THR F  20       2.139  -3.959  24.612  1.00111.24           O  
ANISOU 5157  OG1 THR F  20    16562  18100   7605   5377    312   3419       O  
ATOM   5158  CG2 THR F  20      -0.015  -3.395  25.456  1.00 97.83           C  
ANISOU 5158  CG2 THR F  20    14764  16717   5689   5231    861   3838       C  
ATOM   5159  N   LEU F  21       1.992  -0.370  22.308  1.00 82.47           N  
ANISOU 5159  N   LEU F  21    11729  14665   4942   4526   -235   2281       N  
ATOM   5160  CA  LEU F  21       3.088   0.336  21.633  1.00 79.13           C  
ANISOU 5160  CA  LEU F  21    11088  14203   4774   4479   -593   1809       C  
ATOM   5161  C   LEU F  21       3.734   1.240  22.655  1.00 83.69           C  
ANISOU 5161  C   LEU F  21    11629  15105   5064   4955   -871   1453       C  
ATOM   5162  O   LEU F  21       3.023   1.829  23.454  1.00 84.90           O  
ANISOU 5162  O   LEU F  21    11798  15501   4959   5152   -786   1493       O  
ATOM   5163  CB  LEU F  21       2.586   1.184  20.453  1.00 75.03           C  
ANISOU 5163  CB  LEU F  21    10264  13568   4675   3993   -586   1651       C  
ATOM   5164  CG  LEU F  21       1.461   0.650  19.573  1.00 77.10           C  
ANISOU 5164  CG  LEU F  21    10497  13614   5183   3520   -286   1982       C  
ATOM   5165  CD1 LEU F  21       1.421   1.428  18.300  1.00 73.10           C  
ANISOU 5165  CD1 LEU F  21     9725  12973   5078   3131   -381   1742       C  
ATOM   5166  CD2 LEU F  21       1.596  -0.826  19.273  1.00 79.58           C  
ANISOU 5166  CD2 LEU F  21    11044  13652   5539   3409   -143   2298       C  
ATOM   5167  N   SER F  22       5.064   1.354  22.641  1.00 79.19           N  
ANISOU 5167  N   SER F  22    11000  14558   4531   5154  -1204   1092       N  
ATOM   5168  CA  SER F  22       5.783   2.152  23.633  1.00 80.35           C  
ANISOU 5168  CA  SER F  22    11099  15015   4416   5620  -1517    700       C  
ATOM   5169  C   SER F  22       6.418   3.379  23.013  1.00 80.79           C  
ANISOU 5169  C   SER F  22    10810  15066   4820   5414  -1797    187       C  
ATOM   5170  O   SER F  22       6.887   3.315  21.885  1.00 74.36           O  
ANISOU 5170  O   SER F  22     9833  14020   4399   5046  -1831     91       O  
ATOM   5171  CB  SER F  22       6.874   1.313  24.301  1.00 84.10           C  
ANISOU 5171  CB  SER F  22    11771  15575   4607   6093  -1710    654       C  
ATOM   5172  OG  SER F  22       6.568  -0.071  24.251  1.00 92.41           O  
ANISOU 5172  OG  SER F  22    13134  16432   5543   6091  -1443   1137       O  
ATOM   5173  N   CYS F  23       6.532   4.461  23.796  1.00 81.32           N  
ANISOU 5173  N   CYS F  23    10787  15385   4726   5684  -2009   -158       N  
ATOM   5174  CA  CYS F  23       7.226   5.673  23.364  1.00 80.24           C  
ANISOU 5174  CA  CYS F  23    10350  15234   4904   5522  -2293   -679       C  
ATOM   5175  C   CYS F  23       8.026   6.218  24.534  1.00 83.55           C  
ANISOU 5175  C   CYS F  23    10753  15959   5031   6037  -2649  -1099       C  
ATOM   5176  O   CYS F  23       7.487   6.393  25.617  1.00 82.53           O  
ANISOU 5176  O   CYS F  23    10798  16073   4487   6431  -2634  -1036       O  
ATOM   5177  CB  CYS F  23       6.279   6.726  22.797  1.00 78.68           C  
ANISOU 5177  CB  CYS F  23    10021  14936   4936   5167  -2162   -702       C  
ATOM   5178  SG  CYS F  23       7.108   8.292  22.412  1.00 81.97           S  
ANISOU 5178  SG  CYS F  23    10136  15299   5711   4997  -2492  -1334       S  
ATOM   5179  N   ARG F  24       9.313   6.473  24.297  1.00 82.84           N  
ANISOU 5179  N   ARG F  24    10444  15872   5159   6036  -2966  -1536       N  
ATOM   5180  CA  ARG F  24      10.262   6.940  25.301  1.00 86.97           C  
ANISOU 5180  CA  ARG F  24    10891  16685   5470   6497  -3366  -2016       C  
ATOM   5181  C   ARG F  24      10.815   8.294  24.879  1.00 91.50           C  
ANISOU 5181  C   ARG F  24    11128  17191   6445   6214  -3607  -2557       C  
ATOM   5182  O   ARG F  24      11.367   8.401  23.783  1.00 89.47           O  
ANISOU 5182  O   ARG F  24    10640  16706   6647   5772  -3593  -2666       O  
ATOM   5183  CB  ARG F  24      11.407   5.920  25.464  1.00 88.28           C  
ANISOU 5183  CB  ARG F  24    11069  16939   5533   6782  -3544  -2074       C  
ATOM   5184  CG  ARG F  24      11.013   4.697  26.292  1.00101.78           C  
ANISOU 5184  CG  ARG F  24    13181  18771   6722   7245  -3388  -1623       C  
ATOM   5185  CD  ARG F  24      12.204   4.016  26.937  1.00121.60           C  
ANISOU 5185  CD  ARG F  24    15737  21497   8969   7769  -3694  -1829       C  
ATOM   5186  NE  ARG F  24      11.815   3.238  28.118  1.00142.12           N  
ANISOU 5186  NE  ARG F  24    18757  24292  10949   8364  -3614  -1501       N  
ATOM   5187  CZ  ARG F  24      12.664   2.636  28.954  1.00161.41           C  
ANISOU 5187  CZ  ARG F  24    21346  26976  13005   8974  -3871  -1626       C  
ATOM   5188  NH1 ARG F  24      13.977   2.706  28.750  1.00151.27           N  
ANISOU 5188  NH1 ARG F  24    19775  25795  11904   9071  -4248  -2101       N  
ATOM   5189  NH2 ARG F  24      12.205   1.959  30.001  1.00150.28           N  
ANISOU 5189  NH2 ARG F  24    20367  25716  11014   9506  -3746  -1275       N  
ATOM   5190  N   ALA F  25      10.716   9.304  25.768  1.00 90.09           N  
ANISOU 5190  N   ALA F  25    10938  17206   6087   6483  -3828  -2904       N  
ATOM   5191  CA  ALA F  25      11.193  10.671  25.520  1.00 89.41           C  
ANISOU 5191  CA  ALA F  25    10576  17035   6359   6243  -4070  -3444       C  
ATOM   5192  C   ALA F  25      12.566  10.869  26.208  1.00 92.90           C  
ANISOU 5192  C   ALA F  25    10813  17717   6769   6566  -4533  -4023       C  
ATOM   5193  O   ALA F  25      12.747  10.392  27.326  1.00 93.45           O  
ANISOU 5193  O   ALA F  25    11042  18104   6362   7149  -4708  -4059       O  
ATOM   5194  CB  ALA F  25      10.183  11.681  26.069  1.00 90.81           C  
ANISOU 5194  CB  ALA F  25    10885  17258   6361   6350  -4039  -3490       C  
ATOM   5195  N   SER F  26      13.526  11.552  25.532  1.00 89.20           N  
ANISOU 5195  N   SER F  26     9987  17104   6802   6194  -4718  -4467       N  
ATOM   5196  CA  SER F  26      14.860  11.813  26.090  1.00 93.51           C  
ANISOU 5196  CA  SER F  26    10254  17878   7396   6430  -5168  -5074       C  
ATOM   5197  C   SER F  26      14.798  12.648  27.369  1.00101.83           C  
ANISOU 5197  C   SER F  26    11374  19186   8131   6883  -5505  -5494       C  
ATOM   5198  O   SER F  26      15.580  12.392  28.284  1.00106.04           O  
ANISOU 5198  O   SER F  26    11849  20051   8391   7375  -5863  -5829       O  
ATOM   5199  CB  SER F  26      15.781  12.463  25.059  1.00 96.13           C  
ANISOU 5199  CB  SER F  26    10172  17981   8371   5867  -5235  -5442       C  
ATOM   5200  OG  SER F  26      15.265  13.673  24.533  1.00101.69           O  
ANISOU 5200  OG  SER F  26    10842  18381   9414   5424  -5125  -5545       O  
ATOM   5201  N   LYS F  27      13.856  13.617  27.450  1.00 96.84           N  
ANISOU 5201  N   LYS F  27    10880  18412   7502   6763  -5404  -5483       N  
ATOM   5202  CA  LYS F  27      13.625  14.427  28.659  1.00 99.19           C  
ANISOU 5202  CA  LYS F  27    11300  18934   7455   7217  -5691  -5843       C  
ATOM   5203  C   LYS F  27      12.136  14.323  29.005  1.00101.23           C  
ANISOU 5203  C   LYS F  27    11941  19215   7307   7411  -5364  -5337       C  
ATOM   5204  O   LYS F  27      11.307  13.924  28.160  1.00 94.84           O  
ANISOU 5204  O   LYS F  27    11231  18180   6625   7059  -4945  -4811       O  
ATOM   5205  CB  LYS F  27      13.968  15.922  28.466  1.00102.36           C  
ANISOU 5205  CB  LYS F  27    11476  19127   8288   6892  -5927  -6429       C  
ATOM   5206  CG  LYS F  27      15.200  16.241  27.642  1.00113.04           C  
ANISOU 5206  CG  LYS F  27    12402  20296  10252   6405  -6079  -6834       C  
ATOM   5207  CD  LYS F  27      15.334  17.760  27.463  1.00122.69           C  
ANISOU 5207  CD  LYS F  27    13482  21243  11893   6051  -6240  -7336       C  
ATOM   5208  CE  LYS F  27      16.527  18.185  26.637  1.00140.48           C  
ANISOU 5208  CE  LYS F  27    15297  23285  14793   5509  -6346  -7738       C  
ATOM   5209  NZ  LYS F  27      16.533  17.579  25.283  1.00148.28           N  
ANISOU 5209  NZ  LYS F  27    16202  24018  16119   5004  -5938  -7280       N  
ATOM   5210  N   GLY F  28      11.813  14.733  30.230  1.00100.94           N  
ANISOU 5210  N   GLY F  28    12093  19461   6798   7964  -5567  -5534       N  
ATOM   5211  CA  GLY F  28      10.449  14.731  30.732  1.00100.34           C  
ANISOU 5211  CA  GLY F  28    12353  19481   6290   8227  -5286  -5122       C  
ATOM   5212  C   GLY F  28       9.558  15.652  29.929  1.00102.85           C  
ANISOU 5212  C   GLY F  28    12665  19471   6942   7753  -5046  -5025       C  
ATOM   5213  O   GLY F  28       9.973  16.761  29.582  1.00103.41           O  
ANISOU 5213  O   GLY F  28    12562  19326   7404   7472  -5258  -5492       O  
ATOM   5214  N   VAL F  29       8.359  15.174  29.573  1.00 96.64           N  
ANISOU 5214  N   VAL F  29    12060  18628   6031   7643  -4600  -4419       N  
ATOM   5215  CA  VAL F  29       7.410  15.958  28.787  1.00 95.18           C  
ANISOU 5215  CA  VAL F  29    11881  18162   6120   7241  -4356  -4281       C  
ATOM   5216  C   VAL F  29       6.231  16.427  29.640  1.00103.82           C  
ANISOU 5216  C   VAL F  29    13214  19473   6760   7650  -4254  -4171       C  
ATOM   5217  O   VAL F  29       5.466  17.266  29.173  1.00102.58           O  
ANISOU 5217  O   VAL F  29    13074  19129   6774   7430  -4128  -4162       O  
ATOM   5218  CB  VAL F  29       6.960  15.251  27.464  1.00 93.40           C  
ANISOU 5218  CB  VAL F  29    11599  17660   6228   6694  -3950  -3761       C  
ATOM   5219  CG1 VAL F  29       8.147  15.058  26.533  1.00 91.50           C  
ANISOU 5219  CG1 VAL F  29    11104  17179   6484   6267  -4067  -3953       C  
ATOM   5220  CG2 VAL F  29       6.271  13.912  27.715  1.00 92.09           C  
ANISOU 5220  CG2 VAL F  29    11613  17681   5696   6881  -3620  -3154       C  
ATOM   5221  N   SER F  30       6.104  15.926  30.889  1.00105.52           N  
ANISOU 5221  N   SER F  30    13623  20088   6384   8275  -4313  -4106       N  
ATOM   5222  CA  SER F  30       5.050  16.335  31.813  1.00109.03           C  
ANISOU 5222  CA  SER F  30    14292  20796   6338   8735  -4216  -4018       C  
ATOM   5223  C   SER F  30       5.381  17.630  32.537  1.00121.52           C  
ANISOU 5223  C   SER F  30    15893  22444   7836   9046  -4638  -4670       C  
ATOM   5224  O   SER F  30       6.411  17.705  33.211  1.00124.65           O  
ANISOU 5224  O   SER F  30    16253  22990   8119   9352  -5045  -5124       O  
ATOM   5225  CB  SER F  30       4.754  15.234  32.825  1.00114.14           C  
ANISOU 5225  CB  SER F  30    15169  21835   6363   9280  -4055  -3633       C  
ATOM   5226  OG  SER F  30       4.288  14.066  32.171  1.00120.21           O  
ANISOU 5226  OG  SER F  30    15954  22507   7215   8971  -3626  -3004       O  
ATOM   5227  N   THR F  31       4.506  18.654  32.392  1.00121.07           N  
ANISOU 5227  N   THR F  31    15895  22274   7831   8985  -4557  -4739       N  
ATOM   5228  CA  THR F  31       4.658  19.963  33.043  1.00125.75           C  
ANISOU 5228  CA  THR F  31    16551  22880   8347   9277  -4937  -5351       C  
ATOM   5229  C   THR F  31       3.283  20.550  33.407  1.00131.01           C  
ANISOU 5229  C   THR F  31    17418  23681   8681   9561  -4718  -5178       C  
ATOM   5230  O   THR F  31       2.383  20.569  32.561  1.00126.32           O  
ANISOU 5230  O   THR F  31    16798  22912   8287   9210  -4358  -4795       O  
ATOM   5231  CB  THR F  31       5.398  20.951  32.112  1.00135.11           C  
ANISOU 5231  CB  THR F  31    17539  23592  10206   8719  -5173  -5813       C  
ATOM   5232  OG1 THR F  31       6.520  20.309  31.493  1.00135.52           O  
ANISOU 5232  OG1 THR F  31    17354  23501  10635   8344  -5257  -5858       O  
ATOM   5233  CG2 THR F  31       5.845  22.221  32.847  1.00135.33           C  
ANISOU 5233  CG2 THR F  31    17620  23596  10205   8997  -5641  -6534       C  
ATOM   5234  N   SER F  32       3.133  21.042  34.651  1.00133.66           N  
ANISOU 5234  N   SER F  32    17942  24339   8504  10215  -4948  -5485       N  
ATOM   5235  CA  SER F  32       1.906  21.695  35.158  1.00136.05           C  
ANISOU 5235  CA  SER F  32    18438  24823   8434  10588  -4788  -5404       C  
ATOM   5236  C   SER F  32       0.637  20.797  35.180  1.00138.17           C  
ANISOU 5236  C   SER F  32    18773  25364   8362  10682  -4223  -4660       C  
ATOM   5237  O   SER F  32      -0.465  21.285  34.917  1.00137.27           O  
ANISOU 5237  O   SER F  32    18687  25240   8230  10648  -3971  -4477       O  
ATOM   5238  CB  SER F  32       1.624  22.983  34.381  1.00139.43           C  
ANISOU 5238  CB  SER F  32    18835  24832   9311  10228  -4864  -5694       C  
ATOM   5239  OG  SER F  32       2.793  23.763  34.193  1.00150.65           O  
ANISOU 5239  OG  SER F  32    20165  25908  11168   9972  -5307  -6313       O  
ATOM   5240  N   GLY F  33       0.800  19.517  35.516  1.00133.69           N  
ANISOU 5240  N   GLY F  33    18231  25038   7529  10810  -4035  -4257       N  
ATOM   5241  CA  GLY F  33      -0.311  18.572  35.599  1.00132.13           C  
ANISOU 5241  CA  GLY F  33    18093  25087   7025  10874  -3493  -3556       C  
ATOM   5242  C   GLY F  33      -0.697  17.863  34.313  1.00129.95           C  
ANISOU 5242  C   GLY F  33    17632  24529   7216  10190  -3112  -3055       C  
ATOM   5243  O   GLY F  33      -1.602  17.029  34.338  1.00128.97           O  
ANISOU 5243  O   GLY F  33    17529  24585   6888  10184  -2660  -2480       O  
ATOM   5244  N   TYR F  34      -0.029  18.167  33.182  1.00123.46           N  
ANISOU 5244  N   TYR F  34    16626  23268   7015   9610  -3275  -3265       N  
ATOM   5245  CA  TYR F  34      -0.302  17.523  31.891  1.00118.60           C  
ANISOU 5245  CA  TYR F  34    15842  22366   6854   8966  -2958  -2842       C  
ATOM   5246  C   TYR F  34       0.986  16.969  31.273  1.00115.32           C  
ANISOU 5246  C   TYR F  34    15305  21684   6826   8605  -3153  -2962       C  
ATOM   5247  O   TYR F  34       2.047  17.575  31.420  1.00114.20           O  
ANISOU 5247  O   TYR F  34    15123  21437   6832   8653  -3571  -3496       O  
ATOM   5248  CB  TYR F  34      -0.948  18.518  30.913  1.00118.75           C  
ANISOU 5248  CB  TYR F  34    15760  22096   7265   8589  -2896  -2926       C  
ATOM   5249  CG  TYR F  34      -2.376  18.866  31.268  1.00124.20           C  
ANISOU 5249  CG  TYR F  34    16513  23050   7628   8862  -2613  -2694       C  
ATOM   5250  CD1 TYR F  34      -3.411  17.966  31.038  1.00125.38           C  
ANISOU 5250  CD1 TYR F  34    16597  23371   7670   8743  -2144  -2098       C  
ATOM   5251  CD2 TYR F  34      -2.696  20.096  31.833  1.00128.43           C  
ANISOU 5251  CD2 TYR F  34    17159  23666   7971   9238  -2814  -3087       C  
ATOM   5252  CE1 TYR F  34      -4.729  18.281  31.358  1.00127.82           C  
ANISOU 5252  CE1 TYR F  34    16911  23961   7695   8986  -1870  -1896       C  
ATOM   5253  CE2 TYR F  34      -4.011  20.424  32.156  1.00130.90           C  
ANISOU 5253  CE2 TYR F  34    17511  24252   7972   9521  -2551  -2886       C  
ATOM   5254  CZ  TYR F  34      -5.028  19.516  31.913  1.00137.64           C  
ANISOU 5254  CZ  TYR F  34    18258  25310   8731   9391  -2072  -2288       C  
ATOM   5255  OH  TYR F  34      -6.332  19.828  32.233  1.00141.28           O  
ANISOU 5255  OH  TYR F  34    18705  26083   8892   9668  -1797  -2096       O  
ATOM   5256  N   SER F  35       0.863  15.838  30.543  1.00106.23           N  
ANISOU 5256  N   SER F  35    14081  20423   5858   8231  -2846  -2479       N  
ATOM   5257  CA  SER F  35       1.959  15.187  29.825  1.00102.01           C  
ANISOU 5257  CA  SER F  35    13425  19639   5697   7863  -2956  -2508       C  
ATOM   5258  C   SER F  35       1.757  15.525  28.348  1.00 98.78           C  
ANISOU 5258  C   SER F  35    12836  18825   5869   7209  -2830  -2445       C  
ATOM   5259  O   SER F  35       0.786  15.070  27.751  1.00 94.13           O  
ANISOU 5259  O   SER F  35    12227  18196   5342   6962  -2466  -1996       O  
ATOM   5260  CB  SER F  35       1.943  13.675  30.055  1.00104.62           C  
ANISOU 5260  CB  SER F  35    13850  20110   5790   7948  -2703  -2011       C  
ATOM   5261  OG  SER F  35       1.750  13.318  31.414  1.00111.21           O  
ANISOU 5261  OG  SER F  35    14907  21342   6005   8582  -2688  -1920       O  
ATOM   5262  N   TYR F  36       2.616  16.389  27.783  1.00 93.71           N  
ANISOU 5262  N   TYR F  36    12071  17895   5640   6946  -3124  -2908       N  
ATOM   5263  CA  TYR F  36       2.472  16.827  26.392  1.00 88.93           C  
ANISOU 5263  CA  TYR F  36    11334  16896   5560   6366  -3012  -2874       C  
ATOM   5264  C   TYR F  36       2.960  15.772  25.362  1.00 89.53           C  
ANISOU 5264  C   TYR F  36    11285  16768   5963   5918  -2856  -2587       C  
ATOM   5265  O   TYR F  36       3.954  15.999  24.673  1.00 88.50           O  
ANISOU 5265  O   TYR F  36    11017  16377   6230   5601  -3023  -2848       O  
ATOM   5266  CB  TYR F  36       3.161  18.188  26.193  1.00 90.59           C  
ANISOU 5266  CB  TYR F  36    11490  16847   6082   6246  -3341  -3451       C  
ATOM   5267  CG  TYR F  36       2.487  19.294  26.972  1.00 95.31           C  
ANISOU 5267  CG  TYR F  36    12236  17566   6410   6627  -3456  -3703       C  
ATOM   5268  CD1 TYR F  36       1.254  19.803  26.573  1.00 96.18           C  
ANISOU 5268  CD1 TYR F  36    12418  17627   6500   6579  -3218  -3489       C  
ATOM   5269  CD2 TYR F  36       3.059  19.804  28.136  1.00 99.54           C  
ANISOU 5269  CD2 TYR F  36    12845  18293   6682   7077  -3813  -4166       C  
ATOM   5270  CE1 TYR F  36       0.605  20.786  27.314  1.00100.31           C  
ANISOU 5270  CE1 TYR F  36    13089  18283   6741   6979  -3317  -3715       C  
ATOM   5271  CE2 TYR F  36       2.428  20.808  28.869  1.00102.83           C  
ANISOU 5271  CE2 TYR F  36    13421  18825   6823   7465  -3926  -4410       C  
ATOM   5272  CZ  TYR F  36       1.196  21.291  28.458  1.00110.71           C  
ANISOU 5272  CZ  TYR F  36    14498  19768   7798   7420  -3668  -4173       C  
ATOM   5273  OH  TYR F  36       0.548  22.293  29.142  1.00118.96           O  
ANISOU 5273  OH  TYR F  36    15708  20923   8567   7824  -3774  -4417       O  
ATOM   5274  N   LEU F  37       2.229  14.639  25.250  1.00 83.73           N  
ANISOU 5274  N   LEU F  37    10600  16146   5069   5887  -2523  -2054       N  
ATOM   5275  CA  LEU F  37       2.546  13.531  24.344  1.00 81.05           C  
ANISOU 5275  CA  LEU F  37    10186  15628   4982   5513  -2356  -1745       C  
ATOM   5276  C   LEU F  37       1.248  13.065  23.694  1.00 81.37           C  
ANISOU 5276  C   LEU F  37    10233  15634   5051   5272  -1967  -1256       C  
ATOM   5277  O   LEU F  37       0.261  12.881  24.390  1.00 79.79           O  
ANISOU 5277  O   LEU F  37    10122  15692   4502   5535  -1776  -1010       O  
ATOM   5278  CB  LEU F  37       3.198  12.374  25.135  1.00 83.03           C  
ANISOU 5278  CB  LEU F  37    10527  16082   4940   5818  -2403  -1625       C  
ATOM   5279  CG  LEU F  37       4.015  11.286  24.391  1.00 84.99           C  
ANISOU 5279  CG  LEU F  37    10712  16146   5433   5542  -2372  -1473       C  
ATOM   5280  CD1 LEU F  37       3.128  10.221  23.777  1.00 81.58           C  
ANISOU 5280  CD1 LEU F  37    10341  15626   5030   5285  -1985   -911       C  
ATOM   5281  CD2 LEU F  37       5.028  11.871  23.398  1.00 86.70           C  
ANISOU 5281  CD2 LEU F  37    10720  16072   6149   5158  -2575  -1837       C  
ATOM   5282  N   HIS F  38       1.242  12.898  22.374  1.00 77.10           N  
ANISOU 5282  N   HIS F  38     9583  14793   4917   4785  -1853  -1135       N  
ATOM   5283  CA  HIS F  38       0.032  12.488  21.631  1.00 76.22           C  
ANISOU 5283  CA  HIS F  38     9442  14635   4885   4519  -1522   -723       C  
ATOM   5284  C   HIS F  38       0.345  11.337  20.683  1.00 77.55           C  
ANISOU 5284  C   HIS F  38     9566  14594   5306   4149  -1387   -454       C  
ATOM   5285  O   HIS F  38       1.501  11.150  20.312  1.00 75.94           O  
ANISOU 5285  O   HIS F  38     9326  14222   5307   4029  -1555   -636       O  
ATOM   5286  CB  HIS F  38      -0.558  13.656  20.828  1.00 75.64           C  
ANISOU 5286  CB  HIS F  38     9302  14394   5045   4316  -1520   -867       C  
ATOM   5287  CG  HIS F  38      -0.426  14.989  21.487  1.00 81.78           C  
ANISOU 5287  CG  HIS F  38    10132  15228   5713   4602  -1752  -1275       C  
ATOM   5288  ND1 HIS F  38      -1.279  15.385  22.497  1.00 86.48           N  
ANISOU 5288  ND1 HIS F  38    10805  16131   5922   5010  -1711  -1263       N  
ATOM   5289  CD2 HIS F  38       0.464  15.977  21.253  1.00 84.57           C  
ANISOU 5289  CD2 HIS F  38    10475  15353   6306   4523  -2016  -1706       C  
ATOM   5290  CE1 HIS F  38      -0.890  16.603  22.837  1.00 88.03           C  
ANISOU 5290  CE1 HIS F  38    11054  16263   6128   5181  -1974  -1700       C  
ATOM   5291  NE2 HIS F  38       0.149  17.002  22.103  1.00 87.17           N  
ANISOU 5291  NE2 HIS F  38    10894  15819   6409   4876  -2160  -1976       N  
ATOM   5292  N   TRP F  39      -0.701  10.578  20.294  1.00 72.98           N  
ANISOU 5292  N   TRP F  39     8977  14033   4718   3972  -1085    -39       N  
ATOM   5293  CA  TRP F  39      -0.596   9.430  19.400  1.00 69.89           C  
ANISOU 5293  CA  TRP F  39     8568  13439   4548   3627   -939    238       C  
ATOM   5294  C   TRP F  39      -1.408   9.642  18.136  1.00 70.81           C  
ANISOU 5294  C   TRP F  39     8568  13378   4959   3238   -798    350       C  
ATOM   5295  O   TRP F  39      -2.472  10.265  18.181  1.00 70.93           O  
ANISOU 5295  O   TRP F  39     8527  13522   4902   3278   -698    390       O  
ATOM   5296  CB  TRP F  39      -1.041   8.153  20.109  1.00 70.53           C  
ANISOU 5296  CB  TRP F  39     8765  13677   4357   3760   -713    636       C  
ATOM   5297  CG  TRP F  39      -0.138   7.773  21.244  1.00 74.20           C  
ANISOU 5297  CG  TRP F  39     9384  14291   4518   4164   -858    554       C  
ATOM   5298  CD1 TRP F  39      -0.199   8.218  22.531  1.00 79.99           C  
ANISOU 5298  CD1 TRP F  39    10211  15324   4859   4629   -930    449       C  
ATOM   5299  CD2 TRP F  39       1.039   6.956  21.158  1.00 74.27           C  
ANISOU 5299  CD2 TRP F  39     9469  14168   4582   4179   -988    520       C  
ATOM   5300  NE1 TRP F  39       0.831   7.674  23.271  1.00 81.29           N  
ANISOU 5300  NE1 TRP F  39    10512  15558   4815   4940  -1095    368       N  
ATOM   5301  CE2 TRP F  39       1.585   6.868  22.460  1.00 81.20           C  
ANISOU 5301  CE2 TRP F  39    10491  15290   5072   4675  -1127    421       C  
ATOM   5302  CE3 TRP F  39       1.624   6.203  20.129  1.00 73.11           C  
ANISOU 5302  CE3 TRP F  39     9296  13739   4742   3856   -986    586       C  
ATOM   5303  CZ2 TRP F  39       2.688   6.060  22.755  1.00 81.86           C  
ANISOU 5303  CZ2 TRP F  39    10685  15349   5070   4862  -1272    384       C  
ATOM   5304  CZ3 TRP F  39       2.736   5.431  20.415  1.00 75.66           C  
ANISOU 5304  CZ3 TRP F  39     9722  14034   4993   4033  -1125    539       C  
ATOM   5305  CH2 TRP F  39       3.266   5.375  21.708  1.00 79.78           C  
ANISOU 5305  CH2 TRP F  39    10374  14804   5133   4532  -1274    433       C  
ATOM   5306  N   TYR F  40      -0.878   9.146  16.991  1.00 63.91           N  
ANISOU 5306  N   TYR F  40     7658  12221   4403   2892   -806    377       N  
ATOM   5307  CA  TYR F  40      -1.522   9.253  15.696  1.00 60.71           C  
ANISOU 5307  CA  TYR F  40     7163  11634   4272   2537   -699    469       C  
ATOM   5308  C   TYR F  40      -1.467   7.939  14.942  1.00 63.04           C  
ANISOU 5308  C   TYR F  40     7469  11759   4723   2256   -573    732       C  
ATOM   5309  O   TYR F  40      -0.443   7.273  14.981  1.00 62.28           O  
ANISOU 5309  O   TYR F  40     7442  11559   4662   2266   -653    706       O  
ATOM   5310  CB  TYR F  40      -0.818  10.314  14.832  1.00 59.17           C  
ANISOU 5310  CB  TYR F  40     6930  11206   4346   2392   -874    145       C  
ATOM   5311  CG  TYR F  40      -0.803  11.701  15.425  1.00 59.33           C  
ANISOU 5311  CG  TYR F  40     6963  11307   4271   2625  -1021   -157       C  
ATOM   5312  CD1 TYR F  40       0.245  12.121  16.235  1.00 63.76           C  
ANISOU 5312  CD1 TYR F  40     7557  11908   4760   2841  -1235   -455       C  
ATOM   5313  CD2 TYR F  40      -1.774  12.633  15.086  1.00 57.70           C  
ANISOU 5313  CD2 TYR F  40     6738  11112   4073   2623   -972   -183       C  
ATOM   5314  CE1 TYR F  40       0.282  13.411  16.756  1.00 67.70           C  
ANISOU 5314  CE1 TYR F  40     8083  12444   5197   3038  -1391   -768       C  
ATOM   5315  CE2 TYR F  40      -1.735  13.930  15.579  1.00 59.17           C  
ANISOU 5315  CE2 TYR F  40     6974  11324   4185   2840  -1117   -476       C  
ATOM   5316  CZ  TYR F  40      -0.705  14.321  16.414  1.00 70.51           C  
ANISOU 5316  CZ  TYR F  40     8454  12777   5560   3033  -1326   -773       C  
ATOM   5317  OH  TYR F  40      -0.701  15.596  16.932  1.00 69.78           O  
ANISOU 5317  OH  TYR F  40     8424  12691   5398   3246  -1482  -1083       O  
ATOM   5318  N   GLN F  41      -2.525   7.630  14.178  1.00 58.90           N  
ANISOU 5318  N   GLN F  41     6869  11197   4313   2010   -402    943       N  
ATOM   5319  CA  GLN F  41      -2.623   6.448  13.305  1.00 57.32           C  
ANISOU 5319  CA  GLN F  41     6675  10804   4298   1705   -292   1165       C  
ATOM   5320  C   GLN F  41      -2.412   6.902  11.840  1.00 58.59           C  
ANISOU 5320  C   GLN F  41     6781  10723   4760   1438   -373   1016       C  
ATOM   5321  O   GLN F  41      -3.014   7.894  11.430  1.00 56.59           O  
ANISOU 5321  O   GLN F  41     6451  10503   4548   1424   -389    910       O  
ATOM   5322  CB  GLN F  41      -4.027   5.826  13.442  1.00 59.62           C  
ANISOU 5322  CB  GLN F  41     6891  11237   4525   1599    -53   1472       C  
ATOM   5323  CG  GLN F  41      -4.323   4.645  12.535  1.00 64.31           C  
ANISOU 5323  CG  GLN F  41     7480  11626   5328   1258     57   1684       C  
ATOM   5324  CD  GLN F  41      -5.774   4.263  12.642  1.00 68.16           C  
ANISOU 5324  CD  GLN F  41     7827  12275   5793   1124    281   1925       C  
ATOM   5325  OE1 GLN F  41      -6.640   4.947  12.112  1.00 65.24           O  
ANISOU 5325  OE1 GLN F  41     7284  12008   5496   1050    287   1855       O  
ATOM   5326  NE2 GLN F  41      -6.090   3.160  13.308  1.00 59.58           N  
ANISOU 5326  NE2 GLN F  41     6808  11217   4612   1089    477   2214       N  
ATOM   5327  N   GLN F  42      -1.619   6.167  11.042  1.00 53.83           N  
ANISOU 5327  N   GLN F  42     6232   9882   4339   1255   -411   1022       N  
ATOM   5328  CA  GLN F  42      -1.439   6.511   9.620  1.00 51.01           C  
ANISOU 5328  CA  GLN F  42     5843   9302   4234   1019   -457    913       C  
ATOM   5329  C   GLN F  42      -1.636   5.309   8.716  1.00 57.06           C  
ANISOU 5329  C   GLN F  42     6639   9899   5144    769   -379   1097       C  
ATOM   5330  O   GLN F  42      -0.835   4.380   8.764  1.00 57.32           O  
ANISOU 5330  O   GLN F  42     6764   9817   5199    759   -397   1147       O  
ATOM   5331  CB  GLN F  42      -0.062   7.157   9.326  1.00 50.29           C  
ANISOU 5331  CB  GLN F  42     5779   9068   4261   1049   -608    638       C  
ATOM   5332  CG  GLN F  42      -0.040   7.786   7.916  1.00 53.36           C  
ANISOU 5332  CG  GLN F  42     6153   9254   4867    842   -614    539       C  
ATOM   5333  CD  GLN F  42       1.192   8.572   7.563  1.00 57.55           C  
ANISOU 5333  CD  GLN F  42     6688   9638   5540    827   -712    281       C  
ATOM   5334  OE1 GLN F  42       2.299   8.259   7.976  1.00 55.12           O  
ANISOU 5334  OE1 GLN F  42     6368   9327   5248    892   -788    174       O  
ATOM   5335  NE2 GLN F  42       1.050   9.523   6.665  1.00 48.59           N  
ANISOU 5335  NE2 GLN F  42     5569   8365   4528    725   -698    186       N  
ATOM   5336  N   LYS F  43      -2.655   5.357   7.844  1.00 55.87           N  
ANISOU 5336  N   LYS F  43     6411   9723   5092    585   -318   1167       N  
ATOM   5337  CA  LYS F  43      -2.880   4.311   6.840  1.00 56.09           C  
ANISOU 5337  CA  LYS F  43     6462   9571   5278    335   -278   1289       C  
ATOM   5338  C   LYS F  43      -2.132   4.741   5.574  1.00 60.17           C  
ANISOU 5338  C   LYS F  43     7024   9878   5959    247   -375   1111       C  
ATOM   5339  O   LYS F  43      -1.914   5.941   5.390  1.00 57.99           O  
ANISOU 5339  O   LYS F  43     6730   9615   5687    329   -430    941       O  
ATOM   5340  CB  LYS F  43      -4.355   4.152   6.509  1.00 59.24           C  
ANISOU 5340  CB  LYS F  43     6728  10076   5706    189   -186   1415       C  
ATOM   5341  CG  LYS F  43      -5.267   4.017   7.722  1.00 69.85           C  
ANISOU 5341  CG  LYS F  43     7978  11681   6883    279    -49   1583       C  
ATOM   5342  CD  LYS F  43      -5.869   2.648   7.876  1.00 77.33           C  
ANISOU 5342  CD  LYS F  43     8918  12586   7878     79     96   1833       C  
ATOM   5343  CE  LYS F  43      -6.970   2.647   8.911  1.00 81.72           C  
ANISOU 5343  CE  LYS F  43     9334  13428   8288    132    277   2007       C  
ATOM   5344  NZ  LYS F  43      -7.967   1.592   8.637  1.00 92.38           N  
ANISOU 5344  NZ  LYS F  43    10579  14745   9777   -169    427   2206       N  
ATOM   5345  N   PRO F  44      -1.710   3.813   4.686  1.00 59.81           N  
ANISOU 5345  N   PRO F  44     7057   9626   6043     92   -386   1147       N  
ATOM   5346  CA  PRO F  44      -0.973   4.243   3.479  1.00 57.87           C  
ANISOU 5346  CA  PRO F  44     6860   9203   5925     33   -448    990       C  
ATOM   5347  C   PRO F  44      -1.782   5.205   2.596  1.00 61.10           C  
ANISOU 5347  C   PRO F  44     7222   9626   6365     -9   -455    924       C  
ATOM   5348  O   PRO F  44      -2.984   5.027   2.432  1.00 61.88           O  
ANISOU 5348  O   PRO F  44     7243   9819   6448    -75   -431   1012       O  
ATOM   5349  CB  PRO F  44      -0.658   2.924   2.763  1.00 59.64           C  
ANISOU 5349  CB  PRO F  44     7180   9238   6244   -101   -450   1069       C  
ATOM   5350  CG  PRO F  44      -0.770   1.867   3.804  1.00 65.84           C  
ANISOU 5350  CG  PRO F  44     8005  10059   6951    -74   -404   1239       C  
ATOM   5351  CD  PRO F  44      -1.843   2.340   4.739  1.00 62.79           C  
ANISOU 5351  CD  PRO F  44     7505   9902   6448    -24   -335   1330       C  
ATOM   5352  N   GLY F  45      -1.134   6.280   2.149  1.00 57.80           N  
ANISOU 5352  N   GLY F  45     6845   9133   5982     48   -481    765       N  
ATOM   5353  CA  GLY F  45      -1.748   7.295   1.301  1.00 57.21           C  
ANISOU 5353  CA  GLY F  45     6788   9036   5912     58   -483    701       C  
ATOM   5354  C   GLY F  45      -2.678   8.257   2.010  1.00 61.67           C  
ANISOU 5354  C   GLY F  45     7281   9790   6362    196   -486    684       C  
ATOM   5355  O   GLY F  45      -3.340   9.061   1.353  1.00 62.27           O  
ANISOU 5355  O   GLY F  45     7380   9866   6413    243   -497    643       O  
ATOM   5356  N   GLN F  46      -2.758   8.183   3.351  1.00 56.97           N  
ANISOU 5356  N   GLN F  46     6613   9366   5668    298   -478    713       N  
ATOM   5357  CA  GLN F  46      -3.645   9.027   4.132  1.00 54.86           C  
ANISOU 5357  CA  GLN F  46     6273   9308   5262    464   -475    696       C  
ATOM   5358  C   GLN F  46      -2.839   9.842   5.114  1.00 53.35           C  
ANISOU 5358  C   GLN F  46     6124   9136   5011    628   -519    550       C  
ATOM   5359  O   GLN F  46      -1.750   9.438   5.520  1.00 51.80           O  
ANISOU 5359  O   GLN F  46     5955   8874   4852    617   -546    505       O  
ATOM   5360  CB  GLN F  46      -4.693   8.186   4.864  1.00 20.00           C  
ATOM   5361  CG  GLN F  46      -5.699   7.511   3.948  1.00 20.00           C  
ATOM   5362  CD  GLN F  46      -6.675   6.631   4.701  1.00 20.00           C  
ATOM   5363  OE1 GLN F  46      -6.371   6.147   5.792  1.00 20.00           O  
ATOM   5364  NE2 GLN F  46      -7.853   6.420   4.122  1.00 20.00           N  
ATOM   5365  N   ALA F  47      -3.391  10.974   5.531  1.00 48.62           N  
ANISOU 5365  N   ALA F  47     5524   8640   4309    802   -542    459       N  
ATOM   5366  CA  ALA F  47      -2.766  11.812   6.540  1.00 48.20           C  
ANISOU 5366  CA  ALA F  47     5510   8616   4188    977   -607    288       C  
ATOM   5367  C   ALA F  47      -2.801  11.128   7.888  1.00 52.36           C  
ANISOU 5367  C   ALA F  47     5965   9376   4554   1105   -598    365       C  
ATOM   5368  O   ALA F  47      -3.698  10.335   8.143  1.00 52.00           O  
ANISOU 5368  O   ALA F  47     5832   9507   4418   1093   -508    564       O  
ATOM   5369  CB  ALA F  47      -3.497  13.144   6.646  1.00 49.45           C  
ANISOU 5369  CB  ALA F  47     5713   8823   4254   1160   -636    178       C  
ATOM   5370  N   PRO F  48      -1.875  11.465   8.805  1.00 51.06           N  
ANISOU 5370  N   PRO F  48     5833   9227   4341   1242   -687    203       N  
ATOM   5371  CA  PRO F  48      -1.980  10.929  10.169  1.00 51.91           C  
ANISOU 5371  CA  PRO F  48     5908   9584   4232   1440   -682    275       C  
ATOM   5372  C   PRO F  48      -3.314  11.339  10.818  1.00 56.66           C  
ANISOU 5372  C   PRO F  48     6455  10452   4621   1629   -611    359       C  
ATOM   5373  O   PRO F  48      -3.901  12.370  10.455  1.00 55.65           O  
ANISOU 5373  O   PRO F  48     6333  10314   4498   1686   -631    260       O  
ATOM   5374  CB  PRO F  48      -0.785  11.545  10.897  1.00 53.95           C  
ANISOU 5374  CB  PRO F  48     6209   9810   4479   1588   -838      3       C  
ATOM   5375  CG  PRO F  48       0.125  12.009   9.844  1.00 57.51           C  
ANISOU 5375  CG  PRO F  48     6684   9970   5196   1380   -888   -160       C  
ATOM   5376  CD  PRO F  48      -0.722  12.378   8.672  1.00 52.70           C  
ANISOU 5376  CD  PRO F  48     6105   9237   4683   1232   -796    -65       C  
ATOM   5377  N   ARG F  49      -3.815  10.499  11.727  1.00 54.82           N  
ANISOU 5377  N   ARG F  49     6176  10455   4200   1731   -509    556       N  
ATOM   5378  CA  ARG F  49      -5.101  10.702  12.410  1.00 56.80           C  
ANISOU 5378  CA  ARG F  49     6338  11007   4236   1906   -395    673       C  
ATOM   5379  C   ARG F  49      -4.858  10.716  13.886  1.00 62.01           C  
ANISOU 5379  C   ARG F  49     7050  11891   4620   2218   -407    652       C  
ATOM   5380  O   ARG F  49      -4.287   9.754  14.392  1.00 61.57           O  
ANISOU 5380  O   ARG F  49     7051  11840   4504   2224   -376    771       O  
ATOM   5381  CB  ARG F  49      -6.089   9.580  12.027  1.00 56.00           C  
ANISOU 5381  CB  ARG F  49     6112  10988   4178   1693   -203    976       C  
ATOM   5382  CG  ARG F  49      -7.269   9.413  12.958  1.00 68.53           C  
ANISOU 5382  CG  ARG F  49     7575  12925   5537   1848    -28   1155       C  
ATOM   5383  CD  ARG F  49      -8.414   8.622  12.363  1.00 77.47           C  
ANISOU 5383  CD  ARG F  49     8522  14134   6779   1592    147   1385       C  
ATOM   5384  NE  ARG F  49      -8.427   7.216  12.790  1.00 79.43           N  
ANISOU 5384  NE  ARG F  49     8781  14379   7021   1439    320   1664       N  
ATOM   5385  CZ  ARG F  49      -9.400   6.600  13.467  1.00 93.76           C  
ANISOU 5385  CZ  ARG F  49    10467  16436   8720   1424    557   1913       C  
ATOM   5386  NH1 ARG F  49     -10.481   7.270  13.862  1.00 82.57           N  
ANISOU 5386  NH1 ARG F  49     8861  15347   7164   1581    653   1909       N  
ATOM   5387  NH2 ARG F  49      -9.293   5.312  13.768  1.00 87.67           N  
ANISOU 5387  NH2 ARG F  49     9762  15579   7968   1260    716   2170       N  
ATOM   5388  N   LEU F  50      -5.298  11.781  14.587  1.00 60.89           N  
ANISOU 5388  N   LEU F  50     6912  11936   4286   2511   -454    500       N  
ATOM   5389  CA  LEU F  50      -5.144  11.882  16.051  1.00 63.22           C  
ANISOU 5389  CA  LEU F  50     7270  12485   4265   2873   -476    457       C  
ATOM   5390  C   LEU F  50      -6.046  10.863  16.762  1.00 69.33           C  
ANISOU 5390  C   LEU F  50     7976  13543   4822   2932   -223    804       C  
ATOM   5391  O   LEU F  50      -7.229  10.756  16.442  1.00 69.16           O  
ANISOU 5391  O   LEU F  50     7806  13659   4812   2836    -48    978       O  
ATOM   5392  CB  LEU F  50      -5.477  13.307  16.524  1.00 64.40           C  
ANISOU 5392  CB  LEU F  50     7452  12750   4267   3175   -591    194       C  
ATOM   5393  CG  LEU F  50      -5.240  13.637  18.025  1.00 71.51           C  
ANISOU 5393  CG  LEU F  50     8445  13906   4821   3606   -670     63       C  
ATOM   5394  CD1 LEU F  50      -3.741  13.676  18.394  1.00 72.20           C  
ANISOU 5394  CD1 LEU F  50     8645  13833   4953   3662   -905   -193       C  
ATOM   5395  CD2 LEU F  50      -5.839  14.987  18.394  1.00 72.99           C  
ANISOU 5395  CD2 LEU F  50     8660  14213   4858   3901   -752   -165       C  
ATOM   5396  N   LEU F  51      -5.465  10.095  17.696  1.00 68.03           N  
ANISOU 5396  N   LEU F  51     7920  13458   4470   3085   -200    905       N  
ATOM   5397  CA  LEU F  51      -6.166   9.061  18.467  1.00 70.53           C  
ANISOU 5397  CA  LEU F  51     8230  14004   4564   3149     69   1263       C  
ATOM   5398  C   LEU F  51      -6.355   9.482  19.922  1.00 75.56           C  
ANISOU 5398  C   LEU F  51     8946  14982   4783   3622     93   1232       C  
ATOM   5399  O   LEU F  51      -7.458   9.409  20.458  1.00 76.47           O  
ANISOU 5399  O   LEU F  51     8972  15387   4696   3738    329   1436       O  
ATOM   5400  CB  LEU F  51      -5.345   7.758  18.451  1.00 70.99           C  
ANISOU 5400  CB  LEU F  51     8417  13875   4680   3012     99   1443       C  
ATOM   5401  CG  LEU F  51      -5.037   7.122  17.102  1.00 74.37           C  
ANISOU 5401  CG  LEU F  51     8809  13966   5483   2581     81   1494       C  
ATOM   5402  CD1 LEU F  51      -3.880   6.134  17.244  1.00 74.99           C  
ANISOU 5402  CD1 LEU F  51     9062  13861   5571   2582     14   1545       C  
ATOM   5403  CD2 LEU F  51      -6.264   6.434  16.533  1.00 78.30           C  
ANISOU 5403  CD2 LEU F  51     9159  14482   6108   2274    338   1791       C  
ATOM   5404  N   ILE F  52      -5.233   9.835  20.576  1.00 72.75           N  
ANISOU 5404  N   ILE F  52     8748  14602   4290   3899   -149    976       N  
ATOM   5405  CA  ILE F  52      -5.130  10.185  21.986  1.00 74.40           C  
ANISOU 5405  CA  ILE F  52     9080  15108   4079   4395   -196    888       C  
ATOM   5406  C   ILE F  52      -4.314  11.464  22.087  1.00 77.34           C  
ANISOU 5406  C   ILE F  52     9499  15406   4483   4587   -551    401       C  
ATOM   5407  O   ILE F  52      -3.257  11.553  21.449  1.00 74.41           O  
ANISOU 5407  O   ILE F  52     9138  14751   4382   4397   -766    185       O  
ATOM   5408  CB  ILE F  52      -4.390   9.049  22.755  1.00 78.64           C  
ANISOU 5408  CB  ILE F  52     9800  15671   4410   4552   -162   1069       C  
ATOM   5409  CG1 ILE F  52      -5.118   7.687  22.655  1.00 79.61           C  
ANISOU 5409  CG1 ILE F  52     9923  15795   4530   4325    207   1571       C  
ATOM   5410  CG2 ILE F  52      -4.112   9.440  24.229  1.00 82.50           C  
ANISOU 5410  CG2 ILE F  52    10449  16468   4430   5127   -267    927       C  
ATOM   5411  CD1 ILE F  52      -6.408   7.569  23.414  1.00 87.51           C  
ANISOU 5411  CD1 ILE F  52    10876  17136   5238   4487    540   1864       C  
ATOM   5412  N   TYR F  53      -4.770  12.420  22.928  1.00 76.16           N  
ANISOU 5412  N   TYR F  53     9379  15510   4049   4972   -606    223       N  
ATOM   5413  CA  TYR F  53      -4.059  13.671  23.187  1.00 75.80           C  
ANISOU 5413  CA  TYR F  53     9402  15395   4004   5189   -946   -261       C  
ATOM   5414  C   TYR F  53      -3.767  13.766  24.675  1.00 83.31           C  
ANISOU 5414  C   TYR F  53    10503  16653   4498   5728  -1052   -386       C  
ATOM   5415  O   TYR F  53      -4.557  13.294  25.494  1.00 83.47           O  
ANISOU 5415  O   TYR F  53    10562  16999   4156   5994   -812   -105       O  
ATOM   5416  CB  TYR F  53      -4.832  14.904  22.704  1.00 75.86           C  
ANISOU 5416  CB  TYR F  53     9347  15368   4109   5179   -973   -436       C  
ATOM   5417  CG  TYR F  53      -6.208  15.082  23.310  1.00 80.00           C  
ANISOU 5417  CG  TYR F  53     9823  16264   4311   5457   -739   -245       C  
ATOM   5418  CD1 TYR F  53      -7.335  14.555  22.692  1.00 80.37           C  
ANISOU 5418  CD1 TYR F  53     9696  16394   4447   5214   -435    107       C  
ATOM   5419  CD2 TYR F  53      -6.394  15.847  24.458  1.00 85.04           C  
ANISOU 5419  CD2 TYR F  53    10568  17177   4566   5969   -837   -455       C  
ATOM   5420  CE1 TYR F  53      -8.603  14.730  23.232  1.00 82.48           C  
ANISOU 5420  CE1 TYR F  53     9868  17035   4436   5461   -208    267       C  
ATOM   5421  CE2 TYR F  53      -7.663  16.047  24.997  1.00 88.99           C  
ANISOU 5421  CE2 TYR F  53    11006  18044   4762   6246   -608   -291       C  
ATOM   5422  CZ  TYR F  53      -8.770  15.499  24.369  1.00 94.38           C  
ANISOU 5422  CZ  TYR F  53    11483  18825   5554   5983   -286     72       C  
ATOM   5423  OH  TYR F  53     -10.031  15.641  24.903  1.00 95.86           O  
ANISOU 5423  OH  TYR F  53    11556  19413   5452   6243    -35    242       O  
ATOM   5424  N   LEU F  54      -2.611  14.350  25.013  1.00 83.02           N  
ANISOU 5424  N   LEU F  54    10544  16519   4481   5888  -1406   -810       N  
ATOM   5425  CA  LEU F  54      -2.120  14.503  26.390  1.00 87.57           C  
ANISOU 5425  CA  LEU F  54    11271  17369   4633   6427  -1595  -1022       C  
ATOM   5426  C   LEU F  54      -1.943  13.131  27.065  1.00 92.94           C  
ANISOU 5426  C   LEU F  54    12053  18238   5021   6597  -1429   -667       C  
ATOM   5427  O   LEU F  54      -2.306  12.937  28.220  1.00 94.46           O  
ANISOU 5427  O   LEU F  54    12384  18771   4737   7060  -1342   -555       O  
ATOM   5428  CB  LEU F  54      -3.025  15.447  27.197  1.00 90.76           C  
ANISOU 5428  CB  LEU F  54    11737  18057   4689   6847  -1576  -1137       C  
ATOM   5429  CG  LEU F  54      -3.176  16.854  26.614  1.00 94.27           C  
ANISOU 5429  CG  LEU F  54    12142  18289   5387   6744  -1760  -1506       C  
ATOM   5430  CD1 LEU F  54      -4.285  17.608  27.327  1.00 98.08           C  
ANISOU 5430  CD1 LEU F  54    12684  19080   5501   7168  -1674  -1533       C  
ATOM   5431  CD2 LEU F  54      -1.852  17.620  26.684  1.00 95.97           C  
ANISOU 5431  CD2 LEU F  54    12407  18272   5788   6763  -2193  -2054       C  
ATOM   5432  N   ALA F  55      -1.471  12.163  26.265  1.00 89.35           N  
ANISOU 5432  N   ALA F  55    11547  17545   4856   6211  -1349   -455       N  
ATOM   5433  CA  ALA F  55      -1.158  10.782  26.598  1.00 91.80           C  
ANISOU 5433  CA  ALA F  55    11971  17901   5007   6262  -1203   -115       C  
ATOM   5434  C   ALA F  55      -2.284   9.896  27.128  1.00100.39           C  
ANISOU 5434  C   ALA F  55    13149  19220   5773   6378   -779    413       C  
ATOM   5435  O   ALA F  55      -2.022   8.710  27.294  1.00101.71           O  
ANISOU 5435  O   ALA F  55    13443  19357   5845   6376   -635    724       O  
ATOM   5436  CB  ALA F  55      -0.013  10.752  27.590  1.00 95.93           C  
ANISOU 5436  CB  ALA F  55    12634  18556   5258   6706  -1522   -410       C  
ATOM   5437  N   SER F  56      -3.511  10.398  27.337  1.00 99.25           N  
ANISOU 5437  N   SER F  56    12934  19280   5497   6438   -558    538       N  
ATOM   5438  CA  SER F  56      -4.583   9.595  27.945  1.00101.79           C  
ANISOU 5438  CA  SER F  56    13315  19864   5497   6563   -129   1031       C  
ATOM   5439  C   SER F  56      -5.990   9.885  27.418  1.00102.38           C  
ANISOU 5439  C   SER F  56    13171  20026   5700   6310    174   1238       C  
ATOM   5440  O   SER F  56      -6.714   8.935  27.106  1.00101.03           O  
ANISOU 5440  O   SER F  56    12934  19841   5610   6023    534   1674       O  
ATOM   5441  CB  SER F  56      -4.546   9.741  29.465  1.00110.33           C  
ANISOU 5441  CB  SER F  56    14611  21326   5983   7227   -157    983       C  
ATOM   5442  OG  SER F  56      -4.309  11.079  29.881  1.00122.80           O  
ANISOU 5442  OG  SER F  56    16185  23024   7449   7556   -496    480       O  
ATOM   5443  N   TYR F  57      -6.387  11.171  27.349  1.00 98.14           N  
ANISOU 5443  N   TYR F  57    12527  19586   5174   6434     28    920       N  
ATOM   5444  CA  TYR F  57      -7.737  11.566  26.911  1.00 97.79           C  
ANISOU 5444  CA  TYR F  57    12264  19679   5214   6281    275   1059       C  
ATOM   5445  C   TYR F  57      -8.021  11.175  25.442  1.00 94.71           C  
ANISOU 5445  C   TYR F  57    11670  18975   5341   5660    363   1199       C  
ATOM   5446  O   TYR F  57      -7.252  11.499  24.521  1.00 89.51           O  
ANISOU 5446  O   TYR F  57    10999  17972   5039   5395     97    944       O  
ATOM   5447  CB  TYR F  57      -7.931  13.072  27.091  1.00 20.00           C  
ATOM   5448  CG  TYR F  57      -7.884  13.529  28.533  1.00 20.00           C  
ATOM   5449  CD1 TYR F  57      -9.029  13.523  29.320  1.00 20.00           C  
ATOM   5450  CD2 TYR F  57      -6.697  13.964  29.103  1.00 20.00           C  
ATOM   5451  CE1 TYR F  57      -8.991  13.939  30.637  1.00 20.00           C  
ATOM   5452  CE2 TYR F  57      -6.649  14.383  30.421  1.00 20.00           C  
ATOM   5453  CZ  TYR F  57      -7.798  14.368  31.182  1.00 20.00           C  
ATOM   5454  OH  TYR F  57      -7.758  14.785  32.493  1.00 20.00           O  
ATOM   5455  N   LEU F  58      -9.132  10.442  25.250  1.00 92.16           N  
ANISOU 5455  N   LEU F  58    11181  18786   5048   5435    748   1602       N  
ATOM   5456  CA  LEU F  58      -9.542   9.938  23.941  1.00 89.74           C  
ANISOU 5456  CA  LEU F  58    10675  18231   5191   4871    855   1759       C  
ATOM   5457  C   LEU F  58     -10.092  11.051  23.059  1.00 93.55           C  
ANISOU 5457  C   LEU F  58    10964  18678   5900   4763    721   1502       C  
ATOM   5458  O   LEU F  58     -10.876  11.887  23.515  1.00 96.39           O  
ANISOU 5458  O   LEU F  58    11242  19338   6042   5065    763   1406       O  
ATOM   5459  CB  LEU F  58     -10.573   8.807  24.104  1.00 91.82           C  
ANISOU 5459  CB  LEU F  58    10810  18663   5415   4668   1307   2248       C  
ATOM   5460  CG  LEU F  58     -10.975   8.029  22.845  1.00 93.61           C  
ANISOU 5460  CG  LEU F  58    10844  18633   6092   4074   1431   2439       C  
ATOM   5461  CD1 LEU F  58      -9.782   7.311  22.231  1.00 91.07           C  
ANISOU 5461  CD1 LEU F  58    10704  17879   6020   3815   1247   2415       C  
ATOM   5462  CD2 LEU F  58     -12.050   7.020  23.188  1.00 97.96           C  
ANISOU 5462  CD2 LEU F  58    11253  19384   6584   3901   1888   2890       C  
ATOM   5463  N   GLU F  59      -9.669  11.055  21.798  1.00 86.82           N  
ANISOU 5463  N   GLU F  59    10063  17462   5462   4367    562   1393       N  
ATOM   5464  CA  GLU F  59     -10.068  12.056  20.810  1.00 84.55           C  
ANISOU 5464  CA  GLU F  59     9645  17071   5410   4248    421   1161       C  
ATOM   5465  C   GLU F  59     -11.485  11.768  20.311  1.00 88.43           C  
ANISOU 5465  C   GLU F  59     9847  17763   5990   4046    692   1400       C  
ATOM   5466  O   GLU F  59     -11.803  10.620  20.010  1.00 87.77           O  
ANISOU 5466  O   GLU F  59     9654  17645   6049   3715    911   1706       O  
ATOM   5467  CB  GLU F  59      -9.045  12.060  19.632  1.00 81.87           C  
ANISOU 5467  CB  GLU F  59     9379  16267   5459   3902    181    988       C  
ATOM   5468  CG  GLU F  59      -9.364  12.951  18.433  1.00 81.94           C  
ANISOU 5468  CG  GLU F  59     9301  16097   5736   3733     54    795       C  
ATOM   5469  CD  GLU F  59      -9.608  14.419  18.719  1.00 90.32           C  
ANISOU 5469  CD  GLU F  59    10418  17250   6652   4083   -105    489       C  
ATOM   5470  OE1 GLU F  59      -9.031  14.955  19.697  1.00 87.61           O  
ANISOU 5470  OE1 GLU F  59    10236  16972   6079   4423   -245    285       O  
ATOM   5471  OE2 GLU F  59     -10.351  15.044  17.928  1.00 69.89           O  
ANISOU 5471  OE2 GLU F  59     7726  14652   4177   4030   -107    434       O  
ATOM   5472  N   SER F  60     -12.328  12.810  20.214  1.00 86.34           N  
ANISOU 5472  N   SER F  60     9453  17701   5649   4249    666   1242       N  
ATOM   5473  CA  SER F  60     -13.693  12.696  19.653  1.00 86.54           C  
ANISOU 5473  CA  SER F  60     9156  17953   5773   4091    873   1396       C  
ATOM   5474  C   SER F  60     -13.707  11.900  18.332  1.00 85.04           C  
ANISOU 5474  C   SER F  60     8841  17476   5993   3558    885   1516       C  
ATOM   5475  O   SER F  60     -12.865  12.141  17.468  1.00 80.55           O  
ANISOU 5475  O   SER F  60     8418  16528   5659   3390    645   1338       O  
ATOM   5476  CB  SER F  60     -14.277  14.079  19.399  1.00 89.42           C  
ANISOU 5476  CB  SER F  60     9467  18436   6072   4376    720   1112       C  
ATOM   5477  OG  SER F  60     -14.325  14.802  20.615  1.00106.21           O  
ANISOU 5477  OG  SER F  60    11711  20836   7809   4885    706    986       O  
ATOM   5478  N   GLY F  61     -14.631  10.945  18.222  1.00 83.76           N  
ANISOU 5478  N   GLY F  61     8416  17497   5912   3299   1172   1811       N  
ATOM   5479  CA  GLY F  61     -14.793  10.092  17.048  1.00 82.46           C  
ANISOU 5479  CA  GLY F  61     8109  17102   6119   2800   1200   1928       C  
ATOM   5480  C   GLY F  61     -13.934   8.836  17.004  1.00 88.43           C  
ANISOU 5480  C   GLY F  61     9040  17545   7016   2496   1254   2128       C  
ATOM   5481  O   GLY F  61     -14.148   7.996  16.125  1.00 88.26           O  
ANISOU 5481  O   GLY F  61     8903  17345   7286   2083   1305   2247       O  
ATOM   5482  N   VAL F  62     -12.963   8.670  17.941  1.00 85.51           N  
ANISOU 5482  N   VAL F  62     8953  17107   6429   2716   1227   2154       N  
ATOM   5483  CA  VAL F  62     -12.040   7.523  17.937  1.00 84.29           C  
ANISOU 5483  CA  VAL F  62     9005  16647   6374   2499   1247   2321       C  
ATOM   5484  C   VAL F  62     -12.619   6.350  18.796  1.00 89.78           C  
ANISOU 5484  C   VAL F  62     9666  17514   6931   2426   1626   2727       C  
ATOM   5485  O   VAL F  62     -13.101   6.600  19.899  1.00 90.76           O  
ANISOU 5485  O   VAL F  62     9772  17988   6726   2746   1808   2826       O  
ATOM   5486  CB  VAL F  62     -10.612   7.988  18.376  1.00 86.97           C  
ANISOU 5486  CB  VAL F  62     9658  16806   6580   2777    975   2093       C  
ATOM   5487  CG1 VAL F  62      -9.640   6.813  18.595  1.00 86.70           C  
ANISOU 5487  CG1 VAL F  62     9850  16526   6567   2666    998   2265       C  
ATOM   5488  CG2 VAL F  62     -10.040   8.957  17.339  1.00 83.05           C  
ANISOU 5488  CG2 VAL F  62     9186  16060   6311   2717    658   1744       C  
ATOM   5489  N   PRO F  63     -12.554   5.079  18.315  1.00 86.82           N  
ANISOU 5489  N   PRO F  63     9313  16880   6795   2021   1755   2965       N  
ATOM   5490  CA  PRO F  63     -13.098   3.951  19.100  1.00 90.27           C  
ANISOU 5490  CA  PRO F  63     9752  17420   7125   1917   2143   3371       C  
ATOM   5491  C   PRO F  63     -12.545   3.777  20.505  1.00 97.88           C  
ANISOU 5491  C   PRO F  63    11011  18507   7671   2327   2255   3523       C  
ATOM   5492  O   PRO F  63     -11.402   4.137  20.804  1.00 95.08           O  
ANISOU 5492  O   PRO F  63    10923  18039   7163   2622   1992   3329       O  
ATOM   5493  CB  PRO F  63     -12.778   2.721  18.247  1.00 91.07           C  
ANISOU 5493  CB  PRO F  63     9929  17104   7570   1448   2160   3518       C  
ATOM   5494  CG  PRO F  63     -12.583   3.240  16.881  1.00 92.61           C  
ANISOU 5494  CG  PRO F  63    10010  17102   8077   1250   1851   3211       C  
ATOM   5495  CD  PRO F  63     -12.016   4.613  17.020  1.00 85.67           C  
ANISOU 5495  CD  PRO F  63     9202  16326   7023   1643   1569   2876       C  
ATOM   5496  N   ALA F  64     -13.385   3.173  21.356  1.00100.23           N  
ANISOU 5496  N   ALA F  64    11246  19048   7789   2335   2662   3878       N  
ATOM   5497  CA  ALA F  64     -13.138   2.925  22.774  1.00103.73           C  
ANISOU 5497  CA  ALA F  64    11955  19677   7782   2743   2861   4098       C  
ATOM   5498  C   ALA F  64     -11.910   2.041  23.024  1.00105.80           C  
ANISOU 5498  C   ALA F  64    12637  19585   7977   2799   2772   4207       C  
ATOM   5499  O   ALA F  64     -11.195   2.242  24.012  1.00105.85           O  
ANISOU 5499  O   ALA F  64    12926  19696   7597   3273   2693   4176       O  
ATOM   5500  CB  ALA F  64     -14.368   2.297  23.412  1.00 20.00           C  
ATOM   5501  N   ARG F  65     -11.679   1.067  22.123  1.00100.87           N  
ANISOU 5501  N   ARG F  65    12052  18555   7718   2341   2771   4317       N  
ATOM   5502  CA  ARG F  65     -10.539   0.138  22.175  1.00 99.88           C  
ANISOU 5502  CA  ARG F  65    12313  18056   7582   2357   2677   4415       C  
ATOM   5503  C   ARG F  65      -9.147   0.814  22.221  1.00 99.83           C  
ANISOU 5503  C   ARG F  65    12512  17970   7449   2727   2233   4043       C  
ATOM   5504  O   ARG F  65      -8.193   0.180  22.671  1.00100.82           O  
ANISOU 5504  O   ARG F  65    12971  17924   7412   2926   2168   4121       O  
ATOM   5505  CB  ARG F  65     -10.591  -0.876  21.012  1.00 97.79           C  
ANISOU 5505  CB  ARG F  65    12016  17365   7775   1791   2702   4520       C  
ATOM   5506  CG  ARG F  65     -10.635  -0.263  19.627  1.00100.60           C  
ANISOU 5506  CG  ARG F  65    12098  17605   8520   1497   2409   4175       C  
ATOM   5507  CD  ARG F  65     -10.277  -1.280  18.573  1.00113.24           C  
ANISOU 5507  CD  ARG F  65    13787  18747  10492   1069   2345   4222       C  
ATOM   5508  NE  ARG F  65     -10.578  -0.797  17.224  1.00124.34           N  
ANISOU 5508  NE  ARG F  65    14908  20077  12261    757   2136   3949       N  
ATOM   5509  CZ  ARG F  65     -11.777  -0.809  16.644  1.00143.01           C  
ANISOU 5509  CZ  ARG F  65    16927  22548  14861    414   2276   3983       C  
ATOM   5510  NH1 ARG F  65     -11.927  -0.344  15.412  1.00132.39           N  
ANISOU 5510  NH1 ARG F  65    15372  21129  13799    205   2043   3711       N  
ATOM   5511  NH2 ARG F  65     -12.836  -1.283  17.292  1.00137.38           N  
ANISOU 5511  NH2 ARG F  65    16067  22034  14095    289   2656   4285       N  
ATOM   5512  N   PHE F  66      -9.022   2.063  21.741  1.00 91.03           N  
ANISOU 5512  N   PHE F  66    11204  16965   6420   2810   1933   3640       N  
ATOM   5513  CA  PHE F  66      -7.756   2.781  21.810  1.00 87.12           C  
ANISOU 5513  CA  PHE F  66    10860  16406   5836   3122   1532   3268       C  
ATOM   5514  C   PHE F  66      -7.690   3.518  23.137  1.00 93.54           C  
ANISOU 5514  C   PHE F  66    11774  17587   6180   3683   1511   3182       C  
ATOM   5515  O   PHE F  66      -8.622   4.244  23.488  1.00 95.08           O  
ANISOU 5515  O   PHE F  66    11788  18100   6239   3806   1637   3169       O  
ATOM   5516  CB  PHE F  66      -7.623   3.802  20.674  1.00 83.81           C  
ANISOU 5516  CB  PHE F  66    10222  15886   5735   2937   1238   2883       C  
ATOM   5517  CG  PHE F  66      -7.557   3.192  19.302  1.00 81.98           C  
ANISOU 5517  CG  PHE F  66     9910  15299   5939   2443   1200   2903       C  
ATOM   5518  CD1 PHE F  66      -6.336   2.880  18.722  1.00 81.32           C  
ANISOU 5518  CD1 PHE F  66     9983  14898   6019   2375    958   2752       C  
ATOM   5519  CD2 PHE F  66      -8.711   2.972  18.567  1.00 83.65           C  
ANISOU 5519  CD2 PHE F  66     9871  15519   6394   2065   1387   3040       C  
ATOM   5520  CE1 PHE F  66      -6.275   2.310  17.457  1.00 79.31           C  
ANISOU 5520  CE1 PHE F  66     9672  14327   6135   1955    923   2763       C  
ATOM   5521  CE2 PHE F  66      -8.647   2.423  17.290  1.00 83.57           C  
ANISOU 5521  CE2 PHE F  66     9799  15189   6766   1639   1323   3026       C  
ATOM   5522  CZ  PHE F  66      -7.430   2.097  16.743  1.00 79.06           C  
ANISOU 5522  CZ  PHE F  66     9418  14293   6327   1595   1095   2893       C  
ATOM   5523  N   SER F  67      -6.585   3.357  23.857  1.00 89.58           N  
ANISOU 5523  N   SER F  67    11555  17059   5421   4051   1332   3097       N  
ATOM   5524  CA  SER F  67      -6.342   4.065  25.102  1.00 91.90           C  
ANISOU 5524  CA  SER F  67    11976  17687   5257   4628   1236   2947       C  
ATOM   5525  C   SER F  67      -4.843   4.320  25.223  1.00 94.42           C  
ANISOU 5525  C   SER F  67    12465  17880   5529   4890    816   2590       C  
ATOM   5526  O   SER F  67      -4.046   3.559  24.678  1.00 91.40           O  
ANISOU 5526  O   SER F  67    12184  17197   5346   4706    718   2615       O  
ATOM   5527  CB  SER F  67      -6.841   3.254  26.302  1.00 99.58           C  
ANISOU 5527  CB  SER F  67    13160  18875   5800   4906   1608   3378       C  
ATOM   5528  OG  SER F  67      -6.368   1.916  26.254  1.00106.66           O  
ANISOU 5528  OG  SER F  67    14306  19488   6730   4777   1731   3684       O  
ATOM   5529  N   GLY F  68      -4.487   5.363  25.968  1.00 92.53           N  
ANISOU 5529  N   GLY F  68    12249  17887   5021   5330    575   2251       N  
ATOM   5530  CA  GLY F  68      -3.104   5.735  26.232  1.00 90.99           C  
ANISOU 5530  CA  GLY F  68    12171  17645   4758   5621    158   1855       C  
ATOM   5531  C   GLY F  68      -2.847   5.853  27.721  1.00 97.18           C  
ANISOU 5531  C   GLY F  68    13186  18761   4978   6264    106   1820       C  
ATOM   5532  O   GLY F  68      -3.752   6.191  28.480  1.00 98.09           O  
ANISOU 5532  O   GLY F  68    13316  19183   4772   6516    318   1957       O  
ATOM   5533  N   SER F  69      -1.608   5.581  28.147  1.00 94.91           N  
ANISOU 5533  N   SER F  69    13072  18438   4550   6560   -185   1620       N  
ATOM   5534  CA  SER F  69      -1.194   5.712  29.544  1.00 98.93           C  
ANISOU 5534  CA  SER F  69    13815  19268   4507   7228   -317   1513       C  
ATOM   5535  C   SER F  69       0.254   6.215  29.613  1.00 99.65           C  
ANISOU 5535  C   SER F  69    13893  19323   4647   7449   -836    972       C  
ATOM   5536  O   SER F  69       0.998   6.082  28.642  1.00 96.28           O  
ANISOU 5536  O   SER F  69    13334  18604   4642   7091  -1010    811       O  
ATOM   5537  CB  SER F  69      -1.337   4.374  30.268  1.00107.77           C  
ANISOU 5537  CB  SER F  69    15255  20435   5258   7457     -3   2021       C  
ATOM   5538  OG  SER F  69      -2.639   3.832  30.097  1.00118.98           O  
ANISOU 5538  OG  SER F  69    16646  21844   6718   7153    499   2525       O  
ATOM   5539  N   GLY F  70       0.622   6.823  30.733  1.00 97.62           N  
ANISOU 5539  N   GLY F  70    13748  19375   3968   8028  -1079    675       N  
ATOM   5540  CA  GLY F  70       1.981   7.298  30.953  1.00 97.13           C  
ANISOU 5540  CA  GLY F  70    13654  19332   3919   8283  -1587    129       C  
ATOM   5541  C   GLY F  70       2.172   8.719  31.445  1.00101.15           C  
ANISOU 5541  C   GLY F  70    14056  20031   4344   8555  -1938   -430       C  
ATOM   5542  O   GLY F  70       1.315   9.593  31.297  1.00 98.39           O  
ANISOU 5542  O   GLY F  70    13597  19718   4067   8435  -1842   -484       O  
ATOM   5543  N   SER F  71       3.349   8.937  32.030  1.00101.56           N  
ANISOU 5543  N   SER F  71    14139  20199   4250   8936  -2372   -875       N  
ATOM   5544  CA  SER F  71       3.815  10.225  32.528  1.00103.06           C  
ANISOU 5544  CA  SER F  71    14232  20536   4392   9206  -2798  -1501       C  
ATOM   5545  C   SER F  71       5.339  10.233  32.446  1.00110.72           C  
ANISOU 5545  C   SER F  71    15077  21446   5545   9262  -3264  -1985       C  
ATOM   5546  O   SER F  71       5.947   9.171  32.325  1.00110.37           O  
ANISOU 5546  O   SER F  71    15100  21355   5481   9289  -3248  -1796       O  
ATOM   5547  CB  SER F  71       3.377  10.442  33.976  1.00106.56           C  
ANISOU 5547  CB  SER F  71    14929  21400   4160   9917  -2810  -1512       C  
ATOM   5548  OG  SER F  71       3.818   9.386  34.813  1.00107.76           O  
ANISOU 5548  OG  SER F  71    15349  21752   3841  10405  -2798  -1294       O  
ATOM   5549  N   GLY F  72       5.923  11.424  32.518  1.00110.17           N  
ANISOU 5549  N   GLY F  72    14827  21381   5654   9284  -3669  -2608       N  
ATOM   5550  CA  GLY F  72       7.368  11.625  32.493  1.00111.26           C  
ANISOU 5550  CA  GLY F  72    14777  21499   5999   9325  -4142  -3160       C  
ATOM   5551  C   GLY F  72       8.010  11.389  31.145  1.00109.84           C  
ANISOU 5551  C   GLY F  72    14328  20957   6450   8683  -4124  -3176       C  
ATOM   5552  O   GLY F  72       7.944  12.244  30.263  1.00104.53           O  
ANISOU 5552  O   GLY F  72    13442  20012   6261   8186  -4131  -3369       O  
ATOM   5553  N   THR F  73       8.703  10.245  31.020  1.00107.78           N  
ANISOU 5553  N   THR F  73    14095  20699   6159   8741  -4119  -2995       N  
ATOM   5554  CA  THR F  73       9.418   9.843  29.815  1.00104.46           C  
ANISOU 5554  CA  THR F  73    13439  19983   6266   8224  -4107  -2997       C  
ATOM   5555  C   THR F  73       8.891   8.558  29.166  1.00105.30           C  
ANISOU 5555  C   THR F  73    13701  19910   6399   7985  -3682  -2346       C  
ATOM   5556  O   THR F  73       9.274   8.321  28.034  1.00102.00           O  
ANISOU 5556  O   THR F  73    13098  19216   6442   7501  -3618  -2314       O  
ATOM   5557  CB  THR F  73      10.906   9.661  30.162  1.00110.98           C  
ANISOU 5557  CB  THR F  73    14108  20970   7089   8506  -4550  -3469       C  
ATOM   5558  OG1 THR F  73      11.027   8.795  31.291  1.00112.04           O  
ANISOU 5558  OG1 THR F  73    14535  21422   6611   9183  -4611  -3310       O  
ATOM   5559  CG2 THR F  73      11.603  10.976  30.448  1.00108.73           C  
ANISOU 5559  CG2 THR F  73    13560  20762   6992   8534  -4991  -4191       C  
ATOM   5560  N   ASP F  74       8.076   7.715  29.856  1.00103.12           N  
ANISOU 5560  N   ASP F  74    13761  19773   5647   8313  -3392  -1841       N  
ATOM   5561  CA  ASP F  74       7.582   6.445  29.298  1.00100.65           C  
ANISOU 5561  CA  ASP F  74    13618  19262   5362   8085  -2993  -1231       C  
ATOM   5562  C   ASP F  74       6.085   6.528  29.021  1.00 99.43           C  
ANISOU 5562  C   ASP F  74    13540  19016   5222   7795  -2554   -787       C  
ATOM   5563  O   ASP F  74       5.307   6.783  29.932  1.00 98.10           O  
ANISOU 5563  O   ASP F  74    13538  19087   4646   8134  -2435   -661       O  
ATOM   5564  CB  ASP F  74       7.869   5.268  30.246  1.00106.65           C  
ANISOU 5564  CB  ASP F  74    14719  20210   5595   8654  -2967   -960       C  
ATOM   5565  CG  ASP F  74       9.335   4.899  30.372  1.00128.49           C  
ANISOU 5565  CG  ASP F  74    17413  23051   8356   8932  -3363  -1319       C  
ATOM   5566  OD1 ASP F  74      10.189   5.796  30.215  1.00131.37           O  
ANISOU 5566  OD1 ASP F  74    17462  23476   8979   8877  -3750  -1908       O  
ATOM   5567  OD2 ASP F  74       9.626   3.723  30.696  1.00138.61           O  
ANISOU 5567  OD2 ASP F  74    18960  24344   9360   9233  -3290  -1022       O  
ATOM   5568  N   PHE F  75       5.688   6.294  27.757  1.00 93.43           N  
ANISOU 5568  N   PHE F  75    12649  17931   4917   7188  -2316   -557       N  
ATOM   5569  CA  PHE F  75       4.289   6.373  27.328  1.00 91.82           C  
ANISOU 5569  CA  PHE F  75    12453  17635   4801   6855  -1923   -175       C  
ATOM   5570  C   PHE F  75       3.866   5.147  26.557  1.00 92.60           C  
ANISOU 5570  C   PHE F  75    12639  17478   5068   6495  -1580    332       C  
ATOM   5571  O   PHE F  75       4.655   4.596  25.798  1.00 90.97           O  
ANISOU 5571  O   PHE F  75    12376  17048   5140   6277  -1670    291       O  
ATOM   5572  CB  PHE F  75       4.071   7.628  26.499  1.00 90.75           C  
ANISOU 5572  CB  PHE F  75    12040  17360   5079   6459  -2013   -487       C  
ATOM   5573  CG  PHE F  75       4.279   8.865  27.329  1.00 95.32           C  
ANISOU 5573  CG  PHE F  75    12574  18168   5474   6811  -2312   -957       C  
ATOM   5574  CD1 PHE F  75       5.544   9.413  27.478  1.00100.22           C  
ANISOU 5574  CD1 PHE F  75    13066  18810   6203   6942  -2738  -1496       C  
ATOM   5575  CD2 PHE F  75       3.238   9.406  28.066  1.00 99.45           C  
ANISOU 5575  CD2 PHE F  75    13196  18916   5675   7064  -2175   -867       C  
ATOM   5576  CE1 PHE F  75       5.745  10.524  28.288  1.00104.05           C  
ANISOU 5576  CE1 PHE F  75    13526  19492   6515   7276  -3037  -1958       C  
ATOM   5577  CE2 PHE F  75       3.423  10.555  28.819  1.00105.14           C  
ANISOU 5577  CE2 PHE F  75    13901  19830   6219   7407  -2467  -1323       C  
ATOM   5578  CZ  PHE F  75       4.679  11.105  28.937  1.00104.74           C  
ANISOU 5578  CZ  PHE F  75    13734  19761   6300   7508  -2907  -1873       C  
ATOM   5579  N   THR F  76       2.622   4.713  26.771  1.00 88.84           N  
ANISOU 5579  N   THR F  76    12292  17041   4421   6440  -1186    798       N  
ATOM   5580  CA  THR F  76       2.074   3.526  26.142  1.00 87.31           C  
ANISOU 5580  CA  THR F  76    12198  16603   4374   6093   -835   1294       C  
ATOM   5581  C   THR F  76       0.726   3.814  25.493  1.00 88.62           C  
ANISOU 5581  C   THR F  76    12204  16703   4766   5656   -523   1523       C  
ATOM   5582  O   THR F  76      -0.124   4.459  26.113  1.00 89.53           O  
ANISOU 5582  O   THR F  76    12292  17068   4656   5824   -405   1553       O  
ATOM   5583  CB  THR F  76       1.953   2.411  27.187  1.00100.71           C  
ANISOU 5583  CB  THR F  76    14258  18414   5595   6500   -628   1698       C  
ATOM   5584  OG1 THR F  76       3.268   2.008  27.569  1.00100.80           O  
ANISOU 5584  OG1 THR F  76    14408  18444   5448   6873   -937   1486       O  
ATOM   5585  CG2 THR F  76       1.175   1.199  26.671  1.00100.76           C  
ANISOU 5585  CG2 THR F  76    14395  18158   5731   6130   -207   2251       C  
ATOM   5586  N   LEU F  77       0.548   3.325  24.241  1.00 80.55           N  
ANISOU 5586  N   LEU F  77    11073  15360   4171   5127   -403   1669       N  
ATOM   5587  CA  LEU F  77      -0.702   3.365  23.503  1.00 78.35           C  
ANISOU 5587  CA  LEU F  77    10641  14996   4133   4688   -112   1907       C  
ATOM   5588  C   LEU F  77      -1.128   1.926  23.433  1.00 87.41           C  
ANISOU 5588  C   LEU F  77    11975  15973   5264   4521    210   2397       C  
ATOM   5589  O   LEU F  77      -0.386   1.093  22.910  1.00 87.14           O  
ANISOU 5589  O   LEU F  77    12050  15675   5384   4405    139   2438       O  
ATOM   5590  CB  LEU F  77      -0.544   3.923  22.072  1.00 73.15           C  
ANISOU 5590  CB  LEU F  77     9731  14090   3974   4224   -250   1665       C  
ATOM   5591  CG  LEU F  77      -1.794   3.849  21.155  1.00 74.48           C  
ANISOU 5591  CG  LEU F  77     9734  14151   4413   3762     19   1900       C  
ATOM   5592  CD1 LEU F  77      -2.815   4.922  21.526  1.00 74.52           C  
ANISOU 5592  CD1 LEU F  77     9589  14427   4297   3858     96   1834       C  
ATOM   5593  CD2 LEU F  77      -1.415   3.996  19.703  1.00 69.27           C  
ANISOU 5593  CD2 LEU F  77     8924  13190   4207   3342   -111   1728       C  
ATOM   5594  N   THR F  78      -2.314   1.630  23.957  1.00 87.82           N  
ANISOU 5594  N   THR F  78    12066  16171   5131   4514    570   2763       N  
ATOM   5595  CA  THR F  78      -2.871   0.288  23.959  1.00 90.30           C  
ANISOU 5595  CA  THR F  78    12558  16311   5442   4314    932   3258       C  
ATOM   5596  C   THR F  78      -4.007   0.201  22.927  1.00 93.33           C  
ANISOU 5596  C   THR F  78    12681  16560   6218   3737   1163   3414       C  
ATOM   5597  O   THR F  78      -4.682   1.197  22.681  1.00 92.02           O  
ANISOU 5597  O   THR F  78    12243  16579   6141   3648   1149   3247       O  
ATOM   5598  CB  THR F  78      -3.368  -0.034  25.383  1.00 97.65           C  
ANISOU 5598  CB  THR F  78    13723  17519   5860   4733   1210   3580       C  
ATOM   5599  OG1 THR F  78      -2.264   0.005  26.292  1.00 96.04           O  
ANISOU 5599  OG1 THR F  78    13771  17442   5277   5301    955   3409       O  
ATOM   5600  CG2 THR F  78      -4.044  -1.377  25.479  1.00 94.87           C  
ANISOU 5600  CG2 THR F  78    13567  16977   5500   4508   1643   4127       C  
ATOM   5601  N   ILE F  79      -4.206  -0.990  22.333  1.00 90.95           N  
ANISOU 5601  N   ILE F  79    12476  15940   6142   3373   1359   3716       N  
ATOM   5602  CA  ILE F  79      -5.330  -1.300  21.443  1.00 90.47           C  
ANISOU 5602  CA  ILE F  79    12190  15748   6434   2829   1599   3898       C  
ATOM   5603  C   ILE F  79      -5.897  -2.620  21.981  1.00100.97           C  
ANISOU 5603  C   ILE F  79    13755  16955   7655   2731   2005   4406       C  
ATOM   5604  O   ILE F  79      -5.577  -3.692  21.458  1.00100.25           O  
ANISOU 5604  O   ILE F  79    13847  16487   7754   2494   2042   4563       O  
ATOM   5605  CB  ILE F  79      -4.991  -1.396  19.932  1.00 89.35           C  
ANISOU 5605  CB  ILE F  79    11909  15276   6765   2400   1396   3695       C  
ATOM   5606  CG1 ILE F  79      -4.091  -0.228  19.465  1.00 85.52           C  
ANISOU 5606  CG1 ILE F  79    11291  14842   6363   2542    995   3213       C  
ATOM   5607  CG2 ILE F  79      -6.306  -1.455  19.126  1.00 90.04           C  
ANISOU 5607  CG2 ILE F  79    11705  15340   7165   1910   1609   3817       C  
ATOM   5608  CD1 ILE F  79      -3.711  -0.282  17.934  1.00 81.73           C  
ANISOU 5608  CD1 ILE F  79    10688  14044   6321   2147    812   3019       C  
ATOM   5609  N   SER F  80      -6.695  -2.530  23.072  1.00102.94           N  
ANISOU 5609  N   SER F  80    14027  17515   7572   2946   2314   4661       N  
ATOM   5610  CA  SER F  80      -7.328  -3.662  23.770  1.00108.27           C  
ANISOU 5610  CA  SER F  80    14929  18119   8089   2887   2769   5180       C  
ATOM   5611  C   SER F  80      -7.621  -4.892  22.890  1.00112.91           C  
ANISOU 5611  C   SER F  80    15570  18250   9080   2328   2947   5430       C  
ATOM   5612  O   SER F  80      -7.257  -6.010  23.269  1.00116.03           O  
ANISOU 5612  O   SER F  80    16356  18368   9364   2382   3104   5737       O  
ATOM   5613  CB  SER F  80      -8.612  -3.210  24.467  1.00115.44           C  
ANISOU 5613  CB  SER F  80    15616  19429   8817   2915   3127   5374       C  
ATOM   5614  OG  SER F  80      -9.569  -2.724  23.540  1.00121.72           O  
ANISOU 5614  OG  SER F  80    15959  20292   9997   2464   3157   5248       O  
ATOM   5615  N   SER F  81      -8.238  -4.650  21.749  1.00105.97           N  
ANISOU 5615  N   SER F  81    14327  17287   8652   1822   2907   5285       N  
ATOM   5616  CA  SER F  81      -8.546  -5.693  20.821  1.00106.10           C  
ANISOU 5616  CA  SER F  81    14354  16877   9081   1274   3025   5449       C  
ATOM   5617  C   SER F  81      -8.459  -5.093  19.441  1.00105.35           C  
ANISOU 5617  C   SER F  81    13950  16684   9395    960   2700   5063       C  
ATOM   5618  O   SER F  81      -9.190  -4.178  19.126  1.00103.76           O  
ANISOU 5618  O   SER F  81    13362  16762   9300    846   2680   4891       O  
ATOM   5619  CB  SER F  81      -9.942  -6.218  21.069  1.00113.95           C  
ANISOU 5619  CB  SER F  81    15195  17928  10175    906   3510   5830       C  
ATOM   5620  OG  SER F  81     -10.268  -7.221  20.128  1.00122.61           O  
ANISOU 5620  OG  SER F  81    16274  18603  11710    343   3595   5938       O  
ATOM   5621  N   LEU F  82      -7.556  -5.612  18.624  1.00100.07           N  
ANISOU 5621  N   LEU F  82    13461  15629   8931    855   2451   4928       N  
ATOM   5622  CA  LEU F  82      -7.339  -5.123  17.264  1.00 95.27           C  
ANISOU 5622  CA  LEU F  82    12609  14906   8685    590   2143   4568       C  
ATOM   5623  C   LEU F  82      -8.451  -5.503  16.335  1.00100.55           C  
ANISOU 5623  C   LEU F  82    12996  15465   9742     29   2296   4635       C  
ATOM   5624  O   LEU F  82      -9.170  -6.447  16.588  1.00104.18           O  
ANISOU 5624  O   LEU F  82    13511  15791  10280   -243   2623   4968       O  
ATOM   5625  CB  LEU F  82      -6.074  -5.735  16.685  1.00 92.55           C  
ANISOU 5625  CB  LEU F  82    12538  14196   8433    651   1863   4419       C  
ATOM   5626  CG  LEU F  82      -4.743  -5.147  17.073  1.00 94.43           C  
ANISOU 5626  CG  LEU F  82    12934  14561   8384   1164   1590   4196       C  
ATOM   5627  CD1 LEU F  82      -3.633  -6.136  16.808  1.00 93.65           C  
ANISOU 5627  CD1 LEU F  82    13185  14110   8289   1276   1450   4208       C  
ATOM   5628  CD2 LEU F  82      -4.539  -3.878  16.295  1.00 93.26           C  
ANISOU 5628  CD2 LEU F  82    12489  14601   8343   1203   1291   3774       C  
ATOM   5629  N   GLU F  83      -8.565  -4.764  15.243  1.00 93.68           N  
ANISOU 5629  N   GLU F  83    11833  14645   9116   -135   2051   4305       N  
ATOM   5630  CA  GLU F  83      -9.553  -5.034  14.219  1.00 93.63           C  
ANISOU 5630  CA  GLU F  83    11523  14566   9486   -621   2086   4256       C  
ATOM   5631  C   GLU F  83      -8.824  -4.935  12.890  1.00 92.95           C  
ANISOU 5631  C   GLU F  83    11471  14210   9635   -721   1736   3946       C  
ATOM   5632  O   GLU F  83      -7.690  -4.493  12.869  1.00 89.17           O  
ANISOU 5632  O   GLU F  83    11158  13704   9017   -408   1501   3762       O  
ATOM   5633  CB  GLU F  83     -10.708  -4.055  14.306  1.00 20.00           C  
ATOM   5634  CG  GLU F  83     -11.921  -4.514  13.529  1.00 20.00           C  
ATOM   5635  CD  GLU F  83     -12.970  -5.162  14.395  1.00 20.00           C  
ATOM   5636  OE1 GLU F  83     -12.948  -4.925  15.607  1.00 20.00           O  
ATOM   5637  OE2 GLU F  83     -13.821  -5.901  13.866  1.00 20.00           O  
ATOM   5638  N   PRO F  84      -9.488  -5.389  11.762  1.00 90.46           N  
ANISOU 5638  N   PRO F  84    10990  13713   9666  -1135   1688   3865       N  
ATOM   5639  CA  PRO F  84      -8.714  -5.277  10.513  1.00 87.28           C  
ANISOU 5639  CA  PRO F  84    10635  13080   9445  -1184   1365   3571       C  
ATOM   5640  C   PRO F  84      -8.327  -3.849  10.156  1.00 87.93           C  
ANISOU 5640  C   PRO F  84    10554  13414   9442   -930   1117   3249       C  
ATOM   5641  O   PRO F  84      -7.293  -3.632   9.564  1.00 84.27           O  
ANISOU 5641  O   PRO F  84    10204  12783   9031   -848    876   3034       O  
ATOM   5642  CB  PRO F  84      -9.646  -5.846   9.457  1.00 90.55           C  
ANISOU 5642  CB  PRO F  84    10868  13321  10216  -1662   1384   3549       C  
ATOM   5643  CG  PRO F  84     -10.480  -6.808  10.175  1.00 99.38           C  
ANISOU 5643  CG  PRO F  84    11892  14492  11376  -1906   1734   3861       C  
ATOM   5644  CD  PRO F  84     -10.812  -6.059  11.405  1.00 95.83           C  
ANISOU 5644  CD  PRO F  84    11413  14409  10589  -1570   1918   4013       C  
ATOM   5645  N   GLU F  85      -9.170  -2.903  10.516  1.00 84.85           N  
ANISOU 5645  N   GLU F  85     9905  13416   8920   -804   1195   3224       N  
ATOM   5646  CA  GLU F  85      -8.948  -1.475  10.281  1.00 81.41           C  
ANISOU 5646  CA  GLU F  85     9333  13210   8387   -555    995   2944       C  
ATOM   5647  C   GLU F  85      -7.818  -0.882  11.164  1.00 82.55           C  
ANISOU 5647  C   GLU F  85     9685  13428   8250   -135    907   2879       C  
ATOM   5648  O   GLU F  85      -7.404   0.242  10.914  1.00 79.10           O  
ANISOU 5648  O   GLU F  85     9191  13097   7765     54    720   2626       O  
ATOM   5649  CB  GLU F  85     -10.273  -0.693  10.486  1.00 84.33           C  
ANISOU 5649  CB  GLU F  85     9352  13964   8727   -569   1108   2933       C  
ATOM   5650  CG  GLU F  85     -10.670  -0.453  11.936  1.00 97.52           C  
ANISOU 5650  CG  GLU F  85    10997  15946  10110   -330   1340   3125       C  
ATOM   5651  CD  GLU F  85     -12.127  -0.090  12.156  1.00114.06           C  
ANISOU 5651  CD  GLU F  85    12725  18402  12213   -422   1531   3188       C  
ATOM   5652  OE1 GLU F  85     -12.820  -0.837  12.883  1.00 92.96           O  
ANISOU 5652  OE1 GLU F  85     9992  15814   9516   -561   1838   3476       O  
ATOM   5653  OE2 GLU F  85     -12.564   0.966  11.644  1.00111.99           O  
ANISOU 5653  OE2 GLU F  85    12238  18344  11967   -336   1386   2955       O  
ATOM   5654  N   ASP F  86      -7.346  -1.597  12.204  1.00 80.36           N  
ANISOU 5654  N   ASP F  86     9647  13102   7785     21   1036   3095       N  
ATOM   5655  CA  ASP F  86      -6.289  -1.081  13.089  1.00 78.39           C  
ANISOU 5655  CA  ASP F  86     9578  12952   7256    443    926   3007       C  
ATOM   5656  C   ASP F  86      -4.863  -1.345  12.583  1.00 76.79           C  
ANISOU 5656  C   ASP F  86     9586  12477   7115    525    693   2842       C  
ATOM   5657  O   ASP F  86      -3.921  -0.727  13.082  1.00 74.53           O  
ANISOU 5657  O   ASP F  86     9375  12285   6658    846    538   2670       O  
ATOM   5658  CB  ASP F  86      -6.447  -1.670  14.493  1.00 84.05           C  
ANISOU 5658  CB  ASP F  86    10463  13787   7686    645   1165   3309       C  
ATOM   5659  CG  ASP F  86      -7.750  -1.325  15.172  1.00101.57           C  
ANISOU 5659  CG  ASP F  86    12469  16337   9787    635   1423   3474       C  
ATOM   5660  OD1 ASP F  86      -8.504  -0.484  14.626  1.00102.92           O  
ANISOU 5660  OD1 ASP F  86    12343  16689  10075    528   1379   3313       O  
ATOM   5661  OD2 ASP F  86      -8.027  -1.900  16.248  1.00109.13           O  
ANISOU 5661  OD2 ASP F  86    13561  17383  10521    755   1679   3770       O  
ATOM   5662  N   PHE F  87      -4.688  -2.246  11.614  1.00 71.54           N  
ANISOU 5662  N   PHE F  87     9002  11491   6690    252    663   2871       N  
ATOM   5663  CA  PHE F  87      -3.357  -2.562  11.105  1.00 68.98           C  
ANISOU 5663  CA  PHE F  87     8863  10927   6419    342    462   2720       C  
ATOM   5664  C   PHE F  87      -2.922  -1.359  10.290  1.00 68.28           C  
ANISOU 5664  C   PHE F  87     8604  10909   6432    369    249   2385       C  
ATOM   5665  O   PHE F  87      -3.552  -1.028   9.287  1.00 66.83           O  
ANISOU 5665  O   PHE F  87     8258  10692   6442    130    225   2299       O  
ATOM   5666  CB  PHE F  87      -3.370  -3.881  10.315  1.00 71.72           C  
ANISOU 5666  CB  PHE F  87     9365  10911   6977     61    501   2847       C  
ATOM   5667  CG  PHE F  87      -3.757  -5.052  11.197  1.00 77.51           C  
ANISOU 5667  CG  PHE F  87    10314  11530   7608     36    737   3200       C  
ATOM   5668  CD1 PHE F  87      -2.826  -5.653  12.031  1.00 81.09           C  
ANISOU 5668  CD1 PHE F  87    11074  11899   7839    344    736   3311       C  
ATOM   5669  CD2 PHE F  87      -5.072  -5.488  11.264  1.00 82.28           C  
ANISOU 5669  CD2 PHE F  87    10805  12137   8319   -273    975   3422       C  
ATOM   5670  CE1 PHE F  87      -3.186  -6.713  12.853  1.00 85.40           C  
ANISOU 5670  CE1 PHE F  87    11867  12313   8266    343    979   3664       C  
ATOM   5671  CE2 PHE F  87      -5.429  -6.548  12.086  1.00 88.28           C  
ANISOU 5671  CE2 PHE F  87    11780  12767   8996   -320   1235   3771       C  
ATOM   5672  CZ  PHE F  87      -4.484  -7.153  12.876  1.00 87.52           C  
ANISOU 5672  CZ  PHE F  87    12041  12547   8665     -4   1243   3904       C  
ATOM   5673  N   ALA F  88      -1.958  -0.604  10.839  1.00 62.39           N  
ANISOU 5673  N   ALA F  88     7882  10291   5532    677    109   2199       N  
ATOM   5674  CA  ALA F  88      -1.491   0.671  10.285  1.00 58.41           C  
ANISOU 5674  CA  ALA F  88     7233   9857   5104    725    -65   1888       C  
ATOM   5675  C   ALA F  88      -0.194   1.081  10.990  1.00 62.01           C  
ANISOU 5675  C   ALA F  88     7758  10389   5416   1044   -222   1699       C  
ATOM   5676  O   ALA F  88       0.303   0.331  11.842  1.00 64.16           O  
ANISOU 5676  O   ALA F  88     8193  10671   5514   1249   -209   1812       O  
ATOM   5677  CB  ALA F  88      -2.561   1.738  10.531  1.00 59.00           C  
ANISOU 5677  CB  ALA F  88     7119  10178   5122    734     -7   1857       C  
ATOM   5678  N   VAL F  89       0.338   2.275  10.679  1.00 56.27           N  
ANISOU 5678  N   VAL F  89     6909   9716   4755   1097   -369   1408       N  
ATOM   5679  CA  VAL F  89       1.511   2.787  11.396  1.00 55.70           C  
ANISOU 5679  CA  VAL F  89     6847   9746   4572   1379   -533   1180       C  
ATOM   5680  C   VAL F  89       0.980   3.684  12.524  1.00 61.80           C  
ANISOU 5680  C   VAL F  89     7568  10791   5122   1608   -532   1134       C  
ATOM   5681  O   VAL F  89      -0.078   4.298  12.366  1.00 60.71           O  
ANISOU 5681  O   VAL F  89     7337  10733   4997   1513   -445   1175       O  
ATOM   5682  CB  VAL F  89       2.464   3.582  10.485  1.00 20.00           C  
ATOM   5683  CG1 VAL F  89       3.566   4.234  11.305  1.00 20.00           C  
ATOM   5684  CG2 VAL F  89       3.053   2.677   9.412  1.00 20.00           C  
ATOM   5685  N   TYR F  90       1.688   3.722  13.672  1.00 59.93           N  
ANISOU 5685  N   TYR F  90     7397  10713   4659   1942   -636   1043       N  
ATOM   5686  CA  TYR F  90       1.302   4.554  14.801  1.00 61.27           C  
ANISOU 5686  CA  TYR F  90     7545  11151   4585   2216   -662    965       C  
ATOM   5687  C   TYR F  90       2.475   5.423  15.211  1.00 64.76           C  
ANISOU 5687  C   TYR F  90     7930  11667   5011   2432   -918    581       C  
ATOM   5688  O   TYR F  90       3.584   4.907  15.356  1.00 64.07           O  
ANISOU 5688  O   TYR F  90     7880  11546   4918   2551  -1047    479       O  
ATOM   5689  CB  TYR F  90       0.867   3.679  15.955  1.00 66.15           C  
ANISOU 5689  CB  TYR F  90     8324  11925   4885   2454   -523   1252       C  
ATOM   5690  CG  TYR F  90      -0.457   3.023  15.676  1.00 68.65           C  
ANISOU 5690  CG  TYR F  90     8647  12204   5231   2214   -246   1608       C  
ATOM   5691  CD1 TYR F  90      -0.525   1.803  15.016  1.00 70.94           C  
ANISOU 5691  CD1 TYR F  90     9030  12253   5671   1968   -131   1841       C  
ATOM   5692  CD2 TYR F  90      -1.646   3.668  15.972  1.00 70.35           C  
ANISOU 5692  CD2 TYR F  90     8751  12618   5361   2211   -113   1678       C  
ATOM   5693  CE1 TYR F  90      -1.748   1.237  14.667  1.00 73.31           C  
ANISOU 5693  CE1 TYR F  90     9296  12501   6056   1691    107   2124       C  
ATOM   5694  CE2 TYR F  90      -2.873   3.126  15.607  1.00 72.38           C  
ANISOU 5694  CE2 TYR F  90     8944  12859   5697   1948    131   1963       C  
ATOM   5695  CZ  TYR F  90      -2.921   1.909  14.954  1.00 79.15           C  
ANISOU 5695  CZ  TYR F  90     9879  13467   6729   1671    237   2179       C  
ATOM   5696  OH  TYR F  90      -4.146   1.359  14.684  1.00 79.31           O  
ANISOU 5696  OH  TYR F  90     9814  13481   6838   1400    473   2440       O  
ATOM   5697  N   TYR F  91       2.241   6.743  15.369  1.00 60.57           N  
ANISOU 5697  N   TYR F  91     7299  11227   4487   2479  -1000    348       N  
ATOM   5698  CA  TYR F  91       3.288   7.699  15.739  1.00 60.83           C  
ANISOU 5698  CA  TYR F  91     7258  11305   4549   2637  -1249    -57       C  
ATOM   5699  C   TYR F  91       2.995   8.401  17.028  1.00 66.19           C  
ANISOU 5699  C   TYR F  91     7972  12248   4930   2995  -1336   -184       C  
ATOM   5700  O   TYR F  91       1.864   8.781  17.242  1.00 64.06           O  
ANISOU 5700  O   TYR F  91     7720  12079   4542   3025  -1205    -53       O  
ATOM   5701  CB  TYR F  91       3.400   8.789  14.667  1.00 59.40           C  
ANISOU 5701  CB  TYR F  91     6958  10925   4688   2353  -1288   -275       C  
ATOM   5702  CG  TYR F  91       3.998   8.318  13.372  1.00 58.60           C  
ANISOU 5702  CG  TYR F  91     6808  10570   4886   2038  -1249   -251       C  
ATOM   5703  CD1 TYR F  91       5.372   8.184  13.228  1.00 61.37           C  
ANISOU 5703  CD1 TYR F  91     7081  10864   5373   2039  -1395   -478       C  
ATOM   5704  CD2 TYR F  91       3.204   8.123  12.247  1.00 56.52           C  
ANISOU 5704  CD2 TYR F  91     6556  10142   4777   1752  -1079    -41       C  
ATOM   5705  CE1 TYR F  91       5.937   7.798  12.015  1.00 60.40           C  
ANISOU 5705  CE1 TYR F  91     6909  10529   5513   1771  -1342   -463       C  
ATOM   5706  CE2 TYR F  91       3.757   7.762  11.027  1.00 54.67           C  
ANISOU 5706  CE2 TYR F  91     6295   9684   4795   1494  -1047    -39       C  
ATOM   5707  CZ  TYR F  91       5.121   7.586  10.913  1.00 59.22           C  
ANISOU 5707  CZ  TYR F  91     6807  10207   5487   1505  -1164   -237       C  
ATOM   5708  OH  TYR F  91       5.664   7.209   9.702  1.00 54.12           O  
ANISOU 5708  OH  TYR F  91     6133   9361   5068   1274  -1111   -226       O  
ATOM   5709  N   CYS F  92       4.036   8.680  17.826  1.00 66.96           N  
ANISOU 5709  N   CYS F  92     8055  12463   4923   3270  -1578   -490       N  
ATOM   5710  CA  CYS F  92       3.932   9.483  19.050  1.00 69.89           C  
ANISOU 5710  CA  CYS F  92     8460  13083   5012   3645  -1725   -706       C  
ATOM   5711  C   CYS F  92       4.554  10.869  18.724  1.00 70.94           C  
ANISOU 5711  C   CYS F  92     8455  13095   5402   3534  -1941  -1162       C  
ATOM   5712  O   CYS F  92       5.432  10.965  17.859  1.00 67.94           O  
ANISOU 5712  O   CYS F  92     7953  12508   5353   3264  -2014  -1331       O  
ATOM   5713  CB  CYS F  92       4.656   8.817  20.216  1.00 73.85           C  
ANISOU 5713  CB  CYS F  92     9057  13810   5192   4067  -1872   -755       C  
ATOM   5714  SG  CYS F  92       6.446   8.727  19.988  1.00 78.63           S  
ANISOU 5714  SG  CYS F  92     9512  14346   6016   4066  -2179  -1151       S  
ATOM   5715  N   GLN F  93       4.086  11.924  19.406  1.00 67.85           N  
ANISOU 5715  N   GLN F  93     8095  12825   4861   3738  -2026  -1352       N  
ATOM   5716  CA  GLN F  93       4.544  13.303  19.206  1.00 66.55           C  
ANISOU 5716  CA  GLN F  93     7848  12516   4924   3646  -2219  -1779       C  
ATOM   5717  C   GLN F  93       4.578  14.041  20.549  1.00 71.08           C  
ANISOU 5717  C   GLN F  93     8483  13330   5196   4081  -2443  -2083       C  
ATOM   5718  O   GLN F  93       3.635  13.893  21.328  1.00 69.90           O  
ANISOU 5718  O   GLN F  93     8459  13419   4682   4382  -2341  -1885       O  
ATOM   5719  CB  GLN F  93       3.557  14.019  18.276  1.00 65.63           C  
ANISOU 5719  CB  GLN F  93     7753  12198   4986   3375  -2040  -1657       C  
ATOM   5720  CG  GLN F  93       3.969  15.428  17.840  1.00 75.36           C  
ANISOU 5720  CG  GLN F  93     8950  13181   6501   3211  -2182  -2037       C  
ATOM   5721  CD  GLN F  93       2.911  16.457  18.172  1.00 86.50           C  
ANISOU 5721  CD  GLN F  93    10479  14629   7760   3383  -2164  -2083       C  
ATOM   5722  OE1 GLN F  93       1.728  16.244  17.937  1.00 75.32           O  
ANISOU 5722  OE1 GLN F  93     9116  13285   6216   3394  -1954  -1768       O  
ATOM   5723  NE2 GLN F  93       3.297  17.586  18.758  1.00 86.81           N  
ANISOU 5723  NE2 GLN F  93    10552  14628   7804   3536  -2392  -2494       N  
ATOM   5724  N   HIS F  94       5.621  14.868  20.799  1.00 69.98           N  
ANISOU 5724  N   HIS F  94     8247  13129   5212   4107  -2739  -2573       N  
ATOM   5725  CA  HIS F  94       5.695  15.653  22.032  1.00 73.93           C  
ANISOU 5725  CA  HIS F  94     8808  13835   5446   4518  -2995  -2928       C  
ATOM   5726  C   HIS F  94       5.432  17.108  21.688  1.00 77.96           C  
ANISOU 5726  C   HIS F  94     9335  14107   6180   4360  -3060  -3211       C  
ATOM   5727  O   HIS F  94       5.648  17.522  20.535  1.00 73.40           O  
ANISOU 5727  O   HIS F  94     8684  13191   6014   3923  -2976  -3232       O  
ATOM   5728  CB  HIS F  94       7.064  15.528  22.768  1.00 77.50           C  
ANISOU 5728  CB  HIS F  94     9144  14433   5868   4736  -3338  -3336       C  
ATOM   5729  CG  HIS F  94       8.124  16.487  22.297  1.00 81.55           C  
ANISOU 5729  CG  HIS F  94     9462  14700   6824   4441  -3566  -3830       C  
ATOM   5730  ND1 HIS F  94       9.074  16.120  21.361  1.00 82.13           N  
ANISOU 5730  ND1 HIS F  94     9332  14587   7288   4061  -3543  -3867       N  
ATOM   5731  CD2 HIS F  94       8.308  17.789  22.607  1.00 85.27           C  
ANISOU 5731  CD2 HIS F  94     9922  15064   7413   4455  -3786  -4281       C  
ATOM   5732  CE1 HIS F  94       9.806  17.204  21.149  1.00 83.28           C  
ANISOU 5732  CE1 HIS F  94     9330  14531   7780   3841  -3731  -4327       C  
ATOM   5733  NE2 HIS F  94       9.379  18.228  21.883  1.00 85.68           N  
ANISOU 5733  NE2 HIS F  94     9754  14858   7943   4059  -3890  -4593       N  
ATOM   5734  N   SER F  95       5.060  17.894  22.721  1.00 78.37           N  
ANISOU 5734  N   SER F  95     9501  14326   5949   4744  -3225  -3453       N  
ATOM   5735  CA  SER F  95       4.906  19.344  22.595  1.00 80.53           C  
ANISOU 5735  CA  SER F  95     9834  14368   6397   4675  -3345  -3793       C  
ATOM   5736  C   SER F  95       5.131  20.107  23.938  1.00 90.37           C  
ANISOU 5736  C   SER F  95    11160  15814   7361   5143  -3680  -4254       C  
ATOM   5737  O   SER F  95       4.584  21.192  24.147  1.00 89.83           O  
ANISOU 5737  O   SER F  95    11228  15653   7250   5261  -3744  -4448       O  
ATOM   5738  CB  SER F  95       3.577  19.712  21.935  1.00 80.07           C  
ANISOU 5738  CB  SER F  95     9900  14191   6331   4568  -3064  -3472       C  
ATOM   5739  OG  SER F  95       2.457  19.424  22.754  1.00 87.12           O  
ANISOU 5739  OG  SER F  95    10913  15431   6758   4978  -2944  -3225       O  
ATOM   5740  N   ARG F  96       5.999  19.574  24.807  1.00 92.33           N  
ANISOU 5740  N   ARG F  96    11333  16321   7429   5418  -3919  -4463       N  
ATOM   5741  CA  ARG F  96       6.386  20.269  26.034  1.00 98.37           C  
ANISOU 5741  CA  ARG F  96    12151  17274   7949   5856  -4289  -4963       C  
ATOM   5742  C   ARG F  96       7.389  21.380  25.690  1.00105.46           C  
ANISOU 5742  C   ARG F  96    12912  17834   9325   5543  -4576  -5538       C  
ATOM   5743  O   ARG F  96       7.559  22.312  26.471  1.00109.53           O  
ANISOU 5743  O   ARG F  96    13493  18371   9752   5798  -4879  -6011       O  
ATOM   5744  CB  ARG F  96       7.027  19.297  27.038  1.00103.99           C  
ANISOU 5744  CB  ARG F  96    12827  18385   8300   6275  -4465  -5002       C  
ATOM   5745  N   ASP F  97       8.049  21.277  24.529  1.00100.81           N  
ANISOU 5745  N   ASP F  97    12136  16929   9239   4992  -4470  -5502       N  
ATOM   5746  CA  ASP F  97       9.073  22.217  24.089  1.00103.38           C  
ANISOU 5746  CA  ASP F  97    12294  16913  10074   4612  -4675  -5996       C  
ATOM   5747  C   ASP F  97       9.121  22.254  22.560  1.00101.90           C  
ANISOU 5747  C   ASP F  97    12033  16318  10365   4001  -4365  -5730       C  
ATOM   5748  O   ASP F  97       8.740  21.266  21.932  1.00 99.02           O  
ANISOU 5748  O   ASP F  97    11661  16016   9948   3894  -4080  -5240       O  
ATOM   5749  CB  ASP F  97      10.431  21.716  24.643  1.00108.78           C  
ANISOU 5749  CB  ASP F  97    12704  17824  10803   4708  -4990  -6365       C  
ATOM   5750  CG  ASP F  97      11.651  22.450  24.132  1.00123.04           C  
ANISOU 5750  CG  ASP F  97    14239  19326  13186   4254  -5173  -6857       C  
ATOM   5751  OD1 ASP F  97      11.593  23.700  24.032  1.00126.00           O  
ANISOU 5751  OD1 ASP F  97    14691  19376  13808   4075  -5263  -7181       O  
ATOM   5752  OD2 ASP F  97      12.659  21.777  23.821  1.00127.82           O  
ANISOU 5752  OD2 ASP F  97    14555  20010  14001   4074  -5215  -6918       O  
ATOM   5753  N   LEU F  98       9.589  23.373  21.961  1.00 97.66           N  
ANISOU 5753  N   LEU F  98    11460  15356  10289   3606  -4415  -6051       N  
ATOM   5754  CA  LEU F  98       9.766  23.454  20.511  1.00 94.31           C  
ANISOU 5754  CA  LEU F  98    10975  14540  10319   3037  -4122  -5828       C  
ATOM   5755  C   LEU F  98      11.277  23.268  20.230  1.00 96.40           C  
ANISOU 5755  C   LEU F  98    10882  14754  10990   2708  -4253  -6147       C  
ATOM   5756  O   LEU F  98      12.090  23.691  21.046  1.00 98.15           O  
ANISOU 5756  O   LEU F  98    10950  15072  11271   2824  -4599  -6671       O  
ATOM   5757  CB  LEU F  98       9.258  24.786  19.954  1.00 20.00           C  
ATOM   5758  CG  LEU F  98       7.748  25.022  20.034  1.00 20.00           C  
ATOM   5759  CD1 LEU F  98       7.401  26.434  19.585  1.00 20.00           C  
ATOM   5760  CD2 LEU F  98       6.997  23.992  19.205  1.00 20.00           C  
ATOM   5761  N   PRO F  99      11.682  22.495  19.196  1.00 89.62           N  
ANISOU 5761  N   PRO F  99     9860  13828  10361   2367  -4006  -5850       N  
ATOM   5762  CA  PRO F  99      10.853  21.897  18.144  1.00 84.17           C  
ANISOU 5762  CA  PRO F  99     9312  13032   9635   2204  -3619  -5265       C  
ATOM   5763  C   PRO F  99      10.002  20.715  18.567  1.00 83.65           C  
ANISOU 5763  C   PRO F  99     9356  13337   9090   2584  -3528  -4836       C  
ATOM   5764  O   PRO F  99      10.374  19.945  19.449  1.00 82.66           O  
ANISOU 5764  O   PRO F  99     9132  13572   8705   2908  -3707  -4907       O  
ATOM   5765  CB  PRO F  99      11.889  21.474  17.090  1.00 85.16           C  
ANISOU 5765  CB  PRO F  99     9172  13010  10175   1754  -3474  -5235       C  
ATOM   5766  CG  PRO F  99      13.116  21.200  17.870  1.00 92.76           C  
ANISOU 5766  CG  PRO F  99     9818  14233  11194   1867  -3790  -5669       C  
ATOM   5767  CD  PRO F  99      13.114  22.243  18.945  1.00 92.53           C  
ANISOU 5767  CD  PRO F  99     9854  14210  11093   2091  -4114  -6145       C  
ATOM   5768  N   LEU F 100       8.842  20.577  17.896  1.00 77.25           N  
ANISOU 5768  N   LEU F 100     8754  12424   8173   2532  -3236  -4384       N  
ATOM   5769  CA  LEU F 100       7.932  19.453  18.074  1.00 74.01           C  
ANISOU 5769  CA  LEU F 100     8440  12299   7382   2783  -3076  -3923       C  
ATOM   5770  C   LEU F 100       8.599  18.300  17.305  1.00 75.11           C  
ANISOU 5770  C   LEU F 100     8407  12450   7682   2547  -2943  -3703       C  
ATOM   5771  O   LEU F 100       9.154  18.533  16.221  1.00 73.62           O  
ANISOU 5771  O   LEU F 100     8119  11974   7879   2139  -2827  -3725       O  
ATOM   5772  CB  LEU F 100       6.543  19.777  17.470  1.00 71.87           C  
ANISOU 5772  CB  LEU F 100     8393  11891   7025   2743  -2820  -3572       C  
ATOM   5773  CG  LEU F 100       5.910  21.081  17.985  1.00 78.90           C  
ANISOU 5773  CG  LEU F 100     9471  12687   7822   2931  -2929  -3806       C  
ATOM   5774  CD1 LEU F 100       4.585  21.304  17.375  1.00 76.03           C  
ANISOU 5774  CD1 LEU F 100     9293  12237   7359   2928  -2689  -3464       C  
ATOM   5775  CD2 LEU F 100       5.796  21.078  19.516  1.00 81.60           C  
ANISOU 5775  CD2 LEU F 100     9849  13395   7762   3439  -3173  -4017       C  
ATOM   5776  N   THR F 101       8.640  17.095  17.889  1.00 70.43           N  
ANISOU 5776  N   THR F 101     7786  12179   6797   2819  -2967  -3519       N  
ATOM   5777  CA  THR F 101       9.227  15.951  17.197  1.00 67.92           C  
ANISOU 5777  CA  THR F 101     7340  11868   6599   2644  -2850  -3306       C  
ATOM   5778  C   THR F 101       8.299  14.779  17.303  1.00 68.53           C  
ANISOU 5778  C   THR F 101     7568  12120   6351   2824  -2663  -2825       C  
ATOM   5779  O   THR F 101       7.516  14.695  18.244  1.00 66.52           O  
ANISOU 5779  O   THR F 101     7458  12087   5729   3169  -2684  -2724       O  
ATOM   5780  CB  THR F 101      10.645  15.587  17.680  1.00 70.54           C  
ANISOU 5780  CB  THR F 101     7432  12365   7006   2737  -3103  -3650       C  
ATOM   5781  OG1 THR F 101      10.599  15.113  19.029  1.00 69.84           O  
ANISOU 5781  OG1 THR F 101     7408  12636   6493   3241  -3305  -3710       O  
ATOM   5782  CG2 THR F 101      11.636  16.725  17.507  1.00 71.61           C  
ANISOU 5782  CG2 THR F 101     7360  12314   7534   2484  -3274  -4151       C  
ATOM   5783  N   PHE F 102       8.398  13.876  16.313  1.00 63.37           N  
ANISOU 5783  N   PHE F 102     6881  11355   5840   2579  -2467  -2532       N  
ATOM   5784  CA  PHE F 102       7.623  12.647  16.271  1.00 61.08           C  
ANISOU 5784  CA  PHE F 102     6721  11175   5311   2675  -2278  -2078       C  
ATOM   5785  C   PHE F 102       8.555  11.472  16.550  1.00 66.44           C  
ANISOU 5785  C   PHE F 102     7331  11999   5915   2821  -2365  -2064       C  
ATOM   5786  O   PHE F 102       9.749  11.546  16.257  1.00 67.68           O  
ANISOU 5786  O   PHE F 102     7297  12109   6308   2710  -2494  -2338       O  
ATOM   5787  CB  PHE F 102       6.985  12.454  14.875  1.00 58.45           C  
ANISOU 5787  CB  PHE F 102     6432  10587   5189   2304  -2007  -1765       C  
ATOM   5788  CG  PHE F 102       5.842  13.394  14.600  1.00 58.28           C  
ANISOU 5788  CG  PHE F 102     6519  10460   5165   2231  -1896  -1692       C  
ATOM   5789  CD1 PHE F 102       6.073  14.656  14.077  1.00 62.15           C  
ANISOU 5789  CD1 PHE F 102     6987  10716   5912   2036  -1933  -1946       C  
ATOM   5790  CD2 PHE F 102       4.536  13.015  14.857  1.00 58.14           C  
ANISOU 5790  CD2 PHE F 102     6624  10575   4892   2361  -1747  -1371       C  
ATOM   5791  CE1 PHE F 102       5.015  15.523  13.823  1.00 62.83           C  
ANISOU 5791  CE1 PHE F 102     7202  10698   5970   2017  -1842  -1879       C  
ATOM   5792  CE2 PHE F 102       3.477  13.860  14.552  1.00 61.16           C  
ANISOU 5792  CE2 PHE F 102     7082  10888   5267   2320  -1653  -1315       C  
ATOM   5793  CZ  PHE F 102       3.720  15.105  14.027  1.00 60.29           C  
ANISOU 5793  CZ  PHE F 102     6980  10541   5388   2168  -1709  -1567       C  
ATOM   5794  N   GLY F 103       7.983  10.367  17.006  1.00 61.99           N  
ANISOU 5794  N   GLY F 103     6923  11585   5045   3039  -2263  -1720       N  
ATOM   5795  CA  GLY F 103       8.714   9.117  17.111  1.00 61.83           C  
ANISOU 5795  CA  GLY F 103     6907  11647   4941   3174  -2296  -1618       C  
ATOM   5796  C   GLY F 103       8.858   8.522  15.714  1.00 60.87           C  
ANISOU 5796  C   GLY F 103     6745  11271   5112   2797  -2113  -1421       C  
ATOM   5797  O   GLY F 103       8.219   8.985  14.761  1.00 57.49           O  
ANISOU 5797  O   GLY F 103     6321  10637   4885   2475  -1943  -1306       O  
ATOM   5798  N   GLY F 104       9.671   7.488  15.588  1.00 56.90           N  
ANISOU 5798  N   GLY F 104     6223  10791   4606   2874  -2151  -1382       N  
ATOM   5799  CA  GLY F 104       9.939   6.859  14.299  1.00 54.96           C  
ANISOU 5799  CA  GLY F 104     5944  10325   4614   2570  -2004  -1233       C  
ATOM   5800  C   GLY F 104       8.848   5.978  13.727  1.00 59.32           C  
ANISOU 5800  C   GLY F 104     6702  10730   5106   2430  -1753   -782       C  
ATOM   5801  O   GLY F 104       8.940   5.559  12.567  1.00 57.75           O  
ANISOU 5801  O   GLY F 104     6491  10331   5121   2164  -1632   -671       O  
ATOM   5802  N   GLY F 105       7.836   5.683  14.541  1.00 58.25           N  
ANISOU 5802  N   GLY F 105     6746  10703   4682   2611  -1674   -535       N  
ATOM   5803  CA  GLY F 105       6.684   4.893  14.151  1.00 56.06           C  
ANISOU 5803  CA  GLY F 105     6638  10310   4351   2466  -1433   -121       C  
ATOM   5804  C   GLY F 105       6.799   3.440  14.562  1.00 62.97           C  
ANISOU 5804  C   GLY F 105     7709  11190   5027   2655  -1383    143       C  
ATOM   5805  O   GLY F 105       7.900   2.920  14.779  1.00 63.56           O  
ANISOU 5805  O   GLY F 105     7783  11304   5062   2854  -1529     13       O  
ATOM   5806  N   THR F 106       5.638   2.797  14.700  1.00 61.48           N  
ANISOU 5806  N   THR F 106     7689  10961   4709   2600  -1171    513       N  
ATOM   5807  CA  THR F 106       5.471   1.368  14.972  1.00 62.22           C  
ANISOU 5807  CA  THR F 106     8022  10977   4643   2698  -1051    844       C  
ATOM   5808  C   THR F 106       4.400   0.864  13.974  1.00 63.70           C  
ANISOU 5808  C   THR F 106     8249  10934   5021   2302   -820   1131       C  
ATOM   5809  O   THR F 106       3.282   1.393  13.960  1.00 60.62           O  
ANISOU 5809  O   THR F 106     7795  10599   4638   2154   -689   1233       O  
ATOM   5810  CB  THR F 106       5.102   1.134  16.452  1.00 68.54           C  
ANISOU 5810  CB  THR F 106     8995  12002   5043   3080  -1015   1000       C  
ATOM   5811  OG1 THR F 106       6.259   1.343  17.251  1.00 71.69           O  
ANISOU 5811  OG1 THR F 106     9378  12590   5270   3472  -1270    716       O  
ATOM   5812  CG2 THR F 106       4.562  -0.261  16.730  1.00 64.71           C  
ANISOU 5812  CG2 THR F 106     8794  11393   4398   3113   -800   1429       C  
ATOM   5813  N   LYS F 107       4.762  -0.111  13.117  1.00 61.95           N  
ANISOU 5813  N   LYS F 107     8116  10469   4955   2149   -792   1225       N  
ATOM   5814  CA  LYS F 107       3.833  -0.714  12.156  1.00 60.96           C  
ANISOU 5814  CA  LYS F 107     8038  10111   5012   1789   -612   1461       C  
ATOM   5815  C   LYS F 107       3.190  -1.955  12.779  1.00 68.07           C  
ANISOU 5815  C   LYS F 107     9193  10927   5741   1838   -434   1833       C  
ATOM   5816  O   LYS F 107       3.898  -2.920  13.098  1.00 67.14           O  
ANISOU 5816  O   LYS F 107     9288  10711   5510   2041   -470   1913       O  
ATOM   5817  CB  LYS F 107       4.532  -1.117  10.851  1.00 62.13           C  
ANISOU 5817  CB  LYS F 107     8168  10023   5413   1602   -677   1353       C  
ATOM   5818  CG  LYS F 107       3.564  -1.680   9.803  1.00 73.83           C  
ANISOU 5818  CG  LYS F 107     9693  11274   7085   1241   -529   1546       C  
ATOM   5819  CD  LYS F 107       4.275  -2.061   8.506  1.00 89.90           C  
ANISOU 5819  CD  LYS F 107    11731  13091   9335   1100   -599   1424       C  
ATOM   5820  CE  LYS F 107       3.392  -2.898   7.599  1.00109.29           C  
ANISOU 5820  CE  LYS F 107    14288  15300  11937    802   -486   1615       C  
ATOM   5821  NZ  LYS F 107       4.076  -3.286   6.330  1.00118.36           N  
ANISOU 5821  NZ  LYS F 107    15465  16246  13260    704   -557   1488       N  
ATOM   5822  N   VAL F 108       1.837  -1.944  12.879  1.00 66.76           N  
ANISOU 5822  N   VAL F 108     9003  10784   5577   1636   -230   2061       N  
ATOM   5823  CA  VAL F 108       1.064  -3.065  13.389  1.00 69.66           C  
ANISOU 5823  CA  VAL F 108     9584  11049   5836   1591     -3   2438       C  
ATOM   5824  C   VAL F 108       0.611  -3.856  12.156  1.00 72.96           C  
ANISOU 5824  C   VAL F 108    10025  11148   6548   1190     72   2541       C  
ATOM   5825  O   VAL F 108      -0.221  -3.392  11.384  1.00 69.27           O  
ANISOU 5825  O   VAL F 108     9358  10682   6278    889    116   2502       O  
ATOM   5826  CB  VAL F 108      -0.085  -2.618  14.321  1.00 75.36           C  
ANISOU 5826  CB  VAL F 108    10238  12021   6375   1629    188   2614       C  
ATOM   5827  CG1 VAL F 108      -0.860  -3.826  14.847  1.00 78.99           C  
ANISOU 5827  CG1 VAL F 108    10917  12354   6740   1548    469   3030       C  
ATOM   5828  CG2 VAL F 108       0.471  -1.808  15.496  1.00 75.93           C  
ANISOU 5828  CG2 VAL F 108    10306  12403   6140   2068     67   2458       C  
ATOM   5829  N   GLU F 109       1.231  -5.031  11.959  1.00 73.47           N  
ANISOU 5829  N   GLU F 109    10344  10943   6628   1228     57   2640       N  
ATOM   5830  CA  GLU F 109       1.044  -5.952  10.827  1.00 72.63           C  
ANISOU 5830  CA  GLU F 109    10329  10491   6778    912     85   2706       C  
ATOM   5831  C   GLU F 109       0.199  -7.168  11.294  1.00 78.32           C  
ANISOU 5831  C   GLU F 109    11294  10996   7467    770    330   3087       C  
ATOM   5832  O   GLU F 109       0.132  -7.472  12.503  1.00 79.21           O  
ANISOU 5832  O   GLU F 109    11584  11193   7317   1006    460   3308       O  
ATOM   5833  CB  GLU F 109       2.452  -6.361  10.292  1.00 73.43           C  
ANISOU 5833  CB  GLU F 109    10552  10440   6908   1099   -118   2514       C  
ATOM   5834  CG  GLU F 109       2.593  -7.685   9.553  1.00 89.75           C  
ANISOU 5834  CG  GLU F 109    12873  12119   9110    961   -100   2626       C  
ATOM   5835  CD  GLU F 109       3.992  -8.268   9.553  1.00115.20           C  
ANISOU 5835  CD  GLU F 109    16290  15247  12235   1296   -262   2513       C  
ATOM   5836  OE1 GLU F 109       4.335  -8.974  10.528  1.00113.56           O  
ANISOU 5836  OE1 GLU F 109    16354  15002  11792   1593   -227   2686       O  
ATOM   5837  OE2 GLU F 109       4.723  -8.074   8.555  1.00110.03           O  
ANISOU 5837  OE2 GLU F 109    15527  14552  11727   1274   -411   2263       O  
ATOM   5838  N   ILE F 110      -0.458  -7.843  10.323  1.00 74.26           N  
ANISOU 5838  N   ILE F 110    10791  10201   7223    380    396   3158       N  
ATOM   5839  CA  ILE F 110      -1.322  -9.006  10.574  1.00 76.95           C  
ANISOU 5839  CA  ILE F 110    11335  10280   7621    142    635   3494       C  
ATOM   5840  C   ILE F 110      -0.466 -10.273  10.647  1.00 82.57           C  
ANISOU 5840  C   ILE F 110    12468  10632   8273    305    608   3610       C  
ATOM   5841  O   ILE F 110       0.311 -10.532   9.725  1.00 79.52           O  
ANISOU 5841  O   ILE F 110    12143  10062   8008    324    414   3409       O  
ATOM   5842  CB  ILE F 110      -2.415  -9.166   9.474  1.00 79.33           C  
ANISOU 5842  CB  ILE F 110    11441  10438   8262   -360    684   3469       C  
ATOM   5843  CG1 ILE F 110      -3.234  -7.876   9.255  1.00 76.92           C  
ANISOU 5843  CG1 ILE F 110    10718  10493   8016   -484    676   3318       C  
ATOM   5844  CG2 ILE F 110      -3.339 -10.350   9.788  1.00 83.39           C  
ANISOU 5844  CG2 ILE F 110    12133  10676   8875   -655    949   3805       C  
ATOM   5845  CD1 ILE F 110      -3.640  -7.700   7.861  1.00 84.75           C  
ANISOU 5845  CD1 ILE F 110    11515  11396   9290   -788    548   3108       C  
ATOM   5846  N   LYS F 111      -0.657 -11.081  11.709  1.00 83.75           N  
ANISOU 5846  N   LYS F 111    12923  10667   8230    426    820   3948       N  
ATOM   5847  CA  LYS F 111       0.047 -12.353  11.914  1.00 86.67           C  
ANISOU 5847  CA  LYS F 111    13759  10665   8506    616    828   4113       C  
ATOM   5848  C   LYS F 111      -0.623 -13.387  11.032  1.00 93.13           C  
ANISOU 5848  C   LYS F 111    14707  11030   9647    159    922   4221       C  
ATOM   5849  O   LYS F 111      -1.829 -13.314  10.782  1.00 93.90           O  
ANISOU 5849  O   LYS F 111    14588  11125   9963   -276   1084   4304       O  
ATOM   5850  CB  LYS F 111       0.051 -12.814  13.390  1.00 92.80           C  
ANISOU 5850  CB  LYS F 111    14858  11473   8929    937   1040   4459       C  
ATOM   5851  N   ARG F 112       0.154 -14.349  10.562  1.00 90.21           N  
ANISOU 5851  N   ARG F 112    14678  10288   9312    267    806   4196       N  
ATOM   5852  CA  ARG F 112      -0.340 -15.322   9.603  1.00 91.26           C  
ANISOU 5852  CA  ARG F 112    14952   9960   9761   -140    833   4227       C  
ATOM   5853  C   ARG F 112       0.589 -16.542   9.573  1.00 96.47           C  
ANISOU 5853  C   ARG F 112    16130  10190  10335    124    760   4299       C  
ATOM   5854  O   ARG F 112       1.715 -16.470  10.076  1.00 95.70           O  
ANISOU 5854  O   ARG F 112    16191  10218   9953    634    629   4243       O  
ATOM   5855  CB  ARG F 112      -0.436 -14.611   8.202  1.00 87.86           C  
ANISOU 5855  CB  ARG F 112    14136   9645   9600   -386    609   3849       C  
ATOM   5856  CG  ARG F 112      -0.599 -15.565   7.042  1.00 98.58           C  
ANISOU 5856  CG  ARG F 112    15655  10553  11249   -689    529   3764       C  
ATOM   5857  CD  ARG F 112      -0.945 -14.979   5.718  1.00 99.64           C  
ANISOU 5857  CD  ARG F 112    15445  10778  11634   -964    356   3449       C  
ATOM   5858  NE  ARG F 112      -1.767 -15.913   4.938  1.00113.17           N  
ANISOU 5858  NE  ARG F 112    17259  12084  13655  -1400    380   3463       N  
ATOM   5859  CZ  ARG F 112      -1.356 -17.084   4.441  1.00135.70           C  
ANISOU 5859  CZ  ARG F 112    20499  14465  16596  -1401    302   3453       C  
ATOM   5860  NH1 ARG F 112      -0.102 -17.494   4.622  1.00120.19           N  
ANISOU 5860  NH1 ARG F 112    18859  12387  14420   -959    195   3434       N  
ATOM   5861  NH2 ARG F 112      -2.196 -17.854   3.758  1.00134.56           N  
ANISOU 5861  NH2 ARG F 112    20413  13960  16753  -1833    316   3439       N  
ATOM   5862  N   THR F 113       0.090 -17.673   9.039  1.00 95.59           N  
ANISOU 5862  N   THR F 113    16288   9568  10465   -212    845   4421       N  
ATOM   5863  CA  THR F 113       0.882 -18.895   8.872  1.00 98.02           C  
ANISOU 5863  CA  THR F 113    17119   9399  10725      8    768   4475       C  
ATOM   5864  C   THR F 113       1.951 -18.649   7.802  1.00 98.79           C  
ANISOU 5864  C   THR F 113    17120   9564  10851    238    425   4071       C  
ATOM   5865  O   THR F 113       1.723 -17.893   6.853  1.00 94.61           O  
ANISOU 5865  O   THR F 113    16188   9244  10514     13    292   3789       O  
ATOM   5866  CB  THR F 113      -0.018 -20.102   8.546  1.00103.92           C  
ANISOU 5866  CB  THR F 113    18156   9565  11762   -466    949   4684       C  
ATOM   5867  OG1 THR F 113      -0.955 -19.747   7.518  1.00102.34           O  
ANISOU 5867  OG1 THR F 113    17552   9402  11930   -999    904   4480       O  
ATOM   5868  CG2 THR F 113      -0.761 -20.599   9.766  1.00100.39           C  
ANISOU 5868  CG2 THR F 113    17949   8978  11218   -571   1326   5145       C  
ATOM   5869  N   VAL F 114       3.128 -19.262   7.971  1.00 96.43           N  
ANISOU 5869  N   VAL F 114    17188   9113  10338    716    293   4047       N  
ATOM   5870  CA  VAL F 114       4.241 -19.043   7.050  1.00 92.98           C  
ANISOU 5870  CA  VAL F 114    16650   8783   9895    986     -4   3676       C  
ATOM   5871  C   VAL F 114       3.906 -19.600   5.682  1.00 95.67           C  
ANISOU 5871  C   VAL F 114    17032   8765  10552    636    -99   3506       C  
ATOM   5872  O   VAL F 114       3.475 -20.738   5.566  1.00 97.77           O  
ANISOU 5872  O   VAL F 114    17687   8518  10944    447    -14   3673       O  
ATOM   5873  CB  VAL F 114       5.572 -19.611   7.603  1.00 99.08           C  
ANISOU 5873  CB  VAL F 114    17787   9507  10350   1617   -123   3684       C  
ATOM   5874  CG1 VAL F 114       6.691 -19.513   6.560  1.00 96.54           C  
ANISOU 5874  CG1 VAL F 114    17360   9268  10054   1867   -403   3303       C  
ATOM   5875  CG2 VAL F 114       5.972 -18.898   8.898  1.00 98.52           C  
ANISOU 5875  CG2 VAL F 114    17609   9875   9948   2004    -87   3774       C  
ATOM   5876  N   ALA F 115       4.039 -18.763   4.656  1.00 90.13           N  
ANISOU 5876  N   ALA F 115    15934   8331   9983    535   -266   3175       N  
ATOM   5877  CA  ALA F 115       3.810 -19.140   3.263  1.00 89.49           C  
ANISOU 5877  CA  ALA F 115    15854   7988  10160    267   -396   2955       C  
ATOM   5878  C   ALA F 115       5.109 -18.886   2.523  1.00 93.46           C  
ANISOU 5878  C   ALA F 115    16297   8660  10553    661   -625   2641       C  
ATOM   5879  O   ALA F 115       5.718 -17.822   2.692  1.00 89.48           O  
ANISOU 5879  O   ALA F 115    15458   8619   9920    877   -678   2501       O  
ATOM   5880  CB  ALA F 115       2.682 -18.318   2.661  1.00 87.42           C  
ANISOU 5880  CB  ALA F 115    15158   7919  10138   -214   -364   2856       C  
ATOM   5881  N   ALA F 116       5.562 -19.880   1.742  1.00 94.21           N  
ANISOU 5881  N   ALA F 116    16725   8374  10696    766   -750   2530       N  
ATOM   5882  CA  ALA F 116       6.784 -19.761   0.953  1.00 92.65           C  
ANISOU 5882  CA  ALA F 116    16485   8316  10400   1140   -947   2232       C  
ATOM   5883  C   ALA F 116       6.506 -18.875  -0.270  1.00 93.64           C  
ANISOU 5883  C   ALA F 116    16209   8678  10692    889  -1028   1957       C  
ATOM   5884  O   ALA F 116       5.344 -18.742  -0.663  1.00 92.48           O  
ANISOU 5884  O   ALA F 116    15942   8439  10755    438   -979   1981       O  
ATOM   5885  CB  ALA F 116       7.261 -21.135   0.506  1.00 96.92           C  
ANISOU 5885  CB  ALA F 116    17538   8359  10929   1341  -1047   2205       C  
ATOM   5886  N   PRO F 117       7.531 -18.261  -0.893  1.00 88.92           N  
ANISOU 5886  N   PRO F 117    15397   8387  10002   1174  -1142   1697       N  
ATOM   5887  CA  PRO F 117       7.266 -17.445  -2.075  1.00 86.00           C  
ANISOU 5887  CA  PRO F 117    14702   8212   9763    961  -1195   1465       C  
ATOM   5888  C   PRO F 117       7.231 -18.266  -3.348  1.00 90.82           C  
ANISOU 5888  C   PRO F 117    15549   8489  10468    923  -1322   1288       C  
ATOM   5889  O   PRO F 117       8.090 -19.121  -3.555  1.00 92.25           O  
ANISOU 5889  O   PRO F 117    16029   8475  10547   1258  -1410   1215       O  
ATOM   5890  CB  PRO F 117       8.445 -16.447  -2.095  1.00 85.42           C  
ANISOU 5890  CB  PRO F 117    14310   8603   9542   1289  -1222   1289       C  
ATOM   5891  CG  PRO F 117       9.394 -16.892  -0.963  1.00 91.81           C  
ANISOU 5891  CG  PRO F 117    15289   9449  10144   1711  -1228   1389       C  
ATOM   5892  CD  PRO F 117       8.975 -18.283  -0.607  1.00 91.37           C  
ANISOU 5892  CD  PRO F 117    15736   8891  10089   1704  -1222   1591       C  
ATOM   5893  N   SER F 118       6.252 -17.988  -4.210  1.00 86.55           N  
ANISOU 5893  N   SER F 118    14871   7907  10107    550  -1348   1196       N  
ATOM   5894  CA  SER F 118       6.178 -18.589  -5.534  1.00 87.05           C  
ANISOU 5894  CA  SER F 118    15111   7718  10249    519  -1495    976       C  
ATOM   5895  C   SER F 118       7.096 -17.669  -6.370  1.00 86.65           C  
ANISOU 5895  C   SER F 118    14795   8058  10071    781  -1531    745       C  
ATOM   5896  O   SER F 118       6.751 -16.505  -6.600  1.00 83.55           O  
ANISOU 5896  O   SER F 118    14042   7998   9706    624  -1477    703       O  
ATOM   5897  CB  SER F 118       4.738 -18.594  -6.050  1.00 90.99           C  
ANISOU 5897  CB  SER F 118    15528   8066  10976     33  -1522    953       C  
ATOM   5898  OG  SER F 118       3.850 -19.086  -5.059  1.00100.48           O  
ANISOU 5898  OG  SER F 118    16834   9037  12307   -263  -1410   1210       O  
ATOM   5899  N   VAL F 119       8.331 -18.132  -6.663  1.00 82.54           N  
ANISOU 5899  N   VAL F 119    14439   7526   9397   1205  -1592    623       N  
ATOM   5900  CA  VAL F 119       9.327 -17.326  -7.381  1.00 78.46           C  
ANISOU 5900  CA  VAL F 119    13664   7387   8759   1469  -1582    424       C  
ATOM   5901  C   VAL F 119       9.255 -17.532  -8.884  1.00 79.81           C  
ANISOU 5901  C   VAL F 119    13925   7464   8936   1482  -1680    193       C  
ATOM   5902  O   VAL F 119       9.063 -18.651  -9.365  1.00 81.09           O  
ANISOU 5902  O   VAL F 119    14451   7236   9125   1513  -1808    123       O  
ATOM   5903  CB  VAL F 119      10.770 -17.538  -6.849  1.00 82.38           C  
ANISOU 5903  CB  VAL F 119    14186   8040   9077   1944  -1573    396       C  
ATOM   5904  CG1 VAL F 119      11.766 -16.609  -7.554  1.00 79.65           C  
ANISOU 5904  CG1 VAL F 119    13503   8115   8644   2153  -1520    197       C  
ATOM   5905  CG2 VAL F 119      10.825 -17.326  -5.337  1.00 81.79           C  
ANISOU 5905  CG2 VAL F 119    14036   8077   8962   1970  -1500    608       C  
ATOM   5906  N   PHE F 120       9.392 -16.414  -9.617  1.00 73.55           N  
ANISOU 5906  N   PHE F 120    12814   7021   8111   1462  -1617     76       N  
ATOM   5907  CA  PHE F 120       9.413 -16.357 -11.076  1.00 72.06           C  
ANISOU 5907  CA  PHE F 120    12666   6843   7872   1527  -1678   -139       C  
ATOM   5908  C   PHE F 120      10.522 -15.405 -11.491  1.00 73.12           C  
ANISOU 5908  C   PHE F 120    12519   7390   7871   1780  -1542   -232       C  
ATOM   5909  O   PHE F 120      10.800 -14.428 -10.791  1.00 69.49           O  
ANISOU 5909  O   PHE F 120    11745   7230   7428   1725  -1408   -140       O  
ATOM   5910  CB  PHE F 120       8.069 -15.864 -11.646  1.00 71.83           C  
ANISOU 5910  CB  PHE F 120    12540   6791   7961   1150  -1722   -159       C  
ATOM   5911  CG  PHE F 120       6.841 -16.580 -11.127  1.00 73.77           C  
ANISOU 5911  CG  PHE F 120    12942   6696   8392    802  -1815    -54       C  
ATOM   5912  CD1 PHE F 120       6.256 -16.208  -9.921  1.00 74.70           C  
ANISOU 5912  CD1 PHE F 120    12894   6874   8614    553  -1714    171       C  
ATOM   5913  CD2 PHE F 120       6.247 -17.592 -11.860  1.00 77.11           C  
ANISOU 5913  CD2 PHE F 120    13661   6746   8892    711  -1994   -192       C  
ATOM   5914  CE1 PHE F 120       5.107 -16.847  -9.457  1.00 76.76           C  
ANISOU 5914  CE1 PHE F 120    13269   6839   9057    209  -1757    281       C  
ATOM   5915  CE2 PHE F 120       5.084 -18.215 -11.407  1.00 81.60           C  
ANISOU 5915  CE2 PHE F 120    14331   7000   9672    335  -2058   -104       C  
ATOM   5916  CZ  PHE F 120       4.526 -17.846 -10.204  1.00 78.74           C  
ANISOU 5916  CZ  PHE F 120    13788   6713   9415     81  -1922    144       C  
ATOM   5917  N   ILE F 121      11.142 -15.692 -12.641  1.00 71.24           N  
ANISOU 5917  N   ILE F 121    12399   7163   7506   2047  -1570   -421       N  
ATOM   5918  CA  ILE F 121      12.212 -14.888 -13.230  1.00 68.97           C  
ANISOU 5918  CA  ILE F 121    11867   7246   7092   2288  -1411   -520       C  
ATOM   5919  C   ILE F 121      11.777 -14.491 -14.649  1.00 70.38           C  
ANISOU 5919  C   ILE F 121    12078   7463   7197   2252  -1405   -646       C  
ATOM   5920  O   ILE F 121      11.119 -15.287 -15.336  1.00 71.39           O  
ANISOU 5920  O   ILE F 121    12504   7305   7314   2233  -1582   -747       O  
ATOM   5921  CB  ILE F 121      13.603 -15.610 -13.180  1.00 73.78           C  
ANISOU 5921  CB  ILE F 121    12561   7905   7568   2740  -1407   -621       C  
ATOM   5922  CG1 ILE F 121      14.729 -14.648 -13.654  1.00 73.69           C  
ANISOU 5922  CG1 ILE F 121    12202   8332   7466   2931  -1193   -707       C  
ATOM   5923  CG2 ILE F 121      13.625 -16.911 -13.989  1.00 76.87           C  
ANISOU 5923  CG2 ILE F 121    13381   7964   7863   2978  -1579   -769       C  
ATOM   5924  CD1 ILE F 121      16.170 -15.143 -13.442  1.00 82.09           C  
ANISOU 5924  CD1 ILE F 121    13212   9559   8418   3366  -1161   -811       C  
ATOM   5925  N   PHE F 122      12.115 -13.253 -15.068  1.00 63.99           N  
ANISOU 5925  N   PHE F 122    10977   6994   6341   2237  -1207   -641       N  
ATOM   5926  CA  PHE F 122      11.786 -12.746 -16.395  1.00 65.01           C  
ANISOU 5926  CA  PHE F 122    11144   7200   6358   2253  -1165   -733       C  
ATOM   5927  C   PHE F 122      13.039 -12.188 -17.048  1.00 71.25           C  
ANISOU 5927  C   PHE F 122    11776   8295   7000   2533   -930   -796       C  
ATOM   5928  O   PHE F 122      13.724 -11.364 -16.439  1.00 70.48           O  
ANISOU 5928  O   PHE F 122    11363   8452   6965   2494   -736   -717       O  
ATOM   5929  CB  PHE F 122      10.727 -11.614 -16.355  1.00 64.35           C  
ANISOU 5929  CB  PHE F 122    10885   7209   6358   1914  -1119   -628       C  
ATOM   5930  CG  PHE F 122       9.433 -11.962 -15.663  1.00 65.32           C  
ANISOU 5930  CG  PHE F 122    11069   7104   6645   1595  -1304   -552       C  
ATOM   5931  CD1 PHE F 122       8.502 -12.781 -16.276  1.00 68.86           C  
ANISOU 5931  CD1 PHE F 122    11777   7283   7105   1526  -1529   -662       C  
ATOM   5932  CD2 PHE F 122       9.107 -11.398 -14.435  1.00 64.59           C  
ANISOU 5932  CD2 PHE F 122    10754   7089   6699   1354  -1243   -383       C  
ATOM   5933  CE1 PHE F 122       7.308 -13.109 -15.643  1.00 69.15           C  
ANISOU 5933  CE1 PHE F 122    11830   7122   7321   1199  -1672   -596       C  
ATOM   5934  CE2 PHE F 122       7.892 -11.694 -13.816  1.00 66.59           C  
ANISOU 5934  CE2 PHE F 122    11043   7160   7099   1058  -1376   -301       C  
ATOM   5935  CZ  PHE F 122       7.004 -12.561 -14.419  1.00 66.17           C  
ANISOU 5935  CZ  PHE F 122    11226   6836   7080    967  -1580   -403       C  
ATOM   5936  N   PRO F 123      13.326 -12.559 -18.303  1.00 70.04           N  
ANISOU 5936  N   PRO F 123    11824   8136   6654   2804   -930   -942       N  
ATOM   5937  CA  PRO F 123      14.473 -11.959 -18.990  1.00 70.85           C  
ANISOU 5937  CA  PRO F 123    11757   8552   6610   3052   -655   -980       C  
ATOM   5938  C   PRO F 123      14.139 -10.560 -19.530  1.00 72.98           C  
ANISOU 5938  C   PRO F 123    11856   9019   6855   2873   -436   -884       C  
ATOM   5939  O   PRO F 123      12.967 -10.166 -19.563  1.00 69.77           O  
ANISOU 5939  O   PRO F 123    11511   8501   6498   2624   -542   -825       O  
ATOM   5940  CB  PRO F 123      14.694 -12.927 -20.151  1.00 75.60           C  
ANISOU 5940  CB  PRO F 123    12694   9042   6988   3412   -757  -1166       C  
ATOM   5941  CG  PRO F 123      13.323 -13.379 -20.497  1.00 79.79           C  
ANISOU 5941  CG  PRO F 123    13515   9266   7535   3243  -1035  -1216       C  
ATOM   5942  CD  PRO F 123      12.603 -13.495 -19.192  1.00 73.56           C  
ANISOU 5942  CD  PRO F 123    12649   8300   7000   2894  -1172  -1090       C  
ATOM   5943  N   PRO F 124      15.136  -9.817 -20.050  1.00 70.72           N  
ANISOU 5943  N   PRO F 124    11374   9017   6478   3013   -122   -871       N  
ATOM   5944  CA  PRO F 124      14.817  -8.539 -20.692  1.00 68.79           C  
ANISOU 5944  CA  PRO F 124    11050   8907   6179   2877    105   -766       C  
ATOM   5945  C   PRO F 124      14.094  -8.810 -21.997  1.00 71.64           C  
ANISOU 5945  C   PRO F 124    11762   9159   6299   3043      0   -844       C  
ATOM   5946  O   PRO F 124      14.393  -9.799 -22.661  1.00 73.76           O  
ANISOU 5946  O   PRO F 124    12264   9362   6400   3350   -108   -996       O  
ATOM   5947  CB  PRO F 124      16.190  -7.900 -20.950  1.00 72.32           C  
ANISOU 5947  CB  PRO F 124    11228   9656   6594   3010    482   -747       C  
ATOM   5948  CG  PRO F 124      17.191  -8.791 -20.327  1.00 79.19           C  
ANISOU 5948  CG  PRO F 124    11979  10589   7519   3205    425   -856       C  
ATOM   5949  CD  PRO F 124      16.567 -10.137 -20.195  1.00 74.94           C  
ANISOU 5949  CD  PRO F 124    11777   9759   6939   3324     53   -956       C  
ATOM   5950  N   SER F 125      13.139  -7.968 -22.348  1.00 65.36           N  
ANISOU 5950  N   SER F 125    11018   8345   5473   2871      5   -760       N  
ATOM   5951  CA  SER F 125      12.397  -8.118 -23.603  1.00 66.22           C  
ANISOU 5951  CA  SER F 125    11449   8382   5329   3050   -114   -848       C  
ATOM   5952  C   SER F 125      13.267  -7.714 -24.770  1.00 72.23           C  
ANISOU 5952  C   SER F 125    12283   9347   5816   3367    202   -841       C  
ATOM   5953  O   SER F 125      14.159  -6.885 -24.601  1.00 70.44           O  
ANISOU 5953  O   SER F 125    11809   9316   5639   3321    560   -711       O  
ATOM   5954  CB  SER F 125      11.150  -7.237 -23.589  1.00 66.22           C  
ANISOU 5954  CB  SER F 125    11453   8344   5365   2805   -192   -756       C  
ATOM   5955  OG  SER F 125      11.466  -5.852 -23.607  1.00 63.23           O  
ANISOU 5955  OG  SER F 125    10899   8140   4987   2707    149   -573       O  
ATOM   5956  N   ASP F 126      12.991  -8.274 -25.957  1.00 73.47           N  
ANISOU 5956  N   ASP F 126    12773   9458   5682   3684     78   -985       N  
ATOM   5957  CA  ASP F 126      13.690  -7.913 -27.198  1.00 75.69           C  
ANISOU 5957  CA  ASP F 126    13183   9936   5639   4032    383   -971       C  
ATOM   5958  C   ASP F 126      13.533  -6.396 -27.414  1.00 77.39           C  
ANISOU 5958  C   ASP F 126    13298  10282   5822   3880    709   -741       C  
ATOM   5959  O   ASP F 126      14.513  -5.718 -27.713  1.00 78.19           O  
ANISOU 5959  O   ASP F 126    13268  10579   5864   3950   1132   -612       O  
ATOM   5960  CB  ASP F 126      13.084  -8.641 -28.421  1.00 80.27           C  
ANISOU 5960  CB  ASP F 126    14182  10427   5891   4381    127  -1172       C  
ATOM   5961  CG  ASP F 126      13.444 -10.108 -28.602  1.00 94.25           C  
ANISOU 5961  CG  ASP F 126    16143  12076   7595   4656   -124  -1418       C  
ATOM   5962  OD1 ASP F 126      14.493 -10.536 -28.062  1.00 95.79           O  
ANISOU 5962  OD1 ASP F 126    16165  12334   7896   4715      7  -1419       O  
ATOM   5963  OD2 ASP F 126      12.710 -10.817 -29.347  1.00 97.38           O  
ANISOU 5963  OD2 ASP F 126    16869  12320   7810   4848   -451  -1628       O  
ATOM   5964  N   GLU F 127      12.297  -5.874 -27.239  1.00 70.81           N  
ANISOU 5964  N   GLU F 127    12522   9336   5044   3665    518   -693       N  
ATOM   5965  CA  GLU F 127      11.996  -4.442 -27.400  1.00 69.89           C  
ANISOU 5965  CA  GLU F 127    12366   9295   4893   3532    778   -479       C  
ATOM   5966  C   GLU F 127      12.935  -3.563 -26.577  1.00 74.85           C  
ANISOU 5966  C   GLU F 127    12639  10028   5772   3273   1156   -294       C  
ATOM   5967  O   GLU F 127      13.407  -2.552 -27.084  1.00 77.90           O  
ANISOU 5967  O   GLU F 127    13021  10520   6056   3302   1549   -126       O  
ATOM   5968  CB  GLU F 127      10.547  -4.135 -27.010  1.00 68.41           C  
ANISOU 5968  CB  GLU F 127    12216   8977   4801   3310    464   -482       C  
ATOM   5969  CG  GLU F 127      10.036  -2.813 -27.543  1.00 80.29           C  
ANISOU 5969  CG  GLU F 127    13826  10535   6144   3324    654   -310       C  
ATOM   5970  CD  GLU F 127       8.689  -2.416 -26.977  1.00104.81           C  
ANISOU 5970  CD  GLU F 127    16889  13552   9380   3091    371   -307       C  
ATOM   5971  OE1 GLU F 127       7.858  -3.322 -26.740  1.00107.79           O  
ANISOU 5971  OE1 GLU F 127    17288  13833   9835   3039    -39   -492       O  
ATOM   5972  OE2 GLU F 127       8.465  -1.204 -26.756  1.00100.01           O  
ANISOU 5972  OE2 GLU F 127    16220  12967   8811   2955    567   -122       O  
ATOM   5973  N   GLN F 128      13.234  -3.964 -25.338  1.00 69.61           N  
ANISOU 5973  N   GLN F 128    11691   9332   5425   3035   1044   -332       N  
ATOM   5974  CA  GLN F 128      14.120  -3.203 -24.453  1.00 68.37           C  
ANISOU 5974  CA  GLN F 128    11164   9283   5531   2785   1338   -211       C  
ATOM   5975  C   GLN F 128      15.548  -3.303 -24.905  1.00 74.72           C  
ANISOU 5975  C   GLN F 128    11841  10282   6267   2978   1686   -220       C  
ATOM   5976  O   GLN F 128      16.238  -2.293 -24.937  1.00 74.75           O  
ANISOU 5976  O   GLN F 128    11656  10405   6340   2858   2079    -82       O  
ATOM   5977  CB  GLN F 128      14.010  -3.678 -22.993  1.00 66.49           C  
ANISOU 5977  CB  GLN F 128    10682   8973   5608   2533   1084   -268       C  
ATOM   5978  CG  GLN F 128      14.819  -2.795 -22.042  1.00 73.96           C  
ANISOU 5978  CG  GLN F 128    11241  10036   6822   2273   1342   -173       C  
ATOM   5979  CD  GLN F 128      14.802  -3.212 -20.592  1.00 76.31           C  
ANISOU 5979  CD  GLN F 128    11308  10298   7390   2077   1112   -227       C  
ATOM   5980  OE1 GLN F 128      14.583  -4.386 -20.236  1.00 62.05           O  
ANISOU 5980  OE1 GLN F 128     9592   8399   5587   2174    817   -337       O  
ATOM   5981  NE2 GLN F 128      15.169  -2.265 -19.737  1.00 65.65           N  
ANISOU 5981  NE2 GLN F 128     9655   9025   6265   1821   1274   -155       N  
ATOM   5982  N   LEU F 129      16.003  -4.512 -25.240  1.00 74.49           N  
ANISOU 5982  N   LEU F 129    11908  10284   6112   3274   1552   -388       N  
ATOM   5983  CA  LEU F 129      17.376  -4.754 -25.689  1.00 77.07           C  
ANISOU 5983  CA  LEU F 129    12099  10832   6352   3515   1862   -428       C  
ATOM   5984  C   LEU F 129      17.794  -3.873 -26.877  1.00 84.41           C  
ANISOU 5984  C   LEU F 129    13124  11906   7041   3657   2313   -283       C  
ATOM   5985  O   LEU F 129      18.961  -3.508 -26.948  1.00 85.34           O  
ANISOU 5985  O   LEU F 129    12972  12236   7218   3662   2705   -233       O  
ATOM   5986  CB  LEU F 129      17.604  -6.246 -25.977  1.00 78.62           C  
ANISOU 5986  CB  LEU F 129    12478  10998   6395   3872   1593   -646       C  
ATOM   5987  CG  LEU F 129      17.580  -7.177 -24.739  1.00 81.52           C  
ANISOU 5987  CG  LEU F 129    12721  11244   7009   3768   1243   -768       C  
ATOM   5988  CD1 LEU F 129      17.455  -8.638 -25.143  1.00 82.40           C  
ANISOU 5988  CD1 LEU F 129    13149  11215   6944   4110    921   -976       C  
ATOM   5989  CD2 LEU F 129      18.832  -7.007 -23.864  1.00 85.45           C  
ANISOU 5989  CD2 LEU F 129    12775  11957   7733   3693   1452   -768       C  
ATOM   5990  N   LYS F 130      16.849  -3.434 -27.733  1.00 83.75           N  
ANISOU 5990  N   LYS F 130    13393  11718   6710   3743   2284   -201       N  
ATOM   5991  CA  LYS F 130      17.168  -2.500 -28.831  1.00 87.83           C  
ANISOU 5991  CA  LYS F 130    14053  12344   6975   3880   2738    -19       C  
ATOM   5992  C   LYS F 130      17.523  -1.070 -28.310  1.00 92.57           C  
ANISOU 5992  C   LYS F 130    14376  12962   7833   3492   3132    209       C  
ATOM   5993  O   LYS F 130      18.138  -0.302 -29.051  1.00 95.85           O  
ANISOU 5993  O   LYS F 130    14816  13482   8122   3549   3611    378       O  
ATOM   5994  CB  LYS F 130      16.017  -2.423 -29.859  1.00 91.37           C  
ANISOU 5994  CB  LYS F 130    14979  12677   7061   4122   2561     -5       C  
ATOM   5995  N   SER F 131      17.138  -0.727 -27.052  1.00 86.58           N  
ANISOU 5995  N   SER F 131    13376  12093   7430   3106   2941    211       N  
ATOM   5996  CA  SER F 131      17.387   0.575 -26.404  1.00 85.92           C  
ANISOU 5996  CA  SER F 131    13033  11985   7628   2716   3233    379       C  
ATOM   5997  C   SER F 131      18.748   0.722 -25.674  1.00 91.10           C  
ANISOU 5997  C   SER F 131    13191  12820   8602   2512   3503    339       C  
ATOM   5998  O   SER F 131      19.015   1.801 -25.142  1.00 91.31           O  
ANISOU 5998  O   SER F 131    12990  12819   8884   2174   3746    448       O  
ATOM   5999  CB  SER F 131      16.268   0.890 -25.404  1.00 86.22           C  
ANISOU 5999  CB  SER F 131    13059  11834   7868   2434   2880    379       C  
ATOM   6000  OG  SER F 131      16.476   0.337 -24.107  1.00 90.41           O  
ANISOU 6000  OG  SER F 131    13264  12383   8707   2241   2623    240       O  
ATOM   6001  N   GLY F 132      19.550  -0.341 -25.590  1.00 87.94           N  
ANISOU 6001  N   GLY F 132    12622  12594   8198   2716   3431    163       N  
ATOM   6002  CA  GLY F 132      20.850  -0.290 -24.922  1.00 88.65           C  
ANISOU 6002  CA  GLY F 132    12212  12901   8569   2577   3646     83       C  
ATOM   6003  C   GLY F 132      20.887  -0.690 -23.455  1.00 88.16           C  
ANISOU 6003  C   GLY F 132    11840  12834   8824   2382   3298    -72       C  
ATOM   6004  O   GLY F 132      21.979  -0.808 -22.898  1.00 89.04           O  
ANISOU 6004  O   GLY F 132    11534  13158   9138   2338   3410   -186       O  
ATOM   6005  N   THR F 133      19.724  -0.917 -22.813  1.00 80.17           N  
ANISOU 6005  N   THR F 133    11012  11603   7846   2285   2880    -83       N  
ATOM   6006  CA  THR F 133      19.660  -1.337 -21.406  1.00 77.14           C  
ANISOU 6006  CA  THR F 133    10392  11199   7718   2131   2546   -205       C  
ATOM   6007  C   THR F 133      18.962  -2.689 -21.306  1.00 77.71           C  
ANISOU 6007  C   THR F 133    10741  11142   7642   2366   2101   -316       C  
ATOM   6008  O   THR F 133      18.301  -3.106 -22.252  1.00 76.59           O  
ANISOU 6008  O   THR F 133    10974  10890   7236   2573   2010   -302       O  
ATOM   6009  CB  THR F 133      19.013  -0.248 -20.528  1.00 86.20           C  
ANISOU 6009  CB  THR F 133    11440  12214   9100   1742   2509   -107       C  
ATOM   6010  OG1 THR F 133      17.756   0.159 -21.084  1.00 93.12           O  
ANISOU 6010  OG1 THR F 133    12695  12881   9807   1722   2428     29       O  
ATOM   6011  CG2 THR F 133      19.902   0.974 -20.378  1.00 85.13           C  
ANISOU 6011  CG2 THR F 133    10963  12190   9192   1475   2917    -51       C  
ATOM   6012  N   ALA F 134      19.140  -3.383 -20.170  1.00 72.67           N  
ANISOU 6012  N   ALA F 134     9928  10512   7170   2344   1828   -434       N  
ATOM   6013  CA  ALA F 134      18.563  -4.707 -19.927  1.00 70.72           C  
ANISOU 6013  CA  ALA F 134     9935  10107   6828   2532   1425   -531       C  
ATOM   6014  C   ALA F 134      18.120  -4.848 -18.481  1.00 69.86           C  
ANISOU 6014  C   ALA F 134     9704   9903   6938   2321   1146   -538       C  
ATOM   6015  O   ALA F 134      18.943  -4.731 -17.579  1.00 67.32           O  
ANISOU 6015  O   ALA F 134     9046   9739   6793   2269   1183   -598       O  
ATOM   6016  CB  ALA F 134      19.587  -5.781 -20.245  1.00 74.30           C  
ANISOU 6016  CB  ALA F 134    10367  10701   7164   2903   1426   -687       C  
ATOM   6017  N   SER F 135      16.824  -5.099 -18.260  1.00 64.88           N  
ANISOU 6017  N   SER F 135     9330   9032   6288   2209    870   -484       N  
ATOM   6018  CA  SER F 135      16.268  -5.280 -16.929  1.00 61.31           C  
ANISOU 6018  CA  SER F 135     8806   8479   6010   2020    620   -463       C  
ATOM   6019  C   SER F 135      15.860  -6.737 -16.779  1.00 64.13           C  
ANISOU 6019  C   SER F 135     9434   8642   6289   2196    302   -536       C  
ATOM   6020  O   SER F 135      15.027  -7.232 -17.539  1.00 61.18           O  
ANISOU 6020  O   SER F 135     9377   8089   5782   2255    164   -547       O  
ATOM   6021  CB  SER F 135      15.065  -4.367 -16.712  1.00 61.51           C  
ANISOU 6021  CB  SER F 135     8882   8389   6100   1724    582   -333       C  
ATOM   6022  OG  SER F 135      15.427  -3.010 -16.912  1.00 69.44           O  
ANISOU 6022  OG  SER F 135     9694   9520   7172   1568    884   -260       O  
ATOM   6023  N   VAL F 136      16.433  -7.414 -15.773  1.00 62.64           N  
ANISOU 6023  N   VAL F 136     9134   8481   6186   2285    177   -593       N  
ATOM   6024  CA  VAL F 136      16.099  -8.793 -15.459  1.00 63.49           C  
ANISOU 6024  CA  VAL F 136     9516   8363   6243   2438   -110   -640       C  
ATOM   6025  C   VAL F 136      15.269  -8.679 -14.178  1.00 66.91           C  
ANISOU 6025  C   VAL F 136     9913   8678   6831   2173   -271   -528       C  
ATOM   6026  O   VAL F 136      15.705  -8.008 -13.243  1.00 65.54           O  
ANISOU 6026  O   VAL F 136     9445   8677   6780   2072   -197   -500       O  
ATOM   6027  CB  VAL F 136      17.352  -9.673 -15.290  1.00 69.64           C  
ANISOU 6027  CB  VAL F 136    10244   9251   6963   2792   -123   -771       C  
ATOM   6028  CG1 VAL F 136      16.984 -11.137 -15.417  1.00 70.76           C  
ANISOU 6028  CG1 VAL F 136    10788   9097   6999   3002   -388   -828       C  
ATOM   6029  CG2 VAL F 136      18.431  -9.298 -16.303  1.00 71.32           C  
ANISOU 6029  CG2 VAL F 136    10296   9729   7074   2998    152   -863       C  
ATOM   6030  N   VAL F 137      14.060  -9.274 -14.159  1.00 64.05           N  
ANISOU 6030  N   VAL F 137     9833   8037   6467   2052   -481   -474       N  
ATOM   6031  CA  VAL F 137      13.116  -9.146 -13.049  1.00 62.58           C  
ANISOU 6031  CA  VAL F 137     9624   7741   6412   1784   -602   -348       C  
ATOM   6032  C   VAL F 137      12.816 -10.489 -12.378  1.00 69.90           C  
ANISOU 6032  C   VAL F 137    108