CNRS Nantes University UFIP UFIP
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***  gne  ***

elNémo ID: 20072412394531508

Job options:

ID        	=	 20072412394531508
JOBID     	=	 gne
USERID    	=	 unknown
PRIVAT    	=	 0

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

DOPROJMODS	=	 0
DORMSD    	=	 0

NRBL      	=	 0
CUTOFF    	=	 0
CAONLY    	=	 0


Input data for this run:

HEADER gne

HEADER    ISOMERASE                               27-APR-15   4ZHT              
TITLE     CRYSTAL STRUCTURE OF UDP-GLCNAC 2-EPIMERASE                           
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: BIFUNCTIONAL UDP-N-ACETYLGLUCOSAMINE 2-EPIMERASE/N-        
COMPND   3 ACETYLMANNOSAMINE KINASE;                                            
COMPND   4 CHAIN: A, B, C, D;                                                   
COMPND   5 FRAGMENT: UNP RESIDUES 1-405;                                        
COMPND   6 SYNONYM: UDP-GLCNAC-2-EPIMERASE/MANAC KINASE;                        
COMPND   7 EC: 3.2.1.183;                                                       
COMPND   8 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: GNE, GLCNE;                                                    
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 511693;                                     
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21                                       
KEYWDS    INHIBITOR, COMPLEX, EPIMERASE, ISOMERASE                              
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    S.C.CHEN,C.S.YANG,T.P.KO,Y.CHEN                                       
REVDAT   2   09-NOV-16 4ZHT    1       JRNL                                     
REVDAT   1   01-JUN-16 4ZHT    0                                                
JRNL        AUTH   S.C.CHEN,C.H.HUANG,S.J.LAI,C.S.YANG,T.H.HSIAO,C.H.LIN,       
JRNL        AUTH 2 P.K.FU,T.P.KO,Y.CHEN                                         
JRNL        TITL   MECHANISM AND INHIBITION OF HUMAN UDP-GLCNAC 2-EPIMERASE,    
JRNL        TITL 2 THE KEY ENZYME IN SIALIC ACID BIOSYNTHESIS.                  
JRNL        REF    SCI REP                       V.   6 23274 2016              
JRNL        REFN                   ESSN 2045-2322                               
JRNL        PMID   26980148                                                     
JRNL        DOI    10.1038/SREP23274                                            
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.69 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.8.0103                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.69                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 30.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.4                           
REMARK   3   NUMBER OF REFLECTIONS             : 41334                          
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) : 0.191                           
REMARK   3   R VALUE            (WORKING SET) : 0.189                           
REMARK   3   FREE R VALUE                     : 0.225                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2183                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.69                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.76                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 2940                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 96.29                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2930                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 151                          
REMARK   3   BIN FREE R VALUE                    : 0.3300                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 12071                                   
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 279                                     
REMARK   3   SOLVENT ATOMS            : 331                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 76.45                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 1.97000                                              
REMARK   3    B22 (A**2) : 0.42000                                              
REMARK   3    B33 (A**2) : -2.49000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.74000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): NULL          
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.342         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.287         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 27.699        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.956                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.938                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A): 12587 ; 0.011 ; 0.019       
REMARK   3   BOND LENGTHS OTHERS               (A): 12234 ; 0.006 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 17034 ; 1.640 ; 2.000       
REMARK   3   BOND ANGLES OTHERS          (DEGREES): 28155 ; 1.405 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  1528 ; 6.865 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   554 ;35.957 ;23.736       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  2106 ;17.096 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    88 ;18.431 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  1957 ; 0.088 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A): 13868 ; 0.008 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  2833 ; 0.005 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  6124 ; 1.974 ; 4.401       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  6123 ; 1.973 ; 4.401       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  7648 ; 3.335 ; 6.600       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  7649 ; 3.335 ; 6.601       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  6463 ; 2.330 ; 4.752       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  6464 ; 2.330 ; 4.752       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  9387 ; 3.783 ; 7.018       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2): 13387 ; 6.568 ;35.339       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2): 13367 ; 6.555 ;35.294       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NCS TYPE: LOCAL                                                    
REMARK   3   NUMBER OF DIFFERENT NCS PAIRS  : 6                                 
REMARK   3  GROUP  CHAIN1    RANGE     CHAIN2     RANGE    COUNT RMS  WEIGHT    
REMARK   3    1     A     8    388       B     8    388   49162  0.07  0.05     
REMARK   3    2     A     7    387       C     7    387   49336  0.06  0.05     
REMARK   3    3     A     8    389       D     8    389   49626  0.06  0.05     
REMARK   3    4     B     8    387       C     8    387   49204  0.06  0.05     
REMARK   3    5     B     8    388       D     8    388   49500  0.06  0.05     
REMARK   3    6     C     8    387       D     8    387   49162  0.07  0.05     
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 4                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A     7        A   390                          
REMARK   3    ORIGIN FOR THE GROUP (A):   0.4239  68.5287  52.6858              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6671 T22:   0.1284                                     
REMARK   3      T33:   0.0243 T12:  -0.0541                                     
REMARK   3      T13:  -0.0709 T23:   0.0005                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.8026 L22:   1.1509                                     
REMARK   3      L33:   1.9916 L12:  -0.1184                                     
REMARK   3      L13:  -0.7946 L23:   0.0885                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0161 S12:   0.2678 S13:   0.1219                       
REMARK   3      S21:  -0.1907 S22:   0.0840 S23:   0.0091                       
REMARK   3      S31:  -0.3200 S32:  -0.1171 S33:  -0.0679                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B     8        B   389                          
REMARK   3    ORIGIN FOR THE GROUP (A): -31.6348  50.9145  66.3786              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4835 T22:   0.2278                                     
REMARK   3      T33:   0.1524 T12:  -0.0488                                     
REMARK   3      T13:  -0.1361 T23:  -0.0462                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.9981 L22:   1.3066                                     
REMARK   3      L33:   1.2272 L12:   0.0542                                     
REMARK   3      L13:  -0.5014 L23:   0.3284                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0921 S12:   0.3719 S13:  -0.2967                       
REMARK   3      S21:  -0.2066 S22:  -0.0292 S23:   0.3281                       
REMARK   3      S31:   0.0283 S32:  -0.5018 S33:   0.1213                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   C     6        C   388                          
REMARK   3    ORIGIN FOR THE GROUP (A):  15.9890  38.3485  13.3363              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2117 T22:   0.1417                                     
REMARK   3      T33:   0.1582 T12:  -0.0871                                     
REMARK   3      T13:  -0.0233 T23:  -0.0519                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.3655 L22:   2.3974                                     
REMARK   3      L33:   1.8796 L12:   0.0707                                     
REMARK   3      L13:   0.4523 L23:   0.5626                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0933 S12:  -0.0523 S13:  -0.2849                       
REMARK   3      S21:   0.2004 S22:   0.1798 S23:  -0.4825                       
REMARK   3      S31:  -0.2928 S32:   0.2569 S33:  -0.2732                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   D     8        D   390                          
REMARK   3    ORIGIN FOR THE GROUP (A):   0.1060   3.3021  20.8672              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4686 T22:   0.1076                                     
REMARK   3      T33:   0.3047 T12:  -0.1254                                     
REMARK   3      T13:  -0.2127 T23:   0.1751                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.0892 L22:   3.3764                                     
REMARK   3      L33:   2.3229 L12:  -0.1234                                     
REMARK   3      L13:   0.4462 L23:   0.2993                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.4062 S12:  -0.2420 S13:  -0.3964                       
REMARK   3      S21:   0.9306 S22:   0.0319 S23:   0.0706                       
REMARK   3      S31:   0.4457 S32:  -0.1476 S33:  -0.4381                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS                                                           
REMARK   4                                                                      
REMARK   4 4ZHT COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 01-MAY-15.                  
REMARK 100 THE DEPOSITION ID IS D_1000209314.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 19-APR-14                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.1                                
REMARK 200  NUMBER OF CRYSTALS USED        : NULL                               
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : NSRRC                              
REMARK 200  BEAMLINE                       : BL13B1                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9791                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315R                  
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 43536                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.690                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 30.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.8                               
REMARK 200  DATA REDUNDANCY                : 7.500                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 14.8000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD                          
REMARK 200 SOFTWARE USED: PHENIX                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 42.87                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.15                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2 M AMMONIUM ACETATE, 0.1 M HEPES,     
REMARK 280  PH 7.1, 19% PEG 3350, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE    
REMARK 280  277K                                                                
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1                          
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y,-Z                                                 
REMARK 290       3555   X+1/2,Y+1/2,Z                                           
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        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   3  1.000000  0.000000  0.000000       53.02050            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       49.05100            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000       53.02050            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       49.05100            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
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: 19750 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 49730 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -104.0 KCAL/MOL                       
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   2 -1.000000  0.000000  0.000000      -16.30713            
REMARK 350   BIOMT2   2  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000      153.86024            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
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: 20480 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 49470 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -94.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D                                  
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 350   BIOMT1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   2  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 375                                                                      
REMARK 375 SPECIAL POSITION                                                     
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS            
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL          
REMARK 375 POSITIONS.                                                           
REMARK 375                                                                      
REMARK 375 ATOM RES CSSEQI                                                      
REMARK 375      HOH A 667  LIES ON A SPECIAL POSITION.                          
REMARK 375      HOH B 644  LIES ON A SPECIAL POSITION.                          
REMARK 375      HOH B 662  LIES ON A SPECIAL POSITION.                          
REMARK 375      HOH B 664  LIES ON A SPECIAL POSITION.                          
REMARK 375      HOH C 635  LIES ON A SPECIAL POSITION.                          
REMARK 375      HOH C 648  LIES ON A SPECIAL POSITION.                          
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     MSE A     1                                                      
REMARK 465     GLU A     2                                                      
REMARK 465     LYS A     3                                                      
REMARK 465     ASN A     4                                                      
REMARK 465     GLY A     5                                                      
REMARK 465     ASN A     6                                                      
REMARK 465     PRO A   391                                                      
REMARK 465     VAL A   392                                                      
REMARK 465     LYS A   393                                                      
REMARK 465     GLU A   394                                                      
REMARK 465     ASN A   395                                                      
REMARK 465     ILE A   396                                                      
REMARK 465     SER A   397                                                      
REMARK 465     GLN A   398                                                      
REMARK 465     ASP A   399                                                      
REMARK 465     ILE A   400                                                      
REMARK 465     ASP A   401                                                      
REMARK 465     HIS A   402                                                      
REMARK 465     ILE A   403                                                      
REMARK 465     LEU A   404                                                      
REMARK 465     GLU A   405                                                      
REMARK 465     HIS A   406                                                      
REMARK 465     HIS A   407                                                      
REMARK 465     HIS A   408                                                      
REMARK 465     HIS A   409                                                      
REMARK 465     HIS A   410                                                      
REMARK 465     HIS A   411                                                      
REMARK 465     MSE B     1                                                      
REMARK 465     GLU B     2                                                      
REMARK 465     LYS B     3                                                      
REMARK 465     ASN B     4                                                      
REMARK 465     GLY B     5                                                      
REMARK 465     ASN B     6                                                      
REMARK 465     ASN B     7                                                      
REMARK 465     PRO B   390                                                      
REMARK 465     PRO B   391                                                      
REMARK 465     VAL B   392                                                      
REMARK 465     LYS B   393                                                      
REMARK 465     GLU B   394                                                      
REMARK 465     ASN B   395                                                      
REMARK 465     ILE B   396                                                      
REMARK 465     SER B   397                                                      
REMARK 465     GLN B   398                                                      
REMARK 465     ASP B   399                                                      
REMARK 465     ILE B   400                                                      
REMARK 465     ASP B   401                                                      
REMARK 465     HIS B   402                                                      
REMARK 465     ILE B   403                                                      
REMARK 465     LEU B   404                                                      
REMARK 465     GLU B   405                                                      
REMARK 465     HIS B   406                                                      
REMARK 465     HIS B   407                                                      
REMARK 465     HIS B   408                                                      
REMARK 465     HIS B   409                                                      
REMARK 465     HIS B   410                                                      
REMARK 465     HIS B   411                                                      
REMARK 465     MSE C     1                                                      
REMARK 465     GLU C     2                                                      
REMARK 465     LYS C     3                                                      
REMARK 465     ASN C     4                                                      
REMARK 465     GLY C     5                                                      
REMARK 465     PHE C   389                                                      
REMARK 465     PRO C   390                                                      
REMARK 465     PRO C   391                                                      
REMARK 465     VAL C   392                                                      
REMARK 465     LYS C   393                                                      
REMARK 465     GLU C   394                                                      
REMARK 465     ASN C   395                                                      
REMARK 465     ILE C   396                                                      
REMARK 465     SER C   397                                                      
REMARK 465     GLN C   398                                                      
REMARK 465     ASP C   399                                                      
REMARK 465     ILE C   400                                                      
REMARK 465     ASP C   401                                                      
REMARK 465     HIS C   402                                                      
REMARK 465     ILE C   403                                                      
REMARK 465     LEU C   404                                                      
REMARK 465     GLU C   405                                                      
REMARK 465     HIS C   406                                                      
REMARK 465     HIS C   407                                                      
REMARK 465     HIS C   408                                                      
REMARK 465     HIS C   409                                                      
REMARK 465     HIS C   410                                                      
REMARK 465     HIS C   411                                                      
REMARK 465     MSE D     1                                                      
REMARK 465     GLU D     2                                                      
REMARK 465     LYS D     3                                                      
REMARK 465     ASN D     4                                                      
REMARK 465     GLY D     5                                                      
REMARK 465     ASN D     6                                                      
REMARK 465     ASN D     7                                                      
REMARK 465     PRO D   391                                                      
REMARK 465     VAL D   392                                                      
REMARK 465     LYS D   393                                                      
REMARK 465     GLU D   394                                                      
REMARK 465     ASN D   395                                                      
REMARK 465     ILE D   396                                                      
REMARK 465     SER D   397                                                      
REMARK 465     GLN D   398                                                      
REMARK 465     ASP D   399                                                      
REMARK 465     ILE D   400                                                      
REMARK 465     ASP D   401                                                      
REMARK 465     HIS D   402                                                      
REMARK 465     ILE D   403                                                      
REMARK 465     LEU D   404                                                      
REMARK 465     GLU D   405                                                      
REMARK 465     HIS D   406                                                      
REMARK 465     HIS D   407                                                      
REMARK 465     HIS D   408                                                      
REMARK 465     HIS D   409                                                      
REMARK 465     HIS D   410                                                      
REMARK 465     HIS D   411                                                      
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   O    GLN D   354     O    HOH D   601              2.01            
REMARK 500   O    GLY A   135     O    HOH A   601              2.06            
REMARK 500   NH2  ARG A     8     OD2  ASP A   105              2.07            
REMARK 500   NH2  ARG C    59     O    HOH C   601              2.08            
REMARK 500   O    GLU C   329     O    HOH C   602              2.09            
REMARK 500   NE2  GLN A   380     O    HOH A   602              2.10            
REMARK 500   O    LEU B   189     O    HOH B   601              2.10            
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    ARG A   8   NE  -  CZ  -  NH1 ANGL. DEV. =   4.4 DEGREES          
REMARK 500    ARG A 177   NE  -  CZ  -  NH1 ANGL. DEV. =   4.0 DEGREES          
REMARK 500    LYS A 195   CD  -  CE  -  NZ  ANGL. DEV. =  17.0 DEGREES          
REMARK 500    LYS A 212   CD  -  CE  -  NZ  ANGL. DEV. =  17.9 DEGREES          
REMARK 500    ASP A 225   CB  -  CG  -  OD1 ANGL. DEV. =   5.5 DEGREES          
REMARK 500    ARG B 177   NE  -  CZ  -  NH1 ANGL. DEV. =   4.0 DEGREES          
REMARK 500    ARG B 202   NE  -  CZ  -  NH1 ANGL. DEV. =  -3.6 DEGREES          
REMARK 500    ARG B 263   NE  -  CZ  -  NH2 ANGL. DEV. =   3.0 DEGREES          
REMARK 500    ARG C 177   NE  -  CZ  -  NH1 ANGL. DEV. =   4.1 DEGREES          
REMARK 500    ARG C 263   NE  -  CZ  -  NH2 ANGL. DEV. =   3.0 DEGREES          
REMARK 500    ARG D 177   NE  -  CZ  -  NH1 ANGL. DEV. =   4.2 DEGREES          
REMARK 500    ARG D 335   NE  -  CZ  -  NH1 ANGL. DEV. =   3.6 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    ASN A  56       59.29     31.29                                   
REMARK 500    GLU A 134       44.29     75.56                                   
REMARK 500    LYS A 193       83.91    -61.57                                   
REMARK 500    ASN A 194       99.41    -47.00                                   
REMARK 500    LYS A 195     -155.21    -73.67                                   
REMARK 500    ASP A 196       83.17    -56.34                                   
REMARK 500    ASN A 300       27.99   -145.68                                   
REMARK 500    GLN A 322        3.69     87.79                                   
REMARK 500    GLU A 381      -91.43   -162.10                                   
REMARK 500    ASN B  56       59.97     30.86                                   
REMARK 500    GLU B 134       44.55     74.56                                   
REMARK 500    LYS B 193       90.22    -17.84                                   
REMARK 500    LYS B 195     -156.43    -72.61                                   
REMARK 500    ASP B 196       84.51    -56.41                                   
REMARK 500    ASN B 300       27.39   -145.20                                   
REMARK 500    GLN B 322        4.46     86.22                                   
REMARK 500    GLU B 381      -91.58   -161.41                                   
REMARK 500    ASN C  56       59.69     30.24                                   
REMARK 500    GLU C 134       44.22     74.48                                   
REMARK 500    LYS C 193       88.47    -16.36                                   
REMARK 500    LYS C 195     -160.91    -72.12                                   
REMARK 500    ASP C 196       84.62    -54.44                                   
REMARK 500    ASN C 300       27.72   -145.59                                   
REMARK 500    GLN C 322        5.68     87.04                                   
REMARK 500    GLU C 381      -91.72   -162.66                                   
REMARK 500    ASN D  56       59.98     30.61                                   
REMARK 500    GLU D 134       44.54     74.75                                   
REMARK 500    LYS D 193       84.14    -62.96                                   
REMARK 500    ASN D 194       98.85    -46.08                                   
REMARK 500    LYS D 195     -156.47    -72.31                                   
REMARK 500    ASP D 196       83.74    -56.75                                   
REMARK 500    ASN D 300       27.44   -144.28                                   
REMARK 500    GLN D 322        4.72     86.41                                   
REMARK 500    GLU D 381      -91.87   -161.90                                   
REMARK 500    CYS D 388       69.57   -100.86                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS                                         
REMARK 500                                                                      
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH          
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED           
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND               
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.                                  
REMARK 500                                 MODEL     OMEGA                      
REMARK 500 ALA B  192     LYS B  193                  142.78                    
REMARK 500 ALA C  192     LYS C  193                  141.49                    
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH A 700        DISTANCE =  6.54 ANGSTROMS                       
REMARK 525    HOH A 701        DISTANCE =  6.95 ANGSTROMS                       
REMARK 525    HOH B 673        DISTANCE =  6.11 ANGSTROMS                       
REMARK 525    HOH B 674        DISTANCE =  6.47 ANGSTROMS                       
REMARK 525    HOH B 675        DISTANCE =  6.50 ANGSTROMS                       
REMARK 525    HOH B 676        DISTANCE =  6.64 ANGSTROMS                       
REMARK 525    HOH B 677        DISTANCE =  6.64 ANGSTROMS                       
REMARK 525    HOH B 678        DISTANCE =  8.06 ANGSTROMS                       
REMARK 525    HOH C 691        DISTANCE =  5.82 ANGSTROMS                       
REMARK 525    HOH C 692        DISTANCE =  5.98 ANGSTROMS                       
REMARK 525    HOH C 693        DISTANCE =  6.05 ANGSTROMS                       
REMARK 525    HOH C 694        DISTANCE =  6.08 ANGSTROMS                       
REMARK 525    HOH C 695        DISTANCE =  6.13 ANGSTROMS                       
REMARK 525    HOH C 696        DISTANCE =  6.20 ANGSTROMS                       
REMARK 525    HOH C 697        DISTANCE =  6.48 ANGSTROMS                       
REMARK 525    HOH C 698        DISTANCE =  7.82 ANGSTROMS                       
REMARK 525    HOH D 652        DISTANCE =  6.32 ANGSTROMS                       
REMARK 525    HOH D 653        DISTANCE =  6.80 ANGSTROMS                       
REMARK 525    HOH D 654        DISTANCE =  7.28 ANGSTROMS                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue UDP A 501                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue NCC A 502                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue UDP B 501                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue NCC B 502                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue UDP C 501                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue NCC C 502                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue BM7 C 503                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue UDP D 501                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue NCC D 502                 
DBREF  4ZHT A    1   405  UNP    Q9Y223   GLCNE_HUMAN      1    405             
DBREF  4ZHT B    1   405  UNP    Q9Y223   GLCNE_HUMAN      1    405             
DBREF  4ZHT C    1   405  UNP    Q9Y223   GLCNE_HUMAN      1    405             
DBREF  4ZHT D    1   405  UNP    Q9Y223   GLCNE_HUMAN      1    405             
SEQADV 4ZHT HIS A  406  UNP  Q9Y223              EXPRESSION TAG                 
SEQADV 4ZHT HIS A  407  UNP  Q9Y223              EXPRESSION TAG                 
SEQADV 4ZHT HIS A  408  UNP  Q9Y223              EXPRESSION TAG                 
SEQADV 4ZHT HIS A  409  UNP  Q9Y223              EXPRESSION TAG                 
SEQADV 4ZHT HIS A  410  UNP  Q9Y223              EXPRESSION TAG                 
SEQADV 4ZHT HIS A  411  UNP  Q9Y223              EXPRESSION TAG                 
SEQADV 4ZHT HIS B  406  UNP  Q9Y223              EXPRESSION TAG                 
SEQADV 4ZHT HIS B  407  UNP  Q9Y223              EXPRESSION TAG                 
SEQADV 4ZHT HIS B  408  UNP  Q9Y223              EXPRESSION TAG                 
SEQADV 4ZHT HIS B  409  UNP  Q9Y223              EXPRESSION TAG                 
SEQADV 4ZHT HIS B  410  UNP  Q9Y223              EXPRESSION TAG                 
SEQADV 4ZHT HIS B  411  UNP  Q9Y223              EXPRESSION TAG                 
SEQADV 4ZHT HIS C  406  UNP  Q9Y223              EXPRESSION TAG                 
SEQADV 4ZHT HIS C  407  UNP  Q9Y223              EXPRESSION TAG                 
SEQADV 4ZHT HIS C  408  UNP  Q9Y223              EXPRESSION TAG                 
SEQADV 4ZHT HIS C  409  UNP  Q9Y223              EXPRESSION TAG                 
SEQADV 4ZHT HIS C  410  UNP  Q9Y223              EXPRESSION TAG                 
SEQADV 4ZHT HIS C  411  UNP  Q9Y223              EXPRESSION TAG                 
SEQADV 4ZHT HIS D  406  UNP  Q9Y223              EXPRESSION TAG                 
SEQADV 4ZHT HIS D  407  UNP  Q9Y223              EXPRESSION TAG                 
SEQADV 4ZHT HIS D  408  UNP  Q9Y223              EXPRESSION TAG                 
SEQADV 4ZHT HIS D  409  UNP  Q9Y223              EXPRESSION TAG                 
SEQADV 4ZHT HIS D  410  UNP  Q9Y223              EXPRESSION TAG                 
SEQADV 4ZHT HIS D  411  UNP  Q9Y223              EXPRESSION TAG                 
SEQRES   1 A  411  MSE GLU LYS ASN GLY ASN ASN ARG LYS LEU ARG VAL CYS          
SEQRES   2 A  411  VAL ALA THR CYS ASN ARG ALA ASP TYR SER LYS LEU ALA          
SEQRES   3 A  411  PRO ILE MSE PHE GLY ILE LYS THR GLU PRO GLU PHE PHE          
SEQRES   4 A  411  GLU LEU ASP VAL VAL VAL LEU GLY SER HIS LEU ILE ASP          
SEQRES   5 A  411  ASP TYR GLY ASN THR TYR ARG MSE ILE GLU GLN ASP ASP          
SEQRES   6 A  411  PHE ASP ILE ASN THR ARG LEU HIS THR ILE VAL ARG GLY          
SEQRES   7 A  411  GLU ASP GLU ALA ALA MSE VAL GLU SER VAL GLY LEU ALA          
SEQRES   8 A  411  LEU VAL LYS LEU PRO ASP VAL LEU ASN ARG LEU LYS PRO          
SEQRES   9 A  411  ASP ILE MSE ILE VAL HIS GLY ASP ARG PHE ASP ALA LEU          
SEQRES  10 A  411  ALA LEU ALA THR SER ALA ALA LEU MSE ASN ILE ARG ILE          
SEQRES  11 A  411  LEU HIS ILE GLU GLY GLY GLU VAL SER GLY THR ILE ASP          
SEQRES  12 A  411  ASP SER ILE ARG HIS ALA ILE THR LYS LEU ALA HIS TYR          
SEQRES  13 A  411  HIS VAL CYS CYS THR ARG SER ALA GLU GLN HIS LEU ILE          
SEQRES  14 A  411  SER MSE CYS GLU ASP HIS ASP ARG ILE LEU LEU ALA GLY          
SEQRES  15 A  411  CYS PRO SER TYR ASP LYS LEU LEU SER ALA LYS ASN LYS          
SEQRES  16 A  411  ASP TYR MSE SER ILE ILE ARG MSE TRP LEU GLY ASP ASP          
SEQRES  17 A  411  VAL LYS SER LYS ASP TYR ILE VAL ALA LEU GLN HIS PRO          
SEQRES  18 A  411  VAL THR THR ASP ILE LYS HIS SER ILE LYS MSE PHE GLU          
SEQRES  19 A  411  LEU THR LEU ASP ALA LEU ILE SER PHE ASN LYS ARG THR          
SEQRES  20 A  411  LEU VAL LEU PHE PRO ASN ILE ASP ALA GLY SER LYS GLU          
SEQRES  21 A  411  MSE VAL ARG VAL MSE ARG LYS LYS GLY ILE GLU HIS HIS          
SEQRES  22 A  411  PRO ASN PHE ARG ALA VAL LYS HIS VAL PRO PHE ASP GLN          
SEQRES  23 A  411  PHE ILE GLN LEU VAL ALA HIS ALA GLY CYS MSE ILE GLY          
SEQRES  24 A  411  ASN SER SER CYS GLY VAL ARG GLU VAL GLY ALA PHE GLY          
SEQRES  25 A  411  THR PRO VAL ILE ASN LEU GLY THR ARG GLN ILE GLY ARG          
SEQRES  26 A  411  GLU THR GLY GLU ASN VAL LEU HIS VAL ARG ASP ALA ASP          
SEQRES  27 A  411  THR GLN ASP LYS ILE LEU GLN ALA LEU HIS LEU GLN PHE          
SEQRES  28 A  411  GLY LYS GLN TYR PRO CYS SER LYS ILE TYR GLY ASP GLY          
SEQRES  29 A  411  ASN ALA VAL PRO ARG ILE LEU LYS PHE LEU LYS SER ILE          
SEQRES  30 A  411  ASP LEU GLN GLU PRO LEU GLN LYS LYS PHE CYS PHE PRO          
SEQRES  31 A  411  PRO VAL LYS GLU ASN ILE SER GLN ASP ILE ASP HIS ILE          
SEQRES  32 A  411  LEU GLU HIS HIS HIS HIS HIS HIS                              
SEQRES   1 B  411  MSE GLU LYS ASN GLY ASN ASN ARG LYS LEU ARG VAL CYS          
SEQRES   2 B  411  VAL ALA THR CYS ASN ARG ALA ASP TYR SER LYS LEU ALA          
SEQRES   3 B  411  PRO ILE MSE PHE GLY ILE LYS THR GLU PRO GLU PHE PHE          
SEQRES   4 B  411  GLU LEU ASP VAL VAL VAL LEU GLY SER HIS LEU ILE ASP          
SEQRES   5 B  411  ASP TYR GLY ASN THR TYR ARG MSE ILE GLU GLN ASP ASP          
SEQRES   6 B  411  PHE ASP ILE ASN THR ARG LEU HIS THR ILE VAL ARG GLY          
SEQRES   7 B  411  GLU ASP GLU ALA ALA MSE VAL GLU SER VAL GLY LEU ALA          
SEQRES   8 B  411  LEU VAL LYS LEU PRO ASP VAL LEU ASN ARG LEU LYS PRO          
SEQRES   9 B  411  ASP ILE MSE ILE VAL HIS GLY ASP ARG PHE ASP ALA LEU          
SEQRES  10 B  411  ALA LEU ALA THR SER ALA ALA LEU MSE ASN ILE ARG ILE          
SEQRES  11 B  411  LEU HIS ILE GLU GLY GLY GLU VAL SER GLY THR ILE ASP          
SEQRES  12 B  411  ASP SER ILE ARG HIS ALA ILE THR LYS LEU ALA HIS TYR          
SEQRES  13 B  411  HIS VAL CYS CYS THR ARG SER ALA GLU GLN HIS LEU ILE          
SEQRES  14 B  411  SER MSE CYS GLU ASP HIS ASP ARG ILE LEU LEU ALA GLY          
SEQRES  15 B  411  CYS PRO SER TYR ASP LYS LEU LEU SER ALA LYS ASN LYS          
SEQRES  16 B  411  ASP TYR MSE SER ILE ILE ARG MSE TRP LEU GLY ASP ASP          
SEQRES  17 B  411  VAL LYS SER LYS ASP TYR ILE VAL ALA LEU GLN HIS PRO          
SEQRES  18 B  411  VAL THR THR ASP ILE LYS HIS SER ILE LYS MSE PHE GLU          
SEQRES  19 B  411  LEU THR LEU ASP ALA LEU ILE SER PHE ASN LYS ARG THR          
SEQRES  20 B  411  LEU VAL LEU PHE PRO ASN ILE ASP ALA GLY SER LYS GLU          
SEQRES  21 B  411  MSE VAL ARG VAL MSE ARG LYS LYS GLY ILE GLU HIS HIS          
SEQRES  22 B  411  PRO ASN PHE ARG ALA VAL LYS HIS VAL PRO PHE ASP GLN          
SEQRES  23 B  411  PHE ILE GLN LEU VAL ALA HIS ALA GLY CYS MSE ILE GLY          
SEQRES  24 B  411  ASN SER SER CYS GLY VAL ARG GLU VAL GLY ALA PHE GLY          
SEQRES  25 B  411  THR PRO VAL ILE ASN LEU GLY THR ARG GLN ILE GLY ARG          
SEQRES  26 B  411  GLU THR GLY GLU ASN VAL LEU HIS VAL ARG ASP ALA ASP          
SEQRES  27 B  411  THR GLN ASP LYS ILE LEU GLN ALA LEU HIS LEU GLN PHE          
SEQRES  28 B  411  GLY LYS GLN TYR PRO CYS SER LYS ILE TYR GLY ASP GLY          
SEQRES  29 B  411  ASN ALA VAL PRO ARG ILE LEU LYS PHE LEU LYS SER ILE          
SEQRES  30 B  411  ASP LEU GLN GLU PRO LEU GLN LYS LYS PHE CYS PHE PRO          
SEQRES  31 B  411  PRO VAL LYS GLU ASN ILE SER GLN ASP ILE ASP HIS ILE          
SEQRES  32 B  411  LEU GLU HIS HIS HIS HIS HIS HIS                              
SEQRES   1 C  411  MSE GLU LYS ASN GLY ASN ASN ARG LYS LEU ARG VAL CYS          
SEQRES   2 C  411  VAL ALA THR CYS ASN ARG ALA ASP TYR SER LYS LEU ALA          
SEQRES   3 C  411  PRO ILE MSE PHE GLY ILE LYS THR GLU PRO GLU PHE PHE          
SEQRES   4 C  411  GLU LEU ASP VAL VAL VAL LEU GLY SER HIS LEU ILE ASP          
SEQRES   5 C  411  ASP TYR GLY ASN THR TYR ARG MSE ILE GLU GLN ASP ASP          
SEQRES   6 C  411  PHE ASP ILE ASN THR ARG LEU HIS THR ILE VAL ARG GLY          
SEQRES   7 C  411  GLU ASP GLU ALA ALA MSE VAL GLU SER VAL GLY LEU ALA          
SEQRES   8 C  411  LEU VAL LYS LEU PRO ASP VAL LEU ASN ARG LEU LYS PRO          
SEQRES   9 C  411  ASP ILE MSE ILE VAL HIS GLY ASP ARG PHE ASP ALA LEU          
SEQRES  10 C  411  ALA LEU ALA THR SER ALA ALA LEU MSE ASN ILE ARG ILE          
SEQRES  11 C  411  LEU HIS ILE GLU GLY GLY GLU VAL SER GLY THR ILE ASP          
SEQRES  12 C  411  ASP SER ILE ARG HIS ALA ILE THR LYS LEU ALA HIS TYR          
SEQRES  13 C  411  HIS VAL CYS CYS THR ARG SER ALA GLU GLN HIS LEU ILE          
SEQRES  14 C  411  SER MSE CYS GLU ASP HIS ASP ARG ILE LEU LEU ALA GLY          
SEQRES  15 C  411  CYS PRO SER TYR ASP LYS LEU LEU SER ALA LYS ASN LYS          
SEQRES  16 C  411  ASP TYR MSE SER ILE ILE ARG MSE TRP LEU GLY ASP ASP          
SEQRES  17 C  411  VAL LYS SER LYS ASP TYR ILE VAL ALA LEU GLN HIS PRO          
SEQRES  18 C  411  VAL THR THR ASP ILE LYS HIS SER ILE LYS MSE PHE GLU          
SEQRES  19 C  411  LEU THR LEU ASP ALA LEU ILE SER PHE ASN LYS ARG THR          
SEQRES  20 C  411  LEU VAL LEU PHE PRO ASN ILE ASP ALA GLY SER LYS GLU          
SEQRES  21 C  411  MSE VAL ARG VAL MSE ARG LYS LYS GLY ILE GLU HIS HIS          
SEQRES  22 C  411  PRO ASN PHE ARG ALA VAL LYS HIS VAL PRO PHE ASP GLN          
SEQRES  23 C  411  PHE ILE GLN LEU VAL ALA HIS ALA GLY CYS MSE ILE GLY          
SEQRES  24 C  411  ASN SER SER CYS GLY VAL ARG GLU VAL GLY ALA PHE GLY          
SEQRES  25 C  411  THR PRO VAL ILE ASN LEU GLY THR ARG GLN ILE GLY ARG          
SEQRES  26 C  411  GLU THR GLY GLU ASN VAL LEU HIS VAL ARG ASP ALA ASP          
SEQRES  27 C  411  THR GLN ASP LYS ILE LEU GLN ALA LEU HIS LEU GLN PHE          
SEQRES  28 C  411  GLY LYS GLN TYR PRO CYS SER LYS ILE TYR GLY ASP GLY          
SEQRES  29 C  411  ASN ALA VAL PRO ARG ILE LEU LYS PHE LEU LYS SER ILE          
SEQRES  30 C  411  ASP LEU GLN GLU PRO LEU GLN LYS LYS PHE CYS PHE PRO          
SEQRES  31 C  411  PRO VAL LYS GLU ASN ILE SER GLN ASP ILE ASP HIS ILE          
SEQRES  32 C  411  LEU GLU HIS HIS HIS HIS HIS HIS                              
SEQRES   1 D  411  MSE GLU LYS ASN GLY ASN ASN ARG LYS LEU ARG VAL CYS          
SEQRES   2 D  411  VAL ALA THR CYS ASN ARG ALA ASP TYR SER LYS LEU ALA          
SEQRES   3 D  411  PRO ILE MSE PHE GLY ILE LYS THR GLU PRO GLU PHE PHE          
SEQRES   4 D  411  GLU LEU ASP VAL VAL VAL LEU GLY SER HIS LEU ILE ASP          
SEQRES   5 D  411  ASP TYR GLY ASN THR TYR ARG MSE ILE GLU GLN ASP ASP          
SEQRES   6 D  411  PHE ASP ILE ASN THR ARG LEU HIS THR ILE VAL ARG GLY          
SEQRES   7 D  411  GLU ASP GLU ALA ALA MSE VAL GLU SER VAL GLY LEU ALA          
SEQRES   8 D  411  LEU VAL LYS LEU PRO ASP VAL LEU ASN ARG LEU LYS PRO          
SEQRES   9 D  411  ASP ILE MSE ILE VAL HIS GLY ASP ARG PHE ASP ALA LEU          
SEQRES  10 D  411  ALA LEU ALA THR SER ALA ALA LEU MSE ASN ILE ARG ILE          
SEQRES  11 D  411  LEU HIS ILE GLU GLY GLY GLU VAL SER GLY THR ILE ASP          
SEQRES  12 D  411  ASP SER ILE ARG HIS ALA ILE THR LYS LEU ALA HIS TYR          
SEQRES  13 D  411  HIS VAL CYS CYS THR ARG SER ALA GLU GLN HIS LEU ILE          
SEQRES  14 D  411  SER MSE CYS GLU ASP HIS ASP ARG ILE LEU LEU ALA GLY          
SEQRES  15 D  411  CYS PRO SER TYR ASP LYS LEU LEU SER ALA LYS ASN LYS          
SEQRES  16 D  411  ASP TYR MSE SER ILE ILE ARG MSE TRP LEU GLY ASP ASP          
SEQRES  17 D  411  VAL LYS SER LYS ASP TYR ILE VAL ALA LEU GLN HIS PRO          
SEQRES  18 D  411  VAL THR THR ASP ILE LYS HIS SER ILE LYS MSE PHE GLU          
SEQRES  19 D  411  LEU THR LEU ASP ALA LEU ILE SER PHE ASN LYS ARG THR          
SEQRES  20 D  411  LEU VAL LEU PHE PRO ASN ILE ASP ALA GLY SER LYS GLU          
SEQRES  21 D  411  MSE VAL ARG VAL MSE ARG LYS LYS GLY ILE GLU HIS HIS          
SEQRES  22 D  411  PRO ASN PHE ARG ALA VAL LYS HIS VAL PRO PHE ASP GLN          
SEQRES  23 D  411  PHE ILE GLN LEU VAL ALA HIS ALA GLY CYS MSE ILE GLY          
SEQRES  24 D  411  ASN SER SER CYS GLY VAL ARG GLU VAL GLY ALA PHE GLY          
SEQRES  25 D  411  THR PRO VAL ILE ASN LEU GLY THR ARG GLN ILE GLY ARG          
SEQRES  26 D  411  GLU THR GLY GLU ASN VAL LEU HIS VAL ARG ASP ALA ASP          
SEQRES  27 D  411  THR GLN ASP LYS ILE LEU GLN ALA LEU HIS LEU GLN PHE          
SEQRES  28 D  411  GLY LYS GLN TYR PRO CYS SER LYS ILE TYR GLY ASP GLY          
SEQRES  29 D  411  ASN ALA VAL PRO ARG ILE LEU LYS PHE LEU LYS SER ILE          
SEQRES  30 D  411  ASP LEU GLN GLU PRO LEU GLN LYS LYS PHE CYS PHE PRO          
SEQRES  31 D  411  PRO VAL LYS GLU ASN ILE SER GLN ASP ILE ASP HIS ILE          
SEQRES  32 D  411  LEU GLU HIS HIS HIS HIS HIS HIS                              
MODRES 4ZHT MSE A   29  MET  MODIFIED RESIDUE                                   
MODRES 4ZHT MSE A   60  MET  MODIFIED RESIDUE                                   
MODRES 4ZHT MSE A   84  MET  MODIFIED RESIDUE                                   
MODRES 4ZHT MSE A  107  MET  MODIFIED RESIDUE                                   
MODRES 4ZHT MSE A  126  MET  MODIFIED RESIDUE                                   
MODRES 4ZHT MSE A  171  MET  MODIFIED RESIDUE                                   
MODRES 4ZHT MSE A  198  MET  MODIFIED RESIDUE                                   
MODRES 4ZHT MSE A  203  MET  MODIFIED RESIDUE                                   
MODRES 4ZHT MSE A  232  MET  MODIFIED RESIDUE                                   
MODRES 4ZHT MSE A  261  MET  MODIFIED RESIDUE                                   
MODRES 4ZHT MSE A  265  MET  MODIFIED RESIDUE                                   
MODRES 4ZHT MSE A  297  MET  MODIFIED RESIDUE                                   
MODRES 4ZHT MSE B   29  MET  MODIFIED RESIDUE                                   
MODRES 4ZHT MSE B   60  MET  MODIFIED RESIDUE                                   
MODRES 4ZHT MSE B   84  MET  MODIFIED RESIDUE                                   
MODRES 4ZHT MSE B  107  MET  MODIFIED RESIDUE                                   
MODRES 4ZHT MSE B  126  MET  MODIFIED RESIDUE                                   
MODRES 4ZHT MSE B  171  MET  MODIFIED RESIDUE                                   
MODRES 4ZHT MSE B  198  MET  MODIFIED RESIDUE                                   
MODRES 4ZHT MSE B  203  MET  MODIFIED RESIDUE                                   
MODRES 4ZHT MSE B  232  MET  MODIFIED RESIDUE                                   
MODRES 4ZHT MSE B  261  MET  MODIFIED RESIDUE                                   
MODRES 4ZHT MSE B  265  MET  MODIFIED RESIDUE                                   
MODRES 4ZHT MSE B  297  MET  MODIFIED RESIDUE                                   
MODRES 4ZHT MSE C   29  MET  MODIFIED RESIDUE                                   
MODRES 4ZHT MSE C   60  MET  MODIFIED RESIDUE                                   
MODRES 4ZHT MSE C   84  MET  MODIFIED RESIDUE                                   
MODRES 4ZHT MSE C  107  MET  MODIFIED RESIDUE                                   
MODRES 4ZHT MSE C  126  MET  MODIFIED RESIDUE                                   
MODRES 4ZHT MSE C  171  MET  MODIFIED RESIDUE                                   
MODRES 4ZHT MSE C  198  MET  MODIFIED RESIDUE                                   
MODRES 4ZHT MSE C  203  MET  MODIFIED RESIDUE                                   
MODRES 4ZHT MSE C  232  MET  MODIFIED RESIDUE                                   
MODRES 4ZHT MSE C  261  MET  MODIFIED RESIDUE                                   
MODRES 4ZHT MSE C  265  MET  MODIFIED RESIDUE                                   
MODRES 4ZHT MSE C  297  MET  MODIFIED RESIDUE                                   
MODRES 4ZHT MSE D   29  MET  MODIFIED RESIDUE                                   
MODRES 4ZHT MSE D   60  MET  MODIFIED RESIDUE                                   
MODRES 4ZHT MSE D   84  MET  MODIFIED RESIDUE                                   
MODRES 4ZHT MSE D  107  MET  MODIFIED RESIDUE                                   
MODRES 4ZHT MSE D  126  MET  MODIFIED RESIDUE                                   
MODRES 4ZHT MSE D  171  MET  MODIFIED RESIDUE                                   
MODRES 4ZHT MSE D  198  MET  MODIFIED RESIDUE                                   
MODRES 4ZHT MSE D  203  MET  MODIFIED RESIDUE                                   
MODRES 4ZHT MSE D  232  MET  MODIFIED RESIDUE                                   
MODRES 4ZHT MSE D  261  MET  MODIFIED RESIDUE                                   
MODRES 4ZHT MSE D  265  MET  MODIFIED RESIDUE                                   
MODRES 4ZHT MSE D  297  MET  MODIFIED RESIDUE                                   
HET    MSE  A  29       8                                                       
HET    MSE  A  60       8                                                       
HET    MSE  A  84       8                                                       
HET    MSE  A 107       8                                                       
HET    MSE  A 126       8                                                       
HET    MSE  A 171       8                                                       
HET    MSE  A 198       8                                                       
HET    MSE  A 203       8                                                       
HET    MSE  A 232       8                                                       
HET    MSE  A 261       8                                                       
HET    MSE  A 265       8                                                       
HET    MSE  A 297       8                                                       
HET    MSE  B  29       8                                                       
HET    MSE  B  60       8                                                       
HET    MSE  B  84       8                                                       
HET    MSE  B 107       8                                                       
HET    MSE  B 126       8                                                       
HET    MSE  B 171       8                                                       
HET    MSE  B 198       8                                                       
HET    MSE  B 203       8                                                       
HET    MSE  B 232       8                                                       
HET    MSE  B 261       8                                                       
HET    MSE  B 265       8                                                       
HET    MSE  B 297       8                                                       
HET    MSE  C  29       8                                                       
HET    MSE  C  60       8                                                       
HET    MSE  C  84       8                                                       
HET    MSE  C 107       8                                                       
HET    MSE  C 126       8                                                       
HET    MSE  C 171       8                                                       
HET    MSE  C 198       8                                                       
HET    MSE  C 203       8                                                       
HET    MSE  C 232       8                                                       
HET    MSE  C 261       8                                                       
HET    MSE  C 265       8                                                       
HET    MSE  C 297       8                                                       
HET    MSE  D  29       8                                                       
HET    MSE  D  60       8                                                       
HET    MSE  D  84       8                                                       
HET    MSE  D 107       8                                                       
HET    MSE  D 126       8                                                       
HET    MSE  D 171       8                                                       
HET    MSE  D 198       8                                                       
HET    MSE  D 203       8                                                       
HET    MSE  D 232       8                                                       
HET    MSE  D 261       8                                                       
HET    MSE  D 265       8                                                       
HET    MSE  D 297       8                                                       
HET    UDP  A 501      25                                                       
HET    NCC  A 502      41                                                       
HET    UDP  B 501      25                                                       
HET    NCC  B 502      41                                                       
HET    UDP  C 501      25                                                       
HET    NCC  C 502      41                                                       
HET    BM7  C 503      15                                                       
HET    UDP  D 501      25                                                       
HET    NCC  D 502      41                                                       
HETNAM     MSE SELENOMETHIONINE                                                 
HETNAM     UDP URIDINE-5'-DIPHOSPHATE                                           
HETNAM     NCC CYTIDINE-5'-MONOPHOSPHATE-5-N-ACETYLNEURAMINIC ACID              
HETNAM     BM7 2-(ACETYLAMINO)-2-DEOXY-BETA-D-MANNOPYRANOSE                     
FORMUL   1  MSE    48(C5 H11 N O2 SE)                                           
FORMUL   5  UDP    4(C9 H14 N2 O12 P2)                                          
FORMUL   6  NCC    4(C20 H31 N4 O16 P)                                          
FORMUL  11  BM7    C8 H15 N O6                                                  
FORMUL  14  HOH   *331(H2 O)                                                    
HELIX    1 AA1 ASN A   18  THR A   34  1                                  17    
HELIX    2 AA2 SER A   48  ASN A   56  5                                   9    
HELIX    3 AA3 THR A   57  ASP A   64  1                                   8    
HELIX    4 AA4 ASP A   80  LYS A  103  1                                  24    
HELIX    5 AA5 ARG A  113  MSE A  126  1                                  14    
HELIX    6 AA6 THR A  141  ALA A  154  1                                  14    
HELIX    7 AA7 THR A  161  MSE A  171  1                                  11    
HELIX    8 AA8 ASP A  174  ASP A  176  5                                   3    
HELIX    9 AA9 PRO A  184  LEU A  190  1                                   7    
HELIX   10 AB1 ASP A  196  GLY A  206  1                                  11    
HELIX   11 AB2 VAL A  222  THR A  224  5                                   3    
HELIX   12 AB3 ASP A  225  ASN A  244  1                                  20    
HELIX   13 AB4 GLY A  257  LYS A  268  1                                  12    
HELIX   14 AB5 GLY A  269  HIS A  273  5                                   5    
HELIX   15 AB6 PRO A  283  HIS A  293  1                                  11    
HELIX   16 AB7 SER A  301  GLU A  307  1                                   7    
HELIX   17 AB8 VAL A  308  GLY A  312  5                                   5    
HELIX   18 AB9 THR A  339  PHE A  351  1                                  13    
HELIX   19 AC1 ASN A  365  ILE A  377  1                                  13    
HELIX   20 AC2 ASN B   18  THR B   34  1                                  17    
HELIX   21 AC3 SER B   48  ASN B   56  5                                   9    
HELIX   22 AC4 THR B   57  ASP B   64  1                                   8    
HELIX   23 AC5 ASP B   80  LYS B  103  1                                  24    
HELIX   24 AC6 ARG B  113  MSE B  126  1                                  14    
HELIX   25 AC7 THR B  141  ALA B  154  1                                  14    
HELIX   26 AC8 THR B  161  MSE B  171  1                                  11    
HELIX   27 AC9 ASP B  174  ASP B  176  5                                   3    
HELIX   28 AD1 PRO B  184  LEU B  190  1                                   7    
HELIX   29 AD2 ASP B  196  GLY B  206  1                                  11    
HELIX   30 AD3 VAL B  222  THR B  224  5                                   3    
HELIX   31 AD4 ASP B  225  ASN B  244  1                                  20    
HELIX   32 AD5 GLY B  257  LYS B  268  1                                  12    
HELIX   33 AD6 GLY B  269  HIS B  273  5                                   5    
HELIX   34 AD7 PRO B  283  HIS B  293  1                                  11    
HELIX   35 AD8 SER B  301  GLU B  307  1                                   7    
HELIX   36 AD9 VAL B  308  GLY B  312  5                                   5    
HELIX   37 AE1 THR B  339  PHE B  351  1                                  13    
HELIX   38 AE2 ASN B  365  ILE B  377  1                                  13    
HELIX   39 AE3 ASN C   18  THR C   34  1                                  17    
HELIX   40 AE4 SER C   48  ASN C   56  5                                   9    
HELIX   41 AE5 THR C   57  ASP C   64  1                                   8    
HELIX   42 AE6 ASP C   80  LYS C  103  1                                  24    
HELIX   43 AE7 ARG C  113  MSE C  126  1                                  14    
HELIX   44 AE8 THR C  141  ALA C  154  1                                  14    
HELIX   45 AE9 THR C  161  MSE C  171  1                                  11    
HELIX   46 AF1 ASP C  174  ASP C  176  5                                   3    
HELIX   47 AF2 PRO C  184  LEU C  190  1                                   7    
HELIX   48 AF3 ASP C  196  GLY C  206  1                                  11    
HELIX   49 AF4 VAL C  222  THR C  224  5                                   3    
HELIX   50 AF5 ASP C  225  ASN C  244  1                                  20    
HELIX   51 AF6 GLY C  257  LYS C  268  1                                  12    
HELIX   52 AF7 GLY C  269  HIS C  273  5                                   5    
HELIX   53 AF8 PRO C  283  HIS C  293  1                                  11    
HELIX   54 AF9 SER C  301  GLU C  307  1                                   7    
HELIX   55 AG1 VAL C  308  GLY C  312  5                                   5    
HELIX   56 AG2 THR C  339  PHE C  351  1                                  13    
HELIX   57 AG3 ASN C  365  ILE C  377  1                                  13    
HELIX   58 AG4 ASN D   18  THR D   34  1                                  17    
HELIX   59 AG5 SER D   48  ASN D   56  5                                   9    
HELIX   60 AG6 THR D   57  ASP D   64  1                                   8    
HELIX   61 AG7 ASP D   80  LYS D  103  1                                  24    
HELIX   62 AG8 ARG D  113  MSE D  126  1                                  14    
HELIX   63 AG9 THR D  141  ALA D  154  1                                  14    
HELIX   64 AH1 THR D  161  MSE D  171  1                                  11    
HELIX   65 AH2 ASP D  174  ASP D  176  5                                   3    
HELIX   66 AH3 PRO D  184  LEU D  190  1                                   7    
HELIX   67 AH4 ASP D  196  GLY D  206  1                                  11    
HELIX   68 AH5 VAL D  222  THR D  224  5                                   3    
HELIX   69 AH6 ASP D  225  ASN D  244  1                                  20    
HELIX   70 AH7 GLY D  257  LYS D  268  1                                  12    
HELIX   71 AH8 GLY D  269  HIS D  273  5                                   5    
HELIX   72 AH9 PRO D  283  HIS D  293  1                                  11    
HELIX   73 AI1 SER D  301  GLU D  307  1                                   7    
HELIX   74 AI2 VAL D  308  GLY D  312  5                                   5    
HELIX   75 AI3 THR D  339  PHE D  351  1                                  13    
HELIX   76 AI4 ASN D  365  ILE D  377  1                                  13    
SHEET    1 AA1 7 ILE A  68  LEU A  72  0                                        
SHEET    2 AA1 7 PHE A  39  LEU A  46  1  N  VAL A  45   O  THR A  70           
SHEET    3 AA1 7 LEU A  10  THR A  16  1  N  VAL A  12   O  GLU A  40           
SHEET    4 AA1 7 ILE A 106  HIS A 110  1  O  ILE A 106   N  CYS A  13           
SHEET    5 AA1 7 ARG A 129  ILE A 133  1  O  ILE A 133   N  VAL A 109           
SHEET    6 AA1 7 TYR A 156  CYS A 159  1  O  TYR A 156   N  HIS A 132           
SHEET    7 AA1 7 ILE A 178  LEU A 180  1  O  LEU A 179   N  HIS A 157           
SHEET    1 AA2 6 PHE A 276  VAL A 279  0                                        
SHEET    2 AA2 6 THR A 247  LEU A 250  1  N  VAL A 249   O  ARG A 277           
SHEET    3 AA2 6 ILE A 215  LEU A 218  1  N  ALA A 217   O  LEU A 248           
SHEET    4 AA2 6 CYS A 296  GLY A 299  1  O  ILE A 298   N  LEU A 218           
SHEET    5 AA2 6 VAL A 315  LEU A 318  1  O  LEU A 318   N  GLY A 299           
SHEET    6 AA2 6 VAL A 331  VAL A 334  1  O  LEU A 332   N  VAL A 315           
SHEET    1 AA3 7 ILE B  68  LEU B  72  0                                        
SHEET    2 AA3 7 PHE B  39  LEU B  46  1  N  VAL B  45   O  THR B  70           
SHEET    3 AA3 7 LEU B  10  THR B  16  1  N  VAL B  12   O  GLU B  40           
SHEET    4 AA3 7 ILE B 106  HIS B 110  1  O  ILE B 106   N  CYS B  13           
SHEET    5 AA3 7 ARG B 129  ILE B 133  1  O  ILE B 133   N  VAL B 109           
SHEET    6 AA3 7 TYR B 156  CYS B 159  1  O  TYR B 156   N  HIS B 132           
SHEET    7 AA3 7 ILE B 178  LEU B 180  1  O  LEU B 179   N  HIS B 157           
SHEET    1 AA4 6 PHE B 276  VAL B 279  0                                        
SHEET    2 AA4 6 THR B 247  LEU B 250  1  N  VAL B 249   O  ARG B 277           
SHEET    3 AA4 6 ILE B 215  LEU B 218  1  N  ALA B 217   O  LEU B 248           
SHEET    4 AA4 6 CYS B 296  GLY B 299  1  O  ILE B 298   N  LEU B 218           
SHEET    5 AA4 6 VAL B 315  LEU B 318  1  O  LEU B 318   N  GLY B 299           
SHEET    6 AA4 6 VAL B 331  VAL B 334  1  O  LEU B 332   N  VAL B 315           
SHEET    1 AA5 7 ILE C  68  LEU C  72  0                                        
SHEET    2 AA5 7 PHE C  39  LEU C  46  1  N  VAL C  45   O  THR C  70           
SHEET    3 AA5 7 LEU C  10  THR C  16  1  N  VAL C  12   O  GLU C  40           
SHEET    4 AA5 7 ILE C 106  HIS C 110  1  O  ILE C 106   N  CYS C  13           
SHEET    5 AA5 7 ARG C 129  ILE C 133  1  O  ILE C 133   N  VAL C 109           
SHEET    6 AA5 7 TYR C 156  CYS C 159  1  O  TYR C 156   N  HIS C 132           
SHEET    7 AA5 7 ILE C 178  LEU C 180  1  O  LEU C 179   N  HIS C 157           
SHEET    1 AA6 6 PHE C 276  VAL C 279  0                                        
SHEET    2 AA6 6 THR C 247  LEU C 250  1  N  VAL C 249   O  ARG C 277           
SHEET    3 AA6 6 ILE C 215  LEU C 218  1  N  ALA C 217   O  LEU C 248           
SHEET    4 AA6 6 CYS C 296  GLY C 299  1  O  ILE C 298   N  LEU C 218           
SHEET    5 AA6 6 VAL C 315  LEU C 318  1  O  LEU C 318   N  GLY C 299           
SHEET    6 AA6 6 VAL C 331  VAL C 334  1  O  LEU C 332   N  VAL C 315           
SHEET    1 AA7 7 ILE D  68  LEU D  72  0                                        
SHEET    2 AA7 7 PHE D  39  LEU D  46  1  N  VAL D  45   O  THR D  70           
SHEET    3 AA7 7 LEU D  10  THR D  16  1  N  VAL D  12   O  GLU D  40           
SHEET    4 AA7 7 ILE D 106  HIS D 110  1  O  ILE D 106   N  CYS D  13           
SHEET    5 AA7 7 ARG D 129  ILE D 133  1  O  ILE D 133   N  VAL D 109           
SHEET    6 AA7 7 TYR D 156  CYS D 159  1  O  TYR D 156   N  HIS D 132           
SHEET    7 AA7 7 ILE D 178  LEU D 180  1  O  LEU D 179   N  HIS D 157           
SHEET    1 AA8 6 PHE D 276  VAL D 279  0                                        
SHEET    2 AA8 6 THR D 247  LEU D 250  1  N  VAL D 249   O  ARG D 277           
SHEET    3 AA8 6 ILE D 215  LEU D 218  1  N  ALA D 217   O  LEU D 248           
SHEET    4 AA8 6 CYS D 296  GLY D 299  1  O  ILE D 298   N  LEU D 218           
SHEET    5 AA8 6 VAL D 315  LEU D 318  1  O  LEU D 318   N  GLY D 299           
SHEET    6 AA8 6 VAL D 331  VAL D 334  1  O  LEU D 332   N  VAL D 315           
LINK         C   ILE A  28                 N   MSE A  29     1555   1555  1.32  
LINK         C   MSE A  29                 N   PHE A  30     1555   1555  1.33  
LINK         C   ARG A  59                 N   MSE A  60     1555   1555  1.34  
LINK         C   MSE A  60                 N   ILE A  61     1555   1555  1.32  
LINK         C   ALA A  83                 N   MSE A  84     1555   1555  1.32  
LINK         C   MSE A  84                 N   VAL A  85     1555   1555  1.33  
LINK         C   ILE A 106                 N   MSE A 107     1555   1555  1.33  
LINK         C   MSE A 107                 N   ILE A 108     1555   1555  1.33  
LINK         C   LEU A 125                 N   MSE A 126     1555   1555  1.33  
LINK         C   MSE A 126                 N   ASN A 127     1555   1555  1.34  
LINK         C   SER A 170                 N   MSE A 171     1555   1555  1.32  
LINK         C   MSE A 171                 N   CYS A 172     1555   1555  1.34  
LINK         C   TYR A 197                 N   MSE A 198     1555   1555  1.33  
LINK         C   MSE A 198                 N   SER A 199     1555   1555  1.33  
LINK         C   ARG A 202                 N   MSE A 203     1555   1555  1.32  
LINK         C   MSE A 203                 N   TRP A 204     1555   1555  1.34  
LINK         C   LYS A 231                 N   MSE A 232     1555   1555  1.33  
LINK         C   MSE A 232                 N   PHE A 233     1555   1555  1.33  
LINK         C   GLU A 260                 N   MSE A 261     1555   1555  1.33  
LINK         C   MSE A 261                 N   VAL A 262     1555   1555  1.34  
LINK         C   VAL A 264                 N   MSE A 265     1555   1555  1.32  
LINK         C   MSE A 265                 N   ARG A 266     1555   1555  1.34  
LINK         C   CYS A 296                 N   MSE A 297     1555   1555  1.32  
LINK         C   MSE A 297                 N   ILE A 298     1555   1555  1.32  
LINK         C   ILE B  28                 N   MSE B  29     1555   1555  1.32  
LINK         C   MSE B  29                 N   PHE B  30     1555   1555  1.34  
LINK         C   ARG B  59                 N   MSE B  60     1555   1555  1.33  
LINK         C   MSE B  60                 N   ILE B  61     1555   1555  1.32  
LINK         C   ALA B  83                 N   MSE B  84     1555   1555  1.32  
LINK         C   MSE B  84                 N   VAL B  85     1555   1555  1.33  
LINK         C   ILE B 106                 N   MSE B 107     1555   1555  1.33  
LINK         C   MSE B 107                 N   ILE B 108     1555   1555  1.33  
LINK         C   LEU B 125                 N   MSE B 126     1555   1555  1.34  
LINK         C   MSE B 126                 N   ASN B 127     1555   1555  1.34  
LINK         C   SER B 170                 N   MSE B 171     1555   1555  1.34  
LINK         C   MSE B 171                 N   CYS B 172     1555   1555  1.34  
LINK         C   TYR B 197                 N   MSE B 198     1555   1555  1.33  
LINK         C   MSE B 198                 N   SER B 199     1555   1555  1.33  
LINK         C   ARG B 202                 N   MSE B 203     1555   1555  1.33  
LINK         C   MSE B 203                 N   TRP B 204     1555   1555  1.33  
LINK         C   LYS B 231                 N   MSE B 232     1555   1555  1.32  
LINK         C   MSE B 232                 N   PHE B 233     1555   1555  1.33  
LINK         C   GLU B 260                 N   MSE B 261     1555   1555  1.32  
LINK         C   MSE B 261                 N   VAL B 262     1555   1555  1.33  
LINK         C   VAL B 264                 N   MSE B 265     1555   1555  1.33  
LINK         C   MSE B 265                 N   ARG B 266     1555   1555  1.33  
LINK         C   CYS B 296                 N   MSE B 297     1555   1555  1.32  
LINK         C   MSE B 297                 N   ILE B 298     1555   1555  1.33  
LINK         C   ILE C  28                 N   MSE C  29     1555   1555  1.32  
LINK         C   MSE C  29                 N   PHE C  30     1555   1555  1.33  
LINK         C   ARG C  59                 N   MSE C  60     1555   1555  1.34  
LINK         C   MSE C  60                 N   ILE C  61     1555   1555  1.32  
LINK         C   ALA C  83                 N   MSE C  84     1555   1555  1.31  
LINK         C   MSE C  84                 N   VAL C  85     1555   1555  1.33  
LINK         C   ILE C 106                 N   MSE C 107     1555   1555  1.33  
LINK         C   MSE C 107                 N   ILE C 108     1555   1555  1.33  
LINK         C   LEU C 125                 N   MSE C 126     1555   1555  1.33  
LINK         C   MSE C 126                 N   ASN C 127     1555   1555  1.33  
LINK         C   SER C 170                 N   MSE C 171     1555   1555  1.33  
LINK         C   MSE C 171                 N   CYS C 172     1555   1555  1.34  
LINK         C   TYR C 197                 N   MSE C 198     1555   1555  1.33  
LINK         C   MSE C 198                 N   SER C 199     1555   1555  1.33  
LINK         C   ARG C 202                 N   MSE C 203     1555   1555  1.32  
LINK         C   MSE C 203                 N   TRP C 204     1555   1555  1.33  
LINK         C   LYS C 231                 N   MSE C 232     1555   1555  1.32  
LINK         C   MSE C 232                 N   PHE C 233     1555   1555  1.33  
LINK         C   GLU C 260                 N   MSE C 261     1555   1555  1.32  
LINK         C   MSE C 261                 N   VAL C 262     1555   1555  1.34  
LINK         C   VAL C 264                 N   MSE C 265     1555   1555  1.32  
LINK         C   MSE C 265                 N   ARG C 266     1555   1555  1.33  
LINK         C   CYS C 296                 N   MSE C 297     1555   1555  1.32  
LINK         C   MSE C 297                 N   ILE C 298     1555   1555  1.32  
LINK         C   ILE D  28                 N   MSE D  29     1555   1555  1.33  
LINK         C   MSE D  29                 N   PHE D  30     1555   1555  1.33  
LINK         C   ARG D  59                 N   MSE D  60     1555   1555  1.33  
LINK         C   MSE D  60                 N   ILE D  61     1555   1555  1.32  
LINK         C   ALA D  83                 N   MSE D  84     1555   1555  1.31  
LINK         C   MSE D  84                 N   VAL D  85     1555   1555  1.33  
LINK         C   ILE D 106                 N   MSE D 107     1555   1555  1.33  
LINK         C   MSE D 107                 N   ILE D 108     1555   1555  1.33  
LINK         C   LEU D 125                 N   MSE D 126     1555   1555  1.33  
LINK         C   MSE D 126                 N   ASN D 127     1555   1555  1.33  
LINK         C   SER D 170                 N   MSE D 171     1555   1555  1.34  
LINK         C   MSE D 171                 N   CYS D 172     1555   1555  1.35  
LINK         C   TYR D 197                 N   MSE D 198     1555   1555  1.33  
LINK         C   MSE D 198                 N   SER D 199     1555   1555  1.33  
LINK         C   ARG D 202                 N   MSE D 203     1555   1555  1.32  
LINK         C   MSE D 203                 N   TRP D 204     1555   1555  1.34  
LINK         C   LYS D 231                 N   MSE D 232     1555   1555  1.33  
LINK         C   MSE D 232                 N   PHE D 233     1555   1555  1.32  
LINK         C   GLU D 260                 N   MSE D 261     1555   1555  1.33  
LINK         C   MSE D 261                 N   VAL D 262     1555   1555  1.32  
LINK         C   VAL D 264                 N   MSE D 265     1555   1555  1.33  
LINK         C   MSE D 265                 N   ARG D 266     1555   1555  1.33  
LINK         C   CYS D 296                 N   MSE D 297     1555   1555  1.32  
LINK         C   MSE D 297                 N   ILE D 298     1555   1555  1.33  
CISPEP   1 GLU A  381    PRO A  382          0       -27.28                     
CISPEP   2 GLU B  381    PRO B  382          0       -28.17                     
CISPEP   3 GLU C  381    PRO C  382          0       -28.34                     
CISPEP   4 GLU D  381    PRO D  382          0       -26.62                     
SITE     1 AC1 18 ARG A  19  ALA A  20  SER A  23  LYS A  24                    
SITE     2 AC1 18 ARG A 113  LEU A 218  HIS A 220  LEU A 250                    
SITE     3 AC1 18 ASN A 253  HIS A 281  VAL A 282  PHE A 284                    
SITE     4 AC1 18 PHE A 287  SER A 301  SER A 302  GLU A 307                    
SITE     5 AC1 18 ARG A 321  HOH A 630                                          
SITE     1 AC2 14 ASP A  53  LYS A 259  ARG A 266  GLU A 271                    
SITE     2 AC2 14 ALA A 278  VAL A 279  LYS A 280  HIS A 281                    
SITE     3 AC2 14 HOH A 619  HOH A 632  HOH A 640  ARG B 263                    
SITE     4 AC2 14 ARG B 266  NCC B 502                                          
SITE     1 AC3 17 ARG B  19  ALA B  20  SER B  23  LYS B  24                    
SITE     2 AC3 17 ARG B 113  LEU B 218  HIS B 220  LEU B 250                    
SITE     3 AC3 17 ASN B 253  HIS B 281  VAL B 282  PHE B 284                    
SITE     4 AC3 17 PHE B 287  SER B 301  SER B 302  GLU B 307                    
SITE     5 AC3 17 ARG B 321                                                     
SITE     1 AC4 15 ARG A 263  ARG A 266  NCC A 502  HOH A 606                    
SITE     2 AC4 15 ASP B  53  PHE B 251  LYS B 259  ARG B 266                    
SITE     3 AC4 15 GLU B 271  ALA B 278  VAL B 279  LYS B 280                    
SITE     4 AC4 15 HIS B 281  HOH B 625  HOH B 636                               
SITE     1 AC5 17 ARG C  19  SER C  23  LYS C  24  ARG C 113                    
SITE     2 AC5 17 LEU C 218  HIS C 220  LEU C 250  ASN C 253                    
SITE     3 AC5 17 HIS C 281  VAL C 282  PHE C 284  PHE C 287                    
SITE     4 AC5 17 SER C 301  SER C 302  GLU C 307  ARG C 321                    
SITE     5 AC5 17 BM7 C 503                                                     
SITE     1 AC6 12 ASP C  53  LYS C 259  VAL C 262  ARG C 263                    
SITE     2 AC6 12 ARG C 266  LYS C 267  GLU C 271  ALA C 278                    
SITE     3 AC6 12 VAL C 279  LYS C 280  HIS C 281  HOH C 637                    
SITE     1 AC7 11 ARG C  19  TYR C  22  SER C  23  ALA C  26                    
SITE     2 AC7 11 MSE C  60  ASP C  64  HIS C 281  PRO C 283                    
SITE     3 AC7 11 PHE C 284  ASP C 285  UDP C 501                               
SITE     1 AC8 17 ARG D  19  SER D  23  LYS D  24  ARG D 113                    
SITE     2 AC8 17 LEU D 218  HIS D 220  LEU D 250  ASN D 253                    
SITE     3 AC8 17 HIS D 281  VAL D 282  PHE D 284  PHE D 287                    
SITE     4 AC8 17 SER D 301  SER D 302  GLU D 307  ARG D 321                    
SITE     5 AC8 17 HOH D 626                                                     
SITE     1 AC9 13 ASP D  53  LYS D 259  VAL D 262  ARG D 263                    
SITE     2 AC9 13 ARG D 266  GLU D 271  ALA D 278  VAL D 279                    
SITE     3 AC9 13 LYS D 280  HIS D 281  HOH D 611  HOH D 627                    
SITE     4 AC9 13 HOH D 628                                                     
CRYST1  106.041   98.102  154.722  90.00  96.05  90.00 C 1 2 1      16          
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      0.009430  0.000000  0.000999        0.00000                         
SCALE2      0.000000  0.010193  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.006499        0.00000                         
ATOM      1  N   ASN A   7     -21.819  95.267  61.773  1.00127.43           N  
ANISOU    1  N   ASN A   7    21670  11943  14804   4401    997   1696       N  
ATOM      2  CA  ASN A   7     -21.257  94.015  61.178  1.00126.04           C  
ANISOU    2  CA  ASN A   7    21334  12038  14517   4143    803   1679       C  
ATOM      3  C   ASN A   7     -20.840  93.084  62.291  1.00125.38           C  
ANISOU    3  C   ASN A   7    21167  12056  14413   3890    769   1432       C  
ATOM      4  O   ASN A   7     -19.961  93.441  63.078  1.00129.96           O  
ANISOU    4  O   ASN A   7    21936  12405  15036   3723    867   1261       O  
ATOM      5  CB  ASN A   7     -20.032  94.293  60.307  1.00125.49           C  
ANISOU    5  CB  ASN A   7    21454  11799  14424   3961    794   1730       C  
ATOM      6  CG  ASN A   7     -20.398  94.845  58.940  1.00129.42           C  
ANISOU    6  CG  ASN A   7    21979  12301  14892   4173    770   2006       C  
ATOM      7  OD1 ASN A   7     -20.644  94.088  57.997  1.00128.26           O  
ANISOU    7  OD1 ASN A   7    21649  12443  14640   4168    607   2123       O  
ATOM      8  ND2 ASN A   7     -20.434  96.175  58.824  1.00131.69           N  
ANISOU    8  ND2 ASN A   7    22502  12265  15266   4362    937   2112       N  
ATOM      9  N   ARG A   8     -21.500  91.932  62.384  1.00120.94           N  
ANISOU    9  N   ARG A   8    20328  11836  13789   3870    638   1416       N  
ATOM     10  CA  ARG A   8     -21.073  90.853  63.270  1.00115.18           C  
ANISOU   10  CA  ARG A   8    19498  11241  13021   3618    582   1214       C  
ATOM     11  C   ARG A   8     -19.994  90.091  62.509  1.00107.18           C  
ANISOU   11  C   ARG A   8    18484  10303  11936   3350    454   1207       C  
ATOM     12  O   ARG A   8     -20.241  89.585  61.417  1.00105.29           O  
ANISOU   12  O   ARG A   8    18111  10260  11634   3369    328   1345       O  
ATOM     13  CB  ARG A   8     -22.301  89.984  63.666  1.00117.75           C  
ANISOU   13  CB  ARG A   8    19533  11883  13323   3721    517   1214       C  
ATOM     14  CG  ARG A   8     -22.212  88.998  64.811  1.00117.15           C  
ANISOU   14  CG  ARG A   8    19348  11938  13223   3542    503   1023       C  
ATOM     15  CD  ARG A   8     -22.918  87.636  64.640  1.00117.76           C  
ANISOU   15  CD  ARG A   8    19120  12379  13242   3490    364   1041       C  
ATOM     16  NE  ARG A   8     -21.973  86.709  63.996  1.00116.97           N  
ANISOU   16  NE  ARG A   8    18998  12369  13074   3228    231   1020       N  
ATOM     17  CZ  ARG A   8     -21.277  85.702  64.544  1.00114.82           C  
ANISOU   17  CZ  ARG A   8    18692  12167  12764   2977    184    880       C  
ATOM     18  NH1 ARG A   8     -21.398  85.298  65.801  1.00114.03           N  
ANISOU   18  NH1 ARG A   8    18558  12095  12672   2921    242    741       N  
ATOM     19  NH2 ARG A   8     -20.440  85.035  63.762  1.00115.28           N  
ANISOU   19  NH2 ARG A   8    18746  12282  12770   2783     73    889       N  
ATOM     20  N   LYS A   9     -18.788  90.038  63.070  1.00101.31           N  
ANISOU   20  N   LYS A   9    17889   9407  11198   3103    489   1045       N  
ATOM     21  CA  LYS A   9     -17.654  89.387  62.404  1.00 96.52           C  
ANISOU   21  CA  LYS A   9    17295   8846  10530   2847    386   1027       C  
ATOM     22  C   LYS A   9     -17.811  87.870  62.439  1.00 89.17           C  
ANISOU   22  C   LYS A   9    16120   8233   9526   2711    239    977       C  
ATOM     23  O   LYS A   9     -18.381  87.323  63.384  1.00 86.14           O  
ANISOU   23  O   LYS A   9    15612   7971   9145   2724    243    883       O  
ATOM     24  CB  LYS A   9     -16.327  89.762  63.065  1.00 97.87           C  
ANISOU   24  CB  LYS A   9    17674   8779  10730   2625    466    858       C  
ATOM     25  CG  LYS A   9     -16.072  91.252  63.126  1.00102.94           C  
ANISOU   25  CG  LYS A   9    18578   9076  11458   2719    630    875       C  
ATOM     26  CD  LYS A   9     -14.629  91.568  63.482  1.00104.51           C  
ANISOU   26  CD  LYS A   9    18967   9065  11676   2458    685    722       C  
ATOM     27  CE  LYS A   9     -14.478  93.045  63.813  1.00108.99           C  
ANISOU   27  CE  LYS A   9    19796   9272  12343   2542    872    695       C  
ATOM     28  NZ  LYS A   9     -13.112  93.381  64.291  1.00109.47           N  
ANISOU   28  NZ  LYS A   9    20030   9136  12427   2274    933    516       N  
ATOM     29  N   LEU A  10     -17.295  87.209  61.407  1.00 83.91           N  
ANISOU   29  N   LEU A  10    15395   7690   8794   2581    121   1040       N  
ATOM     30  CA  LEU A  10     -17.317  85.760  61.325  1.00 79.65           C  
ANISOU   30  CA  LEU A  10    14648   7424   8190   2432    -10    989       C  
ATOM     31  C   LEU A  10     -16.157  85.193  62.161  1.00 76.59           C  
ANISOU   31  C   LEU A  10    14321   6982   7799   2174     -4    806       C  
ATOM     32  O   LEU A  10     -14.995  85.511  61.910  1.00 75.15           O  
ANISOU   32  O   LEU A  10    14290   6647   7615   2029     14    772       O  
ATOM     33  CB  LEU A  10     -17.214  85.314  59.864  1.00 77.89           C  
ANISOU   33  CB  LEU A  10    14350   7349   7894   2400   -131   1121       C  
ATOM     34  CG  LEU A  10     -17.447  83.830  59.590  1.00 76.08           C  
ANISOU   34  CG  LEU A  10    13892   7413   7600   2277   -267   1087       C  
ATOM     35  CD1 LEU A  10     -18.903  83.464  59.823  1.00 76.69           C  
ANISOU   35  CD1 LEU A  10    13754   7701   7682   2442   -299   1126       C  
ATOM     36  CD2 LEU A  10     -17.028  83.473  58.173  1.00 76.41           C  
ANISOU   36  CD2 LEU A  10    13913   7556   7562   2203   -370   1182       C  
ATOM     37  N   ARG A  11     -16.477  84.376  63.163  1.00 74.99           N  
ANISOU   37  N   ARG A  11    13994   6906   7590   2124    -15    694       N  
ATOM     38  CA  ARG A  11     -15.459  83.781  64.036  1.00 74.27           C  
ANISOU   38  CA  ARG A  11    13943   6792   7484   1904    -14    530       C  
ATOM     39  C   ARG A  11     -14.945  82.506  63.377  1.00 70.67           C  
ANISOU   39  C   ARG A  11    13364   6516   6970   1727   -140    533       C  
ATOM     40  O   ARG A  11     -15.705  81.544  63.215  1.00 68.02           O  
ANISOU   40  O   ARG A  11    12838   6396   6610   1745   -212    563       O  
ATOM     41  CB  ARG A  11     -16.073  83.481  65.404  1.00 77.75           C  
ANISOU   41  CB  ARG A  11    14314   7292   7934   1945     38    426       C  
ATOM     42  CG  ARG A  11     -16.624  84.730  66.085  1.00 82.92           C  
ANISOU   42  CG  ARG A  11    15091   7770   8645   2129    174    409       C  
ATOM     43  CD  ARG A  11     -17.261  84.405  67.457  1.00 84.61           C  
ANISOU   43  CD  ARG A  11    15231   8060   8855   2172    234    303       C  
ATOM     44  NE  ARG A  11     -16.291  83.830  68.385  1.00 83.38           N  
ANISOU   44  NE  ARG A  11    15117   7905   8655   1967    228    148       N  
ATOM     45  CZ  ARG A  11     -15.314  84.513  68.984  1.00 84.85           C  
ANISOU   45  CZ  ARG A  11    15491   7903   8842   1871    292     27       C  
ATOM     46  NH1 ARG A  11     -15.162  85.833  68.787  1.00 85.77           N  
ANISOU   46  NH1 ARG A  11    15791   7783   9014   1951    384     32       N  
ATOM     47  NH2 ARG A  11     -14.475  83.871  69.800  1.00 84.74           N  
ANISOU   47  NH2 ARG A  11    15484   7939   8774   1691    267   -103       N  
ATOM     48  N   VAL A  12     -13.674  82.529  62.967  1.00 68.01           N  
ANISOU   48  N   VAL A  12    13135   6087   6617   1559   -158    500       N  
ATOM     49  CA  VAL A  12     -13.060  81.422  62.250  1.00 65.67           C  
ANISOU   49  CA  VAL A  12    12747   5933   6269   1396   -263    503       C  
ATOM     50  C   VAL A  12     -11.969  80.799  63.084  1.00 63.88           C  
ANISOU   50  C   VAL A  12    12545   5693   6032   1201   -265    358       C  
ATOM     51  O   VAL A  12     -11.048  81.472  63.524  1.00 64.43           O  
ANISOU   51  O   VAL A  12    12762   5597   6119   1123   -206    282       O  
ATOM     52  CB  VAL A  12     -12.425  81.843  60.907  1.00 65.19           C  
ANISOU   52  CB  VAL A  12    12772   5810   6186   1360   -289    599       C  
ATOM     53  CG1 VAL A  12     -11.832  80.625  60.195  1.00 63.41           C  
ANISOU   53  CG1 VAL A  12    12444   5744   5905   1196   -392    588       C  
ATOM     54  CG2 VAL A  12     -13.454  82.499  60.006  1.00 66.90           C  
ANISOU   54  CG2 VAL A  12    12971   6049   6398   1567   -294    762       C  
ATOM     55  N   CYS A  13     -12.067  79.492  63.259  1.00 63.17           N  
ANISOU   55  N   CYS A  13    12305   5783   5912   1120   -334    324       N  
ATOM     56  CA  CYS A  13     -11.045  78.730  63.915  1.00 62.66           C  
ANISOU   56  CA  CYS A  13    12241   5737   5828    947   -350    212       C  
ATOM     57  C   CYS A  13     -10.318  77.924  62.859  1.00 61.73           C  
ANISOU   57  C   CYS A  13    12076   5698   5679    817   -430    240       C  
ATOM     58  O   CYS A  13     -10.949  77.242  62.059  1.00 61.46           O  
ANISOU   58  O   CYS A  13    11923   5802   5626    842   -493    309       O  
ATOM     59  CB  CYS A  13     -11.687  77.830  64.961  1.00 63.59           C  
ANISOU   59  CB  CYS A  13    12238   5984   5939    960   -349    159       C  
ATOM     60  SG  CYS A  13     -10.519  76.674  65.684  1.00 66.79           S  
ANISOU   60  SG  CYS A  13    12619   6448   6310    770   -382     52       S  
ATOM     61  N   VAL A  14      -8.996  78.020  62.820  1.00 61.87           N  
ANISOU   61  N   VAL A  14    12183   5634   5690    676   -427    181       N  
ATOM     62  CA  VAL A  14      -8.204  77.172  61.948  1.00 61.66           C  
ANISOU   62  CA  VAL A  14    12108   5685   5633    547   -491    190       C  
ATOM     63  C   VAL A  14      -7.341  76.314  62.847  1.00 63.35           C  
ANISOU   63  C   VAL A  14    12289   5941   5838    420   -502     82       C  
ATOM     64  O   VAL A  14      -6.571  76.822  63.653  1.00 66.21           O  
ANISOU   64  O   VAL A  14    12738   6212   6206    365   -462      0       O  
ATOM     65  CB  VAL A  14      -7.308  77.977  60.997  1.00 62.83           C  
ANISOU   65  CB  VAL A  14    12377   5717   5779    489   -474    227       C  
ATOM     66  CG1 VAL A  14      -6.641  77.044  59.989  1.00 62.71           C  
ANISOU   66  CG1 VAL A  14    12296   5804   5725    374   -538    244       C  
ATOM     67  CG2 VAL A  14      -8.111  79.039  60.234  1.00 63.74           C  
ANISOU   67  CG2 VAL A  14    12557   5758   5902    637   -446    347       C  
ATOM     68  N   ALA A  15      -7.479  75.003  62.722  1.00 64.73           N  
ANISOU   68  N   ALA A  15    12338   6257   5996    375   -555     82       N  
ATOM     69  CA  ALA A  15      -6.607  74.071  63.411  1.00 64.49           C  
ANISOU   69  CA  ALA A  15    12273   6275   5955    265   -569      4       C  
ATOM     70  C   ALA A  15      -5.598  73.549  62.409  1.00 64.67           C  
ANISOU   70  C   ALA A  15    12287   6321   5963    151   -608      9       C  
ATOM     71  O   ALA A  15      -5.987  73.138  61.291  1.00 72.18           O  
ANISOU   71  O   ALA A  15    13185   7336   6904    156   -644     70       O  
ATOM     72  CB  ALA A  15      -7.405  72.933  64.010  1.00 64.34           C  
ANISOU   72  CB  ALA A  15    12133   6376   5935    294   -581      2       C  
ATOM     73  N   THR A  16      -4.330  73.532  62.824  1.00 61.11           N  
ANISOU   73  N   THR A  16    11876   5836   5507     49   -601    -60       N  
ATOM     74  CA  THR A  16      -3.208  73.042  62.031  1.00 58.71           C  
ANISOU   74  CA  THR A  16    11560   5554   5193    -63   -625    -69       C  
ATOM     75  C   THR A  16      -2.532  71.940  62.866  1.00 58.83           C  
ANISOU   75  C   THR A  16    11506   5646   5201   -122   -642   -131       C  
ATOM     76  O   THR A  16      -2.380  72.087  64.078  1.00 57.41           O  
ANISOU   76  O   THR A  16    11340   5459   5013   -112   -627   -185       O  
ATOM     77  CB  THR A  16      -2.254  74.185  61.621  1.00 57.29           C  
ANISOU   77  CB  THR A  16    11490   5260   5017   -127   -594    -83       C  
ATOM     78  OG1 THR A  16      -1.048  73.664  61.060  1.00 56.56           O  
ANISOU   78  OG1 THR A  16    11371   5202   4914   -243   -609   -107       O  
ATOM     79  CG2 THR A  16      -1.888  75.039  62.744  1.00 59.12           C  
ANISOU   79  CG2 THR A  16    11797   5406   5259   -140   -555   -159       C  
ATOM     80  N   CYS A  17      -2.207  70.812  62.225  1.00 59.09           N  
ANISOU   80  N   CYS A  17    11464   5755   5231   -171   -669   -119       N  
ATOM     81  CA  CYS A  17      -1.611  69.661  62.916  1.00 59.40           C  
ANISOU   81  CA  CYS A  17    11437   5863   5270   -207   -679   -157       C  
ATOM     82  C   CYS A  17      -0.245  69.242  62.395  1.00 57.10           C  
ANISOU   82  C   CYS A  17    11130   5589   4975   -301   -688   -184       C  
ATOM     83  O   CYS A  17       0.480  68.516  63.082  1.00 59.69           O  
ANISOU   83  O   CYS A  17    11414   5964   5300   -323   -693   -217       O  
ATOM     84  CB  CYS A  17      -2.557  68.458  62.854  1.00 60.52           C  
ANISOU   84  CB  CYS A  17    11493   6075   5425   -168   -686   -123       C  
ATOM     85  SG  CYS A  17      -4.300  68.914  62.851  1.00 68.62           S  
ANISOU   85  SG  CYS A  17    12506   7105   6460    -65   -680    -73       S  
ATOM     86  N   ASN A  18       0.101  69.662  61.189  1.00 54.35           N  
ANISOU   86  N   ASN A  18    10812   5212   4624   -347   -687   -165       N  
ATOM     87  CA  ASN A  18       1.281  69.157  60.514  1.00 52.95           C  
ANISOU   87  CA  ASN A  18    10607   5064   4445   -430   -686   -185       C  
ATOM     88  C   ASN A  18       1.650  70.158  59.439  1.00 52.28           C  
ANISOU   88  C   ASN A  18    10592   4921   4348   -478   -669   -163       C  
ATOM     89  O   ASN A  18       0.771  70.858  58.920  1.00 52.54           O  
ANISOU   89  O   ASN A  18    10677   4912   4372   -429   -666   -110       O  
ATOM     90  CB  ASN A  18       0.966  67.782  59.892  1.00 52.98           C  
ANISOU   90  CB  ASN A  18    10538   5136   4455   -425   -697   -168       C  
ATOM     91  CG  ASN A  18       2.202  67.085  59.286  1.00 52.69           C  
ANISOU   91  CG  ASN A  18    10465   5133   4420   -497   -686   -196       C  
ATOM     92  OD1 ASN A  18       2.674  67.450  58.197  1.00 50.93           O  
ANISOU   92  OD1 ASN A  18    10268   4903   4180   -549   -674   -189       O  
ATOM     93  ND2 ASN A  18       2.728  66.088  59.996  1.00 50.91           N  
ANISOU   93  ND2 ASN A  18    10179   4948   4213   -490   -682   -221       N  
ATOM     94  N   ARG A  19       2.939  70.246  59.122  1.00 51.03           N  
ANISOU   94  N   ARG A  19    10433   4766   4191   -567   -652   -196       N  
ATOM     95  CA  ARG A  19       3.398  71.090  58.029  1.00 51.79           C  
ANISOU   95  CA  ARG A  19    10592   4809   4273   -626   -621   -169       C  
ATOM     96  C   ARG A  19       2.628  70.807  56.728  1.00 53.24           C  
ANISOU   96  C   ARG A  19    10782   5021   4424   -591   -629   -100       C  
ATOM     97  O   ARG A  19       2.560  71.669  55.815  1.00 55.95           O  
ANISOU   97  O   ARG A  19    11200   5316   4742   -600   -606    -45       O  
ATOM     98  CB  ARG A  19       4.871  70.855  57.761  1.00 52.02           C  
ANISOU   98  CB  ARG A  19    10584   4873   4308   -729   -599   -215       C  
ATOM     99  CG  ARG A  19       5.055  69.750  56.729  1.00 53.88           C  
ANISOU   99  CG  ARG A  19    10760   5186   4526   -739   -599   -199       C  
ATOM    100  CD  ARG A  19       6.472  69.529  56.321  1.00 54.81           C  
ANISOU  100  CD  ARG A  19    10835   5342   4648   -829   -567   -238       C  
ATOM    101  NE  ARG A  19       6.606  68.218  55.720  1.00 54.56           N  
ANISOU  101  NE  ARG A  19    10733   5386   4608   -817   -567   -245       N  
ATOM    102  CZ  ARG A  19       7.727  67.516  55.721  1.00 55.13           C  
ANISOU  102  CZ  ARG A  19    10730   5518   4698   -854   -546   -287       C  
ATOM    103  NH1 ARG A  19       8.837  68.020  56.251  1.00 58.05           N  
ANISOU  103  NH1 ARG A  19    11070   5898   5087   -915   -533   -327       N  
ATOM    104  NH2 ARG A  19       7.747  66.319  55.182  1.00 53.43           N  
ANISOU  104  NH2 ARG A  19    10465   5352   4481   -832   -536   -296       N  
ATOM    105  N   ALA A  20       2.116  69.579  56.594  1.00 53.65           N  
ANISOU  105  N   ALA A  20    10758   5155   4471   -559   -658   -103       N  
ATOM    106  CA  ALA A  20       1.419  69.163  55.372  1.00 54.79           C  
ANISOU  106  CA  ALA A  20    10891   5352   4574   -541   -674    -60       C  
ATOM    107  C   ALA A  20       0.121  69.896  55.168  1.00 53.68           C  
ANISOU  107  C   ALA A  20    10789   5195   4411   -456   -697      6       C  
ATOM    108  O   ALA A  20      -0.307  70.053  54.042  1.00 53.76           O  
ANISOU  108  O   ALA A  20    10815   5241   4368   -443   -709     58       O  
ATOM    109  CB  ALA A  20       1.170  67.662  55.371  1.00 55.73           C  
ANISOU  109  CB  ALA A  20    10920   5549   4703   -540   -692    -98       C  
ATOM    110  N   ASP A  21      -0.515  70.319  56.252  1.00 52.69           N  
ANISOU  110  N   ASP A  21    10672   5027   4320   -391   -701      7       N  
ATOM    111  CA  ASP A  21      -1.656  71.208  56.115  1.00 53.81           C  
ANISOU  111  CA  ASP A  21    10856   5140   4448   -296   -711     76       C  
ATOM    112  C   ASP A  21      -1.265  72.681  56.202  1.00 54.15           C  
ANISOU  112  C   ASP A  21    11017   5057   4500   -290   -667    107       C  
ATOM    113  O   ASP A  21      -1.944  73.537  55.616  1.00 53.62           O  
ANISOU  113  O   ASP A  21    11008   4953   4410   -217   -661    188       O  
ATOM    114  CB  ASP A  21      -2.754  70.874  57.118  1.00 54.81           C  
ANISOU  114  CB  ASP A  21    10926   5292   4604   -214   -729     68       C  
ATOM    115  CG  ASP A  21      -2.320  71.059  58.552  1.00 56.46           C  
ANISOU  115  CG  ASP A  21    11154   5444   4855   -219   -703     10       C  
ATOM    116  OD1 ASP A  21      -1.996  72.225  58.918  1.00 53.18           O  
ANISOU  116  OD1 ASP A  21    10828   4929   4449   -213   -671      8       O  
ATOM    117  OD2 ASP A  21      -2.332  70.025  59.293  1.00 56.30           O  
ANISOU  117  OD2 ASP A  21    11061   5478   4852   -229   -712    -32       O  
ATOM    118  N   TYR A  22      -0.199  72.972  56.947  1.00 52.41           N  
ANISOU  118  N   TYR A  22    10828   4772   4313   -364   -633     42       N  
ATOM    119  CA  TYR A  22       0.163  74.335  57.205  1.00 52.89           C  
ANISOU  119  CA  TYR A  22    11000   4699   4394   -376   -582     47       C  
ATOM    120  C   TYR A  22       0.604  75.051  55.934  1.00 54.18           C  
ANISOU  120  C   TYR A  22    11243   4811   4531   -415   -545    116       C  
ATOM    121  O   TYR A  22       0.422  76.266  55.834  1.00 55.27           O  
ANISOU  121  O   TYR A  22    11492   4826   4682   -383   -498    166       O  
ATOM    122  CB  TYR A  22       1.225  74.454  58.339  1.00 52.12           C  
ANISOU  122  CB  TYR A  22    10904   4565   4331   -463   -561    -56       C  
ATOM    123  CG  TYR A  22       1.468  75.894  58.768  1.00 51.36           C  
ANISOU  123  CG  TYR A  22    10929   4319   4266   -482   -503    -74       C  
ATOM    124  CD1 TYR A  22       0.425  76.683  59.168  1.00 51.55           C  
ANISOU  124  CD1 TYR A  22    11022   4259   4304   -374   -483    -41       C  
ATOM    125  CD2 TYR A  22       2.727  76.470  58.676  1.00 51.52           C  
ANISOU  125  CD2 TYR A  22    10994   4278   4303   -612   -459   -123       C  
ATOM    126  CE1 TYR A  22       0.605  78.020  59.476  1.00 53.79           C  
ANISOU  126  CE1 TYR A  22    11433   4382   4623   -388   -415    -58       C  
ATOM    127  CE2 TYR A  22       2.933  77.798  59.012  1.00 53.10           C  
ANISOU  127  CE2 TYR A  22    11313   4323   4538   -645   -394   -148       C  
ATOM    128  CZ  TYR A  22       1.865  78.580  59.418  1.00 54.11           C  
ANISOU  128  CZ  TYR A  22    11526   4350   4684   -531   -369   -117       C  
ATOM    129  OH  TYR A  22       2.033  79.908  59.788  1.00 54.78           O  
ANISOU  129  OH  TYR A  22    11743   4258   4810   -559   -292   -149       O  
ATOM    130  N   SER A  23       1.192  74.326  54.988  1.00 55.09           N  
ANISOU  130  N   SER A  23    11312   5010   4608   -482   -556    121       N  
ATOM    131  CA  SER A  23       1.578  74.930  53.710  1.00 57.49           C  
ANISOU  131  CA  SER A  23    11690   5284   4869   -516   -516    197       C  
ATOM    132  C   SER A  23       0.372  75.449  52.910  1.00 59.30           C  
ANISOU  132  C   SER A  23    11967   5514   5048   -394   -532    317       C  
ATOM    133  O   SER A  23       0.505  76.385  52.128  1.00 62.18           O  
ANISOU  133  O   SER A  23    12433   5804   5385   -387   -485    404       O  
ATOM    134  CB  SER A  23       2.420  73.979  52.861  1.00 57.53           C  
ANISOU  134  CB  SER A  23    11629   5393   4834   -606   -520    170       C  
ATOM    135  OG  SER A  23       1.650  72.903  52.347  1.00 60.21           O  
ANISOU  135  OG  SER A  23    11888   5862   5127   -555   -579    179       O  
ATOM    136  N   LYS A  24      -0.786  74.836  53.118  1.00 60.10           N  
ANISOU  136  N   LYS A  24    11991   5705   5137   -297   -596    326       N  
ATOM    137  CA  LYS A  24      -1.987  75.169  52.385  1.00 61.87           C  
ANISOU  137  CA  LYS A  24    12225   5974   5307   -173   -629    433       C  
ATOM    138  C   LYS A  24      -2.979  75.929  53.212  1.00 60.87           C  
ANISOU  138  C   LYS A  24    12128   5772   5226    -47   -624    467       C  
ATOM    139  O   LYS A  24      -3.906  76.505  52.660  1.00 61.55           O  
ANISOU  139  O   LYS A  24    12239   5868   5276     73   -637    572       O  
ATOM    140  CB  LYS A  24      -2.623  73.888  51.834  1.00 65.27           C  
ANISOU  140  CB  LYS A  24    12530   6586   5684   -165   -706    415       C  
ATOM    141  CG  LYS A  24      -1.755  73.215  50.771  1.00 68.70           C  
ANISOU  141  CG  LYS A  24    12949   7098   6055   -270   -703    393       C  
ATOM    142  CD  LYS A  24      -2.120  71.760  50.585  1.00 70.99           C  
ANISOU  142  CD  LYS A  24    13114   7534   6322   -300   -761    321       C  
ATOM    143  CE  LYS A  24      -1.274  71.029  49.559  1.00 73.79           C  
ANISOU  143  CE  LYS A  24    13455   7963   6616   -400   -750    283       C  
ATOM    144  NZ  LYS A  24       0.175  71.056  49.867  1.00 76.76           N  
ANISOU  144  NZ  LYS A  24    13865   8259   7040   -500   -683    230       N  
ATOM    145  N   LEU A  25      -2.809  75.939  54.526  1.00 59.82           N  
ANISOU  145  N   LEU A  25    11990   5574   5165    -65   -604    380       N  
ATOM    146  CA  LEU A  25      -3.663  76.759  55.360  1.00 59.64           C  
ANISOU  146  CA  LEU A  25    12010   5463   5186     52   -581    401       C  
ATOM    147  C   LEU A  25      -3.061  78.126  55.650  1.00 60.02           C  
ANISOU  147  C   LEU A  25    12211   5313   5278     35   -494    408       C  
ATOM    148  O   LEU A  25      -3.807  79.089  55.820  1.00 62.44           O  
ANISOU  148  O   LEU A  25    12594   5522   5607    156   -457    470       O  
ATOM    149  CB  LEU A  25      -4.004  76.058  56.657  1.00 58.69           C  
ANISOU  149  CB  LEU A  25    11804   5388   5107     60   -603    307       C  
ATOM    150  CG  LEU A  25      -4.868  74.810  56.581  1.00 59.27           C  
ANISOU  150  CG  LEU A  25    11731   5629   5156     93   -672    302       C  
ATOM    151  CD1 LEU A  25      -4.884  74.074  57.912  1.00 59.45           C  
ANISOU  151  CD1 LEU A  25    11687   5678   5220     70   -674    208       C  
ATOM    152  CD2 LEU A  25      -6.278  75.186  56.172  1.00 61.40           C  
ANISOU  152  CD2 LEU A  25    11973   5950   5407    242   -697    396       C  
ATOM    153  N   ALA A  26      -1.742  78.233  55.740  1.00 58.94           N  
ANISOU  153  N   ALA A  26    12119   5115   5161   -111   -454    340       N  
ATOM    154  CA  ALA A  26      -1.132  79.513  56.104  1.00 60.02           C  
ANISOU  154  CA  ALA A  26    12398   5057   5349   -154   -363    323       C  
ATOM    155  C   ALA A  26      -1.589  80.669  55.197  1.00 62.14           C  
ANISOU  155  C   ALA A  26    12796   5204   5608    -61   -305    465       C  
ATOM    156  O   ALA A  26      -1.935  81.737  55.715  1.00 63.54           O  
ANISOU  156  O   ALA A  26    13085   5219   5839      7   -239    477       O  
ATOM    157  CB  ALA A  26       0.391  79.420  56.163  1.00 59.68           C  
ANISOU  157  CB  ALA A  26    12362   4991   5322   -341   -332    234       C  
ATOM    158  N   PRO A  27      -1.640  80.455  53.859  1.00 61.36           N  
ANISOU  158  N   PRO A  27    12689   5185   5438    -46   -327    574       N  
ATOM    159  CA  PRO A  27      -2.135  81.503  52.987  1.00 61.31           C  
ANISOU  159  CA  PRO A  27    12803   5081   5409     63   -277    730       C  
ATOM    160  C   PRO A  27      -3.526  81.978  53.335  1.00 61.79           C  
ANISOU  160  C   PRO A  27    12872   5118   5485    266   -289    802       C  
ATOM    161  O   PRO A  27      -3.800  83.175  53.272  1.00 64.67           O  
ANISOU  161  O   PRO A  27    13376   5311   5885    358   -208    887       O  
ATOM    162  CB  PRO A  27      -2.159  80.835  51.634  1.00 62.14           C  
ANISOU  162  CB  PRO A  27    12849   5352   5410     61   -332    816       C  
ATOM    163  CG  PRO A  27      -1.077  79.827  51.704  1.00 61.13           C  
ANISOU  163  CG  PRO A  27    12634   5316   5276   -113   -355    694       C  
ATOM    164  CD  PRO A  27      -1.162  79.292  53.093  1.00 60.14           C  
ANISOU  164  CD  PRO A  27    12427   5204   5218   -132   -387    558       C  
ATOM    165  N   ILE A  28      -4.397  81.063  53.723  1.00 60.88           N  
ANISOU  165  N   ILE A  28    12611   5166   5351    336   -378    767       N  
ATOM    166  CA  ILE A  28      -5.753  81.438  54.121  1.00 62.39           C  
ANISOU  166  CA  ILE A  28    12783   5360   5561    529   -389    825       C  
ATOM    167  C   ILE A  28      -5.748  82.224  55.446  1.00 62.14           C  
ANISOU  167  C   ILE A  28    12838   5146   5624    551   -309    743       C  
ATOM    168  O   ILE A  28      -6.467  83.208  55.604  1.00 61.61           O  
ANISOU  168  O   ILE A  28    12857   4958   5593    702   -252    815       O  
ATOM    169  CB  ILE A  28      -6.651  80.199  54.241  1.00 61.54           C  
ANISOU  169  CB  ILE A  28    12485   5481   5415    574   -497    795       C  
ATOM    170  CG1 ILE A  28      -6.772  79.529  52.877  1.00 61.01           C  
ANISOU  170  CG1 ILE A  28    12343   5592   5246    563   -573    872       C  
ATOM    171  CG2 ILE A  28      -8.052  80.572  54.738  1.00 63.24           C  
ANISOU  171  CG2 ILE A  28    12659   5712   5655    770   -503    847       C  
ATOM    172  CD1 ILE A  28      -7.336  78.132  52.953  1.00 60.56           C  
ANISOU  172  CD1 ILE A  28    12102   5750   5157    538   -670    804       C  
HETATM  173  N   MSE A  29      -4.941  81.766  56.389  1.00 61.59           N  
ANISOU  173  N   MSE A  29    12744   5067   5591    405   -305    589       N  
HETATM  174  CA  MSE A  29      -4.793  82.437  57.679  1.00 62.99           C  
ANISOU  174  CA  MSE A  29    13000   5092   5841    395   -234    483       C  
HETATM  175  C   MSE A  29      -4.295  83.849  57.492  1.00 64.12           C  
ANISOU  175  C   MSE A  29    13337   4990   6034    381   -118    516       C  
HETATM  176  O   MSE A  29      -4.803  84.777  58.128  1.00 64.84           O  
ANISOU  176  O   MSE A  29    13527   4926   6181    482    -43    510       O  
HETATM  177  CB  MSE A  29      -3.859  81.657  58.566  1.00 63.94           C  
ANISOU  177  CB  MSE A  29    13053   5271   5967    228   -261    323       C  
HETATM  178  CG  MSE A  29      -4.483  80.321  58.982  1.00 65.22           C  
ANISOU  178  CG  MSE A  29    13042   5641   6097    261   -353    289       C  
HETATM  179 SE   MSE A  29      -3.139  79.419  60.069  1.00 69.98          SE  
ANISOU  179 SE   MSE A  29    13580   6306   6702     62   -378    110      SE  
HETATM  180  CE  MSE A  29      -2.952  77.695  59.212  1.00 70.66           C  
ANISOU  180  CE  MSE A  29    13497   6619   6732      1   -477    135       C  
ATOM    181  N   PHE A  30      -3.332  84.034  56.592  1.00 63.15           N  
ANISOU  181  N   PHE A  30    13274   4824   5894    261    -92    556       N  
ATOM    182  CA  PHE A  30      -2.862  85.368  56.240  1.00 62.93           C  
ANISOU  182  CA  PHE A  30    13438   4555   5915    240     29    610       C  
ATOM    183  C   PHE A  30      -3.971  86.228  55.653  1.00 63.87           C  
ANISOU  183  C   PHE A  30    13647   4583   6035    462     72    785       C  
ATOM    184  O   PHE A  30      -4.074  87.401  55.955  1.00 66.28           O  
ANISOU  184  O   PHE A  30    14112   4659   6411    518    185    803       O  
ATOM    185  CB  PHE A  30      -1.700  85.280  55.256  1.00 63.41           C  
ANISOU  185  CB  PHE A  30    13525   4620   5945     77     48    640       C  
ATOM    186  CG  PHE A  30      -0.382  84.944  55.895  1.00 63.45           C  
ANISOU  186  CG  PHE A  30    13497   4630   5980   -148     55    469       C  
ATOM    187  CD1 PHE A  30       0.204  85.827  56.814  1.00 64.38           C  
ANISOU  187  CD1 PHE A  30    13724   4556   6179   -247    146    349       C  
ATOM    188  CD2 PHE A  30       0.308  83.773  55.558  1.00 62.05           C  
ANISOU  188  CD2 PHE A  30    13179   4647   5748   -265    -23    423       C  
ATOM    189  CE1 PHE A  30       1.434  85.545  57.387  1.00 64.10           C  
ANISOU  189  CE1 PHE A  30    13642   4547   6162   -456    145    191       C  
ATOM    190  CE2 PHE A  30       1.543  83.483  56.142  1.00 61.91           C  
ANISOU  190  CE2 PHE A  30    13120   4646   5758   -458    -17    274       C  
ATOM    191  CZ  PHE A  30       2.101  84.367  57.061  1.00 62.82           C  
ANISOU  191  CZ  PHE A  30    13328   4593   5945   -554     60    159       C  
ATOM    192  N   GLY A  31      -4.781  85.643  54.796  1.00 63.38           N  
ANISOU  192  N   GLY A  31    13483   4704   5895    587    -14    912       N  
ATOM    193  CA  GLY A  31      -5.881  86.350  54.171  1.00 65.07           C  
ANISOU  193  CA  GLY A  31    13751   4880   6092    816      5   1093       C  
ATOM    194  C   GLY A  31      -6.880  86.822  55.185  1.00 65.71           C  
ANISOU  194  C   GLY A  31    13841   4886   6239    981     38   1065       C  
ATOM    195  O   GLY A  31      -7.284  87.980  55.182  1.00 67.73           O  
ANISOU  195  O   GLY A  31    14243   4942   6547   1119    139   1152       O  
ATOM    196  N   ILE A  32      -7.269  85.911  56.062  1.00 65.78           N  
ANISOU  196  N   ILE A  32    13697   5048   6245    968    -37    944       N  
ATOM    197  CA  ILE A  32      -8.265  86.198  57.089  1.00 67.50           C  
ANISOU  197  CA  ILE A  32    13897   5233   6516   1121    -11    905       C  
ATOM    198  C   ILE A  32      -7.777  87.291  58.048  1.00 69.46           C  
ANISOU  198  C   ILE A  32    14326   5206   6859   1082    124    803       C  
ATOM    199  O   ILE A  32      -8.517  88.204  58.391  1.00 70.91           O  
ANISOU  199  O   ILE A  32    14600   5243   7097   1253    207    846       O  
ATOM    200  CB  ILE A  32      -8.626  84.928  57.859  1.00 65.23           C  
ANISOU  200  CB  ILE A  32    13415   5166   6203   1081   -109    789       C  
ATOM    201  CG1 ILE A  32      -9.441  83.998  56.961  1.00 65.11           C  
ANISOU  201  CG1 ILE A  32    13225   5405   6108   1161   -229    893       C  
ATOM    202  CG2 ILE A  32      -9.430  85.264  59.108  1.00 65.84           C  
ANISOU  202  CG2 ILE A  32    13490   5188   6337   1201    -59    717       C  
ATOM    203  CD1 ILE A  32      -9.568  82.577  57.497  1.00 64.06           C  
ANISOU  203  CD1 ILE A  32    12905   5486   5948   1071   -323    783       C  
ATOM    204  N   LYS A  33      -6.529  87.178  58.458  1.00 70.52           N  
ANISOU  204  N   LYS A  33    14505   5278   7011    856    145    662       N  
ATOM    205  CA  LYS A  33      -5.908  88.143  59.333  1.00 73.94           C  
ANISOU  205  CA  LYS A  33    15101   5467   7524    771    265    537       C  
ATOM    206  C   LYS A  33      -5.774  89.527  58.697  1.00 77.66           C  
ANISOU  206  C   LYS A  33    15786   5664   8055    826    400    648       C  
ATOM    207  O   LYS A  33      -5.859  90.522  59.424  1.00 79.71           O  
ANISOU  207  O   LYS A  33    16193   5696   8394    861    519    581       O  
ATOM    208  CB  LYS A  33      -4.534  87.631  59.768  1.00 73.76           C  
ANISOU  208  CB  LYS A  33    15051   5481   7494    505    241    371       C  
ATOM    209  CG  LYS A  33      -3.874  88.428  60.866  1.00 75.52           C  
ANISOU  209  CG  LYS A  33    15400   5508   7783    388    340    196       C  
ATOM    210  CD  LYS A  33      -2.589  87.755  61.277  1.00 75.89           C  
ANISOU  210  CD  LYS A  33    15374   5655   7805    141    287     41       C  
ATOM    211  CE  LYS A  33      -1.831  88.609  62.273  1.00 78.40           C  
ANISOU  211  CE  LYS A  33    15818   5789   8181     -1    382   -141       C  
ATOM    212  NZ  LYS A  33      -0.621  87.906  62.765  1.00 77.92           N  
ANISOU  212  NZ  LYS A  33    15656   5862   8085   -226    316   -295       N  
ATOM    213  N   THR A  34      -5.585  89.607  57.375  1.00 79.08           N  
ANISOU  213  N   THR A  34    15994   5857   8195    836    392    814       N  
ATOM    214  CA  THR A  34      -5.539  90.921  56.692  1.00 83.85           C  
ANISOU  214  CA  THR A  34    16810   6197   8851    911    529    954       C  
ATOM    215  C   THR A  34      -6.890  91.630  56.581  1.00 85.11           C  
ANISOU  215  C   THR A  34    17023   6279   9034   1212    575   1106       C  
ATOM    216  O   THR A  34      -6.927  92.783  56.183  1.00 89.40           O  
ANISOU  216  O   THR A  34    17758   6574   9634   1299    705   1219       O  
ATOM    217  CB  THR A  34      -4.924  90.887  55.249  1.00 86.79           C  
ANISOU  217  CB  THR A  34    17214   6599   9161    844    523   1109       C  
ATOM    218  OG1 THR A  34      -5.749  90.122  54.344  1.00 86.68           O  
ANISOU  218  OG1 THR A  34    17053   6841   9041    993    398   1262       O  
ATOM    219  CG2 THR A  34      -3.470  90.360  55.259  1.00 86.72           C  
ANISOU  219  CG2 THR A  34    17172   6633   9142    546    507    971       C  
ATOM    220  N   GLU A  35      -7.991  90.962  56.908  1.00 85.01           N  
ANISOU  220  N   GLU A  35    16843   6472   8982   1373    477   1117       N  
ATOM    221  CA  GLU A  35      -9.306  91.590  56.918  1.00 87.73           C  
ANISOU  221  CA  GLU A  35    17210   6768   9353   1667    517   1247       C  
ATOM    222  C   GLU A  35      -9.970  91.468  58.298  1.00 86.91           C  
ANISOU  222  C   GLU A  35    17042   6680   9297   1736    528   1095       C  
ATOM    223  O   GLU A  35     -10.973  90.752  58.441  1.00 85.16           O  
ANISOU  223  O   GLU A  35    16636   6687   9031   1871    432   1122       O  
ATOM    224  CB  GLU A  35     -10.192  90.980  55.831  1.00 89.74           C  
ANISOU  224  CB  GLU A  35    17306   7283   9505   1834    392   1439       C  
ATOM    225  CG  GLU A  35      -9.576  91.046  54.445  1.00 92.47           C  
ANISOU  225  CG  GLU A  35    17709   7643   9780   1774    377   1592       C  
ATOM    226  CD  GLU A  35     -10.600  90.947  53.327  1.00 96.34           C  
ANISOU  226  CD  GLU A  35    18111   8317  10175   2006    296   1820       C  
ATOM    227  OE1 GLU A  35     -11.603  90.211  53.484  1.00 96.33           O  
ANISOU  227  OE1 GLU A  35    17910   8562  10129   2125    182   1821       O  
ATOM    228  OE2 GLU A  35     -10.406  91.615  52.280  1.00 99.48           O  
ANISOU  228  OE2 GLU A  35    18637   8621  10538   2068    348   2003       O  
ATOM    229  N   PRO A  36      -9.448  92.214  59.305  1.00 87.53           N  
ANISOU  229  N   PRO A  36    17277   6514   9464   1646    653    935       N  
ATOM    230  CA  PRO A  36     -10.071  92.240  60.633  1.00 87.97           C  
ANISOU  230  CA  PRO A  36    17301   6563   9559   1722    686    790       C  
ATOM    231  C   PRO A  36     -11.516  92.731  60.686  1.00 90.58           C  
ANISOU  231  C   PRO A  36    17617   6880   9920   2041    729    915       C  
ATOM    232  O   PRO A  36     -12.193  92.461  61.664  1.00 89.45           O  
ANISOU  232  O   PRO A  36    17384   6818   9783   2119    725    816       O  
ATOM    233  CB  PRO A  36      -9.203  93.228  61.419  1.00 88.86           C  
ANISOU  233  CB  PRO A  36    17633   6368   9760   1579    836    625       C  
ATOM    234  CG  PRO A  36      -7.957  93.404  60.643  1.00 88.38           C  
ANISOU  234  CG  PRO A  36    17667   6212   9699   1364    852    643       C  
ATOM    235  CD  PRO A  36      -8.316  93.160  59.224  1.00 88.51           C  
ANISOU  235  CD  PRO A  36    17625   6347   9657   1480    785    885       C  
ATOM    236  N   GLU A  37     -11.988  93.418  59.648  1.00 94.82           N  
ANISOU  236  N   GLU A  37    18229   7331  10467   2230    769   1135       N  
ATOM    237  CA  GLU A  37     -13.320  94.016  59.665  1.00 99.40           C  
ANISOU  237  CA  GLU A  37    18805   7879  11083   2555    824   1267       C  
ATOM    238  C   GLU A  37     -14.403  92.963  59.455  1.00 97.00           C  
ANISOU  238  C   GLU A  37    18221   7936  10696   2691    668   1341       C  
ATOM    239  O   GLU A  37     -15.515  93.137  59.931  1.00 98.67           O  
ANISOU  239  O   GLU A  37    18361   8191  10935   2914    694   1367       O  
ATOM    240  CB  GLU A  37     -13.458  95.125  58.594  1.00105.00           C  
ANISOU  240  CB  GLU A  37    19691   8377  11825   2730    921   1499       C  
ATOM    241  CG  GLU A  37     -13.117  94.751  57.145  1.00106.95           C  
ANISOU  241  CG  GLU A  37    19894   8764  11977   2690    821   1684       C  
ATOM    242  CD  GLU A  37     -11.658  95.005  56.734  1.00108.48           C  
ANISOU  242  CD  GLU A  37    20253   8782  12180   2419    877   1641       C  
ATOM    243  OE1 GLU A  37     -10.755  95.025  57.615  1.00106.74           O  
ANISOU  243  OE1 GLU A  37    20105   8435  12014   2185    931   1421       O  
ATOM    244  OE2 GLU A  37     -11.421  95.184  55.512  1.00111.07           O  
ANISOU  244  OE2 GLU A  37    20633   9113  12455   2441    866   1829       O  
ATOM    245  N   PHE A  38     -14.076  91.903  58.710  1.00 94.89           N  
ANISOU  245  N   PHE A  38    17802   7921  10331   2556    515   1375       N  
ATOM    246  CA  PHE A  38     -15.019  90.826  58.381  1.00 93.90           C  
ANISOU  246  CA  PHE A  38    17408   8147  10122   2645    359   1439       C  
ATOM    247  C   PHE A  38     -14.783  89.512  59.149  1.00 89.28           C  
ANISOU  247  C   PHE A  38    16646   7776   9499   2445    259   1252       C  
ATOM    248  O   PHE A  38     -15.687  88.682  59.206  1.00 88.01           O  
ANISOU  248  O   PHE A  38    16269   7872   9296   2522    163   1267       O  
ATOM    249  CB  PHE A  38     -14.984  90.526  56.872  1.00 96.30           C  
ANISOU  249  CB  PHE A  38    17654   8605  10330   2664    255   1626       C  
ATOM    250  CG  PHE A  38     -15.456  91.674  55.996  1.00100.81           C  
ANISOU  250  CG  PHE A  38    18356   9034  10912   2910    330   1857       C  
ATOM    251  CD1 PHE A  38     -16.792  92.075  56.009  1.00103.47           C  
ANISOU  251  CD1 PHE A  38    18615   9434  11265   3217    340   1983       C  
ATOM    252  CD2 PHE A  38     -14.569  92.331  55.135  1.00101.47           C  
ANISOU  252  CD2 PHE A  38    18635   8930  10987   2841    393   1959       C  
ATOM    253  CE1 PHE A  38     -17.227  93.122  55.205  1.00106.58           C  
ANISOU  253  CE1 PHE A  38    19128   9700  11665   3464    409   2211       C  
ATOM    254  CE2 PHE A  38     -15.000  93.381  54.340  1.00105.32           C  
ANISOU  254  CE2 PHE A  38    19255   9280  11482   3076    470   2187       C  
ATOM    255  CZ  PHE A  38     -16.330  93.776  54.371  1.00107.14           C  
ANISOU  255  CZ  PHE A  38    19410   9571  11727   3396    475   2318       C  
ATOM    256  N   PHE A  39     -13.594  89.317  59.730  1.00 85.20           N  
ANISOU  256  N   PHE A  39    16214   7160   8997   2194    283   1082       N  
ATOM    257  CA  PHE A  39     -13.227  88.039  60.342  1.00 80.17           C  
ANISOU  257  CA  PHE A  39    15423   6721   8315   2000    186    928       C  
ATOM    258  C   PHE A  39     -12.530  88.177  61.698  1.00 77.70           C  
ANISOU  258  C   PHE A  39    15200   6274   8048   1854    262    715       C  
ATOM    259  O   PHE A  39     -11.647  89.018  61.845  1.00 77.06           O  
ANISOU  259  O   PHE A  39    15312   5954   8013   1758    357    656       O  
ATOM    260  CB  PHE A  39     -12.256  87.292  59.429  1.00 78.20           C  
ANISOU  260  CB  PHE A  39    15137   6576   7999   1798     90    943       C  
ATOM    261  CG  PHE A  39     -12.781  87.000  58.065  1.00 78.22           C  
ANISOU  261  CG  PHE A  39    15044   6745   7930   1898      0   1127       C  
ATOM    262  CD1 PHE A  39     -13.756  86.033  57.873  1.00 77.05           C  
ANISOU  262  CD1 PHE A  39    14671   6877   7727   1974   -115   1163       C  
ATOM    263  CD2 PHE A  39     -12.263  87.667  56.950  1.00 79.87           C  
ANISOU  263  CD2 PHE A  39    15388   6840   8119   1900     29   1261       C  
ATOM    264  CE1 PHE A  39     -14.229  85.757  56.600  1.00 78.49           C  
ANISOU  264  CE1 PHE A  39    14759   7233   7829   2055   -208   1319       C  
ATOM    265  CE2 PHE A  39     -12.734  87.398  55.674  1.00 80.12           C  
ANISOU  265  CE2 PHE A  39    15333   7045   8063   1993    -59   1431       C  
ATOM    266  CZ  PHE A  39     -13.720  86.444  55.498  1.00 79.59           C  
ANISOU  266  CZ  PHE A  39    15036   7269   7935   2071   -184   1454       C  
ATOM    267  N   GLU A  40     -12.912  87.330  62.655  1.00 76.12           N  
ANISOU  267  N   GLU A  40    14857   6237   7827   1829    218    603       N  
ATOM    268  CA  GLU A  40     -12.095  87.052  63.849  1.00 76.80           C  
ANISOU  268  CA  GLU A  40    14980   6288   7913   1645    242    399       C  
ATOM    269  C   GLU A  40     -11.436  85.697  63.648  1.00 72.32           C  
ANISOU  269  C   GLU A  40    14269   5931   7278   1451    114    357       C  
ATOM    270  O   GLU A  40     -12.091  84.756  63.224  1.00 71.53           O  
ANISOU  270  O   GLU A  40    13991   6047   7136   1496     20    429       O  
ATOM    271  CB  GLU A  40     -12.940  87.037  65.145  1.00 80.18           C  
ANISOU  271  CB  GLU A  40    15360   6749   8355   1754    295    304       C  
ATOM    272  CG  GLU A  40     -13.301  88.400  65.741  1.00 86.44           C  
ANISOU  272  CG  GLU A  40    16330   7292   9219   1899    450    269       C  
ATOM    273  CD  GLU A  40     -12.279  88.996  66.694  1.00 90.99           C  
ANISOU  273  CD  GLU A  40    17082   7672   9815   1737    539     76       C  
ATOM    274  OE1 GLU A  40     -11.190  88.386  66.894  1.00 93.21           O  
ANISOU  274  OE1 GLU A  40    17347   8016  10053   1505    474    -28       O  
ATOM    275  OE2 GLU A  40     -12.588  90.100  67.239  1.00 94.57           O  
ANISOU  275  OE2 GLU A  40    17689   7911  10330   1848    676     27       O  
ATOM    276  N   LEU A  41     -10.141  85.602  63.955  1.00 70.67           N  
ANISOU  276  N   LEU A  41    14133   5656   7060   1236    115    236       N  
ATOM    277  CA  LEU A  41      -9.342  84.366  63.776  1.00 67.20           C  
ANISOU  277  CA  LEU A  41    13575   5392   6563   1049      7    191       C  
ATOM    278  C   LEU A  41      -8.807  83.809  65.098  1.00 65.54           C  
ANISOU  278  C   LEU A  41    13333   5237   6329    924      1     18       C  
ATOM    279  O   LEU A  41      -8.117  84.513  65.822  1.00 65.02           O  
ANISOU  279  O   LEU A  41    13396   5025   6282    843     70   -102       O  
ATOM    280  CB  LEU A  41      -8.140  84.647  62.867  1.00 66.52           C  
ANISOU  280  CB  LEU A  41    13583   5213   6478    898      5    213       C  
ATOM    281  CG  LEU A  41      -7.144  83.501  62.632  1.00 65.05           C  
ANISOU  281  CG  LEU A  41    13295   5178   6242    703    -88    162       C  
ATOM    282  CD1 LEU A  41      -7.743  82.492  61.658  1.00 64.53           C  
ANISOU  282  CD1 LEU A  41    13073   5314   6128    754   -187    280       C  
ATOM    283  CD2 LEU A  41      -5.785  84.009  62.149  1.00 64.53           C  
ANISOU  283  CD2 LEU A  41    13346   4982   6190    532    -53    131       C  
ATOM    284  N   ASP A  42      -9.078  82.534  65.368  1.00 65.15           N  
ANISOU  284  N   ASP A  42    13117   5403   6234    900    -81      7       N  
ATOM    285  CA  ASP A  42      -8.435  81.781  66.464  1.00 65.53           C  
ANISOU  285  CA  ASP A  42    13118   5538   6241    770   -107   -129       C  
ATOM    286  C   ASP A  42      -7.674  80.602  65.891  1.00 63.54           C  
ANISOU  286  C   ASP A  42    12760   5429   5952    629   -205   -114       C  
ATOM    287  O   ASP A  42      -8.230  79.803  65.148  1.00 65.03           O  
ANISOU  287  O   ASP A  42    12830   5748   6130    668   -267    -20       O  
ATOM    288  CB  ASP A  42      -9.473  81.269  67.452  1.00 66.81           C  
ANISOU  288  CB  ASP A  42    13182   5817   6384    878    -96   -152       C  
ATOM    289  CG  ASP A  42     -10.124  82.389  68.233  1.00 71.67           C  
ANISOU  289  CG  ASP A  42    13905   6295   7030   1011     12   -198       C  
ATOM    290  OD1 ASP A  42      -9.398  83.183  68.877  1.00 73.41           O  
ANISOU  290  OD1 ASP A  42    14267   6370   7254    940     74   -316       O  
ATOM    291  OD2 ASP A  42     -11.368  82.514  68.158  1.00 76.23           O  
ANISOU  291  OD2 ASP A  42    14424   6907   7630   1187     39   -118       O  
ATOM    292  N   VAL A  43      -6.406  80.488  66.247  1.00 62.32           N  
ANISOU  292  N   VAL A  43    12643   5255   5778    465   -216   -215       N  
ATOM    293  CA  VAL A  43      -5.542  79.425  65.744  1.00 60.21           C  
ANISOU  293  CA  VAL A  43    12286   5109   5481    333   -297   -210       C  
ATOM    294  C   VAL A  43      -5.307  78.354  66.812  1.00 58.57           C  
ANISOU  294  C   VAL A  43    11981   5044   5227    282   -336   -289       C  
ATOM    295  O   VAL A  43      -4.925  78.681  67.951  1.00 58.59           O  
ANISOU  295  O   VAL A  43    12034   5020   5205    248   -306   -400       O  
ATOM    296  CB  VAL A  43      -4.193  80.014  65.312  1.00 61.34           C  
ANISOU  296  CB  VAL A  43    12523   5145   5636    184   -282   -256       C  
ATOM    297  CG1 VAL A  43      -3.182  78.922  65.015  1.00 60.74           C  
ANISOU  297  CG1 VAL A  43    12351   5198   5529     48   -354   -275       C  
ATOM    298  CG2 VAL A  43      -4.400  80.905  64.100  1.00 62.48           C  
ANISOU  298  CG2 VAL A  43    12758   5160   5819    232   -243   -148       C  
ATOM    299  N   VAL A  44      -5.521  77.093  66.437  1.00 55.42           N  
ANISOU  299  N   VAL A  44    11451   4794   4811    276   -400   -232       N  
ATOM    300  CA  VAL A  44      -5.267  75.963  67.323  1.00 53.89           C  
ANISOU  300  CA  VAL A  44    11168   4731   4577    232   -433   -281       C  
ATOM    301  C   VAL A  44      -4.164  75.074  66.760  1.00 53.36           C  
ANISOU  301  C   VAL A  44    11043   4733   4497    107   -491   -282       C  
ATOM    302  O   VAL A  44      -4.230  74.657  65.592  1.00 53.43           O  
ANISOU  302  O   VAL A  44    11009   4767   4523     94   -523   -208       O  
ATOM    303  CB  VAL A  44      -6.529  75.126  67.504  1.00 53.97           C  
ANISOU  303  CB  VAL A  44    11068   4849   4587    333   -438   -218       C  
ATOM    304  CG1 VAL A  44      -6.263  73.949  68.435  1.00 53.98           C  
ANISOU  304  CG1 VAL A  44    10991   4970   4548    292   -458   -254       C  
ATOM    305  CG2 VAL A  44      -7.641  75.982  68.079  1.00 55.43           C  
ANISOU  305  CG2 VAL A  44    11294   4980   4785    469   -373   -217       C  
ATOM    306  N   VAL A  45      -3.143  74.807  67.573  1.00 51.73           N  
ANISOU  306  N   VAL A  45    10835   4564   4255     21   -505   -366       N  
ATOM    307  CA  VAL A  45      -2.003  74.004  67.140  1.00 50.50           C  
ANISOU  307  CA  VAL A  45    10622   4475   4089    -86   -554   -373       C  
ATOM    308  C   VAL A  45      -2.012  72.699  67.892  1.00 49.91           C  
ANISOU  308  C   VAL A  45    10449   4532   3980    -72   -582   -370       C  
ATOM    309  O   VAL A  45      -2.122  72.680  69.110  1.00 52.72           O  
ANISOU  309  O   VAL A  45    10810   4926   4293    -42   -569   -418       O  
ATOM    310  CB  VAL A  45      -0.668  74.733  67.353  1.00 50.28           C  
ANISOU  310  CB  VAL A  45    10655   4398   4050   -202   -551   -465       C  
ATOM    311  CG1 VAL A  45       0.496  73.878  66.900  1.00 49.44           C  
ANISOU  311  CG1 VAL A  45    10471   4375   3936   -300   -597   -467       C  
ATOM    312  CG2 VAL A  45      -0.659  76.036  66.580  1.00 51.21           C  
ANISOU  312  CG2 VAL A  45    10884   4361   4210   -222   -506   -458       C  
ATOM    313  N   LEU A  46      -1.913  71.606  67.154  1.00 49.36           N  
ANISOU  313  N   LEU A  46    10299   4526   3927    -92   -612   -313       N  
ATOM    314  CA  LEU A  46      -1.951  70.288  67.741  1.00 49.14           C  
ANISOU  314  CA  LEU A  46    10186   4601   3881    -76   -626   -293       C  
ATOM    315  C   LEU A  46      -1.154  69.319  66.904  1.00 46.99           C  
ANISOU  315  C   LEU A  46     9854   4371   3628   -141   -656   -269       C  
ATOM    316  O   LEU A  46      -0.471  69.725  65.962  1.00 47.32           O  
ANISOU  316  O   LEU A  46     9918   4375   3686   -206   -668   -278       O  
ATOM    317  CB  LEU A  46      -3.392  69.850  67.932  1.00 49.73           C  
ANISOU  317  CB  LEU A  46    10221   4701   3971     15   -600   -237       C  
ATOM    318  CG  LEU A  46      -4.251  69.638  66.708  1.00 51.52           C  
ANISOU  318  CG  LEU A  46    10410   4919   4244     34   -606   -172       C  
ATOM    319  CD1 LEU A  46      -5.321  68.615  67.031  1.00 52.91           C  
ANISOU  319  CD1 LEU A  46    10501   5164   4435     84   -588   -128       C  
ATOM    320  CD2 LEU A  46      -4.910  70.917  66.234  1.00 53.58           C  
ANISOU  320  CD2 LEU A  46    10734   5104   4521     87   -591   -158       C  
ATOM    321  N   GLY A  47      -1.158  68.062  67.289  1.00 45.99           N  
ANISOU  321  N   GLY A  47     9658   4317   3497   -124   -658   -242       N  
ATOM    322  CA  GLY A  47      -0.533  67.037  66.466  1.00 46.68           C  
ANISOU  322  CA  GLY A  47     9690   4433   3612   -171   -673   -218       C  
ATOM    323  C   GLY A  47       0.967  67.171  66.331  1.00 47.76           C  
ANISOU  323  C   GLY A  47     9825   4586   3734   -242   -696   -262       C  
ATOM    324  O   GLY A  47       1.662  67.490  67.305  1.00 49.90           O  
ANISOU  324  O   GLY A  47    10102   4894   3962   -249   -709   -307       O  
ATOM    325  N   SER A  48       1.458  66.888  65.122  1.00 47.79           N  
ANISOU  325  N   SER A  48     9810   4578   3768   -296   -701   -252       N  
ATOM    326  CA  SER A  48       2.888  66.781  64.820  1.00 49.28           C  
ANISOU  326  CA  SER A  48     9971   4797   3953   -363   -714   -285       C  
ATOM    327  C   SER A  48       3.669  68.024  65.122  1.00 49.57           C  
ANISOU  327  C   SER A  48    10051   4815   3966   -423   -725   -347       C  
ATOM    328  O   SER A  48       4.876  67.972  65.346  1.00 50.84           O  
ANISOU  328  O   SER A  48    10172   5030   4113   -474   -740   -389       O  
ATOM    329  CB  SER A  48       3.087  66.462  63.337  1.00 51.77           C  
ANISOU  329  CB  SER A  48    10276   5093   4301   -410   -705   -266       C  
ATOM    330  OG  SER A  48       2.127  65.527  62.880  1.00 55.71           O  
ANISOU  330  OG  SER A  48    10750   5591   4823   -372   -692   -223       O  
ATOM    331  N   HIS A  49       3.003  69.165  65.034  1.00 50.20           N  
ANISOU  331  N   HIS A  49    10211   4814   4047   -421   -711   -356       N  
ATOM    332  CA  HIS A  49       3.644  70.445  65.254  1.00 50.81           C  
ANISOU  332  CA  HIS A  49    10349   4842   4113   -490   -704   -422       C  
ATOM    333  C   HIS A  49       4.422  70.508  66.576  1.00 51.61           C  
ANISOU  333  C   HIS A  49    10423   5018   4168   -511   -729   -498       C  
ATOM    334  O   HIS A  49       5.448  71.165  66.639  1.00 52.10           O  
ANISOU  334  O   HIS A  49    10489   5084   4223   -604   -734   -567       O  
ATOM    335  CB  HIS A  49       2.595  71.557  65.231  1.00 51.09           C  
ANISOU  335  CB  HIS A  49    10483   4770   4159   -448   -674   -413       C  
ATOM    336  CG  HIS A  49       2.124  71.934  63.859  1.00 50.07           C  
ANISOU  336  CG  HIS A  49    10396   4566   4061   -448   -654   -348       C  
ATOM    337  ND1 HIS A  49       2.973  72.054  62.779  1.00 49.85           N  
ANISOU  337  ND1 HIS A  49    10369   4523   4045   -531   -647   -340       N  
ATOM    338  CD2 HIS A  49       0.908  72.318  63.421  1.00 50.02           C  
ANISOU  338  CD2 HIS A  49    10432   4504   4067   -369   -639   -288       C  
ATOM    339  CE1 HIS A  49       2.295  72.472  61.727  1.00 49.19           C  
ANISOU  339  CE1 HIS A  49    10336   4380   3972   -504   -629   -273       C  
ATOM    340  NE2 HIS A  49       1.037  72.635  62.089  1.00 50.08           N  
ANISOU  340  NE2 HIS A  49    10470   4471   4086   -402   -629   -239       N  
ATOM    341  N   LEU A  50       3.951  69.812  67.611  1.00 51.49           N  
ANISOU  341  N   LEU A  50    10375   5072   4116   -430   -742   -484       N  
ATOM    342  CA  LEU A  50       4.598  69.879  68.925  1.00 52.40           C  
ANISOU  342  CA  LEU A  50    10466   5279   4163   -436   -771   -550       C  
ATOM    343  C   LEU A  50       5.644  68.804  69.159  1.00 53.04           C  
ANISOU  343  C   LEU A  50    10441   5489   4221   -437   -809   -537       C  
ATOM    344  O   LEU A  50       6.027  68.584  70.284  1.00 54.44           O  
ANISOU  344  O   LEU A  50    10582   5770   4330   -411   -840   -565       O  
ATOM    345  CB  LEU A  50       3.547  69.832  70.027  1.00 52.58           C  
ANISOU  345  CB  LEU A  50    10521   5315   4142   -342   -758   -541       C  
ATOM    346  CG  LEU A  50       2.368  70.801  69.896  1.00 53.84           C  
ANISOU  346  CG  LEU A  50    10775   5355   4326   -308   -714   -544       C  
ATOM    347  CD1 LEU A  50       1.444  70.588  71.089  1.00 55.44           C  
ANISOU  347  CD1 LEU A  50    10988   5598   4475   -211   -696   -537       C  
ATOM    348  CD2 LEU A  50       2.805  72.263  69.822  1.00 54.32           C  
ANISOU  348  CD2 LEU A  50    10921   5324   4391   -390   -698   -636       C  
ATOM    349  N   ILE A  51       6.139  68.150  68.115  1.00 53.03           N  
ANISOU  349  N   ILE A  51    10388   5489   4270   -461   -805   -495       N  
ATOM    350  CA  ILE A  51       6.961  66.967  68.290  1.00 53.55           C  
ANISOU  350  CA  ILE A  51    10355   5664   4327   -429   -826   -462       C  
ATOM    351  C   ILE A  51       8.324  67.218  67.680  1.00 54.02           C  
ANISOU  351  C   ILE A  51    10355   5765   4402   -523   -841   -510       C  
ATOM    352  O   ILE A  51       8.435  67.462  66.487  1.00 56.27           O  
ANISOU  352  O   ILE A  51    10659   5980   4740   -583   -812   -506       O  
ATOM    353  CB  ILE A  51       6.294  65.737  67.638  1.00 53.68           C  
ANISOU  353  CB  ILE A  51    10355   5646   4395   -359   -793   -370       C  
ATOM    354  CG1 ILE A  51       4.860  65.542  68.158  1.00 53.63           C  
ANISOU  354  CG1 ILE A  51    10398   5595   4383   -282   -769   -325       C  
ATOM    355  CG2 ILE A  51       7.113  64.483  67.900  1.00 54.97           C  
ANISOU  355  CG2 ILE A  51    10428   5902   4555   -307   -801   -330       C  
ATOM    356  CD1 ILE A  51       4.756  65.437  69.677  1.00 54.51           C  
ANISOU  356  CD1 ILE A  51    10505   5787   4419   -217   -785   -326       C  
ATOM    357  N   ASP A  52       9.356  67.117  68.502  1.00 55.33           N  
ANISOU  357  N   ASP A  52    10442   6063   4517   -533   -885   -553       N  
ATOM    358  CA  ASP A  52      10.735  67.251  68.062  1.00 56.57           C  
ANISOU  358  CA  ASP A  52    10513   6295   4687   -618   -901   -600       C  
ATOM    359  C   ASP A  52      11.103  66.383  66.832  1.00 57.01           C  
ANISOU  359  C   ASP A  52    10519   6331   4810   -608   -864   -542       C  
ATOM    360  O   ASP A  52      11.778  66.860  65.906  1.00 57.76           O  
ANISOU  360  O   ASP A  52    10598   6405   4941   -706   -841   -576       O  
ATOM    361  CB  ASP A  52      11.668  66.901  69.210  1.00 57.91           C  
ANISOU  361  CB  ASP A  52    10576   6645   4782   -588   -963   -629       C  
ATOM    362  CG  ASP A  52      13.105  67.276  68.939  1.00 59.97           C  
ANISOU  362  CG  ASP A  52    10732   7006   5046   -694   -988   -702       C  
ATOM    363  OD1 ASP A  52      13.825  66.570  68.215  1.00 60.72           O  
ANISOU  363  OD1 ASP A  52    10741   7143   5186   -682   -972   -664       O  
ATOM    364  OD2 ASP A  52      13.558  68.256  69.529  1.00 65.27           O  
ANISOU  364  OD2 ASP A  52    11397   7728   5672   -791  -1022   -806       O  
ATOM    365  N   ASP A  53      10.677  65.121  66.808  1.00 56.68           N  
ANISOU  365  N   ASP A  53    10458   6291   4785   -497   -847   -458       N  
ATOM    366  CA  ASP A  53      10.960  64.262  65.643  1.00 55.84           C  
ANISOU  366  CA  ASP A  53    10317   6155   4741   -486   -803   -415       C  
ATOM    367  C   ASP A  53      10.500  64.856  64.333  1.00 53.93           C  
ANISOU  367  C   ASP A  53    10151   5797   4543   -566   -761   -426       C  
ATOM    368  O   ASP A  53      11.117  64.612  63.325  1.00 53.78           O  
ANISOU  368  O   ASP A  53    10097   5778   4557   -605   -729   -429       O  
ATOM    369  CB  ASP A  53      10.303  62.884  65.780  1.00 56.25           C  
ANISOU  369  CB  ASP A  53    10371   6185   4817   -365   -775   -331       C  
ATOM    370  CG  ASP A  53      10.969  62.010  66.822  1.00 57.77           C  
ANISOU  370  CG  ASP A  53    10479   6494   4974   -263   -799   -291       C  
ATOM    371  OD1 ASP A  53      12.118  62.282  67.251  1.00 59.33           O  
ANISOU  371  OD1 ASP A  53    10588   6818   5136   -281   -842   -328       O  
ATOM    372  OD2 ASP A  53      10.296  61.051  67.229  1.00 58.94           O  
ANISOU  372  OD2 ASP A  53    10650   6612   5132   -165   -773   -217       O  
ATOM    373  N   TYR A  54       9.393  65.587  64.359  1.00 53.77           N  
ANISOU  373  N   TYR A  54    10229   5684   4515   -577   -759   -425       N  
ATOM    374  CA  TYR A  54       8.844  66.230  63.183  1.00 54.61           C  
ANISOU  374  CA  TYR A  54    10413   5688   4648   -635   -726   -420       C  
ATOM    375  C   TYR A  54       9.391  67.650  62.900  1.00 57.36           C  
ANISOU  375  C   TYR A  54    10802   6001   4991   -749   -720   -477       C  
ATOM    376  O   TYR A  54       9.002  68.269  61.906  1.00 60.24           O  
ANISOU  376  O   TYR A  54    11237   6277   5371   -793   -688   -460       O  
ATOM    377  CB  TYR A  54       7.298  66.178  63.234  1.00 54.76           C  
ANISOU  377  CB  TYR A  54    10506   5629   4669   -570   -721   -374       C  
ATOM    378  CG  TYR A  54       6.743  64.773  62.965  1.00 55.79           C  
ANISOU  378  CG  TYR A  54    10606   5764   4825   -498   -702   -321       C  
ATOM    379  CD1 TYR A  54       6.922  64.165  61.744  1.00 57.88           C  
ANISOU  379  CD1 TYR A  54    10856   6014   5119   -521   -671   -310       C  
ATOM    380  CD2 TYR A  54       6.056  64.059  63.941  1.00 57.20           C  
ANISOU  380  CD2 TYR A  54    10776   5958   4999   -413   -706   -286       C  
ATOM    381  CE1 TYR A  54       6.437  62.886  61.493  1.00 59.23           C  
ANISOU  381  CE1 TYR A  54    11007   6177   5321   -469   -645   -279       C  
ATOM    382  CE2 TYR A  54       5.577  62.787  63.710  1.00 56.44           C  
ANISOU  382  CE2 TYR A  54    10658   5848   4937   -361   -676   -242       C  
ATOM    383  CZ  TYR A  54       5.772  62.198  62.479  1.00 59.99           C  
ANISOU  383  CZ  TYR A  54    11095   6274   5422   -393   -646   -245       C  
ATOM    384  OH  TYR A  54       5.309  60.923  62.210  1.00 60.84           O  
ANISOU  384  OH  TYR A  54    11189   6356   5572   -356   -607   -218       O  
ATOM    385  N   GLY A  55      10.302  68.145  63.735  1.00 59.46           N  
ANISOU  385  N   GLY A  55    11022   6337   5233   -800   -748   -542       N  
ATOM    386  CA  GLY A  55      11.036  69.402  63.506  1.00 60.36           C  
ANISOU  386  CA  GLY A  55    11159   6422   5353   -932   -732   -611       C  
ATOM    387  C   GLY A  55      10.546  70.616  64.281  1.00 61.54           C  
ANISOU  387  C   GLY A  55    11401   6499   5482   -967   -738   -666       C  
ATOM    388  O   GLY A  55      10.832  71.744  63.922  1.00 63.98           O  
ANISOU  388  O   GLY A  55    11771   6728   5810  -1073   -704   -710       O  
ATOM    389  N   ASN A  56       9.880  70.380  65.396  1.00 61.36           N  
ANISOU  389  N   ASN A  56    11389   6504   5419   -881   -774   -668       N  
ATOM    390  CA  ASN A  56       9.071  71.395  66.101  1.00 59.61           C  
ANISOU  390  CA  ASN A  56    11274   6196   5178   -878   -768   -708       C  
ATOM    391  C   ASN A  56       8.427  72.444  65.198  1.00 56.86           C  
ANISOU  391  C   ASN A  56    11049   5679   4874   -914   -710   -688       C  
ATOM    392  O   ASN A  56       8.652  73.629  65.349  1.00 58.50           O  
ANISOU  392  O   ASN A  56    11329   5806   5090   -999   -683   -755       O  
ATOM    393  CB  ASN A  56       9.921  72.005  67.203  1.00 59.92           C  
ANISOU  393  CB  ASN A  56    11281   6314   5170   -955   -801   -823       C  
ATOM    394  CG  ASN A  56      10.176  71.009  68.334  1.00 59.96           C  
ANISOU  394  CG  ASN A  56    11186   6488   5107   -872   -864   -822       C  
ATOM    395  OD1 ASN A  56       9.255  70.435  68.980  1.00 60.22           O  
ANISOU  395  OD1 ASN A  56    11240   6532   5106   -753   -874   -770       O  
ATOM    396  ND2 ASN A  56      11.442  70.808  68.597  1.00 61.25           N  
ANISOU  396  ND2 ASN A  56    11234   6790   5245   -933   -904   -874       N  
ATOM    397  N   THR A  57       7.597  71.998  64.263  1.00 54.79           N  
ANISOU  397  N   THR A  57    10815   5365   4638   -845   -690   -593       N  
ATOM    398  CA  THR A  57       7.056  72.909  63.236  1.00 54.11           C  
ANISOU  398  CA  THR A  57    10835   5139   4584   -866   -639   -551       C  
ATOM    399  C   THR A  57       5.996  73.899  63.720  1.00 54.77           C  
ANISOU  399  C   THR A  57    11033   5107   4670   -814   -616   -554       C  
ATOM    400  O   THR A  57       5.603  74.770  62.954  1.00 56.07           O  
ANISOU  400  O   THR A  57    11293   5149   4860   -822   -570   -515       O  
ATOM    401  CB  THR A  57       6.556  72.185  61.969  1.00 51.69           C  
ANISOU  401  CB  THR A  57    10516   4832   4290   -818   -630   -455       C  
ATOM    402  OG1 THR A  57       5.466  71.312  62.289  1.00 52.09           O  
ANISOU  402  OG1 THR A  57    10541   4918   4330   -701   -657   -407       O  
ATOM    403  CG2 THR A  57       7.694  71.400  61.333  1.00 50.53           C  
ANISOU  403  CG2 THR A  57    10275   4774   4147   -880   -631   -460       C  
ATOM    404  N   TYR A  58       5.599  73.841  64.988  1.00 55.70           N  
ANISOU  404  N   TYR A  58    11147   5260   4756   -759   -640   -600       N  
ATOM    405  CA  TYR A  58       4.864  74.972  65.589  1.00 57.39           C  
ANISOU  405  CA  TYR A  58    11474   5359   4972   -731   -605   -637       C  
ATOM    406  C   TYR A  58       5.655  76.280  65.453  1.00 60.25           C  
ANISOU  406  C   TYR A  58    11919   5611   5361   -860   -558   -715       C  
ATOM    407  O   TYR A  58       5.067  77.347  65.380  1.00 61.17           O  
ANISOU  407  O   TYR A  58    12157   5579   5505   -843   -502   -716       O  
ATOM    408  CB  TYR A  58       4.489  74.722  67.053  1.00 55.72           C  
ANISOU  408  CB  TYR A  58    11242   5219   4708   -668   -632   -693       C  
ATOM    409  CG  TYR A  58       5.639  74.873  68.008  1.00 56.11           C  
ANISOU  409  CG  TYR A  58    11250   5355   4712   -764   -662   -812       C  
ATOM    410  CD1 TYR A  58       5.934  76.097  68.588  1.00 56.60           C  
ANISOU  410  CD1 TYR A  58    11397   5340   4769   -845   -632   -926       C  
ATOM    411  CD2 TYR A  58       6.449  73.793  68.333  1.00 56.55           C  
ANISOU  411  CD2 TYR A  58    11179   5576   4730   -774   -720   -813       C  
ATOM    412  CE1 TYR A  58       6.995  76.243  69.452  1.00 56.63           C  
ANISOU  412  CE1 TYR A  58    11350   5444   4722   -946   -669  -1049       C  
ATOM    413  CE2 TYR A  58       7.518  73.934  69.216  1.00 56.69           C  
ANISOU  413  CE2 TYR A  58    11141   5702   4695   -856   -760   -921       C  
ATOM    414  CZ  TYR A  58       7.778  75.165  69.758  1.00 56.53           C  
ANISOU  414  CZ  TYR A  58    11198   5618   4663   -949   -738  -1042       C  
ATOM    415  OH  TYR A  58       8.827  75.315  70.597  1.00 59.20           O  
ANISOU  415  OH  TYR A  58    11470   6080   4941  -1042   -784  -1159       O  
ATOM    416  N   ARG A  59       6.977  76.183  65.405  1.00 63.01           N  
ANISOU  416  N   ARG A  59    12200   6031   5707   -987   -573   -778       N  
ATOM    417  CA  ARG A  59       7.815  77.348  65.224  1.00 66.89           C  
ANISOU  417  CA  ARG A  59    12757   6426   6232  -1135   -522   -858       C  
ATOM    418  C   ARG A  59       7.541  78.101  63.935  1.00 66.76           C  
ANISOU  418  C   ARG A  59    12848   6246   6272  -1152   -447   -773       C  
ATOM    419  O   ARG A  59       7.662  79.334  63.914  1.00 66.79           O  
ANISOU  419  O   ARG A  59    12968   6095   6313  -1228   -377   -819       O  
ATOM    420  CB  ARG A  59       9.283  76.959  65.305  1.00 71.26           C  
ANISOU  420  CB  ARG A  59    13185   7115   6774  -1266   -556   -930       C  
ATOM    421  CG  ARG A  59       9.741  76.584  66.699  1.00 76.76           C  
ANISOU  421  CG  ARG A  59    13793   7965   7405  -1274   -625  -1035       C  
ATOM    422  CD  ARG A  59      11.234  76.430  66.611  1.00 85.12           C  
ANISOU  422  CD  ARG A  59    14729   9147   8462  -1413   -649  -1104       C  
ATOM    423  NE  ARG A  59      11.871  75.750  67.725  1.00 94.99           N  
ANISOU  423  NE  ARG A  59    15848  10602   9640  -1406   -733  -1174       N  
ATOM    424  CZ  ARG A  59      12.953  74.966  67.630  1.00 99.63           C  
ANISOU  424  CZ  ARG A  59    16279  11361  10214  -1439   -779  -1176       C  
ATOM    425  NH1 ARG A  59      13.509  74.642  66.448  1.00 95.11           N  
ANISOU  425  NH1 ARG A  59    15655  10785   9696  -1478   -746  -1115       N  
ATOM    426  NH2 ARG A  59      13.454  74.451  68.757  1.00102.46           N  
ANISOU  426  NH2 ARG A  59    16526  11908  10493  -1415   -859  -1235       N  
HETATM  427  N   MSE A  60       7.196  77.376  62.865  1.00 64.99           N  
ANISOU  427  N   MSE A  60    12588   6054   6049  -1086   -456   -653       N  
HETATM  428  CA  MSE A  60       6.825  77.997  61.586  1.00 64.99           C  
ANISOU  428  CA  MSE A  60    12687   5925   6080  -1077   -393   -552       C  
HETATM  429  C   MSE A  60       5.604  78.859  61.735  1.00 64.37           C  
ANISOU  429  C   MSE A  60    12740   5700   6018   -969   -354   -508       C  
HETATM  430  O   MSE A  60       5.481  79.898  61.086  1.00 66.93           O  
ANISOU  430  O   MSE A  60    13186   5865   6376   -987   -279   -461       O  
HETATM  431  CB  MSE A  60       6.452  76.983  60.525  1.00 65.20           C  
ANISOU  431  CB  MSE A  60    12651   6036   6084  -1002   -422   -440       C  
HETATM  432  CG  MSE A  60       7.584  76.040  60.114  1.00 67.47           C  
ANISOU  432  CG  MSE A  60    12813   6461   6360  -1084   -446   -461       C  
HETATM  433 SE   MSE A  60       9.259  77.059  59.695  1.00 73.87          SE  
ANISOU  433 SE   MSE A  60    13642   7214   7208  -1305   -369   -533      SE  
HETATM  434  CE  MSE A  60      10.795  76.377  60.722  1.00 73.95           C  
ANISOU  434  CE  MSE A  60    13471   7413   7211  -1420   -424   -676       C  
ATOM    435  N   ILE A  61       4.709  78.455  62.616  1.00 62.77           N  
ANISOU  435  N   ILE A  61    12513   5544   5791   -853   -395   -520       N  
ATOM    436  CA  ILE A  61       3.526  79.233  62.916  1.00 63.95           C  
ANISOU  436  CA  ILE A  61    12770   5570   5957   -737   -357   -489       C  
ATOM    437  C   ILE A  61       3.910  80.477  63.733  1.00 64.40           C  
ANISOU  437  C   ILE A  61    12938   5485   6042   -816   -293   -606       C  
ATOM    438  O   ILE A  61       3.472  81.583  63.432  1.00 66.03           O  
ANISOU  438  O   ILE A  61    13283   5511   6292   -787   -215   -574       O  
ATOM    439  CB  ILE A  61       2.467  78.366  63.624  1.00 63.47           C  
ANISOU  439  CB  ILE A  61    12636   5615   5861   -596   -412   -470       C  
ATOM    440  CG1 ILE A  61       2.106  77.150  62.753  1.00 62.06           C  
ANISOU  440  CG1 ILE A  61    12354   5561   5663   -539   -466   -368       C  
ATOM    441  CG2 ILE A  61       1.199  79.170  63.894  1.00 65.33           C  
ANISOU  441  CG2 ILE A  61    12971   5735   6117   -462   -366   -434       C  
ATOM    442  CD1 ILE A  61       1.575  75.976  63.543  1.00 61.80           C  
ANISOU  442  CD1 ILE A  61    12214   5666   5600   -465   -522   -377       C  
ATOM    443  N   GLU A  62       4.762  80.299  64.731  1.00 64.55           N  
ANISOU  443  N   GLU A  62    12899   5588   6036   -918   -324   -741       N  
ATOM    444  CA  GLU A  62       5.265  81.428  65.529  1.00 65.62           C  
ANISOU  444  CA  GLU A  62    13130   5610   6192  -1026   -269   -882       C  
ATOM    445  C   GLU A  62       6.018  82.443  64.657  1.00 66.39           C  
ANISOU  445  C   GLU A  62    13324   5546   6355  -1165   -183   -882       C  
ATOM    446  O   GLU A  62       5.812  83.650  64.809  1.00 66.35           O  
ANISOU  446  O   GLU A  62    13469   5343   6398  -1188    -93   -923       O  
ATOM    447  CB  GLU A  62       6.147  80.945  66.693  1.00 66.00           C  
ANISOU  447  CB  GLU A  62    13072   5822   6183  -1121   -335  -1028       C  
ATOM    448  CG  GLU A  62       5.390  80.114  67.730  1.00 66.75           C  
ANISOU  448  CG  GLU A  62    13100   6053   6208   -987   -399  -1034       C  
ATOM    449  CD  GLU A  62       6.232  79.721  68.940  1.00 69.78           C  
ANISOU  449  CD  GLU A  62    13391   6604   6518  -1066   -464  -1170       C  
ATOM    450  OE1 GLU A  62       7.496  79.800  68.878  1.00 73.47           O  
ANISOU  450  OE1 GLU A  62    13797   7132   6984  -1222   -484  -1249       O  
ATOM    451  OE2 GLU A  62       5.621  79.358  69.982  1.00 70.13           O  
ANISOU  451  OE2 GLU A  62    13419   6728   6497   -970   -494  -1198       O  
ATOM    452  N   GLN A  63       6.842  81.956  63.723  1.00 66.59           N  
ANISOU  452  N   GLN A  63    13270   5646   6384  -1250   -198   -830       N  
ATOM    453  CA  GLN A  63       7.622  82.833  62.825  1.00 68.55           C  
ANISOU  453  CA  GLN A  63    13598   5756   6689  -1392   -109   -818       C  
ATOM    454  C   GLN A  63       6.817  83.564  61.760  1.00 68.03           C  
ANISOU  454  C   GLN A  63    13680   5503   6663  -1300    -25   -668       C  
ATOM    455  O   GLN A  63       7.292  84.547  61.213  1.00 69.24           O  
ANISOU  455  O   GLN A  63    13945   5490   6870  -1404     73   -659       O  
ATOM    456  CB  GLN A  63       8.757  82.073  62.177  1.00 68.79           C  
ANISOU  456  CB  GLN A  63    13493   5938   6707  -1505   -143   -810       C  
ATOM    457  CG  GLN A  63       9.838  81.755  63.190  1.00 72.56           C  
ANISOU  457  CG  GLN A  63    13846   6564   7160  -1638   -199   -973       C  
ATOM    458  CD  GLN A  63      10.852  80.743  62.706  1.00 76.53           C  
ANISOU  458  CD  GLN A  63    14179   7258   7641  -1703   -250   -960       C  
ATOM    459  OE1 GLN A  63      10.950  80.458  61.492  1.00 80.33           O  
ANISOU  459  OE1 GLN A  63    14652   7734   8133  -1694   -221   -847       O  
ATOM    460  NE2 GLN A  63      11.553  80.106  63.664  1.00 76.15           N  
ANISOU  460  NE2 GLN A  63    13987   7395   7550  -1746   -331  -1069       N  
ATOM    461  N   ASP A  64       5.601  83.094  61.503  1.00 67.20           N  
ANISOU  461  N   ASP A  64    13572   5430   6530  -1106    -63   -550       N  
ATOM    462  CA  ASP A  64       4.650  83.805  60.664  1.00 68.72           C  
ANISOU  462  CA  ASP A  64    13896   5464   6747   -980      2   -404       C  
ATOM    463  C   ASP A  64       3.819  84.827  61.459  1.00 69.60           C  
ANISOU  463  C   ASP A  64    14147   5398   6900   -890     66   -442       C  
ATOM    464  O   ASP A  64       2.953  85.500  60.879  1.00 68.04           O  
ANISOU  464  O   ASP A  64    14065   5059   6728   -759    127   -319       O  
ATOM    465  CB  ASP A  64       3.732  82.802  59.927  1.00 67.89           C  
ANISOU  465  CB  ASP A  64    13705   5501   6589   -818    -74   -262       C  
ATOM    466  CG  ASP A  64       4.460  82.023  58.827  1.00 67.75           C  
ANISOU  466  CG  ASP A  64    13598   5607   6536   -894   -104   -201       C  
ATOM    467  OD1 ASP A  64       5.572  82.401  58.416  1.00 67.00           O  
ANISOU  467  OD1 ASP A  64    13524   5468   6463  -1050    -50   -231       O  
ATOM    468  OD2 ASP A  64       3.890  81.031  58.326  1.00 69.86           O  
ANISOU  468  OD2 ASP A  64    13771   6016   6753   -797   -175   -124       O  
ATOM    469  N   ASP A  65       4.089  84.936  62.760  1.00 71.56           N  
ANISOU  469  N   ASP A  65    14382   5659   7147   -952     55   -609       N  
ATOM    470  CA  ASP A  65       3.472  85.912  63.652  1.00 76.60           C  
ANISOU  470  CA  ASP A  65    15152   6131   7821   -894    126   -685       C  
ATOM    471  C   ASP A  65       2.003  85.692  63.949  1.00 73.45           C  
ANISOU  471  C   ASP A  65    14752   5752   7401   -663    104   -607       C  
ATOM    472  O   ASP A  65       1.284  86.645  64.243  1.00 76.63           O  
ANISOU  472  O   ASP A  65    15291   5975   7847   -567    189   -607       O  
ATOM    473  CB  ASP A  65       3.713  87.369  63.154  1.00 84.41           C  
ANISOU  473  CB  ASP A  65    16340   6836   8896   -961    271   -672       C  
ATOM    474  CG  ASP A  65       5.136  87.849  63.438  1.00 89.12           C  
ANISOU  474  CG  ASP A  65    16952   7383   9525  -1221    314   -830       C  
ATOM    475  OD1 ASP A  65       5.537  87.693  64.625  1.00 92.82           O  
ANISOU  475  OD1 ASP A  65    17364   7939   9964  -1306    271  -1010       O  
ATOM    476  OD2 ASP A  65       5.820  88.358  62.494  1.00 89.35           O  
ANISOU  476  OD2 ASP A  65    17044   7302   9601  -1336    389   -773       O  
ATOM    477  N   PHE A  66       1.554  84.456  63.927  1.00 69.27           N  
ANISOU  477  N   PHE A  66    14071   5435   6812   -575      0   -550       N  
ATOM    478  CA  PHE A  66       0.179  84.181  64.334  1.00 69.81           C  
ANISOU  478  CA  PHE A  66    14116   5546   6861   -373    -21   -495       C  
ATOM    479  C   PHE A  66       0.122  83.973  65.847  1.00 69.88           C  
ANISOU  479  C   PHE A  66    14091   5626   6834   -380    -42   -648       C  
ATOM    480  O   PHE A  66       0.985  83.309  66.412  1.00 68.12           O  
ANISOU  480  O   PHE A  66    13774   5542   6566   -501   -104   -747       O  
ATOM    481  CB  PHE A  66      -0.373  82.953  63.620  1.00 67.82           C  
ANISOU  481  CB  PHE A  66    13719   5482   6564   -281   -114   -367       C  
ATOM    482  CG  PHE A  66      -0.564  83.134  62.143  1.00 67.96           C  
ANISOU  482  CG  PHE A  66    13770   5457   6596   -239    -99   -207       C  
ATOM    483  CD1 PHE A  66      -1.567  83.961  61.665  1.00 70.03           C  
ANISOU  483  CD1 PHE A  66    14131   5589   6887    -82    -41    -92       C  
ATOM    484  CD2 PHE A  66       0.247  82.459  61.237  1.00 67.41           C  
ANISOU  484  CD2 PHE A  66    13626   5485   6499   -344   -144   -168       C  
ATOM    485  CE1 PHE A  66      -1.737  84.143  60.309  1.00 72.11           C  
ANISOU  485  CE1 PHE A  66    14426   5828   7145    -35    -32     62       C  
ATOM    486  CE2 PHE A  66       0.079  82.625  59.880  1.00 69.05           C  
ANISOU  486  CE2 PHE A  66    13866   5667   6699   -305   -130    -23       C  
ATOM    487  CZ  PHE A  66      -0.920  83.460  59.410  1.00 71.56           C  
ANISOU  487  CZ  PHE A  66    14286   5864   7036   -150    -78     95       C  
ATOM    488  N   ASP A  67      -0.880  84.568  66.493  1.00 71.36           N  
ANISOU  488  N   ASP A  67    14356   5721   7036   -244     14   -663       N  
ATOM    489  CA  ASP A  67      -1.118  84.333  67.910  1.00 71.94           C  
ANISOU  489  CA  ASP A  67    14398   5875   7060   -223      0   -793       C  
ATOM    490  C   ASP A  67      -1.767  82.977  68.009  1.00 67.74           C  
ANISOU  490  C   ASP A  67    13701   5564   6471   -123    -92   -715       C  
ATOM    491  O   ASP A  67      -2.874  82.775  67.502  1.00 65.56           O  
ANISOU  491  O   ASP A  67    13396   5302   6211     33    -93   -587       O  
ATOM    492  CB  ASP A  67      -2.017  85.415  68.544  1.00 76.24           C  
ANISOU  492  CB  ASP A  67    15082   6245   7639   -100    105   -836       C  
ATOM    493  CG  ASP A  67      -1.369  86.811  68.506  1.00 82.67           C  
ANISOU  493  CG  ASP A  67    16081   6808   8522   -209    216   -928       C  
ATOM    494  OD1 ASP A  67      -0.105  86.882  68.535  1.00 84.09           O  
ANISOU  494  OD1 ASP A  67    16260   6993   8696   -416    201  -1030       O  
ATOM    495  OD2 ASP A  67      -2.117  87.839  68.439  1.00 86.01           O  
ANISOU  495  OD2 ASP A  67    16647   7024   9007    -89    325   -898       O  
ATOM    496  N   ILE A  68      -1.067  82.045  68.651  1.00 64.35           N  
ANISOU  496  N   ILE A  68    13162   5309   5978   -217   -169   -791       N  
ATOM    497  CA  ILE A  68      -1.616  80.731  68.877  1.00 61.29           C  
ANISOU  497  CA  ILE A  68    12629   5117   5540   -136   -243   -728       C  
ATOM    498  C   ILE A  68      -2.466  80.779  70.141  1.00 61.32           C  
ANISOU  498  C   ILE A  68    12642   5152   5503    -30   -213   -789       C  
ATOM    499  O   ILE A  68      -1.953  80.990  71.223  1.00 61.35           O  
ANISOU  499  O   ILE A  68    12673   5179   5454    -97   -207   -925       O  
ATOM    500  CB  ILE A  68      -0.511  79.676  68.989  1.00 59.67           C  
ANISOU  500  CB  ILE A  68    12306   5077   5286   -261   -327   -763       C  
ATOM    501  CG1 ILE A  68       0.297  79.588  67.686  1.00 57.88           C  
ANISOU  501  CG1 ILE A  68    12063   4828   5099   -358   -347   -700       C  
ATOM    502  CG2 ILE A  68      -1.133  78.309  69.279  1.00 59.39           C  
ANISOU  502  CG2 ILE A  68    12137   5219   5207   -172   -386   -694       C  
ATOM    503  CD1 ILE A  68       1.595  78.813  67.792  1.00 56.17           C  
ANISOU  503  CD1 ILE A  68    11747   4747   4847   -494   -412   -755       C  
ATOM    504  N   ASN A  69      -3.773  80.584  69.995  1.00 62.11           N  
ANISOU  504  N   ASN A  69    12712   5266   5620    132   -195   -689       N  
ATOM    505  CA  ASN A  69      -4.688  80.571  71.144  1.00 63.03           C  
ANISOU  505  CA  ASN A  69    12825   5424   5698    245   -156   -733       C  
ATOM    506  C   ASN A  69      -4.423  79.367  72.043  1.00 62.26           C  
ANISOU  506  C   ASN A  69    12613   5526   5516    209   -218   -768       C  
ATOM    507  O   ASN A  69      -4.284  79.510  73.249  1.00 63.79           O  
ANISOU  507  O   ASN A  69    12836   5757   5643    198   -198   -879       O  
ATOM    508  CB  ASN A  69      -6.150  80.555  70.655  1.00 63.75           C  
ANISOU  508  CB  ASN A  69    12880   5506   5833    426   -126   -604       C  
ATOM    509  CG  ASN A  69      -7.167  80.560  71.796  1.00 65.93           C  
ANISOU  509  CG  ASN A  69    13144   5828   6077    552    -71   -642       C  
ATOM    510  OD1 ASN A  69      -7.317  79.584  72.528  1.00 66.46           O  
ANISOU  510  OD1 ASN A  69    13114   6054   6083    552   -103   -652       O  
ATOM    511  ND2 ASN A  69      -7.885  81.661  71.941  1.00 69.10           N  
ANISOU  511  ND2 ASN A  69    13647   6085   6519    668     20   -655       N  
ATOM    512  N   THR A  70      -4.385  78.185  71.427  1.00 61.62           N  
ANISOU  512  N   THR A  70    12408   5568   5435    198   -288   -669       N  
ATOM    513  CA  THR A  70      -4.381  76.918  72.125  1.00 60.67           C  
ANISOU  513  CA  THR A  70    12175   5623   5251    199   -334   -659       C  
ATOM    514  C   THR A  70      -3.397  75.923  71.510  1.00 58.82           C  
ANISOU  514  C   THR A  70    11855   5479   5013     95   -413   -622       C  
ATOM    515  O   THR A  70      -3.293  75.844  70.304  1.00 60.18           O  
ANISOU  515  O   THR A  70    12010   5612   5240     71   -433   -550       O  
ATOM    516  CB  THR A  70      -5.796  76.328  72.098  1.00 60.72           C  
ANISOU  516  CB  THR A  70    12104   5689   5275    335   -312   -558       C  
ATOM    517  OG1 THR A  70      -6.712  77.264  72.683  1.00 63.36           O  
ANISOU  517  OG1 THR A  70    12511   5946   5615    446   -231   -593       O  
ATOM    518  CG2 THR A  70      -5.859  75.032  72.907  1.00 60.52           C  
ANISOU  518  CG2 THR A  70    11977   5828   5188    338   -338   -542       C  
ATOM    519  N   ARG A  71      -2.688  75.185  72.363  1.00 58.65           N  
ANISOU  519  N   ARG A  71    11782   5582   4920     44   -452   -669       N  
ATOM    520  CA  ARG A  71      -1.769  74.115  71.972  1.00 58.65           C  
ANISOU  520  CA  ARG A  71    11690   5682   4911    -31   -519   -633       C  
ATOM    521  C   ARG A  71      -2.217  72.831  72.616  1.00 56.98           C  
ANISOU  521  C   ARG A  71    11388   5602   4657     32   -531   -573       C  
ATOM    522  O   ARG A  71      -2.459  72.826  73.814  1.00 56.04           O  
ANISOU  522  O   ARG A  71    11282   5543   4466     76   -510   -615       O  
ATOM    523  CB  ARG A  71      -0.374  74.406  72.490  1.00 61.49           C  
ANISOU  523  CB  ARG A  71    12065   6080   5218   -146   -555   -742       C  
ATOM    524  CG  ARG A  71       0.191  75.669  71.913  1.00 65.37           C  
ANISOU  524  CG  ARG A  71    12648   6433   5754   -236   -532   -811       C  
ATOM    525  CD  ARG A  71       1.516  76.040  72.545  1.00 67.56           C  
ANISOU  525  CD  ARG A  71    12930   6759   5977   -364   -564   -942       C  
ATOM    526  NE  ARG A  71       1.847  77.436  72.177  1.00 69.44           N  
ANISOU  526  NE  ARG A  71    13284   6833   6265   -450   -514  -1025       N  
ATOM    527  CZ  ARG A  71       2.882  77.831  71.429  1.00 70.33           C  
ANISOU  527  CZ  ARG A  71    13402   6898   6421   -582   -522  -1054       C  
ATOM    528  NH1 ARG A  71       3.778  76.965  70.950  1.00 68.88           N  
ANISOU  528  NH1 ARG A  71    13108   6829   6234   -644   -582  -1017       N  
ATOM    529  NH2 ARG A  71       3.024  79.129  71.156  1.00 73.23           N  
ANISOU  529  NH2 ARG A  71    13891   7092   6840   -652   -457  -1121       N  
ATOM    530  N   LEU A  72      -2.321  71.753  71.842  1.00 55.32           N  
ANISOU  530  N   LEU A  72    11095   5435   4489     35   -556   -479       N  
ATOM    531  CA  LEU A  72      -2.775  70.481  72.371  1.00 55.06           C  
ANISOU  531  CA  LEU A  72    10983   5503   4432     88   -552   -413       C  
ATOM    532  C   LEU A  72      -1.827  69.360  71.988  1.00 57.33           C  
ANISOU  532  C   LEU A  72    11200   5857   4725     33   -598   -376       C  
ATOM    533  O   LEU A  72      -1.577  69.166  70.798  1.00 56.74           O  
ANISOU  533  O   LEU A  72    11102   5742   4711    -11   -617   -345       O  
ATOM    534  CB  LEU A  72      -4.129  70.145  71.798  1.00 53.66           C  
ANISOU  534  CB  LEU A  72    10768   5303   4317    158   -517   -331       C  
ATOM    535  CG  LEU A  72      -5.249  71.153  71.894  1.00 53.46           C  
ANISOU  535  CG  LEU A  72    10790   5211   4310    236   -467   -340       C  
ATOM    536  CD1 LEU A  72      -6.478  70.532  71.290  1.00 52.46           C  
ANISOU  536  CD1 LEU A  72    10584   5106   4240    294   -448   -251       C  
ATOM    537  CD2 LEU A  72      -5.550  71.535  73.321  1.00 55.74           C  
ANISOU  537  CD2 LEU A  72    11121   5531   4526    293   -421   -397       C  
ATOM    538  N   HIS A  73      -1.287  68.648  72.983  1.00 60.12           N  
ANISOU  538  N   HIS A  73    11521   6313   5008     46   -612   -376       N  
ATOM    539  CA  HIS A  73      -0.563  67.402  72.747  1.00 61.82           C  
ANISOU  539  CA  HIS A  73    11663   6592   5233     29   -639   -319       C  
ATOM    540  C   HIS A  73      -1.615  66.364  72.353  1.00 62.16           C  
ANISOU  540  C   HIS A  73    11662   6618   5335     77   -597   -223       C  
ATOM    541  O   HIS A  73      -2.365  65.912  73.199  1.00 62.47           O  
ANISOU  541  O   HIS A  73    11694   6696   5346    141   -554   -183       O  
ATOM    542  CB  HIS A  73       0.141  66.910  74.013  1.00 64.71           C  
ANISOU  542  CB  HIS A  73    12007   7079   5498     57   -659   -326       C  
ATOM    543  CG  HIS A  73       1.367  67.675  74.394  1.00 69.32           C  
ANISOU  543  CG  HIS A  73    12604   7715   6017     -6   -714   -425       C  
ATOM    544  ND1 HIS A  73       1.321  68.912  75.013  1.00 74.97           N  
ANISOU  544  ND1 HIS A  73    13389   8417   6678    -30   -713   -530       N  
ATOM    545  CD2 HIS A  73       2.678  67.350  74.312  1.00 71.15           C  
ANISOU  545  CD2 HIS A  73    12780   8024   6228    -53   -769   -442       C  
ATOM    546  CE1 HIS A  73       2.553  69.327  75.265  1.00 74.77           C  
ANISOU  546  CE1 HIS A  73    13349   8456   6601   -106   -768   -615       C  
ATOM    547  NE2 HIS A  73       3.395  68.395  74.852  1.00 74.67           N  
ANISOU  547  NE2 HIS A  73    13253   8510   6607   -117   -806   -560       N  
ATOM    548  N   THR A  74      -1.681  65.972  71.080  1.00 61.84           N  
ANISOU  548  N   THR A  74    11592   6528   5376     38   -603   -191       N  
ATOM    549  CA  THR A  74      -2.689  64.996  70.650  1.00 59.74           C  
ANISOU  549  CA  THR A  74    11279   6249   5170     62   -564   -120       C  
ATOM    550  C   THR A  74      -2.120  63.739  70.008  1.00 56.32           C  
ANISOU  550  C   THR A  74    10796   5820   4782     28   -566    -79       C  
ATOM    551  O   THR A  74      -2.864  62.949  69.442  1.00 56.33           O  
ANISOU  551  O   THR A  74    10761   5798   4843     22   -535    -39       O  
ATOM    552  CB  THR A  74      -3.683  65.624  69.658  1.00 61.51           C  
ANISOU  552  CB  THR A  74    11507   6414   5449     57   -559   -120       C  
ATOM    553  OG1 THR A  74      -3.006  65.945  68.442  1.00 66.36           O  
ANISOU  553  OG1 THR A  74    12131   6989   6093     -7   -599   -141       O  
ATOM    554  CG2 THR A  74      -4.323  66.861  70.245  1.00 62.67           C  
ANISOU  554  CG2 THR A  74    11707   6540   5564    108   -542   -154       C  
ATOM    555  N   ILE A  75      -0.828  63.512  70.121  1.00 53.51           N  
ANISOU  555  N   ILE A  75    10433   5496   4399      8   -597    -94       N  
ATOM    556  CA  ILE A  75      -0.250  62.351  69.501  1.00 52.53           C  
ANISOU  556  CA  ILE A  75    10267   5367   4323    -10   -590    -59       C  
ATOM    557  C   ILE A  75       0.188  61.328  70.517  1.00 51.31           C  
ANISOU  557  C   ILE A  75    10091   5266   4136     50   -566     -2       C  
ATOM    558  O   ILE A  75       0.960  61.626  71.440  1.00 50.60           O  
ANISOU  558  O   ILE A  75    10004   5252   3969     80   -598    -14       O  
ATOM    559  CB  ILE A  75       0.905  62.745  68.573  1.00 52.88           C  
ANISOU  559  CB  ILE A  75    10307   5406   4380    -76   -633   -107       C  
ATOM    560  CG1 ILE A  75       0.285  63.314  67.323  1.00 52.71           C  
ANISOU  560  CG1 ILE A  75    10303   5320   4403   -127   -637   -128       C  
ATOM    561  CG2 ILE A  75       1.787  61.534  68.263  1.00 53.24           C  
ANISOU  561  CG2 ILE A  75    10305   5465   4456    -73   -621    -76       C  
ATOM    562  CD1 ILE A  75       1.289  63.897  66.389  1.00 55.64           C  
ANISOU  562  CD1 ILE A  75    10682   5679   4778   -195   -668   -172       C  
ATOM    563  N   VAL A  76      -0.294  60.106  70.305  1.00 50.22           N  
ANISOU  563  N   VAL A  76     9932   5089   4059     65   -510     60       N  
ATOM    564  CA  VAL A  76       0.103  58.957  71.124  1.00 49.11           C  
ANISOU  564  CA  VAL A  76     9779   4974   3905    132   -470    137       C  
ATOM    565  C   VAL A  76       1.297  58.344  70.455  1.00 47.41           C  
ANISOU  565  C   VAL A  76     9535   4752   3724    122   -484    137       C  
ATOM    566  O   VAL A  76       1.348  58.252  69.247  1.00 48.47           O  
ANISOU  566  O   VAL A  76     9661   4830   3925     59   -484     99       O  
ATOM    567  CB  VAL A  76      -1.007  57.924  71.223  1.00 48.63           C  
ANISOU  567  CB  VAL A  76     9718   4854   3905    146   -383    204       C  
ATOM    568  CG1 VAL A  76      -0.508  56.661  71.894  1.00 48.97           C  
ANISOU  568  CG1 VAL A  76     9761   4895   3949    216   -328    297       C  
ATOM    569  CG2 VAL A  76      -2.167  58.534  71.979  1.00 48.85           C  
ANISOU  569  CG2 VAL A  76     9762   4906   3893    166   -361    208       C  
ATOM    570  N   ARG A  77       2.251  57.949  71.267  1.00 46.85           N  
ANISOU  570  N   ARG A  77     9448   4753   3600    191   -496    179       N  
ATOM    571  CA  ARG A  77       3.563  57.555  70.836  1.00 46.79           C  
ANISOU  571  CA  ARG A  77     9399   4773   3606    201   -520    176       C  
ATOM    572  C   ARG A  77       3.521  56.081  70.589  1.00 47.56           C  
ANISOU  572  C   ARG A  77     9495   4793   3783    248   -439    254       C  
ATOM    573  O   ARG A  77       2.765  55.372  71.238  1.00 48.84           O  
ANISOU  573  O   ARG A  77     9685   4918   3954    296   -374    331       O  
ATOM    574  CB  ARG A  77       4.541  57.844  71.945  1.00 47.92           C  
ANISOU  574  CB  ARG A  77     9512   5052   3643    267   -577    190       C  
ATOM    575  CG  ARG A  77       5.967  57.985  71.506  1.00 48.63           C  
ANISOU  575  CG  ARG A  77     9539   5210   3728    253   -630    150       C  
ATOM    576  CD  ARG A  77       6.785  58.455  72.711  1.00 48.87           C  
ANISOU  576  CD  ARG A  77     9530   5404   3635    303   -702    145       C  
ATOM    577  NE  ARG A  77       8.220  58.451  72.439  1.00 49.94           N  
ANISOU  577  NE  ARG A  77     9579   5633   3761    303   -752    118       N  
ATOM    578  CZ  ARG A  77       9.171  58.801  73.301  1.00 49.79           C  
ANISOU  578  CZ  ARG A  77     9496   5782   3640    335   -826    101       C  
ATOM    579  NH1 ARG A  77       8.846  59.177  74.508  1.00 50.35           N  
ANISOU  579  NH1 ARG A  77     9591   5942   3598    371   -858    106       N  
ATOM    580  NH2 ARG A  77      10.446  58.793  72.929  1.00 50.44           N  
ANISOU  580  NH2 ARG A  77     9482   5952   3728    325   -868     71       N  
ATOM    581  N   GLY A  78       4.362  55.623  69.683  1.00 47.92           N  
ANISOU  581  N   GLY A  78     9510   4810   3885    233   -433    235       N  
ATOM    582  CA  GLY A  78       4.267  54.280  69.156  1.00 49.11           C  
ANISOU  582  CA  GLY A  78     9672   4853   4132    255   -344    281       C  
ATOM    583  C   GLY A  78       4.538  54.151  67.676  1.00 50.43           C  
ANISOU  583  C   GLY A  78     9831   4955   4375    175   -332    204       C  
ATOM    584  O   GLY A  78       4.974  53.121  67.220  1.00 51.78           O  
ANISOU  584  O   GLY A  78     9999   5061   4614    205   -269    224       O  
ATOM    585  N   GLU A  79       4.254  55.197  66.914  1.00 53.37           N  
ANISOU  585  N   GLU A  79    10204   5341   4733     77   -385    119       N  
ATOM    586  CA  GLU A  79       4.582  55.266  65.489  1.00 54.50           C  
ANISOU  586  CA  GLU A  79    10338   5448   4920     -1   -384     44       C  
ATOM    587  C   GLU A  79       4.118  54.018  64.739  1.00 54.69           C  
ANISOU  587  C   GLU A  79    10385   5358   5035    -20   -296     42       C  
ATOM    588  O   GLU A  79       4.864  53.432  63.947  1.00 53.50           O  
ANISOU  588  O   GLU A  79    10223   5177   4928    -23   -260     14       O  
ATOM    589  CB  GLU A  79       6.088  55.545  65.298  1.00 57.30           C  
ANISOU  589  CB  GLU A  79    10641   5879   5249     16   -421     22       C  
ATOM    590  CG  GLU A  79       6.619  56.791  66.028  1.00 59.52           C  
ANISOU  590  CG  GLU A  79    10896   6274   5442     12   -507      4       C  
ATOM    591  CD  GLU A  79       6.892  56.572  67.513  1.00 64.58           C  
ANISOU  591  CD  GLU A  79    11517   6994   6025    115   -525     74       C  
ATOM    592  OE1 GLU A  79       7.390  55.456  67.886  1.00 69.53           O  
ANISOU  592  OE1 GLU A  79    12121   7622   6675    213   -481    146       O  
ATOM    593  OE2 GLU A  79       6.571  57.484  68.322  1.00 65.80           O  
ANISOU  593  OE2 GLU A  79    11686   7208   6106    107   -577     61       O  
ATOM    594  N   ASP A  80       2.881  53.627  65.026  1.00 54.97           N  
ANISOU  594  N   ASP A  80    10450   5335   5100    -36   -254     66       N  
ATOM    595  CA  ASP A  80       2.221  52.530  64.378  1.00 55.80           C  
ANISOU  595  CA  ASP A  80    10578   5329   5292    -81   -169     49       C  
ATOM    596  C   ASP A  80       0.727  52.813  64.273  1.00 55.98           C  
ANISOU  596  C   ASP A  80    10607   5339   5322   -157   -172     26       C  
ATOM    597  O   ASP A  80       0.259  53.893  64.586  1.00 54.82           O  
ANISOU  597  O   ASP A  80    10450   5263   5115   -165   -239     23       O  
ATOM    598  CB  ASP A  80       2.510  51.225  65.133  1.00 59.54           C  
ANISOU  598  CB  ASP A  80    11073   5726   5821      9    -74    135       C  
ATOM    599  CG  ASP A  80       1.968  51.211  66.546  1.00 61.46           C  
ANISOU  599  CG  ASP A  80    11329   5991   6029     79    -62    234       C  
ATOM    600  OD1 ASP A  80       1.516  52.236  67.046  1.00 63.36           O  
ANISOU  600  OD1 ASP A  80    11558   6316   6199     68   -130    230       O  
ATOM    601  OD2 ASP A  80       2.003  50.147  67.187  1.00 68.08           O  
ANISOU  601  OD2 ASP A  80    12196   6757   6912    151     26    320       O  
ATOM    602  N   GLU A  81      -0.009  51.849  63.745  1.00 60.54           N  
ANISOU  602  N   GLU A  81    11197   5827   5977   -219    -98     -1       N  
ATOM    603  CA  GLU A  81      -1.405  52.047  63.397  1.00 61.44           C  
ANISOU  603  CA  GLU A  81    11295   5945   6105   -308   -104    -42       C  
ATOM    604  C   GLU A  81      -2.235  52.225  64.619  1.00 60.94           C  
ANISOU  604  C   GLU A  81    11225   5901   6026   -266    -89     32       C  
ATOM    605  O   GLU A  81      -3.070  53.119  64.659  1.00 59.64           O  
ANISOU  605  O   GLU A  81    11034   5805   5822   -291   -143     17       O  
ATOM    606  CB  GLU A  81      -1.904  50.879  62.572  1.00 63.72           C  
ANISOU  606  CB  GLU A  81    11591   6136   6482   -396    -21   -103       C  
ATOM    607  CG  GLU A  81      -1.236  50.782  61.207  1.00 67.83           C  
ANISOU  607  CG  GLU A  81    12118   6652   7003   -452    -37   -198       C  
ATOM    608  CD  GLU A  81      -0.853  49.358  60.881  1.00 72.32           C  
ANISOU  608  CD  GLU A  81    12724   7089   7663   -465     77   -224       C  
ATOM    609  OE1 GLU A  81       0.093  48.851  61.553  1.00 74.05           O  
ANISOU  609  OE1 GLU A  81    12970   7256   7907   -359    128   -151       O  
ATOM    610  OE2 GLU A  81      -1.502  48.768  59.975  1.00 72.06           O  
ANISOU  610  OE2 GLU A  81    12693   7010   7675   -576    116   -319       O  
ATOM    611  N   ALA A  82      -1.980  51.414  65.646  1.00 63.17           N  
ANISOU  611  N   ALA A  82    11536   6131   6335   -190    -14    121       N  
ATOM    612  CA  ALA A  82      -2.674  51.603  66.931  1.00 61.31           C  
ANISOU  612  CA  ALA A  82    11301   5928   6067   -138      6    203       C  
ATOM    613  C   ALA A  82      -2.507  53.028  67.453  1.00 59.22           C  
ANISOU  613  C   ALA A  82    11022   5783   5695    -90    -95    204       C  
ATOM    614  O   ALA A  82      -3.474  53.647  67.820  1.00 58.73           O  
ANISOU  614  O   ALA A  82    10941   5765   5606   -103   -109    204       O  
ATOM    615  CB  ALA A  82      -2.192  50.611  67.959  1.00 63.06           C  
ANISOU  615  CB  ALA A  82    11562   6089   6306    -43     94    313       C  
ATOM    616  N   ALA A  83      -1.285  53.547  67.421  1.00 58.42           N  
ANISOU  616  N   ALA A  83    10925   5731   5538    -43   -160    195       N  
ATOM    617  CA  ALA A  83      -0.989  54.897  67.895  1.00 57.96           C  
ANISOU  617  CA  ALA A  83    10862   5774   5385    -12   -250    180       C  
ATOM    618  C   ALA A  83      -1.645  55.977  67.057  1.00 57.47           C  
ANISOU  618  C   ALA A  83    10786   5738   5311    -85   -311    104       C  
ATOM    619  O   ALA A  83      -2.092  56.967  67.593  1.00 60.22           O  
ANISOU  619  O   ALA A  83    11138   6138   5604    -65   -348    102       O  
ATOM    620  CB  ALA A  83       0.501  55.136  67.945  1.00 57.44           C  
ANISOU  620  CB  ALA A  83    10792   5757   5275     32   -300    176       C  
HETATM  621  N   MSE A  84      -1.703  55.793  65.755  1.00 56.92           N  
ANISOU  621  N   MSE A  84    10705   5634   5288   -161   -317     45       N  
HETATM  622  CA  MSE A  84      -2.443  56.695  64.882  1.00 56.09           C  
ANISOU  622  CA  MSE A  84    10584   5556   5169   -222   -369    -10       C  
HETATM  623  C   MSE A  84      -3.877  56.791  65.314  1.00 53.45           C  
ANISOU  623  C   MSE A  84    10225   5235   4846   -224   -347      8       C  
HETATM  624  O   MSE A  84      -4.407  57.890  65.463  1.00 52.18           O  
ANISOU  624  O   MSE A  84    10061   5123   4643   -206   -392      2       O  
HETATM  625  CB  MSE A  84      -2.304  56.183  63.469  1.00 60.45           C  
ANISOU  625  CB  MSE A  84    11127   6077   5762   -300   -365    -71       C  
HETATM  626  CG  MSE A  84      -3.197  56.922  62.487  1.00 68.31           C  
ANISOU  626  CG  MSE A  84    12100   7113   6739   -359   -416   -117       C  
HETATM  627 SE   MSE A  84      -2.594  56.693  60.615  1.00 78.87          SE  
ANISOU  627 SE   MSE A  84    13442   8450   8075   -449   -437   -201      SE  
HETATM  628  CE  MSE A  84      -0.726  57.348  60.646  1.00 68.64           C  
ANISOU  628  CE  MSE A  84    12183   7161   6734   -408   -465   -195       C  
ATOM    629  N   VAL A  85      -4.512  55.657  65.607  1.00 52.38           N  
ANISOU  629  N   VAL A  85    10073   5054   4772   -242   -267     35       N  
ATOM    630  CA  VAL A  85      -5.922  55.676  66.027  1.00 51.32           C  
ANISOU  630  CA  VAL A  85     9899   4942   4657   -254   -235     52       C  
ATOM    631  C   VAL A  85      -6.111  56.346  67.404  1.00 51.19           C  
ANISOU  631  C   VAL A  85     9899   4970   4580   -164   -231    110       C  
ATOM    632  O   VAL A  85      -7.048  57.121  67.587  1.00 49.61           O  
ANISOU  632  O   VAL A  85     9669   4820   4358   -152   -247    105       O  
ATOM    633  CB  VAL A  85      -6.556  54.280  66.001  1.00 50.00           C  
ANISOU  633  CB  VAL A  85     9711   4706   4579   -315   -136     62       C  
ATOM    634  CG1 VAL A  85      -7.959  54.287  66.590  1.00 49.67           C  
ANISOU  634  CG1 VAL A  85     9617   4698   4557   -327    -91     87       C  
ATOM    635  CG2 VAL A  85      -6.616  53.814  64.567  1.00 51.49           C  
ANISOU  635  CG2 VAL A  85     9877   4870   4814   -418   -149    -22       C  
ATOM    636  N   GLU A  86      -5.214  56.056  68.337  1.00 51.59           N  
ANISOU  636  N   GLU A  86     9992   5011   4595    -97   -209    163       N  
ATOM    637  CA  GLU A  86      -5.298  56.608  69.683  1.00 53.73           C  
ANISOU  637  CA  GLU A  86    10285   5337   4792    -13   -204    211       C  
ATOM    638  C   GLU A  86      -5.080  58.123  69.657  1.00 51.52           C  
ANISOU  638  C   GLU A  86    10020   5115   4439      8   -290    160       C  
ATOM    639  O   GLU A  86      -5.710  58.852  70.404  1.00 49.08           O  
ANISOU  639  O   GLU A  86     9715   4848   4083     52   -287    165       O  
ATOM    640  CB  GLU A  86      -4.311  55.890  70.641  1.00 56.71           C  
ANISOU  640  CB  GLU A  86    10702   5710   5135     58   -170    283       C  
ATOM    641  CG  GLU A  86      -4.641  54.419  70.866  1.00 58.22           C  
ANISOU  641  CG  GLU A  86    10896   5823   5400     52    -60    354       C  
ATOM    642  CD  GLU A  86      -3.772  53.724  71.908  1.00 62.23           C  
ANISOU  642  CD  GLU A  86    11445   6333   5866    149    -19    451       C  
ATOM    643  OE1 GLU A  86      -3.075  54.388  72.706  1.00 61.24           O  
ANISOU  643  OE1 GLU A  86    11335   6297   5635    225    -76    467       O  
ATOM    644  OE2 GLU A  86      -3.830  52.465  71.978  1.00 67.67           O  
ANISOU  644  OE2 GLU A  86    12152   6933   6625    152     76    517       O  
ATOM    645  N   SER A  87      -4.234  58.578  68.730  1.00 51.27           N  
ANISOU  645  N   SER A  87     9998   5075   4405    -26   -357    107       N  
ATOM    646  CA  SER A  87      -4.046  60.007  68.442  1.00 49.21           C  
ANISOU  646  CA  SER A  87     9758   4842   4095    -25   -428     55       C  
ATOM    647  C   SER A  87      -5.317  60.717  67.993  1.00 49.01           C  
ANISOU  647  C   SER A  87     9710   4823   4086    -34   -435     37       C  
ATOM    648  O   SER A  87      -5.605  61.844  68.411  1.00 50.89           O  
ANISOU  648  O   SER A  87     9973   5080   4280      7   -456     22       O  
ATOM    649  CB  SER A  87      -2.971  60.182  67.382  1.00 47.87           C  
ANISOU  649  CB  SER A  87     9598   4655   3933    -75   -478     12       C  
ATOM    650  OG  SER A  87      -1.707  59.745  67.860  1.00 47.94           O  
ANISOU  650  OG  SER A  87     9617   4678   3919    -53   -482     25       O  
ATOM    651  N   VAL A  88      -6.099  60.070  67.151  1.00 48.93           N  
ANISOU  651  N   VAL A  88     9649   4801   4138    -85   -416     35       N  
ATOM    652  CA  VAL A  88      -7.380  60.647  66.751  1.00 49.10           C  
ANISOU  652  CA  VAL A  88     9626   4855   4173    -83   -426     27       C  
ATOM    653  C   VAL A  88      -8.256  60.783  67.986  1.00 47.98           C  
ANISOU  653  C   VAL A  88     9469   4742   4017    -19   -372     63       C  
ATOM    654  O   VAL A  88      -8.956  61.766  68.180  1.00 48.06           O  
ANISOU  654  O   VAL A  88     9473   4781   4004     31   -383     58       O  
ATOM    655  CB  VAL A  88      -8.093  59.759  65.702  1.00 50.94           C  
ANISOU  655  CB  VAL A  88     9790   5093   4471   -162   -415     10       C  
ATOM    656  CG1 VAL A  88      -9.513  60.258  65.399  1.00 52.45           C  
ANISOU  656  CG1 VAL A  88     9909   5346   4673   -152   -426      8       C  
ATOM    657  CG2 VAL A  88      -7.298  59.705  64.409  1.00 50.31           C  
ANISOU  657  CG2 VAL A  88     9728   4995   4391   -223   -466    -32       C  
ATOM    658  N   GLY A  89      -8.259  59.746  68.804  1.00 47.88           N  
ANISOU  658  N   GLY A  89     9452   4719   4020    -18   -303    104       N  
ATOM    659  CA  GLY A  89      -9.080  59.724  70.004  1.00 47.81           C  
ANISOU  659  CA  GLY A  89     9430   4743   3993     37   -235    146       C  
ATOM    660  C   GLY A  89      -8.672  60.770  70.996  1.00 47.40           C  
ANISOU  660  C   GLY A  89     9440   4718   3850    119   -253    141       C  
ATOM    661  O   GLY A  89      -9.509  61.317  71.693  1.00 47.71           O  
ANISOU  661  O   GLY A  89     9468   4794   3863    174   -218    147       O  
ATOM    662  N   LEU A  90      -7.376  61.030  71.067  1.00 47.91           N  
ANISOU  662  N   LEU A  90     9564   4770   3868    124   -303    120       N  
ATOM    663  CA  LEU A  90      -6.837  61.982  72.023  1.00 49.05           C  
ANISOU  663  CA  LEU A  90     9770   4945   3921    183   -325     96       C  
ATOM    664  C   LEU A  90      -7.281  63.406  71.642  1.00 48.49           C  
ANISOU  664  C   LEU A  90     9718   4863   3840    201   -360     41       C  
ATOM    665  O   LEU A  90      -7.643  64.204  72.521  1.00 49.22           O  
ANISOU  665  O   LEU A  90     9844   4978   3878    262   -338     21       O  
ATOM    666  CB  LEU A  90      -5.316  61.869  72.079  1.00 49.78           C  
ANISOU  666  CB  LEU A  90     9901   5039   3972    168   -375     81       C  
ATOM    667  CG  LEU A  90      -4.575  62.412  73.286  1.00 52.87           C  
ANISOU  667  CG  LEU A  90    10342   5489   4256    217   -392     61       C  
ATOM    668  CD1 LEU A  90      -5.159  61.869  74.584  1.00 54.67           C  
ANISOU  668  CD1 LEU A  90    10572   5769   4431    284   -322    122       C  
ATOM    669  CD2 LEU A  90      -3.095  62.031  73.200  1.00 53.54           C  
ANISOU  669  CD2 LEU A  90    10430   5594   4317    197   -443     57       C  
ATOM    670  N   ALA A  91      -7.299  63.696  70.347  1.00 46.06           N  
ANISOU  670  N   ALA A  91     9394   4521   3584    155   -406     19       N  
ATOM    671  CA  ALA A  91      -7.792  64.977  69.873  1.00 46.70           C  
ANISOU  671  CA  ALA A  91     9495   4581   3665    184   -432    -11       C  
ATOM    672  C   ALA A  91      -9.266  65.105  70.175  1.00 47.92           C  
ANISOU  672  C   ALA A  91     9595   4769   3841    243   -382     14       C  
ATOM    673  O   ALA A  91      -9.734  66.178  70.602  1.00 50.32           O  
ANISOU  673  O   ALA A  91     9932   5066   4119    314   -367     -5       O  
ATOM    674  CB  ALA A  91      -7.537  65.158  68.393  1.00 46.03           C  
ANISOU  674  CB  ALA A  91     9403   4467   3620    129   -487    -21       C  
ATOM    675  N   LEU A  92     -10.007  64.026  69.981  1.00 47.46           N  
ANISOU  675  N   LEU A  92     9453   4746   3834    214   -347     52       N  
ATOM    676  CA  LEU A  92     -11.429  64.076  70.244  1.00 48.64           C  
ANISOU  676  CA  LEU A  92     9526   4943   4009    260   -296     76       C  
ATOM    677  C   LEU A  92     -11.795  64.283  71.715  1.00 50.18           C  
ANISOU  677  C   LEU A  92     9745   5166   4154    335   -222     87       C  
ATOM    678  O   LEU A  92     -12.837  64.874  71.971  1.00 51.59           O  
ANISOU  678  O   LEU A  92     9885   5378   4338    403   -185     90       O  
ATOM    679  CB  LEU A  92     -12.125  62.846  69.688  1.00 48.93           C  
ANISOU  679  CB  LEU A  92     9460   5012   4116    188   -271    102       C  
ATOM    680  CG  LEU A  92     -12.265  62.786  68.172  1.00 48.99           C  
ANISOU  680  CG  LEU A  92     9418   5028   4167    127   -338     83       C  
ATOM    681  CD1 LEU A  92     -12.975  61.491  67.832  1.00 50.04           C  
ANISOU  681  CD1 LEU A  92     9450   5194   4367     41   -299     90       C  
ATOM    682  CD2 LEU A  92     -13.059  63.951  67.599  1.00 49.21           C  
ANISOU  682  CD2 LEU A  92     9413   5094   4190    195   -379     80       C  
ATOM    683  N   VAL A  93     -10.988  63.802  72.674  1.00 51.02           N  
ANISOU  683  N   VAL A  93     9908   5270   4205    332   -197     96       N  
ATOM    684  CA  VAL A  93     -11.319  64.071  74.089  1.00 52.79           C  
ANISOU  684  CA  VAL A  93    10163   5536   4358    408   -128    103       C  
ATOM    685  C   VAL A  93     -10.904  65.454  74.506  1.00 51.39           C  
ANISOU  685  C   VAL A  93    10073   5339   4111    465   -156     36       C  
ATOM    686  O   VAL A  93     -11.564  66.054  75.340  1.00 52.03           O  
ANISOU  686  O   VAL A  93    10169   5448   4151    541    -99     20       O  
ATOM    687  CB  VAL A  93     -10.798  63.025  75.107  1.00 55.07           C  
ANISOU  687  CB  VAL A  93    10476   5853   4596    402    -80    153       C  
ATOM    688  CG1 VAL A  93     -10.984  61.601  74.585  1.00 54.84           C  
ANISOU  688  CG1 VAL A  93    10381   5804   4649    330    -48    214       C  
ATOM    689  CG2 VAL A  93      -9.351  63.256  75.467  1.00 55.92           C  
ANISOU  689  CG2 VAL A  93    10668   5955   4624    400   -141    122       C  
ATOM    690  N   LYS A  94      -9.851  65.974  73.882  1.00 50.47           N  
ANISOU  690  N   LYS A  94    10015   5172   3989    425   -234     -8       N  
ATOM    691  CA  LYS A  94      -9.331  67.302  74.182  1.00 50.22           C  
ANISOU  691  CA  LYS A  94    10076   5103   3902    455   -259    -85       C  
ATOM    692  C   LYS A  94     -10.033  68.450  73.466  1.00 51.38           C  
ANISOU  692  C   LYS A  94    10232   5191   4096    500   -262   -107       C  
ATOM    693  O   LYS A  94     -10.180  69.523  74.061  1.00 57.46           O  
ANISOU  693  O   LYS A  94    11072   5930   4828    560   -232   -161       O  
ATOM    694  CB  LYS A  94      -7.816  67.362  73.940  1.00 49.59           C  
ANISOU  694  CB  LYS A  94    10051   4999   3792    383   -331   -125       C  
ATOM    695  CG  LYS A  94      -7.051  66.701  75.083  1.00 49.93           C  
ANISOU  695  CG  LYS A  94    10111   5113   3747    382   -325   -121       C  
ATOM    696  CD  LYS A  94      -5.680  66.186  74.719  1.00 51.09           C  
ANISOU  696  CD  LYS A  94    10258   5267   3887    313   -391   -123       C  
ATOM    697  CE  LYS A  94      -4.483  67.051  75.036  1.00 52.62           C  
ANISOU  697  CE  LYS A  94    10514   5467   4012    279   -446   -212       C  
ATOM    698  NZ  LYS A  94      -4.602  67.967  76.192  1.00 57.78           N  
ANISOU  698  NZ  LYS A  94    11232   6150   4570    320   -423   -286       N  
ATOM    699  N   LEU A  95     -10.484  68.277  72.224  1.00 49.55           N  
ANISOU  699  N   LEU A  95     9939   4945   3942    479   -293    -67       N  
ATOM    700  CA  LEU A  95     -11.034  69.412  71.446  1.00 48.48           C  
ANISOU  700  CA  LEU A  95     9820   4757   3844    534   -306    -73       C  
ATOM    701  C   LEU A  95     -12.357  69.996  71.910  1.00 48.17           C  
ANISOU  701  C   LEU A  95     9747   4739   3815    650   -239    -61       C  
ATOM    702  O   LEU A  95     -12.505  71.193  71.900  1.00 50.31           O  
ANISOU  702  O   LEU A  95    10086   4943   4085    722   -224    -89       O  
ATOM    703  CB  LEU A  95     -11.156  69.057  69.951  1.00 49.43           C  
ANISOU  703  CB  LEU A  95     9876   4880   4023    486   -366    -29       C  
ATOM    704  CG  LEU A  95      -9.867  69.085  69.137  1.00 48.64           C  
ANISOU  704  CG  LEU A  95     9834   4726   3918    396   -431    -49       C  
ATOM    705  CD1 LEU A  95      -9.993  68.245  67.890  1.00 48.07           C  
ANISOU  705  CD1 LEU A  95     9682   4692   3889    333   -476    -11       C  
ATOM    706  CD2 LEU A  95      -9.489  70.514  68.786  1.00 49.47           C  
ANISOU  706  CD2 LEU A  95    10042   4737   4016    426   -443    -78       C  
ATOM    707  N   PRO A  96     -13.344  69.181  72.277  1.00 47.89           N  
ANISOU  707  N   PRO A  96     9604   4791   3799    672   -191    -18       N  
ATOM    708  CA  PRO A  96     -14.671  69.787  72.527  1.00 49.75           C  
ANISOU  708  CA  PRO A  96     9786   5059   4057    790   -129     -2       C  
ATOM    709  C   PRO A  96     -14.721  70.920  73.549  1.00 51.73           C  
ANISOU  709  C   PRO A  96    10137   5259   4257    888    -65    -59       C  
ATOM    710  O   PRO A  96     -15.429  71.891  73.326  1.00 53.03           O  
ANISOU  710  O   PRO A  96    10306   5392   4451    994    -38    -58       O  
ATOM    711  CB  PRO A  96     -15.507  68.621  73.012  1.00 49.82           C  
ANISOU  711  CB  PRO A  96     9672   5172   4083    771    -72     41       C  
ATOM    712  CG  PRO A  96     -14.914  67.476  72.271  1.00 49.07           C  
ANISOU  712  CG  PRO A  96     9539   5086   4016    645   -130     64       C  
ATOM    713  CD  PRO A  96     -13.430  67.724  72.224  1.00 47.34           C  
ANISOU  713  CD  PRO A  96     9445   4788   3752    592   -187     24       C  
ATOM    714  N   ASP A  97     -13.965  70.825  74.631  1.00 52.73           N  
ANISOU  714  N   ASP A  97    10347   5380   4305    859    -40   -111       N  
ATOM    715  CA  ASP A  97     -13.927  71.923  75.598  1.00 53.73           C  
ANISOU  715  CA  ASP A  97    10583   5459   4373    937     19   -189       C  
ATOM    716  C   ASP A  97     -13.233  73.166  75.010  1.00 53.85           C  
ANISOU  716  C   ASP A  97    10717   5340   4403    937    -20   -246       C  
ATOM    717  O   ASP A  97     -13.640  74.293  75.330  1.00 55.72           O  
ANISOU  717  O   ASP A  97    11025   5505   4639   1032     38   -293       O  
ATOM    718  CB  ASP A  97     -13.279  71.500  76.919  1.00 53.84           C  
ANISOU  718  CB  ASP A  97    10652   5524   4279    903     48   -235       C  
ATOM    719  CG  ASP A  97     -14.122  70.484  77.701  1.00 54.78           C  
ANISOU  719  CG  ASP A  97    10676   5759   4376    929    123   -175       C  
ATOM    720  OD1 ASP A  97     -15.389  70.528  77.694  1.00 55.95           O  
ANISOU  720  OD1 ASP A  97    10737   5948   4572   1009    191   -136       O  
ATOM    721  OD2 ASP A  97     -13.497  69.634  78.370  1.00 54.76           O  
ANISOU  721  OD2 ASP A  97    10685   5815   4305    873    120   -162       O  
ATOM    722  N   VAL A  98     -12.240  72.979  74.145  1.00 51.50           N  
ANISOU  722  N   VAL A  98    10442   5001   4122    835   -105   -240       N  
ATOM    723  CA  VAL A  98     -11.606  74.119  73.475  1.00 52.33           C  
ANISOU  723  CA  VAL A  98    10655   4974   4251    823   -133   -280       C  
ATOM    724  C   VAL A  98     -12.602  74.803  72.518  1.00 54.05           C  
ANISOU  724  C   VAL A  98    10845   5144   4546    927   -120   -216       C  
ATOM    725  O   VAL A  98     -12.709  76.028  72.472  1.00 54.92           O  
ANISOU  725  O   VAL A  98    11053   5138   4674   1000    -80   -246       O  
ATOM    726  CB  VAL A  98     -10.368  73.674  72.681  1.00 51.77           C  
ANISOU  726  CB  VAL A  98    10596   4888   4184    689   -221   -277       C  
ATOM    727  CG1 VAL A  98      -9.742  74.827  71.900  1.00 52.41           C  
ANISOU  727  CG1 VAL A  98    10783   4831   4296    666   -240   -306       C  
ATOM    728  CG2 VAL A  98      -9.350  73.044  73.615  1.00 51.31           C  
ANISOU  728  CG2 VAL A  98    10557   4888   4048    604   -240   -333       C  
ATOM    729  N   LEU A  99     -13.351  74.002  71.773  1.00 54.39           N  
ANISOU  729  N   LEU A  99    10751   5279   4632    938   -151   -127       N  
ATOM    730  CA  LEU A  99     -14.351  74.524  70.857  1.00 56.15           C  
ANISOU  730  CA  LEU A  99    10919   5499   4915   1044   -153    -55       C  
ATOM    731  C   LEU A  99     -15.532  75.224  71.549  1.00 58.98           C  
ANISOU  731  C   LEU A  99    11261   5861   5287   1205    -60    -55       C  
ATOM    732  O   LEU A  99     -16.044  76.221  71.022  1.00 60.74           O  
ANISOU  732  O   LEU A  99    11513   6015   5549   1322    -42    -20       O  
ATOM    733  CB  LEU A  99     -14.826  73.417  69.915  1.00 55.73           C  
ANISOU  733  CB  LEU A  99    10711   5567   4893    995   -217     21       C  
ATOM    734  CG  LEU A  99     -13.700  72.915  69.000  1.00 54.90           C  
ANISOU  734  CG  LEU A  99    10635   5441   4783    858   -302     23       C  
ATOM    735  CD1 LEU A  99     -14.110  71.690  68.212  1.00 54.93           C  
ANISOU  735  CD1 LEU A  99    10494   5564   4810    792   -354     74       C  
ATOM    736  CD2 LEU A  99     -13.241  74.005  68.034  1.00 55.27           C  
ANISOU  736  CD2 LEU A  99    10780   5376   4842    880   -333     41       C  
ATOM    737  N   ASN A 100     -15.980  74.714  72.695  1.00 58.83           N  
ANISOU  737  N   ASN A 100    11194   5922   5234   1222      3    -84       N  
ATOM    738  CA  ASN A 100     -16.991  75.421  73.453  1.00 60.87           C  
ANISOU  738  CA  ASN A 100    11449   6180   5497   1374    105    -99       C  
ATOM    739  C   ASN A 100     -16.481  76.779  73.937  1.00 61.98           C  
ANISOU  739  C   ASN A 100    11773   6157   5617   1430    159   -185       C  
ATOM    740  O   ASN A 100     -17.261  77.737  74.025  1.00 64.62           O  
ANISOU  740  O   ASN A 100    12134   6433   5986   1582    232   -182       O  
ATOM    741  CB  ASN A 100     -17.448  74.606  74.668  1.00 62.79           C  
ANISOU  741  CB  ASN A 100    11623   6540   5693   1368    174   -119       C  
ATOM    742  CG  ASN A 100     -18.580  73.647  74.361  1.00 63.45           C  
ANISOU  742  CG  ASN A 100    11509   6774   5824   1383    179    -35       C  
ATOM    743  OD1 ASN A 100     -19.304  73.813  73.386  1.00 64.26           O  
ANISOU  743  OD1 ASN A 100    11514   6910   5991   1442    146     28       O  
ATOM    744  ND2 ASN A 100     -18.756  72.644  75.230  1.00 63.43           N  
ANISOU  744  ND2 ASN A 100    11444   6870   5785   1328    227    -35       N  
ATOM    745  N   ARG A 101     -15.196  76.852  74.304  1.00 60.63           N  
ANISOU  745  N   ARG A 101    11726   5917   5392   1309    131   -268       N  
ATOM    746  CA  ARG A 101     -14.565  78.112  74.755  1.00 60.50           C  
ANISOU  746  CA  ARG A 101    11892   5739   5356   1323    180   -373       C  
ATOM    747  C   ARG A 101     -14.414  79.108  73.586  1.00 61.86           C  
ANISOU  747  C   ARG A 101    12141   5758   5602   1359    161   -333       C  
ATOM    748  O   ARG A 101     -14.854  80.234  73.679  1.00 61.08           O  
ANISOU  748  O   ARG A 101    12132   5537   5539   1480    240   -352       O  
ATOM    749  CB  ARG A 101     -13.200  77.838  75.396  1.00 59.00           C  
ANISOU  749  CB  ARG A 101    11786   5545   5084   1166    141   -473       C  
ATOM    750  CG  ARG A 101     -12.391  79.075  75.751  1.00 60.43           C  
ANISOU  750  CG  ARG A 101    12148   5565   5248   1136    177   -598       C  
ATOM    751  CD  ARG A 101     -11.303  78.804  76.770  1.00 60.26           C  
ANISOU  751  CD  ARG A 101    12183   5592   5120   1009    155   -718       C  
ATOM    752  NE  ARG A 101     -10.386  77.732  76.365  1.00 59.82           N  
ANISOU  752  NE  ARG A 101    12055   5631   5042    873     48   -676       N  
ATOM    753  CZ  ARG A 101      -9.428  77.843  75.437  1.00 60.46           C  
ANISOU  753  CZ  ARG A 101    12164   5647   5162    766    -22   -668       C  
ATOM    754  NH1 ARG A 101      -9.257  78.965  74.747  1.00 61.81           N  
ANISOU  754  NH1 ARG A 101    12436   5650   5397    771      0   -687       N  
ATOM    755  NH2 ARG A 101      -8.634  76.809  75.172  1.00 59.94           N  
ANISOU  755  NH2 ARG A 101    12024   5678   5071    658   -107   -635       N  
ATOM    756  N   LEU A 102     -13.826  78.658  72.478  1.00 62.47           N  
ANISOU  756  N   LEU A 102    12185   5846   5703   1262     65   -269       N  
ATOM    757  CA  LEU A 102     -13.600  79.527  71.326  1.00 64.51           C  
ANISOU  757  CA  LEU A 102    12520   5971   6019   1286     46   -216       C  
ATOM    758  C   LEU A 102     -14.866  79.965  70.557  1.00 66.97           C  
ANISOU  758  C   LEU A 102    12763   6290   6391   1466     66    -98       C  
ATOM    759  O   LEU A 102     -14.822  80.975  69.865  1.00 68.31           O  
ANISOU  759  O   LEU A 102    13031   6319   6604   1534     87    -57       O  
ATOM    760  CB  LEU A 102     -12.621  78.870  70.352  1.00 63.30           C  
ANISOU  760  CB  LEU A 102    12343   5846   5860   1133    -57   -180       C  
ATOM    761  CG  LEU A 102     -11.229  78.577  70.889  1.00 63.02           C  
ANISOU  761  CG  LEU A 102    12376   5794   5772    962    -87   -284       C  
ATOM    762  CD1 LEU A 102     -10.418  77.895  69.806  1.00 61.98           C  
ANISOU  762  CD1 LEU A 102    12201   5701   5646    838   -180   -233       C  
ATOM    763  CD2 LEU A 102     -10.531  79.835  71.341  1.00 64.60           C  
ANISOU  763  CD2 LEU A 102    12754   5818   5973    938    -25   -389       C  
ATOM    764  N   LYS A 103     -15.945  79.189  70.657  1.00 68.68           N  
ANISOU  764  N   LYS A 103    12809   6674   6612   1536     60    -40       N  
ATOM    765  CA  LYS A 103     -17.231  79.478  70.006  1.00 71.83           C  
ANISOU  765  CA  LYS A 103    13101   7129   7060   1710     71     69       C  
ATOM    766  C   LYS A 103     -17.132  79.932  68.538  1.00 71.20           C  
ANISOU  766  C   LYS A 103    13040   7000   7012   1741      5    175       C  
ATOM    767  O   LYS A 103     -17.641  81.011  68.180  1.00 74.16           O  
ANISOU  767  O   LYS A 103    13474   7275   7426   1904     54    234       O  
ATOM    768  CB  LYS A 103     -18.062  80.447  70.888  1.00 75.62           C  
ANISOU  768  CB  LYS A 103    13632   7537   7563   1892    197     36       C  
ATOM    769  CG  LYS A 103     -19.179  79.730  71.647  1.00 79.30           C  
ANISOU  769  CG  LYS A 103    13928   8181   8021   1961    240     40       C  
ATOM    770  CD  LYS A 103     -19.547  80.334  73.006  1.00 84.26           C  
ANISOU  770  CD  LYS A 103    14630   8753   8631   2059    374    -53       C  
ATOM    771  CE  LYS A 103     -20.231  79.221  73.907  1.00 87.56           C  
ANISOU  771  CE  LYS A 103    14886   9368   9012   2036    405    -67       C  
ATOM    772  NZ  LYS A 103     -20.436  79.522  75.365  1.00 88.80           N  
ANISOU  772  NZ  LYS A 103    15110   9510   9120   2090    530   -170       N  
ATOM    773  N   PRO A 104     -16.492  79.106  67.682  1.00 68.39           N  
ANISOU  773  N   PRO A 104    12634   6715   6633   1595    -98    205       N  
ATOM    774  CA  PRO A 104     -16.337  79.434  66.266  1.00 68.61           C  
ANISOU  774  CA  PRO A 104    12677   6719   6670   1610   -164    305       C  
ATOM    775  C   PRO A 104     -17.619  79.289  65.444  1.00 69.51           C  
ANISOU  775  C   PRO A 104    12626   6987   6798   1751   -207    426       C  
ATOM    776  O   PRO A 104     -18.427  78.424  65.719  1.00 70.43           O  
ANISOU  776  O   PRO A 104    12569   7277   6914   1755   -225    426       O  
ATOM    777  CB  PRO A 104     -15.322  78.407  65.782  1.00 66.32           C  
ANISOU  777  CB  PRO A 104    12363   6489   6344   1405   -252    279       C  
ATOM    778  CG  PRO A 104     -15.598  77.227  66.610  1.00 65.67           C  
ANISOU  778  CG  PRO A 104    12156   6547   6246   1336   -258    223       C  
ATOM    779  CD  PRO A 104     -15.940  77.776  67.970  1.00 66.99           C  
ANISOU  779  CD  PRO A 104    12380   6653   6419   1421   -154    154       C  
ATOM    780  N   ASP A 105     -17.783  80.140  64.434  1.00 70.28           N  
ANISOU  780  N   ASP A 105    12774   7024   6904   1862   -221    531       N  
ATOM    781  CA  ASP A 105     -18.879  80.010  63.489  1.00 70.78           C  
ANISOU  781  CA  ASP A 105    12676   7255   6963   1990   -285    653       C  
ATOM    782  C   ASP A 105     -18.556  78.980  62.437  1.00 69.35           C  
ANISOU  782  C   ASP A 105    12394   7224   6732   1843   -408    679       C  
ATOM    783  O   ASP A 105     -19.468  78.333  61.915  1.00 71.21           O  
ANISOU  783  O   ASP A 105    12437   7667   6950   1876   -477    729       O  
ATOM    784  CB  ASP A 105     -19.173  81.342  62.818  1.00 72.28           C  
ANISOU  784  CB  ASP A 105    12967   7324   7170   2184   -250    770       C  
ATOM    785  CG  ASP A 105     -19.693  82.345  63.789  1.00 73.94           C  
ANISOU  785  CG  ASP A 105    13259   7396   7437   2357   -121    749       C  
ATOM    786  OD1 ASP A 105     -20.689  82.062  64.497  1.00 72.60           O  
ANISOU  786  OD1 ASP A 105    12949   7346   7287   2450    -88    729       O  
ATOM    787  OD2 ASP A 105     -19.106  83.453  63.860  1.00 75.00           O  
ANISOU  787  OD2 ASP A 105    13604   7292   7601   2400    -41    748       O  
ATOM    788  N   ILE A 106     -17.275  78.867  62.095  1.00 66.43           N  
ANISOU  788  N   ILE A 106    12150   6753   6337   1684   -432    641       N  
ATOM    789  CA  ILE A 106     -16.835  77.900  61.119  1.00 65.39           C  
ANISOU  789  CA  ILE A 106    11945   6744   6156   1537   -535    650       C  
ATOM    790  C   ILE A 106     -15.429  77.464  61.439  1.00 64.23           C  
ANISOU  790  C   ILE A 106    11907   6497   6000   1339   -529    552       C  
ATOM    791  O   ILE A 106     -14.622  78.245  61.944  1.00 61.80           O  
ANISOU  791  O   ILE A 106    11765   6004   5711   1321   -462    510       O  
ATOM    792  CB  ILE A 106     -16.929  78.463  59.662  1.00 66.92           C  
ANISOU  792  CB  ILE A 106    12159   6960   6305   1615   -594    780       C  
ATOM    793  CG1 ILE A 106     -16.613  77.382  58.631  1.00 66.12           C  
ANISOU  793  CG1 ILE A 106    11963   7018   6141   1468   -701    778       C  
ATOM    794  CG2 ILE A 106     -15.998  79.650  59.431  1.00 67.20           C  
ANISOU  794  CG2 ILE A 106    12421   6763   6349   1633   -533    814       C  
ATOM    795  CD1 ILE A 106     -17.261  77.634  57.292  1.00 68.37           C  
ANISOU  795  CD1 ILE A 106    12176   7437   6362   1573   -780    906       C  
HETATM  796  N   MSE A 107     -15.136  76.215  61.104  1.00 65.95           N  
ANISOU  796  N   MSE A 107    12025   6841   6190   1191   -597    513       N  
HETATM  797  CA  MSE A 107     -13.798  75.688  61.233  1.00 68.74           C  
ANISOU  797  CA  MSE A 107    12458   7128   6532   1011   -603    434       C  
HETATM  798  C   MSE A 107     -13.228  75.191  59.943  1.00 65.38           C  
ANISOU  798  C   MSE A 107    12018   6763   6060    911   -679    464       C  
HETATM  799  O   MSE A 107     -13.879  74.451  59.205  1.00 65.03           O  
ANISOU  799  O   MSE A 107    11838   6881   5988    903   -746    493       O  
HETATM  800  CB  MSE A 107     -13.847  74.537  62.215  1.00 76.64           C  
ANISOU  800  CB  MSE A 107    13366   8205   7546    922   -594    348       C  
HETATM  801  CG  MSE A 107     -12.566  74.629  63.024  1.00 82.66           C  
ANISOU  801  CG  MSE A 107    14258   8837   8310    819   -553    263       C  
HETATM  802 SE   MSE A 107     -12.295  73.024  64.044  1.00 96.79          SE  
ANISOU  802 SE   MSE A 107    15952  10721  10100    690   -552    177      SE  
HETATM  803  CE  MSE A 107     -13.191  71.586  63.010  1.00 93.37           C  
ANISOU  803  CE  MSE A 107    15320  10487   9669    638   -625    217       C  
ATOM    804  N   ILE A 108     -11.988  75.581  59.671  1.00 62.31           N  
ANISOU  804  N   ILE A 108    11767   6249   5659    824   -664    446       N  
ATOM    805  CA  ILE A 108     -11.314  75.193  58.439  1.00 60.07           C  
ANISOU  805  CA  ILE A 108    11488   6008   5325    726   -721    471       C  
ATOM    806  C   ILE A 108     -10.500  73.940  58.712  1.00 58.40           C  
ANISOU  806  C   ILE A 108    11231   5842   5114    559   -740    374       C  
ATOM    807  O   ILE A 108      -9.629  73.906  59.600  1.00 57.00           O  
ANISOU  807  O   ILE A 108    11119   5573   4962    487   -698    300       O  
ATOM    808  CB  ILE A 108     -10.433  76.331  57.865  1.00 59.61           C  
ANISOU  808  CB  ILE A 108    11599   5794   5255    725   -684    519       C  
ATOM    809  CG1 ILE A 108     -11.305  77.578  57.653  1.00 61.59           C  
ANISOU  809  CG1 ILE A 108    11903   5981   5514    913   -652    627       C  
ATOM    810  CG2 ILE A 108      -9.797  75.904  56.545  1.00 59.44           C  
ANISOU  810  CG2 ILE A 108    11575   5836   5170    630   -737    550       C  
ATOM    811  CD1 ILE A 108     -10.605  78.783  57.051  1.00 63.27           C  
ANISOU  811  CD1 ILE A 108    12292   6023   5722    932   -600    696       C  
ATOM    812  N   VAL A 109     -10.757  72.928  57.899  1.00 58.89           N  
ANISOU  812  N   VAL A 109    11184   6047   5142    501   -803    376       N  
ATOM    813  CA  VAL A 109     -10.062  71.657  57.980  1.00 58.57           C  
ANISOU  813  CA  VAL A 109    11097   6050   5105    354   -818    295       C  
ATOM    814  C   VAL A 109      -9.445  71.379  56.613  1.00 58.49           C  
ANISOU  814  C   VAL A 109    11101   6085   5037    275   -861    310       C  
ATOM    815  O   VAL A 109     -10.095  71.541  55.590  1.00 58.06           O  
ANISOU  815  O   VAL A 109    11004   6123   4930    324   -910    372       O  
ATOM    816  CB  VAL A 109     -11.050  70.543  58.321  1.00 59.16           C  
ANISOU  816  CB  VAL A 109    11019   6255   5201    345   -838    264       C  
ATOM    817  CG1 VAL A 109     -10.344  69.205  58.405  1.00 58.71           C  
ANISOU  817  CG1 VAL A 109    10928   6222   5157    203   -839    187       C  
ATOM    818  CG2 VAL A 109     -11.724  70.847  59.631  1.00 60.22           C  
ANISOU  818  CG2 VAL A 109    11137   6360   5383    432   -786    258       C  
ATOM    819  N   HIS A 110      -8.195  70.937  56.612  1.00 58.54           N  
ANISOU  819  N   HIS A 110    11158   6036   5045    157   -844    253       N  
ATOM    820  CA  HIS A 110      -7.520  70.590  55.388  1.00 58.86           C  
ANISOU  820  CA  HIS A 110    11213   6119   5032     74   -871    254       C  
ATOM    821  C   HIS A 110      -7.200  69.090  55.295  1.00 57.05           C  
ANISOU  821  C   HIS A 110    10902   5962   4810    -38   -885    171       C  
ATOM    822  O   HIS A 110      -6.761  68.460  56.272  1.00 56.15           O  
ANISOU  822  O   HIS A 110    10776   5808   4750    -83   -852    111       O  
ATOM    823  CB  HIS A 110      -6.230  71.393  55.226  1.00 60.46           C  
ANISOU  823  CB  HIS A 110    11546   6196   5228     29   -829    261       C  
ATOM    824  CG  HIS A 110      -5.394  70.923  54.079  1.00 63.13           C  
ANISOU  824  CG  HIS A 110    11895   6578   5513    -67   -841    250       C  
ATOM    825  ND1 HIS A 110      -4.494  69.875  54.194  1.00 62.62           N  
ANISOU  825  ND1 HIS A 110    11798   6527   5465   -178   -830    167       N  
ATOM    826  CD2 HIS A 110      -5.401  71.280  52.775  1.00 64.04           C  
ANISOU  826  CD2 HIS A 110    12041   6740   5550    -61   -862    314       C  
ATOM    827  CE1 HIS A 110      -3.948  69.644  53.015  1.00 64.37           C  
ANISOU  827  CE1 HIS A 110    12035   6795   5628   -239   -837    171       C  
ATOM    828  NE2 HIS A 110      -4.496  70.468  52.137  1.00 66.50           N  
ANISOU  828  NE2 HIS A 110    12342   7091   5833   -175   -859    259       N  
ATOM    829  N   GLY A 111      -7.434  68.535  54.100  1.00 55.66           N  
ANISOU  829  N   GLY A 111    10676   5896   4576    -79   -929    171       N  
ATOM    830  CA  GLY A 111      -6.750  67.341  53.654  1.00 54.11           C  
ANISOU  830  CA  GLY A 111    10450   5734   4373   -198   -926     93       C  
ATOM    831  C   GLY A 111      -7.352  66.004  54.017  1.00 53.63           C  
ANISOU  831  C   GLY A 111    10281   5738   4355   -248   -930     23       C  
ATOM    832  O   GLY A 111      -8.577  65.858  54.106  1.00 54.54           O  
ANISOU  832  O   GLY A 111    10308   5937   4475   -207   -960     33       O  
ATOM    833  N   ASP A 112      -6.456  65.045  54.246  1.00 52.60           N  
ANISOU  833  N   ASP A 112    10158   5563   4261   -335   -891    -45       N  
ATOM    834  CA  ASP A 112      -6.776  63.607  54.275  1.00 52.73           C  
ANISOU  834  CA  ASP A 112    10095   5622   4316   -410   -879   -120       C  
ATOM    835  C   ASP A 112      -6.132  62.803  55.398  1.00 49.50           C  
ANISOU  835  C   ASP A 112     9695   5125   3989   -436   -817   -157       C  
ATOM    836  O   ASP A 112      -6.211  61.605  55.430  1.00 48.39           O  
ANISOU  836  O   ASP A 112     9510   4987   3888   -498   -789   -213       O  
ATOM    837  CB  ASP A 112      -6.391  63.006  52.897  1.00 54.55           C  
ANISOU  837  CB  ASP A 112    10324   5916   4485   -495   -896   -173       C  
ATOM    838  CG  ASP A 112      -4.887  63.208  52.520  1.00 54.51           C  
ANISOU  838  CG  ASP A 112    10409   5842   4458   -529   -861   -180       C  
ATOM    839  OD1 ASP A 112      -4.073  63.614  53.373  1.00 56.75           O  
ANISOU  839  OD1 ASP A 112    10744   6032   4785   -504   -825   -159       O  
ATOM    840  OD2 ASP A 112      -4.504  62.960  51.359  1.00 55.31           O  
ANISOU  840  OD2 ASP A 112    10525   5996   4494   -584   -868   -212       O  
ATOM    841  N   ARG A 113      -5.490  63.469  56.327  1.00 50.21           N  
ANISOU  841  N   ARG A 113     9842   5134   4098   -388   -793   -125       N  
ATOM    842  CA  ARG A 113      -4.801  62.796  57.419  1.00 50.91           C  
ANISOU  842  CA  ARG A 113     9941   5157   4246   -398   -743   -147       C  
ATOM    843  C   ARG A 113      -5.733  62.486  58.608  1.00 53.41           C  
ANISOU  843  C   ARG A 113    10209   5472   4609   -353   -720   -130       C  
ATOM    844  O   ARG A 113      -6.764  63.142  58.800  1.00 51.21           O  
ANISOU  844  O   ARG A 113     9904   5230   4322   -296   -740    -97       O  
ATOM    845  CB  ARG A 113      -3.627  63.641  57.867  1.00 50.34           C  
ANISOU  845  CB  ARG A 113     9943   5021   4161   -379   -734   -131       C  
ATOM    846  CG  ARG A 113      -2.512  63.600  56.859  1.00 50.79           C  
ANISOU  846  CG  ARG A 113    10034   5075   4189   -439   -731   -156       C  
ATOM    847  CD  ARG A 113      -1.425  64.600  57.149  1.00 52.84           C  
ANISOU  847  CD  ARG A 113    10358   5283   4434   -436   -724   -143       C  
ATOM    848  NE  ARG A 113      -0.350  64.385  56.203  1.00 54.18           N  
ANISOU  848  NE  ARG A 113    10543   5459   4581   -501   -709   -169       N  
ATOM    849  CZ  ARG A 113       0.882  63.955  56.477  1.00 56.34           C  
ANISOU  849  CZ  ARG A 113    10812   5717   4878   -533   -679   -201       C  
ATOM    850  NH1 ARG A 113       1.288  63.724  57.730  1.00 55.33           N  
ANISOU  850  NH1 ARG A 113    10666   5568   4787   -505   -667   -208       N  
ATOM    851  NH2 ARG A 113       1.747  63.794  55.455  1.00 58.37           N  
ANISOU  851  NH2 ARG A 113    11077   5991   5111   -589   -659   -224       N  
ATOM    852  N   PHE A 114      -5.328  61.495  59.415  1.00 57.20           N  
ANISOU  852  N   PHE A 114    10682   5912   5139   -371   -670   -147       N  
ATOM    853  CA  PHE A 114      -6.100  61.044  60.577  1.00 58.87           C  
ANISOU  853  CA  PHE A 114    10855   6119   5392   -336   -631   -126       C  
ATOM    854  C   PHE A 114      -6.539  62.197  61.462  1.00 58.95           C  
ANISOU  854  C   PHE A 114    10885   6132   5379   -250   -641    -85       C  
ATOM    855  O   PHE A 114      -7.687  62.248  61.885  1.00 57.41           O  
ANISOU  855  O   PHE A 114    10639   5973   5200   -214   -629    -66       O  
ATOM    856  CB  PHE A 114      -5.334  59.975  61.370  1.00 61.76           C  
ANISOU  856  CB  PHE A 114    11235   6430   5800   -347   -572   -129       C  
ATOM    857  CG  PHE A 114      -4.130  60.481  62.132  1.00 65.03           C  
ANISOU  857  CG  PHE A 114    11708   6813   6188   -303   -573   -112       C  
ATOM    858  CD1 PHE A 114      -4.265  61.021  63.425  1.00 67.37           C  
ANISOU  858  CD1 PHE A 114    12021   7109   6464   -235   -564    -80       C  
ATOM    859  CD2 PHE A 114      -2.846  60.371  61.598  1.00 68.41           C  
ANISOU  859  CD2 PHE A 114    12165   7222   6605   -334   -581   -136       C  
ATOM    860  CE1 PHE A 114      -3.163  61.476  64.144  1.00 67.65           C  
ANISOU  860  CE1 PHE A 114    12102   7136   6467   -206   -573    -79       C  
ATOM    861  CE2 PHE A 114      -1.731  60.802  62.328  1.00 71.20           C  
ANISOU  861  CE2 PHE A 114    12551   7566   6934   -302   -586   -129       C  
ATOM    862  CZ  PHE A 114      -1.888  61.353  63.602  1.00 69.76           C  
ANISOU  862  CZ  PHE A 114    12385   7392   6728   -242   -587   -103       C  
ATOM    863  N   ASP A 115      -5.628  63.151  61.669  1.00 61.46           N  
ANISOU  863  N   ASP A 115    11276   6413   5663   -222   -658    -80       N  
ATOM    864  CA  ASP A 115      -5.875  64.373  62.443  1.00 61.92           C  
ANISOU  864  CA  ASP A 115    11375   6453   5697   -146   -662    -58       C  
ATOM    865  C   ASP A 115      -7.059  65.193  61.925  1.00 58.33           C  
ANISOU  865  C   ASP A 115    10898   6032   5232    -94   -686    -30       C  
ATOM    866  O   ASP A 115      -7.807  65.726  62.708  1.00 56.58           O  
ANISOU  866  O   ASP A 115    10672   5813   5013    -21   -668    -11       O  
ATOM    867  CB  ASP A 115      -4.616  65.267  62.417  1.00 68.73           C  
ANISOU  867  CB  ASP A 115    12321   7266   6528   -158   -677    -75       C  
ATOM    868  CG  ASP A 115      -3.625  64.967  63.552  1.00 74.82           C  
ANISOU  868  CG  ASP A 115    13114   8021   7294   -161   -656    -96       C  
ATOM    869  OD1 ASP A 115      -3.971  65.097  64.762  1.00 82.58           O  
ANISOU  869  OD1 ASP A 115    14101   9009   8267   -107   -633    -90       O  
ATOM    870  OD2 ASP A 115      -2.472  64.621  63.211  1.00 77.73           O  
ANISOU  870  OD2 ASP A 115    13489   8383   7660   -212   -662   -117       O  
ATOM    871  N   ALA A 116      -7.195  65.331  60.602  1.00 57.12           N  
ANISOU  871  N   ALA A 116    10732   5910   5058   -122   -727    -24       N  
ATOM    872  CA  ALA A 116      -8.311  66.099  59.998  1.00 55.19           C  
ANISOU  872  CA  ALA A 116    10458   5717   4794    -58   -760     16       C  
ATOM    873  C   ALA A 116      -9.662  65.443  60.203  1.00 53.34           C  
ANISOU  873  C   ALA A 116    10108   5568   4589    -42   -755     20       C  
ATOM    874  O   ALA A 116     -10.680  66.117  60.306  1.00 52.69           O  
ANISOU  874  O   ALA A 116     9988   5528   4504     42   -764     57       O  
ATOM    875  CB  ALA A 116      -8.081  66.287  58.517  1.00 56.37           C  
ANISOU  875  CB  ALA A 116    10618   5901   4898    -95   -807     25       C  
ATOM    876  N   LEU A 117      -9.661  64.123  60.308  1.00 52.51           N  
ANISOU  876  N   LEU A 117     9947   5484   4519   -122   -732    -18       N  
ATOM    877  CA  LEU A 117     -10.877  63.386  60.595  1.00 53.13           C  
ANISOU  877  CA  LEU A 117     9914   5635   4637   -132   -711    -23       C  
ATOM    878  C   LEU A 117     -11.359  63.629  62.027  1.00 52.48           C  
ANISOU  878  C   LEU A 117     9827   5530   4581    -57   -655      3       C  
ATOM    879  O   LEU A 117     -12.554  63.693  62.277  1.00 52.58           O  
ANISOU  879  O   LEU A 117     9751   5612   4612    -16   -643     21       O  
ATOM    880  CB  LEU A 117     -10.671  61.890  60.319  1.00 52.95           C  
ANISOU  880  CB  LEU A 117     9852   5613   4654   -249   -684    -76       C  
ATOM    881  CG  LEU A 117     -11.859  60.985  60.625  1.00 53.49           C  
ANISOU  881  CG  LEU A 117     9806   5741   4776   -291   -647    -91       C  
ATOM    882  CD1 LEU A 117     -13.067  61.331  59.779  1.00 54.30           C  
ANISOU  882  CD1 LEU A 117     9798   5975   4857   -284   -706    -93       C  
ATOM    883  CD2 LEU A 117     -11.441  59.552  60.425  1.00 53.77           C  
ANISOU  883  CD2 LEU A 117     9837   5732   4859   -407   -602   -145       C  
ATOM    884  N   ALA A 118     -10.424  63.795  62.953  1.00 52.45           N  
ANISOU  884  N   ALA A 118     9912   5443   4570    -38   -620      3       N  
ATOM    885  CA  ALA A 118     -10.762  64.178  64.329  1.00 53.13           C  
ANISOU  885  CA  ALA A 118    10015   5513   4659     39   -568     24       C  
ATOM    886  C   ALA A 118     -11.410  65.539  64.382  1.00 54.11           C  
ANISOU  886  C   ALA A 118    10153   5647   4760    144   -582     48       C  
ATOM    887  O   ALA A 118     -12.435  65.737  65.064  1.00 56.48           O  
ANISOU  887  O   ALA A 118    10399   5987   5074    214   -544     67       O  
ATOM    888  CB  ALA A 118      -9.521  64.190  65.205  1.00 52.76           C  
ANISOU  888  CB  ALA A 118    10062   5395   4588     36   -546     11       C  
ATOM    889  N   LEU A 119     -10.797  66.482  63.673  1.00 53.62           N  
ANISOU  889  N   LEU A 119    10165   5540   4666    161   -627     51       N  
ATOM    890  CA  LEU A 119     -11.313  67.846  63.620  1.00 54.37           C  
ANISOU  890  CA  LEU A 119    10295   5615   4745    269   -632     82       C  
ATOM    891  C   LEU A 119     -12.699  67.902  62.976  1.00 55.27           C  
ANISOU  891  C   LEU A 119    10295   5833   4872    326   -656    122       C  
ATOM    892  O   LEU A 119     -13.614  68.506  63.548  1.00 58.16           O  
ANISOU  892  O   LEU A 119    10630   6219   5249    432   -624    147       O  
ATOM    893  CB  LEU A 119     -10.349  68.755  62.869  1.00 54.16           C  
ANISOU  893  CB  LEU A 119    10377   5511   4689    259   -666     86       C  
ATOM    894  CG  LEU A 119      -9.083  69.027  63.670  1.00 54.15           C  
ANISOU  894  CG  LEU A 119    10482   5417   4675    222   -640     41       C  
ATOM    895  CD1 LEU A 119      -7.934  69.425  62.778  1.00 53.56           C  
ANISOU  895  CD1 LEU A 119    10484   5285   4579    157   -671     33       C  
ATOM    896  CD2 LEU A 119      -9.345  70.101  64.721  1.00 56.01           C  
ANISOU  896  CD2 LEU A 119    10785   5590   4905    314   -594     31       C  
ATOM    897  N   ALA A 120     -12.868  67.245  61.830  1.00 52.03           N  
ANISOU  897  N   ALA A 120     9812   5499   4455    256   -710    122       N  
ATOM    898  CA  ALA A 120     -14.153  67.224  61.172  1.00 52.24           C  
ANISOU  898  CA  ALA A 120     9711   5654   4483    298   -746    152       C  
ATOM    899  C   ALA A 120     -15.212  66.591  62.052  1.00 51.68           C  
ANISOU  899  C   ALA A 120     9521   5654   4460    308   -695    142       C  
ATOM    900  O   ALA A 120     -16.335  67.085  62.146  1.00 52.98           O  
ANISOU  900  O   ALA A 120     9598   5897   4633    406   -693    178       O  
ATOM    901  CB  ALA A 120     -14.056  66.491  59.839  1.00 53.81           C  
ANISOU  901  CB  ALA A 120     9855   5934   4657    197   -812    130       C  
ATOM    902  N   THR A 121     -14.851  65.508  62.720  1.00 50.15           N  
ANISOU  902  N   THR A 121     9324   5430   4298    213   -646    102       N  
ATOM    903  CA  THR A 121     -15.797  64.765  63.542  1.00 50.13           C  
ANISOU  903  CA  THR A 121     9214   5489   4344    201   -583     97       C  
ATOM    904  C   THR A 121     -16.302  65.632  64.656  1.00 50.22           C  
ANISOU  904  C   THR A 121     9242   5483   4354    330   -525    128       C  
ATOM    905  O   THR A 121     -17.518  65.709  64.905  1.00 50.14           O  
ANISOU  905  O   THR A 121     9114   5568   4370    387   -498    147       O  
ATOM    906  CB  THR A 121     -15.155  63.469  64.097  1.00 49.48           C  
ANISOU  906  CB  THR A 121     9157   5349   4293     85   -528     63       C  
ATOM    907  OG1 THR A 121     -14.796  62.617  63.002  1.00 50.10           O  
ANISOU  907  OG1 THR A 121     9213   5442   4379    -33   -571     24       O  
ATOM    908  CG2 THR A 121     -16.113  62.698  65.001  1.00 49.87           C  
ANISOU  908  CG2 THR A 121     9108   5446   4393     66   -444     69       C  
ATOM    909  N   SER A 122     -15.362  66.281  65.331  1.00 50.78           N  
ANISOU  909  N   SER A 122     9456   5442   4395    372   -503    124       N  
ATOM    910  CA  SER A 122     -15.695  67.072  66.512  1.00 52.34           C  
ANISOU  910  CA  SER A 122     9694   5610   4584    485   -437    134       C  
ATOM    911  C   SER A 122     -16.563  68.261  66.133  1.00 52.39           C  
ANISOU  911  C   SER A 122     9670   5647   4589    621   -452    170       C  
ATOM    912  O   SER A 122     -17.593  68.498  66.753  1.00 52.74           O  
ANISOU  912  O   SER A 122     9639   5748   4651    710   -398    186       O  
ATOM    913  CB  SER A 122     -14.426  67.480  67.252  1.00 53.30           C  
ANISOU  913  CB  SER A 122     9971   5614   4664    481   -419    104       C  
ATOM    914  OG  SER A 122     -13.727  68.474  66.555  1.00 56.06           O  
ANISOU  914  OG  SER A 122    10419   5890   4991    503   -470    101       O  
ATOM    915  N   ALA A 123     -16.207  68.950  65.046  1.00 52.63           N  
ANISOU  915  N   ALA A 123     9748   5650   4599    641   -522    190       N  
ATOM    916  CA  ALA A 123     -17.032  70.070  64.548  1.00 53.02           C  
ANISOU  916  CA  ALA A 123     9771   5727   4646    786   -539    244       C  
ATOM    917  C   ALA A 123     -18.446  69.659  64.133  1.00 53.21           C  
ANISOU  917  C   ALA A 123     9598   5922   4694    822   -559    277       C  
ATOM    918  O   ALA A 123     -19.416  70.294  64.548  1.00 52.39           O  
ANISOU  918  O   ALA A 123     9434   5862   4607    959   -519    309       O  
ATOM    919  CB  ALA A 123     -16.357  70.728  63.384  1.00 54.09           C  
ANISOU  919  CB  ALA A 123     9994   5809   4749    787   -608    274       C  
ATOM    920  N   ALA A 124     -18.539  68.581  63.339  1.00 52.09           N  
ANISOU  920  N   ALA A 124     9354   5879   4555    696   -615    258       N  
ATOM    921  CA  ALA A 124     -19.816  68.089  62.839  1.00 52.62           C  
ANISOU  921  CA  ALA A 124     9220   6128   4642    696   -646    271       C  
ATOM    922  C   ALA A 124     -20.750  67.671  63.938  1.00 54.08           C  
ANISOU  922  C   ALA A 124     9294   6374   4877    714   -558    261       C  
ATOM    923  O   ALA A 124     -21.914  68.032  63.941  1.00 55.59           O  
ANISOU  923  O   ALA A 124     9349   6685   5086    816   -552    294       O  
ATOM    924  CB  ALA A 124     -19.600  66.925  61.923  1.00 52.66           C  
ANISOU  924  CB  ALA A 124     9160   6205   4642    527   -707    226       C  
ATOM    925  N   LEU A 125     -20.237  66.942  64.923  1.00 54.92           N  
ANISOU  925  N   LEU A 125     9458   6401   5004    627   -483    221       N  
ATOM    926  CA  LEU A 125     -21.095  66.478  66.028  1.00 56.03           C  
ANISOU  926  CA  LEU A 125     9503   6598   5187    637   -384    218       C  
ATOM    927  C   LEU A 125     -21.474  67.581  67.009  1.00 56.80           C  
ANISOU  927  C   LEU A 125     9646   6660   5275    808   -312    244       C  
ATOM    928  O   LEU A 125     -22.443  67.445  67.728  1.00 56.35           O  
ANISOU  928  O   LEU A 125     9478   6682   5247    854   -235    253       O  
ATOM    929  CB  LEU A 125     -20.437  65.311  66.755  1.00 56.01           C  
ANISOU  929  CB  LEU A 125     9553   6525   5201    498   -322    183       C  
ATOM    930  CG  LEU A 125     -20.418  63.993  65.977  1.00 55.98           C  
ANISOU  930  CG  LEU A 125     9468   6569   5232    323   -355    147       C  
ATOM    931  CD1 LEU A 125     -19.504  63.017  66.693  1.00 54.96           C  
ANISOU  931  CD1 LEU A 125     9439   6327   5113    219   -290    129       C  
ATOM    932  CD2 LEU A 125     -21.813  63.388  65.877  1.00 57.63           C  
ANISOU  932  CD2 LEU A 125     9465   6935   5496    280   -327    141       C  
HETATM  933  N   MSE A 126     -20.726  68.681  67.010  1.00 58.44           N  
ANISOU  933  N   MSE A 126    10014   6744   5444    899   -328    252       N  
HETATM  934  CA  MSE A 126     -21.071  69.862  67.831  1.00 61.52           C  
ANISOU  934  CA  MSE A 126    10464   7082   5825   1070   -258    266       C  
HETATM  935  C   MSE A 126     -21.774  70.952  67.058  1.00 63.24           C  
ANISOU  935  C   MSE A 126    10637   7339   6049   1229   -298    322       C  
HETATM  936  O   MSE A 126     -21.922  72.064  67.564  1.00 63.11           O  
ANISOU  936  O   MSE A 126    10702   7245   6029   1380   -242    333       O  
HETATM  937  CB  MSE A 126     -19.796  70.397  68.458  1.00 60.97           C  
ANISOU  937  CB  MSE A 126    10609   6841   5714   1063   -234    227       C  
HETATM  938  CG  MSE A 126     -19.352  69.375  69.470  1.00 60.87           C  
ANISOU  938  CG  MSE A 126    10616   6820   5689    952   -177    188       C  
HETATM  939 SE   MSE A 126     -17.868  70.218  70.424  1.00 62.01          SE  
ANISOU  939 SE   MSE A 126    11008   6786   5765    965   -149    128      SE  
HETATM  940  CE  MSE A 126     -16.470  69.478  69.293  1.00 63.51           C  
ANISOU  940  CE  MSE A 126    11253   6927   5948    794   -261    120       C  
ATOM    941  N   ASN A 127     -22.259  70.646  65.847  1.00 64.87           N  
ANISOU  941  N   ASN A 127    10713   7671   6261   1204   -390    357       N  
ATOM    942  CA  ASN A 127     -22.934  71.651  65.029  1.00 68.07           C  
ANISOU  942  CA  ASN A 127    11067   8133   6661   1368   -438    429       C  
ATOM    943  C   ASN A 127     -22.126  72.896  64.706  1.00 64.64           C  
ANISOU  943  C   ASN A 127    10833   7529   6198   1466   -450    462       C  
ATOM    944  O   ASN A 127     -22.677  73.967  64.605  1.00 64.91           O  
ANISOU  944  O   ASN A 127    10875   7547   6238   1650   -430    521       O  
ATOM    945  CB  ASN A 127     -24.280  72.035  65.662  1.00 73.02           C  
ANISOU  945  CB  ASN A 127    11550   8867   7326   1526   -365    458       C  
ATOM    946  CG  ASN A 127     -25.408  71.490  64.855  1.00 78.12           C  
ANISOU  946  CG  ASN A 127    11948   9745   7986   1520   -433    490       C  
ATOM    947  OD1 ASN A 127     -25.759  72.030  63.804  1.00 78.21           O  
ANISOU  947  OD1 ASN A 127    11904   9838   7975   1614   -520    554       O  
ATOM    948  ND2 ASN A 127     -25.865  70.300  65.251  1.00 81.09           N  
ANISOU  948  ND2 ASN A 127    12181  10233   8397   1379   -403    440       N  
ATOM    949  N   ILE A 128     -20.823  72.737  64.538  1.00 61.31           N  
ANISOU  949  N   ILE A 128    10568   6979   5748   1342   -476    424       N  
ATOM    950  CA  ILE A 128     -19.980  73.808  64.061  1.00 60.08           C  
ANISOU  950  CA  ILE A 128    10592   6666   5566   1397   -492    453       C  
ATOM    951  C   ILE A 128     -19.770  73.556  62.563  1.00 60.54           C  
ANISOU  951  C   ILE A 128    10614   6800   5586   1338   -605    500       C  
ATOM    952  O   ILE A 128     -19.427  72.445  62.162  1.00 58.74           O  
ANISOU  952  O   ILE A 128    10327   6645   5344   1176   -657    458       O  
ATOM    953  CB  ILE A 128     -18.650  73.838  64.804  1.00 57.55           C  
ANISOU  953  CB  ILE A 128    10457   6174   5235   1293   -449    378       C  
ATOM    954  CG1 ILE A 128     -18.885  74.137  66.277  1.00 57.74           C  
ANISOU  954  CG1 ILE A 128    10521   6140   5276   1357   -340    327       C  
ATOM    955  CG2 ILE A 128     -17.728  74.897  64.228  1.00 57.18           C  
ANISOU  955  CG2 ILE A 128    10589   5965   5168   1319   -462    401       C  
ATOM    956  CD1 ILE A 128     -17.688  73.789  67.161  1.00 56.49           C  
ANISOU  956  CD1 ILE A 128    10492   5878   5093   1229   -308    241       C  
ATOM    957  N   ARG A 129     -19.968  74.589  61.751  1.00 61.86           N  
ANISOU  957  N   ARG A 129    10823   6947   5734   1476   -635    588       N  
ATOM    958  CA  ARG A 129     -19.745  74.503  60.308  1.00 62.82           C  
ANISOU  958  CA  ARG A 129    10928   7140   5798   1440   -738    644       C  
ATOM    959  C   ARG A 129     -18.298  74.212  59.951  1.00 60.15           C  
ANISOU  959  C   ARG A 129    10738   6685   5430   1275   -758    597       C  
ATOM    960  O   ARG A 129     -17.391  74.678  60.641  1.00 59.31           O  
ANISOU  960  O   ARG A 129    10793   6396   5343   1249   -693    557       O  
ATOM    961  CB  ARG A 129     -20.098  75.821  59.649  1.00 65.88           C  
ANISOU  961  CB  ARG A 129    11374   7489   6166   1639   -744    763       C  
ATOM    962  CG  ARG A 129     -21.552  76.214  59.739  1.00 68.98           C  
ANISOU  962  CG  ARG A 129    11608   8021   6580   1835   -739    833       C  
ATOM    963  CD  ARG A 129     -21.704  77.574  59.110  1.00 72.51           C  
ANISOU  963  CD  ARG A 129    12152   8386   7009   2041   -732    962       C  
ATOM    964  NE  ARG A 129     -23.107  77.861  58.871  1.00 76.75           N  
ANISOU  964  NE  ARG A 129    12505   9105   7548   2238   -757   1051       N  
ATOM    965  CZ  ARG A 129     -23.959  78.276  59.801  1.00 80.64           C  
ANISOU  965  CZ  ARG A 129    12938   9596   8105   2389   -672   1052       C  
ATOM    966  NH1 ARG A 129     -23.555  78.465  61.073  1.00 80.04           N  
ANISOU  966  NH1 ARG A 129    12983   9341   8088   2362   -554    963       N  
ATOM    967  NH2 ARG A 129     -25.228  78.516  59.457  1.00 83.73           N  
ANISOU  967  NH2 ARG A 129    13141  10178   8495   2573   -705   1141       N  
ATOM    968  N   ILE A 130     -18.103  73.495  58.845  1.00 58.61           N  
ANISOU  968  N   ILE A 130    10481   6603   5184   1169   -847    600       N  
ATOM    969  CA  ILE A 130     -16.796  73.016  58.408  1.00 57.47           C  
ANISOU  969  CA  ILE A 130    10442   6382   5010   1004   -868    551       C  
ATOM    970  C   ILE A 130     -16.556  73.419  56.957  1.00 58.84           C  
ANISOU  970  C   ILE A 130    10651   6598   5108   1021   -941    627       C  
ATOM    971  O   ILE A 130     -17.395  73.169  56.072  1.00 59.39           O  
ANISOU  971  O   ILE A 130    10585   6851   5127   1059  -1019    672       O  
ATOM    972  CB  ILE A 130     -16.671  71.483  58.443  1.00 57.44           C  
ANISOU  972  CB  ILE A 130    10332   6478   5014    825   -896    459       C  
ATOM    973  CG1 ILE A 130     -16.841  70.941  59.854  1.00 57.39           C  
ANISOU  973  CG1 ILE A 130    10295   6437   5073    793   -820    393       C  
ATOM    974  CG2 ILE A 130     -15.298  71.028  57.904  1.00 56.90           C  
ANISOU  974  CG2 ILE A 130    10371   6333   4914    673   -914    414       C  
ATOM    975  CD1 ILE A 130     -17.273  69.482  59.871  1.00 58.01           C  
ANISOU  975  CD1 ILE A 130    10223   6645   5172    662   -837    330       C  
ATOM    976  N   LEU A 131     -15.407  74.040  56.728  1.00 58.40           N  
ANISOU  976  N   LEU A 131    10773   6380   5036    990   -913    640       N  
ATOM    977  CA  LEU A 131     -14.905  74.284  55.402  1.00 58.82           C  
ANISOU  977  CA  LEU A 131    10883   6454   5010    968   -966    701       C  
ATOM    978  C   LEU A 131     -13.781  73.300  55.204  1.00 57.05           C  
ANISOU  978  C   LEU A 131    10688   6213   4772    768   -977    607       C  
ATOM    979  O   LEU A 131     -12.724  73.421  55.818  1.00 54.64           O  
ANISOU  979  O   LEU A 131    10501   5753   4505    693   -918    555       O  
ATOM    980  CB  LEU A 131     -14.381  75.711  55.261  1.00 59.93           C  
ANISOU  980  CB  LEU A 131    11208   6411   5151   1069   -910    788       C  
ATOM    981  CG  LEU A 131     -14.009  76.097  53.826  1.00 61.62           C  
ANISOU  981  CG  LEU A 131    11484   6655   5273   1077   -955    883       C  
ATOM    982  CD1 LEU A 131     -15.259  76.482  53.032  1.00 64.12           C  
ANISOU  982  CD1 LEU A 131    11696   7137   5528   1251  -1021   1007       C  
ATOM    983  CD2 LEU A 131     -13.029  77.254  53.799  1.00 62.57           C  
ANISOU  983  CD2 LEU A 131    11817   6546   5409   1092   -874    933       C  
ATOM    984  N   HIS A 132     -13.995  72.358  54.294  1.00 57.77           N  
ANISOU  984  N   HIS A 132    10671   6471   4806    685  -1052    584       N  
ATOM    985  CA  HIS A 132     -13.001  71.355  53.988  1.00 56.22           C  
ANISOU  985  CA  HIS A 132    10493   6270   4595    506  -1059    494       C  
ATOM    986  C   HIS A 132     -12.208  71.706  52.730  1.00 56.06           C  
ANISOU  986  C   HIS A 132    10567   6245   4487    472  -1085    540       C  
ATOM    987  O   HIS A 132     -12.777  71.797  51.652  1.00 57.84           O  
ANISOU  987  O   HIS A 132    10738   6612   4625    518  -1153    600       O  
ATOM    988  CB  HIS A 132     -13.681  70.005  53.842  1.00 56.05           C  
ANISOU  988  CB  HIS A 132    10304   6416   4573    415  -1107    416       C  
ATOM    989  CG  HIS A 132     -12.732  68.877  53.614  1.00 54.81           C  
ANISOU  989  CG  HIS A 132    10164   6243   4416    240  -1100    317       C  
ATOM    990  ND1 HIS A 132     -13.051  67.790  52.837  1.00 55.28           N  
ANISOU  990  ND1 HIS A 132    10118   6449   4437    138  -1153    252       N  
ATOM    991  CD2 HIS A 132     -11.459  68.688  54.023  1.00 54.14           C  
ANISOU  991  CD2 HIS A 132    10188   6016   4363    156  -1046    270       C  
ATOM    992  CE1 HIS A 132     -12.033  66.950  52.823  1.00 54.85           C  
ANISOU  992  CE1 HIS A 132    10113   6326   4399      5  -1120    170       C  
ATOM    993  NE2 HIS A 132     -11.044  67.481  53.514  1.00 53.79           N  
ANISOU  993  NE2 HIS A 132    10103   6026   4305     19  -1059    186       N  
ATOM    994  N   ILE A 133     -10.889  71.836  52.887  1.00 55.60           N  
ANISOU  994  N   ILE A 133    10639   6039   4447    386  -1031    508       N  
ATOM    995  CA  ILE A 133      -9.970  72.182  51.800  1.00 56.56           C  
ANISOU  995  CA  ILE A 133    10861   6134   4494    339  -1032    547       C  
ATOM    996  C   ILE A 133      -9.356  70.925  51.221  1.00 56.54           C  
ANISOU  996  C   ILE A 133    10812   6214   4457    183  -1056    452       C  
ATOM    997  O   ILE A 133      -8.916  70.060  51.964  1.00 55.04           O  
ANISOU  997  O   ILE A 133    10594   5985   4333     90  -1029    354       O  
ATOM    998  CB  ILE A 133      -8.769  73.041  52.286  1.00 57.05           C  
ANISOU  998  CB  ILE A 133    11086   5988   4602    314   -949    554       C  
ATOM    999  CG1 ILE A 133      -9.192  74.187  53.238  1.00 57.50           C  
ANISOU  999  CG1 ILE A 133    11209   5912   4724    442   -897    604       C  
ATOM   1000  CG2 ILE A 133      -8.001  73.609  51.092  1.00 57.49           C  
ANISOU 1000  CG2 ILE A 133    11246   6019   4577    289   -939    623       C  
ATOM   1001  CD1 ILE A 133     -10.157  75.191  52.632  1.00 59.15           C  
ANISOU 1001  CD1 ILE A 133    11433   6149   4890    613   -914    740       C  
ATOM   1002  N   GLU A 134      -9.289  70.859  49.892  1.00 58.88           N  
ANISOU 1002  N   GLU A 134    11108   6616   4644    163  -1101    486       N  
ATOM   1003  CA  GLU A 134      -8.609  69.803  49.132  1.00 59.93           C  
ANISOU 1003  CA  GLU A 134    11222   6821   4728     21  -1114    398       C  
ATOM   1004  C   GLU A 134      -9.416  68.510  49.121  1.00 60.21           C  
ANISOU 1004  C   GLU A 134    11106   7002   4768    -41  -1165    301       C  
ATOM   1005  O   GLU A 134      -8.877  67.417  49.212  1.00 55.67           O  
ANISOU 1005  O   GLU A 134    10508   6419   4225   -164  -1143    192       O  
ATOM   1006  CB  GLU A 134      -7.182  69.597  49.616  1.00 62.31           C  
ANISOU 1006  CB  GLU A 134    11611   6972   5090    -81  -1037    335       C  
ATOM   1007  CG  GLU A 134      -6.235  68.992  48.595  1.00 67.18           C  
ANISOU 1007  CG  GLU A 134    12256   7631   5638   -194  -1028    286       C  
ATOM   1008  CD  GLU A 134      -4.838  68.800  49.177  1.00 70.12           C  
ANISOU 1008  CD  GLU A 134    12693   7866   6081   -282   -952    226       C  
ATOM   1009  OE1 GLU A 134      -4.536  67.692  49.693  1.00 71.24           O  
ANISOU 1009  OE1 GLU A 134    12778   8004   6283   -357   -936    125       O  
ATOM   1010  OE2 GLU A 134      -4.060  69.774  49.133  1.00 70.76           O  
ANISOU 1010  OE2 GLU A 134    12878   7844   6161   -273   -904    284       O  
ATOM   1011  N   GLY A 135     -10.715  68.670  48.894  1.00 64.60           N  
ANISOU 1011  N   GLY A 135    11558   7698   5286     44  -1233    345       N  
ATOM   1012  CA  GLY A 135     -11.675  67.605  49.027  1.00 68.05           C  
ANISOU 1012  CA  GLY A 135    11838   8273   5744     -7  -1277    259       C  
ATOM   1013  C   GLY A 135     -11.781  66.542  47.942  1.00 71.49           C  
ANISOU 1013  C   GLY A 135    12198   8870   6094   -129  -1331    165       C  
ATOM   1014  O   GLY A 135     -11.905  65.347  48.256  1.00 81.07           O  
ANISOU 1014  O   GLY A 135    13336  10100   7367   -245  -1317     44       O  
ATOM   1015  N   GLY A 136     -11.764  66.895  46.676  1.00 70.74           N  
ANISOU 1015  N   GLY A 136    12123   8895   5858   -110  -1387    210       N  
ATOM   1016  CA  GLY A 136     -12.196  65.886  45.671  1.00 73.12           C  
ANISOU 1016  CA  GLY A 136    12321   9394   6064   -218  -1455    107       C  
ATOM   1017  C   GLY A 136     -11.160  64.988  45.002  1.00 70.55           C  
ANISOU 1017  C   GLY A 136    12058   9047   5700   -370  -1419     -6       C  
ATOM   1018  O   GLY A 136     -11.450  64.385  43.964  1.00 69.90           O  
ANISOU 1018  O   GLY A 136    11917   9136   5505   -445  -1477    -81       O  
ATOM   1019  N   GLU A 137      -9.984  64.859  45.605  1.00 66.96           N  
ANISOU 1019  N   GLU A 137    11710   8395   5335   -415  -1325    -30       N  
ATOM   1020  CA  GLU A 137      -8.846  64.272  44.936  1.00 66.79           C  
ANISOU 1020  CA  GLU A 137    11766   8339   5272   -523  -1278   -109       C  
ATOM   1021  C   GLU A 137      -8.724  62.780  45.221  1.00 66.12           C  
ANISOU 1021  C   GLU A 137    11626   8227   5267   -662  -1238   -272       C  
ATOM   1022  O   GLU A 137      -9.477  62.223  46.015  1.00 64.28           O  
ANISOU 1022  O   GLU A 137    11303   7988   5130   -680  -1240   -317       O  
ATOM   1023  CB  GLU A 137      -7.593  65.023  45.327  1.00 66.87           C  
ANISOU 1023  CB  GLU A 137    11914   8167   5326   -491  -1198    -38       C  
ATOM   1024  CG  GLU A 137      -7.788  66.534  45.203  1.00 69.50           C  
ANISOU 1024  CG  GLU A 137    12312   8487   5607   -352  -1219    126       C  
ATOM   1025  CD  GLU A 137      -6.507  67.337  45.042  1.00 70.75           C  
ANISOU 1025  CD  GLU A 137    12615   8511   5756   -348  -1146    193       C  
ATOM   1026  OE1 GLU A 137      -5.402  66.767  45.158  1.00 71.26           O  
ANISOU 1026  OE1 GLU A 137    12720   8490   5864   -445  -1079    114       O  
ATOM   1027  OE2 GLU A 137      -6.617  68.564  44.825  1.00 73.92           O  
ANISOU 1027  OE2 GLU A 137    13086   8886   6111   -245  -1149    329       O  
ATOM   1028  N   VAL A 138      -7.792  62.142  44.514  1.00 66.70           N  
ANISOU 1028  N   VAL A 138    11757   8287   5298   -757  -1194   -357       N  
ATOM   1029  CA  VAL A 138      -7.582  60.695  44.550  1.00 65.90           C  
ANISOU 1029  CA  VAL A 138    11623   8155   5257   -889  -1145   -518       C  
ATOM   1030  C   VAL A 138      -6.100  60.417  44.747  1.00 64.63           C  
ANISOU 1030  C   VAL A 138    11566   7835   5154   -921  -1043   -544       C  
ATOM   1031  O   VAL A 138      -5.296  60.916  43.993  1.00 64.40           O  
ANISOU 1031  O   VAL A 138    11614   7818   5035   -912  -1028   -509       O  
ATOM   1032  CB  VAL A 138      -8.032  60.073  43.211  1.00 67.06           C  
ANISOU 1032  CB  VAL A 138    11723   8490   5265   -980  -1199   -625       C  
ATOM   1033  CG1 VAL A 138      -7.818  58.558  43.190  1.00 67.12           C  
ANISOU 1033  CG1 VAL A 138    11711   8448   5341  -1124  -1134   -805       C  
ATOM   1034  CG2 VAL A 138      -9.492  60.419  42.940  1.00 67.60           C  
ANISOU 1034  CG2 VAL A 138    11670   8753   5259   -942  -1314   -593       C  
ATOM   1035  N   SER A 139      -5.743  59.608  45.737  1.00 64.54           N  
ANISOU 1035  N   SER A 139    11550   7683   5287   -955   -971   -599       N  
ATOM   1036  CA  SER A 139      -4.334  59.253  45.977  1.00 64.47           C  
ANISOU 1036  CA  SER A 139    11620   7537   5339   -975   -876   -625       C  
ATOM   1037  C   SER A 139      -4.047  57.749  46.166  1.00 65.21           C  
ANISOU 1037  C   SER A 139    11699   7554   5523  -1064   -799   -760       C  
ATOM   1038  O   SER A 139      -2.909  57.380  46.433  1.00 65.46           O  
ANISOU 1038  O   SER A 139    11782   7474   5613  -1066   -718   -777       O  
ATOM   1039  CB  SER A 139      -3.772  60.082  47.141  1.00 63.56           C  
ANISOU 1039  CB  SER A 139    11545   7295   5309   -887   -850   -516       C  
ATOM   1040  OG  SER A 139      -4.347  59.723  48.391  1.00 64.42           O  
ANISOU 1040  OG  SER A 139    11604   7335   5535   -863   -841   -511       O  
ATOM   1041  N   GLY A 140      -5.058  56.896  46.030  1.00 68.34           N  
ANISOU 1041  N   GLY A 140    12023   8007   5934  -1137   -818   -852       N  
ATOM   1042  CA  GLY A 140      -4.880  55.451  46.110  1.00 71.69           C  
ANISOU 1042  CA  GLY A 140    12445   8347   6445  -1230   -735   -986       C  
ATOM   1043  C   GLY A 140      -4.226  54.856  47.357  1.00 73.07           C  
ANISOU 1043  C   GLY A 140    12648   8334   6778  -1198   -639   -966       C  
ATOM   1044  O   GLY A 140      -3.452  53.897  47.240  1.00 78.27           O  
ANISOU 1044  O   GLY A 140    13349   8898   7492  -1239   -548  -1046       O  
ATOM   1045  N   THR A 141      -4.500  55.412  48.537  1.00 70.41           N  
ANISOU 1045  N   THR A 141    12292   7949   6512  -1118   -655   -858       N  
ATOM   1046  CA  THR A 141      -4.207  54.721  49.791  1.00 70.84           C  
ANISOU 1046  CA  THR A 141    12354   7853   6706  -1093   -575   -840       C  
ATOM   1047  C   THR A 141      -5.433  54.793  50.683  1.00 69.21           C  
ANISOU 1047  C   THR A 141    12078   7661   6555  -1079   -604   -798       C  
ATOM   1048  O   THR A 141      -6.480  55.251  50.265  1.00 69.33           O  
ANISOU 1048  O   THR A 141    12030   7803   6509  -1096   -681   -798       O  
ATOM   1049  CB  THR A 141      -2.971  55.307  50.519  1.00 73.63           C  
ANISOU 1049  CB  THR A 141    12765   8121   7088   -997   -546   -748       C  
ATOM   1050  OG1 THR A 141      -3.190  56.682  50.864  1.00 75.54           O  
ANISOU 1050  OG1 THR A 141    13004   8415   7281   -922   -619   -642       O  
ATOM   1051  CG2 THR A 141      -1.741  55.204  49.646  1.00 76.43           C  
ANISOU 1051  CG2 THR A 141    13174   8469   7396  -1013   -506   -791       C  
ATOM   1052  N   ILE A 142      -5.304  54.323  51.915  1.00 67.99           N  
ANISOU 1052  N   ILE A 142    11931   7389   6513  -1043   -538   -758       N  
ATOM   1053  CA  ILE A 142      -6.295  54.580  52.957  1.00 66.84           C  
ANISOU 1053  CA  ILE A 142    11729   7250   6416  -1005   -554   -692       C  
ATOM   1054  C   ILE A 142      -6.734  56.071  53.008  1.00 64.85           C  
ANISOU 1054  C   ILE A 142    11455   7099   6084   -922   -650   -601       C  
ATOM   1055  O   ILE A 142      -7.863  56.365  53.395  1.00 64.05           O  
ANISOU 1055  O   ILE A 142    11283   7061   5991   -906   -685   -571       O  
ATOM   1056  CB  ILE A 142      -5.759  54.096  54.336  1.00 67.33           C  
ANISOU 1056  CB  ILE A 142    11827   7171   6582   -947   -470   -632       C  
ATOM   1057  CG1 ILE A 142      -6.816  54.179  55.442  1.00 68.13           C  
ANISOU 1057  CG1 ILE A 142    11873   7277   6736   -918   -465   -573       C  
ATOM   1058  CG2 ILE A 142      -4.524  54.900  54.769  1.00 66.59           C  
ANISOU 1058  CG2 ILE A 142    11795   7042   6461   -848   -479   -555       C  
ATOM   1059  CD1 ILE A 142      -8.053  53.364  55.179  1.00 70.03           C  
ANISOU 1059  CD1 ILE A 142    12035   7552   7018  -1025   -445   -647       C  
ATOM   1060  N   ASP A 143      -5.859  56.992  52.604  1.00 62.93           N  
ANISOU 1060  N   ASP A 143    11272   6868   5771   -869   -683   -557       N  
ATOM   1061  CA  ASP A 143      -6.171  58.427  52.603  1.00 63.78           C  
ANISOU 1061  CA  ASP A 143    11381   7042   5809   -786   -757   -468       C  
ATOM   1062  C   ASP A 143      -7.407  58.806  51.755  1.00 63.67           C  
ANISOU 1062  C   ASP A 143    11294   7179   5718   -800   -838   -475       C  
ATOM   1063  O   ASP A 143      -8.151  59.708  52.127  1.00 63.93           O  
ANISOU 1063  O   ASP A 143    11295   7260   5736   -721   -885   -399       O  
ATOM   1064  CB  ASP A 143      -4.952  59.264  52.182  1.00 64.85           C  
ANISOU 1064  CB  ASP A 143    11600   7152   5885   -751   -762   -429       C  
ATOM   1065  CG  ASP A 143      -3.678  58.930  52.996  1.00 68.25           C  
ANISOU 1065  CG  ASP A 143    12083   7463   6385   -734   -692   -424       C  
ATOM   1066  OD1 ASP A 143      -3.762  58.395  54.136  1.00 69.49           O  
ANISOU 1066  OD1 ASP A 143    12225   7553   6625   -711   -651   -413       O  
ATOM   1067  OD2 ASP A 143      -2.569  59.225  52.494  1.00 72.81           O  
ANISOU 1067  OD2 ASP A 143    12712   8025   6926   -740   -678   -426       O  
ATOM   1068  N   ASP A 144      -7.638  58.112  50.643  1.00 63.83           N  
ANISOU 1068  N   ASP A 144    11284   7280   5688   -894   -855   -568       N  
ATOM   1069  CA  ASP A 144      -8.903  58.238  49.904  1.00 64.69           C  
ANISOU 1069  CA  ASP A 144    11296   7556   5725   -920   -936   -591       C  
ATOM   1070  C   ASP A 144     -10.099  58.069  50.836  1.00 64.02           C  
ANISOU 1070  C   ASP A 144    11111   7492   5719   -907   -937   -575       C  
ATOM   1071  O   ASP A 144     -10.994  58.906  50.861  1.00 64.50           O  
ANISOU 1071  O   ASP A 144    11107   7657   5740   -834  -1005   -508       O  
ATOM   1072  CB  ASP A 144      -9.025  57.180  48.800  1.00 66.31           C  
ANISOU 1072  CB  ASP A 144    11472   7835   5887  -1055   -936   -731       C  
ATOM   1073  CG  ASP A 144      -8.207  57.505  47.555  1.00 67.56           C  
ANISOU 1073  CG  ASP A 144    11701   8048   5919  -1066   -960   -749       C  
ATOM   1074  OD1 ASP A 144      -7.383  58.426  47.590  1.00 68.64           O  
ANISOU 1074  OD1 ASP A 144    11918   8139   6023   -983   -958   -656       O  
ATOM   1075  OD2 ASP A 144      -8.375  56.814  46.528  1.00 68.94           O  
ANISOU 1075  OD2 ASP A 144    11854   8314   6026  -1168   -973   -864       O  
ATOM   1076  N   SER A 145     -10.103  56.980  51.598  1.00 62.42           N  
ANISOU 1076  N   SER A 145    10897   7187   5630   -972   -855   -629       N  
ATOM   1077  CA  SER A 145     -11.185  56.712  52.542  1.00 61.61           C  
ANISOU 1077  CA  SER A 145    10703   7094   5611   -972   -834   -614       C  
ATOM   1078  C   SER A 145     -11.395  57.888  53.504  1.00 60.74           C  
ANISOU 1078  C   SER A 145    10599   6972   5506   -828   -852   -487       C  
ATOM   1079  O   SER A 145     -12.528  58.347  53.696  1.00 61.66           O  
ANISOU 1079  O   SER A 145    10618   7192   5616   -786   -894   -452       O  
ATOM   1080  CB  SER A 145     -10.929  55.424  53.335  1.00 61.62           C  
ANISOU 1080  CB  SER A 145    10725   6949   5737  -1047   -720   -665       C  
ATOM   1081  OG  SER A 145     -11.703  54.361  52.824  1.00 64.41           O  
ANISOU 1081  OG  SER A 145    10999   7352   6121  -1188   -702   -782       O  
ATOM   1082  N   ILE A 146     -10.298  58.381  54.073  1.00 57.22           N  
ANISOU 1082  N   ILE A 146    10263   6408   5071   -754   -820   -426       N  
ATOM   1083  CA  ILE A 146     -10.354  59.414  55.083  1.00 55.33           C  
ANISOU 1083  CA  ILE A 146    10048   6131   4843   -631   -820   -326       C  
ATOM   1084  C   ILE A 146     -10.826  60.684  54.429  1.00 54.73           C  
ANISOU 1084  C   ILE A 146     9957   6158   4677   -549   -905   -266       C  
ATOM   1085  O   ILE A 146     -11.710  61.360  54.951  1.00 56.09           O  
ANISOU 1085  O   ILE A 146    10078   6377   4857   -464   -924   -207       O  
ATOM   1086  CB  ILE A 146      -8.976  59.670  55.740  1.00 55.15           C  
ANISOU 1086  CB  ILE A 146    10143   5972   4838   -587   -774   -291       C  
ATOM   1087  CG1 ILE A 146      -8.324  58.391  56.235  1.00 55.78           C  
ANISOU 1087  CG1 ILE A 146    10248   5951   4994   -652   -692   -338       C  
ATOM   1088  CG2 ILE A 146      -9.112  60.619  56.915  1.00 55.78           C  
ANISOU 1088  CG2 ILE A 146    10246   6013   4933   -477   -766   -210       C  
ATOM   1089  CD1 ILE A 146      -9.246  57.482  57.037  1.00 57.82           C  
ANISOU 1089  CD1 ILE A 146    10437   6197   5335   -686   -635   -352       C  
ATOM   1090  N   ARG A 147     -10.249  61.011  53.277  1.00 53.68           N  
ANISOU 1090  N   ARG A 147     9873   6062   4459   -565   -949   -274       N  
ATOM   1091  CA  ARG A 147     -10.597  62.241  52.611  1.00 53.18           C  
ANISOU 1091  CA  ARG A 147     9816   6085   4306   -476  -1021   -198       C  
ATOM   1092  C   ARG A 147     -12.077  62.280  52.332  1.00 53.36           C  
ANISOU 1092  C   ARG A 147     9701   6267   4304   -454  -1083   -193       C  
ATOM   1093  O   ARG A 147     -12.733  63.246  52.649  1.00 53.49           O  
ANISOU 1093  O   ARG A 147     9694   6319   4311   -336  -1110   -108       O  
ATOM   1094  CB  ARG A 147      -9.825  62.425  51.318  1.00 54.75           C  
ANISOU 1094  CB  ARG A 147    10079   6317   4404   -512  -1053   -210       C  
ATOM   1095  CG  ARG A 147      -9.973  63.828  50.717  1.00 56.64           C  
ANISOU 1095  CG  ARG A 147    10359   6609   4551   -402  -1109   -102       C  
ATOM   1096  CD  ARG A 147      -8.902  64.151  49.703  1.00 57.56           C  
ANISOU 1096  CD  ARG A 147    10576   6711   4581   -430  -1108    -92       C  
ATOM   1097  NE  ARG A 147      -8.686  62.990  48.870  1.00 59.30           N  
ANISOU 1097  NE  ARG A 147    10766   6998   4765   -554  -1110   -204       N  
ATOM   1098  CZ  ARG A 147      -7.602  62.204  48.858  1.00 59.96           C  
ANISOU 1098  CZ  ARG A 147    10904   6994   4885   -641  -1045   -280       C  
ATOM   1099  NH1 ARG A 147      -6.518  62.444  49.593  1.00 56.64           N  
ANISOU 1099  NH1 ARG A 147    10565   6425   4528   -624   -981   -255       N  
ATOM   1100  NH2 ARG A 147      -7.606  61.147  48.033  1.00 63.09           N  
ANISOU 1100  NH2 ARG A 147    11266   7460   5244   -749  -1046   -391       N  
ATOM   1101  N   HIS A 148     -12.608  61.214  51.770  1.00 54.62           N  
ANISOU 1101  N   HIS A 148     9767   6523   4459   -569  -1099   -289       N  
ATOM   1102  CA  HIS A 148     -14.014  61.180  51.403  1.00 57.03           C  
ANISOU 1102  CA  HIS A 148     9920   7013   4735   -568  -1167   -299       C  
ATOM   1103  C   HIS A 148     -14.960  61.078  52.604  1.00 56.68           C  
ANISOU 1103  C   HIS A 148     9780   6962   4791   -532  -1128   -278       C  
ATOM   1104  O   HIS A 148     -16.134  61.426  52.493  1.00 59.13           O  
ANISOU 1104  O   HIS A 148     9961   7423   5081   -480  -1182   -251       O  
ATOM   1105  CB  HIS A 148     -14.276  60.037  50.438  1.00 59.28           C  
ANISOU 1105  CB  HIS A 148    10130   7407   4985   -725  -1193   -431       C  
ATOM   1106  CG  HIS A 148     -13.461  60.107  49.187  1.00 61.33           C  
ANISOU 1106  CG  HIS A 148    10471   7701   5129   -762  -1231   -460       C  
ATOM   1107  ND1 HIS A 148     -13.240  61.279  48.500  1.00 62.96           N  
ANISOU 1107  ND1 HIS A 148    10732   7968   5221   -651  -1293   -360       N  
ATOM   1108  CD2 HIS A 148     -12.825  59.142  48.490  1.00 62.25           C  
ANISOU 1108  CD2 HIS A 148    10627   7799   5225   -894  -1204   -577       C  
ATOM   1109  CE1 HIS A 148     -12.495  61.031  47.437  1.00 63.51           C  
ANISOU 1109  CE1 HIS A 148    10869   8064   5198   -719  -1305   -411       C  
ATOM   1110  NE2 HIS A 148     -12.223  59.741  47.414  1.00 62.89           N  
ANISOU 1110  NE2 HIS A 148    10781   7939   5174   -864  -1251   -548       N  
ATOM   1111  N   ALA A 149     -14.481  60.578  53.742  1.00 54.65           N  
ANISOU 1111  N   ALA A 149     9579   6547   4638   -555  -1032   -288       N  
ATOM   1112  CA  ALA A 149     -15.311  60.558  54.943  1.00 54.15           C  
ANISOU 1112  CA  ALA A 149     9441   6472   4659   -510   -983   -257       C  
ATOM   1113  C   ALA A 149     -15.399  61.987  55.496  1.00 53.49           C  
ANISOU 1113  C   ALA A 149     9402   6367   4554   -334   -996   -142       C  
ATOM   1114  O   ALA A 149     -16.476  62.422  55.904  1.00 54.64           O  
ANISOU 1114  O   ALA A 149     9446   6598   4715   -255  -1006   -100       O  
ATOM   1115  CB  ALA A 149     -14.777  59.584  55.966  1.00 52.79           C  
ANISOU 1115  CB  ALA A 149     9322   6147   4587   -581   -875   -292       C  
ATOM   1116  N   ILE A 150     -14.285  62.711  55.479  1.00 51.22           N  
ANISOU 1116  N   ILE A 150     9262   5966   4233   -277   -992    -97       N  
ATOM   1117  CA  ILE A 150     -14.296  64.117  55.856  1.00 51.85           C  
ANISOU 1117  CA  ILE A 150     9403   6008   4290   -122  -1001      0       C  
ATOM   1118  C   ILE A 150     -15.253  64.958  54.981  1.00 53.78           C  
ANISOU 1118  C   ILE A 150     9568   6405   4461    -26  -1084     61       C  
ATOM   1119  O   ILE A 150     -16.017  65.774  55.496  1.00 52.57           O  
ANISOU 1119  O   ILE A 150     9376   6275   4322    104  -1081    128       O  
ATOM   1120  CB  ILE A 150     -12.886  64.709  55.822  1.00 51.01           C  
ANISOU 1120  CB  ILE A 150     9463   5760   4158   -108   -982     22       C  
ATOM   1121  CG1 ILE A 150     -12.040  64.070  56.928  1.00 49.66           C  
ANISOU 1121  CG1 ILE A 150     9356   5453   4058   -161   -902    -16       C  
ATOM   1122  CG2 ILE A 150     -12.919  66.226  56.023  1.00 51.52           C  
ANISOU 1122  CG2 ILE A 150     9601   5777   4196     39   -989    116       C  
ATOM   1123  CD1 ILE A 150     -10.559  64.306  56.774  1.00 49.03           C  
ANISOU 1123  CD1 ILE A 150     9408   5262   3957   -188   -887    -21       C  
ATOM   1124  N   THR A 151     -15.234  64.709  53.671  1.00 55.96           N  
ANISOU 1124  N   THR A 151     9815   6792   4655    -85  -1156     35       N  
ATOM   1125  CA  THR A 151     -16.145  65.360  52.722  1.00 57.90           C  
ANISOU 1125  CA  THR A 151     9971   7215   4811      1  -1248     95       C  
ATOM   1126  C   THR A 151     -17.586  65.215  53.209  1.00 60.28           C  
ANISOU 1126  C   THR A 151    10093   7653   5157     45  -1261     97       C  
ATOM   1127  O   THR A 151     -18.349  66.198  53.208  1.00 63.54           O  
ANISOU 1127  O   THR A 151    10455   8139   5545    203  -1294    191       O  
ATOM   1128  CB  THR A 151     -15.947  64.819  51.279  1.00 58.07           C  
ANISOU 1128  CB  THR A 151     9970   7365   4728   -101  -1323     39       C  
ATOM   1129  OG1 THR A 151     -14.817  65.468  50.685  1.00 56.53           O  
ANISOU 1129  OG1 THR A 151     9935   7078   4465    -75  -1321     88       O  
ATOM   1130  CG2 THR A 151     -17.164  65.052  50.389  1.00 59.68           C  
ANISOU 1130  CG2 THR A 151    10019   7815   4842    -47  -1428     67       C  
ATOM   1131  N   LYS A 152     -17.944  64.016  53.666  1.00 59.26           N  
ANISOU 1131  N   LYS A 152     9868   7546   5101    -87  -1223      0       N  
ATOM   1132  CA  LYS A 152     -19.326  63.743  54.059  1.00 60.08           C  
ANISOU 1132  CA  LYS A 152     9781   7795   5250    -76  -1229    -12       C  
ATOM   1133  C   LYS A 152     -19.748  64.463  55.312  1.00 58.61           C  
ANISOU 1133  C   LYS A 152     9597   7537   5135     64  -1161     63       C  
ATOM   1134  O   LYS A 152     -20.920  64.770  55.498  1.00 59.13           O  
ANISOU 1134  O   LYS A 152     9513   7740   5213    148  -1179     98       O  
ATOM   1135  CB  LYS A 152     -19.553  62.237  54.187  1.00 61.04           C  
ANISOU 1135  CB  LYS A 152     9813   7940   5437   -274  -1190   -140       C  
ATOM   1136  CG  LYS A 152     -19.654  61.548  52.837  1.00 62.20           C  
ANISOU 1136  CG  LYS A 152     9891   8235   5505   -408  -1273   -233       C  
ATOM   1137  CD  LYS A 152     -21.005  61.820  52.188  1.00 64.98           C  
ANISOU 1137  CD  LYS A 152    10036   8855   5796   -367  -1375   -223       C  
ATOM   1138  CE  LYS A 152     -20.982  61.502  50.703  1.00 67.69           C  
ANISOU 1138  CE  LYS A 152    10338   9365   6012   -457  -1482   -293       C  
ATOM   1139  NZ  LYS A 152     -20.235  62.554  49.953  1.00 67.88           N  
ANISOU 1139  NZ  LYS A 152    10502   9369   5918   -327  -1539   -192       N  
ATOM   1140  N   LEU A 153     -18.788  64.717  56.185  1.00 57.41           N  
ANISOU 1140  N   LEU A 153     9608   7180   5025     89  -1082     82       N  
ATOM   1141  CA  LEU A 153     -19.049  65.448  57.427  1.00 56.47           C  
ANISOU 1141  CA  LEU A 153     9517   6975   4960    220  -1009    142       C  
ATOM   1142  C   LEU A 153     -19.154  66.926  57.149  1.00 55.80           C  
ANISOU 1142  C   LEU A 153     9491   6886   4824    407  -1045    245       C  
ATOM   1143  O   LEU A 153     -19.987  67.614  57.752  1.00 56.43           O  
ANISOU 1143  O   LEU A 153     9513   6996   4931    547  -1017    300       O  
ATOM   1144  CB  LEU A 153     -17.947  65.179  58.442  1.00 54.66           C  
ANISOU 1144  CB  LEU A 153     9441   6547   4780    173   -920    117       C  
ATOM   1145  CG  LEU A 153     -17.774  63.715  58.834  1.00 54.75           C  
ANISOU 1145  CG  LEU A 153     9417   6532   4851      7   -866     33       C  
ATOM   1146  CD1 LEU A 153     -16.518  63.545  59.672  1.00 53.89           C  
ANISOU 1146  CD1 LEU A 153     9469   6239   4767    -17   -796     24       C  
ATOM   1147  CD2 LEU A 153     -18.983  63.195  59.589  1.00 55.76           C  
ANISOU 1147  CD2 LEU A 153     9392   6747   5046     -3   -813     21       C  
ATOM   1148  N   ALA A 154     -18.325  67.383  56.220  1.00 55.19           N  
ANISOU 1148  N   ALA A 154     9528   6767   4675    410  -1095    272       N  
ATOM   1149  CA  ALA A 154     -18.139  68.800  55.957  1.00 55.87           C  
ANISOU 1149  CA  ALA A 154     9719   6790   4716    574  -1108    376       C  
ATOM   1150  C   ALA A 154     -19.300  69.451  55.208  1.00 58.22           C  
ANISOU 1150  C   ALA A 154     9892   7269   4960    716  -1182    461       C  
ATOM   1151  O   ALA A 154     -19.867  68.905  54.259  1.00 59.74           O  
ANISOU 1151  O   ALA A 154     9949   7655   5093    664  -1269    442       O  
ATOM   1152  CB  ALA A 154     -16.843  69.036  55.206  1.00 54.60           C  
ANISOU 1152  CB  ALA A 154     9720   6525   4497    518  -1125    382       C  
ATOM   1153  N   HIS A 155     -19.594  70.667  55.628  1.00 59.00           N  
ANISOU 1153  N   HIS A 155    10045   7297   5072    903  -1148    555       N  
ATOM   1154  CA  HIS A 155     -20.736  71.410  55.157  1.00 61.75           C  
ANISOU 1154  CA  HIS A 155    10279   7797   5386   1083  -1199    654       C  
ATOM   1155  C   HIS A 155     -20.392  72.235  53.916  1.00 62.85           C  
ANISOU 1155  C   HIS A 155    10506   7950   5423   1169  -1266    758       C  
ATOM   1156  O   HIS A 155     -21.265  72.497  53.111  1.00 63.22           O  
ANISOU 1156  O   HIS A 155    10429   8188   5401   1274  -1348    831       O  
ATOM   1157  CB  HIS A 155     -21.215  72.339  56.274  1.00 62.08           C  
ANISOU 1157  CB  HIS A 155    10350   7735   5502   1258  -1109    706       C  
ATOM   1158  CG  HIS A 155     -21.458  71.635  57.568  1.00 60.87           C  
ANISOU 1158  CG  HIS A 155    10137   7551   5438   1185  -1027    617       C  
ATOM   1159  ND1 HIS A 155     -20.458  71.391  58.484  1.00 59.05           N  
ANISOU 1159  ND1 HIS A 155    10053   7129   5251   1086   -947    548       N  
ATOM   1160  CD2 HIS A 155     -22.589  71.123  58.097  1.00 61.47           C  
ANISOU 1160  CD2 HIS A 155    10020   7773   5560   1196  -1011    590       C  
ATOM   1161  CE1 HIS A 155     -20.964  70.753  59.519  1.00 59.26           C  
ANISOU 1161  CE1 HIS A 155     9990   7184   5342   1047   -884    491       C  
ATOM   1162  NE2 HIS A 155     -22.258  70.589  59.313  1.00 60.81           N  
ANISOU 1162  NE2 HIS A 155     9983   7577   5546   1109   -915    515       N  
ATOM   1163  N   TYR A 156     -19.138  72.685  53.832  1.00 62.31           N  
ANISOU 1163  N   TYR A 156    10649   7680   5343   1132  -1224    769       N  
ATOM   1164  CA  TYR A 156     -18.653  73.501  52.737  1.00 63.67           C  
ANISOU 1164  CA  TYR A 156    10939   7828   5424   1201  -1261    872       C  
ATOM   1165  C   TYR A 156     -17.332  72.939  52.247  1.00 62.79           C  
ANISOU 1165  C   TYR A 156    10945   7635   5275   1014  -1261    803       C  
ATOM   1166  O   TYR A 156     -16.509  72.489  53.031  1.00 61.67           O  
ANISOU 1166  O   TYR A 156    10879   7350   5202    893  -1196    711       O  
ATOM   1167  CB  TYR A 156     -18.455  74.954  53.173  1.00 64.33           C  
ANISOU 1167  CB  TYR A 156    11186   7709   5545   1378  -1180    979       C  
ATOM   1168  CG  TYR A 156     -19.709  75.595  53.688  1.00 66.45           C  
ANISOU 1168  CG  TYR A 156    11353   8038   5857   1585  -1163   1051       C  
ATOM   1169  CD1 TYR A 156     -20.557  76.313  52.839  1.00 69.85           C  
ANISOU 1169  CD1 TYR A 156    11717   8602   6218   1779  -1223   1193       C  
ATOM   1170  CD2 TYR A 156     -20.065  75.478  55.022  1.00 66.41           C  
ANISOU 1170  CD2 TYR A 156    11312   7965   5955   1599  -1084    982       C  
ATOM   1171  CE1 TYR A 156     -21.729  76.897  53.312  1.00 71.84           C  
ANISOU 1171  CE1 TYR A 156    11862   8918   6515   1986  -1204   1262       C  
ATOM   1172  CE2 TYR A 156     -21.219  76.049  55.507  1.00 68.07           C  
ANISOU 1172  CE2 TYR A 156    11422   8234   6206   1792  -1058   1043       C  
ATOM   1173  CZ  TYR A 156     -22.045  76.756  54.658  1.00 71.39           C  
ANISOU 1173  CZ  TYR A 156    11770   8784   6568   1987  -1116   1181       C  
ATOM   1174  OH  TYR A 156     -23.181  77.330  55.165  1.00 74.00           O  
ANISOU 1174  OH  TYR A 156    11995   9174   6947   2194  -1083   1243       O  
ATOM   1175  N   HIS A 157     -17.138  73.007  50.936  1.00 64.18           N  
ANISOU 1175  N   HIS A 157    11135   7913   5335   1005  -1333    856       N  
ATOM   1176  CA  HIS A 157     -16.045  72.341  50.271  1.00 63.65           C  
ANISOU 1176  CA  HIS A 157    11144   7826   5215    830  -1344    786       C  
ATOM   1177  C   HIS A 157     -15.298  73.303  49.383  1.00 65.11           C  
ANISOU 1177  C   HIS A 157    11492   7930   5317    888  -1336    898       C  
ATOM   1178  O   HIS A 157     -15.911  73.999  48.562  1.00 67.41           O  
ANISOU 1178  O   HIS A 157    11764   8330   5517   1031  -1389   1025       O  
ATOM   1179  CB  HIS A 157     -16.604  71.222  49.395  1.00 64.69           C  
ANISOU 1179  CB  HIS A 157    11107   8207   5264    725  -1445    713       C  
ATOM   1180  CG  HIS A 157     -17.347  70.179  50.159  1.00 63.35           C  
ANISOU 1180  CG  HIS A 157    10771   8121   5177    643  -1447    599       C  
ATOM   1181  ND1 HIS A 157     -18.723  70.142  50.218  1.00 63.91           N  
ANISOU 1181  ND1 HIS A 157    10653   8382   5248    729  -1502    621       N  
ATOM   1182  CD2 HIS A 157     -16.902  69.114  50.864  1.00 60.99           C  
ANISOU 1182  CD2 HIS A 157    10463   7746   4961    480  -1395    468       C  
ATOM   1183  CE1 HIS A 157     -19.096  69.102  50.934  1.00 63.11           C  
ANISOU 1183  CE1 HIS A 157    10436   8311   5230    610  -1478    504       C  
ATOM   1184  NE2 HIS A 157     -18.012  68.466  51.341  1.00 61.95           N  
ANISOU 1184  NE2 HIS A 157    10404   7999   5135    463  -1412    415       N  
ATOM   1185  N   VAL A 158     -13.978  73.267  49.480  1.00 64.45           N  
ANISOU 1185  N   VAL A 158    11558   7675   5255    770  -1271    852       N  
ATOM   1186  CA  VAL A 158     -13.115  74.038  48.616  1.00 66.79           C  
ANISOU 1186  CA  VAL A 158    12012   7889   5476    784  -1248    942       C  
ATOM   1187  C   VAL A 158     -12.182  73.065  47.876  1.00 69.10           C  
ANISOU 1187  C   VAL A 158    12315   8233   5704    595  -1266    846       C  
ATOM   1188  O   VAL A 158     -11.259  72.525  48.478  1.00 69.62           O  
ANISOU 1188  O   VAL A 158    12427   8180   5844    463  -1209    741       O  
ATOM   1189  CB  VAL A 158     -12.305  75.036  49.442  1.00 65.04           C  
ANISOU 1189  CB  VAL A 158    11966   7396   5348    814  -1136    973       C  
ATOM   1190  CG1 VAL A 158     -11.338  75.838  48.569  1.00 65.25           C  
ANISOU 1190  CG1 VAL A 158    12163   7319   5309    806  -1094   1064       C  
ATOM   1191  CG2 VAL A 158     -13.252  75.957  50.177  1.00 65.76           C  
ANISOU 1191  CG2 VAL A 158    12051   7429   5504   1003  -1108   1053       C  
ATOM   1192  N   CYS A 159     -12.401  72.867  46.574  1.00 71.55           N  
ANISOU 1192  N   CYS A 159    12586   8726   5872    593  -1341    885       N  
ATOM   1193  CA  CYS A 159     -11.535  71.985  45.789  1.00 72.36           C  
ANISOU 1193  CA  CYS A 159    12706   8884   5903    424  -1350    792       C  
ATOM   1194  C   CYS A 159     -10.602  72.766  44.839  1.00 73.95           C  
ANISOU 1194  C   CYS A 159    13068   9021   6007    433  -1311    893       C  
ATOM   1195  O   CYS A 159     -10.768  73.964  44.606  1.00 71.29           O  
ANISOU 1195  O   CYS A 159    12820   8626   5640    577  -1291   1049       O  
ATOM   1196  CB  CYS A 159     -12.366  70.954  45.034  1.00 73.82           C  
ANISOU 1196  CB  CYS A 159    12724   9332   5992    369  -1455    717       C  
ATOM   1197  SG  CYS A 159     -13.667  71.641  43.991  1.00 77.15           S  
ANISOU 1197  SG  CYS A 159    13054  10004   6256    549  -1572    865       S  
ATOM   1198  N   CYS A 160      -9.573  72.063  44.372  1.00 75.49           N  
ANISOU 1198  N   CYS A 160    13304   9209   6169    276  -1283    801       N  
ATOM   1199  CA  CYS A 160      -8.431  72.660  43.688  1.00 75.56           C  
ANISOU 1199  CA  CYS A 160    13468   9122   6117    243  -1215    866       C  
ATOM   1200  C   CYS A 160      -8.409  72.450  42.185  1.00 78.70           C  
ANISOU 1200  C   CYS A 160    13865   9710   6325    223  -1267    901       C  
ATOM   1201  O   CYS A 160      -7.594  73.067  41.509  1.00 83.71           O  
ANISOU 1201  O   CYS A 160    14630  10285   6891    216  -1208    984       O  
ATOM   1202  CB  CYS A 160      -7.149  72.095  44.288  1.00 74.91           C  
ANISOU 1202  CB  CYS A 160    13435   8888   6136     86  -1131    742       C  
ATOM   1203  SG  CYS A 160      -7.007  72.389  46.078  1.00 76.19           S  
ANISOU 1203  SG  CYS A 160    13614   8833   6500    102  -1066    699       S  
ATOM   1204  N   THR A 161      -9.261  71.558  41.663  1.00 78.22           N  
ANISOU 1204  N   THR A 161    13660   9881   6178    200  -1369    828       N  
ATOM   1205  CA  THR A 161      -9.325  71.240  40.235  1.00 77.14           C  
ANISOU 1205  CA  THR A 161    13507   9960   5842    171  -1431    834       C  
ATOM   1206  C   THR A 161     -10.770  70.993  39.802  1.00 80.20           C  
ANISOU 1206  C   THR A 161    13733  10609   6129    252  -1567    846       C  
ATOM   1207  O   THR A 161     -11.638  70.793  40.630  1.00 79.91           O  
ANISOU 1207  O   THR A 161    13580  10587   6194    291  -1604    811       O  
ATOM   1208  CB  THR A 161      -8.540  69.958  39.891  1.00 75.80           C  
ANISOU 1208  CB  THR A 161    13318   9827   5655    -22  -1409    649       C  
ATOM   1209  OG1 THR A 161      -9.270  68.806  40.328  1.00 75.97           O  
ANISOU 1209  OG1 THR A 161    13184   9946   5735    -97  -1468    494       O  
ATOM   1210  CG2 THR A 161      -7.136  69.950  40.507  1.00 73.15           C  
ANISOU 1210  CG2 THR A 161    13095   9252   5444   -117  -1282    603       C  
ATOM   1211  N   ARG A 162     -11.010  70.979  38.495  1.00 84.76           N  
ANISOU 1211  N   ARG A 162    14296  11408   6500    270  -1639    889       N  
ATOM   1212  CA  ARG A 162     -12.337  70.714  37.970  1.00 88.91           C  
ANISOU 1212  CA  ARG A 162    14653  12220   6906    334  -1780    890       C  
ATOM   1213  C   ARG A 162     -12.725  69.247  38.193  1.00 85.28           C  
ANISOU 1213  C   ARG A 162    14035  11875   6491    164  -1829    659       C  
ATOM   1214  O   ARG A 162     -13.874  68.928  38.480  1.00 84.75           O  
ANISOU 1214  O   ARG A 162    13799  11954   6445    193  -1915    621       O  
ATOM   1215  CB  ARG A 162     -12.392  71.070  36.485  1.00 97.25           C  
ANISOU 1215  CB  ARG A 162    15745  13496   7710    391  -1845    993       C  
ATOM   1216  CG  ARG A 162     -13.809  71.124  35.921  1.00106.13           C  
ANISOU 1216  CG  ARG A 162    16699  14933   8691    509  -2000   1047       C  
ATOM   1217  CD  ARG A 162     -14.123  72.226  34.936  1.00115.39           C  
ANISOU 1217  CD  ARG A 162    17931  16245   9667    705  -2051   1281       C  
ATOM   1218  NE  ARG A 162     -13.870  73.616  35.355  1.00122.36           N  
ANISOU 1218  NE  ARG A 162    18968  16894  10628    887  -1960   1505       N  
ATOM   1219  CZ  ARG A 162     -14.786  74.467  35.843  1.00127.11           C  
ANISOU 1219  CZ  ARG A 162    19522  17486  11288   1096  -1989   1656       C  
ATOM   1220  NH1 ARG A 162     -16.050  74.082  36.050  1.00130.38           N  
ANISOU 1220  NH1 ARG A 162    19719  18119  11699   1154  -2111   1611       N  
ATOM   1221  NH2 ARG A 162     -14.430  75.722  36.141  1.00127.59           N  
ANISOU 1221  NH2 ARG A 162    19753  17309  11416   1247  -1887   1850       N  
ATOM   1222  N   SER A 163     -11.754  68.357  38.057  1.00 81.98           N  
ANISOU 1222  N   SER A 163    13672  11384   6093    -13  -1764    507       N  
ATOM   1223  CA  SER A 163     -11.985  66.932  38.272  1.00 81.42           C  
ANISOU 1223  CA  SER A 163    13480  11376   6078   -185  -1783    285       C  
ATOM   1224  C   SER A 163     -12.312  66.594  39.746  1.00 78.21           C  
ANISOU 1224  C   SER A 163    13005  10808   5900   -200  -1742    227       C  
ATOM   1225  O   SER A 163     -13.159  65.742  40.022  1.00 79.14           O  
ANISOU 1225  O   SER A 163    12972  11035   6063   -271  -1793    106       O  
ATOM   1226  CB  SER A 163     -10.765  66.149  37.764  1.00 82.59           C  
ANISOU 1226  CB  SER A 163    13725  11457   6196   -347  -1704    154       C  
ATOM   1227  OG  SER A 163     -10.801  64.789  38.146  1.00 83.33           O  
ANISOU 1227  OG  SER A 163    13738  11537   6387   -510  -1686    -56       O  
ATOM   1228  N   ALA A 164     -11.644  67.267  40.681  1.00 74.04           N  
ANISOU 1228  N   ALA A 164    12590  10030   5512   -140  -1646    309       N  
ATOM   1229  CA  ALA A 164     -12.014  67.201  42.093  1.00 71.17           C  
ANISOU 1229  CA  ALA A 164    12175   9526   5340   -116  -1610    291       C  
ATOM   1230  C   ALA A 164     -13.448  67.703  42.356  1.00 71.81           C  
ANISOU 1230  C   ALA A 164    12120   9744   5419     23  -1695    375       C  
ATOM   1231  O   ALA A 164     -14.171  67.116  43.166  1.00 70.92           O  
ANISOU 1231  O   ALA A 164    11883   9646   5415     -8  -1704    297       O  
ATOM   1232  CB  ALA A 164     -11.008  67.964  42.942  1.00 69.03           C  
ANISOU 1232  CB  ALA A 164    12056   8983   5187    -72  -1500    367       C  
ATOM   1233  N   GLU A 165     -13.849  68.779  41.682  1.00 72.50           N  
ANISOU 1233  N   GLU A 165    12231   9931   5384    183  -1750    541       N  
ATOM   1234  CA  GLU A 165     -15.194  69.296  41.802  1.00 75.56           C  
ANISOU 1234  CA  GLU A 165    12483  10471   5753    338  -1834    634       C  
ATOM   1235  C   GLU A 165     -16.200  68.263  41.333  1.00 77.55           C  
ANISOU 1235  C   GLU A 165    12527  11002   5936    246  -1944    504       C  
ATOM   1236  O   GLU A 165     -17.228  68.058  41.985  1.00 78.89           O  
ANISOU 1236  O   GLU A 165    12539  11247   6186    277  -1979    478       O  
ATOM   1237  CB  GLU A 165     -15.355  70.594  41.008  1.00 79.31           C  
ANISOU 1237  CB  GLU A 165    13033  11009   6090    533  -1870    845       C  
ATOM   1238  CG  GLU A 165     -16.770  71.171  40.985  1.00 83.11           C  
ANISOU 1238  CG  GLU A 165    13364  11680   6532    722  -1966    960       C  
ATOM   1239  CD  GLU A 165     -16.868  72.509  40.255  1.00 87.39           C  
ANISOU 1239  CD  GLU A 165    14004  12252   6949    939  -1984   1193       C  
ATOM   1240  OE1 GLU A 165     -16.250  72.672  39.171  1.00 88.86           O  
ANISOU 1240  OE1 GLU A 165    14292  12493   6975    919  -1995   1246       O  
ATOM   1241  OE2 GLU A 165     -17.590  73.391  40.769  1.00 90.62           O  
ANISOU 1241  OE2 GLU A 165    14386  12628   7417   1136  -1982   1328       O  
ATOM   1242  N   GLN A 166     -15.919  67.620  40.206  1.00 79.50           N  
ANISOU 1242  N   GLN A 166    12768  11404   6031    128  -1994    417       N  
ATOM   1243  CA  GLN A 166     -16.845  66.624  39.674  1.00 82.24           C  
ANISOU 1243  CA  GLN A 166    12921  12027   6300     19  -2101    273       C  
ATOM   1244  C   GLN A 166     -16.928  65.404  40.585  1.00 77.84           C  
ANISOU 1244  C   GLN A 166    12283  11374   5916   -158  -2046     80       C  
ATOM   1245  O   GLN A 166     -17.999  64.821  40.740  1.00 76.18           O  
ANISOU 1245  O   GLN A 166    11883  11332   5729   -207  -2111     -5       O  
ATOM   1246  CB  GLN A 166     -16.503  66.214  38.227  1.00 87.11           C  
ANISOU 1246  CB  GLN A 166    13561  12837   6699    -73  -2163    208       C  
ATOM   1247  CG  GLN A 166     -16.701  67.307  37.197  1.00 93.26           C  
ANISOU 1247  CG  GLN A 166    14378  13785   7269    104  -2242    401       C  
ATOM   1248  CD  GLN A 166     -15.975  67.085  35.870  1.00 98.69           C  
ANISOU 1248  CD  GLN A 166    15162  14587   7746     25  -2259    367       C  
ATOM   1249  OE1 GLN A 166     -15.868  65.958  35.356  1.00101.32           O  
ANISOU 1249  OE1 GLN A 166    15443  15032   8019   -163  -2281    165       O  
ATOM   1250  NE2 GLN A 166     -15.488  68.181  35.294  1.00101.14           N  
ANISOU 1250  NE2 GLN A 166    15618  14867   7941    172  -2240    565       N  
ATOM   1251  N   HIS A 167     -15.802  65.015  41.172  1.00 74.07           N  
ANISOU 1251  N   HIS A 167    11945  10635   5559   -253  -1923     17       N  
ATOM   1252  CA  HIS A 167     -15.808  63.900  42.115  1.00 72.98           C  
ANISOU 1252  CA  HIS A 167    11755  10380   5594   -401  -1855   -139       C  
ATOM   1253  C   HIS A 167     -16.705  64.173  43.315  1.00 71.26           C  
ANISOU 1253  C   HIS A 167    11432  10122   5521   -313  -1845    -86       C  
ATOM   1254  O   HIS A 167     -17.510  63.316  43.670  1.00 72.23           O  
ANISOU 1254  O   HIS A 167    11403  10329   5712   -411  -1860   -200       O  
ATOM   1255  CB  HIS A 167     -14.410  63.552  42.579  1.00 72.01           C  
ANISOU 1255  CB  HIS A 167    11801   9988   5570   -483  -1728   -187       C  
ATOM   1256  CG  HIS A 167     -13.568  62.924  41.517  1.00 74.26           C  
ANISOU 1256  CG  HIS A 167    12162  10309   5744   -609  -1716   -291       C  
ATOM   1257  ND1 HIS A 167     -12.189  62.967  41.541  1.00 73.05           N  
ANISOU 1257  ND1 HIS A 167    12175   9962   5617   -637  -1618   -287       N  
ATOM   1258  CD2 HIS A 167     -13.908  62.255  40.387  1.00 76.71           C  
ANISOU 1258  CD2 HIS A 167    12402  10835   5908   -713  -1788   -407       C  
ATOM   1259  CE1 HIS A 167     -11.715  62.336  40.481  1.00 74.50           C  
ANISOU 1259  CE1 HIS A 167    12389  10234   5683   -748  -1622   -393       C  
ATOM   1260  NE2 HIS A 167     -12.737  61.892  39.768  1.00 76.91           N  
ANISOU 1260  NE2 HIS A 167    12559  10783   5877   -798  -1724   -471       N  
ATOM   1261  N   LEU A 168     -16.617  65.378  43.889  1.00 68.77           N  
ANISOU 1261  N   LEU A 168    11193   9687   5246   -132  -1816     81       N  
ATOM   1262  CA  LEU A 168     -17.512  65.779  44.967  1.00 67.31           C  
ANISOU 1262  CA  LEU A 168    10914   9480   5180    -22  -1805    143       C  
ATOM   1263  C   LEU A 168     -18.982  65.734  44.543  1.00 68.74           C  
ANISOU 1263  C   LEU A 168    10871   9954   5290     25  -1922    147       C  
ATOM   1264  O   LEU A 168     -19.824  65.218  45.289  1.00 67.32           O  
ANISOU 1264  O   LEU A 168    10542   9819   5215    -13  -1914     83       O  
ATOM   1265  CB  LEU A 168     -17.151  67.178  45.501  1.00 67.73           C  
ANISOU 1265  CB  LEU A 168    11103   9361   5269    172  -1753    321       C  
ATOM   1266  CG  LEU A 168     -15.803  67.356  46.242  1.00 65.40           C  
ANISOU 1266  CG  LEU A 168    11005   8768   5075    137  -1631    321       C  
ATOM   1267  CD1 LEU A 168     -15.464  68.819  46.463  1.00 65.21           C  
ANISOU 1267  CD1 LEU A 168    11120   8603   5053    316  -1592    489       C  
ATOM   1268  CD2 LEU A 168     -15.789  66.637  47.565  1.00 63.28           C  
ANISOU 1268  CD2 LEU A 168    10706   8363   4974     58  -1551    227       C  
ATOM   1269  N   ILE A 169     -19.284  66.232  43.343  1.00 70.97           N  
ANISOU 1269  N   ILE A 169    11123  10449   5390    103  -2029    220       N  
ATOM   1270  CA  ILE A 169     -20.652  66.193  42.839  1.00 74.05           C  
ANISOU 1270  CA  ILE A 169    11285  11157   5692    152  -2157    223       C  
ATOM   1271  C   ILE A 169     -21.082  64.745  42.598  1.00 75.37           C  
ANISOU 1271  C   ILE A 169    11297  11475   5863    -84  -2193      3       C  
ATOM   1272  O   ILE A 169     -22.219  64.400  42.919  1.00 77.79           O  
ANISOU 1272  O   ILE A 169    11395  11946   6216   -102  -2239    -45       O  
ATOM   1273  CB  ILE A 169     -20.856  67.067  41.574  1.00 75.94           C  
ANISOU 1273  CB  ILE A 169    11529  11607   5714    303  -2269    365       C  
ATOM   1274  CG1 ILE A 169     -20.636  68.534  41.934  1.00 76.18           C  
ANISOU 1274  CG1 ILE A 169    11697  11476   5769    550  -2221    591       C  
ATOM   1275  CG2 ILE A 169     -22.271  66.900  40.998  1.00 77.75           C  
ANISOU 1275  CG2 ILE A 169    11496  12207   5836    339  -2418    350       C  
ATOM   1276  CD1 ILE A 169     -20.624  69.478  40.752  1.00 78.25           C  
ANISOU 1276  CD1 ILE A 169    12019  11882   5830    712  -2300    761       C  
ATOM   1277  N   SER A 170     -20.198  63.912  42.041  1.00 74.77           N  
ANISOU 1277  N   SER A 170    11321  11343   5745   -266  -2164   -131       N  
ATOM   1278  CA  SER A 170     -20.496  62.472  41.869  1.00 76.06           C  
ANISOU 1278  CA  SER A 170    11367  11598   5934   -509  -2171   -359       C  
ATOM   1279  C   SER A 170     -20.716  61.768  43.205  1.00 75.00           C  
ANISOU 1279  C   SER A 170    11185  11289   6023   -599  -2065   -439       C  
ATOM   1280  O   SER A 170     -21.542  60.877  43.299  1.00 76.90           O  
ANISOU 1280  O   SER A 170    11253  11655   6308   -740  -2086   -576       O  
ATOM   1281  CB  SER A 170     -19.381  61.723  41.129  1.00 75.43           C  
ANISOU 1281  CB  SER A 170    11431  11439   5787   -674  -2130   -488       C  
ATOM   1282  OG  SER A 170     -19.460  61.899  39.726  1.00 76.20           O  
ANISOU 1282  OG  SER A 170    11512  11785   5655   -670  -2244   -492       O  
HETATM 1283  N   MSE A 171     -20.003  62.192  44.234  1.00 73.09           N  
ANISOU 1283  N   MSE A 171    11090  10767   5913   -520  -1952   -352       N  
HETATM 1284  CA  MSE A 171     -20.200  61.642  45.580  1.00 73.74           C  
ANISOU 1284  CA  MSE A 171    11139  10684   6195   -576  -1847   -399       C  
HETATM 1285  C   MSE A 171     -21.422  62.224  46.265  1.00 75.44           C  
ANISOU 1285  C   MSE A 171    11188  11008   6465   -443  -1876   -308       C  
HETATM 1286  O   MSE A 171     -21.550  62.094  47.490  1.00 75.47           O  
ANISOU 1286  O   MSE A 171    11188  10860   6623   -434  -1781   -299       O  
HETATM 1287  CB  MSE A 171     -18.913  61.827  46.403  1.00 71.72           C  
ANISOU 1287  CB  MSE A 171    11100  10106   6041   -549  -1721   -351       C  
HETATM 1288  CG  MSE A 171     -17.868  60.770  46.063  1.00 71.91           C  
ANISOU 1288  CG  MSE A 171    11237  10008   6077   -730  -1658   -491       C  
HETATM 1289 SE   MSE A 171     -16.206  61.023  47.116  1.00 73.88          SE  
ANISOU 1289 SE   MSE A 171    11735   9884   6448   -685  -1509   -426      SE  
HETATM 1290  CE  MSE A 171     -15.659  62.802  46.696  1.00 71.27           C  
ANISOU 1290  CE  MSE A 171    11538   9536   6005   -467  -1551   -224       C  
ATOM   1291  N   CYS A 172     -22.324  62.852  45.495  1.00 77.74           N  
ANISOU 1291  N   CYS A 172    11339  11570   6626   -331  -2004   -239       N  
ATOM   1292  CA  CYS A 172     -23.600  63.406  45.969  1.00 79.70           C  
ANISOU 1292  CA  CYS A 172    11396  11975   6908   -191  -2047   -155       C  
ATOM   1293  C   CYS A 172     -23.511  64.619  46.891  1.00 77.38           C  
ANISOU 1293  C   CYS A 172    11196  11513   6690     41  -1983     24       C  
ATOM   1294  O   CYS A 172     -24.390  64.822  47.724  1.00 78.23           O  
ANISOU 1294  O   CYS A 172    11175  11657   6892    121  -1957     61       O  
ATOM   1295  CB  CYS A 172     -24.470  62.324  46.613  1.00 82.07           C  
ANISOU 1295  CB  CYS A 172    11505  12343   7333   -357  -2012   -298       C  
ATOM   1296  SG  CYS A 172     -24.712  60.877  45.583  1.00 89.31           S  
ANISOU 1296  SG  CYS A 172    12298  13455   8178   -649  -2078   -534       S  
ATOM   1297  N   GLU A 173     -22.482  65.445  46.735  1.00 76.06           N  
ANISOU 1297  N   GLU A 173    11249  11168   6481    147  -1951    132       N  
ATOM   1298  CA  GLU A 173     -22.427  66.716  47.462  1.00 76.58           C  
ANISOU 1298  CA  GLU A 173    11411  11086   6601    374  -1897    301       C  
ATOM   1299  C   GLU A 173     -23.188  67.808  46.717  1.00 80.44           C  
ANISOU 1299  C   GLU A 173    11821  11775   6964    595  -2001    458       C  
ATOM   1300  O   GLU A 173     -23.318  67.773  45.491  1.00 83.83           O  
ANISOU 1300  O   GLU A 173    12203  12413   7234    586  -2112    465       O  
ATOM   1301  CB  GLU A 173     -20.979  67.148  47.758  1.00 73.79           C  
ANISOU 1301  CB  GLU A 173    11326  10430   6278    381  -1801    342       C  
ATOM   1302  CG  GLU A 173     -20.257  66.257  48.784  1.00 70.75           C  
ANISOU 1302  CG  GLU A 173    11019   9825   6036    220  -1685    223       C  
ATOM   1303  CD  GLU A 173     -20.909  66.254  50.168  1.00 69.55           C  
ANISOU 1303  CD  GLU A 173    10792   9604   6030    268  -1608    226       C  
ATOM   1304  OE1 GLU A 173     -21.609  67.223  50.523  1.00 68.14           O  
ANISOU 1304  OE1 GLU A 173    10566   9460   5861    457  -1614    340       O  
ATOM   1305  OE2 GLU A 173     -20.729  65.258  50.905  1.00 67.38           O  
ANISOU 1305  OE2 GLU A 173    10505   9237   5856    119  -1535    117       O  
ATOM   1306  N   ASP A 174     -23.705  68.760  47.485  1.00 83.16           N  
ANISOU 1306  N   ASP A 174    12153  12059   7381    800  -1959    583       N  
ATOM   1307  CA  ASP A 174     -24.488  69.878  46.975  1.00 88.31           C  
ANISOU 1307  CA  ASP A 174    12735  12873   7945   1050  -2036    754       C  
ATOM   1308  C   ASP A 174     -23.556  70.828  46.258  1.00 87.82           C  
ANISOU 1308  C   ASP A 174    12899  12685   7781   1159  -2034    888       C  
ATOM   1309  O   ASP A 174     -22.640  71.363  46.864  1.00 85.21           O  
ANISOU 1309  O   ASP A 174    12782  12065   7529   1187  -1923    929       O  
ATOM   1310  CB  ASP A 174     -25.183  70.592  48.150  1.00 90.33           C  
ANISOU 1310  CB  ASP A 174    12943  13044   8332   1233  -1958    837       C  
ATOM   1311  CG  ASP A 174     -26.065  71.766  47.720  1.00 95.08           C  
ANISOU 1311  CG  ASP A 174    13462  13800   8861   1520  -2022   1023       C  
ATOM   1312  OD1 ASP A 174     -26.162  72.101  46.514  1.00 96.75           O  
ANISOU 1312  OD1 ASP A 174    13656  14191   8911   1596  -2133   1109       O  
ATOM   1313  OD2 ASP A 174     -26.665  72.376  48.629  1.00 98.80           O  
ANISOU 1313  OD2 ASP A 174    13892  14209   9436   1684  -1954   1089       O  
ATOM   1314  N   HIS A 175     -23.799  71.042  44.973  1.00 92.28           N  
ANISOU 1314  N   HIS A 175    13415  13479   8167   1216  -2154    956       N  
ATOM   1315  CA  HIS A 175     -22.930  71.901  44.177  1.00 94.74           C  
ANISOU 1315  CA  HIS A 175    13940  13690   8366   1310  -2149   1092       C  
ATOM   1316  C   HIS A 175     -22.894  73.361  44.683  1.00 95.15           C  
ANISOU 1316  C   HIS A 175    14132  13540   8477   1570  -2068   1290       C  
ATOM   1317  O   HIS A 175     -21.851  74.020  44.596  1.00 94.90           O  
ANISOU 1317  O   HIS A 175    14339  13272   8444   1595  -1989   1365       O  
ATOM   1318  CB  HIS A 175     -23.249  71.773  42.679  1.00 98.02           C  
ANISOU 1318  CB  HIS A 175    14266  14417   8557   1316  -2298   1124       C  
ATOM   1319  CG  HIS A 175     -24.572  72.324  42.249  1.00103.00           C  
ANISOU 1319  CG  HIS A 175    14692  15345   9096   1530  -2414   1251       C  
ATOM   1320  ND1 HIS A 175     -24.696  73.561  41.656  1.00106.06           N  
ANISOU 1320  ND1 HIS A 175    15159  15761   9378   1791  -2441   1481       N  
ATOM   1321  CD2 HIS A 175     -25.807  71.763  42.211  1.00105.31           C  
ANISOU 1321  CD2 HIS A 175    14697  15943   9373   1516  -2518   1180       C  
ATOM   1322  CE1 HIS A 175     -25.959  73.757  41.312  1.00108.75           C  
ANISOU 1322  CE1 HIS A 175    15265  16412   9641   1948  -2560   1555       C  
ATOM   1323  NE2 HIS A 175     -26.653  72.681  41.637  1.00108.61           N  
ANISOU 1323  NE2 HIS A 175    15014  16576   9676   1780  -2611   1370       N  
ATOM   1324  N   ASP A 176     -24.007  73.833  45.259  1.00 95.82           N  
ANISOU 1324  N   ASP A 176    14072  13707   8628   1752  -2075   1362       N  
ATOM   1325  CA  ASP A 176     -24.081  75.145  45.944  1.00 95.14           C  
ANISOU 1325  CA  ASP A 176    14108  13408   8631   1997  -1976   1523       C  
ATOM   1326  C   ASP A 176     -23.054  75.344  47.066  1.00 91.97           C  
ANISOU 1326  C   ASP A 176    13926  12632   8386   1921  -1817   1466       C  
ATOM   1327  O   ASP A 176     -22.731  76.486  47.400  1.00 94.72           O  
ANISOU 1327  O   ASP A 176    14449  12756   8782   2084  -1727   1591       O  
ATOM   1328  CB  ASP A 176     -25.477  75.375  46.572  1.00 96.43           C  
ANISOU 1328  CB  ASP A 176    14049  13724   8866   2171  -1993   1562       C  
ATOM   1329  CG  ASP A 176     -26.581  75.628  45.545  1.00 99.26           C  
ANISOU 1329  CG  ASP A 176    14199  14441   9074   2343  -2143   1680       C  
ATOM   1330  OD1 ASP A 176     -26.303  75.853  44.356  1.00 98.28           O  
ANISOU 1330  OD1 ASP A 176    14128  14430   8780   2375  -2227   1768       O  
ATOM   1331  OD2 ASP A 176     -27.750  75.632  45.966  1.00101.14           O  
ANISOU 1331  OD2 ASP A 176    14212  14854   9360   2456  -2172   1690       O  
ATOM   1332  N   ARG A 177     -22.605  74.253  47.685  1.00 86.76           N  
ANISOU 1332  N   ARG A 177    13249  11909   7807   1683  -1781   1281       N  
ATOM   1333  CA  ARG A 177     -21.660  74.324  48.782  1.00 82.96           C  
ANISOU 1333  CA  ARG A 177    12948  11112   7462   1602  -1645   1215       C  
ATOM   1334  C   ARG A 177     -20.244  73.927  48.370  1.00 77.82           C  
ANISOU 1334  C   ARG A 177    12475  10317   6774   1411  -1619   1147       C  
ATOM   1335  O   ARG A 177     -19.398  73.668  49.226  1.00 75.99           O  
ANISOU 1335  O   ARG A 177    12358   9870   6644   1294  -1525   1057       O  
ATOM   1336  CB  ARG A 177     -22.191  73.486  49.952  1.00 84.23           C  
ANISOU 1336  CB  ARG A 177    12967  11284   7750   1507  -1604   1079       C  
ATOM   1337  CG  ARG A 177     -23.557  73.980  50.429  1.00 89.02           C  
ANISOU 1337  CG  ARG A 177    13401  12020   8402   1709  -1610   1152       C  
ATOM   1338  CD  ARG A 177     -23.861  73.636  51.897  1.00 91.74           C  
ANISOU 1338  CD  ARG A 177    13695  12263   8897   1673  -1508   1060       C  
ATOM   1339  NE  ARG A 177     -24.584  74.583  52.790  1.00 94.08           N  
ANISOU 1339  NE  ARG A 177    13975  12491   9277   1897  -1430   1144       N  
ATOM   1340  CZ  ARG A 177     -25.280  75.692  52.477  1.00 97.90           C  
ANISOU 1340  CZ  ARG A 177    14436  13027   9733   2158  -1444   1299       C  
ATOM   1341  NH1 ARG A 177     -25.527  76.100  51.226  1.00100.77           N  
ANISOU 1341  NH1 ARG A 177    14764  13551   9970   2266  -1550   1418       N  
ATOM   1342  NH2 ARG A 177     -25.797  76.403  53.476  1.00 99.00           N  
ANISOU 1342  NH2 ARG A 177    14580  13064   9971   2329  -1345   1339       N  
ATOM   1343  N   ILE A 178     -19.974  73.926  47.067  1.00 74.99           N  
ANISOU 1343  N   ILE A 178    12141  10085   6266   1393  -1698   1196       N  
ATOM   1344  CA  ILE A 178     -18.637  73.672  46.538  1.00 71.72           C  
ANISOU 1344  CA  ILE A 178    11897   9550   5803   1237  -1669   1152       C  
ATOM   1345  C   ILE A 178     -18.107  74.959  45.904  1.00 72.18           C  
ANISOU 1345  C   ILE A 178    12146   9489   5790   1385  -1635   1330       C  
ATOM   1346  O   ILE A 178     -18.801  75.603  45.136  1.00 72.58           O  
ANISOU 1346  O   ILE A 178    12152   9690   5733   1559  -1702   1476       O  
ATOM   1347  CB  ILE A 178     -18.638  72.545  45.472  1.00 71.00           C  
ANISOU 1347  CB  ILE A 178    11697   9695   5582   1069  -1772   1048       C  
ATOM   1348  CG1 ILE A 178     -19.206  71.252  46.042  1.00 69.82           C  
ANISOU 1348  CG1 ILE A 178    11363   9655   5510    913  -1796    871       C  
ATOM   1349  CG2 ILE A 178     -17.217  72.265  44.977  1.00 69.74           C  
ANISOU 1349  CG2 ILE A 178    11713   9401   5381    913  -1725    995       C  
ATOM   1350  CD1 ILE A 178     -19.481  70.175  45.015  1.00 70.48           C  
ANISOU 1350  CD1 ILE A 178    11311   9996   5472    761  -1902    759       C  
ATOM   1351  N   LEU A 179     -16.857  75.293  46.212  1.00 70.99           N  
ANISOU 1351  N   LEU A 179    12202   9076   5696   1309  -1531   1319       N  
ATOM   1352  CA  LEU A 179     -16.132  76.380  45.566  1.00 71.12           C  
ANISOU 1352  CA  LEU A 179    12419   8953   5650   1393  -1479   1467       C  
ATOM   1353  C   LEU A 179     -14.875  75.801  44.904  1.00 70.89           C  
ANISOU 1353  C   LEU A 179    12489   8890   5555   1191  -1464   1389       C  
ATOM   1354  O   LEU A 179     -14.066  75.140  45.559  1.00 68.98           O  
ANISOU 1354  O   LEU A 179    12280   8523   5404   1020  -1408   1246       O  
ATOM   1355  CB  LEU A 179     -15.737  77.420  46.603  1.00 70.40           C  
ANISOU 1355  CB  LEU A 179    12489   8558   5700   1479  -1349   1517       C  
ATOM   1356  CG  LEU A 179     -14.760  78.509  46.140  1.00 71.50           C  
ANISOU 1356  CG  LEU A 179    12865   8486   5815   1516  -1259   1640       C  
ATOM   1357  CD1 LEU A 179     -15.480  79.525  45.258  1.00 74.39           C  
ANISOU 1357  CD1 LEU A 179    13256   8930   6077   1752  -1290   1859       C  
ATOM   1358  CD2 LEU A 179     -14.089  79.186  47.323  1.00 69.90           C  
ANISOU 1358  CD2 LEU A 179    12817   7969   5770   1501  -1123   1605       C  
ATOM   1359  N   LEU A 180     -14.707  76.055  43.612  1.00 73.32           N  
ANISOU 1359  N   LEU A 180    12843   9315   5700   1221  -1509   1490       N  
ATOM   1360  CA  LEU A 180     -13.503  75.650  42.891  1.00 73.23           C  
ANISOU 1360  CA  LEU A 180    12938   9271   5615   1052  -1481   1436       C  
ATOM   1361  C   LEU A 180     -12.545  76.827  42.930  1.00 73.59           C  
ANISOU 1361  C   LEU A 180    13211   9051   5696   1099  -1358   1558       C  
ATOM   1362  O   LEU A 180     -12.721  77.784  42.195  1.00 79.06           O  
ANISOU 1362  O   LEU A 180    13990   9752   6295   1248  -1354   1740       O  
ATOM   1363  CB  LEU A 180     -13.852  75.245  41.452  1.00 74.32           C  
ANISOU 1363  CB  LEU A 180    12999   9697   5540   1050  -1593   1469       C  
ATOM   1364  CG  LEU A 180     -12.680  75.037  40.490  1.00 74.79           C  
ANISOU 1364  CG  LEU A 180    13183   9744   5486    916  -1558   1454       C  
ATOM   1365  CD1 LEU A 180     -11.563  74.170  41.054  1.00 72.56           C  
ANISOU 1365  CD1 LEU A 180    12941   9314   5314    695  -1482   1268       C  
ATOM   1366  CD2 LEU A 180     -13.198  74.457  39.190  1.00 77.56           C  
ANISOU 1366  CD2 LEU A 180    13426  10418   5623    903  -1683   1448       C  
ATOM   1367  N   ALA A 181     -11.566  76.779  43.823  1.00 72.22           N  
ANISOU 1367  N   ALA A 181    13134   8644   5662    976  -1256   1460       N  
ATOM   1368  CA  ALA A 181     -10.676  77.932  44.101  1.00 72.04           C  
ANISOU 1368  CA  ALA A 181    13319   8342   5708   1001  -1126   1549       C  
ATOM   1369  C   ALA A 181      -9.250  77.768  43.566  1.00 71.46           C  
ANISOU 1369  C   ALA A 181    13366   8185   5600    828  -1058   1509       C  
ATOM   1370  O   ALA A 181      -8.566  78.751  43.300  1.00 69.85           O  
ANISOU 1370  O   ALA A 181    13331   7811   5396    850   -964   1617       O  
ATOM   1371  CB  ALA A 181     -10.629  78.197  45.613  1.00 70.09           C  
ANISOU 1371  CB  ALA A 181    13096   7886   5648   1003  -1053   1473       C  
ATOM   1372  N   GLY A 182      -8.807  76.525  43.429  1.00 72.08           N  
ANISOU 1372  N   GLY A 182    13356   8375   5656    656  -1097   1351       N  
ATOM   1373  CA  GLY A 182      -7.391  76.217  43.352  1.00 73.36           C  
ANISOU 1373  CA  GLY A 182    13604   8428   5840    478  -1017   1266       C  
ATOM   1374  C   GLY A 182      -6.839  75.921  44.739  1.00 73.38           C  
ANISOU 1374  C   GLY A 182    13602   8262   6018    382   -960   1129       C  
ATOM   1375  O   GLY A 182      -7.436  76.274  45.756  1.00 71.13           O  
ANISOU 1375  O   GLY A 182    13296   7893   5837    466   -954   1128       O  
ATOM   1376  N   CYS A 183      -5.680  75.263  44.759  1.00 75.52           N  
ANISOU 1376  N   CYS A 183    13889   8494   6312    213   -915   1015       N  
ATOM   1377  CA  CYS A 183      -4.932  74.997  45.982  1.00 75.51           C  
ANISOU 1377  CA  CYS A 183    13892   8342   6457    114   -858    893       C  
ATOM   1378  C   CYS A 183      -4.319  76.317  46.445  1.00 77.55           C  
ANISOU 1378  C   CYS A 183    14303   8371   6790    137   -756    967       C  
ATOM   1379  O   CYS A 183      -3.774  77.058  45.636  1.00 79.09           O  
ANISOU 1379  O   CYS A 183    14613   8511   6927    133   -698   1066       O  
ATOM   1380  CB  CYS A 183      -3.842  73.958  45.724  1.00 74.63           C  
ANISOU 1380  CB  CYS A 183    13750   8270   6336    -55   -838    767       C  
ATOM   1381  SG  CYS A 183      -2.876  73.457  47.167  1.00 76.50           S  
ANISOU 1381  SG  CYS A 183    13967   8366   6732   -172   -783    619       S  
ATOM   1382  N   PRO A 184      -4.433  76.630  47.746  1.00 79.03           N  
ANISOU 1382  N   PRO A 184    14497   8425   7104    160   -727    917       N  
ATOM   1383  CA  PRO A 184      -3.763  77.834  48.250  1.00 79.78           C  
ANISOU 1383  CA  PRO A 184    14740   8292   7278    153   -622    954       C  
ATOM   1384  C   PRO A 184      -2.229  77.831  48.138  1.00 78.72           C  
ANISOU 1384  C   PRO A 184    14671   8071   7167    -19   -545    892       C  
ATOM   1385  O   PRO A 184      -1.638  78.904  48.056  1.00 79.96           O  
ANISOU 1385  O   PRO A 184    14964   8063   7353    -38   -452    954       O  
ATOM   1386  CB  PRO A 184      -4.187  77.878  49.716  1.00 79.06           C  
ANISOU 1386  CB  PRO A 184    14614   8120   7304    191   -621    873       C  
ATOM   1387  CG  PRO A 184      -5.488  77.141  49.752  1.00 79.28           C  
ANISOU 1387  CG  PRO A 184    14500   8322   7299    291   -718    873       C  
ATOM   1388  CD  PRO A 184      -5.349  76.046  48.748  1.00 78.13           C  
ANISOU 1388  CD  PRO A 184    14265   8365   7056    212   -783    843       C  
ATOM   1389  N   SER A 185      -1.596  76.655  48.106  1.00 75.80           N  
ANISOU 1389  N   SER A 185    14204   7807   6787   -142   -574    775       N  
ATOM   1390  CA  SER A 185      -0.133  76.571  47.919  1.00 74.32           C  
ANISOU 1390  CA  SER A 185    14054   7568   6615   -299   -502    717       C  
ATOM   1391  C   SER A 185       0.336  77.326  46.659  1.00 74.73           C  
ANISOU 1391  C   SER A 185    14219   7592   6580   -315   -437    839       C  
ATOM   1392  O   SER A 185       1.458  77.832  46.617  1.00 70.33           O  
ANISOU 1392  O   SER A 185    13737   6926   6059   -424   -346    830       O  
ATOM   1393  CB  SER A 185       0.362  75.096  47.898  1.00 73.03           C  
ANISOU 1393  CB  SER A 185    13763   7543   6440   -400   -545    588       C  
ATOM   1394  OG  SER A 185      -0.078  74.379  46.752  1.00 71.05           O  
ANISOU 1394  OG  SER A 185    13461   7461   6072   -381   -598    614       O  
ATOM   1395  N   TYR A 186      -0.520  77.333  45.636  1.00 76.68           N  
ANISOU 1395  N   TYR A 186    14467   7958   6709   -211   -487    949       N  
ATOM   1396  CA  TYR A 186      -0.249  78.022  44.382  1.00 78.79           C  
ANISOU 1396  CA  TYR A 186    14843   8225   6869   -198   -433   1089       C  
ATOM   1397  C   TYR A 186      -0.216  79.517  44.518  1.00 80.43           C  
ANISOU 1397  C   TYR A 186    15210   8222   7125   -138   -339   1217       C  
ATOM   1398  O   TYR A 186       0.477  80.176  43.751  1.00 82.04           O  
ANISOU 1398  O   TYR A 186    15528   8356   7285   -185   -248   1308       O  
ATOM   1399  CB  TYR A 186      -1.233  77.583  43.273  1.00 80.19           C  
ANISOU 1399  CB  TYR A 186    14967   8615   6886    -94   -527   1170       C  
ATOM   1400  CG  TYR A 186      -0.712  76.372  42.531  1.00 80.15           C  
ANISOU 1400  CG  TYR A 186    14875   8785   6790   -207   -557   1072       C  
ATOM   1401  CD1 TYR A 186      -0.366  76.442  41.172  1.00 81.45           C  
ANISOU 1401  CD1 TYR A 186    15095   9048   6803   -227   -531   1152       C  
ATOM   1402  CD2 TYR A 186      -0.471  75.176  43.208  1.00 79.93           C  
ANISOU 1402  CD2 TYR A 186    14725   8810   6833   -297   -595    898       C  
ATOM   1403  CE1 TYR A 186       0.158  75.348  40.503  1.00 80.47           C  
ANISOU 1403  CE1 TYR A 186    14900   9075   6597   -333   -545   1049       C  
ATOM   1404  CE2 TYR A 186       0.053  74.070  42.545  1.00 80.27           C  
ANISOU 1404  CE2 TYR A 186    14701   8991   6807   -397   -606    801       C  
ATOM   1405  CZ  TYR A 186       0.363  74.164  41.193  1.00 79.89           C  
ANISOU 1405  CZ  TYR A 186    14706   9040   6606   -416   -581    870       C  
ATOM   1406  OH  TYR A 186       0.870  73.065  40.554  1.00 78.86           O  
ANISOU 1406  OH  TYR A 186    14513   9041   6407   -512   -583    762       O  
ATOM   1407  N   ASP A 187      -0.960  80.060  45.476  1.00 82.84           N  
ANISOU 1407  N   ASP A 187    15532   8419   7522    -34   -350   1225       N  
ATOM   1408  CA  ASP A 187      -0.816  81.483  45.836  1.00 85.23           C  
ANISOU 1408  CA  ASP A 187    15998   8477   7906      4   -240   1311       C  
ATOM   1409  C   ASP A 187       0.646  81.834  46.138  1.00 85.22           C  
ANISOU 1409  C   ASP A 187    16069   8321   7987   -187   -126   1232       C  
ATOM   1410  O   ASP A 187       1.133  82.881  45.728  1.00 85.39           O  
ANISOU 1410  O   ASP A 187    16241   8181   8022   -212    -12   1330       O  
ATOM   1411  CB  ASP A 187      -1.735  81.872  47.016  1.00 85.45           C  
ANISOU 1411  CB  ASP A 187    16018   8412   8036    125   -262   1286       C  
ATOM   1412  CG  ASP A 187      -3.217  81.942  46.618  1.00 86.47           C  
ANISOU 1412  CG  ASP A 187    16105   8658   8092    342   -344   1411       C  
ATOM   1413  OD1 ASP A 187      -3.644  81.118  45.773  1.00 88.35           O  
ANISOU 1413  OD1 ASP A 187    16239   9122   8208    368   -439   1435       O  
ATOM   1414  OD2 ASP A 187      -3.950  82.824  47.142  1.00 87.16           O  
ANISOU 1414  OD2 ASP A 187    16259   8616   8241    487   -313   1479       O  
ATOM   1415  N   LYS A 188       1.333  80.939  46.832  1.00 86.96           N  
ANISOU 1415  N   LYS A 188    16178   8600   8262   -322   -155   1058       N  
ATOM   1416  CA  LYS A 188       2.750  81.125  47.141  1.00 90.41           C  
ANISOU 1416  CA  LYS A 188    16644   8936   8772   -511    -64    965       C  
ATOM   1417  C   LYS A 188       3.693  80.705  46.022  1.00 90.79           C  
ANISOU 1417  C   LYS A 188    16677   9081   8734   -626    -25    983       C  
ATOM   1418  O   LYS A 188       4.710  81.370  45.813  1.00 89.40           O  
ANISOU 1418  O   LYS A 188    16585   8789   8593   -749     87    994       O  
ATOM   1419  CB  LYS A 188       3.121  80.392  48.431  1.00 90.43           C  
ANISOU 1419  CB  LYS A 188    16528   8965   8864   -592   -111    780       C  
ATOM   1420  CG  LYS A 188       2.741  81.162  49.690  1.00 94.40           C  
ANISOU 1420  CG  LYS A 188    17087   9304   9475   -549    -90    735       C  
ATOM   1421  CD  LYS A 188       3.911  81.252  50.664  1.00 99.21           C  
ANISOU 1421  CD  LYS A 188    17680   9836  10179   -718    -43    583       C  
ATOM   1422  CE  LYS A 188       4.258  82.681  51.049  1.00102.91           C  
ANISOU 1422  CE  LYS A 188    18305  10062  10731   -768     73    594       C  
ATOM   1423  NZ  LYS A 188       3.594  83.028  52.342  1.00107.42           N  
ANISOU 1423  NZ  LYS A 188    18894  10546  11374   -694     53    520       N  
ATOM   1424  N   LEU A 189       3.377  79.601  45.331  1.00 92.59           N  
ANISOU 1424  N   LEU A 189    16799   9521   8857   -595   -111    974       N  
ATOM   1425  CA  LEU A 189       4.207  79.102  44.207  1.00 92.04           C  
ANISOU 1425  CA  LEU A 189    16712   9566   8690   -692    -75    982       C  
ATOM   1426  C   LEU A 189       4.281  80.089  43.060  1.00 93.55           C  
ANISOU 1426  C   LEU A 189    17052   9700   8794   -665     13   1160       C  
ATOM   1427  O   LEU A 189       5.372  80.383  42.578  1.00 94.31           O  
ANISOU 1427  O   LEU A 189    17198   9749   8886   -794    120   1170       O  
ATOM   1428  CB  LEU A 189       3.701  77.761  43.648  1.00 90.64           C  
ANISOU 1428  CB  LEU A 189    16408   9621   8408   -653   -182    934       C  
ATOM   1429  CG  LEU A 189       3.751  76.516  44.544  1.00 89.93           C  
ANISOU 1429  CG  LEU A 189    16166   9616   8387   -692   -259    762       C  
ATOM   1430  CD1 LEU A 189       3.090  75.348  43.847  1.00 88.17           C  
ANISOU 1430  CD1 LEU A 189    15847   9597   8055   -647   -351    734       C  
ATOM   1431  CD2 LEU A 189       5.177  76.161  44.920  1.00 89.67           C  
ANISOU 1431  CD2 LEU A 189    16087   9556   8427   -850   -192    645       C  
ATOM   1432  N   LEU A 190       3.123  80.582  42.620  1.00 94.60           N  
ANISOU 1432  N   LEU A 190    17248   9843   8852   -495    -27   1306       N  
ATOM   1433  CA  LEU A 190       3.048  81.507  41.471  1.00 97.71           C  
ANISOU 1433  CA  LEU A 190    17788  10195   9139   -435     49   1506       C  
ATOM   1434  C   LEU A 190       3.373  82.966  41.825  1.00103.43           C  
ANISOU 1434  C   LEU A 190    18686  10642   9970   -445    186   1599       C  
ATOM   1435  O   LEU A 190       3.487  83.803  40.928  1.00101.11           O  
ANISOU 1435  O   LEU A 190    18533  10276   9607   -414    280   1771       O  
ATOM   1436  CB  LEU A 190       1.675  81.399  40.782  1.00 96.25           C  
ANISOU 1436  CB  LEU A 190    17588  10165   8816   -235    -57   1633       C  
ATOM   1437  CG  LEU A 190       1.217  79.985  40.353  1.00 92.01           C  
ANISOU 1437  CG  LEU A 190    16887   9906   8167   -227   -193   1539       C  
ATOM   1438  CD1 LEU A 190      -0.192  80.025  39.779  1.00 91.90           C  
ANISOU 1438  CD1 LEU A 190    16849  10041   8025    -32   -302   1662       C  
ATOM   1439  CD2 LEU A 190       2.182  79.338  39.367  1.00 90.22           C  
ANISOU 1439  CD2 LEU A 190    16641   9805   7831   -360   -152   1499       C  
ATOM   1440  N   SER A 191       3.511  83.255  43.128  1.00110.82           N  
ANISOU 1440  N   SER A 191    19616  11420  11068   -489    202   1485       N  
ATOM   1441  CA  SER A 191       4.051  84.537  43.626  1.00115.40           C  
ANISOU 1441  CA  SER A 191    20349  11722  11774   -555    345   1513       C  
ATOM   1442  C   SER A 191       5.481  84.402  44.163  1.00120.44           C  
ANISOU 1442  C   SER A 191    20947  12300  12512   -792    420   1351       C  
ATOM   1443  O   SER A 191       5.918  85.241  44.941  1.00124.04           O  
ANISOU 1443  O   SER A 191    21483  12546  13097   -875    508   1301       O  
ATOM   1444  CB  SER A 191       3.149  85.081  44.747  1.00114.08           C  
ANISOU 1444  CB  SER A 191    20215  11415  11714   -432    316   1493       C  
ATOM   1445  OG  SER A 191       1.781  85.058  44.378  1.00111.34           O  
ANISOU 1445  OG  SER A 191    19861  11159  11282   -206    228   1621       O  
ATOM   1446  N   ALA A 192       6.192  83.332  43.794  1.00124.53           N  
ANISOU 1446  N   ALA A 192    21333  13007  12975   -900    382   1258       N  
ATOM   1447  CA  ALA A 192       7.470  82.994  44.438  1.00126.67           C  
ANISOU 1447  CA  ALA A 192    21516  13270  13341  -1103    423   1085       C  
ATOM   1448  C   ALA A 192       8.582  83.858  43.849  1.00129.09           C  
ANISOU 1448  C   ALA A 192    21930  13447  13669  -1259    590   1142       C  
ATOM   1449  O   ALA A 192       9.241  83.464  42.898  1.00129.74           O  
ANISOU 1449  O   ALA A 192    21983  13643  13666  -1332    634   1171       O  
ATOM   1450  CB  ALA A 192       7.791  81.496  44.301  1.00123.97           C  
ANISOU 1450  CB  ALA A 192    20990  13171  12941  -1141    328    967       C  
ATOM   1451  N   LYS A 193       8.744  85.064  44.382  1.00134.03           N  
ANISOU 1451  N   LYS A 193    22688  13828  14406  -1308    694   1161       N  
ATOM   1452  CA  LYS A 193       9.896  85.910  44.016  1.00140.71           C  
ANISOU 1452  CA  LYS A 193    23629  14529  15306  -1495    867   1185       C  
ATOM   1453  C   LYS A 193      11.301  85.338  44.350  1.00143.11           C  
ANISOU 1453  C   LYS A 193    23783  14926  15667  -1719    892   1007       C  
ATOM   1454  O   LYS A 193      11.929  85.713  45.351  1.00142.80           O  
ANISOU 1454  O   LYS A 193    23718  14782  15757  -1857    926    867       O  
ATOM   1455  CB  LYS A 193       9.781  87.367  44.531  1.00144.22           C  
ANISOU 1455  CB  LYS A 193    24260  14665  15870  -1515    988   1231       C  
ATOM   1456  CG  LYS A 193       9.245  88.380  43.521  1.00148.50           C  
ANISOU 1456  CG  LYS A 193    25014  15055  16354  -1401   1099   1477       C  
ATOM   1457  CD  LYS A 193       9.091  89.799  44.166  1.00151.57           C  
ANISOU 1457  CD  LYS A 193    25595  15109  16885  -1412   1226   1506       C  
ATOM   1458  CE  LYS A 193       7.618  90.181  44.254  1.00152.28           C  
ANISOU 1458  CE  LYS A 193    25781  15129  16948  -1141   1167   1639       C  
ATOM   1459  NZ  LYS A 193       7.384  91.528  44.846  1.00154.20           N  
ANISOU 1459  NZ  LYS A 193    26221  15039  17327  -1123   1297   1671       N  
ATOM   1460  N   ASN A 194      11.800  84.498  43.438  1.00145.14           N  
ANISOU 1460  N   ASN A 194    23946  15379  15820  -1753    887   1020       N  
ATOM   1461  CA  ASN A 194      13.106  83.799  43.557  1.00142.63           C  
ANISOU 1461  CA  ASN A 194    23465  15191  15534  -1935    909    872       C  
ATOM   1462  C   ASN A 194      14.186  84.788  43.984  1.00139.73           C  
ANISOU 1462  C   ASN A 194    23142  14651  15298  -2149   1052    812       C  
ATOM   1463  O   ASN A 194      14.701  85.579  43.190  1.00136.85           O  
ANISOU 1463  O   ASN A 194    22890  14180  14925  -2244   1207    919       O  
ATOM   1464  CB  ASN A 194      13.481  82.983  42.284  1.00141.54           C  
ANISOU 1464  CB  ASN A 194    23266  15254  15257  -1935    926    927       C  
ATOM   1465  CG  ASN A 194      13.632  83.824  41.022  1.00141.84           C  
ANISOU 1465  CG  ASN A 194    23466  15213  15211  -1955   1075   1117       C  
ATOM   1466  OD1 ASN A 194      13.172  84.957  40.946  1.00139.92           O  
ANISOU 1466  OD1 ASN A 194    23401  14769  14993  -1916   1148   1247       O  
ATOM   1467  ND2 ASN A 194      14.272  83.244  40.009  1.00142.27           N  
ANISOU 1467  ND2 ASN A 194    23465  15429  15162  -2009   1126   1138       N  
ATOM   1468  N   LYS A 195      14.475  84.757  45.282  1.00135.33           N  
ANISOU 1468  N   LYS A 195    22497  14064  14857  -2223   1000    640       N  
ATOM   1469  CA  LYS A 195      15.527  85.594  45.852  1.00134.97           C  
ANISOU 1469  CA  LYS A 195    22459  13881  14939  -2447   1115    540       C  
ATOM   1470  C   LYS A 195      16.852  84.996  45.427  1.00129.12           C  
ANISOU 1470  C   LYS A 195    21558  13311  14191  -2613   1165    465       C  
ATOM   1471  O   LYS A 195      16.915  84.315  44.412  1.00130.17           O  
ANISOU 1471  O   LYS A 195    21650  13592  14214  -2558   1167    544       O  
ATOM   1472  CB  LYS A 195      15.421  85.673  47.374  1.00135.08           C  
ANISOU 1472  CB  LYS A 195    22417  13849  15059  -2471   1029    367       C  
ATOM   1473  CG  LYS A 195      14.054  86.185  47.777  1.00135.38           C  
ANISOU 1473  CG  LYS A 195    22604  13733  15099  -2286    981    441       C  
ATOM   1474  CD  LYS A 195      14.157  87.028  49.078  1.00137.59           C  
ANISOU 1474  CD  LYS A 195    22933  13835  15508  -2381   1003    301       C  
ATOM   1475  CE  LYS A 195      13.999  88.538  48.790  1.00140.70           C  
ANISOU 1475  CE  LYS A 195    23569  13920  15971  -2425   1172    403       C  
ATOM   1476  NZ  LYS A 195      14.083  89.698  49.756  1.00140.87           N  
ANISOU 1476  NZ  LYS A 195    23713  13686  16123  -2533   1257    299       N  
ATOM   1477  N   ASP A 196      17.905  85.248  46.194  1.00119.42           N  
ANISOU 1477  N   ASP A 196    20229  12070  13072  -2814   1205    308       N  
ATOM   1478  CA  ASP A 196      19.090  84.412  46.138  1.00110.00           C  
ANISOU 1478  CA  ASP A 196    18820  11094  11882  -2937   1201    195       C  
ATOM   1479  C   ASP A 196      18.715  82.936  46.420  1.00101.43           C  
ANISOU 1479  C   ASP A 196    17570  10240  10727  -2774   1027    136       C  
ATOM   1480  O   ASP A 196      18.786  82.448  47.564  1.00102.62           O  
ANISOU 1480  O   ASP A 196    17593  10468  10927  -2765    912     -5       O  
ATOM   1481  CB  ASP A 196      20.142  84.944  47.115  1.00110.49           C  
ANISOU 1481  CB  ASP A 196    18788  11117  12075  -3164   1244     21       C  
ATOM   1482  CG  ASP A 196      21.547  84.513  46.767  1.00111.92           C  
ANISOU 1482  CG  ASP A 196    18779  11474  12271  -3337   1310    -54       C  
ATOM   1483  OD1 ASP A 196      21.750  83.813  45.741  1.00113.25           O  
ANISOU 1483  OD1 ASP A 196    18897  11782  12350  -3283   1338     26       O  
ATOM   1484  OD2 ASP A 196      22.467  84.884  47.531  1.00113.25           O  
ANISOU 1484  OD2 ASP A 196    18842  11649  12540  -3531   1337   -204       O  
ATOM   1485  N   TYR A 197      18.259  82.254  45.368  1.00 91.69           N  
ANISOU 1485  N   TYR A 197    16354   9110   9374  -2641   1012    250       N  
ATOM   1486  CA  TYR A 197      17.933  80.833  45.440  1.00 86.25           C  
ANISOU 1486  CA  TYR A 197    15525   8627   8619  -2500    874    201       C  
ATOM   1487  C   TYR A 197      19.192  79.969  45.574  1.00 84.83           C  
ANISOU 1487  C   TYR A 197    15125   8639   8466  -2602    879     74       C  
ATOM   1488  O   TYR A 197      19.132  78.854  46.103  1.00 83.37           O  
ANISOU 1488  O   TYR A 197    14798   8601   8275  -2514    762    -12       O  
ATOM   1489  CB  TYR A 197      17.080  80.379  44.237  1.00 85.06           C  
ANISOU 1489  CB  TYR A 197    15459   8533   8325  -2343    861    345       C  
ATOM   1490  CG  TYR A 197      17.768  80.373  42.894  1.00 84.45           C  
ANISOU 1490  CG  TYR A 197    15397   8522   8166  -2415    991    427       C  
ATOM   1491  CD1 TYR A 197      18.489  79.263  42.456  1.00 83.76           C  
ANISOU 1491  CD1 TYR A 197    15152   8638   8034  -2431    991    357       C  
ATOM   1492  CD2 TYR A 197      17.698  81.482  42.053  1.00 87.45           C  
ANISOU 1492  CD2 TYR A 197    15957   8757   8510  -2459   1125    579       C  
ATOM   1493  CE1 TYR A 197      19.137  79.272  41.221  1.00 85.91           C  
ANISOU 1493  CE1 TYR A 197    15439   8977   8224  -2498   1122    427       C  
ATOM   1494  CE2 TYR A 197      18.346  81.508  40.824  1.00 88.91           C  
ANISOU 1494  CE2 TYR A 197    16162   9007   8610  -2528   1256    661       C  
ATOM   1495  CZ  TYR A 197      19.051  80.395  40.405  1.00 87.06           C  
ANISOU 1495  CZ  TYR A 197    15764   8986   8326  -2548   1253    581       C  
ATOM   1496  OH  TYR A 197      19.696  80.439  39.201  1.00 87.58           O  
ANISOU 1496  OH  TYR A 197    15852   9119   8303  -2617   1392    657       O  
HETATM 1497  N   MSE A 198      20.325  80.468  45.085  1.00 85.59           N  
ANISOU 1497  N   MSE A 198    15191   8733   8594  -2782   1021     68       N  
HETATM 1498  CA  MSE A 198      21.601  79.763  45.220  1.00 85.07           C  
ANISOU 1498  CA  MSE A 198    14904   8853   8565  -2887   1039    -51       C  
HETATM 1499  C   MSE A 198      22.058  79.671  46.646  1.00 82.33           C  
ANISOU 1499  C   MSE A 198    14411   8548   8320  -2948    949   -211       C  
HETATM 1500  O   MSE A 198      22.591  78.633  47.051  1.00 82.92           O  
ANISOU 1500  O   MSE A 198    14292   8812   8402  -2913    876   -307       O  
HETATM 1501  CB  MSE A 198      22.709  80.439  44.408  1.00 89.56           C  
ANISOU 1501  CB  MSE A 198    15469   9406   9152  -3082   1224    -21       C  
HETATM 1502  CG  MSE A 198      22.547  80.170  42.920  1.00 92.20           C  
ANISOU 1502  CG  MSE A 198    15885   9786   9359  -3019   1312    117       C  
HETATM 1503 SE   MSE A 198      22.793  78.240  42.594  1.00 95.86          SE  
ANISOU 1503 SE   MSE A 198    16137  10543   9740  -2872   1220     39      SE  
HETATM 1504  CE  MSE A 198      24.715  78.311  42.167  1.00100.96           C  
ANISOU 1504  CE  MSE A 198    16587  11324  10446  -3102   1399    -34       C  
ATOM   1505  N   SER A 199      21.852  80.727  47.428  1.00 79.50           N  
ANISOU 1505  N   SER A 199    14147   8021   8038  -3030    954   -244       N  
ATOM   1506  CA  SER A 199      22.265  80.689  48.820  1.00 79.02           C  
ANISOU 1506  CA  SER A 199    13952   8012   8057  -3094    864   -405       C  
ATOM   1507  C   SER A 199      21.329  79.839  49.677  1.00 76.69           C  
ANISOU 1507  C   SER A 199    13629   7777   7731  -2895    690   -436       C  
ATOM   1508  O   SER A 199      21.710  79.439  50.780  1.00 77.59           O  
ANISOU 1508  O   SER A 199    13597   8000   7883  -2907    595   -563       O  
ATOM   1509  CB  SER A 199      22.414  82.098  49.406  1.00 79.41           C  
ANISOU 1509  CB  SER A 199    14110   7862   8198  -3266    935   -455       C  
ATOM   1510  OG  SER A 199      21.171  82.745  49.448  1.00 78.46           O  
ANISOU 1510  OG  SER A 199    14213   7534   8064  -3157    925   -364       O  
ATOM   1511  N   ILE A 200      20.113  79.593  49.187  1.00 74.95           N  
ANISOU 1511  N   ILE A 200    13545   7492   7438  -2717    651   -319       N  
ATOM   1512  CA  ILE A 200      19.220  78.590  49.772  1.00 73.95           C  
ANISOU 1512  CA  ILE A 200    13379   7444   7272  -2523    501   -332       C  
ATOM   1513  C   ILE A 200      19.643  77.169  49.367  1.00 72.69           C  
ANISOU 1513  C   ILE A 200    13057   7495   7067  -2446    462   -350       C  
ATOM   1514  O   ILE A 200      19.620  76.253  50.194  1.00 73.19           O  
ANISOU 1514  O   ILE A 200    12995   7672   7138  -2362    354   -424       O  
ATOM   1515  CB  ILE A 200      17.743  78.855  49.418  1.00 74.23           C  
ANISOU 1515  CB  ILE A 200    13604   7347   7253  -2368    472   -209       C  
ATOM   1516  CG1 ILE A 200      17.296  80.182  50.027  1.00 78.06           C  
ANISOU 1516  CG1 ILE A 200    14242   7619   7797  -2418    503   -206       C  
ATOM   1517  CG2 ILE A 200      16.838  77.750  49.962  1.00 72.77           C  
ANISOU 1517  CG2 ILE A 200    13365   7254   7031  -2183    328   -225       C  
ATOM   1518  CD1 ILE A 200      16.000  80.734  49.458  1.00 79.17           C  
ANISOU 1518  CD1 ILE A 200    14582   7607   7889  -2285    516    -59       C  
ATOM   1519  N   ILE A 201      20.049  76.975  48.122  1.00 72.35           N  
ANISOU 1519  N   ILE A 201    13017   7499   6973  -2472    558   -284       N  
ATOM   1520  CA  ILE A 201      20.640  75.694  47.723  1.00 72.48           C  
ANISOU 1520  CA  ILE A 201    12874   7707   6958  -2420    548   -319       C  
ATOM   1521  C   ILE A 201      21.889  75.381  48.564  1.00 72.57           C  
ANISOU 1521  C   ILE A 201    12671   7853   7046  -2513    534   -448       C  
ATOM   1522  O   ILE A 201      22.049  74.265  49.055  1.00 70.98           O  
ANISOU 1522  O   ILE A 201    12330   7789   6847  -2413    452   -506       O  
ATOM   1523  CB  ILE A 201      20.907  75.632  46.188  1.00 73.87           C  
ANISOU 1523  CB  ILE A 201    13099   7910   7055  -2444    671   -231       C  
ATOM   1524  CG1 ILE A 201      19.565  75.524  45.459  1.00 72.70           C  
ANISOU 1524  CG1 ILE A 201    13119   7696   6808  -2301    637   -116       C  
ATOM   1525  CG2 ILE A 201      21.778  74.427  45.804  1.00 73.32           C  
ANISOU 1525  CG2 ILE A 201    12851   8034   6970  -2421    691   -290       C  
ATOM   1526  CD1 ILE A 201      19.619  75.870  43.994  1.00 74.83           C  
ANISOU 1526  CD1 ILE A 201    13495   7954   6982  -2332    758     -5       C  
ATOM   1527  N   ARG A 202      22.738  76.375  48.769  1.00 74.86           N  
ANISOU 1527  N   ARG A 202    12937   8106   7401  -2700    611   -493       N  
ATOM   1528  CA  ARG A 202      23.953  76.185  49.555  1.00 76.87           C  
ANISOU 1528  CA  ARG A 202    12974   8508   7723  -2804    595   -621       C  
ATOM   1529  C   ARG A 202      23.737  75.894  51.036  1.00 74.72           C  
ANISOU 1529  C   ARG A 202    12622   8285   7482  -2742    447   -714       C  
ATOM   1530  O   ARG A 202      24.447  75.077  51.629  1.00 71.98           O  
ANISOU 1530  O   ARG A 202    12075   8120   7152  -2711    385   -791       O  
ATOM   1531  CB  ARG A 202      24.879  77.367  49.346  1.00 82.93           C  
ANISOU 1531  CB  ARG A 202    13738   9220   8551  -3042    723   -651       C  
ATOM   1532  CG  ARG A 202      25.822  77.048  48.198  1.00 86.48           C  
ANISOU 1532  CG  ARG A 202    14094   9780   8982  -3106    853   -620       C  
ATOM   1533  CD  ARG A 202      26.712  78.181  47.716  1.00 89.73           C  
ANISOU 1533  CD  ARG A 202    14517  10130   9447  -3347   1014   -624       C  
ATOM   1534  NE  ARG A 202      26.035  79.477  47.825  1.00 91.96           N  
ANISOU 1534  NE  ARG A 202    15022  10165   9753  -3429   1055   -576       N  
ATOM   1535  CZ  ARG A 202      25.795  80.337  46.821  1.00 94.38           C  
ANISOU 1535  CZ  ARG A 202    15518  10304  10037  -3496   1197   -455       C  
ATOM   1536  NH1 ARG A 202      26.203  80.107  45.559  1.00 94.65           N  
ANISOU 1536  NH1 ARG A 202    15552  10396  10012  -3510   1320   -367       N  
ATOM   1537  NH2 ARG A 202      25.154  81.477  47.110  1.00 95.59           N  
ANISOU 1537  NH2 ARG A 202    15869  10224  10226  -3548   1223   -420       N  
HETATM 1538  N   MSE A 203      22.744  76.549  51.617  1.00 75.68           N  
ANISOU 1538  N   MSE A 203    12899   8248   7604  -2713    395   -700       N  
HETATM 1539  CA  MSE A 203      22.364  76.307  53.009  1.00 77.39           C  
ANISOU 1539  CA  MSE A 203    13071   8500   7834  -2640    258   -778       C  
HETATM 1540  C   MSE A 203      21.995  74.874  53.229  1.00 73.66           C  
ANISOU 1540  C   MSE A 203    12511   8157   7319  -2441    159   -761       C  
HETATM 1541  O   MSE A 203      22.515  74.251  54.124  1.00 72.30           O  
ANISOU 1541  O   MSE A 203    12177   8134   7158  -2409     79   -837       O  
HETATM 1542  CB  MSE A 203      21.185  77.212  53.314  1.00 81.52           C  
ANISOU 1542  CB  MSE A 203    13808   8810   8354  -2614    244   -739       C  
HETATM 1543  CG  MSE A 203      20.721  77.219  54.765  1.00 86.44           C  
ANISOU 1543  CG  MSE A 203    14418   9439   8985  -2561    124   -823       C  
HETATM 1544 SE   MSE A 203      19.332  78.666  54.868  1.00 94.21          SE  
ANISOU 1544 SE   MSE A 203    15699  10115   9982  -2555    163   -765      SE  
HETATM 1545  CE  MSE A 203      20.190  80.142  53.861  1.00 91.57           C  
ANISOU 1545  CE  MSE A 203    15465   9617   9709  -2805    357   -744       C  
ATOM   1546  N   TRP A 204      21.114  74.333  52.375  1.00 71.60           N  
ANISOU 1546  N   TRP A 204    12355   7843   7005  -2308    168   -659       N  
ATOM   1547  CA  TRP A 204      20.476  73.027  52.588  1.00 67.20           C  
ANISOU 1547  CA  TRP A 204    11759   7360   6412  -2117     79   -637       C  
ATOM   1548  C   TRP A 204      21.170  71.845  51.940  1.00 68.18           C  
ANISOU 1548  C   TRP A 204    11748   7632   6523  -2060    110   -637       C  
ATOM   1549  O   TRP A 204      20.941  70.716  52.371  1.00 69.19           O  
ANISOU 1549  O   TRP A 204    11806   7838   6645  -1919     39   -645       O  
ATOM   1550  CB  TRP A 204      19.012  73.079  52.127  1.00 64.99           C  
ANISOU 1550  CB  TRP A 204    11665   6945   6083  -2005     60   -543       C  
ATOM   1551  CG  TRP A 204      18.170  73.923  53.023  1.00 63.63           C  
ANISOU 1551  CG  TRP A 204    11604   6645   5926  -1999      5   -548       C  
ATOM   1552  CD1 TRP A 204      17.725  75.193  52.787  1.00 64.07           C  
ANISOU 1552  CD1 TRP A 204    11819   6534   5989  -2069     59   -508       C  
ATOM   1553  CD2 TRP A 204      17.695  73.566  54.319  1.00 61.82           C  
ANISOU 1553  CD2 TRP A 204    11340   6443   5706  -1913   -103   -598       C  
ATOM   1554  NE1 TRP A 204      17.004  75.650  53.865  1.00 63.34           N  
ANISOU 1554  NE1 TRP A 204    11790   6361   5915  -2031     -8   -539       N  
ATOM   1555  CE2 TRP A 204      16.965  74.663  54.815  1.00 62.49           C  
ANISOU 1555  CE2 TRP A 204    11564   6377   5802  -1938   -109   -595       C  
ATOM   1556  CE3 TRP A 204      17.817  72.424  55.114  1.00 60.95           C  
ANISOU 1556  CE3 TRP A 204    11099   6465   5592  -1810   -187   -638       C  
ATOM   1557  CZ2 TRP A 204      16.368  74.652  56.086  1.00 61.83           C  
ANISOU 1557  CZ2 TRP A 204    11486   6283   5720  -1870   -198   -642       C  
ATOM   1558  CZ3 TRP A 204      17.233  72.424  56.371  1.00 60.30           C  
ANISOU 1558  CZ3 TRP A 204    11026   6374   5509  -1745   -276   -672       C  
ATOM   1559  CH2 TRP A 204      16.519  73.531  56.842  1.00 59.71           C  
ANISOU 1559  CH2 TRP A 204    11086   6160   5440  -1779   -281   -678       C  
ATOM   1560  N   LEU A 205      21.960  72.066  50.887  1.00 68.96           N  
ANISOU 1560  N   LEU A 205    11821   7761   6619  -2158    225   -622       N  
ATOM   1561  CA  LEU A 205      22.635  70.952  50.183  1.00 69.77           C  
ANISOU 1561  CA  LEU A 205    11801   8000   6707  -2099    273   -626       C  
ATOM   1562  C   LEU A 205      24.154  70.938  50.254  1.00 71.61           C  
ANISOU 1562  C   LEU A 205    11833   8383   6989  -2205    332   -696       C  
ATOM   1563  O   LEU A 205      24.753  69.853  50.176  1.00 72.06           O  
ANISOU 1563  O   LEU A 205    11746   8579   7054  -2117    336   -721       O  
ATOM   1564  CB  LEU A 205      22.167  70.884  48.731  1.00 68.85           C  
ANISOU 1564  CB  LEU A 205    11813   7825   6521  -2081    361   -546       C  
ATOM   1565  CG  LEU A 205      20.739  70.324  48.655  1.00 68.33           C  
ANISOU 1565  CG  LEU A 205    11876   7683   6401  -1928    284   -493       C  
ATOM   1566  CD1 LEU A 205      19.788  71.257  47.944  1.00 68.70           C  
ANISOU 1566  CD1 LEU A 205    12122   7589   6390  -1955    311   -404       C  
ATOM   1567  CD2 LEU A 205      20.724  68.933  48.025  1.00 68.68           C  
ANISOU 1567  CD2 LEU A 205    11869   7816   6411  -1810    297   -501       C  
ATOM   1568  N   GLY A 206      24.761  72.107  50.436  1.00 73.11           N  
ANISOU 1568  N   GLY A 206    12011   8547   7218  -2387    379   -731       N  
ATOM   1569  CA  GLY A 206      26.207  72.223  50.596  1.00 77.22           C  
ANISOU 1569  CA  GLY A 206    12325   9222   7792  -2513    429   -808       C  
ATOM   1570  C   GLY A 206      26.769  73.273  49.676  1.00 80.79           C  
ANISOU 1570  C   GLY A 206    12826   9614   8256  -2709    577   -789       C  
ATOM   1571  O   GLY A 206      26.126  73.670  48.711  1.00 81.24           O  
ANISOU 1571  O   GLY A 206    13067   9535   8266  -2714    651   -699       O  
ATOM   1572  N   ASP A 207      27.987  73.702  49.972  1.00 86.37           N  
ANISOU 1572  N   ASP A 207    13359  10433   9022  -2870    621   -871       N  
ATOM   1573  CA  ASP A 207      28.572  74.884  49.320  1.00 91.31           C  
ANISOU 1573  CA  ASP A 207    14028  10986   9679  -3096    765   -867       C  
ATOM   1574  C   ASP A 207      28.835  74.778  47.820  1.00 89.75           C  
ANISOU 1574  C   ASP A 207    13877  10784   9438  -3116    923   -782       C  
ATOM   1575  O   ASP A 207      28.764  75.775  47.102  1.00 87.92           O  
ANISOU 1575  O   ASP A 207    13790  10414   9201  -3252   1042   -722       O  
ATOM   1576  CB  ASP A 207      29.850  75.342  50.039  1.00 96.56           C  
ANISOU 1576  CB  ASP A 207    14473  11792  10423  -3282    773   -991       C  
ATOM   1577  CG  ASP A 207      29.583  76.461  51.023  1.00101.77           C  
ANISOU 1577  CG  ASP A 207    15210  12331  11124  -3419    719  -1060       C  
ATOM   1578  OD1 ASP A 207      29.894  77.633  50.689  1.00109.08           O  
ANISOU 1578  OD1 ASP A 207    16212  13137  12094  -3633    836  -1070       O  
ATOM   1579  OD2 ASP A 207      29.043  76.170  52.118  1.00104.15           O  
ANISOU 1579  OD2 ASP A 207    15508  12648  11415  -3313    570  -1104       O  
ATOM   1580  N   ASP A 208      29.090  73.564  47.366  1.00 89.12           N  
ANISOU 1580  N   ASP A 208    13689  10847   9324  -2973    926   -774       N  
ATOM   1581  CA  ASP A 208      29.613  73.321  46.023  1.00 92.61           C  
ANISOU 1581  CA  ASP A 208    14119  11342   9724  -2997   1081   -725       C  
ATOM   1582  C   ASP A 208      28.540  72.788  45.052  1.00 90.40           C  
ANISOU 1582  C   ASP A 208    14035  10973   9339  -2841   1093   -625       C  
ATOM   1583  O   ASP A 208      28.869  72.270  43.983  1.00 92.39           O  
ANISOU 1583  O   ASP A 208    14271  11296   9536  -2811   1199   -596       O  
ATOM   1584  CB  ASP A 208      30.783  72.328  46.113  1.00 94.61           C  
ANISOU 1584  CB  ASP A 208    14098  11833  10014  -2950   1099   -800       C  
ATOM   1585  CG  ASP A 208      30.388  71.014  46.804  1.00 93.50           C  
ANISOU 1585  CG  ASP A 208    13885  11772   9867  -2717    959   -826       C  
ATOM   1586  OD1 ASP A 208      29.714  71.066  47.867  1.00 92.04           O  
ANISOU 1586  OD1 ASP A 208    13745  11529   9696  -2659    815   -843       O  
ATOM   1587  OD2 ASP A 208      30.761  69.940  46.293  1.00 95.05           O  
ANISOU 1587  OD2 ASP A 208    13986  12082  10046  -2593   1002   -829       O  
ATOM   1588  N   VAL A 209      27.264  72.944  45.411  1.00 86.79           N  
ANISOU 1588  N   VAL A 209    13756  10370   8850  -2751    987   -579       N  
ATOM   1589  CA  VAL A 209      26.145  72.407  44.649  1.00 83.61           C  
ANISOU 1589  CA  VAL A 209    13521   9899   8346  -2600    968   -498       C  
ATOM   1590  C   VAL A 209      25.618  73.455  43.664  1.00 81.73           C  
ANISOU 1590  C   VAL A 209    13497   9514   8039  -2681   1064   -385       C  
ATOM   1591  O   VAL A 209      25.454  74.618  44.012  1.00 80.57           O  
ANISOU 1591  O   VAL A 209    13446   9235   7932  -2793   1076   -358       O  
ATOM   1592  CB  VAL A 209      25.016  71.951  45.596  1.00 82.53           C  
ANISOU 1592  CB  VAL A 209    13444   9701   8213  -2448    800   -506       C  
ATOM   1593  CG1 VAL A 209      23.872  71.290  44.825  1.00 82.62           C  
ANISOU 1593  CG1 VAL A 209    13600   9666   8125  -2298    773   -439       C  
ATOM   1594  CG2 VAL A 209      25.557  70.975  46.634  1.00 82.80           C  
ANISOU 1594  CG2 VAL A 209    13274   9874   8312  -2364    709   -600       C  
ATOM   1595  N   LYS A 210      25.350  73.018  42.435  1.00 79.90           N  
ANISOU 1595  N   LYS A 210    13347   9310   7701  -2618   1136   -321       N  
ATOM   1596  CA  LYS A 210      24.845  73.884  41.377  1.00 80.58           C  
ANISOU 1596  CA  LYS A 210    13636   9285   7694  -2667   1228   -196       C  
ATOM   1597  C   LYS A 210      23.389  73.628  41.105  1.00 76.81           C  
ANISOU 1597  C   LYS A 210    13328   8734   7120  -2512   1131   -124       C  
ATOM   1598  O   LYS A 210      22.958  72.498  41.164  1.00 74.79           O  
ANISOU 1598  O   LYS A 210    13029   8555   6833  -2373   1047   -170       O  
ATOM   1599  CB  LYS A 210      25.622  73.608  40.071  1.00 83.32           C  
ANISOU 1599  CB  LYS A 210    13950   9744   7962  -2714   1389   -171       C  
ATOM   1600  CG  LYS A 210      27.068  74.001  40.133  1.00 87.14           C  
ANISOU 1600  CG  LYS A 210    14271  10304   8531  -2887   1516   -224       C  
ATOM   1601  CD  LYS A 210      27.846  73.647  38.838  1.00 91.45           C  
ANISOU 1601  CD  LYS A 210    14775  10976   8995  -2922   1685   -204       C  
ATOM   1602  CE  LYS A 210      28.695  72.355  38.956  1.00 93.35           C  
ANISOU 1602  CE  LYS A 210    14785  11411   9270  -2846   1688   -322       C  
ATOM   1603  NZ  LYS A 210      29.006  71.627  37.675  1.00 95.79           N  
ANISOU 1603  NZ  LYS A 210    15091  11837   9466  -2794   1814   -312       N  
ATOM   1604  N   SER A 211      22.669  74.678  40.713  1.00 75.57           N  
ANISOU 1604  N   SER A 211    13365   8433   6913  -2538   1156     -6       N  
ATOM   1605  CA  SER A 211      21.281  74.558  40.284  1.00 74.11           C  
ANISOU 1605  CA  SER A 211    13342   8194   6620  -2395   1075     80       C  
ATOM   1606  C   SER A 211      21.088  73.382  39.341  1.00 73.78           C  
ANISOU 1606  C   SER A 211    13279   8297   6458  -2290   1075     65       C  
ATOM   1607  O   SER A 211      21.925  73.130  38.468  1.00 74.90           O  
ANISOU 1607  O   SER A 211    13372   8538   6547  -2347   1198     58       O  
ATOM   1608  CB  SER A 211      20.823  75.844  39.578  1.00 75.65           C  
ANISOU 1608  CB  SER A 211    13740   8251   6750  -2442   1156    234       C  
ATOM   1609  OG  SER A 211      19.487  75.743  39.117  1.00 74.35           O  
ANISOU 1609  OG  SER A 211    13717   8060   6471  -2295   1074    325       O  
ATOM   1610  N   LYS A 212      19.966  72.686  39.501  1.00 72.54           N  
ANISOU 1610  N   LYS A 212    13161   8146   6253  -2144    944     56       N  
ATOM   1611  CA  LYS A 212      19.598  71.525  38.656  1.00 72.97           C  
ANISOU 1611  CA  LYS A 212    13210   8324   6192  -2043    929     25       C  
ATOM   1612  C   LYS A 212      20.563  70.346  38.743  1.00 70.33           C  
ANISOU 1612  C   LYS A 212    12699   8115   5904  -2038    966   -104       C  
ATOM   1613  O   LYS A 212      20.475  69.446  37.922  1.00 71.74           O  
ANISOU 1613  O   LYS A 212    12877   8391   5989  -1979    992   -141       O  
ATOM   1614  CB  LYS A 212      19.394  71.925  37.145  1.00 74.47           C  
ANISOU 1614  CB  LYS A 212    13537   8551   6205  -2057   1026    134       C  
ATOM   1615  CG  LYS A 212      18.358  73.023  36.854  1.00 76.75           C  
ANISOU 1615  CG  LYS A 212    14012   8730   6418  -2029    994    287       C  
ATOM   1616  CD  LYS A 212      16.910  72.621  37.012  1.00 78.18           C  
ANISOU 1616  CD  LYS A 212    14254   8907   6542  -1886    839    301       C  
ATOM   1617  CE  LYS A 212      15.928  73.816  36.907  1.00 80.33           C  
ANISOU 1617  CE  LYS A 212    14693   9060   6767  -1845    807    459       C  
ATOM   1618  NZ  LYS A 212      16.219  75.308  36.857  1.00 81.58           N  
ANISOU 1618  NZ  LYS A 212    14969   9070   6957  -1927    907    592       N  
ATOM   1619  N   ASP A 213      21.471  70.342  39.714  1.00 68.26           N  
ANISOU 1619  N   ASP A 213    12292   7859   5783  -2093    971   -176       N  
ATOM   1620  CA  ASP A 213      22.420  69.241  39.876  1.00 68.25           C  
ANISOU 1620  CA  ASP A 213    12112   7980   5838  -2068   1005   -288       C  
ATOM   1621  C   ASP A 213      22.246  68.475  41.223  1.00 66.33           C  
ANISOU 1621  C   ASP A 213    11758   7733   5709  -1975    874   -370       C  
ATOM   1622  O   ASP A 213      23.184  67.820  41.695  1.00 66.44           O  
ANISOU 1622  O   ASP A 213    11604   7835   5805  -1963    895   -450       O  
ATOM   1623  CB  ASP A 213      23.848  69.755  39.728  1.00 70.56           C  
ANISOU 1623  CB  ASP A 213    12290   8333   6186  -2207   1142   -303       C  
ATOM   1624  CG  ASP A 213      24.830  68.667  39.299  1.00 73.19           C  
ANISOU 1624  CG  ASP A 213    12469   8816   6523  -2174   1230   -391       C  
ATOM   1625  OD1 ASP A 213      25.964  68.685  39.822  1.00 75.74           O  
ANISOU 1625  OD1 ASP A 213    12618   9210   6949  -2236   1275   -446       O  
ATOM   1626  OD2 ASP A 213      24.499  67.806  38.434  1.00 75.33           O  
ANISOU 1626  OD2 ASP A 213    12786   9141   6695  -2087   1258   -410       O  
ATOM   1627  N   TYR A 214      21.051  68.550  41.822  1.00 63.16           N  
ANISOU 1627  N   TYR A 214    11449   7239   5308  -1902    746   -343       N  
ATOM   1628  CA  TYR A 214      20.774  67.872  43.082  1.00 61.35           C  
ANISOU 1628  CA  TYR A 214    11137   7001   5172  -1812    627   -404       C  
ATOM   1629  C   TYR A 214      19.401  67.194  43.080  1.00 59.77           C  
ANISOU 1629  C   TYR A 214    11031   6758   4921  -1688    527   -396       C  
ATOM   1630  O   TYR A 214      18.555  67.465  42.219  1.00 60.75           O  
ANISOU 1630  O   TYR A 214    11288   6853   4939  -1679    526   -337       O  
ATOM   1631  CB  TYR A 214      20.907  68.851  44.264  1.00 60.81           C  
ANISOU 1631  CB  TYR A 214    11047   6862   5196  -1879    569   -395       C  
ATOM   1632  CG  TYR A 214      19.967  70.021  44.198  1.00 60.12           C  
ANISOU 1632  CG  TYR A 214    11130   6643   5070  -1915    540   -306       C  
ATOM   1633  CD1 TYR A 214      18.730  69.989  44.850  1.00 58.06           C  
ANISOU 1633  CD1 TYR A 214    10947   6302   4810  -1821    420   -285       C  
ATOM   1634  CD2 TYR A 214      20.309  71.172  43.485  1.00 60.62           C  
ANISOU 1634  CD2 TYR A 214    11276   6655   5099  -2036    643   -236       C  
ATOM   1635  CE1 TYR A 214      17.842  71.068  44.769  1.00 58.12           C  
ANISOU 1635  CE1 TYR A 214    11109   6188   4784  -1834    399   -198       C  
ATOM   1636  CE2 TYR A 214      19.436  72.260  43.410  1.00 60.76           C  
ANISOU 1636  CE2 TYR A 214    11461   6537   5087  -2051    626   -142       C  
ATOM   1637  CZ  TYR A 214      18.197  72.204  44.041  1.00 59.45           C  
ANISOU 1637  CZ  TYR A 214    11368   6299   4921  -1943    502   -123       C  
ATOM   1638  OH  TYR A 214      17.323  73.274  43.933  1.00 58.78           O  
ANISOU 1638  OH  TYR A 214    11444   6082   4806  -1938    491    -24       O  
ATOM   1639  N   ILE A 215      19.196  66.312  44.047  1.00 58.22           N  
ANISOU 1639  N   ILE A 215    10757   6565   4798  -1596    444   -453       N  
ATOM   1640  CA  ILE A 215      17.952  65.571  44.175  1.00 58.12           C  
ANISOU 1640  CA  ILE A 215    10810   6512   4758  -1489    355   -458       C  
ATOM   1641  C   ILE A 215      17.299  65.877  45.516  1.00 57.26           C  
ANISOU 1641  C   ILE A 215    10705   6329   4721  -1451    239   -442       C  
ATOM   1642  O   ILE A 215      17.986  65.999  46.530  1.00 56.30           O  
ANISOU 1642  O   ILE A 215    10484   6220   4685  -1464    219   -469       O  
ATOM   1643  CB  ILE A 215      18.197  64.054  44.094  1.00 58.68           C  
ANISOU 1643  CB  ILE A 215    10800   6641   4853  -1399    376   -541       C  
ATOM   1644  CG1 ILE A 215      18.752  63.679  42.714  1.00 60.55           C  
ANISOU 1644  CG1 ILE A 215    11044   6952   5006  -1428    497   -570       C  
ATOM   1645  CG2 ILE A 215      16.905  63.290  44.344  1.00 57.88           C  
ANISOU 1645  CG2 ILE A 215    10761   6488   4741  -1307    288   -553       C  
ATOM   1646  CD1 ILE A 215      19.312  62.275  42.617  1.00 60.22           C  
ANISOU 1646  CD1 ILE A 215    10911   6963   5006  -1349    553   -661       C  
ATOM   1647  N   VAL A 216      15.970  66.013  45.506  1.00 56.37           N  
ANISOU 1647  N   VAL A 216    10700   6152   4563  -1403    163   -401       N  
ATOM   1648  CA  VAL A 216      15.182  66.126  46.724  1.00 55.22           C  
ANISOU 1648  CA  VAL A 216    10563   5941   4475  -1348     58   -391       C  
ATOM   1649  C   VAL A 216      14.440  64.799  46.863  1.00 55.90           C  
ANISOU 1649  C   VAL A 216    10634   6039   4567  -1246     12   -433       C  
ATOM   1650  O   VAL A 216      13.634  64.465  46.010  1.00 55.93           O  
ANISOU 1650  O   VAL A 216    10707   6049   4495  -1225      8   -427       O  
ATOM   1651  CB  VAL A 216      14.228  67.335  46.645  1.00 55.08           C  
ANISOU 1651  CB  VAL A 216    10674   5840   4414  -1368     18   -309       C  
ATOM   1652  CG1 VAL A 216      13.234  67.357  47.798  1.00 53.97           C  
ANISOU 1652  CG1 VAL A 216    10549   5636   4318  -1296    -84   -301       C  
ATOM   1653  CG2 VAL A 216      15.035  68.625  46.672  1.00 56.02           C  
ANISOU 1653  CG2 VAL A 216    10811   5920   4552  -1477     77   -275       C  
ATOM   1654  N   ALA A 217      14.726  64.046  47.927  1.00 56.80           N  
ANISOU 1654  N   ALA A 217    10655   6158   4766  -1187    -18   -474       N  
ATOM   1655  CA  ALA A 217      14.114  62.745  48.157  1.00 56.64           C  
ANISOU 1655  CA  ALA A 217    10619   6130   4769  -1095    -45   -512       C  
ATOM   1656  C   ALA A 217      13.160  62.787  49.340  1.00 57.28           C  
ANISOU 1656  C   ALA A 217    10718   6152   4891  -1038   -139   -486       C  
ATOM   1657  O   ALA A 217      13.567  63.057  50.460  1.00 58.72           O  
ANISOU 1657  O   ALA A 217    10845   6333   5130  -1024   -173   -480       O  
ATOM   1658  CB  ALA A 217      15.183  61.696  48.378  1.00 56.75           C  
ANISOU 1658  CB  ALA A 217    10521   6193   4846  -1049     11   -567       C  
ATOM   1659  N   LEU A 218      11.891  62.496  49.089  1.00 59.11           N  
ANISOU 1659  N   LEU A 218    11020   6349   5089  -1006   -181   -476       N  
ATOM   1660  CA  LEU A 218      10.858  62.570  50.110  1.00 61.37           C  
ANISOU 1660  CA  LEU A 218    11326   6584   5406   -955   -261   -448       C  
ATOM   1661  C   LEU A 218       9.899  61.417  49.903  1.00 63.56           C  
ANISOU 1661  C   LEU A 218    11616   6847   5684   -907   -272   -479       C  
ATOM   1662  O   LEU A 218       9.057  61.431  48.984  1.00 68.61           O  
ANISOU 1662  O   LEU A 218    12312   7498   6255   -928   -283   -481       O  
ATOM   1663  CB  LEU A 218      10.156  63.917  50.006  1.00 63.79           C  
ANISOU 1663  CB  LEU A 218    11714   6857   5664   -987   -304   -386       C  
ATOM   1664  CG  LEU A 218       8.965  64.296  50.871  1.00 66.78           C  
ANISOU 1664  CG  LEU A 218    12129   7184   6058   -938   -380   -349       C  
ATOM   1665  CD1 LEU A 218       9.246  64.166  52.363  1.00 69.61           C  
ANISOU 1665  CD1 LEU A 218    12432   7524   6490   -899   -410   -360       C  
ATOM   1666  CD2 LEU A 218       8.567  65.733  50.547  1.00 67.81           C  
ANISOU 1666  CD2 LEU A 218    12345   7278   6140   -969   -395   -285       C  
ATOM   1667  N   GLN A 219      10.055  60.393  50.736  1.00 64.72           N  
ANISOU 1667  N   GLN A 219    11708   6975   5907   -845   -266   -504       N  
ATOM   1668  CA  GLN A 219       9.270  59.171  50.626  1.00 63.03           C  
ANISOU 1668  CA  GLN A 219    11502   6728   5715   -810   -256   -543       C  
ATOM   1669  C   GLN A 219       8.608  58.853  51.970  1.00 59.43           C  
ANISOU 1669  C   GLN A 219    11031   6225   5324   -746   -302   -511       C  
ATOM   1670  O   GLN A 219       9.256  58.875  53.001  1.00 58.00           O  
ANISOU 1670  O   GLN A 219    10802   6043   5190   -700   -308   -485       O  
ATOM   1671  CB  GLN A 219      10.152  58.007  50.154  1.00 65.02           C  
ANISOU 1671  CB  GLN A 219    11716   6985   6002   -791   -167   -605       C  
ATOM   1672  CG  GLN A 219       9.356  57.006  49.321  1.00 68.11           C  
ANISOU 1672  CG  GLN A 219    12150   7352   6376   -807   -136   -673       C  
ATOM   1673  CD  GLN A 219      10.138  55.795  48.879  1.00 72.66           C  
ANISOU 1673  CD  GLN A 219    12703   7908   6994   -781    -35   -745       C  
ATOM   1674  OE1 GLN A 219       9.746  54.656  49.167  1.00 79.64           O  
ANISOU 1674  OE1 GLN A 219    13593   8721   7943   -744     -1   -782       O  
ATOM   1675  NE2 GLN A 219      11.291  56.022  48.267  1.00 73.56           N  
ANISOU 1675  NE2 GLN A 219    12788   8076   7083   -795     22   -762       N  
ATOM   1676  N   HIS A 220       7.314  58.562  51.923  1.00 56.61           N  
ANISOU 1676  N   HIS A 220    10709   5839   4959   -745   -333   -513       N  
ATOM   1677  CA  HIS A 220       6.527  58.269  53.081  1.00 56.76           C  
ANISOU 1677  CA  HIS A 220    10719   5815   5029   -694   -367   -481       C  
ATOM   1678  C   HIS A 220       6.106  56.827  53.093  1.00 56.40           C  
ANISOU 1678  C   HIS A 220    10668   5719   5041   -674   -318   -523       C  
ATOM   1679  O   HIS A 220       5.856  56.255  52.047  1.00 60.75           O  
ANISOU 1679  O   HIS A 220    11239   6271   5571   -721   -284   -587       O  
ATOM   1680  CB  HIS A 220       5.256  59.113  53.086  1.00 57.15           C  
ANISOU 1680  CB  HIS A 220    10805   5873   5034   -710   -435   -447       C  
ATOM   1681  CG  HIS A 220       5.510  60.573  52.994  1.00 57.08           C  
ANISOU 1681  CG  HIS A 220    10824   5889   4974   -730   -473   -404       C  
ATOM   1682  ND1 HIS A 220       6.431  61.210  53.794  1.00 57.32           N  
ANISOU 1682  ND1 HIS A 220    10836   5916   5024   -718   -476   -380       N  
ATOM   1683  CD2 HIS A 220       4.991  61.520  52.185  1.00 56.54           C  
ANISOU 1683  CD2 HIS A 220    10802   5845   4833   -762   -504   -379       C  
ATOM   1684  CE1 HIS A 220       6.476  62.491  53.483  1.00 56.91           C  
ANISOU 1684  CE1 HIS A 220    10826   5868   4926   -753   -497   -351       C  
ATOM   1685  NE2 HIS A 220       5.603  62.704  52.514  1.00 58.64           N  
ANISOU 1685  NE2 HIS A 220    11090   6100   5089   -771   -513   -340       N  
ATOM   1686  N   PRO A 221       5.953  56.251  54.293  1.00 56.77           N  
ANISOU 1686  N   PRO A 221    10695   5718   5156   -609   -311   -488       N  
ATOM   1687  CA  PRO A 221       5.466  54.892  54.369  1.00 56.84           C  
ANISOU 1687  CA  PRO A 221    10710   5655   5231   -595   -251   -519       C  
ATOM   1688  C   PRO A 221       3.989  54.867  54.011  1.00 57.44           C  
ANISOU 1688  C   PRO A 221    10808   5727   5288   -654   -283   -544       C  
ATOM   1689  O   PRO A 221       3.284  55.842  54.243  1.00 54.69           O  
ANISOU 1689  O   PRO A 221    10461   5421   4895   -662   -354   -504       O  
ATOM   1690  CB  PRO A 221       5.695  54.524  55.836  1.00 57.06           C  
ANISOU 1690  CB  PRO A 221    10714   5646   5320   -503   -242   -448       C  
ATOM   1691  CG  PRO A 221       5.547  55.835  56.562  1.00 56.91           C  
ANISOU 1691  CG  PRO A 221    10687   5685   5251   -494   -326   -393       C  
ATOM   1692  CD  PRO A 221       6.153  56.851  55.638  1.00 55.92           C  
ANISOU 1692  CD  PRO A 221    10564   5620   5060   -551   -354   -419       C  
ATOM   1693  N   VAL A 222       3.546  53.749  53.445  1.00 61.32           N  
ANISOU 1693  N   VAL A 222    11313   6170   5815   -696   -225   -614       N  
ATOM   1694  CA  VAL A 222       2.126  53.459  53.223  1.00 63.52           C  
ANISOU 1694  CA  VAL A 222    11593   6446   6093   -759   -245   -650       C  
ATOM   1695  C   VAL A 222       1.733  52.516  54.352  1.00 65.57           C  
ANISOU 1695  C   VAL A 222    11849   6609   6454   -718   -190   -617       C  
ATOM   1696  O   VAL A 222       2.368  51.484  54.540  1.00 66.87           O  
ANISOU 1696  O   VAL A 222    12030   6685   6690   -685   -102   -631       O  
ATOM   1697  CB  VAL A 222       1.895  52.774  51.866  1.00 65.50           C  
ANISOU 1697  CB  VAL A 222    11862   6707   6317   -850   -209   -767       C  
ATOM   1698  CG1 VAL A 222       0.422  52.473  51.651  1.00 66.76           C  
ANISOU 1698  CG1 VAL A 222    12004   6886   6474   -927   -238   -814       C  
ATOM   1699  CG2 VAL A 222       2.417  53.659  50.739  1.00 65.33           C  
ANISOU 1699  CG2 VAL A 222    11853   6785   6184   -880   -250   -788       C  
ATOM   1700  N   THR A 223       0.690  52.879  55.089  1.00 68.42           N  
ANISOU 1700  N   THR A 223    12190   6985   6819   -715   -235   -568       N  
ATOM   1701  CA  THR A 223       0.377  52.257  56.387  1.00 71.36           C  
ANISOU 1701  CA  THR A 223    12560   7281   7272   -660   -188   -504       C  
ATOM   1702  C   THR A 223      -0.156  50.832  56.203  1.00 78.83           C  
ANISOU 1702  C   THR A 223    13522   8124   8305   -716    -92   -564       C  
ATOM   1703  O   THR A 223       0.018  49.962  57.073  1.00 81.81           O  
ANISOU 1703  O   THR A 223    13919   8400   8764   -663    -11   -515       O  
ATOM   1704  CB  THR A 223      -0.666  53.088  57.166  1.00 70.71           C  
ANISOU 1704  CB  THR A 223    12450   7251   7162   -646   -254   -442       C  
ATOM   1705  OG1 THR A 223      -1.926  53.072  56.481  1.00 70.47           O  
ANISOU 1705  OG1 THR A 223    12392   7264   7119   -734   -280   -500       O  
ATOM   1706  CG2 THR A 223      -0.193  54.564  57.338  1.00 67.69           C  
ANISOU 1706  CG2 THR A 223    12066   6952   6699   -598   -340   -393       C  
ATOM   1707  N   THR A 224      -0.777  50.612  55.037  1.00 80.07           N  
ANISOU 1707  N   THR A 224    13674   8310   8439   -826    -99   -670       N  
ATOM   1708  CA  THR A 224      -1.378  49.339  54.653  1.00 78.98           C  
ANISOU 1708  CA  THR A 224    13549   8082   8375   -916    -12   -762       C  
ATOM   1709  C   THR A 224      -0.338  48.257  54.445  1.00 78.30           C  
ANISOU 1709  C   THR A 224    13519   7871   8358   -888    101   -801       C  
ATOM   1710  O   THR A 224      -0.637  47.092  54.678  1.00 82.10           O  
ANISOU 1710  O   THR A 224    14032   8222   8940   -918    205   -831       O  
ATOM   1711  CB  THR A 224      -2.236  49.470  53.360  1.00 81.76           C  
ANISOU 1711  CB  THR A 224    13873   8530   8659  -1046    -65   -883       C  
ATOM   1712  OG1 THR A 224      -1.392  49.523  52.210  1.00 80.93           O  
ANISOU 1712  OG1 THR A 224    13799   8460   8491  -1067    -64   -959       O  
ATOM   1713  CG2 THR A 224      -3.120  50.744  53.357  1.00 82.02           C  
ANISOU 1713  CG2 THR A 224    13846   8713   8603  -1048   -191   -836       C  
ATOM   1714  N   ASP A 225       0.869  48.630  54.009  1.00 77.15           N  
ANISOU 1714  N   ASP A 225    13387   7760   8167   -831     91   -799       N  
ATOM   1715  CA  ASP A 225       1.946  47.662  53.714  1.00 80.34           C  
ANISOU 1715  CA  ASP A 225    13834   8059   8632   -789    201   -839       C  
ATOM   1716  C   ASP A 225       3.320  48.226  54.142  1.00 77.62           C  
ANISOU 1716  C   ASP A 225    13473   7756   8263   -661    183   -750       C  
ATOM   1717  O   ASP A 225       4.150  48.616  53.313  1.00 80.24           O  
ANISOU 1717  O   ASP A 225    13799   8151   8536   -663    171   -794       O  
ATOM   1718  CB  ASP A 225       1.944  47.274  52.209  1.00 83.29           C  
ANISOU 1718  CB  ASP A 225    14232   8445   8966   -897    231   -996       C  
ATOM   1719  CG  ASP A 225       2.707  45.950  51.924  1.00 87.86           C  
ANISOU 1719  CG  ASP A 225    14869   8873   9639   -872    381  -1065       C  
ATOM   1720  OD1 ASP A 225       2.622  45.307  50.832  1.00 92.44           O  
ANISOU 1720  OD1 ASP A 225    15487   9422  10214   -965    441  -1211       O  
ATOM   1721  OD2 ASP A 225       3.439  45.550  52.822  1.00 88.51           O  
ANISOU 1721  OD2 ASP A 225    14962   8867   9798   -748    442   -969       O  
ATOM   1722  N   ILE A 226       3.566  48.240  55.442  1.00 76.89           N  
ANISOU 1722  N   ILE A 226    13368   7635   8211   -555    185   -629       N  
ATOM   1723  CA  ILE A 226       4.836  48.732  55.972  1.00 77.72           C  
ANISOU 1723  CA  ILE A 226    13441   7794   8293   -439    161   -549       C  
ATOM   1724  C   ILE A 226       6.034  47.905  55.509  1.00 79.61           C  
ANISOU 1724  C   ILE A 226    13691   7974   8582   -376    259   -582       C  
ATOM   1725  O   ILE A 226       7.029  48.501  55.079  1.00 77.40           O  
ANISOU 1725  O   ILE A 226    13374   7783   8249   -352    230   -591       O  
ATOM   1726  CB  ILE A 226       4.811  48.935  57.524  1.00 78.86           C  
ANISOU 1726  CB  ILE A 226    13566   7944   8452   -336    133   -414       C  
ATOM   1727  CG1 ILE A 226       3.965  50.179  57.849  1.00 77.89           C  
ANISOU 1727  CG1 ILE A 226    13419   7922   8251   -385     18   -388       C  
ATOM   1728  CG2 ILE A 226       6.222  49.100  58.107  1.00 78.18           C  
ANISOU 1728  CG2 ILE A 226    13440   7908   8357   -209    127   -341       C  
ATOM   1729  CD1 ILE A 226       3.634  50.423  59.311  1.00 80.93           C  
ANISOU 1729  CD1 ILE A 226    13794   8320   8636   -310     -9   -278       C  
ATOM   1730  N   LYS A 227       5.957  46.567  55.520  1.00 84.10           N  
ANISOU 1730  N   LYS A 227    14310   8392   9252   -354    383   -606       N  
ATOM   1731  CA  LYS A 227       7.167  45.805  55.103  1.00 85.08           C  
ANISOU 1731  CA  LYS A 227    14443   8457   9427   -270    484   -633       C  
ATOM   1732  C   LYS A 227       7.582  46.101  53.650  1.00 79.42           C  
ANISOU 1732  C   LYS A 227    13723   7805   8646   -353    485   -762       C  
ATOM   1733  O   LYS A 227       8.774  46.084  53.343  1.00 75.06           O  
ANISOU 1733  O   LYS A 227    13140   7287   8090   -280    521   -765       O  
ATOM   1734  CB  LYS A 227       7.324  44.336  55.510  1.00 91.35           C  
ANISOU 1734  CB  LYS A 227    15294   9063  10349   -185    634   -609       C  
ATOM   1735  CG  LYS A 227       6.198  43.355  55.385  1.00 96.30           C  
ANISOU 1735  CG  LYS A 227    16001   9528  11059   -277    724   -671       C  
ATOM   1736  CD  LYS A 227       6.907  41.998  55.369  1.00102.47           C  
ANISOU 1736  CD  LYS A 227    16844  10128  11962   -175    892   -674       C  
ATOM   1737  CE  LYS A 227       6.058  40.874  55.943  1.00106.78           C  
ANISOU 1737  CE  LYS A 227    17472  10470  12628   -191   1010   -649       C  
ATOM   1738  NZ  LYS A 227       6.857  39.955  56.798  1.00109.41           N  
ANISOU 1738  NZ  LYS A 227    17840  10667  13061      0   1129   -519       N  
ATOM   1739  N   HIS A 228       6.611  46.406  52.790  1.00 77.98           N  
ANISOU 1739  N   HIS A 228    13564   7657   8405   -500    443   -861       N  
ATOM   1740  CA  HIS A 228       6.900  46.803  51.401  1.00 78.83           C  
ANISOU 1740  CA  HIS A 228    13673   7852   8424   -584    431   -975       C  
ATOM   1741  C   HIS A 228       7.446  48.236  51.338  1.00 73.10           C  
ANISOU 1741  C   HIS A 228    12889   7291   7593   -575    320   -916       C  
ATOM   1742  O   HIS A 228       8.388  48.506  50.584  1.00 76.40           O  
ANISOU 1742  O   HIS A 228    13289   7773   7964   -568    342   -953       O  
ATOM   1743  CB  HIS A 228       5.667  46.613  50.506  1.00 80.45           C  
ANISOU 1743  CB  HIS A 228    13919   8058   8591   -739    418  -1099       C  
ATOM   1744  CG  HIS A 228       5.932  46.809  49.046  1.00 84.61           C  
ANISOU 1744  CG  HIS A 228    14460   8666   9019   -822    423  -1224       C  
ATOM   1745  ND1 HIS A 228       5.042  47.486  48.239  1.00 86.27           N  
ANISOU 1745  ND1 HIS A 228    14667   8995   9114   -941    330  -1283       N  
ATOM   1746  CD2 HIS A 228       6.971  46.459  48.249  1.00 88.47           C  
ANISOU 1746  CD2 HIS A 228    14965   9152   9496   -796    508  -1294       C  
ATOM   1747  CE1 HIS A 228       5.507  47.537  47.005  1.00 87.96           C  
ANISOU 1747  CE1 HIS A 228    14901   9276   9241   -990    357  -1383       C  
ATOM   1748  NE2 HIS A 228       6.677  46.922  46.982  1.00 91.38           N  
ANISOU 1748  NE2 HIS A 228    15347   9635   9737   -907    468  -1396       N  
ATOM   1749  N   SER A 229       6.879  49.140  52.128  1.00 66.12           N  
ANISOU 1749  N   SER A 229    11977   6468   6676   -575    214   -826       N  
ATOM   1750  CA  SER A 229       7.434  50.482  52.252  1.00 64.15           C  
ANISOU 1750  CA  SER A 229    11680   6346   6345   -561    122   -764       C  
ATOM   1751  C   SER A 229       8.914  50.484  52.647  1.00 63.92           C  
ANISOU 1751  C   SER A 229    11599   6342   6344   -456    157   -714       C  
ATOM   1752  O   SER A 229       9.693  51.305  52.152  1.00 65.69           O  
ANISOU 1752  O   SER A 229    11789   6664   6506   -474    131   -719       O  
ATOM   1753  CB  SER A 229       6.642  51.303  53.265  1.00 63.25           C  
ANISOU 1753  CB  SER A 229    11551   6265   6213   -555     23   -675       C  
ATOM   1754  OG  SER A 229       5.323  51.530  52.802  1.00 63.23           O  
ANISOU 1754  OG  SER A 229    11575   6278   6171   -649    -23   -716       O  
ATOM   1755  N   ILE A 230       9.280  49.582  53.558  1.00 65.03           N  
ANISOU 1755  N   ILE A 230    11729   6401   6576   -347    218   -660       N  
ATOM   1756  CA  ILE A 230      10.668  49.416  54.033  1.00 65.21           C  
ANISOU 1756  CA  ILE A 230    11687   6457   6633   -225    253   -606       C  
ATOM   1757  C   ILE A 230      11.548  49.001  52.875  1.00 66.01           C  
ANISOU 1757  C   ILE A 230    11781   6561   6736   -230    343   -694       C  
ATOM   1758  O   ILE A 230      12.611  49.601  52.662  1.00 67.43           O  
ANISOU 1758  O   ILE A 230    11892   6848   6880   -210    331   -686       O  
ATOM   1759  CB  ILE A 230      10.829  48.327  55.167  1.00 64.38           C  
ANISOU 1759  CB  ILE A 230    11582   6250   6627    -85    317   -522       C  
ATOM   1760  CG1 ILE A 230      10.041  48.643  56.439  1.00 62.62           C  
ANISOU 1760  CG1 ILE A 230    11364   6029   6399    -63    243   -424       C  
ATOM   1761  CG2 ILE A 230      12.285  48.120  55.580  1.00 64.90           C  
ANISOU 1761  CG2 ILE A 230    11565   6373   6720     53    349   -464       C  
ATOM   1762  CD1 ILE A 230      10.387  49.952  57.071  1.00 62.98           C  
ANISOU 1762  CD1 ILE A 230    11343   6220   6364    -61    123   -367       C  
ATOM   1763  N   LYS A 231      11.120  47.957  52.166  1.00 67.79           N  
ANISOU 1763  N   LYS A 231    12078   6671   7007   -260    440   -783       N  
ATOM   1764  CA  LYS A 231      11.932  47.363  51.112  1.00 68.44           C  
ANISOU 1764  CA  LYS A 231    12166   6736   7100   -250    550   -878       C  
ATOM   1765  C   LYS A 231      12.137  48.358  49.989  1.00 66.15           C  
ANISOU 1765  C   LYS A 231    11863   6578   6693   -358    506   -943       C  
ATOM   1766  O   LYS A 231      13.244  48.502  49.471  1.00 65.49           O  
ANISOU 1766  O   LYS A 231    11730   6563   6591   -328    554   -964       O  
ATOM   1767  CB  LYS A 231      11.303  46.054  50.620  1.00 71.67           C  
ANISOU 1767  CB  LYS A 231    12669   6982   7580   -277    665   -976       C  
ATOM   1768  CG  LYS A 231      12.145  45.272  49.603  1.00 76.56           C  
ANISOU 1768  CG  LYS A 231    13307   7557   8223   -250    802  -1085       C  
ATOM   1769  CD  LYS A 231      13.435  44.707  50.217  1.00 79.77           C  
ANISOU 1769  CD  LYS A 231    13653   7934   8720    -66    886  -1007       C  
ATOM   1770  CE  LYS A 231      14.583  44.566  49.210  1.00 80.41           C  
ANISOU 1770  CE  LYS A 231    13701   8068   8783    -34    980  -1088       C  
ATOM   1771  NZ  LYS A 231      14.792  43.169  48.757  1.00 79.82           N  
ANISOU 1771  NZ  LYS A 231    13697   7823   8806     29   1153  -1178       N  
HETATM 1772  N   MSE A 232      11.080  49.078  49.641  1.00 64.85           N  
ANISOU 1772  N   MSE A 232    11736   6455   6446   -478    417   -964       N  
HETATM 1773  CA  MSE A 232      11.162  50.054  48.570  1.00 66.50           C  
ANISOU 1773  CA  MSE A 232    11947   6785   6534   -576    374  -1008       C  
HETATM 1774  C   MSE A 232      12.124  51.155  48.895  1.00 64.24           C  
ANISOU 1774  C   MSE A 232    11585   6611   6213   -548    324   -927       C  
HETATM 1775  O   MSE A 232      12.881  51.606  48.031  1.00 65.13           O  
ANISOU 1775  O   MSE A 232    11677   6805   6263   -583    356   -960       O  
HETATM 1776  CB  MSE A 232       9.804  50.688  48.314  1.00 69.78           C  
ANISOU 1776  CB  MSE A 232    12407   7232   6871   -683    275  -1016       C  
HETATM 1777  CG  MSE A 232       9.837  51.512  47.022  1.00 73.09           C  
ANISOU 1777  CG  MSE A 232    12847   7767   7156   -777    251  -1065       C  
HETATM 1778 SE   MSE A 232       7.994  52.010  46.571  1.00 78.19          SE  
ANISOU 1778 SE   MSE A 232    13546   8456   7705   -892    136  -1088      SE  
HETATM 1779  CE  MSE A 232       7.438  50.241  45.870  1.00 81.41           C  
ANISOU 1779  CE  MSE A 232    14009   8759   8161   -945    245  -1260       C  
ATOM   1780  N   PHE A 233      12.073  51.614  50.137  1.00 61.48           N  
ANISOU 1780  N   PHE A 233    11193   6268   5897   -496    249   -825       N  
ATOM   1781  CA  PHE A 233      12.912  52.699  50.602  1.00 60.56           C  
ANISOU 1781  CA  PHE A 233    11002   6255   5752   -484    192   -756       C  
ATOM   1782  C   PHE A 233      14.395  52.292  50.622  1.00 61.33           C  
ANISOU 1782  C   PHE A 233    11012   6395   5896   -400    271   -757       C  
ATOM   1783  O   PHE A 233      15.245  53.066  50.191  1.00 61.72           O  
ANISOU 1783  O   PHE A 233    11006   6543   5899   -438    273   -760       O  
ATOM   1784  CB  PHE A 233      12.401  53.174  51.970  1.00 60.00           C  
ANISOU 1784  CB  PHE A 233    10916   6179   5702   -449     96   -665       C  
ATOM   1785  CG  PHE A 233      12.963  54.500  52.436  1.00 58.76           C  
ANISOU 1785  CG  PHE A 233    10702   6123   5500   -474     19   -612       C  
ATOM   1786  CD1 PHE A 233      13.195  55.546  51.557  1.00 59.30           C  
ANISOU 1786  CD1 PHE A 233    10780   6259   5492   -572      5   -634       C  
ATOM   1787  CD2 PHE A 233      13.205  54.711  53.773  1.00 58.25           C  
ANISOU 1787  CD2 PHE A 233    10583   6082   5465   -406    -35   -541       C  
ATOM   1788  CE1 PHE A 233      13.699  56.759  51.996  1.00 58.65           C  
ANISOU 1788  CE1 PHE A 233    10655   6248   5380   -608    -52   -592       C  
ATOM   1789  CE2 PHE A 233      13.701  55.923  54.222  1.00 58.53           C  
ANISOU 1789  CE2 PHE A 233    10571   6207   5462   -444   -103   -512       C  
ATOM   1790  CZ  PHE A 233      13.944  56.948  53.331  1.00 58.65           C  
ANISOU 1790  CZ  PHE A 233    10599   6270   5416   -550   -108   -540       C  
ATOM   1791  N   GLU A 234      14.693  51.073  51.064  1.00 62.96           N  
ANISOU 1791  N   GLU A 234    11204   6522   6194   -285    346   -753       N  
ATOM   1792  CA  GLU A 234      16.051  50.511  50.973  1.00 64.76           C  
ANISOU 1792  CA  GLU A 234    11347   6785   6473   -184    438   -759       C  
ATOM   1793  C   GLU A 234      16.584  50.583  49.538  1.00 65.31           C  
ANISOU 1793  C   GLU A 234    11424   6900   6492   -252    520   -855       C  
ATOM   1794  O   GLU A 234      17.689  51.088  49.293  1.00 67.58           O  
ANISOU 1794  O   GLU A 234    11618   7299   6759   -248    541   -850       O  
ATOM   1795  CB  GLU A 234      16.081  49.051  51.441  1.00 67.08           C  
ANISOU 1795  CB  GLU A 234    11660   6950   6875    -48    529   -747       C  
ATOM   1796  CG  GLU A 234      16.002  48.837  52.942  1.00 68.69           C  
ANISOU 1796  CG  GLU A 234    11829   7135   7133     65    475   -630       C  
ATOM   1797  CD  GLU A 234      15.751  47.384  53.354  1.00 72.97           C  
ANISOU 1797  CD  GLU A 234    12428   7515   7781    185    574   -608       C  
ATOM   1798  OE1 GLU A 234      15.654  46.478  52.461  1.00 77.91           O  
ANISOU 1798  OE1 GLU A 234    13124   8027   8451    178    694   -700       O  
ATOM   1799  OE2 GLU A 234      15.632  47.144  54.582  1.00 71.44           O  
ANISOU 1799  OE2 GLU A 234    12218   7301   7625    286    539   -500       O  
ATOM   1800  N   LEU A 235      15.783  50.106  48.594  1.00 62.89           N  
ANISOU 1800  N   LEU A 235    11222   6517   6156   -323    567   -946       N  
ATOM   1801  CA  LEU A 235      16.196  50.090  47.199  1.00 62.79           C  
ANISOU 1801  CA  LEU A 235    11230   6548   6077   -387    651  -1045       C  
ATOM   1802  C   LEU A 235      16.350  51.508  46.663  1.00 61.51           C  
ANISOU 1802  C   LEU A 235    11049   6519   5801   -499    584  -1025       C  
ATOM   1803  O   LEU A 235      17.297  51.800  45.905  1.00 62.50           O  
ANISOU 1803  O   LEU A 235    11129   6731   5885   -519    651  -1055       O  
ATOM   1804  CB  LEU A 235      15.202  49.307  46.342  1.00 62.79           C  
ANISOU 1804  CB  LEU A 235    11350   6452   6054   -452    701  -1157       C  
ATOM   1805  CG  LEU A 235      15.085  47.820  46.692  1.00 63.00           C  
ANISOU 1805  CG  LEU A 235    11415   6318   6201   -356    801  -1197       C  
ATOM   1806  CD1 LEU A 235      13.794  47.245  46.140  1.00 62.86           C  
ANISOU 1806  CD1 LEU A 235    11513   6206   6164   -455    809  -1297       C  
ATOM   1807  CD2 LEU A 235      16.300  47.060  46.204  1.00 64.13           C  
ANISOU 1807  CD2 LEU A 235    11520   6450   6394   -261    949  -1251       C  
ATOM   1808  N   THR A 236      15.432  52.381  47.053  1.00 59.02           N  
ANISOU 1808  N   THR A 236    10771   6213   5438   -568    464   -970       N  
ATOM   1809  CA  THR A 236      15.519  53.785  46.660  1.00 58.80           C  
ANISOU 1809  CA  THR A 236    10738   6286   5314   -666    403   -933       C  
ATOM   1810  C   THR A 236      16.823  54.423  47.129  1.00 58.27           C  
ANISOU 1810  C   THR A 236    10554   6309   5275   -641    410   -880       C  
ATOM   1811  O   THR A 236      17.478  55.136  46.382  1.00 57.74           O  
ANISOU 1811  O   THR A 236    10465   6327   5146   -710    446   -889       O  
ATOM   1812  CB  THR A 236      14.342  54.598  47.221  1.00 58.08           C  
ANISOU 1812  CB  THR A 236    10700   6177   5190   -716    276   -872       C  
ATOM   1813  OG1 THR A 236      13.096  53.967  46.883  1.00 56.71           O  
ANISOU 1813  OG1 THR A 236    10612   5934   4999   -740    262   -922       O  
ATOM   1814  CG2 THR A 236      14.355  56.038  46.661  1.00 59.02           C  
ANISOU 1814  CG2 THR A 236    10839   6377   5207   -815    229   -833       C  
ATOM   1815  N   LEU A 237      17.208  54.168  48.366  1.00 59.44           N  
ANISOU 1815  N   LEU A 237    10623   6448   5510   -547    378   -826       N  
ATOM   1816  CA  LEU A 237      18.448  54.741  48.877  1.00 61.62           C  
ANISOU 1816  CA  LEU A 237    10769   6830   5811   -528    375   -785       C  
ATOM   1817  C   LEU A 237      19.651  54.132  48.160  1.00 65.83           C  
ANISOU 1817  C   LEU A 237    11223   7420   6368   -482    502   -837       C  
ATOM   1818  O   LEU A 237      20.520  54.873  47.681  1.00 66.24           O  
ANISOU 1818  O   LEU A 237    11207   7577   6385   -548    533   -843       O  
ATOM   1819  CB  LEU A 237      18.545  54.600  50.394  1.00 61.22           C  
ANISOU 1819  CB  LEU A 237    10649   6780   5829   -432    300   -715       C  
ATOM   1820  CG  LEU A 237      17.495  55.450  51.126  1.00 59.21           C  
ANISOU 1820  CG  LEU A 237    10459   6494   5541   -489    178   -666       C  
ATOM   1821  CD1 LEU A 237      17.389  55.048  52.576  1.00 59.45           C  
ANISOU 1821  CD1 LEU A 237    10447   6510   5629   -382    117   -603       C  
ATOM   1822  CD2 LEU A 237      17.796  56.930  51.023  1.00 59.86           C  
ANISOU 1822  CD2 LEU A 237    10521   6655   5565   -608    127   -651       C  
ATOM   1823  N   ASP A 238      19.661  52.805  48.008  1.00 68.76           N  
ANISOU 1823  N   ASP A 238    11612   7714   6798   -377    587   -879       N  
ATOM   1824  CA  ASP A 238      20.719  52.149  47.232  1.00 71.87           C  
ANISOU 1824  CA  ASP A 238    11944   8147   7215   -322    725   -939       C  
ATOM   1825  C   ASP A 238      20.921  52.792  45.854  1.00 71.13           C  
ANISOU 1825  C   ASP A 238    11886   8122   7018   -450    784  -1000       C  
ATOM   1826  O   ASP A 238      22.065  53.065  45.464  1.00 73.55           O  
ANISOU 1826  O   ASP A 238    12088   8536   7319   -455    856  -1010       O  
ATOM   1827  CB  ASP A 238      20.442  50.658  47.076  1.00 75.73           C  
ANISOU 1827  CB  ASP A 238    12495   8504   7772   -213    820   -993       C  
ATOM   1828  CG  ASP A 238      20.565  49.886  48.400  1.00 79.41           C  
ANISOU 1828  CG  ASP A 238    12909   8911   8350    -53    799   -917       C  
ATOM   1829  OD1 ASP A 238      21.412  50.255  49.264  1.00 81.19           O  
ANISOU 1829  OD1 ASP A 238    12998   9242   8607     14    752   -840       O  
ATOM   1830  OD2 ASP A 238      19.817  48.884  48.563  1.00 81.26           O  
ANISOU 1830  OD2 ASP A 238    13239   8995   8638      2    834   -934       O  
ATOM   1831  N   ALA A 239      19.824  53.071  45.151  1.00 68.46           N  
ANISOU 1831  N   ALA A 239    11685   7736   6591   -553    752  -1033       N  
ATOM   1832  CA  ALA A 239      19.874  53.772  43.854  1.00 68.38           C  
ANISOU 1832  CA  ALA A 239    11726   7797   6458   -675    795  -1073       C  
ATOM   1833  C   ALA A 239      20.490  55.160  43.989  1.00 68.52           C  
ANISOU 1833  C   ALA A 239    11673   7920   6439   -760    754  -1001       C  
ATOM   1834  O   ALA A 239      21.365  55.553  43.207  1.00 67.92           O  
ANISOU 1834  O   ALA A 239    11552   7936   6319   -811    841  -1019       O  
ATOM   1835  CB  ALA A 239      18.479  53.893  43.251  1.00 67.29           C  
ANISOU 1835  CB  ALA A 239    11736   7605   6226   -758    739  -1101       C  
ATOM   1836  N   LEU A 240      20.034  55.905  44.991  1.00 68.27           N  
ANISOU 1836  N   LEU A 240    11637   7871   6430   -781    630   -924       N  
ATOM   1837  CA  LEU A 240      20.553  57.250  45.221  1.00 69.43           C  
ANISOU 1837  CA  LEU A 240    11730   8095   6553   -872    590   -864       C  
ATOM   1838  C   LEU A 240      22.042  57.233  45.560  1.00 70.93           C  
ANISOU 1838  C   LEU A 240    11747   8390   6811   -840    651   -865       C  
ATOM   1839  O   LEU A 240      22.777  58.120  45.104  1.00 73.88           O  
ANISOU 1839  O   LEU A 240    12071   8847   7149   -938    693   -856       O  
ATOM   1840  CB  LEU A 240      19.754  57.966  46.302  1.00 68.07           C  
ANISOU 1840  CB  LEU A 240    11590   7874   6397   -890    451   -797       C  
ATOM   1841  CG  LEU A 240      18.357  58.370  45.819  1.00 68.00           C  
ANISOU 1841  CG  LEU A 240    11735   7795   6304   -949    392   -783       C  
ATOM   1842  CD1 LEU A 240      17.406  58.545  47.001  1.00 67.21           C  
ANISOU 1842  CD1 LEU A 240    11666   7625   6244   -915    270   -734       C  
ATOM   1843  CD2 LEU A 240      18.409  59.633  44.976  1.00 67.43           C  
ANISOU 1843  CD2 LEU A 240    11719   7764   6137  -1073    406   -749       C  
ATOM   1844  N   ILE A 241      22.486  56.214  46.302  1.00 70.31           N  
ANISOU 1844  N   ILE A 241    11576   8309   6827   -701    663   -873       N  
ATOM   1845  CA  ILE A 241      23.901  56.052  46.609  1.00 71.29           C  
ANISOU 1845  CA  ILE A 241    11518   8552   7016   -644    720   -875       C  
ATOM   1846  C   ILE A 241      24.689  55.768  45.333  1.00 73.76           C  
ANISOU 1846  C   ILE A 241    11802   8925   7298   -662    873   -938       C  
ATOM   1847  O   ILE A 241      25.717  56.405  45.101  1.00 77.38           O  
ANISOU 1847  O   ILE A 241    12142   9504   7751   -726    923   -936       O  
ATOM   1848  CB  ILE A 241      24.156  54.937  47.632  1.00 71.95           C  
ANISOU 1848  CB  ILE A 241    11518   8619   7201   -464    705   -856       C  
ATOM   1849  CG1 ILE A 241      23.556  55.313  48.993  1.00 71.08           C  
ANISOU 1849  CG1 ILE A 241    11413   8482   7112   -448    557   -788       C  
ATOM   1850  CG2 ILE A 241      25.657  54.686  47.799  1.00 74.20           C  
ANISOU 1850  CG2 ILE A 241    11599   9046   7545   -387    775   -859       C  
ATOM   1851  CD1 ILE A 241      23.413  54.142  49.934  1.00 69.93           C  
ANISOU 1851  CD1 ILE A 241    11245   8280   7045   -270    541   -754       C  
ATOM   1852  N   SER A 242      24.195  54.868  44.490  1.00 73.14           N  
ANISOU 1852  N   SER A 242    11832   8766   7191   -619    952   -999       N  
ATOM   1853  CA  SER A 242      24.868  54.567  43.222  1.00 75.52           C  
ANISOU 1853  CA  SER A 242    12123   9122   7446   -636   1106  -1071       C  
ATOM   1854  C   SER A 242      24.862  55.749  42.250  1.00 74.53           C  
ANISOU 1854  C   SER A 242    12054   9062   7201   -806   1129  -1063       C  
ATOM   1855  O   SER A 242      25.889  56.050  41.620  1.00 76.05           O  
ANISOU 1855  O   SER A 242    12157   9364   7374   -849   1237  -1079       O  
ATOM   1856  CB  SER A 242      24.223  53.372  42.522  1.00 76.82           C  
ANISOU 1856  CB  SER A 242    12413   9180   7595   -569   1181  -1156       C  
ATOM   1857  OG  SER A 242      23.972  52.339  43.448  1.00 79.30           O  
ANISOU 1857  OG  SER A 242    12717   9395   8018   -425   1154  -1148       O  
ATOM   1858  N   PHE A 243      23.712  56.413  42.125  1.00 70.83           N  
ANISOU 1858  N   PHE A 243    11729   8528   6653   -897   1035  -1030       N  
ATOM   1859  CA  PHE A 243      23.581  57.545  41.200  1.00 70.01           C  
ANISOU 1859  CA  PHE A 243    11702   8468   6427  -1045   1054  -1003       C  
ATOM   1860  C   PHE A 243      24.501  58.697  41.635  1.00 70.23           C  
ANISOU 1860  C   PHE A 243    11614   8582   6489  -1133   1049   -941       C  
ATOM   1861  O   PHE A 243      24.977  59.467  40.811  1.00 69.24           O  
ANISOU 1861  O   PHE A 243    11493   8520   6292  -1243   1129   -926       O  
ATOM   1862  CB  PHE A 243      22.118  57.996  41.127  1.00 67.89           C  
ANISOU 1862  CB  PHE A 243    11600   8113   6080  -1097    941   -968       C  
ATOM   1863  CG  PHE A 243      21.824  58.952  40.009  1.00 67.79           C  
ANISOU 1863  CG  PHE A 243    11695   8137   5924  -1218    970   -936       C  
ATOM   1864  CD1 PHE A 243      21.944  58.553  38.681  1.00 69.69           C  
ANISOU 1864  CD1 PHE A 243    11994   8430   6054  -1237   1083   -997       C  
ATOM   1865  CD2 PHE A 243      21.387  60.238  40.267  1.00 67.23           C  
ANISOU 1865  CD2 PHE A 243    11678   8045   5820  -1307    889   -843       C  
ATOM   1866  CE1 PHE A 243      21.653  59.434  37.635  1.00 69.89           C  
ANISOU 1866  CE1 PHE A 243    12125   8500   5929  -1339   1110   -953       C  
ATOM   1867  CE2 PHE A 243      21.098  61.126  39.222  1.00 69.02           C  
ANISOU 1867  CE2 PHE A 243    12014   8298   5910  -1404    921   -794       C  
ATOM   1868  CZ  PHE A 243      21.229  60.725  37.906  1.00 68.57           C  
ANISOU 1868  CZ  PHE A 243    12011   8307   5734  -1418   1029   -842       C  
ATOM   1869  N   ASN A 244      24.703  58.805  42.953  1.00 70.20           N  
ANISOU 1869  N   ASN A 244    11509   8575   6588  -1091    955   -907       N  
ATOM   1870  CA  ASN A 244      25.760  59.608  43.568  1.00 71.07           C  
ANISOU 1870  CA  ASN A 244    11462   8783   6757  -1155    951   -878       C  
ATOM   1871  C   ASN A 244      25.811  61.072  43.160  1.00 71.00           C  
ANISOU 1871  C   ASN A 244    11502   8788   6686  -1333    959   -832       C  
ATOM   1872  O   ASN A 244      26.858  61.603  42.801  1.00 71.04           O  
ANISOU 1872  O   ASN A 244    11404   8890   6696  -1421   1050   -835       O  
ATOM   1873  CB  ASN A 244      27.115  58.933  43.344  1.00 72.97           C  
ANISOU 1873  CB  ASN A 244    11523   9146   7053  -1089   1073   -926       C  
ATOM   1874  CG  ASN A 244      28.162  59.380  44.341  1.00 73.41           C  
ANISOU 1874  CG  ASN A 244    11374   9318   7197  -1105   1036   -909       C  
ATOM   1875  OD1 ASN A 244      29.264  59.737  43.946  1.00 72.60           O  
ANISOU 1875  OD1 ASN A 244    11138   9339   7106  -1171   1132   -925       O  
ATOM   1876  ND2 ASN A 244      27.818  59.374  45.648  1.00 72.63           N  
ANISOU 1876  ND2 ASN A 244    11245   9194   7157  -1049    896   -878       N  
ATOM   1877  N   LYS A 245      24.651  61.712  43.235  1.00 71.20           N  
ANISOU 1877  N   LYS A 245    11687   8708   6657  -1381    868   -784       N  
ATOM   1878  CA  LYS A 245      24.530  63.149  43.105  1.00 72.50           C  
ANISOU 1878  CA  LYS A 245    11919   8847   6780  -1531    855   -723       C  
ATOM   1879  C   LYS A 245      23.880  63.687  44.364  1.00 72.41           C  
ANISOU 1879  C   LYS A 245    11930   8759   6820  -1531    710   -690       C  
ATOM   1880  O   LYS A 245      23.089  62.995  44.979  1.00 73.28           O  
ANISOU 1880  O   LYS A 245    12076   8814   6952  -1422    620   -696       O  
ATOM   1881  CB  LYS A 245      23.723  63.492  41.870  1.00 73.71           C  
ANISOU 1881  CB  LYS A 245    12254   8949   6803  -1579    897   -688       C  
ATOM   1882  CG  LYS A 245      24.405  62.991  40.589  1.00 77.44           C  
ANISOU 1882  CG  LYS A 245    12708   9510   7206  -1586   1051   -728       C  
ATOM   1883  CD  LYS A 245      24.130  63.886  39.358  1.00 79.58           C  
ANISOU 1883  CD  LYS A 245    13120   9776   7338  -1695   1124   -667       C  
ATOM   1884  CE  LYS A 245      25.350  64.561  38.635  1.00 83.19           C  
ANISOU 1884  CE  LYS A 245    13508  10324   7775  -1817   1281   -650       C  
ATOM   1885  NZ  LYS A 245      26.195  63.711  37.746  1.00 86.55           N  
ANISOU 1885  NZ  LYS A 245    13856  10862   8166  -1783   1427   -720       N  
ATOM   1886  N   ARG A 246      24.231  64.915  44.756  1.00 72.42           N  
ANISOU 1886  N   ARG A 246    11914   8757   6844  -1658    697   -659       N  
ATOM   1887  CA  ARG A 246      23.856  65.450  46.064  1.00 70.93           C  
ANISOU 1887  CA  ARG A 246    11719   8516   6712  -1665    572   -648       C  
ATOM   1888  C   ARG A 246      22.358  65.377  46.322  1.00 68.52           C  
ANISOU 1888  C   ARG A 246    11574   8088   6370  -1593    469   -610       C  
ATOM   1889  O   ARG A 246      21.568  65.877  45.524  1.00 69.98           O  
ANISOU 1889  O   ARG A 246    11912   8198   6476  -1629    485   -561       O  
ATOM   1890  CB  ARG A 246      24.326  66.894  46.209  1.00 72.62           C  
ANISOU 1890  CB  ARG A 246    11933   8716   6943  -1837    596   -628       C  
ATOM   1891  CG  ARG A 246      24.152  67.470  47.605  1.00 72.84           C  
ANISOU 1891  CG  ARG A 246    11932   8710   7031  -1860    479   -642       C  
ATOM   1892  CD  ARG A 246      25.223  66.980  48.562  1.00 73.85           C  
ANISOU 1892  CD  ARG A 246    11840   8983   7237  -1833    447   -707       C  
ATOM   1893  NE  ARG A 246      26.342  67.909  48.577  1.00 77.82           N  
ANISOU 1893  NE  ARG A 246    12232   9558   7776  -2003    510   -741       N  
ATOM   1894  CZ  ARG A 246      27.467  67.778  47.885  1.00 80.10           C  
ANISOU 1894  CZ  ARG A 246    12391   9964   8079  -2062    626   -765       C  
ATOM   1895  NH1 ARG A 246      28.394  68.731  47.966  1.00 82.00           N  
ANISOU 1895  NH1 ARG A 246    12536  10261   8359  -2240    680   -797       N  
ATOM   1896  NH2 ARG A 246      27.690  66.711  47.118  1.00 81.82           N  
ANISOU 1896  NH2 ARG A 246    12569  10242   8274  -1951    696   -765       N  
ATOM   1897  N   THR A 247      21.984  64.796  47.460  1.00 65.84           N  
ANISOU 1897  N   THR A 247    11192   7737   6084  -1491    366   -626       N  
ATOM   1898  CA  THR A 247      20.597  64.434  47.733  1.00 64.14           C  
ANISOU 1898  CA  THR A 247    11101   7424   5844  -1403    278   -600       C  
ATOM   1899  C   THR A 247      20.120  64.904  49.112  1.00 62.60           C  
ANISOU 1899  C   THR A 247    10908   7183   5693  -1389    162   -587       C  
ATOM   1900  O   THR A 247      20.683  64.533  50.131  1.00 63.20           O  
ANISOU 1900  O   THR A 247    10862   7323   5829  -1343    119   -616       O  
ATOM   1901  CB  THR A 247      20.415  62.908  47.588  1.00 64.03           C  
ANISOU 1901  CB  THR A 247    11059   7427   5842  -1266    290   -635       C  
ATOM   1902  OG1 THR A 247      20.750  62.530  46.253  1.00 63.35           O  
ANISOU 1902  OG1 THR A 247    10992   7375   5700  -1284    401   -658       O  
ATOM   1903  CG2 THR A 247      18.979  62.473  47.886  1.00 63.30           C  
ANISOU 1903  CG2 THR A 247    11081   7237   5732  -1189    206   -615       C  
ATOM   1904  N   LEU A 248      19.090  65.748  49.122  1.00 62.08           N  
ANISOU 1904  N   LEU A 248    10982   7014   5590  -1424    115   -542       N  
ATOM   1905  CA  LEU A 248      18.402  66.132  50.344  1.00 60.15           C  
ANISOU 1905  CA  LEU A 248    10767   6713   5374  -1396     11   -532       C  
ATOM   1906  C   LEU A 248      17.380  65.065  50.623  1.00 59.80           C  
ANISOU 1906  C   LEU A 248    10759   6636   5326  -1263    -46   -524       C  
ATOM   1907  O   LEU A 248      16.406  64.926  49.872  1.00 59.88           O  
ANISOU 1907  O   LEU A 248    10877   6590   5284  -1240    -44   -495       O  
ATOM   1908  CB  LEU A 248      17.701  67.475  50.181  1.00 59.86           C  
ANISOU 1908  CB  LEU A 248    10870   6570   5304  -1476      0   -484       C  
ATOM   1909  CG  LEU A 248      16.997  68.030  51.416  1.00 59.66           C  
ANISOU 1909  CG  LEU A 248    10884   6476   5305  -1455    -92   -480       C  
ATOM   1910  CD1 LEU A 248      18.015  68.349  52.499  1.00 61.74           C  
ANISOU 1910  CD1 LEU A 248    11026   6807   5625  -1511   -114   -540       C  
ATOM   1911  CD2 LEU A 248      16.194  69.289  51.101  1.00 59.73           C  
ANISOU 1911  CD2 LEU A 248    11048   6363   5282  -1509    -87   -424       C  
ATOM   1912  N   VAL A 249      17.575  64.329  51.722  1.00 59.03           N  
ANISOU 1912  N   VAL A 249    10569   6578   5281  -1178    -97   -546       N  
ATOM   1913  CA  VAL A 249      16.613  63.321  52.173  1.00 56.30           C  
ANISOU 1913  CA  VAL A 249    10255   6190   4944  -1057   -147   -534       C  
ATOM   1914  C   VAL A 249      15.786  63.869  53.343  1.00 55.13           C  
ANISOU 1914  C   VAL A 249    10154   5990   4802  -1038   -239   -510       C  
ATOM   1915  O   VAL A 249      16.306  64.108  54.417  1.00 54.50           O  
ANISOU 1915  O   VAL A 249    10000   5958   4750  -1034   -282   -525       O  
ATOM   1916  CB  VAL A 249      17.301  62.039  52.606  1.00 56.27           C  
ANISOU 1916  CB  VAL A 249    10135   6252   4992   -954   -129   -557       C  
ATOM   1917  CG1 VAL A 249      16.280  60.934  52.775  1.00 56.15           C  
ANISOU 1917  CG1 VAL A 249    10176   6169   4989   -847   -147   -545       C  
ATOM   1918  CG2 VAL A 249      18.310  61.624  51.570  1.00 58.26           C  
ANISOU 1918  CG2 VAL A 249    10323   6568   5245   -974    -28   -590       C  
ATOM   1919  N   LEU A 250      14.503  64.107  53.092  1.00 55.34           N  
ANISOU 1919  N   LEU A 250    10299   5930   4796  -1026   -268   -478       N  
ATOM   1920  CA  LEU A 250      13.564  64.508  54.125  1.00 56.25           C  
ANISOU 1920  CA  LEU A 250    10463   5992   4914   -991   -345   -455       C  
ATOM   1921  C   LEU A 250      13.118  63.264  54.885  1.00 55.38           C  
ANISOU 1921  C   LEU A 250    10317   5888   4836   -876   -375   -452       C  
ATOM   1922  O   LEU A 250      12.789  62.276  54.276  1.00 55.69           O  
ANISOU 1922  O   LEU A 250    10365   5913   4879   -832   -343   -455       O  
ATOM   1923  CB  LEU A 250      12.325  65.147  53.509  1.00 57.16           C  
ANISOU 1923  CB  LEU A 250    10706   6026   4986  -1006   -358   -414       C  
ATOM   1924  CG  LEU A 250      12.324  66.614  53.126  1.00 58.68           C  
ANISOU 1924  CG  LEU A 250    10977   6168   5149  -1095   -344   -389       C  
ATOM   1925  CD1 LEU A 250      12.320  67.455  54.384  1.00 58.78           C  
ANISOU 1925  CD1 LEU A 250    10993   6148   5189  -1109   -391   -400       C  
ATOM   1926  CD2 LEU A 250      13.479  66.972  52.213  1.00 60.64           C  
ANISOU 1926  CD2 LEU A 250    11198   6454   5385  -1190   -267   -402       C  
ATOM   1927  N   PHE A 251      13.065  63.328  56.207  1.00 54.37           N  
ANISOU 1927  N   PHE A 251    10156   5774   4726   -832   -431   -447       N  
ATOM   1928  CA  PHE A 251      12.563  62.210  56.988  1.00 53.35           C  
ANISOU 1928  CA  PHE A 251    10006   5640   4621   -720   -452   -427       C  
ATOM   1929  C   PHE A 251      11.095  61.926  56.622  1.00