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***  DESMOND1  ***

elNémo ID: 23012322142769668

Job options:

ID        	=	 23012322142769668
JOBID     	=	 DESMOND1
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 DESMOND1

HEADER    TRANSFERASE/TRANSFERASE INHIBITOR       10-JUN-13   4L52              
TITLE     CRYSTAL STRUCTURE OF 1-(4-{4-[7-AMINO-2-(1,2,3-BENZOTHIADIAZOL-7-YL)  
TITLE    2 FURO[2,3-C]PYRIDIN-4-YL]-1H-PYRAZOL-1-YL}PIPERIDIN-1-YL)ETHAN-1-ONE  
TITLE    3 BOUND TO TAK1-TAB1                                                   
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: MITOGEN-ACTIVATED PROTEIN KINASE KINASE KINASE 7, TGF-BETA-
COMPND   3 ACTIVATED KINASE 1 AND MAP3K7-BINDING PROTEIN 1 CHIMERA;             
COMPND   4 CHAIN: A;                                                            
COMPND   5 FRAGMENT: SEE REMARK 999;                                            
COMPND   6 SYNONYM: TAK1-TAB1 FUSION PROTEIN, TRANSFORMING GROWTH FACTOR-BETA-  
COMPND   7 ACTIVATED KINASE 1, TGF-BETA-ACTIVATED KINASE 1, MITOGEN-ACTIVATED   
COMPND   8 PROTEIN KINASE KINASE KINASE 7-INTERACTING PROTEIN 1, TGF-BETA-      
COMPND   9 ACTIVATED KINASE 1-BINDING PROTEIN 1, TAK1-BINDING PROTEIN 1;        
COMPND  10 EC: 2.7.11.25;                                                       
COMPND  11 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: MAP3K7, TAK1, MAP3K7IP1, TAB1;                                 
SOURCE   6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            
SOURCE   7 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;                             
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 7108;                                       
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS                           
KEYWDS    TAK1 KINASE, TRANSFERASE-TRANSFERASE INHIBITOR COMPLEX                
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.WANG,K.R.HORNBERGER,A.P.CREW,A.JESTEL,K.MASKOS,M.MOERTL             
REVDAT   5   15-NOV-17 4L52    1       REMARK                                   
REVDAT   4   26-JUL-17 4L52    1       SOURCE REMARK                            
REVDAT   3   07-AUG-13 4L52    1       JRNL                                     
REVDAT   2   31-JUL-13 4L52    1       JRNL                                     
REVDAT   1   03-JUL-13 4L52    0                                                
JRNL        AUTH   K.R.HORNBERGER,D.M.BERGER,A.P.CREW,H.DONG,A.KLEINBERG,       
JRNL        AUTH 2 A.H.LI,M.R.MEDEIROS,M.J.MULVIHILL,K.SIU,J.TARRANT,J.WANG,    
JRNL        AUTH 3 F.WENG,V.L.WILDE,M.ALBERTELLA,M.BITTNER,A.COOKE,M.J.GRAY,    
JRNL        AUTH 4 P.MARESCA,E.MAY,P.MEYN,W.PEICK,D.ROMASHKO,M.TANOWITZ,B.TOKAR 
JRNL        TITL   DISCOVERY AND OPTIMIZATION OF 7-AMINOFURO[2,3-C]PYRIDINE     
JRNL        TITL 2 INHIBITORS OF TAK1.                                          
JRNL        REF    BIOORG.MED.CHEM.LETT.         V.  23  4517 2013              
JRNL        REFN                   ISSN 0960-894X                               
JRNL        PMID   23850198                                                     
JRNL        DOI    10.1016/J.BMCL.2013.06.053                                   
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.54 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.2.0005                                      
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) : 2.54                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 97.51                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 93.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 16952                          
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) : 0.196                           
REMARK   3   R VALUE            (WORKING SET) : 0.195                           
REMARK   3   FREE R VALUE                     : 0.230                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 3.800                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 666                             
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) : 2.54                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.61                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1250                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 96.01                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3100                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 49                           
REMARK   3   BIN FREE R VALUE                    : 0.4150                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2341                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 33                                      
REMARK   3   SOLVENT ATOMS            : 35                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 66.69                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -5.32000                                             
REMARK   3    B22 (A**2) : -2.52000                                             
REMARK   3    B33 (A**2) : 7.84000                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.284         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.224         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.168         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 16.314        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.952                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.940                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  2380 ; 0.011 ; 0.021       
REMARK   3   BOND LENGTHS OTHERS               (A):  2101 ; 0.001 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  3250 ; 1.422 ; 1.964       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  4857 ; 0.797 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   295 ; 6.544 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):    98 ;34.630 ;23.061       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   349 ;16.546 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    14 ;18.913 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   341 ; 0.069 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  2674 ; 0.004 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):   494 ; 0.001 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):   524 ; 0.218 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  2090 ; 0.185 ; 0.200       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  1194 ; 0.188 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  1232 ; 0.089 ; 0.200       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):    49 ; 0.150 ; 0.200       
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):    11 ; 0.089 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):    40 ; 0.166 ; 0.200       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):     3 ; 0.015 ; 0.200       
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):  1884 ; 2.438 ; 2.000       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):   594 ; 0.434 ; 2.000       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  2378 ; 2.994 ; 3.000       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1103 ; 4.461 ; 4.000       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):   872 ; 6.204 ; 6.000       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  NULL ;  NULL ;  NULL       
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   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 2                                          
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    26        A   106                          
REMARK   3    ORIGIN FOR THE GROUP (A):   -8.585  -50.504   -8.096              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5247 T22:   0.4422                                     
REMARK   3      T33:   0.2092 T12:  -0.0361                                     
REMARK   3      T13:   0.0073 T23:   0.0538                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.7779 L22:   7.3677                                     
REMARK   3      L33:   6.5293 L12:   4.0625                                     
REMARK   3      L13:  -1.5515 L23:  -5.8721                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.4772 S12:  -0.8134 S13:  -0.3739                       
REMARK   3      S21:   1.1196 S22:  -0.0305 S23:  -0.0175                       
REMARK   3      S31:   0.2322 S32:  -0.3257 S33:  -0.4466                       
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 :   A   107        A   496                          
REMARK   3    ORIGIN FOR THE GROUP (A):   -6.238  -44.247  -33.602              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.1167 T22:  -0.0982                                     
REMARK   3      T33:  -0.1613 T12:  -0.0189                                     
REMARK   3      T13:  -0.0041 T23:   0.0552                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.5654 L22:   3.7535                                     
REMARK   3      L33:   2.1241 L12:  -0.8899                                     
REMARK   3      L13:  -0.2047 L23:  -0.2281                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0453 S12:  -0.0080 S13:  -0.3720                       
REMARK   3      S21:  -0.0312 S22:   0.0561 S23:  -0.0339                       
REMARK   3      S31:   0.2111 S32:  -0.0395 S33:  -0.0107                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : BABINET MODEL WITH 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 4L52 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 11-JUN-13.                  
REMARK 100 THE DEPOSITION ID IS D_1000080190.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 29-SEP-10                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SLS                                
REMARK 200  BEAMLINE                       : X06SA                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0000                             
REMARK 200  MONOCHROMATOR                  : LN2 COOLED FIXED-EXIT SI(111)      
REMARK 200  OPTICS                         : DYNAMICALLY BENDABLE MIRROR        
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS 6M                 
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XSCALE                             
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 18760                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.540                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 97.510                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 93.9                               
REMARK 200  DATA REDUNDANCY                : 3.400                              
REMARK 200  R MERGE                    (I) : 0.05900                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : NULL                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.54                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.76                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 95.9                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.50                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.44900                            
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: NULL                         
REMARK 200 SOFTWARE USED: MOLREP                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 69.14                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.99                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.75 M SODIUM CITRATE, 0.2 M SODIUM      
REMARK 280  CHLORIDE, 0.1 M TRIS, PH 7.0, VAPOR DIFFUSION, HANGING DROP,        
REMARK 280  TEMPERATURE 293K                                                    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 2 2 2                          
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z                                                 
REMARK 290       3555   -X,Y,-Z                                                 
REMARK 290       4555   X,-Y,-Z                                                 
REMARK 290       5555   X+1/2,Y+1/2,Z+1/2                                       
REMARK 290       6555   -X+1/2,-Y+1/2,Z+1/2                                     
REMARK 290       7555   -X+1/2,Y+1/2,-Z+1/2                                     
REMARK 290       8555   X+1/2,-Y+1/2,-Z+1/2                                     
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000       29.08000            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       66.89200            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000       71.11850            
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000       29.08000            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       66.89200            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       71.11850            
REMARK 290   SMTRY1   7 -1.000000  0.000000  0.000000       29.08000            
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       66.89200            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000       71.11850            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000       29.08000            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000       66.89200            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000       71.11850            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     ALA A   179                                                      
REMARK 465     CYS A   180                                                      
REMARK 465     ASP A   181                                                      
REMARK 465     ILE A   182                                                      
REMARK 465     GLN A   183                                                      
REMARK 465     THR A   184                                                      
REMARK 465     HIS A   185                                                      
REMARK 465     MET A   186                                                      
REMARK 465     THR A   187                                                      
REMARK 465     ASN A   188                                                      
REMARK 465     ASN A   189                                                      
REMARK 465     LYS A   190                                                      
REMARK 480                                                                      
REMARK 480 ZERO OCCUPANCY ATOM                                                  
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO                  
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS                
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;              
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):         
REMARK 480   M RES C SSEQI ATOMS                                                
REMARK 480     LEU A   28   CG   CD1  CD2                                       
REMARK 480     LYS A   34   CG   CD   CE   NZ                                   
REMARK 480     GLU A   35   CG   CD   OE1  OE2                                  
REMARK 480     GLU A   37   CG   CD   OE1  OE2                                  
REMARK 480     LYS A   54   CD   CE   NZ                                        
REMARK 480     LYS A   58   CD   CE   NZ                                        
REMARK 480     ILE A   65   CD1                                                 
REMARK 480     GLU A   68   CG   CD   OE1  OE2                                  
REMARK 480     ARG A   71   CD   NE   CZ   NH1  NH2                             
REMARK 480     LYS A   72   CG   CD   CE   NZ                                   
REMARK 480     LEU A   78   CD1  CD2                                            
REMARK 480     ARG A   79   CG   CD   NE   CZ   NH1  NH2                        
REMARK 480     LYS A   91   CG   CD   CE   NZ                                   
REMARK 480     LEU A   92   CD1  CD2                                            
REMARK 480     LEU A   97   CG   CD1  CD2                                       
REMARK 480     ASN A   98   CG   OD1  ND2                                       
REMARK 480     LEU A  102   CD1  CD2                                            
REMARK 480     LYS A  150   CG   CD   CE   NZ                                   
REMARK 480     GLU A  231   CG   CD   OE1  OE2                                  
REMARK 480     LYS A  253   CD   CE   NZ                                        
REMARK 480     LYS A  257   CD   CE   NZ                                        
REMARK 480     LYS A  269   CE   NZ                                             
REMARK 480     LEU A  470   CG   CD1  CD2                                       
REMARK 480     GLU A  474   CG   CD   OE1  OE2                                  
REMARK 480     ASP A  475   CG   OD1  OD2                                       
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
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   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    LEU A 102   CG    LEU A 102   CD1    -0.243                       
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    GLU A  39     -159.83   -137.11                                   
REMARK 500    TRP A  55      114.13   -160.16                                   
REMARK 500    ASN A  85      106.16   -172.20                                   
REMARK 500    ASN A  98      -70.49    -51.26                                   
REMARK 500    ARG A 155      -19.36     79.45                                   
REMARK 500    ARG A 155      -28.97     80.85                                   
REMARK 500    ASP A 475      -28.42    130.03                                   
REMARK 500    HIS A 495     -115.91   -112.65                                   
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 ASN A   98     PRO A   99                  135.37                    
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 1UL A 501                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 4L3P   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF 2-(1-BENZOTHIOPHEN-7-YL)-4-[1-(PIPERIDIN-4-YL)- 
REMARK 900 1H-PYRAZOL-4-YL]FURO[2,3-C]PYRIDIN-7-AMINE BOUND TO TAK1-TAB1        
REMARK 900 RELATED ID: 4L53   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF (1R,4R)-4-{4-[7-AMINO-2-(1,2,3-BENZOTHIADIAZOL- 
REMARK 900 7-YL)-3-CHLOROFURO[2,3-C]PYRIDIN-4-YL]-1H-PYRAZOL-1-YL}CYCLOHEXAN-1- 
REMARK 900 OL BOUND TO TAK1-TAB1                                                
REMARK 999                                                                      
REMARK 999 SEQUENCE                                                             
REMARK 999 PROTEIN IS A CHIMERA COMPRISING THE KINASE DOMAIN OF TAK1 (UNP       
REMARK 999 O43318 RESIDUES 31-303) AND RESIDUES 468-496 OF TAB1 (UNP Q15750).   
DBREF  4L52 A   31   303  UNP    O43318   M3K7_HUMAN      31    303             
DBREF  4L52 A  468   496  UNP    Q15750   TAB1_HUMAN     468    496             
SEQADV 4L52 GLY A   26  UNP  O43318              EXPRESSION TAG                 
SEQADV 4L52 SER A   27  UNP  O43318              EXPRESSION TAG                 
SEQADV 4L52 LEU A   28  UNP  O43318              EXPRESSION TAG                 
SEQADV 4L52 HIS A   29  UNP  O43318              EXPRESSION TAG                 
SEQADV 4L52 MET A   30  UNP  O43318              EXPRESSION TAG                 
SEQRES   1 A  307  GLY SER LEU HIS MET ILE ASP TYR LYS GLU ILE GLU VAL          
SEQRES   2 A  307  GLU GLU VAL VAL GLY ARG GLY ALA PHE GLY VAL VAL CYS          
SEQRES   3 A  307  LYS ALA LYS TRP ARG ALA LYS ASP VAL ALA ILE LYS GLN          
SEQRES   4 A  307  ILE GLU SER GLU SER GLU ARG LYS ALA PHE ILE VAL GLU          
SEQRES   5 A  307  LEU ARG GLN LEU SER ARG VAL ASN HIS PRO ASN ILE VAL          
SEQRES   6 A  307  LYS LEU TYR GLY ALA CYS LEU ASN PRO VAL CYS LEU VAL          
SEQRES   7 A  307  MET GLU TYR ALA GLU GLY GLY SER LEU TYR ASN VAL LEU          
SEQRES   8 A  307  HIS GLY ALA GLU PRO LEU PRO TYR TYR THR ALA ALA HIS          
SEQRES   9 A  307  ALA MET SER TRP CYS LEU GLN CYS SER GLN GLY VAL ALA          
SEQRES  10 A  307  TYR LEU HIS SER MET GLN PRO LYS ALA LEU ILE HIS ARG          
SEQRES  11 A  307  ASP LEU LYS PRO PRO ASN LEU LEU LEU VAL ALA GLY GLY          
SEQRES  12 A  307  THR VAL LEU LYS ILE CYS ASP PHE GLY THR ALA CYS ASP          
SEQRES  13 A  307  ILE GLN THR HIS MET THR ASN ASN LYS GLY SER ALA ALA          
SEQRES  14 A  307  TRP MET ALA PRO GLU VAL PHE GLU GLY SER ASN TYR SER          
SEQRES  15 A  307  GLU LYS CYS ASP VAL PHE SER TRP GLY ILE ILE LEU TRP          
SEQRES  16 A  307  GLU VAL ILE THR ARG ARG LYS PRO PHE ASP GLU ILE GLY          
SEQRES  17 A  307  GLY PRO ALA PHE ARG ILE MET TRP ALA VAL HIS ASN GLY          
SEQRES  18 A  307  THR ARG PRO PRO LEU ILE LYS ASN LEU PRO LYS PRO ILE          
SEQRES  19 A  307  GLU SER LEU MET THR ARG CYS TRP SER LYS ASP PRO SER          
SEQRES  20 A  307  GLN ARG PRO SER MET GLU GLU ILE VAL LYS ILE MET THR          
SEQRES  21 A  307  HIS LEU MET ARG TYR PHE PRO GLY ALA ASP GLU PRO LEU          
SEQRES  22 A  307  GLN TYR PRO CYS GLN HIS SER LEU PRO PRO GLY GLU ASP          
SEQRES  23 A  307  GLY ARG VAL GLU PRO TYR VAL ASP PHE ALA GLU PHE TYR          
SEQRES  24 A  307  ARG LEU TRP SER VAL ASP HIS GLY                              
HET    1UL  A 501      33                                                       
HETNAM     1UL 1-(4-{4-[7-AMINO-2-(1,2,3-BENZOTHIADIAZOL-7-YL)FURO[2,           
HETNAM   2 1UL  3-C]PYRIDIN-4-YL]-1H-PYRAZOL-1-YL}PIPERIDIN-1-YL)               
HETNAM   3 1UL  ETHANONE                                                        
FORMUL   2  1UL    C23 H21 N7 O2 S                                              
FORMUL   3  HOH   *35(H2 O)                                                     
HELIX    1   1 ASP A   32  LYS A   34  5                                   3    
HELIX    2   2 SER A   67  SER A   69  5                                   3    
HELIX    3   3 GLU A   70  SER A   82  1                                  13    
HELIX    4   4 LEU A  112  GLY A  118  1                                   7    
HELIX    5   5 THR A  126  MET A  147  1                                  22    
HELIX    6   6 LYS A  158  PRO A  160  5                                   3    
HELIX    7   7 SER A  192  MET A  196  5                                   5    
HELIX    8   8 ALA A  197  GLU A  202  1                                   6    
HELIX    9   9 GLU A  208  ARG A  225  1                                  18    
HELIX   10  10 PRO A  235  ASN A  245  1                                  11    
HELIX   11  11 PRO A  256  TRP A  267  1                                  12    
HELIX   12  12 ASP A  270  ARG A  274  5                                   5    
HELIX   13  13 SER A  276  MET A  288  1                                  13    
HELIX   14  14 ARG A  289  PHE A  291  5                                   3    
HELIX   15  15 PHE A  484  HIS A  495  1                                  12    
SHEET    1   A 5 ILE A  36  GLY A  43  0                                        
SHEET    2   A 5 VAL A  49  TRP A  55 -1  O  VAL A  50   N  GLY A  43           
SHEET    3   A 5 LYS A  58  GLN A  64 -1  O  ILE A  62   N  CYS A  51           
SHEET    4   A 5 CYS A 101  GLU A 105 -1  O  MET A 104   N  ALA A  61           
SHEET    5   A 5 LEU A  92  CYS A  96 -1  N  GLY A  94   O  VAL A 103           
SHEET    1   B 3 GLY A 110  SER A 111  0                                        
SHEET    2   B 3 LEU A 162  VAL A 165 -1  O  LEU A 164   N  GLY A 110           
SHEET    3   B 3 VAL A 170  ILE A 173 -1  O  LYS A 172   N  LEU A 163           
SHEET    1   C 2 LEU A 122  PRO A 123  0                                        
SHEET    2   C 2 PRO A 301  CYS A 302 -1  O  CYS A 302   N  LEU A 122           
SHEET    1   D 2 LEU A 251  ILE A 252  0                                        
SHEET    2   D 2 ARG A 477  VAL A 478  1  O  VAL A 478   N  LEU A 251           
SSBOND   1 CYS A   96    CYS A  101                          1555   1555  2.71  
CISPEP   1 GLU A  120    PRO A  121          0         5.10                     
CISPEP   2 GLN A  148    PRO A  149          0        -4.62                     
SITE     1 AC1 10 VAL A  42  ALA A  61  MET A 104  GLU A 105                    
SITE     2 AC1 10 TYR A 106  ALA A 107  GLU A 108  LEU A 163                    
SITE     3 AC1 10 CYS A 174  ASP A 175                                          
CRYST1   58.160  133.784  142.237  90.00  90.00  90.00 I 2 2 2       8          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.017194  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.007475  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.007031        0.00000                         
ATOM      1  N   GLY A  26       4.869 -40.636  -5.335  1.00 99.18           N  
ANISOU    1  N   GLY A  26    14801  13907   8975  -3028  -3385   1097       N  
ATOM      2  CA  GLY A  26       4.865 -42.111  -5.120  1.00 98.67           C  
ANISOU    2  CA  GLY A  26    14321  13914   9254  -2791  -3487   1474       C  
ATOM      3  C   GLY A  26       4.246 -42.478  -3.785  1.00101.66           C  
ANISOU    3  C   GLY A  26    15284  14265   9077  -3198  -3504   1493       C  
ATOM      4  O   GLY A  26       4.953 -42.830  -2.842  1.00106.90           O  
ANISOU    4  O   GLY A  26    16012  15111   9494  -3712  -4029   2012       O  
ATOM      5  N   SER A  27       2.924 -42.364  -3.707  1.00 97.82           N  
ANISOU    5  N   SER A  27    15206  13569   8392  -2995  -2931    974       N  
ATOM      6  CA  SER A  27       2.172 -42.747  -2.517  1.00100.47           C  
ANISOU    6  CA  SER A  27    16093  13861   8221  -3301  -2815    940       C  
ATOM      7  C   SER A  27       0.794 -43.235  -2.928  1.00 96.52           C  
ANISOU    7  C   SER A  27    15528  13195   7952  -2757  -2196    581       C  
ATOM      8  O   SER A  27       0.271 -42.828  -3.970  1.00 91.02           O  
ANISOU    8  O   SER A  27    14615  12378   7590  -2297  -1798    244       O  
ATOM      9  CB  SER A  27       2.042 -41.568  -1.545  1.00104.96           C  
ANISOU    9  CB  SER A  27    17590  14333   7955  -3945  -2742    684       C  
ATOM     10  OG  SER A  27       0.882 -40.798  -1.803  1.00102.52           O  
ANISOU   10  OG  SER A  27    17683  13750   7520  -3655  -2011     86       O  
ATOM     11  N   LEU A  28       0.208 -44.107  -2.114  1.00 98.04           N  
ANISOU   11  N   LEU A  28    15887  13402   7960  -2854  -2152    709       N  
ATOM     12  CA  LEU A  28      -1.129 -44.626  -2.400  1.00 95.74           C  
ANISOU   12  CA  LEU A  28    15531  12993   7852  -2421  -1613    461       C  
ATOM     13  C   LEU A  28      -2.039 -44.389  -1.206  1.00 99.70           C  
ANISOU   13  C   LEU A  28    16736  13434   7711  -2748  -1271    295       C  
ATOM     14  O   LEU A  28      -1.718 -44.777  -0.076  1.00105.15           O  
ANISOU   14  O   LEU A  28    17766  14227   7959  -3248  -1586    560       O  
ATOM     15  CB  LEU A  28      -1.089 -46.118  -2.753  1.00 93.35           C  
ANISOU   15  CB  LEU A  28    14669  12739   8061  -2116  -1807    795       C  
ATOM     16  CG  LEU A  28      -2.159 -46.927  -3.290  0.00 91.81           C  
ANISOU   16  CG  LEU A  28    14242  12454   8188  -1700  -1452    691       C  
ATOM     17  CD1 LEU A  28      -2.846 -46.241  -4.460  0.00 87.65           C  
ANISOU   17  CD1 LEU A  28    13551  11822   7929  -1305  -1000    307       C  
ATOM     18  CD2 LEU A  28      -1.604 -48.289  -3.698  0.00 91.46           C  
ANISOU   18  CD2 LEU A  28    13704  12397   8651  -1484  -1769   1070       C  
ATOM     19  N   HIS A  29      -3.158 -43.718  -1.468  1.00 98.83           N  
ANISOU   19  N   HIS A  29    16837  13157   7558  -2475   -605   -107       N  
ATOM     20  CA  HIS A  29      -4.229 -43.577  -0.498  1.00101.79           C  
ANISOU   20  CA  HIS A  29    17789  13439   7447  -2619    -89   -265       C  
ATOM     21  C   HIS A  29      -4.769 -44.971  -0.233  1.00101.00           C  
ANISOU   21  C   HIS A  29    17390  13471   7515  -2516   -173     20       C  
ATOM     22  O   HIS A  29      -4.903 -45.775  -1.156  1.00 95.69           O  
ANISOU   22  O   HIS A  29    16080  12844   7432  -2112   -278    151       O  
ATOM     23  CB  HIS A  29      -5.336 -42.650  -1.019  1.00101.80           C  
ANISOU   23  CB  HIS A  29    17881  13231   7567  -2211    690   -638       C  
ATOM     24  CG  HIS A  29      -6.264 -42.152   0.049  1.00107.45           C  
ANISOU   24  CG  HIS A  29    19324  13780   7720  -2380   1342   -829       C  
ATOM     25  ND1 HIS A  29      -7.270 -42.929   0.585  1.00107.89           N  
ANISOU   25  ND1 HIS A  29    19369  13905   7722  -2292   1661   -698       N  
ATOM     26  CD2 HIS A  29      -6.340 -40.953   0.675  1.00113.83           C  
ANISOU   26  CD2 HIS A  29    20936  14326   7989  -2631   1790  -1140       C  
ATOM     27  CE1 HIS A  29      -7.922 -42.232   1.499  1.00116.62           C  
ANISOU   27  CE1 HIS A  29    21207  14813   8292  -2451   2313   -911       C  
ATOM     28  NE2 HIS A  29      -7.377 -41.031   1.574  1.00118.99           N  
ANISOU   28  NE2 HIS A  29    22053  14880   8279  -2657   2426  -1201       N  
ATOM     29  N   MET A  30      -5.050 -45.256   1.033  1.00105.63           N  
ANISOU   29  N   MET A  30    18496  14099   7541  -2932   -133    116       N  
ATOM     30  CA  MET A  30      -5.484 -46.578   1.449  1.00106.73           C  
ANISOU   30  CA  MET A  30    18421  14369   7761  -2934   -275    428       C  
ATOM     31  C   MET A  30      -6.973 -46.558   1.751  1.00107.53           C  
ANISOU   31  C   MET A  30    18713  14414   7728  -2738    449    269       C  
ATOM     32  O   MET A  30      -7.496 -45.602   2.333  1.00110.32           O  
ANISOU   32  O   MET A  30    19664  14633   7621  -2859   1015     -8       O  
ATOM     33  CB  MET A  30      -4.714 -47.012   2.688  1.00113.00           C  
ANISOU   33  CB  MET A  30    19604  15301   8028  -3594   -808    752       C  
ATOM     34  CG  MET A  30      -3.205 -46.969   2.515  1.00116.12           C  
ANISOU   34  CG  MET A  30    19783  15792   8544  -3852  -1539   1041       C  
ATOM     35  SD  MET A  30      -2.499 -48.570   2.129  1.00114.85           S  
ANISOU   35  SD  MET A  30    18816  15762   9061  -3645  -2180   1638       S  
ATOM     36  CE  MET A  30      -2.602 -49.407   3.718  1.00117.54           C  
ANISOU   36  CE  MET A  30    19576  16263   8821  -4286  -2493   2054       C  
ATOM     37  N   ILE A  31      -7.643 -47.632   1.357  1.00105.22           N  
ANISOU   37  N   ILE A  31    17926  14206   7848  -2444    450    480       N  
ATOM     38  CA  ILE A  31      -9.087 -47.736   1.447  1.00106.15           C  
ANISOU   38  CA  ILE A  31    18022  14325   7985  -2208   1084    452       C  
ATOM     39  C   ILE A  31      -9.419 -49.010   2.208  1.00108.29           C  
ANISOU   39  C   ILE A  31    18282  14748   8116  -2431    862    794       C  
ATOM     40  O   ILE A  31      -8.756 -50.027   2.022  1.00108.46           O  
ANISOU   40  O   ILE A  31    17991  14831   8388  -2494    254   1067       O  
ATOM     41  CB  ILE A  31      -9.688 -47.740   0.014  1.00102.47           C  
ANISOU   41  CB  ILE A  31    16906  13830   8198  -1666   1278    422       C  
ATOM     42  CG1 ILE A  31      -9.721 -46.303  -0.525  1.00101.41           C  
ANISOU   42  CG1 ILE A  31    16873  13537   8119  -1450   1705     91       C  
ATOM     43  CG2 ILE A  31     -11.080 -48.372  -0.022  1.00103.31           C  
ANISOU   43  CG2 ILE A  31    16749  14032   8472  -1478   1661    633       C  
ATOM     44  CD1 ILE A  31     -10.062 -46.185  -1.996  1.00 97.13           C  
ANISOU   44  CD1 ILE A  31    15705  12984   8216  -1013   1770     85       C  
ATOM     45  N   ASP A  32     -10.410 -48.961   3.095  1.00111.53           N  
ANISOU   45  N   ASP A  32    19049  15199   8129  -2549   1378    803       N  
ATOM     46  CA  ASP A  32     -10.903 -50.202   3.693  1.00112.53           C  
ANISOU   46  CA  ASP A  32    19085  15488   8184  -2716   1209   1153       C  
ATOM     47  C   ASP A  32     -11.914 -50.817   2.731  1.00107.64           C  
ANISOU   47  C   ASP A  32    17830  14918   8151  -2284   1389   1317       C  
ATOM     48  O   ASP A  32     -12.855 -50.156   2.282  1.00104.05           O  
ANISOU   48  O   ASP A  32    17225  14439   7870  -1962   1998   1219       O  
ATOM     49  CB  ASP A  32     -11.466 -50.024   5.121  1.00119.43           C  
ANISOU   49  CB  ASP A  32    20625  16417   8334  -3105   1632   1152       C  
ATOM     50  CG  ASP A  32     -12.538 -48.947   5.228  1.00124.09           C  
ANISOU   50  CG  ASP A  32    21482  16890   8775  -2844   2616    892       C  
ATOM     51  OD1 ASP A  32     -12.627 -48.074   4.334  1.00119.58           O  
ANISOU   51  OD1 ASP A  32    20705  16170   8559  -2449   2922    667       O  
ATOM     52  OD2 ASP A  32     -13.277 -48.971   6.241  1.00129.15           O  
ANISOU   52  OD2 ASP A  32    22553  17574   8943  -3036   3115    939       O  
ATOM     53  N   TYR A  33     -11.673 -52.077   2.383  1.00105.86           N  
ANISOU   53  N   TYR A  33    17238  14740   8244  -2303    838   1606       N  
ATOM     54  CA  TYR A  33     -12.523 -52.813   1.450  1.00103.66           C  
ANISOU   54  CA  TYR A  33    16435  14489   8461  -2030    875   1798       C  
ATOM     55  C   TYR A  33     -13.966 -52.950   1.965  1.00106.34           C  
ANISOU   55  C   TYR A  33    16763  14995   8647  -2039   1403   2002       C  
ATOM     56  O   TYR A  33     -14.914 -52.939   1.176  1.00104.62           O  
ANISOU   56  O   TYR A  33    16135  14833   8784  -1792   1679   2126       O  
ATOM     57  CB  TYR A  33     -11.904 -54.190   1.191  1.00102.49           C  
ANISOU   57  CB  TYR A  33    16081  14281   8578  -2125    212   2060       C  
ATOM     58  CG  TYR A  33     -12.647 -55.053   0.198  1.00 99.72           C  
ANISOU   58  CG  TYR A  33    15320  13898   8670  -1957    164   2245       C  
ATOM     59  CD1 TYR A  33     -13.670 -55.892   0.615  1.00104.47           C  
ANISOU   59  CD1 TYR A  33    15876  14629   9187  -2115    232   2566       C  
ATOM     60  CD2 TYR A  33     -12.313 -55.051  -1.149  1.00 97.24           C  
ANISOU   60  CD2 TYR A  33    14713  13424   8811  -1708     32   2119       C  
ATOM     61  CE1 TYR A  33     -14.350 -56.695  -0.279  1.00102.68           C  
ANISOU   61  CE1 TYR A  33    15341  14370   9303  -2070    133   2771       C  
ATOM     62  CE2 TYR A  33     -12.991 -55.858  -2.059  1.00 95.58           C  
ANISOU   62  CE2 TYR A  33    14241  13160   8915  -1671    -37   2291       C  
ATOM     63  CZ  TYR A  33     -14.010 -56.675  -1.610  1.00 97.07           C  
ANISOU   63  CZ  TYR A  33    14412  13477   8995  -1874     -6   2625       C  
ATOM     64  OH  TYR A  33     -14.699 -57.481  -2.473  1.00 95.28           O  
ANISOU   64  OH  TYR A  33    13989  13200   9013  -1943   -121   2833       O  
ATOM     65  N   LYS A  34     -14.120 -53.057   3.286  1.00110.49           N  
ANISOU   65  N   LYS A  34    17730  15617   8634  -2359   1541   2081       N  
ATOM     66  CA  LYS A  34     -15.437 -53.204   3.923  1.00114.60           C  
ANISOU   66  CA  LYS A  34    18270  16312   8963  -2386   2090   2310       C  
ATOM     67  C   LYS A  34     -16.364 -52.005   3.696  1.00116.07           C  
ANISOU   67  C   LYS A  34    18398  16479   9223  -2035   2957   2181       C  
ATOM     68  O   LYS A  34     -17.583 -52.144   3.815  1.00118.64           O  
ANISOU   68  O   LYS A  34    18478  16961   9638  -1914   3443   2479       O  
ATOM     69  CB  LYS A  34     -15.285 -53.464   5.432  1.00118.62           C  
ANISOU   69  CB  LYS A  34    19365  16909   8797  -2848   2089   2376       C  
ATOM     70  CG  LYS A  34     -14.648 -54.769   5.826  0.00120.74           C  
ANISOU   70  CG  LYS A  34    19628  17235   9013  -3205   1311   2666       C  
ATOM     71  CD  LYS A  34     -14.508 -54.893   7.339  0.00126.38           C  
ANISOU   71  CD  LYS A  34    20951  18063   9004  -3728   1315   2751       C  
ATOM     72  CE  LYS A  34     -13.892 -56.223   7.739  0.00126.75           C  
ANISOU   72  CE  LYS A  34    20933  18169   9059  -4080    517   3131       C  
ATOM     73  NZ  LYS A  34     -13.739 -56.346   9.215  0.00132.58           N  
ANISOU   73  NZ  LYS A  34    22266  19050   9060  -4669    459   3264       N  
ATOM     74  N   GLU A  35     -15.789 -50.841   3.379  1.00115.04           N  
ANISOU   74  N   GLU A  35    18467  16155   9087  -1870   3156   1796       N  
ATOM     75  CA  GLU A  35     -16.563 -49.628   3.078  1.00116.42           C  
ANISOU   75  CA  GLU A  35    18585  16236   9413  -1482   3990   1678       C  
ATOM     76  C   GLU A  35     -16.831 -49.437   1.574  1.00111.91           C  
ANISOU   76  C   GLU A  35    17314  15664   9544  -1096   3907   1769       C  
ATOM     77  O   GLU A  35     -17.238 -48.350   1.148  1.00112.25           O  
ANISOU   77  O   GLU A  35    17255  15594   9801   -758   4480   1672       O  
ATOM     78  CB  GLU A  35     -15.850 -48.393   3.645  1.00118.07           C  
ANISOU   78  CB  GLU A  35    19510  16188   9164  -1568   4314   1208       C  
ATOM     79  CG  GLU A  35     -16.105 -48.258   5.204  0.00127.35           C  
ANISOU   79  CG  GLU A  35    21475  17341   9571  -1922   4804   1143       C  
ATOM     80  CD  GLU A  35     -17.527 -47.901   5.610  0.00132.20           C  
ANISOU   80  CD  GLU A  35    22066  17970  10193  -1628   5839   1325       C  
ATOM     81  OE1 GLU A  35     -18.182 -47.112   4.895  0.00131.97           O  
ANISOU   81  OE1 GLU A  35    21678  17833  10632  -1127   6436   1353       O  
ATOM     82  OE2 GLU A  35     -17.989 -48.407   6.654  0.00136.72           O  
ANISOU   82  OE2 GLU A  35    22956  18668  10322  -1895   6073   1488       O  
ATOM     83  N   ILE A  36     -16.602 -50.485   0.780  1.00107.62           N  
ANISOU   83  N   ILE A  36    16339  15216   9337  -1171   3217   1965       N  
ATOM     84  CA  ILE A  36     -16.941 -50.484  -0.645  1.00104.28           C  
ANISOU   84  CA  ILE A  36    15300  14819   9501   -929   3088   2106       C  
ATOM     85  C   ILE A  36     -18.103 -51.444  -0.879  1.00105.18           C  
ANISOU   85  C   ILE A  36    14951  15169   9842  -1001   3061   2640       C  
ATOM     86  O   ILE A  36     -18.109 -52.544  -0.330  1.00106.29           O  
ANISOU   86  O   ILE A  36    15202  15394   9788  -1286   2717   2824       O  
ATOM     87  CB  ILE A  36     -15.756 -50.951  -1.525  1.00 99.08           C  
ANISOU   87  CB  ILE A  36    14574  14032   9039  -1001   2347   1906       C  
ATOM     88  CG1 ILE A  36     -14.525 -50.074  -1.297  1.00 98.59           C  
ANISOU   88  CG1 ILE A  36    14918  13783   8760   -992   2271   1462       C  
ATOM     89  CG2 ILE A  36     -16.139 -50.932  -3.009  1.00 95.35           C  
ANISOU   89  CG2 ILE A  36    13560  13579   9089   -829   2243   2034       C  
ATOM     90  CD1 ILE A  36     -13.254 -50.649  -1.904  1.00 94.79           C  
ANISOU   90  CD1 ILE A  36    14388  13193   8436  -1074   1569   1341       C  
ATOM     91  N   GLU A  37     -19.072 -51.020  -1.693  1.00105.74           N  
ANISOU   91  N   GLU A  37    14494  15352  10328   -781   3390   2939       N  
ATOM     92  CA  GLU A  37     -20.179 -51.881  -2.119  1.00107.55           C  
ANISOU   92  CA  GLU A  37    14211  15838  10816   -920   3275   3532       C  
ATOM     93  C   GLU A  37     -20.025 -52.218  -3.603  1.00103.89           C  
ANISOU   93  C   GLU A  37    13384  15354  10737  -1004   2740   3606       C  
ATOM     94  O   GLU A  37     -20.284 -51.384  -4.473  1.00103.57           O  
ANISOU   94  O   GLU A  37    12999  15322  11030   -800   2937   3661       O  
ATOM     95  CB  GLU A  37     -21.533 -51.212  -1.846  1.00112.38           C  
ANISOU   95  CB  GLU A  37    14438  16650  11610   -677   4070   3992       C  
ATOM     96  CG  GLU A  37     -22.735 -52.205  -2.028  0.00116.35           C  
ANISOU   96  CG  GLU A  37    14415  17492  12303   -919   3928   4727       C  
ATOM     97  CD  GLU A  37     -24.067 -51.595  -1.619  0.00122.28           C  
ANISOU   97  CD  GLU A  37    14727  18471  13263   -652   4769   5288       C  
ATOM     98  OE1 GLU A  37     -24.118 -50.378  -1.343  0.00124.13           O  
ANISOU   98  OE1 GLU A  37    15047  18555  13562   -235   5508   5106       O  
ATOM     99  OE2 GLU A  37     -25.069 -52.340  -1.578  0.00125.10           O  
ANISOU   99  OE2 GLU A  37    14653  19142  13736   -860   4716   5947       O  
ATOM    100  N   VAL A  38     -19.588 -53.445  -3.877  1.00102.19           N  
ANISOU  100  N   VAL A  38    13294  15077  10457  -1323   2086   3611       N  
ATOM    101  CA  VAL A  38     -19.313 -53.903  -5.242  1.00100.00           C  
ANISOU  101  CA  VAL A  38    12857  14699  10438  -1474   1582   3605       C  
ATOM    102  C   VAL A  38     -20.602 -54.252  -5.998  1.00103.18           C  
ANISOU  102  C   VAL A  38    12758  15359  11086  -1709   1540   4228       C  
ATOM    103  O   VAL A  38     -21.592 -54.668  -5.404  1.00108.90           O  
ANISOU  103  O   VAL A  38    13290  16329  11759  -1851   1695   4715       O  
ATOM    104  CB  VAL A  38     -18.322 -55.100  -5.227  1.00 97.49           C  
ANISOU  104  CB  VAL A  38    12944  14130   9966  -1701    989   3375       C  
ATOM    105  CG1 VAL A  38     -18.187 -55.761  -6.601  1.00 95.45           C  
ANISOU  105  CG1 VAL A  38    12633  13718   9914  -1919    550   3403       C  
ATOM    106  CG2 VAL A  38     -16.966 -54.628  -4.751  1.00 95.32           C  
ANISOU  106  CG2 VAL A  38    13035  13636   9546  -1491    956   2855       C  
ATOM    107  N   GLU A  39     -20.560 -54.079  -7.315  1.00102.17           N  
ANISOU  107  N   GLU A  39    12424  15190  11205  -1797   1304   4245       N  
ATOM    108  CA  GLU A  39     -21.721 -54.216  -8.190  1.00104.97           C  
ANISOU  108  CA  GLU A  39    12275  15809  11798  -2090   1211   4880       C  
ATOM    109  C   GLU A  39     -21.315 -54.994  -9.464  1.00102.41           C  
ANISOU  109  C   GLU A  39    12148  15299  11463  -2511    599   4784       C  
ATOM    110  O   GLU A  39     -20.302 -55.697  -9.464  1.00100.67           O  
ANISOU  110  O   GLU A  39    12443  14746  11061  -2563    297   4322       O  
ATOM    111  CB  GLU A  39     -22.227 -52.809  -8.524  1.00106.84           C  
ANISOU  111  CB  GLU A  39    12013  16211  12370  -1744   1712   5069       C  
ATOM    112  CG  GLU A  39     -23.698 -52.561  -8.290  1.00114.51           C  
ANISOU  112  CG  GLU A  39    12351  17570  13587  -1746   2098   5885       C  
ATOM    113  CD  GLU A  39     -24.016 -51.076  -8.346  1.00116.48           C  
ANISOU  113  CD  GLU A  39    12199  17868  14192  -1243   2756   5987       C  
ATOM    114  OE1 GLU A  39     -24.026 -50.507  -9.459  1.00120.01           O  
ANISOU  114  OE1 GLU A  39    12336  18333  14928  -1267   2621   6096       O  
ATOM    115  OE2 GLU A  39     -24.231 -50.472  -7.275  1.00124.92           O  
ANISOU  115  OE2 GLU A  39    13313  18921  15231   -835   3431   5945       O  
ATOM    116  N   GLU A  40     -22.090 -54.871 -10.541  1.00102.80           N  
ANISOU  116  N   GLU A  40    11813  15543  11704  -2828    442   5249       N  
ATOM    117  CA  GLU A  40     -21.884 -55.690 -11.745  1.00101.14           C  
ANISOU  117  CA  GLU A  40    11882  15157  11389  -3365   -115   5222       C  
ATOM    118  C   GLU A  40     -20.530 -55.486 -12.444  1.00 95.83           C  
ANISOU  118  C   GLU A  40    11641  14089  10681  -3192   -228   4493       C  
ATOM    119  O   GLU A  40     -19.924 -54.410 -12.387  1.00 89.82           O  
ANISOU  119  O   GLU A  40    10772  13291  10066  -2721     67   4136       O  
ATOM    120  CB  GLU A  40     -23.036 -55.498 -12.751  1.00103.89           C  
ANISOU  120  CB  GLU A  40    11713  15849  11910  -3835   -289   5952       C  
ATOM    121  CG  GLU A  40     -22.978 -54.238 -13.623  1.00104.57           C  
ANISOU  121  CG  GLU A  40    11409  16031  12290  -3634   -125   5951       C  
ATOM    122  CD  GLU A  40     -23.519 -52.982 -12.948  1.00107.32           C  
ANISOU  122  CD  GLU A  40    11141  16642  12993  -3057    496   6230       C  
ATOM    123  OE1 GLU A  40     -23.528 -52.913 -11.704  1.00105.52           O  
ANISOU  123  OE1 GLU A  40    10966  16412  12717  -2666    897   6121       O  
ATOM    124  OE2 GLU A  40     -23.926 -52.048 -13.674  1.00112.71           O  
ANISOU  124  OE2 GLU A  40    11321  17505  13998  -3004    612   6565       O  
ATOM    125  N   VAL A  41     -20.073 -56.549 -13.099  1.00 95.93           N  
ANISOU  125  N   VAL A  41    12172  13784  10494  -3589   -627   4300       N  
ATOM    126  CA  VAL A  41     -18.832 -56.533 -13.858  1.00 91.26           C  
ANISOU  126  CA  VAL A  41    12008  12793   9875  -3468   -708   3679       C  
ATOM    127  C   VAL A  41     -19.010 -55.608 -15.035  1.00 91.22           C  
ANISOU  127  C   VAL A  41    11712  12933  10013  -3574   -706   3747       C  
ATOM    128  O   VAL A  41     -20.064 -55.597 -15.679  1.00 96.11           O  
ANISOU  128  O   VAL A  41    12037  13832  10648  -4058   -881   4313       O  
ATOM    129  CB  VAL A  41     -18.452 -57.948 -14.383  1.00 93.02           C  
ANISOU  129  CB  VAL A  41    12904  12584   9856  -3908  -1045   3525       C  
ATOM    130  CG1 VAL A  41     -17.425 -57.875 -15.519  1.00 90.02           C  
ANISOU  130  CG1 VAL A  41    12915  11825   9463  -3891  -1070   3014       C  
ATOM    131  CG2 VAL A  41     -17.920 -58.816 -13.249  1.00 89.39           C  
ANISOU  131  CG2 VAL A  41    12773  11877   9314  -3690  -1038   3354       C  
ATOM    132  N   VAL A  42     -17.974 -54.826 -15.302  1.00 86.06           N  
ANISOU  132  N   VAL A  42    11114  12115   9469  -3156   -538   3227       N  
ATOM    133  CA  VAL A  42     -17.972 -53.926 -16.440  1.00 83.83           C  
ANISOU  133  CA  VAL A  42    10600  11934   9318  -3233   -543   3226       C  
ATOM    134  C   VAL A  42     -16.748 -54.124 -17.351  1.00 82.36           C  
ANISOU  134  C   VAL A  42    10908  11351   9033  -3235   -635   2642       C  
ATOM    135  O   VAL A  42     -16.741 -53.624 -18.475  1.00 83.84           O  
ANISOU  135  O   VAL A  42    11030  11582   9242  -3456   -713   2640       O  
ATOM    136  CB  VAL A  42     -18.074 -52.445 -15.979  1.00 80.73           C  
ANISOU  136  CB  VAL A  42     9661  11796   9216  -2703   -163   3261       C  
ATOM    137  CG1 VAL A  42     -19.393 -52.197 -15.265  1.00 79.76           C  
ANISOU  137  CG1 VAL A  42     9016  12051   9237  -2703     31   3918       C  
ATOM    138  CG2 VAL A  42     -16.902 -52.052 -15.088  1.00 75.20           C  
ANISOU  138  CG2 VAL A  42     9181  10879   8514  -2119     80   2677       C  
ATOM    139  N   GLY A  43     -15.731 -54.853 -16.886  1.00 81.43           N  
ANISOU  139  N   GLY A  43    11259  10854   8828  -2997   -608   2205       N  
ATOM    140  CA  GLY A  43     -14.500 -55.026 -17.654  1.00 80.36           C  
ANISOU  140  CA  GLY A  43    11543  10324   8666  -2889   -587   1687       C  
ATOM    141  C   GLY A  43     -13.582 -56.135 -17.173  1.00 82.04           C  
ANISOU  141  C   GLY A  43    12262  10085   8823  -2711   -570   1395       C  
ATOM    142  O   GLY A  43     -13.729 -56.648 -16.054  1.00 85.23           O  
ANISOU  142  O   GLY A  43    12666  10499   9218  -2589   -589   1532       O  
ATOM    143  N   ARG A  44     -12.647 -56.513 -18.045  1.00 81.86           N  
ANISOU  143  N   ARG A  44    12670   9654   8779  -2701   -505   1029       N  
ATOM    144  CA  ARG A  44     -11.582 -57.470 -17.733  1.00 83.27           C  
ANISOU  144  CA  ARG A  44    13286   9336   9015  -2423   -397    763       C  
ATOM    145  C   ARG A  44     -10.363 -57.131 -18.572  1.00 82.46           C  
ANISOU  145  C   ARG A  44    13323   8965   9044  -2135   -178    357       C  
ATOM    146  O   ARG A  44     -10.395 -57.264 -19.791  1.00 83.73           O  
ANISOU  146  O   ARG A  44    13823   8938   9052  -2471   -127    219       O  
ATOM    147  CB  ARG A  44     -12.005 -58.908 -18.029  1.00 86.99           C  
ANISOU  147  CB  ARG A  44    14381   9409   9262  -2892   -493    864       C  
ATOM    148  CG  ARG A  44     -12.816 -59.541 -16.930  1.00 90.78           C  
ANISOU  148  CG  ARG A  44    14789  10032   9671  -3035   -679   1235       C  
ATOM    149  CD  ARG A  44     -12.737 -61.060 -16.973  1.00 95.64           C  
ANISOU  149  CD  ARG A  44    16093  10094  10151  -3292   -715   1238       C  
ATOM    150  NE  ARG A  44     -13.663 -61.658 -16.015  1.00 98.23           N  
ANISOU  150  NE  ARG A  44    16343  10611  10371  -3538   -944   1648       N  
ATOM    151  CZ  ARG A  44     -14.979 -61.766 -16.198  1.00102.97           C  
ANISOU  151  CZ  ARG A  44    16869  11522  10733  -4145  -1191   2054       C  
ATOM    152  NH1 ARG A  44     -15.729 -62.324 -15.257  1.00104.09           N  
ANISOU  152  NH1 ARG A  44    16911  11836  10801  -4317  -1366   2440       N  
ATOM    153  NH2 ARG A  44     -15.558 -61.320 -17.312  1.00104.52           N  
ANISOU  153  NH2 ARG A  44    17058  11887  10769  -4614  -1285   2140       N  
ATOM    154  N   GLY A  45      -9.292 -56.694 -17.918  1.00 81.25           N  
ANISOU  154  N   GLY A  45    12919   8806   9146  -1564    -58    202       N  
ATOM    155  CA  GLY A  45      -8.069 -56.308 -18.617  1.00 79.49           C  
ANISOU  155  CA  GLY A  45    12722   8382   9098  -1239    159   -113       C  
ATOM    156  C   GLY A  45      -7.127 -57.480 -18.816  1.00 81.81           C  
ANISOU  156  C   GLY A  45    13491   8076   9517  -1042    384   -245       C  
ATOM    157  O   GLY A  45      -7.567 -58.620 -18.975  1.00 82.30           O  
ANISOU  157  O   GLY A  45    14062   7779   9427  -1337    399   -189       O  
ATOM    158  N   ALA A  46      -5.825 -57.184 -18.814  1.00 82.03           N  
ANISOU  158  N   ALA A  46    13346   7979   9841   -543    580   -380       N  
ATOM    159  CA  ALA A  46      -4.773 -58.204 -18.883  1.00 84.73           C  
ANISOU  159  CA  ALA A  46    14003   7751  10441   -202    876   -416       C  
ATOM    160  C   ALA A  46      -4.962 -59.255 -17.782  1.00 86.81           C  
ANISOU  160  C   ALA A  46    14387   7824  10772   -157    749   -140       C  
ATOM    161  O   ALA A  46      -4.853 -60.455 -18.037  1.00 89.99           O  
ANISOU  161  O   ALA A  46    15319   7663  11209   -183    959   -142       O  
ATOM    162  CB  ALA A  46      -3.394 -57.549 -18.768  1.00 83.14           C  
ANISOU  162  CB  ALA A  46    13367   7611  10611    348   1018   -431       C  
ATOM    163  N   PHE A  47      -5.247 -58.785 -16.566  1.00 83.89           N  
ANISOU  163  N   PHE A  47    13574   7900  10399   -110    432     91       N  
ATOM    164  CA  PHE A  47      -5.583 -59.656 -15.440  1.00 85.19           C  
ANISOU  164  CA  PHE A  47    13810   7998  10562   -153    247    385       C  
ATOM    165  C   PHE A  47      -6.598 -58.990 -14.503  1.00 81.43           C  
ANISOU  165  C   PHE A  47    13015   8093   9832   -397    -63    547       C  
ATOM    166  O   PHE A  47      -6.726 -57.764 -14.454  1.00 75.65           O  
ANISOU  166  O   PHE A  47    11921   7791   9033   -374   -114    467       O  
ATOM    167  CB  PHE A  47      -4.321 -60.060 -14.662  1.00 87.82           C  
ANISOU  167  CB  PHE A  47    13945   8127  11294    332    284    606       C  
ATOM    168  CG  PHE A  47      -3.558 -58.898 -14.102  1.00 85.15           C  
ANISOU  168  CG  PHE A  47    13042   8225  11088    592    145    670       C  
ATOM    169  CD1 PHE A  47      -3.923 -58.328 -12.884  1.00 84.36           C  
ANISOU  169  CD1 PHE A  47    12655   8590  10809    471   -179    852       C  
ATOM    170  CD2 PHE A  47      -2.475 -58.362 -14.796  1.00 87.18           C  
ANISOU  170  CD2 PHE A  47    13102   8414  11609    916    353    555       C  
ATOM    171  CE1 PHE A  47      -3.225 -57.233 -12.373  1.00 83.97           C  
ANISOU  171  CE1 PHE A  47    12201   8903  10801    618   -316    894       C  
ATOM    172  CE2 PHE A  47      -1.766 -57.271 -14.289  1.00 85.92           C  
ANISOU  172  CE2 PHE A  47    12450   8660  11534   1080    177    644       C  
ATOM    173  CZ  PHE A  47      -2.144 -56.704 -13.075  1.00 83.91           C  
ANISOU  173  CZ  PHE A  47    11985   8840  11059    904   -172    804       C  
ATOM    174  N   GLY A  48      -7.305 -59.819 -13.747  1.00 83.43           N  
ANISOU  174  N   GLY A  48    13430   8314   9956   -615   -225    789       N  
ATOM    175  CA  GLY A  48      -8.314 -59.342 -12.829  1.00 81.36           C  
ANISOU  175  CA  GLY A  48    12915   8543   9455   -837   -432    980       C  
ATOM    176  C   GLY A  48      -9.626 -59.036 -13.521  1.00 79.83           C  
ANISOU  176  C   GLY A  48    12747   8579   9006  -1268   -451    985       C  
ATOM    177  O   GLY A  48      -9.868 -59.446 -14.654  1.00 82.25           O  
ANISOU  177  O   GLY A  48    13379   8630   9241  -1528   -388    877       O  
ATOM    178  N   VAL A  49     -10.465 -58.296 -12.817  1.00 77.47           N  
ANISOU  178  N   VAL A  49    12111   8759   8566  -1362   -521   1153       N  
ATOM    179  CA  VAL A  49     -11.838 -58.062 -13.209  1.00 77.51           C  
ANISOU  179  CA  VAL A  49    12010   9052   8388  -1762   -559   1348       C  
ATOM    180  C   VAL A  49     -12.215 -56.683 -12.677  1.00 76.79           C  
ANISOU  180  C   VAL A  49    11443   9437   8298  -1590   -444   1390       C  
ATOM    181  O   VAL A  49     -11.891 -56.361 -11.540  1.00 77.45           O  
ANISOU  181  O   VAL A  49    11413   9649   8365  -1354   -405   1398       O  
ATOM    182  CB  VAL A  49     -12.770 -59.156 -12.611  1.00 79.79           C  
ANISOU  182  CB  VAL A  49    12480   9329   8506  -2117   -725   1702       C  
ATOM    183  CG1 VAL A  49     -12.889 -59.026 -11.081  1.00 76.78           C  
ANISOU  183  CG1 VAL A  49    11883   9213   8079  -1945   -737   1890       C  
ATOM    184  CG2 VAL A  49     -14.147 -59.113 -13.264  1.00 81.45           C  
ANISOU  184  CG2 VAL A  49    12601   9792   8554  -2625   -813   1998       C  
ATOM    185  N   VAL A  50     -12.879 -55.863 -13.487  1.00 75.85           N  
ANISOU  185  N   VAL A  50    11081   9549   8190  -1730   -373   1434       N  
ATOM    186  CA  VAL A  50     -13.292 -54.534 -13.035  1.00 72.33           C  
ANISOU  186  CA  VAL A  50    10211   9481   7789  -1532   -180   1495       C  
ATOM    187  C   VAL A  50     -14.800 -54.500 -12.819  1.00 73.72           C  
ANISOU  187  C   VAL A  50    10115   9986   7908  -1806   -136   1968       C  
ATOM    188  O   VAL A  50     -15.560 -55.064 -13.606  1.00 74.69           O  
ANISOU  188  O   VAL A  50    10258  10132   7990  -2229   -305   2239       O  
ATOM    189  CB  VAL A  50     -12.886 -53.451 -14.035  1.00 70.86           C  
ANISOU  189  CB  VAL A  50     9848   9333   7744  -1405    -86   1267       C  
ATOM    190  CG1 VAL A  50     -13.170 -52.054 -13.465  1.00 65.88           C  
ANISOU  190  CG1 VAL A  50     8858   8993   7181  -1137    170   1292       C  
ATOM    191  CG2 VAL A  50     -11.408 -53.600 -14.393  1.00 69.01           C  
ANISOU  191  CG2 VAL A  50     9853   8776   7590  -1168   -124    868       C  
ATOM    192  N   CYS A  51     -15.223 -53.831 -11.752  1.00 74.02           N  
ANISOU  192  N   CYS A  51     9919  10274   7931  -1591    108   2098       N  
ATOM    193  CA  CYS A  51     -16.638 -53.727 -11.420  1.00 76.97           C  
ANISOU  193  CA  CYS A  51     9960  10977   8309  -1758    254   2609       C  
ATOM    194  C   CYS A  51     -17.077 -52.312 -11.149  1.00 76.71           C  
ANISOU  194  C   CYS A  51     9543  11178   8423  -1448    677   2687       C  
ATOM    195  O   CYS A  51     -16.305 -51.497 -10.664  1.00 73.10           O  
ANISOU  195  O   CYS A  51     9195  10632   7946  -1104    883   2318       O  
ATOM    196  CB  CYS A  51     -16.936 -54.547 -10.178  1.00 79.39           C  
ANISOU  196  CB  CYS A  51    10421  11318   8423  -1821    247   2789       C  
ATOM    197  SG  CYS A  51     -16.676 -56.266 -10.456  1.00 81.97           S  
ANISOU  197  SG  CYS A  51    11187  11341   8615  -2209   -205   2820       S  
ATOM    198  N   LYS A  52     -18.338 -52.045 -11.459  1.00 81.65           N  
ANISOU  198  N   LYS A  52     9727  12091   9206  -1596    811   3222       N  
ATOM    199  CA  LYS A  52     -19.029 -50.858 -10.971  1.00 85.53           C  
ANISOU  199  CA  LYS A  52     9825  12790   9881  -1267   1339   3453       C  
ATOM    200  C   LYS A  52     -19.182 -51.028  -9.458  1.00 87.51           C  
ANISOU  200  C   LYS A  52    10266  13067   9918  -1095   1650   3446       C  
ATOM    201  O   LYS A  52     -19.416 -52.138  -8.985  1.00 86.52           O  
ANISOU  201  O   LYS A  52    10294  12974   9604  -1355   1427   3616       O  
ATOM    202  CB  LYS A  52     -20.396 -50.728 -11.671  1.00 90.03           C  
ANISOU  202  CB  LYS A  52     9796  13682  10727  -1505   1371   4190       C  
ATOM    203  CG  LYS A  52     -21.431 -49.798 -11.016  1.00 94.86           C  
ANISOU  203  CG  LYS A  52     9917  14529  11596  -1169   2003   4663       C  
ATOM    204  CD  LYS A  52     -21.058 -48.326 -11.102  1.00 96.11           C  
ANISOU  204  CD  LYS A  52     9982  14563  11974   -688   2457   4389       C  
ATOM    205  CE  LYS A  52     -22.248 -47.446 -10.739  1.00101.24           C  
ANISOU  205  CE  LYS A  52    10069  15408  12990   -370   3125   5000       C  
ATOM    206  NZ  LYS A  52     -21.852 -46.026 -10.562  1.00102.71           N  
ANISOU  206  NZ  LYS A  52    10320  15369  13337    148   3682   4666       N  
ATOM    207  N   ALA A  53     -19.014 -49.939  -8.709  1.00 89.26           N  
ANISOU  207  N   ALA A  53    10546  13243  10127   -697   2163   3232       N  
ATOM    208  CA  ALA A  53     -19.133 -49.975  -7.248  1.00 93.57           C  
ANISOU  208  CA  ALA A  53    11368  13793  10391   -574   2524   3185       C  
ATOM    209  C   ALA A  53     -19.387 -48.593  -6.655  1.00 97.50           C  
ANISOU  209  C   ALA A  53    11862  14246  10938   -168   3257   3106       C  
ATOM    210  O   ALA A  53     -19.298 -47.570  -7.351  1.00 95.02           O  
ANISOU  210  O   ALA A  53    11355  13858  10889     56   3446   3026       O  
ATOM    211  CB  ALA A  53     -17.884 -50.586  -6.622  1.00 91.43           C  
ANISOU  211  CB  ALA A  53    11669  13307   9762   -669   2165   2696       C  
ATOM    212  N   LYS A  54     -19.720 -48.586  -5.362  1.00102.52           N  
ANISOU  212  N   LYS A  54    12758  14898  11296    -93   3697   3134       N  
ATOM    213  CA  LYS A  54     -19.903 -47.353  -4.598  1.00106.68           C  
ANISOU  213  CA  LYS A  54    13494  15286  11753    263   4492   2984       C  
ATOM    214  C   LYS A  54     -18.864 -47.292  -3.475  1.00107.83           C  
ANISOU  214  C   LYS A  54    14423  15216  11332    167   4474   2417       C  
ATOM    215  O   LYS A  54     -18.437 -48.331  -2.965  1.00106.66           O  
ANISOU  215  O   LYS A  54    14527  15121  10878   -140   4011   2363       O  
ATOM    216  CB  LYS A  54     -21.329 -47.270  -4.041  1.00112.25           C  
ANISOU  216  CB  LYS A  54    13851  16188  12613    426   5181   3578       C  
ATOM    217  CG  LYS A  54     -22.410 -47.080  -5.102  1.00110.41           C  
ANISOU  217  CG  LYS A  54    12773  16190  12989    531   5275   4264       C  
ATOM    218  CD  LYS A  54     -23.807 -47.113  -4.488  0.00120.93           C  
ANISOU  218  CD  LYS A  54    13682  17758  14508    685   5945   4966       C  
ATOM    219  CE  LYS A  54     -24.883 -46.976  -5.552  0.00122.84           C  
ANISOU  219  CE  LYS A  54    12997  18290  15387    716   5948   5793       C  
ATOM    220  NZ  LYS A  54     -26.252 -46.980  -4.967  0.00129.72           N  
ANISOU  220  NZ  LYS A  54    13349  19421  16516    900   6633   6591       N  
ATOM    221  N   TRP A  55     -18.446 -46.078  -3.115  1.00111.68           N  
ANISOU  221  N   TRP A  55    15307  15449  11679    385   4947   2035       N  
ATOM    222  CA  TRP A  55     -17.457 -45.873  -2.046  1.00114.37           C  
ANISOU  222  CA  TRP A  55    16446  15587  11423    199   4923   1535       C  
ATOM    223  C   TRP A  55     -17.512 -44.440  -1.502  1.00120.00           C  
ANISOU  223  C   TRP A  55    17634  16002  11961    440   5733   1248       C  
ATOM    224  O   TRP A  55     -17.177 -43.498  -2.217  1.00117.81           O  
ANISOU  224  O   TRP A  55    17291  15545  11925    647   5816   1057       O  
ATOM    225  CB  TRP A  55     -16.045 -46.188  -2.551  1.00110.33           C  
ANISOU  225  CB  TRP A  55    16075  15008  10837    -23   4098   1189       C  
ATOM    226  CG  TRP A  55     -14.966 -45.784  -1.589  1.00111.58           C  
ANISOU  226  CG  TRP A  55    16981  14981  10434   -255   4017    759       C  
ATOM    227  CD1 TRP A  55     -14.664 -46.379  -0.395  1.00115.54           C  
ANISOU  227  CD1 TRP A  55    17973  15519  10407   -603   3875    731       C  
ATOM    228  CD2 TRP A  55     -14.054 -44.689  -1.733  1.00111.37           C  
ANISOU  228  CD2 TRP A  55    17307  14722  10287   -237   4027    354       C  
ATOM    229  NE1 TRP A  55     -13.620 -45.720   0.211  1.00116.82           N  
ANISOU  229  NE1 TRP A  55    18776  15501  10110   -844   3772    359       N  
ATOM    230  CE2 TRP A  55     -13.225 -44.681  -0.591  1.00115.41           C  
ANISOU  230  CE2 TRP A  55    18532  15149  10168   -626   3862    117       C  
ATOM    231  CE3 TRP A  55     -13.859 -43.710  -2.716  1.00109.73           C  
ANISOU  231  CE3 TRP A  55    16886  14379  10427     24   4131    203       C  
ATOM    232  CZ2 TRP A  55     -12.213 -43.736  -0.407  1.00115.86           C  
ANISOU  232  CZ2 TRP A  55    19104  14998   9918   -795   3775   -250       C  
ATOM    233  CZ3 TRP A  55     -12.851 -42.771  -2.532  1.00109.73           C  
ANISOU  233  CZ3 TRP A  55    17393  14155  10145    -93   4074   -194       C  
ATOM    234  CH2 TRP A  55     -12.042 -42.793  -1.387  1.00113.56           C  
ANISOU  234  CH2 TRP A  55    18597  14565   9986   -514   3890   -410       C  
ATOM    235  N   ARG A  56     -17.912 -44.295  -0.232  1.00128.35           N  
ANISOU  235  N   ARG A  56    19229  16974  12564    385   6341   1207       N  
ATOM    236  CA  ARG A  56     -18.213 -42.986   0.380  1.00134.46           C  
ANISOU  236  CA  ARG A  56    20541  17397  13149    634   7323    980       C  
ATOM    237  C   ARG A  56     -19.198 -42.214  -0.506  1.00136.14           C  
ANISOU  237  C   ARG A  56    20088  17561  14077   1188   7945   1337       C  
ATOM    238  O   ARG A  56     -18.912 -41.093  -0.948  1.00136.12           O  
ANISOU  238  O   ARG A  56    20216  17260  14242   1425   8233   1098       O  
ATOM    239  CB  ARG A  56     -16.942 -42.147   0.603  1.00135.08           C  
ANISOU  239  CB  ARG A  56    21392  17149  12785    414   7137    369       C  
ATOM    240  CG  ARG A  56     -15.939 -42.704   1.606  1.00136.63           C  
ANISOU  240  CG  ARG A  56    22309  17370  12235   -181   6589     83       C  
ATOM    241  CD  ARG A  56     -14.633 -41.916   1.510  1.00136.36           C  
ANISOU  241  CD  ARG A  56    22811  17094  11906   -429   6213   -384       C  
ATOM    242  NE  ARG A  56     -13.601 -42.363   2.448  1.00139.42           N  
ANISOU  242  NE  ARG A  56    23851  17525  11596  -1059   5626   -565       N  
ATOM    243  CZ  ARG A  56     -12.328 -41.960   2.424  1.00139.38           C  
ANISOU  243  CZ  ARG A  56    24226  17423  11308  -1413   5063   -837       C  
ATOM    244  NH1 ARG A  56     -11.901 -41.098   1.502  1.00137.84           N  
ANISOU  244  NH1 ARG A  56    23858  17068  11446  -1188   5016  -1019       N  
ATOM    245  NH2 ARG A  56     -11.468 -42.429   3.321  1.00141.67           N  
ANISOU  245  NH2 ARG A  56    25033  17803  10991  -2027   4508   -864       N  
ATOM    246  N   ALA A  57     -20.339 -42.846  -0.788  1.00136.57           N  
ANISOU  246  N   ALA A  57    19394  17928  14569   1352   8090   1971       N  
ATOM    247  CA  ALA A  57     -21.381 -42.284  -1.661  1.00137.78           C  
ANISOU  247  CA  ALA A  57    18739  18136  15474   1820   8583   2519       C  
ATOM    248  C   ALA A  57     -20.883 -41.860  -3.058  1.00131.71           C  
ANISOU  248  C   ALA A  57    17520  17357  15165   1888   8039   2473       C  
ATOM    249  O   ALA A  57     -21.517 -41.035  -3.715  1.00134.11           O  
ANISOU  249  O   ALA A  57    17332  17590  16035   2280   8512   2810       O  
ATOM    250  CB  ALA A  57     -22.083 -41.110  -0.959  1.00145.60           C  
ANISOU  250  CB  ALA A  57    20052  18762  16506   2292   9880   2545       C  
ATOM    251  N   LYS A  58     -19.771 -42.436  -3.513  1.00124.36           N  
ANISOU  251  N   LYS A  58    16731  16499  14020   1516   7076   2109       N  
ATOM    252  CA  LYS A  58     -19.169 -42.069  -4.796  1.00119.58           C  
ANISOU  252  CA  LYS A  58    15800  15877  13760   1531   6553   1998       C  
ATOM    253  C   LYS A  58     -19.327 -43.231  -5.773  1.00115.44           C  
ANISOU  253  C   LYS A  58    14638  15719  13504   1265   5754   2367       C  
ATOM    254  O   LYS A  58     -19.141 -44.388  -5.400  1.00114.77           O  
ANISOU  254  O   LYS A  58    14678  15795  13135    945   5288   2369       O  
ATOM    255  CB  LYS A  58     -17.680 -41.731  -4.616  1.00115.90           C  
ANISOU  255  CB  LYS A  58    16026  15165  12844   1320   6133   1294       C  
ATOM    256  CG  LYS A  58     -17.053 -40.939  -5.752  1.00110.79           C  
ANISOU  256  CG  LYS A  58    15184  14403  12509   1424   5867   1110       C  
ATOM    257  CD  LYS A  58     -15.613 -40.496  -5.460  0.00111.19           C  
ANISOU  257  CD  LYS A  58    15920  14219  12107   1209   5526    483       C  
ATOM    258  CE  LYS A  58     -15.550 -39.390  -4.418  0.00116.24           C  
ANISOU  258  CE  LYS A  58    17339  14470  12358   1300   6264    152       C  
ATOM    259  NZ  LYS A  58     -14.172 -38.848  -4.262  0.00114.64           N  
ANISOU  259  NZ  LYS A  58    17758  14060  11739   1021   5873   -374       N  
ATOM    260  N   ASP A  59     -19.691 -42.918  -7.015  1.00113.48           N  
ANISOU  260  N   ASP A  59    13753  15579  13784   1362   5613   2700       N  
ATOM    261  CA  ASP A  59     -19.643 -43.897  -8.102  1.00108.59           C  
ANISOU  261  CA  ASP A  59    12695  15229  13336   1019   4810   2937       C  
ATOM    262  C   ASP A  59     -18.181 -44.165  -8.446  1.00101.46           C  
ANISOU  262  C   ASP A  59    12223  14182  12144    800   4146   2314       C  
ATOM    263  O   ASP A  59     -17.360 -43.248  -8.496  1.00 98.25           O  
ANISOU  263  O   ASP A  59    12119  13542  11671    947   4232   1874       O  
ATOM    264  CB  ASP A  59     -20.421 -43.403  -9.322  1.00109.72           C  
ANISOU  264  CB  ASP A  59    12089  15531  14068   1106   4843   3492       C  
ATOM    265  CG  ASP A  59     -21.920 -43.359  -9.072  1.00120.27           C  
ANISOU  265  CG  ASP A  59    12832  17090  15773   1275   5401   4301       C  
ATOM    266  OD1 ASP A  59     -22.452 -44.304  -8.441  1.00123.50           O  
ANISOU  266  OD1 ASP A  59    13224  17695  16007   1093   5369   4572       O  
ATOM    267  OD2 ASP A  59     -22.569 -42.382  -9.507  1.00128.93           O  
ANISOU  267  OD2 ASP A  59    13447  18173  17368   1595   5878   4719       O  
ATOM    268  N   VAL A  60     -17.867 -45.433  -8.680  1.00 98.26           N  
ANISOU  268  N   VAL A  60    11842  13902  11589    452   3511   2319       N  
ATOM    269  CA  VAL A  60     -16.486 -45.909  -8.609  1.00 93.19           C  
ANISOU  269  CA  VAL A  60    11665  13107  10636    283   2988   1791       C  
ATOM    270  C   VAL A  60     -16.288 -47.189  -9.436  1.00 88.36           C  
ANISOU  270  C   VAL A  60    10921  12582  10069    -44   2339   1900       C  
ATOM    271  O   VAL A  60     -17.222 -47.974  -9.627  1.00 89.88           O  
ANISOU  271  O   VAL A  60    10839  12959  10352   -244   2250   2352       O  
ATOM    272  CB  VAL A  60     -16.078 -46.105  -7.093  1.00 95.99           C  
ANISOU  272  CB  VAL A  60    12593  13361  10516    253   3148   1539       C  
ATOM    273  CG1 VAL A  60     -15.428 -47.455  -6.815  1.00 93.70           C  
ANISOU  273  CG1 VAL A  60    12523  13092   9987    -46   2560   1468       C  
ATOM    274  CG2 VAL A  60     -15.182 -44.969  -6.619  1.00 96.57           C  
ANISOU  274  CG2 VAL A  60    13131  13195  10367    390   3368   1064       C  
ATOM    275  N   ALA A  61     -15.074 -47.370  -9.945  1.00 81.62           N  
ANISOU  275  N   ALA A  61    10284  11574   9154   -107   1921   1508       N  
ATOM    276  CA  ALA A  61     -14.668 -48.626 -10.562  1.00 79.26           C  
ANISOU  276  CA  ALA A  61    10045  11234   8836   -377   1399   1507       C  
ATOM    277  C   ALA A  61     -13.591 -49.260  -9.688  1.00 77.35           C  
ANISOU  277  C   ALA A  61    10231  10832   8324   -393   1172   1220       C  
ATOM    278  O   ALA A  61     -12.745 -48.553  -9.150  1.00 77.30           O  
ANISOU  278  O   ALA A  61    10446  10736   8187   -246   1243    920       O  
ATOM    279  CB  ALA A  61     -14.134 -48.389 -11.962  1.00 75.84           C  
ANISOU  279  CB  ALA A  61     9483  10729   8602   -420   1159   1354       C  
ATOM    280  N   ILE A  62     -13.632 -50.582  -9.526  1.00 76.61           N  
ANISOU  280  N   ILE A  62    10259  10703   8148   -606    883   1364       N  
ATOM    281  CA  ILE A  62     -12.560 -51.300  -8.832  1.00 76.26           C  
ANISOU  281  CA  ILE A  62    10549  10492   7934   -627    612   1189       C  
ATOM    282  C   ILE A  62     -12.162 -52.539  -9.602  1.00 72.22           C  
ANISOU  282  C   ILE A  62    10117   9783   7541   -772    255   1214       C  
ATOM    283  O   ILE A  62     -13.018 -53.199 -10.182  1.00 72.03           O  
ANISOU  283  O   ILE A  62    10016   9785   7569   -992    194   1451       O  
ATOM    284  CB  ILE A  62     -12.940 -51.718  -7.373  1.00 78.63           C  
ANISOU  284  CB  ILE A  62    11047  10885   7945   -722    698   1359       C  
ATOM    285  CG1 ILE A  62     -13.991 -52.824  -7.342  1.00 80.66           C  
ANISOU  285  CG1 ILE A  62    11218  11231   8200   -954    624   1742       C  
ATOM    286  CG2 ILE A  62     -13.457 -50.534  -6.585  1.00 81.86           C  
ANISOU  286  CG2 ILE A  62    11485  11429   8191   -593   1178   1328       C  
ATOM    287  CD1 ILE A  62     -14.010 -53.541  -6.025  1.00 87.10           C  
ANISOU  287  CD1 ILE A  62    12279  12078   8736  -1087    560   1880       C  
ATOM    288  N   LYS A  63     -10.871 -52.850  -9.622  1.00 70.65           N  
ANISOU  288  N   LYS A  63    10086   9368   7388   -667     42   1008       N  
ATOM    289  CA  LYS A  63     -10.451 -54.156 -10.108  1.00 73.52           C  
ANISOU  289  CA  LYS A  63    10617   9455   7861   -753   -197   1053       C  
ATOM    290  C   LYS A  63      -9.948 -55.020  -8.950  1.00 76.29           C  
ANISOU  290  C   LYS A  63    11159   9710   8116   -768   -378   1197       C  
ATOM    291  O   LYS A  63      -9.310 -54.529  -8.018  1.00 75.20           O  
ANISOU  291  O   LYS A  63    11042   9663   7866   -682   -413   1166       O  
ATOM    292  CB  LYS A  63      -9.454 -54.066 -11.276  1.00 70.25           C  
ANISOU  292  CB  LYS A  63    10211   8809   7671   -607   -239    802       C  
ATOM    293  CG  LYS A  63      -8.060 -53.635 -10.946  1.00 72.89           C  
ANISOU  293  CG  LYS A  63    10521   9075   8101   -348   -306    650       C  
ATOM    294  CD  LYS A  63      -7.174 -53.585 -12.200  1.00 70.93           C  
ANISOU  294  CD  LYS A  63    10245   8608   8098   -193   -278    444       C  
ATOM    295  CE  LYS A  63      -6.922 -54.960 -12.786  1.00 76.88           C  
ANISOU  295  CE  LYS A  63    11246   8971   8993   -215   -296    491       C  
ATOM    296  NZ  LYS A  63      -5.636 -55.011 -13.533  1.00 79.29           N  
ANISOU  296  NZ  LYS A  63    11542   9016   9567     54   -216    347       N  
ATOM    297  N   GLN A  64     -10.294 -56.304  -9.011  1.00 80.00           N  
ANISOU  297  N   GLN A  64    11795   9996   8603   -939   -513   1389       N  
ATOM    298  CA  GLN A  64      -9.940 -57.276  -7.993  1.00 83.57           C  
ANISOU  298  CA  GLN A  64    12417  10334   9002   -987   -707   1600       C  
ATOM    299  C   GLN A  64      -9.133 -58.391  -8.635  1.00 86.57           C  
ANISOU  299  C   GLN A  64    12986  10258   9648   -899   -827   1602       C  
ATOM    300  O   GLN A  64      -9.113 -58.525  -9.863  1.00 84.94           O  
ANISOU  300  O   GLN A  64    12864   9831   9578   -888   -729   1433       O  
ATOM    301  CB  GLN A  64     -11.208 -57.858  -7.365  1.00 85.24           C  
ANISOU  301  CB  GLN A  64    12683  10711   8994  -1281   -715   1890       C  
ATOM    302  CG  GLN A  64     -12.027 -56.847  -6.577  1.00 85.25           C  
ANISOU  302  CG  GLN A  64    12523  11119   8749  -1319   -484   1942       C  
ATOM    303  CD  GLN A  64     -13.370 -57.393  -6.107  1.00 87.22           C  
ANISOU  303  CD  GLN A  64    12747  11564   8828  -1592   -430   2287       C  
ATOM    304  OE1 GLN A  64     -13.682 -57.349  -4.918  1.00 89.54           O  
ANISOU  304  OE1 GLN A  64    13091  12050   8879  -1665   -353   2437       O  
ATOM    305  NE2 GLN A  64     -14.171 -57.897  -7.040  1.00 84.82           N  
ANISOU  305  NE2 GLN A  64    12382  11225   8620  -1794   -475   2442       N  
ATOM    306  N   ILE A  65      -8.453 -59.175  -7.800  1.00 90.97           N  
ANISOU  306  N   ILE A  65    13631  10653  10279   -842  -1009   1814       N  
ATOM    307  CA  ILE A  65      -7.847 -60.423  -8.251  1.00 94.48           C  
ANISOU  307  CA  ILE A  65    14295  10596  11009   -741  -1052   1908       C  
ATOM    308  C   ILE A  65      -8.940 -61.490  -8.292  1.00 97.04           C  
ANISOU  308  C   ILE A  65    14907  10778  11187  -1072  -1103   2071       C  
ATOM    309  O   ILE A  65      -9.665 -61.667  -7.313  1.00 98.58           O  
ANISOU  309  O   ILE A  65    15079  11231  11146  -1300  -1234   2306       O  
ATOM    310  CB  ILE A  65      -6.664 -60.886  -7.343  1.00 98.21           C  
ANISOU  310  CB  ILE A  65    14682  10933  11698   -539  -1242   2190       C  
ATOM    311  CG1 ILE A  65      -7.093 -61.100  -5.886  1.00102.89           C  
ANISOU  311  CG1 ILE A  65    15271  11808  12013   -793  -1484   2503       C  
ATOM    312  CG2 ILE A  65      -5.537 -59.874  -7.377  1.00 99.38           C  
ANISOU  312  CG2 ILE A  65    14540  11226  11995   -280  -1242   2100       C  
ATOM    313  CD1 ILE A  65      -6.077 -61.827  -5.009  0.00104.66           C  
ANISOU  313  CD1 ILE A  65    15436  11873  12456   -703  -1745   2910       C  
ATOM    314  N   GLU A  66      -9.086 -62.169  -9.431  1.00 98.34           N  
ANISOU  314  N   GLU A  66    15382  10539  11446  -1150   -990   1949       N  
ATOM    315  CA  GLU A  66      -9.996 -63.324  -9.536  1.00101.09           C  
ANISOU  315  CA  GLU A  66    16103  10660  11648  -1528  -1078   2129       C  
ATOM    316  C   GLU A  66      -9.361 -64.559  -8.888  1.00103.98           C  
ANISOU  316  C   GLU A  66    16699  10591  12219  -1410  -1177   2377       C  
ATOM    317  O   GLU A  66     -10.055 -65.478  -8.453  1.00105.27           O  
ANISOU  317  O   GLU A  66    17096  10658  12242  -1714  -1333   2627       O  
ATOM    318  CB  GLU A  66     -10.353 -63.616 -11.002  1.00101.23           C  
ANISOU  318  CB  GLU A  66    16494  10354  11615  -1758   -933   1910       C  
ATOM    319  CG  GLU A  66     -11.485 -62.761 -11.544  1.00100.42           C  
ANISOU  319  CG  GLU A  66    16197  10709  11250  -2102   -953   1883       C  
ATOM    320  CD  GLU A  66     -11.724 -62.974 -13.030  1.00102.84           C  
ANISOU  320  CD  GLU A  66    16890  10721  11462  -2407   -861   1689       C  
ATOM    321  OE1 GLU A  66     -11.062 -62.301 -13.856  1.00103.79           O  
ANISOU  321  OE1 GLU A  66    16963  10774  11700  -2190   -672   1383       O  
ATOM    322  OE2 GLU A  66     -12.590 -63.808 -13.368  1.00105.44           O  
ANISOU  322  OE2 GLU A  66    17599  10900  11563  -2925   -996   1863       O  
ATOM    323  N   SER A  67      -8.034 -64.549  -8.819  1.00104.91           N  
ANISOU  323  N   SER A  67    16701  10462  12697   -966  -1092   2365       N  
ATOM    324  CA  SER A  67      -7.251 -65.673  -8.352  1.00109.20           C  
ANISOU  324  CA  SER A  67    17393  10530  13568   -757  -1127   2656       C  
ATOM    325  C   SER A  67      -6.061 -65.178  -7.524  1.00109.22           C  
ANISOU  325  C   SER A  67    16932  10723  13842   -397  -1244   2879       C  
ATOM    326  O   SER A  67      -5.451 -64.158  -7.847  1.00105.21           O  
ANISOU  326  O   SER A  67    16132  10433  13411   -180  -1155   2692       O  
ATOM    327  CB  SER A  67      -6.771 -66.475  -9.565  1.00111.89           C  
ANISOU  327  CB  SER A  67    18198  10133  14183   -579   -778   2471       C  
ATOM    328  OG  SER A  67      -5.517 -67.084  -9.328  1.00117.07           O  
ANISOU  328  OG  SER A  67    18788  10339  15355   -106   -649   2716       O  
ATOM    329  N   GLU A  68      -5.733 -65.917  -6.465  1.00114.13           N  
ANISOU  329  N   GLU A  68    17493  11272  14600   -389  -1481   3326       N  
ATOM    330  CA  GLU A  68      -4.575 -65.614  -5.609  1.00115.37           C  
ANISOU  330  CA  GLU A  68    17219  11598  15017   -150  -1680   3684       C  
ATOM    331  C   GLU A  68      -3.252 -65.544  -6.395  1.00116.83           C  
ANISOU  331  C   GLU A  68    17217  11421  15752    368  -1416   3691       C  
ATOM    332  O   GLU A  68      -2.325 -64.833  -6.004  1.00116.51           O  
ANISOU  332  O   GLU A  68    16739  11661  15866    530  -1557   3886       O  
ATOM    333  CB  GLU A  68      -4.464 -66.657  -4.488  1.00118.87           C  
ANISOU  333  CB  GLU A  68    17677  11920  15570   -260  -1979   4240       C  
ATOM    334  CG  GLU A  68      -5.633 -66.664  -3.489  0.00120.54           C  
ANISOU  334  CG  GLU A  68    17996  12572  15232   -773  -2262   4325       C  
ATOM    335  CD  GLU A  68      -5.835 -65.343  -2.766  0.00117.17           C  
ANISOU  335  CD  GLU A  68    17320  12838  14359   -994  -2410   4212       C  
ATOM    336  OE1 GLU A  68      -4.837 -64.639  -2.503  0.00117.09           O  
ANISOU  336  OE1 GLU A  68    17011  13006  14470   -843  -2512   4308       O  
ATOM    337  OE2 GLU A  68      -6.998 -65.011  -2.453  0.00115.10           O  
ANISOU  337  OE2 GLU A  68    17182  12927  13625  -1331  -2401   4057       O  
ATOM    338  N   SER A  69      -3.182 -66.276  -7.505  1.00118.36           N  
ANISOU  338  N   SER A  69    17775  10988  16208    587  -1015   3495       N  
ATOM    339  CA  SER A  69      -1.998 -66.301  -8.364  1.00119.90           C  
ANISOU  339  CA  SER A  69    17859  10764  16935   1112   -628   3482       C  
ATOM    340  C   SER A  69      -1.683 -64.957  -9.006  1.00115.14           C  
ANISOU  340  C   SER A  69    16975  10545  16231   1202   -528   3124       C  
ATOM    341  O   SER A  69      -0.540 -64.700  -9.369  1.00116.43           O  
ANISOU  341  O   SER A  69    16825  10589  16826   1620   -335   3249       O  
ATOM    342  CB  SER A  69      -2.179 -67.346  -9.462  1.00122.94           C  
ANISOU  342  CB  SER A  69    18878  10354  17478   1233   -139   3246       C  
ATOM    343  OG  SER A  69      -2.424 -68.622  -8.897  1.00128.39           O  
ANISOU  343  OG  SER A  69    19872  10617  18294   1162   -211   3589       O  
ATOM    344  N   GLU A  70      -2.694 -64.104  -9.146  1.00110.39           N  
ANISOU  344  N   GLU A  70    16453  10398  15093    821   -645   2731       N  
ATOM    345  CA  GLU A  70      -2.513 -62.777  -9.737  1.00106.21           C  
ANISOU  345  CA  GLU A  70    15679  10238  14438    865   -570   2389       C  
ATOM    346  C   GLU A  70      -1.991 -61.721  -8.740  1.00103.18           C  
ANISOU  346  C   GLU A  70    14795  10439  13971    833   -920   2601       C  
ATOM    347  O   GLU A  70      -1.810 -60.567  -9.113  1.00 99.08           O  
ANISOU  347  O   GLU A  70    14077  10231  13338    850   -891   2348       O  
ATOM    348  CB  GLU A  70      -3.835 -62.287 -10.363  1.00103.13           C  
ANISOU  348  CB  GLU A  70    15563  10059  13563    479   -519   1945       C  
ATOM    349  CG  GLU A  70      -4.488 -63.247 -11.376  1.00106.13           C  
ANISOU  349  CG  GLU A  70    16526   9917  13880    319   -252   1735       C  
ATOM    350  CD  GLU A  70      -5.718 -62.648 -12.079  1.00102.91           C  
ANISOU  350  CD  GLU A  70    16283   9792  13026   -110   -258   1408       C  
ATOM    351  OE1 GLU A  70      -6.403 -61.777 -11.497  1.00101.23           O  
ANISOU  351  OE1 GLU A  70    15774  10149  12538   -314   -479   1426       O  
ATOM    352  OE2 GLU A  70      -6.004 -63.058 -13.223  1.00106.96           O  
ANISOU  352  OE2 GLU A  70    17241   9936  13465   -264    -22   1166       O  
ATOM    353  N   ARG A  71      -1.744 -62.105  -7.489  1.00105.65           N  
ANISOU  353  N   ARG A  71    14952  10885  14306    736  -1261   3072       N  
ATOM    354  CA  ARG A  71      -1.304 -61.152  -6.454  1.00105.49           C  
ANISOU  354  CA  ARG A  71    14588  11405  14086    561  -1634   3292       C  
ATOM    355  C   ARG A  71      -0.085 -60.322  -6.893  1.00104.99           C  
ANISOU  355  C   ARG A  71    14135  11442  14316    834  -1602   3342       C  
ATOM    356  O   ARG A  71      -0.073 -59.104  -6.727  1.00100.60           O  
ANISOU  356  O   ARG A  71    13465  11310  13450    654  -1729   3152       O  
ATOM    357  CB  ARG A  71      -1.006 -61.884  -5.128  1.00108.50           C  
ANISOU  357  CB  ARG A  71    14872  11837  14516    400  -2020   3899       C  
ATOM    358  CG  ARG A  71      -1.062 -61.006  -3.877  1.00107.46           C  
ANISOU  358  CG  ARG A  71    14647  12287  13895    -34  -2429   4046       C  
ATOM    359  CD  ARG A  71       0.099 -61.189  -2.884  0.00115.36           C  
ANISOU  359  CD  ARG A  71    15304  13420  15108   -115  -2868   4753       C  
ATOM    360  NE  ARG A  71      -0.335 -61.780  -1.613  0.00117.84           N  
ANISOU  360  NE  ARG A  71    15768  13884  15123   -523  -3217   5123       N  
ATOM    361  CZ  ARG A  71       0.101 -62.931  -1.094  0.00122.69           C  
ANISOU  361  CZ  ARG A  71    16248  14261  16107   -472  -3430   5742       C  
ATOM    362  NH1 ARG A  71       1.014 -63.676  -1.715  0.00125.82           N  
ANISOU  362  NH1 ARG A  71    16351  14207  17248     26  -3279   6098       N  
ATOM    363  NH2 ARG A  71      -0.381 -63.341   0.075  0.00124.90           N  
ANISOU  363  NH2 ARG A  71    16695  14741  16022   -917  -3765   6036       N  
ATOM    364  N   LYS A  72       0.917 -60.986  -7.472  1.00109.89           N  
ANISOU  364  N   LYS A  72    14568  11643  15542   1274  -1389   3611       N  
ATOM    365  CA  LYS A  72       2.213 -60.356  -7.787  1.00112.08           C  
ANISOU  365  CA  LYS A  72    14373  12017  16194   1559  -1377   3837       C  
ATOM    366  C   LYS A  72       2.159 -59.298  -8.900  1.00109.05           C  
ANISOU  366  C   LYS A  72    14005  11748  15679   1638  -1105   3277       C  
ATOM    367  O   LYS A  72       2.696 -58.203  -8.739  1.00109.17           O  
ANISOU  367  O   LYS A  72    13724  12163  15593   1544  -1313   3310       O  
ATOM    368  CB  LYS A  72       3.258 -61.425  -8.137  1.00117.43           C  
ANISOU  368  CB  LYS A  72    14822  12166  17629   2081  -1108   4335       C  
ATOM    369  CG  LYS A  72       3.951 -62.063  -6.936  0.00124.44           C  
ANISOU  369  CG  LYS A  72    15346  13106  18829   2056  -1513   5174       C  
ATOM    370  CD  LYS A  72       5.012 -61.164  -6.318  0.00125.93           C  
ANISOU  370  CD  LYS A  72    14943  13808  19095   1927  -1956   5689       C  
ATOM    371  CE  LYS A  72       5.823 -61.904  -5.269  0.00132.67           C  
ANISOU  371  CE  LYS A  72    15368  14673  20369   1916  -2350   6659       C  
ATOM    372  NZ  LYS A  72       6.873 -61.040  -4.662  0.00135.05           N  
ANISOU  372  NZ  LYS A  72    15098  15507  20710   1677  -2858   7252       N  
ATOM    373  N   ALA A  73       1.530 -59.624 -10.027  1.00108.33           N  
ANISOU  373  N   ALA A  73    14287  11304  15568   1756   -669   2794       N  
ATOM    374  CA  ALA A  73       1.394 -58.672 -11.146  1.00104.61           C  
ANISOU  374  CA  ALA A  73    13858  10935  14953   1782   -420   2277       C  
ATOM    375  C   ALA A  73       0.608 -57.430 -10.724  1.00100.47           C  
ANISOU  375  C   ALA A  73    13339  10960  13874   1378   -699   1986       C  
ATOM    376  O   ALA A  73       0.917 -56.305 -11.123  1.00 98.19           O  
ANISOU  376  O   ALA A  73    12861  10936  13509   1377   -702   1791       O  
ATOM    377  CB  ALA A  73       0.708 -59.348 -12.328  1.00104.36           C  
ANISOU  377  CB  ALA A  73    14324  10433  14893   1827     30   1858       C  
ATOM    378  N   PHE A  74      -0.413 -57.676  -9.908  1.00101.12           N  
ANISOU  378  N   PHE A  74    13654  11177  13591   1052   -890   1983       N  
ATOM    379  CA  PHE A  74      -1.307 -56.661  -9.337  1.00 97.50           C  
ANISOU  379  CA  PHE A  74    13263  11169  12615    692  -1060   1762       C  
ATOM    380  C   PHE A  74      -0.576 -55.680  -8.401  1.00 97.13           C  
ANISOU  380  C   PHE A  74    12972  11511  12423    556  -1383   1966       C  
ATOM    381  O   PHE A  74      -0.993 -54.534  -8.250  1.00 93.66           O  
ANISOU  381  O   PHE A  74    12584  11376  11627    357  -1402   1703       O  
ATOM    382  CB  PHE A  74      -2.402 -57.399  -8.555  1.00102.02           C  
ANISOU  382  CB  PHE A  74    14109  11744  12909    419  -1155   1852       C  
ATOM    383  CG  PHE A  74      -3.673 -56.636  -8.385  1.00100.15           C  
ANISOU  383  CG  PHE A  74    14017  11821  12215    130  -1104   1569       C  
ATOM    384  CD1 PHE A  74      -3.784 -55.646  -7.412  1.00103.17           C  
ANISOU  384  CD1 PHE A  74    14364  12587  12247    -76  -1247   1574       C  
ATOM    385  CD2 PHE A  74      -4.786 -56.949  -9.160  1.00102.95           C  
ANISOU  385  CD2 PHE A  74    14568  12067  12481     34   -895   1353       C  
ATOM    386  CE1 PHE A  74      -4.969 -54.954  -7.238  1.00101.15           C  
ANISOU  386  CE1 PHE A  74    14233  12568  11630   -270  -1089   1355       C  
ATOM    387  CE2 PHE A  74      -5.977 -56.263  -8.997  1.00101.44           C  
ANISOU  387  CE2 PHE A  74    14412  12179  11952   -197   -820   1211       C  
ATOM    388  CZ  PHE A  74      -6.070 -55.264  -8.035  1.00100.67           C  
ANISOU  388  CZ  PHE A  74    14246  12429  11576   -298   -872   1210       C  
ATOM    389  N   ILE A  75       0.501 -56.143  -7.768  1.00100.03           N  
ANISOU  389  N   ILE A  75    13094  11847  13064    631  -1636   2477       N  
ATOM    390  CA  ILE A  75       1.292 -55.310  -6.856  1.00101.01           C  
ANISOU  390  CA  ILE A  75    13016  12339  13023    390  -2026   2773       C  
ATOM    391  C   ILE A  75       2.198 -54.380  -7.678  1.00 99.04           C  
ANISOU  391  C   ILE A  75    12473  12176  12984    575  -1963   2684       C  
ATOM    392  O   ILE A  75       2.356 -53.204  -7.349  1.00 96.62           O  
ANISOU  392  O   ILE A  75    12177  12189  12347    307  -2148   2581       O  
ATOM    393  CB  ILE A  75       2.109 -56.189  -5.817  1.00105.84           C  
ANISOU  393  CB  ILE A  75    13414  12938  13863    317  -2407   3501       C  
ATOM    394  CG1 ILE A  75       1.708 -55.857  -4.372  1.00104.25           C  
ANISOU  394  CG1 ILE A  75    13452  13086  13072   -245  -2799   3653       C  
ATOM    395  CG2 ILE A  75       3.638 -56.064  -6.000  1.00109.04           C  
ANISOU  395  CG2 ILE A  75    13294  13372  14764    527  -2576   4021       C  
ATOM    396  CD1 ILE A  75       0.317 -56.339  -3.978  1.00 99.60           C  
ANISOU  396  CD1 ILE A  75    13279  12448  12115   -416  -2650   3382       C  
ATOM    397  N   VAL A  76       2.772 -54.913  -8.755  1.00 99.97           N  
ANISOU  397  N   VAL A  76    12380  11976  13627   1018  -1664   2714       N  
ATOM    398  CA  VAL A  76       3.622 -54.131  -9.655  1.00 99.59           C  
ANISOU  398  CA  VAL A  76    12035  11988  13816   1230  -1541   2639       C  
ATOM    399  C   VAL A  76       2.841 -52.979 -10.277  1.00 94.35           C  
ANISOU  399  C   VAL A  76    11593  11495  12761   1078  -1391   2016       C  
ATOM    400  O   VAL A  76       3.343 -51.858 -10.369  1.00 94.18           O  
ANISOU  400  O   VAL A  76    11412  11734  12636    975  -1525   1966       O  
ATOM    401  CB  VAL A  76       4.208 -55.013 -10.773  1.00101.71           C  
ANISOU  401  CB  VAL A  76    12153  11811  14683   1752  -1100   2712       C  
ATOM    402  CG1 VAL A  76       4.833 -54.162 -11.876  1.00102.06           C  
ANISOU  402  CG1 VAL A  76    11974  11916  14887   1951   -877   2502       C  
ATOM    403  CG2 VAL A  76       5.230 -55.981 -10.193  1.00106.19           C  
ANISOU  403  CG2 VAL A  76    12361  12212  15776   1988  -1216   3456       C  
ATOM    404  N   GLU A  77       1.613 -53.258 -10.701  1.00 91.44           N  
ANISOU  404  N   GLU A  77    11573  10979  12191   1042  -1133   1600       N  
ATOM    405  CA  GLU A  77       0.750 -52.225 -11.272  1.00 87.42           C  
ANISOU  405  CA  GLU A  77    11226  10628  11361    900   -984   1102       C  
ATOM    406  C   GLU A  77       0.468 -51.073 -10.292  1.00 85.75           C  
ANISOU  406  C   GLU A  77    11104  10777  10702    561  -1226   1048       C  
ATOM    407  O   GLU A  77       0.381 -49.923 -10.713  1.00 85.22           O  
ANISOU  407  O   GLU A  77    11027  10860  10494    506  -1161    774       O  
ATOM    408  CB  GLU A  77      -0.563 -52.837 -11.775  1.00 85.74           C  
ANISOU  408  CB  GLU A  77    11325  10230  11023    850   -730    822       C  
ATOM    409  CG  GLU A  77      -1.442 -51.852 -12.538  1.00 82.16           C  
ANISOU  409  CG  GLU A  77    10946   9923  10349    732   -560    417       C  
ATOM    410  CD  GLU A  77      -2.647 -52.497 -13.204  1.00 84.44           C  
ANISOU  410  CD  GLU A  77    11479  10049  10556    626   -356    250       C  
ATOM    411  OE1 GLU A  77      -3.004 -53.639 -12.825  1.00 93.40           O  
ANISOU  411  OE1 GLU A  77    12799  10990  11699    579   -373    412       O  
ATOM    412  OE2 GLU A  77      -3.240 -51.851 -14.105  1.00 83.85           O  
ANISOU  412  OE2 GLU A  77    11406  10051  10403    544   -212      3       O  
ATOM    413  N   LEU A  78       0.318 -51.376  -9.001  1.00 87.02           N  
ANISOU  413  N   LEU A  78    11404  11041  10618    315  -1471   1302       N  
ATOM    414  CA  LEU A  78       0.163 -50.327  -7.974  1.00 87.50           C  
ANISOU  414  CA  LEU A  78    11672  11384  10191    -57  -1659   1260       C  
ATOM    415  C   LEU A  78       1.428 -49.477  -7.842  1.00 89.28           C  
ANISOU  415  C   LEU A  78    11703  11783  10435   -171  -1952   1455       C  
ATOM    416  O   LEU A  78       1.338 -48.258  -7.682  1.00 88.10           O  
ANISOU  416  O   LEU A  78    11739  11785   9950   -391  -1961   1222       O  
ATOM    417  CB  LEU A  78      -0.217 -50.909  -6.597  1.00 89.65           C  
ANISOU  417  CB  LEU A  78    12191  11727  10147   -360  -1860   1516       C  
ATOM    418  CG  LEU A  78      -1.693 -51.250  -6.344  1.00 85.49           C  
ANISOU  418  CG  LEU A  78    11958  11162   9364   -425  -1592   1296       C  
ATOM    419  CD1 LEU A  78      -1.779 -52.021  -4.990  0.00 94.34           C  
ANISOU  419  CD1 LEU A  78    13261  12346  10237   -717  -1848   1655       C  
ATOM    420  CD2 LEU A  78      -2.599 -50.127  -6.395  0.00 88.51           C  
ANISOU  420  CD2 LEU A  78    12559  11654   9416   -514  -1301    910       C  
ATOM    421  N   ARG A  79       2.597 -50.121  -7.911  1.00 92.62           N  
ANISOU  421  N   ARG A  79    11752  12168  11270    -25  -2172   1925       N  
ATOM    422  CA  ARG A  79       3.884 -49.423  -7.773  1.00 95.30           C  
ANISOU  422  CA  ARG A  79    11811  12715  11683   -166  -2512   2263       C  
ATOM    423  C   ARG A  79       4.121 -48.459  -8.927  1.00 92.67           C  
ANISOU  423  C   ARG A  79    11336  12402  11473     15  -2307   1925       C  
ATOM    424  O   ARG A  79       4.757 -47.423  -8.743  1.00 95.38           O  
ANISOU  424  O   ARG A  79    11646  12960  11633   -247  -2557   1995       O  
ATOM    425  CB  ARG A  79       5.050 -50.416  -7.674  1.00 99.34           C  
ANISOU  425  CB  ARG A  79    11838  13173  12734     30  -2729   2953       C  
ATOM    426  CG  ARG A  79       5.248 -50.982  -6.265  0.00105.80           C  
ANISOU  426  CG  ARG A  79    12715  14119  13365   -349  -3173   3498       C  
ATOM    427  CD  ARG A  79       6.409 -51.968  -6.219  0.00110.79           C  
ANISOU  427  CD  ARG A  79    12774  14680  14640   -100  -3362   4285       C  
ATOM    428  NE  ARG A  79       7.641 -51.396  -6.765  0.00112.51           N  
ANISOU  428  NE  ARG A  79    12484  15048  15215     13  -3482   4632       N  
ATOM    429  CZ  ARG A  79       8.761 -52.081  -6.988  0.00117.11           C  
ANISOU  429  CZ  ARG A  79    12445  15567  16485    347  -3526   5344       C  
ATOM    430  NH1 ARG A  79       8.838 -53.379  -6.706  0.00120.53           N  
ANISOU  430  NH1 ARG A  79    12708  15745  17342    617  -3457   5784       N  
ATOM    431  NH2 ARG A  79       9.820 -51.459  -7.497  0.00118.83           N  
ANISOU  431  NH2 ARG A  79    12186  15967  16998    428  -3615   5661       N  
ATOM    432  N   GLN A  80       3.612 -48.807 -10.108  1.00 89.69           N  
ANISOU  432  N   GLN A  80    10911  11799  11367    401  -1879   1579       N  
ATOM    433  CA  GLN A  80       3.642 -47.915 -11.266  1.00 86.73           C  
ANISOU  433  CA  GLN A  80    10449  11440  11064    541  -1655   1215       C  
ATOM    434  C   GLN A  80       2.574 -46.827 -11.122  1.00 81.87           C  
ANISOU  434  C   GLN A  80    10207  10921   9979    296  -1555    752       C  
ATOM    435  O   GLN A  80       2.891 -45.641 -11.142  1.00 80.67           O  
ANISOU  435  O   GLN A  80    10084  10921   9647    121  -1661    645       O  
ATOM    436  CB  GLN A  80       3.445 -48.709 -12.565  1.00 85.81           C  
ANISOU  436  CB  GLN A  80    10232  11037  11334    948  -1238   1032       C  
ATOM    437  CG  GLN A  80       4.652 -49.587 -12.931  1.00 92.90           C  
ANISOU  437  CG  GLN A  80    10747  11774  12776   1291  -1183   1467       C  
ATOM    438  CD  GLN A  80       4.333 -50.694 -13.940  1.00 93.78           C  
ANISOU  438  CD  GLN A  80    10969  11476  13186   1641   -712   1295       C  
ATOM    439  OE1 GLN A  80       3.203 -51.181 -14.024  1.00 99.80           O  
ANISOU  439  OE1 GLN A  80    12098  12078  13745   1558   -559   1004       O  
ATOM    440  NE2 GLN A  80       5.345 -51.107 -14.696  1.00 98.73           N  
ANISOU  440  NE2 GLN A  80    11307  11920  14286   2008   -461   1508       N  
ATOM    441  N   LEU A  81       1.318 -47.230 -10.948  1.00 79.87           N  
ANISOU  441  N   LEU A  81    10231  10566   9549    283  -1336    527       N  
ATOM    442  CA  LEU A  81       0.205 -46.272 -10.780  1.00 78.59           C  
ANISOU  442  CA  LEU A  81    10375  10466   9021    120  -1146    169       C  
ATOM    443  C   LEU A  81       0.369 -45.290  -9.598  1.00 79.50           C  
ANISOU  443  C   LEU A  81    10803  10725   8677   -248  -1333    187       C  
ATOM    444  O   LEU A  81      -0.232 -44.216  -9.602  1.00 78.37           O  
ANISOU  444  O   LEU A  81    10896  10589   8292   -335  -1128   -106       O  
ATOM    445  CB  LEU A  81      -1.144 -47.008 -10.661  1.00 79.70           C  
ANISOU  445  CB  LEU A  81    10693  10506   9082    152   -900     68       C  
ATOM    446  CG  LEU A  81      -1.886 -47.321 -11.969  1.00 79.40           C  
ANISOU  446  CG  LEU A  81    10540  10348   9281    347   -615   -130       C  
ATOM    447  CD1 LEU A  81      -2.873 -48.450 -11.794  1.00 79.89           C  
ANISOU  447  CD1 LEU A  81    10728  10303   9323    326   -511    -56       C  
ATOM    448  CD2 LEU A  81      -2.611 -46.085 -12.466  1.00 82.40           C  
ANISOU  448  CD2 LEU A  81    10938  10816   9555    316   -402   -396       C  
ATOM    449  N   SER A  82       1.162 -45.656  -8.590  1.00 82.75           N  
ANISOU  449  N   SER A  82    11255  11228   8959   -492  -1704    554       N  
ATOM    450  CA  SER A  82       1.485 -44.731  -7.492  1.00 84.83           C  
ANISOU  450  CA  SER A  82    11902  11618   8711   -964  -1942    601       C  
ATOM    451  C   SER A  82       2.319 -43.552  -7.984  1.00 82.82           C  
ANISOU  451  C   SER A  82    11571  11444   8454  -1067  -2082    541       C  
ATOM    452  O   SER A  82       2.246 -42.465  -7.420  1.00 82.43           O  
ANISOU  452  O   SER A  82    11967  11407   7947  -1419  -2098    369       O  
ATOM    453  CB  SER A  82       2.234 -45.448  -6.366  1.00 89.35           C  
ANISOU  453  CB  SER A  82    12489  12309   9152  -1290  -2401   1114       C  
ATOM    454  OG  SER A  82       3.530 -45.854  -6.783  1.00 92.58           O  
ANISOU  454  OG  SER A  82    12368  12804  10005  -1177  -2736   1569       O  
ATOM    455  N   ARG A  83       3.111 -43.787  -9.028  1.00 81.95           N  
ANISOU  455  N   ARG A  83    10937  11361   8837   -771  -2151    687       N  
ATOM    456  CA  ARG A  83       3.998 -42.774  -9.601  1.00 82.94           C  
ANISOU  456  CA  ARG A  83    10890  11595   9029   -847  -2311    701       C  
ATOM    457  C   ARG A  83       3.331 -41.923 -10.687  1.00 76.94           C  
ANISOU  457  C   ARG A  83    10154  10737   8344   -620  -1927    216       C  
ATOM    458  O   ARG A  83       3.686 -40.761 -10.850  1.00 77.48           O  
ANISOU  458  O   ARG A  83    10327  10855   8256   -806  -2009    103       O  
ATOM    459  CB  ARG A  83       5.280 -43.427 -10.144  1.00 84.95           C  
ANISOU  459  CB  ARG A  83    10528  11951   9798   -642  -2550   1183       C  
ATOM    460  CG  ARG A  83       6.362 -43.655  -9.082  1.00 93.91           C  
ANISOU  460  CG  ARG A  83    11551  13290  10841  -1031  -3103   1824       C  
ATOM    461  CD  ARG A  83       7.376 -44.748  -9.469  1.00 99.22           C  
ANISOU  461  CD  ARG A  83    11554  13990  12154   -687  -3206   2415       C  
ATOM    462  NE  ARG A  83       8.176 -44.427 -10.663  1.00105.24           N  
ANISOU  462  NE  ARG A  83    11828  14797  13363   -373  -3089   2481       N  
ATOM    463  CZ  ARG A  83       8.028 -44.973 -11.877  1.00101.84           C  
ANISOU  463  CZ  ARG A  83    11146  14163  13387    180  -2618   2265       C  
ATOM    464  NH1 ARG A  83       7.098 -45.898 -12.123  1.00100.47           N  
ANISOU  464  NH1 ARG A  83    11159  13714  13300    473  -2241   1972       N  
ATOM    465  NH2 ARG A  83       8.830 -44.591 -12.866  1.00 99.62           N  
ANISOU  465  NH2 ARG A  83    10456  13952  13443    393  -2523   2357       N  
ATOM    466  N   VAL A  84       2.368 -42.476 -11.421  1.00 72.96           N  
ANISOU  466  N   VAL A  84     9565  10095   8062   -274  -1544    -27       N  
ATOM    467  CA  VAL A  84       1.759 -41.730 -12.526  1.00 69.56           C  
ANISOU  467  CA  VAL A  84     9080   9603   7745    -95  -1232   -383       C  
ATOM    468  C   VAL A  84       0.743 -40.721 -12.025  1.00 68.68           C  
ANISOU  468  C   VAL A  84     9402   9416   7276   -248   -994   -671       C  
ATOM    469  O   VAL A  84       0.124 -40.905 -10.985  1.00 72.25           O  
ANISOU  469  O   VAL A  84    10208   9818   7426   -391   -911   -676       O  
ATOM    470  CB  VAL A  84       1.051 -42.618 -13.578  1.00 66.84           C  
ANISOU  470  CB  VAL A  84     8518   9151   7728    229   -936   -494       C  
ATOM    471  CG1 VAL A  84       1.939 -43.769 -14.022  1.00 68.88           C  
ANISOU  471  CG1 VAL A  84     8458   9371   8341    433  -1027   -235       C  
ATOM    472  CG2 VAL A  84      -0.280 -43.126 -13.061  1.00 70.12           C  
ANISOU  472  CG2 VAL A  84     9179   9479   7983    222   -712   -581       C  
ATOM    473  N   ASN A  85       0.566 -39.669 -12.808  1.00 65.69           N  
ANISOU  473  N   ASN A  85     8986   9010   6963   -191   -837   -889       N  
ATOM    474  CA  ASN A  85      -0.346 -38.598 -12.485  1.00 65.34           C  
ANISOU  474  CA  ASN A  85     9313   8833   6679   -257   -524  -1133       C  
ATOM    475  C   ASN A  85      -0.468 -37.637 -13.667  1.00 61.94           C  
ANISOU  475  C   ASN A  85     8674   8379   6483   -121   -379  -1291       C  
ATOM    476  O   ASN A  85       0.441 -36.851 -13.945  1.00 61.07           O  
ANISOU  476  O   ASN A  85     8536   8314   6352   -253   -598  -1297       O  
ATOM    477  CB  ASN A  85       0.142 -37.835 -11.265  1.00 70.34           C  
ANISOU  477  CB  ASN A  85    10480   9416   6829   -645   -675  -1142       C  
ATOM    478  CG  ASN A  85      -0.523 -36.490 -11.139  1.00 73.60           C  
ANISOU  478  CG  ASN A  85    11313   9612   7038   -689   -303  -1420       C  
ATOM    479  OD1 ASN A  85       0.125 -35.460 -11.296  1.00 79.13           O  
ANISOU  479  OD1 ASN A  85    12168  10268   7628   -876   -438  -1492       O  
ATOM    480  ND2 ASN A  85      -1.840 -36.492 -10.908  1.00 75.49           N  
ANISOU  480  ND2 ASN A  85    11711   9699   7272   -494    198  -1539       N  
ATOM    481  N   HIS A  86      -1.599 -37.703 -14.356  1.00 58.82           N  
ANISOU  481  N   HIS A  86     8110   7934   6307    102    -44  -1364       N  
ATOM    482  CA  HIS A  86      -1.760 -37.013 -15.610  1.00 56.22           C  
ANISOU  482  CA  HIS A  86     7493   7619   6249    215     47  -1433       C  
ATOM    483  C   HIS A  86      -3.237 -36.992 -15.981  1.00 56.19           C  
ANISOU  483  C   HIS A  86     7382   7557   6412    374    429  -1409       C  
ATOM    484  O   HIS A  86      -3.953 -37.946 -15.690  1.00 54.69           O  
ANISOU  484  O   HIS A  86     7168   7385   6225    423    530  -1306       O  
ATOM    485  CB  HIS A  86      -0.972 -37.742 -16.684  1.00 53.59           C  
ANISOU  485  CB  HIS A  86     6759   7431   6173    276   -188  -1357       C  
ATOM    486  CG  HIS A  86      -0.946 -37.024 -17.992  1.00 57.89           C  
ANISOU  486  CG  HIS A  86     7034   8024   6938    314   -153  -1419       C  
ATOM    487  ND1 HIS A  86      -1.944 -37.160 -18.934  1.00 50.37           N  
ANISOU  487  ND1 HIS A  86     5877   7082   6180    382     42  -1402       N  
ATOM    488  CD2 HIS A  86      -0.053 -36.146 -18.509  1.00 57.01           C  
ANISOU  488  CD2 HIS A  86     6821   7973   6866    241   -321  -1455       C  
ATOM    489  CE1 HIS A  86      -1.662 -36.400 -19.977  1.00 53.70           C  
ANISOU  489  CE1 HIS A  86     6093   7565   6745    348     -4  -1436       C  
ATOM    490  NE2 HIS A  86      -0.522 -35.773 -19.744  1.00 51.95           N  
ANISOU  490  NE2 HIS A  86     5929   7370   6441    285   -206  -1485       N  
ATOM    491  N   PRO A  87      -3.704 -35.903 -16.622  1.00 57.85           N  
ANISOU  491  N   PRO A  87     7492   7705   6783    438    626  -1439       N  
ATOM    492  CA  PRO A  87      -5.129 -35.758 -16.976  1.00 56.18           C  
ANISOU  492  CA  PRO A  87     7089   7460   6795    583    987  -1286       C  
ATOM    493  C   PRO A  87      -5.717 -36.842 -17.871  1.00 52.00           C  
ANISOU  493  C   PRO A  87     6182   7102   6473    569    903  -1096       C  
ATOM    494  O   PRO A  87      -6.907 -37.088 -17.808  1.00 57.06           O  
ANISOU  494  O   PRO A  87     6696   7758   7225    623   1139   -880       O  
ATOM    495  CB  PRO A  87      -5.169 -34.403 -17.700  1.00 55.88           C  
ANISOU  495  CB  PRO A  87     6937   7345   6950    626   1095  -1300       C  
ATOM    496  CG  PRO A  87      -4.002 -33.666 -17.156  1.00 55.31           C  
ANISOU  496  CG  PRO A  87     7234   7167   6615    498    924  -1524       C  
ATOM    497  CD  PRO A  87      -2.940 -34.698 -17.009  1.00 57.41           C  
ANISOU  497  CD  PRO A  87     7478   7606   6729    364    516  -1551       C  
ATOM    498  N   ASN A  88      -4.891 -37.481 -18.679  1.00 48.77           N  
ANISOU  498  N   ASN A  88     5628   6804   6099    475    596  -1151       N  
ATOM    499  CA  ASN A  88      -5.348 -38.494 -19.626  1.00 48.55           C  
ANISOU  499  CA  ASN A  88     5379   6878   6190    378    522  -1019       C  
ATOM    500  C   ASN A  88      -4.991 -39.905 -19.179  1.00 48.47           C  
ANISOU  500  C   ASN A  88     5525   6840   6050    359    403  -1041       C  
ATOM    501  O   ASN A  88      -4.889 -40.835 -19.995  1.00 49.54           O  
ANISOU  501  O   ASN A  88     5610   6985   6227    260    312  -1024       O  
ATOM    502  CB  ASN A  88      -4.771 -38.195 -21.015  1.00 44.82           C  
ANISOU  502  CB  ASN A  88     4696   6490   5842    272    366  -1071       C  
ATOM    503  CG  ASN A  88      -5.261 -36.864 -21.548  1.00 47.04           C  
ANISOU  503  CG  ASN A  88     4778   6800   6295    267    465   -976       C  
ATOM    504  OD1 ASN A  88      -4.487 -35.910 -21.685  1.00 44.79           O  
ANISOU  504  OD1 ASN A  88     4502   6494   6023    297    399  -1107       O  
ATOM    505  ND2 ASN A  88      -6.567 -36.769 -21.791  1.00 36.15           N  
ANISOU  505  ND2 ASN A  88     3198   5466   5072    226    623   -688       N  
ATOM    506  N   ILE A  89      -4.800 -40.057 -17.875  1.00 50.55           N  
ANISOU  506  N   ILE A  89     6029   7039   6139    428    423  -1071       N  
ATOM    507  CA  ILE A  89      -4.642 -41.365 -17.265  1.00 51.97           C  
ANISOU  507  CA  ILE A  89     6348   7180   6216    416    329  -1019       C  
ATOM    508  C   ILE A  89      -5.670 -41.517 -16.172  1.00 50.49           C  
ANISOU  508  C   ILE A  89     6317   6976   5890    420    520   -904       C  
ATOM    509  O   ILE A  89      -5.962 -40.571 -15.441  1.00 55.36           O  
ANISOU  509  O   ILE A  89     7078   7557   6400    464    714   -941       O  
ATOM    510  CB  ILE A  89      -3.232 -41.579 -16.726  1.00 52.81           C  
ANISOU  510  CB  ILE A  89     6559   7261   6245    446     98  -1079       C  
ATOM    511  CG1 ILE A  89      -2.257 -41.719 -17.894  1.00 50.64           C  
ANISOU  511  CG1 ILE A  89     6081   7000   6160    485    -20  -1131       C  
ATOM    512  CG2 ILE A  89      -3.173 -42.851 -15.922  1.00 56.92           C  
ANISOU  512  CG2 ILE A  89     7217   7724   6685    446     19   -959       C  
ATOM    513  CD1 ILE A  89      -0.806 -41.691 -17.471  1.00 55.90           C  
ANISOU  513  CD1 ILE A  89     6718   7689   6832    530   -242  -1083       C  
ATOM    514  N   VAL A  90      -6.232 -42.710 -16.078  1.00 51.07           N  
ANISOU  514  N   VAL A  90     6403   7049   5953    361    505   -764       N  
ATOM    515  CA  VAL A  90      -7.345 -42.949 -15.172  1.00 55.80           C  
ANISOU  515  CA  VAL A  90     7088   7668   6445    349    708   -597       C  
ATOM    516  C   VAL A  90      -6.954 -42.652 -13.717  1.00 59.65           C  
ANISOU  516  C   VAL A  90     7902   8102   6661    376    759   -680       C  
ATOM    517  O   VAL A  90      -5.924 -43.130 -13.228  1.00 60.85           O  
ANISOU  517  O   VAL A  90     8207   8222   6690    328    502   -737       O  
ATOM    518  CB  VAL A  90      -7.884 -44.381 -15.341  1.00 54.21           C  
ANISOU  518  CB  VAL A  90     6875   7470   6252    223    611   -419       C  
ATOM    519  CG1 VAL A  90      -6.893 -45.417 -14.816  1.00 57.15           C  
ANISOU  519  CG1 VAL A  90     7454   7731   6528    227    384   -482       C  
ATOM    520  CG2 VAL A  90      -9.233 -44.520 -14.685  1.00 56.39           C  
ANISOU  520  CG2 VAL A  90     7117   7828   6479    187    839   -162       C  
ATOM    521  N   LYS A  91      -7.766 -41.826 -13.054  1.00 64.55           N  
ANISOU  521  N   LYS A  91     8637   8700   7191    435   1115   -654       N  
ATOM    522  CA  LYS A  91      -7.555 -41.466 -11.646  1.00 68.86           C  
ANISOU  522  CA  LYS A  91     9619   9161   7384    385   1244   -753       C  
ATOM    523  C   LYS A  91      -7.721 -42.689 -10.736  1.00 72.01           C  
ANISOU  523  C   LYS A  91    10171   9604   7586    270   1136   -616       C  
ATOM    524  O   LYS A  91      -8.826 -43.235 -10.604  1.00 71.91           O  
ANISOU  524  O   LYS A  91    10049   9648   7626    297   1342   -414       O  
ATOM    525  CB  LYS A  91      -8.530 -40.360 -11.199  1.00 70.61           C  
ANISOU  525  CB  LYS A  91     9981   9276   7571    514   1798   -751       C  
ATOM    526  CG  LYS A  91      -8.242 -39.762  -9.799  0.00 74.89           C  
ANISOU  526  CG  LYS A  91    11142   9656   7657    402   2009   -935       C  
ATOM    527  CD  LYS A  91      -9.081 -38.519  -9.497  0.00 78.36           C  
ANISOU  527  CD  LYS A  91    11795   9881   8097    585   2668   -985       C  
ATOM    528  CE  LYS A  91      -8.521 -37.265 -10.160  0.00 77.51           C  
ANISOU  528  CE  LYS A  91    11719   9624   8108    639   2679  -1172       C  
ATOM    529  NZ  LYS A  91      -7.189 -36.879  -9.617  0.00 78.21           N  
ANISOU  529  NZ  LYS A  91    12304   9629   7784    334   2330  -1440       N  
ATOM    530  N   LEU A  92      -6.610 -43.125 -10.146  1.00 72.81           N  
ANISOU  530  N   LEU A  92    10478   9697   7489    122    783   -662       N  
ATOM    531  CA  LEU A  92      -6.639 -44.092  -9.058  1.00 76.31           C  
ANISOU  531  CA  LEU A  92    11140  10166   7687    -29    666   -520       C  
ATOM    532  C   LEU A  92      -6.932 -43.336  -7.758  1.00 80.43           C  
ANISOU  532  C   LEU A  92    12153  10635   7770   -175    953   -606       C  
ATOM    533  O   LEU A  92      -6.059 -42.641  -7.247  1.00 84.20           O  
ANISOU  533  O   LEU A  92    12956  11061   7974   -361    816   -736       O  
ATOM    534  CB  LEU A  92      -5.288 -44.819  -8.971  1.00 76.50           C  
ANISOU  534  CB  LEU A  92    11133  10204   7729   -134    169   -438       C  
ATOM    535  CG  LEU A  92      -5.195 -45.962  -7.951  1.00 76.97           C  
ANISOU  535  CG  LEU A  92    11347  10288   7611   -297    -38   -212       C  
ATOM    536  CD1 LEU A  92      -6.099 -47.093  -8.281  0.00 77.07           C  
ANISOU  536  CD1 LEU A  92    11190  10288   7807   -208     44    -67       C  
ATOM    537  CD2 LEU A  92      -3.744 -46.404  -7.806  0.00 79.04           C  
ANISOU  537  CD2 LEU A  92    11532  10559   7939   -384   -505    -48       C  
ATOM    538  N   TYR A  93      -8.155 -43.443  -7.231  1.00 83.27           N  
ANISOU  538  N   TYR A  93    12603  10997   8039   -124   1373   -516       N  
ATOM    539  CA  TYR A  93      -8.478 -42.837  -5.919  1.00 86.64           C  
ANISOU  539  CA  TYR A  93    13594  11330   7994   -272   1746   -609       C  
ATOM    540  C   TYR A  93      -7.605 -43.421  -4.811  1.00 87.23           C  
ANISOU  540  C   TYR A  93    14062  11449   7633   -649   1342   -568       C  
ATOM    541  O   TYR A  93      -6.846 -42.707  -4.161  1.00 89.87           O  
ANISOU  541  O   TYR A  93    14866  11704   7576   -925   1249   -717       O  
ATOM    542  CB  TYR A  93      -9.945 -43.041  -5.524  1.00 90.65           C  
ANISOU  542  CB  TYR A  93    14065  11861   8518   -128   2295   -438       C  
ATOM    543  CG  TYR A  93     -10.976 -42.323  -6.368  1.00 92.95           C  
ANISOU  543  CG  TYR A  93    13986  12116   9215    213   2788   -356       C  
ATOM    544  CD1 TYR A  93     -10.676 -41.138  -7.053  1.00 95.04           C  
ANISOU  544  CD1 TYR A  93    14218  12239   9653    363   2923   -540       C  
ATOM    545  CD2 TYR A  93     -12.277 -42.817  -6.454  1.00 96.99           C  
ANISOU  545  CD2 TYR A  93    14151  12750   9952    361   3108    -20       C  
ATOM    546  CE1 TYR A  93     -11.642 -40.484  -7.823  1.00 94.07           C  
ANISOU  546  CE1 TYR A  93    13701  12089   9952    671   3360   -375       C  
ATOM    547  CE2 TYR A  93     -13.247 -42.170  -7.213  1.00 97.91           C  
ANISOU  547  CE2 TYR A  93    13844  12870  10489    648   3532    188       C  
ATOM    548  CZ  TYR A  93     -12.926 -41.006  -7.893  1.00 96.19           C  
ANISOU  548  CZ  TYR A  93    13580  12500  10467    811   3660     17       C  
ATOM    549  OH  TYR A  93     -13.898 -40.380  -8.639  1.00 94.47           O  
ANISOU  549  OH  TYR A  93    12891  12292  10710   1088   4059    309       O  
ATOM    550  N   GLY A  94      -7.716 -44.726  -4.603  1.00 86.25           N  
ANISOU  550  N   GLY A  94    13752  11448   7569   -707   1074   -322       N  
ATOM    551  CA  GLY A  94      -6.931 -45.408  -3.579  1.00 89.05           C  
ANISOU  551  CA  GLY A  94    14388  11867   7579  -1067    647   -174       C  
ATOM    552  C   GLY A  94      -6.776 -46.887  -3.862  1.00 87.03           C  
ANISOU  552  C   GLY A  94    13750  11693   7624  -1019    252    116       C  
ATOM    553  O   GLY A  94      -7.080 -47.355  -4.963  1.00 84.07           O  
ANISOU  553  O   GLY A  94    12946  11302   7697   -745    255    149       O  
ATOM    554  N   ALA A  95      -6.306 -47.621  -2.860  1.00 88.96           N  
ANISOU  554  N   ALA A  95    14200  12001   7599  -1323    -83    341       N  
ATOM    555  CA  ALA A  95      -6.107 -49.058  -2.985  1.00 88.49           C  
ANISOU  555  CA  ALA A  95    13845  11960   7818  -1287   -441    651       C  
ATOM    556  C   ALA A  95      -6.387 -49.744  -1.664  1.00 92.57           C  
ANISOU  556  C   ALA A  95    14672  12562   7938  -1620   -538    887       C  
ATOM    557  O   ALA A  95      -6.672 -49.085  -0.660  1.00 97.45           O  
ANISOU  557  O   ALA A  95    15768  13231   8028  -1904   -322    790       O  
ATOM    558  CB  ALA A  95      -4.686 -49.348  -3.430  1.00 87.35           C  
ANISOU  558  CB  ALA A  95    13440  11783   7965  -1261   -933    809       C  
ATOM    559  N   CYS A  96      -6.298 -51.069  -1.665  1.00 91.97           N  
ANISOU  559  N   CYS A  96    14376  12472   8098  -1602   -835   1195       N  
ATOM    560  CA  CYS A  96      -6.371 -51.830  -0.429  1.00 96.07           C  
ANISOU  560  CA  CYS A  96    15141  13081   8281  -1951  -1043   1494       C  
ATOM    561  C   CYS A  96      -5.654 -53.164  -0.558  1.00 95.88           C  
ANISOU  561  C   CYS A  96    14819  12975   8636  -1910  -1523   1889       C  
ATOM    562  O   CYS A  96      -5.493 -53.671  -1.665  1.00 91.09           O  
ANISOU  562  O   CYS A  96    13865  12199   8545  -1562  -1537   1880       O  
ATOM    563  CB  CYS A  96      -7.826 -52.042  -0.035  1.00 97.52           C  
ANISOU  563  CB  CYS A  96    15471  13328   8253  -1964   -607   1461       C  
ATOM    564  SG  CYS A  96      -8.776 -52.929  -1.241  1.00 98.56           S  
ANISOU  564  SG  CYS A  96    15155  13375   8920  -1603   -458   1517       S  
ATOM    565  N   LEU A  97      -5.208 -53.708   0.578  1.00100.19           N  
ANISOU  565  N   LEU A  97    15539  13614   8916  -2283  -1889   2251       N  
ATOM    566  CA  LEU A  97      -4.584 -55.028   0.620  1.00102.19           C  
ANISOU  566  CA  LEU A  97    15518  13761   9547  -2246  -2315   2716       C  
ATOM    567  C   LEU A  97      -5.384 -56.040   1.439  1.00105.41           C  
ANISOU  567  C   LEU A  97    16087  14207   9759  -2460  -2351   2966       C  
ATOM    568  O   LEU A  97      -4.991 -57.203   1.493  1.00107.19           O  
ANISOU  568  O   LEU A  97    16117  14298  10311  -2418  -2664   3364       O  
ATOM    569  CB  LEU A  97      -3.155 -54.926   1.157  1.00103.94           C  
ANISOU  569  CB  LEU A  97    15656  14066   9771  -2500  -2841   3109       C  
ATOM    570  CG  LEU A  97      -2.255 -54.099   0.174  0.00104.42           C  
ANISOU  570  CG  LEU A  97    15444  14074  10156  -2231  -2843   2943       C  
ATOM    571  CD1 LEU A  97      -0.857 -54.056   0.713  0.00108.31           C  
ANISOU  571  CD1 LEU A  97    15773  14691  10690  -2514  -3401   3456       C  
ATOM    572  CD2 LEU A  97      -2.266 -54.599  -1.262  0.00100.48           C  
ANISOU  572  CD2 LEU A  97    14554  13307  10318  -1647  -2616   2799       C  
ATOM    573  N   ASN A  98      -6.498 -55.614   2.053  1.00108.27           N  
ANISOU  573  N   ASN A  98    16790  14725   9621  -2663  -1993   2761       N  
ATOM    574  CA  ASN A  98      -7.340 -56.513   2.875  1.00111.53           C  
ANISOU  574  CA  ASN A  98    17361  15219   9797  -2898  -1991   3007       C  
ATOM    575  C   ASN A  98      -7.666 -57.775   2.061  1.00111.21           C  
ANISOU  575  C   ASN A  98    16995  14958  10304  -2599  -2064   3178       C  
ATOM    576  O   ASN A  98      -7.183 -58.858   2.412  1.00114.88           O  
ANISOU  576  O   ASN A  98    17379  15318  10951  -2692  -2458   3591       O  
ATOM    577  CB  ASN A  98      -8.595 -55.800   3.406  1.00112.31           C  
ANISOU  577  CB  ASN A  98    17799  15490   9384  -3030  -1434   2741       C  
ATOM    578  CG  ASN A  98      -8.308 -54.657   4.371  0.00116.92           C  
ANISOU  578  CG  ASN A  98    18892  16210   9321  -3408  -1305   2566       C  
ATOM    579  OD1 ASN A  98      -8.855 -53.558   4.269  0.00116.46           O  
ANISOU  579  OD1 ASN A  98    19055  16155   9039  -3311   -767   2189       O  
ATOM    580  ND2 ASN A  98      -7.420 -54.928   5.321  0.00120.84           N  
ANISOU  580  ND2 ASN A  98    19607  16797   9511  -3878  -1810   2882       N  
ATOM    581  N   PRO A  99      -8.518 -57.654   1.012  1.00107.25           N  
ANISOU  581  N   PRO A  99    16345  14371  10036  -2292  -1690   2902       N  
ATOM    582  CA  PRO A  99      -8.208 -58.299  -0.264  1.00103.70           C  
ANISOU  582  CA  PRO A  99    15619  13618  10165  -1948  -1763   2884       C  
ATOM    583  C   PRO A  99      -7.634 -57.239  -1.230  1.00 99.84           C  
ANISOU  583  C   PRO A  99    14979  13083   9875  -1668  -1610   2533       C  
ATOM    584  O   PRO A  99      -8.093 -56.093  -1.226  1.00 97.71           O  
ANISOU  584  O   PRO A  99    14785  12990   9351  -1676  -1299   2245       O  
ATOM    585  CB  PRO A  99      -9.575 -58.806  -0.733  1.00102.07           C  
ANISOU  585  CB  PRO A  99    15399  13400   9982  -1941  -1509   2861       C  
ATOM    586  CG  PRO A  99     -10.559 -57.812  -0.173  1.00102.44           C  
ANISOU  586  CG  PRO A  99    15555  13768   9599  -2069  -1115   2710       C  
ATOM    587  CD  PRO A  99      -9.867 -57.055   0.967  1.00106.87           C  
ANISOU  587  CD  PRO A  99    16374  14490   9743  -2283  -1182   2682       C  
ATOM    588  N   VAL A 100      -6.637 -57.603  -2.035  1.00 98.24           N  
ANISOU  588  N   VAL A 100    14572  12624  10131  -1410  -1783   2574       N  
ATOM    589  CA  VAL A 100      -5.916 -56.606  -2.842  1.00 95.54           C  
ANISOU  589  CA  VAL A 100    14073  12268   9962  -1182  -1693   2300       C  
ATOM    590  C   VAL A 100      -6.765 -56.074  -4.011  1.00 91.95           C  
ANISOU  590  C   VAL A 100    13556  11786   9595   -996  -1314   1924       C  
ATOM    591  O   VAL A 100      -7.305 -56.847  -4.808  1.00 91.66           O  
ANISOU  591  O   VAL A 100    13492  11556   9777   -910  -1227   1920       O  
ATOM    592  CB  VAL A 100      -4.529 -57.123  -3.325  1.00 95.99           C  
ANISOU  592  CB  VAL A 100    13889  12076  10507   -940  -1939   2518       C  
ATOM    593  CG1 VAL A 100      -4.661 -58.241  -4.346  1.00 96.73           C  
ANISOU  593  CG1 VAL A 100    13937  11776  11040   -670  -1816   2531       C  
ATOM    594  CG2 VAL A 100      -3.706 -55.980  -3.889  1.00 95.25           C  
ANISOU  594  CG2 VAL A 100    13629  12058  10502   -793  -1902   2307       C  
ATOM    595  N   CYS A 101      -6.893 -54.750  -4.094  1.00 89.35           N  
ANISOU  595  N   CYS A 101    13234  11640   9075   -985  -1103   1644       N  
ATOM    596  CA  CYS A 101      -7.772 -54.134  -5.080  1.00 86.56           C  
ANISOU  596  CA  CYS A 101    12780  11312   8796   -848   -756   1373       C  
ATOM    597  C   CYS A 101      -7.475 -52.646  -5.272  1.00 84.03           C  
ANISOU  597  C   CYS A 101    12441  11106   8380   -767   -579   1087       C  
ATOM    598  O   CYS A 101      -6.996 -51.984  -4.354  1.00 85.68           O  
ANISOU  598  O   CYS A 101    12842  11424   8288   -919   -637   1071       O  
ATOM    599  CB  CYS A 101      -9.234 -54.323  -4.677  1.00 88.71           C  
ANISOU  599  CB  CYS A 101    13123  11734   8848  -1000   -514   1469       C  
ATOM    600  SG  CYS A 101      -9.904 -52.976  -3.707  1.00 99.38           S  
ANISOU  600  SG  CYS A 101    14654  13345   9761  -1092   -115   1340       S  
ATOM    601  N   LEU A 102      -7.775 -52.144  -6.473  1.00 80.51           N  
ANISOU  601  N   LEU A 102    11806  10621   8164   -582   -381    883       N  
ATOM    602  CA  LEU A 102      -7.561 -50.743  -6.857  1.00 77.01           C  
ANISOU  602  CA  LEU A 102    11314  10246   7698   -478   -197    617       C  
ATOM    603  C   LEU A 102      -8.902 -50.034  -7.008  1.00 74.48           C  
ANISOU  603  C   LEU A 102    10950  10045   7303   -451    225    558       C  
ATOM    604  O   LEU A 102      -9.822 -50.610  -7.565  1.00 73.61           O  
ANISOU  604  O   LEU A 102    10678   9951   7340   -458    308    697       O  
ATOM    605  CB  LEU A 102      -6.794 -50.685  -8.179  1.00 74.50           C  
ANISOU  605  CB  LEU A 102    10768   9794   7744   -282   -296    485       C  
ATOM    606  CG  LEU A 102      -5.285 -50.918  -8.037  1.00 76.22           C  
ANISOU  606  CG  LEU A 102    10949   9924   8089   -232   -618    565       C  
ATOM    607  CD1 LEU A 102      -4.858 -52.023  -7.577  0.00 78.62           C  
ANISOU  607  CD1 LEU A 102    11277  10124   8472   -264   -843    825       C  
ATOM    608  CD2 LEU A 102      -4.666 -50.406  -9.444  0.00 73.58           C  
ANISOU  608  CD2 LEU A 102    10382   9504   8072    -12   -563    361       C  
ATOM    609  N   VAL A 103      -9.015 -48.800  -6.508  1.00 74.85           N  
ANISOU  609  N   VAL A 103    11150  10157   7132   -439    503    398       N  
ATOM    610  CA  VAL A 103     -10.262 -48.020  -6.611  1.00 77.84           C  
ANISOU  610  CA  VAL A 103    11450  10612   7514   -337   1002    401       C  
ATOM    611  C   VAL A 103     -10.068 -46.823  -7.553  1.00 77.95           C  
ANISOU  611  C   VAL A 103    11303  10579   7737   -150   1159    191       C  
ATOM    612  O   VAL A 103      -9.327 -45.891  -7.237  1.00 80.30           O  
ANISOU  612  O   VAL A 103    11833  10806   7870   -153   1184    -34       O  
ATOM    613  CB  VAL A 103     -10.764 -47.526  -5.217  1.00 82.45           C  
ANISOU  613  CB  VAL A 103    12417  11235   7676   -437   1375    401       C  
ATOM    614  CG1 VAL A 103     -12.086 -46.747  -5.337  1.00 84.63           C  
ANISOU  614  CG1 VAL A 103    12551  11552   8052   -243   2001    482       C  
ATOM    615  CG2 VAL A 103     -10.942 -48.706  -4.252  1.00 82.86           C  
ANISOU  615  CG2 VAL A 103    12631  11360   7494   -664   1192    633       C  
ATOM    616  N   MET A 104     -10.737 -46.865  -8.707  1.00 76.61           N  
ANISOU  616  N   MET A 104    10754  10451   7903    -49   1228    300       N  
ATOM    617  CA  MET A 104     -10.616 -45.833  -9.736  1.00 75.36           C  
ANISOU  617  CA  MET A 104    10383  10267   7983    100   1331    163       C  
ATOM    618  C   MET A 104     -11.886 -45.028  -9.904  1.00 77.92           C  
ANISOU  618  C   MET A 104    10480  10663   8462    236   1815    350       C  
ATOM    619  O   MET A 104     -12.944 -45.371  -9.369  1.00 81.45           O  
ANISOU  619  O   MET A 104    10861  11206   8880    224   2076    632       O  
ATOM    620  CB  MET A 104     -10.333 -46.468 -11.090  1.00 73.79           C  
ANISOU  620  CB  MET A 104     9918  10060   8061     56   1011    188       C  
ATOM    621  CG  MET A 104      -9.134 -47.368 -11.112  1.00 75.69           C  
ANISOU  621  CG  MET A 104    10304  10183   8271     -1    618     79       C  
ATOM    622  SD  MET A 104      -9.226 -48.402 -12.548  1.00 68.41           S  
ANISOU  622  SD  MET A 104     9220   9179   7593    -98    416    152       S  
ATOM    623  CE  MET A 104     -10.539 -49.549 -12.116  1.00 74.14           C  
ANISOU  623  CE  MET A 104     9972   9969   8228   -315    435    500       C  
ATOM    624  N   GLU A 105     -11.768 -43.961 -10.685  1.00 77.73           N  
ANISOU  624  N   GLU A 105    10291  10596   8645    375   1938    248       N  
ATOM    625  CA  GLU A 105     -12.923 -43.191 -11.117  1.00 80.84           C  
ANISOU  625  CA  GLU A 105    10341  11050   9324    535   2362    521       C  
ATOM    626  C   GLU A 105     -13.783 -44.028 -12.054  1.00 79.01           C  
ANISOU  626  C   GLU A 105     9656  11014   9349    376   2166    930       C  
ATOM    627  O   GLU A 105     -13.306 -44.960 -12.704  1.00 74.20           O  
ANISOU  627  O   GLU A 105     9050  10423   8720    161   1713    879       O  
ATOM    628  CB  GLU A 105     -12.492 -41.888 -11.810  1.00 81.62           C  
ANISOU  628  CB  GLU A 105    10367  11040   9603    690   2468    336       C  
ATOM    629  CG  GLU A 105     -11.653 -42.070 -13.085  1.00 82.12           C  
ANISOU  629  CG  GLU A 105    10250  11141   9811    568   1982    202       C  
ATOM    630  CD  GLU A 105     -11.254 -40.744 -13.721  1.00 81.28           C  
ANISOU  630  CD  GLU A 105    10067  10945   9871    702   2085     47       C  
ATOM    631  OE1 GLU A 105     -12.151 -39.956 -14.101  1.00 91.93           O  
ANISOU  631  OE1 GLU A 105    11116  12307  11505    844   2423    307       O  
ATOM    632  OE2 GLU A 105     -10.040 -40.496 -13.846  1.00 82.02           O  
ANISOU  632  OE2 GLU A 105    10366  10958   9839    661   1822   -280       O  
ATOM    633  N   TYR A 106     -15.061 -43.685 -12.108  1.00 82.18           N  
ANISOU  633  N   TYR A 106     9692  11542   9990    463   2538   1374       N  
ATOM    634  CA  TYR A 106     -16.003 -44.407 -12.934  1.00 84.38           C  
ANISOU  634  CA  TYR A 106     9526  12049  10487    221   2335   1877       C  
ATOM    635  C   TYR A 106     -16.218 -43.696 -14.274  1.00 86.33           C  
ANISOU  635  C   TYR A 106     9349  12374  11079    181   2251   2078       C  
ATOM    636  O   TYR A 106     -16.817 -42.617 -14.341  1.00 88.76           O  
ANISOU  636  O   TYR A 106     9345  12695  11684    429   2664   2331       O  
ATOM    637  CB  TYR A 106     -17.326 -44.550 -12.199  1.00 84.48           C  
ANISOU  637  CB  TYR A 106     9287  12220  10590    288   2745   2397       C  
ATOM    638  CG  TYR A 106     -18.305 -45.374 -12.963  1.00 81.38           C  
ANISOU  638  CG  TYR A 106     8446  12099  10375    -62   2460   2996       C  
ATOM    639  CD1 TYR A 106     -18.093 -46.727 -13.136  1.00 78.39           C  
ANISOU  639  CD1 TYR A 106     8278  11750   9757   -452   1954   2962       C  
ATOM    640  CD2 TYR A 106     -19.427 -44.804 -13.533  1.00 83.91           C  
ANISOU  640  CD2 TYR A 106     8145  12630  11107    -39   2680   3642       C  
ATOM    641  CE1 TYR A 106     -18.975 -47.499 -13.846  1.00 82.10           C  
ANISOU  641  CE1 TYR A 106     8439  12442  10315   -877   1652   3507       C  
ATOM    642  CE2 TYR A 106     -20.324 -45.571 -14.246  1.00 88.54           C  
ANISOU  642  CE2 TYR A 106     8325  13502  11816   -476   2336   4270       C  
ATOM    643  CZ  TYR A 106     -20.090 -46.920 -14.398  1.00 84.29           C  
ANISOU  643  CZ  TYR A 106     8095  12978  10955   -927   1810   4173       C  
ATOM    644  OH  TYR A 106     -20.970 -47.703 -15.098  1.00 88.82           O  
ANISOU  644  OH  TYR A 106     8368  13806  11572  -1459   1435   4789       O  
ATOM    645  N   ALA A 107     -15.716 -44.305 -15.340  1.00 70.73           N  
ANISOU  645  N   ALA A 107     9758  10495   6620    806   1781   2391       N  
ATOM    646  CA  ALA A 107     -15.931 -43.800 -16.684  1.00 69.96           C  
ANISOU  646  CA  ALA A 107     9468  10278   6835    670   1661   2193       C  
ATOM    647  C   ALA A 107     -17.370 -44.082 -17.070  1.00 73.64           C  
ANISOU  647  C   ALA A 107     9707  10696   7578    574   1898   2311       C  
ATOM    648  O   ALA A 107     -17.715 -45.210 -17.424  1.00 72.89           O  
ANISOU  648  O   ALA A 107     9489  10469   7736    445   1965   2495       O  
ATOM    649  CB  ALA A 107     -14.984 -44.457 -17.650  1.00 68.72           C  
ANISOU  649  CB  ALA A 107     9269   9957   6885    547   1421   2157       C  
ATOM    650  N   GLU A 108     -18.207 -43.048 -16.985  1.00 78.83           N  
ANISOU  650  N   GLU A 108    10298  11447   8206    640   2019   2200       N  
ATOM    651  CA  GLU A 108     -19.648 -43.178 -17.256  1.00 81.46           C  
ANISOU  651  CA  GLU A 108    10385  11763   8803    572   2252   2306       C  
ATOM    652  C   GLU A 108     -19.849 -43.704 -18.674  1.00 80.61           C  
ANISOU  652  C   GLU A 108    10053  11475   9099    365   2100   2275       C  
ATOM    653  O   GLU A 108     -20.754 -44.504 -18.922  1.00 81.88           O  
ANISOU  653  O   GLU A 108    10012  11558   9539    245   2239   2437       O  
ATOM    654  CB  GLU A 108     -20.397 -41.840 -17.110  1.00 85.15           C  
ANISOU  654  CB  GLU A 108    10805  12346   9204    693   2359   2147       C  
ATOM    655  CG  GLU A 108     -19.811 -40.808 -16.118  1.00 92.16           C  
ANISOU  655  CG  GLU A 108    11957  13383   9675    902   2351   1988       C  
ATOM    656  CD  GLU A 108     -18.705 -39.930 -16.738  1.00 95.76           C  
ANISOU  656  CD  GLU A 108    12519  13784  10081    900   2021   1707       C  
ATOM    657  OE1 GLU A 108     -17.545 -40.051 -16.285  1.00 95.84           O  
ANISOU  657  OE1 GLU A 108    12735  13819   9861    940   1855   1662       O  
ATOM    658  OE2 GLU A 108     -18.989 -39.133 -17.674  1.00 94.39           O  
ANISOU  658  OE2 GLU A 108    12214  13540  10109    858   1927   1547       O  
ATOM    659  N   GLY A 109     -18.990 -43.247 -19.592  1.00 77.35           N  
ANISOU  659  N   GLY A 109     9680  10998   8711    326   1815   2062       N  
ATOM    660  CA  GLY A 109     -19.053 -43.636 -21.006  1.00 73.87           C  
ANISOU  660  CA  GLY A 109     9071  10408   8589    154   1641   1991       C  
ATOM    661  C   GLY A 109     -18.537 -45.037 -21.265  1.00 74.66           C  
ANISOU  661  C   GLY A 109     9182  10359   8828     32   1579   2114       C  
ATOM    662  O   GLY A 109     -18.839 -45.668 -22.297  1.00 75.16           O  
ANISOU  662  O   GLY A 109     9090  10285   9181   -123   1493   2095       O  
ATOM    663  N   GLY A 110     -17.753 -45.535 -20.316  1.00 71.74           N  
ANISOU  663  N   GLY A 110     9002  10011   8246    113   1612   2234       N  
ATOM    664  CA  GLY A 110     -17.152 -46.839 -20.452  1.00 65.68           C  
ANISOU  664  CA  GLY A 110     8268   9089   7597     30   1555   2361       C  
ATOM    665  C   GLY A 110     -16.100 -46.745 -21.527  1.00 56.96           C  
ANISOU  665  C   GLY A 110     7195   7896   6552    -18   1279   2157       C  
ATOM    666  O   GLY A 110     -15.515 -45.703 -21.742  1.00 50.74           O  
ANISOU  666  O   GLY A 110     6474   7192   5612     50   1144   1969       O  
ATOM    667  N   SER A 111     -15.910 -47.852 -22.210  1.00 54.27           N  
ANISOU  667  N   SER A 111     6796   7372   6452   -140   1216   2197       N  
ATOM    668  CA  SER A 111     -14.812 -48.082 -23.127  1.00 50.46           C  
ANISOU  668  CA  SER A 111     6361   6786   6027   -174    996   2048       C  
ATOM    669  C   SER A 111     -14.944 -47.274 -24.413  1.00 47.52           C  
ANISOU  669  C   SER A 111     5893   6423   5737   -237    853   1810       C  
ATOM    670  O   SER A 111     -16.056 -47.090 -24.912  1.00 46.56           O  
ANISOU  670  O   SER A 111     5617   6303   5769   -318    899   1784       O  
ATOM    671  CB  SER A 111     -14.865 -49.565 -23.467  1.00 46.52           C  
ANISOU  671  CB  SER A 111     5811   6068   5797   -288   1016   2164       C  
ATOM    672  OG  SER A 111     -13.914 -49.900 -24.437  1.00 52.80           O  
ANISOU  672  OG  SER A 111     6637   6747   6678   -320    832   2012       O  
ATOM    673  N   LEU A 112     -13.826 -46.823 -24.980  1.00 44.64           N  
ANISOU  673  N   LEU A 112     5611   6065   5288   -199    681   1650       N  
ATOM    674  CA  LEU A 112     -13.879 -46.251 -26.328  1.00 45.50           C  
ANISOU  674  CA  LEU A 112     5645   6159   5483   -264    553   1456       C  
ATOM    675  C   LEU A 112     -14.369 -47.305 -27.294  1.00 45.70           C  
ANISOU  675  C   LEU A 112     5565   6031   5767   -403    523   1440       C  
ATOM    676  O   LEU A 112     -15.090 -46.988 -28.216  1.00 44.19           O  
ANISOU  676  O   LEU A 112     5266   5848   5677   -475    468   1338       O  
ATOM    677  CB  LEU A 112     -12.531 -45.726 -26.811  1.00 43.03           C  
ANISOU  677  CB  LEU A 112     5427   5859   5063   -210    404   1315       C  
ATOM    678  CG  LEU A 112     -12.480 -45.185 -28.257  1.00 45.63           C  
ANISOU  678  CG  LEU A 112     5705   6175   5457   -265    291   1141       C  
ATOM    679  CD1 LEU A 112     -13.478 -44.081 -28.475  1.00 47.84           C  
ANISOU  679  CD1 LEU A 112     5909   6552   5715   -260    311   1098       C  
ATOM    680  CD2 LEU A 112     -11.093 -44.666 -28.628  1.00 45.50           C  
ANISOU  680  CD2 LEU A 112     5772   6171   5347   -211    186   1035       C  
ATOM    681  N   TYR A 113     -13.988 -48.562 -27.063  1.00 48.46           N  
ANISOU  681  N   TYR A 113     5951   6234   6227   -436    548   1538       N  
ATOM    682  CA  TYR A 113     -14.413 -49.658 -27.925  1.00 49.89           C  
ANISOU  682  CA  TYR A 113     6047   6233   6677   -574    515   1502       C  
ATOM    683  C   TYR A 113     -15.926 -49.737 -27.967  1.00 50.43           C  
ANISOU  683  C   TYR A 113     5939   6299   6922   -685    596   1555       C  
ATOM    684  O   TYR A 113     -16.530 -49.976 -29.011  1.00 50.08           O  
ANISOU  684  O   TYR A 113     5782   6188   7057   -802    501   1429       O  
ATOM    685  CB  TYR A 113     -13.861 -50.998 -27.428  1.00 53.45           C  
ANISOU  685  CB  TYR A 113     6566   6502   7242   -578    566   1640       C  
ATOM    686  CG  TYR A 113     -14.110 -52.137 -28.393  1.00 53.61           C  
ANISOU  686  CG  TYR A 113     6523   6295   7550   -715    509   1555       C  
ATOM    687  CD1 TYR A 113     -13.213 -52.401 -29.434  1.00 57.45           C  
ANISOU  687  CD1 TYR A 113     7075   6698   8055   -708    372   1362       C  
ATOM    688  CD2 TYR A 113     -15.257 -52.922 -28.288  1.00 57.08           C  
ANISOU  688  CD2 TYR A 113     6833   6604   8252   -855    596   1653       C  
ATOM    689  CE1 TYR A 113     -13.440 -53.430 -30.327  1.00 58.01           C  
ANISOU  689  CE1 TYR A 113     7111   6559   8372   -823    314   1247       C  
ATOM    690  CE2 TYR A 113     -15.499 -53.957 -29.180  1.00 59.75           C  
ANISOU  690  CE2 TYR A 113     7115   6715   8871   -993    522   1542       C  
ATOM    691  CZ  TYR A 113     -14.588 -54.200 -30.194  1.00 62.07           C  
ANISOU  691  CZ  TYR A 113     7503   6931   9151   -970    375   1327       C  
ATOM    692  OH  TYR A 113     -14.828 -55.216 -31.083  1.00 70.16           O  
ANISOU  692  OH  TYR A 113     8492   7728  10436  -1097    295   1182       O  
ATOM    693  N   ASN A 114     -16.531 -49.538 -26.811  1.00 50.34           N  
ANISOU  693  N   ASN A 114     5901   6371   6856   -641    771   1740       N  
ATOM    694  CA  ASN A 114     -17.973 -49.596 -26.705  1.00 52.14           C  
ANISOU  694  CA  ASN A 114     5932   6608   7270   -734    886   1821       C  
ATOM    695  C   ASN A 114     -18.639 -48.436 -27.451  1.00 49.40           C  
ANISOU  695  C   ASN A 114     5469   6401   6899   -730    797   1663       C  
ATOM    696  O   ASN A 114     -19.649 -48.608 -28.097  1.00 51.52           O  
ANISOU  696  O   ASN A 114     5548   6636   7392   -846    760   1621       O  
ATOM    697  CB  ASN A 114     -18.383 -49.568 -25.245  1.00 51.66           C  
ANISOU  697  CB  ASN A 114     5888   6629   7112   -656   1129   2064       C  
ATOM    698  CG  ASN A 114     -19.786 -50.062 -25.035  1.00 59.09           C  
ANISOU  698  CG  ASN A 114     6607   7519   8325   -776   1298   2208       C  
ATOM    699  OD1 ASN A 114     -20.123 -51.167 -25.454  1.00 66.61           O  
ANISOU  699  OD1 ASN A 114     7458   8272   9579   -932   1286   2246       O  
ATOM    700  ND2 ASN A 114     -20.617 -49.254 -24.377  1.00 57.41           N  
ANISOU  700  ND2 ASN A 114     6309   7475   8030   -704   1464   2286       N  
ATOM    701  N   VAL A 115     -18.059 -47.254 -27.355  1.00 47.23           N  
ANISOU  701  N   VAL A 115     5305   6274   6366   -596    752   1579       N  
ATOM    702  CA  VAL A 115     -18.615 -46.084 -28.000  1.00 47.36           C  
ANISOU  702  CA  VAL A 115     5234   6410   6351   -566    677   1455       C  
ATOM    703  C   VAL A 115     -18.598 -46.233 -29.499  1.00 47.23           C  
ANISOU  703  C   VAL A 115     5166   6333   6446   -658    467   1282       C  
ATOM    704  O   VAL A 115     -19.553 -45.852 -30.176  1.00 46.77           O  
ANISOU  704  O   VAL A 115     4949   6321   6501   -701    399   1225       O  
ATOM    705  CB  VAL A 115     -17.835 -44.838 -27.598  1.00 46.37           C  
ANISOU  705  CB  VAL A 115     5262   6411   5946   -410    665   1394       C  
ATOM    706  CG1 VAL A 115     -18.101 -43.677 -28.536  1.00 48.98           C  
ANISOU  706  CG1 VAL A 115     5540   6815   6253   -379    545   1252       C  
ATOM    707  CG2 VAL A 115     -18.211 -44.474 -26.180  1.00 51.77           C  
ANISOU  707  CG2 VAL A 115     5972   7195   6505   -306    870   1531       C  
ATOM    708  N   LEU A 116     -17.501 -46.790 -30.004  1.00 44.82           N  
ANISOU  708  N   LEU A 116     4997   5933   6099   -674    364   1200       N  
ATOM    709  CA  LEU A 116     -17.319 -46.966 -31.422  1.00 42.89           C  
ANISOU  709  CA  LEU A 116     4751   5640   5904   -739    178   1023       C  
ATOM    710  C   LEU A 116     -18.172 -48.103 -31.958  1.00 43.61           C  
ANISOU  710  C   LEU A 116     4702   5598   6270   -899    126    996       C  
ATOM    711  O   LEU A 116     -18.824 -47.959 -32.984  1.00 44.41           O  
ANISOU  711  O   LEU A 116     4702   5725   6446   -962    -19    871       O  
ATOM    712  CB  LEU A 116     -15.851 -47.245 -31.732  1.00 40.79           C  
ANISOU  712  CB  LEU A 116     4667   5313   5517   -692    120    946       C  
ATOM    713  CG  LEU A 116     -14.854 -46.144 -31.382  1.00 39.64           C  
ANISOU  713  CG  LEU A 116     4648   5279   5134   -557    131    938       C  
ATOM    714  CD1 LEU A 116     -13.425 -46.606 -31.690  1.00 44.97           C  
ANISOU  714  CD1 LEU A 116     5457   5879   5751   -524     84    875       C  
ATOM    715  CD2 LEU A 116     -15.160 -44.878 -32.114  1.00 38.81           C  
ANISOU  715  CD2 LEU A 116     4517   5295   4935   -516     56    851       C  
ATOM    716  N   HIS A 117     -18.157 -49.230 -31.264  1.00 43.98           N  
ANISOU  716  N   HIS A 117     4744   5495   6471   -964    235   1113       N  
ATOM    717  CA  HIS A 117     -18.635 -50.484 -31.848  1.00 46.35           C  
ANISOU  717  CA  HIS A 117     4952   5601   7056  -1128    168   1055       C  
ATOM    718  C   HIS A 117     -19.656 -51.211 -31.010  1.00 47.91           C  
ANISOU  718  C   HIS A 117     4980   5701   7521  -1236    325   1244       C  
ATOM    719  O   HIS A 117     -20.162 -52.235 -31.438  1.00 48.90           O  
ANISOU  719  O   HIS A 117     5001   5645   7933  -1394    272   1201       O  
ATOM    720  CB  HIS A 117     -17.472 -51.440 -32.072  1.00 46.68           C  
ANISOU  720  CB  HIS A 117     5164   5469   7102  -1123    135    996       C  
ATOM    721  CG  HIS A 117     -16.299 -50.826 -32.765  1.00 39.36           C  
ANISOU  721  CG  HIS A 117     4404   4626   5924  -1007     31    845       C  
ATOM    722  ND1 HIS A 117     -16.360 -50.356 -34.058  1.00 48.32           N  
ANISOU  722  ND1 HIS A 117     5544   5836   6981  -1017   -137    639       N  
ATOM    723  CD2 HIS A 117     -15.024 -50.639 -32.353  1.00 37.86           C  
ANISOU  723  CD2 HIS A 117     4373   4457   5555   -881     76    880       C  
ATOM    724  CE1 HIS A 117     -15.170 -49.901 -34.414  1.00 48.16           C  
ANISOU  724  CE1 HIS A 117     5679   5871   6748   -904   -161    566       C  
ATOM    725  NE2 HIS A 117     -14.343 -50.052 -33.394  1.00 48.19           N  
ANISOU  725  NE2 HIS A 117     5764   5842   6705   -826    -40    702       N  
ATOM    726  N   GLY A 118     -19.974 -50.670 -29.840  1.00 49.59           N  
ANISOU  726  N   GLY A 118     5165   6032   7646  -1154    521   1444       N  
ATOM    727  CA  GLY A 118     -20.770 -51.367 -28.848  1.00 52.96           C  
ANISOU  727  CA  GLY A 118     5464   6376   8284  -1228    736   1677       C  
ATOM    728  C   GLY A 118     -22.223 -51.445 -29.216  1.00 58.97           C  
ANISOU  728  C   GLY A 118     5932   7130   9345  -1374    729   1672       C  
ATOM    729  O   GLY A 118     -22.602 -51.230 -30.367  1.00 63.86           O  
ANISOU  729  O   GLY A 118     6450   7767  10045  -1443    510   1466       O  
ATOM    730  N   ALA A 119     -23.046 -51.770 -28.231  1.00 63.85           N  
ANISOU  730  N   ALA A 119     6403   7727  10129  -1417    970   1908       N  
ATOM    731  CA  ALA A 119     -24.470 -51.931 -28.458  1.00 68.35           C  
ANISOU  731  CA  ALA A 119     6646   8278  11044  -1568    995   1936       C  
ATOM    732  C   ALA A 119     -25.193 -50.603 -28.767  1.00 69.54           C  
ANISOU  732  C   ALA A 119     6649   8671  11102  -1479    938   1853       C  
ATOM    733  O   ALA A 119     -24.789 -49.506 -28.344  1.00 62.62           O  
ANISOU  733  O   ALA A 119     5908   7982   9903  -1287    998   1860       O  
ATOM    734  CB  ALA A 119     -25.114 -52.619 -27.259  1.00 72.03           C  
ANISOU  734  CB  ALA A 119     6993   8661  11715  -1627   1316   2246       C  
ATOM    735  N   GLU A 120     -26.281 -50.745 -29.511  1.00 74.34           N  
ANISOU  735  N   GLU A 120     6966   9256  12023  -1624    810   1769       N  
ATOM    736  CA  GLU A 120     -27.080 -49.622 -29.934  1.00 77.65           C  
ANISOU  736  CA  GLU A 120     7202   9876  12425  -1552    724   1694       C  
ATOM    737  C   GLU A 120     -27.969 -49.190 -28.780  1.00 78.38           C  
ANISOU  737  C   GLU A 120     7108  10081  12591  -1483   1045   1929       C  
ATOM    738  O   GLU A 120     -28.350 -50.013 -27.960  1.00 79.48           O  
ANISOU  738  O   GLU A 120     7150  10112  12936  -1575   1287   2136       O  
ATOM    739  CB  GLU A 120     -27.909 -49.967 -31.186  1.00 81.43           C  
ANISOU  739  CB  GLU A 120     7428  10301  13211  -1725    432   1511       C  
ATOM    740  CG  GLU A 120     -27.089 -49.889 -32.499  1.00 84.04           C  
ANISOU  740  CG  GLU A 120     7964  10622  13343  -1715     91   1233       C  
ATOM    741  CD  GLU A 120     -27.938 -49.582 -33.734  1.00 87.57           C  
ANISOU  741  CD  GLU A 120     8196  11151  13927  -1779   -224   1043       C  
ATOM    742  OE1 GLU A 120     -29.123 -49.989 -33.779  1.00 98.03           O  
ANISOU  742  OE1 GLU A 120     9182  12436  15630  -1928   -250   1075       O  
ATOM    743  OE2 GLU A 120     -27.409 -48.928 -34.665  1.00101.06           O  
ANISOU  743  OE2 GLU A 120    10070  12966  15363  -1677   -448    871       O  
ATOM    744  N   PRO A 121     -28.300 -47.890 -28.716  1.00 77.14           N  
ANISOU  744  N   PRO A 121     6907  10134  12268  -1310   1065   1905       N  
ATOM    745  CA  PRO A 121     -27.947 -46.907 -29.738  1.00 71.07           C  
ANISOU  745  CA  PRO A 121     6231   9477  11296  -1207    785   1690       C  
ATOM    746  C   PRO A 121     -26.511 -46.419 -29.572  1.00 67.57           C  
ANISOU  746  C   PRO A 121     6174   9063  10439  -1058    768   1628       C  
ATOM    747  O   PRO A 121     -26.041 -46.201 -28.454  1.00 67.09           O  
ANISOU  747  O   PRO A 121     6271   9040  10178   -942   1001   1754       O  
ATOM    748  CB  PRO A 121     -28.962 -45.784 -29.518  1.00 72.35           C  
ANISOU  748  CB  PRO A 121     6167   9818  11505  -1077    876   1741       C  
ATOM    749  CG  PRO A 121     -29.401 -45.914 -28.100  1.00 76.81           C  
ANISOU  749  CG  PRO A 121     6660  10407  12116  -1030   1267   1975       C  
ATOM    750  CD  PRO A 121     -29.037 -47.288 -27.592  1.00 78.59           C  
ANISOU  750  CD  PRO A 121     6958  10453  12451  -1188   1391   2100       C  
ATOM    751  N   LEU A 122     -25.815 -46.283 -30.691  1.00 63.24           N  
ANISOU  751  N   LEU A 122     5768   8498   9764  -1064    490   1432       N  
ATOM    752  CA  LEU A 122     -24.488 -45.719 -30.691  1.00 59.49           C  
ANISOU  752  CA  LEU A 122     5612   8056   8937   -931    453   1361       C  
ATOM    753  C   LEU A 122     -24.570 -44.205 -30.800  1.00 56.99           C  
ANISOU  753  C   LEU A 122     5318   7903   8432   -753    430   1320       C  
ATOM    754  O   LEU A 122     -25.434 -43.689 -31.493  1.00 58.43           O  
ANISOU  754  O   LEU A 122     5311   8158   8733   -746    306   1272       O  
ATOM    755  CB  LEU A 122     -23.702 -46.258 -31.886  1.00 60.63           C  
ANISOU  755  CB  LEU A 122     5892   8106   9038  -1012    196   1179       C  
ATOM    756  CG  LEU A 122     -23.365 -47.747 -31.890  1.00 58.28           C  
ANISOU  756  CG  LEU A 122     5631   7606   8905  -1170    194   1179       C  
ATOM    757  CD1 LEU A 122     -22.929 -48.205 -33.279  1.00 59.75           C  
ANISOU  757  CD1 LEU A 122     5894   7718   9089  -1248    -81    954       C  
ATOM    758  CD2 LEU A 122     -22.287 -48.012 -30.890  1.00 57.73           C  
ANISOU  758  CD2 LEU A 122     5789   7486   8659  -1093    370   1291       C  
ATOM    759  N   PRO A 123     -23.634 -43.485 -30.166  1.00 54.22           N  
ANISOU  759  N   PRO A 123     5203   7600   7798   -606    525   1329       N  
ATOM    760  CA  PRO A 123     -23.640 -42.036 -30.248  1.00 52.55           C  
ANISOU  760  CA  PRO A 123     5033   7505   7430   -440    508   1282       C  
ATOM    761  C   PRO A 123     -23.042 -41.524 -31.547  1.00 47.78           C  
ANISOU  761  C   PRO A 123     4534   6905   6715   -425    255   1135       C  
ATOM    762  O   PRO A 123     -22.137 -42.140 -32.088  1.00 46.17           O  
ANISOU  762  O   PRO A 123     4477   6628   6438   -496    143   1060       O  
ATOM    763  CB  PRO A 123     -22.730 -41.632 -29.098  1.00 51.77           C  
ANISOU  763  CB  PRO A 123     5163   7425   7082   -321    678   1322       C  
ATOM    764  CG  PRO A 123     -21.723 -42.708 -29.069  1.00 53.16           C  
ANISOU  764  CG  PRO A 123     5495   7496   7206   -414    640   1321       C  
ATOM    765  CD  PRO A 123     -22.496 -43.968 -29.366  1.00 53.90           C  
ANISOU  765  CD  PRO A 123     5399   7498   7582   -586    631   1377       C  
ATOM    766  N   TYR A 124     -23.552 -40.401 -32.031  1.00 46.67           N  
ANISOU  766  N   TYR A 124     4320   6849   6565   -320    182   1108       N  
ATOM    767  CA  TYR A 124     -22.930 -39.682 -33.128  1.00 45.43           C  
ANISOU  767  CA  TYR A 124     4294   6707   6258   -266    -12   1010       C  
ATOM    768  C   TYR A 124     -21.655 -39.022 -32.581  1.00 43.66           C  
ANISOU  768  C   TYR A 124     4330   6460   5800   -171     76    991       C  
ATOM    769  O   TYR A 124     -21.588 -38.640 -31.399  1.00 42.51           O  
ANISOU  769  O   TYR A 124     4226   6325   5600    -91    261   1041       O  
ATOM    770  CB  TYR A 124     -23.913 -38.643 -33.683  1.00 47.21           C  
ANISOU  770  CB  TYR A 124     4358   7019   6561   -163    -97   1025       C  
ATOM    771  CG  TYR A 124     -23.340 -37.581 -34.591  1.00 46.55           C  
ANISOU  771  CG  TYR A 124     4422   6956   6308    -58   -237    978       C  
ATOM    772  CD1 TYR A 124     -23.008 -37.871 -35.913  1.00 54.64           C  
ANISOU  772  CD1 TYR A 124     5512   7989   7258   -115   -461    906       C  
ATOM    773  CD2 TYR A 124     -23.159 -36.267 -34.148  1.00 51.02           C  
ANISOU  773  CD2 TYR A 124     5069   7526   6792    104   -138   1008       C  
ATOM    774  CE1 TYR A 124     -22.486 -36.890 -36.770  1.00 49.74           C  
ANISOU  774  CE1 TYR A 124     5035   7391   6475    -14   -564    897       C  
ATOM    775  CE2 TYR A 124     -22.632 -35.258 -35.018  1.00 47.99           C  
ANISOU  775  CE2 TYR A 124     4819   7134   6282    195   -254    993       C  
ATOM    776  CZ  TYR A 124     -22.304 -35.587 -36.319  1.00 50.37           C  
ANISOU  776  CZ  TYR A 124     5180   7455   6503    135   -457    954       C  
ATOM    777  OH  TYR A 124     -21.796 -34.641 -37.194  1.00 50.77           O  
ANISOU  777  OH  TYR A 124     5366   7503   6420    225   -547    971       O  
ATOM    778  N   TYR A 125     -20.628 -38.953 -33.420  1.00 40.21           N  
ANISOU  778  N   TYR A 125     4061   5991   5225   -185    -55    912       N  
ATOM    779  CA  TYR A 125     -19.431 -38.182 -33.102  1.00 37.35           C  
ANISOU  779  CA  TYR A 125     3907   5603   4681   -103     -7    886       C  
ATOM    780  C   TYR A 125     -18.798 -37.590 -34.373  1.00 37.93           C  
ANISOU  780  C   TYR A 125     4085   5676   4653    -80   -156    830       C  
ATOM    781  O   TYR A 125     -19.034 -38.062 -35.513  1.00 30.93           O  
ANISOU  781  O   TYR A 125     3162   4810   3782   -139   -305    794       O  
ATOM    782  CB  TYR A 125     -18.418 -39.004 -32.297  1.00 33.59           C  
ANISOU  782  CB  TYR A 125     3561   5070   4132   -154     78    883       C  
ATOM    783  CG  TYR A 125     -17.696 -40.122 -33.019  1.00 35.89           C  
ANISOU  783  CG  TYR A 125     3916   5299   4422   -263    -18    830       C  
ATOM    784  CD1 TYR A 125     -16.561 -39.870 -33.776  1.00 44.97           C  
ANISOU  784  CD1 TYR A 125     5209   6425   5451   -251    -98    761       C  
ATOM    785  CD2 TYR A 125     -18.117 -41.441 -32.916  1.00 36.32           C  
ANISOU  785  CD2 TYR A 125     3888   5302   4611   -374    -11    851       C  
ATOM    786  CE1 TYR A 125     -15.880 -40.901 -34.447  1.00 34.31           C  
ANISOU  786  CE1 TYR A 125     3922   5018   4098   -329   -165    698       C  
ATOM    787  CE2 TYR A 125     -17.445 -42.471 -33.576  1.00 34.79           C  
ANISOU  787  CE2 TYR A 125     3764   5027   4428   -460    -94    782       C  
ATOM    788  CZ  TYR A 125     -16.324 -42.194 -34.336  1.00 38.71           C  
ANISOU  788  CZ  TYR A 125     4408   5515   4784   -428   -168    699       C  
ATOM    789  OH  TYR A 125     -15.624 -43.212 -34.970  1.00 34.65           O  
ANISOU  789  OH  TYR A 125     3968   4920   4278   -492   -226    619       O  
ATOM    790  N   THR A 126     -17.993 -36.553 -34.138  1.00 35.41           N  
ANISOU  790  N   THR A 126     3898   5330   4227      6   -109    824       N  
ATOM    791  CA  THR A 126     -17.462 -35.711 -35.178  1.00 35.39           C  
ANISOU  791  CA  THR A 126     3987   5318   4143     51   -198    814       C  
ATOM    792  C   THR A 126     -15.980 -35.997 -35.407  1.00 37.16           C  
ANISOU  792  C   THR A 126     4372   5489   4259      3   -196    767       C  
ATOM    793  O   THR A 126     -15.314 -36.581 -34.552  1.00 34.63           O  
ANISOU  793  O   THR A 126     4099   5134   3927    -36   -125    742       O  
ATOM    794  CB  THR A 126     -17.612 -34.265 -34.777  1.00 33.50           C  
ANISOU  794  CB  THR A 126     3765   5051   3912    176   -136    846       C  
ATOM    795  OG1 THR A 126     -16.675 -33.970 -33.753  1.00 33.08           O  
ANISOU  795  OG1 THR A 126     3826   4936   3807    189    -32    805       O  
ATOM    796  CG2 THR A 126     -19.035 -33.971 -34.253  1.00 36.97           C  
ANISOU  796  CG2 THR A 126     4032   5537   4478    249    -89    890       C  
ATOM    797  N   ALA A 127     -15.466 -35.573 -36.564  1.00 37.97           N  
ANISOU  797  N   ALA A 127     4552   5591   4282     17   -266    769       N  
ATOM    798  CA  ALA A 127     -14.018 -35.582 -36.807  1.00 35.52           C  
ANISOU  798  CA  ALA A 127     4374   5231   3892     -9   -233    741       C  
ATOM    799  C   ALA A 127     -13.303 -34.965 -35.637  1.00 35.38           C  
ANISOU  799  C   ALA A 127     4400   5146   3899     16   -137    731       C  
ATOM    800  O   ALA A 127     -12.234 -35.425 -35.244  1.00 37.80           O  
ANISOU  800  O   ALA A 127     4760   5415   4185    -26   -105    692       O  
ATOM    801  CB  ALA A 127     -13.673 -34.804 -38.067  1.00 36.68           C  
ANISOU  801  CB  ALA A 127     4595   5386   3955     35   -273    786       C  
ATOM    802  N   ALA A 128     -13.886 -33.902 -35.093  1.00 34.91           N  
ANISOU  802  N   ALA A 128     4313   5066   3885     94   -103    757       N  
ATOM    803  CA  ALA A 128     -13.244 -33.160 -34.022  1.00 35.16           C  
ANISOU  803  CA  ALA A 128     4402   5027   3930    126    -34    716       C  
ATOM    804  C   ALA A 128     -13.086 -34.055 -32.806  1.00 34.65           C  
ANISOU  804  C   ALA A 128     4335   4990   3840     95      9    672       C  
ATOM    805  O   ALA A 128     -12.045 -34.065 -32.155  1.00 38.47           O  
ANISOU  805  O   ALA A 128     4887   5437   4292     78     19    622       O  
ATOM    806  CB  ALA A 128     -14.032 -31.882 -33.690  1.00 33.91           C  
ANISOU  806  CB  ALA A 128     4221   4830   3832    231      0    732       C  
ATOM    807  N   HIS A 129     -14.109 -34.844 -32.531  1.00 37.66           N  
ANISOU  807  N   HIS A 129     4631   5436   4243     86     29    703       N  
ATOM    808  CA  HIS A 129     -14.050 -35.810 -31.462  1.00 38.61           C  
ANISOU  808  CA  HIS A 129     4751   5580   4337     58     85    703       C  
ATOM    809  C   HIS A 129     -12.979 -36.843 -31.735  1.00 41.32           C  
ANISOU  809  C   HIS A 129     5146   5898   4656    -21     42    688       C  
ATOM    810  O   HIS A 129     -12.241 -37.223 -30.830  1.00 43.91           O  
ANISOU  810  O   HIS A 129     5532   6217   4936    -20     65    677       O  
ATOM    811  CB  HIS A 129     -15.391 -36.510 -31.317  1.00 38.19           C  
ANISOU  811  CB  HIS A 129     4570   5583   4358     43    127    763       C  
ATOM    812  CG  HIS A 129     -16.410 -35.684 -30.614  1.00 41.91           C  
ANISOU  812  CG  HIS A 129     4976   6090   4856    141    219    783       C  
ATOM    813  ND1 HIS A 129     -17.593 -35.295 -31.202  1.00 38.15           N  
ANISOU  813  ND1 HIS A 129     4363   5646   4485    176    203    821       N  
ATOM    814  CD2 HIS A 129     -16.416 -35.163 -29.363  1.00 40.84           C  
ANISOU  814  CD2 HIS A 129     4897   5969   4653    227    328    762       C  
ATOM    815  CE1 HIS A 129     -18.288 -34.576 -30.340  1.00 43.98           C  
ANISOU  815  CE1 HIS A 129     5063   6407   5240    282    319    828       C  
ATOM    816  NE2 HIS A 129     -17.590 -34.469 -29.221  1.00 39.83           N  
ANISOU  816  NE2 HIS A 129     4665   5870   4596    316    401    783       N  
ATOM    817  N   ALA A 130     -12.925 -37.316 -32.977  1.00 40.28           N  
ANISOU  817  N   ALA A 130     4996   5759   4549    -75    -25    685       N  
ATOM    818  CA  ALA A 130     -12.022 -38.381 -33.344  1.00 39.01           C  
ANISOU  818  CA  ALA A 130     4875   5565   4381   -137    -51    660       C  
ATOM    819  C   ALA A 130     -10.587 -37.956 -33.081  1.00 40.06           C  
ANISOU  819  C   ALA A 130     5085   5660   4474   -119    -45    628       C  
ATOM    820  O   ALA A 130      -9.831 -38.685 -32.421  1.00 40.38           O  
ANISOU  820  O   ALA A 130     5150   5679   4512   -130    -37    624       O  
ATOM    821  CB  ALA A 130     -12.197 -38.748 -34.820  1.00 39.48           C  
ANISOU  821  CB  ALA A 130     4926   5634   4441   -177   -123    633       C  
ATOM    822  N   MET A 131     -10.211 -36.790 -33.604  1.00 36.49           N  
ANISOU  822  N   MET A 131     4661   5192   4013    -92    -52    617       N  
ATOM    823  CA  MET A 131      -8.869 -36.283 -33.409  1.00 36.39           C  
ANISOU  823  CA  MET A 131     4688   5131   4007    -93    -49    587       C  
ATOM    824  C   MET A 131      -8.626 -35.934 -31.916  1.00 39.37           C  
ANISOU  824  C   MET A 131     5086   5503   4372    -60    -49    553       C  
ATOM    825  O   MET A 131      -7.555 -36.160 -31.373  1.00 41.56           O  
ANISOU  825  O   MET A 131     5376   5762   4652    -69    -77    521       O  
ATOM    826  CB  MET A 131      -8.657 -35.059 -34.277  1.00 38.80           C  
ANISOU  826  CB  MET A 131     5011   5399   4333    -79    -39    604       C  
ATOM    827  CG  MET A 131      -8.926 -35.271 -35.789  1.00 37.48           C  
ANISOU  827  CG  MET A 131     4853   5263   4125    -88    -44    646       C  
ATOM    828  SD  MET A 131      -7.698 -36.313 -36.572  1.00 35.59           S  
ANISOU  828  SD  MET A 131     4635   5024   3864   -130    -18    618       S  
ATOM    829  CE  MET A 131      -6.285 -35.232 -36.636  1.00 37.40           C  
ANISOU  829  CE  MET A 131     4864   5179   4165   -138     46    640       C  
ATOM    830  N   SER A 132      -9.608 -35.379 -31.237  1.00 37.44           N  
ANISOU  830  N   SER A 132     4841   5281   4103     -9    -23    553       N  
ATOM    831  CA  SER A 132      -9.367 -34.988 -29.853  1.00 40.07           C  
ANISOU  831  CA  SER A 132     5221   5621   4381     38    -23    499       C  
ATOM    832  C   SER A 132      -9.032 -36.200 -28.970  1.00 41.96           C  
ANISOU  832  C   SER A 132     5479   5910   4553     35    -29    524       C  
ATOM    833  O   SER A 132      -8.182 -36.140 -28.072  1.00 39.61           O  
ANISOU  833  O   SER A 132     5230   5621   4200     58    -80    477       O  
ATOM    834  CB  SER A 132     -10.575 -34.255 -29.291  1.00 36.62           C  
ANISOU  834  CB  SER A 132     4785   5207   3920    113     39    491       C  
ATOM    835  OG  SER A 132     -10.404 -34.117 -27.913  1.00 42.42           O  
ANISOU  835  OG  SER A 132     5588   5975   4556    169     50    433       O  
ATOM    836  N   TRP A 133      -9.708 -37.305 -29.263  1.00 43.45           N  
ANISOU  836  N   TRP A 133     5627   6125   4758      6     10    602       N  
ATOM    837  CA  TRP A 133      -9.486 -38.557 -28.583  1.00 41.19           C  
ANISOU  837  CA  TRP A 133     5354   5856   4440      1     19    661       C  
ATOM    838  C   TRP A 133      -8.043 -39.041 -28.767  1.00 43.22           C  
ANISOU  838  C   TRP A 133     5626   6072   4722    -20    -56    638       C  
ATOM    839  O   TRP A 133      -7.345 -39.332 -27.788  1.00 48.91           O  
ANISOU  839  O   TRP A 133     6388   6814   5380     20    -96    647       O  
ATOM    840  CB  TRP A 133     -10.484 -39.585 -29.084  1.00 36.99           C  
ANISOU  840  CB  TRP A 133     4757   5317   3980    -50     71    736       C  
ATOM    841  CG  TRP A 133     -11.879 -39.335 -28.602  1.00 38.00           C  
ANISOU  841  CG  TRP A 133     4838   5497   4103    -23    159    785       C  
ATOM    842  CD1 TRP A 133     -12.251 -38.637 -27.501  1.00 39.62           C  
ANISOU  842  CD1 TRP A 133     5081   5762   4211     59    226    784       C  
ATOM    843  CD2 TRP A 133     -13.084 -39.832 -29.183  1.00 36.39           C  
ANISOU  843  CD2 TRP A 133     4527   5293   4007    -75    195    834       C  
ATOM    844  NE1 TRP A 133     -13.607 -38.644 -27.369  1.00 36.55           N  
ANISOU  844  NE1 TRP A 133     4607   5412   3869     71    327    843       N  
ATOM    845  CE2 TRP A 133     -14.145 -39.386 -28.382  1.00 36.69           C  
ANISOU  845  CE2 TRP A 133     4519   5392   4027    -19    300    880       C  
ATOM    846  CE3 TRP A 133     -13.366 -40.626 -30.298  1.00 37.69           C  
ANISOU  846  CE3 TRP A 133     4624   5411   4284   -163    142    830       C  
ATOM    847  CZ2 TRP A 133     -15.469 -39.681 -28.669  1.00 40.53           C  
ANISOU  847  CZ2 TRP A 133     4866   5897   4636    -54    354    938       C  
ATOM    848  CZ3 TRP A 133     -14.677 -40.926 -30.582  1.00 36.52           C  
ANISOU  848  CZ3 TRP A 133     4352   5278   4245   -206    166    869       C  
ATOM    849  CH2 TRP A 133     -15.713 -40.450 -29.778  1.00 42.45           C  
ANISOU  849  CH2 TRP A 133     5030   6091   5007   -156    271    931       C  
ATOM    850  N   CYS A 134      -7.597 -39.092 -30.007  1.00 37.72           N  
ANISOU  850  N   CYS A 134     4894   5328   4108    -68    -74    612       N  
ATOM    851  CA  CYS A 134      -6.232 -39.476 -30.320  1.00 38.57           C  
ANISOU  851  CA  CYS A 134     4991   5397   4268    -79   -118    588       C  
ATOM    852  C   CYS A 134      -5.189 -38.521 -29.721  1.00 39.33           C  
ANISOU  852  C   CYS A 134     5089   5495   4362    -57   -183    528       C  
ATOM    853  O   CYS A 134      -4.145 -38.951 -29.183  1.00 42.03           O  
ANISOU  853  O   CYS A 134     5414   5836   4721    -37   -247    524       O  
ATOM    854  CB  CYS A 134      -6.066 -39.583 -31.847  1.00 34.86           C  
ANISOU  854  CB  CYS A 134     4494   4891   3860   -122    -91    567       C  
ATOM    855  SG  CYS A 134      -7.177 -40.871 -32.519  1.00 40.14           S  
ANISOU  855  SG  CYS A 134     5158   5545   4548   -159    -62    594       S  
ATOM    856  N   LEU A 135      -5.457 -37.231 -29.804  1.00 35.59           N  
ANISOU  856  N   LEU A 135     4625   5012   3886    -60   -181    479       N  
ATOM    857  CA  LEU A 135      -4.562 -36.273 -29.186  1.00 36.09           C  
ANISOU  857  CA  LEU A 135     4686   5052   3972    -55   -256    399       C  
ATOM    858  C   LEU A 135      -4.414 -36.622 -27.730  1.00 38.99           C  
ANISOU  858  C   LEU A 135     5104   5483   4227      3   -329    380       C  
ATOM    859  O   LEU A 135      -3.303 -36.651 -27.201  1.00 42.04           O  
ANISOU  859  O   LEU A 135     5466   5872   4634      8   -435    336       O  
ATOM    860  CB  LEU A 135      -5.104 -34.863 -29.284  1.00 33.07           C  
ANISOU  860  CB  LEU A 135     4330   4628   3607    -53   -235    347       C  
ATOM    861  CG  LEU A 135      -4.334 -33.793 -28.527  1.00 33.32           C  
ANISOU  861  CG  LEU A 135     4372   4610   3677    -56   -324    232       C  
ATOM    862  CD1 LEU A 135      -2.844 -33.846 -28.822  1.00 39.56           C  
ANISOU  862  CD1 LEU A 135     5073   5356   4603   -116   -391    210       C  
ATOM    863  CD2 LEU A 135      -4.893 -32.444 -28.877  1.00 28.64           C  
ANISOU  863  CD2 LEU A 135     3803   3932   3147    -56   -281    195       C  
ATOM    864  N   GLN A 136      -5.535 -36.874 -27.073  1.00 39.68           N  
ANISOU  864  N   GLN A 136     5255   5628   4192     52   -273    419       N  
ATOM    865  CA  GLN A 136      -5.512 -37.056 -25.610  1.00 40.67           C  
ANISOU  865  CA  GLN A 136     5460   5834   4157    128   -321    410       C  
ATOM    866  C   GLN A 136      -4.779 -38.329 -25.211  1.00 41.28           C  
ANISOU  866  C   GLN A 136     5531   5940   4212    150   -377    495       C  
ATOM    867  O   GLN A 136      -4.123 -38.390 -24.176  1.00 43.60           O  
ANISOU  867  O   GLN A 136     5872   6293   4401    209   -485    473       O  
ATOM    868  CB  GLN A 136      -6.936 -37.052 -25.073  1.00 39.17           C  
ANISOU  868  CB  GLN A 136     5328   5704   3852    181   -201    457       C  
ATOM    869  CG  GLN A 136      -7.575 -35.663 -25.123  1.00 32.58           C  
ANISOU  869  CG  GLN A 136     4513   4844   3020    203   -164    355       C  
ATOM    870  CD  GLN A 136      -9.000 -35.685 -24.639  1.00 41.24           C  
ANISOU  870  CD  GLN A 136     5636   6005   4030    267    -24    408       C  
ATOM    871  OE1 GLN A 136      -9.283 -35.855 -23.428  1.00 48.44           O  
ANISOU  871  OE1 GLN A 136     6634   7006   4766    351     16    415       O  
ATOM    872  NE2 GLN A 136      -9.910 -35.516 -25.562  1.00 28.06           N  
ANISOU  872  NE2 GLN A 136     3888   4299   2474    238     56    452       N  
ATOM    873  N   CYS A 137      -4.897 -39.336 -26.063  1.00 40.16           N  
ANISOU  873  N   CYS A 137     5336   5752   4173    109   -313    587       N  
ATOM    874  CA  CYS A 137      -4.240 -40.621 -25.868  1.00 41.41           C  
ANISOU  874  CA  CYS A 137     5479   5896   4357    134   -347    678       C  
ATOM    875  C   CYS A 137      -2.724 -40.464 -25.990  1.00 41.95           C  
ANISOU  875  C   CYS A 137     5477   5944   4517    136   -474    615       C  
ATOM    876  O   CYS A 137      -1.966 -40.954 -25.151  1.00 43.48           O  
ANISOU  876  O   CYS A 137     5678   6176   4667    201   -579    650       O  
ATOM    877  CB  CYS A 137      -4.755 -41.608 -26.921  1.00 38.77           C  
ANISOU  877  CB  CYS A 137     5103   5485   4142     80   -248    746       C  
ATOM    878  SG  CYS A 137      -4.004 -43.230 -26.878  1.00 42.74           S  
ANISOU  878  SG  CYS A 137     5589   5919   4733    112   -266    848       S  
ATOM    879  N   SER A 138      -2.294 -39.751 -27.025  1.00 40.50           N  
ANISOU  879  N   SER A 138     5218   5706   4464     70   -462    535       N  
ATOM    880  CA  SER A 138      -0.880 -39.522 -27.261  1.00 40.13           C  
ANISOU  880  CA  SER A 138     5066   5631   4549     56   -551    481       C  
ATOM    881  C   SER A 138      -0.266 -38.673 -26.167  1.00 39.41           C  
ANISOU  881  C   SER A 138     4978   5589   4406     79   -710    391       C  
ATOM    882  O   SER A 138       0.866 -38.920 -25.763  1.00 43.55           O  
ANISOU  882  O   SER A 138     5423   6129   4993    105   -839    378       O  
ATOM    883  CB  SER A 138      -0.653 -38.884 -28.632  1.00 40.31           C  
ANISOU  883  CB  SER A 138     5015   5586   4714    -21   -465    440       C  
ATOM    884  OG  SER A 138      -1.053 -37.537 -28.640  1.00 44.13           O  
ANISOU  884  OG  SER A 138     5526   6056   5185    -61   -463    370       O  
ATOM    885  N   GLN A 139      -1.004 -37.675 -25.690  1.00 38.24           N  
ANISOU  885  N   GLN A 139     4917   5463   4151     75   -710    316       N  
ATOM    886  CA  GLN A 139      -0.612 -36.925 -24.493  1.00 40.19           C  
ANISOU  886  CA  GLN A 139     5210   5763   4297    111   -870    201       C  
ATOM    887  C   GLN A 139      -0.403 -37.837 -23.282  1.00 42.44           C  
ANISOU  887  C   GLN A 139     5564   6158   4402    216   -977    264       C  
ATOM    888  O   GLN A 139       0.571 -37.681 -22.544  1.00 45.43           O  
ANISOU  888  O   GLN A 139     5914   6584   4763    247  -1171    193       O  
ATOM    889  CB  GLN A 139      -1.663 -35.887 -24.132  1.00 38.67           C  
ANISOU  889  CB  GLN A 139     5130   5573   3990    121   -816    115       C  
ATOM    890  CG  GLN A 139      -1.668 -34.693 -25.065  1.00 43.83           C  
ANISOU  890  CG  GLN A 139     5726   6107   4820     33   -765     35       C  
ATOM    891  CD  GLN A 139      -2.906 -33.831 -24.929  1.00 41.11           C  
ANISOU  891  CD  GLN A 139     5483   5746   4392     62   -669    -12       C  
ATOM    892  OE1 GLN A 139      -3.944 -34.267 -24.444  1.00 53.76           O  
ANISOU  892  OE1 GLN A 139     7172   7426   5828    134   -585     46       O  
ATOM    893  NE2 GLN A 139      -2.796 -32.605 -25.360  1.00 40.84           N  
ANISOU  893  NE2 GLN A 139     5426   5597   4495      9   -669   -105       N  
ATOM    894  N   GLY A 140      -1.316 -38.781 -23.079  1.00 42.09           N  
ANISOU  894  N   GLY A 140     5605   6154   4233    271   -858    405       N  
ATOM    895  CA  GLY A 140      -1.183 -39.750 -21.984  1.00 43.29           C  
ANISOU  895  CA  GLY A 140     5836   6400   4212    379   -926    518       C  
ATOM    896  C   GLY A 140       0.033 -40.658 -22.124  1.00 42.55           C  
ANISOU  896  C   GLY A 140     5634   6282   4250    406  -1039    590       C  
ATOM    897  O   GLY A 140       0.775 -40.857 -21.166  1.00 45.10           O  
ANISOU  897  O   GLY A 140     5975   6689   4472    491  -1218    598       O  
ATOM    898  N   VAL A 141       0.239 -41.210 -23.318  1.00 38.18           N  
ANISOU  898  N   VAL A 141     4969   5620   3916    346   -939    637       N  
ATOM    899  CA  VAL A 141       1.363 -42.120 -23.565  1.00 38.02           C  
ANISOU  899  CA  VAL A 141     4832   5559   4053    386  -1010    703       C  
ATOM    900  C   VAL A 141       2.699 -41.377 -23.565  1.00 36.12           C  
ANISOU  900  C   VAL A 141     4443   5332   3948    365  -1185    579       C  
ATOM    901  O   VAL A 141       3.722 -41.913 -23.158  1.00 37.67           O  
ANISOU  901  O   VAL A 141     4551   5553   4209    437  -1331    618       O  
ATOM    902  CB  VAL A 141       1.211 -42.850 -24.923  1.00 37.03           C  
ANISOU  902  CB  VAL A 141     4639   5310   4119    333   -838    752       C  
ATOM    903  CG1 VAL A 141       2.425 -43.752 -25.203  1.00 36.53           C  
ANISOU  903  CG1 VAL A 141     4448   5194   4239    393   -893    803       C  
ATOM    904  CG2 VAL A 141      -0.051 -43.684 -24.932  1.00 35.36           C  
ANISOU  904  CG2 VAL A 141     4544   5067   3826    337   -691    868       C  
ATOM    905  N   ALA A 142       2.695 -40.151 -24.059  1.00 36.67           N  
ANISOU  905  N   ALA A 142     4469   5371   4092    264  -1169    439       N  
ATOM    906  CA  ALA A 142       3.904 -39.349 -24.092  1.00 38.40           C  
ANISOU  906  CA  ALA A 142     4529   5579   4483    214  -1320    318       C  
ATOM    907  C   ALA A 142       4.391 -39.170 -22.675  1.00 40.97           C  
ANISOU  907  C   ALA A 142     4891   6017   4660    290  -1578    258       C  
ATOM    908  O   ALA A 142       5.603 -39.246 -22.414  1.00 46.90           O  
ANISOU  908  O   ALA A 142     5485   6789   5545    309  -1765    227       O  
ATOM    909  CB  ALA A 142       3.638 -38.007 -24.715  1.00 37.73           C  
ANISOU  909  CB  ALA A 142     4428   5424   4485     95  -1250    194       C  
ATOM    910  N   TYR A 143       3.450 -38.939 -21.759  1.00 38.94           N  
ANISOU  910  N   TYR A 143     4836   5841   4120    343  -1591    240       N  
ATOM    911  CA  TYR A 143       3.786 -38.799 -20.347  1.00 42.23           C  
ANISOU  911  CA  TYR A 143     5339   6392   4316    438  -1832    179       C  
ATOM    912  C   TYR A 143       4.460 -40.060 -19.862  1.00 43.53           C  
ANISOU  912  C   TYR A 143     5466   6622   4451    561  -1946    342       C  
ATOM    913  O   TYR A 143       5.500 -39.983 -19.243  1.00 49.62           O  
ANISOU  913  O   TYR A 143     6148   7463   5242    607  -2204    284       O  
ATOM    914  CB  TYR A 143       2.547 -38.474 -19.514  1.00 44.59           C  
ANISOU  914  CB  TYR A 143     5880   6774   4289    497  -1761    159       C  
ATOM    915  CG  TYR A 143       2.741 -38.534 -18.016  1.00 47.57           C  
ANISOU  915  CG  TYR A 143     6402   7319   4353    631  -1976    129       C  
ATOM    916  CD1 TYR A 143       3.134 -37.416 -17.298  1.00 51.30           C  
ANISOU  916  CD1 TYR A 143     6913   7845   4734    623  -2192   -111       C  
ATOM    917  CD2 TYR A 143       2.509 -39.716 -17.313  1.00 54.40           C  
ANISOU  917  CD2 TYR A 143     7380   8287   5004    771  -1961    342       C  
ATOM    918  CE1 TYR A 143       3.309 -37.473 -15.905  1.00 53.50           C  
ANISOU  918  CE1 TYR A 143     7350   8303   4676    761  -2408   -157       C  
ATOM    919  CE2 TYR A 143       2.686 -39.788 -15.920  1.00 57.01           C  
ANISOU  919  CE2 TYR A 143     7867   8794   4998    915  -2157    336       C  
ATOM    920  CZ  TYR A 143       3.075 -38.663 -15.228  1.00 56.60           C  
ANISOU  920  CZ  TYR A 143     7863   8819   4822    914  -2384     78       C  
ATOM    921  OH  TYR A 143       3.238 -38.735 -13.868  1.00 59.15           O  
ANISOU  921  OH  TYR A 143     8363   9337   4774   1067  -2590     57       O  
ATOM    922  N   LEU A 144       3.873 -41.212 -20.167  1.00 43.11           N  
ANISOU  922  N   LEU A 144     5470   6534   4375    613  -1763    543       N  
ATOM    923  CA  LEU A 144       4.419 -42.511 -19.775  1.00 46.30           C  
ANISOU  923  CA  LEU A 144     5852   6963   4778    742  -1836    730       C  
ATOM    924  C   LEU A 144       5.840 -42.712 -20.303  1.00 48.64           C  
ANISOU  924  C   LEU A 144     5894   7207   5378    737  -1966    705       C  
ATOM    925  O   LEU A 144       6.753 -43.171 -19.576  1.00 47.64           O  
ANISOU  925  O   LEU A 144     5702   7157   5242    852  -2193    760       O  
ATOM    926  CB  LEU A 144       3.532 -43.638 -20.325  1.00 47.13           C  
ANISOU  926  CB  LEU A 144     6029   6970   4907    754  -1579    922       C  
ATOM    927  CG  LEU A 144       2.105 -43.814 -19.781  1.00 52.61           C  
ANISOU  927  CG  LEU A 144     6940   7706   5343    777  -1417   1020       C  
ATOM    928  CD1 LEU A 144       1.455 -45.051 -20.414  1.00 46.61           C  
ANISOU  928  CD1 LEU A 144     6194   6815   4700    770  -1199   1205       C  
ATOM    929  CD2 LEU A 144       2.098 -43.942 -18.257  1.00 49.54           C  
ANISOU  929  CD2 LEU A 144     6714   7484   4627    922  -1565   1100       C  
ATOM    930  N   HIS A 145       6.009 -42.374 -21.579  1.00 46.42           N  
ANISOU  930  N   HIS A 145     5469   6805   5364    615  -1815    633       N  
ATOM    931  CA  HIS A 145       7.281 -42.538 -22.270  1.00 47.52           C  
ANISOU  931  CA  HIS A 145     5349   6883   5823    602  -1863    615       C  
ATOM    932  C   HIS A 145       8.359 -41.622 -21.717  1.00 48.98           C  
ANISOU  932  C   HIS A 145     5373   7139   6097    572  -2138    465       C  
ATOM    933  O   HIS A 145       9.536 -41.899 -21.902  1.00 54.14           O  
ANISOU  933  O   HIS A 145     5794   7782   6996    601  -2245    476       O  
ATOM    934  CB  HIS A 145       7.100 -42.276 -23.767  1.00 42.89           C  
ANISOU  934  CB  HIS A 145     4679   6167   5448    479  -1607    573       C  
ATOM    935  CG  HIS A 145       6.412 -43.386 -24.487  1.00 44.20           C  
ANISOU  935  CG  HIS A 145     4931   6246   5617    514  -1378    702       C  
ATOM    936  ND1 HIS A 145       6.172 -43.358 -25.840  1.00 43.57           N  
ANISOU  936  ND1 HIS A 145     4814   6067   5675    432  -1152    674       N  
ATOM    937  CD2 HIS A 145       5.924 -44.568 -24.042  1.00 47.81           C  
ANISOU  937  CD2 HIS A 145     5512   6690   5962    620  -1348    855       C  
ATOM    938  CE1 HIS A 145       5.559 -44.471 -26.196  1.00 39.93           C  
ANISOU  938  CE1 HIS A 145     4449   5536   5188    481  -1012    775       C  
ATOM    939  NE2 HIS A 145       5.397 -45.221 -25.125  1.00 40.15           N  
ANISOU  939  NE2 HIS A 145     4568   5600   5087    588  -1119    892       N  
ATOM    940  N   SER A 146       7.953 -40.545 -21.049  1.00 49.28           N  
ANISOU  940  N   SER A 146     5526   7241   5958    516  -2251    316       N  
ATOM    941  CA  SER A 146       8.882 -39.552 -20.513  1.00 56.00           C  
ANISOU  941  CA  SER A 146     6237   8138   6900    461  -2529    130       C  
ATOM    942  C   SER A 146       9.273 -39.829 -19.068  1.00 60.26           C  
ANISOU  942  C   SER A 146     6849   8846   7200    603  -2856    125       C  
ATOM    943  O   SER A 146      10.152 -39.179 -18.523  1.00 63.06           O  
ANISOU  943  O   SER A 146     7073   9256   7629    576  -3146    -32       O  
ATOM    944  CB  SER A 146       8.258 -38.154 -20.594  1.00 55.59           C  
ANISOU  944  CB  SER A 146     6279   8038   6803    324  -2485    -62       C  
ATOM    945  OG  SER A 146       7.262 -37.974 -19.602  1.00 60.67           O  
ANISOU  945  OG  SER A 146     7203   8781   7069    397  -2522    -98       O  
ATOM    946  N   MET A 147       8.597 -40.792 -18.459  1.00 64.49           N  
ANISOU  946  N   MET A 147     7595   9460   7448    751  -2809    301       N  
ATOM    947  CA  MET A 147       8.859 -41.207 -17.083  1.00 69.09           C  
ANISOU  947  CA  MET A 147     8292  10219   7740    919  -3089    353       C  
ATOM    948  C   MET A 147      10.340 -41.409 -16.750  1.00 71.43           C  
ANISOU  948  C   MET A 147     8335  10576   8228    981  -3419    334       C  
ATOM    949  O   MET A 147      11.101 -41.964 -17.549  1.00 68.12           O  
ANISOU  949  O   MET A 147     7669  10063   8152    976  -3361    421       O  
ATOM    950  CB  MET A 147       8.143 -42.529 -16.825  1.00 71.48           C  
ANISOU  950  CB  MET A 147     8778  10540   7842   1067  -2924    632       C  
ATOM    951  CG  MET A 147       7.701 -42.711 -15.413  1.00 79.21           C  
ANISOU  951  CG  MET A 147    10018  11703   8376   1222  -3070    699       C  
ATOM    952  SD  MET A 147       6.099 -41.941 -15.214  1.00 85.77           S  
ANISOU  952  SD  MET A 147    11136  12553   8899   1155  -2822    611       S  
ATOM    953  CE  MET A 147       5.038 -43.202 -15.900  1.00 77.27           C  
ANISOU  953  CE  MET A 147    10139  11347   7874   1170  -2431    907       C  
ATOM    954  N   GLN A 148      10.725 -40.961 -15.558  1.00 75.85           N  
ANISOU  954  N   GLN A 148     8958  11303   8559   1050  -3768    213       N  
ATOM    955  CA  GLN A 148      12.052 -41.230 -15.003  1.00 81.20           C  
ANISOU  955  CA  GLN A 148     9418  12081   9352   1144  -4144    209       C  
ATOM    956  C   GLN A 148      11.914 -42.081 -13.732  1.00 84.11           C  
ANISOU  956  C   GLN A 148    10012  12644   9303   1385  -4338    387       C  
ATOM    957  O   GLN A 148      10.885 -42.014 -13.051  1.00 83.72           O  
ANISOU  957  O   GLN A 148    10291  12684   8835   1445  -4254    411       O  
ATOM    958  CB  GLN A 148      12.779 -39.915 -14.679  1.00 84.50           C  
ANISOU  958  CB  GLN A 148     9687  12536   9884   1013  -4458   -113       C  
ATOM    959  CG  GLN A 148      13.002 -38.985 -15.885  1.00 84.01           C  
ANISOU  959  CG  GLN A 148     9392  12274  10255    771  -4276   -272       C  
ATOM    960  CD  GLN A 148      13.889 -39.599 -16.961  1.00 84.98           C  
ANISOU  960  CD  GLN A 148     9169  12279  10841    744  -4149   -134       C  
ATOM    961  OE1 GLN A 148      14.759 -40.424 -16.676  1.00 92.87           O  
ANISOU  961  OE1 GLN A 148     9995  13351  11942    880  -4335     -9       O  
ATOM    962  NE2 GLN A 148      13.672 -39.195 -18.205  1.00 83.65           N  
ANISOU  962  NE2 GLN A 148     8903  11934  10947    582  -3824   -151       N  
ATOM    963  N   PRO A 149      12.940 -42.892 -13.406  1.00 86.95           N  
ANISOU  963  N   PRO A 149    10195  13071   9772   1536  -4584    530       N  
ATOM    964  CA  PRO A 149      14.179 -43.165 -14.151  1.00 86.53           C  
ANISOU  964  CA  PRO A 149     9736  12924  10218   1509  -4664    546       C  
ATOM    965  C   PRO A 149      14.013 -43.926 -15.468  1.00 83.16           C  
ANISOU  965  C   PRO A 149     9192  12284  10122   1471  -4259    715       C  
ATOM    966  O   PRO A 149      14.913 -43.866 -16.301  1.00 85.04           O  
ANISOU  966  O   PRO A 149     9095  12422  10794   1400  -4238    670       O  
ATOM    967  CB  PRO A 149      14.991 -44.044 -13.186  1.00 90.29           C  
ANISOU  967  CB  PRO A 149    10162  13561  10583   1754  -5017    720       C  
ATOM    968  CG  PRO A 149      14.343 -43.890 -11.860  1.00 94.05           C  
ANISOU  968  CG  PRO A 149    11004  14246  10486   1875  -5202    716       C  
ATOM    969  CD  PRO A 149      12.907 -43.630 -12.130  1.00 89.09           C  
ANISOU  969  CD  PRO A 149    10681  13541   9628   1780  -4812    711       C  
ATOM    970  N   LYS A 150      12.907 -44.659 -15.637  1.00 78.91           N  
ANISOU  970  N   LYS A 150     8918  11679   9386   1523  -3947    903       N  
ATOM    971  CA  LYS A 150      12.708 -45.504 -16.819  1.00 75.21           C  
ANISOU  971  CA  LYS A 150     8372  11009   9194   1507  -3590   1054       C  
ATOM    972  C   LYS A 150      11.325 -45.289 -17.419  1.00 72.68           C  
ANISOU  972  C   LYS A 150     8285  10589   8743   1379  -3225   1038       C  
ATOM    973  O   LYS A 150      10.328 -45.171 -16.702  1.00 73.93           O  
ANISOU  973  O   LYS A 150     8731  10828   8532   1403  -3193   1068       O  
ATOM    974  CB  LYS A 150      12.922 -46.985 -16.490  1.00 75.63           C  
ANISOU  974  CB  LYS A 150     8455  11042   9239   1736  -3602   1351       C  
ATOM    975  CG  LYS A 150      12.014 -47.689 -15.705  0.00 77.77           C  
ANISOU  975  CG  LYS A 150     9045  11358   9147   1863  -3544   1560       C  
ATOM    976  CD  LYS A 150      12.498 -49.103 -15.431  0.00 80.00           C  
ANISOU  976  CD  LYS A 150     9295  11590   9513   2092  -3593   1856       C  
ATOM    977  CE  LYS A 150      11.446 -49.925 -14.713  0.00 80.20           C  
ANISOU  977  CE  LYS A 150     9662  11619   9192   2209  -3461   2119       C  
ATOM    978  NZ  LYS A 150      11.927 -51.299 -14.401  0.00 82.76           N  
ANISOU  978  NZ  LYS A 150     9966  11868   9609   2442  -3514   2431       N  
ATOM    979  N   ALA A 151      11.285 -45.218 -18.747  1.00 69.74           N  
ANISOU  979  N   ALA A 151     7776  10050   8673   1249  -2952    989       N  
ATOM    980  CA  ALA A 151      10.051 -45.000 -19.471  1.00 65.08           C  
ANISOU  980  CA  ALA A 151     7362   9361   8006   1123  -2625    964       C  
ATOM    981  C   ALA A 151       9.120 -46.172 -19.232  1.00 63.44           C  
ANISOU  981  C   ALA A 151     7382   9108   7613   1233  -2456   1193       C  
ATOM    982  O   ALA A 151       9.574 -47.308 -19.187  1.00 66.05           O  
ANISOU  982  O   ALA A 151     7660   9382   8053   1373  -2469   1373       O  
ATOM    983  CB  ALA A 151      10.331 -44.864 -20.950  1.00 63.05           C  
ANISOU  983  CB  ALA A 151     6910   8949   8099   1000  -2390    895       C  
ATOM    984  N   LEU A 152       7.832 -45.890 -19.049  1.00 61.01           N  
ANISOU  984  N   LEU A 152     7316   8816   7049   1172  -2299   1192       N  
ATOM    985  CA  LEU A 152       6.814 -46.933 -19.057  1.00 61.59           C  
ANISOU  985  CA  LEU A 152     7576   8807   7018   1224  -2076   1398       C  
ATOM    986  C   LEU A 152       6.260 -47.097 -20.452  1.00 57.05           C  
ANISOU  986  C   LEU A 152     6957   8055   6665   1093  -1781   1356       C  
ATOM    987  O   LEU A 152       5.795 -46.133 -21.056  1.00 59.05           O  
ANISOU  987  O   LEU A 152     7206   8303   6926    947  -1682   1191       O  
ATOM    988  CB  LEU A 152       5.649 -46.600 -18.136  1.00 61.79           C  
ANISOU  988  CB  LEU A 152     7865   8946   6665   1231  -2034   1433       C  
ATOM    989  CG  LEU A 152       5.891 -46.522 -16.639  1.00 68.74           C  
ANISOU  989  CG  LEU A 152     8881  10027   7209   1382  -2287   1496       C  
ATOM    990  CD1 LEU A 152       4.592 -46.933 -15.951  1.00 75.13           C  
ANISOU  990  CD1 LEU A 152     9962  10879   7706   1433  -2103   1672       C  
ATOM    991  CD2 LEU A 152       7.070 -47.377 -16.142  1.00 81.36           C  
ANISOU  991  CD2 LEU A 152    10374  11657   8884   1557  -2526   1648       C  
ATOM    992  N   ILE A 153       6.309 -48.317 -20.957  1.00 55.36           N  
ANISOU  992  N   ILE A 153     6718   7692   6626   1155  -1652   1502       N  
ATOM    993  CA  ILE A 153       5.674 -48.654 -22.219  1.00 55.16           C  
ANISOU  993  CA  ILE A 153     6691   7500   6769   1049  -1383   1467       C  
ATOM    994  C   ILE A 153       4.319 -49.285 -21.880  1.00 56.60           C  
ANISOU  994  C   ILE A 153     7088   7631   6786   1040  -1225   1614       C  
ATOM    995  O   ILE A 153       4.228 -50.135 -20.970  1.00 61.95           O  
ANISOU  995  O   ILE A 153     7867   8308   7363   1165  -1269   1822       O  
ATOM    996  CB  ILE A 153       6.562 -49.624 -23.023  1.00 54.49           C  
ANISOU  996  CB  ILE A 153     6447   7261   6996   1123  -1330   1505       C  
ATOM    997  CG1 ILE A 153       7.962 -49.020 -23.213  1.00 54.83           C  
ANISOU  997  CG1 ILE A 153     6243   7371   7219   1145  -1487   1389       C  
ATOM    998  CG2 ILE A 153       5.934 -49.948 -24.376  1.00 53.14           C  
ANISOU  998  CG2 ILE A 153     6292   6928   6971   1018  -1068   1430       C  
ATOM    999  CD1 ILE A 153       9.038 -50.061 -23.428  1.00 56.62           C  
ANISOU  999  CD1 ILE A 153     6304   7497   7710   1298  -1517   1481       C  
ATOM   1000  N   HIS A 154       3.266 -48.860 -22.575  1.00 53.71           N  
ANISOU 1000  N   HIS A 154     6783   7227   6398    897  -1043   1522       N  
ATOM   1001  CA  HIS A 154       1.931 -49.392 -22.305  1.00 55.84           C  
ANISOU 1001  CA  HIS A 154     7217   7448   6553    866   -884   1651       C  
ATOM   1002  C   HIS A 154       1.819 -50.861 -22.727  1.00 58.71           C  
ANISOU 1002  C   HIS A 154     7587   7600   7119    904   -764   1795       C  
ATOM   1003  O   HIS A 154       1.355 -51.712 -21.942  1.00 60.29           O  
ANISOU 1003  O   HIS A 154     7900   7755   7253    974   -726   2012       O  
ATOM   1004  CB  HIS A 154       0.873 -48.568 -23.003  1.00 53.84           C  
ANISOU 1004  CB  HIS A 154     6991   7205   6260    710   -744   1511       C  
ATOM   1005  CG  HIS A 154      -0.520 -48.916 -22.595  1.00 54.52           C  
ANISOU 1005  CG  HIS A 154     7212   7276   6227    674   -595   1633       C  
ATOM   1006  ND1 HIS A 154      -1.036 -50.185 -22.723  1.00 56.29           N  
ANISOU 1006  ND1 HIS A 154     7474   7338   6575    676   -470   1792       N  
ATOM   1007  CD2 HIS A 154      -1.518 -48.156 -22.092  1.00 59.31           C  
ANISOU 1007  CD2 HIS A 154     7908   7997   6632    630   -537   1618       C  
ATOM   1008  CE1 HIS A 154      -2.285 -50.200 -22.295  1.00 55.65           C  
ANISOU 1008  CE1 HIS A 154     7484   7278   6381    625   -341   1884       C  
ATOM   1009  NE2 HIS A 154      -2.604 -48.981 -21.907  1.00 59.47           N  
ANISOU 1009  NE2 HIS A 154     7999   7937   6659    606   -372   1782       N  
ATOM   1010  N  AARG A 155       2.239 -51.133 -23.961  0.50 56.85           N  
ANISOU 1010  N  AARG A 155     7240   7232   7129    861   -695   1675       N  
ATOM   1011  N  BARG A 155       2.260 -51.142 -23.954  0.50 57.99           N  
ANISOU 1011  N  BARG A 155     7383   7375   7274    863   -697   1676       N  
ATOM   1012  CA AARG A 155       2.301 -52.488 -24.533  0.50 58.28           C  
ANISOU 1012  CA AARG A 155     7415   7185   7545    900   -590   1749       C  
ATOM   1013  CA BARG A 155       2.277 -52.493 -24.557  0.50 60.31           C  
ANISOU 1013  CA BARG A 155     7672   7438   7804    897   -586   1747       C  
ATOM   1014  C  AARG A 155       0.951 -53.024 -25.026  0.50 57.47           C  
ANISOU 1014  C  AARG A 155     7410   6941   7486    779   -409   1763       C  
ATOM   1015  C  BARG A 155       0.938 -52.940 -25.127  0.50 58.41           C  
ANISOU 1015  C  BARG A 155     7522   7065   7605    767   -405   1741       C  
ATOM   1016  O  AARG A 155       0.924 -53.962 -25.825  0.50 58.16           O  
ANISOU 1016  O  AARG A 155     7484   6822   7790    768   -314   1736       O  
ATOM   1017  O  BARG A 155       0.902 -53.721 -26.082  0.50 59.02           O  
ANISOU 1017  O  BARG A 155     7579   6953   7894    740   -307   1676       O  
ATOM   1018  CB AARG A 155       2.943 -53.503 -23.569  0.50 60.80           C  
ANISOU 1018  CB AARG A 155     7754   7445   7903   1080   -683   1980       C  
ATOM   1019  CB BARG A 155       2.788 -53.581 -23.600  0.50 63.42           C  
ANISOU 1019  CB BARG A 155     8100   7758   8237   1068   -661   1988       C  
ATOM   1020  CG AARG A 155       4.342 -53.139 -23.059  0.50 63.81           C  
ANISOU 1020  CG AARG A 155     8009   7956   8279   1217   -899   1978       C  
ATOM   1021  CG BARG A 155       4.291 -53.684 -23.484  0.50 69.23           C  
ANISOU 1021  CG BARG A 155     8691   8522   9092   1219   -821   1987       C  
ATOM   1022  CD AARG A 155       4.927 -54.260 -22.165  0.50 65.78           C  
ANISOU 1022  CD AARG A 155     8282   8133   8578   1416   -997   2232       C  
ATOM   1023  CD BARG A 155       4.715 -55.071 -22.974  0.50 73.64           C  
ANISOU 1023  CD BARG A 155     9273   8914   9792   1392   -843   2221       C  
ATOM   1024  NE AARG A 155       6.358 -54.088 -21.887  0.50 66.12           N  
ANISOU 1024  NE AARG A 155     8156   8268   8698   1558  -1210   2219       N  
ATOM   1025  NE BARG A 155       4.894 -56.029 -24.072  0.50 78.85           N  
ANISOU 1025  NE BARG A 155     9880   9314  10764   1400   -697   2157       N  
ATOM   1026  CZ AARG A 155       6.872 -53.337 -20.911  0.50 69.29           C  
ANISOU 1026  CZ AARG A 155     8536   8897   8895   1620  -1445   2231       C  
ATOM   1027  CZ BARG A 155       4.010 -56.952 -24.455  0.50 76.79           C  
ANISOU 1027  CZ BARG A 155     9728   8826  10624   1339   -528   2206       C  
ATOM   1028  NH1AARG A 155       6.089 -52.652 -20.076  0.50 70.24           N  
ANISOU 1028  NH1AARG A 155     8816   9184   8688   1568  -1485   2251       N  
ATOM   1029  NH1BARG A 155       2.833 -57.096 -23.854  0.50 76.40           N  
ANISOU 1029  NH1BARG A 155     9826   8766  10436   1258   -459   2348       N  
ATOM   1030  NH2AARG A 155       8.192 -53.266 -20.771  0.50 66.16           N  
ANISOU 1030  NH2AARG A 155     7947   8563   8629   1739  -1646   2210       N  
ATOM   1031  NH2BARG A 155       4.319 -57.748 -25.466  0.50 76.90           N  
ANISOU 1031  NH2BARG A 155     9692   8611  10915   1361   -422   2102       N  
ATOM   1032  N   ASP A 156      -0.155 -52.448 -24.561  1.00 56.97           N  
ANISOU 1032  N   ASP A 156     7432   6982   7233    691   -363   1793       N  
ATOM   1033  CA  ASP A 156      -1.478 -52.955 -24.904  1.00 57.57           C  
ANISOU 1033  CA  ASP A 156     7568   6935   7370    572   -206   1825       C  
ATOM   1034  C   ASP A 156      -2.477 -51.849 -25.251  1.00 55.89           C  
ANISOU 1034  C   ASP A 156     7359   6851   7026    437   -155   1693       C  
ATOM   1035  O   ASP A 156      -3.638 -51.909 -24.833  1.00 55.56           O  
ANISOU 1035  O   ASP A 156     7370   6816   6922    373    -61   1787       O  
ATOM   1036  CB  ASP A 156      -1.987 -53.809 -23.731  1.00 61.89           C  
ANISOU 1036  CB  ASP A 156     8217   7427   7871    633   -157   2106       C  
ATOM   1037  CG  ASP A 156      -2.960 -54.918 -24.163  1.00 66.87           C  
ANISOU 1037  CG  ASP A 156     8872   7815   8721    534      0   2181       C  
ATOM   1038  OD1 ASP A 156      -3.330 -54.997 -25.354  1.00 74.15           O  
ANISOU 1038  OD1 ASP A 156     9741   8628   9803    415     51   1992       O  
ATOM   1039  OD2 ASP A 156      -3.353 -55.727 -23.286  1.00 85.56           O  
ANISOU 1039  OD2 ASP A 156    11314  10096  11101    577     69   2436       O  
ATOM   1040  N   LEU A 157      -2.039 -50.850 -26.022  1.00 51.85           N  
ANISOU 1040  N   LEU A 157     6779   6431   6491    399   -205   1491       N  
ATOM   1041  CA  LEU A 157      -2.949 -49.786 -26.449  1.00 49.05           C  
ANISOU 1041  CA  LEU A 157     6423   6179   6035    286   -162   1371       C  
ATOM   1042  C   LEU A 157      -4.001 -50.285 -27.428  1.00 46.50           C  
ANISOU 1042  C   LEU A 157     6095   5732   5842    165    -54   1315       C  
ATOM   1043  O   LEU A 157      -3.678 -50.850 -28.463  1.00 45.45           O  
ANISOU 1043  O   LEU A 157     5932   5474   5863    144    -37   1213       O  
ATOM   1044  CB  LEU A 157      -2.212 -48.646 -27.126  1.00 49.59           C  
ANISOU 1044  CB  LEU A 157     6423   6344   6076    272   -227   1193       C  
ATOM   1045  CG  LEU A 157      -1.780 -47.416 -26.354  1.00 53.31           C  
ANISOU 1045  CG  LEU A 157     6890   6985   6379    307   -332   1160       C  
ATOM   1046  CD1 LEU A 157      -1.683 -46.272 -27.370  1.00 51.13           C  
ANISOU 1046  CD1 LEU A 157     6554   6750   6122    228   -322    987       C  
ATOM   1047  CD2 LEU A 157      -2.732 -47.077 -25.216  1.00 58.62           C  
ANISOU 1047  CD2 LEU A 157     7658   7758   6855    318   -314   1252       C  
ATOM   1048  N   LYS A 158      -5.256 -50.041 -27.085  1.00 45.02           N  
ANISOU 1048  N   LYS A 158     5930   5589   5586     94     15   1369       N  
ATOM   1049  CA  LYS A 158      -6.384 -50.447 -27.880  1.00 43.95           C  
ANISOU 1049  CA  LYS A 158     5767   5356   5578    -30     91   1321       C  
ATOM   1050  C   LYS A 158      -7.656 -49.881 -27.244  1.00 44.47           C  
ANISOU 1050  C   LYS A 158     5827   5526   5543    -81    162   1399       C  
ATOM   1051  O   LYS A 158      -7.718 -49.679 -26.033  1.00 46.35           O  
ANISOU 1051  O   LYS A 158     6115   5857   5639    -10    191   1542       O  
ATOM   1052  CB  LYS A 158      -6.453 -51.966 -27.975  1.00 44.08           C  
ANISOU 1052  CB  LYS A 158     5794   5146   5810    -48    139   1405       C  
ATOM   1053  CG  LYS A 158      -6.467 -52.654 -26.619  1.00 46.68           C  
ANISOU 1053  CG  LYS A 158     6177   5436   6122     26    187   1661       C  
ATOM   1054  CD  LYS A 158      -6.688 -54.131 -26.774  1.00 47.27           C  
ANISOU 1054  CD  LYS A 158     6259   5248   6453    -11    252   1753       C  
ATOM   1055  CE  LYS A 158      -6.789 -54.828 -25.435  1.00 50.81           C  
ANISOU 1055  CE  LYS A 158     6771   5650   6886     62    323   2051       C  
ATOM   1056  NZ  LYS A 158      -6.948 -56.275 -25.678  1.00 52.93           N  
ANISOU 1056  NZ  LYS A 158     7043   5616   7452     20    388   2137       N  
ATOM   1057  N   PRO A 159      -8.681 -49.620 -28.059  1.00 45.19           N  
ANISOU 1057  N   PRO A 159     5856   5613   5699   -192    190   1304       N  
ATOM   1058  CA  PRO A 159      -9.872 -48.956 -27.548  1.00 43.45           C  
ANISOU 1058  CA  PRO A 159     5601   5505   5404   -227    263   1362       C  
ATOM   1059  C   PRO A 159     -10.533 -49.547 -26.293  1.00 44.52           C  
ANISOU 1059  C   PRO A 159     5753   5628   5534   -211    390   1588       C  
ATOM   1060  O   PRO A 159     -11.115 -48.789 -25.524  1.00 44.23           O  
ANISOU 1060  O   PRO A 159     5722   5735   5348   -173    459   1648       O  
ATOM   1061  CB  PRO A 159     -10.824 -49.006 -28.737  1.00 44.02           C  
ANISOU 1061  CB  PRO A 159     5581   5525   5621   -352    251   1241       C  
ATOM   1062  CG  PRO A 159      -9.928 -48.960 -29.912  1.00 45.99           C  
ANISOU 1062  CG  PRO A 159     5853   5736   5884   -347    150   1066       C  
ATOM   1063  CD  PRO A 159      -8.784 -49.867 -29.508  1.00 46.25           C  
ANISOU 1063  CD  PRO A 159     5950   5659   5965   -275    146   1129       C  
ATOM   1064  N   PRO A 160     -10.510 -50.876 -26.111  1.00 44.88           N  
ANISOU 1064  N   PRO A 160     5808   5496   5747   -237    440   1719       N  
ATOM   1065  CA  PRO A 160     -10.985 -51.459 -24.841  1.00 47.95           C  
ANISOU 1065  CA  PRO A 160     6233   5873   6113   -204    580   1980       C  
ATOM   1066  C   PRO A 160     -10.304 -50.944 -23.563  1.00 50.25           C  
ANISOU 1066  C   PRO A 160     6647   6333   6113    -40    576   2096       C  
ATOM   1067  O   PRO A 160     -10.907 -51.026 -22.495  1.00 52.28           O  
ANISOU 1067  O   PRO A 160     6943   6658   6261      1    713   2291       O  
ATOM   1068  CB  PRO A 160     -10.717 -52.959 -25.022  1.00 45.61           C  
ANISOU 1068  CB  PRO A 160     5945   5320   6065   -242    599   2079       C  
ATOM   1069  CG  PRO A 160     -10.807 -53.171 -26.483  1.00 44.35           C  
ANISOU 1069  CG  PRO A 160     5710   5036   6107   -357    511   1847       C  
ATOM   1070  CD  PRO A 160     -10.164 -51.931 -27.080  1.00 47.84           C  
ANISOU 1070  CD  PRO A 160     6164   5658   6357   -302    390   1638       C  
ATOM   1071  N   ASN A 161      -9.072 -50.436 -23.685  1.00 51.64           N  
ANISOU 1071  N   ASN A 161     6875   6577   6167     50    422   1975       N  
ATOM   1072  CA  ASN A 161      -8.306 -49.840 -22.567  1.00 52.51           C  
ANISOU 1072  CA  ASN A 161     7093   6858   5999    201    356   2028       C  
ATOM   1073  C   ASN A 161      -8.440 -48.328 -22.467  1.00 51.28           C  
ANISOU 1073  C   ASN A 161     6944   6896   5645    222    313   1864       C  
ATOM   1074  O   ASN A 161      -7.887 -47.736 -21.563  1.00 55.75           O  
ANISOU 1074  O   ASN A 161     7600   7605   5978    335    244   1866       O  
ATOM   1075  CB  ASN A 161      -6.803 -50.137 -22.723  1.00 53.29           C  
ANISOU 1075  CB  ASN A 161     7214   6913   6121    286    190   1984       C  
ATOM   1076  CG  ASN A 161      -6.479 -51.593 -22.560  1.00 58.80           C  
ANISOU 1076  CG  ASN A 161     7934   7423   6984    318    219   2169       C  
ATOM   1077  OD1 ASN A 161      -7.280 -52.362 -22.022  1.00 75.48           O  
ANISOU 1077  OD1 ASN A 161    10076   9456   9145    297    362   2376       O  
ATOM   1078  ND2 ASN A 161      -5.293 -51.988 -23.004  1.00 60.02           N  
ANISOU 1078  ND2 ASN A 161     8066   7493   7245    376     99   2109       N  
ATOM   1079  N   LEU A 162      -9.119 -47.708 -23.426  1.00 51.54           N  
ANISOU 1079  N   LEU A 162     6885   6923   5776    120    335   1713       N  
ATOM   1080  CA  LEU A 162      -9.299 -46.254 -23.474  1.00 47.46           C  
ANISOU 1080  CA  LEU A 162     6365   6548   5119    136    302   1556       C  
ATOM   1081  C   LEU A 162     -10.696 -45.927 -22.988  1.00 48.33           C  
ANISOU 1081  C   LEU A 162     6452   6731   5180    124    468   1627       C  
ATOM   1082  O   LEU A 162     -11.666 -46.274 -23.653  1.00 50.44           O  
ANISOU 1082  O   LEU A 162     6609   6924   5632     20    550   1643       O  
ATOM   1083  CB  LEU A 162      -9.124 -45.724 -24.901  1.00 43.22           C  
ANISOU 1083  CB  LEU A 162     5741   5959   4719     52    221   1363       C  
ATOM   1084  CG  LEU A 162      -7.794 -46.005 -25.591  1.00 38.17           C  
ANISOU 1084  CG  LEU A 162     5096   5245   4159     57     94   1279       C  
ATOM   1085  CD1 LEU A 162      -7.805 -45.440 -26.995  1.00 46.91           C  
ANISOU 1085  CD1 LEU A 162     6135   6324   5366    -20     58   1115       C  
ATOM   1086  CD2 LEU A 162      -6.630 -45.458 -24.834  1.00 42.25           C  
ANISOU 1086  CD2 LEU A 162     5672   5851   4531    158    -19   1252       C  
ATOM   1087  N   LEU A 163     -10.783 -45.279 -21.822  1.00 50.23           N  
ANISOU 1087  N   LEU A 163     6790   7120   5173    236    513   1660       N  
ATOM   1088  CA  LEU A 163     -12.044 -44.913 -21.187  1.00 47.51           C  
ANISOU 1088  CA  LEU A 163     6434   6869   4750    260    702   1733       C  
ATOM   1089  C   LEU A 163     -12.385 -43.466 -21.428  1.00 44.46           C  
ANISOU 1089  C   LEU A 163     6026   6569   4297    284    682   1542       C  
ATOM   1090  O   LEU A 163     -11.501 -42.637 -21.476  1.00 40.95           O  
ANISOU 1090  O   LEU A 163     5646   6159   3753    328    533   1384       O  
ATOM   1091  CB  LEU A 163     -11.932 -45.088 -19.690  1.00 51.04           C  
ANISOU 1091  CB  LEU A 163     7034   7438   4923    398    785   1884       C  
ATOM   1092  CG  LEU A 163     -11.508 -46.444 -19.170  1.00 55.03           C  
ANISOU 1092  CG  LEU A 163     7600   7871   5436    419    809   2116       C  
ATOM   1093  CD1 LEU A 163     -11.467 -46.334 -17.669  1.00 53.97           C  
ANISOU 1093  CD1 LEU A 163     7640   7907   4958    582    887   2250       C  
ATOM   1094  CD2 LEU A 163     -12.464 -47.540 -19.620  1.00 57.28           C  
ANISOU 1094  CD2 LEU A 163     7757   8001   6005    293    975   2287       C  
ATOM   1095  N   LEU A 164     -13.678 -43.163 -21.515  1.00 46.26           N  
ANISOU 1095  N   LEU A 164     6155   6824   4598    261    839   1567       N  
ATOM   1096  CA  LEU A 164     -14.168 -41.797 -21.740  1.00 45.30           C  
ANISOU 1096  CA  LEU A 164     6001   6767   4443    300    845   1406       C  
ATOM   1097  C   LEU A 164     -14.945 -41.215 -20.543  1.00 46.10           C  
ANISOU 1097  C   LEU A 164     6164   7008   4346    430   1033   1444       C  
ATOM   1098  O   LEU A 164     -15.718 -41.913 -19.883  1.00 45.46           O  
ANISOU 1098  O   LEU A 164     6056   6963   4252    444   1231   1631       O  
ATOM   1099  CB  LEU A 164     -15.055 -41.777 -22.981  1.00 43.43           C  
ANISOU 1099  CB  LEU A 164     5575   6455   4473    187    852   1377       C  
ATOM   1100  CG  LEU A 164     -14.361 -42.261 -24.267  1.00 50.96           C  
ANISOU 1100  CG  LEU A 164     6483   7285   5593     72    678   1310       C  
ATOM   1101  CD1 LEU A 164     -15.307 -42.171 -25.464  1.00 48.68           C  
ANISOU 1101  CD1 LEU A 164     6025   6950   5520    -23    663   1269       C  
ATOM   1102  CD2 LEU A 164     -13.077 -41.484 -24.564  1.00 52.97           C  
ANISOU 1102  CD2 LEU A 164     6837   7538   5750    109    509   1155       C  
ATOM   1103  N   VAL A 165     -14.725 -39.930 -20.279  1.00 44.95           N  
ANISOU 1103  N   VAL A 165     6100   6926   4054    525    982   1265       N  
ATOM   1104  CA  VAL A 165     -15.449 -39.202 -19.237  1.00 48.00           C  
ANISOU 1104  CA  VAL A 165     6557   7437   4245    667   1158   1245       C  
ATOM   1105  C   VAL A 165     -15.976 -37.860 -19.756  1.00 47.83           C  
ANISOU 1105  C   VAL A 165     6468   7396   4310    702   1156   1065       C  
ATOM   1106  O   VAL A 165     -15.894 -37.565 -20.955  1.00 46.07           O  
ANISOU 1106  O   VAL A 165     6134   7070   4302    608   1031    995       O  
ATOM   1107  CB  VAL A 165     -14.581 -38.966 -17.970  1.00 48.60           C  
ANISOU 1107  CB  VAL A 165     6870   7625   3969    803   1105   1190       C  
ATOM   1108  CG1 VAL A 165     -14.353 -40.260 -17.251  1.00 47.25           C  
ANISOU 1108  CG1 VAL A 165     6771   7500   3683    815   1167   1420       C  
ATOM   1109  CG2 VAL A 165     -13.279 -38.313 -18.317  1.00 48.44           C  
ANISOU 1109  CG2 VAL A 165     6926   7553   3927    785    830    985       C  
ATOM   1110  N   ALA A 166     -16.562 -37.075 -18.855  1.00 51.16           N  
ANISOU 1110  N   ALA A 166     6962   7915   4561    850   1310   1004       N  
ATOM   1111  CA  ALA A 166     -17.016 -35.732 -19.183  1.00 52.76           C  
ANISOU 1111  CA  ALA A 166     7127   8084   4833    917   1317    828       C  
ATOM   1112  C   ALA A 166     -17.869 -35.689 -20.458  1.00 51.10           C  
ANISOU 1112  C   ALA A 166     6676   7787   4952    823   1324    878       C  
ATOM   1113  O   ALA A 166     -17.632 -34.857 -21.328  1.00 52.24           O  
ANISOU 1113  O   ALA A 166     6788   7839   5222    799   1184    753       O  
ATOM   1114  CB  ALA A 166     -15.815 -34.819 -19.333  1.00 54.52           C  
ANISOU 1114  CB  ALA A 166     7488   8239   4989    923   1081    606       C  
ATOM   1115  N   GLY A 167     -18.848 -36.585 -20.563  1.00 49.75           N  
ANISOU 1115  N   GLY A 167     6335   7645   4921    768   1480   1066       N  
ATOM   1116  CA  GLY A 167     -19.741 -36.647 -21.721  1.00 49.05           C  
ANISOU 1116  CA  GLY A 167     6002   7495   5141    678   1466   1115       C  
ATOM   1117  C   GLY A 167     -19.123 -37.113 -23.038  1.00 47.68           C  
ANISOU 1117  C   GLY A 167     5773   7212   5131    517   1231   1101       C  
ATOM   1118  O   GLY A 167     -19.565 -36.706 -24.088  1.00 45.61           O  
ANISOU 1118  O   GLY A 167     5376   6902   5053    479   1145   1065       O  
ATOM   1119  N   GLY A 168     -18.114 -37.978 -22.980  1.00 48.16           N  
ANISOU 1119  N   GLY A 168     5941   7241   5117    438   1132   1135       N  
ATOM   1120  CA  GLY A 168     -17.460 -38.515 -24.175  1.00 43.37           C  
ANISOU 1120  CA  GLY A 168     5298   6534   4645    301    936   1114       C  
ATOM   1121  C   GLY A 168     -16.310 -37.641 -24.598  1.00 43.23           C  
ANISOU 1121  C   GLY A 168     5405   6471   4548    321    760    957       C  
ATOM   1122  O   GLY A 168     -15.685 -37.876 -25.626  1.00 43.76           O  
ANISOU 1122  O   GLY A 168     5458   6466   4704    231    613    923       O  
ATOM   1123  N   THR A 169     -16.021 -36.633 -23.784  1.00 46.34           N  
ANISOU 1123  N   THR A 169     5923   6903   4779    440    785    854       N  
ATOM   1124  CA  THR A 169     -15.146 -35.520 -24.169  1.00 44.31           C  
ANISOU 1124  CA  THR A 169     5752   6582   4501    461    641    693       C  
ATOM   1125  C   THR A 169     -13.691 -35.770 -23.806  1.00 42.41           C  
ANISOU 1125  C   THR A 169     5647   6326   4139    436    508    637       C  
ATOM   1126  O   THR A 169     -12.772 -35.342 -24.497  1.00 41.46           O  
ANISOU 1126  O   THR A 169     5544   6129   4080    385    366    554       O  
ATOM   1127  CB  THR A 169     -15.596 -34.269 -23.410  1.00 45.84           C  
ANISOU 1127  CB  THR A 169     6010   6802   4607    604    729    582       C  
ATOM   1128  OG1 THR A 169     -16.947 -33.995 -23.753  1.00 54.80           O  
ANISOU 1128  OG1 THR A 169     6992   7950   5879    645    855    639       O  
ATOM   1129  CG2 THR A 169     -14.788 -33.079 -23.762  1.00 54.38           C  
ANISOU 1129  CG2 THR A 169     7170   7783   5709    617    595    420       C  
ATOM   1130  N   VAL A 170     -13.484 -36.443 -22.688  1.00 43.24           N  
ANISOU 1130  N   VAL A 170     5843   6513   4073    482    558    695       N  
ATOM   1131  CA  VAL A 170     -12.155 -36.580 -22.146  1.00 42.41           C  
ANISOU 1131  CA  VAL A 170     5865   6417   3833    490    418    637       C  
ATOM   1132  C   VAL A 170     -11.833 -38.043 -22.190  1.00 42.08           C  
ANISOU 1132  C   VAL A 170     5799   6375   3814    427    410    797       C  
ATOM   1133  O   VAL A 170     -12.650 -38.851 -21.759  1.00 46.28           O  
ANISOU 1133  O   VAL A 170     6306   6953   4328    439    559    950       O  
ATOM   1134  CB  VAL A 170     -12.105 -36.023 -20.709  1.00 42.93           C  
ANISOU 1134  CB  VAL A 170     6090   6587   3634    629    454    553       C  
ATOM   1135  CG1 VAL A 170     -10.813 -36.423 -19.981  1.00 36.61           C  
ANISOU 1135  CG1 VAL A 170     5413   5831   2666    649    293    527       C  
ATOM   1136  CG2 VAL A 170     -12.259 -34.518 -20.759  1.00 38.71           C  
ANISOU 1136  CG2 VAL A 170     5586   6005   3115    685    437    357       C  
ATOM   1137  N   LEU A 171     -10.658 -38.374 -22.718  1.00 39.19           N  
ANISOU 1137  N   LEU A 171     5432   5946   3513    364    251    768       N  
ATOM   1138  CA  LEU A 171     -10.204 -39.762 -22.789  1.00 39.98           C  
ANISOU 1138  CA  LEU A 171     5516   6018   3656    319    230    906       C  
ATOM   1139  C   LEU A 171      -9.100 -40.061 -21.778  1.00 42.91           C  
ANISOU 1139  C   LEU A 171     6002   6446   3855    393    120    915       C  
ATOM   1140  O   LEU A 171      -8.212 -39.240 -21.533  1.00 47.13           O  
ANISOU 1140  O   LEU A 171     6587   6999   4319    424    -22    769       O  
ATOM   1141  CB  LEU A 171      -9.712 -40.080 -24.184  1.00 36.53           C  
ANISOU 1141  CB  LEU A 171     4981   5469   3429    211    148    878       C  
ATOM   1142  CG  LEU A 171      -9.138 -41.466 -24.436  1.00 36.95           C  
ANISOU 1142  CG  LEU A 171     5014   5457   3568    168    117    983       C  
ATOM   1143  CD1 LEU A 171      -9.457 -41.904 -25.848  1.00 48.30           C  
ANISOU 1143  CD1 LEU A 171     6348   6797   5206     64    126    972       C  
ATOM   1144  CD2 LEU A 171      -7.636 -41.482 -24.207  1.00 40.24           C  
ANISOU 1144  CD2 LEU A 171     5473   5870   3947    202    -34    932       C  
ATOM   1145  N   LYS A 172      -9.144 -41.270 -21.233  1.00 43.20           N  
ANISOU 1145  N   LYS A 172     6070   6498   3845    416    175   1094       N  
ATOM   1146  CA  LYS A 172      -8.256 -41.682 -20.163  1.00 45.28           C  
ANISOU 1146  CA  LYS A 172     6451   6836   3918    513     77   1150       C  
ATOM   1147  C   LYS A 172      -7.798 -43.077 -20.419  1.00 46.81           C  
ANISOU 1147  C   LYS A 172     6607   6941   4236    482     61   1316       C  
ATOM   1148  O   LYS A 172      -8.585 -43.915 -20.822  1.00 49.80           O  
ANISOU 1148  O   LYS A 172     6925   7240   4758    419    201   1448       O  
ATOM   1149  CB  LYS A 172      -8.979 -41.585 -18.814  1.00 43.72           C  
ANISOU 1149  CB  LYS A 172     6387   6781   3443    634    207   1232       C  
ATOM   1150  CG  LYS A 172      -8.782 -40.222 -18.182  1.00 46.24           C  
ANISOU 1150  CG  LYS A 172     6808   7201   3558    717    127   1020       C  
ATOM   1151  CD  LYS A 172     -10.063 -39.607 -17.716  1.00 52.66           C  
ANISOU 1151  CD  LYS A 172     7660   8090   4259    778    337   1007       C  
ATOM   1152  CE  LYS A 172      -9.783 -38.406 -16.843  1.00 46.07           C  
ANISOU 1152  CE  LYS A 172     6973   7356   3174    893    255    793       C  
ATOM   1153  NZ  LYS A 172      -9.308 -38.887 -15.510  1.00 60.63           N  
ANISOU 1153  NZ  LYS A 172     9000   9354   4681   1027    204    869       N  
ATOM   1154  N   ILE A 173      -6.509 -43.309 -20.188  1.00 50.13           N  
ANISOU 1154  N   ILE A 173     7055   7366   4628    529   -119   1298       N  
ATOM   1155  CA  ILE A 173      -5.861 -44.600 -20.398  1.00 48.84           C  
ANISOU 1155  CA  ILE A 173     6858   7106   4595    529   -159   1443       C  
ATOM   1156  C   ILE A 173      -5.881 -45.398 -19.107  1.00 50.97           C  
ANISOU 1156  C   ILE A 173     7255   7450   4661    652   -131   1658       C  
ATOM   1157  O   ILE A 173      -5.835 -44.824 -18.012  1.00 47.96           O  
ANISOU 1157  O   ILE A 173     6999   7229   3995    759   -175   1641       O  
ATOM   1158  CB  ILE A 173      -4.415 -44.357 -20.826  1.00 47.49           C  
ANISOU 1158  CB  ILE A 173     6622   6907   4515    532   -368   1315       C  
ATOM   1159  CG1 ILE A 173      -4.403 -43.671 -22.186  1.00 52.12           C  
ANISOU 1159  CG1 ILE A 173     7089   7409   5303    412   -360   1144       C  
ATOM   1160  CG2 ILE A 173      -3.623 -45.637 -20.903  1.00 48.04           C  
ANISOU 1160  CG2 ILE A 173     6660   6886   4709    571   -422   1457       C  
ATOM   1161  CD1 ILE A 173      -3.059 -43.090 -22.537  1.00 54.54           C  
ANISOU 1161  CD1 ILE A 173     7321   7711   5692    408   -535   1002       C  
ATOM   1162  N   CYS A 174      -5.946 -46.721 -19.244  1.00 55.34           N  
ANISOU 1162  N   CYS A 174     7788   7881   5357    642    -57   1859       N  
ATOM   1163  CA  CYS A 174      -5.836 -47.642 -18.112  1.00 61.45           C  
ANISOU 1163  CA  CYS A 174     8681   8692   5974    764    -30   2113       C  
ATOM   1164  C   CYS A 174      -5.226 -48.975 -18.560  1.00 63.41           C  
ANISOU 1164  C   CYS A 174     8875   8753   6466    760    -60   2258       C  
ATOM   1165  O   CYS A 174      -4.952 -49.141 -19.725  1.00 64.56           O  
ANISOU 1165  O   CYS A 174     8898   8756   6875    663    -87   2139       O  
ATOM   1166  CB  CYS A 174      -7.213 -47.849 -17.497  1.00 62.48           C  
ANISOU 1166  CB  CYS A 174     8877   8865   5999    763    223   2285       C  
ATOM   1167  SG  CYS A 174      -8.376 -48.612 -18.599  1.00 57.89           S  
ANISOU 1167  SG  CYS A 174     8143   8069   5784    581    435   2353       S  
ATOM   1168  N   ASP A 175      -4.981 -49.903 -17.637  1.00 72.60           N  
ANISOU 1168  N   ASP A 175    10138   9915   7530    880    -54   2514       N  
ATOM   1169  CA  ASP A 175      -4.504 -51.263 -17.991  1.00 77.13           C  
ANISOU 1169  CA  ASP A 175    10670  10275   8359    892    -55   2681       C  
ATOM   1170  C   ASP A 175      -3.097 -51.307 -18.617  1.00 79.81           C  
ANISOU 1170  C   ASP A 175    10913  10557   8854    929   -275   2540       C  
ATOM   1171  O   ASP A 175      -2.787 -52.187 -19.426  1.00 81.38           O  
ANISOU 1171  O   ASP A 175    11028  10546   9346    893   -254   2558       O  
ATOM   1172  CB  ASP A 175      -5.513 -51.925 -18.950  1.00 76.60           C  
ANISOU 1172  CB  ASP A 175    10512   9990   8602    725    147   2702       C  
ATOM   1173  CG  ASP A 175      -5.396 -53.442 -18.987  1.00 77.49           C  
ANISOU 1173  CG  ASP A 175    10629   9863   8951    742    214   2935       C  
ATOM   1174  OD1 ASP A 175      -5.079 -54.058 -17.949  1.00 69.17           O  
ANISOU 1174  OD1 ASP A 175     9688   8829   7765    884    209   3195       O  
ATOM   1175  OD2 ASP A 175      -5.629 -54.015 -20.071  1.00 85.20           O  
ANISOU 1175  OD2 ASP A 175    11506  10622  10244    617    269   2854       O  
ATOM   1176  N   PHE A 176      -2.238 -50.377 -18.219  1.00 83.72           N  
ANISOU 1176  N   PHE A 176    11412  11233   9166   1005   -481   2396       N  
ATOM   1177  CA  PHE A 176      -0.927 -50.190 -18.877  1.00 85.23           C  
ANISOU 1177  CA  PHE A 176    11467  11391   9526   1019   -676   2232       C  
ATOM   1178  C   PHE A 176       0.247 -50.826 -18.107  1.00 90.29           C  
ANISOU 1178  C   PHE A 176    12119  12063  10124   1199   -874   2382       C  
ATOM   1179  O   PHE A 176       0.066 -51.358 -17.003  1.00 95.23           O  
ANISOU 1179  O   PHE A 176    12887  12754  10542   1326   -876   2620       O  
ATOM   1180  CB  PHE A 176      -0.658 -48.689 -19.151  1.00 82.82           C  
ANISOU 1180  CB  PHE A 176    11103  11225   9139    952   -788   1947       C  
ATOM   1181  CG  PHE A 176      -0.829 -47.800 -17.950  1.00 82.85           C  
ANISOU 1181  CG  PHE A 176    11239  11452   8789   1027   -879   1917       C  
ATOM   1182  CD1 PHE A 176       0.174 -47.676 -17.013  1.00 80.14           C  
ANISOU 1182  CD1 PHE A 176    10932  11247   8270   1167  -1123   1931       C  
ATOM   1183  CD2 PHE A 176      -1.999 -47.083 -17.768  1.00 82.02           C  
ANISOU 1183  CD2 PHE A 176    11218  11419   8526    967   -727   1860       C  
ATOM   1184  CE1 PHE A 176       0.013 -46.869 -15.920  1.00 85.17           C  
ANISOU 1184  CE1 PHE A 176    11713  12092   8558   1242  -1218   1872       C  
ATOM   1185  CE2 PHE A 176      -2.164 -46.279 -16.671  1.00 84.45           C  
ANISOU 1185  CE2 PHE A 176    11664  11925   8498   1051   -794   1810       C  
ATOM   1186  CZ  PHE A 176      -1.157 -46.172 -15.745  1.00 85.98           C  
ANISOU 1186  CZ  PHE A 176    11918  12257   8495   1187  -1042   1806       C  
ATOM   1187  N   GLY A 177       1.437 -50.775 -18.711  1.00 91.52           N  
ANISOU 1187  N   GLY A 177    12118  12176  10481   1219  -1030   2257       N  
ATOM   1188  CA  GLY A 177       2.665 -51.309 -18.117  1.00 95.52           C  
ANISOU 1188  CA  GLY A 177    12581  12712  11001   1394  -1247   2372       C  
ATOM   1189  C   GLY A 177       2.597 -52.810 -17.947  1.00 99.56           C  
ANISOU 1189  C   GLY A 177    13145  13041  11644   1496  -1154   2660       C  
ATOM   1190  O   GLY A 177       3.173 -53.357 -17.010  1.00104.08           O  
ANISOU 1190  O   GLY A 177    13773  13667  12105   1675  -1297   2866       O  
ATOM   1191  N   THR A 178       1.904 -53.474 -18.874  1.00100.56           N  
ANISOU 1191  N   THR A 178    13253  12939  12015   1384   -926   2670       N  
ATOM   1192  CA  THR A 178       1.502 -54.875 -18.711  1.00102.22           C  
ANISOU 1192  CA  THR A 178    13540  12933  12365   1438   -784   2943       C  
ATOM   1193  C   THR A 178       2.270 -55.798 -19.660  1.00103.80           C  
ANISOU 1193  C   THR A 178    13609  12882  12947   1472   -776   2913       C  
ATOM   1194  O   THR A 178       3.200 -56.495 -19.245  1.00106.61           O  
ANISOU 1194  O   THR A 178    13937  13186  13385   1651   -899   3068       O  
ATOM   1195  CB  THR A 178      -0.033 -55.037 -18.916  1.00101.72           C  
ANISOU 1195  CB  THR A 178    13567  12778  12303   1278   -522   2991       C  
ATOM   1196  OG1 THR A 178      -0.456 -56.315 -18.424  1.00101.55           O  
ANISOU 1196  OG1 THR A 178    13642  12571  12371   1339   -394   3305       O  
ATOM   1197  CG2 THR A 178      -0.431 -54.865 -20.396  1.00 97.36           C  
ANISOU 1197  CG2 THR A 178    12900  12082  12010   1091   -407   2733       C  
ATOM   1198  N   GLY A 191      -7.308 -60.727 -27.282  1.00 76.14           N  
ANISOU 1198  N   GLY A 191     9990   7425  11515   -166    532   2137       N  
ATOM   1199  CA  GLY A 191      -7.842 -60.132 -28.506  1.00 71.15           C  
ANISOU 1199  CA  GLY A 191     9295   6872  10868   -306    469   1811       C  
ATOM   1200  C   GLY A 191      -7.156 -58.830 -28.825  1.00 66.01           C  
ANISOU 1200  C   GLY A 191     8640   6536   9906   -217    376   1654       C  
ATOM   1201  O   GLY A 191      -7.789 -57.855 -29.166  1.00 65.82           O  
ANISOU 1201  O   GLY A 191     8567   6713   9730   -302    350   1540       O  
ATOM   1202  N   SER A 192      -5.839 -58.832 -28.734  1.00 65.14           N  
ANISOU 1202  N   SER A 192     8568   6452   9731    -44    327   1653       N  
ATOM   1203  CA  SER A 192      -5.051 -57.615 -28.848  1.00 61.13           C  
ANISOU 1203  CA  SER A 192     8042   6226   8957     46    248   1551       C  
ATOM   1204  C   SER A 192      -4.342 -57.458 -30.221  1.00 57.88           C  
ANISOU 1204  C   SER A 192     7614   5803   8572     66    203   1254       C  
ATOM   1205  O   SER A 192      -3.872 -56.359 -30.562  1.00 54.15           O  
ANISOU 1205  O   SER A 192     7112   5556   7906     97    156   1141       O  
ATOM   1206  CB  SER A 192      -4.038 -57.609 -27.705  1.00 61.85           C  
ANISOU 1206  CB  SER A 192     8160   6393   8947    229    214   1770       C  
ATOM   1207  OG  SER A 192      -2.989 -56.701 -27.943  1.00 70.48           O  
ANISOU 1207  OG  SER A 192     9215   7682   9882    325    124   1647       O  
ATOM   1208  N   ALA A 193      -4.309 -58.539 -31.002  1.00 55.27           N  
ANISOU 1208  N   ALA A 193     7310   5207   8482     46    230   1128       N  
ATOM   1209  CA  ALA A 193      -3.462 -58.645 -32.188  1.00 54.63           C  
ANISOU 1209  CA  ALA A 193     7238   5084   8436    113    220    872       C  
ATOM   1210  C   ALA A 193      -3.683 -57.560 -33.239  1.00 51.94           C  
ANISOU 1210  C   ALA A 193     6883   4960   7892     43    188    640       C  
ATOM   1211  O   ALA A 193      -2.740 -57.169 -33.924  1.00 53.88           O  
ANISOU 1211  O   ALA A 193     7120   5292   8059    136    195    503       O  
ATOM   1212  CB  ALA A 193      -3.622 -60.009 -32.818  1.00 55.96           C  
ANISOU 1212  CB  ALA A 193     7457   4912   8892     87    257    754       C  
ATOM   1213  N   ALA A 194      -4.908 -57.068 -33.364  1.00 49.34           N  
ANISOU 1213  N   ALA A 194     6541   4718   7486   -112    161    614       N  
ATOM   1214  CA  ALA A 194      -5.207 -56.043 -34.351  1.00 47.88           C  
ANISOU 1214  CA  ALA A 194     6350   4735   7109   -170    120    422       C  
ATOM   1215  C   ALA A 194      -4.501 -54.721 -34.087  1.00 45.04           C  
ANISOU 1215  C   ALA A 194     5954   4638   6520    -90    111    475       C  
ATOM   1216  O   ALA A 194      -4.402 -53.906 -34.998  1.00 49.32           O  
ANISOU 1216  O   ALA A 194     6500   5324   6914    -99     99    327       O  
ATOM   1217  CB  ALA A 194      -6.705 -55.813 -34.444  1.00 48.31           C  
ANISOU 1217  CB  ALA A 194     6373   4823   7160   -340     80    409       C  
ATOM   1218  N   TRP A 195      -4.030 -54.494 -32.863  1.00 43.20           N  
ANISOU 1218  N   TRP A 195     5692   4466   6254    -14    112    684       N  
ATOM   1219  CA  TRP A 195      -3.313 -53.256 -32.513  1.00 43.88           C  
ANISOU 1219  CA  TRP A 195     5737   4780   6155     54     82    721       C  
ATOM   1220  C   TRP A 195      -1.848 -53.473 -32.103  1.00 44.86           C  
ANISOU 1220  C   TRP A 195     5824   4889   6332    208     73    782       C  
ATOM   1221  O   TRP A 195      -1.220 -52.563 -31.577  1.00 44.91           O  
ANISOU 1221  O   TRP A 195     5780   5060   6224    259     26    835       O  
ATOM   1222  CB  TRP A 195      -4.029 -52.535 -31.369  1.00 41.27           C  
ANISOU 1222  CB  TRP A 195     5398   4589   5695     15     57    885       C  
ATOM   1223  CG  TRP A 195      -5.440 -52.233 -31.647  1.00 38.52           C  
ANISOU 1223  CG  TRP A 195     5049   4274   5313   -120     69    851       C  
ATOM   1224  CD1 TRP A 195      -5.920 -51.134 -32.277  1.00 41.00           C  
ANISOU 1224  CD1 TRP A 195     5343   4741   5493   -177     45    743       C  
ATOM   1225  CD2 TRP A 195      -6.577 -53.028 -31.301  1.00 39.21           C  
ANISOU 1225  CD2 TRP A 195     5136   4236   5528   -213    106    937       C  
ATOM   1226  NE1 TRP A 195      -7.289 -51.198 -32.373  1.00 44.23           N  
ANISOU 1226  NE1 TRP A 195     5732   5140   5936   -291     51    746       N  
ATOM   1227  CE2 TRP A 195      -7.717 -52.354 -31.773  1.00 39.99           C  
ANISOU 1227  CE2 TRP A 195     5194   4432   5567   -324     93    862       C  
ATOM   1228  CE3 TRP A 195      -6.744 -54.238 -30.628  1.00 48.98           C  
ANISOU 1228  CE3 TRP A 195     6391   5278   6942   -213    155   1089       C  
ATOM   1229  CZ2 TRP A 195      -8.999 -52.850 -31.599  1.00 43.36           C  
ANISOU 1229  CZ2 TRP A 195     5576   4777   6121   -443    124    919       C  
ATOM   1230  CZ3 TRP A 195      -8.031 -54.738 -30.464  1.00 47.07           C  
ANISOU 1230  CZ3 TRP A 195     6117   4939   6829   -342    203   1155       C  
ATOM   1231  CH2 TRP A 195      -9.137 -54.043 -30.941  1.00 45.11           C  
ANISOU 1231  CH2 TRP A 195     5806   4802   6531   -459    186   1064       C  
ATOM   1232  N   MET A 196      -1.304 -54.658 -32.348  1.00 47.51           N  
ANISOU 1232  N   MET A 196     6172   5020   6859    284    109    764       N  
ATOM   1233  CA  MET A 196       0.024 -55.000 -31.869  1.00 53.03           C  
ANISOU 1233  CA  MET A 196     6815   5688   7648    446     93    849       C  
ATOM   1234  C   MET A 196       1.070 -54.775 -32.929  1.00 54.06           C  
ANISOU 1234  C   MET A 196     6885   5846   7809    520    144    674       C  
ATOM   1235  O   MET A 196       0.950 -55.283 -34.049  1.00 57.16           O  
ANISOU 1235  O   MET A 196     7325   6127   8266    505    222    495       O  
ATOM   1236  CB  MET A 196       0.090 -56.464 -31.456  1.00 56.93           C  
ANISOU 1236  CB  MET A 196     7347   5918   8364    518    117    959       C  
ATOM   1237  CG  MET A 196      -0.110 -56.704 -29.970  1.00 63.87           C  
ANISOU 1237  CG  MET A 196     8247   6801   9221    558     64   1239       C  
ATOM   1238  SD  MET A 196       0.626 -58.272 -29.441  1.00 75.44           S  
ANISOU 1238  SD  MET A 196     9727   7980  10959    727     78   1411       S  
ATOM   1239  CE  MET A 196      -0.779 -59.382 -29.610  1.00 80.33           C  
ANISOU 1239  CE  MET A 196    10450   8311  11762    579    171   1438       C  
ATOM   1240  N   ALA A 197       2.111 -54.030 -32.568  1.00 53.57           N  
ANISOU 1240  N   ALA A 197     6716   5935   7705    601    103    721       N  
ATOM   1241  CA  ALA A 197       3.263 -53.837 -33.444  1.00 52.97           C  
ANISOU 1241  CA  ALA A 197     6545   5887   7695    687    175    597       C  
ATOM   1242  C   ALA A 197       3.907 -55.197 -33.800  1.00 53.36           C  
ANISOU 1242  C   ALA A 197     6591   5711   7975    825    251    559       C  
ATOM   1243  O   ALA A 197       4.090 -56.031 -32.912  1.00 57.00           O  
ANISOU 1243  O   ALA A 197     7047   6042   8568    911    194    712       O  
ATOM   1244  CB  ALA A 197       4.265 -52.937 -32.758  1.00 53.01           C  
ANISOU 1244  CB  ALA A 197     6402   6060   7678    744     93    686       C  
ATOM   1245  N   PRO A 198       4.237 -55.431 -35.090  1.00 51.16           N  
ANISOU 1245  N   PRO A 198     6325   5378   7735    858    385    360       N  
ATOM   1246  CA  PRO A 198       4.748 -56.732 -35.514  1.00 54.96           C  
ANISOU 1246  CA  PRO A 198     6825   5623   8435    993    473    284       C  
ATOM   1247  C   PRO A 198       5.993 -57.240 -34.787  1.00 56.03           C  
ANISOU 1247  C   PRO A 198     6815   5693   8783   1184    451    426       C  
ATOM   1248  O   PRO A 198       6.145 -58.438 -34.650  1.00 59.25           O  
ANISOU 1248  O   PRO A 198     7256   5862   9394   1291    474    449       O  
ATOM   1249  CB  PRO A 198       5.040 -56.532 -37.015  1.00 52.33           C  
ANISOU 1249  CB  PRO A 198     6519   5330   8033   1010    632     40       C  
ATOM   1250  CG  PRO A 198       5.111 -55.115 -37.203  1.00 49.65           C  
ANISOU 1250  CG  PRO A 198     6116   5251   7496    928    628     53       C  
ATOM   1251  CD  PRO A 198       4.152 -54.517 -36.238  1.00 50.83           C  
ANISOU 1251  CD  PRO A 198     6298   5488   7525    788    473    196       C  
ATOM   1252  N   GLU A 199       6.862 -56.348 -34.322  1.00 57.04           N  
ANISOU 1252  N   GLU A 199     6775   6016   8883   1226    393    518       N  
ATOM   1253  CA  GLU A 199       8.074 -56.763 -33.603  1.00 59.91           C  
ANISOU 1253  CA  GLU A 199     6967   6344   9452   1411    335    656       C  
ATOM   1254  C   GLU A 199       7.765 -57.294 -32.208  1.00 60.88           C  
ANISOU 1254  C   GLU A 199     7132   6397   9601   1447    165    892       C  
ATOM   1255  O   GLU A 199       8.585 -57.969 -31.606  1.00 66.25           O  
ANISOU 1255  O   GLU A 199     7716   6989  10467   1621    105   1025       O  
ATOM   1256  CB  GLU A 199       9.113 -55.618 -33.527  1.00 59.70           C  
ANISOU 1256  CB  GLU A 199     6722   6549   9414   1429    302    672       C  
ATOM   1257  CG  GLU A 199       8.824 -54.460 -32.534  1.00 59.75           C  
ANISOU 1257  CG  GLU A 199     6700   6767   9237   1308    114    788       C  
ATOM   1258  CD  GLU A 199       7.978 -53.297 -33.100  1.00 61.76           C  
ANISOU 1258  CD  GLU A 199     7044   7165   9256   1112    159    682       C  
ATOM   1259  OE1 GLU A 199       7.482 -53.392 -34.249  1.00 58.47           O  
ANISOU 1259  OE1 GLU A 199     6732   6703   8782   1057    318    532       O  
ATOM   1260  OE2 GLU A 199       7.811 -52.283 -32.369  1.00 53.62           O  
ANISOU 1260  OE2 GLU A 199     5985   6294   8094   1024     24    748       O  
ATOM   1261  N   VAL A 200       6.590 -56.975 -31.685  1.00 60.14           N  
ANISOU 1261  N   VAL A 200     7178   6354   9319   1294     94    959       N  
ATOM   1262  CA  VAL A 200       6.212 -57.424 -30.366  1.00 63.08           C  
ANISOU 1262  CA  VAL A 200     7612   6682   9673   1325    -36   1199       C  
ATOM   1263  C   VAL A 200       5.866 -58.889 -30.454  1.00 67.42           C  
ANISOU 1263  C   VAL A 200     8270   6919  10430   1388     41   1245       C  
ATOM   1264  O   VAL A 200       6.522 -59.715 -29.829  1.00 71.67           O  
ANISOU 1264  O   VAL A 200     8765   7325  11141   1560     -6   1409       O  
ATOM   1265  CB  VAL A 200       5.022 -56.637 -29.821  1.00 60.50           C  
ANISOU 1265  CB  VAL A 200     7396   6502   9089   1148    -94   1252       C  
ATOM   1266  CG1 VAL A 200       4.505 -57.275 -28.569  1.00 63.88           C  
ANISOU 1266  CG1 VAL A 200     7920   6858   9495   1184   -171   1505       C  
ATOM   1267  CG2 VAL A 200       5.434 -55.211 -29.539  1.00 59.07           C  
ANISOU 1267  CG2 VAL A 200     7114   6601   8731   1105   -193   1225       C  
ATOM   1268  N   PHE A 201       4.864 -59.223 -31.263  1.00 71.06           N  
ANISOU 1268  N   PHE A 201     8861   7246  10892   1253    149   1095       N  
ATOM   1269  CA  PHE A 201       4.415 -60.617 -31.356  1.00 75.13           C  
ANISOU 1269  CA  PHE A 201     9486   7427  11632   1279    217   1119       C  
ATOM   1270  C   PHE A 201       5.403 -61.535 -32.064  1.00 80.96           C  
ANISOU 1270  C   PHE A 201    10177   7949  12637   1461    311   1000       C  
ATOM   1271  O   PHE A 201       5.313 -62.754 -31.913  1.00 85.40           O  
ANISOU 1271  O   PHE A 201    10807   8206  13437   1536    347   1065       O  
ATOM   1272  CB  PHE A 201       2.986 -60.757 -31.921  1.00 73.89           C  
ANISOU 1272  CB  PHE A 201     9470   7177  11429   1066    273    990       C  
ATOM   1273  CG  PHE A 201       2.778 -60.174 -33.293  1.00 70.07           C  
ANISOU 1273  CG  PHE A 201     9002   6789  10831    969    342    681       C  
ATOM   1274  CD1 PHE A 201       3.448 -60.669 -34.394  1.00 71.93           C  
ANISOU 1274  CD1 PHE A 201     9239   6903  11190   1069    447    454       C  
ATOM   1275  CD2 PHE A 201       1.846 -59.169 -33.488  1.00 70.23           C  
ANISOU 1275  CD2 PHE A 201     9054   7015  10616    789    309    623       C  
ATOM   1276  CE1 PHE A 201       3.224 -60.143 -35.655  1.00 71.89           C  
ANISOU 1276  CE1 PHE A 201     9276   7003  11036    991    514    185       C  
ATOM   1277  CE2 PHE A 201       1.619 -58.644 -34.752  1.00 68.26           C  
ANISOU 1277  CE2 PHE A 201     8835   6859  10243    712    362    364       C  
ATOM   1278  CZ  PHE A 201       2.304 -59.136 -35.835  1.00 64.74           C  
ANISOU 1278  CZ  PHE A 201     8403   6308   9885    813    463    149       C  
ATOM   1279  N   GLU A 202       6.367 -60.969 -32.796  1.00 84.11           N  
ANISOU 1279  N   GLU A 202    10452   8491  13016   1541    365    841       N  
ATOM   1280  CA  GLU A 202       7.497 -61.776 -33.285  1.00 89.14           C  
ANISOU 1280  CA  GLU A 202    11001   8955  13913   1760    462    767       C  
ATOM   1281  C   GLU A 202       8.508 -62.067 -32.151  1.00 92.61           C  
ANISOU 1281  C   GLU A 202    11291   9393  14504   1964    344   1037       C  
ATOM   1282  O   GLU A 202       9.572 -62.652 -32.381  1.00 94.21           O  
ANISOU 1282  O   GLU A 202    11372   9480  14942   2176    403   1020       O  
ATOM   1283  CB  GLU A 202       8.155 -61.151 -34.538  1.00 88.81           C  
ANISOU 1283  CB  GLU A 202    10876   9056  13811   1784    603    507       C  
ATOM   1284  CG  GLU A 202       9.426 -60.324 -34.325  1.00 92.28           C  
ANISOU 1284  CG  GLU A 202    11072   9731  14259   1896    580    577       C  
ATOM   1285  CD  GLU A 202       9.892 -59.589 -35.584  1.00 90.94           C  
ANISOU 1285  CD  GLU A 202    10836   9717  14000   1880    753    348       C  
ATOM   1286  OE1 GLU A 202       9.040 -59.058 -36.335  1.00 90.34           O  
ANISOU 1286  OE1 GLU A 202    10900   9724  13700   1712    810    194       O  
ATOM   1287  OE2 GLU A 202      11.122 -59.528 -35.807  1.00 94.45           O  
ANISOU 1287  OE2 GLU A 202    11077  10209  14602   2041    835    340       O  
ATOM   1288  N   GLY A 203       8.164 -61.653 -30.929  1.00 94.10           N  
ANISOU 1288  N   GLY A 203    11489   9720  14546   1913    176   1283       N  
ATOM   1289  CA  GLY A 203       8.949 -61.969 -29.737  1.00 96.78           C  
ANISOU 1289  CA  GLY A 203    11726  10069  14979   2101     23   1564       C  
ATOM   1290  C   GLY A 203      10.232 -61.170 -29.625  1.00 98.01           C  
ANISOU 1290  C   GLY A 203    11634  10468  15137   2214    -67   1558       C  
ATOM   1291  O   GLY A 203      10.916 -61.229 -28.605  1.00 99.14           O  
ANISOU 1291  O   GLY A 203    11669  10683  15318   2360   -242   1776       O  
ATOM   1292  N   SER A 204      10.545 -60.402 -30.666  1.00 97.48           N  
ANISOU 1292  N   SER A 204    11474  10533  15030   2143     47   1316       N  
ATOM   1293  CA  SER A 204      11.822 -59.714 -30.759  1.00 97.79           C  
ANISOU 1293  CA  SER A 204    11245  10763  15147   2241      9   1287       C  
ATOM   1294  C   SER A 204      11.883 -58.496 -29.824  1.00 95.86           C  
ANISOU 1294  C   SER A 204    10919  10819  14686   2143   -209   1394       C  
ATOM   1295  O   SER A 204      10.942 -58.217 -29.069  1.00 94.21           O  
ANISOU 1295  O   SER A 204    10874  10675  14248   2022   -320   1497       O  
ATOM   1296  CB  SER A 204      12.100 -59.300 -32.213  1.00 97.29           C  
ANISOU 1296  CB  SER A 204    11124  10736  15106   2194    240   1013       C  
ATOM   1297  OG  SER A 204      11.349 -58.159 -32.578  1.00 94.44           O  
ANISOU 1297  OG  SER A 204    10846  10568  14468   1964    256    906       O  
ATOM   1298  N   ASN A 205      13.020 -57.804 -29.866  1.00 95.60           N  
ANISOU 1298  N   ASN A 205    10620  10955  14747   2202   -266   1365       N  
ATOM   1299  CA  ASN A 205      13.221 -56.592 -29.094  1.00 92.66           C  
ANISOU 1299  CA  ASN A 205    10144  10851  14211   2106   -477   1415       C  
ATOM   1300  C   ASN A 205      12.240 -55.534 -29.549  1.00 88.09           C  
ANISOU 1300  C   ASN A 205     9708  10395  13367   1856   -404   1277       C  
ATOM   1301  O   ASN A 205      11.991 -55.385 -30.753  1.00 87.33           O  
ANISOU 1301  O   ASN A 205     9653  10256  13273   1776   -181   1101       O  
ATOM   1302  CB  ASN A 205      14.655 -56.081 -29.262  1.00 94.85           C  
ANISOU 1302  CB  ASN A 205    10076  11253  14711   2196   -520   1376       C  
ATOM   1303  CG  ASN A 205      15.659 -56.934 -28.528  1.00101.41           C  
ANISOU 1303  CG  ASN A 205    10726  12018  15785   2450   -678   1548       C  
ATOM   1304  OD1 ASN A 205      15.658 -56.983 -27.299  1.00107.04           O  
ANISOU 1304  OD1 ASN A 205    11463  12807  16399   2508   -948   1728       O  
ATOM   1305  ND2 ASN A 205      16.524 -57.615 -29.274  1.00109.91           N  
ANISOU 1305  ND2 ASN A 205    11626  12960  17173   2621   -509   1497       N  
ATOM   1306  N   TYR A 206      11.677 -54.812 -28.584  1.00 83.88           N  
ANISOU 1306  N   TYR A 206     9261  10015  12595   1751   -592   1357       N  
ATOM   1307  CA  TYR A 206      10.781 -53.709 -28.883  1.00 77.70           C  
ANISOU 1307  CA  TYR A 206     8594   9356  11572   1531   -549   1242       C  
ATOM   1308  C   TYR A 206      11.049 -52.529 -27.944  1.00 74.75           C  
ANISOU 1308  C   TYR A 206     8135   9207  11061   1465   -779   1270       C  
ATOM   1309  O   TYR A 206      11.936 -52.608 -27.095  1.00 75.51           O  
ANISOU 1309  O   TYR A 206     8080   9371  11241   1588   -986   1369       O  
ATOM   1310  CB  TYR A 206       9.336 -54.190 -28.805  1.00 77.13           C  
ANISOU 1310  CB  TYR A 206     8803   9182  11323   1443   -480   1276       C  
ATOM   1311  CG  TYR A 206       8.897 -54.692 -27.452  1.00 76.52           C  
ANISOU 1311  CG  TYR A 206     8846   9097  11131   1506   -644   1493       C  
ATOM   1312  CD1 TYR A 206       8.362 -53.823 -26.506  1.00 74.23           C  
ANISOU 1312  CD1 TYR A 206     8635   8991  10578   1420   -792   1548       C  
ATOM   1313  CD2 TYR A 206       8.979 -56.037 -27.133  1.00 81.22           C  
ANISOU 1313  CD2 TYR A 206     9494   9493  11873   1658   -633   1645       C  
ATOM   1314  CE1 TYR A 206       7.930 -54.274 -25.274  1.00 76.75           C  
ANISOU 1314  CE1 TYR A 206     9087   9323  10752   1489   -914   1757       C  
ATOM   1315  CE2 TYR A 206       8.550 -56.505 -25.899  1.00 86.34           C  
ANISOU 1315  CE2 TYR A 206    10269  10134  12401   1721   -759   1879       C  
ATOM   1316  CZ  TYR A 206       8.026 -55.617 -24.970  1.00 83.97           C  
ANISOU 1316  CZ  TYR A 206    10051  10047  11806   1638   -894   1937       C  
ATOM   1317  OH  TYR A 206       7.605 -56.082 -23.739  1.00 82.92           O  
ANISOU 1317  OH  TYR A 206    10060   9927  11518   1716   -996   2180       O  
ATOM   1318  N   SER A 207      10.289 -51.441 -28.112  1.00 70.68           N  
ANISOU 1318  N   SER A 207     7713   8799  10343   1280   -756   1173       N  
ATOM   1319  CA  SER A 207      10.494 -50.202 -27.352  1.00 68.48           C  
ANISOU 1319  CA  SER A 207     7366   8709   9943   1198   -954   1148       C  
ATOM   1320  C   SER A 207       9.201 -49.372 -27.239  1.00 64.38           C  
ANISOU 1320  C   SER A 207     7058   8257   9146   1031   -927   1095       C  
ATOM   1321  O   SER A 207       8.125 -49.851 -27.574  1.00 63.28           O  
ANISOU 1321  O   SER A 207     7108   8030   8904    988   -787   1109       O  
ATOM   1322  CB  SER A 207      11.585 -49.376 -28.044  1.00 69.62           C  
ANISOU 1322  CB  SER A 207     7245   8913  10297   1155   -921   1031       C  
ATOM   1323  OG  SER A 207      11.142 -48.888 -29.312  1.00 69.30           O  
ANISOU 1323  OG  SER A 207     7250   8837  10245   1028   -673    909       O  
ATOM   1324  N   GLU A 208       9.321 -48.130 -26.765  1.00 61.12           N  
ANISOU 1324  N   GLU A 208     6598   7988   8638    939  -1066   1026       N  
ATOM   1325  CA  GLU A 208       8.245 -47.135 -26.843  1.00 57.53           C  
ANISOU 1325  CA  GLU A 208     6297   7588   7971    783  -1017    944       C  
ATOM   1326  C   GLU A 208       7.504 -47.158 -28.167  1.00 52.84           C  
ANISOU 1326  C   GLU A 208     5784   6905   7387    690   -759    874       C  
ATOM   1327  O   GLU A 208       6.324 -46.828 -28.215  1.00 51.04           O  
ANISOU 1327  O   GLU A 208     5727   6688   6979    601   -698    856       O  
ATOM   1328  CB  GLU A 208       8.791 -45.699 -26.696  1.00 59.24           C  
ANISOU 1328  CB  GLU A 208     6383   7912   8214    682  -1134    825       C  
ATOM   1329  CG  GLU A 208       9.394 -45.349 -25.347  1.00 69.59           C  
ANISOU 1329  CG  GLU A 208     7633   9342   9464    738  -1436    837       C  
ATOM   1330  CD  GLU A 208      10.851 -45.761 -25.234  1.00 78.20           C  
ANISOU 1330  CD  GLU A 208     8457  10440  10816    844  -1570    867       C  
ATOM   1331  OE1 GLU A 208      11.382 -46.304 -26.230  1.00 76.81           O  
ANISOU 1331  OE1 GLU A 208     8143  10168  10873    878  -1393    879       O  
ATOM   1332  OE2 GLU A 208      11.458 -45.550 -24.155  1.00 81.57           O  
ANISOU 1332  OE2 GLU A 208     8810  10974  11209    904  -1854    873       O  
ATOM   1333  N   LYS A 209       8.202 -47.478 -29.254  1.00 50.16           N  
ANISOU 1333  N   LYS A 209     5317   6492   7251    716   -609    827       N  
ATOM   1334  CA  LYS A 209       7.608 -47.335 -30.573  1.00 47.47           C  
ANISOU 1334  CA  LYS A 209     5051   6098   6886    632   -383    739       C  
ATOM   1335  C   LYS A 209       6.444 -48.303 -30.848  1.00 45.61           C  
ANISOU 1335  C   LYS A 209     5023   5761   6546    635   -287    759       C  
ATOM   1336  O   LYS A 209       5.658 -48.048 -31.753  1.00 41.02           O  
ANISOU 1336  O   LYS A 209     4543   5166   5878    547   -156    682       O  
ATOM   1337  CB  LYS A 209       8.665 -47.453 -31.664  1.00 48.01           C  
ANISOU 1337  CB  LYS A 209     4946   6129   7169    675   -226    682       C  
ATOM   1338  CG  LYS A 209       9.764 -46.384 -31.610  1.00 49.95           C  
ANISOU 1338  CG  LYS A 209     4955   6460   7563    634   -279    657       C  
ATOM   1339  CD  LYS A 209       9.223 -44.971 -31.614  1.00 50.17           C  
ANISOU 1339  CD  LYS A 209     5035   6562   7466    474   -304    607       C  
ATOM   1340  CE  LYS A 209      10.303 -43.955 -31.982  1.00 50.79           C  
ANISOU 1340  CE  LYS A 209     4874   6676   7749    408   -273    573       C  
ATOM   1341  NZ  LYS A 209      10.748 -44.148 -33.364  1.00 55.18           N  
ANISOU 1341  NZ  LYS A 209     5358   7191   8417    428      2    557       N  
ATOM   1342  N   CYS A 210       6.308 -49.380 -30.063  1.00 43.36           N  
ANISOU 1342  N   CYS A 210     4798   5402   6276    732   -360    869       N  
ATOM   1343  CA  CYS A 210       5.196 -50.302 -30.241  1.00 44.20           C  
ANISOU 1343  CA  CYS A 210     5081   5387   6327    715   -275    896       C  
ATOM   1344  C   CYS A 210       3.885 -49.611 -29.921  1.00 43.81           C  
ANISOU 1344  C   CYS A 210     5171   5414   6062    587   -292    899       C  
ATOM   1345  O   CYS A 210       2.883 -49.840 -30.600  1.00 43.60           O  
ANISOU 1345  O   CYS A 210     5250   5326   5991    508   -188    846       O  
ATOM   1346  CB  CYS A 210       5.354 -51.584 -29.415  1.00 47.41           C  
ANISOU 1346  CB  CYS A 210     5518   5674   6821    845   -337   1047       C  
ATOM   1347  SG  CYS A 210       5.378 -51.365 -27.627  1.00 53.39           S  
ANISOU 1347  SG  CYS A 210     6303   6556   7427    906   -559   1234       S  
ATOM   1348  N   ASP A 211       3.898 -48.743 -28.913  1.00 42.65           N  
ANISOU 1348  N   ASP A 211     5015   5403   5787    571   -428    944       N  
ATOM   1349  CA  ASP A 211       2.732 -47.909 -28.609  1.00 41.09           C  
ANISOU 1349  CA  ASP A 211     4930   5290   5391    465   -431    930       C  
ATOM   1350  C   ASP A 211       2.330 -46.984 -29.753  1.00 41.36           C  
ANISOU 1350  C   ASP A 211     4961   5353   5403    351   -328    796       C  
ATOM   1351  O   ASP A 211       1.165 -46.684 -29.911  1.00 43.38           O  
ANISOU 1351  O   ASP A 211     5314   5623   5545    273   -280    782       O  
ATOM   1352  CB  ASP A 211       3.001 -47.072 -27.360  1.00 41.85           C  
ANISOU 1352  CB  ASP A 211     5017   5527   5356    488   -599    964       C  
ATOM   1353  CG  ASP A 211       3.123 -47.928 -26.102  1.00 42.40           C  
ANISOU 1353  CG  ASP A 211     5142   5602   5365    607   -708   1127       C  
ATOM   1354  OD1 ASP A 211       2.600 -49.071 -26.083  1.00 37.55           O  
ANISOU 1354  OD1 ASP A 211     4608   4874   4787    642   -626   1239       O  
ATOM   1355  OD2 ASP A 211       3.734 -47.447 -25.130  1.00 46.74           O  
ANISOU 1355  OD2 ASP A 211     5661   6267   5831    666   -881   1145       O  
ATOM   1356  N   VAL A 212       3.298 -46.531 -30.545  1.00 43.46           N  
ANISOU 1356  N   VAL A 212     5105   5627   5781    351   -289    716       N  
ATOM   1357  CA  VAL A 212       3.040 -45.604 -31.661  1.00 41.51           C  
ANISOU 1357  CA  VAL A 212     4858   5410   5503    259   -183    619       C  
ATOM   1358  C   VAL A 212       2.315 -46.332 -32.795  1.00 41.06           C  
ANISOU 1358  C   VAL A 212     4895   5276   5430    239    -46    569       C  
ATOM   1359  O   VAL A 212       1.408 -45.809 -33.411  1.00 38.79           O  
ANISOU 1359  O   VAL A 212     4686   5018   5035    162      3    525       O  
ATOM   1360  CB  VAL A 212       4.372 -45.002 -32.174  1.00 41.06           C  
ANISOU 1360  CB  VAL A 212     4631   5377   5593    269   -152    576       C  
ATOM   1361  CG1 VAL A 212       4.194 -44.284 -33.487  1.00 43.09           C  
ANISOU 1361  CG1 VAL A 212     4901   5647   5824    199      2    511       C  
ATOM   1362  CG2 VAL A 212       4.943 -44.079 -31.132  1.00 39.77           C  
ANISOU 1362  CG2 VAL A 212     4374   5290   5447    253   -314    588       C  
ATOM   1363  N   PHE A 213       2.729 -47.556 -33.055  1.00 41.85           N  
ANISOU 1363  N   PHE A 213     4986   5269   5644    319      1    568       N  
ATOM   1364  CA  PHE A 213       2.038 -48.379 -33.995  1.00 42.72           C  
ANISOU 1364  CA  PHE A 213     5199   5286   5747    303     99    496       C  
ATOM   1365  C   PHE A 213       0.590 -48.522 -33.587  1.00 44.44           C  
ANISOU 1365  C   PHE A 213     5531   5491   5862    222     53    530       C  
ATOM   1366  O   PHE A 213      -0.307 -48.297 -34.393  1.00 45.49           O  
ANISOU 1366  O   PHE A 213     5735   5640   5910    146     92    454       O  
ATOM   1367  CB  PHE A 213       2.687 -49.743 -34.047  1.00 43.95           C  
ANISOU 1367  CB  PHE A 213     5333   5296   6068    413    135    497       C  
ATOM   1368  CG  PHE A 213       2.119 -50.626 -35.092  1.00 43.97           C  
ANISOU 1368  CG  PHE A 213     5441   5179   6085    402    231    379       C  
ATOM   1369  CD1 PHE A 213       0.911 -51.262 -34.894  1.00 48.00           C  
ANISOU 1369  CD1 PHE A 213     6061   5600   6576    333    195    388       C  
ATOM   1370  CD2 PHE A 213       2.789 -50.831 -36.270  1.00 42.62           C  
ANISOU 1370  CD2 PHE A 213     5257   4984   5952    461    360    251       C  
ATOM   1371  CE1 PHE A 213       0.392 -52.091 -35.854  1.00 45.01           C  
ANISOU 1371  CE1 PHE A 213     5774   5099   6231    311    253    251       C  
ATOM   1372  CE2 PHE A 213       2.262 -51.647 -37.229  1.00 50.09           C  
ANISOU 1372  CE2 PHE A 213     6320   5823   6889    456    429    109       C  
ATOM   1373  CZ  PHE A 213       1.053 -52.273 -37.017  1.00 43.13           C  
ANISOU 1373  CZ  PHE A 213     5545   4843   6001    374    359    100       C  
ATOM   1374  N   SER A 214       0.365 -48.906 -32.333  1.00 44.19           N  
ANISOU 1374  N   SER A 214     5513   5440   5837    246    -29    655       N  
ATOM   1375  CA  SER A 214      -0.996 -49.084 -31.821  1.00 43.61           C  
ANISOU 1375  CA  SER A 214     5526   5355   5689    174    -45    716       C  
ATOM   1376  C   SER A 214      -1.822 -47.833 -32.055  1.00 42.51           C  
ANISOU 1376  C   SER A 214     5404   5343   5403     84    -49    671       C  
ATOM   1377  O   SER A 214      -2.992 -47.875 -32.458  1.00 42.60           O  
ANISOU 1377  O   SER A 214     5464   5345   5378      6    -23    643       O  
ATOM   1378  CB  SER A 214      -0.986 -49.384 -30.326  1.00 40.93           C  
ANISOU 1378  CB  SER A 214     5200   5025   5326    229   -117    883       C  
ATOM   1379  OG  SER A 214      -0.329 -50.602 -30.080  1.00 37.01           O  
ANISOU 1379  OG  SER A 214     4695   4393   4976    323   -117    955       O  
ATOM   1380  N   TRP A 215      -1.191 -46.711 -31.798  1.00 41.60           N  
ANISOU 1380  N   TRP A 215     5238   5338   5229     98    -89    663       N  
ATOM   1381  CA  TRP A 215      -1.882 -45.459 -31.858  1.00 40.52           C  
ANISOU 1381  CA  TRP A 215     5119   5302   4974     32    -97    635       C  
ATOM   1382  C   TRP A 215      -2.278 -45.139 -33.291  1.00 38.46           C  
ANISOU 1382  C   TRP A 215     4877   5044   4694    -21    -26    540       C  
ATOM   1383  O   TRP A 215      -3.379 -44.645 -33.537  1.00 39.78           O  
ANISOU 1383  O   TRP A 215     5083   5252   4781    -78    -25    530       O  
ATOM   1384  CB  TRP A 215      -1.004 -44.387 -31.259  1.00 36.65           C  
ANISOU 1384  CB  TRP A 215     4568   4892   4464     56   -164    633       C  
ATOM   1385  CG  TRP A 215      -1.642 -43.094 -31.256  1.00 34.50           C  
ANISOU 1385  CG  TRP A 215     4319   4692   4097      1   -170    602       C  
ATOM   1386  CD1 TRP A 215      -2.339 -42.537 -30.246  1.00 33.49           C  
ANISOU 1386  CD1 TRP A 215     4238   4622   3865      1   -218    631       C  
ATOM   1387  CD2 TRP A 215      -1.636 -42.149 -32.323  1.00 33.28           C  
ANISOU 1387  CD2 TRP A 215     4147   4552   3943    -46   -115    542       C  
ATOM   1388  NE1 TRP A 215      -2.770 -41.284 -30.605  1.00 39.69           N  
ANISOU 1388  NE1 TRP A 215     5029   5442   4607    -43   -202    579       N  
ATOM   1389  CE2 TRP A 215      -2.350 -41.024 -31.882  1.00 34.38           C  
ANISOU 1389  CE2 TRP A 215     4319   4741   4002    -74   -143    538       C  
ATOM   1390  CE3 TRP A 215      -1.101 -42.151 -33.611  1.00 29.51           C  
ANISOU 1390  CE3 TRP A 215     3641   4052   3518    -55    -30    501       C  
ATOM   1391  CZ2 TRP A 215      -2.545 -39.915 -32.674  1.00 29.02           C  
ANISOU 1391  CZ2 TRP A 215     3641   4072   3315   -113   -102    510       C  
ATOM   1392  CZ3 TRP A 215      -1.297 -41.050 -34.399  1.00 30.20           C  
ANISOU 1392  CZ3 TRP A 215     3738   4170   3568    -95     19    484       C  
ATOM   1393  CH2 TRP A 215      -2.004 -39.944 -33.928  1.00 31.06           C  
ANISOU 1393  CH2 TRP A 215     3874   4310   3619   -125    -24    496       C  
ATOM   1394  N   GLY A 216      -1.380 -45.434 -34.223  1.00 39.18           N  
ANISOU 1394  N   GLY A 216     4939   5099   4849     11     34    477       N  
ATOM   1395  CA  GLY A 216      -1.665 -45.321 -35.657  1.00 38.53           C  
ANISOU 1395  CA  GLY A 216     4900   5026   4713    -16    108    386       C  
ATOM   1396  C   GLY A 216      -2.909 -46.097 -36.043  1.00 39.12           C  
ANISOU 1396  C   GLY A 216     5054   5053   4759    -63     90    342       C  
ATOM   1397  O   GLY A 216      -3.736 -45.612 -36.825  1.00 43.98           O  
ANISOU 1397  O   GLY A 216     5712   5724   5273   -110     84    296       O  
ATOM   1398  N   ILE A 217      -3.047 -47.300 -35.491  1.00 38.19           N  
ANISOU 1398  N   ILE A 217     4945   4823   4744    -53     72    363       N  
ATOM   1399  CA  ILE A 217      -4.214 -48.160 -35.755  1.00 37.34           C  
ANISOU 1399  CA  ILE A 217     4886   4633   4667   -118     48    322       C  
ATOM   1400  C   ILE A 217      -5.489 -47.561 -35.158  1.00 37.60           C  
ANISOU 1400  C   ILE A 217     4906   4737   4644   -192      0    396       C  
ATOM   1401  O   ILE A 217      -6.547 -47.601 -35.763  1.00 40.24           O  
ANISOU 1401  O   ILE A 217     5251   5079   4959   -261    -31    339       O  
ATOM   1402  CB  ILE A 217      -4.001 -49.584 -35.194  1.00 36.63           C  
ANISOU 1402  CB  ILE A 217     4803   4373   4743    -90     57    358       C  
ATOM   1403  CG1 ILE A 217      -2.809 -50.266 -35.873  1.00 40.89           C  
ANISOU 1403  CG1 ILE A 217     5351   4824   5362      0    116    267       C  
ATOM   1404  CG2 ILE A 217      -5.256 -50.461 -35.382  1.00 42.69           C  
ANISOU 1404  CG2 ILE A 217     5601   5027   5592   -185     31    323       C  
ATOM   1405  CD1 ILE A 217      -3.000 -50.581 -37.382  1.00 39.63           C  
ANISOU 1405  CD1 ILE A 217     5263   4637   5158    -15    152     71       C  
ATOM   1406  N   ILE A 218      -5.391 -47.015 -33.958  1.00 38.48           N  
ANISOU 1406  N   ILE A 218     4988   4905   4730   -168    -10    515       N  
ATOM   1407  CA  ILE A 218      -6.546 -46.437 -33.309  1.00 35.51           C  
ANISOU 1407  CA  ILE A 218     4596   4598   4298   -214    -26    585       C  
ATOM   1408  C   ILE A 218      -7.046 -45.230 -34.116  1.00 33.29           C  
ANISOU 1408  C   ILE A 218     4309   4423   3915   -240    -42    523       C  
ATOM   1409  O   ILE A 218      -8.249 -45.031 -34.285  1.00 32.05           O  
ANISOU 1409  O   ILE A 218     4130   4299   3748   -291    -61    524       O  
ATOM   1410  CB  ILE A 218      -6.198 -46.013 -31.891  1.00 32.61           C  
ANISOU 1410  CB  ILE A 218     4225   4285   3881   -159    -31    698       C  
ATOM   1411  CG1 ILE A 218      -5.918 -47.255 -31.047  1.00 41.89           C  
ANISOU 1411  CG1 ILE A 218     5415   5359   5141   -125    -18    800       C  
ATOM   1412  CG2 ILE A 218      -7.335 -45.239 -31.301  1.00 29.61           C  
ANISOU 1412  CG2 ILE A 218     3835   3992   3423   -185    -20    747       C  
ATOM   1413  CD1 ILE A 218      -5.343 -46.990 -29.672  1.00 34.32           C  
ANISOU 1413  CD1 ILE A 218     4474   4465   4103    -43    -47    910       C  
ATOM   1414  N   LEU A 219      -6.118 -44.410 -34.580  1.00 35.03           N  
ANISOU 1414  N   LEU A 219     4537   4694   4080   -200    -33    486       N  
ATOM   1415  CA  LEU A 219      -6.461 -43.250 -35.426  1.00 36.27           C  
ANISOU 1415  CA  LEU A 219     4702   4933   4145   -211    -36    454       C  
ATOM   1416  C   LEU A 219      -7.350 -43.681 -36.603  1.00 33.74           C  
ANISOU 1416  C   LEU A 219     4408   4616   3796   -252    -66    380       C  
ATOM   1417  O   LEU A 219      -8.410 -43.126 -36.844  1.00 35.93           O  
ANISOU 1417  O   LEU A 219     4669   4952   4030   -277   -109    390       O  
ATOM   1418  CB  LEU A 219      -5.186 -42.577 -35.966  1.00 34.54           C  
ANISOU 1418  CB  LEU A 219     4484   4733   3907   -173      8    433       C  
ATOM   1419  CG  LEU A 219      -5.450 -41.248 -36.663  1.00 38.90           C  
ANISOU 1419  CG  LEU A 219     5051   5354   4377   -176     20    445       C  
ATOM   1420  CD1 LEU A 219      -6.066 -40.265 -35.654  1.00 36.60           C  
ANISOU 1420  CD1 LEU A 219     4735   5089   4082   -179    -16    501       C  
ATOM   1421  CD2 LEU A 219      -4.170 -40.678 -37.273  1.00 40.28           C  
ANISOU 1421  CD2 LEU A 219     5214   5530   4561   -151     96    446       C  
ATOM   1422  N   TRP A 220      -6.906 -44.700 -37.310  1.00 32.55           N  
ANISOU 1422  N   TRP A 220     4295   4399   3674   -250    -53    295       N  
ATOM   1423  CA  TRP A 220      -7.671 -45.263 -38.385  1.00 35.56           C  
ANISOU 1423  CA  TRP A 220     4714   4774   4023   -289   -106    189       C  
ATOM   1424  C   TRP A 220      -9.051 -45.675 -37.926  1.00 38.12           C  
ANISOU 1424  C   TRP A 220     4980   5073   4432   -367   -179    209       C  
ATOM   1425  O   TRP A 220     -10.045 -45.486 -38.643  1.00 35.81           O  
ANISOU 1425  O   TRP A 220     4674   4835   4096   -406   -263    158       O  
ATOM   1426  CB  TRP A 220      -6.960 -46.504 -38.856  1.00 34.50           C  
ANISOU 1426  CB  TRP A 220     4630   4529   3950   -270    -74     83       C  
ATOM   1427  CG  TRP A 220      -7.619 -47.129 -39.983  1.00 39.56           C  
ANISOU 1427  CG  TRP A 220     5329   5154   4547   -306   -142    -67       C  
ATOM   1428  CD1 TRP A 220      -7.447 -46.821 -41.292  1.00 35.59           C  
ANISOU 1428  CD1 TRP A 220     4913   4736   3872   -266   -145   -171       C  
ATOM   1429  CD2 TRP A 220      -8.568 -48.196 -39.935  1.00 39.92           C  
ANISOU 1429  CD2 TRP A 220     5356   5090   4722   -391   -226   -140       C  
ATOM   1430  NE1 TRP A 220      -8.234 -47.620 -42.062  1.00 40.19           N  
ANISOU 1430  NE1 TRP A 220     5542   5283   4444   -315   -249   -326       N  
ATOM   1431  CE2 TRP A 220      -8.937 -48.477 -41.260  1.00 32.18           C  
ANISOU 1431  CE2 TRP A 220     4453   4137   3637   -403   -306   -318       C  
ATOM   1432  CE3 TRP A 220      -9.150 -48.938 -38.898  1.00 40.04           C  
ANISOU 1432  CE3 TRP A 220     5295   4983   4933   -461   -237    -66       C  
ATOM   1433  CZ2 TRP A 220      -9.849 -49.484 -41.592  1.00 38.12           C  
ANISOU 1433  CZ2 TRP A 220     5198   4786   4501   -495   -421   -453       C  
ATOM   1434  CZ3 TRP A 220     -10.077 -49.938 -39.227  1.00 37.78           C  
ANISOU 1434  CZ3 TRP A 220     4990   4582   4780   -560   -323   -170       C  
ATOM   1435  CH2 TRP A 220     -10.407 -50.200 -40.565  1.00 39.75           C  
ANISOU 1435  CH2 TRP A 220     5307   4849   4947   -582   -426   -375       C  
ATOM   1436  N   GLU A 221      -9.088 -46.288 -36.743  1.00 38.99           N  
ANISOU 1436  N   GLU A 221     5047   5100   4668   -385   -147    292       N  
ATOM   1437  CA  GLU A 221     -10.298 -46.897 -36.217  1.00 39.82           C  
ANISOU 1437  CA  GLU A 221     5081   5151   4897   -466   -175    334       C  
ATOM   1438  C   GLU A 221     -11.366 -45.841 -35.919  1.00 40.76           C  
ANISOU 1438  C   GLU A 221     5124   5391   4971   -479   -196    404       C  
ATOM   1439  O   GLU A 221     -12.548 -46.040 -36.248  1.00 41.05           O  
ANISOU 1439  O   GLU A 221     5083   5434   5078   -549   -258    380       O  
ATOM   1440  CB  GLU A 221      -9.981 -47.740 -34.965  1.00 38.60           C  
ANISOU 1440  CB  GLU A 221     4916   4887   4864   -461   -105    448       C  
ATOM   1441  CG  GLU A 221     -11.177 -48.519 -34.426  1.00 41.31           C  
ANISOU 1441  CG  GLU A 221     5181   5147   5368   -555    -97    517       C  
ATOM   1442  CD  GLU A 221     -10.827 -49.592 -33.388  1.00 49.58           C  
ANISOU 1442  CD  GLU A 221     6242   6052   6545   -548    -20    641       C  
ATOM   1443  OE1 GLU A 221      -9.629 -49.751 -33.037  1.00 50.92           O  
ANISOU 1443  OE1 GLU A 221     6480   6194   6675   -459      7    671       O  
ATOM   1444  OE2 GLU A 221     -11.773 -50.282 -32.921  1.00 54.82           O  
ANISOU 1444  OE2 GLU A 221     6837   6627   7364   -632     15    724       O  
ATOM   1445  N   VAL A 222     -10.963 -44.722 -35.314  1.00 37.76           N  
ANISOU 1445  N   VAL A 222     4755   5097   4495   -409   -150    480       N  
ATOM   1446  CA  VAL A 222     -11.938 -43.699 -34.934  1.00 37.63           C  
ANISOU 1446  CA  VAL A 222     4672   5176   4450   -399   -150    543       C  
ATOM   1447  C   VAL A 222     -12.396 -42.880 -36.158  1.00 39.23           C  
ANISOU 1447  C   VAL A 222     4871   5460   4573   -388   -231    483       C  
ATOM   1448  O   VAL A 222     -13.544 -42.441 -36.238  1.00 41.95           O  
ANISOU 1448  O   VAL A 222     5130   5863   4947   -399   -272    508       O  
ATOM   1449  CB  VAL A 222     -11.439 -42.775 -33.783  1.00 29.70           C  
ANISOU 1449  CB  VAL A 222     3691   4217   3376   -325    -81    623       C  
ATOM   1450  CG1 VAL A 222     -11.088 -43.580 -32.546  1.00 37.92           C  
ANISOU 1450  CG1 VAL A 222     4747   5203   4457   -317    -19    701       C  
ATOM   1451  CG2 VAL A 222     -10.265 -42.008 -34.190  1.00 41.00           C  
ANISOU 1451  CG2 VAL A 222     5191   5666   4722   -274    -87    582       C  
ATOM   1452  N   ILE A 223     -11.501 -42.664 -37.104  1.00 36.12           N  
ANISOU 1452  N   ILE A 223     4566   5079   4081   -356   -247    418       N  
ATOM   1453  CA  ILE A 223     -11.889 -42.017 -38.357  1.00 38.12           C  
ANISOU 1453  CA  ILE A 223     4843   5415   4228   -335   -324    378       C  
ATOM   1454  C   ILE A 223     -12.876 -42.848 -39.185  1.00 39.27           C  
ANISOU 1454  C   ILE A 223     4951   5566   4403   -399   -447    286       C  
ATOM   1455  O   ILE A 223     -13.816 -42.277 -39.776  1.00 36.84           O  
ANISOU 1455  O   ILE A 223     4596   5346   4056   -389   -547    291       O  
ATOM   1456  CB  ILE A 223     -10.663 -41.681 -39.213  1.00 36.64           C  
ANISOU 1456  CB  ILE A 223     4767   5242   3914   -283   -280    345       C  
ATOM   1457  CG1 ILE A 223      -9.845 -40.589 -38.503  1.00 36.75           C  
ANISOU 1457  CG1 ILE A 223     4785   5253   3924   -234   -190    435       C  
ATOM   1458  CG2 ILE A 223     -11.096 -41.178 -40.550  1.00 36.32           C  
ANISOU 1458  CG2 ILE A 223     4775   5294   3732   -253   -357    319       C  
ATOM   1459  CD1 ILE A 223      -8.421 -40.486 -38.982  1.00 38.43           C  
ANISOU 1459  CD1 ILE A 223     5063   5447   4090   -203   -109    419       C  
ATOM   1460  N   THR A 224     -12.666 -44.171 -39.227  1.00 37.35           N  
ANISOU 1460  N   THR A 224     4724   5221   4245   -461   -455    197       N  
ATOM   1461  CA  THR A 224     -13.528 -45.078 -40.000  1.00 40.39           C  
ANISOU 1461  CA  THR A 224     5077   5581   4690   -541   -589     72       C  
ATOM   1462  C   THR A 224     -14.691 -45.696 -39.203  1.00 41.98           C  
ANISOU 1462  C   THR A 224     5119   5716   5116   -642   -616    114       C  
ATOM   1463  O   THR A 224     -15.657 -46.176 -39.788  1.00 40.39           O  
ANISOU 1463  O   THR A 224     4839   5511   4997   -721   -753     26       O  
ATOM   1464  CB  THR A 224     -12.728 -46.267 -40.590  1.00 41.94           C  
ANISOU 1464  CB  THR A 224     5381   5666   4888   -558   -586    -78       C  
ATOM   1465  OG1 THR A 224     -12.132 -47.024 -39.527  1.00 44.20           O  
ANISOU 1465  OG1 THR A 224     5656   5812   5327   -575   -472    -20       O  
ATOM   1466  CG2 THR A 224     -11.650 -45.780 -41.567  1.00 42.13           C  
ANISOU 1466  CG2 THR A 224     5553   5765   4690   -459   -544   -134       C  
ATOM   1467  N   ARG A 225     -14.571 -45.714 -37.876  1.00 41.83           N  
ANISOU 1467  N   ARG A 225     5051   5645   5195   -640   -484    250       N  
ATOM   1468  CA  ARG A 225     -15.479 -46.476 -37.010  1.00 41.00           C  
ANISOU 1468  CA  ARG A 225     4812   5456   5311   -734   -450    320       C  
ATOM   1469  C   ARG A 225     -15.616 -47.913 -37.488  1.00 44.65           C  
ANISOU 1469  C   ARG A 225     5270   5760   5935   -844   -518    200       C  
ATOM   1470  O   ARG A 225     -16.703 -48.470 -37.472  1.00 47.15           O  
ANISOU 1470  O   ARG A 225     5446   6023   6447   -956   -577    190       O  
ATOM   1471  CB  ARG A 225     -16.837 -45.790 -36.912  1.00 41.00           C  
ANISOU 1471  CB  ARG A 225     4645   5559   5375   -752   -495    380       C  
ATOM   1472  CG  ARG A 225     -17.633 -46.186 -35.701  1.00 38.95           C  
ANISOU 1472  CG  ARG A 225     4240   5248   5310   -810   -376    519       C  
ATOM   1473  CD  ARG A 225     -18.926 -45.386 -35.575  1.00 41.26           C  
ANISOU 1473  CD  ARG A 225     4348   5656   5671   -801   -393    584       C  
ATOM   1474  NE  ARG A 225     -19.469 -45.460 -34.215  1.00 39.05           N  
ANISOU 1474  NE  ARG A 225     3962   5364   5510   -805   -207    750       N  
ATOM   1475  CZ  ARG A 225     -20.273 -44.563 -33.646  1.00 40.28           C  
ANISOU 1475  CZ  ARG A 225     3998   5628   5680   -738   -125    845       C  
ATOM   1476  NH1 ARG A 225     -20.672 -43.490 -34.298  1.00 40.80           N  
ANISOU 1476  NH1 ARG A 225     4020   5808   5674   -663   -226    804       N  
ATOM   1477  NH2 ARG A 225     -20.662 -44.735 -32.397  1.00 48.74           N  
ANISOU 1477  NH2 ARG A 225     5002   6689   6828   -732     72    993       N  
ATOM   1478  N   ARG A 226     -14.493 -48.510 -37.902  1.00 46.28           N  
ANISOU 1478  N   ARG A 226     5621   5879   6083   -812   -503    105       N  
ATOM   1479  CA  ARG A 226     -14.431 -49.929 -38.266  1.00 46.15           C  
ANISOU 1479  CA  ARG A 226     5632   5671   6233   -898   -545    -21       C  
ATOM   1480  C   ARG A 226     -13.429 -50.651 -37.387  1.00 47.23           C  
ANISOU 1480  C   ARG A 226     5838   5659   6448   -858   -402     69       C  
ATOM   1481  O   ARG A 226     -12.410 -50.073 -37.005  1.00 45.81           O  
ANISOU 1481  O   ARG A 226     5734   5547   6125   -745   -317    143       O  
ATOM   1482  CB  ARG A 226     -13.958 -50.079 -39.696  1.00 47.83           C  
ANISOU 1482  CB  ARG A 226     5972   5904   6297   -867   -656   -246       C  
ATOM   1483  CG  ARG A 226     -14.911 -49.564 -40.715  1.00 48.20           C  
ANISOU 1483  CG  ARG A 226     5975   6090   6251   -899   -836   -356       C  
ATOM   1484  CD  ARG A 226     -14.339 -49.750 -42.109  1.00 53.00           C  
ANISOU 1484  CD  ARG A 226     6750   6733   6657   -845   -929   -576       C  
ATOM   1485  NE  ARG A 226     -15.322 -49.359 -43.115  1.00 57.11           N  
ANISOU 1485  NE  ARG A 226     7235   7392   7073   -873  -1139   -687       N  
ATOM   1486  CZ  ARG A 226     -16.069 -50.195 -43.824  1.00 65.25           C  
ANISOU 1486  CZ  ARG A 226     8238   8358   8196   -976  -1331   -891       C  
ATOM   1487  NH1 ARG A 226     -15.950 -51.514 -43.693  1.00 71.29           N  
ANISOU 1487  NH1 ARG A 226     9016   8892   9180  -1070  -1326  -1020       N  
ATOM   1488  NH2 ARG A 226     -16.936 -49.700 -44.698  1.00 75.17           N  
ANISOU 1488  NH2 ARG A 226     9455   9775   9331   -981  -1544   -972       N  
ATOM   1489  N   LYS A 227     -13.700 -51.923 -37.098  1.00 48.84           N  
ANISOU 1489  N   LYS A 227     6010   5651   6897   -951   -389     64       N  
ATOM   1490  CA  LYS A 227     -12.774 -52.761 -36.338  1.00 48.07           C  
ANISOU 1490  CA  LYS A 227     5982   5385   6897   -904   -270    156       C  
ATOM   1491  C   LYS A 227     -11.627 -53.153 -37.233  1.00 49.01           C  
ANISOU 1491  C   LYS A 227     6242   5442   6938   -822   -290    -22       C  
ATOM   1492  O   LYS A 227     -11.853 -53.705 -38.297  1.00 56.36           O  
ANISOU 1492  O   LYS A 227     7211   6296   7907   -874   -390   -239       O  
ATOM   1493  CB  LYS A 227     -13.479 -54.011 -35.848  1.00 51.29           C  
ANISOU 1493  CB  LYS A 227     6313   5557   7619  -1032   -243    214       C  
ATOM   1494  CG  LYS A 227     -14.668 -53.723 -34.928  1.00 53.06           C  
ANISOU 1494  CG  LYS A 227     6375   5834   7950  -1116   -183    410       C  
ATOM   1495  CD  LYS A 227     -15.237 -55.004 -34.340  1.00 51.49           C  
ANISOU 1495  CD  LYS A 227     6100   5379   8085  -1242   -113    516       C  
ATOM   1496  CE  LYS A 227     -16.669 -54.781 -33.825  1.00 55.70           C  
ANISOU 1496  CE  LYS A 227     6428   5963   8771  -1364    -73    649       C  
ATOM   1497  NZ  LYS A 227     -17.420 -56.039 -33.540  1.00 54.39           N  
ANISOU 1497  NZ  LYS A 227     6149   5529   8989  -1533    -26    717       N  
ATOM   1498  N   PRO A 228     -10.385 -52.855 -36.829  1.00 49.85           N  
ANISOU 1498  N   PRO A 228     6420   5588   6931   -688   -199     55       N  
ATOM   1499  CA  PRO A 228      -9.283 -53.214 -37.712  1.00 49.42           C  
ANISOU 1499  CA  PRO A 228     6477   5482   6817   -598   -191   -112       C  
ATOM   1500  C   PRO A 228      -9.156 -54.720 -37.889  1.00 53.79           C  
ANISOU 1500  C   PRO A 228     7074   5757   7607   -629   -186   -212       C  
ATOM   1501  O   PRO A 228      -9.237 -55.478 -36.922  1.00 57.88           O  
ANISOU 1501  O   PRO A 228     7555   6105   8330   -654   -130    -60       O  
ATOM   1502  CB  PRO A 228      -8.055 -52.628 -37.021  1.00 46.92           C  
ANISOU 1502  CB  PRO A 228     6177   5251   6399   -463    -96     28       C  
ATOM   1503  CG  PRO A 228      -8.460 -52.315 -35.638  1.00 48.53           C  
ANISOU 1503  CG  PRO A 228     6309   5494   6637   -481    -60    259       C  
ATOM   1504  CD  PRO A 228      -9.932 -52.199 -35.589  1.00 48.67           C  
ANISOU 1504  CD  PRO A 228     6248   5535   6709   -609   -109    277       C  
ATOM   1505  N   PHE A 229      -9.002 -55.135 -39.141  1.00 57.65           N  
ANISOU 1505  N   PHE A 229     7650   6195   8059   -624   -243   -470       N  
ATOM   1506  CA  PHE A 229      -8.837 -56.538 -39.508  1.00 61.55           C  
ANISOU 1506  CA  PHE A 229     8208   6407   8771   -642   -246   -629       C  
ATOM   1507  C   PHE A 229     -10.042 -57.387 -39.118  1.00 64.67           C  
ANISOU 1507  C   PHE A 229     8520   6598   9452   -818   -313   -609       C  
ATOM   1508  O   PHE A 229      -9.912 -58.556 -38.734  1.00 67.16           O  
ANISOU 1508  O   PHE A 229     8849   6629  10042   -841   -268   -590       O  
ATOM   1509  CB  PHE A 229      -7.541 -57.088 -38.910  1.00 63.40           C  
ANISOU 1509  CB  PHE A 229     8482   6508   9101   -499   -112   -528       C  
ATOM   1510  CG  PHE A 229      -6.350 -56.208 -39.152  1.00 57.96           C  
ANISOU 1510  CG  PHE A 229     7825   6019   8180   -341    -35   -514       C  
ATOM   1511  CD1 PHE A 229      -5.850 -56.039 -40.439  1.00 60.02           C  
ANISOU 1511  CD1 PHE A 229     8181   6357   8268   -269    -26   -745       C  
ATOM   1512  CD2 PHE A 229      -5.738 -55.535 -38.095  1.00 58.04           C  
ANISOU 1512  CD2 PHE A 229     7767   6144   8143   -267     28   -271       C  
ATOM   1513  CE1 PHE A 229      -4.752 -55.216 -40.673  1.00 61.05           C  
ANISOU 1513  CE1 PHE A 229     8318   6664   8214   -135     71   -711       C  
ATOM   1514  CE2 PHE A 229      -4.633 -54.723 -38.312  1.00 57.33           C  
ANISOU 1514  CE2 PHE A 229     7677   6220   7885   -142     92   -261       C  
ATOM   1515  CZ  PHE A 229      -4.134 -54.566 -39.608  1.00 61.02           C  
ANISOU 1515  CZ  PHE A 229     8220   6751   8215    -81    126   -470       C  
ATOM   1516  N   ASP A 230     -11.220 -56.794 -39.248  1.00 65.24           N  
ANISOU 1516  N   ASP A 230     8496   6808   9485   -941   -418   -606       N  
ATOM   1517  CA  ASP A 230     -12.431 -57.509 -38.972  1.00 68.59           C  
ANISOU 1517  CA  ASP A 230     8804   7060  10198  -1124   -484   -594       C  
ATOM   1518  C   ASP A 230     -12.673 -58.568 -40.025  1.00 73.21           C  
ANISOU 1518  C   ASP A 230     9453   7425  10940  -1209   -610   -910       C  
ATOM   1519  O   ASP A 230     -13.121 -59.670 -39.691  1.00 77.24           O  
ANISOU 1519  O   ASP A 230     9913   7641  11793  -1331   -609   -908       O  
ATOM   1520  CB  ASP A 230     -13.618 -56.565 -38.926  1.00 68.18           C  
ANISOU 1520  CB  ASP A 230     8606   7225  10073  -1220   -571   -528       C  
ATOM   1521  CG  ASP A 230     -14.803 -57.177 -38.234  1.00 73.21           C  
ANISOU 1521  CG  ASP A 230     9070   7704  11043  -1399   -571   -407       C  
ATOM   1522  OD1 ASP A 230     -14.598 -57.825 -37.177  1.00 76.69           O  
ANISOU 1522  OD1 ASP A 230     9492   7965  11681  -1405   -421   -194       O  
ATOM   1523  OD2 ASP A 230     -15.931 -57.016 -38.746  1.00 74.97           O  
ANISOU 1523  OD2 ASP A 230     9167   7983  11334  -1530   -719   -512       O  
ATOM   1524  N   GLU A 231     -12.380 -58.249 -41.289  1.00 74.92           N  
ANISOU 1524  N   GLU A 231     9788   7772  10905  -1144   -714  -1180       N  
ATOM   1525  CA  GLU A 231     -12.679 -59.177 -42.403  1.00 79.49           C  
ANISOU 1525  CA  GLU A 231    10451   8175  11578  -1219   -866  -1535       C  
ATOM   1526  C   GLU A 231     -11.670 -60.329 -42.505  1.00 82.42           C  
ANISOU 1526  C   GLU A 231    10964   8250  12101  -1131   -761  -1660       C  
ATOM   1527  O   GLU A 231     -11.956 -61.336 -43.158  1.00 83.55           O  
ANISOU 1527  O   GLU A 231    11168   8152  12424  -1211   -866  -1938       O  
ATOM   1528  CB  GLU A 231     -12.772 -58.436 -43.745  1.00 79.83           C  
ANISOU 1528  CB  GLU A 231    10594   8482  11255  -1164  -1018  -1781       C  
ATOM   1529  CG  GLU A 231     -13.559 -59.217 -44.834  0.00 82.74           C  
ANISOU 1529  CG  GLU A 231    11005   8728  11706  -1290  -1256  -2151       C  
ATOM   1530  CD  GLU A 231     -13.859 -58.374 -46.062  0.00 83.39           C  
ANISOU 1530  CD  GLU A 231    11171   9119  11396  -1239  -1437  -2344       C  
ATOM   1531  OE1 GLU A 231     -13.208 -57.325 -46.252  0.00 80.79           O  
ANISOU 1531  OE1 GLU A 231    10915   9055  10724  -1080  -1338  -2229       O  
ATOM   1532  OE2 GLU A 231     -14.750 -58.768 -46.845  0.00 86.11           O  
ANISOU 1532  OE2 GLU A 231    11505   9433  11781  -1360  -1686  -2609       O  
ATOM   1533  N   ILE A 232     -10.496 -60.183 -41.876  1.00 81.38           N  
ANISOU 1533  N   ILE A 232    10878   8130  11911   -962   -568  -1471       N  
ATOM   1534  CA  ILE A 232      -9.530 -61.292 -41.795  1.00 83.08           C  
ANISOU 1534  CA  ILE A 232    11196   8050  12322   -860   -452  -1535       C  
ATOM   1535  C   ILE A 232     -10.094 -62.404 -40.927  1.00 86.32           C  
ANISOU 1535  C   ILE A 232    11522   8105  13169   -996   -436  -1408       C  
ATOM   1536  O   ILE A 232     -10.439 -63.482 -41.430  1.00 91.92           O  
ANISOU 1536  O   ILE A 232    12278   8514  14132  -1088   -511  -1643       O  
ATOM   1537  CB  ILE A 232      -8.154 -60.854 -41.251  1.00 80.63           C  
ANISOU 1537  CB  ILE A 232    10915   7845  11876   -646   -268  -1336       C  
ATOM   1538  CG1 ILE A 232      -7.339 -60.216 -42.374  1.00 76.74           C  
ANISOU 1538  CG1 ILE A 232    10542   7576  11038   -494   -242  -1540       C  
ATOM   1539  CG2 ILE A 232      -7.378 -62.047 -40.683  1.00 80.82           C  
ANISOU 1539  CG2 ILE A 232    10974   7531  12205   -559   -148  -1272       C  
ATOM   1540  CD1 ILE A 232      -6.196 -59.381 -41.887  1.00 76.72           C  
ANISOU 1540  CD1 ILE A 232    10510   7770  10868   -326    -93  -1326       C  
ATOM   1541  N   GLY A 233     -10.191 -62.147 -39.628  1.00 84.00           N  
ANISOU 1541  N   GLY A 233    11114   7839  12964  -1008   -333  -1038       N  
ATOM   1542  CA  GLY A 233     -10.795 -63.119 -38.725  1.00 86.04           C  
ANISOU 1542  CA  GLY A 233    11286   7783  13623  -1139   -288   -854       C  
ATOM   1543  C   GLY A 233     -10.007 -64.411 -38.570  1.00 88.55           C  
ANISOU 1543  C   GLY A 233    11702   7716  14228  -1055   -195   -875       C  
ATOM   1544  O   GLY A 233      -8.782 -64.439 -38.719  1.00 89.34           O  
ANISOU 1544  O   GLY A 233    11907   7830  14208   -847   -113   -907       O  
ATOM   1545  N   GLY A 234     -10.721 -65.492 -38.280  1.00 90.16           N  
ANISOU 1545  N   GLY A 234    11858   7560  14840  -1217   -203   -851       N  
ATOM   1546  CA  GLY A 234     -10.102 -66.660 -37.664  1.00 89.20           C  
ANISOU 1546  CA  GLY A 234    11792   7053  15046  -1141    -76   -710       C  
ATOM   1547  C   GLY A 234      -9.481 -66.233 -36.338  1.00 84.98           C  
ANISOU 1547  C   GLY A 234    11224   6660  14405   -993     78   -272       C  
ATOM   1548  O   GLY A 234      -9.812 -65.166 -35.800  1.00 83.00           O  
ANISOU 1548  O   GLY A 234    10887   6744  13904  -1009     85    -78       O  
ATOM   1549  N   PRO A 235      -8.586 -67.058 -35.789  1.00 82.68           N  
ANISOU 1549  N   PRO A 235    11002   6112  14299   -840    190   -116       N  
ATOM   1550  CA  PRO A 235      -7.822 -66.681 -34.591  1.00 78.88           C  
ANISOU 1550  CA  PRO A 235    10509   5780  13683   -662    303    272       C  
ATOM   1551  C   PRO A 235      -6.767 -65.578 -34.812  1.00 73.19           C  
ANISOU 1551  C   PRO A 235     9813   5439  12555   -463    291    220       C  
ATOM   1552  O   PRO A 235      -6.485 -65.166 -35.947  1.00 67.68           O  
ANISOU 1552  O   PRO A 235     9161   4874  11680   -433    228   -106       O  
ATOM   1553  CB  PRO A 235      -7.143 -67.992 -34.176  1.00 82.29           C  
ANISOU 1553  CB  PRO A 235    11013   5791  14462   -543    395    396       C  
ATOM   1554  CG  PRO A 235      -7.830 -69.079 -34.989  1.00 87.32           C  
ANISOU 1554  CG  PRO A 235    11681   6019  15476   -717    347    112       C  
ATOM   1555  CD  PRO A 235      -8.286 -68.428 -36.233  1.00 87.56           C  
ANISOU 1555  CD  PRO A 235    11714   6267  15289   -823    206   -295       C  
ATOM   1556  N   ALA A 236      -6.178 -65.125 -33.710  1.00 70.00           N  
ANISOU 1556  N   ALA A 236     9382   5203  12012   -326    353    550       N  
ATOM   1557  CA  ALA A 236      -5.250 -64.003 -33.737  1.00 68.27           C  
ANISOU 1557  CA  ALA A 236     9153   5344  11442   -166    336    544       C  
ATOM   1558  C   ALA A 236      -4.046 -64.246 -34.654  1.00 67.34           C  
ANISOU 1558  C   ALA A 236     9096   5173  11319     10    347    294       C  
ATOM   1559  O   ALA A 236      -3.553 -63.326 -35.305  1.00 60.96           O  
ANISOU 1559  O   ALA A 236     8280   4638  10243     70    326    133       O  
ATOM   1560  CB  ALA A 236      -4.772 -63.683 -32.318  1.00 68.82           C  
ANISOU 1560  CB  ALA A 236     9191   5547  11412    -43    378    931       C  
ATOM   1561  N   PHE A 237      -3.573 -65.486 -34.707  1.00 70.43           N  
ANISOU 1561  N   PHE A 237     9542   5200  12017    100    399    272       N  
ATOM   1562  CA  PHE A 237      -2.405 -65.797 -35.528  1.00 70.44           C  
ANISOU 1562  CA  PHE A 237     9592   5131  12040    293    440     43       C  
ATOM   1563  C   PHE A 237      -2.599 -65.456 -37.026  1.00 68.87           C  
ANISOU 1563  C   PHE A 237     9455   5032  11679    233    407   -381       C  
ATOM   1564  O   PHE A 237      -1.616 -65.224 -37.727  1.00 68.01           O  
ANISOU 1564  O   PHE A 237     9369   5025  11446    396    460   -553       O  
ATOM   1565  CB  PHE A 237      -1.933 -67.243 -35.305  1.00 70.94           C  
ANISOU 1565  CB  PHE A 237     9709   4750  12496    410    508     92       C  
ATOM   1566  CG  PHE A 237      -2.831 -68.286 -35.888  1.00 73.43           C  
ANISOU 1566  CG  PHE A 237    10102   4685  13112    246    494   -119       C  
ATOM   1567  CD1 PHE A 237      -2.767 -68.601 -37.240  1.00 75.57           C  
ANISOU 1567  CD1 PHE A 237    10465   4851  13397    243    479   -558       C  
ATOM   1568  CD2 PHE A 237      -3.705 -68.986 -35.085  1.00 76.55           C  
ANISOU 1568  CD2 PHE A 237    10484   4815  13785     99    500    116       C  
ATOM   1569  CE1 PHE A 237      -3.585 -69.570 -37.784  1.00 75.31           C  
ANISOU 1569  CE1 PHE A 237    10506   4456  13652     84    437   -788       C  
ATOM   1570  CE2 PHE A 237      -4.520 -69.959 -35.620  1.00 79.92           C  
ANISOU 1570  CE2 PHE A 237    10963   4865  14538    -72    477    -88       C  
ATOM   1571  CZ  PHE A 237      -4.460 -70.252 -36.974  1.00 79.28           C  
ANISOU 1571  CZ  PHE A 237    10971   4678  14473    -83    430   -556       C  
ATOM   1572  N   ARG A 238      -3.845 -65.400 -37.500  1.00 67.78           N  
ANISOU 1572  N   ARG A 238     9337   4884  11532      8    320   -534       N  
ATOM   1573  CA  ARG A 238      -4.107 -65.038 -38.895  1.00 69.91           C  
ANISOU 1573  CA  ARG A 238     9678   5279  11604    -46    258   -921       C  
ATOM   1574  C   ARG A 238      -3.848 -63.549 -39.094  1.00 64.00           C  
ANISOU 1574  C   ARG A 238     8884   4984  10450     -8    248   -888       C  
ATOM   1575  O   ARG A 238      -3.380 -63.131 -40.145  1.00 66.90           O  
ANISOU 1575  O   ARG A 238     9316   5506  10598     72    266  -1132       O  
ATOM   1576  CB  ARG A 238      -5.532 -65.402 -39.325  1.00 71.19           C  
ANISOU 1576  CB  ARG A 238     9853   5306  11888   -297    132  -1093       C  
ATOM   1577  CG  ARG A 238      -6.002 -66.786 -38.824  1.00 82.42           C  
ANISOU 1577  CG  ARG A 238    11280   6262  13773   -392    143  -1030       C  
ATOM   1578  CD  ARG A 238      -7.036 -67.495 -39.729  1.00 86.86           C  
ANISOU 1578  CD  ARG A 238    11892   6584  14529   -598     13  -1375       C  
ATOM   1579  NE  ARG A 238      -7.807 -66.556 -40.548  1.00 93.63           N  
ANISOU 1579  NE  ARG A 238    12730   7764  15079   -723   -132  -1582       N  
ATOM   1580  CZ  ARG A 238      -7.751 -66.475 -41.877  1.00 95.82           C  
ANISOU 1580  CZ  ARG A 238    13126   8120  15160   -700   -223  -1988       C  
ATOM   1581  NH1 ARG A 238      -6.986 -67.298 -42.584  1.00100.25           N  
ANISOU 1581  NH1 ARG A 238    13838   8452  15803   -561   -171  -2268       N  
ATOM   1582  NH2 ARG A 238      -8.484 -65.570 -42.512  1.00 94.72           N  
ANISOU 1582  NH2 ARG A 238    12964   8293  14734   -803   -365  -2115       N  
ATOM   1583  N   ILE A 239      -4.138 -62.754 -38.077  1.00 59.12           N  
ANISOU 1583  N   ILE A 239     8163   4568   9732    -58    232   -584       N  
ATOM   1584  CA  ILE A 239      -3.890 -61.318 -38.127  1.00 56.41           C  
ANISOU 1584  CA  ILE A 239     7769   4619   9044    -26    223   -527       C  
ATOM   1585  C   ILE A 239      -2.409 -61.061 -37.958  1.00 55.73           C  
ANISOU 1585  C   ILE A 239     7658   4623   8895    193    320   -452       C  
ATOM   1586  O   ILE A 239      -1.844 -60.205 -38.621  1.00 58.29           O  
ANISOU 1586  O   ILE A 239     7978   5182   8985    261    352   -556       O  
ATOM   1587  CB  ILE A 239      -4.693 -60.568 -37.047  1.00 52.75           C  
ANISOU 1587  CB  ILE A 239     7210   4324   8507   -142    178   -246       C  
ATOM   1588  CG1 ILE A 239      -6.180 -60.584 -37.408  1.00 56.66           C  
ANISOU 1588  CG1 ILE A 239     7692   4798   9037   -360     82   -347       C  
ATOM   1589  CG2 ILE A 239      -4.250 -59.135 -36.927  1.00 48.55           C  
ANISOU 1589  CG2 ILE A 239     6628   4151   7668    -82    180   -165       C  
ATOM   1590  CD1 ILE A 239      -7.079 -60.374 -36.239  1.00 56.52           C  
ANISOU 1590  CD1 ILE A 239     7578   4812   9084   -475     80    -63       C  
ATOM   1591  N   MET A 240      -1.776 -61.810 -37.072  1.00 57.15           N  
ANISOU 1591  N   MET A 240     7806   4610   9297    305    369   -258       N  
ATOM   1592  CA  MET A 240      -0.346 -61.708 -36.893  1.00 55.75           C  
ANISOU 1592  CA  MET A 240     7575   4489   9118    522    444   -189       C  
ATOM   1593  C   MET A 240       0.385 -62.032 -38.183  1.00 56.31           C  
ANISOU 1593  C   MET A 240     7707   4502   9187    641    535   -497       C  
ATOM   1594  O   MET A 240       1.253 -61.287 -38.598  1.00 56.37           O  
ANISOU 1594  O   MET A 240     7663   4725   9028    748    599   -540       O  
ATOM   1595  CB  MET A 240       0.116 -62.632 -35.781  1.00 57.64           C  
ANISOU 1595  CB  MET A 240     7784   4495   9624    633    459     65       C  
ATOM   1596  CG  MET A 240      -0.274 -62.143 -34.414  1.00 54.44           C  
ANISOU 1596  CG  MET A 240     7318   4222   9145    580    394    401       C  
ATOM   1597  SD  MET A 240       0.228 -63.321 -33.143  1.00 65.29           S  
ANISOU 1597  SD  MET A 240     8685   5314  10808    728    409    726       S  
ATOM   1598  CE  MET A 240      -0.691 -62.630 -31.762  1.00 67.73           C  
ANISOU 1598  CE  MET A 240     8974   5823  10937    604    346   1057       C  
ATOM   1599  N   TRP A 241       0.054 -63.142 -38.823  1.00 60.06           N  
ANISOU 1599  N   TRP A 241     8291   4678   9850    625    552   -715       N  
ATOM   1600  CA  TRP A 241       0.678 -63.447 -40.101  1.00 61.61           C  
ANISOU 1600  CA  TRP A 241     8573   4830  10006    746    649  -1041       C  
ATOM   1601  C   TRP A 241       0.446 -62.321 -41.093  1.00 60.48           C  
ANISOU 1601  C   TRP A 241     8467   5019   9494    684    642  -1215       C  
ATOM   1602  O   TRP A 241       1.367 -61.916 -41.804  1.00 62.06           O  
ANISOU 1602  O   TRP A 241     8666   5368   9546    829    764  -1325       O  
ATOM   1603  CB  TRP A 241       0.132 -64.732 -40.678  1.00 67.64           C  
ANISOU 1603  CB  TRP A 241     9474   5226  11002    700    634  -1296       C  
ATOM   1604  CG  TRP A 241       0.507 -64.973 -42.115  1.00 70.68           C  
ANISOU 1604  CG  TRP A 241     9990   5595  11270    797    714  -1692       C  
ATOM   1605  CD1 TRP A 241      -0.235 -64.661 -43.224  1.00 73.70           C  
ANISOU 1605  CD1 TRP A 241    10495   6100  11407    683    645  -1989       C  
ATOM   1606  CD2 TRP A 241       1.690 -65.605 -42.591  1.00 70.85           C  
ANISOU 1606  CD2 TRP A 241    10042   5474  11405   1041    881  -1837       C  
ATOM   1607  NE1 TRP A 241       0.423 -65.057 -44.358  1.00 77.03           N  
ANISOU 1607  NE1 TRP A 241    11043   6474  11751    843    763  -2314       N  
ATOM   1608  CE2 TRP A 241       1.608 -65.639 -43.999  1.00 76.65           C  
ANISOU 1608  CE2 TRP A 241    10936   6258  11929   1066    924  -2232       C  
ATOM   1609  CE3 TRP A 241       2.818 -66.137 -41.967  1.00 76.83           C  
ANISOU 1609  CE3 TRP A 241    10702   6076  12413   1257    996  -1669       C  
ATOM   1610  CZ2 TRP A 241       2.615 -66.186 -44.793  1.00 81.37           C  
ANISOU 1610  CZ2 TRP A 241    11605   6755  12558   1300   1108  -2470       C  
ATOM   1611  CZ3 TRP A 241       3.822 -66.682 -42.757  1.00 80.35           C  
ANISOU 1611  CZ3 TRP A 241    11193   6411  12927   1488   1170  -1898       C  
ATOM   1612  CH2 TRP A 241       3.714 -66.701 -44.155  1.00 81.09           C  
ANISOU 1612  CH2 TRP A 241    11453   6556  12803   1509   1239  -2299       C  
ATOM   1613  N   ALA A 242      -0.784 -61.815 -41.137  1.00 57.06           N  
ANISOU 1613  N   ALA A 242     8058   4698   8923    477    509  -1222       N  
ATOM   1614  CA  ALA A 242      -1.139 -60.778 -42.094  1.00 55.37           C  
ANISOU 1614  CA  ALA A 242     7892   4782   8363    418    480  -1372       C  
ATOM   1615  C   ALA A 242      -0.228 -59.565 -41.918  1.00 53.49           C  
ANISOU 1615  C   ALA A 242     7552   4849   7924    518    570  -1202       C  
ATOM   1616  O   ALA A 242       0.503 -59.182 -42.845  1.00 51.83           O  
ANISOU 1616  O   ALA A 242     7380   4778   7537    633    688  -1342       O  
ATOM   1617  CB  ALA A 242      -2.596 -60.383 -41.913  1.00 53.15           C  
ANISOU 1617  CB  ALA A 242     7604   4573   8017    192    311  -1336       C  
ATOM   1618  N   VAL A 243      -0.277 -59.002 -40.707  1.00 50.95           N  
ANISOU 1618  N   VAL A 243     7103   4615   7641    473    520   -902       N  
ATOM   1619  CA  VAL A 243       0.451 -57.792 -40.323  1.00 50.85           C  
ANISOU 1619  CA  VAL A 243     6974   4871   7478    528    562   -723       C  
ATOM   1620  C   VAL A 243       1.974 -57.948 -40.466  1.00 54.75           C  
ANISOU 1620  C   VAL A 243     7393   5355   8055    734    712   -722       C  
ATOM   1621  O   VAL A 243       2.660 -57.079 -41.010  1.00 57.08           O  
ANISOU 1621  O   VAL A 243     7641   5857   8190    793    807   -742       O  
ATOM   1622  CB  VAL A 243       0.127 -57.411 -38.863  1.00 48.33           C  
ANISOU 1622  CB  VAL A 243     6550   4593   7219    459    466   -426       C  
ATOM   1623  CG1 VAL A 243       1.040 -56.280 -38.381  1.00 50.43           C  
ANISOU 1623  CG1 VAL A 243     6689   5091   7379    528    493   -265       C  
ATOM   1624  CG2 VAL A 243      -1.330 -56.995 -38.728  1.00 46.24           C  
ANISOU 1624  CG2 VAL A 243     6321   4395   6851    266    348   -406       C  
ATOM   1625  N   HIS A 244       2.495 -59.054 -39.955  1.00 56.98           N  
ANISOU 1625  N   HIS A 244     7650   5389   8611    844    739   -679       N  
ATOM   1626  CA  HIS A 244       3.886 -59.428 -40.161  1.00 58.41           C  
ANISOU 1626  CA  HIS A 244     7751   5515   8927   1058    884   -705       C  
ATOM   1627  C   HIS A 244       4.298 -59.349 -41.639  1.00 61.12           C  
ANISOU 1627  C   HIS A 244     8178   5926   9118   1141   1047   -984       C  
ATOM   1628  O   HIS A 244       5.380 -58.872 -41.947  1.00 63.90           O  
ANISOU 1628  O   HIS A 244     8423   6415   9440   1270   1189   -968       O  
ATOM   1629  CB  HIS A 244       4.090 -60.847 -39.650  1.00 60.07           C  
ANISOU 1629  CB  HIS A 244     7977   5383   9462   1159    884   -678       C  
ATOM   1630  CG  HIS A 244       5.484 -61.341 -39.798  1.00 64.52           C  
ANISOU 1630  CG  HIS A 244     8444   5861  10211   1400   1027   -696       C  
ATOM   1631  ND1 HIS A 244       6.578 -60.585 -39.441  1.00 67.94           N  
ANISOU 1631  ND1 HIS A 244     8683   6497  10635   1507   1071   -542       N  
ATOM   1632  CD2 HIS A 244       5.969 -62.520 -40.251  1.00 73.45           C  
ANISOU 1632  CD2 HIS A 244     9627   6714  11565   1561   1137   -853       C  
ATOM   1633  CE1 HIS A 244       7.679 -61.273 -39.675  1.00 70.79           C  
ANISOU 1633  CE1 HIS A 244     8963   6726  11209   1726   1205   -592       C  
ATOM   1634  NE2 HIS A 244       7.337 -62.451 -40.167  1.00 75.19           N  
ANISOU 1634  NE2 HIS A 244     9675   6988  11904   1773   1255   -781       N  
ATOM   1635  N   ASN A 245       3.429 -59.814 -42.538  1.00 62.16           N  
ANISOU 1635  N   ASN A 245     8497   5969   9152   1065   1025  -1237       N  
ATOM   1636  CA  ASN A 245       3.722 -59.866 -43.979  1.00 63.51           C  
ANISOU 1636  CA  ASN A 245     8796   6198   9137   1156   1172  -1530       C  
ATOM   1637  C   ASN A 245       3.436 -58.570 -44.729  1.00 61.31           C  
ANISOU 1637  C   ASN A 245     8556   6251   8490   1079   1187  -1551       C  
ATOM   1638  O   ASN A 245       3.551 -58.518 -45.959  1.00 63.90           O  
ANISOU 1638  O   ASN A 245     9017   6665   8595   1147   1301  -1778       O  
ATOM   1639  CB  ASN A 245       2.972 -61.025 -44.658  1.00 65.39           C  
ANISOU 1639  CB  ASN A 245     9235   6178   9433   1125   1120  -1833       C  
ATOM   1640  CG  ASN A 245       3.903 -62.072 -45.179  1.00 75.94           C  
ANISOU 1640  CG  ASN A 245    10620   7292  10940   1343   1297  -2032       C  
ATOM   1641  OD1 ASN A 245       3.777 -63.251 -44.853  1.00 85.95           O  
ANISOU 1641  OD1 ASN A 245    11930   8224  12503   1369   1261  -2097       O  
ATOM   1642  ND2 ASN A 245       4.873 -61.649 -45.984  1.00 82.26           N  
ANISOU 1642  ND2 ASN A 245    11409   8270  11577   1509   1510  -2118       N  
ATOM   1643  N   GLY A 246       3.041 -57.540 -43.999  1.00 55.27           N  
ANISOU 1643  N   GLY A 246     7689   5663   7649    949   1076  -1315       N  
ATOM   1644  CA  GLY A 246       2.943 -56.210 -44.570  1.00 54.01           C  
ANISOU 1644  CA  GLY A 246     7533   5803   7187    898   1107  -1275       C  
ATOM   1645  C   GLY A 246       1.570 -55.596 -44.511  1.00 50.41           C  
ANISOU 1645  C   GLY A 246     7144   5451   6559    705    915  -1248       C  
ATOM   1646  O   GLY A 246       1.442 -54.410 -44.711  1.00 49.41           O  
ANISOU 1646  O   GLY A 246     6995   5553   6227    656    916  -1150       O  
ATOM   1647  N   THR A 247       0.550 -56.397 -44.220  1.00 52.58           N  
ANISOU 1647  N   THR A 247     7486   5546   6946    598    756  -1322       N  
ATOM   1648  CA  THR A 247      -0.851 -55.965 -44.303  1.00 50.70           C  
ANISOU 1648  CA  THR A 247     7302   5390   6570    420    571  -1335       C  
ATOM   1649  C   THR A 247      -1.201 -54.852 -43.308  1.00 48.49           C  
ANISOU 1649  C   THR A 247     6889   5268   6266    322    495  -1057       C  
ATOM   1650  O   THR A 247      -0.861 -54.929 -42.110  1.00 46.35           O  
ANISOU 1650  O   THR A 247     6496   4928   6188    328    491   -855       O  
ATOM   1651  CB  THR A 247      -1.800 -57.175 -44.084  1.00 52.46           C  
ANISOU 1651  CB  THR A 247     7582   5346   7004    317    432  -1458       C  
ATOM   1652  OG1 THR A 247      -1.674 -58.078 -45.184  1.00 55.44           O  
ANISOU 1652  OG1 THR A 247     8117   5593   7355    388    469  -1777       O  
ATOM   1653  CG2 THR A 247      -3.253 -56.753 -43.990  1.00 54.35           C  
ANISOU 1653  CG2 THR A 247     7819   5663   7169    126    238  -1437       C  
ATOM   1654  N   ARG A 248      -1.877 -53.816 -43.804  1.00 45.88           N  
ANISOU 1654  N   ARG A 248     6590   5150   5690    247    431  -1048       N  
ATOM   1655  CA  ARG A 248      -2.354 -52.719 -42.939  1.00 42.96           C  
ANISOU 1655  CA  ARG A 248     6113   4920   5289    156    354   -817       C  
ATOM   1656  C   ARG A 248      -3.802 -52.426 -43.264  1.00 42.31           C  
ANISOU 1656  C   ARG A 248     6078   4907   5091     22    189   -870       C  
ATOM   1657  O   ARG A 248      -4.330 -52.946 -44.246  1.00 42.66           O  
ANISOU 1657  O   ARG A 248     6238   4925   5047      4    125  -1087       O  
ATOM   1658  CB  ARG A 248      -1.502 -51.453 -43.109  1.00 41.09           C  
ANISOU 1658  CB  ARG A 248     5822   4887   4904    222    470   -696       C  
ATOM   1659  CG  ARG A 248      -0.021 -51.626 -42.737  1.00 41.10           C  
ANISOU 1659  CG  ARG A 248     5725   4841   5052    348    624   -626       C  
ATOM   1660  CD  ARG A 248       0.161 -51.840 -41.228  1.00 44.66           C  
ANISOU 1660  CD  ARG A 248     6044   5194   5729    329    556   -445       C  
ATOM   1661  NE  ARG A 248       1.575 -51.873 -40.855  1.00 43.75           N  
ANISOU 1661  NE  ARG A 248     5806   5063   5754    451    666   -367       N  
ATOM   1662  CZ  ARG A 248       2.370 -52.925 -41.011  1.00 53.35           C  
ANISOU 1662  CZ  ARG A 248     7011   6129   7130    574    756   -445       C  
ATOM   1663  NH1 ARG A 248       3.646 -52.841 -40.640  1.00 50.35           N  
ANISOU 1663  NH1 ARG A 248     6483   5757   6891    686    843   -356       N  
ATOM   1664  NH2 ARG A 248       1.901 -54.066 -41.537  1.00 55.17           N  
ANISOU 1664  NH2 ARG A 248     7369   6190   7404    587    752   -620       N  
ATOM   1665  N   PRO A 249      -4.470 -51.628 -42.419  1.00 43.21           N  
ANISOU 1665  N   PRO A 249     6096   5106   5215    -65    110   -685       N  
ATOM   1666  CA  PRO A 249      -5.842 -51.301 -42.718  1.00 44.10           C  
ANISOU 1666  CA  PRO A 249     6220   5293   5241   -179    -42   -721       C  
ATOM   1667  C   PRO A 249      -5.900 -50.522 -44.001  1.00 49.09           C  
ANISOU 1667  C   PRO A 249     6952   6117   5585   -135    -50   -816       C  
ATOM   1668  O   PRO A 249      -4.929 -49.843 -44.349  1.00 52.78           O  
ANISOU 1668  O   PRO A 249     7442   6691   5922    -37     86   -762       O  
ATOM   1669  CB  PRO A 249      -6.251 -50.407 -41.551  1.00 43.20           C  
ANISOU 1669  CB  PRO A 249     5983   5256   5173   -232    -67   -487       C  
ATOM   1670  CG  PRO A 249      -5.307 -50.722 -40.472  1.00 41.72           C  
ANISOU 1670  CG  PRO A 249     5733   4971   5147   -177     27   -357       C  
ATOM   1671  CD  PRO A 249      -4.034 -51.008 -41.156  1.00 41.83           C  
ANISOU 1671  CD  PRO A 249     5800   4964   5130    -57    147   -452       C  
ATOM   1672  N   PRO A 250      -7.019 -50.619 -44.719  1.00 51.30           N  
ANISOU 1672  N   PRO A 250     7285   6442   5767   -206   -210   -947       N  
ATOM   1673  CA  PRO A 250      -7.119 -49.894 -45.975  1.00 51.56           C  
ANISOU 1673  CA  PRO A 250     7432   6671   5486   -148   -236  -1024       C  
ATOM   1674  C   PRO A 250      -7.007 -48.390 -45.805  1.00 49.99           C  
ANISOU 1674  C   PRO A 250     7184   6656   5155   -117   -184   -802       C  
ATOM   1675  O   PRO A 250      -7.260 -47.854 -44.730  1.00 48.61           O  
ANISOU 1675  O   PRO A 250     6879   6470   5120   -170   -192   -622       O  
ATOM   1676  CB  PRO A 250      -8.508 -50.271 -46.501  1.00 53.89           C  
ANISOU 1676  CB  PRO A 250     7747   6975   5754   -249   -473  -1179       C  
ATOM   1677  CG  PRO A 250      -9.235 -50.874 -45.358  1.00 54.21           C  
ANISOU 1677  CG  PRO A 250     7638   6846   6115   -380   -548  -1115       C  
ATOM   1678  CD  PRO A 250      -8.217 -51.420 -44.426  1.00 53.14           C  
ANISOU 1678  CD  PRO A 250     7464   6544   6180   -340   -378  -1025       C  
ATOM   1679  N   LEU A 251      -6.611 -47.727 -46.878  1.00 52.98           N  
ANISOU 1679  N   LEU A 251     7678   7193   5260    -25   -119   -817       N  
ATOM   1680  CA  LEU A 251      -6.581 -46.280 -46.930  1.00 53.37           C  
ANISOU 1680  CA  LEU A 251     7703   7401   5176      5    -75   -614       C  
ATOM   1681  C   LEU A 251      -8.003 -45.731 -46.980  1.00 52.91           C  
ANISOU 1681  C   LEU A 251     7609   7431   5065    -62   -287   -573       C  
ATOM   1682  O   LEU A 251      -8.956 -46.450 -47.304  1.00 49.94           O  
ANISOU 1682  O   LEU A 251     7248   7033   4694   -121   -470   -730       O  
ATOM   1683  CB  LEU A 251      -5.790 -45.817 -48.154  1.00 59.28           C  
ANISOU 1683  CB  LEU A 251     8596   8285   5642    128     72   -626       C  
ATOM   1684  CG  LEU A 251      -4.272 -46.103 -48.108  1.00 64.38           C  
ANISOU 1684  CG  LEU A 251     9237   8869   6357    211    325   -620       C  
ATOM   1685  CD1 LEU A 251      -3.674 -46.021 -49.506  1.00 66.22           C  
ANISOU 1685  CD1 LEU A 251     9643   9232   6287    338    473   -696       C  
ATOM   1686  CD2 LEU A 251      -3.530 -45.166 -47.150  1.00 60.85           C  
ANISOU 1686  CD2 LEU A 251     8635   8403   6083    196    447   -387       C  
ATOM   1687  N   ILE A 252      -8.127 -44.447 -46.657  1.00 52.48           N  
ANISOU 1687  N   ILE A 252     7493   7463   4984    -50   -262   -366       N  
ATOM   1688  CA  ILE A 252      -9.412 -43.817 -46.380  1.00 50.19           C  
ANISOU 1688  CA  ILE A 252     7118   7233   4721   -102   -433   -284       C  
ATOM   1689  C   ILE A 252      -9.723 -42.737 -47.420  1.00 49.62           C  
ANISOU 1689  C   ILE A 252     7137   7336   4381    -20   -476   -199       C  
ATOM   1690  O   ILE A 252      -8.992 -41.767 -47.535  1.00 50.94           O  
ANISOU 1690  O   ILE A 252     7337   7546   4473     45   -325    -43       O  
ATOM   1691  CB  ILE A 252      -9.378 -43.181 -44.973  1.00 47.52           C  
ANISOU 1691  CB  ILE A 252     6630   6825   4602   -144   -370   -107       C  
ATOM   1692  CG1 ILE A 252      -9.076 -44.247 -43.920  1.00 47.35           C  
ANISOU 1692  CG1 ILE A 252     6532   6643   4815   -208   -330   -159       C  
ATOM   1693  CG2 ILE A 252     -10.695 -42.445 -44.660  1.00 49.77           C  
ANISOU 1693  CG2 ILE A 252     6816   7170   4923   -175   -513    -15       C  
ATOM   1694  CD1 ILE A 252      -8.646 -43.674 -42.572  1.00 41.87           C  
ANISOU 1694  CD1 ILE A 252     5735   5896   4278   -217   -236     -1       C  
ATOM   1695  N   LYS A 253     -10.810 -42.905 -48.165  1.00 51.71           N  
ANISOU 1695  N   LYS A 253     7436   7696   4518    -25   -691   -292       N  
ATOM   1696  CA  LYS A 253     -11.213 -41.932 -49.169  1.00 52.69           C  
ANISOU 1696  CA  LYS A 253     7653   7997   4372     68   -766   -198       C  
ATOM   1697  C   LYS A 253     -11.199 -40.525 -48.594  1.00 51.04           C  
ANISOU 1697  C   LYS A 253     7362   7795   4234    100   -679     64       C  
ATOM   1698  O   LYS A 253     -11.857 -40.267 -47.601  1.00 50.24           O  
ANISOU 1698  O   LYS A 253     7101   7630   4358     40   -736    131       O  
ATOM   1699  CB  LYS A 253     -12.618 -42.241 -49.700  1.00 55.54           C  
ANISOU 1699  CB  LYS A 253     7985   8448   4671     39  -1068   -313       C  
ATOM   1700  CG  LYS A 253     -12.663 -43.246 -50.838  1.00 60.64           C  
ANISOU 1700  CG  LYS A 253     8792   9156   5095     57  -1194   -574       C  
ATOM   1701  CD  LYS A 253     -14.028 -43.548 -51.375  0.00 61.33           C  
ANISOU 1701  CD  LYS A 253     8834   9333   5135     17  -1528   -707       C  
ATOM   1702  CE  LYS A 253     -14.639 -42.349 -52.091  0.00 63.35           C  
ANISOU 1702  CE  LYS A 253     9127   9794   5150    131  -1656   -534       C  
ATOM   1703  NZ  LYS A 253     -15.922 -42.697 -52.763  0.00 66.45           N  
ANISOU 1703  NZ  LYS A 253     9479  10303   5468    108  -2019   -687       N  
ATOM   1704  N   ASN A 254     -10.435 -39.625 -49.213  1.00 53.23           N  
ANISOU 1704  N   ASN A 254     7752   8140   4331    198   -526    211       N  
ATOM   1705  CA  ASN A 254     -10.521 -38.192 -48.920  1.00 52.16           C  
ANISOU 1705  CA  ASN A 254     7570   8008   4242    240   -468    457       C  
ATOM   1706  C   ASN A 254      -9.889 -37.802 -47.582  1.00 49.12           C  
ANISOU 1706  C   ASN A 254     7051   7465   4146    176   -314    542       C  
ATOM   1707  O   ASN A 254     -10.184 -36.739 -47.027  1.00 45.51           O  
ANISOU 1707  O   ASN A 254     6520   6967   3803    186   -305    696       O  
ATOM   1708  CB  ASN A 254     -11.993 -37.726 -48.961  1.00 56.01           C  
ANISOU 1708  CB  ASN A 254     7979   8567   4736    255   -707    507       C  
ATOM   1709  CG  ASN A 254     -12.137 -36.208 -48.983  1.00 57.82           C  
ANISOU 1709  CG  ASN A 254     8202   8807   4959    339   -660    762       C  
ATOM   1710  OD1 ASN A 254     -11.399 -35.518 -49.689  1.00 65.73           O  
ANISOU 1710  OD1 ASN A 254     9336   9845   5795    419   -516    902       O  
ATOM   1711  ND2 ASN A 254     -13.085 -35.681 -48.191  1.00 59.30           N  
ANISOU 1711  ND2 ASN A 254     8233   8949   5347    325   -761    828       N  
ATOM   1712  N   LEU A 255      -9.017 -38.659 -47.063  1.00 48.03           N  
ANISOU 1712  N   LEU A 255     6890   7236   4124    121   -204    433       N  
ATOM   1713  CA  LEU A 255      -8.318 -38.361 -45.817  1.00 45.09           C  
ANISOU 1713  CA  LEU A 255     6403   6733   3997     70    -81    498       C  
ATOM   1714  C   LEU A 255      -7.302 -37.267 -46.121  1.00 45.57           C  
ANISOU 1714  C   LEU A 255     6501   6784   4030    116    105    660       C  
ATOM   1715  O   LEU A 255      -6.577 -37.365 -47.102  1.00 50.03           O  
ANISOU 1715  O   LEU A 255     7172   7409   4430    171    226    668       O  
ATOM   1716  CB  LEU A 255      -7.611 -39.609 -45.309  1.00 45.22           C  
ANISOU 1716  CB  LEU A 255     6388   6664   4128     21    -26    353       C  
ATOM   1717  CG  LEU A 255      -6.859 -39.480 -43.985  1.00 42.85           C  
ANISOU 1717  CG  LEU A 255     5972   6246   4062    -25     65    401       C  
ATOM   1718  CD1 LEU A 255      -7.799 -39.295 -42.821  1.00 44.46           C  
ANISOU 1718  CD1 LEU A 255     6072   6407   4414    -77    -45    428       C  
ATOM   1719  CD2 LEU A 255      -5.960 -40.682 -43.778  1.00 38.54           C  
ANISOU 1719  CD2 LEU A 255     5419   5629   3594    -35    137    284       C  
ATOM   1720  N   PRO A 256      -7.281 -36.197 -45.330  1.00 42.11           N  
ANISOU 1720  N   PRO A 256     5981   6268   3753     98    136    790       N  
ATOM   1721  CA  PRO A 256      -6.237 -35.196 -45.528  1.00 43.51           C  
ANISOU 1721  CA  PRO A 256     6169   6396   3968    115    319    937       C  
ATOM   1722  C   PRO A 256      -4.842 -35.764 -45.410  1.00 44.09           C  
ANISOU 1722  C   PRO A 256     6208   6423   4121     87    482    884       C  
ATOM   1723  O   PRO A 256      -4.556 -36.523 -44.491  1.00 47.58           O  
ANISOU 1723  O   PRO A 256     6564   6804   4711     36    452    772       O  
ATOM   1724  CB  PRO A 256      -6.500 -34.204 -44.398  1.00 40.89           C  
ANISOU 1724  CB  PRO A 256     5734   5950   3851     78    287   1012       C  
ATOM   1725  CG  PRO A 256      -7.943 -34.314 -44.169  1.00 41.04           C  
ANISOU 1725  CG  PRO A 256     5737   6017   3841     95    104    976       C  
ATOM   1726  CD  PRO A 256      -8.229 -35.779 -44.293  1.00 41.98           C  
ANISOU 1726  CD  PRO A 256     5862   6201   3888     67     19    808       C  
ATOM   1727  N   LYS A 257      -3.970 -35.352 -46.317  1.00 46.94           N  
ANISOU 1727  N   LYS A 257     6628   6813   4395    129    664    985       N  
ATOM   1728  CA  LYS A 257      -2.622 -35.903 -46.417  1.00 46.85           C  
ANISOU 1728  CA  LYS A 257     6572   6778   4450    124    846    943       C  
ATOM   1729  C   LYS A 257      -1.749 -35.723 -45.180  1.00 43.58           C  
ANISOU 1729  C   LYS A 257     5982   6231   4346     44    881    939       C  
ATOM   1730  O   LYS A 257      -1.005 -36.630 -44.828  1.00 43.01           O  
ANISOU 1730  O   LYS A 257     5839   6135   4367     35    920    834       O  
ATOM   1731  CB  LYS A 257      -1.927 -35.351 -47.659  1.00 49.29           C  
ANISOU 1731  CB  LYS A 257     6971   7153   4605    190   1066   1088       C  
ATOM   1732  CG  LYS A 257      -2.407 -36.038 -48.943  1.00 55.01           C  
ANISOU 1732  CG  LYS A 257     7886   8039   4976    291   1055   1017       C  
ATOM   1733  CD  LYS A 257      -1.881 -35.291 -50.169  0.00 55.44           C  
ANISOU 1733  CD  LYS A 257     8057   8178   4828    374   1277   1209       C  
ATOM   1734  CE  LYS A 257      -2.532 -35.800 -51.446  0.00 57.94           C  
ANISOU 1734  CE  LYS A 257     8597   8681   4735    491   1221   1145       C  
ATOM   1735  NZ  LYS A 257      -1.995 -35.120 -52.657  0.00 61.73           N  
ANISOU 1735  NZ  LYS A 257     9217   9265   4972    591   1461   1349       N  
ATOM   1736  N   PRO A 258      -1.829 -34.568 -44.515  1.00 43.03           N  
ANISOU 1736  N   PRO A 258     5843   6069   4436     -7    854   1043       N  
ATOM   1737  CA  PRO A 258      -1.108 -34.439 -43.240  1.00 44.95           C  
ANISOU 1737  CA  PRO A 258     5929   6198   4953    -83    831   1000       C  
ATOM   1738  C   PRO A 258      -1.406 -35.584 -42.278  1.00 40.85           C  
ANISOU 1738  C   PRO A 258     5371   5683   4468    -96    685    840       C  
ATOM   1739  O   PRO A 258      -0.493 -36.124 -41.644  1.00 43.28           O  
ANISOU 1739  O   PRO A 258     5573   5950   4923   -117    703    780       O  
ATOM   1740  CB  PRO A 258      -1.641 -33.125 -42.666  1.00 46.15           C  
ANISOU 1740  CB  PRO A 258     6065   6259   5212   -120    762   1085       C  
ATOM   1741  CG  PRO A 258      -2.044 -32.334 -43.879  1.00 46.15           C  
ANISOU 1741  CG  PRO A 258     6179   6295   5060    -65    849   1247       C  
ATOM   1742  CD  PRO A 258      -2.555 -33.338 -44.864  1.00 44.18           C  
ANISOU 1742  CD  PRO A 258     6054   6202   4532     12    833   1194       C  
ATOM   1743  N   ILE A 259      -2.666 -35.978 -42.225  1.00 39.59           N  
ANISOU 1743  N   ILE A 259     5288   5573   4181    -77    547    787       N  
ATOM   1744  CA  ILE A 259      -3.123 -37.004 -41.295  1.00 42.97           C  
ANISOU 1744  CA  ILE A 259     5685   5992   4649    -95    420    669       C  
ATOM   1745  C   ILE A 259      -2.770 -38.413 -41.800  1.00 42.66           C  
ANISOU 1745  C   ILE A 259     5677   5982   4550    -65    453    563       C  
ATOM   1746  O   ILE A 259      -2.395 -39.293 -41.015  1.00 43.03           O  
ANISOU 1746  O   ILE A 259     5663   5979   4706    -76    421    493       O  
ATOM   1747  CB  ILE A 259      -4.651 -36.908 -41.069  1.00 41.17           C  
ANISOU 1747  CB  ILE A 259     5499   5798   4346    -94    277    660       C  
ATOM   1748  CG1 ILE A 259      -5.008 -35.521 -40.551  1.00 42.33           C  
ANISOU 1748  CG1 ILE A 259     5620   5899   4564   -101    256    750       C  
ATOM   1749  CG2 ILE A 259      -5.075 -37.936 -40.084  1.00 41.07           C  
ANISOU 1749  CG2 ILE A 259     5445   5765   4394   -120    182    570       C  
ATOM   1750  CD1 ILE A 259      -6.480 -35.265 -40.336  1.00 47.48           C  
ANISOU 1750  CD1 ILE A 259     6287   6584   5169    -82    140    759       C  
ATOM   1751  N   GLU A 260      -2.925 -38.613 -43.101  1.00 39.95           N  
ANISOU 1751  N   GLU A 260     5442   5715   4024    -17    511    551       N  
ATOM   1752  CA  GLU A 260      -2.528 -39.836 -43.739  1.00 43.44           C  
ANISOU 1752  CA  GLU A 260     5935   6175   4394     25    565    431       C  
ATOM   1753  C   GLU A 260      -1.039 -40.108 -43.575  1.00 44.21           C  
ANISOU 1753  C   GLU A 260     5941   6222   4636     47    722    432       C  
ATOM   1754  O   GLU A 260      -0.652 -41.225 -43.217  1.00 45.33           O  
ANISOU 1754  O   GLU A 260     6047   6310   4865     64    715    331       O  
ATOM   1755  CB  GLU A 260      -2.841 -39.787 -45.234  1.00 46.20           C  
ANISOU 1755  CB  GLU A 260     6437   6636   4480     90    614    420       C  
ATOM   1756  CG  GLU A 260      -2.379 -41.026 -45.959  1.00 48.74           C  
ANISOU 1756  CG  GLU A 260     6834   6972   4711    148    685    264       C  
ATOM   1757  CD  GLU A 260      -3.117 -41.268 -47.249  1.00 54.23           C  
ANISOU 1757  CD  GLU A 260     7709   7786   5112    205    635    183       C  
ATOM   1758  OE1 GLU A 260      -2.470 -41.209 -48.316  1.00 64.38           O  
ANISOU 1758  OE1 GLU A 260     9095   9151   6214    290    801    187       O  
ATOM   1759  OE2 GLU A 260      -4.336 -41.538 -47.193  1.00 72.22           O  
ANISOU 1759  OE2 GLU A 260    10020  10081   7337    168    430    113       O  
ATOM   1760  N   SER A 261      -0.190 -39.117 -43.851  1.00 44.05           N  
ANISOU 1760  N   SER A 261     5866   6207   4665     48    868    554       N  
ATOM   1761  CA  SER A 261       1.249 -39.346 -43.664  1.00 44.51           C  
ANISOU 1761  CA  SER A 261     5790   6219   4904     63   1014    560       C  
ATOM   1762  C   SER A 261       1.553 -39.692 -42.211  1.00 42.08           C  
ANISOU 1762  C   SER A 261     5342   5824   4823     19    886    524       C  
ATOM   1763  O   SER A 261       2.379 -40.566 -41.960  1.00 42.84           O  
ANISOU 1763  O   SER A 261     5355   5884   5038     59    926    465       O  
ATOM   1764  CB  SER A 261       2.130 -38.194 -44.148  1.00 45.37           C  
ANISOU 1764  CB  SER A 261     5829   6331   5080     49   1200    711       C  
ATOM   1765  OG  SER A 261       1.557 -36.940 -43.901  1.00 52.62           O  
ANISOU 1765  OG  SER A 261     6758   7224   6011    -12   1134    824       O  
ATOM   1766  N   LEU A 262       0.878 -39.049 -41.257  1.00 39.32           N  
ANISOU 1766  N   LEU A 262     4974   5446   4520    -44    733    557       N  
ATOM   1767  CA  LEU A 262       1.130 -39.374 -39.843  1.00 41.16           C  
ANISOU 1767  CA  LEU A 262     5102   5619   4918    -70    605    524       C  
ATOM   1768  C   LEU A 262       0.739 -40.820 -39.530  1.00 40.78           C  
ANISOU 1768  C   LEU A 262     5098   5554   4842    -31    530    433       C  
ATOM   1769  O   LEU A 262       1.539 -41.621 -39.014  1.00 41.90           O  
ANISOU 1769  O   LEU A 262     5156   5651   5113      5    527    404       O  
ATOM   1770  CB  LEU A 262       0.354 -38.437 -38.944  1.00 40.52           C  
ANISOU 1770  CB  LEU A 262     5027   5522   4844   -127    473    559       C  
ATOM   1771  CG  LEU A 262       0.595 -38.605 -37.458  1.00 40.36           C  
ANISOU 1771  CG  LEU A 262     4926   5465   4945   -144    338    530       C  
ATOM   1772  CD1 LEU A 262       2.002 -38.238 -37.094  1.00 44.56           C  
ANISOU 1772  CD1 LEU A 262     5301   5959   5670   -160    362    543       C  
ATOM   1773  CD2 LEU A 262      -0.381 -37.721 -36.715  1.00 42.64           C  
ANISOU 1773  CD2 LEU A 262     5262   5751   5188   -179    233    543       C  
ATOM   1774  N   MET A 263      -0.494 -41.152 -39.880  1.00 37.97           N  
ANISOU 1774  N   MET A 263     4866   5225   4338    -38    467    394       N  
ATOM   1775  CA  MET A 263      -1.033 -42.464 -39.608  1.00 37.90           C  
ANISOU 1775  CA  MET A 263     4901   5173   4327    -25    394    313       C  
ATOM   1776  C   MET A 263      -0.127 -43.533 -40.174  1.00 38.79           C  
ANISOU 1776  C   MET A 263     5008   5241   4488     44    496    236       C  
ATOM   1777  O   MET A 263       0.166 -44.522 -39.510  1.00 39.43           O  
ANISOU 1777  O   MET A 263     5050   5241   4690     72    460    209       O  
ATOM   1778  CB  MET A 263      -2.404 -42.574 -40.258  1.00 38.49           C  
ANISOU 1778  CB  MET A 263     5089   5289   4246    -51    328    269       C  
ATOM   1779  CG  MET A 263      -3.144 -43.876 -39.997  1.00 39.73           C  
ANISOU 1779  CG  MET A 263     5282   5380   4434    -67    243    186       C  
ATOM   1780  SD  MET A 263      -4.826 -43.777 -40.623  1.00 43.41           S  
ANISOU 1780  SD  MET A 263     5826   5906   4762   -120    127    143       S  
ATOM   1781  CE  MET A 263      -4.514 -43.821 -42.396  1.00 46.00           C  
ANISOU 1781  CE  MET A 263     6277   6310   4892    -60    201     44       C  
ATOM   1782  N   THR A 264       0.300 -43.361 -41.420  1.00 41.11           N  
ANISOU 1782  N   THR A 264     5352   5587   4682     88    635    207       N  
ATOM   1783  CA  THR A 264       1.059 -44.424 -42.087  1.00 43.58           C  
ANISOU 1783  CA  THR A 264     5681   5860   5016    174    755    106       C  
ATOM   1784  C   THR A 264       2.531 -44.479 -41.669  1.00 43.79           C  
ANISOU 1784  C   THR A 264     5543   5848   5247    227    861    152       C  
ATOM   1785  O   THR A 264       3.137 -45.529 -41.778  1.00 46.04           O  
ANISOU 1785  O   THR A 264     5806   6064   5622    309    924     76       O  
ATOM   1786  CB  THR A 264       0.964 -44.336 -43.622  1.00 44.86           C  
ANISOU 1786  CB  THR A 264     5980   6108   4955    224    881     40       C  
ATOM   1787  OG1 THR A 264       1.492 -43.097 -44.053  1.00 40.16           O  
ANISOU 1787  OG1 THR A 264     5345   5596   4317    221   1007    167       O  
ATOM   1788  CG2 THR A 264      -0.482 -44.426 -44.081  1.00 50.59           C  
ANISOU 1788  CG2 THR A 264     6855   6878   5488    181    739    -28       C  
ATOM   1789  N   ARG A 265       3.101 -43.362 -41.210  1.00 43.85           N  
ANISOU 1789  N   ARG A 265     5424   5888   5349    184    875    269       N  
ATOM   1790  CA  ARG A 265       4.412 -43.383 -40.535  1.00 46.38           C  
ANISOU 1790  CA  ARG A 265     5544   6168   5908    212    907    315       C  
ATOM   1791  C   ARG A 265       4.336 -44.164 -39.240  1.00 46.52           C  
ANISOU 1791  C   ARG A 265     5514   6114   6048    224    732    306       C  
ATOM   1792  O   ARG A 265       5.273 -44.865 -38.882  1.00 48.75           O  
ANISOU 1792  O   ARG A 265     5678   6345   6500    299    748    302       O  
ATOM   1793  CB  ARG A 265       4.859 -41.981 -40.135  1.00 46.01           C  
ANISOU 1793  CB  ARG A 265     5372   6150   5958    132    899    422       C  
ATOM   1794  CG  ARG A 265       5.506 -41.192 -41.198  1.00 49.82           C  
ANISOU 1794  CG  ARG A 265     5814   6678   6437    131   1113    485       C  
ATOM   1795  CD  ARG A 265       5.733 -39.784 -40.714  1.00 55.68           C  
ANISOU 1795  CD  ARG A 265     6450   7409   7299     27   1074    586       C  
ATOM   1796  NE  ARG A 265       6.847 -39.661 -39.773  1.00 61.48           N  
ANISOU 1796  NE  ARG A 265     6949   8096   8313      4   1010    600       N  
ATOM   1797  CZ  ARG A 265       6.971 -38.685 -38.874  1.00 60.89           C  
ANISOU 1797  CZ  ARG A 265     6779   7986   8371    -91    872    631       C  
ATOM   1798  NH1 ARG A 265       6.034 -37.741 -38.752  1.00 54.71           N  
ANISOU 1798  NH1 ARG A 265     6116   7194   7478   -163    801    656       N  
ATOM   1799  NH2 ARG A 265       8.033 -38.663 -38.071  1.00 62.92           N  
ANISOU 1799  NH2 ARG A 265     6814   8213   8879   -105    790    623       N  
ATOM   1800  N   CYS A 266       3.241 -43.976 -38.500  1.00 44.27           N  
ANISOU 1800  N   CYS A 266     5312   5831   5679    157    571    324       N  
ATOM   1801  CA  CYS A 266       3.013 -44.730 -37.264  1.00 42.89           C  
ANISOU 1801  CA  CYS A 266     5125   5596   5575    171    420    342       C  
ATOM   1802  C   CYS A 266       2.961 -46.264 -37.492  1.00 43.29           C  
ANISOU 1802  C   CYS A 266     5234   5547   5668    248    448    277       C  
ATOM   1803  O   CYS A 266       3.297 -47.017 -36.588  1.00 42.05           O  
ANISOU 1803  O   CYS A 266     5026   5321   5632    300    372    318       O  
ATOM   1804  CB  CYS A 266       1.748 -44.225 -36.563  1.00 39.56           C  
ANISOU 1804  CB  CYS A 266     4791   5205   5036     92    290    376       C  
ATOM   1805  SG  CYS A 266       1.938 -42.572 -35.782  1.00 44.60           S  
ANISOU 1805  SG  CYS A 266     5350   5910   5684     24    212    439       S  
ATOM   1806  N   TRP A 267       2.592 -46.704 -38.701  1.00 42.37           N  
ANISOU 1806  N   TRP A 267     5228   5417   5454    263    552    175       N  
ATOM   1807  CA  TRP A 267       2.441 -48.133 -39.029  1.00 43.46           C  
ANISOU 1807  CA  TRP A 267     5443   5432   5637    326    576     76       C  
ATOM   1808  C   TRP A 267       3.697 -48.786 -39.602  1.00 45.16           C  
ANISOU 1808  C   TRP A 267     5590   5594   5976    453    728     15       C  
ATOM   1809  O   TRP A 267       3.663 -49.968 -39.950  1.00 48.44           O  
ANISOU 1809  O   TRP A 267     6075   5886   6445    521    765    -88       O  
ATOM   1810  CB  TRP A 267       1.411 -48.340 -40.141  1.00 46.63           C  
ANISOU 1810  CB  TRP A 267     6011   5845   5861    285    596    -51       C  
ATOM   1811  CG  TRP A 267       0.030 -48.022 -39.886  1.00 48.24           C  
ANISOU 1811  CG  TRP A 267     6289   6081   5960    177    464    -33       C  
ATOM   1812  CD1 TRP A 267      -0.602 -47.891 -38.678  1.00 58.40           C  
ANISOU 1812  CD1 TRP A 267     7538   7351   7298    115    341     73       C  
ATOM   1813  CD2 TRP A 267      -0.963 -47.842 -40.884  1.00 49.10           C  
ANISOU 1813  CD2 TRP A 267     6520   6249   5888    129    442   -126       C  
ATOM   1814  NE1 TRP A 267      -1.948 -47.604 -38.876  1.00 58.04           N  
ANISOU 1814  NE1 TRP A 267     7564   7348   7139     26    262     55       N  
ATOM   1815  CE2 TRP A 267      -2.187 -47.577 -40.225  1.00 50.92           C  
ANISOU 1815  CE2 TRP A 267     6753   6492   6101     31    304    -68       C  
ATOM   1816  CE3 TRP A 267      -0.940 -47.876 -42.277  1.00 57.22           C  
ANISOU 1816  CE3 TRP A 267     7655   7334   6752    168    523   -254       C  
ATOM   1817  CZ2 TRP A 267      -3.366 -47.359 -40.913  1.00 46.85           C  
ANISOU 1817  CZ2 TRP A 267     6318   6036   5447    -31    227   -131       C  
ATOM   1818  CZ3 TRP A 267      -2.123 -47.639 -42.962  1.00 56.62           C  
ANISOU 1818  CZ3 TRP A 267     7685   7328   6499    108    428   -319       C  
ATOM   1819  CH2 TRP A 267      -3.316 -47.398 -42.282  1.00 51.82           C  
ANISOU 1819  CH2 TRP A 267     7051   6723   5914      8    274   -258       C  
ATOM   1820  N   SER A 268       4.784 -48.046 -39.761  1.00 43.70           N  
ANISOU 1820  N   SER A 268     5264   5487   5854    488    829     69       N  
ATOM   1821  CA  SER A 268       5.962 -48.592 -40.451  1.00 46.56           C  
ANISOU 1821  CA  SER A 268     5543   5815   6331    619   1016     11       C  
ATOM   1822  C   SER A 268       6.438 -49.903 -39.845  1.00 46.60           C  
ANISOU 1822  C   SER A 268     5496   5666   6544    731    978     -6       C  
ATOM   1823  O   SER A 268       6.516 -50.047 -38.618  1.00 42.11           O  
ANISOU 1823  O   SER A 268     4845   5058   6099    725    818    102       O  
ATOM   1824  CB  SER A 268       7.126 -47.592 -40.408  1.00 46.73           C  
ANISOU 1824  CB  SER A 268     5356   5929   6470    624   1109    110       C  
ATOM   1825  OG  SER A 268       6.675 -46.270 -40.607  1.00 45.57           O  
ANISOU 1825  OG  SER A 268     5238   5892   6185    505   1100    173       O  
ATOM   1826  N   LYS A 269       6.775 -50.858 -40.702  1.00 51.03           N  
ANISOU 1826  N   LYS A 269     6114   6138   7136    847   1128   -139       N  
ATOM   1827  CA  LYS A 269       7.386 -52.095 -40.218  1.00 54.06           C  
ANISOU 1827  CA  LYS A 269     6431   6352   7756    982   1122   -149       C  
ATOM   1828  C   LYS A 269       8.528 -51.716 -39.275  1.00 56.21           C  
ANISOU 1828  C   LYS A 269     6445   6667   8245   1036   1072      9       C  
ATOM   1829  O   LYS A 269       8.596 -52.178 -38.135  1.00 58.04           O  
ANISOU 1829  O   LYS A 269     6618   6823   8613   1064    907    114       O  
ATOM   1830  CB  LYS A 269       7.916 -52.960 -41.373  1.00 54.33           C  
ANISOU 1830  CB  LYS A 269     6522   6303   7819   1131   1342   -327       C  
ATOM   1831  CG  LYS A 269       8.588 -54.251 -40.906  1.00 58.10           C  
ANISOU 1831  CG  LYS A 269     6925   6576   8573   1293   1349   -336       C  
ATOM   1832  CD  LYS A 269       8.902 -55.226 -42.048  1.00 62.69           C  
ANISOU 1832  CD  LYS A 269     7610   7036   9172   1444   1559   -555       C  
ATOM   1833  CE  LYS A 269       9.625 -56.465 -41.530  0.00 64.83           C  
ANISOU 1833  CE  LYS A 269     7790   7083   9760   1622   1569   -546       C  
ATOM   1834  NZ  LYS A 269       8.800 -57.245 -40.567  0.00 64.57           N  
ANISOU 1834  NZ  LYS A 269     7850   6860   9823   1565   1354   -478       N  
ATOM   1835  N   ASP A 270       9.401 -50.844 -39.765  1.00 55.83           N  
ANISOU 1835  N   ASP A 270     6244   6746   8224   1045   1211     33       N  
ATOM   1836  CA  ASP A 270      10.602 -50.472 -39.057  1.00 55.44           C  
ANISOU 1836  CA  ASP A 270     5913   6738   8413   1094   1176    153       C  
ATOM   1837  C   ASP A 270      10.248 -49.481 -37.943  1.00 53.60           C  
ANISOU 1837  C   ASP A 270     5631   6594   8140    950    940    275       C  
ATOM   1838  O   ASP A 270       9.796 -48.384 -38.225  1.00 51.67           O  
ANISOU 1838  O   ASP A 270     5435   6452   7745    818    951    284       O  
ATOM   1839  CB  ASP A 270      11.570 -49.857 -40.057  1.00 57.47           C  
ANISOU 1839  CB  ASP A 270     6021   7090   8726   1131   1433    134       C  
ATOM   1840  CG  ASP A 270      12.904 -49.495 -39.449  1.00 63.29           C  
ANISOU 1840  CG  ASP A 270     6419   7864   9763   1178   1413    244       C  
ATOM   1841  OD1 ASP A 270      13.040 -49.526 -38.209  1.00 69.81           O  
ANISOU 1841  OD1 ASP A 270     7139   8674  10711   1166   1161    334       O  
ATOM   1842  OD2 ASP A 270      13.820 -49.159 -40.226  1.00 71.84           O  
ANISOU 1842  OD2 ASP A 270     7336   9003  10956   1227   1652    243       O  
ATOM   1843  N   PRO A 271      10.445 -49.867 -36.671  1.00 54.99           N  
ANISOU 1843  N   PRO A 271     5726   6728   8441    990    725    369       N  
ATOM   1844  CA  PRO A 271      10.127 -48.999 -35.530  1.00 54.33           C  
ANISOU 1844  CA  PRO A 271     5616   6732   8294    877    492    463       C  
ATOM   1845  C   PRO A 271      10.829 -47.657 -35.521  1.00 56.33           C  
ANISOU 1845  C   PRO A 271     5677   7106   8618    788    488    490       C  
ATOM   1846  O   PRO A 271      10.254 -46.666 -35.049  1.00 56.73           O  
ANISOU 1846  O   PRO A 271     5783   7229   8543    655    367    510       O  
ATOM   1847  CB  PRO A 271      10.609 -49.812 -34.327  1.00 54.46           C  
ANISOU 1847  CB  PRO A 271     5542   6690   8461    995    302    561       C  
ATOM   1848  CG  PRO A 271      10.582 -51.176 -34.773  1.00 56.22           C  
ANISOU 1848  CG  PRO A 271     5845   6755   8762   1129    413    524       C  
ATOM   1849  CD  PRO A 271      10.957 -51.163 -36.210  1.00 54.55           C  
ANISOU 1849  CD  PRO A 271     5614   6536   8575   1159    686    397       C  
ATOM   1850  N   SER A 272      12.068 -47.618 -36.009  1.00 59.10           N  
ANISOU 1850  N   SER A 272     5791   7468   9194    860    625    490       N  
ATOM   1851  CA  SER A 272      12.836 -46.367 -36.004  1.00 60.39           C  
ANISOU 1851  CA  SER A 272     5731   7722   9491    763    631    524       C  
ATOM   1852  C   SER A 272      12.255 -45.326 -36.973  1.00 60.04           C  
ANISOU 1852  C   SER A 272     5808   7728   9277    626    804    499       C  
ATOM   1853  O   SER A 272      12.555 -44.138 -36.852  1.00 63.13           O  
ANISOU 1853  O   SER A 272     6077   8170   9741    505    778    535       O  
ATOM   1854  CB  SER A 272      14.299 -46.644 -36.333  1.00 62.46           C  
ANISOU 1854  CB  SER A 272     5682   7978  10070    876    763    543       C  
ATOM   1855  OG  SER A 272      14.388 -47.580 -37.378  1.00 64.92           O  
ANISOU 1855  OG  SER A 272     6067   8228  10371   1011   1025    484       O  
ATOM   1856  N   GLN A 273      11.435 -45.785 -37.924  1.00 58.27           N  
ANISOU 1856  N   GLN A 273     5822   7482   8836    650    966    436       N  
ATOM   1857  CA  GLN A 273      10.740 -44.910 -38.876  1.00 57.07           C  
ANISOU 1857  CA  GLN A 273     5826   7385   8474    547   1109    425       C  
ATOM   1858  C   GLN A 273       9.460 -44.305 -38.298  1.00 51.85           C  
ANISOU 1858  C   GLN A 273     5353   6743   7605    423    915    433       C  
ATOM   1859  O   GLN A 273       8.906 -43.355 -38.847  1.00 49.17           O  
ANISOU 1859  O   GLN A 273     5108   6449   7125    328    979    451       O  
ATOM   1860  CB  GLN A 273      10.429 -45.666 -40.175  1.00 57.97           C  
ANISOU 1860  CB  GLN A 273     6115   7486   8424    639   1342    336       C  
ATOM   1861  CG  GLN A 273      11.608 -45.725 -41.146  1.00 66.15           C  
ANISOU 1861  CG  GLN A 273     6989   8547   9597    736   1639    338       C  
ATOM   1862  CD  GLN A 273      11.366 -46.684 -42.290  1.00 69.18           C  
ANISOU 1862  CD  GLN A 273     7562   8910   9811    864   1846    213       C  
ATOM   1863  OE1 GLN A 273      10.250 -46.794 -42.798  1.00 79.45           O  
ANISOU 1863  OE1 GLN A 273     9132  10223  10833    830   1822    138       O  
ATOM   1864  NE2 GLN A 273      12.412 -47.394 -42.699  1.00 83.73           N  
ANISOU 1864  NE2 GLN A 273     9262  10721  11831   1020   2043    176       N  
ATOM   1865  N   ARG A 274       8.991 -44.838 -37.177  1.00 50.07           N  
ANISOU 1865  N   ARG A 274     5179   6482   7363    434    690    435       N  
ATOM   1866  CA  ARG A 274       7.810 -44.275 -36.528  1.00 45.67           C  
ANISOU 1866  CA  ARG A 274     4778   5948   6624    331    523    446       C  
ATOM   1867  C   ARG A 274       8.177 -42.998 -35.791  1.00 41.72           C  
ANISOU 1867  C   ARG A 274     4149   5493   6209    232    400    488       C  
ATOM   1868  O   ARG A 274       9.258 -42.896 -35.228  1.00 41.02           O  
ANISOU 1868  O   ARG A 274     3847   5408   6331    253    325    510       O  
ATOM   1869  CB  ARG A 274       7.211 -45.282 -35.560  1.00 44.50           C  
ANISOU 1869  CB  ARG A 274     4728   5750   6428    382    356    453       C  
ATOM   1870  CG  ARG A 274       6.746 -46.546 -36.236  1.00 46.66           C  
ANISOU 1870  CG  ARG A 274     5139   5941   6648    459    458    396       C  
ATOM   1871  CD  ARG A 274       6.278 -47.572 -35.222  1.00 46.25           C  
ANISOU 1871  CD  ARG A 274     5157   5810   6605    508    310    437       C  
ATOM   1872  NE  ARG A 274       6.341 -48.908 -35.806  1.00 49.15           N  
ANISOU 1872  NE  ARG A 274     5583   6052   7040    609    412    379       N  
ATOM   1873  CZ  ARG A 274       6.452 -50.029 -35.108  1.00 49.13           C  
ANISOU 1873  CZ  ARG A 274     5584   5936   7148    701    339    429       C  
ATOM   1874  NH1 ARG A 274       6.455 -50.002 -33.776  1.00 47.27           N  
ANISOU 1874  NH1 ARG A 274     5312   5720   6928    710    158    553       N  
ATOM   1875  NH2 ARG A 274       6.535 -51.185 -35.746  1.00 48.66           N  
ANISOU 1875  NH2 ARG A 274     5580   5735   7174    791    448    355       N  
ATOM   1876  N   PRO A 275       7.274 -42.018 -35.782  1.00 40.77           N  
ANISOU 1876  N   PRO A 275     4150   5399   5940    127    364    491       N  
ATOM   1877  CA  PRO A 275       7.543 -40.853 -34.970  1.00 42.09           C  
ANISOU 1877  CA  PRO A 275     4219   5582   6192     36    224    502       C  
ATOM   1878  C   PRO A 275       7.473 -41.197 -33.501  1.00 42.19           C  
ANISOU 1878  C   PRO A 275     4229   5609   6192     67    -25    492       C  
ATOM   1879  O   PRO A 275       6.857 -42.183 -33.129  1.00 45.55           O  
ANISOU 1879  O   PRO A 275     4779   6030   6499    137    -75    502       O  
ATOM   1880  CB  PRO A 275       6.373 -39.941 -35.291  1.00 40.32           C  
ANISOU 1880  CB  PRO A 275     4169   5366   5784    -49    249    503       C  
ATOM   1881  CG  PRO A 275       5.283 -40.868 -35.626  1.00 40.16           C  
ANISOU 1881  CG  PRO A 275     4343   5354   5563      3    279    487       C  
ATOM   1882  CD  PRO A 275       5.964 -41.918 -36.439  1.00 39.59           C  
ANISOU 1882  CD  PRO A 275     4223   5263   5557     93    426    474       C  
ATOM   1883  N   SER A 276       8.090 -40.369 -32.677  1.00 45.45           N  
ANISOU 1883  N   SER A 276     4508   6036   6724     13   -182    473       N  
ATOM   1884  CA  SER A 276       7.916 -40.437 -31.243  1.00 45.26           C  
ANISOU 1884  CA  SER A 276     4520   6051   6624     38   -435    452       C  
ATOM   1885  C   SER A 276       6.551 -39.894 -30.907  1.00 44.86           C  
ANISOU 1885  C   SER A 276     4692   6016   6338    -12   -466    430       C  
ATOM   1886  O   SER A 276       5.973 -39.122 -31.661  1.00 47.84           O  
ANISOU 1886  O   SER A 276     5138   6367   6672    -87   -342    421       O  
ATOM   1887  CB  SER A 276       8.967 -39.597 -30.546  1.00 44.58           C  
ANISOU 1887  CB  SER A 276     4229   5978   6730    -16   -610    403       C  
ATOM   1888  OG  SER A 276       8.870 -38.256 -30.984  1.00 46.83           O  
ANISOU 1888  OG  SER A 276     4496   6218   7079   -149   -546    362       O  
ATOM   1889  N   MET A 277       6.053 -40.300 -29.754  1.00 48.00           N  
ANISOU 1889  N   MET A 277     5195   6460   6583     43   -627    435       N  
ATOM   1890  CA  MET A 277       4.778 -39.848 -29.233  1.00 45.69           C  
ANISOU 1890  CA  MET A 277     5096   6195   6071     17   -657    416       C  
ATOM   1891  C   MET A 277       4.852 -38.338 -29.024  1.00 45.83           C  
ANISOU 1891  C   MET A 277     5086   6200   6127    -78   -721    325       C  
ATOM   1892  O   MET A 277       3.924 -37.611 -29.400  1.00 45.67           O  
ANISOU 1892  O   MET A 277     5175   6154   6022   -130   -634    308       O  
ATOM   1893  CB  MET A 277       4.462 -40.603 -27.923  1.00 49.07           C  
ANISOU 1893  CB  MET A 277     5619   6686   6338    111   -808    457       C  
ATOM   1894  CG  MET A 277       2.987 -40.825 -27.598  1.00 50.57           C  
ANISOU 1894  CG  MET A 277     6012   6899   6303    123   -751    496       C  
ATOM   1895  SD  MET A 277       1.961 -41.517 -28.925  1.00 46.84           S  
ANISOU 1895  SD  MET A 277     5617   6358   5821     95   -524    546       S  
ATOM   1896  CE  MET A 277       1.848 -43.241 -28.515  1.00 41.36           C  
ANISOU 1896  CE  MET A 277     4969   5633   5111    192   -522    660       C  
ATOM   1897  N   GLU A 278       5.973 -37.838 -28.499  1.00 47.41           N  
ANISOU 1897  N   GLU A 278     5126   6401   6487   -104   -873    263       N  
ATOM   1898  CA  GLU A 278       6.108 -36.385 -28.311  1.00 48.49           C  
ANISOU 1898  CA  GLU A 278     5228   6488   6707   -210   -941    157       C  
ATOM   1899  C   GLU A 278       5.874 -35.640 -29.616  1.00 46.32           C  
ANISOU 1899  C   GLU A 278     4941   6121   6537   -299   -722    191       C  
ATOM   1900  O   GLU A 278       5.205 -34.614 -29.624  1.00 49.06           O  
ANISOU 1900  O   GLU A 278     5383   6415   6842   -356   -703    146       O  
ATOM   1901  CB  GLU A 278       7.445 -35.968 -27.704  1.00 51.69           C  
ANISOU 1901  CB  GLU A 278     5422   6890   7327   -249  -1142     74       C  
ATOM   1902  CG  GLU A 278       7.497 -35.976 -26.150  1.00 64.64           C  
ANISOU 1902  CG  GLU A 278     7126   8622   8812   -188  -1434    -22       C  
ATOM   1903  CD  GLU A 278       6.369 -35.170 -25.418  1.00 71.82           C  
ANISOU 1903  CD  GLU A 278     8267   9541   9480   -194  -1485   -124       C  
ATOM   1904  OE1 GLU A 278       5.538 -34.467 -26.073  1.00 65.95           O  
ANISOU 1904  OE1 GLU A 278     7617   8717   8722   -254  -1314   -126       O  
ATOM   1905  OE2 GLU A 278       6.342 -35.251 -24.155  1.00 58.25           O  
ANISOU 1905  OE2 GLU A 278     6637   7920   7577   -122  -1700   -200       O  
ATOM   1906  N   GLU A 279       6.387 -36.173 -30.717  1.00 45.04           N  
ANISOU 1906  N   GLU A 279     4678   5941   6493   -294   -548    276       N  
ATOM   1907  CA  GLU A 279       6.131 -35.579 -32.013  1.00 44.31           C  
ANISOU 1907  CA  GLU A 279     4603   5786   6446   -355   -325    335       C  
ATOM   1908  C   GLU A 279       4.670 -35.707 -32.406  1.00 40.32           C  
ANISOU 1908  C   GLU A 279     4323   5302   5694   -321   -236    369       C  
ATOM   1909  O   GLU A 279       4.107 -34.760 -32.919  1.00 38.25           O  
ANISOU 1909  O   GLU A 279     4129   4989   5416   -373   -156    386       O  
ATOM   1910  CB  GLU A 279       7.016 -36.182 -33.086  1.00 44.59           C  
ANISOU 1910  CB  GLU A 279     4498   5820   6626   -334   -144    411       C  
ATOM   1911  CG  GLU A 279       6.576 -35.836 -34.502  1.00 48.55           C  
ANISOU 1911  CG  GLU A 279     5078   6294   7075   -357    105    493       C  
ATOM   1912  CD  GLU A 279       7.626 -36.120 -35.557  1.00 53.26           C  
ANISOU 1912  CD  GLU A 279     5517   6885   7834   -347    313    561       C  
ATOM   1913  OE1 GLU A 279       8.666 -36.756 -35.236  1.00 70.22           O  
ANISOU 1913  OE1 GLU A 279     7480   9049  10150   -308    274    545       O  
ATOM   1914  OE2 GLU A 279       7.397 -35.700 -36.718  1.00 53.50           O  
ANISOU 1914  OE2 GLU A 279     5610   6903   7816   -364    523    640       O  
ATOM   1915  N   ILE A 280       4.057 -36.867 -32.182  1.00 39.94           N  
ANISOU 1915  N   ILE A 280     4377   5319   5479   -237   -252    387       N  
ATOM   1916  CA  ILE A 280       2.628 -37.022 -32.491  1.00 40.07           C  
ANISOU 1916  CA  ILE A 280     4576   5358   5291   -216   -189    411       C  
ATOM   1917  C   ILE A 280       1.786 -36.006 -31.728  1.00 41.70           C  
ANISOU 1917  C   ILE A 280     4876   5555   5413   -242   -276    364       C  
ATOM   1918  O   ILE A 280       0.880 -35.397 -32.290  1.00 44.86           O  
ANISOU 1918  O   ILE A 280     5362   5935   5747   -259   -197    386       O  
ATOM   1919  CB  ILE A 280       2.074 -38.399 -32.140  1.00 39.95           C  
ANISOU 1919  CB  ILE A 280     4641   5390   5148   -139   -214    434       C  
ATOM   1920  CG1 ILE A 280       2.653 -39.478 -33.047  1.00 38.53           C  
ANISOU 1920  CG1 ILE A 280     4409   5197   5033    -97   -104    464       C  
ATOM   1921  CG2 ILE A 280       0.557 -38.395 -32.281  1.00 39.81           C  
ANISOU 1921  CG2 ILE A 280     4775   5392   4958   -139   -177    449       C  
ATOM   1922  CD1 ILE A 280       2.447 -40.875 -32.486  1.00 39.00           C  
ANISOU 1922  CD1 ILE A 280     4513   5263   5044    -21   -155    485       C  
ATOM   1923  N   VAL A 281       2.089 -35.820 -30.453  1.00 40.98           N  
ANISOU 1923  N   VAL A 281     4769   5483   5318   -230   -441    293       N  
ATOM   1924  CA  VAL A 281       1.371 -34.834 -29.656  1.00 40.60           C  
ANISOU 1924  CA  VAL A 281     4818   5424   5186   -239   -518    217       C  
ATOM   1925  C   VAL A 281       1.468 -33.462 -30.271  1.00 37.78           C  
ANISOU 1925  C   VAL A 281     4429   4956   4969   -320   -460    193       C  
ATOM   1926  O   VAL A 281       0.486 -32.736 -30.309  1.00 39.84           O  
ANISOU 1926  O   VAL A 281     4795   5184   5160   -314   -420    183       O  
ATOM   1927  CB  VAL A 281       1.931 -34.744 -28.203  1.00 40.62           C  
ANISOU 1927  CB  VAL A 281     4806   5467   5158   -213   -727    115       C  
ATOM   1928  CG1 VAL A 281       1.423 -33.520 -27.503  1.00 36.80           C  
ANISOU 1928  CG1 VAL A 281     4411   4945   4625   -229   -797     -4       C  
ATOM   1929  CG2 VAL A 281       1.528 -35.959 -27.428  1.00 42.36           C  
ANISOU 1929  CG2 VAL A 281     5110   5795   5191   -115   -774    167       C  
ATOM   1930  N   LYS A 282       2.661 -33.092 -30.703  1.00 38.07           N  
ANISOU 1930  N   LYS A 282     4312   4926   5225   -391   -451    193       N  
ATOM   1931  CA  LYS A 282       2.891 -31.743 -31.192  1.00 42.29           C  
ANISOU 1931  CA  LYS A 282     4803   5327   5939   -481   -396    184       C  
ATOM   1932  C   LYS A 282       2.089 -31.563 -32.484  1.00 42.18           C  
ANISOU 1932  C   LYS A 282     4872   5291   5862   -470   -197    313       C  
ATOM   1933  O   LYS A 282       1.288 -30.638 -32.594  1.00 41.60           O  
ANISOU 1933  O   LYS A 282     4892   5148   5767   -474   -168    317       O  
ATOM   1934  CB  LYS A 282       4.400 -31.449 -31.374  1.00 42.48           C  
ANISOU 1934  CB  LYS A 282     4610   5281   6250   -571   -414    175       C  
ATOM   1935  CG  LYS A 282       4.799 -30.036 -30.888  1.00 47.88           C  
ANISOU 1935  CG  LYS A 282     5236   5814   7144   -676   -513     66       C  
ATOM   1936  CD  LYS A 282       6.311 -29.844 -30.739  1.00 57.58           C  
ANISOU 1936  CD  LYS A 282     6214   6985   8679   -775   -595     23       C  
ATOM   1937  CE  LYS A 282       6.782 -28.384 -31.075  1.00 62.54           C  
ANISOU 1937  CE  LYS A 282     6742   7401   9621   -922   -552      7       C  
ATOM   1938  NZ  LYS A 282       8.290 -28.219 -30.984  1.00 54.58           N  
ANISOU 1938  NZ  LYS A 282     5442   6332   8963  -1038   -624    -27       N  
ATOM   1939  N   ILE A 283       2.260 -32.491 -33.421  1.00 41.54           N  
ANISOU 1939  N   ILE A 283     4769   5278   5736   -440    -73    409       N  
ATOM   1940  CA  ILE A 283       1.525 -32.484 -34.666  1.00 42.74           C  
ANISOU 1940  CA  ILE A 283     5013   5444   5782   -415     88    519       C  
ATOM   1941  C   ILE A 283       0.007 -32.384 -34.420  1.00 44.95           C  
ANISOU 1941  C   ILE A 283     5448   5759   5872   -360     47    510       C  
ATOM   1942  O   ILE A 283      -0.695 -31.555 -35.040  1.00 44.51           O  
ANISOU 1942  O   ILE A 283     5461   5656   5794   -355    113    574       O  
ATOM   1943  CB  ILE A 283       1.853 -33.779 -35.508  1.00 46.10           C  
ANISOU 1943  CB  ILE A 283     5420   5960   6136   -367    191    570       C  
ATOM   1944  CG1 ILE A 283       3.182 -33.617 -36.269  1.00 49.98           C  
ANISOU 1944  CG1 ILE A 283     5763   6412   6814   -409    327    629       C  
ATOM   1945  CG2 ILE A 283       0.749 -34.115 -36.529  1.00 40.17           C  
ANISOU 1945  CG2 ILE A 283     4811   5269   5183   -316    282    634       C  
ATOM   1946  CD1 ILE A 283       3.723 -34.901 -36.808  1.00 42.94           C  
ANISOU 1946  CD1 ILE A 283     4830   5595   5889   -348    412    638       C  
ATOM   1947  N   MET A 284      -0.499 -33.256 -33.553  1.00 40.05           N  
ANISOU 1947  N   MET A 284     4872   5219   5125   -310    -50    450       N  
ATOM   1948  CA  MET A 284      -1.933 -33.351 -33.341  1.00 39.62           C  
ANISOU 1948  CA  MET A 284     4931   5213   4910   -257    -64    453       C  
ATOM   1949  C   MET A 284      -2.488 -32.103 -32.678  1.00 41.87           C  
ANISOU 1949  C   MET A 284     5262   5428   5218   -253   -109    401       C  
ATOM   1950  O   MET A 284      -3.576 -31.640 -33.012  1.00 44.27           O  
ANISOU 1950  O   MET A 284     5633   5727   5463   -215    -68    441       O  
ATOM   1951  CB  MET A 284      -2.265 -34.577 -32.511  1.00 38.24           C  
ANISOU 1951  CB  MET A 284     4782   5127   4623   -212   -131    424       C  
ATOM   1952  CG  MET A 284      -2.127 -35.893 -33.262  1.00 35.29           C  
ANISOU 1952  CG  MET A 284     4395   4799   4213   -199    -75    470       C  
ATOM   1953  SD  MET A 284      -3.406 -36.200 -34.490  1.00 42.92           S  
ANISOU 1953  SD  MET A 284     5439   5805   5065   -184      4    526       S  
ATOM   1954  CE  MET A 284      -4.891 -36.330 -33.485  1.00 50.55           C  
ANISOU 1954  CE  MET A 284     6457   6814   5936   -152    -55    517       C  
ATOM   1955  N   THR A 285      -1.738 -31.559 -31.735  1.00 43.34           N  
ANISOU 1955  N   THR A 285     5410   5558   5500   -283   -204    301       N  
ATOM   1956  CA  THR A 285      -2.062 -30.253 -31.168  1.00 44.51           C  
ANISOU 1956  CA  THR A 285     5603   5602   5708   -286   -244    220       C  
ATOM   1957  C   THR A 285      -2.227 -29.211 -32.274  1.00 44.84           C  
ANISOU 1957  C   THR A 285     5645   5520   5872   -316   -134    313       C  
ATOM   1958  O   THR A 285      -3.173 -28.432 -32.267  1.00 47.47           O  
ANISOU 1958  O   THR A 285     6053   5796   6188   -268   -109    317       O  
ATOM   1959  CB  THR A 285      -0.954 -29.785 -30.221  1.00 44.75           C  
ANISOU 1959  CB  THR A 285     5569   5569   5864   -341   -379     82       C  
ATOM   1960  OG1 THR A 285      -0.723 -30.796 -29.225  1.00 45.08           O  
ANISOU 1960  OG1 THR A 285     5617   5741   5772   -297   -492     23       O  
ATOM   1961  CG2 THR A 285      -1.330 -28.480 -29.567  1.00 41.08           C  
ANISOU 1961  CG2 THR A 285     5173   4982   5455   -338   -431    -41       C  
ATOM   1962  N   HIS A 286      -1.306 -29.210 -33.229  1.00 43.96           N  
ANISOU 1962  N   HIS A 286     5450   5369   5885   -381    -54    402       N  
ATOM   1963  CA  HIS A 286      -1.379 -28.265 -34.330  1.00 43.44           C  
ANISOU 1963  CA  HIS A 286     5393   5190   5921   -404     71    530       C  
ATOM   1964  C   HIS A 286      -2.612 -28.488 -35.170  1.00 41.01           C  
ANISOU 1964  C   HIS A 286     5184   4963   5435   -318    140    643       C  
ATOM   1965  O   HIS A 286      -3.329 -27.543 -35.405  1.00 47.79           O  
ANISOU 1965  O   HIS A 286     6101   5735   6321   -282    166    695       O  
ATOM   1966  CB  HIS A 286      -0.103 -28.254 -35.179  1.00 44.68           C  
ANISOU 1966  CB  HIS A 286     5435   5302   6238   -486    175    621       C  
ATOM   1967  CG  HIS A 286       1.103 -27.763 -34.434  1.00 52.94           C  
ANISOU 1967  CG  HIS A 286     6348   6236   7530   -588     97    517       C  
ATOM   1968  ND1 HIS A 286       1.017 -26.870 -33.383  1.00 55.93           N  
ANISOU 1968  ND1 HIS A 286     6743   6495   8014   -617    -36    370       N  
ATOM   1969  CD2 HIS A 286       2.421 -28.051 -34.575  1.00 54.64           C  
ANISOU 1969  CD2 HIS A 286     6400   6444   7916   -665    119    524       C  
ATOM   1970  CE1 HIS A 286       2.227 -26.636 -32.909  1.00 57.29           C  
ANISOU 1970  CE1 HIS A 286     6768   6591   8408   -718   -116    282       C  
ATOM   1971  NE2 HIS A 286       3.098 -27.331 -33.621  1.00 54.04           N  
ANISOU 1971  NE2 HIS A 286     6231   6247   8055   -750    -21    384       N  
ATOM   1972  N   LEU A 287      -2.903 -29.723 -35.571  1.00 38.53           N  
ANISOU 1972  N   LEU A 287     4885   4803   4952   -281    152    671       N  
ATOM   1973  CA  LEU A 287      -4.069 -29.988 -36.419  1.00 36.95           C  
ANISOU 1973  CA  LEU A 287     4761   4687   4589   -210    185    761       C  
ATOM   1974  C   LEU A 287      -5.396 -29.627 -35.796  1.00 39.12           C  
ANISOU 1974  C   LEU A 287     5086   4968   4808   -141    121    726       C  
ATOM   1975  O   LEU A 287      -6.327 -29.295 -36.517  1.00 44.41           O  
ANISOU 1975  O   LEU A 287     5799   5657   5418    -82    141    816       O  
ATOM   1976  CB  LEU A 287      -4.125 -31.437 -36.842  1.00 33.76           C  
ANISOU 1976  CB  LEU A 287     4360   4426   4040   -196    187    755       C  
ATOM   1977  CG  LEU A 287      -3.004 -31.880 -37.770  1.00 38.01           C  
ANISOU 1977  CG  LEU A 287     4864   4982   4597   -229    288    805       C  
ATOM   1978  CD1 LEU A 287      -3.063 -33.375 -37.873  1.00 38.89           C  
ANISOU 1978  CD1 LEU A 287     4982   5203   4593   -208    267    749       C  
ATOM   1979  CD2 LEU A 287      -3.101 -31.211 -39.185  1.00 31.93           C  
ANISOU 1979  CD2 LEU A 287     4153   4204   3776   -205    405    954       C  
ATOM   1980  N   MET A 288      -5.486 -29.688 -34.470  1.00 40.29           N  
ANISOU 1980  N   MET A 288     5228   5112   4969   -137     47    599       N  
ATOM   1981  CA  MET A 288      -6.719 -29.356 -33.747  1.00 40.29           C  
ANISOU 1981  CA  MET A 288     5268   5124   4918    -59     16    555       C  
ATOM   1982  C   MET A 288      -7.231 -27.955 -34.026  1.00 41.92           C  
ANISOU 1982  C   MET A 288     5506   5198   5225    -12     48    598       C  
ATOM   1983  O   MET A 288      -8.382 -27.652 -33.751  1.00 46.76           O  
ANISOU 1983  O   MET A 288     6137   5824   5804     75     47    596       O  
ATOM   1984  CB  MET A 288      -6.525 -29.493 -32.227  1.00 37.78           C  
ANISOU 1984  CB  MET A 288     4959   4817   4580    -53    -52    407       C  
ATOM   1985  CG  MET A 288      -6.497 -30.927 -31.681  1.00 40.19           C  
ANISOU 1985  CG  MET A 288     5251   5261   4758    -56    -85    387       C  
ATOM   1986  SD  MET A 288      -7.657 -32.095 -32.397  1.00 41.52           S  
ANISOU 1986  SD  MET A 288     5405   5556   4814    -29    -45    488       S  
ATOM   1987  CE  MET A 288      -9.203 -31.429 -31.810  1.00 40.22           C  
ANISOU 1987  CE  MET A 288     5256   5404   4622     66    -18    480       C  
ATOM   1988  N   ARG A 289      -6.368 -27.089 -34.529  1.00 45.79           N  
ANISOU 1988  N   ARG A 289     5990   5546   5862    -65     87    643       N  
ATOM   1989  CA  ARG A 289      -6.787 -25.767 -35.010  1.00 47.68           C  
ANISOU 1989  CA  ARG A 289     6266   5629   6222    -20    134    728       C  
ATOM   1990  C   ARG A 289      -7.906 -25.899 -36.000  1.00 46.60           C  
ANISOU 1990  C   ARG A 289     6153   5583   5970     72    158    878       C  
ATOM   1991  O   ARG A 289      -8.772 -25.037 -36.065  1.00 50.41           O  
ANISOU 1991  O   ARG A 289     6661   5987   6505    163    165    927       O  
ATOM   1992  CB  ARG A 289      -5.639 -25.064 -35.728  1.00 48.12           C  
ANISOU 1992  CB  ARG A 289     6301   5536   6448   -108    206    820       C  
ATOM   1993  CG  ARG A 289      -5.894 -23.604 -35.987  1.00 52.72           C  
ANISOU 1993  CG  ARG A 289     6922   5898   7209    -75    254    897       C  
ATOM   1994  CD  ARG A 289      -4.666 -22.943 -36.589  1.00 60.62           C  
ANISOU 1994  CD  ARG A 289     7884   6733   8417   -187    343    995       C  
ATOM   1995  NE  ARG A 289      -5.023 -21.764 -37.370  1.00 67.76           N  
ANISOU 1995  NE  ARG A 289     8842   7458   9446   -138    430   1178       N  
ATOM   1996  CZ  ARG A 289      -5.304 -20.571 -36.848  1.00 75.78           C  
ANISOU 1996  CZ  ARG A 289     9890   8238  10667   -113    417   1127       C  
ATOM   1997  NH1 ARG A 289      -5.309 -20.377 -35.528  1.00 80.67           N  
ANISOU 1997  NH1 ARG A 289    10504   8787  11360   -128    316    874       N  
ATOM   1998  NH2 ARG A 289      -5.609 -19.564 -37.655  1.00 75.08           N  
ANISOU 1998  NH2 ARG A 289     9851   7978  10697    -59    507   1331       N  
ATOM   1999  N   TYR A 290      -7.853 -26.972 -36.788  1.00 44.33           N  
ANISOU 1999  N   TYR A 290     5855   5454   5534     53    161    943       N  
ATOM   2000  CA  TYR A 290      -8.791 -27.213 -37.878  1.00 44.16           C  
ANISOU 2000  CA  TYR A 290     5856   5542   5381    127    151   1073       C  
ATOM   2001  C   TYR A 290      -9.953 -28.162 -37.492  1.00 43.19           C  
ANISOU 2001  C   TYR A 290     5694   5574   5142    173     72   1008       C  
ATOM   2002  O   TYR A 290     -10.753 -28.576 -38.353  1.00 44.18           O  
ANISOU 2002  O   TYR A 290     5816   5813   5158    219     27   1083       O  
ATOM   2003  CB  TYR A 290      -7.978 -27.717 -39.076  1.00 39.93           C  
ANISOU 2003  CB  TYR A 290     5347   5072   4754     81    209   1171       C  
ATOM   2004  CG  TYR A 290      -6.834 -26.779 -39.320  1.00 39.31           C  
ANISOU 2004  CG  TYR A 290     5275   4829   4831     24    313   1246       C  
ATOM   2005  CD1 TYR A 290      -7.062 -25.500 -39.789  1.00 37.79           C  
ANISOU 2005  CD1 TYR A 290     5125   4495   4740     73    364   1390       C  
ATOM   2006  CD2 TYR A 290      -5.533 -27.134 -39.009  1.00 44.54           C  
ANISOU 2006  CD2 TYR A 290     5884   5462   5578    -79    360   1177       C  
ATOM   2007  CE1 TYR A 290      -6.043 -24.604 -39.962  1.00 40.97           C  
ANISOU 2007  CE1 TYR A 290     5520   4716   5331      5    470   1467       C  
ATOM   2008  CE2 TYR A 290      -4.493 -26.244 -39.196  1.00 32.60           C  
ANISOU 2008  CE2 TYR A 290     4343   3786   4256   -148    458   1246       C  
ATOM   2009  CZ  TYR A 290      -4.743 -24.977 -39.670  1.00 39.94           C  
ANISOU 2009  CZ  TYR A 290     5318   4561   5295   -116    519   1392       C  
ATOM   2010  OH  TYR A 290      -3.697 -24.073 -39.874  1.00 40.71           O  
ANISOU 2010  OH  TYR A 290     5375   4468   5623   -202    632   1477       O  
ATOM   2011  N   PHE A 291     -10.046 -28.478 -36.200  1.00 40.05           N  
ANISOU 2011  N   PHE A 291     5266   5180   4773    159     53    871       N  
ATOM   2012  CA  PHE A 291     -11.071 -29.376 -35.679  1.00 37.69           C  
ANISOU 2012  CA  PHE A 291     4915   5008   4396    188     12    822       C  
ATOM   2013  C   PHE A 291     -11.696 -28.763 -34.431  1.00 38.45           C  
ANISOU 2013  C   PHE A 291     5000   5054   4556    256     32    741       C  
ATOM   2014  O   PHE A 291     -11.532 -29.273 -33.321  1.00 31.67           O  
ANISOU 2014  O   PHE A 291     4141   4229   3663    236     39    638       O  
ATOM   2015  CB  PHE A 291     -10.457 -30.741 -35.341  1.00 36.50           C  
ANISOU 2015  CB  PHE A 291     4753   4943   4174    104     -2    753       C  
ATOM   2016  CG  PHE A 291     -10.015 -31.492 -36.534  1.00 39.00           C  
ANISOU 2016  CG  PHE A 291     5083   5320   4414     59    -12    804       C  
ATOM   2017  CD1 PHE A 291     -10.940 -32.172 -37.309  1.00 37.72           C  
ANISOU 2017  CD1 PHE A 291     4899   5263   4169     76    -65    839       C  
ATOM   2018  CD2 PHE A 291      -8.679 -31.471 -36.930  1.00 40.61           C  
ANISOU 2018  CD2 PHE A 291     5317   5477   4636      3     34    810       C  
ATOM   2019  CE1 PHE A 291     -10.551 -32.837 -38.439  1.00 34.51           C  
ANISOU 2019  CE1 PHE A 291     4530   4917   3667     47    -78    859       C  
ATOM   2020  CE2 PHE A 291      -8.268 -32.135 -38.067  1.00 34.26           C  
ANISOU 2020  CE2 PHE A 291     4538   4735   3745    -19     53    850       C  
ATOM   2021  CZ  PHE A 291      -9.196 -32.823 -38.823  1.00 41.02           C  
ANISOU 2021  CZ  PHE A 291     5403   5698   4485      7     -5    865       C  
ATOM   2022  N   PRO A 292     -12.444 -27.672 -34.603  1.00 40.01           N  
ANISOU 2022  N   PRO A 292     5194   5174   4833    353     48    790       N  
ATOM   2023  CA  PRO A 292     -13.163 -27.137 -33.456  1.00 43.27           C  
ANISOU 2023  CA  PRO A 292     5595   5549   5295    442     87    701       C  
ATOM   2024  C   PRO A 292     -14.362 -28.024 -33.065  1.00 44.39           C  
ANISOU 2024  C   PRO A 292     5642   5848   5375    484     96    704       C  
ATOM   2025  O   PRO A 292     -14.819 -28.825 -33.862  1.00 43.54           O  
ANISOU 2025  O   PRO A 292     5469   5851   5225    454     46    785       O  
ATOM   2026  CB  PRO A 292     -13.627 -25.773 -33.960  1.00 42.53           C  
ANISOU 2026  CB  PRO A 292     5515   5315   5330    546    105    777       C  
ATOM   2027  CG  PRO A 292     -13.758 -25.946 -35.388  1.00 41.15           C  
ANISOU 2027  CG  PRO A 292     5322   5194   5120    539     58    942       C  
ATOM   2028  CD  PRO A 292     -12.689 -26.883 -35.811  1.00 42.85           C  
ANISOU 2028  CD  PRO A 292     5567   5477   5235    406     39    936       C  
ATOM   2029  N   GLY A 293     -14.841 -27.898 -31.837  1.00 45.44           N  
ANISOU 2029  N   GLY A 293     5770   5991   5504    549    163    611       N  
ATOM   2030  CA  GLY A 293     -16.044 -28.613 -31.415  1.00 45.83           C  
ANISOU 2030  CA  GLY A 293     5708   6173   5531    595    210    636       C  
ATOM   2031  C   GLY A 293     -15.811 -29.858 -30.576  1.00 44.37           C  
ANISOU 2031  C   GLY A 293     5527   6097   5237    520    240    595       C  
ATOM   2032  O   GLY A 293     -16.757 -30.546 -30.211  1.00 45.05           O  
ANISOU 2032  O   GLY A 293     5512   6284   5321    537    298    635       O  
ATOM   2033  N   ALA A 294     -14.559 -30.135 -30.241  1.00 42.98           N  
ANISOU 2033  N   ALA A 294     5452   5890   4986    441    206    530       N  
ATOM   2034  CA  ALA A 294     -14.215 -31.329 -29.479  1.00 42.30           C  
ANISOU 2034  CA  ALA A 294     5383   5893   4795    382    220    514       C  
ATOM   2035  C   ALA A 294     -14.715 -31.299 -28.014  1.00 41.17           C  
ANISOU 2035  C   ALA A 294     5271   5806   4564    469    328    457       C  
ATOM   2036  O   ALA A 294     -14.704 -32.297 -27.333  1.00 43.18           O  
ANISOU 2036  O   ALA A 294     5532   6147   4727    444    367    484       O  
ATOM   2037  CB  ALA A 294     -12.730 -31.509 -29.513  1.00 41.86           C  
ANISOU 2037  CB  ALA A 294     5413   5790   4702    298    143    463       C  
ATOM   2038  N   ASP A 295     -15.145 -30.140 -27.557  1.00 42.89           N  
ANISOU 2038  N   ASP A 295     5521   5970   4806    583    385    382       N  
ATOM   2039  CA  ASP A 295     -15.697 -29.933 -26.215  1.00 46.65           C  
ANISOU 2039  CA  ASP A 295     6043   6502   5180    699    511    310       C  
ATOM   2040  C   ASP A 295     -17.193 -30.275 -26.135  1.00 46.08           C  
ANISOU 2040  C   ASP A 295     5823   6525   5161    769    651    412       C  
ATOM   2041  O   ASP A 295     -17.792 -30.190 -25.067  1.00 46.18           O  
ANISOU 2041  O   ASP A 295     5854   6605   5088    875    799    380       O  
ATOM   2042  CB  ASP A 295     -15.529 -28.457 -25.841  1.00 48.01           C  
ANISOU 2042  CB  ASP A 295     6312   6546   5381    801    517    158       C  
ATOM   2043  CG  ASP A 295     -15.975 -27.506 -26.986  1.00 64.42           C  
ANISOU 2043  CG  ASP A 295     8315   8499   7662    834    490    211       C  
ATOM   2044  OD1 ASP A 295     -15.251 -27.407 -28.025  1.00 68.82           O  
ANISOU 2044  OD1 ASP A 295     8871   8977   8298    736    378    263       O  
ATOM   2045  OD2 ASP A 295     -17.059 -26.878 -26.865  1.00 81.57           O  
ANISOU 2045  OD2 ASP A 295    10424  10656   9911    968    590    217       O  
ATOM   2046  N   GLU A 296     -17.792 -30.635 -27.263  1.00 44.87           N  
ANISOU 2046  N   GLU A 296     5518   6383   5148    715    605    531       N  
ATOM   2047  CA  GLU A 296     -19.217 -30.956 -27.325  1.00 48.33           C  
ANISOU 2047  CA  GLU A 296     5768   6904   5690    763    706    632       C  
ATOM   2048  C   GLU A 296     -19.515 -32.385 -26.880  1.00 48.18           C  
ANISOU 2048  C   GLU A 296     5678   6994   5634    676    777    723       C  
ATOM   2049  O   GLU A 296     -19.022 -33.313 -27.491  1.00 49.24           O  
ANISOU 2049  O   GLU A 296     5805   7127   5776    542    671    769       O  
ATOM   2050  CB  GLU A 296     -19.715 -30.801 -28.764  1.00 49.29           C  
ANISOU 2050  CB  GLU A 296     5752   7001   5975    733    584    714       C  
ATOM   2051  CG  GLU A 296     -19.885 -29.357 -29.175  1.00 59.97           C  
ANISOU 2051  CG  GLU A 296     7124   8248   7414    858    560    682       C  
ATOM   2052  CD  GLU A 296     -20.872 -28.609 -28.272  1.00 69.56           C  
ANISOU 2052  CD  GLU A 296     8281   9467   8682   1034    731    645       C  
ATOM   2053  OE1 GLU A 296     -21.962 -29.165 -27.981  1.00 73.77           O  
ANISOU 2053  OE1 GLU A 296     8638  10110   9281   1064    836    718       O  
ATOM   2054  OE2 GLU A 296     -20.547 -27.473 -27.850  1.00 68.85           O  
ANISOU 2054  OE2 GLU A 296     8315   9260   8583   1141    767    536       O  
ATOM   2055  N   PRO A 297     -20.371 -32.571 -25.861  1.00 48.28           N  
ANISOU 2055  N   PRO A 297     5630   7090   5622    758    971    760       N  
ATOM   2056  CA  PRO A 297     -20.663 -33.926 -25.411  1.00 47.75           C  
ANISOU 2056  CA  PRO A 297     5495   7105   5542    670   1061    877       C  
ATOM   2057  C   PRO A 297     -21.440 -34.760 -26.422  1.00 48.60           C  
ANISOU 2057  C   PRO A 297     5376   7221   5867    550    996    989       C  
ATOM   2058  O   PRO A 297     -22.247 -34.226 -27.175  1.00 54.90           O  
ANISOU 2058  O   PRO A 297     6016   8015   6827    585    949    999       O  
ATOM   2059  CB  PRO A 297     -21.511 -33.701 -24.156  1.00 49.05           C  
ANISOU 2059  CB  PRO A 297     5636   7358   5643    810   1317    900       C  
ATOM   2060  CG  PRO A 297     -22.106 -32.391 -24.324  1.00 46.33           C  
ANISOU 2060  CG  PRO A 297     5242   6980   5382    957   1350    819       C  
ATOM   2061  CD  PRO A 297     -21.121 -31.569 -25.083  1.00 49.39           C  
ANISOU 2061  CD  PRO A 297     5762   7246   5756    939   1139    703       C  
ATOM   2062  N   LEU A 298     -21.189 -36.065 -26.431  1.00 47.92           N  
ANISOU 2062  N   LEU A 298     5278   7139   5791    412    979   1065       N  
ATOM   2063  CA  LEU A 298     -21.894 -36.988 -27.307  1.00 47.05           C  
ANISOU 2063  CA  LEU A 298     4962   7020   5893    278    907   1145       C  
ATOM   2064  C   LEU A 298     -23.344 -37.060 -26.868  1.00 48.94           C  
ANISOU 2064  C   LEU A 298     4963   7328   6305    318   1086   1245       C  
ATOM   2065  O   LEU A 298     -23.628 -37.440 -25.748  1.00 56.11           O  
ANISOU 2065  O   LEU A 298     5872   8283   7163    351   1305   1329       O  
ATOM   2066  CB  LEU A 298     -21.274 -38.386 -27.234  1.00 44.66           C  
ANISOU 2066  CB  LEU A 298     4717   6674   5576    134    880   1199       C  
ATOM   2067  CG  LEU A 298     -19.774 -38.565 -27.465  1.00 44.77           C  
ANISOU 2067  CG  LEU A 298     4950   6627   5432     96    744   1122       C  
ATOM   2068  CD1 LEU A 298     -19.417 -40.027 -27.244  1.00 42.83           C  
ANISOU 2068  CD1 LEU A 298     4724   6332   5217    -22    759   1204       C  
ATOM   2069  CD2 LEU A 298     -19.341 -38.138 -28.845  1.00 48.26           C  
ANISOU 2069  CD2 LEU A 298     5406   7025   5907     59    535   1028       C  
ATOM   2070  N   GLN A 299     -24.277 -36.677 -27.719  1.00 51.09           N  
ANISOU 2070  N   GLN A 299     5021   7614   6775    326   1004   1249       N  
ATOM   2071  CA  GLN A 299     -25.667 -36.680 -27.279  1.00 52.60           C  
ANISOU 2071  CA  GLN A 299     4948   7875   7163    374   1183   1346       C  
ATOM   2072  C   GLN A 299     -26.685 -37.071 -28.318  1.00 52.27           C  
ANISOU 2072  C   GLN A 299     4606   7842   7411    277   1040   1386       C  
ATOM   2073  O   GLN A 299     -27.869 -37.115 -28.012  1.00 55.42           O  
ANISOU 2073  O   GLN A 299     4738   8298   8021    304   1178   1473       O  
ATOM   2074  CB  GLN A 299     -26.020 -35.315 -26.712  1.00 53.42           C  
ANISOU 2074  CB  GLN A 299     5074   8017   7206    594   1321   1301       C  
ATOM   2075  CG  GLN A 299     -25.763 -34.185 -27.653  1.00 52.77           C  
ANISOU 2075  CG  GLN A 299     5045   7885   7118    677   1122   1204       C  
ATOM   2076  CD  GLN A 299     -25.818 -32.849 -26.959  1.00 54.92           C  
ANISOU 2076  CD  GLN A 299     5415   8148   7304    893   1262   1131       C  
ATOM   2077  OE1 GLN A 299     -24.867 -32.079 -27.028  1.00 65.85           O  
ANISOU 2077  OE1 GLN A 299     7030   9457   8535    944   1178   1025       O  
ATOM   2078  NE2 GLN A 299     -26.922 -32.570 -26.275  1.00 49.53           N  
ANISOU 2078  NE2 GLN A 299     4554   7532   6735   1019   1486   1182       N  
ATOM   2079  N   TYR A 300     -26.238 -37.389 -29.523  1.00 52.10           N  
ANISOU 2079  N   TYR A 300     4619   7774   7402    165    766   1321       N  
ATOM   2080  CA  TYR A 300     -27.145 -37.679 -30.619  1.00 55.79           C  
ANISOU 2080  CA  TYR A 300     4825   8262   8109     83    570   1326       C  
ATOM   2081  C   TYR A 300     -27.006 -39.127 -30.999  1.00 57.92           C  
ANISOU 2081  C   TYR A 300     5056   8472   8479   -137    472   1324       C  
ATOM   2082  O   TYR A 300     -25.892 -39.621 -31.119  1.00 57.46           O  
ANISOU 2082  O   TYR A 300     5234   8345   8254   -206    413   1269       O  
ATOM   2083  CB  TYR A 300     -26.829 -36.769 -31.823  1.00 53.48           C  
ANISOU 2083  CB  TYR A 300     4615   7975   7729    157    316   1243       C  
ATOM   2084  CG  TYR A 300     -26.863 -35.297 -31.463  1.00 51.39           C  
ANISOU 2084  CG  TYR A 300     4418   7726   7384    376    411   1241       C  
ATOM   2085  CD1 TYR A 300     -28.072 -34.641 -31.268  1.00 54.63           C  
ANISOU 2085  CD1 TYR A 300     4578   8194   7985    507    493   1301       C  
ATOM   2086  CD2 TYR A 300     -25.697 -34.577 -31.271  1.00 42.50           C  
ANISOU 2086  CD2 TYR A 300     3589   6540   6021    452    427   1175       C  
ATOM   2087  CE1 TYR A 300     -28.109 -33.302 -30.900  1.00 53.31           C  
ANISOU 2087  CE1 TYR A 300     4481   8012   7764    720    594   1288       C  
ATOM   2088  CE2 TYR A 300     -25.729 -33.228 -30.912  1.00 42.05           C  
ANISOU 2088  CE2 TYR A 300     3596   6461   5918    644    514   1157       C  
ATOM   2089  CZ  TYR A 300     -26.943 -32.606 -30.733  1.00 39.99           C  
ANISOU 2089  CZ  TYR A 300     3107   6246   5842    781    600   1210       C  
ATOM   2090  OH  TYR A 300     -26.986 -31.286 -30.376  1.00 51.76           O  
ANISOU 2090  OH  TYR A 300     4668   7689   7308    982    692   1179       O  
ATOM   2091  N   PRO A 301     -28.130 -39.815 -31.228  1.00 66.47           N  
ANISOU 2091  N   PRO A 301     5829   9566   9861   -250    444   1375       N  
ATOM   2092  CA  PRO A 301     -27.982 -41.214 -31.582  1.00 70.19           C  
ANISOU 2092  CA  PRO A 301     6272   9942  10454   -469    347   1355       C  
ATOM   2093  C   PRO A 301     -27.682 -41.304 -33.051  1.00 72.12           C  
ANISOU 2093  C   PRO A 301     6569  10176  10658   -533      1   1207       C  
ATOM   2094  O   PRO A 301     -27.725 -40.310 -33.769  1.00 72.73           O  
ANISOU 2094  O   PRO A 301     6669  10331  10635   -411   -152   1157       O  
ATOM   2095  CB  PRO A 301     -29.349 -41.810 -31.264  1.00 73.60           C  
ANISOU 2095  CB  PRO A 301     6328  10383  11255   -569    450   1461       C  
ATOM   2096  CG  PRO A 301     -30.280 -40.686 -31.479  1.00 73.12           C  
ANISOU 2096  CG  PRO A 301     6054  10443  11285   -416    425   1476       C  
ATOM   2097  CD  PRO A 301     -29.543 -39.397 -31.253  1.00 69.42           C  
ANISOU 2097  CD  PRO A 301     5851  10022  10504   -195    477   1442       C  
ATOM   2098  N   CYS A 302     -27.387 -42.504 -33.489  1.00 76.77           N  
ANISOU 2098  N   CYS A 302     7186  10664  11321   -714   -113   1142       N  
ATOM   2099  CA  CYS A 302     -26.760 -42.689 -34.765  1.00 79.28           C  
ANISOU 2099  CA  CYS A 302     7654  10962  11505   -760   -400    981       C  
ATOM   2100  C   CYS A 302     -27.155 -44.079 -35.209  1.00 82.05           C  
ANISOU 2100  C   CYS A 302     7869  11204  12103   -980   -528    909       C  
ATOM   2101  O   CYS A 302     -27.162 -45.014 -34.410  1.00 83.21           O  
ANISOU 2101  O   CYS A 302     7977  11232  12405  -1094   -351    986       O  
ATOM   2102  CB  CYS A 302     -25.248 -42.541 -34.572  1.00 75.11           C  
ANISOU 2102  CB  CYS A 302     7484  10388  10667   -694   -331    948       C  
ATOM   2103  SG  CYS A 302     -24.249 -42.911 -35.981  1.00 75.39           S  
ANISOU 2103  SG  CYS A 302     7746  10387  10512   -742   -597    764       S  
ATOM   2104  N   GLN A 303     -27.542 -44.210 -36.465  1.00 87.16           N  
ANISOU 2104  N   GLN A 303     8435  11885  12795  -1039   -837    766       N  
ATOM   2105  CA  GLN A 303     -27.926 -45.507 -36.989  1.00 94.61           C  
ANISOU 2105  CA  GLN A 303     9255  12712  13982  -1256  -1001    651       C  
ATOM   2106  C   GLN A 303     -27.261 -45.692 -38.344  1.00 97.38           C  
ANISOU 2106  C   GLN A 303     9818  13069  14113  -1267  -1297    435       C  
ATOM   2107  O   GLN A 303     -27.865 -46.173 -39.302  1.00100.93           O  
ANISOU 2107  O   GLN A 303    10138  13524  14686  -1374  -1579    282       O  
ATOM   2108  CB  GLN A 303     -29.454 -45.615 -37.054  1.00 98.00           C  
ANISOU 2108  CB  GLN A 303     9266  13185  14785  -1347  -1089    687       C  
ATOM   2109  CG  GLN A 303     -29.992 -46.970 -36.582  1.00104.85           C  
ANISOU 2109  CG  GLN A 303     9925  13871  16041  -1584  -1008    711       C  
ATOM   2110  CD  GLN A 303     -30.944 -46.850 -35.402  1.00110.24           C  
ANISOU 2110  CD  GLN A 303    10308  14569  17010  -1590   -711    939       C  
ATOM   2111  OE1 GLN A 303     -30.974 -45.826 -34.712  1.00111.66           O  
ANISOU 2111  OE1 GLN A 303    10505  14874  17046  -1400   -504   1078       O  
ATOM   2112  NE2 GLN A 303     -31.713 -47.908 -35.152  1.00111.94           N  
ANISOU 2112  NE2 GLN A 303    10248  14645  17638  -1808   -672    978       N  
ATOM   2113  N   HIS A 468     -25.992 -45.304 -38.395  1.00 98.52           N  
ANISOU 2113  N   HIS A 468    10289  13219  13927  -1151  -1224    419       N  
ATOM   2114  CA  HIS A 468     -25.193 -45.419 -39.597  1.00101.12           C  
ANISOU 2114  CA  HIS A 468    10857  13562  14001  -1131  -1435    237       C  
ATOM   2115  C   HIS A 468     -25.056 -46.896 -39.979  1.00106.46           C  
ANISOU 2115  C   HIS A 468    11556  14066  14828  -1320  -1538     67       C  
ATOM   2116  O   HIS A 468     -24.832 -47.758 -39.113  1.00106.36           O  
ANISOU 2116  O   HIS A 468    11535  13883  14993  -1419  -1350    127       O  
ATOM   2117  CB  HIS A 468     -23.798 -44.823 -39.365  1.00 98.88           C  
ANISOU 2117  CB  HIS A 468    10885  13287  13399   -990  -1272    281       C  
ATOM   2118  CG  HIS A 468     -22.863 -45.747 -38.641  1.00 98.52           C  
ANISOU 2118  CG  HIS A 468    10985  13073  13376  -1056  -1087    288       C  
ATOM   2119  ND1 HIS A 468     -23.153 -46.281 -37.402  1.00 97.27           N  
ANISOU 2119  ND1 HIS A 468    10709  12811  13436  -1126   -876    424       N  
ATOM   2120  CD2 HIS A 468     -21.658 -46.255 -38.997  1.00 94.46           C  
ANISOU 2120  CD2 HIS A 468    10716  12476  12698  -1052  -1080    187       C  
ATOM   2121  CE1 HIS A 468     -22.162 -47.065 -37.022  1.00 95.19           C  
ANISOU 2121  CE1 HIS A 468    10622  12409  13139  -1158   -766    415       C  
ATOM   2122  NE2 HIS A 468     -21.242 -47.066 -37.970  1.00 93.29           N  
ANISOU 2122  NE2 HIS A 468    10591  12174  12681  -1114   -887    266       N  
ATOM   2123  N   SER A 469     -25.212 -47.178 -41.273  1.00110.87           N  
ANISOU 2123  N   SER A 469    12149  14666  15312  -1360  -1840   -144       N  
ATOM   2124  CA  SER A 469     -24.844 -48.477 -41.830  1.00113.28           C  
ANISOU 2124  CA  SER A 469    12558  14803  15681  -1503  -1956   -361       C  
ATOM   2125  C   SER A 469     -23.337 -48.483 -42.070  1.00112.88           C  
ANISOU 2125  C   SER A 469    12863  14721  15305  -1395  -1850   -417       C  
ATOM   2126  O   SER A 469     -22.681 -47.446 -41.959  1.00110.93           O  
ANISOU 2126  O   SER A 469    12758  14597  14792  -1228  -1736   -302       O  
ATOM   2127  CB  SER A 469     -25.594 -48.751 -43.135  1.00116.32           C  
ANISOU 2127  CB  SER A 469    12859  15259  16079  -1575  -2337   -596       C  
ATOM   2128  OG  SER A 469     -26.941 -49.096 -42.878  1.00120.31           O  
ANISOU 2128  OG  SER A 469    12998  15733  16980  -1727  -2442   -576       O  
ATOM   2129  N   LEU A 470     -22.797 -49.656 -42.393  1.00116.04           N  
ANISOU 2129  N   LEU A 470    13391  14942  15757  -1493  -1884   -595       N  
ATOM   2130  CA  LEU A 470     -21.366 -49.819 -42.672  1.00115.31           C  
ANISOU 2130  CA  LEU A 470    13611  14803  15399  -1395  -1781   -667       C  
ATOM   2131  C   LEU A 470     -21.149 -50.105 -44.173  1.00118.71           C  
ANISOU 2131  C   LEU A 470    14211  15288  15605  -1376  -2034   -952       C  
ATOM   2132  O   LEU A 470     -21.064 -51.268 -44.577  1.00120.47           O  
ANISOU 2132  O   LEU A 470    14485  15337  15949  -1486  -2125  -1168       O  
ATOM   2133  CB  LEU A 470     -20.784 -50.944 -41.799  1.00114.42           C  
ANISOU 2133  CB  LEU A 470    13537  14430  15506  -1481  -1583   -634       C  
ATOM   2134  CG  LEU A 470     -19.838 -50.674 -40.708  0.00112.50           C  
ANISOU 2134  CG  LEU A 470    13393  14152  15199  -1384  -1298   -426       C  
ATOM   2135  CD1 LEU A 470     -20.279 -49.529 -39.810  0.00110.82           C  
ANISOU 2135  CD1 LEU A 470    13052  14093  14962  -1309  -1169   -182       C  
ATOM   2136  CD2 LEU A 470     -19.627 -51.944 -39.899  0.00113.29           C  
ANISOU 2136  CD2 LEU A 470    13476  13984  15583  -1495  -1160   -385       C  
ATOM   2137  N   PRO A 471     -21.061 -49.042 -45.006  1.00120.05           N  
ANISOU 2137  N   PRO A 471    14480  15693  15440  -1229  -2141   -953       N  
ATOM   2138  CA  PRO A 471     -20.977 -49.237 -46.463  1.00123.02           C  
ANISOU 2138  CA  PRO A 471    15023  16164  15554  -1193  -2392  -1210       C  
ATOM   2139  C   PRO A 471     -19.592 -49.719 -46.930  1.00123.76           C  
ANISOU 2139  C   PRO A 471    15423  16185  15415  -1115  -2267  -1346       C  
ATOM   2140  O   PRO A 471     -18.642 -48.929 -46.915  1.00122.30           O  
ANISOU 2140  O   PRO A 471    15396  16096  14978   -963  -2085  -1215       O  
ATOM   2141  CB  PRO A 471     -21.278 -47.838 -47.016  1.00122.76           C  
ANISOU 2141  CB  PRO A 471    14998  16404  15241  -1037  -2489  -1085       C  
ATOM   2142  CG  PRO A 471     -20.815 -46.899 -45.951  1.00118.50           C  
ANISOU 2142  CG  PRO A 471    14435  15878  14712   -945  -2201   -796       C  
ATOM   2143  CD  PRO A 471     -21.022 -47.609 -44.639  1.00117.38           C  
ANISOU 2143  CD  PRO A 471    14122  15535  14943  -1080  -2030   -712       C  
ATOM   2144  N   PRO A 472     -19.472 -50.999 -47.360  1.00126.81           N  
ANISOU 2144  N   PRO A 472    15884  16393  15904  -1216  -2358  -1614       N  
ATOM   2145  CA  PRO A 472     -18.135 -51.520 -47.702  1.00126.00           C  
ANISOU 2145  CA  PRO A 472    16052  16199  15625  -1128  -2202  -1739       C  
ATOM   2146  C   PRO A 472     -17.551 -50.886 -48.970  1.00126.87           C  
ANISOU 2146  C   PRO A 472    16411  16535  15258   -954  -2261  -1842       C  
ATOM   2147  O   PRO A 472     -18.222 -50.839 -50.007  1.00129.36           O  
ANISOU 2147  O   PRO A 472    16762  16990  15399   -952  -2538  -2021       O  
ATOM   2148  CB  PRO A 472     -18.374 -53.029 -47.905  1.00129.31           C  
ANISOU 2148  CB  PRO A 472    16470  16358  16305  -1284  -2321  -2022       C  
ATOM   2149  CG  PRO A 472     -19.769 -53.297 -47.416  1.00130.61           C  
ANISOU 2149  CG  PRO A 472    16331  16451  16844  -1477  -2488  -1988       C  
ATOM   2150  CD  PRO A 472     -20.515 -52.016 -47.580  1.00129.70           C  
ANISOU 2150  CD  PRO A 472    16089  16621  16570  -1410  -2605  -1826       C  
ATOM   2151  N   GLY A 473     -16.312 -50.404 -48.877  1.00123.76           N  
ANISOU 2151  N   GLY A 473    16182  16182  14660   -807  -2002  -1720       N  
ATOM   2152  CA  GLY A 473     -15.650 -49.748 -50.001  1.00123.58           C  
ANISOU 2152  CA  GLY A 473    16394  16369  14193   -633  -1988  -1764       C  
ATOM   2153  C   GLY A 473     -15.250 -50.739 -51.076  1.00126.68           C  
ANISOU 2153  C   GLY A 473    17007  16715  14410   -606  -2070  -2107       C  
ATOM   2154  O   GLY A 473     -15.481 -51.944 -50.935  1.00129.02           O  
ANISOU 2154  O   GLY A 473    17271  16791  14961   -730  -2148  -2323       O  
ATOM   2155  N   GLU A 474     -14.639 -50.231 -52.146  1.00126.20           N  
ANISOU 2155  N   GLU A 474    17179  16854  13919   -438  -2036  -2156       N  
ATOM   2156  CA  GLU A 474     -14.190 -51.064 -53.273  1.00127.13           C  
ANISOU 2156  CA  GLU A 474    17549  16968  13788   -371  -2087  -2493       C  
ATOM   2157  C   GLU A 474     -13.613 -52.410 -52.813  1.00125.85           C  
ANISOU 2157  C   GLU A 474    17403  16494  13922   -442  -1964  -2685       C  
ATOM   2158  O   GLU A 474     -13.898 -53.455 -53.408  1.00128.62           O  
ANISOU 2158  O   GLU A 474    17846  16729  14297   -497  -2135  -3027       O  
ATOM   2159  CB  GLU A 474     -13.135 -50.309 -54.095  1.00127.40           C  
ANISOU 2159  CB  GLU A 474    17825  17211  13372   -155  -1880  -2415       C  
ATOM   2160  CG  GLU A 474     -13.633 -49.167 -54.915  0.00129.24           C  
ANISOU 2160  CG  GLU A 474    18128  17749  13228    -52  -2022  -2289       C  
ATOM   2161  CD  GLU A 474     -12.541 -48.502 -55.741  0.00129.70           C  
ANISOU 2161  CD  GLU A 474    18433  17991  12854    157  -1777  -2196       C  
ATOM   2162  OE1 GLU A 474     -11.352 -48.851 -55.572  0.00128.72           O  
ANISOU 2162  OE1 GLU A 474    18387  17758  12761    217  -1473  -2208       O  
ATOM   2163  OE2 GLU A 474     -12.874 -47.623 -56.562  0.00131.12           O  
ANISOU 2163  OE2 GLU A 474    18720  18425  12675    267  -1882  -2095       O  
ATOM   2164  N   ASP A 475     -12.834 -52.347 -51.731  1.00118.91           N  
ANISOU 2164  N   ASP A 475    16429  15474  13276   -438  -1682  -2459       N  
ATOM   2165  CA  ASP A 475     -12.018 -53.444 -51.194  1.00115.29           C  
ANISOU 2165  CA  ASP A 475    15992  14731  13080   -453  -1498  -2553       C  
ATOM   2166  C   ASP A 475     -10.616 -52.879 -50.981  1.00110.79           C  
ANISOU 2166  C   ASP A 475    15493  14220  12381   -290  -1166  -2359       C  
ATOM   2167  O   ASP A 475      -9.889 -53.343 -50.105  1.00111.05           O  
ANISOU 2167  O   ASP A 475    15459  14059  12674   -290   -976  -2269       O  
ATOM   2168  CB  ASP A 475     -11.957 -54.681 -52.101  1.00119.32           C  
ANISOU 2168  CB  ASP A 475    16685  15102  13551   -451  -1606  -2965       C  
ATOM   2169  CG  ASP A 475     -11.160 -55.839 -51.421  0.00121.98           C  
ANISOU 2169  CG  ASP A 475    17018  15101  14230   -464  -1411  -3031       C  
ATOM   2170  OD1 ASP A 475     -11.453 -56.203 -50.262  0.00120.02           O  
ANISOU 2170  OD1 ASP A 475    16574  14645  14382   -594  -1386  -2871       O  
ATOM   2171  OD2 ASP A 475     -10.238 -56.360 -52.083  0.00123.34           O  
ANISOU 2171  OD2 ASP A 475    17390  15225  14250   -326  -1275  -3235       O  
ATOM   2172  N   GLY A 476     -10.250 -51.876 -51.786  1.00105.92           N  
ANISOU 2172  N   GLY A 476    15004  13869  11373   -150  -1104  -2284       N  
ATOM   2173  CA  GLY A 476      -8.996 -51.136 -51.610  1.00 98.62           C  
ANISOU 2173  CA  GLY A 476    14108  13023  10338    -13   -796  -2064       C  
ATOM   2174  C   GLY A 476      -9.106 -50.012 -50.588  1.00 90.27           C  
ANISOU 2174  C   GLY A 476    12860  12025   9414    -55   -735  -1710       C  
ATOM   2175  O   GLY A 476      -8.339 -49.961 -49.630  1.00 86.72           O  
ANISOU 2175  O   GLY A 476    12307  11466   9177    -51   -544  -1547       O  
ATOM   2176  N   ARG A 477     -10.053 -49.103 -50.804  1.00 84.73           N  
ANISOU 2176  N   ARG A 477    12115  11497   8580    -83   -906  -1600       N  
ATOM   2177  CA  ARG A 477     -10.234 -47.942 -49.944  1.00 78.68           C  
ANISOU 2177  CA  ARG A 477    11190  10793   7911   -106   -856  -1288       C  
ATOM   2178  C   ARG A 477     -11.600 -47.965 -49.270  1.00 74.05           C  
ANISOU 2178  C   ARG A 477    10415  10165   7553   -248  -1079  -1250       C  
ATOM   2179  O   ARG A 477     -12.552 -48.525 -49.819  1.00 78.67           O  
ANISOU 2179  O   ARG A 477    11004  10760   8127   -314  -1320  -1442       O  
ATOM   2180  CB  ARG A 477     -10.091 -46.649 -50.745  1.00 79.73           C  
ANISOU 2180  CB  ARG A 477    11422  11164   7707     14   -816  -1134       C  
ATOM   2181  CG  ARG A 477      -8.646 -46.224 -51.013  1.00 84.50           C  
ANISOU 2181  CG  ARG A 477    12129  11806   8171    141   -513  -1034       C  
ATOM   2182  CD  ARG A 477      -8.467 -44.692 -50.935  1.00 83.03           C  
ANISOU 2182  CD  ARG A 477    11908  11750   7889    195   -411   -732       C  
ATOM   2183  NE  ARG A 477      -7.057 -44.294 -51.030  1.00 85.05           N  
ANISOU 2183  NE  ARG A 477    12208  12009   8099    285   -108   -617       N  
ATOM   2184  CZ  ARG A 477      -6.539 -43.152 -50.566  1.00 86.73           C  
ANISOU 2184  CZ  ARG A 477    12338  12236   8382    298     44   -359       C  
ATOM   2185  NH1 ARG A 477      -7.296 -42.246 -49.943  1.00 83.21           N  
ANISOU 2185  NH1 ARG A 477    11778  11797   8041    243    -67   -189       N  
ATOM   2186  NH2 ARG A 477      -5.234 -42.919 -50.708  1.00 86.03           N  
ANISOU 2186  NH2 ARG A 477    12266  12139   8284    365    316   -279       N  
ATOM   2187  N   VAL A 478     -11.679 -47.353 -48.085  1.00 63.87           N  
ANISOU 2187  N   VAL A 478     8957   8835   6475   -291   -995  -1013       N  
ATOM   2188  CA  VAL A 478     -12.926 -47.224 -47.344  1.00 60.75           C  
ANISOU 2188  CA  VAL A 478     8365   8417   6300   -405  -1148   -933       C  
ATOM   2189  C   VAL A 478     -13.280 -45.765 -47.141  1.00 56.64           C  
ANISOU 2189  C   VAL A 478     7774   8051   5694   -350  -1142   -697       C  
ATOM   2190  O   VAL A 478     -12.419 -44.909 -47.207  1.00 55.92           O  
ANISOU 2190  O   VAL A 478     7760   8026   5462   -251   -979   -560       O  
ATOM   2191  CB  VAL A 478     -12.874 -47.928 -45.947  1.00 56.02           C  
ANISOU 2191  CB  VAL A 478     7620   7606   6058   -508  -1050   -867       C  
ATOM   2192  CG1 VAL A 478     -12.605 -49.414 -46.112  1.00 62.07           C  
ANISOU 2192  CG1 VAL A 478     8448   8178   6960   -565  -1063  -1089       C  
ATOM   2193  CG2 VAL A 478     -11.847 -47.314 -45.032  1.00 49.58           C  
ANISOU 2193  CG2 VAL A 478     6790   6769   5277   -443   -820   -664       C  
ATOM   2194  N   GLU A 479     -14.553 -45.493 -46.877  1.00 57.14           N  
ANISOU 2194  N   GLU A 479     7679   8156   5876   -415  -1313   -648       N  
ATOM   2195  CA  GLU A 479     -15.015 -44.141 -46.547  1.00 55.41           C  
ANISOU 2195  CA  GLU A 479     7369   8051   5634   -359  -1308   -425       C  
ATOM   2196  C   GLU A 479     -14.811 -43.867 -45.055  1.00 50.85           C  
ANISOU 2196  C   GLU A 479     6661   7363   5297   -394  -1131   -258       C  
ATOM   2197  O   GLU A 479     -14.973 -44.759 -44.220  1.00 47.19           O  
ANISOU 2197  O   GLU A 479     6102   6760   5067   -493  -1101   -295       O  
ATOM   2198  CB  GLU A 479     -16.504 -43.980 -46.856  1.00 59.62           C  
ANISOU 2198  CB  GLU A 479     7758   8678   6218   -398  -1564   -445       C  
ATOM   2199  CG  GLU A 479     -16.928 -44.392 -48.271  1.00 69.94           C  
ANISOU 2199  CG  GLU A 479     9172  10102   7300   -380  -1811   -645       C  
ATOM   2200  CD  GLU A 479     -16.833 -43.277 -49.282  1.00 78.19           C  
ANISOU 2200  CD  GLU A 479    10356  11352   8001   -223  -1862   -545       C  
ATOM   2201  OE1 GLU A 479     -16.358 -42.170 -48.937  1.00 80.50           O  
ANISOU 2201  OE1 GLU A 479    10666  11672   8248   -133  -1689   -319       O  
ATOM   2202  OE2 GLU A 479     -17.250 -43.520 -50.433  1.00 92.01           O  
ANISOU 2202  OE2 GLU A 479    12204  13231   9527   -189  -2086   -694       O  
ATOM   2203  N   PRO A 480     -14.468 -42.622 -44.707  1.00 44.94           N  
ANISOU 2203  N   PRO A 480     5915   6671   4488   -309  -1015    -72       N  
ATOM   2204  CA  PRO A 480     -14.466 -42.294 -43.303  1.00 42.78           C  
ANISOU 2204  CA  PRO A 480     5522   6317   4417   -335   -888     62       C  
ATOM   2205  C   PRO A 480     -15.892 -42.224 -42.779  1.00 43.30           C  
ANISOU 2205  C   PRO A 480     5394   6400   4660   -388   -998    104       C  
ATOM   2206  O   PRO A 480     -16.840 -42.115 -43.558  1.00 43.06           O  
ANISOU 2206  O   PRO A 480     5309   6463   4588   -386  -1184     63       O  
ATOM   2207  CB  PRO A 480     -13.804 -40.926 -43.261  1.00 40.06           C  
ANISOU 2207  CB  PRO A 480     5241   6024   3958   -231   -769    214       C  
ATOM   2208  CG  PRO A 480     -14.060 -40.357 -44.585  1.00 40.97           C  
ANISOU 2208  CG  PRO A 480     5446   6271   3851   -154   -878    217       C  
ATOM   2209  CD  PRO A 480     -14.081 -41.484 -45.543  1.00 42.28           C  
ANISOU 2209  CD  PRO A 480     5697   6460   3908   -188   -991     25       C  
ATOM   2210  N   TYR A 481     -16.021 -42.359 -41.463  1.00 41.15           N  
ANISOU 2210  N   TYR A 481     5012   6041   4582   -433   -883    184       N  
ATOM   2211  CA  TYR A 481     -17.268 -42.123 -40.773  1.00 42.85           C  
ANISOU 2211  CA  TYR A 481     5031   6275   4974   -462   -915    262       C  
ATOM   2212  C   TYR A 481     -17.392 -40.611 -40.531  1.00 42.95           C  
ANISOU 2212  C   TYR A 481     5032   6367   4921   -343   -862    403       C  
ATOM   2213  O   TYR A 481     -18.457 -40.026 -40.735  1.00 45.53           O  
ANISOU 2213  O   TYR A 481     5233   6772   5293   -306   -959    452       O  
ATOM   2214  CB  TYR A 481     -17.305 -42.917 -39.445  1.00 43.74           C  
ANISOU 2214  CB  TYR A 481     5059   6267   5292   -543   -782    303       C  
ATOM   2215  CG  TYR A 481     -18.370 -42.441 -38.515  1.00 39.19           C  
ANISOU 2215  CG  TYR A 481     4299   5721   4870   -539   -729    423       C  
ATOM   2216  CD1 TYR A 481     -19.689 -42.776 -38.734  1.00 35.42           C  
ANISOU 2216  CD1 TYR A 481     3624   5271   4561   -609   -846    406       C  
ATOM   2217  CD2 TYR A 481     -18.072 -41.617 -37.452  1.00 38.82           C  
ANISOU 2217  CD2 TYR A 481     4268   5681   4800   -459   -566    540       C  
ATOM   2218  CE1 TYR A 481     -20.699 -42.322 -37.902  1.00 37.56           C  
ANISOU 2218  CE1 TYR A 481     3704   5579   4988   -592   -773    523       C  
ATOM   2219  CE2 TYR A 481     -19.089 -41.146 -36.604  1.00 44.94           C  
ANISOU 2219  CE2 TYR A 481     4881   6493   5701   -433   -494    639       C  
ATOM   2220  CZ  TYR A 481     -20.399 -41.504 -36.843  1.00 38.22           C  
ANISOU 2220  CZ  TYR A 481     3823   5673   5027   -496   -584    639       C  
ATOM   2221  OH  TYR A 481     -21.421 -41.057 -36.025  1.00 42.99           O  
ANISOU 2221  OH  TYR A 481     4243   6318   5773   -461   -488    742       O  
ATOM   2222  N   VAL A 482     -16.301 -39.988 -40.093  1.00 41.73           N  
ANISOU 2222  N   VAL A 482     4996   6178   4682   -282   -714    462       N  
ATOM   2223  CA  VAL A 482     -16.282 -38.548 -39.865  1.00 42.01           C  
ANISOU 2223  CA  VAL A 482     5040   6246   4674   -175   -656    577       C  
ATOM   2224  C   VAL A 482     -16.180 -37.790 -41.183  1.00 44.45           C  
ANISOU 2224  C   VAL A 482     5442   6636   4810    -96   -748    603       C  
ATOM   2225  O   VAL A 482     -15.818 -38.353 -42.201  1.00 47.47           O  
ANISOU 2225  O   VAL A 482     5922   7056   5059   -113   -821    523       O  
ATOM   2226  CB  VAL A 482     -15.128 -38.113 -38.942  1.00 41.49           C  
ANISOU 2226  CB  VAL A 482     5061   6104   4600   -151   -488    616       C  
ATOM   2227  CG1 VAL A 482     -15.280 -38.746 -37.565  1.00 44.39           C  
ANISOU 2227  CG1 VAL A 482     5354   6414   5097   -201   -397    620       C  
ATOM   2228  CG2 VAL A 482     -13.765 -38.455 -39.532  1.00 42.38           C  
ANISOU 2228  CG2 VAL A 482     5319   6186   4598   -164   -448    565       C  
ATOM   2229  N   ASP A 483     -16.510 -36.508 -41.142  1.00 45.12           N  
ANISOU 2229  N   ASP A 483     5509   6743   4894      3   -734    718       N  
ATOM   2230  CA  ASP A 483     -16.534 -35.651 -42.322  1.00 43.67           C  
ANISOU 2230  CA  ASP A 483     5408   6630   4554    100   -813    793       C  
ATOM   2231  C   ASP A 483     -15.395 -34.593 -42.217  1.00 42.05           C  
ANISOU 2231  C   ASP A 483     5332   6348   4297    158   -655    889       C  
ATOM   2232  O   ASP A 483     -15.276 -33.863 -41.195  1.00 41.81           O  
ANISOU 2232  O   ASP A 483     5264   6228   4394    180   -546    935       O  
ATOM   2233  CB  ASP A 483     -17.908 -34.984 -42.401  1.00 42.49           C  
ANISOU 2233  CB  ASP A 483     5113   6544   4489    178   -933    873       C  
ATOM   2234  CG  ASP A 483     -18.227 -34.437 -43.780  1.00 55.18           C  
ANISOU 2234  CG  ASP A 483     6787   8260   5920    276  -1088    944       C  
ATOM   2235  OD1 ASP A 483     -17.293 -34.057 -44.531  1.00 67.60           O  
ANISOU 2235  OD1 ASP A 483     8542   9836   7305    319  -1035    994       O  
ATOM   2236  OD2 ASP A 483     -19.435 -34.363 -44.114  1.00 73.31           O  
ANISOU 2236  OD2 ASP A 483     8944  10644   8266    319  -1263    964       O  
ATOM   2237  N   PHE A 484     -14.540 -34.543 -43.241  1.00 37.54           N  
ANISOU 2237  N   PHE A 484     4910   5806   3549    177   -634    907       N  
ATOM   2238  CA  PHE A 484     -13.398 -33.603 -43.254  1.00 36.43           C  
ANISOU 2238  CA  PHE A 484     4873   5583   3387    211   -475   1006       C  
ATOM   2239  C   PHE A 484     -13.670 -32.318 -44.023  1.00 38.09           C  
ANISOU 2239  C   PHE A 484     5138   5806   3528    327   -490   1179       C  
ATOM   2240  O   PHE A 484     -12.767 -31.486 -44.166  1.00 41.69           O  
ANISOU 2240  O   PHE A 484     5677   6179   3984    349   -355   1283       O  
ATOM   2241  CB  PHE A 484     -12.121 -34.281 -43.788  1.00 34.55           C  
ANISOU 2241  CB  PHE A 484     4748   5347   3031    165   -380    946       C  
ATOM   2242  CG  PHE A 484     -11.619 -35.373 -42.903  1.00 31.25           C  
ANISOU 2242  CG  PHE A 484     4283   4875   2717     69   -335    809       C  
ATOM   2243  CD1 PHE A 484     -11.001 -35.065 -41.674  1.00 36.09           C  
ANISOU 2243  CD1 PHE A 484     4845   5377   3489     35   -230    814       C  
ATOM   2244  CD2 PHE A 484     -11.793 -36.699 -43.248  1.00 28.84           C  
ANISOU 2244  CD2 PHE A 484     3985   4617   2357     19   -410    673       C  
ATOM   2245  CE1 PHE A 484     -10.559 -36.071 -40.833  1.00 30.47           C  
ANISOU 2245  CE1 PHE A 484     4096   4623   2860    -34   -202    714       C  
ATOM   2246  CE2 PHE A 484     -11.364 -37.727 -42.394  1.00 36.60           C  
ANISOU 2246  CE2 PHE A 484     4924   5526   3457    -58   -366    571       C  
ATOM   2247  CZ  PHE A 484     -10.742 -37.409 -41.190  1.00 31.95           C  
ANISOU 2247  CZ  PHE A 484     4288   4846   3006    -78   -261    606       C  
ATOM   2248  N   ALA A 485     -14.901 -32.135 -44.508  1.00 41.09           N  
ANISOU 2248  N   ALA A 485     5462   6280   3872    400   -655   1224       N  
ATOM   2249  CA  ALA A 485     -15.255 -30.920 -45.254  1.00 41.80           C  
ANISOU 2249  CA  ALA A 485     5603   6381   3896    534   -688   1415       C  
ATOM   2250  C   ALA A 485     -14.884 -29.677 -44.467  1.00 43.00           C  
ANISOU 2250  C   ALA A 485     5747   6356   4236    569   -537   1522       C  
ATOM   2251  O   ALA A 485     -14.226 -28.793 -45.006  1.00 46.63           O  
ANISOU 2251  O   ALA A 485     6318   6747   4652    619   -439   1672       O  
ATOM   2252  CB  ALA A 485     -16.702 -30.897 -45.580  1.00 40.92           C  
ANISOU 2252  CB  ALA A 485     5379   6380   3788    611   -899   1438       C  
ATOM   2253  N   GLU A 486     -15.262 -29.619 -43.185  1.00 44.10           N  
ANISOU 2253  N   GLU A 486     5762   6410   4583    540   -505   1442       N  
ATOM   2254  CA  GLU A 486     -14.962 -28.436 -42.367  1.00 42.99           C  
ANISOU 2254  CA  GLU A 486     5622   6091   4623    577   -379   1499       C  
ATOM   2255  C   GLU A 486     -13.443 -28.264 -42.138  1.00 41.77           C  
ANISOU 2255  C   GLU A 486     5564   5817   4489    490   -220   1482       C  
ATOM   2256  O   GLU A 486     -12.942 -27.138 -42.203  1.00 44.33           O  
ANISOU 2256  O   GLU A 486     5945   5996   4901    524   -128   1593       O  
ATOM   2257  CB  GLU A 486     -15.743 -28.449 -41.057  1.00 45.86           C  
ANISOU 2257  CB  GLU A 486     5846   6414   5162    584   -375   1400       C  
ATOM   2258  CG  GLU A 486     -15.537 -27.231 -40.132  1.00 46.21           C  
ANISOU 2258  CG  GLU A 486     5901   6270   5387    637   -258   1414       C  
ATOM   2259  CD  GLU A 486     -16.240 -25.943 -40.579  1.00 55.84           C  
ANISOU 2259  CD  GLU A 486     7116   7408   6691    793   -280   1572       C  
ATOM   2260  OE1 GLU A 486     -16.789 -25.866 -41.720  1.00 46.29           O  
ANISOU 2260  OE1 GLU A 486     5912   6297   5379    872   -391   1709       O  
ATOM   2261  OE2 GLU A 486     -16.238 -24.993 -39.746  1.00 57.90           O  
ANISOU 2261  OE2 GLU A 486     7375   7500   7122    846   -192   1551       O  
ATOM   2262  N   PHE A 487     -12.705 -29.347 -41.927  1.00 36.04           N  
ANISOU 2262  N   PHE A 487     4847   5139   3707    379   -191   1356       N  
ATOM   2263  CA  PHE A 487     -11.244 -29.245 -41.971  1.00 39.08           C  
ANISOU 2263  CA  PHE A 487     5303   5440   4105    307    -55   1360       C  
ATOM   2264  C   PHE A 487     -10.692 -28.611 -43.268  1.00 41.03           C  
ANISOU 2264  C   PHE A 487     5661   5684   4243    352     16   1537       C  
ATOM   2265  O   PHE A 487      -9.857 -27.696 -43.212  1.00 39.06           O  
ANISOU 2265  O   PHE A 487     5441   5288   4111    335    142   1627       O  
ATOM   2266  CB  PHE A 487     -10.587 -30.603 -41.809  1.00 43.18           C  
ANISOU 2266  CB  PHE A 487     5815   6033   4559    211    -46   1220       C  
ATOM   2267  CG  PHE A 487      -9.103 -30.592 -42.076  1.00 42.23           C  
ANISOU 2267  CG  PHE A 487     5745   5856   4446    153     91   1237       C  
ATOM   2268  CD1 PHE A 487      -8.608 -30.819 -43.347  1.00 53.16           C  
ANISOU 2268  CD1 PHE A 487     7218   7318   5663    173    148   1311       C  
ATOM   2269  CD2 PHE A 487      -8.207 -30.359 -41.045  1.00 49.68           C  
ANISOU 2269  CD2 PHE A 487     6637   6678   5560     84    160   1175       C  
ATOM   2270  CE1 PHE A 487      -7.246 -30.803 -43.587  1.00 51.02           C  
ANISOU 2270  CE1 PHE A 487     6965   6997   5422    124    302   1337       C  
ATOM   2271  CE2 PHE A 487      -6.848 -30.346 -41.279  1.00 47.10           C  
ANISOU 2271  CE2 PHE A 487     6316   6301   5280     26    279   1193       C  
ATOM   2272  CZ  PHE A 487      -6.369 -30.570 -42.553  1.00 42.89           C  
ANISOU 2272  CZ  PHE A 487     5852   5839   4604     46    365   1281       C  
ATOM   2273  N   TYR A 488     -11.119 -29.097 -44.430  1.00 40.72           N  
ANISOU 2273  N   TYR A 488     5687   5803   3981    406    -60   1586       N  
ATOM   2274  CA  TYR A 488     -10.573 -28.548 -45.699  1.00 43.62           C  
ANISOU 2274  CA  TYR A 488     6186   6194   4194    464     28   1771       C  
ATOM   2275  C   TYR A 488     -10.911 -27.062 -45.854  1.00 45.03           C  
ANISOU 2275  C   TYR A 488     6388   6245   4476    559     58   1984       C  
ATOM   2276  O   TYR A 488     -10.132 -26.307 -46.416  1.00 50.83           O  
ANISOU 2276  O   TYR A 488     7204   6893   5215    570    207   2156       O  
ATOM   2277  CB  TYR A 488     -11.062 -29.325 -46.935  1.00 43.71           C  
ANISOU 2277  CB  TYR A 488     6288   6422   3899    527    -86   1769       C  
ATOM   2278  CG  TYR A 488     -10.471 -30.719 -47.089  1.00 43.30           C  
ANISOU 2278  CG  TYR A 488     6258   6466   3727    447    -70   1582       C  
ATOM   2279  CD1 TYR A 488      -9.118 -30.885 -47.349  1.00 44.51           C  
ANISOU 2279  CD1 TYR A 488     6471   6587   3855    402    127   1592       C  
ATOM   2280  CD2 TYR A 488     -11.264 -31.867 -46.987  1.00 34.50           C  
ANISOU 2280  CD2 TYR A 488     5094   5461   2554    419   -245   1398       C  
ATOM   2281  CE1 TYR A 488      -8.554 -32.138 -47.509  1.00 42.33           C  
ANISOU 2281  CE1 TYR A 488     6215   6383   3486    351    155   1422       C  
ATOM   2282  CE2 TYR A 488     -10.698 -33.144 -47.129  1.00 40.27           C  
ANISOU 2282  CE2 TYR A 488     5855   6245   3202    352   -224   1223       C  
ATOM   2283  CZ  TYR A 488      -9.332 -33.266 -47.399  1.00 43.37           C  
ANISOU 2283  CZ  TYR A 488     6318   6603   3557    329    -21   1235       C  
ATOM   2284  OH  TYR A 488      -8.717 -34.501 -47.564  1.00 44.03           O  
ANISOU 2284  OH  TYR A 488     6432   6724   3574    285     18   1064       O  
ATOM   2285  N   ARG A 489     -12.067 -26.646 -45.350  1.00 45.59           N  
ANISOU 2285  N   ARG A 489     6380   6290   4650    629    -68   1980       N  
ATOM   2286  CA  ARG A 489     -12.494 -25.253 -45.473  1.00 47.40           C  
ANISOU 2286  CA  ARG A 489     6628   6381   5001    741    -50   2177       C  
ATOM   2287  C   ARG A 489     -11.662 -24.357 -44.548  1.00 47.19           C  
ANISOU 2287  C   ARG A 489     6580   6094   5254    672    107   2168       C  
ATOM   2288  O   ARG A 489     -11.124 -23.348 -45.004  1.00 50.17           O  
ANISOU 2288  O   ARG A 489     7031   6322   5711    696    226   2357       O  
ATOM   2289  CB  ARG A 489     -14.006 -25.135 -45.196  1.00 48.34           C  
ANISOU 2289  CB  ARG A 489     6644   6556   5166    852   -228   2160       C  
ATOM   2290  CG  ARG A 489     -14.581 -23.713 -45.206  1.00 46.60           C  
ANISOU 2290  CG  ARG A 489     6424   6175   5109    995   -221   2348       C  
ATOM   2291  CD  ARG A 489     -16.117 -23.676 -45.156  1.00 49.01           C  
ANISOU 2291  CD  ARG A 489     6607   6575   5438   1130   -406   2355       C  
ATOM   2292  NE  ARG A 489     -16.684 -24.819 -44.437  1.00 58.53           N  
ANISOU 2292  NE  ARG A 489     7673   7916   6649   1052   -498   2125       N  
ATOM   2293  CZ  ARG A 489     -17.573 -25.709 -44.911  1.00 60.31           C  
ANISOU 2293  CZ  ARG A 489     7818   8356   6741   1069   -685   2074       C  
ATOM   2294  NH1 ARG A 489     -17.970 -26.715 -44.121  1.00 57.31           N  
ANISOU 2294  NH1 ARG A 489     7305   8048   6420    974   -725   1874       N  
ATOM   2295  NH2 ARG A 489     -18.086 -25.615 -46.142  1.00 60.12           N  
ANISOU 2295  NH2 ARG A 489     7840   8472   6530   1178   -839   2220       N  
ATOM   2296  N   LEU A 490     -11.551 -24.739 -43.271  1.00 44.14           N  
ANISOU 2296  N   LEU A 490     6099   5656   5015    585    103   1953       N  
ATOM   2297  CA  LEU A 490     -10.745 -24.005 -42.280  1.00 46.61           C  
ANISOU 2297  CA  LEU A 490     6391   5741   5580    508    211   1886       C  
ATOM   2298  C   LEU A 490      -9.281 -23.917 -42.672  1.00 50.79           C  
ANISOU 2298  C   LEU A 490     6963   6193   6141    398    358   1943       C  
ATOM   2299  O   LEU A 490      -8.631 -22.894 -42.467  1.00 55.27           O  
ANISOU 2299  O   LEU A 490     7538   6539   6922    360    460   2009       O  
ATOM   2300  CB  LEU A 490     -10.818 -24.672 -40.896  1.00 42.04           C  
ANISOU 2300  CB  LEU A 490     5723   5180   5070    438    165   1635       C  
ATOM   2301  CG  LEU A 490     -12.177 -24.546 -40.221  1.00 38.37           C  
ANISOU 2301  CG  LEU A 490     5190   4740   4648    541     74   1571       C  
ATOM   2302  CD1 LEU A 490     -12.291 -25.415 -38.983  1.00 44.67           C  
ANISOU 2302  CD1 LEU A 490     5916   5606   5450    479     47   1356       C  
ATOM   2303  CD2 LEU A 490     -12.423 -23.111 -39.875  1.00 35.76           C  
ANISOU 2303  CD2 LEU A 490     4876   4185   4526    626    120   1630       C  
ATOM   2304  N   TRP A 491      -8.768 -25.018 -43.202  1.00 51.98           N  
ANISOU 2304  N   TRP A 491     7129   6517   6104    343    373   1905       N  
ATOM   2305  CA  TRP A 491      -7.421 -25.073 -43.732  1.00 50.99           C  
ANISOU 2305  CA  TRP A 491     7029   6361   5985    258    531   1973       C  
ATOM   2306  C   TRP A 491      -7.220 -24.099 -44.885  1.00 53.14           C  
ANISOU 2306  C   TRP A 491     7397   6562   6231    321    655   2255       C  
ATOM   2307  O   TRP A 491      -6.178 -23.456 -44.973  1.00 57.69           O  
ANISOU 2307  O   TRP A 491     7961   6979   6979    246    818   2353       O  
ATOM   2308  CB  TRP A 491      -7.138 -26.485 -44.209  1.00 52.28           C  
ANISOU 2308  CB  TRP A 491     7205   6740   5919    232    519   1880       C  
ATOM   2309  CG  TRP A 491      -5.748 -26.721 -44.681  1.00 55.42           C  
ANISOU 2309  CG  TRP A 491     7605   7130   6324    156    695   1921       C  
ATOM   2310  CD1 TRP A 491      -5.256 -26.476 -45.927  1.00 59.77           C  
ANISOU 2310  CD1 TRP A 491     8246   7724   6739    195    847   2117       C  
ATOM   2311  CD2 TRP A 491      -4.677 -27.290 -43.926  1.00 49.93           C  
ANISOU 2311  CD2 TRP A 491     6805   6394   5771     41    746   1770       C  
ATOM   2312  NE1 TRP A 491      -3.940 -26.843 -45.991  1.00 62.74           N  
ANISOU 2312  NE1 TRP A 491     8567   8083   7187    108   1011   2094       N  
ATOM   2313  CE2 TRP A 491      -3.557 -27.349 -44.779  1.00 53.22           C  
ANISOU 2313  CE2 TRP A 491     7233   6826   6163     13    939   1881       C  
ATOM   2314  CE3 TRP A 491      -4.548 -27.723 -42.601  1.00 51.25           C  
ANISOU 2314  CE3 TRP A 491     6870   6519   6082    -30    649   1566       C  
ATOM   2315  CZ2 TRP A 491      -2.320 -27.827 -44.361  1.00 54.09           C  
ANISOU 2315  CZ2 TRP A 491     7228   6904   6419    -85   1029   1788       C  
ATOM   2316  CZ3 TRP A 491      -3.324 -28.213 -42.180  1.00 54.25           C  
ANISOU 2316  CZ3 TRP A 491     7157   6876   6581   -123    715   1477       C  
ATOM   2317  CH2 TRP A 491      -2.219 -28.264 -43.065  1.00 57.81           C  
ANISOU 2317  CH2 TRP A 491     7595   7336   7036   -150    900   1585       C  
ATOM   2318  N   SER A 492      -8.202 -23.987 -45.776  1.00 53.19           N  
ANISOU 2318  N   SER A 492     7493   6688   6031    459    577   2398       N  
ATOM   2319  CA  SER A 492      -8.112 -23.029 -46.892  1.00 54.30           C  
ANISOU 2319  CA  SER A 492     7747   6771   6116    548    687   2704       C  
ATOM   2320  C   SER A 492      -7.992 -21.593 -46.430  1.00 52.00           C  
ANISOU 2320  C   SER A 492     7434   6174   6150    544    767   2830       C  
ATOM   2321  O   SER A 492      -7.260 -20.820 -47.007  1.00 53.94           O  
ANISOU 2321  O   SER A 492     7731   6279   6485    526    945   3050       O  
ATOM   2322  CB  SER A 492      -9.311 -23.149 -47.827  1.00 55.81           C  
ANISOU 2322  CB  SER A 492     8030   7154   6022    716    535   2823       C  
ATOM   2323  OG  SER A 492      -8.955 -23.919 -48.952  1.00 64.19           O  
ANISOU 2323  OG  SER A 492     9201   8436   6753    741    577   2874       O  
ATOM   2324  N   VAL A 493      -8.693 -21.243 -45.364  1.00 53.68           N  
ANISOU 2324  N   VAL A 493     7570   6271   6555    560    649   2685       N  
ATOM   2325  CA  VAL A 493      -8.656 -19.878 -44.868  1.00 57.56           C  
ANISOU 2325  CA  VAL A 493     8051   6449   7370    568    709   2763       C  
ATOM   2326  C   VAL A 493      -7.240 -19.477 -44.408  1.00 61.37           C  
ANISOU 2326  C   VAL A 493     8482   6714   8123    390    870   2721       C  
ATOM   2327  O   VAL A 493      -6.814 -18.343 -44.635  1.00 66.40           O  
ANISOU 2327  O   VAL A 493     9145   7092   8992    373    996   2903       O  
ATOM   2328  CB  VAL A 493      -9.716 -19.661 -43.785  1.00 57.25           C  
ANISOU 2328  CB  VAL A 493     7945   6350   7457    638    562   2582       C  
ATOM   2329  CG1 VAL A 493      -9.607 -18.269 -43.179  1.00 56.70           C  
ANISOU 2329  CG1 VAL A 493     7874   5929   7740    644    628   2610       C  
ATOM   2330  CG2 VAL A 493     -11.120 -19.857 -44.387  1.00 56.30           C  
ANISOU 2330  CG2 VAL A 493     7846   6418   7129    822    414   2680       C  
ATOM   2331  N   ASP A 494      -6.505 -20.417 -43.816  1.00 62.15           N  
ANISOU 2331  N   ASP A 494     8498   6911   8204    259    861   2499       N  
ATOM   2332  CA  ASP A 494      -5.101 -20.204 -43.424  1.00 61.69           C  
ANISOU 2332  CA  ASP A 494     8357   6690   8393     84    987   2446       C  
ATOM   2333  C   ASP A 494      -4.102 -20.289 -44.555  1.00 64.89           C  
ANISOU 2333  C   ASP A 494     8781   7135   8738     35   1192   2667       C  
ATOM   2334  O   ASP A 494      -3.106 -19.583 -44.530  1.00 67.20           O  
ANISOU 2334  O   ASP A 494     9012   7213   9310    -81   1339   2750       O  
ATOM   2335  CB  ASP A 494      -4.661 -21.253 -42.404  1.00 59.15           C  
ANISOU 2335  CB  ASP A 494     7932   6484   8059    -17    893   2145       C  
ATOM   2336  CG  ASP A 494      -5.161 -20.971 -41.018  1.00 52.47           C  
ANISOU 2336  CG  ASP A 494     7044   5529   7362    -20    748   1907       C  
ATOM   2337  OD1 ASP A 494      -5.917 -20.010 -40.838  1.00 55.21           O  
ANISOU 2337  OD1 ASP A 494     7438   5716   7823     64    720   1951       O  
ATOM   2338  OD2 ASP A 494      -4.799 -21.733 -40.106  1.00 51.55           O  
ANISOU 2338  OD2 ASP A 494     6856   5493   7236    -93    667   1678       O  
ATOM   2339  N   HIS A 495      -4.320 -21.201 -45.497  1.00 68.07           N  
ANISOU 2339  N   HIS A 495     9261   7813   8790    114   1205   2739       N  
ATOM   2340  CA  HIS A 495      -3.325 -21.496 -46.531  1.00 72.77           C  
ANISOU 2340  CA  HIS A 495     9878   8495   9275     80   1419   2908       C  
ATOM   2341  C   HIS A 495      -3.855 -21.042 -47.895  1.00 79.40           C  
ANISOU 2341  C   HIS A 495    10890   9411   9868    232   1502   3228       C  
ATOM   2342  O   HIS A 495      -4.069 -19.841 -48.098  1.00 83.11           O  
ANISOU 2342  O   HIS A 495    11406   9670  10502    272   1562   3449       O  
ATOM   2343  CB  HIS A 495      -2.978 -22.984 -46.530  1.00 69.90           C  
ANISOU 2343  CB  HIS A 495     9481   8388   8692     54   1386   2709       C  
ATOM   2344  CG  HIS A 495      -2.453 -23.490 -45.221  1.00 71.21           C  
ANISOU 2344  CG  HIS A 495     9489   8500   9068    -74   1294   2424       C  
ATOM   2345  ND1 HIS A 495      -3.276 -23.965 -44.222  1.00 66.61           N  
ANISOU 2345  ND1 HIS A 495     8882   7966   8459    -55   1074   2193       N  
ATOM   2346  CD2 HIS A 495      -1.188 -23.642 -44.767  1.00 72.87           C  
ANISOU 2346  CD2 HIS A 495     9554   8631   9503   -211   1389   2344       C  
ATOM   2347  CE1 HIS A 495      -2.542 -24.357 -43.198  1.00 65.51           C  
ANISOU 2347  CE1 HIS A 495     8615   7780   8495   -168   1034   1991       C  
ATOM   2348  NE2 HIS A 495      -1.270 -24.175 -43.504  1.00 68.99           N  
ANISOU 2348  NE2 HIS A 495     8972   8144   9097   -264   1207   2070       N  
ATOM   2349  N   GLY A 496      -4.072 -21.983 -48.820  1.00 83.06           N  
ANISOU 2349  N   GLY A 496    11457  10165   9935    325   1497   3250       N  
ATOM   2350  CA  GLY A 496      -4.716 -21.685 -50.107  1.00 86.29           C  
ANISOU 2350  CA  GLY A 496    12052  10704  10028    496   1519   3524       C  
ATOM   2351  C   GLY A 496      -6.089 -22.337 -50.198  1.00 86.96           C  
ANISOU 2351  C   GLY A 496    12202  11011   9828    628   1237   3396       C  
ATOM   2352  O   GLY A 496      -7.116 -21.652 -50.221  1.00 88.07           O  
ANISOU 2352  O   GLY A 496    12382  11100   9982    741   1099   3503       O  
TER    2353      GLY A 496                                                      
HETATM 2354  O1  1UL A 501     -23.486 -49.985 -21.718  1.00101.65           O  
HETATM 2355  C1  1UL A 501     -23.171 -48.901 -21.241  1.00 98.97           C  
HETATM 2356  C23 1UL A 501     -23.297 -47.657 -22.079  1.00 97.10           C  
HETATM 2357  N1  1UL A 501     -22.717 -48.790 -19.975  1.00 95.95           N  
HETATM 2358  C22 1UL A 501     -22.297 -47.540 -19.331  1.00 91.92           C  
HETATM 2359  C21 1UL A 501     -20.777 -47.678 -19.201  1.00 87.72           C  
HETATM 2360  C4  1UL A 501     -20.443 -48.885 -18.324  1.00 79.59           C  
HETATM 2361  C3  1UL A 501     -21.053 -50.155 -18.932  1.00 89.65           C  
HETATM 2362  C2  1UL A 501     -22.560 -49.957 -19.098  1.00 94.42           C  
HETATM 2363  N2  1UL A 501     -18.979 -49.034 -18.090  1.00 66.86           N  
HETATM 2364  C7  1UL A 501     -18.171 -48.402 -17.255  1.00 58.01           C  
HETATM 2365  C6  1UL A 501     -16.906 -48.954 -17.409  1.00 53.65           C  
HETATM 2366  C5  1UL A 501     -17.019 -49.952 -18.381  1.00 61.05           C  
HETATM 2367  N3  1UL A 501     -18.302 -50.023 -18.810  1.00 62.91           N  
HETATM 2368  C8  1UL A 501     -15.773 -48.547 -16.695  1.00 53.73           C  
HETATM 2369  C14 1UL A 501     -15.884 -47.480 -15.799  1.00 52.18           C  
HETATM 2370  N4  1UL A 501     -14.837 -47.028 -15.079  1.00 53.00           N  
HETATM 2371  C13 1UL A 501     -13.629 -47.595 -15.170  1.00 50.10           C  
HETATM 2372  N5  1UL A 501     -12.582 -47.141 -14.443  1.00 56.99           N  
HETATM 2373  C12 1UL A 501     -13.497 -48.650 -16.036  1.00 46.87           C  
HETATM 2374  C9  1UL A 501     -14.517 -49.151 -16.792  1.00 48.71           C  
HETATM 2375  O2  1UL A 501     -12.324 -49.386 -16.287  1.00 51.11           O  
HETATM 2376  C11 1UL A 501     -12.536 -50.301 -17.135  1.00 56.16           C  
HETATM 2377  C10 1UL A 501     -13.888 -50.225 -17.514  1.00 49.94           C  
HETATM 2378  C15 1UL A 501     -11.583 -51.180 -17.619  1.00 56.65           C  
HETATM 2379  C20 1UL A 501     -10.340 -51.220 -17.024  1.00 59.25           C  
HETATM 2380  S   1UL A 501      -9.885 -50.228 -15.631  1.00 67.43           S  
HETATM 2381  N7  1UL A 501      -8.264 -50.970 -15.622  1.00 66.52           N  
HETATM 2382  N6  1UL A 501      -8.215 -51.921 -16.688  1.00 66.35           N  
HETATM 2383  C19 1UL A 501      -9.329 -52.064 -17.468  1.00 63.13           C  
HETATM 2384  C18 1UL A 501      -9.579 -52.887 -18.563  1.00 62.95           C  
HETATM 2385  C17 1UL A 501     -10.825 -52.849 -19.197  1.00 61.22           C  
HETATM 2386  C16 1UL A 501     -11.819 -51.990 -18.735  1.00 63.34           C  
HETATM 2387  O   HOH A 601      -7.163 -58.297 -32.049  1.00 61.25           O  
HETATM 2388  O   HOH A 602       0.520 -50.618 -27.145  1.00 39.91           O  
HETATM 2389  O   HOH A 603       6.836 -60.088 -37.095  1.00 63.19           O  
HETATM 2390  O   HOH A 604       9.669 -51.230 -30.872  1.00 51.46           O  
HETATM 2391  O   HOH A 605     -10.457 -56.637 -42.594  1.00 59.54           O  
HETATM 2392  O   HOH A 606      -3.785 -67.201 -32.334  1.00 56.32           O  
HETATM 2393  O   HOH A 607      -5.097 -33.027 -48.059  1.00 39.03           O  
HETATM 2394  O   HOH A 608      -4.876 -30.704 -46.994  1.00 47.89           O  
HETATM 2395  O   HOH A 609     -13.312 -29.748 -38.803  1.00 31.99           O  
HETATM 2396  O   HOH A 610     -13.799 -31.666 -40.709  1.00 39.74           O  
HETATM 2397  O   HOH A 611     -11.861 -28.840 -30.778  1.00 39.41           O  
HETATM 2398  O   HOH A 612     -15.878 -31.479 -36.213  1.00 44.25           O  
HETATM 2399  O   HOH A 613     -17.921 -39.007 -44.070  1.00 52.33           O  
HETATM 2400  O   HOH A 614     -17.385 -31.443 -41.361  1.00 55.35           O  
HETATM 2401  O   HOH A 615     -18.096 -31.817 -32.215  1.00 41.64           O  
HETATM 2402  O   HOH A 616     -15.822 -53.136 -38.700  1.00 46.20           O  
HETATM 2403  O   HOH A 617     -19.285 -37.650 -38.044  1.00 48.11           O  
HETATM 2404  O   HOH A 618     -16.191 -22.634 -41.660  1.00 42.68           O  
HETATM 2405  O   HOH A 619     -14.626 -28.197 -47.434  1.00 44.88           O  
HETATM 2406  O   HOH A 620       8.175 -34.641 -39.178  1.00 42.62           O  
HETATM 2407  O   HOH A 621      12.155 -41.400 -20.352  1.00 66.60           O  
HETATM 2408  O   HOH A 622     -13.354 -26.080 -30.240  1.00 62.15           O  
HETATM 2409  O   HOH A 623       2.167 -52.563 -29.854  1.00 46.63           O  
HETATM 2410  O   HOH A 624      13.170 -45.905 -31.802  1.00 51.77           O  
HETATM 2411  O   HOH A 625     -23.497 -36.981 -30.380  1.00 46.34           O  
HETATM 2412  O   HOH A 626     -17.343 -35.361 -38.868  1.00 42.33           O  
HETATM 2413  O   HOH A 627     -14.647 -36.460 -45.575  1.00 49.47           O  
HETATM 2414  O   HOH A 628      -9.035 -60.294 -16.708  1.00 70.22           O  
HETATM 2415  O   HOH A 629      -3.497 -39.717 -13.255  1.00 54.09           O  
HETATM 2416  O   HOH A 630     -14.905 -29.032 -36.411  1.00 37.92           O  
HETATM 2417  O   HOH A 631       8.130 -39.047 -26.604  1.00 55.56           O  
HETATM 2418  O   HOH A 632     -19.084 -24.209 -41.921  1.00 42.80           O  
HETATM 2419  O   HOH A 633       6.337 -50.309 -43.626  1.00 58.85           O  
HETATM 2420  O   HOH A 634       9.106 -49.438 -42.029  1.00 70.28           O  
HETATM 2421  O   HOH A 635      -5.704 -48.925 -14.553  1.00 62.78           O  
CONECT  564  600                                                                
CONECT  600  564                                                                
CONECT 2354 2355                                                                
CONECT 2355 2354 2356 2357                                                      
CONECT 2356 2355                                                                
CONECT 2357 2355 2358 2362                                                      
CONECT 2358 2357 2359                                                           
CONECT 2359 2358 2360                                                           
CONECT 2360 2359 2361 2363                                                      
CONECT 2361 2360 2362                                                           
CONECT 2362 2357 2361                                                           
CONECT 2363 2360 2364 2367                                                      
CONECT 2364 2363 2365                                                           
CONECT 2365 2364 2366 2368                                                      
CONECT 2366 2365 2367                                                           
CONECT 2367 2363 2366                                                           
CONECT 2368 2365 2369 2374                                                      
CONECT 2369 2368 2370                                                           
CONECT 2370 2369 2371                                                           
CONECT 2371 2370 2372 2373                                                      
CONECT 2372 2371                                                                
CONECT 2373 2371 2374 2375                                                      
CONECT 2374 2368 2373 2377                                                      
CONECT 2375 2373 2376                                                           
CONECT 2376 2375 2377 2378                                                      
CONECT 2377 2374 2376                                                           
CONECT 2378 2376 2379 2386                                                      
CONECT 2379 2378 2380 2383                                                      
CONECT 2380 2379 2381                                                           
CONECT 2381 2380 2382                                                           
CONECT 2382 2381 2383                                                           
CONECT 2383 2379 2382 2384                                                      
CONECT 2384 2383 2385                                                           
CONECT 2385 2384 2386                                                           
CONECT 2386 2378 2385                                                           
MASTER      413    0    1   15   12    0    3    6 2409    1   35   24          
END                                                                             



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