CNRS Nantes University UFIP UFIP
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***  3NT1_ENZIMA_NEMO  ***

elNémo ID: 22030921275826620

Job options:

ID        	=	 22030921275826620
JOBID     	=	 3NT1_ENZIMA_NEMO
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 3NT1_ENZIMA_NEMO

HEADER    OXIDOREDUCTASE/OXIDOREDUCTASE INHIBITOR 02-JUL-10   3NT1              
TITLE     HIGH RESOLUTION STRUCTURE OF NAPROXEN:COX-2 COMPLEX.                  
CAVEAT     3NT1    NAG A 661 HAS WRONG CHIRALITY AT ATOM C1                     
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: PROSTAGLANDIN-ENDOPEROXIDE SYNTHASE 2;                     
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 FRAGMENT: UNP RESIDUES 18-604, CATALYTIC DOMAIN;                     
COMPND   5 EC: 1.14.99.1;                                                       
COMPND   6 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: MUS MUSCULUS;                                   
SOURCE   3 ORGANISM_COMMON: MOUSE;                                              
SOURCE   4 ORGANISM_TAXID: 10090;                                               
SOURCE   5 GENE: COX-2 PGHS-B, MCG_5001, PTGS2;                                 
SOURCE   6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 7108                                        
KEYWDS    PROSTAGLANDIN H2 SYNTHASE, CYCLOOXYGENASE-2, NAPROXEN,                
KEYWDS   2 OXIDOREDUCTASE, OXIDOREDUCTASE-OXIDOREDUCTASE INHIBITOR COMPLEX      
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    K.C.DUGGAN,J.MUSEE,M.J.WALTERS,J.M.HARP,J.R.KIEFER,J.A.OATES,         
AUTHOR   2 L.J.MARNETT                                                          
REVDAT   4   29-JUL-20 3NT1    1       CAVEAT COMPND REMARK HETNAM              
REVDAT   4 2                   1       LINK   SITE   ATOM                       
REVDAT   3   08-NOV-17 3NT1    1       REMARK                                   
REVDAT   2   17-NOV-10 3NT1    1       JRNL                                     
REVDAT   1   01-SEP-10 3NT1    0                                                
JRNL        AUTH   K.C.DUGGAN,M.J.WALTERS,J.MUSEE,J.M.HARP,J.R.KIEFER,          
JRNL        AUTH 2 J.A.OATES,L.J.MARNETT                                        
JRNL        TITL   MOLECULAR BASIS FOR CYCLOOXYGENASE INHIBITION BY THE         
JRNL        TITL 2 NON-STEROIDAL ANTI-INFLAMMATORY DRUG NAPROXEN.               
JRNL        REF    J.BIOL.CHEM.                  V. 285 34950 2010              
JRNL        REFN                   ISSN 0021-9258                               
JRNL        PMID   20810665                                                     
JRNL        DOI    10.1074/JBC.M110.162982                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.73 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.5.0109                                      
REMARK   3   AUTHORS     : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,              
REMARK   3               : NICHOLLS,WINN,LONG,VAGIN                             
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.73                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 30.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.2                           
REMARK   3   NUMBER OF REFLECTIONS             : 142975                         
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) : 0.168                           
REMARK   3   R VALUE            (WORKING SET) : 0.167                           
REMARK   3   FREE R VALUE                     : 0.186                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 7592                            
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) : 1.73                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.78                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 9768                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 91.72                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2340                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 524                          
REMARK   3   BIN FREE R VALUE                    : 0.2500                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 8948                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 314                                     
REMARK   3   SOLVENT ATOMS            : 1051                                    
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 26.68                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 1.81000                                              
REMARK   3    B22 (A**2) : 0.37000                                              
REMARK   3    B33 (A**2) : -2.18000                                             
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): 0.094         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.089         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.062         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 4.186         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.967                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.960                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  9578 ; 0.007 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  6590 ; 0.001 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 13028 ; 1.076 ; 2.012       
REMARK   3   BOND ANGLES OTHERS          (DEGREES): 15828 ; 0.852 ; 3.004       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  1108 ; 5.304 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   451 ;35.959 ;24.102       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  1558 ;12.240 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    47 ;12.029 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  1381 ; 0.065 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A): 10404 ; 0.004 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  1927 ; 0.001 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  5533 ; 0.340 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  2213 ; 0.072 ; 1.500       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  8996 ; 0.692 ; 2.000       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  4045 ; 1.280 ; 3.000       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  4031 ; 2.178 ; 4.500       
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    33        A   583                          
REMARK   3    ORIGIN FOR THE GROUP (A): -33.9786 -45.1901 -24.6335              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0212 T22:   0.0346                                     
REMARK   3      T33:   0.0335 T12:  -0.0058                                     
REMARK   3      T13:   0.0104 T23:   0.0145                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.9986 L22:   0.7678                                     
REMARK   3      L33:   0.8118 L12:  -0.4797                                     
REMARK   3      L13:  -0.1164 L23:  -0.0353                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0229 S12:  -0.1532 S13:  -0.0451                       
REMARK   3      S21:   0.0844 S22:   0.0468 S23:   0.0590                       
REMARK   3      S31:   0.0156 S32:  -0.0406 S33:  -0.0239                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B    33        B   583                          
REMARK   3    ORIGIN FOR THE GROUP (A): -40.0680 -36.9591 -63.0668              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0219 T22:   0.0348                                     
REMARK   3      T33:   0.0327 T12:   0.0013                                     
REMARK   3      T13:  -0.0102 T23:   0.0057                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.7071 L22:   0.9607                                     
REMARK   3      L33:   1.0265 L12:  -0.4183                                     
REMARK   3      L13:  -0.0762 L23:   0.0170                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0487 S12:   0.1342 S13:  -0.0298                       
REMARK   3      S21:  -0.1068 S22:  -0.0191 S23:   0.0347                       
REMARK   3      S31:   0.0966 S32:  -0.0166 S33:  -0.0296                       
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   : 1.40                                          
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 3NT1 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 07-JUL-10.                  
REMARK 100 THE DEPOSITION ID IS D_1000060243.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 14-MAR-10                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 8                                  
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 21-ID-F                            
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97856                            
REMARK 200  MONOCHROMATOR                  : CRYSTAL                            
REMARK 200  OPTICS                         : CRYSTAL MONOCHROMATOR              
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MAR CCD 300 MM                     
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 150576                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.730                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 35.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.6                               
REMARK 200  DATA REDUNDANCY                : 4.600                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.06700                            
REMARK 200   FOR THE DATA SET  : 23.3000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.73                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.79                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 97.8                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : 0.40900                            
REMARK 200   FOR SHELL         : 2.000                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
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   (%): 55.13                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.74                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: MMP550, MGCL2, PH 8, VAPOR DIFFUSION,    
REMARK 280  HANGING DROP, TEMPERATURE 291K                                      
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       61.14750            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       66.61650            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000       90.63450            
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000       61.14750            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       66.61650            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       90.63450            
REMARK 290   SMTRY1   7 -1.000000  0.000000  0.000000       61.14750            
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       66.61650            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000       90.63450            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000       61.14750            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000       66.61650            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000       90.63450            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 12820 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 41650 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -39.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D                            
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 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     ASP A   584                                                      
REMARK 465     PRO A   585                                                      
REMARK 465     GLN A   586                                                      
REMARK 465     PRO A   587                                                      
REMARK 465     THR A   588                                                      
REMARK 465     LYS A   589                                                      
REMARK 465     THR A   590                                                      
REMARK 465     ALA A   591                                                      
REMARK 465     THR A   592                                                      
REMARK 465     ILE A   593                                                      
REMARK 465     ASN A   594                                                      
REMARK 465     ALA A   595                                                      
REMARK 465     SER A   596                                                      
REMARK 465     ALA A   597                                                      
REMARK 465     SER A   598                                                      
REMARK 465     HIS A   599                                                      
REMARK 465     SER A   600                                                      
REMARK 465     ARG A   601                                                      
REMARK 465     LEU A   602                                                      
REMARK 465     ASP A   603                                                      
REMARK 465     ASP A   604                                                      
REMARK 465     ILE A   605                                                      
REMARK 465     ASN A   606                                                      
REMARK 465     PRO A   607                                                      
REMARK 465     THR A   608                                                      
REMARK 465     VAL A   609                                                      
REMARK 465     LEU A   610                                                      
REMARK 465     ILE A   611                                                      
REMARK 465     LYS A   612                                                      
REMARK 465     ARG A   613                                                      
REMARK 465     ARG A   614                                                      
REMARK 465     SER A   615                                                      
REMARK 465     THR A   616                                                      
REMARK 465     GLU A   617                                                      
REMARK 465     LEU A   618                                                      
REMARK 465     ASP B   584                                                      
REMARK 465     PRO B   585                                                      
REMARK 465     GLN B   586                                                      
REMARK 465     PRO B   587                                                      
REMARK 465     THR B   588                                                      
REMARK 465     LYS B   589                                                      
REMARK 465     THR B   590                                                      
REMARK 465     ALA B   591                                                      
REMARK 465     THR B   592                                                      
REMARK 465     ILE B   593                                                      
REMARK 465     ASN B   594                                                      
REMARK 465     ALA B   595                                                      
REMARK 465     SER B   596                                                      
REMARK 465     ALA B   597                                                      
REMARK 465     SER B   598                                                      
REMARK 465     HIS B   599                                                      
REMARK 465     SER B   600                                                      
REMARK 465     ARG B   601                                                      
REMARK 465     LEU B   602                                                      
REMARK 465     ASP B   603                                                      
REMARK 465     ASP B   604                                                      
REMARK 465     ILE B   605                                                      
REMARK 465     ASN B   606                                                      
REMARK 465     PRO B   607                                                      
REMARK 465     THR B   608                                                      
REMARK 465     VAL B   609                                                      
REMARK 465     LEU B   610                                                      
REMARK 465     ILE B   611                                                      
REMARK 465     LYS B   612                                                      
REMARK 465     ARG B   613                                                      
REMARK 465     ARG B   614                                                      
REMARK 465     SER B   615                                                      
REMARK 465     THR B   616                                                      
REMARK 465     GLU B   617                                                      
REMARK 465     LEU B   618                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    THR A 129      -89.79   -120.78                                   
REMARK 500    ARG A 185      -81.46    -89.43                                   
REMARK 500    ASP A 362       89.70   -152.89                                   
REMARK 500    TRP A 387       50.85    -91.90                                   
REMARK 500    GLU A 398     -118.92     55.65                                   
REMARK 500    ASN A 439       17.18   -140.32                                   
REMARK 500    SER A 496      -51.67     72.10                                   
REMARK 500    THR B 129      -91.23   -123.31                                   
REMARK 500    ARG B 185      -87.19    -89.49                                   
REMARK 500    GLU B 398     -121.29     57.97                                   
REMARK 500    ASN B 439       17.83   -140.82                                   
REMARK 500    SER B 496      -60.99     72.06                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             HEM A 619  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A 388   NE2                                                    
REMARK 620 2 HEM A 619   NA   94.5                                              
REMARK 620 3 HEM A 619   NB   91.7  88.0                                        
REMARK 620 4 HEM A 619   NC   87.8 177.7  91.4                                  
REMARK 620 5 HEM A 619   ND   89.0  90.5 178.4  90.0                            
REMARK 620 6 HOH A 943   O   173.4  78.9  88.4  98.8  90.8                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             HEM B 619  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS B 388   NE2                                                    
REMARK 620 2 HEM B 619   NA   92.8                                              
REMARK 620 3 HEM B 619   NB   92.4  88.7                                        
REMARK 620 4 HEM B 619   NC   89.1 178.1  90.8                                  
REMARK 620 5 HEM B 619   ND   86.9  90.5 178.9  90.0                            
REMARK 620 6 HOH B1002   O   173.6  80.8  87.9  97.3  92.7                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 3PGH   RELATED DB: PDB                                   
REMARK 900 COX-2:FLURBIPROFEN                                                   
REMARK 900 RELATED ID: 1PXX   RELATED DB: PDB                                   
REMARK 900 COX-2:DICLOFENAC                                                     
REMARK 900 RELATED ID: 1CQE   RELATED DB: PDB                                   
REMARK 900 COX-1:FLURBIPROFEN                                                   
REMARK 900 RELATED ID: 3NTB   RELATED DB: PDB                                   
DBREF  3NT1 A   33   618  UNP    Q543K3   Q543K3_MOUSE    18    604             
DBREF  3NT1 B   33   618  UNP    Q543K3   Q543K3_MOUSE    18    604             
SEQRES   1 A  587  ALA ASN PRO CYS CYS SER ASN PRO CYS GLN ASN ARG GLY          
SEQRES   2 A  587  GLU CYS MET SER THR GLY PHE ASP GLN TYR LYS CYS ASP          
SEQRES   3 A  587  CYS THR ARG THR GLY PHE TYR GLY GLU ASN CYS THR THR          
SEQRES   4 A  587  PRO GLU PHE LEU THR ARG ILE LYS LEU LEU LEU LYS PRO          
SEQRES   5 A  587  THR PRO ASN THR VAL HIS TYR ILE LEU THR HIS PHE LYS          
SEQRES   6 A  587  GLY VAL TRP ASN ILE VAL ASN ASN ILE PRO PHE LEU ARG          
SEQRES   7 A  587  SER LEU ILE MET LYS TYR VAL LEU THR SER ARG SER TYR          
SEQRES   8 A  587  LEU ILE ASP SER PRO PRO THR TYR ASN VAL HIS TYR GLY          
SEQRES   9 A  587  TYR LYS SER TRP GLU ALA PHE SER ASN LEU SER TYR TYR          
SEQRES  10 A  587  THR ARG ALA LEU PRO PRO VAL ALA ASP ASP CYS PRO THR          
SEQRES  11 A  587  PRO MET GLY VAL LYS GLY ASN LYS GLU LEU PRO ASP SER          
SEQRES  12 A  587  LYS GLU VAL LEU GLU LYS VAL LEU LEU ARG ARG GLU PHE          
SEQRES  13 A  587  ILE PRO ASP PRO GLN GLY SER ASN MET MET PHE ALA PHE          
SEQRES  14 A  587  PHE ALA GLN HIS PHE THR HIS GLN PHE PHE LYS THR ASP          
SEQRES  15 A  587  HIS LYS ARG GLY PRO GLY PHE THR ARG GLY LEU GLY HIS          
SEQRES  16 A  587  GLY VAL ASP LEU ASN HIS ILE TYR GLY GLU THR LEU ASP          
SEQRES  17 A  587  ARG GLN HIS LYS LEU ARG LEU PHE LYS ASP GLY LYS LEU          
SEQRES  18 A  587  LYS TYR GLN VAL ILE GLY GLY GLU VAL TYR PRO PRO THR          
SEQRES  19 A  587  VAL LYS ASP THR GLN VAL GLU MET ILE TYR PRO PRO HIS          
SEQRES  20 A  587  ILE PRO GLU ASN LEU GLN PHE ALA VAL GLY GLN GLU VAL          
SEQRES  21 A  587  PHE GLY LEU VAL PRO GLY LEU MET MET TYR ALA THR ILE          
SEQRES  22 A  587  TRP LEU ARG GLU HIS ASN ARG VAL CYS ASP ILE LEU LYS          
SEQRES  23 A  587  GLN GLU HIS PRO GLU TRP GLY ASP GLU GLN LEU PHE GLN          
SEQRES  24 A  587  THR SER ARG LEU ILE LEU ILE GLY GLU THR ILE LYS ILE          
SEQRES  25 A  587  VAL ILE GLU ASP TYR VAL GLN HIS LEU SER GLY TYR HIS          
SEQRES  26 A  587  PHE LYS LEU LYS PHE ASP PRO GLU LEU LEU PHE ASN GLN          
SEQRES  27 A  587  GLN PHE GLN TYR GLN ASN ARG ILE ALA SER GLU PHE ASN          
SEQRES  28 A  587  THR LEU TYR HIS TRP HIS PRO LEU LEU PRO ASP THR PHE          
SEQRES  29 A  587  ASN ILE GLU ASP GLN GLU TYR SER PHE LYS GLN PHE LEU          
SEQRES  30 A  587  TYR ASN ASN SER ILE LEU LEU GLU HIS GLY LEU THR GLN          
SEQRES  31 A  587  PHE VAL GLU SER PHE THR ARG GLN ILE ALA GLY ARG VAL          
SEQRES  32 A  587  ALA GLY GLY ARG ASN VAL PRO ILE ALA VAL GLN ALA VAL          
SEQRES  33 A  587  ALA LYS ALA SER ILE ASP GLN SER ARG GLU MET LYS TYR          
SEQRES  34 A  587  GLN SER LEU ASN GLU TYR ARG LYS ARG PHE SER LEU LYS          
SEQRES  35 A  587  PRO TYR THR SER PHE GLU GLU LEU THR GLY GLU LYS GLU          
SEQRES  36 A  587  MET ALA ALA GLU LEU LYS ALA LEU TYR SER ASP ILE ASP          
SEQRES  37 A  587  VAL MET GLU LEU TYR PRO ALA LEU LEU VAL GLU LYS PRO          
SEQRES  38 A  587  ARG PRO ASP ALA ILE PHE GLY GLU THR MET VAL GLU LEU          
SEQRES  39 A  587  GLY ALA PRO PHE SER LEU LYS GLY LEU MET GLY ASN PRO          
SEQRES  40 A  587  ILE CYS SER PRO GLN TYR TRP LYS PRO SER THR PHE GLY          
SEQRES  41 A  587  GLY GLU VAL GLY PHE LYS ILE ILE ASN THR ALA SER ILE          
SEQRES  42 A  587  GLN SER LEU ILE CYS ASN ASN VAL LYS GLY CYS PRO PHE          
SEQRES  43 A  587  THR SER PHE ASN VAL GLN ASP PRO GLN PRO THR LYS THR          
SEQRES  44 A  587  ALA THR ILE ASN ALA SER ALA SER HIS SER ARG LEU ASP          
SEQRES  45 A  587  ASP ILE ASN PRO THR VAL LEU ILE LYS ARG ARG SER THR          
SEQRES  46 A  587  GLU LEU                                                      
SEQRES   1 B  587  ALA ASN PRO CYS CYS SER ASN PRO CYS GLN ASN ARG GLY          
SEQRES   2 B  587  GLU CYS MET SER THR GLY PHE ASP GLN TYR LYS CYS ASP          
SEQRES   3 B  587  CYS THR ARG THR GLY PHE TYR GLY GLU ASN CYS THR THR          
SEQRES   4 B  587  PRO GLU PHE LEU THR ARG ILE LYS LEU LEU LEU LYS PRO          
SEQRES   5 B  587  THR PRO ASN THR VAL HIS TYR ILE LEU THR HIS PHE LYS          
SEQRES   6 B  587  GLY VAL TRP ASN ILE VAL ASN ASN ILE PRO PHE LEU ARG          
SEQRES   7 B  587  SER LEU ILE MET LYS TYR VAL LEU THR SER ARG SER TYR          
SEQRES   8 B  587  LEU ILE ASP SER PRO PRO THR TYR ASN VAL HIS TYR GLY          
SEQRES   9 B  587  TYR LYS SER TRP GLU ALA PHE SER ASN LEU SER TYR TYR          
SEQRES  10 B  587  THR ARG ALA LEU PRO PRO VAL ALA ASP ASP CYS PRO THR          
SEQRES  11 B  587  PRO MET GLY VAL LYS GLY ASN LYS GLU LEU PRO ASP SER          
SEQRES  12 B  587  LYS GLU VAL LEU GLU LYS VAL LEU LEU ARG ARG GLU PHE          
SEQRES  13 B  587  ILE PRO ASP PRO GLN GLY SER ASN MET MET PHE ALA PHE          
SEQRES  14 B  587  PHE ALA GLN HIS PHE THR HIS GLN PHE PHE LYS THR ASP          
SEQRES  15 B  587  HIS LYS ARG GLY PRO GLY PHE THR ARG GLY LEU GLY HIS          
SEQRES  16 B  587  GLY VAL ASP LEU ASN HIS ILE TYR GLY GLU THR LEU ASP          
SEQRES  17 B  587  ARG GLN HIS LYS LEU ARG LEU PHE LYS ASP GLY LYS LEU          
SEQRES  18 B  587  LYS TYR GLN VAL ILE GLY GLY GLU VAL TYR PRO PRO THR          
SEQRES  19 B  587  VAL LYS ASP THR GLN VAL GLU MET ILE TYR PRO PRO HIS          
SEQRES  20 B  587  ILE PRO GLU ASN LEU GLN PHE ALA VAL GLY GLN GLU VAL          
SEQRES  21 B  587  PHE GLY LEU VAL PRO GLY LEU MET MET TYR ALA THR ILE          
SEQRES  22 B  587  TRP LEU ARG GLU HIS ASN ARG VAL CYS ASP ILE LEU LYS          
SEQRES  23 B  587  GLN GLU HIS PRO GLU TRP GLY ASP GLU GLN LEU PHE GLN          
SEQRES  24 B  587  THR SER ARG LEU ILE LEU ILE GLY GLU THR ILE LYS ILE          
SEQRES  25 B  587  VAL ILE GLU ASP TYR VAL GLN HIS LEU SER GLY TYR HIS          
SEQRES  26 B  587  PHE LYS LEU LYS PHE ASP PRO GLU LEU LEU PHE ASN GLN          
SEQRES  27 B  587  GLN PHE GLN TYR GLN ASN ARG ILE ALA SER GLU PHE ASN          
SEQRES  28 B  587  THR LEU TYR HIS TRP HIS PRO LEU LEU PRO ASP THR PHE          
SEQRES  29 B  587  ASN ILE GLU ASP GLN GLU TYR SER PHE LYS GLN PHE LEU          
SEQRES  30 B  587  TYR ASN ASN SER ILE LEU LEU GLU HIS GLY LEU THR GLN          
SEQRES  31 B  587  PHE VAL GLU SER PHE THR ARG GLN ILE ALA GLY ARG VAL          
SEQRES  32 B  587  ALA GLY GLY ARG ASN VAL PRO ILE ALA VAL GLN ALA VAL          
SEQRES  33 B  587  ALA LYS ALA SER ILE ASP GLN SER ARG GLU MET LYS TYR          
SEQRES  34 B  587  GLN SER LEU ASN GLU TYR ARG LYS ARG PHE SER LEU LYS          
SEQRES  35 B  587  PRO TYR THR SER PHE GLU GLU LEU THR GLY GLU LYS GLU          
SEQRES  36 B  587  MET ALA ALA GLU LEU LYS ALA LEU TYR SER ASP ILE ASP          
SEQRES  37 B  587  VAL MET GLU LEU TYR PRO ALA LEU LEU VAL GLU LYS PRO          
SEQRES  38 B  587  ARG PRO ASP ALA ILE PHE GLY GLU THR MET VAL GLU LEU          
SEQRES  39 B  587  GLY ALA PRO PHE SER LEU LYS GLY LEU MET GLY ASN PRO          
SEQRES  40 B  587  ILE CYS SER PRO GLN TYR TRP LYS PRO SER THR PHE GLY          
SEQRES  41 B  587  GLY GLU VAL GLY PHE LYS ILE ILE ASN THR ALA SER ILE          
SEQRES  42 B  587  GLN SER LEU ILE CYS ASN ASN VAL LYS GLY CYS PRO PHE          
SEQRES  43 B  587  THR SER PHE ASN VAL GLN ASP PRO GLN PRO THR LYS THR          
SEQRES  44 B  587  ALA THR ILE ASN ALA SER ALA SER HIS SER ARG LEU ASP          
SEQRES  45 B  587  ASP ILE ASN PRO THR VAL LEU ILE LYS ARG ARG SER THR          
SEQRES  46 B  587  GLU LEU                                                      
MODRES 3NT1 ASN B  410  ASN  GLYCOSYLATION SITE                                 
MODRES 3NT1 ASN A  144  ASN  GLYCOSYLATION SITE                                 
MODRES 3NT1 ASN B  144  ASN  GLYCOSYLATION SITE                                 
MODRES 3NT1 ASN A   68  ASN  GLYCOSYLATION SITE                                 
MODRES 3NT1 ASN B   68  ASN  GLYCOSYLATION SITE                                 
MODRES 3NT1 ASN A  410  ASN  GLYCOSYLATION SITE                                 
HET    NAG  C   1      14                                                       
HET    NAG  C   2      14                                                       
HET    NAG  D   1      14                                                       
HET    NAG  D   2      14                                                       
HET    NAG  A 661      14                                                       
HET    NAG  A 681      14                                                       
HET    BOG  A   3      20                                                       
HET    NPS  A   5      17                                                       
HET    HEM  A 619      43                                                       
HET    BOG  A   6      20                                                       
HET    BOG  A 620      20                                                       
HET     CL  A   1       1                                                       
HET    NAG  B 681      14                                                       
HET    NPS  B   4      17                                                       
HET    BOG  B   3      20                                                       
HET    HEM  B 619      43                                                       
HET    NAG  B   9      14                                                       
HET     CL  B   1       1                                                       
HETNAM     NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE                         
HETNAM     BOG OCTYL BETA-D-GLUCOPYRANOSIDE                                     
HETNAM     NPS (2S)-2-(6-METHOXYNAPHTHALEN-2-YL)PROPANOIC ACID                  
HETNAM     HEM PROTOPORPHYRIN IX CONTAINING FE                                  
HETNAM      CL CHLORIDE ION                                                     
HETSYN     NPS NAPROXEN                                                         
HETSYN     HEM HEME                                                             
FORMUL   3  NAG    8(C8 H15 N O6)                                               
FORMUL   7  BOG    4(C14 H28 O6)                                                
FORMUL   8  NPS    2(C14 H14 O3)                                                
FORMUL   9  HEM    2(C34 H32 FE N4 O4)                                          
FORMUL  12   CL    2(CL 1-)                                                     
FORMUL  19  HOH   *1051(H2 O)                                                   
HELIX    1   1 GLU A   73  LYS A   83  1                                  11
HELIX    2   2 THR A   85  THR A   94  1                                  10
HELIX    3   3 PHE A   96  TYR A  122  1                                  28
HELIX    4   4 SER A  138  ASN A  144  1                                   7
HELIX    5   5 ASP A  173  LEU A  182  1                                  10
HELIX    6   6 ASN A  195  HIS A  207  1                                  13
HELIX    7   7 LEU A  230  GLY A  235  1                                   6
HELIX    8   8 THR A  237  ARG A  245  1                                   9
HELIX    9   9 THR A  265  GLN A  270  1                                   6
HELIX   10  10 PRO A  280  GLN A  284  1                                   5
HELIX   11  11 VAL A  295  HIS A  320  1                                  26
HELIX   12  12 GLY A  324  GLY A  354  1                                  31
HELIX   13  13 ASP A  362  PHE A  367  1                                   6
HELIX   14  14 ALA A  378  LEU A  391  1                                  14
HELIX   15  15 SER A  403  LEU A  408  1                                   6
HELIX   16  16 ASN A  411  GLN A  429  1                                  19
HELIX   17  17 PRO A  441  MET A  458  1                                  18
HELIX   18  18 SER A  462  PHE A  470  1                                   9
HELIX   19  19 SER A  477  GLY A  483  1                                   7
HELIX   20  20 LYS A  485  GLU A  510  1                                  26
HELIX   21  21 GLY A  519  SER A  541  1                                  23
HELIX   22  22 LYS A  546  THR A  561  1                                  16
HELIX   23  23 SER A  563  VAL A  572  1                                  10
SHEET    1   1 1 GLU A  46  GLY A  51  0
SHEET    2   2 1 GLN A  54  ASP A  58  0
SHEET    3   3 1 PHE A  64  TYR A  65  0
SHEET    4   4 1 THR A  71  PRO A  72  0
SHEET    5   5 1 GLN A 255  ILE A 257  0
SHEET    6   6 1 GLU A 260  TYR A 262  0
SHEET    7   7 1 PHE A 395  ILE A 397  0
SHEET    8   8 1 GLN A 400  TYR A 402  0
SSBOND   1 CYS A   36    CYS A   47                          1555   1555  2.05  
SSBOND   2 CYS A   37    CYS A  159                          1555   1555  2.02  
SSBOND   3 CYS A   41    CYS A   57                          1555   1555  2.02  
SSBOND   4 CYS A   59    CYS A   69                          1555   1555  2.03  
SSBOND   5 CYS A  569    CYS A  575                          1555   1555  2.03  
SSBOND   6 CYS B   36    CYS B   47                          1555   1555  2.05  
SSBOND   7 CYS B   37    CYS B  159                          1555   1555  2.03  
SSBOND   8 CYS B   41    CYS B   57                          1555   1555  2.03  
SSBOND   9 CYS B   59    CYS B   69                          1555   1555  2.04  
SSBOND  10 CYS B  569    CYS B  575                          1555   1555  2.03  
LINK         ND2 ASN A  68                 C1  NAG A 661     1555   1555  1.45  
LINK         ND2 ASN A 144                 C1  NAG C   1     1555   1555  1.45  
LINK         ND2 ASN A 410                 C1  NAG A 681     1555   1555  1.45  
LINK         C1  NAG B   9                 ND2 ASN B  68     1555   1555  1.45  
LINK         ND2 ASN B 144                 C1  NAG D   1     1555   1555  1.45  
LINK         ND2 ASN B 410                 C1  NAG B 681     1555   1555  1.44  
LINK         O4  NAG C   1                 C1  NAG C   2     1555   1555  1.44  
LINK         O4  NAG D   1                 C1  NAG D   2     1555   1555  1.44  
LINK         NE2 HIS A 388                FE   HEM A 619     1555   1555  2.76  
LINK        FE   HEM A 619                 O   HOH A 943     1555   1555  2.47  
LINK         NE2 HIS B 388                FE   HEM B 619     1555   1555  2.77  
LINK        FE   HEM B 619                 O   HOH B1002     1555   1555  2.49  
CISPEP   1 SER A  126    PRO A  127          0         0.75                     
CISPEP   2 SER B  126    PRO B  127          0         1.42                     
CRYST1  122.295  133.233  181.269  90.00  90.00  90.00 I 2 2 2      16          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.008177  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.007506  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.005517        0.00000                         
ATOM      1  N   ALA A  33     -54.058 -16.845 -23.914  1.00 39.61           N
ANISOU    1  N   ALA A  33     5169   4755   5124   1499    762   -155       N
ATOM      2  CA  ALA A  33     -54.196 -16.053 -25.171  1.00 39.89           C
ANISOU    2  CA  ALA A  33     5231   4720   5206   1548    763   -104       C
ATOM      3  C   ALA A  33     -54.684 -16.948 -26.308  1.00 38.92           C
ANISOU    3  C   ALA A  33     5021   4687   5080   1529    730    -21       C
ATOM      4  O   ALA A  33     -55.818 -16.811 -26.772  1.00 39.65           O
ANISOU    4  O   ALA A  33     5058   4841   5166   1613    740     26       O
ATOM      5  CB  ALA A  33     -52.874 -15.401 -25.528  1.00 40.03           C
ANISOU    5  CB  ALA A  33     5344   4593   5274   1491    753   -131       C
ATOM      6  N   ASN A  34     -53.826 -17.861 -26.754  1.00 37.65           N
ANISOU    6  N   ASN A  34     4847   4533   4923   1420    689     -8       N
ATOM      7  CA  ASN A  34     -54.220 -18.877 -27.724  1.00 36.60           C
ANISOU    7  CA  ASN A  34     4632   4491   4783   1389    650     56       C
ATOM      8  C   ASN A  34     -55.411 -19.672 -27.163  1.00 36.26           C
ANISOU    8  C   ASN A  34     4486   4585   4708   1413    655     68       C
ATOM      9  O   ASN A  34     -55.340 -20.171 -26.041  1.00 35.96           O
ANISOU    9  O   ASN A  34     4434   4584   4645   1378    669     30       O
ATOM     10  CB  ASN A  34     -53.033 -19.804 -28.025  1.00 35.64           C
ANISOU   10  CB  ASN A  34     4519   4357   4667   1265    609     53       C
ATOM     11  CG  ASN A  34     -53.248 -20.660 -29.259  1.00 35.84           C
ANISOU   11  CG  ASN A  34     4483   4445   4690   1238    566    113       C
ATOM     12  OD1 ASN A  34     -54.300 -21.277 -29.430  1.00 36.38           O
ANISOU   12  OD1 ASN A  34     4464   4618   4742   1263    553    142       O
ATOM     13  ND2 ASN A  34     -52.233 -20.719 -30.120  1.00 35.80           N
ANISOU   13  ND2 ASN A  34     4521   4379   4703   1184    543    129       N
ATOM     14  N   PRO A  35     -56.525 -19.763 -27.919  1.00 35.87           N
ANISOU   14  N   PRO A  35     4362   4611   4658   1476    646    121       N
ATOM     15  CA  PRO A  35     -57.682 -20.517 -27.414  1.00 35.62           C
ANISOU   15  CA  PRO A  35     4220   4708   4607   1493    654    136       C
ATOM     16  C   PRO A  35     -57.439 -22.022 -27.223  1.00 34.16           C
ANISOU   16  C   PRO A  35     3970   4595   4416   1379    621    140       C
ATOM     17  O   PRO A  35     -58.258 -22.696 -26.598  1.00 34.64           O
ANISOU   17  O   PRO A  35     3945   4751   4465   1378    636    149       O
ATOM     18  CB  PRO A  35     -58.755 -20.279 -28.484  1.00 36.38           C
ANISOU   18  CB  PRO A  35     4250   4860   4711   1576    637    192       C
ATOM     19  CG  PRO A  35     -58.016 -19.867 -29.695  1.00 36.21           C
ANISOU   19  CG  PRO A  35     4294   4760   4705   1569    606    215       C
ATOM     20  CD  PRO A  35     -56.812 -19.132 -29.219  1.00 36.23           C
ANISOU   20  CD  PRO A  35     4416   4631   4720   1542    632    171       C
ATOM     21  N   CYS A  36     -56.333 -22.538 -27.749  1.00 32.40           N
ANISOU   21  N   CYS A  36     3786   4324   4201   1288    582    137       N
ATOM     22  CA  CYS A  36     -55.977 -23.943 -27.567  1.00 31.08           C
ANISOU   22  CA  CYS A  36     3571   4208   4031   1181    552    138       C
ATOM     23  C   CYS A  36     -55.117 -24.186 -26.313  1.00 30.08           C
ANISOU   23  C   CYS A  36     3494   4050   3885   1124    574     92       C
ATOM     24  O   CYS A  36     -54.722 -25.316 -26.044  1.00 28.68           O
ANISOU   24  O   CYS A  36     3288   3906   3703   1038    555     93       O
ATOM     25  CB  CYS A  36     -55.282 -24.473 -28.830  1.00 30.59           C
ANISOU   25  CB  CYS A  36     3518   4121   3983   1118    496    160       C
ATOM     26  SG  CYS A  36     -56.411 -24.641 -30.249  1.00 31.09           S
ANISOU   26  SG  CYS A  36     3496   4262   4056   1172    453    213       S
ATOM     27  N   CYS A  37     -54.861 -23.136 -25.531  1.00 30.15           N
ANISOU   27  N   CYS A  37     3576   3998   3882   1176    613     49       N
ATOM     28  CA  CYS A  37     -53.989 -23.240 -24.353  1.00 29.82           C
ANISOU   28  CA  CYS A  37     3589   3926   3815   1131    628     -5       C
ATOM     29  C   CYS A  37     -54.453 -24.246 -23.298  1.00 29.44           C
ANISOU   29  C   CYS A  37     3478   3976   3734   1107    648      0       C
ATOM     30  O   CYS A  37     -53.624 -24.828 -22.607  1.00 29.17           O
ANISOU   30  O   CYS A  37     3469   3936   3678   1042    641    -25       O
ATOM     31  CB  CYS A  37     -53.803 -21.874 -23.684  1.00 30.49           C
ANISOU   31  CB  CYS A  37     3759   3934   3893   1203    664    -60       C
ATOM     32  SG  CYS A  37     -52.685 -20.782 -24.563  1.00 31.64           S
ANISOU   32  SG  CYS A  37     4007   3931   4084   1194    645    -80       S
ATOM     33  N   SER A  38     -55.763 -24.455 -23.180  1.00 29.67           N
ANISOU   33  N   SER A  38     3420   4094   3759   1160    675     37       N
ATOM     34  CA  SER A  38     -56.306 -25.389 -22.183  1.00 29.65           C
ANISOU   34  CA  SER A  38     3350   4185   3729   1142    705     53       C
ATOM     35  C   SER A  38     -56.203 -26.867 -22.592  1.00 28.95           C
ANISOU   35  C   SER A  38     3192   4144   3663   1041    670     95       C
ATOM     36  O   SER A  38     -56.604 -27.745 -21.823  1.00 29.20           O
ANISOU   36  O   SER A  38     3166   4247   3681   1015    697    119       O
ATOM     37  CB  SER A  38     -57.767 -25.052 -21.892  1.00 30.64           C
ANISOU   37  CB  SER A  38     3400   4390   3850   1236    753     80       C
ATOM     38  OG  SER A  38     -58.570 -25.295 -23.029  1.00 30.83           O
ANISOU   38  OG  SER A  38     3343   4456   3917   1242    725    128       O
ATOM     39  N   ASN A  39     -55.677 -27.138 -23.789  1.00 27.68           N
ANISOU   39  N   ASN A  39     3039   3942   3535    987    614    107       N
ATOM     40  CA  ASN A  39     -55.605 -28.500 -24.338  1.00 26.81           C
ANISOU   40  CA  ASN A  39     2868   3869   3452    897    574    141       C
ATOM     41  C   ASN A  39     -56.992 -29.158 -24.387  1.00 26.95           C
ANISOU   41  C   ASN A  39     2762   3985   3492    908    587    186       C
ATOM     42  O   ASN A  39     -57.170 -30.274 -23.886  1.00 26.30           O
ANISOU   42  O   ASN A  39     2623   3950   3418    848    596    210       O
ATOM     43  CB  ASN A  39     -54.624 -29.355 -23.522  1.00 26.46           C
ANISOU   43  CB  ASN A  39     2856   3810   3386    818    574    127       C
ATOM     44  CG  ASN A  39     -53.289 -28.658 -23.286  1.00 26.90           C
ANISOU   44  CG  ASN A  39     3024   3778   3420    810    565     75       C
ATOM     45  OD1 ASN A  39     -52.611 -28.256 -24.229  1.00 27.73           O
ANISOU   45  OD1 ASN A  39     3174   3817   3546    795    529     65       O
ATOM     46  ND2 ASN A  39     -52.906 -28.521 -22.024  1.00 28.47           N
ANISOU   46  ND2 ASN A  39     3264   3979   3577    820    597     44       N
ATOM     47  N   PRO A  40     -57.983 -28.466 -24.992  1.00 26.88           N
ANISOU   47  N   PRO A  40     2708   4006   3499    985    588    201       N
ATOM     48  CA  PRO A  40     -59.369 -28.932 -24.915  1.00 27.42           C
ANISOU   48  CA  PRO A  40     2653   4175   3592   1006    606    241       C
ATOM     49  C   PRO A  40     -59.670 -30.212 -25.691  1.00 27.19           C
ANISOU   49  C   PRO A  40     2533   4188   3609    921    555    269       C
ATOM     50  O   PRO A  40     -60.591 -30.940 -25.311  1.00 27.51           O
ANISOU   50  O   PRO A  40     2469   4305   3677    902    576    301       O
ATOM     51  CB  PRO A  40     -60.169 -27.761 -25.498  1.00 28.06           C
ANISOU   51  CB  PRO A  40     2721   4265   3674   1116    610    244       C
ATOM     52  CG  PRO A  40     -59.229 -27.083 -26.421  1.00 27.65           C
ANISOU   52  CG  PRO A  40     2767   4121   3617   1122    568    222       C
ATOM     53  CD  PRO A  40     -57.866 -27.237 -25.803  1.00 27.16           C
ANISOU   53  CD  PRO A  40     2803   3985   3534   1057    573    187       C
ATOM     54  N   CYS A  41     -58.920 -30.489 -26.762  1.00 26.12           N
ANISOU   54  N   CYS A  41     2435   4003   3486    871    490    257       N
ATOM     55  CA  CYS A  41     -59.233 -31.625 -27.626  1.00 26.14           C
ANISOU   55  CA  CYS A  41     2357   4042   3532    799    432    273       C
ATOM     56  C   CYS A  41     -58.688 -32.905 -27.009  1.00 25.39           C
ANISOU   56  C   CYS A  41     2256   3939   3451    696    437    279       C
ATOM     57  O   CYS A  41     -57.501 -32.992 -26.668  1.00 24.88           O
ANISOU   57  O   CYS A  41     2283   3810   3361    659    440    260       O
ATOM     58  CB  CYS A  41     -58.677 -31.432 -29.043  1.00 25.80           C
ANISOU   58  CB  CYS A  41     2359   3957   3488    797    362    259       C
ATOM     59  SG  CYS A  41     -59.145 -29.857 -29.812  1.00 27.23           S
ANISOU   59  SG  CYS A  41     2569   4132   3646    927    360    261       S
ATOM     60  N   GLN A  42     -59.564 -33.895 -26.859  1.00 25.71           N
ANISOU   60  N   GLN A  42     2186   4043   3538    650    440    307       N
ATOM     61  CA  GLN A  42     -59.200 -35.163 -26.229  1.00 25.46           C
ANISOU   61  CA  GLN A  42     2140   4006   3529    555    453    323       C
ATOM     62  C   GLN A  42     -58.970 -36.254 -27.261  1.00 25.15           C
ANISOU   62  C   GLN A  42     2071   3949   3537    469    380    316       C
ATOM     63  O   GLN A  42     -59.240 -36.066 -28.451  1.00 25.37           O
ANISOU   63  O   GLN A  42     2077   3985   3578    485    318    298       O
ATOM     64  CB  GLN A  42     -60.305 -35.598 -25.257  1.00 26.30           C
ANISOU   64  CB  GLN A  42     2143   4187   3663    556    517    367       C
ATOM     65  CG  GLN A  42     -60.676 -34.546 -24.220  1.00 27.15           C
ANISOU   65  CG  GLN A  42     2270   4324   3721    652    594    373       C
ATOM     66  CD  GLN A  42     -59.481 -34.090 -23.398  1.00 26.43           C
ANISOU   66  CD  GLN A  42     2308   4173   3563    667    622    347       C
ATOM     67  OE1 GLN A  42     -58.829 -34.892 -22.727  1.00 26.25           O
ANISOU   67  OE1 GLN A  42     2313   4131   3530    607    639    358       O
ATOM     68  NE2 GLN A  42     -59.183 -32.796 -23.457  1.00 26.75           N
ANISOU   68  NE2 GLN A  42     2425   4179   3558    748    626    312       N
ATOM     69  N   ASN A  43     -58.449 -37.390 -26.795  1.00 24.98           N
ANISOU   69  N   ASN A  43     2054   3901   3535    383    387    327       N
ATOM     70  CA  ASN A  43     -58.344 -38.612 -27.599  1.00 25.21           C
ANISOU   70  CA  ASN A  43     2046   3913   3619    295    326    321       C
ATOM     71  C   ASN A  43     -57.571 -38.422 -28.904  1.00 24.93           C
ANISOU   71  C   ASN A  43     2076   3832   3566    295    249    279       C
ATOM     72  O   ASN A  43     -57.920 -38.980 -29.948  1.00 24.60           O
ANISOU   72  O   ASN A  43     1983   3802   3561    263    183    261       O
ATOM     73  CB  ASN A  43     -59.739 -39.185 -27.849  1.00 26.21           C
ANISOU   73  CB  ASN A  43     2031   4108   3818    271    315    341       C
ATOM     74  CG  ASN A  43     -60.434 -39.566 -26.558  1.00 27.25           C
ANISOU   74  CG  ASN A  43     2095   4282   3975    258    399    392       C
ATOM     75  OD1 ASN A  43     -59.906 -40.360 -25.784  1.00 28.07           O
ANISOU   75  OD1 ASN A  43     2226   4354   4085    202    435    417       O
ATOM     76  ND2 ASN A  43     -61.597 -38.985 -26.305  1.00 26.81           N
ANISOU   76  ND2 ASN A  43     1953   4301   3931    317    434    414       N
ATOM     77  N   ARG A  44     -56.520 -37.612 -28.808  1.00 24.63           N
ANISOU   77  N   ARG A  44     2148   3742   3468    333    259    262       N
ATOM     78  CA  ARG A  44     -55.613 -37.307 -29.914  1.00 24.63           C
ANISOU   78  CA  ARG A  44     2223   3693   3442    340    204    230       C
ATOM     79  C   ARG A  44     -56.215 -36.439 -31.031  1.00 24.76           C
ANISOU   79  C   ARG A  44     2221   3739   3448    411    164    220       C
ATOM     80  O   ARG A  44     -55.622 -36.307 -32.107  1.00 24.60           O
ANISOU   80  O   ARG A  44     2248   3690   3408    418    115    200       O
ATOM     81  CB  ARG A  44     -54.974 -38.590 -30.452  1.00 24.69           C
ANISOU   81  CB  ARG A  44     2238   3666   3476    253    155    217       C
ATOM     82  CG  ARG A  44     -54.392 -39.433 -29.319  1.00 26.13           C
ANISOU   82  CG  ARG A  44     2441   3821   3668    192    198    235       C
ATOM     83  CD  ARG A  44     -53.193 -40.219 -29.725  1.00 28.36           C
ANISOU   83  CD  ARG A  44     2787   4043   3948    136    163    217       C
ATOM     84  NE  ARG A  44     -52.214 -39.337 -30.346  1.00 29.96           N
ANISOU   84  NE  ARG A  44     3077   4206   4100    177    144    192       N
ATOM     85  CZ  ARG A  44     -51.349 -39.701 -31.283  1.00 31.06           C
ANISOU   85  CZ  ARG A  44     3263   4306   4232    154     96    169       C
ATOM     86  NH1 ARG A  44     -51.300 -40.955 -31.730  1.00 32.63           N
ANISOU   86  NH1 ARG A  44     3436   4495   4467     91     57    160       N
ATOM     87  NH2 ARG A  44     -50.529 -38.792 -31.780  1.00 31.43           N
ANISOU   87  NH2 ARG A  44     3384   4322   4238    195     91    155       N
ATOM     88  N   GLY A  45     -57.362 -35.824 -30.762  1.00 25.10           N
ANISOU   88  N   GLY A  45     2197   3842   3499    472    190    237       N
ATOM     89  CA  GLY A  45     -57.902 -34.792 -31.640  1.00 25.66           C
ANISOU   89  CA  GLY A  45     2261   3939   3550    560    166    233       C
ATOM     90  C   GLY A  45     -56.980 -33.584 -31.633  1.00 25.23           C
ANISOU   90  C   GLY A  45     2323   3820   3443    620    191    227       C
ATOM     91  O   GLY A  45     -56.268 -33.352 -30.655  1.00 24.64           O
ANISOU   91  O   GLY A  45     2311   3699   3350    608    241    224       O
ATOM     92  N   GLU A  46     -56.988 -32.819 -32.723  1.00 25.38           N
ANISOU   92  N   GLU A  46     2371   3834   3440    684    158    225       N
ATOM     93  CA  GLU A  46     -56.055 -31.700 -32.894  1.00 25.10           C
ANISOU   93  CA  GLU A  46     2446   3725   3366    733    179    222       C
ATOM     94  C   GLU A  46     -56.779 -30.363 -32.789  1.00 25.08           C
ANISOU   94  C   GLU A  46     2446   3735   3350    842    215    238       C
ATOM     95  O   GLU A  46     -57.842 -30.177 -33.385  1.00 25.69           O
ANISOU   95  O   GLU A  46     2453   3877   3433    899    190    252       O
ATOM     96  CB  GLU A  46     -55.328 -31.823 -34.236  1.00 25.06           C
ANISOU   96  CB  GLU A  46     2489   3690   3342    726    124    217       C
ATOM     97  CG  GLU A  46     -54.453 -33.061 -34.288  1.00 26.73           C
ANISOU   97  CG  GLU A  46     2714   3876   3564    625     96    198       C
ATOM     98  CD  GLU A  46     -53.733 -33.260 -35.596  1.00 28.57           C
ANISOU   98  CD  GLU A  46     2992   4087   3774    621     45    190       C
ATOM     99  OE1 GLU A  46     -53.708 -32.322 -36.424  1.00 30.47           O
ANISOU   99  OE1 GLU A  46     3271   4320   3986    696     39    205       O
ATOM    100  OE2 GLU A  46     -53.170 -34.370 -35.778  1.00 30.25           O
ANISOU  100  OE2 GLU A  46     3206   4289   3997    546     14    172       O
ATOM    101  N   CYS A  47     -56.195 -29.445 -32.021  1.00 24.72           N
ANISOU  101  N   CYS A  47     2481   3625   3288    872    270    231       N
ATOM    102  CA  CYS A  47     -56.798 -28.142 -31.755  1.00 25.40           C
ANISOU  102  CA  CYS A  47     2581   3706   3362    976    312    240       C
ATOM    103  C   CYS A  47     -56.257 -27.097 -32.719  1.00 25.28           C
ANISOU  103  C   CYS A  47     2649   3626   3330   1036    304    251       C
ATOM    104  O   CYS A  47     -55.049 -26.986 -32.914  1.00 24.41           O
ANISOU  104  O   CYS A  47     2622   3438   3214    996    303    240       O
ATOM    105  CB  CYS A  47     -56.499 -27.696 -30.323  1.00 25.71           C
ANISOU  105  CB  CYS A  47     2665   3709   3394    979    377    220       C
ATOM    106  SG  CYS A  47     -57.508 -26.309 -29.765  1.00 27.48           S
ANISOU  106  SG  CYS A  47     2886   3946   3609   1108    434    225       S
ATOM    107  N   MET A  48     -57.165 -26.338 -33.315  1.00 25.76           N
ANISOU  107  N   MET A  48     2682   3720   3385   1134    301    275       N
ATOM    108  CA  MET A  48     -56.809 -25.234 -34.191  1.00 26.18           C
ANISOU  108  CA  MET A  48     2812   3713   3423   1209    304    297       C
ATOM    109  C   MET A  48     -57.636 -24.024 -33.770  1.00 26.95           C
ANISOU  109  C   MET A  48     2912   3806   3520   1322    352    309       C
ATOM    110  O   MET A  48     -58.843 -24.144 -33.538  1.00 27.56           O
ANISOU  110  O   MET A  48     2898   3972   3602   1368    352    318       O
ATOM    111  CB  MET A  48     -57.119 -25.619 -35.636  1.00 26.33           C
ANISOU  111  CB  MET A  48     2793   3786   3425   1230    239    322       C
ATOM    112  CG  MET A  48     -56.799 -24.564 -36.687  1.00 27.02           C
ANISOU  112  CG  MET A  48     2955   3822   3489   1314    241    357       C
ATOM    113  SD  MET A  48     -57.463 -25.003 -38.310  1.00 26.91           S
ANISOU  113  SD  MET A  48     2881   3904   3441   1364    160    385       S
ATOM    114  CE  MET A  48     -59.215 -24.746 -38.065  1.00 27.75           C
ANISOU  114  CE  MET A  48     2871   4119   3555   1455    153    395       C
ATOM    115  N   SER A  49     -56.994 -22.864 -33.658  1.00 27.00           N
ANISOU  115  N   SER A  49     3021   3711   3527   1367    395    310       N
ATOM    116  CA  SER A  49     -57.728 -21.624 -33.407  1.00 28.11           C
ANISOU  116  CA  SER A  49     3178   3834   3670   1485    439    322       C
ATOM    117  C   SER A  49     -58.559 -21.282 -34.639  1.00 29.23           C
ANISOU  117  C   SER A  49     3280   4030   3796   1581    407    372       C
ATOM    118  O   SER A  49     -58.140 -21.545 -35.763  1.00 28.59           O
ANISOU  118  O   SER A  49     3215   3948   3701   1567    365    396       O
ATOM    119  CB  SER A  49     -56.774 -20.473 -33.068  1.00 28.05           C
ANISOU  119  CB  SER A  49     3294   3688   3675   1503    489    308       C
ATOM    120  OG  SER A  49     -55.900 -20.182 -34.146  1.00 27.72           O
ANISOU  120  OG  SER A  49     3320   3577   3634   1494    474    337       O
ATOM    121  N   THR A  50     -59.743 -20.717 -34.428  1.00 30.72           N
ANISOU  121  N   THR A  50     3416   4272   3984   1683    427    387       N
ATOM    122  CA  THR A  50     -60.613 -20.315 -35.529  1.00 32.21           C
ANISOU  122  CA  THR A  50     3563   4520   4155   1790    396    434       C
ATOM    123  C   THR A  50     -60.972 -18.836 -35.399  1.00 33.76           C
ANISOU  123  C   THR A  50     3819   4654   4354   1922    453    458       C
ATOM    124  O   THR A  50     -61.943 -18.358 -35.986  1.00 35.42           O
ANISOU  124  O   THR A  50     3984   4923   4551   2036    442    496       O
ATOM    125  CB  THR A  50     -61.887 -21.177 -35.556  1.00 32.87           C
ANISOU  125  CB  THR A  50     3498   4752   4239   1795    354    435       C
ATOM    126  OG1 THR A  50     -62.543 -21.095 -34.287  1.00 33.29           O
ANISOU  126  OG1 THR A  50     3504   4835   4311   1809    404    414       O
ATOM    127  CG2 THR A  50     -61.530 -22.631 -35.839  1.00 31.60           C
ANISOU  127  CG2 THR A  50     3283   4642   4081   1667    293    413       C
ATOM    128  N   GLY A  51     -60.150 -18.116 -34.645  1.00 34.07           N
ANISOU  128  N   GLY A  51     3962   4570   4412   1907    511    432       N
ATOM    129  CA  GLY A  51     -60.405 -16.729 -34.286  1.00 35.12           C
ANISOU  129  CA  GLY A  51     4162   4623   4558   2020    572    439       C
ATOM    130  C   GLY A  51     -59.591 -16.422 -33.048  1.00 35.15           C
ANISOU  130  C   GLY A  51     4245   4527   4585   1962    622    379       C
ATOM    131  O   GLY A  51     -58.881 -17.290 -32.536  1.00 34.08           O
ANISOU  131  O   GLY A  51     4105   4394   4451   1842    607    340       O
ATOM    132  N   PHE A  52     -59.696 -15.194 -32.551  1.00 36.32           N
ANISOU  132  N   PHE A  52     4464   4586   4750   2050    679    368       N
ATOM    133  CA  PHE A  52     -58.896 -14.778 -31.399  1.00 36.80           C
ANISOU  133  CA  PHE A  52     4608   4543   4832   2003    722    301       C
ATOM    134  C   PHE A  52     -59.241 -15.520 -30.103  1.00 37.01           C
ANISOU  134  C   PHE A  52     4572   4650   4839   1957    732    246       C
ATOM    135  O   PHE A  52     -58.360 -15.746 -29.274  1.00 36.76           O
ANISOU  135  O   PHE A  52     4589   4568   4812   1871    740    191       O
ATOM    136  CB  PHE A  52     -58.999 -13.264 -31.193  1.00 37.95           C
ANISOU  136  CB  PHE A  52     4846   4571   5003   2115    780    296       C
ATOM    137  CG  PHE A  52     -58.228 -12.474 -32.207  1.00 38.31           C
ANISOU  137  CG  PHE A  52     4985   4490   5079   2129    786    340       C
ATOM    138  CD1 PHE A  52     -58.865 -11.910 -33.300  1.00 40.02           C
ANISOU  138  CD1 PHE A  52     5198   4718   5291   2242    786    416       C
ATOM    139  CD2 PHE A  52     -56.853 -12.325 -32.086  1.00 38.76           C
ANISOU  139  CD2 PHE A  52     5131   4425   5171   2031    793    309       C
ATOM    140  CE1 PHE A  52     -58.147 -11.186 -34.246  1.00 40.26           C
ANISOU  140  CE1 PHE A  52     5317   4633   5348   2258    800    467       C
ATOM    141  CE2 PHE A  52     -56.129 -11.607 -33.028  1.00 38.80           C
ANISOU  141  CE2 PHE A  52     5218   4314   5210   2040    807    357       C
ATOM    142  CZ  PHE A  52     -56.777 -11.038 -34.107  1.00 39.71           C
ANISOU  142  CZ  PHE A  52     5334   4436   5317   2155    813    439       C
ATOM    143  N   ASP A  53     -60.504 -15.915 -29.943  1.00 37.74           N
ANISOU  143  N   ASP A  53     4556   4871   4911   2014    730    266       N
ATOM    144  CA  ASP A  53     -60.965 -16.560 -28.705  1.00 38.18           C
ANISOU  144  CA  ASP A  53     4547   5010   4949   1986    752    227       C
ATOM    145  C   ASP A  53     -61.843 -17.794 -28.957  1.00 37.74           C
ANISOU  145  C   ASP A  53     4347   5109   4882   1952    714    261       C
ATOM    146  O   ASP A  53     -62.702 -18.122 -28.138  1.00 38.11           O
ANISOU  146  O   ASP A  53     4315   5248   4920   1976    742    254       O
ATOM    147  CB  ASP A  53     -61.750 -15.549 -27.858  1.00 39.67           C
ANISOU  147  CB  ASP A  53     4752   5190   5131   2112    815    204       C
ATOM    148  CG  ASP A  53     -60.896 -14.387 -27.380  1.00 41.42           C
ANISOU  148  CG  ASP A  53     5116   5254   5369   2137    854    153       C
ATOM    149  OD1 ASP A  53     -61.316 -13.227 -27.579  1.00 45.61           O
ANISOU  149  OD1 ASP A  53     5693   5723   5912   2256    887    163       O
ATOM    150  OD2 ASP A  53     -59.818 -14.630 -26.792  1.00 43.29           O
ANISOU  150  OD2 ASP A  53     5414   5427   5607   2039    850    101       O
ATOM    151  N   GLN A  54     -61.630 -18.473 -30.082  1.00 36.66           N
ANISOU  151  N   GLN A  54     4176   5002   4752   1895    653    296       N
ATOM    152  CA  GLN A  54     -62.433 -19.641 -30.450  1.00 36.27           C
ANISOU  152  CA  GLN A  54     3991   5089   4701   1857    607    322       C
ATOM    153  C   GLN A  54     -61.529 -20.726 -31.040  1.00 34.31           C
ANISOU  153  C   GLN A  54     3745   4833   4456   1726    549    320       C
ATOM    154  O   GLN A  54     -60.526 -20.414 -31.684  1.00 33.41           O
ANISOU  154  O   GLN A  54     3723   4629   4342   1700    533    321       O
ATOM    155  CB  GLN A  54     -63.525 -19.242 -31.447  1.00 37.50           C
ANISOU  155  CB  GLN A  54     4078   5315   4857   1967    582    371       C
ATOM    156  CG  GLN A  54     -64.495 -18.180 -30.910  1.00 40.84           C
ANISOU  156  CG  GLN A  54     4489   5751   5276   2109    641    378       C
ATOM    157  CD  GLN A  54     -65.587 -17.795 -31.897  1.00 44.53           C
ANISOU  157  CD  GLN A  54     4882   6296   5740   2226    613    430       C
ATOM    158  OE1 GLN A  54     -66.068 -18.624 -32.671  1.00 47.52           O
ANISOU  158  OE1 GLN A  54     5160   6776   6121   2196    549    453       O
ATOM    159  NE2 GLN A  54     -65.992 -16.528 -31.863  1.00 47.09           N
ANISOU  159  NE2 GLN A  54     5256   6575   6062   2364    658    444       N
ATOM    160  N   TYR A  55     -61.874 -21.992 -30.793  1.00 33.15           N
ANISOU  160  N   TYR A  55     3499   4780   4316   1643    523    317       N
ATOM    161  CA  TYR A  55     -61.112 -23.130 -31.326  1.00 31.75           C
ANISOU  161  CA  TYR A  55     3317   4604   4145   1521    467    312       C
ATOM    162  C   TYR A  55     -62.025 -24.161 -31.985  1.00 31.77           C
ANISOU  162  C   TYR A  55     3185   4724   4160   1495    409    334       C
ATOM    163  O   TYR A  55     -63.235 -24.173 -31.766  1.00 31.95           O
ANISOU  163  O   TYR A  55     3107   4839   4196   1550    419    349       O
ATOM    164  CB  TYR A  55     -60.283 -23.806 -30.219  1.00 30.98           C
ANISOU  164  CB  TYR A  55     3251   4472   4047   1417    491    276       C
ATOM    165  CG  TYR A  55     -61.110 -24.558 -29.188  1.00 31.23           C
ANISOU  165  CG  TYR A  55     3184   4596   4087   1394    520    275       C
ATOM    166  CD1 TYR A  55     -61.384 -25.921 -29.334  1.00 30.73           C
ANISOU  166  CD1 TYR A  55     3025   4605   4045   1303    482    286       C
ATOM    167  CD2 TYR A  55     -61.625 -23.906 -28.074  1.00 32.64           C
ANISOU  167  CD2 TYR A  55     3365   4785   4253   1464    588    265       C
ATOM    168  CE1 TYR A  55     -62.153 -26.605 -28.394  1.00 31.44           C
ANISOU  168  CE1 TYR A  55     3021   4775   4149   1280    517    295       C
ATOM    169  CE2 TYR A  55     -62.390 -24.586 -27.128  1.00 33.06           C
ANISOU  169  CE2 TYR A  55     3325   4926   4310   1448    623    272       C
ATOM    170  CZ  TYR A  55     -62.646 -25.935 -27.295  1.00 32.16           C
ANISOU  170  CZ  TYR A  55     3114   4881   4222   1353    589    291       C
ATOM    171  OH  TYR A  55     -63.406 -26.612 -26.368  1.00 31.88           O
ANISOU  171  OH  TYR A  55     2985   4929   4198   1335    632    308       O
ATOM    172  N   LYS A  56     -61.422 -25.024 -32.794  1.00 31.04           N
ANISOU  172  N   LYS A  56     3094   4629   4070   1411    348    331       N
ATOM    173  CA  LYS A  56     -62.094 -26.204 -33.325  1.00 31.16           C
ANISOU  173  CA  LYS A  56     2990   4742   4105   1357    287    335       C
ATOM    174  C   LYS A  56     -61.203 -27.414 -33.091  1.00 29.48           C
ANISOU  174  C   LYS A  56     2792   4503   3906   1221    266    311       C
ATOM    175  O   LYS A  56     -59.976 -27.318 -33.210  1.00 28.67           O
ANISOU  175  O   LYS A  56     2795   4313   3787   1180    267    298       O
ATOM    176  CB  LYS A  56     -62.367 -26.045 -34.823  1.00 31.92           C
ANISOU  176  CB  LYS A  56     3070   4873   4185   1410    218    353       C
ATOM    177  CG  LYS A  56     -63.001 -27.278 -35.465  1.00 34.09           C
ANISOU  177  CG  LYS A  56     3225   5245   4481   1350    141    345       C
ATOM    178  CD  LYS A  56     -63.476 -27.012 -36.876  1.00 37.21           C
ANISOU  178  CD  LYS A  56     3594   5695   4851   1427     71    360       C
ATOM    179  CE  LYS A  56     -64.092 -28.266 -37.483  1.00 39.05           C
ANISOU  179  CE  LYS A  56     3706   6022   5108   1361    -13    337       C
ATOM    180  NZ  LYS A  56     -65.386 -28.634 -36.831  1.00 40.91           N
ANISOU  180  NZ  LYS A  56     3796   6353   5393   1359     -4    339       N
ATOM    181  N   CYS A  57     -61.814 -28.550 -32.763  1.00 28.61           N
ANISOU  181  N   CYS A  57     2575   4467   3830   1151    250    308       N
ATOM    182  CA  CYS A  57     -61.079 -29.810 -32.695  1.00 27.33           C
ANISOU  182  CA  CYS A  57     2416   4283   3685   1025    222    289       C
ATOM    183  C   CYS A  57     -61.302 -30.619 -33.960  1.00 27.14           C
ANISOU  183  C   CYS A  57     2334   4303   3674    990    134    282       C
ATOM    184  O   CYS A  57     -62.437 -30.782 -34.415  1.00 27.75           O
ANISOU  184  O   CYS A  57     2303   4468   3772   1021     98    288       O
ATOM    185  CB  CYS A  57     -61.505 -30.644 -31.490  1.00 27.49           C
ANISOU  185  CB  CYS A  57     2364   4341   3740    961    264    293       C
ATOM    186  SG  CYS A  57     -61.162 -29.873 -29.921  1.00 26.30           S
ANISOU  186  SG  CYS A  57     2284   4146   3562    996    363    293       S
ATOM    187  N   ASP A  58     -60.209 -31.117 -34.517  1.00 26.10           N
ANISOU  187  N   ASP A  58     2274   4113   3528    927     98    264       N
ATOM    188  CA  ASP A  58     -60.239 -32.023 -35.650  1.00 26.16           C
ANISOU  188  CA  ASP A  58     2242   4154   3544    883     14    246       C
ATOM    189  C   ASP A  58     -60.153 -33.441 -35.094  1.00 25.62           C
ANISOU  189  C   ASP A  58     2122   4090   3524    761      5    228       C
ATOM    190  O   ASP A  58     -59.096 -33.873 -34.646  1.00 24.65           O
ANISOU  190  O   ASP A  58     2070   3898   3397    695     26    219       O
ATOM    191  CB  ASP A  58     -59.053 -31.727 -36.573  1.00 25.63           C
ANISOU  191  CB  ASP A  58     2289   4019   3430    892    -12    239       C
ATOM    192  CG  ASP A  58     -59.063 -32.561 -37.834  1.00 26.89           C
ANISOU  192  CG  ASP A  58     2419   4215   3582    864   -100    216       C
ATOM    193  OD1 ASP A  58     -59.921 -33.467 -37.966  1.00 27.31           O
ANISOU  193  OD1 ASP A  58     2364   4338   3675    822   -148    197       O
ATOM    194  OD2 ASP A  58     -58.194 -32.304 -38.700  1.00 27.74           O
ANISOU  194  OD2 ASP A  58     2612   4281   3646    885   -121    216       O
ATOM    195  N   CYS A  59     -61.278 -34.154 -35.114  1.00 26.67           N
ANISOU  195  N   CYS A  59     2125   4301   3706    734    -24    225       N
ATOM    196  CA  CYS A  59     -61.349 -35.493 -34.525  1.00 26.85           C
ANISOU  196  CA  CYS A  59     2088   4327   3788    620    -24    216       C
ATOM    197  C   CYS A  59     -61.125 -36.605 -35.549  1.00 26.87           C
ANISOU  197  C   CYS A  59     2070   4328   3811    548   -112    178       C
ATOM    198  O   CYS A  59     -61.386 -37.771 -35.260  1.00 27.13           O
ANISOU  198  O   CYS A  59     2035   4367   3906    455   -125    168       O
ATOM    199  CB  CYS A  59     -62.697 -35.704 -33.830  1.00 27.80           C
ANISOU  199  CB  CYS A  59     2072   4526   3964    619      5    238       C
ATOM    200  SG  CYS A  59     -63.194 -34.397 -32.682  1.00 29.22           S
ANISOU  200  SG  CYS A  59     2258   4725   4117    721    106    278       S
ATOM    201  N   THR A  60     -60.619 -36.251 -36.732  1.00 26.53           N
ANISOU  201  N   THR A  60     2090   4272   3717    592   -168    158       N
ATOM    202  CA  THR A  60     -60.378 -37.225 -37.800  1.00 26.56           C
ANISOU  202  CA  THR A  60     2086   4279   3727    540   -256    115       C
ATOM    203  C   THR A  60     -59.631 -38.465 -37.298  1.00 25.99           C
ANISOU  203  C   THR A  60     2036   4143   3695    422   -248     98       C
ATOM    204  O   THR A  60     -58.565 -38.355 -36.702  1.00 25.28           O
ANISOU  204  O   THR A  60     2042   3982   3583    402   -196    113       O
ATOM    205  CB  THR A  60     -59.575 -36.595 -38.964  1.00 26.11           C
ANISOU  205  CB  THR A  60     2130   4198   3591    607   -293    105       C
ATOM    206  OG1 THR A  60     -60.311 -35.499 -39.511  1.00 25.83           O
ANISOU  206  OG1 THR A  60     2072   4222   3519    721   -304    125       O
ATOM    207  CG2 THR A  60     -59.318 -37.621 -40.062  1.00 26.70           C
ANISOU  207  CG2 THR A  60     2201   4280   3664    560   -383     55       C
ATOM    208  N   ARG A  61     -60.227 -39.634 -37.543  1.00 26.91           N
ANISOU  208  N   ARG A  61     2061   4287   3876    346   -302     68       N
ATOM    209  CA  ARG A  61     -59.649 -40.948 -37.208  1.00 26.55           C
ANISOU  209  CA  ARG A  61     2026   4182   3879    234   -306     49       C
ATOM    210  C   ARG A  61     -59.311 -41.182 -35.725  1.00 26.26           C
ANISOU  210  C   ARG A  61     2008   4099   3873    183   -212     93       C
ATOM    211  O   ARG A  61     -58.498 -42.046 -35.404  1.00 26.28           O
ANISOU  211  O   ARG A  61     2057   4035   3892    110   -202     88       O
ATOM    212  CB  ARG A  61     -58.427 -41.248 -38.097  1.00 26.13           C
ANISOU  212  CB  ARG A  61     2081   4072   3776    226   -350     14       C
ATOM    213  CG  ARG A  61     -58.793 -41.612 -39.521  1.00 26.79           C
ANISOU  213  CG  ARG A  61     2131   4199   3848    241   -455    -42       C
ATOM    214  CD  ARG A  61     -57.554 -41.921 -40.360  1.00 26.64           C
ANISOU  214  CD  ARG A  61     2222   4126   3774    240   -490    -74       C
ATOM    215  NE  ARG A  61     -56.745 -40.728 -40.623  1.00 25.13           N
ANISOU  215  NE  ARG A  61     2134   3917   3495    328   -454    -42       N
ATOM    216  CZ  ARG A  61     -57.047 -39.777 -41.510  1.00 24.93           C
ANISOU  216  CZ  ARG A  61     2119   3944   3409    428   -482    -37       C
ATOM    217  NH1 ARG A  61     -58.158 -39.841 -42.232  1.00 25.27           N
ANISOU  217  NH1 ARG A  61     2073   4071   3459    460   -554    -65       N
ATOM    218  NH2 ARG A  61     -56.231 -38.735 -41.662  1.00 23.18           N
ANISOU  218  NH2 ARG A  61     1997   3690   3121    497   -438     -2       N
ATOM    219  N   THR A  62     -59.943 -40.435 -34.824  1.00 26.39           N
ANISOU  219  N   THR A  62     1985   4151   3891    227   -144    135       N
ATOM    220  CA  THR A  62     -59.725 -40.630 -33.388  1.00 26.14           C
ANISOU  220  CA  THR A  62     1965   4089   3878    190    -55    177       C
ATOM    221  C   THR A  62     -60.633 -41.715 -32.813  1.00 26.96           C
ANISOU  221  C   THR A  62     1950   4219   4074    108    -41    194       C
ATOM    222  O   THR A  62     -60.330 -42.283 -31.769  1.00 27.20           O
ANISOU  222  O   THR A  62     1992   4214   4128     55     21    226       O
ATOM    223  CB  THR A  62     -59.997 -39.346 -32.584  1.00 25.97           C
ANISOU  223  CB  THR A  62     1960   4095   3814    278     19    213       C
ATOM    224  OG1 THR A  62     -61.351 -38.933 -32.786  1.00 25.97           O
ANISOU  224  OG1 THR A  62     1848   4180   3840    327      9    222       O
ATOM    225  CG2 THR A  62     -59.029 -38.236 -32.999  1.00 24.92           C
ANISOU  225  CG2 THR A  62     1950   3919   3599    352     19    202       C
ATOM    226  N   GLY A  63     -61.743 -41.985 -33.490  1.00 28.11           N
ANISOU  226  N   GLY A  63     1979   4428   4273    100    -98    174       N
ATOM    227  CA  GLY A  63     -62.772 -42.882 -32.960  1.00 29.04           C
ANISOU  227  CA  GLY A  63     1964   4579   4492     25    -81    194       C
ATOM    228  C   GLY A  63     -63.832 -42.149 -32.151  1.00 29.88           C
ANISOU  228  C   GLY A  63     1983   4761   4608     82    -12    243       C
ATOM    229  O   GLY A  63     -64.779 -42.767 -31.656  1.00 30.61           O
ANISOU  229  O   GLY A  63     1953   4891   4785     29     15    269       O
ATOM    230  N   PHE A  64     -63.680 -40.830 -32.034  1.00 29.39           N
ANISOU  230  N   PHE A  64     1982   4719   4465    190     20    254       N
ATOM    231  CA  PHE A  64     -64.595 -39.985 -31.273  1.00 30.06           C
ANISOU  231  CA  PHE A  64     2004   4874   4546    264     89    297       C
ATOM    232  C   PHE A  64     -65.044 -38.816 -32.134  1.00 30.60           C
ANISOU  232  C   PHE A  64     2066   4996   4565    375     46    278       C
ATOM    233  O   PHE A  64     -64.428 -38.520 -33.160  1.00 30.27           O
ANISOU  233  O   PHE A  64     2100   4927   4475    403    -21    241       O
ATOM    234  CB  PHE A  64     -63.898 -39.430 -30.030  1.00 29.55           C
ANISOU  234  CB  PHE A  64     2036   4769   4422    298    188    334       C
ATOM    235  CG  PHE A  64     -63.445 -40.479 -29.053  1.00 29.07           C
ANISOU  235  CG  PHE A  64     1987   4661   4395    207    242    363       C
ATOM    236  CD1 PHE A  64     -62.253 -41.163 -29.246  1.00 28.75           C
ANISOU  236  CD1 PHE A  64     2044   4538   4344    143    214    342       C
ATOM    237  CD2 PHE A  64     -64.196 -40.758 -27.918  1.00 30.83           C
ANISOU  237  CD2 PHE A  64     2129   4927   4658    193    327    418       C
ATOM    238  CE1 PHE A  64     -61.823 -42.122 -28.335  1.00 28.76           C
ANISOU  238  CE1 PHE A  64     2059   4495   4372     67    265    375       C
ATOM    239  CE2 PHE A  64     -63.773 -41.716 -27.002  1.00 30.15           C
ANISOU  239  CE2 PHE A  64     2059   4799   4599    116    381    455       C
ATOM    240  CZ  PHE A  64     -62.594 -42.402 -27.214  1.00 29.60           C
ANISOU  240  CZ  PHE A  64     2085   4642   4518     54    349    434       C
ATOM    241  N   TYR A  65     -66.111 -38.150 -31.707  1.00 31.53           N
ANISOU  241  N   TYR A  65     2096   5192   4693    444     89    308       N
ATOM    242  CA  TYR A  65     -66.582 -36.927 -32.356  1.00 32.22           C
ANISOU  242  CA  TYR A  65     2181   5330   4730    567     64    302       C
ATOM    243  C   TYR A  65     -67.117 -35.953 -31.302  1.00 32.42           C
ANISOU  243  C   TYR A  65     2193   5393   4732    656    161    346       C
ATOM    244  O   TYR A  65     -66.991 -36.204 -30.104  1.00 32.35           O
ANISOU  244  O   TYR A  65     2192   5367   4732    625    246    377       O
ATOM    245  CB  TYR A  65     -67.630 -37.251 -33.428  1.00 33.39           C
ANISOU  245  CB  TYR A  65     2196   5562   4927    566    -29    275       C
ATOM    246  CG  TYR A  65     -68.862 -37.953 -32.913  1.00 35.59           C
ANISOU  246  CG  TYR A  65     2302   5916   5303    512     -8    297       C
ATOM    247  CD1 TYR A  65     -69.999 -37.236 -32.562  1.00 37.71           C
ANISOU  247  CD1 TYR A  65     2467   6276   5583    596     32    330       C
ATOM    248  CD2 TYR A  65     -68.891 -39.338 -32.786  1.00 36.48           C
ANISOU  248  CD2 TYR A  65     2352   6005   5502    378    -27    288       C
ATOM    249  CE1 TYR A  65     -71.135 -37.879 -32.092  1.00 39.24           C
ANISOU  249  CE1 TYR A  65     2493   6543   5873    545     55    355       C
ATOM    250  CE2 TYR A  65     -70.020 -39.991 -32.318  1.00 38.02           C
ANISOU  250  CE2 TYR A  65     2384   6264   5798    321     -3    313       C
ATOM    251  CZ  TYR A  65     -71.138 -39.258 -31.973  1.00 39.27           C
ANISOU  251  CZ  TYR A  65     2434   6519   5966    404     39    348       C
ATOM    252  OH  TYR A  65     -72.262 -39.905 -31.507  1.00 41.01           O
ANISOU  252  OH  TYR A  65     2483   6806   6292    346     67    377       O
ATOM    253  N   GLY A  66     -67.685 -34.836 -31.744  1.00 33.09           N
ANISOU  253  N   GLY A  66     2264   5527   4780    774    152    348       N
ATOM    254  CA  GLY A  66     -68.151 -33.796 -30.833  1.00 33.70           C
ANISOU  254  CA  GLY A  66     2343   5633   4827    876    241    382       C
ATOM    255  C   GLY A  66     -67.117 -32.698 -30.671  1.00 32.93           C
ANISOU  255  C   GLY A  66     2413   5453   4646    949    274    374       C
ATOM    256  O   GLY A  66     -65.973 -32.837 -31.122  1.00 31.85           O
ANISOU  256  O   GLY A  66     2388   5235   4478    908    239    349       O
ATOM    257  N   GLU A  67     -67.514 -31.612 -30.010  1.00 33.61           N
ANISOU  257  N   GLU A  67     2514   5557   4699   1056    344    394       N
ATOM    258  CA  GLU A  67     -66.683 -30.410 -29.915  1.00 33.34           C
ANISOU  258  CA  GLU A  67     2629   5444   4594   1139    373    383       C
ATOM    259  C   GLU A  67     -65.247 -30.689 -29.457  1.00 32.01           C
ANISOU  259  C   GLU A  67     2594   5171   4396   1065    390    363       C
ATOM    260  O   GLU A  67     -64.317 -30.091 -29.994  1.00 31.07           O
ANISOU  260  O   GLU A  67     2593   4976   4237   1087    366    343       O
ATOM    261  CB  GLU A  67     -67.327 -29.359 -28.999  1.00 34.41           C
ANISOU  261  CB  GLU A  67     2759   5609   4706   1253    459    403       C
ATOM    262  CG  GLU A  67     -66.562 -28.028 -28.983  1.00 35.66           C
ANISOU  262  CG  GLU A  67     3068   5680   4802   1344    484    386       C
ATOM    263  CD  GLU A  67     -67.180 -26.976 -28.075  1.00 38.83           C
ANISOU  263  CD  GLU A  67     3473   6102   5179   1461    568    397       C
ATOM    264  OE1 GLU A  67     -68.206 -27.259 -27.423  1.00 41.24           O
ANISOU  264  OE1 GLU A  67     3662   6497   5509   1478    612    422       O
ATOM    265  OE2 GLU A  67     -66.629 -25.853 -28.013  1.00 40.78           O
ANISOU  265  OE2 GLU A  67     3840   6272   5384   1538    591    380       O
ATOM    266  N   ASN A  68     -65.079 -31.591 -28.488  1.00 31.51           N
ANISOU  266  N   ASN A  68     2510   5108   4355    980    432    373       N
ATOM    267  CA  ASN A  68     -63.763 -31.913 -27.918  1.00 30.84           C
ANISOU  267  CA  ASN A  68     2541   4935   4241    914    451    357       C
ATOM    268  C   ASN A  68     -63.286 -33.342 -28.197  1.00 29.61           C
ANISOU  268  C   ASN A  68     2363   4760   4126    784    406    353       C
ATOM    269  O   ASN A  68     -62.366 -33.822 -27.534  1.00 27.96           O
ANISOU  269  O   ASN A  68     2224   4498   3903    723    430    350       O
ATOM    270  CB  ASN A  68     -63.781 -31.707 -26.399  1.00 31.54           C
ANISOU  270  CB  ASN A  68     2651   5030   4305    936    547    372       C
ATOM    271  CG  ASN A  68     -64.078 -30.279 -25.997  1.00 35.40           C
ANISOU  271  CG  ASN A  68     3185   5519   4748   1065    597    365       C
ATOM    272  OD1 ASN A  68     -63.833 -29.341 -26.759  1.00 33.29           O
ANISOU  272  OD1 ASN A  68     2980   5211   4459   1129    565    346       O
ATOM    273  ND2 ASN A  68     -64.595 -30.107 -24.764  1.00 44.60           N
ANISOU  273  ND2 ASN A  68     4322   6727   5897   1106    680    383       N
ATOM    274  N   CYS A  69     -63.903 -34.016 -29.166  1.00 29.73           N
ANISOU  274  N   CYS A  69     2284   4821   4192    745    337    351       N
ATOM    275  CA  CYS A  69     -63.582 -35.410 -29.495  1.00 29.58           C
ANISOU  275  CA  CYS A  69     2234   4783   4222    623    290    342       C
ATOM    276  C   CYS A  69     -63.754 -36.337 -28.284  1.00 29.78           C
ANISOU  276  C   CYS A  69     2210   4818   4286    550    356    375       C
ATOM    277  O   CYS A  69     -62.912 -37.203 -28.038  1.00 28.58           O
ANISOU  277  O   CYS A  69     2108   4610   4142    466    353    372       O
ATOM    278  CB  CYS A  69     -62.153 -35.531 -30.042  1.00 28.72           C
ANISOU  278  CB  CYS A  69     2255   4583   4075    586    247    310       C
ATOM    279  SG  CYS A  69     -61.716 -34.308 -31.296  1.00 29.40           S
ANISOU  279  SG  CYS A  69     2427   4641   4102    680    194    284       S
ATOM    280  N   THR A  70     -64.840 -36.146 -27.534  1.00 30.98           N
ANISOU  280  N   THR A  70     2266   5045   4461    589    418    412       N
ATOM    281  CA  THR A  70     -65.128 -36.980 -26.355  1.00 31.86           C
ANISOU  281  CA  THR A  70     2321   5176   4608    530    493    456       C
ATOM    282  C   THR A  70     -66.350 -37.899 -26.499  1.00 33.35           C
ANISOU  282  C   THR A  70     2340   5436   4896    470    486    484       C
ATOM    283  O   THR A  70     -66.604 -38.710 -25.608  1.00 33.89           O
ANISOU  283  O   THR A  70     2355   5516   5007    410    548    529       O
ATOM    284  CB  THR A  70     -65.321 -36.121 -25.084  1.00 32.07           C
ANISOU  284  CB  THR A  70     2376   5230   4579    619    595    484       C
ATOM    285  OG1 THR A  70     -66.343 -35.145 -25.311  1.00 32.83           O
ANISOU  285  OG1 THR A  70     2407   5396   4670    721    605    487       O
ATOM    286  CG2 THR A  70     -64.020 -35.433 -24.701  1.00 31.56           C
ANISOU  286  CG2 THR A  70     2477   5086   4429    653    609    454       C
ATOM    287  N   THR A  71     -67.106 -37.780 -27.591  1.00 34.05           N
ANISOU  287  N   THR A  71     2342   5573   5023    485    412    461       N
ATOM    288  CA  THR A  71     -68.231 -38.687 -27.835  1.00 35.52           C
ANISOU  288  CA  THR A  71     2359   5823   5313    417    390    477       C
ATOM    289  C   THR A  71     -67.747 -39.868 -28.665  1.00 35.46           C
ANISOU  289  C   THR A  71     2352   5760   5359    300    303    440       C
ATOM    290  O   THR A  71     -67.374 -39.694 -29.825  1.00 35.11           O
ANISOU  290  O   THR A  71     2352   5696   5291    312    210    388       O
ATOM    291  CB  THR A  71     -69.398 -37.991 -28.564  1.00 36.30           C
ANISOU  291  CB  THR A  71     2347   6017   5429    497    348    467       C
ATOM    292  OG1 THR A  71     -69.775 -36.810 -27.850  1.00 36.72           O
ANISOU  292  OG1 THR A  71     2414   6114   5425    619    427    495       O
ATOM    293  CG2 THR A  71     -70.607 -38.922 -28.665  1.00 38.29           C
ANISOU  293  CG2 THR A  71     2409   6342   5797    422    333    484       C
ATOM    294  N   PRO A  72     -67.738 -41.077 -28.076  1.00 36.24           N
ANISOU  294  N   PRO A  72     2408   5830   5530    191    336    470       N
ATOM    295  CA  PRO A  72     -67.231 -42.236 -28.806  1.00 36.31           C
ANISOU  295  CA  PRO A  72     2428   5775   5594     79    259    432       C
ATOM    296  C   PRO A  72     -68.199 -42.777 -29.852  1.00 37.83           C
ANISOU  296  C   PRO A  72     2480   6017   5877     32    166    394       C
ATOM    297  O   PRO A  72     -69.415 -42.743 -29.654  1.00 38.84           O
ANISOU  297  O   PRO A  72     2461   6227   6067     38    188    420       O
ATOM    298  CB  PRO A  72     -66.999 -43.273 -27.704  1.00 36.43           C
ANISOU  298  CB  PRO A  72     2438   5744   5659    -10    339    486       C
ATOM    299  CG  PRO A  72     -67.967 -42.921 -26.642  1.00 37.33           C
ANISOU  299  CG  PRO A  72     2459   5935   5789     32    441    554       C
ATOM    300  CD  PRO A  72     -68.185 -41.435 -26.714  1.00 36.99           C
ANISOU  300  CD  PRO A  72     2447   5950   5658    169    451    541       C
ATOM    301  N   GLU A  73     -67.647 -43.259 -30.962  1.00 38.21           N
ANISOU  301  N   GLU A  73     2572   6018   5928    -12     63    330       N
ATOM    302  CA  GLU A  73     -68.409 -44.026 -31.944  1.00 40.04           C
ANISOU  302  CA  GLU A  73     2681   6280   6250    -79    -35    281       C
ATOM    303  C   GLU A  73     -68.732 -45.391 -31.337  1.00 41.14           C
ANISOU  303  C   GLU A  73     2735   6383   6513   -213     -1    309       C
ATOM    304  O   GLU A  73     -68.094 -45.808 -30.369  1.00 40.31           O
ANISOU  304  O   GLU A  73     2699   6213   6406   -251     82    358       O
ATOM    305  CB  GLU A  73     -67.606 -44.196 -33.236  1.00 39.63           C
ANISOU  305  CB  GLU A  73     2721   6183   6156    -84   -149    202       C
ATOM    306  CG  GLU A  73     -67.408 -42.891 -34.012  1.00 40.52           C
ANISOU  306  CG  GLU A  73     2902   6336   6157     46   -191    177       C
ATOM    307  CD  GLU A  73     -66.271 -42.947 -35.019  1.00 41.68           C
ANISOU  307  CD  GLU A  73     3180   6420   6234     53   -268    120       C
ATOM    308  OE1 GLU A  73     -65.589 -43.988 -35.115  1.00 42.58           O
ANISOU  308  OE1 GLU A  73     3338   6458   6381    -40   -290     96       O
ATOM    309  OE2 GLU A  73     -66.055 -41.931 -35.714  1.00 43.67           O
ANISOU  309  OE2 GLU A  73     3494   6699   6398    155   -301    105       O
ATOM    310  N   PHE A  74     -69.719 -46.084 -31.901  1.00 43.14           N
ANISOU  310  N   PHE A  74     2839   6677   6878   -282    -65    279       N
ATOM    311  CA  PHE A  74     -70.189 -47.343 -31.318  1.00 44.67           C
ANISOU  311  CA  PHE A  74     2930   6836   7207   -412    -26    313       C
ATOM    312  C   PHE A  74     -69.064 -48.367 -31.166  1.00 44.21           C
ANISOU  312  C   PHE A  74     2985   6650   7162   -501    -22    306       C
ATOM    313  O   PHE A  74     -68.918 -48.980 -30.108  1.00 44.28           O
ANISOU  313  O   PHE A  74     2998   6611   7217   -558     75    376       O
ATOM    314  CB  PHE A  74     -71.333 -47.937 -32.141  1.00 46.52           C
ANISOU  314  CB  PHE A  74     2989   7123   7562   -479   -118    261       C
ATOM    315  CG  PHE A  74     -71.957 -49.152 -31.511  1.00 48.74           C
ANISOU  315  CG  PHE A  74     3146   7372   8000   -614    -69    303       C
ATOM    316  CD1 PHE A  74     -72.856 -49.019 -30.460  1.00 50.80           C
ANISOU  316  CD1 PHE A  74     3290   7695   8319   -613     43    392       C
ATOM    317  CD2 PHE A  74     -71.635 -50.427 -31.959  1.00 50.22           C
ANISOU  317  CD2 PHE A  74     3337   7464   8280   -739   -130    255       C
ATOM    318  CE1 PHE A  74     -73.431 -50.139 -29.870  1.00 52.75           C
ANISOU  318  CE1 PHE A  74     3419   7908   8715   -738     97    440       C
ATOM    319  CE2 PHE A  74     -72.208 -51.553 -31.375  1.00 51.81           C
ANISOU  319  CE2 PHE A  74     3425   7624   8636   -867    -81    298       C
ATOM    320  CZ  PHE A  74     -73.105 -51.409 -30.330  1.00 53.26           C
ANISOU  320  CZ  PHE A  74     3488   7869   8879   -869     35    394       C
ATOM    321  N   LEU A  75     -68.262 -48.535 -32.213  1.00 43.81           N
ANISOU  321  N   LEU A  75     3030   6548   7068   -504   -123    227       N
ATOM    322  CA  LEU A  75     -67.143 -49.476 -32.172  1.00 43.52           C
ANISOU  322  CA  LEU A  75     3106   6391   7037   -577   -127    214       C
ATOM    323  C   LEU A  75     -66.142 -49.078 -31.085  1.00 42.55           C
ANISOU  323  C   LEU A  75     3119   6225   6825   -531    -19    282       C
ATOM    324  O   LEU A  75     -65.612 -49.937 -30.375  1.00 42.41           O
ANISOU  324  O   LEU A  75     3143   6127   6845   -600     37    323       O
ATOM    325  CB  LEU A  75     -66.442 -49.556 -33.532  1.00 43.19           C
ANISOU  325  CB  LEU A  75     3149   6317   6944   -565   -251    115       C
ATOM    326  CG  LEU A  75     -65.906 -50.938 -33.912  1.00 44.00           C
ANISOU  326  CG  LEU A  75     3283   6313   7122   -677   -301     69       C
ATOM    327  CD1 LEU A  75     -67.059 -51.825 -34.385  1.00 45.92           C
ANISOU  327  CD1 LEU A  75     3362   6574   7512   -775   -367     26       C
ATOM    328  CD2 LEU A  75     -64.822 -50.835 -34.987  1.00 43.96           C
ANISOU  328  CD2 LEU A  75     3413   6268   7023   -637   -389     -9       C
ATOM    329  N   THR A  76     -65.897 -47.774 -30.956  1.00 41.98           N
ANISOU  329  N   THR A  76     3112   6203   6636   -413      6    294       N
ATOM    330  CA  THR A  76     -65.015 -47.246 -29.916  1.00 41.21           C
ANISOU  330  CA  THR A  76     3135   6076   6448   -360    102    350       C
ATOM    331  C   THR A  76     -65.525 -47.582 -28.509  1.00 42.45           C
ANISOU  331  C   THR A  76     3228   6245   6654   -389    223    441       C
ATOM    332  O   THR A  76     -64.739 -47.948 -27.635  1.00 41.75           O
ANISOU  332  O   THR A  76     3225   6099   6541   -407    291    486       O
ATOM    333  CB  THR A  76     -64.854 -45.717 -30.046  1.00 40.56           C
ANISOU  333  CB  THR A  76     3115   6049   6247   -228    106    341       C
ATOM    334  OG1 THR A  76     -64.476 -45.390 -31.390  1.00 39.41           O
ANISOU  334  OG1 THR A  76     3018   5898   6056   -196     -1    266       O
ATOM    335  CG2 THR A  76     -63.804 -45.198 -29.078  1.00 39.09           C
ANISOU  335  CG2 THR A  76     3064   5822   5968   -179    187    380       C
ATOM    336  N   ARG A  77     -66.832 -47.450 -28.295  1.00 44.35           N
ANISOU  336  N   ARG A  77     3320   6568   6962   -388    250    471       N
ATOM    337  CA  ARG A  77     -67.445 -47.832 -27.016  1.00 45.96           C
ANISOU  337  CA  ARG A  77     3446   6794   7222   -418    369    563       C
ATOM    338  C   ARG A  77     -67.138 -49.290 -26.663  1.00 46.64           C
ANISOU  338  C   ARG A  77     3529   6789   7404   -542    393    594       C
ATOM    339  O   ARG A  77     -66.765 -49.595 -25.527  1.00 46.48           O
ANISOU  339  O   ARG A  77     3555   6738   7369   -550    494    670       O
ATOM    340  CB  ARG A  77     -68.964 -47.619 -27.038  1.00 47.50           C
ANISOU  340  CB  ARG A  77     3459   7092   7498   -413    382    584       C
ATOM    341  CG  ARG A  77     -69.414 -46.215 -26.657  1.00 48.48           C
ANISOU  341  CG  ARG A  77     3575   7313   7531   -279    431    605       C
ATOM    342  CD  ARG A  77     -70.915 -46.174 -26.347  1.00 51.35           C
ANISOU  342  CD  ARG A  77     3749   7778   7984   -279    476    650       C
ATOM    343  NE  ARG A  77     -71.297 -44.951 -25.634  1.00 52.84           N
ANISOU  343  NE  ARG A  77     3939   8050   8086   -150    557    690       N
ATOM    344  CZ  ARG A  77     -71.643 -43.794 -26.206  1.00 53.95           C
ANISOU  344  CZ  ARG A  77     4074   8259   8165    -42    514    651       C
ATOM    345  NH1 ARG A  77     -71.674 -43.656 -27.532  1.00 54.30           N
ANISOU  345  NH1 ARG A  77     4108   8308   8214    -40    388    573       N
ATOM    346  NH2 ARG A  77     -71.963 -42.755 -25.441  1.00 54.62           N
ANISOU  346  NH2 ARG A  77     4166   8408   8177     73    599    691       N
ATOM    347  N   ILE A  78     -67.290 -50.175 -27.647  1.00 47.70           N
ANISOU  347  N   ILE A  78     3614   6878   7634   -634    297    534       N
ATOM    348  CA  ILE A  78     -67.041 -51.607 -27.461  1.00 48.63           C
ANISOU  348  CA  ILE A  78     3725   6894   7856   -757    307    553       C
ATOM    349  C   ILE A  78     -65.572 -51.888 -27.166  1.00 47.79           C
ANISOU  349  C   ILE A  78     3794   6693   7671   -751    323    558       C
ATOM    350  O   ILE A  78     -65.259 -52.616 -26.226  1.00 48.16           O
ANISOU  350  O   ILE A  78     3867   6684   7748   -795    408    631       O
ATOM    351  CB  ILE A  78     -67.488 -52.431 -28.694  1.00 49.46           C
ANISOU  351  CB  ILE A  78     3747   6968   8075   -851    186    467       C
ATOM    352  CG1 ILE A  78     -69.012 -52.397 -28.825  1.00 51.12           C
ANISOU  352  CG1 ILE A  78     3761   7269   8394   -881    179    473       C
ATOM    353  CG2 ILE A  78     -66.996 -53.875 -28.586  1.00 49.74           C
ANISOU  353  CG2 ILE A  78     3813   6878   8209   -970    189    474       C
ATOM    354  CD1 ILE A  78     -69.548 -53.156 -30.025  1.00 52.50           C
ANISOU  354  CD1 ILE A  78     3840   7424   8683   -971     52    379       C
ATOM    355  N   LYS A  79     -64.675 -51.310 -27.963  1.00 47.03           N
ANISOU  355  N   LYS A  79     3814   6583   7474   -692    245    485       N
ATOM    356  CA  LYS A  79     -63.236 -51.472 -27.739  1.00 46.23           C
ANISOU  356  CA  LYS A  79     3875   6401   7291   -677    255    484       C
ATOM    357  C   LYS A  79     -62.831 -50.974 -26.351  1.00 45.76           C
ANISOU  357  C   LYS A  79     3878   6359   7150   -616    374    570       C
ATOM    358  O   LYS A  79     -62.046 -51.627 -25.665  1.00 45.55           O
ANISOU  358  O   LYS A  79     3928   6265   7115   -643    424    613       O
ATOM    359  CB  LYS A  79     -62.420 -50.747 -28.815  1.00 45.36           C
ANISOU  359  CB  LYS A  79     3866   6288   7081   -612    161    398       C
ATOM    360  CG  LYS A  79     -62.467 -51.414 -30.189  1.00 46.67           C
ANISOU  360  CG  LYS A  79     4009   6417   7305   -670     39    307       C
ATOM    361  CD  LYS A  79     -61.335 -50.935 -31.103  1.00 46.66           C
ANISOU  361  CD  LYS A  79     4140   6391   7198   -612    -34    238       C
ATOM    362  CE  LYS A  79     -61.564 -49.518 -31.625  1.00 47.20           C
ANISOU  362  CE  LYS A  79     4213   6546   7173   -504    -64    212       C
ATOM    363  NZ  LYS A  79     -62.661 -49.453 -32.638  1.00 48.53           N
ANISOU  363  NZ  LYS A  79     4266   6781   7394   -509   -150    156       N
ATOM    364  N   LEU A  80     -63.371 -49.824 -25.948  1.00 45.74           N
ANISOU  364  N   LEU A  80     3845   6449   7085   -527    416    591       N
ATOM    365  CA  LEU A  80     -63.131 -49.275 -24.608  1.00 45.54           C
ANISOU  365  CA  LEU A  80     3869   6455   6979   -460    528    665       C
ATOM    366  C   LEU A  80     -63.553 -50.256 -23.513  1.00 46.45           C
ANISOU  366  C   LEU A  80     3923   6554   7171   -524    629    761       C
ATOM    367  O   LEU A  80     -62.827 -50.453 -22.541  1.00 45.96           O
ANISOU  367  O   LEU A  80     3946   6463   7054   -507    700    816       O
ATOM    368  CB  LEU A  80     -63.878 -47.944 -24.416  1.00 45.80           C
ANISOU  368  CB  LEU A  80     3857   6592   6953   -359    556    668       C
ATOM    369  CG  LEU A  80     -63.149 -46.638 -24.764  1.00 45.18           C
ANISOU  369  CG  LEU A  80     3890   6528   6748   -254    519    613       C
ATOM    370  CD1 LEU A  80     -62.300 -46.760 -26.022  1.00 44.85           C
ANISOU  370  CD1 LEU A  80     3926   6425   6691   -275    408    532       C
ATOM    371  CD2 LEU A  80     -64.159 -45.498 -24.898  1.00 46.15           C
ANISOU  371  CD2 LEU A  80     3936   6748   6849   -169    526    606       C
ATOM    372  N   LEU A  81     -64.727 -50.861 -23.684  1.00 47.60           N
ANISOU  372  N   LEU A  81     3920   6722   7445   -595    635    782       N
ATOM    373  CA  LEU A  81     -65.288 -51.779 -22.688  1.00 48.83           C
ANISOU  373  CA  LEU A  81     3998   6865   7690   -660    738    883       C
ATOM    374  C   LEU A  81     -64.404 -53.017 -22.503  1.00 48.30           C
ANISOU  374  C   LEU A  81     4008   6680   7665   -740    745    907       C
ATOM    375  O   LEU A  81     -64.157 -53.442 -21.376  1.00 48.83           O
ANISOU  375  O   LEU A  81     4107   6729   7718   -739    847    999       O
ATOM    376  CB  LEU A  81     -66.712 -52.204 -23.088  1.00 50.39           C
ANISOU  376  CB  LEU A  81     4009   7102   8034   -733    728    889       C
ATOM    377  CG  LEU A  81     -67.771 -52.336 -21.983  1.00 52.64           C
ANISOU  377  CG  LEU A  81     4171   7452   8379   -739    857   1000       C
ATOM    378  CD1 LEU A  81     -67.262 -53.155 -20.796  1.00 53.66           C
ANISOU  378  CD1 LEU A  81     4358   7521   8509   -768    970   1104       C
ATOM    379  CD2 LEU A  81     -68.253 -50.960 -21.522  1.00 52.90           C
ANISOU  379  CD2 LEU A  81     4185   7606   8307   -611    906   1013       C
ATOM    380  N   LEU A  82     -63.923 -53.583 -23.607  1.00 47.51           N
ANISOU  380  N   LEU A  82     3941   6502   7608   -800    637    825       N
ATOM    381  CA  LEU A  82     -63.142 -54.822 -23.563  1.00 47.21           C
ANISOU  381  CA  LEU A  82     3970   6345   7623   -879    634    840       C
ATOM    382  C   LEU A  82     -61.671 -54.618 -23.190  1.00 45.30           C
ANISOU  382  C   LEU A  82     3899   6061   7252   -816    642    840       C
ATOM    383  O   LEU A  82     -61.044 -55.526 -22.646  1.00 45.52           O
ANISOU  383  O   LEU A  82     3985   6010   7300   -854    685    892       O
ATOM    384  CB  LEU A  82     -63.221 -55.553 -24.910  1.00 47.62           C
ANISOU  384  CB  LEU A  82     3989   6329   7775   -966    512    745       C
ATOM    385  CG  LEU A  82     -64.616 -55.889 -25.456  1.00 49.55           C
ANISOU  385  CG  LEU A  82     4060   6605   8163  -1043    479    724       C
ATOM    386  CD1 LEU A  82     -64.503 -56.876 -26.615  1.00 50.67           C
ANISOU  386  CD1 LEU A  82     4191   6654   8407  -1139    366    633       C
ATOM    387  CD2 LEU A  82     -65.546 -56.440 -24.379  1.00 51.02           C
ANISOU  387  CD2 LEU A  82     4131   6803   8453  -1097    599    839       C
ATOM    388  N   LYS A  83     -61.124 -53.437 -23.476  1.00 43.49           N
ANISOU  388  N   LYS A  83     3747   5883   6895   -721    602    784       N
ATOM    389  CA  LYS A  83     -59.685 -53.199 -23.323  1.00 41.53           C
ANISOU  389  CA  LYS A  83     3654   5595   6532   -668    590    766       C
ATOM    390  C   LYS A  83     -59.221 -53.250 -21.861  1.00 40.61           C
ANISOU  390  C   LYS A  83     3595   5485   6348   -627    700    860       C
ATOM    391  O   LYS A  83     -59.691 -52.466 -21.038  1.00 40.64           O
ANISOU  391  O   LYS A  83     3574   5572   6294   -560    772    905       O
ATOM    392  CB  LYS A  83     -59.295 -51.845 -23.930  1.00 40.70           C
ANISOU  392  CB  LYS A  83     3606   5543   6314   -578    529    690       C
ATOM    393  CG  LYS A  83     -57.802 -51.555 -23.877  1.00 40.35           C
ANISOU  393  CG  LYS A  83     3712   5459   6162   -529    509    663       C
ATOM    394  CD  LYS A  83     -57.452 -50.209 -24.493  1.00 40.90           C
ANISOU  394  CD  LYS A  83     3833   5574   6134   -446    455    594       C
ATOM    395  CE  LYS A  83     -55.943 -50.022 -24.533  1.00 40.37           C
ANISOU  395  CE  LYS A  83     3903   5459   5977   -413    430    565       C
ATOM    396  NZ  LYS A  83     -55.522 -48.688 -25.050  1.00 40.27           N
ANISOU  396  NZ  LYS A  83     3947   5481   5874   -334    390    507       N
ATOM    397  N   PRO A  84     -58.289 -54.167 -21.539  1.00 39.36           N
ANISOU  397  N   PRO A  84     3519   5244   6193   -658    714    890       N
ATOM    398  CA  PRO A  84     -57.739 -54.206 -20.184  1.00 38.67           C
ANISOU  398  CA  PRO A  84     3497   5168   6026   -608    810    976       C
ATOM    399  C   PRO A  84     -56.756 -53.070 -19.925  1.00 36.44           C
ANISOU  399  C   PRO A  84     3325   4929   5589   -505    794    936       C
ATOM    400  O   PRO A  84     -56.106 -52.590 -20.855  1.00 35.58           O
ANISOU  400  O   PRO A  84     3272   4802   5443   -490    706    847       O
ATOM    401  CB  PRO A  84     -57.016 -55.555 -20.138  1.00 38.86           C
ANISOU  401  CB  PRO A  84     3574   5083   6108   -673    811   1007       C
ATOM    402  CG  PRO A  84     -56.634 -55.819 -21.537  1.00 38.77           C
ANISOU  402  CG  PRO A  84     3581   5007   6142   -720    694    906       C
ATOM    403  CD  PRO A  84     -57.736 -55.245 -22.380  1.00 39.33           C
ANISOU  403  CD  PRO A  84     3546   5132   6264   -736    644    848       C
ATOM    404  N   THR A  85     -56.646 -52.659 -18.665  1.00 35.46           N
ANISOU  404  N   THR A  85     3233   4862   5378   -436    881   1000       N
ATOM    405  CA  THR A  85     -55.728 -51.588 -18.282  1.00 33.59           C
ANISOU  405  CA  THR A  85     3098   4666   4998   -341    871    961       C
ATOM    406  C   THR A  85     -54.282 -52.072 -18.343  1.00 32.35           C
ANISOU  406  C   THR A  85     3054   4438   4797   -344    830    942       C
ATOM    407  O   THR A  85     -54.031 -53.280 -18.306  1.00 32.28           O
ANISOU  407  O   THR A  85     3052   4359   4854   -404    840    985       O
ATOM    408  CB  THR A  85     -55.998 -51.089 -16.851  1.00 34.09           C
ANISOU  408  CB  THR A  85     3166   4811   4976   -263    974   1032       C
ATOM    409  OG1 THR A  85     -55.671 -52.123 -15.913  1.00 33.69           O
ANISOU  409  OG1 THR A  85     3141   4731   4928   -279   1044   1124       O
ATOM    410  CG2 THR A  85     -57.463 -50.661 -16.681  1.00 34.65           C
ANISOU  410  CG2 THR A  85     3118   4957   5090   -254   1028   1063       C
ATOM    411  N   PRO A  86     -53.322 -51.134 -18.442  1.00 30.51           N
ANISOU  411  N   PRO A  86     2910   4222   4459   -280    786    878       N
ATOM    412  CA  PRO A  86     -51.915 -51.529 -18.400  1.00 29.57           C
ANISOU  412  CA  PRO A  86     2893   4049   4292   -274    753    863       C
ATOM    413  C   PRO A  86     -51.542 -52.324 -17.148  1.00 29.64           C
ANISOU  413  C   PRO A  86     2936   4054   4270   -260    829    955       C
ATOM    414  O   PRO A  86     -50.771 -53.280 -17.239  1.00 29.22           O
ANISOU  414  O   PRO A  86     2928   3932   4241   -293    813    972       O
ATOM    415  CB  PRO A  86     -51.171 -50.190 -18.422  1.00 28.58           C
ANISOU  415  CB  PRO A  86     2838   3965   4057   -198    715    792       C
ATOM    416  CG  PRO A  86     -52.096 -49.261 -19.126  1.00 28.97           C
ANISOU  416  CG  PRO A  86     2826   4053   4129   -189    691    744       C
ATOM    417  CD  PRO A  86     -53.487 -49.706 -18.774  1.00 30.13           C
ANISOU  417  CD  PRO A  86     2866   4232   4349   -218    755    810       C
ATOM    418  N   ASN A  87     -52.079 -51.935 -15.993  1.00 29.78           N
ANISOU  418  N   ASN A  87     2935   4148   4232   -205    912   1014       N
ATOM    419  CA  ASN A  87     -51.788 -52.651 -14.748  1.00 30.22           C
ANISOU  419  CA  ASN A  87     3023   4213   4248   -180    992   1111       C
ATOM    420  C   ASN A  87     -52.272 -54.101 -14.791  1.00 30.99           C
ANISOU  420  C   ASN A  87     3068   4240   4466   -262   1033   1195       C
ATOM    421  O   ASN A  87     -51.597 -54.992 -14.268  1.00 31.10           O
ANISOU  421  O   ASN A  87     3134   4211   4471   -264   1060   1254       O
ATOM    422  CB  ASN A  87     -52.359 -51.911 -13.530  1.00 30.83           C
ANISOU  422  CB  ASN A  87     3086   4392   4234    -98   1077   1157       C
ATOM    423  CG  ASN A  87     -51.578 -50.640 -13.190  1.00 30.66           C
ANISOU  423  CG  ASN A  87     3144   4428   4077     -7   1043   1081       C
ATOM    424  OD1 ASN A  87     -50.449 -50.445 -13.642  1.00 29.73           O
ANISOU  424  OD1 ASN A  87     3099   4273   3924     -4    967   1014       O
ATOM    425  ND2 ASN A  87     -52.180 -49.775 -12.384  1.00 31.21           N
ANISOU  425  ND2 ASN A  87     3199   4587   4075     66   1099   1091       N
ATOM    426  N   THR A  88     -53.420 -54.339 -15.428  1.00 31.38           N
ANISOU  426  N   THR A  88     3015   4274   4633   -331   1036   1197       N
ATOM    427  CA  THR A  88     -53.939 -55.705 -15.601  1.00 32.52           C
ANISOU  427  CA  THR A  88     3102   4340   4916   -424   1066   1264       C
ATOM    428  C   THR A  88     -53.066 -56.526 -16.554  1.00 31.99           C
ANISOU  428  C   THR A  88     3086   4163   4906   -483    983   1214       C
ATOM    429  O   THR A  88     -52.776 -57.687 -16.286  1.00 32.82           O
ANISOU  429  O   THR A  88     3212   4193   5066   -521   1014   1278       O
ATOM    430  CB  THR A  88     -55.392 -55.706 -16.131  1.00 33.36           C
ANISOU  430  CB  THR A  88     3075   4460   5140   -487   1077   1265       C
ATOM    431  OG1 THR A  88     -56.259 -55.110 -15.161  1.00 34.19           O
ANISOU  431  OG1 THR A  88     3124   4665   5202   -433   1170   1329       O
ATOM    432  CG2 THR A  88     -55.868 -57.127 -16.414  1.00 34.47           C
ANISOU  432  CG2 THR A  88     3155   4505   5438   -595   1096   1319       C
ATOM    433  N   VAL A  89     -52.660 -55.923 -17.667  1.00 30.86           N
ANISOU  433  N   VAL A  89     2967   4010   4750   -485    882   1101       N
ATOM    434  CA  VAL A  89     -51.794 -56.600 -18.638  1.00 30.45           C
ANISOU  434  CA  VAL A  89     2967   3863   4739   -529    800   1043       C
ATOM    435  C   VAL A  89     -50.429 -56.919 -18.021  1.00 29.59           C
ANISOU  435  C   VAL A  89     2968   3730   4546   -480    808   1069       C
ATOM    436  O   VAL A  89     -49.921 -58.036 -18.157  1.00 29.48           O
ANISOU  436  O   VAL A  89     2987   3628   4587   -518    803   1095       O
ATOM    437  CB  VAL A  89     -51.614 -55.762 -19.923  1.00 29.56           C
ANISOU  437  CB  VAL A  89     2860   3760   4611   -526    697    923       C
ATOM    438  CG1 VAL A  89     -50.572 -56.392 -20.832  1.00 29.41           C
ANISOU  438  CG1 VAL A  89     2910   3654   4612   -553    620    865       C
ATOM    439  CG2 VAL A  89     -52.943 -55.628 -20.651  1.00 30.53           C
ANISOU  439  CG2 VAL A  89     2871   3899   4828   -579    677    895       C
ATOM    440  N   HIS A  90     -49.854 -55.937 -17.329  1.00 28.87           N
ANISOU  440  N   HIS A  90     2931   3717   4322   -392    820   1061       N
ATOM    441  CA  HIS A  90     -48.595 -56.128 -16.615  1.00 28.60           C
ANISOU  441  CA  HIS A  90     2992   3680   4196   -335    827   1085       C
ATOM    442  C   HIS A  90     -48.691 -57.275 -15.602  1.00 29.65           C
ANISOU  442  C   HIS A  90     3128   3782   4354   -341    915   1207       C
ATOM    443  O   HIS A  90     -47.769 -58.093 -15.491  1.00 29.76           O
ANISOU  443  O   HIS A  90     3205   3738   4365   -338    906   1233       O
ATOM    444  CB  HIS A  90     -48.177 -54.834 -15.908  1.00 27.99           C
ANISOU  444  CB  HIS A  90     2956   3700   3978   -243    832   1057       C
ATOM    445  CG  HIS A  90     -46.910 -54.962 -15.124  1.00 27.36           C
ANISOU  445  CG  HIS A  90     2965   3631   3798   -181    834   1076       C
ATOM    446  ND1 HIS A  90     -46.894 -55.287 -13.786  1.00 28.53           N
ANISOU  446  ND1 HIS A  90     3133   3823   3884   -129    914   1169       N
ATOM    447  CD2 HIS A  90     -45.616 -54.825 -15.495  1.00 26.12           C
ANISOU  447  CD2 HIS A  90     2879   3452   3592   -159    766   1016       C
ATOM    448  CE1 HIS A  90     -45.643 -55.348 -13.366  1.00 27.48           C
ANISOU  448  CE1 HIS A  90     3080   3696   3666    -77    889   1162       C
ATOM    449  NE2 HIS A  90     -44.848 -55.062 -14.381  1.00 27.17           N
ANISOU  449  NE2 HIS A  90     3069   3618   3637    -97    800   1069       N
ATOM    450  N   TYR A  91     -49.801 -57.333 -14.866  1.00 30.51           N
ANISOU  450  N   TYR A  91     3170   3934   4489   -345   1002   1287       N
ATOM    451  CA  TYR A  91     -50.035 -58.430 -13.927  1.00 31.72           C
ANISOU  451  CA  TYR A  91     3317   4057   4678   -355   1097   1416       C
ATOM    452  C   TYR A  91     -49.949 -59.781 -14.634  1.00 31.98           C
ANISOU  452  C   TYR A  91     3344   3958   4848   -444   1077   1433       C
ATOM    453  O   TYR A  91     -49.215 -60.675 -14.195  1.00 31.99           O
ANISOU  453  O   TYR A  91     3407   3903   4844   -432   1101   1495       O
ATOM    454  CB  TYR A  91     -51.401 -58.295 -13.237  1.00 32.89           C
ANISOU  454  CB  TYR A  91     3374   4265   4858   -360   1195   1496       C
ATOM    455  CG  TYR A  91     -51.674 -59.402 -12.238  1.00 34.67           C
ANISOU  455  CG  TYR A  91     3591   4461   5120   -367   1305   1642       C
ATOM    456  CD1 TYR A  91     -51.392 -59.231 -10.886  1.00 35.88           C
ANISOU  456  CD1 TYR A  91     3792   4693   5148   -272   1385   1726       C
ATOM    457  CD2 TYR A  91     -52.201 -60.627 -12.648  1.00 36.26           C
ANISOU  457  CD2 TYR A  91     3741   4555   5483   -468   1329   1695       C
ATOM    458  CE1 TYR A  91     -51.630 -60.245  -9.970  1.00 37.33           C
ANISOU  458  CE1 TYR A  91     3972   4852   5361   -271   1492   1870       C
ATOM    459  CE2 TYR A  91     -52.440 -61.647 -11.740  1.00 37.95           C
ANISOU  459  CE2 TYR A  91     3949   4731   5738   -476   1436   1837       C
ATOM    460  CZ  TYR A  91     -52.153 -61.450 -10.403  1.00 38.53           C
ANISOU  460  CZ  TYR A  91     4072   4889   5680   -375   1520   1929       C
ATOM    461  OH  TYR A  91     -52.391 -62.460  -9.502  1.00 40.56           O
ANISOU  461  OH  TYR A  91     4327   5112   5974   -376   1633   2079       O
ATOM    462  N   ILE A  92     -50.697 -59.918 -15.726  1.00 31.97           N
ANISOU  462  N   ILE A  92     3271   3909   4967   -530   1030   1375       N
ATOM    463  CA  ILE A  92     -50.764 -61.179 -16.466  1.00 32.62           C
ANISOU  463  CA  ILE A  92     3339   3862   5192   -623   1006   1377       C
ATOM    464  C   ILE A  92     -49.393 -61.584 -17.017  1.00 31.68           C
ANISOU  464  C   ILE A  92     3320   3674   5044   -607    932   1321       C
ATOM    465  O   ILE A  92     -49.044 -62.764 -17.003  1.00 32.10           O
ANISOU  465  O   ILE A  92     3405   3626   5167   -640    947   1367       O
ATOM    466  CB  ILE A  92     -51.779 -61.113 -17.629  1.00 32.80           C
ANISOU  466  CB  ILE A  92     3266   3860   5336   -710    950   1301       C
ATOM    467  CG1 ILE A  92     -53.203 -60.917 -17.097  1.00 34.20           C
ANISOU  467  CG1 ILE A  92     3330   4096   5570   -737   1029   1367       C
ATOM    468  CG2 ILE A  92     -51.730 -62.400 -18.454  1.00 34.04           C
ANISOU  468  CG2 ILE A  92     3419   3878   5635   -803    910   1282       C
ATOM    469  CD1 ILE A  92     -54.190 -60.457 -18.149  1.00 34.31           C
ANISOU  469  CD1 ILE A  92     3245   4129   5663   -795    966   1281       C
ATOM    470  N   LEU A  93     -48.619 -60.604 -17.485  1.00 30.38           N
ANISOU  470  N   LEU A  93     3205   3562   4778   -553    856   1225       N
ATOM    471  CA  LEU A  93     -47.293 -60.871 -18.050  1.00 29.66           C
ANISOU  471  CA  LEU A  93     3201   3417   4651   -532    786   1168       C
ATOM    472  C   LEU A  93     -46.247 -61.232 -16.994  1.00 29.90           C
ANISOU  472  C   LEU A  93     3314   3455   4593   -460    829   1242       C
ATOM    473  O   LEU A  93     -45.211 -61.814 -17.326  1.00 29.57           O
ANISOU  473  O   LEU A  93     3338   3350   4547   -449    789   1222       O
ATOM    474  CB  LEU A  93     -46.799 -59.665 -18.866  1.00 28.34           C
ANISOU  474  CB  LEU A  93     3054   3306   4406   -498    699   1050       C
ATOM    475  CG  LEU A  93     -47.430 -59.519 -20.255  1.00 28.34           C
ANISOU  475  CG  LEU A  93     3000   3276   4490   -563    626    957       C
ATOM    476  CD1 LEU A  93     -47.302 -58.089 -20.782  1.00 26.94           C
ANISOU  476  CD1 LEU A  93     2825   3182   4230   -519    571    869       C
ATOM    477  CD2 LEU A  93     -46.808 -60.513 -21.235  1.00 29.09           C
ANISOU  477  CD2 LEU A  93     3134   3262   4656   -606    565    910       C
ATOM    478  N   THR A  94     -46.512 -60.877 -15.737  1.00 30.35           N
ANISOU  478  N   THR A  94     3366   3592   4574   -404    908   1324       N
ATOM    479  CA  THR A  94     -45.563 -61.094 -14.643  1.00 30.59           C
ANISOU  479  CA  THR A  94     3472   3652   4500   -322    947   1393       C
ATOM    480  C   THR A  94     -46.023 -62.186 -13.669  1.00 32.27           C
ANISOU  480  C   THR A  94     3675   3826   4759   -328   1053   1537       C
ATOM    481  O   THR A  94     -45.387 -62.406 -12.639  1.00 32.88           O
ANISOU  481  O   THR A  94     3809   3937   4746   -253   1098   1613       O
ATOM    482  CB  THR A  94     -45.322 -59.790 -13.859  1.00 30.08           C
ANISOU  482  CB  THR A  94     3425   3719   4284   -232    953   1372       C
ATOM    483  OG1 THR A  94     -46.574 -59.278 -13.381  1.00 30.17           O
ANISOU  483  OG1 THR A  94     3365   3795   4302   -238   1017   1409       O
ATOM    484  CG2 THR A  94     -44.652 -58.757 -14.746  1.00 28.60           C
ANISOU  484  CG2 THR A  94     3261   3559   4047   -219    853   1240       C
ATOM    485  N   HIS A  95     -47.118 -62.864 -14.001  1.00 33.40           N
ANISOU  485  N   HIS A  95     3746   3900   5044   -417   1091   1575       N
ATOM    486  CA  HIS A  95     -47.599 -64.008 -13.224  1.00 35.13           C
ANISOU  486  CA  HIS A  95     3950   4059   5338   -440   1194   1715       C
ATOM    487  C   HIS A  95     -47.835 -65.190 -14.162  1.00 36.09           C
ANISOU  487  C   HIS A  95     4051   4029   5632   -545   1170   1705       C
ATOM    488  O   HIS A  95     -47.564 -65.090 -15.357  1.00 35.15           O
ANISOU  488  O   HIS A  95     3936   3865   5556   -587   1072   1587       O
ATOM    489  CB  HIS A  95     -48.880 -63.633 -12.479  1.00 35.87           C
ANISOU  489  CB  HIS A  95     3959   4228   5440   -446   1288   1791       C
ATOM    490  CG  HIS A  95     -48.666 -62.644 -11.377  1.00 35.72           C
ANISOU  490  CG  HIS A  95     3970   4351   5251   -335   1328   1818       C
ATOM    491  ND1 HIS A  95     -48.528 -61.292 -11.607  1.00 34.65           N
ANISOU  491  ND1 HIS A  95     3836   4313   5016   -290   1266   1712       N
ATOM    492  CD2 HIS A  95     -48.565 -62.810 -10.037  1.00 36.74           C
ANISOU  492  CD2 HIS A  95     4131   4539   5288   -255   1422   1936       C
ATOM    493  CE1 HIS A  95     -48.354 -60.668 -10.456  1.00 35.44           C
ANISOU  493  CE1 HIS A  95     3967   4524   4975   -191   1317   1756       C
ATOM    494  NE2 HIS A  95     -48.374 -61.565  -9.487  1.00 36.46           N
ANISOU  494  NE2 HIS A  95     4115   4637   5100   -165   1411   1891       N
ATOM    495  N   PHE A  96     -48.322 -66.305 -13.619  1.00 38.14           N
ANISOU  495  N   PHE A  96     4293   4209   5990   -585   1260   1826       N
ATOM    496  CA  PHE A  96     -48.664 -67.491 -14.414  1.00 39.49           C
ANISOU  496  CA  PHE A  96     4438   4224   6341   -692   1247   1823       C
ATOM    497  C   PHE A  96     -47.463 -68.014 -15.206  1.00 39.30           C
ANISOU  497  C   PHE A  96     4502   4109   6319   -683   1159   1747       C
ATOM    498  O   PHE A  96     -47.583 -68.343 -16.388  1.00 39.09           O
ANISOU  498  O   PHE A  96     4458   3998   6397   -759   1083   1650       O
ATOM    499  CB  PHE A  96     -49.832 -67.192 -15.366  1.00 39.57           C
ANISOU  499  CB  PHE A  96     4340   4226   6469   -793   1205   1740       C
ATOM    500  CG  PHE A  96     -50.974 -66.458 -14.719  1.00 40.33           C
ANISOU  500  CG  PHE A  96     4343   4431   6548   -792   1276   1792       C
ATOM    501  CD1 PHE A  96     -51.237 -65.133 -15.042  1.00 39.47           C
ANISOU  501  CD1 PHE A  96     4200   4442   6356   -761   1224   1700       C
ATOM    502  CD2 PHE A  96     -51.783 -67.091 -13.785  1.00 42.37           C
ANISOU  502  CD2 PHE A  96     4550   4672   6875   -817   1401   1936       C
ATOM    503  CE1 PHE A  96     -52.283 -64.449 -14.445  1.00 40.18           C
ANISOU  503  CE1 PHE A  96     4206   4633   6428   -751   1292   1746       C
ATOM    504  CE2 PHE A  96     -52.838 -66.415 -13.185  1.00 42.73           C
ANISOU  504  CE2 PHE A  96     4507   4824   6903   -809   1473   1986       C
ATOM    505  CZ  PHE A  96     -53.088 -65.091 -13.515  1.00 41.79           C
ANISOU  505  CZ  PHE A  96     4355   4826   6698   -774   1416   1888       C
ATOM    506  N   LYS A  97     -46.311 -68.093 -14.545  1.00 39.55           N
ANISOU  506  N   LYS A  97     4627   4165   6234   -586   1170   1790       N
ATOM    507  CA  LYS A  97     -45.060 -68.493 -15.196  1.00 39.52           C
ANISOU  507  CA  LYS A  97     4708   4096   6211   -558   1091   1723       C
ATOM    508  C   LYS A  97     -45.182 -69.834 -15.933  1.00 40.43           C
ANISOU  508  C   LYS A  97     4829   4035   6495   -643   1081   1721       C
ATOM    509  O   LYS A  97     -44.632 -69.996 -17.021  1.00 39.92           O
ANISOU  509  O   LYS A  97     4796   3911   6462   -663    990   1611       O
ATOM    510  CB  LYS A  97     -43.921 -68.565 -14.173  1.00 39.73           C
ANISOU  510  CB  LYS A  97     4824   4172   6102   -440   1123   1799       C
ATOM    511  CG  LYS A  97     -42.531 -68.465 -14.779  1.00 39.95           C
ANISOU  511  CG  LYS A  97     4928   4192   6059   -386   1030   1709       C
ATOM    512  CD  LYS A  97     -41.492 -69.095 -13.869  1.00 42.85           C
ANISOU  512  CD  LYS A  97     5377   4552   6350   -292   1070   1805       C
ATOM    513  CE  LYS A  97     -40.090 -68.859 -14.387  1.00 42.68           C
ANISOU  513  CE  LYS A  97     5421   4547   6247   -229    979   1716       C
ATOM    514  NZ  LYS A  97     -39.651 -67.460 -14.176  1.00 42.84           N
ANISOU  514  NZ  LYS A  97     5437   4720   6119   -168    933   1647       N
ATOM    515  N   GLY A  98     -45.908 -70.780 -15.339  1.00 41.91           N
ANISOU  515  N   GLY A  98     4989   4142   6794   -691   1177   1842       N
ATOM    516  CA  GLY A  98     -46.104 -72.106 -15.929  1.00 42.97           C
ANISOU  516  CA  GLY A  98     5127   4096   7104   -778   1179   1850       C
ATOM    517  C   GLY A  98     -46.828 -72.071 -17.263  1.00 42.75           C
ANISOU  517  C   GLY A  98     5031   4012   7200   -888   1095   1717       C
ATOM    518  O   GLY A  98     -46.464 -72.794 -18.193  1.00 42.89           O
ANISOU  518  O   GLY A  98     5083   3909   7304   -929   1030   1641       O
ATOM    519  N   VAL A  99     -47.854 -71.229 -17.357  1.00 42.44           N
ANISOU  519  N   VAL A  99     4895   4065   7167   -930   1093   1686       N
ATOM    520  CA  VAL A  99     -48.562 -71.017 -18.619  1.00 42.15           C
ANISOU  520  CA  VAL A  99     4786   4004   7225  -1022   1004   1553       C
ATOM    521  C   VAL A  99     -47.649 -70.359 -19.661  1.00 40.46           C
ANISOU  521  C   VAL A  99     4627   3829   6917   -976    882   1404       C
ATOM    522  O   VAL A  99     -47.640 -70.764 -20.824  1.00 40.38           O
ANISOU  522  O   VAL A  99     4618   3736   6990  -1033    798   1296       O
ATOM    523  CB  VAL A  99     -49.818 -70.139 -18.434  1.00 42.25           C
ANISOU  523  CB  VAL A  99     4682   4126   7245  -1058   1031   1557       C
ATOM    524  CG1 VAL A  99     -50.517 -69.928 -19.768  1.00 42.55           C
ANISOU  524  CG1 VAL A  99     4646   4145   7375  -1145    930   1417       C
ATOM    525  CG2 VAL A  99     -50.775 -70.770 -17.427  1.00 44.04           C
ANISOU  525  CG2 VAL A  99     4843   4319   7569  -1106   1159   1709       C
ATOM    526  N   TRP A 100     -46.889 -69.347 -19.249  1.00 39.06           N
ANISOU  526  N   TRP A 100     4495   3778   6568   -874    871   1397       N
ATOM    527  CA  TRP A 100     -45.969 -68.668 -20.166  1.00 37.47           C
ANISOU  527  CA  TRP A 100     4345   3619   6273   -827    766   1269       C
ATOM    528  C   TRP A 100     -44.876 -69.604 -20.670  1.00 37.89           C
ANISOU  528  C   TRP A 100     4488   3560   6349   -808    726   1239       C
ATOM    529  O   TRP A 100     -44.462 -69.510 -21.821  1.00 37.04           O
ANISOU  529  O   TRP A 100     4401   3428   6243   -816    634   1119       O
ATOM    530  CB  TRP A 100     -45.334 -67.438 -19.511  1.00 36.15           C
ANISOU  530  CB  TRP A 100     4207   3600   5927   -724    771   1276       C
ATOM    531  CG  TRP A 100     -46.290 -66.298 -19.353  1.00 34.75           C
ANISOU  531  CG  TRP A 100     3950   3540   5714   -732    781   1261       C
ATOM    532  CD1 TRP A 100     -46.753 -65.781 -18.185  1.00 34.57           C
ANISOU  532  CD1 TRP A 100     3897   3609   5628   -694    864   1353       C
ATOM    533  CD2 TRP A 100     -46.908 -65.546 -20.401  1.00 33.65           C
ANISOU  533  CD2 TRP A 100     3750   3439   5597   -774    707   1149       C
ATOM    534  NE1 TRP A 100     -47.620 -64.744 -18.433  1.00 34.11           N
ANISOU  534  NE1 TRP A 100     3764   3641   5555   -710    847   1303       N
ATOM    535  CE2 TRP A 100     -47.734 -64.579 -19.788  1.00 33.20           C
ANISOU  535  CE2 TRP A 100     3627   3495   5492   -759    751   1180       C
ATOM    536  CE3 TRP A 100     -46.840 -65.590 -21.800  1.00 32.51           C
ANISOU  536  CE3 TRP A 100     3603   3248   5501   -816    608   1025       C
ATOM    537  CZ2 TRP A 100     -48.489 -63.666 -20.524  1.00 32.62           C
ANISOU  537  CZ2 TRP A 100     3486   3486   5424   -783    699   1096       C
ATOM    538  CZ3 TRP A 100     -47.593 -64.684 -22.530  1.00 31.53           C
ANISOU  538  CZ3 TRP A 100     3411   3193   5377   -840    556    943       C
ATOM    539  CH2 TRP A 100     -48.404 -63.732 -21.890  1.00 31.88           C
ANISOU  539  CH2 TRP A 100     3390   3346   5377   -823    602    980       C
ATOM    540  N   ASN A 101     -44.419 -70.507 -19.807  1.00 39.11           N
ANISOU  540  N   ASN A 101     4697   3648   6517   -778    798   1352       N
ATOM    541  CA  ASN A 101     -43.403 -71.484 -20.188  1.00 39.81           C
ANISOU  541  CA  ASN A 101     4872   3622   6633   -754    771   1338       C
ATOM    542  C   ASN A 101     -43.887 -72.353 -21.353  1.00 40.32           C
ANISOU  542  C   ASN A 101     4918   3545   6858   -852    718   1253       C
ATOM    543  O   ASN A 101     -43.110 -72.690 -22.250  1.00 40.07           O
ANISOU  543  O   ASN A 101     4943   3453   6827   -836    646   1163       O
ATOM    544  CB  ASN A 101     -43.019 -72.364 -18.992  1.00 41.26           C
ANISOU  544  CB  ASN A 101     5107   3751   6817   -708    869   1490       C
ATOM    545  CG  ASN A 101     -41.523 -72.488 -18.816  1.00 42.25           C
ANISOU  545  CG  ASN A 101     5331   3888   6834   -600    847   1494       C
ATOM    546  OD1 ASN A 101     -40.964 -73.579 -18.924  1.00 46.57           O
ANISOU  546  OD1 ASN A 101     5939   4312   7441   -590    855   1521       O
ATOM    547  ND2 ASN A 101     -40.863 -71.365 -18.540  1.00 43.18           N
ANISOU  547  ND2 ASN A 101     5462   4151   6792   -518    818   1465       N
ATOM    548  N   ILE A 102     -45.173 -72.702 -21.335  1.00 40.96           N
ANISOU  548  N   ILE A 102     4915   3576   7073   -953    752   1279       N
ATOM    549  CA  ILE A 102     -45.799 -73.430 -22.436  1.00 41.69           C
ANISOU  549  CA  ILE A 102     4973   3545   7324  -1057    694   1187       C
ATOM    550  C   ILE A 102     -45.892 -72.526 -23.666  1.00 40.15           C
ANISOU  550  C   ILE A 102     4748   3426   7082  -1066    580   1028       C
ATOM    551  O   ILE A 102     -45.490 -72.917 -24.764  1.00 39.76           O
ANISOU  551  O   ILE A 102     4736   3306   7065  -1078    497    915       O
ATOM    552  CB  ILE A 102     -47.218 -73.935 -22.064  1.00 43.26           C
ANISOU  552  CB  ILE A 102     5072   3685   7681  -1168    760   1255       C
ATOM    553  CG1 ILE A 102     -47.161 -74.959 -20.922  1.00 45.26           C
ANISOU  553  CG1 ILE A 102     5357   3842   7998  -1166    879   1420       C
ATOM    554  CG2 ILE A 102     -47.908 -74.547 -23.278  1.00 44.32           C
ANISOU  554  CG2 ILE A 102     5158   3707   7974  -1280    682   1137       C
ATOM    555  CD1 ILE A 102     -46.577 -76.308 -21.313  1.00 47.13           C
ANISOU  555  CD1 ILE A 102     5673   3894   8342  -1185    868   1412       C
ATOM    556  N   VAL A 103     -46.415 -71.316 -23.468  1.00 38.88           N
ANISOU  556  N   VAL A 103     4523   3410   6839  -1052    580   1021       N
ATOM    557  CA  VAL A 103     -46.576 -70.346 -24.550  1.00 37.60           C
ANISOU  557  CA  VAL A 103     4329   3333   6625  -1052    482    886       C
ATOM    558  C   VAL A 103     -45.252 -70.071 -25.267  1.00 36.13           C
ANISOU  558  C   VAL A 103     4235   3163   6330   -972    409    800       C
ATOM    559  O   VAL A 103     -45.202 -70.053 -26.496  1.00 35.67           O
ANISOU  559  O   VAL A 103     4180   3083   6289   -991    318    677       O
ATOM    560  CB  VAL A 103     -47.155 -69.003 -24.032  1.00 36.85           C
ANISOU  560  CB  VAL A 103     4167   3397   6437  -1025    507    912       C
ATOM    561  CG1 VAL A 103     -47.197 -67.969 -25.149  1.00 36.09           C
ANISOU  561  CG1 VAL A 103     4050   3387   6276  -1011    408    779       C
ATOM    562  CG2 VAL A 103     -48.546 -69.208 -23.445  1.00 38.16           C
ANISOU  562  CG2 VAL A 103     4228   3559   6713  -1105    576    987       C
ATOM    563  N   ASN A 104     -44.187 -69.877 -24.491  1.00 35.29           N
ANISOU  563  N   ASN A 104     4200   3098   6111   -881    449    867       N
ATOM    564  CA  ASN A 104     -42.860 -69.590 -25.042  1.00 34.25           C
ANISOU  564  CA  ASN A 104     4149   2990   5873   -800    391    800       C
ATOM    565  C   ASN A 104     -42.304 -70.699 -25.942  1.00 35.22           C
ANISOU  565  C   ASN A 104     4333   2978   6070   -813    342    734       C
ATOM    566  O   ASN A 104     -41.466 -70.431 -26.806  1.00 34.48           O
ANISOU  566  O   ASN A 104     4286   2903   5911   -765    275    644       O
ATOM    567  CB  ASN A 104     -41.859 -69.296 -23.916  1.00 33.48           C
ANISOU  567  CB  ASN A 104     4109   2957   5655   -704    447    893       C
ATOM    568  CG  ASN A 104     -42.177 -68.014 -23.162  1.00 32.45           C
ANISOU  568  CG  ASN A 104     3934   2973   5420   -671    478    929       C
ATOM    569  OD1 ASN A 104     -42.827 -67.109 -23.689  1.00 31.20           O
ANISOU  569  OD1 ASN A 104     3719   2887   5248   -696    440    863       O
ATOM    570  ND2 ASN A 104     -41.711 -67.930 -21.924  1.00 31.42           N
ANISOU  570  ND2 ASN A 104     3834   2891   5214   -607    545   1032       N
ATOM    571  N   ASN A 105     -42.758 -71.933 -25.732  1.00 37.14           N
ANISOU  571  N   ASN A 105     4575   3085   6451   -875    380    781       N
ATOM    572  CA  ASN A 105     -42.295 -73.078 -26.520  1.00 38.25           C
ANISOU  572  CA  ASN A 105     4777   3081   6676   -890    339    721       C
ATOM    573  C   ASN A 105     -43.252 -73.480 -27.647  1.00 38.95           C
ANISOU  573  C   ASN A 105     4814   3094   6892   -989    270    608       C
ATOM    574  O   ASN A 105     -43.086 -74.541 -28.249  1.00 39.94           O
ANISOU  574  O   ASN A 105     4981   3082   7112  -1018    240    557       O
ATOM    575  CB  ASN A 105     -42.030 -74.276 -25.600  1.00 39.84           C
ANISOU  575  CB  ASN A 105     5026   3161   6952   -886    423    842       C
ATOM    576  CG  ASN A 105     -40.886 -74.026 -24.637  1.00 40.32           C
ANISOU  576  CG  ASN A 105     5152   3289   6881   -774    474    935       C
ATOM    577  OD1 ASN A 105     -39.790 -73.631 -25.038  1.00 42.09           O
ANISOU  577  OD1 ASN A 105     5431   3565   6998   -693    427    881       O
ATOM    578  ND2 ASN A 105     -41.136 -74.253 -23.356  1.00 43.60           N
ANISOU  578  ND2 ASN A 105     5557   3706   7302   -766    570   1079       N
ATOM    579  N   ILE A 105A    -44.249 -72.639 -27.924  1.00 38.44           N
ANISOU  579  N   ILE A 105A    4659   3119   6827  -1037    242    567       N
ATOM    580  CA  ILE A 105A    -45.127 -72.818 -29.080  1.00 39.03           C
ANISOU  580  CA  ILE A 105A    4678   3155   6998  -1120    160    444       C
ATOM    581  C   ILE A 105A    -44.873 -71.645 -30.030  1.00 37.75           C
ANISOU  581  C   ILE A 105A    4511   3120   6710  -1068     75    335       C
ATOM    582  O   ILE A 105A    -45.434 -70.564 -29.837  1.00 36.89           O
ANISOU  582  O   ILE A 105A    4338   3136   6542  -1065     79    346       O
ATOM    583  CB  ILE A 105A    -46.609 -72.852 -28.674  1.00 39.96           C
ANISOU  583  CB  ILE A 105A    4679   3270   7233  -1223    195    487       C
ATOM    584  CG1 ILE A 105A    -46.878 -74.020 -27.722  1.00 41.52           C
ANISOU  584  CG1 ILE A 105A    4877   3335   7561  -1277    289    608       C
ATOM    585  CG2 ILE A 105A    -47.500 -72.983 -29.906  1.00 40.53           C
ANISOU  585  CG2 ILE A 105A    4687   3315   7399  -1304     97    350       C
ATOM    586  CD1 ILE A 105A    -48.287 -74.029 -27.157  1.00 43.28           C
ANISOU  586  CD1 ILE A 105A    4982   3565   7899  -1373    343    674       C
ATOM    587  N   PRO A 106     -44.013 -71.847 -31.047  1.00 37.62           N
ANISOU  587  N   PRO A 106     4569   3075   6650  -1021      4    233       N
ATOM    588  CA  PRO A 106     -43.569 -70.740 -31.909  1.00 36.37           C
ANISOU  588  CA  PRO A 106     4423   3038   6359   -956    -64    145       C
ATOM    589  C   PRO A 106     -44.690 -69.878 -32.496  1.00 36.43           C
ANISOU  589  C   PRO A 106     4336   3137   6367   -999   -116     80       C
ATOM    590  O   PRO A 106     -44.581 -68.651 -32.493  1.00 35.47           O
ANISOU  590  O   PRO A 106     4199   3147   6133   -948   -121     82       O
ATOM    591  CB  PRO A 106     -42.804 -71.455 -33.023  1.00 36.64           C
ANISOU  591  CB  PRO A 106     4535   2991   6397   -927   -132     38       C
ATOM    592  CG  PRO A 106     -42.267 -72.674 -32.365  1.00 37.62           C
ANISOU  592  CG  PRO A 106     4719   2979   6594   -928    -75    108       C
ATOM    593  CD  PRO A 106     -43.340 -73.111 -31.406  1.00 38.46           C
ANISOU  593  CD  PRO A 106     4756   3033   6823  -1017     -9    203       C
ATOM    594  N   PHE A 107     -45.758 -70.508 -32.980  1.00 37.57           N
ANISOU  594  N   PHE A 107     4419   3213   6644  -1092   -156     24       N
ATOM    595  CA  PHE A 107     -46.887 -69.768 -33.560  1.00 37.97           C
ANISOU  595  CA  PHE A 107     4372   3350   6704  -1134   -212    -39       C
ATOM    596  C   PHE A 107     -47.475 -68.754 -32.571  1.00 36.96           C
ANISOU  596  C   PHE A 107     4172   3336   6534  -1131   -144     60       C
ATOM    597  O   PHE A 107     -47.764 -67.612 -32.936  1.00 36.14           O
ANISOU  597  O   PHE A 107     4030   3354   6345  -1097   -177     27       O
ATOM    598  CB  PHE A 107     -47.979 -70.734 -34.040  1.00 39.81           C
ANISOU  598  CB  PHE A 107     4539   3481   7106  -1246   -257   -102       C
ATOM    599  CG  PHE A 107     -49.303 -70.071 -34.299  1.00 41.78           C
ANISOU  599  CG  PHE A 107     4665   3818   7391  -1301   -293   -135       C
ATOM    600  CD1 PHE A 107     -49.487 -69.276 -35.424  1.00 43.19           C
ANISOU  600  CD1 PHE A 107     4826   4095   7491  -1266   -389   -246       C
ATOM    601  CD2 PHE A 107     -50.359 -70.227 -33.412  1.00 43.99           C
ANISOU  601  CD2 PHE A 107     4847   4089   7780  -1382   -229    -48       C
ATOM    602  CE1 PHE A 107     -50.710 -68.653 -35.666  1.00 44.54           C
ANISOU  602  CE1 PHE A 107     4881   4352   7691  -1309   -424   -274       C
ATOM    603  CE2 PHE A 107     -51.585 -69.611 -33.646  1.00 45.08           C
ANISOU  603  CE2 PHE A 107     4864   4312   7950  -1428   -261    -76       C
ATOM    604  CZ  PHE A 107     -51.761 -68.824 -34.776  1.00 44.88           C
ANISOU  604  CZ  PHE A 107     4822   4385   7847  -1391   -362   -191       C
ATOM    605  N   LEU A 108     -47.633 -69.181 -31.320  1.00 36.86           N
ANISOU  605  N   LEU A 108     4146   3282   6576  -1158    -47    185       N
ATOM    606  CA  LEU A 108     -48.225 -68.347 -30.275  1.00 36.23           C
ANISOU  606  CA  LEU A 108     4001   3302   6463  -1154     28    286       C
ATOM    607  C   LEU A 108     -47.254 -67.261 -29.789  1.00 34.06           C
ANISOU  607  C   LEU A 108     3785   3138   6020  -1047     57    327       C
ATOM    608  O   LEU A 108     -47.660 -66.120 -29.560  1.00 33.28           O
ANISOU  608  O   LEU A 108     3639   3157   5850  -1020     67    341       O
ATOM    609  CB  LEU A 108     -48.680 -69.231 -29.109  1.00 37.57           C
ANISOU  609  CB  LEU A 108     4142   3389   6744  -1213    126    408       C
ATOM    610  CG  LEU A 108     -49.695 -68.689 -28.103  1.00 39.02           C
ANISOU  610  CG  LEU A 108     4230   3650   6947  -1240    205    508       C
ATOM    611  CD1 LEU A 108     -50.731 -67.776 -28.754  1.00 40.01           C
ANISOU  611  CD1 LEU A 108     4255   3878   7070  -1265    147    435       C
ATOM    612  CD2 LEU A 108     -50.377 -69.857 -27.392  1.00 41.18           C
ANISOU  612  CD2 LEU A 108     4459   3808   7380  -1329    280    598       C
ATOM    613  N   ARG A 109     -45.981 -67.617 -29.632  1.00 32.81           N
ANISOU  613  N   ARG A 109     3727   2937   5803   -986     71    345       N
ATOM    614  CA  ARG A 109     -44.942 -66.641 -29.295  1.00 31.17           C
ANISOU  614  CA  ARG A 109     3576   2826   5441   -887     86    368       C
ATOM    615  C   ARG A 109     -44.865 -65.541 -30.362  1.00 29.95           C
ANISOU  615  C   ARG A 109     3415   2766   5199   -849      9    267       C
ATOM    616  O   ARG A 109     -44.777 -64.353 -30.041  1.00 28.60           O
ANISOU  616  O   ARG A 109     3232   2704   4929   -801     24    287       O
ATOM    617  CB  ARG A 109     -43.579 -67.326 -29.143  1.00 30.99           C
ANISOU  617  CB  ARG A 109     3655   2736   5383   -832     99    387       C
ATOM    618  CG  ARG A 109     -42.431 -66.371 -28.821  1.00 29.95           C
ANISOU  618  CG  ARG A 109     3577   2701   5101   -734    109    405       C
ATOM    619  CD  ARG A 109     -41.195 -67.117 -28.348  1.00 30.56           C
ANISOU  619  CD  ARG A 109     3739   2718   5154   -681    140    454       C
ATOM    620  NE  ARG A 109     -40.069 -66.215 -28.097  1.00 29.14           N
ANISOU  620  NE  ARG A 109     3602   2631   4838   -593    142    461       N
ATOM    621  CZ  ARG A 109     -38.860 -66.313 -28.654  1.00 29.70           C
ANISOU  621  CZ  ARG A 109     3739   2693   4853   -533    108    417       C
ATOM    622  NH1 ARG A 109     -38.569 -67.287 -29.516  1.00 30.67           N
ANISOU  622  NH1 ARG A 109     3902   2717   5035   -543     70    359       N
ATOM    623  NH2 ARG A 109     -37.921 -65.429 -28.340  1.00 29.00           N
ANISOU  623  NH2 ARG A 109     3674   2694   4650   -463    113    429       N
ATOM    624  N   SER A 110     -44.907 -65.951 -31.627  1.00 29.94           N
ANISOU  624  N   SER A 110     3424   2719   5234   -869    -73    159       N
ATOM    625  CA  SER A 110     -44.922 -65.008 -32.743  1.00 29.24           C
ANISOU  625  CA  SER A 110     3328   2714   5068   -834   -148     64       C
ATOM    626  C   SER A 110     -46.153 -64.107 -32.708  1.00 29.01           C
ANISOU  626  C   SER A 110     3202   2776   5046   -862   -154     63       C
ATOM    627  O   SER A 110     -46.034 -62.891 -32.869  1.00 27.88           O
ANISOU  627  O   SER A 110     3054   2736   4802   -807   -163     54       O
ATOM    628  CB  SER A 110     -44.862 -65.754 -34.077  1.00 30.02           C
ANISOU  628  CB  SER A 110     3452   2742   5210   -851   -235    -53       C
ATOM    629  OG  SER A 110     -43.573 -66.300 -34.285  1.00 30.59           O
ANISOU  629  OG  SER A 110     3621   2758   5243   -798   -236    -65       O
ATOM    630  N   LEU A 111     -47.324 -64.711 -32.493  1.00 29.90           N
ANISOU  630  N   LEU A 111     3234   2845   5282   -948   -146     77       N
ATOM    631  CA  LEU A 111     -48.591 -63.969 -32.440  1.00 30.15           C
ANISOU  631  CA  LEU A 111     3161   2960   5336   -980   -150     79       C
ATOM    632  C   LEU A 111     -48.565 -62.875 -31.367  1.00 29.10           C
ANISOU  632  C   LEU A 111     3015   2926   5117   -929    -74    171       C
ATOM    633  O   LEU A 111     -48.953 -61.729 -31.617  1.00 28.17           O
ANISOU  633  O   LEU A 111     2861   2911   4933   -894    -93    149       O
ATOM    634  CB  LEU A 111     -49.756 -64.925 -32.175  1.00 31.86           C
ANISOU  634  CB  LEU A 111     3290   3104   5712  -1085   -136     98       C
ATOM    635  CG  LEU A 111     -51.171 -64.356 -32.308  1.00 33.27           C
ANISOU  635  CG  LEU A 111     3344   3359   5938  -1129   -154     84       C
ATOM    636  CD1 LEU A 111     -51.428 -63.873 -33.730  1.00 33.98           C
ANISOU  636  CD1 LEU A 111     3416   3501   5992  -1111   -267    -43       C
ATOM    637  CD2 LEU A 111     -52.188 -65.409 -31.905  1.00 35.83           C
ANISOU  637  CD2 LEU A 111     3583   3599   6432  -1239   -125    117       C
ATOM    638  N   ILE A 112     -48.095 -63.236 -30.178  1.00 28.81           N
ANISOU  638  N   ILE A 112     3011   2857   5077   -921     11    270       N
ATOM    639  CA  ILE A 112     -48.052 -62.309 -29.046  1.00 28.10           C
ANISOU  639  CA  ILE A 112     2915   2855   4906   -872     85    357       C
ATOM    640  C   ILE A 112     -46.989 -61.221 -29.235  1.00 26.59           C
ANISOU  640  C   ILE A 112     2794   2739   4571   -780     66    330       C
ATOM    641  O   ILE A 112     -47.251 -60.043 -28.966  1.00 25.85           O
ANISOU  641  O   ILE A 112     2673   2741   4406   -741     81    341       O
ATOM    642  CB  ILE A 112     -47.835 -63.063 -27.710  1.00 28.50           C
ANISOU  642  CB  ILE A 112     2985   2855   4989   -882    180    473       C
ATOM    643  CG1 ILE A 112     -49.030 -63.982 -27.425  1.00 30.74           C
ANISOU  643  CG1 ILE A 112     3185   3074   5422   -977    214    514       C
ATOM    644  CG2 ILE A 112     -47.655 -62.081 -26.564  1.00 27.69           C
ANISOU  644  CG2 ILE A 112     2888   2849   4783   -819    250    551       C
ATOM    645  CD1 ILE A 112     -48.751 -65.058 -26.387  1.00 32.39           C
ANISOU  645  CD1 ILE A 112     3425   3195   5687   -997    297    620       C
ATOM    646  N   MET A 113     -45.802 -61.596 -29.714  1.00 26.01           N
ANISOU  646  N   MET A 113     2805   2619   4459   -746     35    295       N
ATOM    647  CA  MET A 113     -44.763 -60.605 -29.967  1.00 24.94           C
ANISOU  647  CA  MET A 113     2729   2547   4199   -666     17    268       C
ATOM    648  C   MET A 113     -45.194 -59.653 -31.076  1.00 24.81           C
ANISOU  648  C   MET A 113     2683   2597   4146   -651    -48    186       C
ATOM    649  O   MET A 113     -44.939 -58.458 -30.992  1.00 23.52           O
ANISOU  649  O   MET A 113     2528   2514   3894   -597    -42    188       O
ATOM    650  CB  MET A 113     -43.425 -61.255 -30.332  1.00 24.44           C
ANISOU  650  CB  MET A 113     2755   2422   4109   -633     -3    245       C
ATOM    651  CG  MET A 113     -42.258 -60.259 -30.383  1.00 23.64           C
ANISOU  651  CG  MET A 113     2710   2387   3886   -553     -7    235       C
ATOM    652  SD  MET A 113     -41.875 -59.590 -28.754  1.00 23.84           S
ANISOU  652  SD  MET A 113     2742   2474   3841   -513     74    333       S
ATOM    653  CE  MET A 113     -40.985 -58.088 -29.195  1.00 21.69           C
ANISOU  653  CE  MET A 113     2503   2291   3449   -441     47    288       C
ATOM    654  N   LYS A 114     -45.855 -60.180 -32.105  1.00 25.94           N
ANISOU  654  N   LYS A 114     2792   2705   4358   -695   -111    115       N
ATOM    655  CA  LYS A 114     -46.376 -59.329 -33.177  1.00 26.25           C
ANISOU  655  CA  LYS A 114     2799   2813   4364   -677   -176     41       C
ATOM    656  C   LYS A 114     -47.308 -58.258 -32.605  1.00 26.30           C
ANISOU  656  C   LYS A 114     2734   2909   4352   -670   -143     81       C
ATOM    657  O   LYS A 114     -47.199 -57.074 -32.957  1.00 25.70           O
ANISOU  657  O   LYS A 114     2664   2909   4192   -614   -158     62       O
ATOM    658  CB  LYS A 114     -47.109 -60.161 -34.232  1.00 27.39           C
ANISOU  658  CB  LYS A 114     2905   2908   4594   -733   -250    -41       C
ATOM    659  CG  LYS A 114     -47.537 -59.351 -35.459  1.00 28.57           C
ANISOU  659  CG  LYS A 114     3030   3131   4695   -701   -327   -123       C
ATOM    660  CD  LYS A 114     -48.379 -60.151 -36.446  1.00 31.99           C
ANISOU  660  CD  LYS A 114     3414   3527   5213   -757   -408   -210       C
ATOM    661  CE  LYS A 114     -47.621 -61.321 -37.055  1.00 33.59           C
ANISOU  661  CE  LYS A 114     3687   3630   5445   -769   -446   -268       C
ATOM    662  NZ  LYS A 114     -47.805 -62.570 -36.269  1.00 36.93           N
ANISOU  662  NZ  LYS A 114     4098   3945   5989   -846   -406   -226       N
ATOM    663  N   TYR A 115     -48.211 -58.674 -31.719  1.00 27.09           N
ANISOU  663  N   TYR A 115     2767   2996   4530   -724    -93    141       N
ATOM    664  CA  TYR A 115     -49.163 -57.751 -31.101  1.00 27.51           C
ANISOU  664  CA  TYR A 115     2746   3133   4573   -717    -54    184       C
ATOM    665  C   TYR A 115     -48.468 -56.731 -30.194  1.00 26.06           C
ANISOU  665  C   TYR A 115     2610   3008   4283   -647      5    239       C
ATOM    666  O   TYR A 115     -48.879 -55.567 -30.154  1.00 25.61           O
ANISOU  666  O   TYR A 115     2525   3032   4173   -606     10    237       O
ATOM    667  CB  TYR A 115     -50.268 -58.501 -30.337  1.00 29.10           C
ANISOU  667  CB  TYR A 115     2862   3308   4888   -792     -6    242       C
ATOM    668  CG  TYR A 115     -51.172 -57.561 -29.568  1.00 31.37           C
ANISOU  668  CG  TYR A 115     3078   3686   5157   -774     48    296       C
ATOM    669  CD1 TYR A 115     -52.183 -56.851 -30.212  1.00 34.41           C
ANISOU  669  CD1 TYR A 115     3383   4140   5551   -772      5    252       C
ATOM    670  CD2 TYR A 115     -50.980 -57.340 -28.206  1.00 33.57           C
ANISOU  670  CD2 TYR A 115     3371   3987   5399   -748    140    389       C
ATOM    671  CE1 TYR A 115     -53.001 -55.964 -29.506  1.00 36.09           C
ANISOU  671  CE1 TYR A 115     3531   4438   5745   -746     58    301       C
ATOM    672  CE2 TYR A 115     -51.783 -56.456 -27.499  1.00 35.57           C
ANISOU  672  CE2 TYR A 115     3564   4325   5627   -722    192    434       C
ATOM    673  CZ  TYR A 115     -52.791 -55.774 -28.150  1.00 36.53           C
ANISOU  673  CZ  TYR A 115     3606   4510   5765   -722    152    390       C
ATOM    674  OH  TYR A 115     -53.584 -54.901 -27.433  1.00 40.11           O
ANISOU  674  OH  TYR A 115     4000   5048   6194   -689    207    435       O
ATOM    675  N   VAL A 116     -47.423 -57.156 -29.478  1.00 24.94           N
ANISOU  675  N   VAL A 116     2539   2825   4112   -629     46    284       N
ATOM    676  CA  VAL A 116     -46.620 -56.226 -28.678  1.00 23.92           C
ANISOU  676  CA  VAL A 116     2460   2748   3879   -562     90    321       C
ATOM    677  C   VAL A 116     -46.016 -55.143 -29.573  1.00 22.89           C
ANISOU  677  C   VAL A 116     2369   2662   3665   -506     40    257       C
ATOM    678  O   VAL A 116     -46.119 -53.958 -29.272  1.00 22.23           O
ANISOU  678  O   VAL A 116     2280   2647   3520   -462     58    265       O
ATOM    679  CB  VAL A 116     -45.484 -56.936 -27.906  1.00 23.79           C
ANISOU  679  CB  VAL A 116     2515   2681   3842   -549    128    370       C
ATOM    680  CG1 VAL A 116     -44.542 -55.909 -27.273  1.00 23.13           C
ANISOU  680  CG1 VAL A 116     2484   2656   3647   -478    153    386       C
ATOM    681  CG2 VAL A 116     -46.058 -57.864 -26.841  1.00 24.50           C
ANISOU  681  CG2 VAL A 116     2572   2735   4002   -592    194    453       C
ATOM    682  N   LEU A 117     -45.416 -55.548 -30.686  1.00 22.53           N
ANISOU  682  N   LEU A 117     2363   2577   3621   -505    -20    196       N
ATOM    683  CA  LEU A 117     -44.792 -54.584 -31.597  1.00 22.04           C
ANISOU  683  CA  LEU A 117     2340   2553   3481   -450    -61    142       C
ATOM    684  C   LEU A 117     -45.803 -53.614 -32.216  1.00 22.69           C
ANISOU  684  C   LEU A 117     2367   2701   3554   -437    -90    111       C
ATOM    685  O   LEU A 117     -45.572 -52.400 -32.231  1.00 22.31           O
ANISOU  685  O   LEU A 117     2334   2706   3436   -384    -81    111       O
ATOM    686  CB  LEU A 117     -44.030 -55.305 -32.712  1.00 21.72           C
ANISOU  686  CB  LEU A 117     2350   2460   3443   -449   -117     83       C
ATOM    687  CG  LEU A 117     -42.828 -56.153 -32.300  1.00 21.28           C
ANISOU  687  CG  LEU A 117     2359   2343   3383   -444    -96    106       C
ATOM    688  CD1 LEU A 117     -42.288 -56.875 -33.528  1.00 20.71           C
ANISOU  688  CD1 LEU A 117     2328   2221   3320   -441   -154     39       C
ATOM    689  CD2 LEU A 117     -41.744 -55.312 -31.629  1.00 20.88           C
ANISOU  689  CD2 LEU A 117     2355   2330   3248   -390    -58    140       C
ATOM    690  N   THR A 118     -46.914 -54.144 -32.718  1.00 23.98           N
ANISOU  690  N   THR A 118     2464   2858   3791   -483   -125     84       N
ATOM    691  CA  THR A 118     -47.892 -53.318 -33.439  1.00 24.91           C
ANISOU  691  CA  THR A 118     2524   3041   3901   -465   -163     49       C
ATOM    692  C   THR A 118     -48.674 -52.394 -32.498  1.00 25.34           C
ANISOU  692  C   THR A 118     2525   3158   3944   -449   -108    102       C
ATOM    693  O   THR A 118     -48.880 -51.212 -32.812  1.00 24.88           O
ANISOU  693  O   THR A 118     2462   3160   3830   -395   -116     90       O
ATOM    694  CB  THR A 118     -48.877 -54.166 -34.282  1.00 26.05           C
ANISOU  694  CB  THR A 118     2603   3166   4129   -520   -226     -4       C
ATOM    695  OG1 THR A 118     -49.643 -55.036 -33.436  1.00 27.17           O
ANISOU  695  OG1 THR A 118     2681   3273   4368   -591   -189     39       O
ATOM    696  CG2 THR A 118     -48.132 -54.984 -35.327  1.00 26.61           C
ANISOU  696  CG2 THR A 118     2732   3180   4200   -525   -287    -70       C
ATOM    697  N   SER A 119     -49.103 -52.921 -31.350  1.00 25.83           N
ANISOU  697  N   SER A 119     2551   3206   4057   -488    -49    162       N
ATOM    698  CA  SER A 119     -49.871 -52.115 -30.392  1.00 26.39           C
ANISOU  698  CA  SER A 119     2571   3340   4116   -468     10    214       C
ATOM    699  C   SER A 119     -49.031 -50.969 -29.806  1.00 25.72           C
ANISOU  699  C   SER A 119     2552   3288   3931   -398     48    233       C
ATOM    700  O   SER A 119     -49.535 -49.860 -29.631  1.00 25.89           O
ANISOU  700  O   SER A 119     2549   3371   3915   -354     65    238       O
ATOM    701  CB  SER A 119     -50.471 -52.987 -29.278  1.00 27.19           C
ANISOU  701  CB  SER A 119     2621   3419   4289   -522     73    282       C
ATOM    702  OG  SER A 119     -49.469 -53.551 -28.455  1.00 27.26           O
ANISOU  702  OG  SER A 119     2699   3381   4279   -523    117    326       O
ATOM    703  N   ARG A 120     -47.757 -51.232 -29.529  1.00 25.50           N
ANISOU  703  N   ARG A 120     2604   3220   3863   -386     59    240       N
ATOM    704  CA  ARG A 120     -46.845 -50.203 -29.017  1.00 25.10           C
ANISOU  704  CA  ARG A 120     2616   3195   3725   -327     85    249       C
ATOM    705  C   ARG A 120     -46.537 -49.150 -30.076  1.00 24.81           C
ANISOU  705  C   ARG A 120     2606   3182   3638   -281     41    197       C
ATOM    706  O   ARG A 120     -46.577 -47.951 -29.802  1.00 24.43           O
ANISOU  706  O   ARG A 120     2567   3176   3542   -234     62    200       O
ATOM    707  CB  ARG A 120     -45.528 -50.824 -28.540  1.00 24.72           C
ANISOU  707  CB  ARG A 120     2639   3101   3653   -328     99    266       C
ATOM    708  CG  ARG A 120     -45.629 -51.699 -27.297  1.00 26.43           C
ANISOU  708  CG  ARG A 120     2846   3300   3897   -355    156    331       C
ATOM    709  CD  ARG A 120     -46.233 -50.957 -26.159  1.00 27.03           C
ANISOU  709  CD  ARG A 120     2893   3435   3942   -327    215    375       C
ATOM    710  NE  ARG A 120     -46.077 -51.624 -24.871  1.00 26.45           N
ANISOU  710  NE  ARG A 120     2829   3355   3867   -333    276    444       N
ATOM    711  CZ  ARG A 120     -46.643 -51.179 -23.754  1.00 26.84           C
ANISOU  711  CZ  ARG A 120     2852   3456   3888   -308    337    491       C
ATOM    712  NH1 ARG A 120     -47.406 -50.093 -23.790  1.00 27.26           N
ANISOU  712  NH1 ARG A 120     2869   3567   3922   -278    344    474       N
ATOM    713  NH2 ARG A 120     -46.457 -51.814 -22.606  1.00 26.66           N
ANISOU  713  NH2 ARG A 120     2843   3431   3856   -305    393    557       N
ATOM    714  N   SER A 121     -46.221 -49.603 -31.283  1.00 24.95           N
ANISOU  714  N   SER A 121     2641   3170   3667   -292    -17    150       N
ATOM    715  CA  SER A 121     -45.802 -48.691 -32.350  1.00 24.97           C
ANISOU  715  CA  SER A 121     2678   3191   3618   -244    -55    109       C
ATOM    716  C   SER A 121     -46.930 -47.747 -32.782  1.00 25.18           C
ANISOU  716  C   SER A 121     2652   3275   3641   -214    -68     98       C
ATOM    717  O   SER A 121     -46.669 -46.609 -33.181  1.00 25.16           O
ANISOU  717  O   SER A 121     2677   3297   3585   -160    -70     88       O
ATOM    718  CB  SER A 121     -45.262 -49.487 -33.536  1.00 24.95           C
ANISOU  718  CB  SER A 121     2706   3151   3624   -256   -112     62       C
ATOM    719  OG  SER A 121     -44.079 -50.176 -33.152  1.00 26.37           O
ANISOU  719  OG  SER A 121     2941   3281   3796   -267    -96     74       O
ATOM    720  N   TYR A 122     -48.173 -48.215 -32.665  1.00 26.07           N
ANISOU  720  N   TYR A 122     2685   3407   3814   -249    -74    104       N
ATOM    721  CA  TYR A 122     -49.365 -47.416 -32.979  1.00 26.76           C
ANISOU  721  CA  TYR A 122     2707   3556   3905   -221    -85     98       C
ATOM    722  C   TYR A 122     -49.443 -46.083 -32.221  1.00 25.56           C
ANISOU  722  C   TYR A 122     2566   3443   3704   -164    -32    129       C
ATOM    723  O   TYR A 122     -50.091 -45.139 -32.686  1.00 25.18           O
ANISOU  723  O   TYR A 122     2491   3440   3635   -116    -44    119       O
ATOM    724  CB  TYR A 122     -50.624 -48.237 -32.684  1.00 28.47           C
ANISOU  724  CB  TYR A 122     2827   3785   4206   -277    -86    110       C
ATOM    725  CG  TYR A 122     -51.908 -47.615 -33.170  1.00 31.90           C
ANISOU  725  CG  TYR A 122     3180   4286   4656   -253   -111     96       C
ATOM    726  CD1 TYR A 122     -52.328 -47.782 -34.486  1.00 36.31           C
ANISOU  726  CD1 TYR A 122     3710   4860   5225   -250   -190     41       C
ATOM    727  CD2 TYR A 122     -52.712 -46.863 -32.311  1.00 35.38           C
ANISOU  727  CD2 TYR A 122     3570   4777   5095   -226    -57    138       C
ATOM    728  CE1 TYR A 122     -53.525 -47.213 -34.940  1.00 38.16           C
ANISOU  728  CE1 TYR A 122     3863   5163   5471   -223   -219     28       C
ATOM    729  CE2 TYR A 122     -53.903 -46.286 -32.755  1.00 37.70           C
ANISOU  729  CE2 TYR A 122     3783   5136   5404   -197    -80    128       C
ATOM    730  CZ  TYR A 122     -54.303 -46.465 -34.068  1.00 39.28           C
ANISOU  730  CZ  TYR A 122     3953   5355   5617   -196   -162     74       C
ATOM    731  OH  TYR A 122     -55.484 -45.900 -34.505  1.00 41.97           O
ANISOU  731  OH  TYR A 122     4210   5768   5971   -162   -189     64       O
ATOM    732  N   LEU A 123     -48.787 -46.009 -31.066  1.00 23.90           N
ANISOU  732  N   LEU A 123     2395   3216   3472   -164     24    163       N
ATOM    733  CA  LEU A 123     -48.791 -44.802 -30.238  1.00 23.34           C
ANISOU  733  CA  LEU A 123     2340   3175   3352   -112     74    184       C
ATOM    734  C   LEU A 123     -47.819 -43.719 -30.718  1.00 22.35           C
ANISOU  734  C   LEU A 123     2289   3037   3167    -61     65    161       C
ATOM    735  O   LEU A 123     -47.832 -42.605 -30.192  1.00 22.09           O
ANISOU  735  O   LEU A 123     2273   3021   3097    -14     98    168       O
ATOM    736  CB  LEU A 123     -48.479 -45.159 -28.777  1.00 23.33           C
ANISOU  736  CB  LEU A 123     2351   3166   3345   -128    135    226       C
ATOM    737  CG  LEU A 123     -49.660 -45.601 -27.908  1.00 24.62           C
ANISOU  737  CG  LEU A 123     2437   3364   3553   -150    179    269       C
ATOM    738  CD1 LEU A 123     -50.600 -44.428 -27.637  1.00 25.71           C
ANISOU  738  CD1 LEU A 123     2536   3562   3671    -94    206    274       C
ATOM    739  CD2 LEU A 123     -50.421 -46.754 -28.536  1.00 26.11           C
ANISOU  739  CD2 LEU A 123     2557   3540   3822   -212    145    267       C
ATOM    740  N   ILE A 124     -46.982 -44.037 -31.703  1.00 21.56           N
ANISOU  740  N   ILE A 124     2232   2904   3057    -68     22    133       N
ATOM    741  CA  ILE A 124     -45.973 -43.098 -32.194  1.00 20.94           C
ANISOU  741  CA  ILE A 124     2221   2808   2928    -26     18    118       C
ATOM    742  C   ILE A 124     -46.387 -42.554 -33.565  1.00 21.16           C
ANISOU  742  C   ILE A 124     2242   2855   2943     12    -24     95       C
ATOM    743  O   ILE A 124     -46.723 -43.322 -34.470  1.00 20.77           O
ANISOU  743  O   ILE A 124     2168   2811   2914     -6    -72     74       O
ATOM    744  CB  ILE A 124     -44.593 -43.782 -32.325  1.00 20.47           C
ANISOU  744  CB  ILE A 124     2219   2701   2857    -52      9    109       C
ATOM    745  CG1 ILE A 124     -44.139 -44.381 -30.983  1.00 20.64           C
ANISOU  745  CG1 ILE A 124     2249   2708   2885    -83     46    134       C
ATOM    746  CG2 ILE A 124     -43.545 -42.799 -32.853  1.00 20.58           C
ANISOU  746  CG2 ILE A 124     2293   2698   2827    -13     10     97       C
ATOM    747  CD1 ILE A 124     -44.106 -43.387 -29.830  1.00 19.92           C
ANISOU  747  CD1 ILE A 124     2170   2636   2763    -54     94    150       C
ATOM    748  N   ASP A 125     -46.362 -41.229 -33.708  1.00 21.09           N
ANISOU  748  N   ASP A 125     2257   2856   2901     68     -6     99       N
ATOM    749  CA  ASP A 125     -46.615 -40.584 -34.995  1.00 21.65           C
ANISOU  749  CA  ASP A 125     2333   2943   2949    118    -38     88       C
ATOM    750  C   ASP A 125     -45.438 -40.823 -35.926  1.00 20.68           C
ANISOU  750  C   ASP A 125     2270   2789   2801    118    -61     74       C
ATOM    751  O   ASP A 125     -44.297 -40.494 -35.588  1.00 20.29           O
ANISOU  751  O   ASP A 125     2274   2701   2734    115    -32     80       O
ATOM    752  CB  ASP A 125     -46.782 -39.070 -34.834  1.00 22.04           C
ANISOU  752  CB  ASP A 125     2403   2999   2973    180     -4    104       C
ATOM    753  CG  ASP A 125     -48.007 -38.690 -34.032  1.00 25.41           C
ANISOU  753  CG  ASP A 125     2771   3465   3417    198     21    117       C
ATOM    754  OD1 ASP A 125     -49.005 -39.447 -34.023  1.00 27.43           O
ANISOU  754  OD1 ASP A 125     2956   3760   3706    174     -1    116       O
ATOM    755  OD2 ASP A 125     -47.970 -37.604 -33.413  1.00 29.51           O
ANISOU  755  OD2 ASP A 125     3316   3976   3922    236     63    127       O
ATOM    756  N   SER A 126     -45.714 -41.388 -37.098  1.00 20.31           N
ANISOU  756  N   SER A 126     2209   2759   2749    124   -114     51       N
ATOM    757  CA  SER A 126     -44.663 -41.699 -38.058  1.00 19.90           C
ANISOU  757  CA  SER A 126     2211   2684   2667    131   -135     36       C
ATOM    758  C   SER A 126     -45.264 -41.715 -39.464  1.00 20.01           C
ANISOU  758  C   SER A 126     2211   2737   2654    174   -190     14       C
ATOM    759  O   SER A 126     -46.105 -42.565 -39.746  1.00 20.62           O
ANISOU  759  O   SER A 126     2237   2840   2757    151   -237    -15       O
ATOM    760  CB  SER A 126     -44.047 -43.059 -37.729  1.00 19.72           C
ANISOU  760  CB  SER A 126     2194   2627   2670     70   -146     20       C
ATOM    761  OG  SER A 126     -42.953 -43.357 -38.583  1.00 19.74           O
ANISOU  761  OG  SER A 126     2250   2608   2643     81   -160      6       O
ATOM    762  N   PRO A 127     -44.862 -40.769 -40.346  1.00 20.03           N
ANISOU  762  N   PRO A 127     2257   2746   2607    239   -183     29       N
ATOM    763  CA  PRO A 127     -43.886 -39.682 -40.178  1.00 19.07           C
ANISOU  763  CA  PRO A 127     2194   2590   2463    267   -128     63       C
ATOM    764  C   PRO A 127     -44.154 -38.740 -38.997  1.00 18.63           C
ANISOU  764  C   PRO A 127     2129   2519   2430    266    -78     88       C
ATOM    765  O   PRO A 127     -45.303 -38.562 -38.584  1.00 18.24           O
ANISOU  765  O   PRO A 127     2030   2503   2399    274    -82     89       O
ATOM    766  CB  PRO A 127     -43.994 -38.911 -41.499  1.00 19.81           C
ANISOU  766  CB  PRO A 127     2312   2710   2504    345   -141     76       C
ATOM    767  CG  PRO A 127     -44.418 -39.922 -42.476  1.00 20.84           C
ANISOU  767  CG  PRO A 127     2421   2880   2616    348   -208     37       C
ATOM    768  CD  PRO A 127     -45.374 -40.811 -41.727  1.00 20.51           C
ANISOU  768  CD  PRO A 127     2310   2853   2628    290   -237      9       C
ATOM    769  N   PRO A 128     -43.092 -38.116 -38.467  1.00 17.68           N
ANISOU  769  N   PRO A 128     2056   2352   2310    259    -30    105       N
ATOM    770  CA  PRO A 128     -43.205 -37.321 -37.252  1.00 17.48           C
ANISOU  770  CA  PRO A 128     2029   2307   2304    254     14    116       C
ATOM    771  C   PRO A 128     -43.850 -35.969 -37.497  1.00 17.67           C
ANISOU  771  C   PRO A 128     2059   2337   2318    319     35    137       C
ATOM    772  O   PRO A 128     -43.932 -35.522 -38.641  1.00 17.99           O
ANISOU  772  O   PRO A 128     2116   2387   2331    371     23    152       O
ATOM    773  CB  PRO A 128     -41.752 -37.142 -36.828  1.00 17.30           C
ANISOU  773  CB  PRO A 128     2056   2233   2284    226     46    118       C
ATOM    774  CG  PRO A 128     -41.012 -37.138 -38.098  1.00 17.19           C
ANISOU  774  CG  PRO A 128     2076   2211   2244    249     36    127       C
ATOM    775  CD  PRO A 128     -41.726 -38.072 -39.018  1.00 17.70           C
ANISOU  775  CD  PRO A 128     2114   2320   2293    259    -16    112       C
ATOM    776  N   THR A 129     -44.271 -35.327 -36.415  1.00 17.80           N
ANISOU  776  N   THR A 129     2065   2346   2352    323     68    139       N
ATOM    777  CA  THR A 129     -45.072 -34.108 -36.481  1.00 18.06           C
ANISOU  777  CA  THR A 129     2096   2384   2381    388     89    156       C
ATOM    778  C   THR A 129     -44.379 -32.929 -35.778  1.00 18.11           C
ANISOU  778  C   THR A 129     2154   2330   2399    398    140    161       C
ATOM    779  O   THR A 129     -43.602 -32.209 -36.399  1.00 18.35           O
ANISOU  779  O   THR A 129     2234   2315   2424    418    158    177       O
ATOM    780  CB  THR A 129     -46.467 -34.373 -35.890  1.00 18.34           C
ANISOU  780  CB  THR A 129     2064   2475   2431    395     79    151       C
ATOM    781  OG1 THR A 129     -46.331 -34.986 -34.599  1.00 17.90           O
ANISOU  781  OG1 THR A 129     1991   2415   2394    339     96    137       O
ATOM    782  CG2 THR A 129     -47.250 -35.313 -36.801  1.00 18.67           C
ANISOU  782  CG2 THR A 129     2051   2573   2468    394     23    144       C
ATOM    783  N   TYR A 130     -44.632 -32.759 -34.484  1.00 18.33           N
ANISOU  783  N   TYR A 130     2171   2354   2441    383    164    145       N
ATOM    784  CA  TYR A 130     -44.279 -31.526 -33.768  1.00 18.42           C
ANISOU  784  CA  TYR A 130     2225   2313   2463    404    208    138       C
ATOM    785  C   TYR A 130     -42.822 -31.462 -33.307  1.00 18.03           C
ANISOU  785  C   TYR A 130     2221   2207   2425    354    222    120       C
ATOM    786  O   TYR A 130     -42.104 -32.458 -33.313  1.00 17.94           O
ANISOU  786  O   TYR A 130     2203   2202   2410    302    202    113       O
ATOM    787  CB  TYR A 130     -45.197 -31.357 -32.554  1.00 18.84           C
ANISOU  787  CB  TYR A 130     2246   2393   2518    418    227    123       C
ATOM    788  CG  TYR A 130     -46.665 -31.466 -32.902  1.00 19.28           C
ANISOU  788  CG  TYR A 130     2244   2513   2570    464    214    140       C
ATOM    789  CD1 TYR A 130     -47.453 -32.495 -32.386  1.00 20.05           C
ANISOU  789  CD1 TYR A 130     2275   2671   2670    435    200    138       C
ATOM    790  CD2 TYR A 130     -47.256 -30.564 -33.785  1.00 20.17           C
ANISOU  790  CD2 TYR A 130     2362   2625   2677    535    216    163       C
ATOM    791  CE1 TYR A 130     -48.807 -32.601 -32.719  1.00 21.77           C
ANISOU  791  CE1 TYR A 130     2428   2951   2893    473    186    152       C
ATOM    792  CE2 TYR A 130     -48.598 -30.665 -34.120  1.00 22.14           C
ANISOU  792  CE2 TYR A 130     2549   2940   2922    580    199    177       C
ATOM    793  CZ  TYR A 130     -49.366 -31.686 -33.584  1.00 22.41           C
ANISOU  793  CZ  TYR A 130     2512   3037   2966    546    182    169       C
ATOM    794  OH  TYR A 130     -50.697 -31.780 -33.920  1.00 24.50           O
ANISOU  794  OH  TYR A 130     2705   3370   3234    586    164    181       O
ATOM    795  N   ASN A 131     -42.387 -30.271 -32.905  1.00 17.86           N
ANISOU  795  N   ASN A 131     2241   2126   2420    371    255    111       N
ATOM    796  CA  ASN A 131     -41.110 -30.128 -32.205  1.00 17.37           C
ANISOU  796  CA  ASN A 131     2211   2014   2374    321    266     82       C
ATOM    797  C   ASN A 131     -41.158 -28.933 -31.258  1.00 17.49           C
ANISOU  797  C   ASN A 131     2257   1984   2406    343    297     52       C
ATOM    798  O   ASN A 131     -42.223 -28.349 -31.068  1.00 17.45           O
ANISOU  798  O   ASN A 131     2246   1990   2396    397    312     54       O
ATOM    799  CB  ASN A 131     -39.909 -30.104 -33.178  1.00 17.27           C
ANISOU  799  CB  ASN A 131     2227   1961   2375    297    266    101       C
ATOM    800  CG  ASN A 131     -39.850 -28.852 -34.052  1.00 17.96           C
ANISOU  800  CG  ASN A 131     2351   1990   2482    343    297    131       C
ATOM    801  OD1 ASN A 131     -40.278 -27.766 -33.665  1.00 18.29           O
ANISOU  801  OD1 ASN A 131     2414   1994   2541    379    323    124       O
ATOM    802  ND2 ASN A 131     -39.280 -29.010 -35.240  1.00 18.33           N
ANISOU  802  ND2 ASN A 131     2410   2031   2526    344    297    168       N
ATOM    803  N   VAL A 132     -40.032 -28.582 -30.643  1.00 17.67           N
ANISOU  803  N   VAL A 132     2309   1957   2449    303    304     18       N
ATOM    804  CA  VAL A 132     -40.031 -27.511 -29.634  1.00 18.13           C
ANISOU  804  CA  VAL A 132     2398   1970   2522    319    325    -26       C
ATOM    805  C   VAL A 132     -40.536 -26.162 -30.176  1.00 18.85           C
ANISOU  805  C   VAL A 132     2522   2001   2640    378    358    -10       C
ATOM    806  O   VAL A 132     -41.122 -25.361 -29.437  1.00 19.29           O
ANISOU  806  O   VAL A 132     2595   2037   2698    419    377    -40       O
ATOM    807  CB  VAL A 132     -38.634 -27.349 -28.978  1.00 18.20           C
ANISOU  807  CB  VAL A 132     2429   1932   2554    261    319    -71       C
ATOM    808  CG1 VAL A 132     -37.604 -26.865 -29.984  1.00 17.78           C
ANISOU  808  CG1 VAL A 132     2398   1811   2546    236    330    -47       C
ATOM    809  CG2 VAL A 132     -38.705 -26.397 -27.779  1.00 19.00           C
ANISOU  809  CG2 VAL A 132     2559   1999   2661    278    331   -132       C
ATOM    810  N   HIS A 133     -40.334 -25.917 -31.468  1.00 18.97           N
ANISOU  810  N   HIS A 133     2549   1987   2673    391    366     39       N
ATOM    811  CA  HIS A 133     -40.723 -24.652 -32.074  1.00 20.00           C
ANISOU  811  CA  HIS A 133     2715   2055   2830    451    401     66       C
ATOM    812  C   HIS A 133     -42.044 -24.664 -32.834  1.00 19.85           C
ANISOU  812  C   HIS A 133     2674   2087   2781    526    400    112       C
ATOM    813  O   HIS A 133     -42.526 -23.600 -33.227  1.00 20.16           O
ANISOU  813  O   HIS A 133     2743   2081   2837    589    430    136       O
ATOM    814  CB  HIS A 133     -39.615 -24.146 -32.987  1.00 20.34           C
ANISOU  814  CB  HIS A 133     2792   2023   2914    427    421     98       C
ATOM    815  CG  HIS A 133     -38.413 -23.657 -32.248  1.00 22.43           C
ANISOU  815  CG  HIS A 133     3080   2214   3228    365    430     49       C
ATOM    816  ND1 HIS A 133     -37.149 -23.669 -32.794  1.00 24.01           N
ANISOU  816  ND1 HIS A 133     3287   2370   3464    312    438     66       N
ATOM    817  CD2 HIS A 133     -38.280 -23.154 -30.996  1.00 24.60           C
ANISOU  817  CD2 HIS A 133     3371   2456   3521    349    429    -19       C
ATOM    818  CE1 HIS A 133     -36.290 -23.181 -31.916  1.00 25.21           C
ANISOU  818  CE1 HIS A 133     3454   2464   3662    261    439      9       C
ATOM    819  NE2 HIS A 133     -36.949 -22.868 -30.815  1.00 25.15           N
ANISOU  819  NE2 HIS A 133     3453   2462   3640    284    430    -46       N
ATOM    820  N   TYR A 134     -42.625 -25.844 -33.031  1.00 19.02           N
ANISOU  820  N   TYR A 134     2518   2074   2636    520    367    124       N
ATOM    821  CA  TYR A 134     -43.843 -25.983 -33.829  1.00 19.03           C
ANISOU  821  CA  TYR A 134     2487   2134   2610    584    355    163       C
ATOM    822  C   TYR A 134     -44.910 -26.819 -33.125  1.00 19.21           C
ANISOU  822  C   TYR A 134     2448   2244   2606    586    333    145       C
ATOM    823  O   TYR A 134     -44.762 -28.040 -32.972  1.00 18.86           O
ANISOU  823  O   TYR A 134     2367   2251   2548    533    303    136       O
ATOM    824  CB  TYR A 134     -43.512 -26.558 -35.213  1.00 18.49           C
ANISOU  824  CB  TYR A 134     2413   2088   2524    581    333    206       C
ATOM    825  CG  TYR A 134     -42.731 -25.574 -36.045  1.00 18.84           C
ANISOU  825  CG  TYR A 134     2515   2054   2592    602    367    243       C
ATOM    826  CD1 TYR A 134     -41.342 -25.601 -36.061  1.00 18.92           C
ANISOU  826  CD1 TYR A 134     2553   2008   2629    540    380    237       C
ATOM    827  CD2 TYR A 134     -43.377 -24.581 -36.770  1.00 19.34           C
ANISOU  827  CD2 TYR A 134     2601   2095   2654    685    391    287       C
ATOM    828  CE1 TYR A 134     -40.619 -24.683 -36.792  1.00 19.20           C
ANISOU  828  CE1 TYR A 134     2635   1966   2694    554    419    276       C
ATOM    829  CE2 TYR A 134     -42.657 -23.652 -37.513  1.00 19.47           C
ANISOU  829  CE2 TYR A 134     2671   2031   2696    705    431    330       C
ATOM    830  CZ  TYR A 134     -41.273 -23.718 -37.518  1.00 19.76           C
ANISOU  830  CZ  TYR A 134     2732   2011   2764    635    447    325       C
ATOM    831  OH  TYR A 134     -40.536 -22.805 -38.242  1.00 21.41           O
ANISOU  831  OH  TYR A 134     2989   2137   3007    649    494    373       O
ATOM    832  N   GLY A 135     -45.970 -26.137 -32.691  1.00 19.53           N
ANISOU  832  N   GLY A 135     2478   2297   2646    650    353    142       N
ATOM    833  CA  GLY A 135     -47.151 -26.777 -32.099  1.00 19.83           C
ANISOU  833  CA  GLY A 135     2450   2420   2663    665    342    136       C
ATOM    834  C   GLY A 135     -48.246 -27.067 -33.117  1.00 20.15           C
ANISOU  834  C   GLY A 135     2437   2529   2689    714    316    174       C
ATOM    835  O   GLY A 135     -49.375 -27.415 -32.746  1.00 20.52           O
ANISOU  835  O   GLY A 135     2422   2647   2729    738    310    175       O
ATOM    836  N   TYR A 136     -47.912 -26.886 -34.394  1.00 20.05           N
ANISOU  836  N   TYR A 136     2447   2498   2671    734    301    207       N
ATOM    837  CA  TYR A 136     -48.755 -27.264 -35.531  1.00 20.05           C
ANISOU  837  CA  TYR A 136     2402   2566   2649    777    264    239       C
ATOM    838  C   TYR A 136     -47.825 -27.946 -36.531  1.00 19.81           C
ANISOU  838  C   TYR A 136     2392   2530   2606    734    234    250       C
ATOM    839  O   TYR A 136     -46.616 -27.734 -36.490  1.00 19.56           O
ANISOU  839  O   TYR A 136     2415   2430   2586    695    255    247       O
ATOM    840  CB  TYR A 136     -49.411 -26.024 -36.154  1.00 20.75           C
ANISOU  840  CB  TYR A 136     2511   2639   2733    880    285    275       C
ATOM    841  CG  TYR A 136     -48.428 -24.920 -36.513  1.00 20.13           C
ANISOU  841  CG  TYR A 136     2520   2457   2670    899    326    296       C
ATOM    842  CD1 TYR A 136     -47.811 -24.887 -37.757  1.00 20.09           C
ANISOU  842  CD1 TYR A 136     2549   2435   2650    910    317    335       C
ATOM    843  CD2 TYR A 136     -48.118 -23.910 -35.603  1.00 20.72           C
ANISOU  843  CD2 TYR A 136     2645   2451   2778    907    374    276       C
ATOM    844  CE1 TYR A 136     -46.901 -23.884 -38.085  1.00 20.32           C
ANISOU  844  CE1 TYR A 136     2653   2366   2702    922    362    362       C
ATOM    845  CE2 TYR A 136     -47.202 -22.902 -35.921  1.00 21.01           C
ANISOU  845  CE2 TYR A 136     2758   2383   2843    915    413    294       C
ATOM    846  CZ  TYR A 136     -46.603 -22.898 -37.165  1.00 21.00           C
ANISOU  846  CZ  TYR A 136     2784   2365   2832    921    409    342       C
ATOM    847  OH  TYR A 136     -45.705 -21.907 -37.500  1.00 21.99           O
ANISOU  847  OH  TYR A 136     2979   2384   2992    926    455    368       O
ATOM    848  N   LYS A 137     -48.373 -28.774 -37.412  1.00 19.38           N
ANISOU  848  N   LYS A 137     2289   2546   2527    741    185    258       N
ATOM    849  CA  LYS A 137     -47.556 -29.471 -38.396  1.00 19.19           C
ANISOU  849  CA  LYS A 137     2285   2524   2483    710    155    264       C
ATOM    850  C   LYS A 137     -46.986 -28.488 -39.430  1.00 19.02           C
ANISOU  850  C   LYS A 137     2328   2454   2444    769    179    308       C
ATOM    851  O   LYS A 137     -47.671 -27.558 -39.861  1.00 19.18           O
ANISOU  851  O   LYS A 137     2356   2478   2453    853    193    340       O
ATOM    852  CB  LYS A 137     -48.361 -30.574 -39.079  1.00 19.55           C
ANISOU  852  CB  LYS A 137     2265   2658   2507    708     91    253       C
ATOM    853  CG  LYS A 137     -48.479 -31.841 -38.237  1.00 21.02           C
ANISOU  853  CG  LYS A 137     2398   2872   2717    624     68    215       C
ATOM    854  CD  LYS A 137     -49.641 -32.721 -38.670  1.00 23.22           C
ANISOU  854  CD  LYS A 137     2594   3235   2993    626     10    201       C
ATOM    855  CE  LYS A 137     -50.912 -32.352 -37.920  1.00 25.73           C
ANISOU  855  CE  LYS A 137     2848   3595   3332    657     24    204       C
ATOM    856  NZ  LYS A 137     -52.150 -32.957 -38.486  1.00 27.08           N
ANISOU  856  NZ  LYS A 137     2931   3853   3506    674    -33    195       N
ATOM    857  N   SER A 138     -45.729 -28.689 -39.811  1.00 18.65           N
ANISOU  857  N   SER A 138     2328   2364   2396    728    190    314       N
ATOM    858  CA  SER A 138     -45.096 -27.817 -40.805  1.00 19.39           C
ANISOU  858  CA  SER A 138     2481   2410   2476    778    222    364       C
ATOM    859  C   SER A 138     -43.985 -28.538 -41.541  1.00 18.86           C
ANISOU  859  C   SER A 138     2437   2341   2389    738    212    369       C
ATOM    860  O   SER A 138     -43.411 -29.502 -41.023  1.00 18.04           O
ANISOU  860  O   SER A 138     2316   2241   2297    661    194    331       O
ATOM    861  CB  SER A 138     -44.533 -26.562 -40.130  1.00 19.64           C
ANISOU  861  CB  SER A 138     2566   2343   2555    779    287    376       C
ATOM    862  OG  SER A 138     -43.404 -26.879 -39.338  1.00 21.08           O
ANISOU  862  OG  SER A 138     2763   2476   2771    691    301    343       O
ATOM    863  N   TRP A 139     -43.664 -28.061 -42.743  1.00 19.23           N
ANISOU  863  N   TRP A 139     2523   2381   2404    797    228    420       N
ATOM    864  CA  TRP A 139     -42.563 -28.646 -43.485  1.00 18.95           C
ANISOU  864  CA  TRP A 139     2512   2342   2346    770    229    431       C
ATOM    865  C   TRP A 139     -41.246 -28.471 -42.729  1.00 18.19           C
ANISOU  865  C   TRP A 139     2443   2164   2303    693    274    422       C
ATOM    866  O   TRP A 139     -40.391 -29.362 -42.761  1.00 17.79           O
ANISOU  866  O   TRP A 139     2389   2122   2250    637    262    402       O
ATOM    867  CB  TRP A 139     -42.439 -28.104 -44.920  1.00 19.67           C
ANISOU  867  CB  TRP A 139     2643   2444   2385    857    247    495       C
ATOM    868  CG  TRP A 139     -41.585 -29.034 -45.684  1.00 19.90           C
ANISOU  868  CG  TRP A 139     2682   2502   2377    834    230    492       C
ATOM    869  CD1 TRP A 139     -40.256 -28.903 -45.945  1.00 19.93           C
ANISOU  869  CD1 TRP A 139     2725   2455   2394    806    279    520       C
ATOM    870  CD2 TRP A 139     -41.971 -30.316 -46.179  1.00 20.09           C
ANISOU  870  CD2 TRP A 139     2671   2610   2351    831    159    449       C
ATOM    871  NE1 TRP A 139     -39.793 -30.016 -46.613  1.00 20.73           N
ANISOU  871  NE1 TRP A 139     2820   2608   2449    795    246    501       N
ATOM    872  CE2 TRP A 139     -40.830 -30.899 -46.765  1.00 20.56           C
ANISOU  872  CE2 TRP A 139     2757   2665   2388    809    170    454       C
ATOM    873  CE3 TRP A 139     -43.184 -31.019 -46.208  1.00 21.20           C
ANISOU  873  CE3 TRP A 139     2758   2828   2468    845     87    405       C
ATOM    874  CZ2 TRP A 139     -40.862 -32.156 -47.371  1.00 21.14           C
ANISOU  874  CZ2 TRP A 139     2814   2805   2414    805    110    412       C
ATOM    875  CZ3 TRP A 139     -43.215 -32.265 -46.817  1.00 21.44           C
ANISOU  875  CZ3 TRP A 139     2767   2921   2457    833     26    363       C
ATOM    876  CH2 TRP A 139     -42.065 -32.818 -47.391  1.00 21.02           C
ANISOU  876  CH2 TRP A 139     2750   2858   2379    815     37    365       C
ATOM    877  N   GLU A 140     -41.086 -27.348 -42.027  1.00 18.51           N
ANISOU  877  N   GLU A 140     2510   2129   2396    690    324    432       N
ATOM    878  CA  GLU A 140     -39.881 -27.147 -41.209  1.00 18.75           C
ANISOU  878  CA  GLU A 140     2558   2083   2482    612    358    413       C
ATOM    879  C   GLU A 140     -39.755 -28.235 -40.139  1.00 18.05           C
ANISOU  879  C   GLU A 140     2430   2026   2404    535    320    348       C
ATOM    880  O   GLU A 140     -38.684 -28.828 -39.983  1.00 18.24           O
ANISOU  880  O   GLU A 140     2453   2038   2439    474    319    333       O
ATOM    881  CB  GLU A 140     -39.862 -25.747 -40.579  1.00 19.38           C
ANISOU  881  CB  GLU A 140     2671   2074   2618    624    410    422       C
ATOM    882  CG  GLU A 140     -38.640 -25.437 -39.696  1.00 19.59           C
ANISOU  882  CG  GLU A 140     2713   2021   2710    543    440    393       C
ATOM    883  CD  GLU A 140     -37.313 -25.417 -40.443  1.00 21.23           C
ANISOU  883  CD  GLU A 140     2941   2192   2934    514    473    431       C
ATOM    884  OE1 GLU A 140     -36.264 -25.541 -39.767  1.00 20.69           O
ANISOU  884  OE1 GLU A 140     2868   2085   2910    438    481    399       O
ATOM    885  OE2 GLU A 140     -37.307 -25.275 -41.690  1.00 22.74           O
ANISOU  885  OE2 GLU A 140     3152   2397   3092    570    492    494       O
ATOM    886  N   ALA A 141     -40.843 -28.504 -39.415  1.00 18.36           N
ANISOU  886  N   ALA A 141     2433   2107   2437    541    290    315       N
ATOM    887  CA  ALA A 141     -40.822 -29.518 -38.350  1.00 17.71           C
ANISOU  887  CA  ALA A 141     2313   2054   2362    474    259    262       C
ATOM    888  C   ALA A 141     -40.600 -30.916 -38.922  1.00 17.71           C
ANISOU  888  C   ALA A 141     2288   2110   2330    445    216    253       C
ATOM    889  O   ALA A 141     -39.852 -31.714 -38.364  1.00 17.43           O
ANISOU  889  O   ALA A 141     2245   2071   2306    383    206    226       O
ATOM    890  CB  ALA A 141     -42.110 -29.467 -37.522  1.00 17.69           C
ANISOU  890  CB  ALA A 141     2275   2087   2360    494    246    239       C
ATOM    891  N   PHE A 142     -41.242 -31.215 -40.045  1.00 18.03           N
ANISOU  891  N   PHE A 142     2319   2202   2331    496    188    273       N
ATOM    892  CA  PHE A 142     -41.016 -32.498 -40.681  1.00 17.68           C
ANISOU  892  CA  PHE A 142     2258   2205   2256    475    145    258       C
ATOM    893  C   PHE A 142     -39.568 -32.658 -41.149  1.00 17.65           C
ANISOU  893  C   PHE A 142     2291   2166   2250    450    168    272       C
ATOM    894  O   PHE A 142     -38.927 -33.670 -40.856  1.00 17.78           O
ANISOU  894  O   PHE A 142     2296   2188   2271    396    150    244       O
ATOM    895  CB  PHE A 142     -41.934 -32.738 -41.879  1.00 18.21           C
ANISOU  895  CB  PHE A 142     2309   2335   2273    540    104    269       C
ATOM    896  CG  PHE A 142     -41.491 -33.905 -42.693  1.00 17.55           C
ANISOU  896  CG  PHE A 142     2225   2288   2157    526     65    252       C
ATOM    897  CD1 PHE A 142     -41.625 -35.185 -42.189  1.00 18.14           C
ANISOU  897  CD1 PHE A 142     2263   2385   2245    466     24    205       C
ATOM    898  CD2 PHE A 142     -40.840 -33.726 -43.910  1.00 18.53           C
ANISOU  898  CD2 PHE A 142     2390   2415   2238    572     77    283       C
ATOM    899  CE1 PHE A 142     -41.160 -36.281 -42.900  1.00 18.52           C
ANISOU  899  CE1 PHE A 142     2316   2456   2267    453    -11    183       C
ATOM    900  CE2 PHE A 142     -40.375 -34.814 -44.623  1.00 18.79           C
ANISOU  900  CE2 PHE A 142     2426   2478   2236    563     44    261       C
ATOM    901  CZ  PHE A 142     -40.537 -36.094 -44.120  1.00 18.99           C
ANISOU  901  CZ  PHE A 142     2416   2522   2278    503     -3    208       C
ATOM    902  N   SER A 143     -39.056 -31.660 -41.865  1.00 17.67           N
ANISOU  902  N   SER A 143     2334   2131   2249    491    212    319       N
ATOM    903  CA  SER A 143     -37.828 -31.823 -42.644  1.00 17.69           C
ANISOU  903  CA  SER A 143     2365   2117   2239    486    236    344       C
ATOM    904  C   SER A 143     -36.528 -31.582 -41.884  1.00 17.64           C
ANISOU  904  C   SER A 143     2368   2047   2285    421    276    340       C
ATOM    905  O   SER A 143     -35.490 -32.113 -42.277  1.00 17.41           O
ANISOU  905  O   SER A 143     2346   2019   2252    399    284    345       O
ATOM    906  CB  SER A 143     -37.853 -30.923 -43.882  1.00 18.50           C
ANISOU  906  CB  SER A 143     2504   2215   2309    566    270    407       C
ATOM    907  OG  SER A 143     -37.777 -29.550 -43.536  1.00 18.01           O
ANISOU  907  OG  SER A 143     2468   2084   2292    579    325    442       O
ATOM    908  N   ASN A 144     -36.576 -30.784 -40.821  1.00 17.26           N
ANISOU  908  N   ASN A 144     2321   1949   2288    394    298    326       N
ATOM    909  CA  ASN A 144     -35.352 -30.388 -40.121  1.00 17.30           C
ANISOU  909  CA  ASN A 144     2335   1893   2348    335    332    318       C
ATOM    910  C   ASN A 144     -34.924 -31.449 -39.110  1.00 16.67           C
ANISOU  910  C   ASN A 144     2225   1834   2276    268    298    265       C
ATOM    911  O   ASN A 144     -35.480 -31.539 -38.018  1.00 16.37           O
ANISOU  911  O   ASN A 144     2170   1802   2249    247    279    227       O
ATOM    912  CB  ASN A 144     -35.538 -29.033 -39.443  1.00 17.41           C
ANISOU  912  CB  ASN A 144     2367   1837   2411    337    368    319       C
ATOM    913  CG  ASN A 144     -34.228 -28.436 -38.980  1.00 18.63           C
ANISOU  913  CG  ASN A 144     2530   1920   2627    281    406    315       C
ATOM    914  OD1 ASN A 144     -33.324 -29.158 -38.542  1.00 16.47           O
ANISOU  914  OD1 ASN A 144     2237   1658   2364    225    391    287       O
ATOM    915  ND2 ASN A 144     -34.109 -27.101 -39.121  1.00 21.49           N
ANISOU  915  ND2 ASN A 144     2924   2206   3035    299    455    344       N
ATOM    916  N   LEU A 145     -33.922 -32.242 -39.480  1.00 16.96           N
ANISOU  916  N   LEU A 145     2256   1884   2305    242    295    267       N
ATOM    917  CA  LEU A 145     -33.497 -33.384 -38.678  1.00 16.84           C
ANISOU  917  CA  LEU A 145     2214   1894   2290    190    261    225       C
ATOM    918  C   LEU A 145     -32.701 -32.993 -37.428  1.00 16.71           C
ANISOU  918  C   LEU A 145     2189   1838   2322    134    273    196       C
ATOM    919  O   LEU A 145     -32.433 -33.840 -36.581  1.00 15.90           O
ANISOU  919  O   LEU A 145     2067   1757   2218     97    245    162       O
ATOM    920  CB  LEU A 145     -32.678 -34.351 -39.532  1.00 16.76           C
ANISOU  920  CB  LEU A 145     2203   1910   2254    190    255    237       C
ATOM    921  CG  LEU A 145     -33.378 -34.909 -40.775  1.00 17.76           C
ANISOU  921  CG  LEU A 145     2339   2085   2325    245    233    252       C
ATOM    922  CD1 LEU A 145     -32.399 -35.750 -41.583  1.00 18.48           C
ANISOU  922  CD1 LEU A 145     2435   2195   2391    250    234    261       C
ATOM    923  CD2 LEU A 145     -34.614 -35.728 -40.404  1.00 18.82           C
ANISOU  923  CD2 LEU A 145     2451   2261   2439    246    180    217       C
ATOM    924  N   SER A 146     -32.351 -31.713 -37.299  1.00 17.23           N
ANISOU  924  N   SER A 146     2272   1844   2431    131    312    207       N
ATOM    925  CA  SER A 146     -31.611 -31.254 -36.125  1.00 17.93           C
ANISOU  925  CA  SER A 146     2352   1894   2567     78    316    169       C
ATOM    926  C   SER A 146     -32.476 -31.142 -34.861  1.00 17.71           C
ANISOU  926  C   SER A 146     2320   1875   2535     74    293    123       C
ATOM    927  O   SER A 146     -31.936 -31.013 -33.768  1.00 18.12           O
ANISOU  927  O   SER A 146     2363   1912   2608     35    283     80       O
ATOM    928  CB  SER A 146     -30.900 -29.930 -36.410  1.00 18.80           C
ANISOU  928  CB  SER A 146     2480   1929   2736     69    365    190       C
ATOM    929  OG  SER A 146     -29.816 -30.133 -37.301  1.00 20.70           O
ANISOU  929  OG  SER A 146     2714   2165   2987     59    391    228       O
ATOM    930  N   TYR A 147     -33.801 -31.173 -35.010  1.00 17.18           N
ANISOU  930  N   TYR A 147     2256   1835   2436    119    283    131       N
ATOM    931  CA  TYR A 147     -34.709 -31.188 -33.864  1.00 17.31           C
ANISOU  931  CA  TYR A 147     2264   1872   2441    122    266     94       C
ATOM    932  C   TYR A 147     -35.020 -32.606 -33.376  1.00 16.54           C
ANISOU  932  C   TYR A 147     2137   1840   2309    104    229     79       C
ATOM    933  O   TYR A 147     -35.190 -33.526 -34.178  1.00 16.26           O
ANISOU  933  O   TYR A 147     2090   1839   2249    112    211    100       O
ATOM    934  CB  TYR A 147     -36.062 -30.597 -34.247  1.00 17.76           C
ANISOU  934  CB  TYR A 147     2329   1934   2484    181    275    114       C
ATOM    935  CG  TYR A 147     -36.155 -29.109 -34.473  1.00 17.78           C
ANISOU  935  CG  TYR A 147     2365   1870   2520    212    314    127       C
ATOM    936  CD1 TYR A 147     -36.003 -28.568 -35.746  1.00 18.44           C
ANISOU  936  CD1 TYR A 147     2470   1926   2611    246    341    179       C
ATOM    937  CD2 TYR A 147     -36.514 -28.251 -33.433  1.00 18.86           C
ANISOU  937  CD2 TYR A 147     2514   1973   2678    218    326     91       C
ATOM    938  CE1 TYR A 147     -36.158 -27.203 -35.969  1.00 18.96           C
ANISOU  938  CE1 TYR A 147     2569   1923   2710    280    382    200       C
ATOM    939  CE2 TYR A 147     -36.672 -26.884 -33.647  1.00 19.91           C
ANISOU  939  CE2 TYR A 147     2682   2036   2846    251    363    103       C
ATOM    940  CZ  TYR A 147     -36.486 -26.365 -34.915  1.00 20.12           C
ANISOU  940  CZ  TYR A 147     2730   2029   2887    281    392    160       C
ATOM    941  OH  TYR A 147     -36.636 -25.008 -35.140  1.00 21.10           O
ANISOU  941  OH  TYR A 147     2892   2074   3050    316    433    179       O
ATOM    942  N   TYR A 148     -35.162 -32.768 -32.063  1.00 16.29           N
ANISOU  942  N   TYR A 148     2096   1822   2273     85    218     42       N
ATOM    943  CA  TYR A 148     -35.928 -33.895 -31.535  1.00 16.26           C
ANISOU  943  CA  TYR A 148     2065   1876   2237     83    194     38       C
ATOM    944  C   TYR A 148     -37.385 -33.640 -31.900  1.00 16.45           C
ANISOU  944  C   TYR A 148     2079   1921   2250    128    198     55       C
ATOM    945  O   TYR A 148     -37.823 -32.496 -31.919  1.00 16.82           O
ANISOU  945  O   TYR A 148     2142   1940   2308    161    220     55       O
ATOM    946  CB  TYR A 148     -35.828 -33.981 -30.015  1.00 16.46           C
ANISOU  946  CB  TYR A 148     2085   1916   2254     65    189      2       C
ATOM    947  CG  TYR A 148     -34.473 -34.365 -29.461  1.00 16.58           C
ANISOU  947  CG  TYR A 148     2101   1925   2273     24    176    -19       C
ATOM    948  CD1 TYR A 148     -33.962 -35.651 -29.637  1.00 17.21           C
ANISOU  948  CD1 TYR A 148     2165   2034   2341      2    156     -4       C
ATOM    949  CD2 TYR A 148     -33.720 -33.453 -28.724  1.00 17.55           C
ANISOU  949  CD2 TYR A 148     2239   2015   2414     10    181    -58       C
ATOM    950  CE1 TYR A 148     -32.725 -36.018 -29.103  1.00 18.06           C
ANISOU  950  CE1 TYR A 148     2269   2142   2450    -28    143    -22       C
ATOM    951  CE2 TYR A 148     -32.476 -33.811 -28.187  1.00 18.34           C
ANISOU  951  CE2 TYR A 148     2330   2119   2518    -25    163    -81       C
ATOM    952  CZ  TYR A 148     -31.988 -35.093 -28.377  1.00 18.82           C
ANISOU  952  CZ  TYR A 148     2373   2214   2562    -42    145    -60       C
ATOM    953  OH  TYR A 148     -30.762 -35.457 -27.852  1.00 20.43           O
ANISOU  953  OH  TYR A 148     2565   2427   2769    -69    125    -80       O
ATOM    954  N   THR A 149     -38.139 -34.693 -32.182  1.00 16.31           N
ANISOU  954  N   THR A 149     2032   1951   2215    129    175     69       N
ATOM    955  CA  THR A 149     -39.574 -34.549 -32.387  1.00 16.45           C
ANISOU  955  CA  THR A 149     2027   2000   2225    168    174     81       C
ATOM    956  C   THR A 149     -40.281 -34.502 -31.026  1.00 16.86           C
ANISOU  956  C   THR A 149     2060   2076   2271    169    186     64       C
ATOM    957  O   THR A 149     -39.647 -34.656 -29.967  1.00 16.75           O
ANISOU  957  O   THR A 149     2055   2057   2253    142    192     43       O
ATOM    958  CB  THR A 149     -40.159 -35.654 -33.321  1.00 16.70           C
ANISOU  958  CB  THR A 149     2028   2071   2246    167    141     96       C
ATOM    959  OG1 THR A 149     -41.466 -35.262 -33.771  1.00 15.79           O
ANISOU  959  OG1 THR A 149     1889   1985   2127    211    137    108       O
ATOM    960  CG2 THR A 149     -40.253 -37.000 -32.621  1.00 15.51           C
ANISOU  960  CG2 THR A 149     1848   1950   2096    124    123     89       C
ATOM    961  N   ARG A 150     -41.584 -34.260 -31.055  1.00 17.11           N
ANISOU  961  N   ARG A 150     2064   2137   2299    206    191     74       N
ATOM    962  CA  ARG A 150     -42.376 -34.151 -29.840  1.00 17.18           C
ANISOU  962  CA  ARG A 150     2052   2175   2300    219    211     64       C
ATOM    963  C   ARG A 150     -43.641 -35.001 -29.932  1.00 17.26           C
ANISOU  963  C   ARG A 150     2003   2244   2312    222    200     84       C
ATOM    964  O   ARG A 150     -44.416 -34.876 -30.881  1.00 17.76           O
ANISOU  964  O   ARG A 150     2042   2324   2381    250    186     99       O
ATOM    965  CB  ARG A 150     -42.719 -32.690 -29.562  1.00 17.66           C
ANISOU  965  CB  ARG A 150     2138   2209   2363    270    241     51       C
ATOM    966  CG  ARG A 150     -41.557 -31.892 -28.983  1.00 17.50           C
ANISOU  966  CG  ARG A 150     2169   2132   2348    257    254     18       C
ATOM    967  CD  ARG A 150     -41.374 -32.175 -27.498  1.00 18.04           C
ANISOU  967  CD  ARG A 150     2237   2223   2395    240    261    -12       C
ATOM    968  NE  ARG A 150     -42.331 -31.433 -26.684  1.00 18.66           N
ANISOU  968  NE  ARG A 150     2314   2318   2459    290    289    -27       N
ATOM    969  CZ  ARG A 150     -42.143 -30.202 -26.212  1.00 18.48           C
ANISOU  969  CZ  ARG A 150     2331   2250   2440    320    308    -64       C
ATOM    970  NH1 ARG A 150     -41.016 -29.534 -26.458  1.00 18.82           N
ANISOU  970  NH1 ARG A 150     2416   2225   2508    298    302    -89       N
ATOM    971  NH2 ARG A 150     -43.095 -29.628 -25.485  1.00 18.69           N
ANISOU  971  NH2 ARG A 150     2355   2298   2450    373    335    -77       N
ATOM    972  N   ALA A 151     -43.815 -35.876 -28.942  1.00 16.98           N
ANISOU  972  N   ALA A 151     1942   2239   2271    192    206     86       N
ATOM    973  CA  ALA A 151     -45.025 -36.683 -28.790  1.00 17.24           C
ANISOU  973  CA  ALA A 151     1912   2324   2316    187    205    108       C
ATOM    974  C   ALA A 151     -46.244 -35.823 -28.491  1.00 17.82           C
ANISOU  974  C   ALA A 151     1956   2429   2387    242    232    113       C
ATOM    975  O   ALA A 151     -47.345 -36.154 -28.903  1.00 17.65           O
ANISOU  975  O   ALA A 151     1875   2447   2383    251    223    131       O
ATOM    976  CB  ALA A 151     -44.837 -37.716 -27.699  1.00 17.06           C
ANISOU  976  CB  ALA A 151     1875   2319   2288    147    218    118       C
ATOM    977  N   LEU A 152     -46.049 -34.741 -27.743  1.00 17.96           N
ANISOU  977  N   LEU A 152     2011   2429   2385    279    264     94       N
ATOM    978  CA  LEU A 152     -47.077 -33.722 -27.577  1.00 18.37           C
ANISOU  978  CA  LEU A 152     2048   2499   2433    344    291     95       C
ATOM    979  C   LEU A 152     -46.479 -32.378 -27.942  1.00 18.66           C
ANISOU  979  C   LEU A 152     2147   2475   2467    381    297     73       C
ATOM    980  O   LEU A 152     -45.325 -32.106 -27.596  1.00 18.16           O
ANISOU  980  O   LEU A 152     2137   2365   2398    358    298     47       O
ATOM    981  CB  LEU A 152     -47.590 -33.653 -26.138  1.00 18.79           C
ANISOU  981  CB  LEU A 152     2087   2590   2465    364    333     91       C
ATOM    982  CG  LEU A 152     -48.596 -34.705 -25.664  1.00 19.47           C
ANISOU  982  CG  LEU A 152     2097   2741   2558    347    347    125       C
ATOM    983  CD1 LEU A 152     -48.940 -34.442 -24.201  1.00 19.51           C
ANISOU  983  CD1 LEU A 152     2104   2781   2529    380    397    122       C
ATOM    984  CD2 LEU A 152     -49.868 -34.716 -26.518  1.00 19.64           C
ANISOU  984  CD2 LEU A 152     2050   2802   2611    371    336    149       C
ATOM    985  N   PRO A 153     -47.274 -31.518 -28.603  1.00 19.10           N
ANISOU  985  N   PRO A 153     2195   2532   2531    440    303     84       N
ATOM    986  CA  PRO A 153     -46.777 -30.197 -28.951  1.00 19.18           C
ANISOU  986  CA  PRO A 153     2267   2476   2547    480    316     70       C
ATOM    987  C   PRO A 153     -46.474 -29.362 -27.713  1.00 19.49           C
ANISOU  987  C   PRO A 153     2348   2483   2574    499    350     31       C
ATOM    988  O   PRO A 153     -47.039 -29.607 -26.636  1.00 19.87           O
ANISOU  988  O   PRO A 153     2371   2576   2601    510    371     21       O
ATOM    989  CB  PRO A 153     -47.940 -29.580 -29.727  1.00 19.53           C
ANISOU  989  CB  PRO A 153     2282   2542   2596    550    320     96       C
ATOM    990  CG  PRO A 153     -49.150 -30.251 -29.182  1.00 20.29           C
ANISOU  990  CG  PRO A 153     2302   2719   2687    559    325    108       C
ATOM    991  CD  PRO A 153     -48.711 -31.658 -28.908  1.00 19.48           C
ANISOU  991  CD  PRO A 153     2174   2641   2586    479    303    109       C
ATOM    992  N   PRO A 154     -45.602 -28.363 -27.863  1.00 19.62           N
ANISOU  992  N   PRO A 154     2429   2421   2606    504    358      7       N
ATOM    993  CA  PRO A 154     -45.316 -27.486 -26.740  1.00 19.94           C
ANISOU  993  CA  PRO A 154     2513   2424   2639    524    384    -42       C
ATOM    994  C   PRO A 154     -46.497 -26.609 -26.349  1.00 20.60           C
ANISOU  994  C   PRO A 154     2591   2520   2714    607    418    -46       C
ATOM    995  O   PRO A 154     -47.359 -26.292 -27.181  1.00 21.21           O
ANISOU  995  O   PRO A 154     2646   2610   2803    657    423    -10       O
ATOM    996  CB  PRO A 154     -44.157 -26.628 -27.260  1.00 19.69           C
ANISOU  996  CB  PRO A 154     2543   2297   2642    506    381    -59       C
ATOM    997  CG  PRO A 154     -44.347 -26.600 -28.710  1.00 20.21           C
ANISOU  997  CG  PRO A 154     2599   2353   2727    519    373     -8       C
ATOM    998  CD  PRO A 154     -44.849 -27.968 -29.065  1.00 19.40           C
ANISOU  998  CD  PRO A 154     2435   2334   2604    494    346     25       C
ATOM    999  N   VAL A 155     -46.530 -26.225 -25.077  1.00 21.10           N
ANISOU  999  N   VAL A 155     2676   2586   2754    628    440    -92       N
ATOM   1000  CA  VAL A 155     -47.462 -25.216 -24.604  1.00 21.89           C
ANISOU 1000  CA  VAL A 155     2787   2684   2846    713    477   -109       C
ATOM   1001  C   VAL A 155     -47.077 -23.904 -25.282  1.00 23.02           C
ANISOU 1001  C   VAL A 155     2991   2724   3030    743    485   -121       C
ATOM   1002  O   VAL A 155     -45.910 -23.506 -25.253  1.00 22.46           O
ANISOU 1002  O   VAL A 155     2973   2577   2983    700    474   -155       O
ATOM   1003  CB  VAL A 155     -47.409 -25.073 -23.074  1.00 22.37           C
ANISOU 1003  CB  VAL A 155     2869   2766   2865    730    497   -165       C
ATOM   1004  CG1 VAL A 155     -48.322 -23.945 -22.603  1.00 22.29           C
ANISOU 1004  CG1 VAL A 155     2878   2745   2846    826    538   -189       C
ATOM   1005  CG2 VAL A 155     -47.790 -26.399 -22.404  1.00 21.25           C
ANISOU 1005  CG2 VAL A 155     2668   2724   2684    702    498   -139       C
ATOM   1006  N   ALA A 156     -48.054 -23.258 -25.913  1.00 24.18           N
ANISOU 1006  N   ALA A 156     3128   2871   3190    817    505    -88       N
ATOM   1007  CA  ALA A 156     -47.815 -22.028 -26.662  1.00 25.57           C
ANISOU 1007  CA  ALA A 156     3361   2948   3407    856    519    -83       C
ATOM   1008  C   ALA A 156     -47.219 -20.947 -25.761  1.00 27.11           C
ANISOU 1008  C   ALA A 156     3629   3053   3617    868    540   -155       C
ATOM   1009  O   ALA A 156     -47.498 -20.905 -24.563  1.00 27.20           O
ANISOU 1009  O   ALA A 156     3643   3095   3596    890    552   -205       O
ATOM   1010  CB  ALA A 156     -49.112 -21.534 -27.301  1.00 26.08           C
ANISOU 1010  CB  ALA A 156     3398   3041   3472    950    538    -37       C
ATOM   1011  N   ASP A 157     -46.400 -20.079 -26.348  1.00 28.99           N
ANISOU 1011  N   ASP A 157     3926   3180   3907    854    544   -160       N
ATOM   1012  CA  ASP A 157     -45.693 -19.041 -25.587  1.00 30.87           C
ANISOU 1012  CA  ASP A 157     4236   3317   4177    850    557   -234       C
ATOM   1013  C   ASP A 157     -46.628 -18.060 -24.884  1.00 32.34           C
ANISOU 1013  C   ASP A 157     4451   3485   4353    948    593   -271       C
ATOM   1014  O   ASP A 157     -46.329 -17.605 -23.778  1.00 33.40           O
ANISOU 1014  O   ASP A 157     4624   3587   4479    951    596   -353       O
ATOM   1015  CB  ASP A 157     -44.729 -18.264 -26.494  1.00 31.46           C
ANISOU 1015  CB  ASP A 157     4362   3270   4323    817    563   -219       C
ATOM   1016  CG  ASP A 157     -43.563 -19.111 -26.988  1.00 32.58           C
ANISOU 1016  CG  ASP A 157     4484   3417   4477    718    530   -200       C
ATOM   1017  OD1 ASP A 157     -43.291 -20.181 -26.405  1.00 34.49           O
ANISOU 1017  OD1 ASP A 157     4688   3738   4677    667    500   -220       O
ATOM   1018  OD2 ASP A 157     -42.906 -18.692 -27.965  1.00 36.23           O
ANISOU 1018  OD2 ASP A 157     4970   3804   4990    694    540   -162       O
ATOM   1019  N   ASP A 158     -47.759 -17.737 -25.505  1.00 33.15           N
ANISOU 1019  N   ASP A 158     4533   3611   4453   1032    618   -216       N
ATOM   1020  CA  ASP A 158     -48.662 -16.729 -24.940  1.00 34.44           C
ANISOU 1020  CA  ASP A 158     4724   3749   4611   1136    656   -246       C
ATOM   1021  C   ASP A 158     -49.726 -17.286 -23.982  1.00 34.11           C
ANISOU 1021  C   ASP A 158     4628   3829   4502   1187    668   -260       C
ATOM   1022  O   ASP A 158     -50.626 -16.556 -23.569  1.00 35.08           O
ANISOU 1022  O   ASP A 158     4762   3953   4614   1284    704   -275       O
ATOM   1023  CB  ASP A 158     -49.299 -15.879 -26.052  1.00 35.47           C
ANISOU 1023  CB  ASP A 158     4870   3829   4779   1217    683   -182       C
ATOM   1024  CG  ASP A 158     -50.207 -16.673 -26.968  1.00 36.85           C
ANISOU 1024  CG  ASP A 158     4965   4113   4925   1243    671    -96       C
ATOM   1025  OD1 ASP A 158     -50.881 -16.035 -27.803  1.00 40.46           O
ANISOU 1025  OD1 ASP A 158     5426   4551   5398   1324    690    -43       O
ATOM   1026  OD2 ASP A 158     -50.244 -17.920 -26.870  1.00 39.99           O
ANISOU 1026  OD2 ASP A 158     5295   4612   5285   1186    641    -83       O
ATOM   1027  N   CYS A 159     -49.614 -18.560 -23.607  1.00 32.79           N
ANISOU 1027  N   CYS A 159     4402   3762   4293   1124    643   -252       N
ATOM   1028  CA  CYS A 159     -50.538 -19.141 -22.634  1.00 32.57           C
ANISOU 1028  CA  CYS A 159     4321   3848   4205   1163    661   -259       C
ATOM   1029  C   CYS A 159     -50.301 -18.541 -21.242  1.00 33.06           C
ANISOU 1029  C   CYS A 159     4442   3885   4236   1194    680   -351       C
ATOM   1030  O   CYS A 159     -49.156 -18.251 -20.876  1.00 33.47           O
ANISOU 1030  O   CYS A 159     4553   3862   4303   1139    658   -413       O
ATOM   1031  CB  CYS A 159     -50.391 -20.665 -22.586  1.00 31.63           C
ANISOU 1031  CB  CYS A 159     4133   3829   4056   1083    633   -224       C
ATOM   1032  SG  CYS A 159     -50.850 -21.512 -24.121  1.00 30.30           S
ANISOU 1032  SG  CYS A 159     3888   3711   3913   1055    606   -128       S
ATOM   1033  N   PRO A 160     -51.377 -18.363 -20.460  1.00 33.09           N
ANISOU 1033  N   PRO A 160     4423   3956   4194   1283    720   -361       N
ATOM   1034  CA  PRO A 160     -51.265 -17.682 -19.168  1.00 33.65           C
ANISOU 1034  CA  PRO A 160     4555   4004   4227   1333    740   -453       C
ATOM   1035  C   PRO A 160     -50.457 -18.422 -18.093  1.00 32.95           C
ANISOU 1035  C   PRO A 160     4475   3961   4085   1269    716   -505       C
ATOM   1036  O   PRO A 160     -49.935 -17.778 -17.183  1.00 33.82           O
ANISOU 1036  O   PRO A 160     4653   4024   4174   1287    714   -597       O
ATOM   1037  CB  PRO A 160     -52.725 -17.511 -18.729  1.00 34.41           C
ANISOU 1037  CB  PRO A 160     4607   4185   4282   1447    793   -431       C
ATOM   1038  CG  PRO A 160     -53.488 -18.511 -19.494  1.00 33.87           C
ANISOU 1038  CG  PRO A 160     4437   4215   4218   1428    791   -332       C
ATOM   1039  CD  PRO A 160     -52.781 -18.664 -20.798  1.00 33.24           C
ANISOU 1039  CD  PRO A 160     4362   4070   4199   1352    748   -291       C
ATOM   1040  N   THR A 161     -50.366 -19.749 -18.186  1.00 31.58           N
ANISOU 1040  N   THR A 161     4234   3877   3888   1201    698   -450       N
ATOM   1041  CA  THR A 161     -49.597 -20.541 -17.216  1.00 30.77           C
ANISOU 1041  CA  THR A 161     4136   3822   3732   1144    675   -487       C
ATOM   1042  C   THR A 161     -48.650 -21.507 -17.928  1.00 29.69           C
ANISOU 1042  C   THR A 161     3975   3680   3627   1031    628   -447       C
ATOM   1043  O   THR A 161     -48.838 -21.804 -19.112  1.00 28.87           O
ANISOU 1043  O   THR A 161     3833   3567   3571   1001    618   -379       O
ATOM   1044  CB  THR A 161     -50.519 -21.330 -16.245  1.00 30.98           C
ANISOU 1044  CB  THR A 161     4107   3983   3680   1191    715   -460       C
ATOM   1045  OG1 THR A 161     -51.142 -22.421 -16.933  1.00 29.12           O
ANISOU 1045  OG1 THR A 161     3781   3824   3461   1155    719   -361       O
ATOM   1046  CG2 THR A 161     -51.589 -20.425 -15.637  1.00 31.87           C
ANISOU 1046  CG2 THR A 161     4233   4114   3761   1314    770   -487       C
ATOM   1047  N   PRO A 162     -47.620 -22.005 -17.214  1.00 29.33           N
ANISOU 1047  N   PRO A 162     3951   3644   3549    972    595   -491       N
ATOM   1048  CA  PRO A 162     -46.663 -22.915 -17.853  1.00 28.32           C
ANISOU 1048  CA  PRO A 162     3802   3509   3450    869    551   -457       C
ATOM   1049  C   PRO A 162     -47.311 -24.147 -18.489  1.00 27.59           C
ANISOU 1049  C   PRO A 162     3627   3498   3359    841    557   -360       C
ATOM   1050  O   PRO A 162     -46.907 -24.550 -19.580  1.00 26.61           O
ANISOU 1050  O   PRO A 162     3484   3344   3283    782    530   -317       O
ATOM   1051  CB  PRO A 162     -45.737 -23.313 -16.700  1.00 28.54           C
ANISOU 1051  CB  PRO A 162     3857   3566   3422    838    525   -518       C
ATOM   1052  CG  PRO A 162     -45.798 -22.158 -15.765  1.00 29.58           C
ANISOU 1052  CG  PRO A 162     4052   3663   3525    908    537   -612       C
ATOM   1053  CD  PRO A 162     -47.219 -21.682 -15.830  1.00 30.03           C
ANISOU 1053  CD  PRO A 162     4090   3745   3573   1002    593   -581       C
ATOM   1054  N   MET A 163     -48.318 -24.718 -17.830  1.00 27.64           N
ANISOU 1054  N   MET A 163     3584   3602   3315    885    594   -327       N
ATOM   1055  CA  MET A 163     -49.006 -25.906 -18.355  1.00 27.28           C
ANISOU 1055  CA  MET A 163     3455   3631   3279    856    600   -239       C
ATOM   1056  C   MET A 163     -50.188 -25.592 -19.273  1.00 27.16           C
ANISOU 1056  C   MET A 163     3391   3626   3303    902    621   -189       C
ATOM   1057  O   MET A 163     -50.814 -26.510 -19.804  1.00 26.97           O
ANISOU 1057  O   MET A 163     3292   3659   3295    876    621   -122       O
ATOM   1058  CB  MET A 163     -49.470 -26.808 -17.206  1.00 27.69           C
ANISOU 1058  CB  MET A 163     3469   3787   3266    869    632   -217       C
ATOM   1059  CG  MET A 163     -48.333 -27.414 -16.421  1.00 28.17           C
ANISOU 1059  CG  MET A 163     3563   3855   3284    819    605   -248       C
ATOM   1060  SD  MET A 163     -47.190 -28.258 -17.517  1.00 28.14           S
ANISOU 1060  SD  MET A 163     3552   3802   3337    707    544   -220       S
ATOM   1061  CE  MET A 163     -46.020 -28.933 -16.334  1.00 29.01           C
ANISOU 1061  CE  MET A 163     3697   3943   3383    673    521   -255       C
ATOM   1062  N   GLY A 164     -50.481 -24.310 -19.471  1.00 27.41           N
ANISOU 1062  N   GLY A 164     3463   3599   3352    970    637   -221       N
ATOM   1063  CA  GLY A 164     -51.561 -23.898 -20.357  1.00 27.73           C
ANISOU 1063  CA  GLY A 164     3462   3647   3427   1025    655   -175       C
ATOM   1064  C   GLY A 164     -52.411 -22.853 -19.677  1.00 28.64           C
ANISOU 1064  C   GLY A 164     3597   3768   3517   1135    704   -207       C
ATOM   1065  O   GLY A 164     -52.133 -21.664 -19.788  1.00 28.88           O
ANISOU 1065  O   GLY A 164     3697   3709   3567   1178    707   -253       O
ATOM   1066  N   VAL A 165     -53.435 -23.310 -18.962  1.00 29.25           N
ANISOU 1066  N   VAL A 165     3611   3946   3554   1181    745   -180       N
ATOM   1067  CA  VAL A 165     -54.309 -22.431 -18.177  1.00 30.71           C
ANISOU 1067  CA  VAL A 165     3808   4155   3706   1294    800   -209       C
ATOM   1068  C   VAL A 165     -54.388 -22.816 -16.694  1.00 31.65           C
ANISOU 1068  C   VAL A 165     3930   4349   3748   1317    836   -236       C
ATOM   1069  O   VAL A 165     -54.759 -21.984 -15.868  1.00 32.29           O
ANISOU 1069  O   VAL A 165     4050   4432   3787   1409    876   -285       O
ATOM   1070  CB  VAL A 165     -55.748 -22.387 -18.751  1.00 31.25           C
ANISOU 1070  CB  VAL A 165     3790   4288   3797   1360    830   -144       C
ATOM   1071  CG1 VAL A 165     -55.739 -21.868 -20.180  1.00 30.86           C
ANISOU 1071  CG1 VAL A 165     3745   4170   3810   1360    797   -119       C
ATOM   1072  CG2 VAL A 165     -56.415 -23.755 -18.664  1.00 30.99           C
ANISOU 1072  CG2 VAL A 165     3647   4370   3758   1316    841    -73       C
ATOM   1073  N   LYS A 166     -54.049 -24.062 -16.359  1.00 31.61           N
ANISOU 1073  N   LYS A 166     3887   4404   3721   1242    825   -203       N
ATOM   1074  CA  LYS A 166     -54.119 -24.537 -14.973  1.00 32.78           C
ANISOU 1074  CA  LYS A 166     4034   4631   3789   1266    863   -214       C
ATOM   1075  C   LYS A 166     -52.871 -24.158 -14.179  1.00 33.06           C
ANISOU 1075  C   LYS A 166     4168   4614   3778   1252    834   -303       C
ATOM   1076  O   LYS A 166     -51.814 -23.895 -14.748  1.00 32.35           O
ANISOU 1076  O   LYS A 166     4129   4433   3727   1191    779   -340       O
ATOM   1077  CB  LYS A 166     -54.285 -26.057 -14.925  1.00 32.45           C
ANISOU 1077  CB  LYS A 166     3911   4671   3746   1194    868   -134       C
ATOM   1078  CG  LYS A 166     -55.578 -26.589 -15.518  1.00 33.55           C
ANISOU 1078  CG  LYS A 166     3939   4880   3930   1202    898    -50       C
ATOM   1079  CD  LYS A 166     -55.562 -28.120 -15.525  1.00 34.42           C
ANISOU 1079  CD  LYS A 166     3979   5047   4053   1113    894     22       C
ATOM   1080  CE  LYS A 166     -56.819 -28.718 -16.145  1.00 35.13           C
ANISOU 1080  CE  LYS A 166     3948   5202   4199   1107    917    101       C
ATOM   1081  NZ  LYS A 166     -58.046 -28.350 -15.403  1.00 36.19           N
ANISOU 1081  NZ  LYS A 166     4030   5419   4302   1204    993    122       N
ATOM   1082  N   GLY A 167     -53.005 -24.150 -12.856  1.00 34.48           N
ANISOU 1082  N   GLY A 167     4370   4857   3872   1311    871   -336       N
ATOM   1083  CA  GLY A 167     -51.868 -23.949 -11.963  1.00 35.11           C
ANISOU 1083  CA  GLY A 167     4534   4911   3895   1301    839   -421       C
ATOM   1084  C   GLY A 167     -51.529 -22.493 -11.712  1.00 36.52           C
ANISOU 1084  C   GLY A 167     4804   5002   4070   1362    827   -530       C
ATOM   1085  O   GLY A 167     -52.232 -21.584 -12.160  1.00 36.88           O
ANISOU 1085  O   GLY A 167     4854   5005   4152   1424    852   -537       O
ATOM   1086  N   ASN A 168     -50.444 -22.285 -10.973  1.00 37.44           N
ANISOU 1086  N   ASN A 168     4992   5090   4143   1344    787   -617       N
ATOM   1087  CA  ASN A 168     -49.949 -20.952 -10.659  1.00 38.73           C
ANISOU 1087  CA  ASN A 168     5248   5160   4308   1387    764   -736       C
ATOM   1088  C   ASN A 168     -49.178 -20.365 -11.833  1.00 38.44           C
ANISOU 1088  C   ASN A 168     5239   4987   4379   1313    714   -754       C
ATOM   1089  O   ASN A 168     -48.862 -21.070 -12.794  1.00 37.22           O
ANISOU 1089  O   ASN A 168     5039   4821   4282   1227    689   -683       O
ATOM   1090  CB  ASN A 168     -49.048 -21.002  -9.418  1.00 39.51           C
ANISOU 1090  CB  ASN A 168     5406   5287   4321   1391    732   -827       C
ATOM   1091  CG  ASN A 168     -49.784 -21.481  -8.174  1.00 41.00           C
ANISOU 1091  CG  ASN A 168     5578   5610   4389   1479    788   -812       C
ATOM   1092  OD1 ASN A 168     -49.299 -22.351  -7.449  1.00 42.73           O
ANISOU 1092  OD1 ASN A 168     5792   5907   4537   1457    775   -801       O
ATOM   1093  ND2 ASN A 168     -50.958 -20.918  -7.925  1.00 42.14           N
ANISOU 1093  ND2 ASN A 168     5715   5787   4510   1585    855   -805       N
ATOM   1094  N   LYS A 169     -48.874 -19.072 -11.743  1.00 39.49           N
ANISOU 1094  N   LYS A 169     5450   5017   4540   1349    702   -850       N
ATOM   1095  CA  LYS A 169     -48.154 -18.349 -12.799  1.00 39.42           C
ANISOU 1095  CA  LYS A 169     5475   4866   4637   1289    664   -869       C
ATOM   1096  C   LYS A 169     -46.767 -18.930 -13.074  1.00 38.50           C
ANISOU 1096  C   LYS A 169     5360   4719   4551   1168    599   -879       C
ATOM   1097  O   LYS A 169     -46.289 -18.892 -14.207  1.00 37.73           O
ANISOU 1097  O   LYS A 169     5252   4545   4539   1098    577   -840       O
ATOM   1098  CB  LYS A 169     -48.022 -16.867 -12.425  1.00 41.00           C
ANISOU 1098  CB  LYS A 169     5764   4957   4857   1350    664   -982       C
ATOM   1099  CG  LYS A 169     -47.448 -15.975 -13.529  1.00 41.99           C
ANISOU 1099  CG  LYS A 169     5927   4926   5101   1302    643   -992       C
ATOM   1100  CD  LYS A 169     -47.282 -14.534 -13.051  1.00 45.04           C
ANISOU 1100  CD  LYS A 169     6406   5196   5513   1359    643  -1111       C
ATOM   1101  CE  LYS A 169     -48.616 -13.804 -12.971  1.00 46.65           C
ANISOU 1101  CE  LYS A 169     6621   5403   5700   1490    708  -1100       C
ATOM   1102  NZ  LYS A 169     -48.486 -12.481 -12.311  1.00 49.13           N
ANISOU 1102  NZ  LYS A 169     7031   5612   6025   1556    710  -1228       N
ATOM   1103  N   GLU A 170     -46.119 -19.442 -12.032  1.00 38.34           N
ANISOU 1103  N   GLU A 170     5352   4759   4456   1151    569   -931       N
ATOM   1104  CA  GLU A 170     -44.823 -20.099 -12.174  1.00 37.60           C
ANISOU 1104  CA  GLU A 170     5251   4655   4380   1045    508   -938       C
ATOM   1105  C   GLU A 170     -44.875 -21.471 -11.527  1.00 36.15           C
ANISOU 1105  C   GLU A 170     5019   4606   4110   1035    511   -884       C
ATOM   1106  O   GLU A 170     -45.584 -21.676 -10.538  1.00 36.82           O
ANISOU 1106  O   GLU A 170     5101   4785   4102   1114    548   -888       O
ATOM   1107  CB  GLU A 170     -43.717 -19.265 -11.518  1.00 38.84           C
ANISOU 1107  CB  GLU A 170     5480   4738   4541   1028    454  -1073       C
ATOM   1108  CG  GLU A 170     -43.535 -17.864 -12.113  1.00 41.45           C
ANISOU 1108  CG  GLU A 170     5865   4915   4970   1028    451  -1133       C
ATOM   1109  CD  GLU A 170     -43.055 -17.874 -13.562  1.00 42.41           C
ANISOU 1109  CD  GLU A 170     5962   4947   5205    941    441  -1063       C
ATOM   1110  OE1 GLU A 170     -42.408 -18.854 -13.992  1.00 44.59           O
ANISOU 1110  OE1 GLU A 170     6192   5260   5490    860    412  -1006       O
ATOM   1111  OE2 GLU A 170     -43.326 -16.887 -14.279  1.00 45.23           O
ANISOU 1111  OE2 GLU A 170     6348   5196   5641    960    464  -1062       O
ATOM   1112  N   LEU A 171     -44.124 -22.411 -12.092  1.00 34.10           N
ANISOU 1112  N   LEU A 171     4722   4355   3881    942    476   -830       N
ATOM   1113  CA  LEU A 171     -43.987 -23.736 -11.501  1.00 32.90           C
ANISOU 1113  CA  LEU A 171     4530   4315   3656    924    472   -780       C
ATOM   1114  C   LEU A 171     -43.139 -23.640 -10.233  1.00 33.04           C
ANISOU 1114  C   LEU A 171     4595   4367   3592    940    432   -877       C
ATOM   1115  O   LEU A 171     -42.399 -22.667 -10.052  1.00 33.10           O
ANISOU 1115  O   LEU A 171     4657   4295   3624    932    390   -983       O
ATOM   1116  CB  LEU A 171     -43.363 -24.711 -12.505  1.00 31.64           C
ANISOU 1116  CB  LEU A 171     4323   4143   3556    823    443   -703       C
ATOM   1117  CG  LEU A 171     -44.319 -25.156 -13.613  1.00 30.75           C
ANISOU 1117  CG  LEU A 171     4152   4035   3498    814    482   -596       C
ATOM   1118  CD1 LEU A 171     -43.566 -25.734 -14.814  1.00 29.86           C
ANISOU 1118  CD1 LEU A 171     4011   3874   3460    718    445   -547       C
ATOM   1119  CD2 LEU A 171     -45.342 -26.153 -13.075  1.00 30.33           C
ANISOU 1119  CD2 LEU A 171     4045   4098   3382    853    531   -520       C
ATOM   1120  N   PRO A 172     -43.252 -24.639  -9.339  1.00 32.58           N
ANISOU 1120  N   PRO A 172     4516   4425   3438    965    444   -842       N
ATOM   1121  CA  PRO A 172     -42.445 -24.600  -8.120  1.00 32.76           C
ANISOU 1121  CA  PRO A 172     4582   4493   3370    990    402   -932       C
ATOM   1122  C   PRO A 172     -40.943 -24.622  -8.397  1.00 31.91           C
ANISOU 1122  C   PRO A 172     4486   4328   3310    899    319   -986       C
ATOM   1123  O   PRO A 172     -40.504 -25.134  -9.432  1.00 30.14           O
ANISOU 1123  O   PRO A 172     4223   4061   3166    815    303   -923       O
ATOM   1124  CB  PRO A 172     -42.871 -25.867  -7.362  1.00 32.83           C
ANISOU 1124  CB  PRO A 172     4556   4638   3281   1024    439   -847       C
ATOM   1125  CG  PRO A 172     -43.579 -26.713  -8.352  1.00 32.40           C
ANISOU 1125  CG  PRO A 172     4433   4589   3290    981    482   -716       C
ATOM   1126  CD  PRO A 172     -44.183 -25.781  -9.346  1.00 32.24           C
ANISOU 1126  CD  PRO A 172     4410   4477   3362    981    501   -721       C
ATOM   1127  N   ASP A 173     -40.181 -24.045  -7.471  1.00 32.28           N
ANISOU 1127  N   ASP A 173     4584   4376   3305    921    267  -1106       N
ATOM   1128  CA  ASP A 173     -38.718 -24.048  -7.513  1.00 32.27           C
ANISOU 1128  CA  ASP A 173     4588   4336   3337    844    184  -1172       C
ATOM   1129  C   ASP A 173     -38.201 -25.461  -7.799  1.00 30.79           C
ANISOU 1129  C   ASP A 173     4347   4211   3143    785    171  -1073       C
ATOM   1130  O   ASP A 173     -38.482 -26.388  -7.042  1.00 30.24           O
ANISOU 1130  O   ASP A 173     4264   4253   2974    830    191  -1022       O
ATOM   1131  CB  ASP A 173     -38.184 -23.542  -6.165  1.00 34.03           C
ANISOU 1131  CB  ASP A 173     4863   4602   3464    899    133  -1305       C
ATOM   1132  CG  ASP A 173     -36.691 -23.266  -6.175  1.00 35.91           C
ANISOU 1132  CG  ASP A 173     5106   4788   3749    821     40  -1398       C
ATOM   1133  OD1 ASP A 173     -36.246 -22.509  -5.287  1.00 41.37           O
ANISOU 1133  OD1 ASP A 173     5845   5478   4396    855    -10  -1533       O
ATOM   1134  OD2 ASP A 173     -35.965 -23.792  -7.038  1.00 39.15           O
ANISOU 1134  OD2 ASP A 173     5473   5164   4239    730     17  -1343       O
ATOM   1135  N   SER A 174     -37.452 -25.623  -8.892  1.00 29.61           N
ANISOU 1135  N   SER A 174     4167   3987   3098    690    142  -1043       N
ATOM   1136  CA  SER A 174     -36.969 -26.945  -9.299  1.00 28.51           C
ANISOU 1136  CA  SER A 174     3977   3893   2963    634    131   -949       C
ATOM   1137  C   SER A 174     -35.986 -27.545  -8.285  1.00 28.97           C
ANISOU 1137  C   SER A 174     4039   4033   2936    640     74   -990       C
ATOM   1138  O   SER A 174     -35.954 -28.761  -8.108  1.00 28.13           O
ANISOU 1138  O   SER A 174     3903   4004   2781    641     85   -906       O
ATOM   1139  CB  SER A 174     -36.352 -26.913 -10.710  1.00 27.68           C
ANISOU 1139  CB  SER A 174     3843   3690   2985    538    114   -915       C
ATOM   1140  OG  SER A 174     -35.248 -26.028 -10.788  1.00 28.06           O
ANISOU 1140  OG  SER A 174     3910   3660   3090    491     55  -1015       O
ATOM   1141  N   LYS A 175     -35.203 -26.694  -7.620  1.00 30.08           N
ANISOU 1141  N   LYS A 175     4216   4155   3060    646     13  -1119       N
ATOM   1142  CA  LYS A 175     -34.306 -27.143  -6.546  1.00 30.92           C
ANISOU 1142  CA  LYS A 175     4328   4350   3072    667    -49  -1173       C
ATOM   1143  C   LYS A 175     -35.108 -27.735  -5.389  1.00 31.24           C
ANISOU 1143  C   LYS A 175     4387   4517   2967    770     -8  -1139       C
ATOM   1144  O   LYS A 175     -34.708 -28.737  -4.797  1.00 31.18           O
ANISOU 1144  O   LYS A 175     4365   4604   2879    788    -24  -1097       O
ATOM   1145  CB  LYS A 175     -33.429 -25.988  -6.038  1.00 32.32           C
ANISOU 1145  CB  LYS A 175     4540   4480   3262    657   -125  -1334       C
ATOM   1146  CG  LYS A 175     -32.428 -26.382  -4.936  1.00 34.22           C
ANISOU 1146  CG  LYS A 175     4782   4816   3404    679   -203  -1404       C
ATOM   1147  CD  LYS A 175     -31.689 -25.173  -4.372  1.00 37.07           C
ANISOU 1147  CD  LYS A 175     5177   5131   3777    674   -282  -1576       C
ATOM   1148  CE  LYS A 175     -30.892 -25.547  -3.118  1.00 38.93           C
ANISOU 1148  CE  LYS A 175     5419   5484   3887    721   -359  -1652       C
ATOM   1149  NZ  LYS A 175     -30.117 -24.408  -2.537  1.00 40.77           N
ANISOU 1149  NZ  LYS A 175     5680   5677   4133    712   -448  -1833       N
ATOM   1150  N   GLU A 176     -36.240 -27.116  -5.072  1.00 31.64           N
ANISOU 1150  N   GLU A 176     4469   4569   2983    842     49  -1152       N
ATOM   1151  CA  GLU A 176     -37.094 -27.598  -3.991  1.00 32.35           C
ANISOU 1151  CA  GLU A 176     4576   4780   2937    946    101  -1115       C
ATOM   1152  C   GLU A 176     -37.717 -28.951  -4.336  1.00 30.75           C
ANISOU 1152  C   GLU A 176     4323   4633   2729    937    167   -952       C
ATOM   1153  O   GLU A 176     -37.747 -29.850  -3.501  1.00 30.93           O
ANISOU 1153  O   GLU A 176     4343   4763   2647    987    182   -900       O
ATOM   1154  CB  GLU A 176     -38.177 -26.571  -3.657  1.00 33.52           C
ANISOU 1154  CB  GLU A 176     4763   4911   3060   1025    152  -1166       C
ATOM   1155  CG  GLU A 176     -38.826 -26.793  -2.300  1.00 36.82           C
ANISOU 1155  CG  GLU A 176     5212   5458   3320   1146    191  -1169       C
ATOM   1156  CD  GLU A 176     -39.408 -25.532  -1.694  1.00 39.99           C
ANISOU 1156  CD  GLU A 176     5673   5844   3679   1232    204  -1282       C
ATOM   1157  OE1 GLU A 176     -39.801 -25.577  -0.513  1.00 43.69           O
ANISOU 1157  OE1 GLU A 176     6175   6418   4008   1338    227  -1307       O
ATOM   1158  OE2 GLU A 176     -39.479 -24.495  -2.389  1.00 42.91           O
ANISOU 1158  OE2 GLU A 176     6058   6094   4151   1199    195  -1343       O
ATOM   1159  N   VAL A 177     -38.209 -29.096  -5.563  1.00 29.17           N
ANISOU 1159  N   VAL A 177     4084   4359   2640    876    205   -873       N
ATOM   1160  CA  VAL A 177     -38.739 -30.384  -6.025  1.00 28.09           C
ANISOU 1160  CA  VAL A 177     3896   4260   2519    852    258   -727       C
ATOM   1161  C   VAL A 177     -37.651 -31.458  -5.933  1.00 27.70           C
ANISOU 1161  C   VAL A 177     3827   4246   2452    809    211   -691       C
ATOM   1162  O   VAL A 177     -37.872 -32.543  -5.387  1.00 27.73           O
ANISOU 1162  O   VAL A 177     3817   4334   2386    840    243   -605       O
ATOM   1163  CB  VAL A 177     -39.253 -30.301  -7.474  1.00 27.30           C
ANISOU 1163  CB  VAL A 177     3757   4068   2548    785    286   -667       C
ATOM   1164  CG1 VAL A 177     -39.710 -31.676  -7.962  1.00 26.11           C
ANISOU 1164  CG1 VAL A 177     3552   3950   2418    753    330   -529       C
ATOM   1165  CG2 VAL A 177     -40.381 -29.276  -7.582  1.00 27.73           C
ANISOU 1165  CG2 VAL A 177     3826   4091   2619    837    336   -693       C
ATOM   1166  N   LEU A 178     -36.475 -31.126  -6.457  1.00 27.09           N
ANISOU 1166  N   LEU A 178     3749   4103   2440    740    137   -755       N
ATOM   1167  CA  LEU A 178     -35.301 -31.999  -6.420  1.00 26.85           C
ANISOU 1167  CA  LEU A 178     3700   4101   2403    699     82   -737       C
ATOM   1168  C   LEU A 178     -34.995 -32.472  -4.997  1.00 27.68           C
ANISOU 1168  C   LEU A 178     3828   4323   2364    777     64   -754       C
ATOM   1169  O   LEU A 178     -34.959 -33.672  -4.727  1.00 27.22           O
ANISOU 1169  O   LEU A 178     3752   4331   2259    791     84   -659       O
ATOM   1170  CB  LEU A 178     -34.093 -31.248  -6.993  1.00 26.96           C
ANISOU 1170  CB  LEU A 178     3712   4031   2499    627      4   -832       C
ATOM   1171  CG  LEU A 178     -32.724 -31.937  -6.984  1.00 27.64           C
ANISOU 1171  CG  LEU A 178     3774   4140   2588    583    -64   -836       C
ATOM   1172  CD1 LEU A 178     -32.667 -33.040  -8.022  1.00 26.23           C
ANISOU 1172  CD1 LEU A 178     3551   3937   2478    524    -37   -717       C
ATOM   1173  CD2 LEU A 178     -31.610 -30.914  -7.216  1.00 29.80           C
ANISOU 1173  CD2 LEU A 178     4050   4345   2929    529   -140   -957       C
ATOM   1174  N   GLU A 179     -34.792 -31.525  -4.089  1.00 28.68           N
ANISOU 1174  N   GLU A 179     3999   4476   2420    833     26   -874       N
ATOM   1175  CA  GLU A 179     -34.378 -31.858  -2.725  1.00 29.85           C
ANISOU 1175  CA  GLU A 179     4175   4743   2424    914     -5   -908       C
ATOM   1176  C   GLU A 179     -35.457 -32.589  -1.928  1.00 30.31           C
ANISOU 1176  C   GLU A 179     4243   4902   2371   1005     81   -809       C
ATOM   1177  O   GLU A 179     -35.145 -33.510  -1.179  1.00 30.71           O
ANISOU 1177  O   GLU A 179     4295   5047   2327   1050     78   -757       O
ATOM   1178  CB  GLU A 179     -33.920 -30.601  -1.979  1.00 31.16           C
ANISOU 1178  CB  GLU A 179     4387   4908   2544    952    -72  -1075       C
ATOM   1179  CG  GLU A 179     -32.600 -30.052  -2.504  1.00 31.84           C
ANISOU 1179  CG  GLU A 179     4458   4918   2723    864   -168  -1173       C
ATOM   1180  CD  GLU A 179     -31.975 -29.023  -1.587  1.00 34.92           C
ANISOU 1180  CD  GLU A 179     4888   5325   3055    901   -249  -1343       C
ATOM   1181  OE1 GLU A 179     -32.717 -28.306  -0.880  1.00 35.05           O
ANISOU 1181  OE1 GLU A 179     4955   5364   3000    980   -224  -1406       O
ATOM   1182  OE2 GLU A 179     -30.728 -28.940  -1.573  1.00 37.19           O
ANISOU 1182  OE2 GLU A 179     5155   5605   3369    852   -339  -1415       O
ATOM   1183  N   LYS A 180     -36.715 -32.191  -2.098  1.00 30.22           N
ANISOU 1183  N   LYS A 180     4236   4871   2376   1034    159   -779       N
ATOM   1184  CA  LYS A 180     -37.805 -32.758  -1.301  1.00 31.05           C
ANISOU 1184  CA  LYS A 180     4345   5073   2379   1123    248   -690       C
ATOM   1185  C   LYS A 180     -38.189 -34.189  -1.700  1.00 30.12           C
ANISOU 1185  C   LYS A 180     4179   4975   2291   1091    309   -525       C
ATOM   1186  O   LYS A 180     -38.462 -35.010  -0.821  1.00 30.86           O
ANISOU 1186  O   LYS A 180     4277   5166   2280   1159    354   -447       O
ATOM   1187  CB  LYS A 180     -39.040 -31.848  -1.329  1.00 31.47           C
ANISOU 1187  CB  LYS A 180     4412   5104   2442   1169    313   -713       C
ATOM   1188  CG  LYS A 180     -38.865 -30.559  -0.525  1.00 33.83           C
ANISOU 1188  CG  LYS A 180     4773   5414   2669   1239    270   -869       C
ATOM   1189  CD  LYS A 180     -40.150 -29.754  -0.465  1.00 35.62           C
ANISOU 1189  CD  LYS A 180     5013   5629   2892   1301    345   -880       C
ATOM   1190  CE  LYS A 180     -40.043 -28.577   0.501  1.00 37.82           C
ANISOU 1190  CE  LYS A 180     5361   5930   3079   1390    310  -1034       C
ATOM   1191  NZ  LYS A 180     -40.164 -28.986   1.918  1.00 40.79           N
ANISOU 1191  NZ  LYS A 180     5771   6451   3277   1506    331  -1032       N
ATOM   1192  N   VAL A 181     -38.205 -34.500  -2.997  1.00 29.06           N
ANISOU 1192  N   VAL A 181     4000   4748   2293    993    312   -470       N
ATOM   1193  CA  VAL A 181     -38.706 -35.810  -3.443  1.00 28.37           C
ANISOU 1193  CA  VAL A 181     3866   4667   2246    959    373   -321       C
ATOM   1194  C   VAL A 181     -37.816 -36.635  -4.389  1.00 27.51           C
ANISOU 1194  C   VAL A 181     3726   4498   2228    865    329   -277       C
ATOM   1195  O   VAL A 181     -38.141 -37.788  -4.660  1.00 26.96           O
ANISOU 1195  O   VAL A 181     3625   4435   2186    842    373   -160       O
ATOM   1196  CB  VAL A 181     -40.118 -35.675  -4.076  1.00 28.04           C
ANISOU 1196  CB  VAL A 181     3790   4591   2274    949    456   -258       C
ATOM   1197  CG1 VAL A 181     -41.070 -35.001  -3.095  1.00 29.17           C
ANISOU 1197  CG1 VAL A 181     3958   4804   2321   1052    513   -284       C
ATOM   1198  CG2 VAL A 181     -40.057 -34.910  -5.395  1.00 27.22           C
ANISOU 1198  CG2 VAL A 181     3669   4372   2301    870    422   -308       C
ATOM   1199  N   LEU A 182     -36.709 -36.075  -4.881  1.00 27.23           N
ANISOU 1199  N   LEU A 182     3698   4405   2242    813    244   -369       N
ATOM   1200  CA  LEU A 182     -35.854 -36.791  -5.833  1.00 26.42           C
ANISOU 1200  CA  LEU A 182     3565   4247   2228    728    205   -331       C
ATOM   1201  C   LEU A 182     -34.522 -37.258  -5.254  1.00 26.95           C
ANISOU 1201  C   LEU A 182     3642   4361   2236    739    136   -358       C
ATOM   1202  O   LEU A 182     -34.066 -38.356  -5.577  1.00 26.41           O
ANISOU 1202  O   LEU A 182     3552   4292   2192    708    133   -280       O
ATOM   1203  CB  LEU A 182     -35.581 -35.941  -7.079  1.00 25.55           C
ANISOU 1203  CB  LEU A 182     3441   4026   2240    649    170   -392       C
ATOM   1204  CG  LEU A 182     -36.797 -35.472  -7.879  1.00 25.61           C
ANISOU 1204  CG  LEU A 182     3433   3977   2321    632    229   -364       C
ATOM   1205  CD1 LEU A 182     -36.326 -34.828  -9.174  1.00 24.88           C
ANISOU 1205  CD1 LEU A 182     3328   3779   2347    554    191   -406       C
ATOM   1206  CD2 LEU A 182     -37.752 -36.621  -8.169  1.00 26.10           C
ANISOU 1206  CD2 LEU A 182     3458   4058   2402    625    299   -233       C
ATOM   1207  N   LEU A 183     -33.902 -36.434  -4.413  1.00 27.79           N
ANISOU 1207  N   LEU A 183     3782   4509   2268    783     77   -472       N
ATOM   1208  CA  LEU A 183     -32.555 -36.721  -3.931  1.00 28.38           C
ANISOU 1208  CA  LEU A 183     3859   4628   2296    789     -3   -517       C
ATOM   1209  C   LEU A 183     -32.506 -37.913  -2.978  1.00 28.71           C
ANISOU 1209  C   LEU A 183     3908   4774   2224    860     19   -427       C
ATOM   1210  O   LEU A 183     -33.373 -38.090  -2.121  1.00 29.20           O
ANISOU 1210  O   LEU A 183     3995   4907   2191    940     80   -383       O
ATOM   1211  CB  LEU A 183     -31.921 -35.491  -3.271  1.00 29.55           C
ANISOU 1211  CB  LEU A 183     4037   4793   2398    816    -79   -673       C
ATOM   1212  CG  LEU A 183     -31.477 -34.367  -4.220  1.00 29.77           C
ANISOU 1212  CG  LEU A 183     4053   4709   2550    732   -124   -770       C
ATOM   1213  CD1 LEU A 183     -30.670 -33.328  -3.433  1.00 32.60           C
ANISOU 1213  CD1 LEU A 183     4438   5089   2861    756   -210   -926       C
ATOM   1214  CD2 LEU A 183     -30.671 -34.882  -5.407  1.00 30.39           C
ANISOU 1214  CD2 LEU A 183     4085   4716   2745    637   -149   -727       C
ATOM   1215  N   ARG A 184     -31.468 -38.723  -3.155  1.00 28.69           N
ANISOU 1215  N   ARG A 184     3886   4780   2235    835    -27   -396       N
ATOM   1216  CA  ARG A 184     -31.263 -39.929  -2.366  1.00 29.14           C
ANISOU 1216  CA  ARG A 184     3949   4924   2196    899    -10   -303       C
ATOM   1217  C   ARG A 184     -30.921 -39.592  -0.920  1.00 30.69           C
ANISOU 1217  C   ARG A 184     4186   5240   2236   1003    -50   -371       C
ATOM   1218  O   ARG A 184     -30.022 -38.795  -0.654  1.00 31.03           O
ANISOU 1218  O   ARG A 184     4233   5298   2258   1003   -140   -498       O
ATOM   1219  CB  ARG A 184     -30.142 -40.760  -2.995  1.00 28.63           C
ANISOU 1219  CB  ARG A 184     3853   4831   2193    846    -58   -268       C
ATOM   1220  CG  ARG A 184     -29.732 -42.006  -2.224  1.00 28.82           C
ANISOU 1220  CG  ARG A 184     3885   4939   2125    914    -52   -175       C
ATOM   1221  CD  ARG A 184     -28.701 -42.778  -3.030  1.00 27.87           C
ANISOU 1221  CD  ARG A 184     3729   4773   2085    856    -93   -141       C
ATOM   1222  NE  ARG A 184     -29.276 -43.337  -4.251  1.00 25.57           N
ANISOU 1222  NE  ARG A 184     3414   4379   1920    778    -34    -58       N
ATOM   1223  CZ  ARG A 184     -28.570 -43.817  -5.275  1.00 23.96           C
ANISOU 1223  CZ  ARG A 184     3179   4108   1815    711    -60    -39       C
ATOM   1224  NH1 ARG A 184     -27.243 -43.804  -5.255  1.00 24.63           N
ANISOU 1224  NH1 ARG A 184     3246   4216   1896    708   -140    -94       N
ATOM   1225  NH2 ARG A 184     -29.198 -44.307  -6.336  1.00 23.00           N
ANISOU 1225  NH2 ARG A 184     3042   3901   1798    648     -6     30       N
ATOM   1226  N   ARG A 185     -31.658 -40.191   0.010  1.00 31.56           N
ANISOU 1226  N   ARG A 185     4322   5435   2233   1092     18   -285       N
ATOM   1227  CA  ARG A 185     -31.266 -40.190   1.409  1.00 33.31           C
ANISOU 1227  CA  ARG A 185     4582   5786   2288   1205    -15   -321       C
ATOM   1228  C   ARG A 185     -30.397 -41.437   1.561  1.00 34.02           C
ANISOU 1228  C   ARG A 185     4659   5917   2350   1221    -38   -233       C
ATOM   1229  O   ARG A 185     -29.168 -41.355   1.474  1.00 35.23           O
ANISOU 1229  O   ARG A 185     4796   6077   2512   1201   -134   -304       O
ATOM   1230  CB  ARG A 185     -32.489 -40.222   2.333  1.00 33.83           C
ANISOU 1230  CB  ARG A 185     4684   5927   2242   1302     79   -263       C
ATOM   1231  CG  ARG A 185     -33.139 -38.860   2.592  1.00 34.01           C
ANISOU 1231  CG  ARG A 185     4734   5947   2242   1327     81   -380       C
ATOM   1232  CD  ARG A 185     -33.771 -38.234   1.352  1.00 32.59           C
ANISOU 1232  CD  ARG A 185     4525   5638   2221   1226    110   -397       C
ATOM   1233  NE  ARG A 185     -34.526 -37.023   1.697  1.00 32.33           N
ANISOU 1233  NE  ARG A 185     4522   5608   2155   1268    128   -491       N
ATOM   1234  CZ  ARG A 185     -34.958 -36.107   0.829  1.00 31.75           C
ANISOU 1234  CZ  ARG A 185     4437   5433   2194   1204    133   -549       C
ATOM   1235  NH1 ARG A 185     -34.729 -36.228  -0.475  1.00 30.89           N
ANISOU 1235  NH1 ARG A 185     4286   5213   2236   1092    121   -525       N
ATOM   1236  NH2 ARG A 185     -35.619 -35.045   1.275  1.00 32.41           N
ANISOU 1236  NH2 ARG A 185     4554   5526   2233   1258    150   -633       N
ATOM   1237  N   GLU A 186     -31.040 -42.591   1.717  1.00 34.08           N
ANISOU 1237  N   GLU A 186     4670   5942   2337   1252     53    -77       N
ATOM   1238  CA  GLU A 186     -30.353 -43.873   1.739  1.00 34.24           C
ANISOU 1238  CA  GLU A 186     4680   5980   2349   1264     48     27       C
ATOM   1239  C   GLU A 186     -30.530 -44.564   0.388  1.00 32.31           C
ANISOU 1239  C   GLU A 186     4395   5611   2270   1155     86    109       C
ATOM   1240  O   GLU A 186     -31.599 -44.472  -0.221  1.00 31.12           O
ANISOU 1240  O   GLU A 186     4232   5392   2201   1105    159    150       O
ATOM   1241  CB  GLU A 186     -30.940 -44.741   2.845  1.00 35.83           C
ANISOU 1241  CB  GLU A 186     4916   6279   2419   1374    129    153       C
ATOM   1242  CG  GLU A 186     -30.026 -45.841   3.328  1.00 38.91           C
ANISOU 1242  CG  GLU A 186     5313   6729   2742   1432    102    230       C
ATOM   1243  CD  GLU A 186     -30.550 -46.501   4.586  1.00 43.02           C
ANISOU 1243  CD  GLU A 186     5877   7361   3109   1559    177    341       C
ATOM   1244  OE1 GLU A 186     -31.787 -46.555   4.752  1.00 45.90           O
ANISOU 1244  OE1 GLU A 186     6251   7720   3469   1572    283    415       O
ATOM   1245  OE2 GLU A 186     -29.734 -46.957   5.414  1.00 47.16           O
ANISOU 1245  OE2 GLU A 186     6423   7982   3513   1650    132    356       O
ATOM   1246  N   PHE A 187     -29.487 -45.252  -0.073  1.00 31.27           N
ANISOU 1246  N   PHE A 187     4242   5455   2186   1123     35    130       N
ATOM   1247  CA  PHE A 187     -29.542 -45.984  -1.339  1.00 29.94           C
ANISOU 1247  CA  PHE A 187     4040   5172   2164   1029     64    203       C
ATOM   1248  C   PHE A 187     -30.688 -46.989  -1.324  1.00 29.83           C
ANISOU 1248  C   PHE A 187     4032   5134   2168   1037    179    355       C
ATOM   1249  O   PHE A 187     -30.810 -47.777  -0.387  1.00 30.43           O
ANISOU 1249  O   PHE A 187     4135   5282   2147   1121    222    448       O
ATOM   1250  CB  PHE A 187     -28.215 -46.703  -1.600  1.00 29.86           C
ANISOU 1250  CB  PHE A 187     4012   5161   2174   1022     -2    214       C
ATOM   1251  CG  PHE A 187     -28.221 -47.590  -2.824  1.00 28.47           C
ANISOU 1251  CG  PHE A 187     3808   4874   2134    940     30    294       C
ATOM   1252  CD1 PHE A 187     -28.180 -48.977  -2.697  1.00 29.09           C
ANISOU 1252  CD1 PHE A 187     3896   4949   2208    971     75    426       C
ATOM   1253  CD2 PHE A 187     -28.247 -47.041  -4.097  1.00 26.92           C
ANISOU 1253  CD2 PHE A 187     3581   4577   2069    838     13    236       C
ATOM   1254  CE1 PHE A 187     -28.170 -49.798  -3.824  1.00 27.92           C
ANISOU 1254  CE1 PHE A 187     3728   4696   2186    898    100    489       C
ATOM   1255  CE2 PHE A 187     -28.235 -47.852  -5.226  1.00 26.81           C
ANISOU 1255  CE2 PHE A 187     3545   4468   2172    769     38    301       C
ATOM   1256  CZ  PHE A 187     -28.198 -49.237  -5.087  1.00 26.61           C
ANISOU 1256  CZ  PHE A 187     3530   4438   2143    799     79    423       C
ATOM   1257  N   ILE A 188     -31.529 -46.934  -2.356  1.00 28.77           N
ANISOU 1257  N   ILE A 188     3873   4901   2158    951    228    377       N
ATOM   1258  CA  ILE A 188     -32.644 -47.862  -2.515  1.00 28.76           C
ANISOU 1258  CA  ILE A 188     3865   4861   2203    937    332    512       C
ATOM   1259  C   ILE A 188     -32.335 -48.792  -3.686  1.00 27.86           C
ANISOU 1259  C   ILE A 188     3724   4641   2219    855    330    568       C
ATOM   1260  O   ILE A 188     -32.368 -48.364  -4.837  1.00 26.51           O
ANISOU 1260  O   ILE A 188     3526   4389   2159    769    305    512       O
ATOM   1261  CB  ILE A 188     -33.976 -47.118  -2.785  1.00 28.65           C
ANISOU 1261  CB  ILE A 188     3836   4819   2229    907    391    497       C
ATOM   1262  CG1 ILE A 188     -34.298 -46.149  -1.639  1.00 30.05           C
ANISOU 1262  CG1 ILE A 188     4044   5099   2276    995    395    433       C
ATOM   1263  CG2 ILE A 188     -35.115 -48.115  -2.979  1.00 28.95           C
ANISOU 1263  CG2 ILE A 188     3855   4817   2328    884    496    635       C
ATOM   1264  CD1 ILE A 188     -35.568 -45.320  -1.863  1.00 30.15           C
ANISOU 1264  CD1 ILE A 188     4042   5091   2323    976    451    409       C
ATOM   1265  N   PRO A 189     -32.031 -50.073  -3.403  1.00 28.20           N
ANISOU 1265  N   PRO A 189     3779   4687   2249    885    357    677       N
ATOM   1266  CA  PRO A 189     -31.660 -50.975  -4.494  1.00 27.60           C
ANISOU 1266  CA  PRO A 189     3683   4511   2294    814    351    721       C
ATOM   1267  C   PRO A 189     -32.857 -51.351  -5.366  1.00 27.03           C
ANISOU 1267  C   PRO A 189     3585   4343   2342    735    422    780       C
ATOM   1268  O   PRO A 189     -33.989 -51.344  -4.890  1.00 27.61           O
ANISOU 1268  O   PRO A 189     3656   4437   2397    751    498    835       O
ATOM   1269  CB  PRO A 189     -31.133 -52.208  -3.758  1.00 28.49           C
ANISOU 1269  CB  PRO A 189     3823   4658   2345    886    371    829       C
ATOM   1270  CG  PRO A 189     -31.890 -52.226  -2.484  1.00 29.80           C
ANISOU 1270  CG  PRO A 189     4015   4913   2396    971    439    894       C
ATOM   1271  CD  PRO A 189     -32.197 -50.794  -2.127  1.00 29.67           C
ANISOU 1271  CD  PRO A 189     3998   4958   2317    986    411    779       C
ATOM   1272  N   ASP A 190     -32.601 -51.686  -6.629  1.00 26.42           N
ANISOU 1272  N   ASP A 190     3486   4168   2386    653    397    766       N
ATOM   1273  CA  ASP A 190     -33.663 -52.128  -7.527  1.00 26.09           C
ANISOU 1273  CA  ASP A 190     3416   4035   2463    576    452    815       C
ATOM   1274  C   ASP A 190     -34.151 -53.525  -7.117  1.00 26.96           C
ANISOU 1274  C   ASP A 190     3535   4120   2589    592    530    956       C
ATOM   1275  O   ASP A 190     -33.358 -54.466  -7.092  1.00 26.83           O
ANISOU 1275  O   ASP A 190     3537   4080   2575    612    517   1005       O
ATOM   1276  CB  ASP A 190     -33.171 -52.162  -8.974  1.00 25.06           C
ANISOU 1276  CB  ASP A 190     3265   3812   2444    495    400    760       C
ATOM   1277  CG  ASP A 190     -34.160 -52.831  -9.909  1.00 25.16           C
ANISOU 1277  CG  ASP A 190     3251   3730   2577    420    448    813       C
ATOM   1278  OD1 ASP A 190     -35.383 -52.718  -9.671  1.00 25.03           O
ANISOU 1278  OD1 ASP A 190     3217   3720   2574    410    510    851       O
ATOM   1279  OD2 ASP A 190     -33.720 -53.481 -10.873  1.00 25.04           O
ANISOU 1279  OD2 ASP A 190     3232   3638   2644    373    423    814       O
ATOM   1280  N   PRO A 191     -35.457 -53.668  -6.814  1.00 27.52           N
ANISOU 1280  N   PRO A 191     3589   4190   2677    584    614   1024       N
ATOM   1281  CA  PRO A 191     -35.971 -54.998  -6.482  1.00 28.45           C
ANISOU 1281  CA  PRO A 191     3709   4270   2828    588    695   1163       C
ATOM   1282  C   PRO A 191     -35.978 -55.984  -7.660  1.00 27.90           C
ANISOU 1282  C   PRO A 191     3624   4074   2903    503    692   1192       C
ATOM   1283  O   PRO A 191     -36.037 -57.193  -7.428  1.00 28.31           O
ANISOU 1283  O   PRO A 191     3688   4081   2986    509    742   1298       O
ATOM   1284  CB  PRO A 191     -37.404 -54.713  -6.012  1.00 29.09           C
ANISOU 1284  CB  PRO A 191     3763   4382   2907    587    782   1211       C
ATOM   1285  CG  PRO A 191     -37.778 -53.469  -6.707  1.00 28.58           C
ANISOU 1285  CG  PRO A 191     3669   4318   2873    543    740   1096       C
ATOM   1286  CD  PRO A 191     -36.521 -52.648  -6.745  1.00 27.85           C
ANISOU 1286  CD  PRO A 191     3605   4264   2713    573    643    983       C
ATOM   1287  N   GLN A 192     -35.934 -55.483  -8.896  1.00 26.63           N
ANISOU 1287  N   GLN A 192     3437   3855   2826    428    637   1099       N
ATOM   1288  CA  GLN A 192     -35.785 -56.350 -10.080  1.00 26.31           C
ANISOU 1288  CA  GLN A 192     3386   3700   2910    355    619   1106       C
ATOM   1289  C   GLN A 192     -34.360 -56.876 -10.269  1.00 25.84           C
ANISOU 1289  C   GLN A 192     3361   3622   2834    383    562   1092       C
ATOM   1290  O   GLN A 192     -34.115 -57.687 -11.160  1.00 26.07           O
ANISOU 1290  O   GLN A 192     3392   3560   2955    338    548   1101       O
ATOM   1291  CB  GLN A 192     -36.257 -55.650 -11.368  1.00 25.67           C
ANISOU 1291  CB  GLN A 192     3268   3570   2917    274    582   1016       C
ATOM   1292  CG  GLN A 192     -37.741 -55.817 -11.629  1.00 26.33           C
ANISOU 1292  CG  GLN A 192     3306   3617   3081    217    644   1057       C
ATOM   1293  CD  GLN A 192     -38.219 -55.080 -12.867  1.00 25.00           C
ANISOU 1293  CD  GLN A 192     3100   3412   2987    149    603    968       C
ATOM   1294  OE1 GLN A 192     -38.894 -54.059 -12.766  1.00 24.76           O
ANISOU 1294  OE1 GLN A 192     3045   3431   2933    152    610    929       O
ATOM   1295  NE2 GLN A 192     -37.876 -55.597 -14.043  1.00 25.33           N
ANISOU 1295  NE2 GLN A 192     3140   3370   3116     94    560    938       N
ATOM   1296  N   GLY A 193     -33.424 -56.414  -9.445  1.00 25.41           N
ANISOU 1296  N   GLY A 193     3333   3657   2664    461    525   1066       N
ATOM   1297  CA  GLY A 193     -32.057 -56.926  -9.473  1.00 25.05           C
ANISOU 1297  CA  GLY A 193     3314   3610   2593    500    473   1061       C
ATOM   1298  C   GLY A 193     -31.169 -56.405 -10.590  1.00 23.79           C
ANISOU 1298  C   GLY A 193     3141   3421   2479    459    391    954       C
ATOM   1299  O   GLY A 193     -30.138 -57.006 -10.875  1.00 23.54           O
ANISOU 1299  O   GLY A 193     3123   3365   2457    477    355    957       O
ATOM   1300  N   SER A 194     -31.543 -55.290 -11.219  1.00 22.64           N
ANISOU 1300  N   SER A 194     2968   3276   2358    409    365    864       N
ATOM   1301  CA  SER A 194     -30.694 -54.678 -12.248  1.00 21.66           C
ANISOU 1301  CA  SER A 194     2830   3129   2270    373    293    766       C
ATOM   1302  C   SER A 194     -29.311 -54.388 -11.677  1.00 21.93           C
ANISOU 1302  C   SER A 194     2875   3235   2222    434    234    727       C
ATOM   1303  O   SER A 194     -29.191 -53.963 -10.529  1.00 22.49           O
ANISOU 1303  O   SER A 194     2957   3395   2192    496    232    727       O
ATOM   1304  CB  SER A 194     -31.296 -53.377 -12.777  1.00 21.41           C
ANISOU 1304  CB  SER A 194     2773   3103   2258    326    279    681       C
ATOM   1305  OG  SER A 194     -32.597 -53.582 -13.294  1.00 20.64           O
ANISOU 1305  OG  SER A 194     2657   2951   2234    273    328    712       O
ATOM   1306  N   ASN A 195     -28.281 -54.614 -12.487  1.00 21.10           N
ANISOU 1306  N   ASN A 195     2763   3095   2157    420    186    692       N
ATOM   1307  CA  ASN A 195     -26.898 -54.462 -12.042  1.00 21.55           C
ANISOU 1307  CA  ASN A 195     2820   3217   2151    475    127    658       C
ATOM   1308  C   ASN A 195     -26.187 -53.364 -12.830  1.00 21.01           C
ANISOU 1308  C   ASN A 195     2721   3152   2109    434     66    549       C
ATOM   1309  O   ASN A 195     -26.815 -52.674 -13.633  1.00 20.60           O
ANISOU 1309  O   ASN A 195     2655   3058   2113    372     72    503       O
ATOM   1310  CB  ASN A 195     -26.159 -55.806 -12.127  1.00 21.79           C
ANISOU 1310  CB  ASN A 195     2868   3214   2198    511    130    728       C
ATOM   1311  CG  ASN A 195     -26.048 -56.339 -13.549  1.00 21.51           C
ANISOU 1311  CG  ASN A 195     2825   3076   2272    452    128    718       C
ATOM   1312  OD1 ASN A 195     -26.202 -55.604 -14.523  1.00 21.66           O
ANISOU 1312  OD1 ASN A 195     2822   3063   2344    391    109    648       O
ATOM   1313  ND2 ASN A 195     -25.793 -57.637 -13.667  1.00 22.48           N
ANISOU 1313  ND2 ASN A 195     2970   3144   2425    476    150    791       N
ATOM   1314  N   MET A 196     -24.888 -53.189 -12.595  1.00 21.45           N
ANISOU 1314  N   MET A 196     2764   3261   2126    470      8    509       N
ATOM   1315  CA  MET A 196     -24.146 -52.116 -13.265  1.00 21.23           C
ANISOU 1315  CA  MET A 196     2701   3238   2127    431    -47    409       C
ATOM   1316  C   MET A 196     -23.848 -52.421 -14.730  1.00 20.53           C
ANISOU 1316  C   MET A 196     2597   3066   2136    378    -48    400       C
ATOM   1317  O   MET A 196     -23.662 -51.492 -15.524  1.00 19.71           O
ANISOU 1317  O   MET A 196     2469   2944   2076    329    -70    330       O
ATOM   1318  CB  MET A 196     -22.871 -51.760 -12.489  1.00 21.91           C
ANISOU 1318  CB  MET A 196     2768   3415   2144    483   -111    364       C
ATOM   1319  CG  MET A 196     -23.135 -51.087 -11.140  1.00 24.34           C
ANISOU 1319  CG  MET A 196     3087   3813   2349    531   -125    339       C
ATOM   1320  SD  MET A 196     -24.207 -49.633 -11.242  1.00 28.63           S
ANISOU 1320  SD  MET A 196     3631   4343   2905    476   -110    264       S
ATOM   1321  CE  MET A 196     -23.187 -48.525 -12.188  1.00 28.13           C
ANISOU 1321  CE  MET A 196     3521   4256   2909    415   -173    154       C
ATOM   1322  N   MET A 197     -23.832 -53.700 -15.112  1.00 20.48           N
ANISOU 1322  N   MET A 197     2610   3007   2166    389    -21    469       N
ATOM   1323  CA  MET A 197     -23.788 -54.041 -16.536  1.00 20.15           C
ANISOU 1323  CA  MET A 197     2562   2881   2213    341    -15    460       C
ATOM   1324  C   MET A 197     -25.019 -53.468 -17.237  1.00 19.53           C
ANISOU 1324  C   MET A 197     2484   2751   2185    276     13    438       C
ATOM   1325  O   MET A 197     -24.918 -52.920 -18.325  1.00 18.59           O
ANISOU 1325  O   MET A 197     2348   2598   2117    231      0    388       O
ATOM   1326  CB  MET A 197     -23.709 -55.557 -16.759  1.00 20.74           C
ANISOU 1326  CB  MET A 197     2663   2898   2318    366     12    537       C
ATOM   1327  CG  MET A 197     -22.406 -56.187 -16.300  1.00 22.25           C
ANISOU 1327  CG  MET A 197     2851   3131   2471    435    -18    559       C
ATOM   1328  SD  MET A 197     -20.962 -55.581 -17.203  1.00 23.90           S
ANISOU 1328  SD  MET A 197     3014   3361   2707    426    -74    480       S
ATOM   1329  CE  MET A 197     -21.210 -56.338 -18.812  1.00 21.58           C
ANISOU 1329  CE  MET A 197     2736   2954   2510    385    -46    488       C
ATOM   1330  N   PHE A 198     -26.176 -53.584 -16.588  1.00 19.47           N
ANISOU 1330  N   PHE A 198     2493   2745   2159    275     54    480       N
ATOM   1331  CA  PHE A 198     -27.416 -53.031 -17.117  1.00 19.07           C
ANISOU 1331  CA  PHE A 198     2437   2658   2150    221     81    463       C
ATOM   1332  C   PHE A 198     -27.381 -51.506 -17.185  1.00 18.89           C
ANISOU 1332  C   PHE A 198     2394   2672   2110    201     55    382       C
ATOM   1333  O   PHE A 198     -27.709 -50.916 -18.221  1.00 18.92           O
ANISOU 1333  O   PHE A 198     2386   2635   2167    154     52    341       O
ATOM   1334  CB  PHE A 198     -28.611 -53.493 -16.275  1.00 19.52           C
ANISOU 1334  CB  PHE A 198     2509   2719   2189    232    135    531       C
ATOM   1335  CG  PHE A 198     -29.913 -52.857 -16.674  1.00 19.53           C
ANISOU 1335  CG  PHE A 198     2496   2698   2226    183    162    514       C
ATOM   1336  CD1 PHE A 198     -30.673 -53.391 -17.709  1.00 20.41           C
ANISOU 1336  CD1 PHE A 198     2601   2733   2421    132    181    528       C
ATOM   1337  CD2 PHE A 198     -30.372 -51.715 -16.027  1.00 20.70           C
ANISOU 1337  CD2 PHE A 198     2637   2904   2324    193    165    478       C
ATOM   1338  CE1 PHE A 198     -31.868 -52.802 -18.093  1.00 20.50           C
ANISOU 1338  CE1 PHE A 198     2592   2730   2465     92    202    511       C
ATOM   1339  CE2 PHE A 198     -31.569 -51.115 -16.406  1.00 20.22           C
ANISOU 1339  CE2 PHE A 198     2560   2825   2296    156    191    463       C
ATOM   1340  CZ  PHE A 198     -32.321 -51.658 -17.437  1.00 20.67           C
ANISOU 1340  CZ  PHE A 198     2605   2812   2436    106    209    482       C
ATOM   1341  N   ALA A 199     -26.986 -50.876 -16.084  1.00 19.24           N
ANISOU 1341  N   ALA A 199     2437   2792   2079    241     35    358       N
ATOM   1342  CA  ALA A 199     -26.938 -49.417 -15.995  1.00 19.60           C
ANISOU 1342  CA  ALA A 199     2468   2869   2108    225      9    277       C
ATOM   1343  C   ALA A 199     -26.046 -48.807 -17.073  1.00 19.23           C
ANISOU 1343  C   ALA A 199     2398   2793   2115    188    -28    216       C
ATOM   1344  O   ALA A 199     -26.457 -47.876 -17.786  1.00 18.61           O
ANISOU 1344  O   ALA A 199     2311   2684   2077    146    -26    172       O
ATOM   1345  CB  ALA A 199     -26.467 -48.987 -14.606  1.00 20.25           C
ANISOU 1345  CB  ALA A 199     2556   3040   2098    280    -16    255       C
ATOM   1346  N   PHE A 200     -24.829 -49.335 -17.203  1.00 19.73           N
ANISOU 1346  N   PHE A 200     2449   2867   2179    206    -59    218       N
ATOM   1347  CA  PHE A 200     -23.891 -48.816 -18.199  1.00 19.48           C
ANISOU 1347  CA  PHE A 200     2388   2814   2198    174    -88    168       C
ATOM   1348  C   PHE A 200     -24.265 -49.196 -19.629  1.00 18.74           C
ANISOU 1348  C   PHE A 200     2299   2644   2178    136    -63    186       C
ATOM   1349  O   PHE A 200     -23.917 -48.479 -20.558  1.00 18.33           O
ANISOU 1349  O   PHE A 200     2229   2567   2169    102    -72    144       O
ATOM   1350  CB  PHE A 200     -22.445 -49.196 -17.858  1.00 20.08           C
ANISOU 1350  CB  PHE A 200     2441   2936   2252    210   -129    162       C
ATOM   1351  CG  PHE A 200     -21.880 -48.402 -16.710  1.00 21.51           C
ANISOU 1351  CG  PHE A 200     2606   3195   2372    235   -172    111       C
ATOM   1352  CD1 PHE A 200     -21.827 -47.016 -16.776  1.00 23.07           C
ANISOU 1352  CD1 PHE A 200     2784   3396   2585    198   -193     34       C
ATOM   1353  CD2 PHE A 200     -21.422 -49.029 -15.563  1.00 24.08           C
ANISOU 1353  CD2 PHE A 200     2937   3589   2625    299   -193    138       C
ATOM   1354  CE1 PHE A 200     -21.327 -46.268 -15.721  1.00 24.33           C
ANISOU 1354  CE1 PHE A 200     2929   3623   2691    218   -239    -26       C
ATOM   1355  CE2 PHE A 200     -20.908 -48.283 -14.507  1.00 24.73           C
ANISOU 1355  CE2 PHE A 200     3003   3749   2644    326   -241     81       C
ATOM   1356  CZ  PHE A 200     -20.870 -46.901 -14.588  1.00 24.27           C
ANISOU 1356  CZ  PHE A 200     2925   3691   2605    283   -265     -6       C
ATOM   1357  N   PHE A 201     -24.990 -50.301 -19.810  1.00 18.50           N
ANISOU 1357  N   PHE A 201     2293   2575   2162    141    -31    245       N
ATOM   1358  CA  PHE A 201     -25.500 -50.650 -21.135  1.00 17.99           C
ANISOU 1358  CA  PHE A 201     2234   2440   2161    105    -12    253       C
ATOM   1359  C   PHE A 201     -26.545 -49.631 -21.572  1.00 17.60           C
ANISOU 1359  C   PHE A 201     2181   2373   2132     66      2    222       C
ATOM   1360  O   PHE A 201     -26.499 -49.144 -22.702  1.00 17.12           O
ANISOU 1360  O   PHE A 201     2113   2280   2112     38     -1    192       O
ATOM   1361  CB  PHE A 201     -26.096 -52.059 -21.175  1.00 17.76           C
ANISOU 1361  CB  PHE A 201     2230   2368   2150    114     16    317       C
ATOM   1362  CG  PHE A 201     -26.476 -52.510 -22.557  1.00 18.23           C
ANISOU 1362  CG  PHE A 201     2296   2358   2274     82     24    313       C
ATOM   1363  CD1 PHE A 201     -25.582 -53.224 -23.340  1.00 17.80           C
ANISOU 1363  CD1 PHE A 201     2246   2274   2243     95     12    314       C
ATOM   1364  CD2 PHE A 201     -27.730 -52.214 -23.081  1.00 18.21           C
ANISOU 1364  CD2 PHE A 201     2293   2323   2302     43     42    307       C
ATOM   1365  CE1 PHE A 201     -25.930 -53.640 -24.623  1.00 18.37           C
ANISOU 1365  CE1 PHE A 201     2328   2286   2366     72     17    303       C
ATOM   1366  CE2 PHE A 201     -28.080 -52.621 -24.363  1.00 18.74           C
ANISOU 1366  CE2 PHE A 201     2366   2334   2421     18     42    296       C
ATOM   1367  CZ  PHE A 201     -27.183 -53.335 -25.130  1.00 18.11           C
ANISOU 1367  CZ  PHE A 201     2296   2224   2360     33     29    292       C
ATOM   1368  N   ALA A 202     -27.477 -49.308 -20.674  1.00 17.90           N
ANISOU 1368  N   ALA A 202     2226   2436   2138     71     21    232       N
ATOM   1369  CA  ALA A 202     -28.492 -48.289 -20.952  1.00 17.93           C
ANISOU 1369  CA  ALA A 202     2226   2430   2156     43     35    204       C
ATOM   1370  C   ALA A 202     -27.831 -46.978 -21.372  1.00 17.82           C
ANISOU 1370  C   ALA A 202     2198   2422   2152     28     11    139       C
ATOM   1371  O   ALA A 202     -28.217 -46.369 -22.376  1.00 17.72           O
ANISOU 1371  O   ALA A 202     2182   2374   2179      1     17    118       O
ATOM   1372  CB  ALA A 202     -29.377 -48.059 -19.722  1.00 17.87           C
ANISOU 1372  CB  ALA A 202     2226   2465   2101     64     58    220       C
ATOM   1373  N   GLN A 203     -26.829 -46.554 -20.608  1.00 18.28           N
ANISOU 1373  N   GLN A 203     2247   2524   2174     47    -18    109       N
ATOM   1374  CA  GLN A 203     -26.158 -45.282 -20.866  1.00 18.54           C
ANISOU 1374  CA  GLN A 203     2263   2558   2222     28    -41     45       C
ATOM   1375  C   GLN A 203     -25.451 -45.322 -22.221  1.00 18.07           C
ANISOU 1375  C   GLN A 203     2188   2457   2219      3    -44     41       C
ATOM   1376  O   GLN A 203     -25.622 -44.423 -23.051  1.00 17.85           O
ANISOU 1376  O   GLN A 203     2157   2397   2229    -25    -36     16       O
ATOM   1377  CB  GLN A 203     -25.156 -44.961 -19.755  1.00 19.35           C
ANISOU 1377  CB  GLN A 203     2352   2719   2279     52    -78     10       C
ATOM   1378  CG  GLN A 203     -24.691 -43.510 -19.757  1.00 20.27           C
ANISOU 1378  CG  GLN A 203     2453   2835   2415     27   -101    -64       C
ATOM   1379  CD  GLN A 203     -23.568 -43.228 -18.775  1.00 22.10           C
ANISOU 1379  CD  GLN A 203     2662   3124   2611     45   -149   -109       C
ATOM   1380  OE1 GLN A 203     -23.018 -44.139 -18.154  1.00 22.47           O
ANISOU 1380  OE1 GLN A 203     2705   3217   2616     81   -167    -83       O
ATOM   1381  NE2 GLN A 203     -23.214 -41.950 -18.638  1.00 23.78           N
ANISOU 1381  NE2 GLN A 203     2861   3332   2843     20   -172   -181       N
ATOM   1382  N   HIS A 204     -24.681 -46.383 -22.442  1.00 17.91           N
ANISOU 1382  N   HIS A 204     2163   2440   2202     19    -53     71       N
ATOM   1383  CA  HIS A 204     -23.926 -46.548 -23.682  1.00 17.43           C
ANISOU 1383  CA  HIS A 204     2088   2348   2185      6    -53     70       C
ATOM   1384  C   HIS A 204     -24.856 -46.616 -24.900  1.00 17.27           C
ANISOU 1384  C   HIS A 204     2085   2275   2200    -14    -26     84       C
ATOM   1385  O   HIS A 204     -24.713 -45.839 -25.850  1.00 16.94           O
ANISOU 1385  O   HIS A 204     2036   2210   2191    -34    -19     64       O
ATOM   1386  CB  HIS A 204     -23.047 -47.809 -23.597  1.00 17.75           C
ANISOU 1386  CB  HIS A 204     2125   2402   2217     38    -64    103       C
ATOM   1387  CG  HIS A 204     -22.167 -48.004 -24.785  1.00 17.14           C
ANISOU 1387  CG  HIS A 204     2031   2303   2178     35    -62    101       C
ATOM   1388  ND1 HIS A 204     -22.492 -48.856 -25.820  1.00 16.57           N
ANISOU 1388  ND1 HIS A 204     1981   2187   2129     39    -43    128       N
ATOM   1389  CD2 HIS A 204     -20.986 -47.432 -25.122  1.00 16.51           C
ANISOU 1389  CD2 HIS A 204     1914   2240   2118     28    -75     75       C
ATOM   1390  CE1 HIS A 204     -21.542 -48.805 -26.737  1.00 17.82           C
ANISOU 1390  CE1 HIS A 204     2119   2339   2311     42    -42    119       C
ATOM   1391  NE2 HIS A 204     -20.622 -47.943 -26.343  1.00 16.98           N
ANISOU 1391  NE2 HIS A 204     1974   2270   2207     34    -58     92       N
ATOM   1392  N   PHE A 205     -25.829 -47.519 -24.848  1.00 17.02           N
ANISOU 1392  N   PHE A 205     2076   2226   2164     -8    -11    120       N
ATOM   1393  CA  PHE A 205     -26.763 -47.720 -25.954  1.00 17.15           C
ANISOU 1393  CA  PHE A 205     2106   2199   2213    -25      5    129       C
ATOM   1394  C   PHE A 205     -27.558 -46.458 -26.300  1.00 17.12           C
ANISOU 1394  C   PHE A 205     2100   2187   2219    -45     15    103       C
ATOM   1395  O   PHE A 205     -27.616 -46.059 -27.470  1.00 16.41           O
ANISOU 1395  O   PHE A 205     2010   2071   2154    -55     20     93       O
ATOM   1396  CB  PHE A 205     -27.707 -48.892 -25.646  1.00 17.40           C
ANISOU 1396  CB  PHE A 205     2153   2213   2244    -21     17    169       C
ATOM   1397  CG  PHE A 205     -28.860 -49.003 -26.588  1.00 17.34           C
ANISOU 1397  CG  PHE A 205     2152   2168   2268    -43     28    170       C
ATOM   1398  CD1 PHE A 205     -28.662 -49.391 -27.909  1.00 16.75           C
ANISOU 1398  CD1 PHE A 205     2085   2060   2221    -45     21    160       C
ATOM   1399  CD2 PHE A 205     -30.157 -48.729 -26.158  1.00 18.41           C
ANISOU 1399  CD2 PHE A 205     2283   2309   2404    -56     43    179       C
ATOM   1400  CE1 PHE A 205     -29.733 -49.489 -28.787  1.00 16.56           C
ANISOU 1400  CE1 PHE A 205     2063   2009   2221    -62     22    155       C
ATOM   1401  CE2 PHE A 205     -31.232 -48.837 -27.032  1.00 17.05           C
ANISOU 1401  CE2 PHE A 205     2108   2109   2263    -75     47    177       C
ATOM   1402  CZ  PHE A 205     -31.014 -49.210 -28.351  1.00 16.58           C
ANISOU 1402  CZ  PHE A 205     2055   2017   2228    -78     32    162       C
ATOM   1403  N   THR A 206     -28.171 -45.825 -25.301  1.00 17.49           N
ANISOU 1403  N   THR A 206     2146   2258   2243    -45     20     94       N
ATOM   1404  CA  THR A 206     -29.027 -44.665 -25.567  1.00 17.43           C
ANISOU 1404  CA  THR A 206     2138   2240   2245    -57     33     72       C
ATOM   1405  C   THR A 206     -28.266 -43.439 -26.063  1.00 17.48           C
ANISOU 1405  C   THR A 206     2138   2235   2270    -67     28     36       C
ATOM   1406  O   THR A 206     -28.829 -42.613 -26.783  1.00 17.02           O
ANISOU 1406  O   THR A 206     2083   2152   2232    -75     41     27       O
ATOM   1407  CB  THR A 206     -29.867 -44.250 -24.343  1.00 17.72           C
ANISOU 1407  CB  THR A 206     2177   2305   2248    -46     43     69       C
ATOM   1408  OG1 THR A 206     -29.006 -43.890 -23.260  1.00 18.57           O
ANISOU 1408  OG1 THR A 206     2283   2450   2323    -33     26     45       O
ATOM   1409  CG2 THR A 206     -30.816 -45.373 -23.931  1.00 17.80           C
ANISOU 1409  CG2 THR A 206     2190   2322   2250    -40     60    115       C
ATOM   1410  N   HIS A 207     -26.985 -43.329 -25.712  1.00 17.88           N
ANISOU 1410  N   HIS A 207     2174   2302   2318    -68     11     18       N
ATOM   1411  CA  HIS A 207     -26.200 -42.147 -26.081  1.00 18.15           C
ANISOU 1411  CA  HIS A 207     2195   2321   2381    -86      9    -16       C
ATOM   1412  C   HIS A 207     -25.771 -42.116 -27.551  1.00 17.78           C
ANISOU 1412  C   HIS A 207     2143   2241   2370    -94     23     -1       C
ATOM   1413  O   HIS A 207     -25.082 -41.187 -27.968  1.00 17.62           O
ANISOU 1413  O   HIS A 207     2109   2204   2381   -110     30    -18       O
ATOM   1414  CB  HIS A 207     -25.007 -41.956 -25.131  1.00 18.89           C
ANISOU 1414  CB  HIS A 207     2265   2448   2464    -87    -19    -46       C
ATOM   1415  CG  HIS A 207     -25.390 -41.345 -23.817  1.00 21.30           C
ANISOU 1415  CG  HIS A 207     2577   2780   2734    -80    -33    -81       C
ATOM   1416  ND1 HIS A 207     -26.555 -41.682 -23.159  1.00 23.83           N
ANISOU 1416  ND1 HIS A 207     2920   3117   3016    -59    -21    -64       N
ATOM   1417  CD2 HIS A 207     -24.778 -40.416 -23.046  1.00 24.48           C
ANISOU 1417  CD2 HIS A 207     2966   3198   3136    -89    -56   -135       C
ATOM   1418  CE1 HIS A 207     -26.638 -40.992 -22.035  1.00 25.10           C
ANISOU 1418  CE1 HIS A 207     3086   3307   3146    -49    -34   -104       C
ATOM   1419  NE2 HIS A 207     -25.572 -40.218 -21.941  1.00 25.29           N
ANISOU 1419  NE2 HIS A 207     3090   3328   3191    -67    -59   -152       N
ATOM   1420  N   GLN A 208     -26.181 -43.112 -28.338  1.00 17.04           N
ANISOU 1420  N   GLN A 208     2062   2138   2273    -81     30     30       N
ATOM   1421  CA  GLN A 208     -26.075 -42.983 -29.791  1.00 17.09           C
ANISOU 1421  CA  GLN A 208     2073   2118   2302    -79     47     43       C
ATOM   1422  C   GLN A 208     -27.206 -42.135 -30.352  1.00 17.06           C
ANISOU 1422  C   GLN A 208     2085   2091   2305    -80     63     42       C
ATOM   1423  O   GLN A 208     -27.026 -41.484 -31.385  1.00 17.89           O
ANISOU 1423  O   GLN A 208     2193   2176   2428    -78     81     48       O
ATOM   1424  CB  GLN A 208     -26.014 -44.334 -30.488  1.00 16.69           C
ANISOU 1424  CB  GLN A 208     2032   2064   2244    -61     42     66       C
ATOM   1425  CG  GLN A 208     -27.306 -45.079 -30.596  1.00 16.16           C
ANISOU 1425  CG  GLN A 208     1984   1988   2168    -57     38     77       C
ATOM   1426  CD  GLN A 208     -27.071 -46.516 -30.980  1.00 16.01           C
ANISOU 1426  CD  GLN A 208     1975   1961   2147    -43     29     92       C
ATOM   1427  OE1 GLN A 208     -26.770 -46.809 -32.141  1.00 16.76           O
ANISOU 1427  OE1 GLN A 208     2080   2043   2246    -28     31     92       O
ATOM   1428  NE2 GLN A 208     -27.176 -47.424 -30.007  1.00 14.78           N
ANISOU 1428  NE2 GLN A 208     1821   1812   1982    -41     19    106       N
ATOM   1429  N   PHE A 209     -28.361 -42.122 -29.686  1.00 16.77           N
ANISOU 1429  N   PHE A 209     2056   2062   2254    -79     60     40       N
ATOM   1430  CA  PHE A 209     -29.486 -41.342 -30.204  1.00 16.91           C
ANISOU 1430  CA  PHE A 209     2084   2064   2278    -73     74     41       C
ATOM   1431  C   PHE A 209     -29.949 -40.193 -29.310  1.00 17.40           C
ANISOU 1431  C   PHE A 209     2147   2124   2338    -76     82     18       C
ATOM   1432  O   PHE A 209     -30.718 -39.351 -29.769  1.00 18.14           O
ANISOU 1432  O   PHE A 209     2249   2201   2441    -66     97     18       O
ATOM   1433  CB  PHE A 209     -30.652 -42.233 -30.679  1.00 16.77           C
ANISOU 1433  CB  PHE A 209     2071   2050   2252    -64     68     59       C
ATOM   1434  CG  PHE A 209     -31.069 -43.310 -29.709  1.00 16.88           C
ANISOU 1434  CG  PHE A 209     2080   2083   2253    -69     58     68       C
ATOM   1435  CD1 PHE A 209     -31.833 -43.008 -28.593  1.00 17.17           C
ANISOU 1435  CD1 PHE A 209     2111   2138   2276    -70     66     67       C
ATOM   1436  CD2 PHE A 209     -30.772 -44.639 -29.969  1.00 15.90           C
ANISOU 1436  CD2 PHE A 209     1957   1954   2129    -70     46     83       C
ATOM   1437  CE1 PHE A 209     -32.244 -44.012 -27.716  1.00 17.12           C
ANISOU 1437  CE1 PHE A 209     2099   2148   2257    -72     65     86       C
ATOM   1438  CE2 PHE A 209     -31.180 -45.643 -29.106  1.00 17.49           C
ANISOU 1438  CE2 PHE A 209     2156   2164   2325    -75     43    101       C
ATOM   1439  CZ  PHE A 209     -31.918 -45.327 -27.974  1.00 17.74           C
ANISOU 1439  CZ  PHE A 209     2180   2217   2343    -76     55    106       C
ATOM   1440  N   PHE A 210     -29.457 -40.123 -28.072  1.00 17.66           N
ANISOU 1440  N   PHE A 210     2174   2177   2359    -83     71     -4       N
ATOM   1441  CA  PHE A 210     -29.610 -38.921 -27.256  1.00 17.93           C
ANISOU 1441  CA  PHE A 210     2213   2206   2393    -84     76    -38       C
ATOM   1442  C   PHE A 210     -28.261 -38.202 -27.248  1.00 18.61           C
ANISOU 1442  C   PHE A 210     2288   2274   2507   -105     69    -66       C
ATOM   1443  O   PHE A 210     -27.335 -38.583 -26.517  1.00 19.21           O
ANISOU 1443  O   PHE A 210     2349   2377   2574   -114     46    -83       O
ATOM   1444  CB  PHE A 210     -30.069 -39.236 -25.824  1.00 17.87           C
ANISOU 1444  CB  PHE A 210     2206   2238   2344    -72     67    -50       C
ATOM   1445  CG  PHE A 210     -31.350 -40.035 -25.737  1.00 17.75           C
ANISOU 1445  CG  PHE A 210     2192   2242   2310    -57     78    -16       C
ATOM   1446  CD1 PHE A 210     -32.436 -39.770 -26.572  1.00 16.73           C
ANISOU 1446  CD1 PHE A 210     2064   2095   2197    -50     94     -1       C
ATOM   1447  CD2 PHE A 210     -31.473 -41.039 -24.789  1.00 17.19           C
ANISOU 1447  CD2 PHE A 210     2118   2208   2206    -49     73      1       C
ATOM   1448  CE1 PHE A 210     -33.612 -40.514 -26.478  1.00 17.62           C
ANISOU 1448  CE1 PHE A 210     2167   2227   2300    -42    102     28       C
ATOM   1449  CE2 PHE A 210     -32.642 -41.782 -24.682  1.00 17.70           C
ANISOU 1449  CE2 PHE A 210     2177   2286   2263    -42     88     36       C
ATOM   1450  CZ  PHE A 210     -33.718 -41.516 -25.530  1.00 17.71           C
ANISOU 1450  CZ  PHE A 210     2172   2269   2288    -42    102     47       C
ATOM   1451  N   LYS A 211     -28.153 -37.186 -28.101  1.00 18.96           N
ANISOU 1451  N   LYS A 211     2338   2275   2591   -113     89    -67       N
ATOM   1452  CA  LYS A 211     -26.937 -36.394 -28.258  1.00 20.02           C
ANISOU 1452  CA  LYS A 211     2457   2382   2769   -141     92    -88       C
ATOM   1453  C   LYS A 211     -27.340 -34.939 -28.415  1.00 20.89           C
ANISOU 1453  C   LYS A 211     2584   2439   2913   -144    114   -106       C
ATOM   1454  O   LYS A 211     -27.308 -34.381 -29.506  1.00 20.93           O
ANISOU 1454  O   LYS A 211     2597   2404   2952   -144    144    -78       O
ATOM   1455  CB  LYS A 211     -26.146 -36.863 -29.479  1.00 20.02           C
ANISOU 1455  CB  LYS A 211     2443   2373   2789   -145    105    -51       C
ATOM   1456  CG  LYS A 211     -25.740 -38.322 -29.427  1.00 20.79           C
ANISOU 1456  CG  LYS A 211     2528   2514   2856   -136     86    -33       C
ATOM   1457  CD  LYS A 211     -24.589 -38.630 -30.379  1.00 21.77           C
ANISOU 1457  CD  LYS A 211     2632   2635   3005   -141     98    -10       C
ATOM   1458  CE  LYS A 211     -24.936 -38.367 -31.828  1.00 22.51           C
ANISOU 1458  CE  LYS A 211     2743   2701   3109   -125    132     26       C
ATOM   1459  NZ  LYS A 211     -23.775 -38.653 -32.727  1.00 22.73           N
ANISOU 1459  NZ  LYS A 211     2750   2731   3155   -124    150     50       N
ATOM   1460  N   THR A 212     -27.737 -34.328 -27.311  1.00 21.86           N
ANISOU 1460  N   THR A 212     2718   2562   3025   -142    103   -150       N
ATOM   1461  CA  THR A 212     -28.310 -32.990 -27.359  1.00 22.97           C
ANISOU 1461  CA  THR A 212     2883   2650   3196   -136    125   -170       C
ATOM   1462  C   THR A 212     -27.282 -31.964 -27.835  1.00 24.19           C
ANISOU 1462  C   THR A 212     3029   2742   3420   -172    139   -183       C
ATOM   1463  O   THR A 212     -26.135 -31.957 -27.376  1.00 24.53           O
ANISOU 1463  O   THR A 212     3044   2790   3487   -207    117   -216       O
ATOM   1464  CB  THR A 212     -28.893 -32.606 -26.003  1.00 23.13           C
ANISOU 1464  CB  THR A 212     2917   2687   3183   -120    108   -222       C
ATOM   1465  OG1 THR A 212     -29.958 -33.512 -25.702  1.00 23.59           O
ANISOU 1465  OG1 THR A 212     2981   2799   3185    -87    107   -196       O
ATOM   1466  CG2 THR A 212     -29.427 -31.173 -26.014  1.00 23.99           C
ANISOU 1466  CG2 THR A 212     3055   2734   3327   -111    131   -249       C
ATOM   1467  N   ASP A 213     -27.701 -31.126 -28.783  1.00 25.12           N
ANISOU 1467  N   ASP A 213     3167   2803   3573   -161    178   -153       N
ATOM   1468  CA  ASP A 213     -26.846 -30.091 -29.342  1.00 26.82           C
ANISOU 1468  CA  ASP A 213     3378   2949   3864   -194    205   -151       C
ATOM   1469  C   ASP A 213     -27.005 -28.856 -28.476  1.00 28.20           C
ANISOU 1469  C   ASP A 213     3572   3069   4074   -205    201   -213       C
ATOM   1470  O   ASP A 213     -27.835 -27.983 -28.745  1.00 28.23           O
ANISOU 1470  O   ASP A 213     3611   3023   4093   -178    230   -205       O
ATOM   1471  CB  ASP A 213     -27.236 -29.801 -30.794  1.00 27.01           C
ANISOU 1471  CB  ASP A 213     3420   2939   3903   -169    252    -81       C
ATOM   1472  CG  ASP A 213     -26.253 -28.880 -31.494  1.00 28.49           C
ANISOU 1472  CG  ASP A 213     3598   3056   4169   -202    291    -61       C
ATOM   1473  OD1 ASP A 213     -25.383 -28.298 -30.818  1.00 29.00           O
ANISOU 1473  OD1 ASP A 213     3642   3087   4289   -251    279   -109       O
ATOM   1474  OD2 ASP A 213     -26.357 -28.743 -32.727  1.00 30.18           O
ANISOU 1474  OD2 ASP A 213     3825   3252   4391   -180    332      4       O
ATOM   1475  N   HIS A 214     -26.196 -28.786 -27.427  1.00 29.72           N
ANISOU 1475  N   HIS A 214     3742   3273   4278   -240    163   -279       N
ATOM   1476  CA  HIS A 214     -26.358 -27.750 -26.414  1.00 31.27           C
ANISOU 1476  CA  HIS A 214     3958   3427   4494   -247    147   -356       C
ATOM   1477  C   HIS A 214     -26.096 -26.345 -26.959  1.00 32.14           C
ANISOU 1477  C   HIS A 214     4085   3430   4698   -273    184   -360       C
ATOM   1478  O   HIS A 214     -26.610 -25.371 -26.409  1.00 33.25           O
ANISOU 1478  O   HIS A 214     4259   3517   4856   -262    186   -410       O
ATOM   1479  CB  HIS A 214     -25.477 -28.055 -25.201  1.00 32.04           C
ANISOU 1479  CB  HIS A 214     4026   3571   4577   -276     90   -430       C
ATOM   1480  CG  HIS A 214     -25.787 -29.371 -24.559  1.00 32.73           C
ANISOU 1480  CG  HIS A 214     4105   3758   4572   -244     59   -422       C
ATOM   1481  ND1 HIS A 214     -26.898 -29.570 -23.768  1.00 33.14           N
ANISOU 1481  ND1 HIS A 214     4188   3850   4553   -195     52   -437       N
ATOM   1482  CD2 HIS A 214     -25.141 -30.560 -24.607  1.00 33.58           C
ANISOU 1482  CD2 HIS A 214     4178   3931   4650   -250     38   -394       C
ATOM   1483  CE1 HIS A 214     -26.919 -30.823 -23.351  1.00 32.90           C
ANISOU 1483  CE1 HIS A 214     4142   3902   4457   -177     30   -416       C
ATOM   1484  NE2 HIS A 214     -25.864 -31.445 -23.846  1.00 33.42           N
ANISOU 1484  NE2 HIS A 214     4171   3982   4546   -208     19   -391       N
ATOM   1485  N   LYS A 215     -25.334 -26.250 -28.049  1.00 32.37           N
ANISOU 1485  N   LYS A 215     4091   3423   4786   -304    218   -305       N
ATOM   1486  CA  LYS A 215     -25.106 -24.973 -28.749  1.00 33.38           C
ANISOU 1486  CA  LYS A 215     4234   3441   5006   -326    267   -286       C
ATOM   1487  C   LYS A 215     -26.416 -24.368 -29.266  1.00 32.52           C
ANISOU 1487  C   LYS A 215     4182   3291   4882   -266    308   -247       C
ATOM   1488  O   LYS A 215     -26.585 -23.144 -29.269  1.00 33.37           O
ANISOU 1488  O   LYS A 215     4320   3304   5053   -270    336   -263       O
ATOM   1489  CB  LYS A 215     -24.155 -25.166 -29.936  1.00 33.85           C
ANISOU 1489  CB  LYS A 215     4259   3488   5115   -356    306   -214       C
ATOM   1490  CG  LYS A 215     -22.753 -25.663 -29.566  1.00 36.19           C
ANISOU 1490  CG  LYS A 215     4490   3820   5442   -415    273   -245       C
ATOM   1491  CD  LYS A 215     -22.214 -26.677 -30.584  1.00 38.37           C
ANISOU 1491  CD  LYS A 215     4733   4152   5695   -407    295   -167       C
ATOM   1492  CE  LYS A 215     -21.637 -26.008 -31.820  1.00 40.10           C
ANISOU 1492  CE  LYS A 215     4942   4303   5991   -427    365    -95       C
ATOM   1493  NZ  LYS A 215     -20.275 -25.459 -31.560  1.00 42.84           N
ANISOU 1493  NZ  LYS A 215     5229   4608   6439   -505    365   -127       N
ATOM   1494  N   ARG A 216     -27.329 -25.229 -29.712  1.00 30.48           N
ANISOU 1494  N   ARG A 216     3935   3101   4544   -211    311   -195       N
ATOM   1495  CA  ARG A 216     -28.619 -24.792 -30.249  1.00 29.75           C
ANISOU 1495  CA  ARG A 216     3886   2988   4428   -148    344   -154       C
ATOM   1496  C   ARG A 216     -29.696 -24.741 -29.167  1.00 28.42           C
ANISOU 1496  C   ARG A 216     3741   2849   4207   -108    318   -209       C
ATOM   1497  O   ARG A 216     -30.486 -23.798 -29.119  1.00 28.69           O
ANISOU 1497  O   ARG A 216     3814   2829   4258    -71    341   -216       O
ATOM   1498  CB  ARG A 216     -29.066 -25.712 -31.390  1.00 29.36           C
ANISOU 1498  CB  ARG A 216     3831   2998   4325   -108    360    -72       C
ATOM   1499  CG  ARG A 216     -28.126 -25.719 -32.595  1.00 31.32           C
ANISOU 1499  CG  ARG A 216     4064   3221   4614   -130    397     -8       C
ATOM   1500  CD  ARG A 216     -28.707 -26.556 -33.729  1.00 33.24           C
ANISOU 1500  CD  ARG A 216     4311   3524   4794    -79    408     64       C
ATOM   1501  NE  ARG A 216     -27.863 -26.564 -34.926  1.00 36.04           N
ANISOU 1501  NE  ARG A 216     4656   3863   5176    -87    449    129       N
ATOM   1502  CZ  ARG A 216     -27.829 -25.605 -35.853  1.00 37.95           C
ANISOU 1502  CZ  ARG A 216     4922   4038   5459    -68    507    188       C
ATOM   1503  NH1 ARG A 216     -28.586 -24.518 -35.747  1.00 39.66           N
ANISOU 1503  NH1 ARG A 216     5178   4190   5702    -39    529    188       N
ATOM   1504  NH2 ARG A 216     -27.019 -25.728 -36.900  1.00 39.22           N
ANISOU 1504  NH2 ARG A 216     5070   4197   5635    -72    547    250       N
ATOM   1505  N   GLY A 217     -29.727 -25.760 -28.308  1.00 26.68           N
ANISOU 1505  N   GLY A 217     3499   2715   3924   -111    273   -243       N
ATOM   1506  CA  GLY A 217     -30.701 -25.841 -27.219  1.00 25.62           C
ANISOU 1506  CA  GLY A 217     3380   2621   3731    -72    251   -290       C
ATOM   1507  C   GLY A 217     -31.123 -27.265 -26.931  1.00 24.05           C
ANISOU 1507  C   GLY A 217     3157   2527   3453    -55    225   -270       C
ATOM   1508  O   GLY A 217     -30.817 -28.171 -27.710  1.00 22.86           O
ANISOU 1508  O   GLY A 217     2984   2411   3291    -66    225   -218       O
ATOM   1509  N   PRO A 218     -31.851 -27.477 -25.818  1.00 23.07           N
ANISOU 1509  N   PRO A 218     3041   2452   3273    -25    207   -310       N
ATOM   1510  CA  PRO A 218     -32.233 -28.829 -25.392  1.00 22.33           C
ANISOU 1510  CA  PRO A 218     2924   2452   3110    -12    186   -290       C
ATOM   1511  C   PRO A 218     -33.155 -29.571 -26.366  1.00 21.37           C
ANISOU 1511  C   PRO A 218     2792   2363   2965     16    205   -217       C
ATOM   1512  O   PRO A 218     -33.223 -30.801 -26.329  1.00 21.28           O
ANISOU 1512  O   PRO A 218     2757   2413   2915     11    189   -190       O
ATOM   1513  CB  PRO A 218     -32.942 -28.588 -24.050  1.00 22.78           C
ANISOU 1513  CB  PRO A 218     2998   2541   3118     24    178   -343       C
ATOM   1514  CG  PRO A 218     -33.377 -27.183 -24.085  1.00 23.34           C
ANISOU 1514  CG  PRO A 218     3103   2537   3226     48    203   -374       C
ATOM   1515  CD  PRO A 218     -32.363 -26.447 -24.895  1.00 23.86           C
ANISOU 1515  CD  PRO A 218     3174   2519   3374      3    210   -373       C
ATOM   1516  N   GLY A 219     -33.856 -28.831 -27.223  1.00 21.16           N
ANISOU 1516  N   GLY A 219     2783   2294   2963     47    236   -186       N
ATOM   1517  CA  GLY A 219     -34.748 -29.431 -28.216  1.00 20.26           C
ANISOU 1517  CA  GLY A 219     2658   2213   2829     76    247   -123       C
ATOM   1518  C   GLY A 219     -34.064 -29.877 -29.502  1.00 19.78           C
ANISOU 1518  C   GLY A 219     2587   2141   2787     55    249    -75       C
ATOM   1519  O   GLY A 219     -34.736 -30.329 -30.438  1.00 19.14           O
ANISOU 1519  O   GLY A 219     2498   2085   2688     82    253    -29       O
ATOM   1520  N   PHE A 220     -32.736 -29.765 -29.546  1.00 19.13           N
ANISOU 1520  N   PHE A 220     2501   2028   2740     10    245    -89       N
ATOM   1521  CA  PHE A 220     -31.955 -30.079 -30.742  1.00 18.98           C
ANISOU 1521  CA  PHE A 220     2474   1998   2741     -7    255    -44       C
ATOM   1522  C   PHE A 220     -31.006 -31.239 -30.511  1.00 18.54           C
ANISOU 1522  C   PHE A 220     2389   1986   2670    -44    227    -50       C
ATOM   1523  O   PHE A 220     -30.474 -31.407 -29.412  1.00 18.85           O
ANISOU 1523  O   PHE A 220     2416   2040   2705    -70    203    -95       O
ATOM   1524  CB  PHE A 220     -31.159 -28.855 -31.170  1.00 19.55           C
ANISOU 1524  CB  PHE A 220     2562   1988   2879    -26    287    -42       C
ATOM   1525  CG  PHE A 220     -32.016 -27.737 -31.679  1.00 20.31           C
ANISOU 1525  CG  PHE A 220     2691   2031   2995     18    322    -19       C
ATOM   1526  CD1 PHE A 220     -32.504 -26.768 -30.813  1.00 22.33           C
ANISOU 1526  CD1 PHE A 220     2970   2246   3268     31    327    -64       C
ATOM   1527  CD2 PHE A 220     -32.354 -27.663 -33.024  1.00 20.81           C
ANISOU 1527  CD2 PHE A 220     2766   2089   3053     55    349     48       C
ATOM   1528  CE1 PHE A 220     -33.302 -25.742 -31.281  1.00 22.65           C
ANISOU 1528  CE1 PHE A 220     3044   2236   3328     79    361    -40       C
ATOM   1529  CE2 PHE A 220     -33.153 -26.636 -33.502  1.00 22.18           C
ANISOU 1529  CE2 PHE A 220     2971   2217   3241    104    382     75       C
ATOM   1530  CZ  PHE A 220     -33.631 -25.677 -32.634  1.00 23.00           C
ANISOU 1530  CZ  PHE A 220     3096   2275   3367    116    389     33       C
ATOM   1531  N   THR A 221     -30.779 -32.020 -31.561  1.00 18.22           N
ANISOU 1531  N   THR A 221     2339   1967   2617    -40    230     -5       N
ATOM   1532  CA  THR A 221     -29.927 -33.200 -31.479  1.00 18.02           C
ANISOU 1532  CA  THR A 221     2288   1982   2576    -65    206     -5       C
ATOM   1533  C   THR A 221     -28.811 -33.165 -32.520  1.00 18.47           C
ANISOU 1533  C   THR A 221     2337   2018   2663    -79    227     26       C
ATOM   1534  O   THR A 221     -28.968 -32.582 -33.596  1.00 18.62           O
ANISOU 1534  O   THR A 221     2372   2007   2697    -58    260     65       O
ATOM   1535  CB  THR A 221     -30.747 -34.494 -31.659  1.00 17.59           C
ANISOU 1535  CB  THR A 221     2227   1983   2472    -43    186     14       C
ATOM   1536  OG1 THR A 221     -29.894 -35.635 -31.499  1.00 17.06           O
ANISOU 1536  OG1 THR A 221     2141   1947   2393    -64    164     14       O
ATOM   1537  CG2 THR A 221     -31.424 -34.548 -33.042  1.00 17.34           C
ANISOU 1537  CG2 THR A 221     2208   1952   2430     -8    200     57       C
ATOM   1538  N   ARG A 222     -27.688 -33.794 -32.179  1.00 19.03           N
ANISOU 1538  N   ARG A 222     2381   2108   2741   -110    211     13       N
ATOM   1539  CA  ARG A 222     -26.599 -34.024 -33.126  1.00 19.95           C
ANISOU 1539  CA  ARG A 222     2482   2221   2879   -120    230     45       C
ATOM   1540  C   ARG A 222     -26.680 -35.416 -33.750  1.00 19.40           C
ANISOU 1540  C   ARG A 222     2409   2200   2762    -96    216     71       C
ATOM   1541  O   ARG A 222     -25.876 -35.744 -34.621  1.00 19.68           O
ANISOU 1541  O   ARG A 222     2434   2240   2802    -92    234     99       O
ATOM   1542  CB  ARG A 222     -25.242 -33.868 -32.433  1.00 21.30           C
ANISOU 1542  CB  ARG A 222     2617   2386   3090   -166    220     14       C
ATOM   1543  CG  ARG A 222     -25.010 -32.495 -31.808  1.00 24.76           C
ANISOU 1543  CG  ARG A 222     3054   2768   3585   -198    229    -22       C
ATOM   1544  CD  ARG A 222     -23.536 -32.234 -31.452  1.00 30.07           C
ANISOU 1544  CD  ARG A 222     3681   3430   4313   -248    223    -47       C
ATOM   1545  NE  ARG A 222     -22.785 -33.453 -31.150  1.00 34.62           N
ANISOU 1545  NE  ARG A 222     4224   4070   4860   -252    191    -52       N
ATOM   1546  CZ  ARG A 222     -22.862 -34.141 -30.008  1.00 36.87           C
ANISOU 1546  CZ  ARG A 222     4502   4404   5103   -249    143    -92       C
ATOM   1547  NH1 ARG A 222     -22.131 -35.244 -29.850  1.00 38.27           N
ANISOU 1547  NH1 ARG A 222     4650   4634   5257   -245    120    -87       N
ATOM   1548  NH2 ARG A 222     -23.664 -33.740 -29.025  1.00 38.40           N
ANISOU 1548  NH2 ARG A 222     4719   4595   5275   -243    122   -134       N
ATOM   1549  N   GLY A 223     -27.629 -36.232 -33.292  1.00 18.75           N
ANISOU 1549  N   GLY A 223     2335   2151   2637    -80    187     59       N
ATOM   1550  CA  GLY A 223     -27.782 -37.606 -33.773  1.00 18.29           C
ANISOU 1550  CA  GLY A 223     2276   2130   2542    -62    169     75       C
ATOM   1551  C   GLY A 223     -28.738 -37.658 -34.947  1.00 18.05           C
ANISOU 1551  C   GLY A 223     2267   2101   2488    -25    178    102       C
ATOM   1552  O   GLY A 223     -29.888 -38.058 -34.792  1.00 17.66           O
ANISOU 1552  O   GLY A 223     2224   2069   2416    -11    158     96       O
ATOM   1553  N   LEU A 224     -28.252 -37.277 -36.127  1.00 18.05           N
ANISOU 1553  N   LEU A 224     2276   2088   2493     -6    207    133       N
ATOM   1554  CA  LEU A 224     -29.130 -37.101 -37.293  1.00 18.26           C
ANISOU 1554  CA  LEU A 224     2326   2119   2493     39    216    159       C
ATOM   1555  C   LEU A 224     -29.646 -38.407 -37.886  1.00 17.89           C
ANISOU 1555  C   LEU A 224     2285   2111   2403     63    184    155       C
ATOM   1556  O   LEU A 224     -30.553 -38.383 -38.720  1.00 18.38           O
ANISOU 1556  O   LEU A 224     2361   2185   2437    100    177    165       O
ATOM   1557  CB  LEU A 224     -28.452 -36.245 -38.375  1.00 18.85           C
ANISOU 1557  CB  LEU A 224     2412   2169   2580     59    263    200       C
ATOM   1558  CG  LEU A 224     -27.936 -34.870 -37.923  1.00 20.25           C
ANISOU 1558  CG  LEU A 224     2586   2295   2814     31    299    206       C
ATOM   1559  CD1 LEU A 224     -27.459 -34.053 -39.116  1.00 21.41           C
ANISOU 1559  CD1 LEU A 224     2747   2415   2974     57    353    260       C
ATOM   1560  CD2 LEU A 224     -29.001 -34.096 -37.136  1.00 20.88           C
ANISOU 1560  CD2 LEU A 224     2677   2353   2905     30    290    184       C
ATOM   1561  N   GLY A 225     -29.073 -39.534 -37.466  1.00 17.27           N
ANISOU 1561  N   GLY A 225     2193   2048   2321     44    162    138       N
ATOM   1562  CA  GLY A 225     -29.599 -40.849 -37.817  1.00 17.05           C
ANISOU 1562  CA  GLY A 225     2171   2044   2264     58    128    125       C
ATOM   1563  C   GLY A 225     -30.867 -41.212 -37.057  1.00 16.60           C
ANISOU 1563  C   GLY A 225     2105   1994   2206     44     98    106       C
ATOM   1564  O   GLY A 225     -31.596 -42.118 -37.464  1.00 16.55           O
ANISOU 1564  O   GLY A 225     2100   2003   2184     54     69     95       O
ATOM   1565  N   HIS A 226     -31.121 -40.523 -35.943  1.00 16.18           N
ANISOU 1565  N   HIS A 226     2042   1934   2174     21    105    100       N
ATOM   1566  CA  HIS A 226     -32.344 -40.700 -35.154  1.00 15.83           C
ANISOU 1566  CA  HIS A 226     1985   1900   2128     12     88     88       C
ATOM   1567  C   HIS A 226     -32.663 -42.163 -34.796  1.00 16.03           C
ANISOU 1567  C   HIS A 226     2000   1939   2150     -3     60     80       C
ATOM   1568  O   HIS A 226     -33.813 -42.604 -34.860  1.00 15.79           O
ANISOU 1568  O   HIS A 226     1959   1921   2120     -2     42     76       O
ATOM   1569  CB  HIS A 226     -33.532 -40.034 -35.867  1.00 16.22           C
ANISOU 1569  CB  HIS A 226     2038   1956   2169     43     88     96       C
ATOM   1570  CG  HIS A 226     -33.549 -38.549 -35.719  1.00 15.68           C
ANISOU 1570  CG  HIS A 226     1978   1866   2112     55    119    105       C
ATOM   1571  ND1 HIS A 226     -34.206 -37.917 -34.688  1.00 16.09           N
ANISOU 1571  ND1 HIS A 226     2022   1915   2176     48    126     94       N
ATOM   1572  CD2 HIS A 226     -32.993 -37.567 -36.469  1.00 14.97           C
ANISOU 1572  CD2 HIS A 226     1906   1752   2028     74    148    125       C
ATOM   1573  CE1 HIS A 226     -34.053 -36.611 -34.806  1.00 15.13           C
ANISOU 1573  CE1 HIS A 226     1916   1764   2069     62    154    101       C
ATOM   1574  NE2 HIS A 226     -33.320 -36.371 -35.877  1.00 15.07           N
ANISOU 1574  NE2 HIS A 226     1924   1741   2062     76    169    123       N
ATOM   1575  N   GLY A 227     -31.645 -42.906 -34.386  1.00 15.89           N
ANISOU 1575  N   GLY A 227     1983   1918   2135    -18     57     78       N
ATOM   1576  CA  GLY A 227     -31.856 -44.305 -34.055  1.00 16.00           C
ANISOU 1576  CA  GLY A 227     1993   1935   2151    -30     35     75       C
ATOM   1577  C   GLY A 227     -30.587 -45.105 -33.895  1.00 16.09           C
ANISOU 1577  C   GLY A 227     2010   1940   2162    -33     33     77       C
ATOM   1578  O   GLY A 227     -29.529 -44.567 -33.555  1.00 15.66           O
ANISOU 1578  O   GLY A 227     1952   1889   2109    -34     48     79       O
ATOM   1579  N   VAL A 228     -30.721 -46.404 -34.134  1.00 16.08           N
ANISOU 1579  N   VAL A 228     2015   1930   2164    -32     14     75       N
ATOM   1580  CA  VAL A 228     -29.650 -47.354 -33.860  1.00 16.35           C
ANISOU 1580  CA  VAL A 228     2055   1957   2199    -29     12     80       C
ATOM   1581  C   VAL A 228     -28.763 -47.498 -35.098  1.00 16.50           C
ANISOU 1581  C   VAL A 228     2089   1973   2207      0     15     73       C
ATOM   1582  O   VAL A 228     -28.875 -48.467 -35.871  1.00 17.15           O
ANISOU 1582  O   VAL A 228     2189   2041   2287     15     -2     62       O
ATOM   1583  CB  VAL A 228     -30.220 -48.708 -33.395  1.00 16.58           C
ANISOU 1583  CB  VAL A 228     2088   1968   2244    -42     -4     84       C
ATOM   1584  CG1 VAL A 228     -29.095 -49.637 -32.949  1.00 16.87           C
ANISOU 1584  CG1 VAL A 228     2134   1996   2281    -31     -4     95       C
ATOM   1585  CG2 VAL A 228     -31.229 -48.501 -32.249  1.00 16.48           C
ANISOU 1585  CG2 VAL A 228     2058   1965   2239    -66      1     98       C
ATOM   1586  N   ASP A 229     -27.881 -46.513 -35.283  1.00 16.31           N
ANISOU 1586  N   ASP A 229     2058   1960   2178      7     37     80       N
ATOM   1587  CA  ASP A 229     -26.925 -46.511 -36.395  1.00 16.07           C
ANISOU 1587  CA  ASP A 229     2035   1933   2136     37     52     83       C
ATOM   1588  C   ASP A 229     -25.496 -46.824 -35.937  1.00 15.98           C
ANISOU 1588  C   ASP A 229     2008   1931   2133     41     62     92       C
ATOM   1589  O   ASP A 229     -24.588 -46.936 -36.760  1.00 16.28           O
ANISOU 1589  O   ASP A 229     2047   1975   2163     68     79     98       O
ATOM   1590  CB  ASP A 229     -26.982 -45.180 -37.186  1.00 16.35           C
ANISOU 1590  CB  ASP A 229     2071   1974   2166     48     77     94       C
ATOM   1591  CG  ASP A 229     -26.653 -43.949 -36.347  1.00 17.21           C
ANISOU 1591  CG  ASP A 229     2159   2082   2298     21     97    101       C
ATOM   1592  OD1 ASP A 229     -26.237 -44.074 -35.177  1.00 16.24           O
ANISOU 1592  OD1 ASP A 229     2018   1963   2189     -3     89     95       O
ATOM   1593  OD2 ASP A 229     -26.829 -42.822 -36.879  1.00 19.43           O
ANISOU 1593  OD2 ASP A 229     2443   2357   2583     26    120    113       O
ATOM   1594  N   LEU A 230     -25.317 -46.981 -34.626  1.00 15.26           N
ANISOU 1594  N   LEU A 230     1900   1844   2052     19     52     93       N
ATOM   1595  CA  LEU A 230     -24.018 -47.244 -34.005  1.00 15.43           C
ANISOU 1595  CA  LEU A 230     1900   1883   2080     23     54     99       C
ATOM   1596  C   LEU A 230     -22.973 -46.137 -34.255  1.00 15.44           C
ANISOU 1596  C   LEU A 230     1872   1899   2096     17     78    103       C
ATOM   1597  O   LEU A 230     -21.770 -46.394 -34.251  1.00 15.47           O
ANISOU 1597  O   LEU A 230     1852   1920   2107     30     85    108       O
ATOM   1598  CB  LEU A 230     -23.490 -48.640 -34.393  1.00 15.59           C
ANISOU 1598  CB  LEU A 230     1934   1896   2092     55     47    103       C
ATOM   1599  CG  LEU A 230     -23.961 -49.798 -33.504  1.00 16.51           C
ANISOU 1599  CG  LEU A 230     2065   1998   2210     53     25    107       C
ATOM   1600  CD1 LEU A 230     -25.499 -49.858 -33.355  1.00 16.14           C
ANISOU 1600  CD1 LEU A 230     2035   1930   2166     28     14    103       C
ATOM   1601  CD2 LEU A 230     -23.436 -51.117 -34.041  1.00 16.97           C
ANISOU 1601  CD2 LEU A 230     2144   2038   2266     89     20    109       C
ATOM   1602  N   ASN A 231     -23.433 -44.894 -34.397  1.00 15.56           N
ANISOU 1602  N   ASN A 231     1884   1905   2122     -2     93    100       N
ATOM   1603  CA  ASN A 231     -22.521 -43.748 -34.519  1.00 15.75           C
ANISOU 1603  CA  ASN A 231     1879   1932   2173    -18    118    104       C
ATOM   1604  C   ASN A 231     -21.647 -43.570 -33.279  1.00 15.91           C
ANISOU 1604  C   ASN A 231     1862   1972   2213    -42    102     89       C
ATOM   1605  O   ASN A 231     -20.591 -42.931 -33.345  1.00 15.99           O
ANISOU 1605  O   ASN A 231     1835   1988   2253    -56    118     90       O
ATOM   1606  CB  ASN A 231     -23.290 -42.448 -34.794  1.00 16.11           C
ANISOU 1606  CB  ASN A 231     1935   1954   2231    -33    137    105       C
ATOM   1607  CG  ASN A 231     -23.978 -41.898 -33.553  1.00 16.29           C
ANISOU 1607  CG  ASN A 231     1957   1972   2259    -61    117     82       C
ATOM   1608  OD1 ASN A 231     -23.341 -41.267 -32.706  1.00 18.29           O
ANISOU 1608  OD1 ASN A 231     2184   2229   2536    -87    113     64       O
ATOM   1609  ND2 ASN A 231     -25.278 -42.135 -33.438  1.00 15.75           N
ANISOU 1609  ND2 ASN A 231     1914   1900   2170    -54    105     79       N
ATOM   1610  N   HIS A 232     -22.088 -44.128 -32.151  1.00 15.73           N
ANISOU 1610  N   HIS A 232     1844   1960   2171    -46     71     76       N
ATOM   1611  CA  HIS A 232     -21.318 -44.056 -30.914  1.00 15.66           C
ANISOU 1611  CA  HIS A 232     1804   1980   2167    -59     48     59       C
ATOM   1612  C   HIS A 232     -20.096 -44.970 -30.942  1.00 16.01           C
ANISOU 1612  C   HIS A 232     1823   2052   2210    -35     41     70       C
ATOM   1613  O   HIS A 232     -19.208 -44.850 -30.090  1.00 16.36           O
ANISOU 1613  O   HIS A 232     1829   2128   2261    -41     21     56       O
ATOM   1614  CB  HIS A 232     -22.206 -44.308 -29.683  1.00 15.69           C
ANISOU 1614  CB  HIS A 232     1825   1993   2142    -62     23     48       C
ATOM   1615  CG  HIS A 232     -22.794 -45.684 -29.604  1.00 15.12           C
ANISOU 1615  CG  HIS A 232     1781   1921   2044    -37     15     70       C
ATOM   1616  ND1 HIS A 232     -23.143 -46.423 -30.716  1.00 15.48           N
ANISOU 1616  ND1 HIS A 232     1850   1942   2090    -20     27     87       N
ATOM   1617  CD2 HIS A 232     -23.156 -46.427 -28.530  1.00 15.73           C
ANISOU 1617  CD2 HIS A 232     1868   2014   2095    -27     -2     78       C
ATOM   1618  CE1 HIS A 232     -23.654 -47.578 -30.327  1.00 16.76           C
ANISOU 1618  CE1 HIS A 232     2032   2098   2237     -6     15    101       C
ATOM   1619  NE2 HIS A 232     -23.681 -47.602 -29.006  1.00 15.46           N
ANISOU 1619  NE2 HIS A 232     1860   1957   2056    -10      1    102       N
ATOM   1620  N   ILE A 233     -20.053 -45.856 -31.939  1.00 15.99           N
ANISOU 1620  N   ILE A 233     1838   2039   2198     -4     56     91       N
ATOM   1621  CA  ILE A 233     -18.882 -46.671 -32.244  1.00 16.31           C
ANISOU 1621  CA  ILE A 233     1857   2101   2239     28     58    104       C
ATOM   1622  C   ILE A 233     -18.122 -46.135 -33.471  1.00 16.43           C
ANISOU 1622  C   ILE A 233     1851   2116   2278     34     97    117       C
ATOM   1623  O   ILE A 233     -16.898 -46.028 -33.451  1.00 16.62           O
ANISOU 1623  O   ILE A 233     1825   2167   2322     38    105    121       O
ATOM   1624  CB  ILE A 233     -19.307 -48.138 -32.503  1.00 16.45           C
ANISOU 1624  CB  ILE A 233     1915   2104   2231     67     50    117       C
ATOM   1625  CG1 ILE A 233     -19.878 -48.750 -31.222  1.00 17.04           C
ANISOU 1625  CG1 ILE A 233     2005   2182   2288     64     21    118       C
ATOM   1626  CG2 ILE A 233     -18.119 -48.958 -33.049  1.00 16.52           C
ANISOU 1626  CG2 ILE A 233     1907   2129   2239    110     60    131       C
ATOM   1627  CD1 ILE A 233     -20.761 -49.977 -31.438  1.00 17.91           C
ANISOU 1627  CD1 ILE A 233     2163   2257   2385     84     16    130       C
ATOM   1628  N   TYR A 234     -18.853 -45.775 -34.524  1.00 16.52           N
ANISOU 1628  N   TYR A 234     1895   2100   2283     38    122    125       N
ATOM   1629  CA  TYR A 234     -18.243 -45.463 -35.821  1.00 16.94           C
ANISOU 1629  CA  TYR A 234     1939   2155   2344     58    165    146       C
ATOM   1630  C   TYR A 234     -18.085 -43.971 -36.126  1.00 17.81           C
ANISOU 1630  C   TYR A 234     2025   2252   2490     24    198    156       C
ATOM   1631  O   TYR A 234     -17.436 -43.607 -37.107  1.00 18.20           O
ANISOU 1631  O   TYR A 234     2058   2305   2550     38    242    182       O
ATOM   1632  CB  TYR A 234     -19.072 -46.117 -36.923  1.00 16.86           C
ANISOU 1632  CB  TYR A 234     1983   2127   2295     97    171    151       C
ATOM   1633  CG  TYR A 234     -19.150 -47.619 -36.800  1.00 16.67           C
ANISOU 1633  CG  TYR A 234     1986   2103   2246    131    145    141       C
ATOM   1634  CD1 TYR A 234     -18.020 -48.414 -37.011  1.00 16.89           C
ANISOU 1634  CD1 TYR A 234     1995   2151   2272    170    154    150       C
ATOM   1635  CD2 TYR A 234     -20.345 -48.253 -36.480  1.00 16.47           C
ANISOU 1635  CD2 TYR A 234     2001   2053   2205    126    113    126       C
ATOM   1636  CE1 TYR A 234     -18.081 -49.796 -36.904  1.00 17.33           C
ANISOU 1636  CE1 TYR A 234     2079   2196   2309    205    132    142       C
ATOM   1637  CE2 TYR A 234     -20.416 -49.637 -36.368  1.00 16.93           C
ANISOU 1637  CE2 TYR A 234     2084   2098   2251    154     92    119       C
ATOM   1638  CZ  TYR A 234     -19.284 -50.403 -36.581  1.00 17.48           C
ANISOU 1638  CZ  TYR A 234     2142   2181   2317    195    101    126       C
ATOM   1639  OH  TYR A 234     -19.366 -51.769 -36.479  1.00 17.98           O
ANISOU 1639  OH  TYR A 234     2235   2222   2372    225     82    120       O
ATOM   1640  N   GLY A 235     -18.691 -43.114 -35.307  1.00 18.23           N
ANISOU 1640  N   GLY A 235     2079   2287   2560    -18    181    137       N
ATOM   1641  CA  GLY A 235     -18.699 -41.678 -35.554  1.00 18.99           C
ANISOU 1641  CA  GLY A 235     2162   2357   2695    -51    212    143       C
ATOM   1642  C   GLY A 235     -19.946 -41.231 -36.297  1.00 19.56           C
ANISOU 1642  C   GLY A 235     2286   2400   2747    -38    228    155       C
ATOM   1643  O   GLY A 235     -20.475 -41.954 -37.142  1.00 19.57           O
ANISOU 1643  O   GLY A 235     2323   2407   2706      3    230    167       O
ATOM   1644  N   GLU A 236     -20.413 -40.028 -35.977  1.00 20.27           N
ANISOU 1644  N   GLU A 236     2379   2459   2865    -70    236    148       N
ATOM   1645  CA  GLU A 236     -21.589 -39.441 -36.620  1.00 20.95           C
ANISOU 1645  CA  GLU A 236     2508   2518   2934    -55    251    162       C
ATOM   1646  C   GLU A 236     -21.299 -39.073 -38.080  1.00 21.81           C
ANISOU 1646  C   GLU A 236     2626   2619   3040    -24    304    208       C
ATOM   1647  O   GLU A 236     -22.155 -39.262 -38.951  1.00 22.45           O
ANISOU 1647  O   GLU A 236     2748   2704   3079     17    308    224       O
ATOM   1648  CB  GLU A 236     -22.042 -38.211 -35.820  1.00 21.35           C
ANISOU 1648  CB  GLU A 236     2557   2533   3021    -93    249    141       C
ATOM   1649  CG  GLU A 236     -23.246 -37.450 -36.367  1.00 22.37           C
ANISOU 1649  CG  GLU A 236     2727   2633   3139    -75    266    156       C
ATOM   1650  CD  GLU A 236     -24.568 -38.208 -36.285  1.00 22.70           C
ANISOU 1650  CD  GLU A 236     2802   2695   3129    -48    232    144       C
ATOM   1651  OE1 GLU A 236     -25.414 -37.984 -37.180  1.00 23.60           O
ANISOU 1651  OE1 GLU A 236     2945   2802   3220    -15    245    166       O
ATOM   1652  OE2 GLU A 236     -24.782 -38.990 -35.331  1.00 21.35           O
ANISOU 1652  OE2 GLU A 236     2626   2545   2943    -59    194    116       O
ATOM   1653  N   THR A 237     -20.089 -38.575 -38.342  1.00 21.97           N
ANISOU 1653  N   THR A 237     2607   2636   3104    -40    343    231       N
ATOM   1654  CA  THR A 237     -19.697 -38.090 -39.663  1.00 22.72           C
ANISOU 1654  CA  THR A 237     2706   2725   3201    -11    405    285       C
ATOM   1655  C   THR A 237     -18.660 -38.998 -40.329  1.00 22.55           C
ANISOU 1655  C   THR A 237     2662   2745   3161     22    426    305       C
ATOM   1656  O   THR A 237     -17.917 -39.722 -39.657  1.00 21.48           O
ANISOU 1656  O   THR A 237     2491   2635   3036      9    399    281       O
ATOM   1657  CB  THR A 237     -19.083 -36.671 -39.576  1.00 23.47           C
ANISOU 1657  CB  THR A 237     2769   2776   3374    -57    451    307       C
ATOM   1658  OG1 THR A 237     -17.854 -36.725 -38.839  1.00 25.56           O
ANISOU 1658  OG1 THR A 237     2968   3050   3692   -102    444    288       O
ATOM   1659  CG2 THR A 237     -20.037 -35.693 -38.888  1.00 24.38           C
ANISOU 1659  CG2 THR A 237     2908   2843   3513    -87    434    283       C
ATOM   1660  N   LEU A 238     -18.599 -38.927 -41.655  1.00 22.66           N
ANISOU 1660  N   LEU A 238     2698   2768   3143     72    475    352       N
ATOM   1661  CA  LEU A 238     -17.637 -39.711 -42.432  1.00 23.07           C
ANISOU 1661  CA  LEU A 238     2733   2861   3171    116    505    375       C
ATOM   1662  C   LEU A 238     -16.180 -39.375 -42.066  1.00 23.36           C
ANISOU 1662  C   LEU A 238     2694   2904   3278     77    538    392       C
ATOM   1663  O   LEU A 238     -15.330 -40.263 -41.995  1.00 23.36           O
ANISOU 1663  O   LEU A 238     2662   2942   3271     95    532    385       O
ATOM   1664  CB  LEU A 238     -17.882 -39.494 -43.932  1.00 23.67           C
ANISOU 1664  CB  LEU A 238     2849   2948   3195    181    558    426       C
ATOM   1665  CG  LEU A 238     -17.279 -40.513 -44.898  1.00 24.38           C
ANISOU 1665  CG  LEU A 238     2947   3088   3228    251    579    439       C
ATOM   1666  CD1 LEU A 238     -17.735 -41.931 -44.563  1.00 23.03           C
ANISOU 1666  CD1 LEU A 238     2804   2937   3009    274    510    381       C
ATOM   1667  CD2 LEU A 238     -17.656 -40.152 -46.339  1.00 25.89           C
ANISOU 1667  CD2 LEU A 238     3185   3293   3359    320    630    488       C
ATOM   1668  N   ASP A 239     -15.899 -38.093 -41.830  1.00 23.87           N
ANISOU 1668  N   ASP A 239     2728   2928   3415     24    571    412       N
ATOM   1669  CA  ASP A 239     -14.553 -37.648 -41.450  1.00 24.78           C
ANISOU 1669  CA  ASP A 239     2760   3043   3610    -25    600    423       C
ATOM   1670  C   ASP A 239     -14.082 -38.336 -40.159  1.00 23.44           C
ANISOU 1670  C   ASP A 239     2548   2900   3458    -58    532    363       C
ATOM   1671  O   ASP A 239     -12.956 -38.826 -40.088  1.00 23.69           O
ANISOU 1671  O   ASP A 239     2520   2971   3510    -56    540    368       O
ATOM   1672  CB  ASP A 239     -14.521 -36.123 -41.294  1.00 26.06           C
ANISOU 1672  CB  ASP A 239     2905   3143   3855    -86    637    443       C
ATOM   1673  CG  ASP A 239     -13.229 -35.615 -40.671  1.00 30.48           C
ANISOU 1673  CG  ASP A 239     3373   3696   4514   -154    649    436       C
ATOM   1674  OD1 ASP A 239     -13.315 -34.913 -39.637  1.00 36.62           O
ANISOU 1674  OD1 ASP A 239     4130   4433   5350   -220    612    390       O
ATOM   1675  OD2 ASP A 239     -12.134 -35.906 -41.210  1.00 35.46           O
ANISOU 1675  OD2 ASP A 239     3948   4362   5162   -141    694    473       O
ATOM   1676  N   ARG A 240     -14.954 -38.385 -39.156  1.00 21.87           N
ANISOU 1676  N   ARG A 240     2378   2685   3246    -82    468    311       N
ATOM   1677  CA  ARG A 240     -14.643 -39.051 -37.888  1.00 20.92           C
ANISOU 1677  CA  ARG A 240     2228   2593   3129   -104    403    258       C
ATOM   1678  C   ARG A 240     -14.477 -40.568 -38.080  1.00 20.09           C
ANISOU 1678  C   ARG A 240     2135   2537   2961    -44    381    256       C
ATOM   1679  O   ARG A 240     -13.535 -41.172 -37.565  1.00 20.36           O
ANISOU 1679  O   ARG A 240     2119   2609   3007    -43    362    244       O
ATOM   1680  CB  ARG A 240     -15.755 -38.773 -36.867  1.00 20.58           C
ANISOU 1680  CB  ARG A 240     2222   2523   3073   -130    349    211       C
ATOM   1681  CG  ARG A 240     -15.388 -39.111 -35.437  1.00 20.72           C
ANISOU 1681  CG  ARG A 240     2204   2566   3101   -160    287    158       C
ATOM   1682  CD  ARG A 240     -16.509 -38.716 -34.481  1.00 20.86           C
ANISOU 1682  CD  ARG A 240     2263   2559   3104   -181    245    117       C
ATOM   1683  NE  ARG A 240     -16.196 -39.096 -33.106  1.00 20.88           N
ANISOU 1683  NE  ARG A 240     2237   2594   3101   -198    185     69       N
ATOM   1684  CZ  ARG A 240     -15.504 -38.357 -32.245  1.00 20.77           C
ANISOU 1684  CZ  ARG A 240     2172   2580   3138   -246    163     30       C
ATOM   1685  NH1 ARG A 240     -15.037 -37.162 -32.589  1.00 22.46           N
ANISOU 1685  NH1 ARG A 240     2355   2753   3426   -291    197     33       N
ATOM   1686  NH2 ARG A 240     -15.278 -38.819 -31.022  1.00 20.05           N
ANISOU 1686  NH2 ARG A 240     2062   2529   3025   -247    104    -13       N
ATOM   1687  N   GLN A 241     -15.400 -41.179 -38.818  1.00 19.11           N
ANISOU 1687  N   GLN A 241     2079   2411   2772      7    382    266       N
ATOM   1688  CA  GLN A 241     -15.321 -42.613 -39.121  1.00 18.84           C
ANISOU 1688  CA  GLN A 241     2066   2410   2681     65    364    261       C
ATOM   1689  C   GLN A 241     -13.990 -42.979 -39.759  1.00 19.57           C
ANISOU 1689  C   GLN A 241     2112   2541   2784     97    407    291       C
ATOM   1690  O   GLN A 241     -13.363 -43.969 -39.387  1.00 18.96           O
ANISOU 1690  O   GLN A 241     2012   2495   2696    122    384    278       O
ATOM   1691  CB  GLN A 241     -16.457 -43.025 -40.061  1.00 18.69           C
ANISOU 1691  CB  GLN A 241     2123   2380   2599    112    366    266       C
ATOM   1692  CG  GLN A 241     -16.499 -44.525 -40.391  1.00 18.53           C
ANISOU 1692  CG  GLN A 241     2134   2381   2524    170    343    251       C
ATOM   1693  CD  GLN A 241     -17.184 -44.802 -41.715  1.00 18.67           C
ANISOU 1693  CD  GLN A 241     2211   2399   2485    226    361    260       C
ATOM   1694  OE1 GLN A 241     -16.542 -45.196 -42.697  1.00 19.71           O
ANISOU 1694  OE1 GLN A 241     2345   2556   2589    281    398    280       O
ATOM   1695  NE2 GLN A 241     -18.487 -44.564 -41.760  1.00 18.19           N
ANISOU 1695  NE2 GLN A 241     2195   2314   2403    217    335    245       N
ATOM   1696  N   HIS A 242     -13.562 -42.179 -40.725  1.00 20.47           N
ANISOU 1696  N   HIS A 242     2209   2651   2919    102    474    336       N
ATOM   1697  CA  HIS A 242     -12.340 -42.479 -41.452  1.00 21.60           C
ANISOU 1697  CA  HIS A 242     2304   2833   3068    139    527    373       C
ATOM   1698  C   HIS A 242     -11.092 -42.339 -40.577  1.00 22.18           C
ANISOU 1698  C   HIS A 242     2285   2932   3212     96    519    366       C
ATOM   1699  O   HIS A 242     -10.126 -43.072 -40.773  1.00 23.34           O
ANISOU 1699  O   HIS A 242     2390   3123   3354    135    533    377       O
ATOM   1700  CB  HIS A 242     -12.276 -41.652 -42.739  1.00 22.21           C
ANISOU 1700  CB  HIS A 242     2392   2903   3146    160    607    433       C
ATOM   1701  CG  HIS A 242     -13.176 -42.176 -43.817  1.00 23.92           C
ANISOU 1701  CG  HIS A 242     2692   3123   3273    233    615    440       C
ATOM   1702  ND1 HIS A 242     -13.170 -41.683 -45.104  1.00 26.54           N
ANISOU 1702  ND1 HIS A 242     3047   3462   3577    278    685    495       N
ATOM   1703  CD2 HIS A 242     -14.085 -43.181 -43.803  1.00 24.02           C
ANISOU 1703  CD2 HIS A 242     2770   3137   3220    270    559    398       C
ATOM   1704  CE1 HIS A 242     -14.055 -42.344 -45.829  1.00 26.63           C
ANISOU 1704  CE1 HIS A 242     3134   3483   3503    342    665    479       C
ATOM   1705  NE2 HIS A 242     -14.613 -43.270 -45.068  1.00 25.08           N
ANISOU 1705  NE2 HIS A 242     2962   3281   3288    334    589    419       N
ATOM   1706  N   LYS A 243     -11.129 -41.447 -39.588  1.00 21.86           N
ANISOU 1706  N   LYS A 243     2209   2864   3232     21    491    341       N
ATOM   1707  CA  LYS A 243     -10.033 -41.325 -38.616  1.00 22.28           C
ANISOU 1707  CA  LYS A 243     2173   2945   3349    -24    465    319       C
ATOM   1708  C   LYS A 243      -9.981 -42.510 -37.642  1.00 21.44           C
ANISOU 1708  C   LYS A 243     2068   2876   3203      2    394    276       C
ATOM   1709  O   LYS A 243      -8.924 -42.814 -37.089  1.00 21.38           O
ANISOU 1709  O   LYS A 243     1987   2912   3225     -1    376    267       O
ATOM   1710  CB  LYS A 243     -10.167 -40.033 -37.800  1.00 22.77           C
ANISOU 1710  CB  LYS A 243     2206   2965   3482   -109    447    292       C
ATOM   1711  CG  LYS A 243      -9.869 -38.747 -38.552  1.00 25.30           C
ANISOU 1711  CG  LYS A 243     2498   3244   3872   -149    521    336       C
ATOM   1712  CD  LYS A 243     -10.317 -37.560 -37.699  1.00 27.24           C
ANISOU 1712  CD  LYS A 243     2742   3431   4176   -227    492    297       C
ATOM   1713  CE  LYS A 243      -9.701 -36.250 -38.122  1.00 30.48           C
ANISOU 1713  CE  LYS A 243     3099   3795   4686   -286    556    332       C
ATOM   1714  NZ  LYS A 243     -10.161 -35.188 -37.175  1.00 31.12           N
ANISOU 1714  NZ  LYS A 243     3185   3816   4823   -358    518    280       N
ATOM   1715  N   LEU A 244     -11.127 -43.148 -37.417  1.00 20.37           N
ANISOU 1715  N   LEU A 244     2013   2722   3005     27    354    254       N
ATOM   1716  CA  LEU A 244     -11.224 -44.293 -36.510  1.00 19.87           C
ANISOU 1716  CA  LEU A 244     1964   2683   2902     54    292    222       C
ATOM   1717  C   LEU A 244     -10.900 -45.625 -37.194  1.00 19.93           C
ANISOU 1717  C   LEU A 244     1993   2717   2862    134    306    241       C
ATOM   1718  O   LEU A 244     -10.666 -46.624 -36.515  1.00 19.60           O
ANISOU 1718  O   LEU A 244     1950   2699   2799    163    265    225       O
ATOM   1719  CB  LEU A 244     -12.623 -44.359 -35.893  1.00 19.28           C
ANISOU 1719  CB  LEU A 244     1960   2572   2791     40    248    193       C
ATOM   1720  CG  LEU A 244     -12.949 -43.249 -34.891  1.00 18.93           C
ANISOU 1720  CG  LEU A 244     1899   2509   2785    -29    219    162       C
ATOM   1721  CD1 LEU A 244     -14.429 -43.239 -34.560  1.00 18.51           C
ANISOU 1721  CD1 LEU A 244     1919   2420   2693    -34    194    144       C
ATOM   1722  CD2 LEU A 244     -12.111 -43.416 -33.626  1.00 19.91           C
ANISOU 1722  CD2 LEU A 244     1961   2674   2928    -46    170    130       C
ATOM   1723  N   ARG A 245     -10.882 -45.636 -38.525  1.00 19.91           N
ANISOU 1723  N   ARG A 245     2014   2710   2840    172    363    274       N
ATOM   1724  CA  ARG A 245     -10.704 -46.877 -39.287  1.00 20.11           C
ANISOU 1724  CA  ARG A 245     2075   2754   2814    254    377    283       C
ATOM   1725  C   ARG A 245      -9.239 -47.191 -39.595  1.00 20.91           C
ANISOU 1725  C   ARG A 245     2101   2907   2935    292    414    309       C
ATOM   1726  O   ARG A 245      -8.410 -46.291 -39.785  1.00 21.38           O
ANISOU 1726  O   ARG A 245     2088   2987   3049    260    456    335       O
ATOM   1727  CB  ARG A 245     -11.536 -46.846 -40.580  1.00 20.09           C
ANISOU 1727  CB  ARG A 245     2144   2726   2762    290    412    297       C
ATOM   1728  CG  ARG A 245     -13.010 -47.180 -40.363  1.00 18.36           C
ANISOU 1728  CG  ARG A 245     2006   2465   2504    283    364    264       C
ATOM   1729  CD  ARG A 245     -13.833 -47.020 -41.626  1.00 18.11           C
ANISOU 1729  CD  ARG A 245     2038   2417   2427    316    392    274       C
ATOM   1730  NE  ARG A 245     -13.395 -47.896 -42.707  1.00 18.56           N
ANISOU 1730  NE  ARG A 245     2118   2497   2435    397    421    281       N
ATOM   1731  CZ  ARG A 245     -13.853 -47.845 -43.956  1.00 19.13           C
ANISOU 1731  CZ  ARG A 245     2241   2571   2457    444    451    290       C
ATOM   1732  NH1 ARG A 245     -14.779 -46.961 -44.302  1.00 18.97           N
ANISOU 1732  NH1 ARG A 245     2250   2531   2428    420    455    298       N
ATOM   1733  NH2 ARG A 245     -13.371 -48.682 -44.874  1.00 20.93           N
ANISOU 1733  NH2 ARG A 245     2490   2824   2637    524    476    290       N
ATOM   1734  N   LEU A 246      -8.934 -48.485 -39.645  1.00 21.33           N
ANISOU 1734  N   LEU A 246     2173   2979   2951    360    400    302       N
ATOM   1735  CA  LEU A 246      -7.587 -48.977 -39.968  1.00 22.37           C
ANISOU 1735  CA  LEU A 246     2241   3164   3093    414    434    325       C
ATOM   1736  C   LEU A 246      -7.347 -49.019 -41.478  1.00 23.00           C
ANISOU 1736  C   LEU A 246     2340   3256   3142    475    509    358       C
ATOM   1737  O   LEU A 246      -6.207 -48.926 -41.935  1.00 23.44           O
ANISOU 1737  O   LEU A 246     2327   3360   3220    503    562    391       O
ATOM   1738  CB  LEU A 246      -7.403 -50.385 -39.387  1.00 22.69           C
ANISOU 1738  CB  LEU A 246     2302   3215   3103    473    389    305       C
ATOM   1739  CG  LEU A 246      -6.043 -51.079 -39.495  1.00 24.42           C
ANISOU 1739  CG  LEU A 246     2456   3492   3331    539    412    323       C
ATOM   1740  CD1 LEU A 246      -4.956 -50.285 -38.781  1.00 26.16           C
ANISOU 1740  CD1 LEU A 246     2555   3763   3619    490    410    335       C
ATOM   1741  CD2 LEU A 246      -6.137 -52.499 -38.933  1.00 25.78           C
ANISOU 1741  CD2 LEU A 246     2673   3653   3468    600    365    304       C
ATOM   1742  N   PHE A 247      -8.429 -49.170 -42.239  1.00 22.80           N
ANISOU 1742  N   PHE A 247     2407   3193   3062    497    512    348       N
ATOM   1743  CA  PHE A 247      -8.385 -49.351 -43.696  1.00 23.54           C
ANISOU 1743  CA  PHE A 247     2540   3300   3104    569    573    370       C
ATOM   1744  C   PHE A 247      -7.653 -50.622 -44.159  1.00 24.23           C
ANISOU 1744  C   PHE A 247     2635   3419   3152    666    587    365       C
ATOM   1745  O   PHE A 247      -7.202 -50.720 -45.304  1.00 24.70           O
ANISOU 1745  O   PHE A 247     2701   3510   3176    734    650    390       O
ATOM   1746  CB  PHE A 247      -7.869 -48.090 -44.392  1.00 24.07           C
ANISOU 1746  CB  PHE A 247     2554   3389   3203    545    649    425       C
ATOM   1747  CG  PHE A 247      -8.833 -46.953 -44.307  1.00 24.26           C
ANISOU 1747  CG  PHE A 247     2604   3369   3245    475    643    428       C
ATOM   1748  CD1 PHE A 247      -8.604 -45.892 -43.445  1.00 24.77           C
ANISOU 1748  CD1 PHE A 247     2603   3421   3389    385    636    435       C
ATOM   1749  CD2 PHE A 247     -10.009 -46.978 -45.042  1.00 24.64           C
ANISOU 1749  CD2 PHE A 247     2743   3389   3231    501    637    417       C
ATOM   1750  CE1 PHE A 247      -9.516 -44.862 -43.347  1.00 25.01           C
ANISOU 1750  CE1 PHE A 247     2663   3405   3435    327    630    436       C
ATOM   1751  CE2 PHE A 247     -10.923 -45.949 -44.948  1.00 25.40           C
ANISOU 1751  CE2 PHE A 247     2864   3447   3342    443    630    422       C
ATOM   1752  CZ  PHE A 247     -10.673 -44.887 -44.097  1.00 24.98           C
ANISOU 1752  CZ  PHE A 247     2748   3375   3368    358    629    433       C
ATOM   1753  N   LYS A 248      -7.575 -51.597 -43.262  1.00 24.39           N
ANISOU 1753  N   LYS A 248     2661   3430   3177    678    531    334       N
ATOM   1754  CA  LYS A 248      -7.179 -52.948 -43.608  1.00 25.26           C
ANISOU 1754  CA  LYS A 248     2804   3548   3246    772    530    319       C
ATOM   1755  C   LYS A 248      -8.207 -53.902 -43.003  1.00 24.17           C
ANISOU 1755  C   LYS A 248     2747   3349   3087    769    458    271       C
ATOM   1756  O   LYS A 248      -8.578 -53.755 -41.834  1.00 23.75           O
ANISOU 1756  O   LYS A 248     2681   3276   3067    706    407    262       O
ATOM   1757  CB  LYS A 248      -5.783 -53.251 -43.066  1.00 26.27           C
ANISOU 1757  CB  LYS A 248     2839   3731   3413    799    543    341       C
ATOM   1758  CG  LYS A 248      -5.314 -54.663 -43.349  1.00 29.22           C
ANISOU 1758  CG  LYS A 248     3245   4109   3748    903    544    327       C
ATOM   1759  CD  LYS A 248      -3.801 -54.787 -43.294  1.00 33.08           C
ANISOU 1759  CD  LYS A 248     3633   4671   4267    951    585    361       C
ATOM   1760  CE  LYS A 248      -3.340 -56.139 -43.819  1.00 35.09           C
ANISOU 1760  CE  LYS A 248     3928   4929   4476   1071    600    349       C
ATOM   1761  NZ  LYS A 248      -3.824 -57.260 -42.972  1.00 37.01           N
ANISOU 1761  NZ  LYS A 248     4232   5118   4711   1088    530    313       N
ATOM   1762  N   ASP A 249      -8.684 -54.846 -43.817  1.00 23.95           N
ANISOU 1762  N   ASP A 249     2804   3292   3006    837    456    241       N
ATOM   1763  CA  ASP A 249      -9.576 -55.928 -43.377  1.00 23.30           C
ANISOU 1763  CA  ASP A 249     2799   3145   2909    843    394    197       C
ATOM   1764  C   ASP A 249     -10.888 -55.455 -42.735  1.00 21.71           C
ANISOU 1764  C   ASP A 249     2629   2897   2723    756    345    179       C
ATOM   1765  O   ASP A 249     -11.516 -56.197 -41.983  1.00 20.73           O
ANISOU 1765  O   ASP A 249     2543   2725   2609    740    295    156       O
ATOM   1766  CB  ASP A 249      -8.824 -56.881 -42.435  1.00 23.86           C
ANISOU 1766  CB  ASP A 249     2843   3217   3005    876    371    201       C
ATOM   1767  CG  ASP A 249      -7.670 -57.601 -43.128  1.00 26.15           C
ANISOU 1767  CG  ASP A 249     3118   3544   3275    979    416    210       C
ATOM   1768  OD1 ASP A 249      -6.755 -58.075 -42.428  1.00 28.12           O
ANISOU 1768  OD1 ASP A 249     3317   3819   3549   1009    412    228       O
ATOM   1769  OD2 ASP A 249      -7.675 -57.691 -44.370  1.00 27.42           O
ANISOU 1769  OD2 ASP A 249     3316   3713   3390   1036    456    198       O
ATOM   1770  N   GLY A 250     -11.298 -54.228 -43.055  1.00 20.95           N
ANISOU 1770  N   GLY A 250     2517   2814   2630    704    364    194       N
ATOM   1771  CA  GLY A 250     -12.539 -53.652 -42.545  1.00 19.78           C
ANISOU 1771  CA  GLY A 250     2394   2628   2493    628    324    180       C
ATOM   1772  C   GLY A 250     -12.478 -53.129 -41.123  1.00 19.20           C
ANISOU 1772  C   GLY A 250     2268   2556   2469    555    295    192       C
ATOM   1773  O   GLY A 250     -13.483 -52.659 -40.583  1.00 18.19           O
ANISOU 1773  O   GLY A 250     2159   2401   2353    494    263    181       O
ATOM   1774  N   LYS A 251     -11.294 -53.162 -40.521  1.00 19.47           N
ANISOU 1774  N   LYS A 251     2234   2631   2533    564    305    214       N
ATOM   1775  CA  LYS A 251     -11.187 -53.021 -39.073  1.00 19.25           C
ANISOU 1775  CA  LYS A 251     2165   2608   2541    514    264    216       C
ATOM   1776  C   LYS A 251     -11.142 -51.577 -38.591  1.00 19.22           C
ANISOU 1776  C   LYS A 251     2103   2624   2575    437    268    227       C
ATOM   1777  O   LYS A 251     -10.893 -50.645 -39.363  1.00 19.41           O
ANISOU 1777  O   LYS A 251     2102   2664   2610    424    313    244       O
ATOM   1778  CB  LYS A 251      -9.973 -53.806 -38.554  1.00 19.81           C
ANISOU 1778  CB  LYS A 251     2188   2716   2622    565    260    228       C
ATOM   1779  CG  LYS A 251     -10.190 -55.317 -38.617  1.00 20.54           C
ANISOU 1779  CG  LYS A 251     2347   2770   2686    632    241    214       C
ATOM   1780  CD  LYS A 251      -9.009 -56.097 -38.071  1.00 20.87           C
ANISOU 1780  CD  LYS A 251     2345   2848   2738    691    238    231       C
ATOM   1781  CE  LYS A 251      -9.273 -57.590 -38.106  1.00 21.59           C
ANISOU 1781  CE  LYS A 251     2509   2887   2807    757    221    218       C
ATOM   1782  NZ  LYS A 251      -8.154 -58.389 -37.521  1.00 23.00           N
ANISOU 1782  NZ  LYS A 251     2648   3098   2993    823    217    239       N
ATOM   1783  N   LEU A 252     -11.425 -51.416 -37.301  1.00 19.02           N
ANISOU 1783  N   LEU A 252     2063   2595   2568    390    222    216       N
ATOM   1784  CA  LEU A 252     -11.218 -50.165 -36.579  1.00 18.68           C
ANISOU 1784  CA  LEU A 252     1960   2572   2566    320    215    216       C
ATOM   1785  C   LEU A 252      -9.831 -50.172 -35.952  1.00 19.12           C
ANISOU 1785  C   LEU A 252     1928   2685   2653    329    209    224       C
ATOM   1786  O   LEU A 252      -9.338 -51.220 -35.535  1.00 19.15           O
ANISOU 1786  O   LEU A 252     1927   2707   2640    380    189    227       O
ATOM   1787  CB  LEU A 252     -12.275 -50.023 -35.482  1.00 18.37           C
ANISOU 1787  CB  LEU A 252     1954   2505   2521    273    165    193       C
ATOM   1788  CG  LEU A 252     -13.710 -49.736 -35.916  1.00 17.53           C
ANISOU 1788  CG  LEU A 252     1916   2348   2395    248    166    183       C
ATOM   1789  CD1 LEU A 252     -14.679 -49.990 -34.769  1.00 17.53           C
ANISOU 1789  CD1 LEU A 252     1948   2326   2385    220    119    166       C
ATOM   1790  CD2 LEU A 252     -13.828 -48.294 -36.423  1.00 18.26           C
ANISOU 1790  CD2 LEU A 252     1987   2437   2514    202    198    188       C
ATOM   1791  N   LYS A 253      -9.203 -49.001 -35.880  1.00 19.21           N
ANISOU 1791  N   LYS A 253     1866   2722   2712    279    227    229       N
ATOM   1792  CA  LYS A 253      -7.920 -48.855 -35.200  1.00 20.18           C
ANISOU 1792  CA  LYS A 253     1891   2903   2874    274    213    230       C
ATOM   1793  C   LYS A 253      -8.034 -49.188 -33.719  1.00 19.77           C
ANISOU 1793  C   LYS A 253     1834   2868   2811    263    143    203       C
ATOM   1794  O   LYS A 253      -9.096 -49.054 -33.109  1.00 19.23           O
ANISOU 1794  O   LYS A 253     1820   2765   2721    233    111    184       O
ATOM   1795  CB  LYS A 253      -7.376 -47.430 -35.337  1.00 20.87           C
ANISOU 1795  CB  LYS A 253     1902   3000   3026    205    241    233       C
ATOM   1796  CG  LYS A 253      -6.884 -47.073 -36.722  1.00 23.52           C
ANISOU 1796  CG  LYS A 253     2218   3339   3381    222    320    272       C
ATOM   1797  CD  LYS A 253      -6.695 -45.572 -36.889  1.00 25.69           C
ANISOU 1797  CD  LYS A 253     2440   3599   3724    144    352    280       C
ATOM   1798  CE  LYS A 253      -5.557 -45.022 -36.041  1.00 28.54           C
ANISOU 1798  CE  LYS A 253     2685   4003   4157     96    328    265       C
ATOM   1799  NZ  LYS A 253      -4.223 -45.522 -36.458  1.00 31.36           N
ANISOU 1799  NZ  LYS A 253     2958   4422   4534    142    362    295       N
ATOM   1800  N   TYR A 254      -6.911 -49.596 -33.146  1.00 20.11           N
ANISOU 1800  N   TYR A 254     1805   2971   2866    293    121    205       N
ATOM   1801  CA  TYR A 254      -6.834 -49.940 -31.735  1.00 20.19           C
ANISOU 1801  CA  TYR A 254     1802   3012   2858    297     54    185       C
ATOM   1802  C   TYR A 254      -5.393 -49.811 -31.268  1.00 20.88           C
ANISOU 1802  C   TYR A 254     1776   3178   2981    307     34    182       C
ATOM   1803  O   TYR A 254      -4.482 -49.638 -32.086  1.00 21.38           O
ANISOU 1803  O   TYR A 254     1776   3267   3082    318     79    202       O
ATOM   1804  CB  TYR A 254      -7.341 -51.372 -31.509  1.00 20.21           C
ANISOU 1804  CB  TYR A 254     1882   2994   2803    368     37    200       C
ATOM   1805  CG  TYR A 254      -6.564 -52.422 -32.273  1.00 21.34           C
ANISOU 1805  CG  TYR A 254     2019   3151   2937    451     69    229       C
ATOM   1806  CD1 TYR A 254      -5.510 -53.105 -31.673  1.00 24.10           C
ANISOU 1806  CD1 TYR A 254     2313   3561   3283    509     45    240       C
ATOM   1807  CD2 TYR A 254      -6.866 -52.721 -33.601  1.00 21.83           C
ANISOU 1807  CD2 TYR A 254     2131   3172   2990    478    123    243       C
ATOM   1808  CE1 TYR A 254      -4.779 -54.059 -32.372  1.00 25.96           C
ANISOU 1808  CE1 TYR A 254     2542   3809   3511    592     77    266       C
ATOM   1809  CE2 TYR A 254      -6.143 -53.681 -34.308  1.00 24.24           C
ANISOU 1809  CE2 TYR A 254     2435   3491   3283    561    154    263       C
ATOM   1810  CZ  TYR A 254      -5.103 -54.344 -33.686  1.00 25.78           C
ANISOU 1810  CZ  TYR A 254     2575   3742   3480    618    132    275       C
ATOM   1811  OH  TYR A 254      -4.377 -55.293 -34.370  1.00 28.04           O
ANISOU 1811  OH  TYR A 254     2859   4040   3754    707    165    295       O
ATOM   1812  N   GLN A 255      -5.194 -49.874 -29.958  1.00 20.80           N
ANISOU 1812  N   GLN A 255     1737   3210   2956    305    -31    158       N
ATOM   1813  CA  GLN A 255      -3.860 -50.010 -29.389  1.00 21.75           C
ANISOU 1813  CA  GLN A 255     1752   3414   3097    331    -64    153       C
ATOM   1814  C   GLN A 255      -3.846 -51.241 -28.498  1.00 21.84           C
ANISOU 1814  C   GLN A 255     1797   3455   3047    411   -110    166       C
ATOM   1815  O   GLN A 255      -4.899 -51.769 -28.131  1.00 20.93           O
ANISOU 1815  O   GLN A 255     1777   3295   2882    426   -121    172       O
ATOM   1816  CB  GLN A 255      -3.448 -48.755 -28.609  1.00 22.58           C
ANISOU 1816  CB  GLN A 255     1774   3556   3251    252   -108    105       C
ATOM   1817  CG  GLN A 255      -4.337 -48.412 -27.428  1.00 22.28           C
ANISOU 1817  CG  GLN A 255     1785   3506   3175    219   -167     65       C
ATOM   1818  CD  GLN A 255      -3.885 -47.166 -26.684  1.00 23.04           C
ANISOU 1818  CD  GLN A 255     1800   3636   3320    143   -215      7       C
ATOM   1819  OE1 GLN A 255      -2.695 -46.880 -26.586  1.00 25.06           O
ANISOU 1819  OE1 GLN A 255     1945   3951   3625    133   -232     -8       O
ATOM   1820  NE2 GLN A 255      -4.837 -46.431 -26.139  1.00 23.15           N
ANISOU 1820  NE2 GLN A 255     1866   3610   3322     91   -237    -31       N
ATOM   1821  N   VAL A 256      -2.649 -51.711 -28.178  1.00 22.53           N
ANISOU 1821  N   VAL A 256     1802   3619   3140    465   -132    175       N
ATOM   1822  CA  VAL A 256      -2.495 -52.877 -27.317  1.00 22.97           C
ANISOU 1822  CA  VAL A 256     1881   3708   3137    551   -174    194       C
ATOM   1823  C   VAL A 256      -1.666 -52.468 -26.114  1.00 23.56           C
ANISOU 1823  C   VAL A 256     1860   3877   3213    546   -248    162       C
ATOM   1824  O   VAL A 256      -0.504 -52.077 -26.256  1.00 23.77           O
ANISOU 1824  O   VAL A 256     1771   3969   3289    540   -255    151       O
ATOM   1825  CB  VAL A 256      -1.856 -54.044 -28.066  1.00 23.45           C
ANISOU 1825  CB  VAL A 256     1945   3774   3191    647   -134    239       C
ATOM   1826  CG1 VAL A 256      -1.844 -55.305 -27.195  1.00 24.35           C
ANISOU 1826  CG1 VAL A 256     2102   3905   3245    740   -172    267       C
ATOM   1827  CG2 VAL A 256      -2.609 -54.299 -29.369  1.00 22.90           C
ANISOU 1827  CG2 VAL A 256     1961   3616   3123    645    -64    257       C
ATOM   1828  N   ILE A 257      -2.291 -52.520 -24.939  1.00 23.29           N
ANISOU 1828  N   ILE A 257     1871   3852   3125    547   -304    145       N
ATOM   1829  CA  ILE A 257      -1.655 -52.120 -23.686  1.00 24.36           C
ANISOU 1829  CA  ILE A 257     1930   4079   3246    547   -385    106       C
ATOM   1830  C   ILE A 257      -1.691 -53.313 -22.743  1.00 24.95           C
ANISOU 1830  C   ILE A 257     2049   4191   3240    648   -422    141       C
ATOM   1831  O   ILE A 257      -2.767 -53.838 -22.442  1.00 24.24           O
ANISOU 1831  O   ILE A 257     2067   4044   3097    666   -411    167       O
ATOM   1832  CB  ILE A 257      -2.372 -50.919 -23.039  1.00 24.04           C
ANISOU 1832  CB  ILE A 257     1901   4023   3208    456   -420     46       C
ATOM   1833  CG1 ILE A 257      -2.526 -49.772 -24.048  1.00 23.90           C
ANISOU 1833  CG1 ILE A 257     1862   3947   3271    358   -370     23       C
ATOM   1834  CG2 ILE A 257      -1.600 -50.440 -21.814  1.00 25.50           C
ANISOU 1834  CG2 ILE A 257     1998   4310   3381    455   -509     -7       C
ATOM   1835  CD1 ILE A 257      -3.273 -48.554 -23.495  1.00 23.37           C
ANISOU 1835  CD1 ILE A 257     1814   3852   3213    271   -398    -36       C
ATOM   1836  N   GLY A 258      -0.517 -53.755 -22.306  1.00 26.38           N
ANISOU 1836  N   GLY A 258     2146   4466   3414    716   -463    148       N
ATOM   1837  CA  GLY A 258      -0.398 -54.964 -21.488  1.00 27.49           C
ANISOU 1837  CA  GLY A 258     2323   4644   3478    828   -493    194       C
ATOM   1838  C   GLY A 258      -0.983 -56.187 -22.177  1.00 27.50           C
ANISOU 1838  C   GLY A 258     2431   4557   3462    891   -427    261       C
ATOM   1839  O   GLY A 258      -1.568 -57.049 -21.526  1.00 27.89           O
ANISOU 1839  O   GLY A 258     2563   4584   3448    951   -434    301       O
ATOM   1840  N   GLY A 259      -0.835 -56.251 -23.499  1.00 27.51           N
ANISOU 1840  N   GLY A 259     2430   4505   3518    877   -361    272       N
ATOM   1841  CA  GLY A 259      -1.367 -57.354 -24.296  1.00 27.18           C
ANISOU 1841  CA  GLY A 259     2487   4374   3467    930   -300    322       C
ATOM   1842  C   GLY A 259      -2.864 -57.321 -24.560  1.00 26.31           C
ANISOU 1842  C   GLY A 259     2496   4156   3346    875   -267    323       C
ATOM   1843  O   GLY A 259      -3.393 -58.244 -25.179  1.00 26.68           O
ANISOU 1843  O   GLY A 259     2627   4122   3387    913   -222    357       O
ATOM   1844  N   GLU A 260      -3.540 -56.257 -24.127  1.00 25.42           N
ANISOU 1844  N   GLU A 260     2385   4040   3233    786   -289    283       N
ATOM   1845  CA  GLU A 260      -4.997 -56.143 -24.239  1.00 24.78           C
ANISOU 1845  CA  GLU A 260     2407   3870   3140    734   -265    283       C
ATOM   1846  C   GLU A 260      -5.383 -55.048 -25.226  1.00 23.54           C
ANISOU 1846  C   GLU A 260     2240   3669   3035    640   -229    246       C
ATOM   1847  O   GLU A 260      -4.763 -53.982 -25.248  1.00 23.18           O
ANISOU 1847  O   GLU A 260     2109   3673   3027    588   -245    207       O
ATOM   1848  CB  GLU A 260      -5.602 -55.815 -22.876  1.00 25.13           C
ANISOU 1848  CB  GLU A 260     2473   3943   3133    717   -315    270       C
ATOM   1849  CG  GLU A 260      -5.592 -56.970 -21.892  1.00 27.97           C
ANISOU 1849  CG  GLU A 260     2874   4324   3429    810   -338    321       C
ATOM   1850  CD  GLU A 260      -6.738 -57.933 -22.115  1.00 30.10           C
ANISOU 1850  CD  GLU A 260     3260   4493   3685    828   -292    370       C
ATOM   1851  OE1 GLU A 260      -7.908 -57.480 -22.189  1.00 31.83           O
ANISOU 1851  OE1 GLU A 260     3533   4653   3906    760   -274    356       O
ATOM   1852  OE2 GLU A 260      -6.473 -59.144 -22.216  1.00 32.50           O
ANISOU 1852  OE2 GLU A 260     3598   4772   3979    910   -275    421       O
ATOM   1853  N   VAL A 261      -6.417 -55.312 -26.021  1.00 22.36           N
ANISOU 1853  N   VAL A 261     2177   3428   2889    620   -183    258       N
ATOM   1854  CA  VAL A 261      -6.908 -54.357 -27.023  1.00 21.46           C
ANISOU 1854  CA  VAL A 261     2068   3269   2816    543   -145    232       C
ATOM   1855  C   VAL A 261      -7.799 -53.272 -26.413  1.00 20.86           C
ANISOU 1855  C   VAL A 261     2007   3183   2738    462   -168    197       C
ATOM   1856  O   VAL A 261      -8.778 -53.560 -25.717  1.00 20.11           O
ANISOU 1856  O   VAL A 261     1978   3060   2604    461   -182    205       O
ATOM   1857  CB  VAL A 261      -7.671 -55.070 -28.167  1.00 20.83           C
ANISOU 1857  CB  VAL A 261     2074   3102   2739    559    -93    253       C
ATOM   1858  CG1 VAL A 261      -8.278 -54.058 -29.146  1.00 20.67           C
ANISOU 1858  CG1 VAL A 261     2064   3039   2749    486    -57    229       C
ATOM   1859  CG2 VAL A 261      -6.747 -56.008 -28.904  1.00 21.45           C
ANISOU 1859  CG2 VAL A 261     2137   3189   2824    639    -65    278       C
ATOM   1860  N   TYR A 262      -7.443 -52.022 -26.692  1.00 20.72           N
ANISOU 1860  N   TYR A 262     1925   3184   2764    396   -166    161       N
ATOM   1861  CA  TYR A 262      -8.210 -50.859 -26.277  1.00 20.07           C
ANISOU 1861  CA  TYR A 262     1853   3084   2688    318   -181    122       C
ATOM   1862  C   TYR A 262      -8.375 -49.916 -27.463  1.00 19.66           C
ANISOU 1862  C   TYR A 262     1793   2988   2691    258   -132    112       C
ATOM   1863  O   TYR A 262      -7.669 -50.046 -28.464  1.00 19.17           O
ANISOU 1863  O   TYR A 262     1696   2927   2661    274    -93    130       O
ATOM   1864  CB  TYR A 262      -7.501 -50.143 -25.126  1.00 21.08           C
ANISOU 1864  CB  TYR A 262     1905   3288   2817    298   -242     80       C
ATOM   1865  CG  TYR A 262      -7.538 -50.926 -23.839  1.00 22.47           C
ANISOU 1865  CG  TYR A 262     2101   3512   2926    358   -293     90       C
ATOM   1866  CD1 TYR A 262      -6.431 -51.636 -23.403  1.00 23.89           C
ANISOU 1866  CD1 TYR A 262     2224   3763   3088    427   -324    106       C
ATOM   1867  CD2 TYR A 262      -8.705 -50.991 -23.082  1.00 24.15           C
ANISOU 1867  CD2 TYR A 262     2390   3699   3087    354   -304     91       C
ATOM   1868  CE1 TYR A 262      -6.471 -52.372 -22.219  1.00 26.02           C
ANISOU 1868  CE1 TYR A 262     2518   4079   3289    491   -368    124       C
ATOM   1869  CE2 TYR A 262      -8.756 -51.722 -21.902  1.00 25.36           C
ANISOU 1869  CE2 TYR A 262     2565   3897   3172    415   -343    110       C
ATOM   1870  CZ  TYR A 262      -7.637 -52.407 -21.479  1.00 26.00           C
ANISOU 1870  CZ  TYR A 262     2594   4049   3234    485   -375    128       C
ATOM   1871  OH  TYR A 262      -7.692 -53.133 -20.312  1.00 29.27           O
ANISOU 1871  OH  TYR A 262     3034   4510   3576    553   -411    154       O
ATOM   1872  N   PRO A 263      -9.316 -48.961 -27.362  1.00 19.19           N
ANISOU 1872  N   PRO A 263     1765   2887   2638    194   -131     85       N
ATOM   1873  CA  PRO A 263      -9.435 -47.971 -28.424  1.00 18.88           C
ANISOU 1873  CA  PRO A 263     1716   2808   2651    139    -85     80       C
ATOM   1874  C   PRO A 263      -8.140 -47.186 -28.601  1.00 19.31           C
ANISOU 1874  C   PRO A 263     1665   2905   2768    109    -83     64       C
ATOM   1875  O   PRO A 263      -7.364 -47.064 -27.658  1.00 19.72           O
ANISOU 1875  O   PRO A 263     1651   3016   2825    108   -133     37       O
ATOM   1876  CB  PRO A 263     -10.570 -47.055 -27.932  1.00 18.77           C
ANISOU 1876  CB  PRO A 263     1745   2756   2631     82    -98     49       C
ATOM   1877  CG  PRO A 263     -11.304 -47.862 -26.905  1.00 18.48           C
ANISOU 1877  CG  PRO A 263     1764   2727   2530    118   -133     52       C
ATOM   1878  CD  PRO A 263     -10.263 -48.706 -26.265  1.00 19.10           C
ANISOU 1878  CD  PRO A 263     1798   2871   2588    174   -167     63       C
ATOM   1879  N   PRO A 264      -7.905 -46.650 -29.808  1.00 19.35           N
ANISOU 1879  N   PRO A 264     1651   2880   2820     85    -24     82       N
ATOM   1880  CA  PRO A 264      -6.696 -45.883 -30.057  1.00 19.89           C
ANISOU 1880  CA  PRO A 264     1615   2983   2959     50    -11     76       C
ATOM   1881  C   PRO A 264      -6.754 -44.528 -29.354  1.00 20.00           C
ANISOU 1881  C   PRO A 264     1591   2986   3021    -34    -42     25       C
ATOM   1882  O   PRO A 264      -7.790 -44.158 -28.798  1.00 19.57           O
ANISOU 1882  O   PRO A 264     1599   2897   2939    -58    -66     -2       O
ATOM   1883  CB  PRO A 264      -6.713 -45.710 -31.574  1.00 19.71           C
ANISOU 1883  CB  PRO A 264     1606   2921   2962     53     70    118       C
ATOM   1884  CG  PRO A 264      -8.159 -45.639 -31.904  1.00 19.30           C
ANISOU 1884  CG  PRO A 264     1660   2803   2871     46     84    121       C
ATOM   1885  CD  PRO A 264      -8.877 -46.505 -30.907  1.00 18.85           C
ANISOU 1885  CD  PRO A 264     1661   2750   2750     78     30    106       C
ATOM   1886  N   THR A 265      -5.649 -43.794 -29.384  1.00 20.97           N
ANISOU 1886  N   THR A 265     1611   3139   3219    -77    -41     10       N
ATOM   1887  CA  THR A 265      -5.577 -42.509 -28.692  1.00 21.35           C
ANISOU 1887  CA  THR A 265     1616   3174   3323   -159    -76    -48       C
ATOM   1888  C   THR A 265      -6.051 -41.358 -29.565  1.00 21.32           C
ANISOU 1888  C   THR A 265     1633   3090   3379   -222    -14    -36       C
ATOM   1889  O   THR A 265      -6.110 -41.465 -30.802  1.00 21.20           O
ANISOU 1889  O   THR A 265     1637   3044   3373   -205     60     21       O
ATOM   1890  CB  THR A 265      -4.149 -42.191 -28.231  1.00 22.47           C
ANISOU 1890  CB  THR A 265     1627   3381   3530   -186   -112    -78       C
ATOM   1891  OG1 THR A 265      -3.309 -41.975 -29.375  1.00 24.01           O
ANISOU 1891  OG1 THR A 265     1753   3573   3796   -199    -41    -32       O
ATOM   1892  CG2 THR A 265      -3.593 -43.325 -27.382  1.00 22.53           C
ANISOU 1892  CG2 THR A 265     1608   3477   3477   -114   -174    -85       C
ATOM   1893  N   VAL A 266      -6.385 -40.255 -28.900  1.00 21.40           N
ANISOU 1893  N   VAL A 266     1641   3065   3425   -290    -45    -91       N
ATOM   1894  CA  VAL A 266      -6.681 -38.994 -29.568  1.00 21.50           C
ANISOU 1894  CA  VAL A 266     1660   2998   3511   -357      7    -86       C
ATOM   1895  C   VAL A 266      -5.485 -38.521 -30.399  1.00 22.64           C
ANISOU 1895  C   VAL A 266     1705   3146   3753   -393     62    -53       C
ATOM   1896  O   VAL A 266      -5.645 -38.040 -31.519  1.00 21.85           O
ANISOU 1896  O   VAL A 266     1622   2992   3689   -407    142     -1       O
ATOM   1897  CB  VAL A 266      -7.073 -37.917 -28.532  1.00 21.85           C
ANISOU 1897  CB  VAL A 266     1708   3009   3583   -421    -47   -164       C
ATOM   1898  CG1 VAL A 266      -7.053 -36.517 -29.148  1.00 22.37           C
ANISOU 1898  CG1 VAL A 266     1757   2991   3750   -499      5   -163       C
ATOM   1899  CG2 VAL A 266      -8.459 -38.244 -27.956  1.00 20.95           C
ANISOU 1899  CG2 VAL A 266     1705   2879   3376   -385    -75   -181       C
ATOM   1900  N   LYS A 267      -4.285 -38.665 -29.854  1.00 23.93           N
ANISOU 1900  N   LYS A 267     1761   3376   3956   -405     21    -81       N
ATOM   1901  CA  LYS A 267      -3.090 -38.210 -30.557  1.00 25.93           C
ANISOU 1901  CA  LYS A 267     1904   3639   4310   -444     72    -50       C
ATOM   1902  C   LYS A 267      -2.858 -38.988 -31.854  1.00 26.18           C
ANISOU 1902  C   LYS A 267     1946   3686   4316   -378    156     39       C
ATOM   1903  O   LYS A 267      -2.481 -38.410 -32.873  1.00 26.42           O
ANISOU 1903  O   LYS A 267     1942   3684   4413   -406    238     90       O
ATOM   1904  CB  LYS A 267      -1.865 -38.322 -29.655  1.00 27.16           C
ANISOU 1904  CB  LYS A 267     1936   3876   4507   -462      1   -101       C
ATOM   1905  CG  LYS A 267      -0.553 -37.980 -30.363  1.00 30.00           C
ANISOU 1905  CG  LYS A 267     2166   4258   4974   -498     55    -65       C
ATOM   1906  CD  LYS A 267       0.323 -37.053 -29.566  1.00 33.33           C
ANISOU 1906  CD  LYS A 267     2467   4693   5502   -589     -3   -138       C
ATOM   1907  CE  LYS A 267      -0.174 -35.621 -29.607  1.00 34.66           C
ANISOU 1907  CE  LYS A 267     2658   4754   5756   -687     17   -169       C
ATOM   1908  NZ  LYS A 267       0.985 -34.684 -29.693  1.00 36.33           N
ANISOU 1908  NZ  LYS A 267     2728   4957   6119   -783     30   -186       N
ATOM   1909  N   ASP A 268      -3.065 -40.299 -31.797  1.00 26.10           N
ANISOU 1909  N   ASP A 268     1984   3725   4209   -289    137     56       N
ATOM   1910  CA  ASP A 268      -2.849 -41.184 -32.941  1.00 26.85           C
ANISOU 1910  CA  ASP A 268     2095   3839   4266   -214    206    127       C
ATOM   1911  C   ASP A 268      -3.888 -40.944 -34.047  1.00 26.11           C
ANISOU 1911  C   ASP A 268     2104   3673   4144   -202    278    174       C
ATOM   1912  O   ASP A 268      -3.536 -40.870 -35.228  1.00 26.94           O
ANISOU 1912  O   ASP A 268     2195   3773   4269   -184    361    234       O
ATOM   1913  CB  ASP A 268      -2.859 -42.640 -32.445  1.00 26.93           C
ANISOU 1913  CB  ASP A 268     2138   3910   4186   -124    157    123       C
ATOM   1914  CG  ASP A 268      -2.803 -43.663 -33.562  1.00 29.45           C
ANISOU 1914  CG  ASP A 268     2496   4241   4454    -37    220    185       C
ATOM   1915  OD1 ASP A 268      -3.454 -44.716 -33.411  1.00 34.35           O
ANISOU 1915  OD1 ASP A 268     3199   4861   4990     29    195    186       O
ATOM   1916  OD2 ASP A 268      -2.103 -43.453 -34.569  1.00 34.58           O
ANISOU 1916  OD2 ASP A 268     3093   4900   5147    -32    293    232       O
ATOM   1917  N   THR A 269      -5.152 -40.793 -33.655  1.00 24.79           N
ANISOU 1917  N   THR A 269     2035   3456   3928   -211    247    146       N
ATOM   1918  CA  THR A 269      -6.273 -40.688 -34.594  1.00 23.85           C
ANISOU 1918  CA  THR A 269     2018   3277   3767   -190    299    182       C
ATOM   1919  C   THR A 269      -6.638 -39.259 -35.013  1.00 24.36           C
ANISOU 1919  C   THR A 269     2089   3268   3897   -259    344    192       C
ATOM   1920  O   THR A 269      -7.218 -39.065 -36.074  1.00 23.34           O
ANISOU 1920  O   THR A 269     2019   3100   3749   -237    407    240       O
ATOM   1921  CB  THR A 269      -7.551 -41.325 -34.006  1.00 22.80           C
ANISOU 1921  CB  THR A 269     1988   3128   3546   -157    245    153       C
ATOM   1922  OG1 THR A 269      -7.920 -40.644 -32.798  1.00 21.47           O
ANISOU 1922  OG1 THR A 269     1818   2943   3396   -214    183     92       O
ATOM   1923  CG2 THR A 269      -7.345 -42.814 -33.717  1.00 22.47           C
ANISOU 1923  CG2 THR A 269     1960   3143   3437    -81    211    154       C
ATOM   1924  N   GLN A 270      -6.309 -38.269 -34.186  1.00 25.66           N
ANISOU 1924  N   GLN A 270     2198   3414   4139   -338    310    145       N
ATOM   1925  CA  GLN A 270      -6.804 -36.895 -34.372  1.00 27.15           C
ANISOU 1925  CA  GLN A 270     2406   3519   4392   -405    342    143       C
ATOM   1926  C   GLN A 270      -8.319 -36.745 -34.218  1.00 26.58           C
ANISOU 1926  C   GLN A 270     2449   3394   4255   -391    324    127       C
ATOM   1927  O   GLN A 270      -8.867 -35.747 -34.683  1.00 26.55           O
ANISOU 1927  O   GLN A 270     2480   3320   4288   -423    367    145       O
ATOM   1928  CB  GLN A 270      -6.412 -36.313 -35.747  1.00 28.19           C
ANISOU 1928  CB  GLN A 270     2516   3616   4577   -412    447    223       C
ATOM   1929  CG  GLN A 270      -5.245 -35.378 -35.729  1.00 32.40           C
ANISOU 1929  CG  GLN A 270     2936   4137   5238   -490    477    227       C
ATOM   1930  CD  GLN A 270      -3.956 -36.085 -35.985  1.00 35.75           C
ANISOU 1930  CD  GLN A 270     3261   4641   5681   -464    495    254       C
ATOM   1931  OE1 GLN A 270      -3.040 -35.528 -36.596  1.00 39.88           O
ANISOU 1931  OE1 GLN A 270     3699   5159   6293   -500    562    300       O
ATOM   1932  NE2 GLN A 270      -3.867 -37.328 -35.529  1.00 37.27           N
ANISOU 1932  NE2 GLN A 270     3461   4908   5792   -399    439    231       N
ATOM   1933  N   VAL A 271      -9.001 -37.698 -33.583  1.00 26.41           N
ANISOU 1933  N   VAL A 271     2484   3406   4144   -344    266     97       N
ATOM   1934  CA  VAL A 271     -10.450 -37.536 -33.360  1.00 26.43           C
ANISOU 1934  CA  VAL A 271     2585   3364   4093   -334    248     80       C
ATOM   1935  C   VAL A 271     -10.680 -36.747 -32.066  1.00 27.00           C
ANISOU 1935  C   VAL A 271     2649   3416   4194   -390    187      6       C
ATOM   1936  O   VAL A 271     -10.011 -36.977 -31.051  1.00 27.60           O
ANISOU 1936  O   VAL A 271     2671   3540   4277   -404    126    -44       O
ATOM   1937  CB  VAL A 271     -11.270 -38.868 -33.371  1.00 26.09           C
ANISOU 1937  CB  VAL A 271     2615   3353   3944   -260    224     89       C
ATOM   1938  CG1 VAL A 271     -10.691 -39.870 -34.360  1.00 25.91           C
ANISOU 1938  CG1 VAL A 271     2582   3369   3893   -201    264    142       C
ATOM   1939  CG2 VAL A 271     -11.416 -39.467 -31.991  1.00 27.10           C
ANISOU 1939  CG2 VAL A 271     2745   3521   4030   -253    144     35       C
ATOM   1940  N   GLU A 272     -11.598 -35.790 -32.131  1.00 26.59           N
ANISOU 1940  N   GLU A 272     2651   3295   4157   -417    203     -3       N
ATOM   1941  CA  GLU A 272     -11.943 -34.961 -30.981  1.00 27.18           C
ANISOU 1941  CA  GLU A 272     2731   3341   4256   -463    151    -76       C
ATOM   1942  C   GLU A 272     -12.642 -35.819 -29.917  1.00 25.25           C
ANISOU 1942  C   GLU A 272     2530   3145   3917   -422     83   -117       C
ATOM   1943  O   GLU A 272     -13.544 -36.595 -30.234  1.00 24.81           O
ANISOU 1943  O   GLU A 272     2541   3099   3788   -369     92    -85       O
ATOM   1944  CB  GLU A 272     -12.866 -33.812 -31.410  1.00 27.73           C
ANISOU 1944  CB  GLU A 272     2858   3321   4356   -487    193    -67       C
ATOM   1945  CG  GLU A 272     -12.241 -32.803 -32.375  1.00 31.75           C
ANISOU 1945  CG  GLU A 272     3330   3770   4965   -531    265    -22       C
ATOM   1946  CD  GLU A 272     -13.236 -31.740 -32.848  1.00 35.19           C
ANISOU 1946  CD  GLU A 272     3833   4116   5423   -540    310     -3       C
ATOM   1947  OE1 GLU A 272     -12.795 -30.716 -33.407  1.00 38.60           O
ANISOU 1947  OE1 GLU A 272     4239   4482   5947   -585    366     25       O
ATOM   1948  OE2 GLU A 272     -14.460 -31.929 -32.667  1.00 38.37           O
ANISOU 1948  OE2 GLU A 272     4312   4513   5753   -500    293    -11       O
ATOM   1949  N   MET A 273     -12.194 -35.695 -28.668  1.00 24.90           N
ANISOU 1949  N   MET A 273     2447   3135   3879   -445     14   -187       N
ATOM   1950  CA  MET A 273     -12.873 -36.289 -27.506  1.00 23.62           C
ANISOU 1950  CA  MET A 273     2328   3016   3631   -409    -48   -228       C
ATOM   1951  C   MET A 273     -12.937 -35.248 -26.392  1.00 24.31           C
ANISOU 1951  C   MET A 273     2407   3085   3746   -454    -98   -314       C
ATOM   1952  O   MET A 273     -12.112 -34.346 -26.343  1.00 24.74           O
ANISOU 1952  O   MET A 273     2400   3113   3887   -514   -103   -350       O
ATOM   1953  CB  MET A 273     -12.111 -37.504 -26.975  1.00 23.40           C
ANISOU 1953  CB  MET A 273     2259   3076   3555   -368    -92   -227       C
ATOM   1954  CG  MET A 273     -12.047 -38.695 -27.913  1.00 21.57           C
ANISOU 1954  CG  MET A 273     2041   2867   3287   -313    -53   -154       C
ATOM   1955  SD  MET A 273     -13.620 -39.545 -28.131  1.00 20.21           S
ANISOU 1955  SD  MET A 273     1977   2678   3025   -257    -37   -117       S
ATOM   1956  CE  MET A 273     -14.000 -40.048 -26.456  1.00 19.71           C
ANISOU 1956  CE  MET A 273     1933   2668   2888   -231   -111   -165       C
ATOM   1957  N   ILE A 274     -13.911 -35.384 -25.495  1.00 24.07           N
ANISOU 1957  N   ILE A 274     2437   3067   3643   -425   -133   -347       N
ATOM   1958  CA  ILE A 274     -13.982 -34.515 -24.321  1.00 24.85           C
ANISOU 1958  CA  ILE A 274     2533   3160   3748   -454   -188   -437       C
ATOM   1959  C   ILE A 274     -13.175 -35.139 -23.180  1.00 25.36           C
ANISOU 1959  C   ILE A 274     2549   3318   3770   -435   -264   -485       C
ATOM   1960  O   ILE A 274     -13.538 -36.193 -22.659  1.00 24.91           O
ANISOU 1960  O   ILE A 274     2522   3323   3621   -374   -287   -466       O
ATOM   1961  CB  ILE A 274     -15.433 -34.278 -23.855  1.00 24.57           C
ANISOU 1961  CB  ILE A 274     2584   3099   3651   -425   -185   -451       C
ATOM   1962  CG1 ILE A 274     -16.279 -33.686 -24.985  1.00 24.50           C
ANISOU 1962  CG1 ILE A 274     2625   3006   3679   -434   -113   -401       C
ATOM   1963  CG2 ILE A 274     -15.446 -33.340 -22.648  1.00 25.33           C
ANISOU 1963  CG2 ILE A 274     2681   3191   3753   -449   -241   -551       C
ATOM   1964  CD1 ILE A 274     -17.765 -33.654 -24.675  1.00 25.56           C
ANISOU 1964  CD1 ILE A 274     2839   3126   3748   -395   -104   -399       C
ATOM   1965  N   TYR A 275     -12.067 -34.494 -22.824  1.00 26.58           N
ANISOU 1965  N   TYR A 275     2624   3480   3994   -486   -304   -545       N
ATOM   1966  CA  TYR A 275     -11.242 -34.900 -21.688  1.00 27.50           C
ANISOU 1966  CA  TYR A 275     2686   3688   4074   -471   -387   -605       C
ATOM   1967  C   TYR A 275     -10.663 -33.657 -21.025  1.00 29.20           C
ANISOU 1967  C   TYR A 275     2852   3880   4363   -539   -440   -709       C
ATOM   1968  O   TYR A 275     -10.274 -32.720 -21.720  1.00 29.33           O
ANISOU 1968  O   TYR A 275     2832   3820   4491   -609   -404   -714       O
ATOM   1969  CB  TYR A 275     -10.063 -35.757 -22.141  1.00 27.54           C
ANISOU 1969  CB  TYR A 275     2612   3754   4100   -459   -387   -560       C
ATOM   1970  CG  TYR A 275     -10.387 -37.177 -22.525  1.00 25.78           C
ANISOU 1970  CG  TYR A 275     2427   3573   3796   -384   -359   -475       C
ATOM   1971  CD1 TYR A 275     -10.315 -37.591 -23.850  1.00 25.06           C
ANISOU 1971  CD1 TYR A 275     2337   3450   3736   -378   -286   -393       C
ATOM   1972  CD2 TYR A 275     -10.724 -38.118 -21.561  1.00 25.23           C
ANISOU 1972  CD2 TYR A 275     2391   3574   3619   -315   -404   -478       C
ATOM   1973  CE1 TYR A 275     -10.601 -38.901 -24.208  1.00 24.42           C
ANISOU 1973  CE1 TYR A 275     2293   3400   3586   -310   -264   -324       C
ATOM   1974  CE2 TYR A 275     -11.010 -39.428 -21.907  1.00 24.47           C
ANISOU 1974  CE2 TYR A 275     2332   3506   3461   -250   -377   -401       C
ATOM   1975  CZ  TYR A 275     -10.947 -39.814 -23.235  1.00 23.75           C
ANISOU 1975  CZ  TYR A 275     2242   3375   3407   -250   -309   -329       C
ATOM   1976  OH  TYR A 275     -11.224 -41.115 -23.586  1.00 23.20           O
ANISOU 1976  OH  TYR A 275     2211   3326   3280   -186   -286   -262       O
ATOM   1977  N   PRO A 276     -10.572 -33.657 -19.682  1.00 30.68           N
ANISOU 1977  N   PRO A 276     3035   4132   4488   -517   -524   -793       N
ATOM   1978  CA  PRO A 276      -9.749 -32.649 -19.005  1.00 32.64           C
ANISOU 1978  CA  PRO A 276     3217   4378   4807   -580   -592   -904       C
ATOM   1979  C   PRO A 276      -8.325 -32.658 -19.563  1.00 34.04           C
ANISOU 1979  C   PRO A 276     3276   4572   5086   -632   -595   -893       C
ATOM   1980  O   PRO A 276      -7.836 -33.717 -19.940  1.00 33.69           O
ANISOU 1980  O   PRO A 276     3197   4591   5012   -590   -582   -823       O
ATOM   1981  CB  PRO A 276      -9.745 -33.119 -17.547  1.00 33.02           C
ANISOU 1981  CB  PRO A 276     3274   4531   4740   -519   -684   -973       C
ATOM   1982  CG  PRO A 276     -10.979 -33.924 -17.396  1.00 31.84           C
ANISOU 1982  CG  PRO A 276     3225   4400   4472   -439   -650   -909       C
ATOM   1983  CD  PRO A 276     -11.240 -34.562 -18.731  1.00 30.19           C
ANISOU 1983  CD  PRO A 276     3033   4150   4289   -432   -560   -790       C
ATOM   1984  N   PRO A 277      -7.653 -31.492 -19.602  1.00 36.19           N
ANISOU 1984  N   PRO A 277     3483   4786   5482   -721   -612   -963       N
ATOM   1985  CA  PRO A 277      -6.338 -31.407 -20.251  1.00 37.30           C
ANISOU 1985  CA  PRO A 277     3504   4933   5737   -780   -601   -944       C
ATOM   1986  C   PRO A 277      -5.218 -32.250 -19.615  1.00 38.36           C
ANISOU 1986  C   PRO A 277     3542   5197   5837   -749   -679   -968       C
ATOM   1987  O   PRO A 277      -4.201 -32.500 -20.269  1.00 39.11           O
ANISOU 1987  O   PRO A 277     3540   5314   6004   -774   -656   -924       O
ATOM   1988  CB  PRO A 277      -5.994 -29.912 -20.147  1.00 38.63           C
ANISOU 1988  CB  PRO A 277     3631   5007   6040   -885   -616  -1033       C
ATOM   1989  CG  PRO A 277      -6.803 -29.410 -19.001  1.00 38.86           C
ANISOU 1989  CG  PRO A 277     3737   5029   6001   -866   -681  -1135       C
ATOM   1990  CD  PRO A 277      -8.080 -30.192 -19.055  1.00 36.91           C
ANISOU 1990  CD  PRO A 277     3606   4798   5618   -774   -640  -1063       C
ATOM   1991  N   HIS A 278      -5.397 -32.679 -18.366  1.00 38.59           N
ANISOU 1991  N   HIS A 278     3595   5314   5752   -689   -767  -1032       N
ATOM   1992  CA  HIS A 278      -4.350 -33.408 -17.641  1.00 39.52           C
ANISOU 1992  CA  HIS A 278     3624   5562   5830   -652   -852  -1063       C
ATOM   1993  C   HIS A 278      -4.369 -34.932 -17.848  1.00 37.91           C
ANISOU 1993  C   HIS A 278     3440   5441   5523   -552   -827   -960       C
ATOM   1994  O   HIS A 278      -3.476 -35.624 -17.356  1.00 38.68           O
ANISOU 1994  O   HIS A 278     3464   5646   5588   -511   -889   -969       O
ATOM   1995  CB  HIS A 278      -4.435 -33.097 -16.138  1.00 40.87           C
ANISOU 1995  CB  HIS A 278     3807   5796   5925   -630   -965  -1188       C
ATOM   1996  CG  HIS A 278      -5.682 -33.611 -15.487  1.00 41.33           C
ANISOU 1996  CG  HIS A 278     3993   5877   5832   -541   -964  -1172       C
ATOM   1997  ND1 HIS A 278      -6.868 -32.906 -15.488  1.00 42.87           N
ANISOU 1997  ND1 HIS A 278     4290   5981   6017   -554   -925  -1189       N
ATOM   1998  CD2 HIS A 278      -5.930 -34.764 -14.822  1.00 42.41           C
ANISOU 1998  CD2 HIS A 278     4170   6116   5828   -437   -992  -1135       C
ATOM   1999  CE1 HIS A 278      -7.793 -33.604 -14.852  1.00 42.40           C
ANISOU 1999  CE1 HIS A 278     4322   5971   5816   -464   -929  -1164       C
ATOM   2000  NE2 HIS A 278      -7.250 -34.735 -14.438  1.00 42.36           N
ANISOU 2000  NE2 HIS A 278     4283   6080   5732   -393   -967  -1129       N
ATOM   2001  N   ILE A 279      -5.367 -35.459 -18.557  1.00 35.51           N
ANISOU 2001  N   ILE A 279     3233   5088   5171   -511   -743   -865       N
ATOM   2002  CA  ILE A 279      -5.440 -36.909 -18.787  1.00 34.01           C
ANISOU 2002  CA  ILE A 279     3070   4962   4892   -420   -717   -770       C
ATOM   2003  C   ILE A 279      -4.226 -37.359 -19.611  1.00 33.70           C
ANISOU 2003  C   ILE A 279     2925   4953   4925   -430   -691   -717       C
ATOM   2004  O   ILE A 279      -3.931 -36.762 -20.645  1.00 33.99           O
ANISOU 2004  O   ILE A 279     2924   4920   5072   -496   -628   -690       O
ATOM   2005  CB  ILE A 279      -6.745 -37.333 -19.510  1.00 32.53           C
ANISOU 2005  CB  ILE A 279     3000   4704   4655   -386   -629   -683       C
ATOM   2006  CG1 ILE A 279      -7.978 -36.935 -18.691  1.00 32.28           C
ANISOU 2006  CG1 ILE A 279     3067   4647   4549   -370   -648   -728       C
ATOM   2007  CG2 ILE A 279      -6.761 -38.843 -19.752  1.00 31.58           C
ANISOU 2007  CG2 ILE A 279     2904   4640   4455   -297   -606   -592       C
ATOM   2008  CD1 ILE A 279      -7.999 -37.510 -17.285  1.00 33.10           C
ANISOU 2008  CD1 ILE A 279     3186   4855   4535   -298   -731   -772       C
ATOM   2009  N   PRO A 280      -3.501 -38.394 -19.141  1.00 33.03           N
ANISOU 2009  N   PRO A 280     2792   4977   4781   -359   -739   -701       N
ATOM   2010  CA  PRO A 280      -2.349 -38.909 -19.887  1.00 32.79           C
ANISOU 2010  CA  PRO A 280     2660   4987   4811   -355   -714   -649       C
ATOM   2011  C   PRO A 280      -2.671 -39.290 -21.333  1.00 30.91           C
ANISOU 2011  C   PRO A 280     2462   4679   4605   -350   -600   -543       C
ATOM   2012  O   PRO A 280      -3.764 -39.781 -21.621  1.00 29.19           O
ANISOU 2012  O   PRO A 280     2357   4417   4318   -307   -553   -491       O
ATOM   2013  CB  PRO A 280      -1.950 -40.156 -19.093  1.00 33.19           C
ANISOU 2013  CB  PRO A 280     2700   5156   4755   -251   -774   -632       C
ATOM   2014  CG  PRO A 280      -2.383 -39.864 -17.703  1.00 34.01           C
ANISOU 2014  CG  PRO A 280     2842   5303   4778   -233   -863   -717       C
ATOM   2015  CD  PRO A 280      -3.641 -39.057 -17.831  1.00 33.35           C
ANISOU 2015  CD  PRO A 280     2861   5115   4697   -279   -822   -735       C
ATOM   2016  N   GLU A 281      -1.707 -39.078 -22.224  1.00 30.39           N
ANISOU 2016  N   GLU A 281     2299   4606   4640   -390   -557   -514       N
ATOM   2017  CA  GLU A 281      -1.908 -39.292 -23.655  1.00 29.23           C
ANISOU 2017  CA  GLU A 281     2182   4396   4529   -389   -447   -421       C
ATOM   2018  C   GLU A 281      -2.537 -40.646 -23.977  1.00 28.20           C
ANISOU 2018  C   GLU A 281     2143   4279   4292   -288   -412   -343       C
ATOM   2019  O   GLU A 281      -3.524 -40.710 -24.707  1.00 26.32           O
ANISOU 2019  O   GLU A 281     2001   3968   4032   -281   -346   -296       O
ATOM   2020  CB  GLU A 281      -0.573 -39.153 -24.395  1.00 30.01           C
ANISOU 2020  CB  GLU A 281     2147   4521   4733   -421   -414   -394       C
ATOM   2021  CG  GLU A 281      -0.672 -39.326 -25.898  1.00 29.07           C
ANISOU 2021  CG  GLU A 281     2051   4346   4648   -415   -298   -299       C
ATOM   2022  CD  GLU A 281       0.672 -39.171 -26.581  1.00 29.27           C
ANISOU 2022  CD  GLU A 281     1939   4405   4776   -443   -260   -269       C
ATOM   2023  OE1 GLU A 281       1.012 -40.009 -27.432  1.00 27.93           O
ANISOU 2023  OE1 GLU A 281     1762   4262   4587   -381   -199   -193       O
ATOM   2024  OE2 GLU A 281       1.392 -38.212 -26.260  1.00 31.85           O
ANISOU 2024  OE2 GLU A 281     2164   4732   5206   -528   -291   -325       O
ATOM   2025  N   ASN A 282      -1.966 -41.725 -23.440  1.00 28.68           N
ANISOU 2025  N   ASN A 282     2173   4433   4290   -210   -458   -331       N
ATOM   2026  CA  ASN A 282      -2.459 -43.073 -23.766  1.00 28.42           C
ANISOU 2026  CA  ASN A 282     2223   4408   4168   -114   -423   -256       C
ATOM   2027  C   ASN A 282      -3.827 -43.392 -23.167  1.00 27.09           C
ANISOU 2027  C   ASN A 282     2183   4207   3904    -82   -437   -258       C
ATOM   2028  O   ASN A 282      -4.498 -44.320 -23.632  1.00 26.91           O
ANISOU 2028  O   ASN A 282     2242   4156   3825    -25   -393   -196       O
ATOM   2029  CB  ASN A 282      -1.435 -44.162 -23.385  1.00 29.62           C
ANISOU 2029  CB  ASN A 282     2308   4662   4285    -32   -462   -235       C
ATOM   2030  CG  ASN A 282      -0.520 -44.560 -24.550  1.00 31.54           C
ANISOU 2030  CG  ASN A 282     2482   4916   4587    -14   -397   -175       C
ATOM   2031  OD1 ASN A 282       0.275 -45.493 -24.430  1.00 35.72           O
ANISOU 2031  OD1 ASN A 282     2962   5520   5090     61   -414   -148       O
ATOM   2032  ND2 ASN A 282      -0.629 -43.856 -25.674  1.00 32.82           N
ANISOU 2032  ND2 ASN A 282     2640   5006   4823    -75   -319   -152       N
ATOM   2033  N   LEU A 283      -4.255 -42.622 -22.166  1.00 27.11           N
ANISOU 2033  N   LEU A 283     2201   4211   3890   -119   -495   -330       N
ATOM   2034  CA  LEU A 283      -5.598 -42.793 -21.588  1.00 26.10           C
ANISOU 2034  CA  LEU A 283     2189   4051   3676    -93   -500   -331       C
ATOM   2035  C   LEU A 283      -6.663 -41.901 -22.226  1.00 25.42           C
ANISOU 2035  C   LEU A 283     2171   3861   3626   -155   -444   -333       C
ATOM   2036  O   LEU A 283      -7.831 -41.976 -21.848  1.00 24.83           O
ANISOU 2036  O   LEU A 283     2189   3757   3489   -138   -441   -332       O
ATOM   2037  CB  LEU A 283      -5.570 -42.576 -20.072  1.00 26.74           C
ANISOU 2037  CB  LEU A 283     2263   4201   3697    -78   -593   -405       C
ATOM   2038  CG  LEU A 283      -4.773 -43.629 -19.293  1.00 27.22           C
ANISOU 2038  CG  LEU A 283     2282   4371   3691      7   -652   -393       C
ATOM   2039  CD1 LEU A 283      -4.654 -43.249 -17.831  1.00 28.67           C
ANISOU 2039  CD1 LEU A 283     2449   4629   3816     19   -748   -475       C
ATOM   2040  CD2 LEU A 283      -5.412 -44.998 -19.442  1.00 27.80           C
ANISOU 2040  CD2 LEU A 283     2441   4438   3682     94   -612   -306       C
ATOM   2041  N   GLN A 284      -6.284 -41.064 -23.192  1.00 25.28           N
ANISOU 2041  N   GLN A 284     2108   3789   3707   -222   -397   -330       N
ATOM   2042  CA  GLN A 284      -7.287 -40.346 -23.981  1.00 24.49           C
ANISOU 2042  CA  GLN A 284     2077   3590   3637   -265   -333   -313       C
ATOM   2043  C   GLN A 284      -7.778 -41.249 -25.108  1.00 23.80           C
ANISOU 2043  C   GLN A 284     2049   3473   3522   -218   -260   -226       C
ATOM   2044  O   GLN A 284      -7.403 -41.066 -26.268  1.00 23.67           O
ANISOU 2044  O   GLN A 284     2006   3423   3564   -236   -198   -185       O
ATOM   2045  CB  GLN A 284      -6.736 -39.035 -24.544  1.00 24.87           C
ANISOU 2045  CB  GLN A 284     2059   3586   3803   -354   -306   -340       C
ATOM   2046  CG  GLN A 284      -6.424 -38.002 -23.477  1.00 26.75           C
ANISOU 2046  CG  GLN A 284     2252   3834   4079   -412   -378   -439       C
ATOM   2047  CD  GLN A 284      -5.908 -36.696 -24.057  1.00 29.38           C
ANISOU 2047  CD  GLN A 284     2522   4099   4542   -507   -347   -462       C
ATOM   2048  OE1 GLN A 284      -6.291 -36.294 -25.158  1.00 30.56           O
ANISOU 2048  OE1 GLN A 284     2703   4171   4738   -531   -265   -408       O
ATOM   2049  NE2 GLN A 284      -5.043 -36.021 -23.312  1.00 31.35           N
ANISOU 2049  NE2 GLN A 284     2683   4377   4851   -560   -413   -544       N
ATOM   2050  N   PHE A 285      -8.622 -42.222 -24.758  1.00 23.22           N
ANISOU 2050  N   PHE A 285     2055   3409   3358   -155   -267   -200       N
ATOM   2051  CA  PHE A 285      -9.155 -43.162 -25.733  1.00 22.80           C
ANISOU 2051  CA  PHE A 285     2063   3326   3275   -108   -209   -129       C
ATOM   2052  C   PHE A 285     -10.087 -42.433 -26.683  1.00 22.06           C
ANISOU 2052  C   PHE A 285     2025   3148   3211   -148   -150   -113       C
ATOM   2053  O   PHE A 285     -10.871 -41.581 -26.258  1.00 22.09           O
ANISOU 2053  O   PHE A 285     2062   3114   3215   -186   -160   -149       O
ATOM   2054  CB  PHE A 285      -9.928 -44.306 -25.055  1.00 22.63           C
ANISOU 2054  CB  PHE A 285     2115   3324   3161    -42   -232   -108       C
ATOM   2055  CG  PHE A 285      -9.087 -45.213 -24.190  1.00 25.74           C
ANISOU 2055  CG  PHE A 285     2467   3799   3512     16   -284   -107       C
ATOM   2056  CD1 PHE A 285      -9.668 -45.869 -23.119  1.00 28.55           C
ANISOU 2056  CD1 PHE A 285     2874   4185   3788     62   -321   -106       C
ATOM   2057  CD2 PHE A 285      -7.740 -45.432 -24.440  1.00 27.80           C
ANISOU 2057  CD2 PHE A 285     2640   4111   3811     29   -292   -102       C
ATOM   2058  CE1 PHE A 285      -8.926 -46.722 -22.303  1.00 29.46           C
ANISOU 2058  CE1 PHE A 285     2959   4378   3858    126   -368    -98       C
ATOM   2059  CE2 PHE A 285      -6.994 -46.282 -23.626  1.00 29.94           C
ANISOU 2059  CE2 PHE A 285     2874   4462   4039     92   -342    -98       C
ATOM   2060  CZ  PHE A 285      -7.593 -46.923 -22.557  1.00 30.01           C
ANISOU 2060  CZ  PHE A 285     2940   4497   3963    142   -381    -96       C
ATOM   2061  N   ALA A 286      -9.996 -42.772 -27.965  1.00 21.24           N
ANISOU 2061  N   ALA A 286     1929   3017   3125   -132    -89    -59       N
ATOM   2062  CA  ALA A 286     -10.826 -42.166 -28.999  1.00 20.39           C
ANISOU 2062  CA  ALA A 286     1873   2838   3038   -156    -30    -35       C
ATOM   2063  C   ALA A 286     -11.819 -43.198 -29.524  1.00 19.38           C
ANISOU 2063  C   ALA A 286     1829   2689   2845   -102     -8      5       C
ATOM   2064  O   ALA A 286     -11.420 -44.261 -30.004  1.00 18.74           O
ANISOU 2064  O   ALA A 286     1749   2631   2741    -50      5     39       O
ATOM   2065  CB  ALA A 286      -9.947 -41.648 -30.123  1.00 20.77           C
ANISOU 2065  CB  ALA A 286     1862   2872   3156   -180     26     -6       C
ATOM   2066  N   VAL A 287     -13.106 -42.875 -29.417  1.00 18.73           N
ANISOU 2066  N   VAL A 287     1815   2563   2737   -114     -6     -3       N
ATOM   2067  CA  VAL A 287     -14.193 -43.737 -29.872  1.00 18.30           C
ANISOU 2067  CA  VAL A 287     1837   2483   2631    -75     10     27       C
ATOM   2068  C   VAL A 287     -15.247 -42.889 -30.593  1.00 18.13           C
ANISOU 2068  C   VAL A 287     1862   2404   2621   -101     45     33       C
ATOM   2069  O   VAL A 287     -15.129 -41.662 -30.655  1.00 18.36           O
ANISOU 2069  O   VAL A 287     1869   2408   2697   -147     59     16       O
ATOM   2070  CB  VAL A 287     -14.824 -44.508 -28.691  1.00 18.05           C
ANISOU 2070  CB  VAL A 287     1843   2475   2542    -49    -35     15       C
ATOM   2071  CG1 VAL A 287     -13.807 -45.478 -28.094  1.00 17.91           C
ANISOU 2071  CG1 VAL A 287     1787   2515   2506     -8    -66     21       C
ATOM   2072  CG2 VAL A 287     -15.335 -43.538 -27.627  1.00 18.22           C
ANISOU 2072  CG2 VAL A 287     1866   2494   2561    -87    -66    -30       C
ATOM   2073  N   GLY A 288     -16.265 -43.544 -31.147  1.00 17.94           N
ANISOU 2073  N   GLY A 288     1902   2357   2559    -71     60     56       N
ATOM   2074  CA  GLY A 288     -17.258 -42.874 -31.976  1.00 17.72           C
ANISOU 2074  CA  GLY A 288     1916   2282   2535    -83     92     66       C
ATOM   2075  C   GLY A 288     -17.942 -41.708 -31.291  1.00 18.05           C
ANISOU 2075  C   GLY A 288     1967   2299   2593   -124     82     36       C
ATOM   2076  O   GLY A 288     -18.121 -40.652 -31.899  1.00 18.10           O
ANISOU 2076  O   GLY A 288     1976   2269   2633   -148    114     41       O
ATOM   2077  N   GLN A 289     -18.291 -41.901 -30.022  1.00 18.12           N
ANISOU 2077  N   GLN A 289     1982   2328   2575   -127     40      7       N
ATOM   2078  CA  GLN A 289     -19.011 -40.903 -29.234  1.00 18.53           C
ANISOU 2078  CA  GLN A 289     2049   2362   2631   -156     26    -29       C
ATOM   2079  C   GLN A 289     -18.023 -40.081 -28.404  1.00 19.50           C
ANISOU 2079  C   GLN A 289     2118   2500   2791   -192      0    -73       C
ATOM   2080  O   GLN A 289     -17.348 -40.617 -27.520  1.00 19.29           O
ANISOU 2080  O   GLN A 289     2061   2522   2744   -181    -39    -92       O
ATOM   2081  CB  GLN A 289     -20.041 -41.599 -28.325  1.00 18.52           C
ANISOU 2081  CB  GLN A 289     2086   2378   2573   -133      0    -33       C
ATOM   2082  CG  GLN A 289     -21.472 -41.043 -28.429  1.00 18.66           C
ANISOU 2082  CG  GLN A 289     2149   2361   2580   -137     16    -34       C
ATOM   2083  CD  GLN A 289     -21.660 -39.708 -27.736  1.00 19.58           C
ANISOU 2083  CD  GLN A 289     2262   2461   2717   -166      9    -78       C
ATOM   2084  OE1 GLN A 289     -20.708 -38.942 -27.562  1.00 20.67           O
ANISOU 2084  OE1 GLN A 289     2364   2595   2896   -195      2   -107       O
ATOM   2085  NE2 GLN A 289     -22.900 -39.412 -27.342  1.00 19.93           N
ANISOU 2085  NE2 GLN A 289     2343   2494   2737   -159     12    -86       N
ATOM   2086  N   GLU A 290     -17.973 -38.773 -28.669  1.00 20.38           N
ANISOU 2086  N   GLU A 290     2220   2568   2957   -232     20    -92       N
ATOM   2087  CA  GLU A 290     -17.004 -37.870 -28.035  1.00 21.99           C
ANISOU 2087  CA  GLU A 290     2369   2773   3213   -277     -3   -140       C
ATOM   2088  C   GLU A 290     -17.113 -37.745 -26.513  1.00 22.16           C
ANISOU 2088  C   GLU A 290     2389   2828   3202   -279    -62   -202       C
ATOM   2089  O   GLU A 290     -16.169 -37.290 -25.872  1.00 22.16           O
ANISOU 2089  O   GLU A 290     2336   2849   3235   -308    -97   -250       O
ATOM   2090  CB  GLU A 290     -17.075 -36.470 -28.665  1.00 22.95           C
ANISOU 2090  CB  GLU A 290     2490   2824   3405   -320     37   -143       C
ATOM   2091  CG  GLU A 290     -18.331 -35.663 -28.333  1.00 26.01           C
ANISOU 2091  CG  GLU A 290     2934   3167   3782   -323     40   -167       C
ATOM   2092  CD  GLU A 290     -18.350 -34.306 -29.030  1.00 31.33           C
ANISOU 2092  CD  GLU A 290     3611   3763   4531   -360     85   -162       C
ATOM   2093  OE1 GLU A 290     -18.009 -34.244 -30.233  1.00 35.03           O
ANISOU 2093  OE1 GLU A 290     4070   4209   5032   -360    135   -106       O
ATOM   2094  OE2 GLU A 290     -18.703 -33.298 -28.377  1.00 35.93           O
ANISOU 2094  OE2 GLU A 290     4208   4307   5138   -384     72   -211       O
ATOM   2095  N   VAL A 291     -18.257 -38.130 -25.941  1.00 21.59           N
ANISOU 2095  N   VAL A 291     2372   2766   3065   -248    -73   -203       N
ATOM   2096  CA  VAL A 291     -18.463 -38.018 -24.496  1.00 22.45           C
ANISOU 2096  CA  VAL A 291     2487   2913   3129   -239   -122   -257       C
ATOM   2097  C   VAL A 291     -18.076 -39.276 -23.700  1.00 22.28           C
ANISOU 2097  C   VAL A 291     2454   2966   3044   -196   -160   -247       C
ATOM   2098  O   VAL A 291     -18.124 -39.261 -22.476  1.00 23.22           O
ANISOU 2098  O   VAL A 291     2577   3130   3118   -180   -203   -287       O
ATOM   2099  CB  VAL A 291     -19.943 -37.641 -24.152  1.00 22.42           C
ANISOU 2099  CB  VAL A 291     2546   2884   3090   -224   -109   -264       C
ATOM   2100  CG1 VAL A 291     -20.406 -36.438 -24.981  1.00 23.40           C
ANISOU 2100  CG1 VAL A 291     2687   2932   3273   -255    -68   -265       C
ATOM   2101  CG2 VAL A 291     -20.888 -38.815 -24.344  1.00 21.90           C
ANISOU 2101  CG2 VAL A 291     2520   2836   2966   -181    -91   -207       C
ATOM   2102  N   PHE A 292     -17.681 -40.355 -24.375  1.00 21.80           N
ANISOU 2102  N   PHE A 292     2384   2922   2979   -172   -144   -193       N
ATOM   2103  CA  PHE A 292     -17.565 -41.668 -23.713  1.00 21.63           C
ANISOU 2103  CA  PHE A 292     2368   2957   2893   -122   -170   -168       C
ATOM   2104  C   PHE A 292     -16.346 -41.843 -22.793  1.00 22.70           C
ANISOU 2104  C   PHE A 292     2448   3160   3016   -111   -223   -201       C
ATOM   2105  O   PHE A 292     -16.229 -42.857 -22.101  1.00 23.06           O
ANISOU 2105  O   PHE A 292     2501   3258   3005    -62   -247   -181       O
ATOM   2106  CB  PHE A 292     -17.666 -42.800 -24.750  1.00 21.11           C
ANISOU 2106  CB  PHE A 292     2320   2875   2825    -94   -134   -103       C
ATOM   2107  CG  PHE A 292     -19.091 -43.146 -25.152  1.00 19.39           C
ANISOU 2107  CG  PHE A 292     2164   2619   2584    -83   -102    -70       C
ATOM   2108  CD1 PHE A 292     -20.181 -42.404 -24.698  1.00 19.47           C
ANISOU 2108  CD1 PHE A 292     2206   2609   2580    -96    -98    -92       C
ATOM   2109  CD2 PHE A 292     -19.334 -44.205 -26.014  1.00 18.57           C
ANISOU 2109  CD2 PHE A 292     2084   2498   2476    -58    -78    -21       C
ATOM   2110  CE1 PHE A 292     -21.478 -42.736 -25.075  1.00 17.99           C
ANISOU 2110  CE1 PHE A 292     2065   2393   2377    -87    -71    -61       C
ATOM   2111  CE2 PHE A 292     -20.622 -44.532 -26.400  1.00 17.67           C
ANISOU 2111  CE2 PHE A 292     2017   2349   2347    -53    -55      3       C
ATOM   2112  CZ  PHE A 292     -21.697 -43.798 -25.928  1.00 17.60           C
ANISOU 2112  CZ  PHE A 292     2033   2328   2327    -68    -51    -15       C
ATOM   2113  N   GLY A 293     -15.464 -40.848 -22.762  1.00 23.48           N
ANISOU 2113  N   GLY A 293     2492   3259   3172   -154   -244   -252       N
ATOM   2114  CA  GLY A 293     -14.418 -40.782 -21.741  1.00 24.67           C
ANISOU 2114  CA  GLY A 293     2585   3477   3310   -150   -307   -302       C
ATOM   2115  C   GLY A 293     -14.930 -40.362 -20.371  1.00 25.21           C
ANISOU 2115  C   GLY A 293     2680   3579   3320   -137   -353   -360       C
ATOM   2116  O   GLY A 293     -14.189 -40.437 -19.390  1.00 26.67           O
ANISOU 2116  O   GLY A 293     2827   3832   3473   -119   -414   -404       O
ATOM   2117  N   LEU A 294     -16.192 -39.928 -20.304  1.00 25.17           N
ANISOU 2117  N   LEU A 294     2740   3531   3295   -140   -326   -362       N
ATOM   2118  CA  LEU A 294     -16.845 -39.483 -19.061  1.00 25.70           C
ANISOU 2118  CA  LEU A 294     2841   3625   3299   -121   -359   -415       C
ATOM   2119  C   LEU A 294     -16.696 -40.482 -17.913  1.00 25.64           C
ANISOU 2119  C   LEU A 294     2839   3706   3196    -55   -399   -404       C
ATOM   2120  O   LEU A 294     -16.332 -40.100 -16.802  1.00 26.14           O
ANISOU 2120  O   LEU A 294     2888   3826   3218    -40   -456   -469       O
ATOM   2121  CB  LEU A 294     -18.340 -39.229 -19.313  1.00 25.41           C
ANISOU 2121  CB  LEU A 294     2873   3535   3248   -118   -309   -390       C
ATOM   2122  CG  LEU A 294     -19.244 -38.849 -18.126  1.00 26.55           C
ANISOU 2122  CG  LEU A 294     3063   3705   3321    -88   -325   -431       C
ATOM   2123  CD1 LEU A 294     -18.889 -37.483 -17.569  1.00 28.18           C
ANISOU 2123  CD1 LEU A 294     3252   3899   3555   -122   -365   -530       C
ATOM   2124  CD2 LEU A 294     -20.709 -38.892 -18.550  1.00 26.54           C
ANISOU 2124  CD2 LEU A 294     3118   3657   3308    -78   -267   -384       C
ATOM   2125  N   VAL A 295     -17.006 -41.750 -18.178  1.00 24.95           N
ANISOU 2125  N   VAL A 295     2777   3630   3074    -12   -370   -323       N
ATOM   2126  CA  VAL A 295     -16.881 -42.790 -17.160  1.00 24.97           C
ANISOU 2126  CA  VAL A 295     2791   3709   2989     57   -398   -296       C
ATOM   2127  C   VAL A 295     -16.344 -44.092 -17.751  1.00 23.94           C
ANISOU 2127  C   VAL A 295     2647   3586   2865     87   -381   -222       C
ATOM   2128  O   VAL A 295     -16.661 -44.439 -18.892  1.00 22.71           O
ANISOU 2128  O   VAL A 295     2504   3368   2756     68   -332   -174       O
ATOM   2129  CB  VAL A 295     -18.227 -43.093 -16.442  1.00 25.23           C
ANISOU 2129  CB  VAL A 295     2892   3748   2946     96   -372   -267       C
ATOM   2130  CG1 VAL A 295     -18.504 -42.058 -15.356  1.00 26.75           C
ANISOU 2130  CG1 VAL A 295     3095   3974   3094     99   -408   -346       C
ATOM   2131  CG2 VAL A 295     -19.353 -43.172 -17.436  1.00 24.82           C
ANISOU 2131  CG2 VAL A 295     2880   3618   2934     70   -306   -218       C
ATOM   2132  N   PRO A 296     -15.525 -44.816 -16.969  1.00 23.95           N
ANISOU 2132  N   PRO A 296     2622   3663   2814    141   -425   -214       N
ATOM   2133  CA  PRO A 296     -14.955 -46.096 -17.379  1.00 23.58           C
ANISOU 2133  CA  PRO A 296     2564   3627   2766    183   -413   -145       C
ATOM   2134  C   PRO A 296     -15.995 -47.137 -17.774  1.00 22.66           C
ANISOU 2134  C   PRO A 296     2514   3462   2634    207   -355    -63       C
ATOM   2135  O   PRO A 296     -15.693 -48.015 -18.572  1.00 22.16           O
ANISOU 2135  O   PRO A 296     2450   3370   2600    221   -329    -13       O
ATOM   2136  CB  PRO A 296     -14.213 -46.559 -16.125  1.00 24.56           C
ANISOU 2136  CB  PRO A 296     2667   3852   2815    248   -473   -154       C
ATOM   2137  CG  PRO A 296     -13.851 -45.339 -15.448  1.00 24.97           C
ANISOU 2137  CG  PRO A 296     2682   3943   2863    219   -528   -248       C
ATOM   2138  CD  PRO A 296     -14.911 -44.341 -15.716  1.00 24.87           C
ANISOU 2138  CD  PRO A 296     2709   3863   2878    164   -495   -281       C
ATOM   2139  N   GLY A 297     -17.195 -47.049 -17.204  1.00 22.36           N
ANISOU 2139  N   GLY A 297     2531   3414   2552    214   -334    -53       N
ATOM   2140  CA  GLY A 297     -18.291 -47.937 -17.588  1.00 21.77           C
ANISOU 2140  CA  GLY A 297     2512   3285   2474    225   -278     19       C
ATOM   2141  C   GLY A 297     -18.677 -47.814 -19.050  1.00 21.02           C
ANISOU 2141  C   GLY A 297     2423   3108   2458    174   -236     29       C
ATOM   2142  O   GLY A 297     -18.986 -48.809 -19.696  1.00 20.77           O
ANISOU 2142  O   GLY A 297     2416   3033   2443    185   -203     85       O
ATOM   2143  N   LEU A 298     -18.670 -46.588 -19.569  1.00 20.49           N
ANISOU 2143  N   LEU A 298     2334   3015   2436    120   -238    -26       N
ATOM   2144  CA  LEU A 298     -18.911 -46.343 -20.993  1.00 19.79           C
ANISOU 2144  CA  LEU A 298     2247   2856   2415     77   -200    -18       C
ATOM   2145  C   LEU A 298     -17.746 -46.855 -21.839  1.00 19.75           C
ANISOU 2145  C   LEU A 298     2204   2850   2450     83   -202     -3       C
ATOM   2146  O   LEU A 298     -17.946 -47.476 -22.880  1.00 19.21           O
ANISOU 2146  O   LEU A 298     2153   2735   2409     84   -169     34       O
ATOM   2147  CB  LEU A 298     -19.120 -44.851 -21.258  1.00 19.64           C
ANISOU 2147  CB  LEU A 298     2216   2812   2435     24   -200    -76       C
ATOM   2148  CG  LEU A 298     -20.425 -44.266 -20.732  1.00 19.97           C
ANISOU 2148  CG  LEU A 298     2299   2840   2449     17   -185    -89       C
ATOM   2149  CD1 LEU A 298     -20.444 -42.754 -20.926  1.00 19.28           C
ANISOU 2149  CD1 LEU A 298     2198   2724   2402    -29   -189   -151       C
ATOM   2150  CD2 LEU A 298     -21.629 -44.909 -21.409  1.00 21.06           C
ANISOU 2150  CD2 LEU A 298     2479   2930   2593     19   -139    -35       C
ATOM   2151  N   MET A 299     -16.527 -46.610 -21.377  1.00 20.42           N
ANISOU 2151  N   MET A 299     2235   2989   2535     91   -243    -34       N
ATOM   2152  CA  MET A 299     -15.346 -47.069 -22.109  1.00 21.08           C
ANISOU 2152  CA  MET A 299     2272   3081   2654    103   -243    -19       C
ATOM   2153  C   MET A 299     -15.239 -48.603 -22.102  1.00 20.43           C
ANISOU 2153  C   MET A 299     2215   3005   2541    165   -234     42       C
ATOM   2154  O   MET A 299     -14.686 -49.197 -23.033  1.00 20.15           O
ANISOU 2154  O   MET A 299     2168   2951   2537    179   -213     68       O
ATOM   2155  CB  MET A 299     -14.091 -46.420 -21.539  1.00 22.31           C
ANISOU 2155  CB  MET A 299     2354   3299   2822     94   -293    -70       C
ATOM   2156  CG  MET A 299     -12.973 -46.250 -22.527  1.00 25.79           C
ANISOU 2156  CG  MET A 299     2733   3738   3330     75   -281    -72       C
ATOM   2157  SD  MET A 299     -13.461 -45.466 -24.086  1.00 27.90           S
ANISOU 2157  SD  MET A 299     3014   3918   3669     16   -218    -65       S
ATOM   2158  CE  MET A 299     -13.568 -43.742 -23.671  1.00 29.53           C
ANISOU 2158  CE  MET A 299     3195   4110   3914    -55   -237   -137       C
ATOM   2159  N   MET A 300     -15.775 -49.241 -21.066  1.00 20.27           N
ANISOU 2159  N   MET A 300     2233   3009   2460    205   -245     68       N
ATOM   2160  CA  MET A 300     -15.862 -50.706 -21.028  1.00 20.12           C
ANISOU 2160  CA  MET A 300     2249   2979   2417    262   -229    133       C
ATOM   2161  C   MET A 300     -16.651 -51.216 -22.230  1.00 19.16           C
ANISOU 2161  C   MET A 300     2171   2774   2336    243   -180    164       C
ATOM   2162  O   MET A 300     -16.163 -52.055 -22.979  1.00 19.18           O
ANISOU 2162  O   MET A 300     2175   2753   2361    269   -165    191       O
ATOM   2163  CB  MET A 300     -16.522 -51.194 -19.728  1.00 20.61           C
ANISOU 2163  CB  MET A 300     2351   3071   2409    302   -237    163       C
ATOM   2164  CG  MET A 300     -16.651 -52.714 -19.637  1.00 21.21           C
ANISOU 2164  CG  MET A 300     2467   3124   2467    360   -215    238       C
ATOM   2165  SD  MET A 300     -17.768 -53.297 -18.348  1.00 23.57           S
ANISOU 2165  SD  MET A 300     2824   3434   2698    395   -198    292       S
ATOM   2166  CE  MET A 300     -19.337 -52.622 -18.902  1.00 23.30           C
ANISOU 2166  CE  MET A 300     2823   3332   2699    322   -157    277       C
ATOM   2167  N   TYR A 301     -17.866 -50.707 -22.416  1.00 18.81           N
ANISOU 2167  N   TYR A 301     2161   2688   2299    201   -157    156       N
ATOM   2168  CA  TYR A 301     -18.692 -51.127 -23.553  1.00 17.93           C
ANISOU 2168  CA  TYR A 301     2086   2501   2223    181   -118    176       C
ATOM   2169  C   TYR A 301     -18.114 -50.670 -24.894  1.00 17.38           C
ANISOU 2169  C   TYR A 301     1991   2409   2202    158   -106    153       C
ATOM   2170  O   TYR A 301     -18.218 -51.387 -25.882  1.00 17.35           O
ANISOU 2170  O   TYR A 301     2010   2362   2221    169    -83    173       O
ATOM   2171  CB  TYR A 301     -20.139 -50.660 -23.407  1.00 17.69           C
ANISOU 2171  CB  TYR A 301     2090   2442   2190    146    -99    173       C
ATOM   2172  CG  TYR A 301     -20.977 -51.570 -22.531  1.00 17.38           C
ANISOU 2172  CG  TYR A 301     2090   2398   2117    171    -88    220       C
ATOM   2173  CD1 TYR A 301     -21.276 -52.867 -22.936  1.00 18.20           C
ANISOU 2173  CD1 TYR A 301     2225   2452   2238    190    -67    267       C
ATOM   2174  CD2 TYR A 301     -21.465 -51.141 -21.307  1.00 18.36           C
ANISOU 2174  CD2 TYR A 301     2218   2564   2194    177    -95    219       C
ATOM   2175  CE1 TYR A 301     -22.034 -53.717 -22.141  1.00 18.55           C
ANISOU 2175  CE1 TYR A 301     2302   2484   2261    210    -50    318       C
ATOM   2176  CE2 TYR A 301     -22.236 -51.984 -20.500  1.00 17.97           C
ANISOU 2176  CE2 TYR A 301     2202   2511   2113    203    -75    272       C
ATOM   2177  CZ  TYR A 301     -22.523 -53.267 -20.929  1.00 17.83           C
ANISOU 2177  CZ  TYR A 301     2214   2440   2123    216    -50    325       C
ATOM   2178  OH  TYR A 301     -23.281 -54.111 -20.142  1.00 18.57           O
ANISOU 2178  OH  TYR A 301     2338   2523   2196    237    -24    385       O
ATOM   2179  N   ALA A 302     -17.493 -49.491 -24.931  1.00 17.10           N
ANISOU 2179  N   ALA A 302     1910   2403   2185    128   -119    112       N
ATOM   2180  CA  ALA A 302     -16.872 -49.023 -26.174  1.00 16.80           C
ANISOU 2180  CA  ALA A 302     1843   2346   2193    109    -99    100       C
ATOM   2181  C   ALA A 302     -15.774 -49.988 -26.604  1.00 16.76           C
ANISOU 2181  C   ALA A 302     1817   2358   2195    156    -98    123       C
ATOM   2182  O   ALA A 302     -15.631 -50.283 -27.789  1.00 17.32           O
ANISOU 2182  O   ALA A 302     1896   2397   2288    164    -68    135       O
ATOM   2183  CB  ALA A 302     -16.313 -47.619 -26.020  1.00 16.69           C
ANISOU 2183  CB  ALA A 302     1778   2356   2206     66   -112     55       C
ATOM   2184  N   THR A 303     -15.012 -50.483 -25.633  1.00 17.30           N
ANISOU 2184  N   THR A 303     1860   2478   2236    194   -129    131       N
ATOM   2185  CA  THR A 303     -13.924 -51.417 -25.905  1.00 17.43           C
ANISOU 2185  CA  THR A 303     1851   2517   2255    248   -130    155       C
ATOM   2186  C   THR A 303     -14.466 -52.768 -26.359  1.00 17.49           C
ANISOU 2186  C   THR A 303     1921   2471   2252    289   -107    196       C
ATOM   2187  O   THR A 303     -13.943 -53.370 -27.306  1.00 17.54           O
ANISOU 2187  O   THR A 303     1928   2458   2277    320    -85    208       O
ATOM   2188  CB  THR A 303     -13.018 -51.589 -24.666  1.00 18.27           C
ANISOU 2188  CB  THR A 303     1913   2699   2330    285   -176    152       C
ATOM   2189  OG1 THR A 303     -12.422 -50.330 -24.327  1.00 18.25           O
ANISOU 2189  OG1 THR A 303     1845   2742   2347    242   -203    103       O
ATOM   2190  CG2 THR A 303     -11.910 -52.592 -24.924  1.00 17.43           C
ANISOU 2190  CG2 THR A 303     1779   2617   2225    350   -177    181       C
ATOM   2191  N   ILE A 304     -15.517 -53.242 -25.691  1.00 17.54           N
ANISOU 2191  N   ILE A 304     1980   2451   2232    291   -108    216       N
ATOM   2192  CA  ILE A 304     -16.133 -54.516 -26.052  1.00 17.54           C
ANISOU 2192  CA  ILE A 304     2041   2390   2234    320    -87    253       C
ATOM   2193  C   ILE A 304     -16.653 -54.488 -27.490  1.00 17.08           C
ANISOU 2193  C   ILE A 304     2008   2270   2210    295    -57    238       C
ATOM   2194  O   ILE A 304     -16.394 -55.416 -28.252  1.00 16.83           O
ANISOU 2194  O   ILE A 304     2000   2204   2191    331    -43    250       O
ATOM   2195  CB  ILE A 304     -17.260 -54.917 -25.061  1.00 17.70           C
ANISOU 2195  CB  ILE A 304     2106   2391   2229    315    -87    281       C
ATOM   2196  CG1 ILE A 304     -16.654 -55.302 -23.712  1.00 18.96           C
ANISOU 2196  CG1 ILE A 304     2252   2611   2343    365   -112    308       C
ATOM   2197  CG2 ILE A 304     -18.082 -56.089 -25.610  1.00 17.90           C
ANISOU 2197  CG2 ILE A 304     2191   2336   2275    324    -61    311       C
ATOM   2198  CD1 ILE A 304     -17.672 -55.437 -22.590  1.00 19.62           C
ANISOU 2198  CD1 ILE A 304     2370   2695   2390    362   -109    337       C
ATOM   2199  N   TRP A 305     -17.372 -53.424 -27.858  1.00 16.53           N
ANISOU 2199  N   TRP A 305     1938   2192   2152    239    -50    210       N
ATOM   2200  CA  TRP A 305     -17.932 -53.298 -29.201  1.00 16.35           C
ANISOU 2200  CA  TRP A 305     1939   2121   2152    220    -26    196       C
ATOM   2201  C   TRP A 305     -16.862 -53.122 -30.283  1.00 16.73           C
ANISOU 2201  C   TRP A 305     1957   2183   2216    241    -10    186       C
ATOM   2202  O   TRP A 305     -17.011 -53.652 -31.386  1.00 16.50           O
ANISOU 2202  O   TRP A 305     1959   2117   2194    260      8    184       O
ATOM   2203  CB  TRP A 305     -18.973 -52.168 -29.264  1.00 16.08           C
ANISOU 2203  CB  TRP A 305     1910   2077   2123    163    -22    175       C
ATOM   2204  CG  TRP A 305     -20.302 -52.543 -28.657  1.00 16.12           C
ANISOU 2204  CG  TRP A 305     1954   2052   2120    146    -25    187       C
ATOM   2205  CD1 TRP A 305     -20.834 -52.084 -27.488  1.00 16.35           C
ANISOU 2205  CD1 TRP A 305     1978   2104   2128    127    -35    190       C
ATOM   2206  CD2 TRP A 305     -21.260 -53.466 -29.196  1.00 16.25           C
ANISOU 2206  CD2 TRP A 305     2016   2011   2149    146    -16    198       C
ATOM   2207  NE1 TRP A 305     -22.071 -52.653 -27.273  1.00 16.34           N
ANISOU 2207  NE1 TRP A 305     2014   2066   2129    116    -26    210       N
ATOM   2208  CE2 TRP A 305     -22.354 -53.503 -28.309  1.00 17.43           C
ANISOU 2208  CE2 TRP A 305     2179   2151   2292    122    -16    213       C
ATOM   2209  CE3 TRP A 305     -21.301 -54.256 -30.349  1.00 17.68           C
ANISOU 2209  CE3 TRP A 305     2224   2146   2347    164     -8    192       C
ATOM   2210  CZ2 TRP A 305     -23.479 -54.306 -28.536  1.00 17.84           C
ANISOU 2210  CZ2 TRP A 305     2266   2149   2364    109     -9    226       C
ATOM   2211  CZ3 TRP A 305     -22.414 -55.044 -30.577  1.00 18.32           C
ANISOU 2211  CZ3 TRP A 305     2343   2171   2445    151     -7    196       C
ATOM   2212  CH2 TRP A 305     -23.487 -55.067 -29.672  1.00 17.86           C
ANISOU 2212  CH2 TRP A 305     2293   2104   2390    121     -8    214       C
ATOM   2213  N   LEU A 306     -15.799 -52.379 -29.969  1.00 17.02           N
ANISOU 2213  N   LEU A 306     1933   2274   2258    237    -17    178       N
ATOM   2214  CA  LEU A 306     -14.640 -52.249 -30.858  1.00 17.75           C
ANISOU 2214  CA  LEU A 306     1985   2391   2370    260      3    177       C
ATOM   2215  C   LEU A 306     -14.054 -53.629 -31.169  1.00 17.85           C
ANISOU 2215  C   LEU A 306     2015   2395   2373    330      9    198       C
ATOM   2216  O   LEU A 306     -13.830 -53.975 -32.334  1.00 17.90           O
ANISOU 2216  O   LEU A 306     2036   2382   2384    358     37    198       O
ATOM   2217  CB  LEU A 306     -13.577 -51.337 -30.223  1.00 18.30           C
ANISOU 2217  CB  LEU A 306     1976   2523   2455    242    -12    165       C
ATOM   2218  CG  LEU A 306     -12.265 -51.086 -30.983  1.00 20.73           C
ANISOU 2218  CG  LEU A 306     2221   2865   2791    259     12    168       C
ATOM   2219  CD1 LEU A 306     -12.504 -50.905 -32.437  1.00 24.11           C
ANISOU 2219  CD1 LEU A 306     2673   3258   3229    260     58    174       C
ATOM   2220  CD2 LEU A 306     -11.544 -49.862 -30.428  1.00 23.39           C
ANISOU 2220  CD2 LEU A 306     2480   3247   3158    212     -3    146       C
ATOM   2221  N   ARG A 307     -13.833 -54.421 -30.125  1.00 18.11           N
ANISOU 2221  N   ARG A 307     2050   2442   2388    362    -16    217       N
ATOM   2222  CA  ARG A 307     -13.331 -55.779 -30.293  1.00 18.71           C
ANISOU 2222  CA  ARG A 307     2150   2501   2458    433    -11    241       C
ATOM   2223  C   ARG A 307     -14.294 -56.607 -31.130  1.00 18.53           C
ANISOU 2223  C   ARG A 307     2203   2399   2439    441      6    239       C
ATOM   2224  O   ARG A 307     -13.863 -57.360 -32.002  1.00 19.03           O
ANISOU 2224  O   ARG A 307     2286   2440   2506    490     24    238       O
ATOM   2225  CB  ARG A 307     -13.093 -56.454 -28.941  1.00 19.01           C
ANISOU 2225  CB  ARG A 307     2186   2563   2473    468    -40    269       C
ATOM   2226  CG  ARG A 307     -11.942 -55.859 -28.155  1.00 19.73           C
ANISOU 2226  CG  ARG A 307     2197   2741   2556    478    -66    265       C
ATOM   2227  CD  ARG A 307     -11.816 -56.511 -26.794  1.00 20.10           C
ANISOU 2227  CD  ARG A 307     2250   2819   2569    520    -98    295       C
ATOM   2228  NE  ARG A 307     -10.755 -55.910 -25.987  1.00 19.84           N
ANISOU 2228  NE  ARG A 307     2137   2876   2524    529   -134    282       N
ATOM   2229  CZ  ARG A 307     -10.317 -56.412 -24.837  1.00 22.76           C
ANISOU 2229  CZ  ARG A 307     2494   3296   2856    581   -167    306       C
ATOM   2230  NH1 ARG A 307     -10.844 -57.532 -24.342  1.00 23.54           N
ANISOU 2230  NH1 ARG A 307     2659   3357   2928    628   -162    352       N
ATOM   2231  NH2 ARG A 307      -9.350 -55.797 -24.170  1.00 22.87           N
ANISOU 2231  NH2 ARG A 307     2429   3399   2860    586   -207    284       N
ATOM   2232  N   GLU A 308     -15.593 -56.461 -30.868  1.00 18.32           N
ANISOU 2232  N   GLU A 308     2217   2332   2412    393      0    234       N
ATOM   2233  CA  GLU A 308     -16.619 -57.207 -31.606  1.00 18.19           C
ANISOU 2233  CA  GLU A 308     2266   2239   2406    390      9    226       C
ATOM   2234  C   GLU A 308     -16.611 -56.872 -33.096  1.00 18.14           C
ANISOU 2234  C   GLU A 308     2267   2222   2404    391     28    195       C
ATOM   2235  O   GLU A 308     -16.733 -57.767 -33.937  1.00 18.10           O
ANISOU 2235  O   GLU A 308     2306   2170   2401    425     36    183       O
ATOM   2236  CB  GLU A 308     -18.008 -56.942 -31.012  1.00 18.27           C
ANISOU 2236  CB  GLU A 308     2301   2221   2420    333     -1    227       C
ATOM   2237  CG  GLU A 308     -19.173 -57.611 -31.745  1.00 18.22           C
ANISOU 2237  CG  GLU A 308     2351   2139   2432    316      2    212       C
ATOM   2238  CD  GLU A 308     -19.089 -59.132 -31.800  1.00 20.11           C
ANISOU 2238  CD  GLU A 308     2636   2317   2687    361      3    227       C
ATOM   2239  OE1 GLU A 308     -19.829 -59.732 -32.620  1.00 20.09           O
ANISOU 2239  OE1 GLU A 308     2677   2251   2707    353      2    203       O
ATOM   2240  OE2 GLU A 308     -18.289 -59.745 -31.049  1.00 21.03           O
ANISOU 2240  OE2 GLU A 308     2746   2447   2797    406      3    261       O
ATOM   2241  N   HIS A 309     -16.461 -55.592 -33.426  1.00 17.61           N
ANISOU 2241  N   HIS A 309     2161   2196   2336    357     38    182       N
ATOM   2242  CA  HIS A 309     -16.381 -55.194 -34.825  1.00 17.56           C
ANISOU 2242  CA  HIS A 309     2159   2187   2325    365     63    163       C
ATOM   2243  C   HIS A 309     -15.230 -55.915 -35.508  1.00 17.79           C
ANISOU 2243  C   HIS A 309     2183   2230   2349    435     83    167       C
ATOM   2244  O   HIS A 309     -15.392 -56.476 -36.589  1.00 17.97           O
ANISOU 2244  O   HIS A 309     2246   2221   2359    471     95    149       O
ATOM   2245  CB  HIS A 309     -16.187 -53.688 -34.987  1.00 17.13           C
ANISOU 2245  CB  HIS A 309     2058   2175   2277    323     78    160       C
ATOM   2246  CG  HIS A 309     -15.985 -53.267 -36.409  1.00 17.36           C
ANISOU 2246  CG  HIS A 309     2089   2208   2297    342    112    153       C
ATOM   2247  ND1 HIS A 309     -17.034 -52.936 -37.243  1.00 16.45           N
ANISOU 2247  ND1 HIS A 309     2016   2066   2170    325    116    136       N
ATOM   2248  CD2 HIS A 309     -14.861 -53.168 -37.160  1.00 18.33           C
ANISOU 2248  CD2 HIS A 309     2181   2366   2419    382    145    163       C
ATOM   2249  CE1 HIS A 309     -16.560 -52.626 -38.438  1.00 16.51           C
ANISOU 2249  CE1 HIS A 309     2021   2091   2163    357    150    138       C
ATOM   2250  NE2 HIS A 309     -15.245 -52.758 -38.415  1.00 17.25           N
ANISOU 2250  NE2 HIS A 309     2070   2221   2264    391    172    156       N
ATOM   2251  N   ASN A 310     -14.061 -55.884 -34.880  1.00 18.49           N
ANISOU 2251  N   ASN A 310     2216   2367   2442    459     84    188       N
ATOM   2252  CA  ASN A 310     -12.877 -56.488 -35.481  1.00 18.91           C
ANISOU 2252  CA  ASN A 310     2251   2443   2491    530    107    195       C
ATOM   2253  C   ASN A 310     -12.965 -58.015 -35.523  1.00 19.32           C
ANISOU 2253  C   ASN A 310     2362   2443   2537    591     99    195       C
ATOM   2254  O   ASN A 310     -12.422 -58.645 -36.437  1.00 19.83           O
ANISOU 2254  O   ASN A 310     2444   2500   2591    654    121    187       O
ATOM   2255  CB  ASN A 310     -11.612 -56.026 -34.765  1.00 19.31           C
ANISOU 2255  CB  ASN A 310     2217   2567   2555    538    106    216       C
ATOM   2256  CG  ASN A 310     -11.242 -54.586 -35.100  1.00 19.22           C
ANISOU 2256  CG  ASN A 310     2143   2599   2560    489    127    213       C
ATOM   2257  OD1 ASN A 310     -11.872 -53.949 -35.938  1.00 18.08           O
ANISOU 2257  OD1 ASN A 310     2022   2434   2414    460    148    203       O
ATOM   2258  ND2 ASN A 310     -10.205 -54.078 -34.450  1.00 18.71           N
ANISOU 2258  ND2 ASN A 310     1996   2595   2516    482    120    223       N
ATOM   2259  N   ARG A 311     -13.660 -58.600 -34.549  1.00 19.14           N
ANISOU 2259  N   ARG A 311     2372   2381   2520    574     70    206       N
ATOM   2260  CA  ARG A 311     -13.923 -60.038 -34.544  1.00 19.82           C
ANISOU 2260  CA  ARG A 311     2521   2398   2610    620     64    208       C
ATOM   2261  C   ARG A 311     -14.807 -60.430 -35.729  1.00 19.45           C
ANISOU 2261  C   ARG A 311     2540   2287   2565    617     69    168       C
ATOM   2262  O   ARG A 311     -14.560 -61.442 -36.387  1.00 20.05           O
ANISOU 2262  O   ARG A 311     2659   2320   2641    676     76    152       O
ATOM   2263  CB  ARG A 311     -14.601 -60.459 -33.238  1.00 19.86           C
ANISOU 2263  CB  ARG A 311     2546   2373   2625    593     40    236       C
ATOM   2264  CG  ARG A 311     -14.739 -61.970 -33.051  1.00 20.50           C
ANISOU 2264  CG  ARG A 311     2688   2379   2722    642     38    251       C
ATOM   2265  CD  ARG A 311     -15.614 -62.297 -31.862  1.00 21.43           C
ANISOU 2265  CD  ARG A 311     2829   2462   2851    607     23    284       C
ATOM   2266  NE  ARG A 311     -17.022 -62.035 -32.152  1.00 21.37           N
ANISOU 2266  NE  ARG A 311     2853   2406   2862    535     18    260       N
ATOM   2267  CZ  ARG A 311     -17.864 -62.908 -32.709  1.00 23.18           C
ANISOU 2267  CZ  ARG A 311     3141   2545   3121    527     18    240       C
ATOM   2268  NH1 ARG A 311     -17.464 -64.132 -33.031  1.00 24.27           N
ANISOU 2268  NH1 ARG A 311     3322   2622   3276    586     24    241       N
ATOM   2269  NH2 ARG A 311     -19.124 -62.555 -32.948  1.00 22.89           N
ANISOU 2269  NH2 ARG A 311     3119   2478   3101    459      9    217       N
ATOM   2270  N   VAL A 312     -15.845 -59.638 -35.981  1.00 18.91           N
ANISOU 2270  N   VAL A 312     2478   2210   2497    551     61    148       N
ATOM   2271  CA  VAL A 312     -16.729 -59.878 -37.117  1.00 18.91           C
ANISOU 2271  CA  VAL A 312     2531   2160   2492    545     58    105       C
ATOM   2272  C   VAL A 312     -15.969 -59.704 -38.439  1.00 19.29           C
ANISOU 2272  C   VAL A 312     2577   2241   2511    601     86     84       C
ATOM   2273  O   VAL A 312     -16.159 -60.486 -39.372  1.00 20.20           O
ANISOU 2273  O   VAL A 312     2745   2314   2616    643     84     47       O
ATOM   2274  CB  VAL A 312     -18.004 -59.000 -37.037  1.00 18.33           C
ANISOU 2274  CB  VAL A 312     2458   2083   2424    468     43     94       C
ATOM   2275  CG1 VAL A 312     -18.783 -59.042 -38.338  1.00 18.61           C
ANISOU 2275  CG1 VAL A 312     2535   2090   2446    469     37     46       C
ATOM   2276  CG2 VAL A 312     -18.879 -59.464 -35.858  1.00 17.89           C
ANISOU 2276  CG2 VAL A 312     2417   1984   2397    424     21    113       C
ATOM   2277  N   CYS A 313     -15.077 -58.717 -38.502  1.00 19.23           N
ANISOU 2277  N   CYS A 313     2508   2307   2492    604    112    106       N
ATOM   2278  CA  CYS A 313     -14.225 -58.532 -39.681  1.00 20.00           C
ANISOU 2278  CA  CYS A 313     2593   2443   2561    662    149     99       C
ATOM   2279  C   CYS A 313     -13.423 -59.803 -39.980  1.00 20.77           C
ANISOU 2279  C   CYS A 313     2717   2522   2652    749    159     92       C
ATOM   2280  O   CYS A 313     -13.336 -60.220 -41.134  1.00 21.46           O
ANISOU 2280  O   CYS A 313     2844   2599   2711    805    175     61       O
ATOM   2281  CB  CYS A 313     -13.264 -57.355 -39.498  1.00 19.62           C
ANISOU 2281  CB  CYS A 313     2463   2473   2518    646    179    133       C
ATOM   2282  SG  CYS A 313     -14.029 -55.739 -39.681  1.00 19.80           S
ANISOU 2282  SG  CYS A 313     2463   2517   2543    566    186    136       S
ATOM   2283  N   ASP A 314     -12.855 -60.418 -38.943  1.00 21.27           N
ANISOU 2283  N   ASP A 314     2762   2583   2738    767    148    120       N
ATOM   2284  CA  ASP A 314     -12.087 -61.657 -39.118  1.00 22.62           C
ANISOU 2284  CA  ASP A 314     2958   2730   2906    856    158    118       C
ATOM   2285  C   ASP A 314     -12.971 -62.772 -39.686  1.00 22.98           C
ANISOU 2285  C   ASP A 314     3096   2680   2953    876    139     73       C
ATOM   2286  O   ASP A 314     -12.548 -63.508 -40.582  1.00 24.03           O
ANISOU 2286  O   ASP A 314     3267   2794   3067    952    155     44       O
ATOM   2287  CB  ASP A 314     -11.462 -62.129 -37.796  1.00 22.85           C
ANISOU 2287  CB  ASP A 314     2955   2769   2958    872    144    161       C
ATOM   2288  CG  ASP A 314     -10.279 -61.283 -37.353  1.00 23.80           C
ANISOU 2288  CG  ASP A 314     2977   2987   3077    877    160    196       C
ATOM   2289  OD1 ASP A 314      -9.626 -60.640 -38.200  1.00 25.27           O
ANISOU 2289  OD1 ASP A 314     3123   3228   3251    894    194    193       O
ATOM   2290  OD2 ASP A 314      -9.993 -61.286 -36.134  1.00 26.08           O
ANISOU 2290  OD2 ASP A 314     3230   3300   3380    865    137    228       O
ATOM   2291  N   ILE A 315     -14.193 -62.886 -39.164  1.00 22.67           N
ANISOU 2291  N   ILE A 315     3092   2583   2939    808    105     64       N
ATOM   2292  CA  ILE A 315     -15.134 -63.910 -39.619  1.00 23.03           C
ANISOU 2292  CA  ILE A 315     3218   2532   3001    810     82     18       C
ATOM   2293  C   ILE A 315     -15.500 -63.712 -41.088  1.00 23.07           C
ANISOU 2293  C   ILE A 315     3257   2539   2970    828     83    -42       C
ATOM   2294  O   ILE A 315     -15.480 -64.663 -41.874  1.00 23.67           O
ANISOU 2294  O   ILE A 315     3392   2563   3039    885     79    -89       O
ATOM   2295  CB  ILE A 315     -16.419 -63.935 -38.753  1.00 22.68           C
ANISOU 2295  CB  ILE A 315     3189   2434   2995    723     50     25       C
ATOM   2296  CG1 ILE A 315     -16.097 -64.448 -37.345  1.00 24.15           C
ANISOU 2296  CG1 ILE A 315     3361   2605   3210    725     49     83       C
ATOM   2297  CG2 ILE A 315     -17.486 -64.821 -39.387  1.00 23.35           C
ANISOU 2297  CG2 ILE A 315     3345   2422   3103    710     23    -31       C
ATOM   2298  CD1 ILE A 315     -17.279 -64.404 -36.392  1.00 23.85           C
ANISOU 2298  CD1 ILE A 315     3330   2526   3206    645     28    104       C
ATOM   2299  N   LEU A 316     -15.814 -62.475 -41.462  1.00 22.45           N
ANISOU 2299  N   LEU A 316     3145   2520   2867    784     90    -41       N
ATOM   2300  CA  LEU A 316     -16.199 -62.168 -42.836  1.00 22.86           C
ANISOU 2300  CA  LEU A 316     3226   2584   2874    805     92    -90       C
ATOM   2301  C   LEU A 316     -15.032 -62.338 -43.809  1.00 23.77           C
ANISOU 2301  C   LEU A 316     3342   2745   2943    902    133    -97       C
ATOM   2302  O   LEU A 316     -15.232 -62.751 -44.953  1.00 24.17           O
ANISOU 2302  O   LEU A 316     3447   2781   2956    953    130   -151       O
ATOM   2303  CB  LEU A 316     -16.779 -60.755 -42.937  1.00 22.01           C
ANISOU 2303  CB  LEU A 316     3081   2530   2752    740     94    -75       C
ATOM   2304  CG  LEU A 316     -18.142 -60.549 -42.272  1.00 21.76           C
ANISOU 2304  CG  LEU A 316     3056   2458   2755    652     54    -81       C
ATOM   2305  CD1 LEU A 316     -18.541 -59.082 -42.350  1.00 20.48           C
ANISOU 2305  CD1 LEU A 316     2852   2352   2576    601     63    -61       C
ATOM   2306  CD2 LEU A 316     -19.210 -61.429 -42.910  1.00 22.62           C
ANISOU 2306  CD2 LEU A 316     3231   2495   2870    650     12   -147       C
ATOM   2307  N   LYS A 317     -13.816 -62.034 -43.355  1.00 24.28           N
ANISOU 2307  N   LYS A 317     3346   2868   3011    931    170    -44       N
ATOM   2308  CA  LYS A 317     -12.635 -62.212 -44.193  1.00 25.52           C
ANISOU 2308  CA  LYS A 317     3493   3074   3131   1026    217    -42       C
ATOM   2309  C   LYS A 317     -12.401 -63.691 -44.518  1.00 26.45           C
ANISOU 2309  C   LYS A 317     3677   3127   3245   1108    208    -84       C
ATOM   2310  O   LYS A 317     -12.013 -64.029 -45.636  1.00 26.75           O
ANISOU 2310  O   LYS A 317     3750   3179   3237   1190    232   -118       O
ATOM   2311  CB  LYS A 317     -11.393 -61.618 -43.526  1.00 25.90           C
ANISOU 2311  CB  LYS A 317     3450   3197   3195   1032    254     23       C
ATOM   2312  CG  LYS A 317     -10.139 -61.762 -44.382  1.00 28.44           C
ANISOU 2312  CG  LYS A 317     3748   3576   3481   1131    309     32       C
ATOM   2313  CD  LYS A 317      -9.088 -60.712 -44.064  1.00 30.35           C
ANISOU 2313  CD  LYS A 317     3886   3910   3737   1116    352     93       C
ATOM   2314  CE  LYS A 317      -8.118 -60.576 -45.225  1.00 32.62           C
ANISOU 2314  CE  LYS A 317     4151   4261   3983   1201    418    103       C
ATOM   2315  NZ  LYS A 317      -8.726 -59.837 -46.380  1.00 33.02           N
ANISOU 2315  NZ  LYS A 317     4232   4327   3985   1194    440     87       N
ATOM   2316  N   GLN A 318     -12.624 -64.556 -43.529  1.00 26.50           N
ANISOU 2316  N   GLN A 318     3704   3063   3301   1091    178    -77       N
ATOM   2317  CA  GLN A 318     -12.552 -66.004 -43.723  1.00 27.77           C
ANISOU 2317  CA  GLN A 318     3936   3140   3474   1159    166   -117       C
ATOM   2318  C   GLN A 318     -13.602 -66.471 -44.738  1.00 27.54           C
ANISOU 2318  C   GLN A 318     3990   3045   3429   1157    133   -200       C
ATOM   2319  O   GLN A 318     -13.301 -67.295 -45.609  1.00 28.30           O
ANISOU 2319  O   GLN A 318     4142   3110   3499   1242    139   -253       O
ATOM   2320  CB  GLN A 318     -12.728 -66.732 -42.382  1.00 28.08           C
ANISOU 2320  CB  GLN A 318     3982   3112   3575   1129    142    -82       C
ATOM   2321  CG  GLN A 318     -12.726 -68.269 -42.454  1.00 31.96           C
ANISOU 2321  CG  GLN A 318     4552   3497   4095   1191    130   -116       C
ATOM   2322  CD  GLN A 318     -11.333 -68.883 -42.492  1.00 36.63           C
ANISOU 2322  CD  GLN A 318     5132   4113   4672   1305    167    -92       C
ATOM   2323  OE1 GLN A 318     -10.349 -68.222 -42.838  1.00 39.80           O
ANISOU 2323  OE1 GLN A 318     5472   4616   5034   1349    204    -68       O
ATOM   2324  NE2 GLN A 318     -11.247 -70.165 -42.136  1.00 39.39           N
ANISOU 2324  NE2 GLN A 318     5538   4368   5059   1353    159    -97       N
ATOM   2325  N  BGLU A 319     -14.815 -65.938 -44.623  0.38 26.39           N
ANISOU 2325  N  BGLU A 319     3848   2881   3297   1065     98   -215       N
ATOM   2326  N  CGLU A 319     -14.824 -65.955 -44.616  0.62 26.88           N
ANISOU 2326  N  CGLU A 319     3912   2942   3361   1065     97   -216       N
ATOM   2327  CA BGLU A 319     -15.908 -66.289 -45.527  0.38 26.26           C
ANISOU 2327  CA BGLU A 319     3899   2811   3269   1053     57   -297       C
ATOM   2328  CA CGLU A 319     -15.903 -66.305 -45.551  0.62 27.24           C
ANISOU 2328  CA CGLU A 319     4024   2934   3392   1054     57   -299       C
ATOM   2329  C  BGLU A 319     -15.749 -65.661 -46.914  0.38 26.45           C
ANISOU 2329  C  BGLU A 319     3931   2908   3211   1106     75   -334       C
ATOM   2330  C  CGLU A 319     -15.700 -65.686 -46.933  0.62 27.03           C
ANISOU 2330  C  CGLU A 319     4005   2982   3283   1110     76   -334       C
ATOM   2331  O  BGLU A 319     -16.204 -66.230 -47.910  0.38 27.06           O
ANISOU 2331  O  BGLU A 319     4074   2951   3258   1145     48   -414       O
ATOM   2332  O  CGLU A 319     -16.074 -66.288 -47.945  0.62 27.65           O
ANISOU 2332  O  CGLU A 319     4149   3027   3330   1156     52   -413       O
ATOM   2333  CB BGLU A 319     -17.248 -65.871 -44.916  0.38 25.45           C
ANISOU 2333  CB BGLU A 319     3785   2675   3208    939     15   -295       C
ATOM   2334  CB CGLU A 319     -17.287 -65.901 -45.011  0.62 26.89           C
ANISOU 2334  CB CGLU A 319     3972   2856   3389    941     13   -302       C
ATOM   2335  CG BGLU A 319     -17.596 -66.629 -43.649  0.38 24.59           C
ANISOU 2335  CG BGLU A 319     3683   2484   3179    889     -3   -265       C
ATOM   2336  CG CGLU A 319     -18.166 -67.079 -44.576  0.62 29.02           C
ANISOU 2336  CG CGLU A 319     4296   3003   3728    904    -31   -339       C
ATOM   2337  CD BGLU A 319     -17.550 -68.134 -43.849  0.38 24.25           C
ANISOU 2337  CD BGLU A 319     3712   2333   3170    940    -19   -313       C
ATOM   2338  CD CGLU A 319     -19.563 -67.022 -45.171  0.62 30.09           C
ANISOU 2338  CD CGLU A 319     4460   3103   3870    844    -84   -408       C
ATOM   2339  OE1BGLU A 319     -18.206 -68.623 -44.790  0.38 23.00           O
ANISOU 2339  OE1BGLU A 319     3609   2124   3005    948    -52   -396       O
ATOM   2340  OE1CGLU A 319     -20.224 -65.964 -45.066  0.62 32.38           O
ANISOU 2340  OE1CGLU A 319     4708   3447   4149    780    -92   -389       O
ATOM   2341  OE2BGLU A 319     -16.861 -68.824 -43.067  0.38 24.23           O
ANISOU 2341  OE2BGLU A 319     3711   2296   3201    973      1   -269       O
ATOM   2342  OE2CGLU A 319     -20.004 -68.038 -45.745  0.62 30.43           O
ANISOU 2342  OE2CGLU A 319     4565   3062   3932    863   -119   -485       O
ATOM   2343  N   HIS A 320     -15.110 -64.495 -46.971  1.00 25.82           N
ANISOU 2343  N   HIS A 320     3786   2929   3097   1107    120   -276       N
ATOM   2344  CA  HIS A 320     -14.950 -63.745 -48.215  1.00 25.84           C
ANISOU 2344  CA  HIS A 320     3788   3008   3021   1154    148   -290       C
ATOM   2345  C   HIS A 320     -13.515 -63.249 -48.407  1.00 25.95           C
ANISOU 2345  C   HIS A 320     3746   3109   3004   1220    220   -231       C
ATOM   2346  O   HIS A 320     -13.234 -62.057 -48.242  1.00 25.25           O
ANISOU 2346  O   HIS A 320     3591   3091   2912   1183    254   -171       O
ATOM   2347  CB  HIS A 320     -15.908 -62.549 -48.235  1.00 24.99           C
ANISOU 2347  CB  HIS A 320     3655   2935   2907   1071    131   -276       C
ATOM   2348  CG  HIS A 320     -17.356 -62.921 -48.143  1.00 24.54           C
ANISOU 2348  CG  HIS A 320     3640   2805   2877   1006     62   -334       C
ATOM   2349  ND1 HIS A 320     -18.077 -63.391 -49.220  1.00 25.20           N
ANISOU 2349  ND1 HIS A 320     3789   2866   2920   1040     22   -418       N
ATOM   2350  CD2 HIS A 320     -18.225 -62.868 -47.105  1.00 23.59           C
ANISOU 2350  CD2 HIS A 320     3503   2637   2823    910     26   -319       C
ATOM   2351  CE1 HIS A 320     -19.324 -63.623 -48.844  1.00 24.55           C
ANISOU 2351  CE1 HIS A 320     3721   2721   2885    961    -37   -454       C
ATOM   2352  NE2 HIS A 320     -19.437 -63.319 -47.565  1.00 23.13           N
ANISOU 2352  NE2 HIS A 320     3492   2525   2770    883    -32   -391       N
ATOM   2353  N   PRO A 321     -12.600 -64.156 -48.795  1.00 26.73           N
ANISOU 2353  N   PRO A 321     3869   3203   3084   1321    247   -248       N
ATOM   2354  CA  PRO A 321     -11.232 -63.707 -49.077  1.00 27.09           C
ANISOU 2354  CA  PRO A 321     3854   3338   3099   1389    320   -192       C
ATOM   2355  C   PRO A 321     -11.155 -62.715 -50.241  1.00 27.04           C
ANISOU 2355  C   PRO A 321     3837   3416   3019   1419    364   -183       C
ATOM   2356  O   PRO A 321     -10.174 -61.977 -50.354  1.00 27.30           O
ANISOU 2356  O   PRO A 321     3800   3530   3041   1443    430   -118       O
ATOM   2357  CB  PRO A 321     -10.494 -65.010 -49.425  1.00 28.14           C
ANISOU 2357  CB  PRO A 321     4034   3438   3218   1501    332   -230       C
ATOM   2358  CG  PRO A 321     -11.566 -65.969 -49.809  1.00 28.79           C
ANISOU 2358  CG  PRO A 321     4217   3423   3298   1503    269   -322       C
ATOM   2359  CD  PRO A 321     -12.749 -65.611 -48.972  1.00 27.40           C
ANISOU 2359  CD  PRO A 321     4033   3197   3178   1376    214   -317       C
ATOM   2360  N   GLU A 322     -12.190 -62.708 -51.083  1.00 27.03           N
ANISOU 2360  N   GLU A 322     3904   3397   2971   1419    328   -245       N
ATOM   2361  CA  GLU A 322     -12.284 -61.824 -52.248  1.00 27.06           C
ANISOU 2361  CA  GLU A 322     3911   3476   2893   1455    364   -239       C
ATOM   2362  C   GLU A 322     -12.737 -60.386 -51.928  1.00 26.36           C
ANISOU 2362  C   GLU A 322     3765   3428   2823   1362    374   -177       C
ATOM   2363  O   GLU A 322     -12.604 -59.490 -52.763  1.00 26.57           O
ANISOU 2363  O   GLU A 322     3778   3524   2792   1391    421   -145       O
ATOM   2364  CB  GLU A 322     -13.215 -62.456 -53.302  1.00 27.83           C
ANISOU 2364  CB  GLU A 322     4107   3542   2926   1503    313   -338       C
ATOM   2365  CG  GLU A 322     -14.729 -62.364 -53.039  1.00 27.17           C
ANISOU 2365  CG  GLU A 322     4053   3400   2870   1410    231   -385       C
ATOM   2366  CD  GLU A 322     -15.261 -63.294 -51.943  1.00 27.29           C
ANISOU 2366  CD  GLU A 322     4083   3309   2977   1340    170   -416       C
ATOM   2367  OE1 GLU A 322     -16.487 -63.237 -51.674  1.00 26.45           O
ANISOU 2367  OE1 GLU A 322     3992   3155   2901   1260    107   -450       O
ATOM   2368  OE2 GLU A 322     -14.481 -64.077 -51.357  1.00 27.24           O
ANISOU 2368  OE2 GLU A 322     4072   3267   3012   1367    186   -403       O
ATOM   2369  N   TRP A 323     -13.262 -60.171 -50.726  1.00 25.18           N
ANISOU 2369  N   TRP A 323     3584   3234   2751   1257    334   -158       N
ATOM   2370  CA  TRP A 323     -13.772 -58.857 -50.333  1.00 24.27           C
ANISOU 2370  CA  TRP A 323     3420   3144   2659   1167    337   -109       C
ATOM   2371  C   TRP A 323     -12.663 -57.876 -49.952  1.00 23.99           C
ANISOU 2371  C   TRP A 323     3294   3173   2650   1152    406    -22       C
ATOM   2372  O   TRP A 323     -11.610 -58.273 -49.451  1.00 24.62           O
ANISOU 2372  O   TRP A 323     3330   3263   2760   1177    433      5       O
ATOM   2373  CB  TRP A 323     -14.720 -59.014 -49.150  1.00 23.44           C
ANISOU 2373  CB  TRP A 323     3313   2970   2624   1065    271   -123       C
ATOM   2374  CG  TRP A 323     -16.129 -59.374 -49.506  1.00 22.97           C
ANISOU 2374  CG  TRP A 323     3318   2859   2549   1040    204   -192       C
ATOM   2375  CD1 TRP A 323     -16.609 -59.802 -50.714  1.00 23.17           C
ANISOU 2375  CD1 TRP A 323     3411   2886   2508   1104    183   -259       C
ATOM   2376  CD2 TRP A 323     -17.239 -59.367 -48.612  1.00 21.56           C
ANISOU 2376  CD2 TRP A 323     3139   2625   2428    945    147   -204       C
ATOM   2377  NE1 TRP A 323     -17.959 -60.038 -50.627  1.00 23.34           N
ANISOU 2377  NE1 TRP A 323     3467   2855   2546   1048    111   -314       N
ATOM   2378  CE2 TRP A 323     -18.372 -59.779 -49.347  1.00 22.38           C
ANISOU 2378  CE2 TRP A 323     3303   2697   2502    950     92   -278       C
ATOM   2379  CE3 TRP A 323     -17.390 -59.040 -47.261  1.00 21.16           C
ANISOU 2379  CE3 TRP A 323     3041   2553   2448    859    137   -161       C
ATOM   2380  CZ2 TRP A 323     -19.640 -59.868 -48.772  1.00 22.33           C
ANISOU 2380  CZ2 TRP A 323     3303   2638   2542    867     32   -305       C
ATOM   2381  CZ3 TRP A 323     -18.650 -59.132 -46.691  1.00 20.61           C
ANISOU 2381  CZ3 TRP A 323     2983   2431   2415    783     82   -185       C
ATOM   2382  CH2 TRP A 323     -19.756 -59.540 -47.444  1.00 21.33           C
ANISOU 2382  CH2 TRP A 323     3128   2491   2485    785     33   -254       C
ATOM   2383  N   GLY A 324     -12.920 -56.591 -50.183  1.00 23.58           N
ANISOU 2383  N   GLY A 324     3210   3160   2590   1110    433     22       N
ATOM   2384  CA  GLY A 324     -12.003 -55.521 -49.790  1.00 23.25           C
ANISOU 2384  CA  GLY A 324     3079   3168   2587   1076    495    102       C
ATOM   2385  C   GLY A 324     -12.356 -54.905 -48.447  1.00 22.02           C
ANISOU 2385  C   GLY A 324     2874   2983   2510    964    461    124       C
ATOM   2386  O   GLY A 324     -13.394 -55.214 -47.854  1.00 21.16           O
ANISOU 2386  O   GLY A 324     2800   2819   2420    912    396     85       O
ATOM   2387  N   ASP A 325     -11.489 -54.015 -47.975  1.00 21.67           N
ANISOU 2387  N   ASP A 325     2745   2977   2512    927    507    185       N
ATOM   2388  CA  ASP A 325     -11.677 -53.337 -46.690  1.00 20.97           C
ANISOU 2388  CA  ASP A 325     2604   2868   2495    826    478    204       C
ATOM   2389  C   ASP A 325     -13.040 -52.636 -46.562  1.00 19.99           C
ANISOU 2389  C   ASP A 325     2514   2709   2370    759    440    190       C
ATOM   2390  O   ASP A 325     -13.703 -52.761 -45.532  1.00 19.31           O
ANISOU 2390  O   ASP A 325     2432   2583   2321    697    385    169       O
ATOM   2391  CB  ASP A 325     -10.537 -52.334 -46.476  1.00 21.40           C
ANISOU 2391  CB  ASP A 325     2562   2972   2595    800    538    267       C
ATOM   2392  CG  ASP A 325     -10.772 -51.416 -45.305  1.00 21.20           C
ANISOU 2392  CG  ASP A 325     2487   2931   2638    697    511    281       C
ATOM   2393  OD1 ASP A 325     -10.578 -51.859 -44.149  1.00 21.13           O
ANISOU 2393  OD1 ASP A 325     2451   2909   2667    666    468    267       O
ATOM   2394  OD2 ASP A 325     -11.133 -50.242 -45.554  1.00 21.78           O
ANISOU 2394  OD2 ASP A 325     2550   3004   2723    653    536    307       O
ATOM   2395  N   GLU A 326     -13.470 -51.917 -47.596  1.00 20.24           N
ANISOU 2395  N   GLU A 326     2573   2760   2359    778    471    203       N
ATOM   2396  CA  GLU A 326     -14.725 -51.163 -47.490  1.00 19.42           C
ANISOU 2396  CA  GLU A 326     2495   2629   2256    721    439    196       C
ATOM   2397  C   GLU A 326     -15.916 -52.089 -47.240  1.00 19.04           C
ANISOU 2397  C   GLU A 326     2508   2531   2193    711    361    130       C
ATOM   2398  O   GLU A 326     -16.712 -51.825 -46.338  1.00 18.01           O
ANISOU 2398  O   GLU A 326     2373   2367   2103    639    319    121       O
ATOM   2399  CB  GLU A 326     -14.976 -50.272 -48.718  1.00 20.25           C
ANISOU 2399  CB  GLU A 326     2621   2766   2308    757    486    226       C
ATOM   2400  CG  GLU A 326     -16.207 -49.350 -48.600  1.00 20.13           C
ANISOU 2400  CG  GLU A 326     2624   2727   2298    702    459    228       C
ATOM   2401  CD  GLU A 326     -16.046 -48.206 -47.598  1.00 21.17           C
ANISOU 2401  CD  GLU A 326     2695   2843   2507    614    474    268       C
ATOM   2402  OE1 GLU A 326     -14.919 -47.949 -47.122  1.00 21.02           O
ANISOU 2402  OE1 GLU A 326     2612   2839   2538    594    511    302       O
ATOM   2403  OE2 GLU A 326     -17.066 -47.552 -47.283  1.00 21.41           O
ANISOU 2403  OE2 GLU A 326     2738   2847   2549    566    445    263       O
ATOM   2404  N   GLN A 327     -16.044 -53.162 -48.024  1.00 19.27           N
ANISOU 2404  N   GLN A 327     2596   2556   2172    782    344     84       N
ATOM   2405  CA  GLN A 327     -17.190 -54.073 -47.862  1.00 18.96           C
ANISOU 2405  CA  GLN A 327     2613   2463   2128    768    271     18       C
ATOM   2406  C   GLN A 327     -17.126 -54.814 -46.528  1.00 18.73           C
ANISOU 2406  C   GLN A 327     2566   2387   2163    720    234      8       C
ATOM   2407  O   GLN A 327     -18.154 -55.042 -45.893  1.00 17.99           O
ANISOU 2407  O   GLN A 327     2490   2249   2098    665    182    -17       O
ATOM   2408  CB  GLN A 327     -17.312 -55.066 -49.022  1.00 19.78           C
ANISOU 2408  CB  GLN A 327     2784   2566   2165    855    257    -39       C
ATOM   2409  CG  GLN A 327     -18.644 -55.840 -49.005  1.00 19.87           C
ANISOU 2409  CG  GLN A 327     2850   2522   2178    832    178   -112       C
ATOM   2410  CD  GLN A 327     -18.989 -56.522 -50.323  1.00 21.51           C
ANISOU 2410  CD  GLN A 327     3126   2736   2310    913    156   -178       C
ATOM   2411  OE1 GLN A 327     -20.128 -56.966 -50.521  1.00 23.86           O
ANISOU 2411  OE1 GLN A 327     3464   2999   2603    894     91   -240       O
ATOM   2412  NE2 GLN A 327     -18.028 -56.602 -51.225  1.00 19.36           N
ANISOU 2412  NE2 GLN A 327     2865   2511   1979   1002    208   -167       N
ATOM   2413  N   LEU A 328     -15.921 -55.185 -46.107  1.00 18.79           N
ANISOU 2413  N   LEU A 328     2538   2408   2192    745    263     33       N
ATOM   2414  CA  LEU A 328     -15.728 -55.785 -44.789  1.00 18.96           C
ANISOU 2414  CA  LEU A 328     2538   2396   2270    707    235     37       C
ATOM   2415  C   LEU A 328     -16.197 -54.838 -43.691  1.00 18.21           C
ANISOU 2415  C   LEU A 328     2400   2299   2220    616    219     64       C
ATOM   2416  O   LEU A 328     -16.922 -55.243 -42.785  1.00 18.21           O
ANISOU 2416  O   LEU A 328     2413   2257   2250    570    176     50       O
ATOM   2417  CB  LEU A 328     -14.261 -56.159 -44.573  1.00 19.29           C
ANISOU 2417  CB  LEU A 328     2537   2470   2323    756    272     66       C
ATOM   2418  CG  LEU A 328     -13.789 -57.366 -45.379  1.00 21.09           C
ANISOU 2418  CG  LEU A 328     2812   2688   2514    851    280     33       C
ATOM   2419  CD1 LEU A 328     -12.264 -57.437 -45.408  1.00 20.98           C
ANISOU 2419  CD1 LEU A 328     2742   2726   2503    908    333     71       C
ATOM   2420  CD2 LEU A 328     -14.383 -58.645 -44.812  1.00 20.85           C
ANISOU 2420  CD2 LEU A 328     2834   2581   2506    848    226     -9       C
ATOM   2421  N   PHE A 329     -15.792 -53.574 -43.778  1.00 18.09           N
ANISOU 2421  N   PHE A 329     2336   2327   2211    592    259    104       N
ATOM   2422  CA  PHE A 329     -16.193 -52.590 -42.785  1.00 17.42           C
ANISOU 2422  CA  PHE A 329     2213   2239   2167    511    246    124       C
ATOM   2423  C   PHE A 329     -17.705 -52.411 -42.750  1.00 17.12           C
ANISOU 2423  C   PHE A 329     2217   2165   2122    470    206     98       C
ATOM   2424  O   PHE A 329     -18.320 -52.471 -41.680  1.00 17.18           O
ANISOU 2424  O   PHE A 329     2219   2146   2161    417    171     92       O
ATOM   2425  CB  PHE A 329     -15.546 -51.225 -43.043  1.00 17.59           C
ANISOU 2425  CB  PHE A 329     2180   2301   2201    493    298    168       C
ATOM   2426  CG  PHE A 329     -16.101 -50.147 -42.170  1.00 16.86           C
ANISOU 2426  CG  PHE A 329     2061   2198   2148    414    284    178       C
ATOM   2427  CD1 PHE A 329     -15.702 -50.042 -40.846  1.00 17.47           C
ANISOU 2427  CD1 PHE A 329     2092   2277   2270    367    263    183       C
ATOM   2428  CD2 PHE A 329     -17.072 -49.279 -42.645  1.00 16.91           C
ANISOU 2428  CD2 PHE A 329     2091   2193   2140    392    287    180       C
ATOM   2429  CE1 PHE A 329     -16.247 -49.072 -40.015  1.00 16.49           C
ANISOU 2429  CE1 PHE A 329     1949   2141   2176    300    247    184       C
ATOM   2430  CE2 PHE A 329     -17.616 -48.312 -41.822  1.00 16.32           C
ANISOU 2430  CE2 PHE A 329     1997   2104   2101    325    274    186       C
ATOM   2431  CZ  PHE A 329     -17.197 -48.207 -40.505  1.00 16.22           C
ANISOU 2431  CZ  PHE A 329     1941   2091   2133    278    254    185       C
ATOM   2432  N   GLN A 330     -18.294 -52.173 -43.920  1.00 17.39           N
ANISOU 2432  N   GLN A 330     2290   2206   2114    500    213     84       N
ATOM   2433  CA  GLN A 330     -19.717 -51.843 -43.999  1.00 16.80           C
ANISOU 2433  CA  GLN A 330     2243   2108   2031    465    177     62       C
ATOM   2434  C   GLN A 330     -20.591 -53.012 -43.565  1.00 16.78           C
ANISOU 2434  C   GLN A 330     2277   2057   2041    450    120     16       C
ATOM   2435  O   GLN A 330     -21.589 -52.822 -42.870  1.00 16.20           O
ANISOU 2435  O   GLN A 330     2202   1960   1994    395     88      9       O
ATOM   2436  CB  GLN A 330     -20.115 -51.415 -45.412  1.00 17.49           C
ANISOU 2436  CB  GLN A 330     2364   2220   2060    512    192     56       C
ATOM   2437  CG  GLN A 330     -19.447 -50.123 -45.921  1.00 17.63           C
ANISOU 2437  CG  GLN A 330     2351   2280   2069    523    256    111       C
ATOM   2438  CD  GLN A 330     -19.868 -48.857 -45.184  1.00 17.56           C
ANISOU 2438  CD  GLN A 330     2308   2262   2101    454    262    141       C
ATOM   2439  OE1 GLN A 330     -20.893 -48.819 -44.505  1.00 19.42           O
ANISOU 2439  OE1 GLN A 330     2551   2471   2357    407    219    120       O
ATOM   2440  NE2 GLN A 330     -19.064 -47.797 -45.328  1.00 17.07           N
ANISOU 2440  NE2 GLN A 330     2207   2222   2057    448    320    192       N
ATOM   2441  N   THR A 331     -20.220 -54.213 -43.988  1.00 17.28           N
ANISOU 2441  N   THR A 331     2374   2103   2089    501    110    -14       N
ATOM   2442  CA  THR A 331     -20.991 -55.404 -43.656  1.00 17.91           C
ANISOU 2442  CA  THR A 331     2491   2125   2190    488     60    -57       C
ATOM   2443  C   THR A 331     -20.896 -55.717 -42.158  1.00 17.68           C
ANISOU 2443  C   THR A 331     2434   2067   2215    438     50    -32       C
ATOM   2444  O   THR A 331     -21.890 -56.091 -41.528  1.00 17.45           O
ANISOU 2444  O   THR A 331     2416   1997   2217    392     15    -45       O
ATOM   2445  CB  THR A 331     -20.541 -56.615 -44.495  1.00 18.64           C
ANISOU 2445  CB  THR A 331     2630   2197   2255    560     55    -98       C
ATOM   2446  OG1 THR A 331     -20.521 -56.257 -45.884  1.00 19.30           O
ANISOU 2446  OG1 THR A 331     2738   2320   2275    617     70   -118       O
ATOM   2447  CG2 THR A 331     -21.494 -57.778 -44.296  1.00 18.87           C
ANISOU 2447  CG2 THR A 331     2701   2155   2314    540      1   -149       C
ATOM   2448  N   SER A 332     -19.713 -55.528 -41.577  1.00 17.50           N
ANISOU 2448  N   SER A 332     2373   2073   2204    450     81      7       N
ATOM   2449  CA  SER A 332     -19.560 -55.694 -40.133  1.00 17.54           C
ANISOU 2449  CA  SER A 332     2349   2066   2249    410     70     33       C
ATOM   2450  C   SER A 332     -20.435 -54.699 -39.365  1.00 16.94           C
ANISOU 2450  C   SER A 332     2249   1996   2191    340     59     47       C
ATOM   2451  O   SER A 332     -21.074 -55.072 -38.390  1.00 16.76           O
ANISOU 2451  O   SER A 332     2229   1944   2194    303     35     51       O
ATOM   2452  CB  SER A 332     -18.095 -55.572 -39.711  1.00 17.61           C
ANISOU 2452  CB  SER A 332     2312   2116   2263    438    100     67       C
ATOM   2453  OG  SER A 332     -17.312 -56.601 -40.296  1.00 19.21           O
ANISOU 2453  OG  SER A 332     2536   2310   2451    509    111     56       O
ATOM   2454  N   ARG A 333     -20.479 -53.445 -39.817  1.00 16.60           N
ANISOU 2454  N   ARG A 333     2184   1989   2135    326     80     57       N
ATOM   2455  CA  ARG A 333     -21.355 -52.449 -39.202  1.00 16.41           C
ANISOU 2455  CA  ARG A 333     2142   1968   2125    267     71     65       C
ATOM   2456  C   ARG A 333     -22.817 -52.900 -39.219  1.00 16.31           C
ANISOU 2456  C   ARG A 333     2162   1917   2116    242     35     38       C
ATOM   2457  O   ARG A 333     -23.500 -52.809 -38.202  1.00 16.51           O
ANISOU 2457  O   ARG A 333     2178   1930   2167    197     19     46       O
ATOM   2458  CB  ARG A 333     -21.216 -51.088 -39.888  1.00 16.57           C
ANISOU 2458  CB  ARG A 333     2144   2022   2131    265    102     80       C
ATOM   2459  CG  ARG A 333     -22.190 -50.037 -39.371  1.00 15.99           C
ANISOU 2459  CG  ARG A 333     2059   1945   2071    212     94     85       C
ATOM   2460  CD  ARG A 333     -21.785 -48.641 -39.797  1.00 16.67           C
ANISOU 2460  CD  ARG A 333     2120   2056   2157    208    132    109       C
ATOM   2461  NE  ARG A 333     -22.481 -47.610 -39.028  1.00 16.10           N
ANISOU 2461  NE  ARG A 333     2033   1978   2107    158    127    114       N
ATOM   2462  CZ  ARG A 333     -22.190 -46.314 -39.074  1.00 16.12           C
ANISOU 2462  CZ  ARG A 333     2012   1989   2125    140    158    135       C
ATOM   2463  NH1 ARG A 333     -21.231 -45.869 -39.877  1.00 16.22           N
ANISOU 2463  NH1 ARG A 333     2009   2017   2135    165    200    159       N
ATOM   2464  NH2 ARG A 333     -22.853 -45.458 -38.302  1.00 17.02           N
ANISOU 2464  NH2 ARG A 333     2117   2092   2259    100    150    133       N
ATOM   2465  N   LEU A 334     -23.295 -53.395 -40.356  1.00 16.55           N
ANISOU 2465  N   LEU A 334     2230   1933   2124    272     21      5       N
ATOM   2466  CA  LEU A 334     -24.686 -53.855 -40.443  1.00 16.43           C
ANISOU 2466  CA  LEU A 334     2238   1884   2120    245    -18    -27       C
ATOM   2467  C   LEU A 334     -24.958 -55.026 -39.489  1.00 16.47           C
ANISOU 2467  C   LEU A 334     2252   1839   2167    221    -40    -29       C
ATOM   2468  O   LEU A 334     -26.016 -55.087 -38.858  1.00 16.09           O
ANISOU 2468  O   LEU A 334     2197   1769   2147    173    -59    -29       O
ATOM   2469  CB  LEU A 334     -25.061 -54.242 -41.875  1.00 17.08           C
ANISOU 2469  CB  LEU A 334     2359   1964   2168    288    -37    -72       C
ATOM   2470  CG  LEU A 334     -25.162 -53.120 -42.914  1.00 16.70           C
ANISOU 2470  CG  LEU A 334     2310   1963   2072    315    -21    -68       C
ATOM   2471  CD1 LEU A 334     -25.675 -53.690 -44.234  1.00 18.29           C
ANISOU 2471  CD1 LEU A 334     2553   2163   2232    360    -51   -121       C
ATOM   2472  CD2 LEU A 334     -26.066 -51.993 -42.416  1.00 17.26           C
ANISOU 2472  CD2 LEU A 334     2353   2048   2157    266    -22    -47       C
ATOM   2473  N   ILE A 335     -23.998 -55.941 -39.385  1.00 16.59           N
ANISOU 2473  N   ILE A 335     2281   1836   2186    256    -32    -25       N
ATOM   2474  CA  ILE A 335     -24.084 -57.063 -38.443  1.00 17.05           C
ANISOU 2474  CA  ILE A 335     2351   1844   2284    243    -43    -15       C
ATOM   2475  C   ILE A 335     -24.141 -56.567 -36.993  1.00 16.65           C
ANISOU 2475  C   ILE A 335     2264   1810   2251    201    -33     31       C
ATOM   2476  O   ILE A 335     -24.998 -57.004 -36.231  1.00 16.41           O
ANISOU 2476  O   ILE A 335     2237   1747   2253    163    -45     40       O
ATOM   2477  CB  ILE A 335     -22.919 -58.076 -38.651  1.00 17.27           C
ANISOU 2477  CB  ILE A 335     2401   1852   2307    302    -33    -16       C
ATOM   2478  CG1 ILE A 335     -23.105 -58.805 -39.986  1.00 18.18           C
ANISOU 2478  CG1 ILE A 335     2563   1936   2407    343    -50    -73       C
ATOM   2479  CG2 ILE A 335     -22.838 -59.080 -37.478  1.00 17.49           C
ANISOU 2479  CG2 ILE A 335     2437   1835   2375    294    -36     12       C
ATOM   2480  CD1 ILE A 335     -21.876 -59.563 -40.466  1.00 18.60           C
ANISOU 2480  CD1 ILE A 335     2639   1986   2444    417    -32    -79       C
ATOM   2481  N   LEU A 336     -23.258 -55.640 -36.617  1.00 16.83           N
ANISOU 2481  N   LEU A 336     2252   1887   2256    208    -11     57       N
ATOM   2482  CA  LEU A 336     -23.278 -55.084 -35.257  1.00 16.61           C
ANISOU 2482  CA  LEU A 336     2191   1882   2236    173     -6     90       C
ATOM   2483  C   LEU A 336     -24.574 -54.321 -34.945  1.00 16.39           C
ANISOU 2483  C   LEU A 336     2154   1856   2216    122    -14     87       C
ATOM   2484  O   LEU A 336     -25.052 -54.364 -33.814  1.00 16.30           O
ANISOU 2484  O   LEU A 336     2134   1843   2217     94    -16    109       O
ATOM   2485  CB  LEU A 336     -22.046 -54.212 -34.961  1.00 16.81           C
ANISOU 2485  CB  LEU A 336     2177   1963   2246    187     13    108       C
ATOM   2486  CG  LEU A 336     -20.858 -54.982 -34.380  1.00 16.70           C
ANISOU 2486  CG  LEU A 336     2154   1959   2234    226     16    129       C
ATOM   2487  CD1 LEU A 336     -20.284 -55.992 -35.400  1.00 17.27           C
ANISOU 2487  CD1 LEU A 336     2256   2005   2302    282     22    114       C
ATOM   2488  CD2 LEU A 336     -19.754 -54.048 -33.870  1.00 17.43           C
ANISOU 2488  CD2 LEU A 336     2193   2111   2319    227     27    143       C
ATOM   2489  N   ILE A 337     -25.145 -53.641 -35.934  1.00 16.61           N
ANISOU 2489  N   ILE A 337     2186   1893   2233    117    -17     63       N
ATOM   2490  CA  ILE A 337     -26.461 -53.023 -35.742  1.00 16.44           C
ANISOU 2490  CA  ILE A 337     2156   1871   2220     76    -26     59       C
ATOM   2491  C   ILE A 337     -27.482 -54.106 -35.389  1.00 16.87           C
ANISOU 2491  C   ILE A 337     2225   1879   2306     51    -46     54       C
ATOM   2492  O   ILE A 337     -28.250 -53.957 -34.431  1.00 16.45           O
ANISOU 2492  O   ILE A 337     2156   1826   2270     16    -44     74       O
ATOM   2493  CB  ILE A 337     -26.916 -52.225 -36.980  1.00 16.48           C
ANISOU 2493  CB  ILE A 337     2166   1893   2204     85    -28     35       C
ATOM   2494  CG1 ILE A 337     -26.067 -50.962 -37.121  1.00 16.29           C
ANISOU 2494  CG1 ILE A 337     2121   1908   2160     97      0     51       C
ATOM   2495  CG2 ILE A 337     -28.387 -51.831 -36.863  1.00 16.67           C
ANISOU 2495  CG2 ILE A 337     2180   1913   2239     50    -45     27       C
ATOM   2496  CD1 ILE A 337     -26.263 -50.237 -38.457  1.00 16.71           C
ANISOU 2496  CD1 ILE A 337     2185   1978   2186    121      8     40       C
ATOM   2497  N   GLY A 338     -27.461 -55.204 -36.136  1.00 17.24           N
ANISOU 2497  N   GLY A 338     2302   1885   2364     71    -63     29       N
ATOM   2498  CA  GLY A 338     -28.373 -56.319 -35.880  1.00 17.79           C
ANISOU 2498  CA  GLY A 338     2385   1898   2478     43    -81     22       C
ATOM   2499  C   GLY A 338     -28.156 -56.951 -34.514  1.00 17.88           C
ANISOU 2499  C   GLY A 338     2393   1887   2513     31    -64     68       C
ATOM   2500  O   GLY A 338     -29.119 -57.244 -33.801  1.00 18.12           O
ANISOU 2500  O   GLY A 338     2413   1896   2577     -8    -64     87       O
ATOM   2501  N   GLU A 339     -26.893 -57.181 -34.155  1.00 17.83           N
ANISOU 2501  N   GLU A 339     2394   1893   2489     70    -49     90       N
ATOM   2502  CA  GLU A 339     -26.545 -57.697 -32.827  1.00 18.03           C
ANISOU 2502  CA  GLU A 339     2416   1911   2523     72    -34    139       C
ATOM   2503  C   GLU A 339     -27.081 -56.808 -31.717  1.00 17.70           C
ANISOU 2503  C   GLU A 339     2343   1912   2471     40    -22    169       C
ATOM   2504  O   GLU A 339     -27.579 -57.304 -30.711  1.00 17.88           O
ANISOU 2504  O   GLU A 339     2365   1917   2511     23    -11    207       O
ATOM   2505  CB  GLU A 339     -25.031 -57.792 -32.651  1.00 18.09           C
ANISOU 2505  CB  GLU A 339     2423   1947   2504    124    -24    155       C
ATOM   2506  CG  GLU A 339     -24.341 -58.857 -33.479  1.00 20.00           C
ANISOU 2506  CG  GLU A 339     2699   2146   2755    170    -28    135       C
ATOM   2507  CD  GLU A 339     -22.940 -59.127 -32.966  1.00 22.57           C
ANISOU 2507  CD  GLU A 339     3018   2499   3061    223    -16    165       C
ATOM   2508  OE1 GLU A 339     -21.965 -58.862 -33.702  1.00 21.89           O
ANISOU 2508  OE1 GLU A 339     2923   2443   2952    262    -11    147       O
ATOM   2509  OE2 GLU A 339     -22.823 -59.597 -31.815  1.00 25.82           O
ANISOU 2509  OE2 GLU A 339     3428   2904   3477    228    -10    209       O
ATOM   2510  N   THR A 340     -26.941 -55.495 -31.893  1.00 16.92           N
ANISOU 2510  N   THR A 340     2219   1868   2342     35    -21    155       N
ATOM   2511  CA  THR A 340     -27.405 -54.531 -30.906  1.00 16.64           C
ANISOU 2511  CA  THR A 340     2156   1873   2292     10    -11    173       C
ATOM   2512  C   THR A 340     -28.920 -54.627 -30.708  1.00 16.46           C
ANISOU 2512  C   THR A 340     2130   1829   2297    -30    -10    177       C
ATOM   2513  O   THR A 340     -29.391 -54.691 -29.582  1.00 16.82           O
ANISOU 2513  O   THR A 340     2165   1883   2343    -44      5    211       O
ATOM   2514  CB  THR A 340     -27.012 -53.092 -31.299  1.00 16.45           C
ANISOU 2514  CB  THR A 340     2112   1896   2242     11     -9    150       C
ATOM   2515  OG1 THR A 340     -25.589 -53.026 -31.500  1.00 16.90           O
ANISOU 2515  OG1 THR A 340     2164   1974   2283     44     -7    148       O
ATOM   2516  CG2 THR A 340     -27.419 -52.104 -30.209  1.00 16.49           C
ANISOU 2516  CG2 THR A 340     2094   1940   2232     -9      0    162       C
ATOM   2517  N   ILE A 341     -29.675 -54.647 -31.799  1.00 16.41           N
ANISOU 2517  N   ILE A 341     2126   1799   2309    -46    -26    144       N
ATOM   2518  CA  ILE A 341     -31.136 -54.724 -31.711  1.00 16.81           C
ANISOU 2518  CA  ILE A 341     2161   1834   2392    -85    -29    144       C
ATOM   2519  C   ILE A 341     -31.573 -56.042 -31.056  1.00 17.13           C
ANISOU 2519  C   ILE A 341     2210   1822   2477   -105    -21    175       C
ATOM   2520  O   ILE A 341     -32.477 -56.057 -30.204  1.00 17.08           O
ANISOU 2520  O   ILE A 341     2182   1818   2489   -134     -3    207       O
ATOM   2521  CB  ILE A 341     -31.793 -54.552 -33.098  1.00 16.67           C
ANISOU 2521  CB  ILE A 341     2144   1808   2384    -92    -56     95       C
ATOM   2522  CG1 ILE A 341     -31.509 -53.146 -33.639  1.00 16.91           C
ANISOU 2522  CG1 ILE A 341     2165   1889   2372    -73    -55     79       C
ATOM   2523  CG2 ILE A 341     -33.300 -54.804 -33.019  1.00 18.13           C
ANISOU 2523  CG2 ILE A 341     2303   1975   2611   -135    -65     93       C
ATOM   2524  CD1 ILE A 341     -32.015 -52.911 -35.053  1.00 17.08           C
ANISOU 2524  CD1 ILE A 341     2191   1911   2387    -64    -81     36       C
ATOM   2525  N   LYS A 342     -30.923 -57.136 -31.453  1.00 17.27           N
ANISOU 2525  N   LYS A 342     2259   1791   2513    -86    -29    170       N
ATOM   2526  CA  LYS A 342     -31.178 -58.458 -30.869  1.00 18.11           C
ANISOU 2526  CA  LYS A 342     2380   1833   2667    -99    -17    204       C
ATOM   2527  C   LYS A 342     -30.978 -58.448 -29.352  1.00 18.08           C
ANISOU 2527  C   LYS A 342     2369   1855   2645    -91     17    271       C
ATOM   2528  O   LYS A 342     -31.831 -58.923 -28.607  1.00 18.17           O
ANISOU 2528  O   LYS A 342     2370   1842   2691   -120     39    312       O
ATOM   2529  CB  LYS A 342     -30.257 -59.500 -31.512  1.00 18.49           C
ANISOU 2529  CB  LYS A 342     2469   1829   2727    -64    -30    186       C
ATOM   2530  CG  LYS A 342     -30.239 -60.879 -30.853  1.00 19.44           C
ANISOU 2530  CG  LYS A 342     2615   1877   2896    -65    -12    229       C
ATOM   2531  CD  LYS A 342     -31.512 -61.668 -31.130  1.00 20.30           C
ANISOU 2531  CD  LYS A 342     2720   1912   3081   -121    -20    217       C
ATOM   2532  CE  LYS A 342     -31.367 -63.133 -30.727  1.00 21.70           C
ANISOU 2532  CE  LYS A 342     2931   1996   3317   -119     -4    253       C
ATOM   2533  NZ  LYS A 342     -32.463 -63.969 -31.313  1.00 23.01           N
ANISOU 2533  NZ  LYS A 342     3097   2077   3570   -176    -22    219       N
ATOM   2534  N   ILE A 343     -29.836 -57.928 -28.911  1.00 17.78           N
ANISOU 2534  N   ILE A 343     2335   1868   2553    -49     22    282       N
ATOM   2535  CA  ILE A 343     -29.496 -57.900 -27.488  1.00 18.15           C
ANISOU 2535  CA  ILE A 343     2378   1949   2569    -29     47    338       C
ATOM   2536  C   ILE A 343     -30.429 -56.958 -26.735  1.00 18.06           C
ANISOU 2536  C   ILE A 343     2337   1987   2540    -56     63    351       C
ATOM   2537  O   ILE A 343     -30.880 -57.271 -25.626  1.00 18.69           O
ANISOU 2537  O   ILE A 343     2413   2072   2617    -57     91    404       O
ATOM   2538  CB  ILE A 343     -28.017 -57.487 -27.267  1.00 17.81           C
ANISOU 2538  CB  ILE A 343     2337   1957   2474     21     38    334       C
ATOM   2539  CG1 ILE A 343     -27.080 -58.587 -27.770  1.00 18.76           C
ANISOU 2539  CG1 ILE A 343     2487   2031   2610     58     31    335       C
ATOM   2540  CG2 ILE A 343     -27.741 -57.217 -25.791  1.00 18.02           C
ANISOU 2540  CG2 ILE A 343     2354   2037   2454     43     54    379       C
ATOM   2541  CD1 ILE A 343     -25.615 -58.173 -27.832  1.00 18.21           C
ANISOU 2541  CD1 ILE A 343     2409   2012   2497    105     19    323       C
ATOM   2542  N   VAL A 344     -30.737 -55.813 -27.342  1.00 17.56           N
ANISOU 2542  N   VAL A 344     2253   1958   2463    -71     49    306       N
ATOM   2543  CA  VAL A 344     -31.614 -54.841 -26.699  1.00 17.17           C
ANISOU 2543  CA  VAL A 344     2176   1953   2395    -89     64    313       C
ATOM   2544  C   VAL A 344     -32.993 -55.446 -26.431  1.00 17.68           C
ANISOU 2544  C   VAL A 344     2225   1986   2508   -126     85    343       C
ATOM   2545  O   VAL A 344     -33.539 -55.276 -25.351  1.00 18.08           O
ANISOU 2545  O   VAL A 344     2262   2065   2543   -128    115    384       O
ATOM   2546  CB  VAL A 344     -31.724 -53.524 -27.509  1.00 16.60           C
ANISOU 2546  CB  VAL A 344     2088   1912   2307    -95     47    261       C
ATOM   2547  CG1 VAL A 344     -32.838 -52.638 -26.958  1.00 16.05           C
ANISOU 2547  CG1 VAL A 344     1992   1877   2230   -113     63    266       C
ATOM   2548  CG2 VAL A 344     -30.378 -52.772 -27.468  1.00 16.11           C
ANISOU 2548  CG2 VAL A 344     2031   1889   2201    -64     36    242       C
ATOM   2549  N   ILE A 345     -33.548 -56.178 -27.389  1.00 18.10           N
ANISOU 2549  N   ILE A 345     2279   1981   2619   -156     69    323       N
ATOM   2550  CA  ILE A 345     -34.881 -56.754 -27.199  1.00 18.56           C
ANISOU 2550  CA  ILE A 345     2312   2006   2735   -201     86    348       C
ATOM   2551  C   ILE A 345     -34.847 -57.978 -26.265  1.00 19.18           C
ANISOU 2551  C   ILE A 345     2405   2039   2843   -202    121    415       C
ATOM   2552  O   ILE A 345     -35.551 -58.021 -25.250  1.00 19.31           O
ANISOU 2552  O   ILE A 345     2402   2072   2864   -213    161    470       O
ATOM   2553  CB  ILE A 345     -35.525 -57.141 -28.550  1.00 18.70           C
ANISOU 2553  CB  ILE A 345     2321   1976   2810   -235     50    295       C
ATOM   2554  CG1 ILE A 345     -35.822 -55.877 -29.371  1.00 18.43           C
ANISOU 2554  CG1 ILE A 345     2266   1991   2744   -231     24    243       C
ATOM   2555  CG2 ILE A 345     -36.799 -57.972 -28.317  1.00 19.79           C
ANISOU 2555  CG2 ILE A 345     2429   2067   3025   -288     66    322       C
ATOM   2556  CD1 ILE A 345     -36.310 -56.144 -30.790  1.00 19.21           C
ANISOU 2556  CD1 ILE A 345     2361   2059   2878   -250    -19    184       C
ATOM   2557  N   GLU A 346     -34.005 -58.949 -26.594  1.00 19.38           N
ANISOU 2557  N   GLU A 346     2469   2010   2886   -184    109    416       N
ATOM   2558  CA  GLU A 346     -34.056 -60.259 -25.952  1.00 20.41           C
ANISOU 2558  CA  GLU A 346     2618   2075   3061   -188    140    477       C
ATOM   2559  C   GLU A 346     -33.298 -60.387 -24.621  1.00 20.61           C
ANISOU 2559  C   GLU A 346     2663   2135   3031   -138    175    547       C
ATOM   2560  O   GLU A 346     -33.550 -61.330 -23.863  1.00 21.33           O
ANISOU 2560  O   GLU A 346     2766   2185   3154   -139    213    617       O
ATOM   2561  CB  GLU A 346     -33.608 -61.338 -26.947  1.00 20.79           C
ANISOU 2561  CB  GLU A 346     2701   2037   3161   -190    112    444       C
ATOM   2562  CG  GLU A 346     -34.547 -61.446 -28.156  1.00 21.47           C
ANISOU 2562  CG  GLU A 346     2767   2081   3310   -243     78    379       C
ATOM   2563  CD  GLU A 346     -34.372 -62.717 -28.970  1.00 23.71           C
ANISOU 2563  CD  GLU A 346     3086   2264   3660   -253     55    348       C
ATOM   2564  OE1 GLU A 346     -33.824 -63.715 -28.447  1.00 24.47           O
ANISOU 2564  OE1 GLU A 346     3217   2303   3778   -232     79    395       O
ATOM   2565  OE2 GLU A 346     -34.816 -62.728 -30.141  1.00 23.81           O
ANISOU 2565  OE2 GLU A 346     3091   2254   3702   -278     12    275       O
ATOM   2566  N   ASP A 347     -32.393 -59.453 -24.330  1.00 20.28           N
ANISOU 2566  N   ASP A 347     2625   2170   2909    -94    161    530       N
ATOM   2567  CA  ASP A 347     -31.703 -59.423 -23.035  1.00 20.41           C
ANISOU 2567  CA  ASP A 347     2655   2239   2862    -42    185    586       C
ATOM   2568  C   ASP A 347     -32.070 -58.200 -22.202  1.00 20.05           C
ANISOU 2568  C   ASP A 347     2582   2282   2754    -35    197    587       C
ATOM   2569  O   ASP A 347     -32.484 -58.330 -21.053  1.00 20.37           O
ANISOU 2569  O   ASP A 347     2620   2349   2769    -20    236    649       O
ATOM   2570  CB  ASP A 347     -30.188 -59.486 -23.229  1.00 20.28           C
ANISOU 2570  CB  ASP A 347     2662   2238   2804     12    155    566       C
ATOM   2571  CG  ASP A 347     -29.732 -60.801 -23.818  1.00 21.98           C
ANISOU 2571  CG  ASP A 347     2912   2368   3073     22    151    576       C
ATOM   2572  OD1 ASP A 347     -30.179 -61.863 -23.328  1.00 24.94           O
ANISOU 2572  OD1 ASP A 347     3304   2682   3489     16    184    637       O
ATOM   2573  OD2 ASP A 347     -28.923 -60.769 -24.765  1.00 23.02           O
ANISOU 2573  OD2 ASP A 347     3053   2490   3203     38    119    524       O
ATOM   2574  N   TYR A 348     -31.930 -57.017 -22.790  1.00 19.56           N
ANISOU 2574  N   TYR A 348     2504   2263   2667    -42    166    520       N
ATOM   2575  CA  TYR A 348     -32.043 -55.754 -22.055  1.00 19.26           C
ANISOU 2575  CA  TYR A 348     2447   2306   2566    -27    170    507       C
ATOM   2576  C   TYR A 348     -33.503 -55.426 -21.736  1.00 19.67           C
ANISOU 2576  C   TYR A 348     2471   2367   2637    -59    203    526       C
ATOM   2577  O   TYR A 348     -33.879 -55.313 -20.565  1.00 20.31           O
ANISOU 2577  O   TYR A 348     2547   2490   2678    -39    238    572       O
ATOM   2578  CB  TYR A 348     -31.365 -54.653 -22.872  1.00 18.45           C
ANISOU 2578  CB  TYR A 348     2338   2230   2443    -25    130    433       C
ATOM   2579  CG  TYR A 348     -31.541 -53.229 -22.403  1.00 18.61           C
ANISOU 2579  CG  TYR A 348     2339   2315   2415    -20    128    402       C
ATOM   2580  CD1 TYR A 348     -30.761 -52.712 -21.376  1.00 19.03           C
ANISOU 2580  CD1 TYR A 348     2398   2430   2402     20    123    401       C
ATOM   2581  CD2 TYR A 348     -32.448 -52.380 -23.030  1.00 18.48           C
ANISOU 2581  CD2 TYR A 348     2303   2299   2420    -50    127    367       C
ATOM   2582  CE1 TYR A 348     -30.903 -51.398 -20.962  1.00 19.98           C
ANISOU 2582  CE1 TYR A 348     2506   2601   2483     25    118    363       C
ATOM   2583  CE2 TYR A 348     -32.594 -51.060 -22.632  1.00 18.60           C
ANISOU 2583  CE2 TYR A 348     2307   2365   2397    -42    127    335       C
ATOM   2584  CZ  TYR A 348     -31.823 -50.575 -21.597  1.00 19.27           C
ANISOU 2584  CZ  TYR A 348     2400   2502   2420     -6    123    331       C
ATOM   2585  OH  TYR A 348     -31.956 -49.265 -21.205  1.00 21.18           O
ANISOU 2585  OH  TYR A 348     2635   2786   2628      2    120    292       O
ATOM   2586  N   VAL A 349     -34.327 -55.300 -22.772  1.00 19.55           N
ANISOU 2586  N   VAL A 349     2434   2316   2678   -105    191    491       N
ATOM   2587  CA  VAL A 349     -35.772 -55.086 -22.590  1.00 19.61           C
ANISOU 2587  CA  VAL A 349     2405   2330   2716   -138    221    509       C
ATOM   2588  C   VAL A 349     -36.421 -56.265 -21.858  1.00 20.51           C
ANISOU 2588  C   VAL A 349     2514   2408   2871   -153    268    588       C
ATOM   2589  O   VAL A 349     -37.271 -56.071 -20.981  1.00 20.99           O
ANISOU 2589  O   VAL A 349     2551   2504   2921   -153    313    632       O
ATOM   2590  CB  VAL A 349     -36.485 -54.838 -23.939  1.00 19.31           C
ANISOU 2590  CB  VAL A 349     2341   2261   2733   -181    191    454       C
ATOM   2591  CG1 VAL A 349     -38.015 -54.883 -23.766  1.00 19.56           C
ANISOU 2591  CG1 VAL A 349     2326   2293   2812   -219    220    479       C
ATOM   2592  CG2 VAL A 349     -36.054 -53.503 -24.528  1.00 19.29           C
ANISOU 2592  CG2 VAL A 349     2340   2300   2688   -164    159    391       C
ATOM   2593  N   GLN A 350     -36.025 -57.486 -22.212  1.00 20.89           N
ANISOU 2593  N   GLN A 350     2586   2383   2968   -164    263    607       N
ATOM   2594  CA  GLN A 350     -36.522 -58.672 -21.521  1.00 21.73           C
ANISOU 2594  CA  GLN A 350     2693   2441   3121   -178    312    689       C
ATOM   2595  C   GLN A 350     -36.345 -58.511 -20.011  1.00 22.20           C
ANISOU 2595  C   GLN A 350     2764   2566   3107   -126    359    759       C
ATOM   2596  O   GLN A 350     -37.292 -58.702 -19.251  1.00 22.49           O
ANISOU 2596  O   GLN A 350     2777   2612   3157   -138    414    822       O
ATOM   2597  CB  GLN A 350     -35.803 -59.938 -22.001  1.00 22.01           C
ANISOU 2597  CB  GLN A 350     2767   2390   3204   -178    298    699       C
ATOM   2598  CG  GLN A 350     -36.324 -61.239 -21.391  1.00 23.36           C
ANISOU 2598  CG  GLN A 350     2944   2491   3441   -197    350    785       C
ATOM   2599  CD  GLN A 350     -37.680 -61.637 -21.937  1.00 24.25           C
ANISOU 2599  CD  GLN A 350     3012   2546   3657   -275    361    781       C
ATOM   2600  OE1 GLN A 350     -37.854 -61.769 -23.151  1.00 24.94           O
ANISOU 2600  OE1 GLN A 350     3091   2586   3800   -314    313    710       O
ATOM   2601  NE2 GLN A 350     -38.647 -61.837 -21.043  1.00 23.48           N
ANISOU 2601  NE2 GLN A 350     2882   2456   3585   -295    423    857       N
ATOM   2602  N   HIS A 351     -35.140 -58.136 -19.586  1.00 21.96           N
ANISOU 2602  N   HIS A 351     2766   2584   2994    -68    338    747       N
ATOM   2603  CA  HIS A 351     -34.874 -57.949 -18.161  1.00 22.23           C
ANISOU 2603  CA  HIS A 351     2814   2689   2944     -9    372    804       C
ATOM   2604  C   HIS A 351     -35.742 -56.854 -17.545  1.00 22.41           C
ANISOU 2604  C   HIS A 351     2806   2788   2922     -6    397    797       C
ATOM   2605  O   HIS A 351     -36.431 -57.082 -16.556  1.00 22.53           O
ANISOU 2605  O   HIS A 351     2813   2828   2918      9    455    868       O
ATOM   2606  CB  HIS A 351     -33.415 -57.597 -17.890  1.00 22.01           C
ANISOU 2606  CB  HIS A 351     2817   2710   2837     51    332    774       C
ATOM   2607  CG  HIS A 351     -33.190 -57.093 -16.500  1.00 22.04           C
ANISOU 2607  CG  HIS A 351     2830   2806   2740    112    352    806       C
ATOM   2608  ND1 HIS A 351     -33.238 -57.917 -15.396  1.00 22.51           N
ANISOU 2608  ND1 HIS A 351     2909   2876   2767    155    400    900       N
ATOM   2609  CD2 HIS A 351     -32.977 -55.841 -16.028  1.00 21.86           C
ANISOU 2609  CD2 HIS A 351     2799   2867   2640    140    331    755       C
ATOM   2610  CE1 HIS A 351     -33.049 -57.196 -14.305  1.00 22.64           C
ANISOU 2610  CE1 HIS A 351     2932   2989   2683    212    406    903       C
ATOM   2611  NE2 HIS A 351     -32.895 -55.932 -14.660  1.00 21.90           N
ANISOU 2611  NE2 HIS A 351     2820   2938   2562    201    362    812       N
ATOM   2612  N   LEU A 352     -35.680 -55.653 -18.110  1.00 21.76           N
ANISOU 2612  N   LEU A 352     2709   2740   2819    -14    357    715       N
ATOM   2613  CA  LEU A 352     -36.352 -54.520 -17.475  1.00 22.11           C
ANISOU 2613  CA  LEU A 352     2732   2858   2811      2    377    701       C
ATOM   2614  C   LEU A 352     -37.881 -54.667 -17.499  1.00 22.29           C
ANISOU 2614  C   LEU A 352     2712   2867   2893    -39    425    738       C
ATOM   2615  O   LEU A 352     -38.565 -54.113 -16.636  1.00 22.43           O
ANISOU 2615  O   LEU A 352     2712   2944   2865    -15    466    762       O
ATOM   2616  CB  LEU A 352     -35.891 -53.190 -18.076  1.00 21.90           C
ANISOU 2616  CB  LEU A 352     2704   2862   2756      5    325    607       C
ATOM   2617  CG  LEU A 352     -36.250 -52.850 -19.514  1.00 21.59           C
ANISOU 2617  CG  LEU A 352     2643   2777   2784    -46    292    549       C
ATOM   2618  CD1 LEU A 352     -37.692 -52.345 -19.633  1.00 23.84           C
ANISOU 2618  CD1 LEU A 352     2886   3073   3100    -72    320    550       C
ATOM   2619  CD2 LEU A 352     -35.266 -51.803 -20.055  1.00 22.67           C
ANISOU 2619  CD2 LEU A 352     2793   2932   2887    -32    242    472       C
ATOM   2620  N   SER A 353     -38.409 -55.423 -18.465  1.00 21.97           N
ANISOU 2620  N   SER A 353     2649   2749   2950    -99    419    740       N
ATOM   2621  CA  SER A 353     -39.855 -55.663 -18.550  1.00 22.08           C
ANISOU 2621  CA  SER A 353     2611   2746   3034   -146    460    773       C
ATOM   2622  C   SER A 353     -40.363 -56.465 -17.362  1.00 22.99           C
ANISOU 2622  C   SER A 353     2720   2866   3149   -134    537    879       C
ATOM   2623  O   SER A 353     -41.485 -56.247 -16.884  1.00 23.35           O
ANISOU 2623  O   SER A 353     2721   2943   3206   -143    588    917       O
ATOM   2624  CB  SER A 353     -40.226 -56.409 -19.839  1.00 22.01           C
ANISOU 2624  CB  SER A 353     2581   2650   3133   -214    429    747       C
ATOM   2625  OG  SER A 353     -39.852 -57.777 -19.778  1.00 22.30           O
ANISOU 2625  OG  SER A 353     2643   2611   3219   -228    443    797       O
ATOM   2626  N   GLY A 354     -39.546 -57.419 -16.921  1.00 23.18           N
ANISOU 2626  N   GLY A 354     2788   2858   3162   -109    547    930       N
ATOM   2627  CA  GLY A 354     -39.933 -58.362 -15.884  1.00 24.26           C
ANISOU 2627  CA  GLY A 354     2927   2984   3307    -97    623   1042       C
ATOM   2628  C   GLY A 354     -40.906 -59.433 -16.338  1.00 24.96           C
ANISOU 2628  C   GLY A 354     2977   2981   3526   -172    657   1090       C
ATOM   2629  O   GLY A 354     -41.426 -60.168 -15.508  1.00 25.67           O
ANISOU 2629  O   GLY A 354     3058   3057   3638   -172    731   1191       O
ATOM   2630  N   TYR A 355     -41.143 -59.546 -17.646  1.00 24.68           N
ANISOU 2630  N   TYR A 355     2918   2881   3576   -236    605   1020       N
ATOM   2631  CA  TYR A 355     -42.163 -60.467 -18.150  1.00 25.65           C
ANISOU 2631  CA  TYR A 355     2996   2920   3832   -317    627   1047       C
ATOM   2632  C   TYR A 355     -41.646 -61.894 -18.188  1.00 26.55           C
ANISOU 2632  C   TYR A 355     3150   2929   4010   -331    638   1098       C
ATOM   2633  O   TYR A 355     -40.462 -62.126 -18.428  1.00 26.17           O
ANISOU 2633  O   TYR A 355     3161   2860   3924   -294    598   1071       O
ATOM   2634  CB  TYR A 355     -42.637 -60.083 -19.559  1.00 25.12           C
ANISOU 2634  CB  TYR A 355     2889   2827   3829   -375    559    946       C
ATOM   2635  CG  TYR A 355     -43.185 -58.679 -19.712  1.00 24.07           C
ANISOU 2635  CG  TYR A 355     2716   2784   3645   -362    542    891       C
ATOM   2636  CD1 TYR A 355     -43.669 -57.958 -18.619  1.00 24.71           C
ANISOU 2636  CD1 TYR A 355     2777   2952   3659   -321    599    938       C
ATOM   2637  CD2 TYR A 355     -43.245 -58.084 -20.963  1.00 23.21           C
ANISOU 2637  CD2 TYR A 355     2592   2672   3554   -385    471    794       C
ATOM   2638  CE1 TYR A 355     -44.167 -56.678 -18.771  1.00 23.86           C
ANISOU 2638  CE1 TYR A 355     2637   2920   3509   -305    585    886       C
ATOM   2639  CE2 TYR A 355     -43.745 -56.812 -21.125  1.00 23.82           C
ANISOU 2639  CE2 TYR A 355     2636   2825   3588   -369    457    748       C
ATOM   2640  CZ  TYR A 355     -44.204 -56.108 -20.028  1.00 24.03           C
ANISOU 2640  CZ  TYR A 355     2644   2930   3554   -329    514    793       C
ATOM   2641  OH  TYR A 355     -44.694 -54.831 -20.194  1.00 23.86           O
ANISOU 2641  OH  TYR A 355     2595   2978   3493   -308    502    745       O
ATOM   2642  N   HIS A 356     -42.550 -62.839 -17.951  1.00 28.04           N
ANISOU 2642  N   HIS A 356     3303   3051   4300   -386    696   1172       N
ATOM   2643  CA  HIS A 356     -42.247 -64.259 -18.111  1.00 29.15           C
ANISOU 2643  CA  HIS A 356     3477   3070   4530   -414    709   1217       C
ATOM   2644  C   HIS A 356     -42.336 -64.673 -19.579  1.00 28.83           C
ANISOU 2644  C   HIS A 356     3426   2937   4590   -483    636   1120       C
ATOM   2645  O   HIS A 356     -41.785 -65.707 -19.973  1.00 29.08           O
ANISOU 2645  O   HIS A 356     3503   2868   4681   -494    620   1120       O
ATOM   2646  CB  HIS A 356     -43.200 -65.110 -17.274  1.00 30.63           C
ANISOU 2646  CB  HIS A 356     3629   3212   4796   -451    806   1338       C
ATOM   2647  CG  HIS A 356     -43.083 -64.871 -15.802  1.00 32.30           C
ANISOU 2647  CG  HIS A 356     3859   3510   4905   -374    886   1445       C
ATOM   2648  ND1 HIS A 356     -41.869 -64.811 -15.152  1.00 33.74           N
ANISOU 2648  ND1 HIS A 356     4115   3734   4971   -281    881   1469       N
ATOM   2649  CD2 HIS A 356     -44.028 -64.688 -14.851  1.00 34.08           C
ANISOU 2649  CD2 HIS A 356     4037   3790   5122   -371    972   1533       C
ATOM   2650  CE1 HIS A 356     -42.072 -64.601 -13.864  1.00 34.90           C
ANISOU 2650  CE1 HIS A 356     4264   3961   5037   -222    957   1563       C
ATOM   2651  NE2 HIS A 356     -43.374 -64.522 -13.655  1.00 35.32           N
ANISOU 2651  NE2 HIS A 356     4246   4022   5151   -274   1016   1606       N
ATOM   2652  N   PHE A 357     -43.050 -63.880 -20.375  1.00 28.08           N
ANISOU 2652  N   PHE A 357     3275   2880   4513   -524    590   1037       N
ATOM   2653  CA  PHE A 357     -43.094 -64.068 -21.823  1.00 27.61           C
ANISOU 2653  CA  PHE A 357     3209   2759   4524   -575    509    931       C
ATOM   2654  C   PHE A 357     -41.720 -63.774 -22.425  1.00 26.71           C
ANISOU 2654  C   PHE A 357     3165   2655   4328   -516    444    860       C
ATOM   2655  O   PHE A 357     -41.069 -62.786 -22.061  1.00 25.86           O
ANISOU 2655  O   PHE A 357     3079   2639   4106   -452    437    849       O
ATOM   2656  CB  PHE A 357     -44.148 -63.153 -22.461  1.00 27.32           C
ANISOU 2656  CB  PHE A 357     3094   2781   4505   -615    477    865       C
ATOM   2657  CG  PHE A 357     -44.143 -63.180 -23.965  1.00 26.59           C
ANISOU 2657  CG  PHE A 357     2998   2647   4457   -652    386    749       C
ATOM   2658  CD1 PHE A 357     -44.462 -64.347 -24.648  1.00 28.75           C
ANISOU 2658  CD1 PHE A 357     3264   2806   4853   -719    363    726       C
ATOM   2659  CD2 PHE A 357     -43.814 -62.043 -24.700  1.00 26.36           C
ANISOU 2659  CD2 PHE A 357     2975   2692   4348   -615    325    664       C
ATOM   2660  CE1 PHE A 357     -44.461 -64.383 -26.030  1.00 28.60           C
ANISOU 2660  CE1 PHE A 357     3245   2756   4866   -745    276    614       C
ATOM   2661  CE2 PHE A 357     -43.808 -62.075 -26.087  1.00 25.33           C
ANISOU 2661  CE2 PHE A 357     2844   2531   4250   -640    245    562       C
ATOM   2662  CZ  PHE A 357     -44.133 -63.246 -26.752  1.00 27.30           C
ANISOU 2662  CZ  PHE A 357     3087   2674   4611   -702    218    535       C
ATOM   2663  N   LYS A 358     -41.296 -64.631 -23.349  1.00 26.72           N
ANISOU 2663  N   LYS A 358     3200   2560   4394   -540    399    810       N
ATOM   2664  CA  LYS A 358     -39.970 -64.531 -23.949  1.00 26.47           C
ANISOU 2664  CA  LYS A 358     3234   2528   4297   -484    345    751       C
ATOM   2665  C   LYS A 358     -40.046 -63.688 -25.221  1.00 25.22           C
ANISOU 2665  C   LYS A 358     3057   2408   4119   -494    269    636       C
ATOM   2666  O   LYS A 358     -40.500 -64.152 -26.274  1.00 25.72           O
ANISOU 2666  O   LYS A 358     3106   2408   4259   -544    224    570       O
ATOM   2667  CB  LYS A 358     -39.414 -65.926 -24.248  1.00 27.49           C
ANISOU 2667  CB  LYS A 358     3416   2533   4497   -490    341    760       C
ATOM   2668  CG  LYS A 358     -37.966 -65.943 -24.722  1.00 28.89           C
ANISOU 2668  CG  LYS A 358     3661   2711   4606   -422    299    715       C
ATOM   2669  CD  LYS A 358     -37.485 -67.367 -24.954  1.00 32.62           C
ANISOU 2669  CD  LYS A 358     4186   3055   5153   -423    301    729       C
ATOM   2670  CE  LYS A 358     -36.151 -67.401 -25.679  1.00 33.55           C
ANISOU 2670  CE  LYS A 358     4363   3171   5215   -360    252    667       C
ATOM   2671  NZ  LYS A 358     -35.099 -66.660 -24.934  1.00 35.60           N
ANISOU 2671  NZ  LYS A 358     4643   3531   5353   -279    264    702       N
ATOM   2672  N   LEU A 359     -39.609 -62.442 -25.105  1.00 24.03           N
ANISOU 2672  N   LEU A 359     2907   2359   3863   -444    256    612       N
ATOM   2673  CA  LEU A 359     -39.619 -61.505 -26.226  1.00 23.06           C
ANISOU 2673  CA  LEU A 359     2772   2281   3709   -442    193    517       C
ATOM   2674  C   LEU A 359     -38.738 -62.025 -27.361  1.00 22.98           C
ANISOU 2674  C   LEU A 359     2811   2215   3707   -428    138    448       C
ATOM   2675  O   LEU A 359     -37.850 -62.853 -27.142  1.00 22.89           O
ANISOU 2675  O   LEU A 359     2850   2150   3697   -401    148    474       O
ATOM   2676  CB  LEU A 359     -39.132 -60.133 -25.772  1.00 22.06           C
ANISOU 2676  CB  LEU A 359     2648   2261   3472   -387    198    514       C
ATOM   2677  CG  LEU A 359     -39.891 -59.475 -24.614  1.00 21.81           C
ANISOU 2677  CG  LEU A 359     2576   2298   3412   -384    253    575       C
ATOM   2678  CD1 LEU A 359     -39.156 -58.237 -24.149  1.00 20.51           C
ANISOU 2678  CD1 LEU A 359     2431   2224   3139   -323    251    563       C
ATOM   2679  CD2 LEU A 359     -41.321 -59.136 -25.019  1.00 21.42           C
ANISOU 2679  CD2 LEU A 359     2456   2262   3420   -437    249    554       C
ATOM   2680  N   LYS A 360     -38.973 -61.522 -28.569  1.00 22.75           N
ANISOU 2680  N   LYS A 360     2767   2201   3675   -439     80    362       N
ATOM   2681  CA  LYS A 360     -38.288 -62.022 -29.756  1.00 23.09           C
ANISOU 2681  CA  LYS A 360     2853   2195   3726   -425     27    290       C
ATOM   2682  C   LYS A 360     -37.924 -60.875 -30.679  1.00 22.10           C
ANISOU 2682  C   LYS A 360     2730   2141   3525   -389    -17    222       C
ATOM   2683  O   LYS A 360     -38.745 -59.996 -30.926  1.00 21.90           O
ANISOU 2683  O   LYS A 360     2659   2172   3490   -405    -29    200       O
ATOM   2684  CB  LYS A 360     -39.205 -63.013 -30.483  1.00 24.35           C
ANISOU 2684  CB  LYS A 360     2992   2267   3993   -490     -4    248       C
ATOM   2685  CG  LYS A 360     -38.568 -63.788 -31.620  1.00 25.55           C
ANISOU 2685  CG  LYS A 360     3195   2350   4163   -477    -55    174       C
ATOM   2686  CD  LYS A 360     -39.612 -64.633 -32.331  1.00 28.35           C
ANISOU 2686  CD  LYS A 360     3519   2626   4624   -547    -94    120       C
ATOM   2687  CE  LYS A 360     -38.995 -65.547 -33.377  1.00 29.44           C
ANISOU 2687  CE  LYS A 360     3716   2684   4786   -531   -142     43       C
ATOM   2688  NZ  LYS A 360     -40.052 -66.317 -34.103  1.00 32.52           N
ANISOU 2688  NZ  LYS A 360     4074   3000   5281   -603   -190    -24       N
ATOM   2689  N   PHE A 361     -36.688 -60.876 -31.171  1.00 21.69           N
ANISOU 2689  N   PHE A 361     2730   2090   3422   -337    -35    194       N
ATOM   2690  CA  PHE A 361     -36.312 -60.011 -32.283  1.00 21.08           C
ANISOU 2690  CA  PHE A 361     2660   2062   3287   -305    -76    127       C
ATOM   2691  C   PHE A 361     -36.500 -60.809 -33.573  1.00 21.82           C
ANISOU 2691  C   PHE A 361     2771   2096   3422   -317   -128     52       C
ATOM   2692  O   PHE A 361     -35.749 -61.754 -33.860  1.00 22.10           O
ANISOU 2692  O   PHE A 361     2855   2070   3474   -297   -135     38       O
ATOM   2693  CB  PHE A 361     -34.881 -59.512 -32.153  1.00 20.39           C
ANISOU 2693  CB  PHE A 361     2611   2015   3122   -242    -65    138       C
ATOM   2694  CG  PHE A 361     -34.405 -58.741 -33.345  1.00 20.12           C
ANISOU 2694  CG  PHE A 361     2588   2022   3035   -207    -98     77       C
ATOM   2695  CD1 PHE A 361     -35.187 -57.727 -33.893  1.00 19.76           C
ANISOU 2695  CD1 PHE A 361     2509   2027   2970   -217   -117     48       C
ATOM   2696  CD2 PHE A 361     -33.179 -59.024 -33.925  1.00 20.34           C
ANISOU 2696  CD2 PHE A 361     2659   2040   3030   -158   -107     56       C
ATOM   2697  CE1 PHE A 361     -34.749 -57.014 -34.998  1.00 19.11           C
ANISOU 2697  CE1 PHE A 361     2441   1983   2837   -180   -143      1       C
ATOM   2698  CE2 PHE A 361     -32.739 -58.308 -35.023  1.00 19.94           C
ANISOU 2698  CE2 PHE A 361     2619   2030   2929   -123   -130      9       C
ATOM   2699  CZ  PHE A 361     -33.524 -57.311 -35.560  1.00 18.34           C
ANISOU 2699  CZ  PHE A 361     2386   1875   2707   -134   -147    -16       C
ATOM   2700  N   ASP A 362     -37.533 -60.441 -34.322  1.00 21.94           N
ANISOU 2700  N   ASP A 362     2749   2132   3456   -347   -166      3       N
ATOM   2701  CA  ASP A 362     -37.883 -61.134 -35.551  1.00 22.66           C
ANISOU 2701  CA  ASP A 362     2850   2176   3585   -360   -224    -79       C
ATOM   2702  C   ASP A 362     -38.596 -60.176 -36.491  1.00 22.09           C
ANISOU 2702  C   ASP A 362     2742   2172   3477   -356   -268   -133       C
ATOM   2703  O   ASP A 362     -39.822 -60.058 -36.456  1.00 21.32           O
ANISOU 2703  O   ASP A 362     2587   2087   3427   -403   -284   -141       O
ATOM   2704  CB  ASP A 362     -38.758 -62.351 -35.260  1.00 24.31           C
ANISOU 2704  CB  ASP A 362     3036   2294   3905   -430   -228    -76       C
ATOM   2705  CG  ASP A 362     -39.076 -63.148 -36.511  1.00 26.06           C
ANISOU 2705  CG  ASP A 362     3272   2459   4171   -446   -295   -172       C
ATOM   2706  OD1 ASP A 362     -38.558 -62.791 -37.595  1.00 27.38           O
ANISOU 2706  OD1 ASP A 362     3472   2661   4271   -394   -336   -237       O
ATOM   2707  OD2 ASP A 362     -39.838 -64.132 -36.410  1.00 30.57           O
ANISOU 2707  OD2 ASP A 362     3822   2949   4844   -510   -306   -184       O
ATOM   2708  N   PRO A 363     -37.821 -59.478 -37.336  1.00 21.19           N
ANISOU 2708  N   PRO A 363     2662   2108   3280   -294   -286   -167       N
ATOM   2709  CA  PRO A 363     -38.397 -58.561 -38.317  1.00 21.29           C
ANISOU 2709  CA  PRO A 363     2651   2188   3249   -275   -326   -214       C
ATOM   2710  C   PRO A 363     -39.543 -59.151 -39.141  1.00 22.40           C
ANISOU 2710  C   PRO A 363     2760   2305   3444   -314   -390   -286       C
ATOM   2711  O   PRO A 363     -40.454 -58.420 -39.521  1.00 22.43           O
ANISOU 2711  O   PRO A 363     2719   2367   3437   -319   -417   -304       O
ATOM   2712  CB  PRO A 363     -37.202 -58.233 -39.208  1.00 20.58           C
ANISOU 2712  CB  PRO A 363     2618   2123   3077   -203   -333   -242       C
ATOM   2713  CG  PRO A 363     -36.060 -58.240 -38.254  1.00 20.22           C
ANISOU 2713  CG  PRO A 363     2600   2067   3016   -184   -276   -179       C
ATOM   2714  CD  PRO A 363     -36.348 -59.417 -37.344  1.00 21.11           C
ANISOU 2714  CD  PRO A 363     2708   2102   3211   -235   -261   -151       C
ATOM   2715  N   GLU A 364     -39.509 -60.457 -39.400  1.00 23.62           N
ANISOU 2715  N   GLU A 364     2939   2376   3661   -340   -416   -327       N
ATOM   2716  CA  GLU A 364     -40.547 -61.102 -40.220  1.00 25.23           C
ANISOU 2716  CA  GLU A 364     3114   2550   3924   -381   -486   -408       C
ATOM   2717  C   GLU A 364     -41.959 -60.955 -39.643  1.00 25.23           C
ANISOU 2717  C   GLU A 364     3026   2562   3998   -453   -487   -386       C
ATOM   2718  O   GLU A 364     -42.938 -61.003 -40.391  1.00 25.72           O
ANISOU 2718  O   GLU A 364     3043   2641   4088   -477   -550   -452       O
ATOM   2719  CB  GLU A 364     -40.206 -62.575 -40.481  1.00 26.69           C
ANISOU 2719  CB  GLU A 364     3343   2625   4172   -400   -508   -455       C
ATOM   2720  CG  GLU A 364     -38.909 -62.730 -41.279  1.00 30.01           C
ANISOU 2720  CG  GLU A 364     3845   3043   4514   -320   -517   -492       C
ATOM   2721  CD  GLU A 364     -38.630 -64.137 -41.765  1.00 35.31           C
ANISOU 2721  CD  GLU A 364     4566   3610   5241   -326   -550   -559       C
ATOM   2722  OE1 GLU A 364     -37.441 -64.435 -42.018  1.00 39.28           O
ANISOU 2722  OE1 GLU A 364     5135   4093   5695   -264   -533   -563       O
ATOM   2723  OE2 GLU A 364     -39.580 -64.937 -41.909  1.00 38.89           O
ANISOU 2723  OE2 GLU A 364     4990   3999   5788   -392   -593   -609       O
ATOM   2724  N   LEU A 365     -42.060 -60.747 -38.330  1.00 24.62           N
ANISOU 2724  N   LEU A 365     2922   2484   3948   -481   -419   -295       N
ATOM   2725  CA  LEU A 365     -43.356 -60.547 -37.667  1.00 25.17           C
ANISOU 2725  CA  LEU A 365     2906   2573   4085   -543   -405   -260       C
ATOM   2726  C   LEU A 365     -44.138 -59.358 -38.219  1.00 24.99           C
ANISOU 2726  C   LEU A 365     2832   2651   4013   -521   -437   -285       C
ATOM   2727  O   LEU A 365     -45.366 -59.339 -38.149  1.00 25.76           O
ANISOU 2727  O   LEU A 365     2850   2766   4171   -570   -456   -292       O
ATOM   2728  CB  LEU A 365     -43.160 -60.339 -36.164  1.00 24.70           C
ANISOU 2728  CB  LEU A 365     2838   2514   4031   -554   -319   -154       C
ATOM   2729  CG  LEU A 365     -42.583 -61.501 -35.355  1.00 25.56           C
ANISOU 2729  CG  LEU A 365     2986   2529   4198   -578   -275   -106       C
ATOM   2730  CD1 LEU A 365     -42.331 -61.043 -33.916  1.00 25.76           C
ANISOU 2730  CD1 LEU A 365     3006   2584   4198   -568   -193     -1       C
ATOM   2731  CD2 LEU A 365     -43.500 -62.714 -35.399  1.00 27.36           C
ANISOU 2731  CD2 LEU A 365     3174   2667   4553   -660   -294   -127       C
ATOM   2732  N   LEU A 366     -43.430 -58.364 -38.749  1.00 24.34           N
ANISOU 2732  N   LEU A 366     2790   2634   3825   -446   -440   -292       N
ATOM   2733  CA  LEU A 366     -44.067 -57.144 -39.242  1.00 24.23           C
ANISOU 2733  CA  LEU A 366     2737   2713   3756   -412   -462   -304       C
ATOM   2734  C   LEU A 366     -44.336 -57.141 -40.752  1.00 24.90           C
ANISOU 2734  C   LEU A 366     2827   2827   3806   -380   -546   -397       C
ATOM   2735  O   LEU A 366     -44.989 -56.220 -41.255  1.00 24.72           O
ANISOU 2735  O   LEU A 366     2767   2882   3742   -350   -573   -410       O
ATOM   2736  CB  LEU A 366     -43.226 -55.925 -38.860  1.00 23.28           C
ANISOU 2736  CB  LEU A 366     2652   2647   3545   -350   -409   -249       C
ATOM   2737  CG  LEU A 366     -43.138 -55.634 -37.357  1.00 23.05           C
ANISOU 2737  CG  LEU A 366     2609   2616   3533   -371   -332   -162       C
ATOM   2738  CD1 LEU A 366     -42.179 -54.491 -37.084  1.00 21.97           C
ANISOU 2738  CD1 LEU A 366     2514   2523   3310   -312   -291   -124       C
ATOM   2739  CD2 LEU A 366     -44.516 -55.335 -36.756  1.00 23.76           C
ANISOU 2739  CD2 LEU A 366     2613   2738   3675   -413   -321   -136       C
ATOM   2740  N   PHE A 367     -43.873 -58.165 -41.470  1.00 25.40           N
ANISOU 2740  N   PHE A 367     2937   2832   3883   -380   -589   -461       N
ATOM   2741  CA  PHE A 367     -43.954 -58.153 -42.936  1.00 26.01           C
ANISOU 2741  CA  PHE A 367     3034   2943   3907   -334   -668   -553       C
ATOM   2742  C   PHE A 367     -45.384 -58.189 -43.484  1.00 27.45           C
ANISOU 2742  C   PHE A 367     3135   3161   4132   -368   -741   -613       C
ATOM   2743  O   PHE A 367     -45.615 -57.728 -44.599  1.00 27.89           O
ANISOU 2743  O   PHE A 367     3193   3282   4120   -313   -801   -671       O
ATOM   2744  CB  PHE A 367     -43.122 -59.279 -43.571  1.00 26.23           C
ANISOU 2744  CB  PHE A 367     3133   2898   3936   -321   -697   -616       C
ATOM   2745  CG  PHE A 367     -41.625 -59.133 -43.403  1.00 25.37           C
ANISOU 2745  CG  PHE A 367     3103   2776   3759   -263   -640   -573       C
ATOM   2746  CD1 PHE A 367     -40.786 -60.172 -43.791  1.00 26.42           C
ANISOU 2746  CD1 PHE A 367     3302   2839   3898   -247   -651   -616       C
ATOM   2747  CD2 PHE A 367     -41.047 -57.985 -42.864  1.00 24.34           C
ANISOU 2747  CD2 PHE A 367     2982   2702   3566   -224   -576   -494       C
ATOM   2748  CE1 PHE A 367     -39.407 -60.065 -43.651  1.00 25.53           C
ANISOU 2748  CE1 PHE A 367     3254   2719   3726   -192   -600   -577       C
ATOM   2749  CE2 PHE A 367     -39.672 -57.883 -42.718  1.00 23.47           C
ANISOU 2749  CE2 PHE A 367     2934   2581   3402   -177   -527   -459       C
ATOM   2750  CZ  PHE A 367     -38.854 -58.926 -43.111  1.00 23.90           C
ANISOU 2750  CZ  PHE A 367     3047   2573   3462   -160   -539   -498       C
ATOM   2751  N   ASN A 368     -46.334 -58.735 -42.723  1.00 28.51           N
ANISOU 2751  N   ASN A 368     3197   3257   4379   -454   -736   -598       N
ATOM   2752  CA  ASN A 368     -47.743 -58.693 -43.130  1.00 29.92           C
ANISOU 2752  CA  ASN A 368     3282   3478   4609   -492   -802   -647       C
ATOM   2753  C   ASN A 368     -48.552 -57.640 -42.366  1.00 29.53           C
ANISOU 2753  C   ASN A 368     3156   3502   4562   -497   -758   -573       C
ATOM   2754  O   ASN A 368     -49.776 -57.695 -42.354  1.00 30.52           O
ANISOU 2754  O   ASN A 368     3188   3654   4755   -544   -792   -592       O
ATOM   2755  CB  ASN A 368     -48.405 -60.084 -43.034  1.00 31.43           C
ANISOU 2755  CB  ASN A 368     3429   3578   4935   -589   -841   -699       C
ATOM   2756  CG  ASN A 368     -48.564 -60.586 -41.599  1.00 32.31           C
ANISOU 2756  CG  ASN A 368     3508   3619   5149   -667   -759   -610       C
ATOM   2757  OD1 ASN A 368     -48.171 -59.931 -40.633  1.00 33.89           O
ANISOU 2757  OD1 ASN A 368     3721   3842   5316   -647   -675   -513       O
ATOM   2758  ND2 ASN A 368     -49.137 -61.774 -41.465  1.00 35.57           N
ANISOU 2758  ND2 ASN A 368     3882   3944   5689   -756   -783   -643       N
ATOM   2759  N   GLN A 369     -47.860 -56.684 -41.746  1.00 28.26           N
ANISOU 2759  N   GLN A 369     3034   3373   4331   -447   -683   -492       N
ATOM   2760  CA  GLN A 369     -48.498 -55.621 -40.972  1.00 27.91           C
ANISOU 2760  CA  GLN A 369     2931   3393   4279   -441   -634   -422       C
ATOM   2761  C   GLN A 369     -48.189 -54.257 -41.571  1.00 27.34           C
ANISOU 2761  C   GLN A 369     2891   3406   4091   -347   -635   -413       C
ATOM   2762  O   GLN A 369     -47.180 -54.084 -42.266  1.00 26.83           O
ANISOU 2762  O   GLN A 369     2906   3341   3947   -288   -643   -433       O
ATOM   2763  CB  GLN A 369     -47.993 -55.640 -39.528  1.00 27.30           C
ANISOU 2763  CB  GLN A 369     2871   3276   4227   -467   -537   -329       C
ATOM   2764  CG  GLN A 369     -48.261 -56.938 -38.780  1.00 28.72           C
ANISOU 2764  CG  GLN A 369     3023   3367   4520   -555   -518   -314       C
ATOM   2765  CD  GLN A 369     -49.739 -57.197 -38.581  1.00 30.63           C
ANISOU 2765  CD  GLN A 369     3153   3625   4860   -622   -538   -320       C
ATOM   2766  OE1 GLN A 369     -50.266 -58.232 -39.001  1.00 34.26           O
ANISOU 2766  OE1 GLN A 369     3577   4032   5408   -685   -590   -377       O
ATOM   2767  NE2 GLN A 369     -50.422 -56.250 -37.955  1.00 31.20           N
ANISOU 2767  NE2 GLN A 369     3166   3767   4921   -609   -497   -265       N
ATOM   2768  N   GLN A 370     -49.050 -53.288 -41.282  1.00 27.34           N
ANISOU 2768  N   GLN A 370     2829   3476   4084   -331   -621   -379       N
ATOM   2769  CA  GLN A 370     -48.757 -51.893 -41.604  1.00 26.88           C
ANISOU 2769  CA  GLN A 370     2802   3486   3926   -244   -602   -351       C
ATOM   2770  C   GLN A 370     -47.757 -51.364 -40.588  1.00 25.59           C
ANISOU 2770  C   GLN A 370     2694   3295   3732   -230   -512   -276       C
ATOM   2771  O   GLN A 370     -48.007 -51.397 -39.381  1.00 25.74           O
ANISOU 2771  O   GLN A 370     2682   3298   3800   -272   -456   -222       O
ATOM   2772  CB  GLN A 370     -50.026 -51.046 -41.579  1.00 27.64           C
ANISOU 2772  CB  GLN A 370     2812   3660   4029   -227   -614   -339       C
ATOM   2773  CG  GLN A 370     -51.017 -51.364 -42.676  1.00 29.84           C
ANISOU 2773  CG  GLN A 370     3030   3986   4322   -225   -711   -416       C
ATOM   2774  CD  GLN A 370     -52.284 -50.537 -42.544  1.00 32.78           C
ANISOU 2774  CD  GLN A 370     3310   4439   4708   -206   -719   -396       C
ATOM   2775  OE1 GLN A 370     -53.041 -50.691 -41.584  1.00 34.65           O
ANISOU 2775  OE1 GLN A 370     3471   4673   5024   -262   -683   -360       O
ATOM   2776  NE2 GLN A 370     -52.516 -49.648 -43.502  1.00 33.57           N
ANISOU 2776  NE2 GLN A 370     3415   4615   4727   -121   -761   -415       N
ATOM   2777  N   PHE A 371     -46.612 -50.896 -41.074  1.00 24.37           N
ANISOU 2777  N   PHE A 371     2622   3140   3498   -172   -499   -273       N
ATOM   2778  CA  PHE A 371     -45.542 -50.430 -40.212  1.00 23.02           C
ANISOU 2778  CA  PHE A 371     2504   2943   3298   -160   -424   -213       C
ATOM   2779  C   PHE A 371     -44.598 -49.557 -41.028  1.00 22.30           C
ANISOU 2779  C   PHE A 371     2481   2876   3116    -83   -419   -213       C
ATOM   2780  O   PHE A 371     -44.254 -49.908 -42.161  1.00 22.85           O
ANISOU 2780  O   PHE A 371     2585   2950   3149    -52   -465   -261       O
ATOM   2781  CB  PHE A 371     -44.780 -51.619 -39.616  1.00 23.03           C
ANISOU 2781  CB  PHE A 371     2538   2869   3345   -210   -404   -209       C
ATOM   2782  CG  PHE A 371     -43.726 -51.227 -38.634  1.00 22.41           C
ANISOU 2782  CG  PHE A 371     2504   2768   3241   -201   -334   -151       C
ATOM   2783  CD1 PHE A 371     -44.061 -50.927 -37.322  1.00 23.50           C
ANISOU 2783  CD1 PHE A 371     2611   2911   3408   -228   -279    -95       C
ATOM   2784  CD2 PHE A 371     -42.397 -51.140 -39.018  1.00 21.28           C
ANISOU 2784  CD2 PHE A 371     2433   2609   3044   -163   -322   -153       C
ATOM   2785  CE1 PHE A 371     -43.087 -50.562 -36.411  1.00 23.78           C
ANISOU 2785  CE1 PHE A 371     2687   2932   3416   -216   -222    -49       C
ATOM   2786  CE2 PHE A 371     -41.428 -50.775 -38.115  1.00 21.92           C
ANISOU 2786  CE2 PHE A 371     2547   2675   3106   -157   -264   -104       C
ATOM   2787  CZ  PHE A 371     -41.773 -50.476 -36.808  1.00 22.17           C
ANISOU 2787  CZ  PHE A 371     2548   2710   3163   -183   -218    -56       C
ATOM   2788  N   GLN A 372     -44.193 -48.429 -40.452  1.00 20.96           N
ANISOU 2788  N   GLN A 372     2330   2723   2913    -53   -362   -159       N
ATOM   2789  CA  GLN A 372     -43.287 -47.493 -41.117  1.00 20.16           C
ANISOU 2789  CA  GLN A 372     2287   2637   2735     14   -344   -146       C
ATOM   2790  C   GLN A 372     -41.852 -47.713 -40.663  1.00 19.13           C
ANISOU 2790  C   GLN A 372     2214   2460   2594      6   -300   -124       C
ATOM   2791  O   GLN A 372     -41.527 -47.530 -39.483  1.00 18.71           O
ANISOU 2791  O   GLN A 372     2159   2385   2564    -22   -251    -86       O
ATOM   2792  CB  GLN A 372     -43.704 -46.047 -40.815  1.00 19.82           C
ANISOU 2792  CB  GLN A 372     2229   2632   2668     53   -308   -104       C
ATOM   2793  CG  GLN A 372     -45.109 -45.705 -41.247  1.00 20.89           C
ANISOU 2793  CG  GLN A 372     2304   2823   2810     72   -349   -120       C
ATOM   2794  CD  GLN A 372     -45.295 -45.778 -42.751  1.00 21.36           C
ANISOU 2794  CD  GLN A 372     2375   2921   2820    124   -412   -163       C
ATOM   2795  OE1 GLN A 372     -44.502 -45.213 -43.516  1.00 20.28           O
ANISOU 2795  OE1 GLN A 372     2296   2791   2618    182   -401   -153       O
ATOM   2796  NE2 GLN A 372     -46.340 -46.483 -43.188  1.00 19.73           N
ANISOU 2796  NE2 GLN A 372     2112   2742   2644    104   -478   -211       N
ATOM   2797  N   TYR A 373     -40.986 -48.094 -41.602  1.00 18.79           N
ANISOU 2797  N   TYR A 373     2220   2407   2512     36   -317   -150       N
ATOM   2798  CA  TYR A 373     -39.573 -48.291 -41.312  1.00 18.49           C
ANISOU 2798  CA  TYR A 373     2232   2332   2461     37   -278   -131       C
ATOM   2799  C   TYR A 373     -38.838 -46.955 -41.325  1.00 18.27           C
ANISOU 2799  C   TYR A 373     2232   2322   2389     80   -229    -88       C
ATOM   2800  O   TYR A 373     -38.057 -46.656 -42.228  1.00 18.13           O
ANISOU 2800  O   TYR A 373     2254   2314   2322    127   -223    -88       O
ATOM   2801  CB  TYR A 373     -38.944 -49.279 -42.297  1.00 18.85           C
ANISOU 2801  CB  TYR A 373     2317   2360   2486     55   -312   -176       C
ATOM   2802  CG  TYR A 373     -39.529 -50.658 -42.154  1.00 18.39           C
ANISOU 2802  CG  TYR A 373     2236   2265   2485      4   -356   -219       C
ATOM   2803  CD1 TYR A 373     -40.447 -51.146 -43.075  1.00 19.18           C
ANISOU 2803  CD1 TYR A 373     2316   2383   2589      8   -423   -279       C
ATOM   2804  CD2 TYR A 373     -39.192 -51.460 -41.069  1.00 18.71           C
ANISOU 2804  CD2 TYR A 373     2275   2252   2581    -48   -330   -200       C
ATOM   2805  CE1 TYR A 373     -41.004 -52.413 -42.933  1.00 20.58           C
ANISOU 2805  CE1 TYR A 373     2470   2516   2833    -48   -463   -322       C
ATOM   2806  CE2 TYR A 373     -39.740 -52.725 -40.917  1.00 19.05           C
ANISOU 2806  CE2 TYR A 373     2299   2251   2688    -99   -363   -233       C
ATOM   2807  CZ  TYR A 373     -40.647 -53.194 -41.846  1.00 19.94           C
ANISOU 2807  CZ  TYR A 373     2390   2373   2814   -103   -429   -295       C
ATOM   2808  OH  TYR A 373     -41.198 -54.452 -41.699  1.00 21.49           O
ANISOU 2808  OH  TYR A 373     2564   2515   3085   -160   -463   -332       O
ATOM   2809  N   GLN A 374     -39.123 -46.158 -40.306  1.00 18.33           N
ANISOU 2809  N   GLN A 374     2216   2331   2416     63   -193    -52       N
ATOM   2810  CA  GLN A 374     -38.442 -44.893 -40.070  1.00 18.51           C
ANISOU 2810  CA  GLN A 374     2261   2356   2414     90   -143    -13       C
ATOM   2811  C   GLN A 374     -38.684 -44.521 -38.615  1.00 18.58           C
ANISOU 2811  C   GLN A 374     2246   2355   2459     54   -110     11       C
ATOM   2812  O   GLN A 374     -39.586 -45.066 -37.980  1.00 19.08           O
ANISOU 2812  O   GLN A 374     2271   2421   2557     20   -123      5       O
ATOM   2813  CB  GLN A 374     -38.970 -43.801 -41.004  1.00 19.22           C
ANISOU 2813  CB  GLN A 374     2355   2482   2466    147   -147     -5       C
ATOM   2814  CG  GLN A 374     -40.475 -43.558 -40.891  1.00 19.43           C
ANISOU 2814  CG  GLN A 374     2333   2542   2509    149   -174    -12       C
ATOM   2815  CD  GLN A 374     -40.968 -42.404 -41.750  1.00 22.54           C
ANISOU 2815  CD  GLN A 374     2731   2971   2860    215   -174      4       C
ATOM   2816  OE1 GLN A 374     -40.838 -41.230 -41.379  1.00 22.19           O
ANISOU 2816  OE1 GLN A 374     2699   2920   2814    236   -130     41       O
ATOM   2817  NE2 GLN A 374     -41.558 -42.731 -42.893  1.00 21.96           N
ANISOU 2817  NE2 GLN A 374     2651   2936   2756    251   -226    -24       N
ATOM   2818  N   ASN A 375     -37.879 -43.604 -38.092  1.00 18.43           N
ANISOU 2818  N   ASN A 375     2248   2324   2432     61    -67     37       N
ATOM   2819  CA  ASN A 375     -38.024 -43.141 -36.715  1.00 18.40           C
ANISOU 2819  CA  ASN A 375     2228   2313   2449     36    -36     54       C
ATOM   2820  C   ASN A 375     -37.418 -41.757 -36.562  1.00 17.68           C
ANISOU 2820  C   ASN A 375     2159   2212   2345     59      2     72       C
ATOM   2821  O   ASN A 375     -36.430 -41.432 -37.216  1.00 17.56           O
ANISOU 2821  O   ASN A 375     2174   2184   2314     76     14     78       O
ATOM   2822  CB  ASN A 375     -37.352 -44.114 -35.730  1.00 18.72           C
ANISOU 2822  CB  ASN A 375     2270   2332   2509     -5    -30     55       C
ATOM   2823  CG  ASN A 375     -37.693 -43.808 -34.271  1.00 19.40           C
ANISOU 2823  CG  ASN A 375     2337   2423   2610    -26     -3     70       C
ATOM   2824  OD1 ASN A 375     -38.857 -43.727 -33.903  1.00 21.53           O
ANISOU 2824  OD1 ASN A 375     2575   2712   2894    -31     -4     73       O
ATOM   2825  ND2 ASN A 375     -36.668 -43.630 -33.445  1.00 22.73           N
ANISOU 2825  ND2 ASN A 375     2777   2832   3026    -35     19     77       N
ATOM   2826  N   ARG A 376     -38.038 -40.941 -35.717  1.00 17.15           N
ANISOU 2826  N   ARG A 376     2078   2151   2288     60     22     80       N
ATOM   2827  CA  ARG A 376     -37.474 -39.650 -35.307  1.00 16.24           C
ANISOU 2827  CA  ARG A 376     1984   2015   2172     73     59     90       C
ATOM   2828  C   ARG A 376     -37.478 -39.662 -33.779  1.00 15.94           C
ANISOU 2828  C   ARG A 376     1935   1976   2147     45     74     84       C
ATOM   2829  O   ARG A 376     -38.492 -40.003 -33.166  1.00 16.17           O
ANISOU 2829  O   ARG A 376     1934   2027   2182     39     70     84       O
ATOM   2830  CB  ARG A 376     -38.322 -38.497 -35.861  1.00 16.28           C
ANISOU 2830  CB  ARG A 376     1990   2027   2170    119     68    101       C
ATOM   2831  CG  ARG A 376     -37.655 -37.124 -35.848  1.00 15.91           C
ANISOU 2831  CG  ARG A 376     1974   1945   2128    137    106    113       C
ATOM   2832  CD  ARG A 376     -36.612 -36.959 -36.962  1.00 16.04           C
ANISOU 2832  CD  ARG A 376     2020   1941   2133    151    116    130       C
ATOM   2833  NE  ARG A 376     -37.170 -37.046 -38.315  1.00 15.62           N
ANISOU 2833  NE  ARG A 376     1971   1914   2051    197     99    144       N
ATOM   2834  CZ  ARG A 376     -37.825 -36.070 -38.952  1.00 15.35           C
ANISOU 2834  CZ  ARG A 376     1945   1882   2003    249    110    167       C
ATOM   2835  NH1 ARG A 376     -38.054 -34.893 -38.372  1.00 14.63           N
ANISOU 2835  NH1 ARG A 376     1863   1763   1934    260    142    177       N
ATOM   2836  NH2 ARG A 376     -38.276 -36.281 -40.184  1.00 16.03           N
ANISOU 2836  NH2 ARG A 376     2036   2002   2054    294     87    177       N
ATOM   2837  N   ILE A 377     -36.344 -39.329 -33.168  1.00 15.99           N
ANISOU 2837  N   ILE A 377     1960   1960   2156     30     92     78       N
ATOM   2838  CA  ILE A 377     -36.180 -39.415 -31.721  1.00 15.82           C
ANISOU 2838  CA  ILE A 377     1932   1943   2134      8    101     69       C
ATOM   2839  C   ILE A 377     -36.961 -38.296 -31.029  1.00 16.11           C
ANISOU 2839  C   ILE A 377     1967   1983   2170     29    122     62       C
ATOM   2840  O   ILE A 377     -36.819 -37.113 -31.369  1.00 16.37           O
ANISOU 2840  O   ILE A 377     2019   1991   2210     50    138     58       O
ATOM   2841  CB  ILE A 377     -34.693 -39.355 -31.304  1.00 15.75           C
ANISOU 2841  CB  ILE A 377     1941   1916   2127    -11    105     58       C
ATOM   2842  CG1 ILE A 377     -33.927 -40.548 -31.898  1.00 14.71           C
ANISOU 2842  CG1 ILE A 377     1810   1785   1995    -25     87     66       C
ATOM   2843  CG2 ILE A 377     -34.551 -39.324 -29.776  1.00 15.62           C
ANISOU 2843  CG2 ILE A 377     1921   1914   2102    -23    110     43       C
ATOM   2844  CD1 ILE A 377     -34.277 -41.911 -31.295  1.00 15.70           C
ANISOU 2844  CD1 ILE A 377     1921   1928   2117    -42     72     72       C
ATOM   2845  N   ALA A 378     -37.789 -38.684 -30.062  1.00 16.11           N
ANISOU 2845  N   ALA A 378     1946   2013   2164     26    126     63       N
ATOM   2846  CA  ALA A 378     -38.623 -37.730 -29.338  1.00 16.41           C
ANISOU 2846  CA  ALA A 378     1979   2061   2196     53    149     55       C
ATOM   2847  C   ALA A 378     -37.915 -37.157 -28.114  1.00 16.30           C
ANISOU 2847  C   ALA A 378     1987   2039   2169     50    163     29       C
ATOM   2848  O   ALA A 378     -37.249 -37.882 -27.369  1.00 16.43           O
ANISOU 2848  O   ALA A 378     2004   2068   2172     28    155     26       O
ATOM   2849  CB  ALA A 378     -39.929 -38.378 -28.924  1.00 16.83           C
ANISOU 2849  CB  ALA A 378     1992   2155   2248     57    152     72       C
ATOM   2850  N   SER A 379     -38.098 -35.855 -27.896  1.00 16.48           N
ANISOU 2850  N   SER A 379     2026   2041   2193     77    181      9       N
ATOM   2851  CA  SER A 379     -37.556 -35.172 -26.731  1.00 17.05           C
ANISOU 2851  CA  SER A 379     2120   2105   2252     79    189    -28       C
ATOM   2852  C   SER A 379     -37.999 -35.844 -25.429  1.00 17.10           C
ANISOU 2852  C   SER A 379     2111   2163   2222     84    195    -29       C
ATOM   2853  O   SER A 379     -37.215 -35.990 -24.496  1.00 17.23           O
ANISOU 2853  O   SER A 379     2140   2189   2216     73    187    -51       O
ATOM   2854  CB  SER A 379     -38.009 -33.711 -26.734  1.00 17.40           C
ANISOU 2854  CB  SER A 379     2185   2117   2308    115    211    -50       C
ATOM   2855  OG  SER A 379     -37.526 -33.027 -25.602  1.00 19.58           O
ANISOU 2855  OG  SER A 379     2485   2383   2572    119    215    -97       O
ATOM   2856  N   GLU A 380     -39.260 -36.251 -25.374  1.00 17.31           N
ANISOU 2856  N   GLU A 380     2110   2225   2244    101    210     -1       N
ATOM   2857  CA  GLU A 380     -39.811 -36.851 -24.160  1.00 17.76           C
ANISOU 2857  CA  GLU A 380     2149   2331   2267    110    227     11       C
ATOM   2858  C   GLU A 380     -39.201 -38.233 -23.876  1.00 17.47           C
ANISOU 2858  C   GLU A 380     2103   2311   2222     76    213     35       C
ATOM   2859  O   GLU A 380     -39.116 -38.655 -22.719  1.00 17.52           O
ANISOU 2859  O   GLU A 380     2111   2352   2193     83    224     40       O
ATOM   2860  CB  GLU A 380     -41.332 -36.945 -24.256  1.00 18.05           C
ANISOU 2860  CB  GLU A 380     2146   2401   2311    134    250     40       C
ATOM   2861  CG  GLU A 380     -42.015 -35.596 -24.468  1.00 18.45           C
ANISOU 2861  CG  GLU A 380     2204   2439   2366    180    267     20       C
ATOM   2862  CD  GLU A 380     -42.425 -35.337 -25.915  1.00 18.40           C
ANISOU 2862  CD  GLU A 380     2186   2410   2397    185    253     35       C
ATOM   2863  OE1 GLU A 380     -41.771 -35.887 -26.836  1.00 18.52           O
ANISOU 2863  OE1 GLU A 380     2205   2403   2430    152    226     45       O
ATOM   2864  OE2 GLU A 380     -43.401 -34.572 -26.125  1.00 17.71           O
ANISOU 2864  OE2 GLU A 380     2085   2331   2315    228    270     38       O
ATOM   2865  N   PHE A 381     -38.798 -38.931 -24.935  1.00 17.08           N
ANISOU 2865  N   PHE A 381     2048   2239   2203     45    189     52       N
ATOM   2866  CA  PHE A 381     -38.080 -40.202 -24.808  1.00 17.33           C
ANISOU 2866  CA  PHE A 381     2078   2273   2233     15    174     72       C
ATOM   2867  C   PHE A 381     -36.711 -39.952 -24.179  1.00 17.68           C
ANISOU 2867  C   PHE A 381     2152   2313   2254     12    161     43       C
ATOM   2868  O   PHE A 381     -36.302 -40.664 -23.266  1.00 17.68           O
ANISOU 2868  O   PHE A 381     2153   2338   2225     11    160     54       O
ATOM   2869  CB  PHE A 381     -37.968 -40.875 -26.179  1.00 17.09           C
ANISOU 2869  CB  PHE A 381     2038   2216   2238     -9    151     86       C
ATOM   2870  CG  PHE A 381     -37.419 -42.283 -26.152  1.00 18.13           C
ANISOU 2870  CG  PHE A 381     2168   2345   2375    -36    138    108       C
ATOM   2871  CD1 PHE A 381     -37.785 -43.191 -25.167  1.00 18.68           C
ANISOU 2871  CD1 PHE A 381     2225   2439   2435    -41    154    139       C
ATOM   2872  CD2 PHE A 381     -36.554 -42.710 -27.152  1.00 18.72           C
ANISOU 2872  CD2 PHE A 381     2255   2391   2467    -51    113    103       C
ATOM   2873  CE1 PHE A 381     -37.290 -44.488 -25.177  1.00 18.56           C
ANISOU 2873  CE1 PHE A 381     2212   2411   2430    -63    144    163       C
ATOM   2874  CE2 PHE A 381     -36.053 -44.015 -27.162  1.00 18.58           C
ANISOU 2874  CE2 PHE A 381     2239   2364   2456    -70    102    122       C
ATOM   2875  CZ  PHE A 381     -36.427 -44.897 -26.178  1.00 18.16           C
ANISOU 2875  CZ  PHE A 381     2175   2328   2398    -76    116    152       C
ATOM   2876  N   ASN A 382     -36.022 -38.913 -24.645  1.00 17.57           N
ANISOU 2876  N   ASN A 382     2157   2267   2252     13    150      7       N
ATOM   2877  CA  ASN A 382     -34.793 -38.466 -24.005  1.00 18.42           C
ANISOU 2877  CA  ASN A 382     2283   2369   2345      8    135    -30       C
ATOM   2878  C   ASN A 382     -35.025 -38.188 -22.518  1.00 18.53           C
ANISOU 2878  C   ASN A 382     2306   2424   2312     34    144    -52       C
ATOM   2879  O   ASN A 382     -34.354 -38.752 -21.664  1.00 18.82           O
ANISOU 2879  O   ASN A 382     2346   2491   2315     35    131    -55       O
ATOM   2880  CB  ASN A 382     -34.246 -37.217 -24.706  1.00 18.95           C
ANISOU 2880  CB  ASN A 382     2366   2389   2445      2    132    -63       C
ATOM   2881  CG  ASN A 382     -32.810 -36.903 -24.322  1.00 21.61           C
ANISOU 2881  CG  ASN A 382     2711   2715   2785    -17    110   -100       C
ATOM   2882  OD1 ASN A 382     -32.313 -37.345 -23.289  1.00 26.43           O
ANISOU 2882  OD1 ASN A 382     3320   3360   3361    -15     94   -114       O
ATOM   2883  ND2 ASN A 382     -32.131 -36.143 -25.168  1.00 25.16           N
ANISOU 2883  ND2 ASN A 382     3166   3117   3277    -34    109   -113       N
ATOM   2884  N   THR A 383     -36.014 -37.357 -22.216  1.00 18.86           N
ANISOU 2884  N   THR A 383     2352   2470   2345     63    168    -65       N
ATOM   2885  CA  THR A 383     -36.293 -36.964 -20.838  1.00 19.48           C
ANISOU 2885  CA  THR A 383     2442   2588   2371     98    180    -91       C
ATOM   2886  C   THR A 383     -36.580 -38.156 -19.928  1.00 19.60           C
ANISOU 2886  C   THR A 383     2444   2660   2341    109    192    -50       C
ATOM   2887  O   THR A 383     -35.985 -38.274 -18.852  1.00 20.06           O
ANISOU 2887  O   THR A 383     2518   2755   2350    126    181    -69       O
ATOM   2888  CB  THR A 383     -37.459 -35.969 -20.779  1.00 19.87           C
ANISOU 2888  CB  THR A 383     2495   2634   2422    135    210   -104       C
ATOM   2889  OG1 THR A 383     -37.083 -34.775 -21.475  1.00 20.63           O
ANISOU 2889  OG1 THR A 383     2611   2671   2557    130    201   -144       O
ATOM   2890  CG2 THR A 383     -37.809 -35.624 -19.333  1.00 20.71           C
ANISOU 2890  CG2 THR A 383     2615   2787   2465    180    226   -132       C
ATOM   2891  N   LEU A 384     -37.462 -39.052 -20.368  1.00 19.34           N
ANISOU 2891  N   LEU A 384     2383   2636   2328    100    212      8       N
ATOM   2892  CA  LEU A 384     -37.859 -40.184 -19.528  1.00 19.55           C
ANISOU 2892  CA  LEU A 384     2396   2709   2323    108    235     59       C
ATOM   2893  C   LEU A 384     -36.711 -41.153 -19.270  1.00 19.19           C
ANISOU 2893  C   LEU A 384     2361   2668   2264     92    210     73       C
ATOM   2894  O   LEU A 384     -36.717 -41.852 -18.258  1.00 19.46           O
ANISOU 2894  O   LEU A 384     2397   2744   2252    112    225    105       O
ATOM   2895  CB  LEU A 384     -39.074 -40.918 -20.109  1.00 19.65           C
ANISOU 2895  CB  LEU A 384     2370   2721   2376     93    261    115       C
ATOM   2896  CG  LEU A 384     -38.925 -41.785 -21.360  1.00 19.69           C
ANISOU 2896  CG  LEU A 384     2359   2685   2439     48    239    139       C
ATOM   2897  CD1 LEU A 384     -38.324 -43.175 -21.033  1.00 19.95           C
ANISOU 2897  CD1 LEU A 384     2393   2719   2468     28    234    179       C
ATOM   2898  CD2 LEU A 384     -40.282 -41.944 -22.044  1.00 20.80           C
ANISOU 2898  CD2 LEU A 384     2457   2824   2622     39    256    166       C
ATOM   2899  N   TYR A 385     -35.715 -41.164 -20.163  1.00 18.61           N
ANISOU 2899  N   TYR A 385     2293   2553   2224     61    175     53       N
ATOM   2900  CA  TYR A 385     -34.564 -42.069 -20.051  1.00 18.37           C
ANISOU 2900  CA  TYR A 385     2269   2525   2186     49    149     66       C
ATOM   2901  C   TYR A 385     -33.428 -41.528 -19.155  1.00 18.95           C
ANISOU 2901  C   TYR A 385     2361   2625   2213     68    121     17       C
ATOM   2902  O   TYR A 385     -32.346 -42.125 -19.095  1.00 18.59           O
ANISOU 2902  O   TYR A 385     2316   2585   2162     61     94     20       O
ATOM   2903  CB  TYR A 385     -34.004 -42.372 -21.446  1.00 17.93           C
ANISOU 2903  CB  TYR A 385     2208   2420   2187     13    128     68       C
ATOM   2904  CG  TYR A 385     -33.893 -43.842 -21.796  1.00 17.28           C
ANISOU 2904  CG  TYR A 385     2117   2326   2123     -4    127    118       C
ATOM   2905  CD1 TYR A 385     -34.505 -44.345 -22.935  1.00 16.85           C
ANISOU 2905  CD1 TYR A 385     2050   2236   2117    -28    130    139       C
ATOM   2906  CD2 TYR A 385     -33.172 -44.730 -20.999  1.00 17.32           C
ANISOU 2906  CD2 TYR A 385     2130   2355   2096      9    120    142       C
ATOM   2907  CE1 TYR A 385     -34.401 -45.688 -23.279  1.00 17.35           C
ANISOU 2907  CE1 TYR A 385     2110   2280   2204    -44    126    177       C
ATOM   2908  CE2 TYR A 385     -33.060 -46.073 -21.343  1.00 17.40           C
ANISOU 2908  CE2 TYR A 385     2138   2343   2129     -3    122    188       C
ATOM   2909  CZ  TYR A 385     -33.685 -46.544 -22.483  1.00 17.40           C
ANISOU 2909  CZ  TYR A 385     2126   2300   2184    -32    125    203       C
ATOM   2910  OH  TYR A 385     -33.586 -47.873 -22.842  1.00 18.64           O
ANISOU 2910  OH  TYR A 385     2284   2428   2369    -45    124    240       O
ATOM   2911  N   HIS A 386     -33.654 -40.409 -18.463  1.00 19.58           N
ANISOU 2911  N   HIS A 386     2454   2723   2261     93    124    -31       N
ATOM   2912  CA  HIS A 386     -32.673 -39.915 -17.484  1.00 20.48           C
ANISOU 2912  CA  HIS A 386     2584   2870   2327    113     91    -87       C
ATOM   2913  C   HIS A 386     -32.771 -40.744 -16.198  1.00 20.93           C
ANISOU 2913  C   HIS A 386     2648   2996   2308    156    102    -53       C
ATOM   2914  O   HIS A 386     -33.309 -40.290 -15.185  1.00 21.30           O
ANISOU 2914  O   HIS A 386     2710   3087   2296    199    118    -71       O
ATOM   2915  CB  HIS A 386     -32.869 -38.422 -17.203  1.00 21.21           C
ANISOU 2915  CB  HIS A 386     2693   2950   2415    127     88   -159       C
ATOM   2916  CG  HIS A 386     -32.473 -37.543 -18.346  1.00 23.04           C
ANISOU 2916  CG  HIS A 386     2922   3112   2719     88     75   -192       C
ATOM   2917  ND1 HIS A 386     -31.687 -36.420 -18.194  1.00 27.94           N
ANISOU 2917  ND1 HIS A 386     3554   3708   3355     78     46   -267       N
ATOM   2918  CD2 HIS A 386     -32.732 -37.643 -19.668  1.00 24.55           C
ANISOU 2918  CD2 HIS A 386     3101   3254   2972     58     88   -159       C
ATOM   2919  CE1 HIS A 386     -31.494 -35.858 -19.377  1.00 26.53           C
ANISOU 2919  CE1 HIS A 386     3370   3464   3248     43     49   -270       C
ATOM   2920  NE2 HIS A 386     -32.120 -36.581 -20.288  1.00 25.65           N
ANISOU 2920  NE2 HIS A 386     3247   3342   3159     35     74   -205       N
ATOM   2921  N   TRP A 387     -32.232 -41.962 -16.253  1.00 20.72           N
ANISOU 2921  N   TRP A 387     2614   2978   2281    149     94     -2       N
ATOM   2922  CA  TRP A 387     -32.407 -42.946 -15.187  1.00 21.48           C
ANISOU 2922  CA  TRP A 387     2718   3131   2312    190    114     53       C
ATOM   2923  C   TRP A 387     -31.282 -42.872 -14.155  1.00 22.67           C
ANISOU 2923  C   TRP A 387     2882   3339   2393    227     72     16       C
ATOM   2924  O   TRP A 387     -30.698 -43.887 -13.776  1.00 22.70           O
ANISOU 2924  O   TRP A 387     2886   3369   2368    245     64     60       O
ATOM   2925  CB  TRP A 387     -32.485 -44.357 -15.779  1.00 21.26           C
ANISOU 2925  CB  TRP A 387     2678   3074   2325    167    132    132       C
ATOM   2926  CG  TRP A 387     -33.707 -44.631 -16.614  1.00 19.64           C
ANISOU 2926  CG  TRP A 387     2455   2826   2180    136    171    173       C
ATOM   2927  CD1 TRP A 387     -34.825 -43.850 -16.730  1.00 20.06           C
ANISOU 2927  CD1 TRP A 387     2500   2878   2245    136    199    160       C
ATOM   2928  CD2 TRP A 387     -33.949 -45.796 -17.409  1.00 19.88           C
ANISOU 2928  CD2 TRP A 387     2473   2813   2268    104    184    231       C
ATOM   2929  NE1 TRP A 387     -35.736 -44.452 -17.566  1.00 19.42           N
ANISOU 2929  NE1 TRP A 387     2395   2759   2224    104    225    206       N
ATOM   2930  CE2 TRP A 387     -35.227 -45.648 -17.994  1.00 19.53           C
ANISOU 2930  CE2 TRP A 387     2408   2746   2269     81    215    246       C
ATOM   2931  CE3 TRP A 387     -33.209 -46.949 -17.688  1.00 19.60           C
ANISOU 2931  CE3 TRP A 387     2441   2756   2251     94    170    267       C
ATOM   2932  CZ2 TRP A 387     -35.778 -46.610 -18.848  1.00 19.71           C
ANISOU 2932  CZ2 TRP A 387     2411   2722   2355     44    227    290       C
ATOM   2933  CZ3 TRP A 387     -33.760 -47.912 -18.539  1.00 19.49           C
ANISOU 2933  CZ3 TRP A 387     2414   2689   2300     59    187    312       C
ATOM   2934  CH2 TRP A 387     -35.029 -47.733 -19.106  1.00 19.35           C
ANISOU 2934  CH2 TRP A 387     2374   2649   2328     32    212    320       C
ATOM   2935  N   HIS A 388     -31.019 -41.669 -13.659  1.00 23.61           N
ANISOU 2935  N   HIS A 388     3011   3477   2482    242     45    -67       N
ATOM   2936  CA  HIS A 388     -29.886 -41.458 -12.760  1.00 24.78           C
ANISOU 2936  CA  HIS A 388     3167   3680   2570    271     -8   -121       C
ATOM   2937  C   HIS A 388     -29.986 -42.181 -11.405  1.00 24.92           C
ANISOU 2937  C   HIS A 388     3203   3783   2482    341      2    -81       C
ATOM   2938  O   HIS A 388     -28.951 -42.448 -10.787  1.00 25.49           O
ANISOU 2938  O   HIS A 388     3275   3905   2505    369    -44   -101       O
ATOM   2939  CB  HIS A 388     -29.615 -39.959 -12.590  1.00 25.82           C
ANISOU 2939  CB  HIS A 388     3306   3801   2704    265    -43   -228       C
ATOM   2940  CG  HIS A 388     -29.144 -39.305 -13.851  1.00 28.28           C
ANISOU 2940  CG  HIS A 388     3598   4032   3115    199    -61   -264       C
ATOM   2941  ND1 HIS A 388     -29.848 -38.301 -14.480  1.00 32.00           N
ANISOU 2941  ND1 HIS A 388     4075   4444   3637    177    -38   -293       N
ATOM   2942  CD2 HIS A 388     -28.065 -39.554 -14.633  1.00 30.26           C
ANISOU 2942  CD2 HIS A 388     3822   4252   3422    157    -92   -266       C
ATOM   2943  CE1 HIS A 388     -29.213 -37.946 -15.584  1.00 31.99           C
ANISOU 2943  CE1 HIS A 388     4056   4380   3718    123    -54   -308       C
ATOM   2944  NE2 HIS A 388     -28.127 -38.690 -15.700  1.00 31.37           N
ANISOU 2944  NE2 HIS A 388     3957   4318   3645    109    -85   -294       N
ATOM   2945  N   PRO A 389     -31.208 -42.536 -10.953  1.00 24.52           N
ANISOU 2945  N   PRO A 389     3165   3755   2398    373     65    -20       N
ATOM   2946  CA  PRO A 389     -31.263 -43.347  -9.737  1.00 25.05           C
ANISOU 2946  CA  PRO A 389     3249   3901   2367    441     84     36       C
ATOM   2947  C   PRO A 389     -30.602 -44.722  -9.837  1.00 24.49           C
ANISOU 2947  C   PRO A 389     3172   3832   2303    443     80    114       C
ATOM   2948  O   PRO A 389     -30.282 -45.303  -8.807  1.00 25.14           O
ANISOU 2948  O   PRO A 389     3271   3983   2298    505     78    149       O
ATOM   2949  CB  PRO A 389     -32.766 -43.496  -9.483  1.00 25.01           C
ANISOU 2949  CB  PRO A 389     3248   3903   2351    461    163     99       C
ATOM   2950  CG  PRO A 389     -33.369 -42.291 -10.097  1.00 25.29           C
ANISOU 2950  CG  PRO A 389     3278   3894   2437    430    166     33       C
ATOM   2951  CD  PRO A 389     -32.549 -42.048 -11.332  1.00 24.32           C
ANISOU 2951  CD  PRO A 389     3136   3696   2406    361    118     -8       C
ATOM   2952  N   LEU A 390     -30.409 -45.244 -11.051  1.00 23.35           N
ANISOU 2952  N   LEU A 390     3007   3612   2255    382     79    142       N
ATOM   2953  CA  LEU A 390     -29.663 -46.498 -11.232  1.00 22.99           C
ANISOU 2953  CA  LEU A 390     2957   3557   2222    384     70    205       C
ATOM   2954  C   LEU A 390     -28.281 -46.438 -10.583  1.00 23.40           C
ANISOU 2954  C   LEU A 390     3010   3669   2212    423      4    161       C
ATOM   2955  O   LEU A 390     -27.772 -47.450 -10.106  1.00 23.48           O
ANISOU 2955  O   LEU A 390     3027   3712   2183    465      2    220       O
ATOM   2956  CB  LEU A 390     -29.476 -46.816 -12.718  1.00 21.96           C
ANISOU 2956  CB  LEU A 390     2805   3338   2200    314     65    212       C
ATOM   2957  CG  LEU A 390     -30.683 -47.266 -13.536  1.00 21.55           C
ANISOU 2957  CG  LEU A 390     2746   3222   2221    272    120    267       C
ATOM   2958  CD1 LEU A 390     -30.285 -47.346 -15.005  1.00 20.77           C
ANISOU 2958  CD1 LEU A 390     2630   3048   2214    213     98    248       C
ATOM   2959  CD2 LEU A 390     -31.210 -48.615 -13.064  1.00 20.77           C
ANISOU 2959  CD2 LEU A 390     2657   3126   2109    296    170    371       C
ATOM   2960  N   LEU A 391     -27.682 -45.248 -10.579  1.00 23.43           N
ANISOU 2960  N   LEU A 391     3003   3685   2213    410    -50     57       N
ATOM   2961  CA  LEU A 391     -26.298 -45.077 -10.153  1.00 24.07           C
ANISOU 2961  CA  LEU A 391     3072   3817   2258    432   -123      0       C
ATOM   2962  C   LEU A 391     -26.122 -45.364  -8.668  1.00 25.03           C
ANISOU 2962  C   LEU A 391     3215   4042   2253    520   -137     11       C
ATOM   2963  O   LEU A 391     -26.928 -44.914  -7.845  1.00 25.39           O
ANISOU 2963  O   LEU A 391     3287   4129   2229    560   -111      0       O
ATOM   2964  CB  LEU A 391     -25.819 -43.658 -10.464  1.00 24.13           C
ANISOU 2964  CB  LEU A 391     3060   3805   2302    390   -173   -117       C
ATOM   2965  CG  LEU A 391     -25.806 -43.287 -11.948  1.00 23.90           C
ANISOU 2965  CG  LEU A 391     3009   3680   2392    309   -164   -130       C
ATOM   2966  CD1 LEU A 391     -25.429 -41.826 -12.116  1.00 24.70           C
ANISOU 2966  CD1 LEU A 391     3098   3759   2527    273   -203   -239       C
ATOM   2967  CD2 LEU A 391     -24.856 -44.198 -12.725  1.00 24.42           C
ANISOU 2967  CD2 LEU A 391     3047   3721   2509    288   -180    -89       C
ATOM   2968  N   PRO A 392     -25.067 -46.120  -8.318  1.00 25.43           N
ANISOU 2968  N   PRO A 392     3256   4138   2267    557   -176     33       N
ATOM   2969  CA  PRO A 392     -24.782 -46.443  -6.927  1.00 26.67           C
ANISOU 2969  CA  PRO A 392     3435   4403   2296    651   -196     47       C
ATOM   2970  C   PRO A 392     -24.120 -45.271  -6.207  1.00 27.67           C
ANISOU 2970  C   PRO A 392     3553   4597   2362    672   -274    -80       C
ATOM   2971  O   PRO A 392     -23.787 -44.267  -6.842  1.00 27.01           O
ANISOU 2971  O   PRO A 392     3444   4468   2350    607   -312   -172       O
ATOM   2972  CB  PRO A 392     -23.803 -47.609  -7.050  1.00 26.80           C
ANISOU 2972  CB  PRO A 392     3436   4430   2316    675   -217    110       C
ATOM   2973  CG  PRO A 392     -23.036 -47.301  -8.290  1.00 26.00           C
ANISOU 2973  CG  PRO A 392     3293   4260   2328    596   -253     60       C
ATOM   2974  CD  PRO A 392     -24.011 -46.626  -9.218  1.00 25.06           C
ANISOU 2974  CD  PRO A 392     3175   4052   2295    520   -209     40       C
ATOM   2975  N   ASP A 393     -23.934 -45.407  -4.896  1.00 29.14           N
ANISOU 2975  N   ASP A 393     3762   4891   2418    763   -298    -83       N
ATOM   2976  CA  ASP A 393     -23.201 -44.418  -4.096  1.00 30.56           C
ANISOU 2976  CA  ASP A 393     3935   5149   2529    793   -385   -209       C
ATOM   2977  C   ASP A 393     -21.709 -44.455  -4.424  1.00 30.38           C
ANISOU 2977  C   ASP A 393     3858   5138   2546    769   -471   -262       C
ATOM   2978  O   ASP A 393     -21.050 -43.415  -4.450  1.00 30.59           O
ANISOU 2978  O   ASP A 393     3855   5169   2598    733   -542   -384       O
ATOM   2979  CB  ASP A 393     -23.389 -44.677  -2.598  1.00 32.13           C
ANISOU 2979  CB  ASP A 393     4173   5470   2564    910   -388   -191       C
ATOM   2980  CG  ASP A 393     -24.794 -44.364  -2.112  1.00 33.76           C
ANISOU 2980  CG  ASP A 393     4426   5682   2718    940   -311   -166       C
ATOM   2981  OD1 ASP A 393     -25.151 -44.853  -1.016  1.00 37.94           O
ANISOU 2981  OD1 ASP A 393     4994   6302   3120   1038   -282   -109       O
ATOM   2982  OD2 ASP A 393     -25.525 -43.625  -2.806  1.00 35.23           O
ANISOU 2982  OD2 ASP A 393     4611   5787   2986    873   -278   -200       O
ATOM   2983  N   THR A 394     -21.188 -45.663  -4.642  1.00 30.26           N
ANISOU 2983  N   THR A 394     3830   5129   2538    791   -462   -168       N
ATOM   2984  CA  THR A 394     -19.802 -45.880  -5.064  1.00 30.13           C
ANISOU 2984  CA  THR A 394     3758   5122   2569    773   -531   -197       C
ATOM   2985  C   THR A 394     -19.760 -46.948  -6.146  1.00 29.38           C
ANISOU 2985  C   THR A 394     3652   4945   2565    738   -479    -93       C
ATOM   2986  O   THR A 394     -20.693 -47.746  -6.274  1.00 28.97           O
ANISOU 2986  O   THR A 394     3640   4853   2513    750   -399     11       O
ATOM   2987  CB  THR A 394     -18.903 -46.346  -3.896  1.00 31.61           C
ANISOU 2987  CB  THR A 394     3938   5438   2632    874   -599   -200       C
ATOM   2988  OG1 THR A 394     -19.379 -47.601  -3.383  1.00 32.15           O
ANISOU 2988  OG1 THR A 394     4051   5537   2626    955   -538    -66       O
ATOM   2989  CG2 THR A 394     -18.876 -45.309  -2.780  1.00 31.99           C
ANISOU 2989  CG2 THR A 394     3998   5577   2579    916   -661   -315       C
ATOM   2990  N   PHE A 395     -18.680 -46.955  -6.924  1.00 28.92           N
ANISOU 2990  N   PHE A 395     3538   4862   2586    694   -523   -123       N
ATOM   2991  CA  PHE A 395     -18.488 -47.942  -7.987  1.00 28.31           C
ANISOU 2991  CA  PHE A 395     3450   4712   2595    666   -482    -38       C
ATOM   2992  C   PHE A 395     -17.491 -48.993  -7.522  1.00 29.35           C
ANISOU 2992  C   PHE A 395     3565   4912   2673    744   -516     15       C
ATOM   2993  O   PHE A 395     -16.314 -48.702  -7.304  1.00 29.51           O
ANISOU 2993  O   PHE A 395     3532   4995   2683    757   -594    -49       O
ATOM   2994  CB  PHE A 395     -18.037 -47.254  -9.273  1.00 27.33           C
ANISOU 2994  CB  PHE A 395     3278   4508   2597    569   -494    -98       C
ATOM   2995  CG  PHE A 395     -19.027 -46.251  -9.783  1.00 26.45           C
ANISOU 2995  CG  PHE A 395     3186   4324   2539    499   -458   -141       C
ATOM   2996  CD1 PHE A 395     -18.981 -44.929  -9.354  1.00 26.43           C
ANISOU 2996  CD1 PHE A 395     3173   4345   2525    476   -502   -251       C
ATOM   2997  CD2 PHE A 395     -20.031 -46.633 -10.664  1.00 24.54           C
ANISOU 2997  CD2 PHE A 395     2973   3993   2358    461   -381    -74       C
ATOM   2998  CE1 PHE A 395     -19.903 -44.004  -9.814  1.00 25.80           C
ANISOU 2998  CE1 PHE A 395     3113   4195   2493    420   -465   -287       C
ATOM   2999  CE2 PHE A 395     -20.952 -45.718 -11.124  1.00 24.74           C
ANISOU 2999  CE2 PHE A 395     3013   3958   2427    405   -349   -110       C
ATOM   3000  CZ  PHE A 395     -20.887 -44.396 -10.696  1.00 25.02           C
ANISOU 3000  CZ  PHE A 395     3041   4014   2450    387   -389   -214       C
ATOM   3001  N   ASN A 396     -17.985 -50.217  -7.356  1.00 29.93           N
ANISOU 3001  N   ASN A 396     3683   4972   2717    796   -456    134       N
ATOM   3002  CA  ASN A 396     -17.255 -51.259  -6.643  1.00 31.16           C
ANISOU 3002  CA  ASN A 396     3841   5202   2797    894   -478    201       C
ATOM   3003  C   ASN A 396     -16.582 -52.232  -7.599  1.00 31.10           C
ANISOU 3003  C   ASN A 396     3811   5135   2872    884   -465    261       C
ATOM   3004  O   ASN A 396     -17.237 -53.099  -8.169  1.00 30.91           O
ANISOU 3004  O   ASN A 396     3824   5025   2896    872   -392    350       O
ATOM   3005  CB  ASN A 396     -18.205 -52.012  -5.709  1.00 31.85           C
ANISOU 3005  CB  ASN A 396     3996   5315   2791    970   -416    303       C
ATOM   3006  CG  ASN A 396     -18.927 -51.092  -4.743  1.00 33.56           C
ANISOU 3006  CG  ASN A 396     4239   5595   2917    990   -421    249       C
ATOM   3007  OD1 ASN A 396     -18.512 -49.952  -4.516  1.00 35.07           O
ANISOU 3007  OD1 ASN A 396     4400   5833   3092    969   -489    128       O
ATOM   3008  ND2 ASN A 396     -20.015 -51.585  -4.163  1.00 35.17           N
ANISOU 3008  ND2 ASN A 396     4499   5799   3064   1033   -345    338       N
ATOM   3009  N   ILE A 397     -15.274 -52.078  -7.777  1.00 31.74           N
ANISOU 3009  N   ILE A 397     3828   5261   2970    890   -536    207       N
ATOM   3010  CA  ILE A 397     -14.521 -52.911  -8.710  1.00 31.75           C
ANISOU 3010  CA  ILE A 397     3802   5214   3048    886   -528    252       C
ATOM   3011  C   ILE A 397     -13.462 -53.677  -7.944  1.00 33.40           C
ANISOU 3011  C   ILE A 397     3990   5519   3181    992   -577    288       C
ATOM   3012  O   ILE A 397     -12.619 -53.076  -7.267  1.00 33.52           O
ANISOU 3012  O   ILE A 397     3955   5639   3141   1021   -660    212       O
ATOM   3013  CB  ILE A 397     -13.874 -52.075  -9.830  1.00 31.21           C
ANISOU 3013  CB  ILE A 397     3667   5103   3088    795   -556    165       C
ATOM   3014  CG1 ILE A 397     -14.950 -51.280 -10.574  1.00 30.59           C
ANISOU 3014  CG1 ILE A 397     3613   4932   3078    699   -508    133       C
ATOM   3015  CG2 ILE A 397     -13.122 -52.981 -10.803  1.00 30.44           C
ANISOU 3015  CG2 ILE A 397     3544   4960   3063    800   -540    215       C
ATOM   3016  CD1 ILE A 397     -14.411 -50.299 -11.586  1.00 31.21           C
ANISOU 3016  CD1 ILE A 397     3632   4972   3255    610   -530     49       C
ATOM   3017  N   GLU A 398     -13.518 -55.005  -8.048  1.00 34.23           N
ANISOU 3017  N   GLU A 398     4132   5587   3285   1050   -528    401       N
ATOM   3018  CA  GLU A 398     -12.633 -55.882  -7.294  1.00 36.34           C
ANISOU 3018  CA  GLU A 398     4392   5939   3475   1165   -563    457       C
ATOM   3019  C   GLU A 398     -12.793 -55.543  -5.799  1.00 37.70           C
ANISOU 3019  C   GLU A 398     4585   6234   3506   1242   -603    445       C
ATOM   3020  O   GLU A 398     -13.903 -55.642  -5.272  1.00 38.09           O
ANISOU 3020  O   GLU A 398     4700   6267   3505   1255   -546    494       O
ATOM   3021  CB  GLU A 398     -11.196 -55.755  -7.834  1.00 36.68           C
ANISOU 3021  CB  GLU A 398     4349   6021   3568   1163   -631    400       C
ATOM   3022  CG  GLU A 398     -10.285 -56.944  -7.553  1.00 39.27           C
ANISOU 3022  CG  GLU A 398     4668   6394   3859   1274   -645    480       C
ATOM   3023  CD  GLU A 398      -8.989 -56.908  -8.362  1.00 40.86           C
ANISOU 3023  CD  GLU A 398     4781   6608   4135   1260   -691    435       C
ATOM   3024  OE1 GLU A 398      -7.986 -57.486  -7.897  1.00 44.14           O
ANISOU 3024  OE1 GLU A 398     5160   7107   4502   1355   -737    461       O
ATOM   3025  OE2 GLU A 398      -8.966 -56.301  -9.458  1.00 41.88           O
ANISOU 3025  OE2 GLU A 398     4875   6667   4369   1159   -678    377       O
ATOM   3026  N   ASP A 399     -11.725 -55.110  -5.134  1.00 39.14           N
ANISOU 3026  N   ASP A 399     4709   6540   3623   1293   -698    375       N
ATOM   3027  CA  ASP A 399     -11.774 -54.758  -3.713  1.00 40.75           C
ANISOU 3027  CA  ASP A 399     4929   6872   3681   1375   -748    350       C
ATOM   3028  C   ASP A 399     -11.816 -53.241  -3.467  1.00 40.58           C
ANISOU 3028  C   ASP A 399     4873   6896   3652   1309   -812    202       C
ATOM   3029  O   ASP A 399     -11.685 -52.791  -2.322  1.00 41.59           O
ANISOU 3029  O   ASP A 399     5002   7140   3659   1373   -873    151       O
ATOM   3030  CB  ASP A 399     -10.577 -55.379  -2.979  1.00 42.40           C
ANISOU 3030  CB  ASP A 399     5103   7204   3805   1496   -820    373       C
ATOM   3031  CG  ASP A 399      -9.235 -55.037  -3.625  1.00 43.78           C
ANISOU 3031  CG  ASP A 399     5173   7405   4056   1460   -899    290       C
ATOM   3032  OD1 ASP A 399      -8.191 -55.298  -2.990  1.00 47.45           O
ANISOU 3032  OD1 ASP A 399     5590   7987   4452   1551   -976    281       O
ATOM   3033  OD2 ASP A 399      -9.222 -54.518  -4.767  1.00 45.65           O
ANISOU 3033  OD2 ASP A 399     5374   7550   4422   1346   -882    238       O
ATOM   3034  N   GLN A 400     -12.002 -52.463  -4.532  1.00 39.14           N
ANISOU 3034  N   GLN A 400     4661   6619   3593   1185   -798    134       N
ATOM   3035  CA  GLN A 400     -12.042 -51.002  -4.440  1.00 38.99           C
ANISOU 3035  CA  GLN A 400     4609   6618   3589   1111   -851     -5       C
ATOM   3036  C   GLN A 400     -13.471 -50.481  -4.520  1.00 37.86           C
ANISOU 3036  C   GLN A 400     4531   6399   3453   1058   -780     -4       C
ATOM   3037  O   GLN A 400     -14.325 -51.094  -5.156  1.00 36.86           O
ANISOU 3037  O   GLN A 400     4452   6175   3379   1032   -688     87       O
ATOM   3038  CB  GLN A 400     -11.212 -50.377  -5.566  1.00 38.64           C
ANISOU 3038  CB  GLN A 400     4480   6521   3679   1011   -884    -83       C
ATOM   3039  CG  GLN A 400      -9.738 -50.742  -5.526  1.00 40.49           C
ANISOU 3039  CG  GLN A 400     4632   6836   3917   1055   -960    -98       C
ATOM   3040  CD  GLN A 400      -9.058 -50.310  -4.240  1.00 43.02           C
ANISOU 3040  CD  GLN A 400     4917   7306   4123   1127  -1067   -178       C
ATOM   3041  OE1 GLN A 400      -9.413 -49.292  -3.644  1.00 44.34           O
ANISOU 3041  OE1 GLN A 400     5093   7505   4248   1103  -1106   -274       O
ATOM   3042  NE2 GLN A 400      -8.077 -51.086  -3.804  1.00 44.57           N
ANISOU 3042  NE2 GLN A 400     5074   7596   4265   1221  -1118   -142       N
ATOM   3043  N   GLU A 401     -13.715 -49.349  -3.863  1.00 37.75           N
ANISOU 3043  N   GLU A 401     4519   6435   3389   1045   -824   -109       N
ATOM   3044  CA  GLU A 401     -15.005 -48.666  -3.906  1.00 37.18           C
ANISOU 3044  CA  GLU A 401     4500   6301   3324    995   -766   -126       C
ATOM   3045  C   GLU A 401     -14.754 -47.216  -4.286  1.00 36.55           C
ANISOU 3045  C   GLU A 401     4375   6195   3316    901   -819   -271       C
ATOM   3046  O   GLU A 401     -14.403 -46.391  -3.435  1.00 37.91           O
ANISOU 3046  O   GLU A 401     4532   6450   3422    924   -897   -377       O
ATOM   3047  CB  GLU A 401     -15.716 -48.743  -2.553  1.00 38.10           C
ANISOU 3047  CB  GLU A 401     4681   6506   3288   1092   -755   -103       C
ATOM   3048  CG  GLU A 401     -16.092 -50.154  -2.140  1.00 39.43           C
ANISOU 3048  CG  GLU A 401     4902   6691   3389   1184   -688     52       C
ATOM   3049  CD  GLU A 401     -16.785 -50.216  -0.792  1.00 42.68           C
ANISOU 3049  CD  GLU A 401     5377   7197   3644   1286   -670     83       C
ATOM   3050  OE1 GLU A 401     -16.831 -51.318  -0.207  1.00 44.84           O
ANISOU 3050  OE1 GLU A 401     5686   7513   3838   1382   -634    202       O
ATOM   3051  OE2 GLU A 401     -17.278 -49.171  -0.310  1.00 43.96           O
ANISOU 3051  OE2 GLU A 401     5553   7388   3760   1275   -688     -9       O
ATOM   3052  N   TYR A 402     -14.921 -46.920  -5.569  1.00 34.49           N
ANISOU 3052  N   TYR A 402     4094   5818   3193    799   -778   -274       N
ATOM   3053  CA  TYR A 402     -14.608 -45.604  -6.111  1.00 33.84           C
ANISOU 3053  CA  TYR A 402     3965   5692   3201    702   -818   -395       C
ATOM   3054  C   TYR A 402     -15.760 -44.625  -5.944  1.00 33.16           C
ANISOU 3054  C   TYR A 402     3929   5561   3108    668   -785   -445       C
ATOM   3055  O   TYR A 402     -16.906 -44.945  -6.260  1.00 32.35           O
ANISOU 3055  O   TYR A 402     3882   5396   3013    661   -699   -370       O
ATOM   3056  CB  TYR A 402     -14.254 -45.722  -7.594  1.00 32.64           C
ANISOU 3056  CB  TYR A 402     3771   5437   3193    617   -783   -368       C
ATOM   3057  CG  TYR A 402     -13.014 -46.550  -7.850  1.00 32.89           C
ANISOU 3057  CG  TYR A 402     3742   5509   3245    646   -818   -333       C
ATOM   3058  CD1 TYR A 402     -11.744 -46.022  -7.633  1.00 34.04           C
ANISOU 3058  CD1 TYR A 402     3805   5722   3407    636   -910   -423       C
ATOM   3059  CD2 TYR A 402     -13.110 -47.861  -8.308  1.00 32.78           C
ANISOU 3059  CD2 TYR A 402     3752   5465   3237    685   -760   -211       C
ATOM   3060  CE1 TYR A 402     -10.604 -46.775  -7.867  1.00 34.34           C
ANISOU 3060  CE1 TYR A 402     3780   5803   3463    668   -941   -389       C
ATOM   3061  CE2 TYR A 402     -11.977 -48.622  -8.547  1.00 33.10           C
ANISOU 3061  CE2 TYR A 402     3740   5542   3296    720   -790   -179       C
ATOM   3062  CZ  TYR A 402     -10.726 -48.075  -8.324  1.00 33.97           C
ANISOU 3062  CZ  TYR A 402     3764   5727   3418    714   -879   -266       C
ATOM   3063  OH  TYR A 402      -9.601 -48.827  -8.559  1.00 34.37           O
ANISOU 3063  OH  TYR A 402     3755   5819   3487    754   -907   -231       O
ATOM   3064  N   SER A 403     -15.444 -43.423  -5.468  1.00 33.55           N
ANISOU 3064  N   SER A 403     3956   5642   3149    644   -854   -577       N
ATOM   3065  CA  SER A 403     -16.411 -42.329  -5.438  1.00 33.41           C
ANISOU 3065  CA  SER A 403     3979   5569   3145    602   -828   -642       C
ATOM   3066  C   SER A 403     -16.652 -41.823  -6.855  1.00 32.34           C
ANISOU 3066  C   SER A 403     3825   5301   3160    493   -778   -640       C
ATOM   3067  O   SER A 403     -15.885 -42.132  -7.767  1.00 31.42           O
ANISOU 3067  O   SER A 403     3656   5147   3135    446   -780   -615       O
ATOM   3068  CB  SER A 403     -15.888 -41.179  -4.577  1.00 34.63           C
ANISOU 3068  CB  SER A 403     4113   5787   3260    604   -924   -793       C
ATOM   3069  OG  SER A 403     -14.755 -40.575  -5.183  1.00 34.74           O
ANISOU 3069  OG  SER A 403     4045   5771   3383    525   -986   -874       O
ATOM   3070  N   PHE A 404     -17.712 -41.040  -7.034  1.00 32.11           N
ANISOU 3070  N   PHE A 404     3841   5207   3154    459   -731   -664       N
ATOM   3071  CA  PHE A 404     -17.967 -40.374  -8.315  1.00 31.58           C
ANISOU 3071  CA  PHE A 404     3760   5017   3221    361   -689   -674       C
ATOM   3072  C   PHE A 404     -16.772 -39.529  -8.754  1.00 32.34           C
ANISOU 3072  C   PHE A 404     3784   5091   3413    288   -754   -769       C
ATOM   3073  O   PHE A 404     -16.383 -39.561  -9.920  1.00 31.63           O
ANISOU 3073  O   PHE A 404     3655   4929   3432    223   -729   -739       O
ATOM   3074  CB  PHE A 404     -19.209 -39.485  -8.235  1.00 31.46           C
ANISOU 3074  CB  PHE A 404     3800   4949   3203    347   -644   -706       C
ATOM   3075  CG  PHE A 404     -20.494 -40.223  -8.435  1.00 30.98           C
ANISOU 3075  CG  PHE A 404     3793   4863   3114    377   -554   -595       C
ATOM   3076  CD1 PHE A 404     -21.084 -40.902  -7.381  1.00 32.17           C
ANISOU 3076  CD1 PHE A 404     3987   5093   3141    465   -535   -545       C
ATOM   3077  CD2 PHE A 404     -21.119 -40.235  -9.675  1.00 30.31           C
ANISOU 3077  CD2 PHE A 404     3713   4677   3127    317   -487   -540       C
ATOM   3078  CE1 PHE A 404     -22.277 -41.585  -7.556  1.00 31.91           C
ANISOU 3078  CE1 PHE A 404     3997   5034   3094    486   -449   -441       C
ATOM   3079  CE2 PHE A 404     -22.320 -40.917  -9.862  1.00 30.07           C
ANISOU 3079  CE2 PHE A 404     3723   4623   3077    338   -409   -444       C
ATOM   3080  CZ  PHE A 404     -22.898 -41.594  -8.796  1.00 30.44           C
ANISOU 3080  CZ  PHE A 404     3809   4746   3012    419   -389   -394       C
ATOM   3081  N   LYS A 405     -16.202 -38.782  -7.812  1.00 33.82           N
ANISOU 3081  N   LYS A 405     3952   5340   3557    302   -838   -885       N
ATOM   3082  CA  LYS A 405     -15.028 -37.948  -8.074  1.00 34.95           C
ANISOU 3082  CA  LYS A 405     4018   5469   3792    231   -909   -986       C
ATOM   3083  C   LYS A 405     -13.854 -38.768  -8.627  1.00 34.62           C
ANISOU 3083  C   LYS A 405     3901   5455   3799    221   -929   -935       C
ATOM   3084  O   LYS A 405     -13.169 -38.326  -9.550  1.00 34.77           O
ANISOU 3084  O   LYS A 405     3858   5412   3940    140   -930   -954       O
ATOM   3085  CB  LYS A 405     -14.606 -37.211  -6.798  1.00 36.58           C
ANISOU 3085  CB  LYS A 405     4217   5757   3925    263  -1006  -1119       C
ATOM   3086  CG  LYS A 405     -13.586 -36.097  -7.008  1.00 39.02           C
ANISOU 3086  CG  LYS A 405     4451   6032   4342    176  -1079  -1245       C
ATOM   3087  CD  LYS A 405     -13.110 -35.533  -5.677  1.00 41.98           C
ANISOU 3087  CD  LYS A 405     4816   6502   4632    217  -1188  -1381       C
ATOM   3088  CE  LYS A 405     -11.919 -34.597  -5.851  1.00 43.83           C
ANISOU 3088  CE  LYS A 405     4959   6714   4982    128  -1271  -1504       C
ATOM   3089  NZ  LYS A 405     -11.229 -34.321  -4.561  1.00 45.94           N
ANISOU 3089  NZ  LYS A 405     5197   7098   5159    176  -1394  -1631       N
ATOM   3090  N   GLN A 406     -13.634 -39.955  -8.067  1.00 34.38           N
ANISOU 3090  N   GLN A 406     3875   5516   3671    307   -941   -865       N
ATOM   3091  CA  GLN A 406     -12.541 -40.832  -8.504  1.00 34.32           C
ANISOU 3091  CA  GLN A 406     3800   5544   3696    314   -960   -812       C
ATOM   3092  C   GLN A 406     -12.842 -41.565  -9.813  1.00 32.97           C
ANISOU 3092  C   GLN A 406     3639   5286   3603    284   -869   -696       C
ATOM   3093  O   GLN A 406     -11.926 -41.937 -10.548  1.00 32.85           O
ANISOU 3093  O   GLN A 406     3559   5263   3658    259   -873   -670       O
ATOM   3094  CB  GLN A 406     -12.213 -41.855  -7.413  1.00 34.92           C
ANISOU 3094  CB  GLN A 406     3884   5747   3638    428  -1003   -774       C
ATOM   3095  CG  GLN A 406     -11.651 -41.234  -6.141  1.00 36.69           C
ANISOU 3095  CG  GLN A 406     4083   6078   3778    467  -1110   -894       C
ATOM   3096  CD  GLN A 406     -11.570 -42.214  -4.983  1.00 37.54           C
ANISOU 3096  CD  GLN A 406     4219   6314   3729    594  -1143   -847       C
ATOM   3097  OE1 GLN A 406     -12.385 -43.132  -4.864  1.00 36.19           O
ANISOU 3097  OE1 GLN A 406     4117   6142   3491    657  -1071   -734       O
ATOM   3098  NE2 GLN A 406     -10.585 -42.013  -4.114  1.00 40.03           N
ANISOU 3098  NE2 GLN A 406     4479   6742   3987    635  -1251   -934       N
ATOM   3099  N   PHE A 407     -14.123 -41.776 -10.096  1.00 32.05           N
ANISOU 3099  N   PHE A 407     3599   5108   3471    290   -789   -631       N
ATOM   3100  CA  PHE A 407     -14.539 -42.575 -11.244  1.00 30.98           C
ANISOU 3100  CA  PHE A 407     3482   4897   3392    272   -707   -524       C
ATOM   3101  C   PHE A 407     -14.561 -41.743 -12.524  1.00 30.79           C
ANISOU 3101  C   PHE A 407     3434   4766   3497    175   -671   -545       C
ATOM   3102  O   PHE A 407     -14.212 -42.242 -13.591  1.00 30.41           O
ANISOU 3102  O   PHE A 407     3362   4675   3519    150   -634   -487       O
ATOM   3103  CB  PHE A 407     -15.926 -43.168 -10.974  1.00 30.53           C
ANISOU 3103  CB  PHE A 407     3510   4823   3267    318   -640   -447       C
ATOM   3104  CG  PHE A 407     -16.221 -44.433 -11.734  1.00 28.91           C
ANISOU 3104  CG  PHE A 407     3326   4578   3082    334   -576   -328       C
ATOM   3105  CD1 PHE A 407     -15.469 -45.582 -11.517  1.00 29.47           C
ANISOU 3105  CD1 PHE A 407     3378   4704   3117    394   -593   -269       C
ATOM   3106  CD2 PHE A 407     -17.283 -44.490 -12.624  1.00 28.60           C
ANISOU 3106  CD2 PHE A 407     3328   4447   3093    296   -500   -278       C
ATOM   3107  CE1 PHE A 407     -15.757 -46.758 -12.201  1.00 29.27           C
ANISOU 3107  CE1 PHE A 407     3377   4631   3112    411   -534   -166       C
ATOM   3108  CE2 PHE A 407     -17.572 -45.662 -13.308  1.00 27.73           C
ANISOU 3108  CE2 PHE A 407     3238   4297   3002    310   -447   -179       C
ATOM   3109  CZ  PHE A 407     -16.811 -46.794 -13.091  1.00 27.87           C
ANISOU 3109  CZ  PHE A 407     3241   4360   2989    366   -463   -125       C
ATOM   3110  N   LEU A 408     -14.977 -40.481 -12.415  1.00 31.26           N
ANISOU 3110  N   LEU A 408     3506   4785   3586    127   -678   -626       N
ATOM   3111  CA  LEU A 408     -15.186 -39.619 -13.589  1.00 31.28           C
ANISOU 3111  CA  LEU A 408     3500   4680   3705     42   -634   -639       C
ATOM   3112  C   LEU A 408     -13.895 -39.302 -14.350  1.00 31.37           C
ANISOU 3112  C   LEU A 408     3425   4673   3819    -18   -657   -664       C
ATOM   3113  O   LEU A 408     -12.885 -38.923 -13.753  1.00 32.20           O
ANISOU 3113  O   LEU A 408     3470   4834   3931    -27   -730   -739       O
ATOM   3114  CB  LEU A 408     -15.906 -38.317 -13.190  1.00 31.77           C
ANISOU 3114  CB  LEU A 408     3599   4702   3772     13   -638   -722       C
ATOM   3115  CG  LEU A 408     -17.444 -38.350 -13.245  1.00 32.66           C
ANISOU 3115  CG  LEU A 408     3792   4771   3845     36   -571   -675       C
ATOM   3116  CD1 LEU A 408     -18.026 -39.684 -12.779  1.00 33.87           C
ANISOU 3116  CD1 LEU A 408     3986   4982   3901    113   -544   -584       C
ATOM   3117  CD2 LEU A 408     -18.037 -37.201 -12.432  1.00 34.93           C
ANISOU 3117  CD2 LEU A 408     4116   5053   4103     38   -592   -768       C
ATOM   3118  N   TYR A 409     -13.953 -39.462 -15.672  1.00 30.52           N
ANISOU 3118  N   TYR A 409     3312   4492   3793    -58   -593   -601       N
ATOM   3119  CA  TYR A 409     -12.820 -39.220 -16.575  1.00 30.69           C
ANISOU 3119  CA  TYR A 409     3255   4490   3917   -113   -594   -604       C
ATOM   3120  C   TYR A 409     -11.555 -39.966 -16.157  1.00 31.18           C
ANISOU 3120  C   TYR A 409     3244   4644   3958    -78   -650   -605       C
ATOM   3121  O   TYR A 409     -10.450 -39.433 -16.264  1.00 31.96           O
ANISOU 3121  O   TYR A 409     3259   4758   4127   -122   -689   -656       O
ATOM   3122  CB  TYR A 409     -12.545 -37.713 -16.712  1.00 31.50           C
ANISOU 3122  CB  TYR A 409     3324   4535   4110   -194   -610   -693       C
ATOM   3123  CG  TYR A 409     -13.630 -36.979 -17.457  1.00 31.69           C
ANISOU 3123  CG  TYR A 409     3408   4455   4178   -232   -542   -677       C
ATOM   3124  CD1 TYR A 409     -13.799 -37.156 -18.828  1.00 31.95           C
ANISOU 3124  CD1 TYR A 409     3445   4420   4273   -256   -469   -600       C
ATOM   3125  CD2 TYR A 409     -14.498 -36.117 -16.793  1.00 33.58           C
ANISOU 3125  CD2 TYR A 409     3701   4668   4390   -234   -552   -738       C
ATOM   3126  CE1 TYR A 409     -14.805 -36.488 -19.523  1.00 31.94           C
ANISOU 3126  CE1 TYR A 409     3499   4331   4307   -283   -410   -582       C
ATOM   3127  CE2 TYR A 409     -15.505 -35.446 -17.476  1.00 33.59           C
ANISOU 3127  CE2 TYR A 409     3755   4576   4430   -261   -490   -720       C
ATOM   3128  CZ  TYR A 409     -15.653 -35.636 -18.838  1.00 33.22           C
ANISOU 3128  CZ  TYR A 409     3709   4467   4444   -285   -420   -641       C
ATOM   3129  OH  TYR A 409     -16.652 -34.973 -19.517  1.00 35.13           O
ANISOU 3129  OH  TYR A 409     4003   4624   4719   -304   -363   -621       O
ATOM   3130  N   ASN A 410     -11.719 -41.203 -15.694  1.00 30.59           N
ANISOU 3130  N   ASN A 410     3200   4631   3793      3   -653   -543       N
ATOM   3131  CA  ASN A 410     -10.602 -41.958 -15.141  1.00 31.42           C
ANISOU 3131  CA  ASN A 410     3245   4833   3861     54   -710   -541       C
ATOM   3132  C   ASN A 410     -10.471 -43.340 -15.767  1.00 30.28           C
ANISOU 3132  C   ASN A 410     3110   4691   3702    106   -666   -435       C
ATOM   3133  O   ASN A 410     -10.799 -44.361 -15.148  1.00 30.08           O
ANISOU 3133  O   ASN A 410     3130   4712   3589    184   -667   -383       O
ATOM   3134  CB  ASN A 410     -10.742 -42.055 -13.621  1.00 32.46           C
ANISOU 3134  CB  ASN A 410     3399   5056   3877    119   -778   -586       C
ATOM   3135  CG  ASN A 410      -9.443 -42.418 -12.935  1.00 35.32           C
ANISOU 3135  CG  ASN A 410     3683   5528   4211    160   -860   -617       C
ATOM   3136  OD1 ASN A 410      -8.460 -42.785 -13.587  1.00 35.26           O
ANISOU 3136  OD1 ASN A 410     3603   5530   4265    150   -860   -592       O
ATOM   3137  ND2 ASN A 410      -9.437 -42.310 -11.595  1.00 40.22           N
ANISOU 3137  ND2 ASN A 410     4314   6236   4732    214   -931   -674       N
ATOM   3138  N   ASN A 411      -9.965 -43.358 -16.995  1.00 29.19           N
ANISOU 3138  N   ASN A 411     2932   4505   3656     65   -624   -404       N
ATOM   3139  CA  ASN A 411      -9.730 -44.604 -17.721  1.00 28.39           C
ANISOU 3139  CA  ASN A 411     2835   4399   3553    111   -581   -315       C
ATOM   3140  C   ASN A 411      -8.611 -45.459 -17.121  1.00 28.68           C
ANISOU 3140  C   ASN A 411     2813   4533   3549    180   -634   -302       C
ATOM   3141  O   ASN A 411      -8.502 -46.640 -17.447  1.00 28.18           O
ANISOU 3141  O   ASN A 411     2769   4475   3463    239   -606   -227       O
ATOM   3142  CB  ASN A 411      -9.436 -44.318 -19.200  1.00 27.97           C
ANISOU 3142  CB  ASN A 411     2751   4274   3601     55   -522   -290       C
ATOM   3143  CG  ASN A 411     -10.639 -43.767 -19.943  1.00 27.80           C
ANISOU 3143  CG  ASN A 411     2799   4156   3608      9   -460   -278       C
ATOM   3144  OD1 ASN A 411     -11.787 -44.069 -19.607  1.00 27.58           O
ANISOU 3144  OD1 ASN A 411     2850   4107   3522     33   -442   -255       O
ATOM   3145  ND2 ASN A 411     -10.381 -42.967 -20.979  1.00 27.35           N
ANISOU 3145  ND2 ASN A 411     2708   4042   3640    -56   -423   -286       N
ATOM   3146  N   SER A 412      -7.786 -44.880 -16.246  1.00 29.38           N
ANISOU 3146  N   SER A 412     2833   4700   3629    176   -714   -379       N
ATOM   3147  CA  SER A 412      -6.753 -45.653 -15.558  1.00 30.08           C
ANISOU 3147  CA  SER A 412     2865   4895   3670    250   -774   -371       C
ATOM   3148  C   SER A 412      -7.365 -46.796 -14.737  1.00 29.60           C
ANISOU 3148  C   SER A 412     2883   4873   3491    350   -774   -308       C
ATOM   3149  O   SER A 412      -6.741 -47.842 -14.582  1.00 29.38           O
ANISOU 3149  O   SER A 412     2836   4899   3427    426   -785   -255       O
ATOM   3150  CB  SER A 412      -5.857 -44.760 -14.683  1.00 31.57           C
ANISOU 3150  CB  SER A 412     2966   5165   3865    226   -870   -476       C
ATOM   3151  OG  SER A 412      -6.538 -44.311 -13.525  1.00 33.09           O
ANISOU 3151  OG  SER A 412     3211   5388   3974    242   -915   -532       O
ATOM   3152  N   ILE A 413      -8.589 -46.596 -14.240  1.00 28.82           N
ANISOU 3152  N   ILE A 413     2871   4743   3335    351   -755   -308       N
ATOM   3153  CA  ILE A 413      -9.324 -47.636 -13.508  1.00 28.57           C
ANISOU 3153  CA  ILE A 413     2921   4735   3199    437   -738   -238       C
ATOM   3154  C   ILE A 413      -9.570 -48.851 -14.406  1.00 27.93           C
ANISOU 3154  C   ILE A 413     2880   4593   3140    467   -666   -133       C
ATOM   3155  O   ILE A 413      -9.374 -49.993 -13.985  1.00 27.84           O
ANISOU 3155  O   ILE A 413     2888   4620   3070    552   -667    -67       O
ATOM   3156  CB  ILE A 413     -10.684 -47.105 -12.960  1.00 28.07           C
ANISOU 3156  CB  ILE A 413     2940   4640   3086    422   -717   -255       C
ATOM   3157  CG1 ILE A 413     -10.451 -46.009 -11.913  1.00 29.43           C
ANISOU 3157  CG1 ILE A 413     3083   4880   3218    411   -794   -363       C
ATOM   3158  CG2 ILE A 413     -11.508 -48.236 -12.342  1.00 27.83           C
ANISOU 3158  CG2 ILE A 413     2992   4622   2962    505   -682   -165       C
ATOM   3159  CD1 ILE A 413     -11.731 -45.381 -11.363  1.00 28.52           C
ANISOU 3159  CD1 ILE A 413     3044   4738   3054    400   -773   -389       C
ATOM   3160  N   LEU A 414      -9.982 -48.596 -15.647  1.00 27.21           N
ANISOU 3160  N   LEU A 414     2801   4404   3132    400   -604   -120       N
ATOM   3161  CA  LEU A 414     -10.216 -49.667 -16.617  1.00 27.04           C
ANISOU 3161  CA  LEU A 414     2818   4318   3140    422   -539    -36       C
ATOM   3162  C   LEU A 414      -8.928 -50.433 -16.915  1.00 27.91           C
ANISOU 3162  C   LEU A 414     2865   4473   3268    472   -556     -9       C
ATOM   3163  O   LEU A 414      -8.916 -51.664 -16.895  1.00 27.40           O
ANISOU 3163  O   LEU A 414     2836   4405   3171    544   -535     64       O
ATOM   3164  CB  LEU A 414     -10.830 -49.108 -17.909  1.00 26.31           C
ANISOU 3164  CB  LEU A 414     2743   4124   3128    342   -479    -40       C
ATOM   3165  CG  LEU A 414     -11.322 -50.130 -18.941  1.00 26.26           C
ANISOU 3165  CG  LEU A 414     2790   4042   3147    358   -412     34       C
ATOM   3166  CD1 LEU A 414     -12.367 -51.056 -18.327  1.00 25.99           C
ANISOU 3166  CD1 LEU A 414     2839   3989   3048    406   -389     93       C
ATOM   3167  CD2 LEU A 414     -11.882 -49.445 -20.180  1.00 26.03           C
ANISOU 3167  CD2 LEU A 414     2774   3929   3189    284   -362     21       C
ATOM   3168  N   LEU A 415      -7.844 -49.704 -17.171  1.00 28.82           N
ANISOU 3168  N   LEU A 415     2885   4627   3438    436   -592    -65       N
ATOM   3169  CA  LEU A 415      -6.536 -50.329 -17.401  1.00 30.24           C
ANISOU 3169  CA  LEU A 415     2990   4863   3637    485   -612    -45       C
ATOM   3170  C   LEU A 415      -6.020 -51.098 -16.186  1.00 31.21           C
ANISOU 3170  C   LEU A 415     3103   5086   3671    584   -671    -26       C
ATOM   3171  O   LEU A 415      -5.422 -52.166 -16.333  1.00 31.74           O
ANISOU 3171  O   LEU A 415     3160   5176   3726    660   -663     33       O
ATOM   3172  CB  LEU A 415      -5.494 -49.283 -17.821  1.00 30.98           C
ANISOU 3172  CB  LEU A 415     2973   4986   3814    419   -641   -114       C
ATOM   3173  CG  LEU A 415      -5.333 -49.076 -19.327  1.00 32.24           C
ANISOU 3173  CG  LEU A 415     3111   5069   4069    364   -572    -94       C
ATOM   3174  CD1 LEU A 415      -4.404 -47.912 -19.607  1.00 33.94           C
ANISOU 3174  CD1 LEU A 415     3217   5308   4369    289   -597   -161       C
ATOM   3175  CD2 LEU A 415      -4.791 -50.339 -19.970  1.00 33.44           C
ANISOU 3175  CD2 LEU A 415     3261   5224   4221    439   -537    -22       C
ATOM   3176  N   GLU A 416      -6.250 -50.553 -14.993  1.00 31.56           N
ANISOU 3176  N   GLU A 416     3152   5192   3649    590   -730    -76       N
ATOM   3177  CA  GLU A 416      -5.760 -51.153 -13.748  1.00 32.62           C
ANISOU 3177  CA  GLU A 416     3275   5434   3685    688   -794    -64       C
ATOM   3178  C   GLU A 416      -6.395 -52.516 -13.469  1.00 31.82           C
ANISOU 3178  C   GLU A 416     3266   5310   3513    779   -749     41       C
ATOM   3179  O   GLU A 416      -5.697 -53.475 -13.150  1.00 31.88           O
ANISOU 3179  O   GLU A 416     3258   5374   3483    871   -767     92       O
ATOM   3180  CB  GLU A 416      -6.027 -50.203 -12.573  1.00 33.42           C
ANISOU 3180  CB  GLU A 416     3375   5600   3724    674   -861   -146       C
ATOM   3181  CG  GLU A 416      -5.591 -50.706 -11.198  1.00 36.44           C
ANISOU 3181  CG  GLU A 416     3751   6106   3989    780   -933   -142       C
ATOM   3182  CD  GLU A 416      -4.086 -50.813 -11.049  1.00 39.81           C
ANISOU 3182  CD  GLU A 416     4063   6635   4430    818  -1006   -172       C
ATOM   3183  OE1 GLU A 416      -3.352 -50.260 -11.899  1.00 42.00           O
ANISOU 3183  OE1 GLU A 416     4253   6892   4812    746  -1009   -215       O
ATOM   3184  OE2 GLU A 416      -3.636 -51.448 -10.070  1.00 43.00           O
ANISOU 3184  OE2 GLU A 416     4459   7141   4737    922  -1060   -150       O
ATOM   3185  N   HIS A 417      -7.718 -52.590 -13.584  1.00 30.38           N
ANISOU 3185  N   HIS A 417     3179   5045   3320    752   -689     74       N
ATOM   3186  CA  HIS A 417      -8.462 -53.808 -13.253  1.00 29.94           C
ANISOU 3186  CA  HIS A 417     3214   4957   3206    825   -642    172       C
ATOM   3187  C   HIS A 417      -8.650 -54.750 -14.445  1.00 29.04           C
ANISOU 3187  C   HIS A 417     3136   4741   3159    824   -569    242       C
ATOM   3188  O   HIS A 417      -8.654 -55.969 -14.271  1.00 29.32           O
ANISOU 3188  O   HIS A 417     3214   4764   3163    904   -544    324       O
ATOM   3189  CB  HIS A 417      -9.828 -53.448 -12.659  1.00 29.56           C
ANISOU 3189  CB  HIS A 417     3244   4879   3108    802   -616    174       C
ATOM   3190  CG  HIS A 417      -9.742 -52.716 -11.356  1.00 30.10           C
ANISOU 3190  CG  HIS A 417     3296   5051   3089    826   -685    113       C
ATOM   3191  ND1 HIS A 417      -9.458 -53.349 -10.165  1.00 31.55           N
ANISOU 3191  ND1 HIS A 417     3494   5330   3165    931   -722    151       N
ATOM   3192  CD2 HIS A 417      -9.905 -51.406 -11.055  1.00 30.65           C
ANISOU 3192  CD2 HIS A 417     3342   5144   3160    763   -723     15       C
ATOM   3193  CE1 HIS A 417      -9.446 -52.461  -9.187  1.00 32.29           C
ANISOU 3193  CE1 HIS A 417     3571   5507   3191    934   -784     74       C
ATOM   3194  NE2 HIS A 417      -9.719 -51.274  -9.699  1.00 31.52           N
ANISOU 3194  NE2 HIS A 417     3451   5364   3161    831   -786    -12       N
ATOM   3195  N   GLY A 418      -8.816 -54.187 -15.641  1.00 27.93           N
ANISOU 3195  N   GLY A 418     2980   4525   3106    738   -534    210       N
ATOM   3196  CA  GLY A 418      -9.067 -54.973 -16.853  1.00 27.12           C
ANISOU 3196  CA  GLY A 418     2916   4325   3066    732   -467    262       C
ATOM   3197  C   GLY A 418     -10.547 -55.241 -17.076  1.00 26.25           C
ANISOU 3197  C   GLY A 418     2899   4118   2957    700   -407    299       C
ATOM   3198  O   GLY A 418     -11.351 -55.136 -16.151  1.00 25.77           O
ANISOU 3198  O   GLY A 418     2883   4072   2838    707   -410    310       O
ATOM   3199  N   LEU A 419     -10.901 -55.599 -18.307  1.00 25.61           N
ANISOU 3199  N   LEU A 419     2847   3944   2941    668   -354    318       N
ATOM   3200  CA  LEU A 419     -12.299 -55.817 -18.680  1.00 25.23           C
ANISOU 3200  CA  LEU A 419     2877   3802   2909    628   -301    345       C
ATOM   3201  C   LEU A 419     -12.932 -56.992 -17.951  1.00 25.21           C
ANISOU 3201  C   LEU A 419     2944   3775   2860    689   -277    424       C
ATOM   3202  O   LEU A 419     -14.108 -56.935 -17.576  1.00 24.83           O
ANISOU 3202  O   LEU A 419     2946   3692   2794    663   -251    442       O
ATOM   3203  CB  LEU A 419     -12.427 -56.058 -20.187  1.00 24.98           C
ANISOU 3203  CB  LEU A 419     2858   3683   2951    593   -256    345       C
ATOM   3204  CG  LEU A 419     -12.491 -54.843 -21.101  1.00 26.18           C
ANISOU 3204  CG  LEU A 419     2974   3817   3155    510   -250    282       C
ATOM   3205  CD1 LEU A 419     -12.550 -55.321 -22.549  1.00 27.29           C
ANISOU 3205  CD1 LEU A 419     3135   3881   3352    500   -206    293       C
ATOM   3206  CD2 LEU A 419     -13.685 -53.987 -20.793  1.00 27.13           C
ANISOU 3206  CD2 LEU A 419     3126   3917   3267    448   -243    256       C
ATOM   3207  N   THR A 420     -12.161 -58.062 -17.775  1.00 25.53           N
ANISOU 3207  N   THR A 420     2985   3830   2885    772   -281    475       N
ATOM   3208  CA  THR A 420     -12.657 -59.257 -17.104  1.00 25.75           C
ANISOU 3208  CA  THR A 420     3080   3828   2877    837   -253    560       C
ATOM   3209  C   THR A 420     -13.160 -58.891 -15.704  1.00 26.08           C
ANISOU 3209  C   THR A 420     3137   3938   2836    855   -272    573       C
ATOM   3210  O   THR A 420     -14.282 -59.231 -15.342  1.00 25.73           O
ANISOU 3210  O   THR A 420     3152   3844   2778    846   -231    620       O
ATOM   3211  CB  THR A 420     -11.581 -60.365 -17.015  1.00 26.57           C
ANISOU 3211  CB  THR A 420     3175   3950   2969    936   -262    611       C
ATOM   3212  OG1 THR A 420     -11.005 -60.592 -18.311  1.00 26.45           O
ANISOU 3212  OG1 THR A 420     3140   3887   3025    925   -247    589       O
ATOM   3213  CG2 THR A 420     -12.186 -61.662 -16.492  1.00 27.31           C
ANISOU 3213  CG2 THR A 420     3349   3984   3042    997   -220    708       C
ATOM   3214  N   GLN A 421     -12.340 -58.172 -14.940  1.00 26.49           N
ANISOU 3214  N   GLN A 421     3129   4102   2832    881   -334    528       N
ATOM   3215  CA  GLN A 421     -12.724 -57.741 -13.591  1.00 27.03           C
ANISOU 3215  CA  GLN A 421     3210   4249   2810    907   -359    527       C
ATOM   3216  C   GLN A 421     -13.878 -56.733 -13.598  1.00 25.76           C
ANISOU 3216  C   GLN A 421     3069   4060   2657    822   -341    482       C
ATOM   3217  O   GLN A 421     -14.738 -56.770 -12.718  1.00 25.57           O
ANISOU 3217  O   GLN A 421     3090   4051   2574    840   -322    515       O
ATOM   3218  CB  GLN A 421     -11.526 -57.141 -12.852  1.00 28.12           C
ANISOU 3218  CB  GLN A 421     3274   4517   2892    950   -441    471       C
ATOM   3219  CG  GLN A 421     -11.799 -56.832 -11.392  1.00 30.90           C
ANISOU 3219  CG  GLN A 421     3642   4962   3134    999   -474    471       C
ATOM   3220  CD  GLN A 421     -12.212 -58.063 -10.608  1.00 33.56           C
ANISOU 3220  CD  GLN A 421     4049   5297   3406   1092   -436    584       C
ATOM   3221  OE1 GLN A 421     -13.317 -58.126 -10.066  1.00 36.36           O
ANISOU 3221  OE1 GLN A 421     4464   5629   3722   1089   -393    625       O
ATOM   3222  NE2 GLN A 421     -11.336 -59.056 -10.565  1.00 35.48           N
ANISOU 3222  NE2 GLN A 421     4283   5558   3638   1177   -445    641       N
ATOM   3223  N   PHE A 422     -13.883 -55.821 -14.568  1.00 24.80           N
ANISOU 3223  N   PHE A 422     2914   3904   2607    736   -344    410       N
ATOM   3224  CA  PHE A 422     -15.006 -54.888 -14.731  1.00 23.94           C
ANISOU 3224  CA  PHE A 422     2825   3756   2515    658   -321    370       C
ATOM   3225  C   PHE A 422     -16.314 -55.655 -14.891  1.00 23.53           C
ANISOU 3225  C   PHE A 422     2846   3618   2477    648   -253    441       C
ATOM   3226  O   PHE A 422     -17.290 -55.390 -14.189  1.00 23.46           O
ANISOU 3226  O   PHE A 422     2870   3617   2427    642   -233    454       O
ATOM   3227  CB  PHE A 422     -14.793 -53.956 -15.932  1.00 23.41           C
ANISOU 3227  CB  PHE A 422     2716   3647   2530    574   -324    298       C
ATOM   3228  CG  PHE A 422     -14.326 -52.581 -15.554  1.00 23.33           C
ANISOU 3228  CG  PHE A 422     2651   3703   2509    538   -378    208       C
ATOM   3229  CD1 PHE A 422     -13.141 -52.408 -14.859  1.00 24.57           C
ANISOU 3229  CD1 PHE A 422     2751   3957   2628    581   -442    175       C
ATOM   3230  CD2 PHE A 422     -15.067 -51.459 -15.897  1.00 24.51           C
ANISOU 3230  CD2 PHE A 422     2805   3817   2692    462   -365    154       C
ATOM   3231  CE1 PHE A 422     -12.706 -51.143 -14.502  1.00 25.32           C
ANISOU 3231  CE1 PHE A 422     2793   4106   2722    542   -496     84       C
ATOM   3232  CE2 PHE A 422     -14.632 -50.185 -15.541  1.00 24.31           C
ANISOU 3232  CE2 PHE A 422     2732   3839   2664    427   -414     67       C
ATOM   3233  CZ  PHE A 422     -13.444 -50.034 -14.847  1.00 25.52           C
ANISOU 3233  CZ  PHE A 422     2827   4084   2784    464   -480     29       C
ATOM   3234  N   VAL A 423     -16.322 -56.618 -15.809  1.00 23.39           N
ANISOU 3234  N   VAL A 423     2849   3517   2519    648   -216    486       N
ATOM   3235  CA  VAL A 423     -17.512 -57.424 -16.056  1.00 23.35           C
ANISOU 3235  CA  VAL A 423     2906   3421   2545    632   -155    550       C
ATOM   3236  C   VAL A 423     -17.926 -58.198 -14.798  1.00 24.30           C
ANISOU 3236  C   VAL A 423     3069   3567   2596    699   -133    632       C
ATOM   3237  O   VAL A 423     -19.086 -58.150 -14.393  1.00 24.32           O
ANISOU 3237  O   VAL A 423     3106   3548   2588    676    -95    662       O
ATOM   3238  CB  VAL A 423     -17.314 -58.398 -17.234  1.00 23.01           C
ANISOU 3238  CB  VAL A 423     2881   3287   2577    629   -128    576       C
ATOM   3239  CG1 VAL A 423     -18.520 -59.331 -17.361  1.00 23.56           C
ANISOU 3239  CG1 VAL A 423     3012   3260   2680    615    -70    641       C
ATOM   3240  CG2 VAL A 423     -17.100 -57.627 -18.535  1.00 22.54           C
ANISOU 3240  CG2 VAL A 423     2787   3198   2581    563   -137    503       C
ATOM   3241  N   GLU A 424     -16.979 -58.892 -14.172  1.00 25.34           N
ANISOU 3241  N   GLU A 424     3197   3751   2679    786   -156    674       N
ATOM   3242  CA  GLU A 424     -17.281 -59.665 -12.961  1.00 26.74           C
ANISOU 3242  CA  GLU A 424     3417   3958   2784    863   -133    763       C
ATOM   3243  C   GLU A 424     -17.852 -58.776 -11.849  1.00 26.75           C
ANISOU 3243  C   GLU A 424     3419   4043   2702    865   -144    743       C
ATOM   3244  O   GLU A 424     -18.844 -59.134 -11.210  1.00 27.10           O
ANISOU 3244  O   GLU A 424     3508   4071   2716    877    -93    809       O
ATOM   3245  CB  GLU A 424     -16.044 -60.427 -12.474  1.00 28.06           C
ANISOU 3245  CB  GLU A 424     3574   4182   2906    965   -165    803       C
ATOM   3246  CG  GLU A 424     -15.642 -61.571 -13.414  1.00 30.18           C
ANISOU 3246  CG  GLU A 424     3860   4356   3250    982   -139    846       C
ATOM   3247  CD  GLU A 424     -14.364 -62.287 -13.004  1.00 35.05           C
ANISOU 3247  CD  GLU A 424     4461   5031   3826   1089   -171    883       C
ATOM   3248  OE1 GLU A 424     -14.098 -63.379 -13.557  1.00 37.39           O
ANISOU 3248  OE1 GLU A 424     4786   5250   4172   1123   -142    935       O
ATOM   3249  OE2 GLU A 424     -13.625 -61.773 -12.136  1.00 38.33           O
ANISOU 3249  OE2 GLU A 424     4835   5570   4160   1141   -228    859       O
ATOM   3250  N   SER A 425     -17.248 -57.606 -11.654  1.00 26.49           N
ANISOU 3250  N   SER A 425     3335   4094   2635    851   -206    649       N
ATOM   3251  CA  SER A 425     -17.663 -56.679 -10.597  1.00 26.71           C
ANISOU 3251  CA  SER A 425     3363   4208   2579    860   -227    612       C
ATOM   3252  C   SER A 425     -19.007 -56.021 -10.888  1.00 26.08           C
ANISOU 3252  C   SER A 425     3305   4073   2533    781   -182    592       C
ATOM   3253  O   SER A 425     -19.880 -55.952 -10.022  1.00 26.17           O
ANISOU 3253  O   SER A 425     3349   4111   2484    803   -150    626       O
ATOM   3254  CB  SER A 425     -16.604 -55.591 -10.398  1.00 26.79           C
ANISOU 3254  CB  SER A 425     3309   4311   2559    858   -312    506       C
ATOM   3255  OG  SER A 425     -15.405 -56.129  -9.861  1.00 27.33           O
ANISOU 3255  OG  SER A 425     3352   4457   2575    944   -361    524       O
ATOM   3256  N   PHE A 426     -19.176 -55.524 -12.105  1.00 25.46           N
ANISOU 3256  N   PHE A 426     3205   3921   2547    695   -177    538       N
ATOM   3257  CA  PHE A 426     -20.411 -54.837 -12.439  1.00 25.18           C
ANISOU 3257  CA  PHE A 426     3184   3838   2546    624   -140    514       C
ATOM   3258  C   PHE A 426     -21.590 -55.792 -12.604  1.00 24.92           C
ANISOU 3258  C   PHE A 426     3198   3724   2548    612    -65    604       C
ATOM   3259  O   PHE A 426     -22.739 -55.383 -12.426  1.00 24.45           O
ANISOU 3259  O   PHE A 426     3152   3649   2487    579    -28    607       O
ATOM   3260  CB  PHE A 426     -20.216 -53.893 -13.633  1.00 24.93           C
ANISOU 3260  CB  PHE A 426     3114   3764   2593    542   -161    427       C
ATOM   3261  CG  PHE A 426     -19.446 -52.629 -13.281  1.00 27.23           C
ANISOU 3261  CG  PHE A 426     3362   4133   2854    535   -226    331       C
ATOM   3262  CD1 PHE A 426     -19.526 -52.070 -12.002  1.00 30.50           C
ANISOU 3262  CD1 PHE A 426     3779   4634   3174    576   -253    305       C
ATOM   3263  CD2 PHE A 426     -18.661 -51.996 -14.224  1.00 29.97           C
ANISOU 3263  CD2 PHE A 426     3662   4462   3265    486   -257    265       C
ATOM   3264  CE1 PHE A 426     -18.828 -50.914 -11.677  1.00 31.85           C
ANISOU 3264  CE1 PHE A 426     3909   4868   3323    565   -317    207       C
ATOM   3265  CE2 PHE A 426     -17.966 -50.836 -13.907  1.00 30.72           C
ANISOU 3265  CE2 PHE A 426     3712   4617   3345    471   -315    176       C
ATOM   3266  CZ  PHE A 426     -18.048 -50.299 -12.634  1.00 31.30           C
ANISOU 3266  CZ  PHE A 426     3791   4772   3332    508   -348    143       C
ATOM   3267  N   THR A 427     -21.311 -57.065 -12.884  1.00 24.86           N
ANISOU 3267  N   THR A 427     3211   3664   2572    642    -42    676       N
ATOM   3268  CA  THR A 427     -22.371 -58.069 -12.913  1.00 25.12           C
ANISOU 3268  CA  THR A 427     3287   3616   2642    634     29    766       C
ATOM   3269  C   THR A 427     -22.922 -58.302 -11.501  1.00 26.04           C
ANISOU 3269  C   THR A 427     3432   3792   2670    695     63    839       C
ATOM   3270  O   THR A 427     -24.119 -58.559 -11.336  1.00 26.08           O
ANISOU 3270  O   THR A 427     3459   3754   2694    669    124    892       O
ATOM   3271  CB  THR A 427     -21.896 -59.397 -13.552  1.00 25.21           C
ANISOU 3271  CB  THR A 427     3319   3547   2714    654     45    823       C
ATOM   3272  OG1 THR A 427     -21.450 -59.149 -14.896  1.00 24.76           O
ANISOU 3272  OG1 THR A 427     3236   3439   2733    602     18    754       O
ATOM   3273  CG2 THR A 427     -23.035 -60.423 -13.577  1.00 25.68           C
ANISOU 3273  CG2 THR A 427     3420   3512   2824    636    117    912       C
ATOM   3274  N   ARG A 428     -22.049 -58.169 -10.498  1.00 26.88           N
ANISOU 3274  N   ARG A 428     3535   4003   2677    776     22    838       N
ATOM   3275  CA  ARG A 428     -22.402 -58.382  -9.088  1.00 28.35           C
ANISOU 3275  CA  ARG A 428     3750   4264   2758    853     48    907       C
ATOM   3276  C   ARG A 428     -22.989 -57.159  -8.383  1.00 28.00           C
ANISOU 3276  C   ARG A 428     3697   4299   2642    846     39    848       C
ATOM   3277  O   ARG A 428     -23.673 -57.313  -7.367  1.00 28.81           O
ANISOU 3277  O   ARG A 428     3829   4445   2670    894     83    910       O
ATOM   3278  CB  ARG A 428     -21.165 -58.820  -8.289  1.00 29.51           C
ANISOU 3278  CB  ARG A 428     3896   4498   2817    958      2    931       C
ATOM   3279  CG  ARG A 428     -20.707 -60.229  -8.544  1.00 32.63           C
ANISOU 3279  CG  ARG A 428     4317   4830   3252   1002     27   1024       C
ATOM   3280  CD  ARG A 428     -19.671 -60.664  -7.504  1.00 36.78           C
ANISOU 3280  CD  ARG A 428     4848   5457   3670   1124    -10   1066       C
ATOM   3281  NE  ARG A 428     -18.503 -59.777  -7.482  1.00 39.28           N
ANISOU 3281  NE  ARG A 428     5108   5870   3945   1138   -105    958       N
ATOM   3282  CZ  ARG A 428     -17.334 -60.007  -8.091  1.00 41.36           C
ANISOU 3282  CZ  ARG A 428     5336   6133   4246   1151   -155    926       C
ATOM   3283  NH1 ARG A 428     -17.116 -61.120  -8.794  1.00 42.12           N
ANISOU 3283  NH1 ARG A 428     5451   6136   4416   1159   -121    991       N
ATOM   3284  NH2 ARG A 428     -16.360 -59.109  -7.988  1.00 42.35           N
ANISOU 3284  NH2 ARG A 428     5403   6352   4337   1156   -239    827       N
ATOM   3285  N   GLN A 429     -22.709 -55.952  -8.874  1.00 26.90           N
ANISOU 3285  N   GLN A 429     3520   4179   2521    792    -15    731       N
ATOM   3286  CA  GLN A 429     -23.146 -54.750  -8.159  1.00 26.71           C
ANISOU 3286  CA  GLN A 429     3491   4231   2427    794    -31    664       C
ATOM   3287  C   GLN A 429     -24.555 -54.331  -8.550  1.00 25.99           C
ANISOU 3287  C   GLN A 429     3408   4079   2387    725     28    666       C
ATOM   3288  O   GLN A 429     -24.836 -54.075  -9.724  1.00 24.58           O
ANISOU 3288  O   GLN A 429     3211   3818   2310    643     33    629       O
ATOM   3289  CB  GLN A 429     -22.192 -53.571  -8.358  1.00 26.63           C
ANISOU 3289  CB  GLN A 429     3438   4271   2411    772   -117    536       C
ATOM   3290  CG  GLN A 429     -22.577 -52.370  -7.470  1.00 27.52           C
ANISOU 3290  CG  GLN A 429     3552   4464   2440    787   -139    463       C
ATOM   3291  CD  GLN A 429     -21.565 -51.239  -7.482  1.00 27.84           C
ANISOU 3291  CD  GLN A 429     3549   4557   2470    771   -229    336       C
ATOM   3292  OE1 GLN A 429     -20.565 -51.282  -8.199  1.00 27.92           O
ANISOU 3292  OE1 GLN A 429     3521   4547   2539    744   -273    302       O
ATOM   3293  NE2 GLN A 429     -21.825 -50.213  -6.680  1.00 27.05           N
ANISOU 3293  NE2 GLN A 429     3455   4524   2297    788   -254    264       N
ATOM   3294  N   ILE A 430     -25.422 -54.224  -7.549  1.00 26.24           N
ANISOU 3294  N   ILE A 430     3465   4160   2344    766     73    707       N
ATOM   3295  CA  ILE A 430     -26.816 -53.864  -7.780  1.00 25.72           C
ANISOU 3295  CA  ILE A 430     3402   4050   2319    713    135    717       C
ATOM   3296  C   ILE A 430     -26.974 -52.368  -8.067  1.00 25.22           C
ANISOU 3296  C   ILE A 430     3317   4005   2262    667     96    596       C
ATOM   3297  O   ILE A 430     -26.254 -51.533  -7.506  1.00 25.67           O
ANISOU 3297  O   ILE A 430     3366   4139   2247    701     34    515       O
ATOM   3298  CB  ILE A 430     -27.709 -54.286  -6.587  1.00 26.82           C
ANISOU 3298  CB  ILE A 430     3575   4241   2376    777    207    811       C
ATOM   3299  CG1 ILE A 430     -29.178 -54.388  -7.017  1.00 26.49           C
ANISOU 3299  CG1 ILE A 430     3528   4128   2410    715    287    858       C
ATOM   3300  CG2 ILE A 430     -27.527 -53.340  -5.399  1.00 27.61           C
ANISOU 3300  CG2 ILE A 430     3684   4465   2342    849    174    753       C
ATOM   3301  CD1 ILE A 430     -30.006 -55.258  -6.097  1.00 29.72           C
ANISOU 3301  CD1 ILE A 430     3962   4553   2775    766    375    987       C
ATOM   3302  N   ALA A 431     -27.909 -52.061  -8.961  1.00 24.10           N
ANISOU 3302  N   ALA A 431     3161   3786   2208    590    131    584       N
ATOM   3303  CA  ALA A 431     -28.252 -50.690  -9.333  1.00 23.63           C
ANISOU 3303  CA  ALA A 431     3084   3725   2167    545    108    484       C
ATOM   3304  C   ALA A 431     -29.436 -50.219  -8.500  1.00 23.96           C
ANISOU 3304  C   ALA A 431     3140   3811   2151    573    161    500       C
ATOM   3305  O   ALA A 431     -30.112 -51.022  -7.856  1.00 25.04           O
ANISOU 3305  O   ALA A 431     3295   3963   2255    610    225    598       O
ATOM   3306  CB  ALA A 431     -28.588 -50.619 -10.823  1.00 22.66           C
ANISOU 3306  CB  ALA A 431     2940   3501   2170    456    115    465       C
ATOM   3307  N   GLY A 432     -29.671 -48.911  -8.500  1.00 23.87           N
ANISOU 3307  N   GLY A 432     3122   3819   2128    557    138    407       N
ATOM   3308  CA  GLY A 432     -30.768 -48.323  -7.741  1.00 24.18           C
ANISOU 3308  CA  GLY A 432     3174   3903   2110    589    185    409       C
ATOM   3309  C   GLY A 432     -32.119 -48.368  -8.430  1.00 23.83           C
ANISOU 3309  C   GLY A 432     3114   3794   2148    535    252    450       C
ATOM   3310  O   GLY A 432     -32.208 -48.474  -9.657  1.00 23.40           O
ANISOU 3310  O   GLY A 432     3037   3656   2198    462    246    442       O
ATOM   3311  N   ARG A 433     -33.174 -48.295  -7.618  1.00 24.65           N
ANISOU 3311  N   ARG A 433     3226   3943   2197    576    316    494       N
ATOM   3312  CA AARG A 433     -34.548 -48.245  -8.120  0.50 24.39           C
ANISOU 3312  CA AARG A 433     3169   3864   2233    533    381    530       C
ATOM   3313  CA BARG A 433     -34.547 -48.242  -8.111  0.50 24.28           C
ANISOU 3313  CA BARG A 433     3156   3852   2218    533    381    530       C
ATOM   3314  C   ARG A 433     -34.829 -46.867  -8.716  1.00 24.00           C
ANISOU 3314  C   ARG A 433     3108   3796   2217    499    352    426       C
ATOM   3315  O   ARG A 433     -34.442 -45.842  -8.146  1.00 24.52           O
ANISOU 3315  O   ARG A 433     3191   3912   2213    538    314    342       O
ATOM   3316  CB AARG A 433     -35.548 -48.554  -7.000  0.50 25.41           C
ANISOU 3316  CB AARG A 433     3307   4058   2291    594    463    612       C
ATOM   3317  CB BARG A 433     -35.517 -48.522  -6.964  0.50 25.24           C
ANISOU 3317  CB BARG A 433     3287   4040   2264    596    461    609       C
ATOM   3318  CG AARG A 433     -36.978 -48.785  -7.486  0.50 25.48           C
ANISOU 3318  CG AARG A 433     3278   4021   2380    547    538    673       C
ATOM   3319  CG BARG A 433     -36.904 -48.931  -7.404  0.50 24.86           C
ANISOU 3319  CG BARG A 433     3203   3945   2296    552    540    683       C
ATOM   3320  CD AARG A 433     -37.940 -49.111  -6.347  0.50 26.26           C
ANISOU 3320  CD AARG A 433     3380   4188   2411    609    628    763       C
ATOM   3321  CD BARG A 433     -37.793 -49.202  -6.210  0.50 25.09           C
ANISOU 3321  CD BARG A 433     3238   4048   2248    619    626    768       C
ATOM   3322  NE AARG A 433     -38.003 -48.056  -5.337  0.50 26.62           N
ANISOU 3322  NE AARG A 433     3451   4328   2335    689    626    703       N
ATOM   3323  NE BARG A 433     -38.913 -50.067  -6.556  0.50 23.99           N
ANISOU 3323  NE BARG A 433     3060   3858   2197    573    705    871       N
ATOM   3324  CZ AARG A 433     -38.765 -48.107  -4.247  0.50 26.76           C
ANISOU 3324  CZ AARG A 433     3477   4424   2268    761    701    764       C
ATOM   3325  CZ BARG A 433     -39.711 -50.652  -5.670  0.50 23.77           C
ANISOU 3325  CZ BARG A 433     3027   3873   2132    615    796    977       C
ATOM   3326  NH1AARG A 433     -39.542 -49.161  -4.028  0.50 27.43           N
ANISOU 3326  NH1AARG A 433     3541   4499   2383    757    788    894       N
ATOM   3327  NH1BARG A 433     -39.521 -50.467  -4.369  0.50 25.50           N
ANISOU 3327  NH1BARG A 433     3283   4192   2213    714    819    996       N
ATOM   3328  NH2AARG A 433     -38.759 -47.105  -3.378  0.50 25.53           N
ANISOU 3328  NH2AARG A 433     3349   4353   1999    837    690    694       N
ATOM   3329  NH2BARG A 433     -40.699 -51.426  -6.087  0.50 21.82           N
ANISOU 3329  NH2BARG A 433     2736   3570   1986    559    863   1065       N
ATOM   3330  N   VAL A 434     -35.507 -46.845  -9.861  1.00 23.04           N
ANISOU 3330  N   VAL A 434     2955   3598   2201    430    368    431       N
ATOM   3331  CA  VAL A 434     -35.763 -45.598 -10.588  1.00 22.76           C
ANISOU 3331  CA  VAL A 434     2909   3533   2208    396    342    343       C
ATOM   3332  C   VAL A 434     -37.056 -44.912 -10.152  1.00 23.08           C
ANISOU 3332  C   VAL A 434     2940   3605   2225    424    397    344       C
ATOM   3333  O   VAL A 434     -37.056 -43.713  -9.880  1.00 23.56           O
ANISOU 3333  O   VAL A 434     3014   3689   2247    450    377    262       O
ATOM   3334  CB  VAL A 434     -35.766 -45.825 -12.111  1.00 21.78           C
ANISOU 3334  CB  VAL A 434     2758   3317   2201    317    323    339       C
ATOM   3335  CG1 VAL A 434     -36.119 -44.532 -12.849  1.00 21.23           C
ANISOU 3335  CG1 VAL A 434     2678   3217   2171    291    305    261       C
ATOM   3336  CG2 VAL A 434     -34.405 -46.340 -12.555  1.00 22.08           C
ANISOU 3336  CG2 VAL A 434     2805   3328   2257    297    267    326       C
ATOM   3337  N   ALA A 435     -38.151 -45.663 -10.094  1.00 23.24           N
ANISOU 3337  N   ALA A 435     2934   3623   2273    417    467    434       N
ATOM   3338  CA  ALA A 435     -39.408 -45.147  -9.544  1.00 23.77           C
ANISOU 3338  CA  ALA A 435     2986   3734   2312    453    530    451       C
ATOM   3339  C   ALA A 435     -39.362 -45.202  -8.018  1.00 24.66           C
ANISOU 3339  C   ALA A 435     3130   3942   2297    542    564    477       C
ATOM   3340  O   ALA A 435     -38.388 -45.692  -7.437  1.00 24.81           O
ANISOU 3340  O   ALA A 435     3181   3991   2256    573    536    487       O
ATOM   3341  CB  ALA A 435     -40.593 -45.950 -10.061  1.00 24.02           C
ANISOU 3341  CB  ALA A 435     2967   3731   2428    408    593    539       C
ATOM   3342  N   GLY A 436     -40.403 -44.686  -7.369  1.00 25.02           N
ANISOU 3342  N   GLY A 436     3168   4041   2298    590    624    488       N
ATOM   3343  CA  GLY A 436     -40.542 -44.801  -5.910  1.00 25.93           C
ANISOU 3343  CA  GLY A 436     3312   4255   2287    684    671    526       C
ATOM   3344  C   GLY A 436     -39.989 -43.645  -5.086  1.00 26.28           C
ANISOU 3344  C   GLY A 436     3404   4364   2218    758    627    419       C
ATOM   3345  O   GLY A 436     -40.201 -43.594  -3.870  1.00 27.48           O
ANISOU 3345  O   GLY A 436     3582   4605   2253    846    665    438       O
ATOM   3346  N   GLY A 437     -39.270 -42.732  -5.736  1.00 25.59           N
ANISOU 3346  N   GLY A 437     3329   4230   2165    723    547    306       N
ATOM   3347  CA  GLY A 437     -38.855 -41.473  -5.115  1.00 25.92           C
ANISOU 3347  CA  GLY A 437     3411   4313   2125    779    501    187       C
ATOM   3348  C   GLY A 437     -37.524 -41.509  -4.379  1.00 26.39           C
ANISOU 3348  C   GLY A 437     3511   4421   2096    818    431    134       C
ATOM   3349  O   GLY A 437     -37.015 -42.578  -4.023  1.00 26.08           O
ANISOU 3349  O   GLY A 437     3475   4410   2023    831    432    206       O
ATOM   3350  N   ARG A 438     -36.964 -40.315  -4.179  1.00 26.26           N
ANISOU 3350  N   ARG A 438     3522   4409   2046    836    367      5       N
ATOM   3351  CA  ARG A 438     -35.807 -40.096  -3.307  1.00 26.83           C
ANISOU 3351  CA  ARG A 438     3631   4543   2019    886    294    -71       C
ATOM   3352  C   ARG A 438     -34.665 -41.087  -3.530  1.00 26.39           C
ANISOU 3352  C   ARG A 438     3565   4481   1980    855    246    -31       C
ATOM   3353  O   ARG A 438     -34.176 -41.715  -2.588  1.00 27.20           O
ANISOU 3353  O   ARG A 438     3687   4665   1981    919    237      2       O
ATOM   3354  CB  ARG A 438     -36.255 -40.090  -1.845  1.00 28.16           C
ANISOU 3354  CB  ARG A 438     3835   4828   2035   1001    335    -57       C
ATOM   3355  CG  ARG A 438     -37.174 -38.927  -1.527  1.00 28.53           C
ANISOU 3355  CG  ARG A 438     3900   4888   2051   1045    367   -125       C
ATOM   3356  CD  ARG A 438     -37.726 -38.980  -0.121  1.00 30.55           C
ANISOU 3356  CD  ARG A 438     4190   5264   2153   1165    421   -101       C
ATOM   3357  NE  ARG A 438     -38.480 -37.767   0.199  1.00 31.04           N
ANISOU 3357  NE  ARG A 438     4274   5337   2181   1215    443   -186       N
ATOM   3358  CZ  ARG A 438     -39.235 -37.605   1.281  1.00 31.91           C
ANISOU 3358  CZ  ARG A 438     4412   5543   2169   1322    506   -171       C
ATOM   3359  NH1 ARG A 438     -39.355 -38.582   2.175  1.00 32.60           N
ANISOU 3359  NH1 ARG A 438     4508   5726   2153   1391    558    -67       N
ATOM   3360  NH2 ARG A 438     -39.876 -36.455   1.473  1.00 32.97           N
ANISOU 3360  NH2 ARG A 438     4566   5677   2283   1364    521   -257       N
ATOM   3361  N   ASN A 439     -34.233 -41.221  -4.777  1.00 25.28           N
ANISOU 3361  N   ASN A 439     3394   4248   1963    762    215    -34       N
ATOM   3362  CA  ASN A 439     -33.112 -42.115  -5.069  1.00 25.06           C
ANISOU 3362  CA  ASN A 439     3355   4210   1959    734    169     -3       C
ATOM   3363  C   ASN A 439     -32.116 -41.593  -6.110  1.00 24.63           C
ANISOU 3363  C   ASN A 439     3279   4079   1999    655     94    -83       C
ATOM   3364  O   ASN A 439     -31.317 -42.365  -6.626  1.00 24.10           O
ANISOU 3364  O   ASN A 439     3194   3987   1977    620     66    -48       O
ATOM   3365  CB  ASN A 439     -33.645 -43.502  -5.462  1.00 24.81           C
ANISOU 3365  CB  ASN A 439     3303   4151   1974    712    235    139       C
ATOM   3366  CG  ASN A 439     -32.673 -44.629  -5.132  1.00 25.04           C
ANISOU 3366  CG  ASN A 439     3336   4210   1967    734    210    197       C
ATOM   3367  OD1 ASN A 439     -31.928 -44.564  -4.149  1.00 26.57           O
ANISOU 3367  OD1 ASN A 439     3554   4486   2054    802    168    164       O
ATOM   3368  ND2 ASN A 439     -32.684 -45.675  -5.950  1.00 25.31           N
ANISOU 3368  ND2 ASN A 439     3349   4179   2088    682    234    282       N
ATOM   3369  N   VAL A 440     -32.135 -40.289  -6.391  1.00 24.58           N
ANISOU 3369  N   VAL A 440     3277   4037   2024    632     64   -189       N
ATOM   3370  CA  VAL A 440     -31.121 -39.675  -7.251  1.00 24.39           C
ANISOU 3370  CA  VAL A 440     3234   3947   2085    564     -5   -270       C
ATOM   3371  C   VAL A 440     -29.882 -39.344  -6.414  1.00 25.25           C
ANISOU 3371  C   VAL A 440     3352   4118   2123    596    -88   -358       C
ATOM   3372  O   VAL A 440     -29.978 -38.563  -5.471  1.00 25.69           O
ANISOU 3372  O   VAL A 440     3436   4226   2098    651   -109   -437       O
ATOM   3373  CB  VAL A 440     -31.644 -38.364  -7.892  1.00 24.31           C
ANISOU 3373  CB  VAL A 440     3226   3865   2144    526      0   -344       C
ATOM   3374  CG1 VAL A 440     -30.526 -37.654  -8.652  1.00 24.24           C
ANISOU 3374  CG1 VAL A 440     3200   3792   2217    459    -69   -428       C
ATOM   3375  CG2 VAL A 440     -32.820 -38.649  -8.824  1.00 23.02           C
ANISOU 3375  CG2 VAL A 440     3047   3644   2056    492     71   -264       C
ATOM   3376  N   PRO A 441     -28.716 -39.934  -6.744  1.00 25.68           N
ANISOU 3376  N   PRO A 441     3380   4170   2206    567   -139   -350       N
ATOM   3377  CA  PRO A 441     -27.532 -39.626  -5.937  1.00 26.90           C
ANISOU 3377  CA  PRO A 441     3534   4391   2295    599   -224   -437       C
ATOM   3378  C   PRO A 441     -27.162 -38.147  -6.024  1.00 27.35           C
ANISOU 3378  C   PRO A 441     3590   4410   2391    564   -279   -577       C
ATOM   3379  O   PRO A 441     -27.238 -37.562  -7.103  1.00 26.74           O
ANISOU 3379  O   PRO A 441     3496   4236   2427    489   -270   -597       O
ATOM   3380  CB  PRO A 441     -26.434 -40.504  -6.546  1.00 26.55           C
ANISOU 3380  CB  PRO A 441     3452   4334   2304    562   -259   -395       C
ATOM   3381  CG  PRO A 441     -26.925 -40.955  -7.837  1.00 25.54           C
ANISOU 3381  CG  PRO A 441     3307   4113   2285    496   -204   -318       C
ATOM   3382  CD  PRO A 441     -28.411 -40.833  -7.870  1.00 24.91           C
ANISOU 3382  CD  PRO A 441     3251   4010   2202    507   -126   -272       C
ATOM   3383  N   ILE A 442     -26.776 -37.550  -4.899  1.00 28.77           N
ANISOU 3383  N   ILE A 442     3790   4663   2477    620   -336   -673       N
ATOM   3384  CA  ILE A 442     -26.503 -36.110  -4.863  1.00 29.49           C
ANISOU 3384  CA  ILE A 442     3888   4715   2604    591   -387   -815       C
ATOM   3385  C   ILE A 442     -25.372 -35.712  -5.829  1.00 29.18           C
ANISOU 3385  C   ILE A 442     3798   4599   2689    496   -443   -866       C
ATOM   3386  O   ILE A 442     -25.357 -34.590  -6.340  1.00 28.56           O
ANISOU 3386  O   ILE A 442     3718   4438   2696    440   -455   -946       O
ATOM   3387  CB  ILE A 442     -26.219 -35.608  -3.423  1.00 31.27           C
ANISOU 3387  CB  ILE A 442     4143   5040   2697    673   -448   -919       C
ATOM   3388  CG1 ILE A 442     -26.290 -34.076  -3.362  1.00 32.32           C
ANISOU 3388  CG1 ILE A 442     4295   5116   2868    649   -482  -1062       C
ATOM   3389  CG2 ILE A 442     -24.876 -36.121  -2.931  1.00 32.08           C
ANISOU 3389  CG2 ILE A 442     4214   5220   2754    688   -534   -947       C
ATOM   3390  CD1 ILE A 442     -26.708 -33.526  -2.019  1.00 34.27           C
ANISOU 3390  CD1 ILE A 442     4595   5446   2978    746   -499  -1146       C
ATOM   3391  N   ALA A 443     -24.460 -36.644  -6.111  1.00 29.04           N
ANISOU 3391  N   ALA A 443     3739   4606   2687    479   -471   -813       N
ATOM   3392  CA  ALA A 443     -23.352 -36.390  -7.041  1.00 29.18           C
ANISOU 3392  CA  ALA A 443     3703   4561   2823    393   -516   -848       C
ATOM   3393  C   ALA A 443     -23.815 -35.908  -8.420  1.00 28.60           C
ANISOU 3393  C   ALA A 443     3622   4364   2882    312   -462   -822       C
ATOM   3394  O   ALA A 443     -23.092 -35.167  -9.086  1.00 29.06           O
ANISOU 3394  O   ALA A 443     3648   4356   3039    242   -494   -882       O
ATOM   3395  CB  ALA A 443     -22.481 -37.637  -7.192  1.00 29.14           C
ANISOU 3395  CB  ALA A 443     3659   4604   2809    400   -535   -772       C
ATOM   3396  N   VAL A 444     -25.006 -36.328  -8.844  1.00 27.93           N
ANISOU 3396  N   VAL A 444     3564   4249   2798    324   -381   -731       N
ATOM   3397  CA  VAL A 444     -25.560 -35.913 -10.138  1.00 27.44           C
ANISOU 3397  CA  VAL A 444     3499   4080   2849    260   -329   -700       C
ATOM   3398  C   VAL A 444     -26.812 -35.038  -9.981  1.00 27.59           C
ANISOU 3398  C   VAL A 444     3561   4066   2857    281   -283   -726       C
ATOM   3399  O   VAL A 444     -27.662 -34.994 -10.870  1.00 26.79           O
ANISOU 3399  O   VAL A 444     3464   3901   2814    257   -224   -670       O
ATOM   3400  CB  VAL A 444     -25.868 -37.134 -11.046  1.00 26.50           C
ANISOU 3400  CB  VAL A 444     3365   3941   2764    244   -276   -574       C
ATOM   3401  CG1 VAL A 444     -24.585 -37.893 -11.374  1.00 27.18           C
ANISOU 3401  CG1 VAL A 444     3408   4044   2876    220   -318   -553       C
ATOM   3402  CG2 VAL A 444     -26.885 -38.061 -10.399  1.00 26.96           C
ANISOU 3402  CG2 VAL A 444     3452   4057   2735    309   -225   -490       C
ATOM   3403  N   GLN A 445     -26.912 -34.323  -8.863  1.00 28.59           N
ANISOU 3403  N   GLN A 445     3718   4238   2909    331   -313   -815       N
ATOM   3404  CA  GLN A 445     -28.093 -33.495  -8.609  1.00 29.24           C
ANISOU 3404  CA  GLN A 445     3843   4296   2971    364   -269   -843       C
ATOM   3405  C   GLN A 445     -28.284 -32.404  -9.668  1.00 28.97           C
ANISOU 3405  C   GLN A 445     3807   4142   3057    300   -252   -878       C
ATOM   3406  O   GLN A 445     -29.419 -32.091 -10.030  1.00 28.84           O
ANISOU 3406  O   GLN A 445     3812   4087   3057    314   -191   -845       O
ATOM   3407  CB  GLN A 445     -28.065 -32.887  -7.196  1.00 30.35           C
ANISOU 3407  CB  GLN A 445     4019   4508   3003    435   -310   -945       C
ATOM   3408  CG  GLN A 445     -27.006 -31.816  -6.951  1.00 31.35           C
ANISOU 3408  CG  GLN A 445     4139   4606   3166    400   -395  -1087       C
ATOM   3409  CD  GLN A 445     -27.141 -31.169  -5.581  1.00 33.70           C
ANISOU 3409  CD  GLN A 445     4481   4971   3352    476   -434  -1196       C
ATOM   3410  OE1 GLN A 445     -28.249 -31.006  -5.063  1.00 34.59           O
ANISOU 3410  OE1 GLN A 445     4638   5111   3393    544   -382  -1184       O
ATOM   3411  NE2 GLN A 445     -26.017 -30.789  -4.992  1.00 34.26           N
ANISOU 3411  NE2 GLN A 445     4536   5073   3407    468   -526  -1306       N
ATOM   3412  N   ALA A 446     -27.183 -31.842 -10.168  1.00 29.29           N
ANISOU 3412  N   ALA A 446     3819   4126   3182    233   -303   -940       N
ATOM   3413  CA  ALA A 446     -27.252 -30.770 -11.173  1.00 29.45           C
ANISOU 3413  CA  ALA A 446     3840   4028   3322    173   -286   -970       C
ATOM   3414  C   ALA A 446     -27.829 -31.267 -12.500  1.00 28.53           C
ANISOU 3414  C   ALA A 446     3709   3858   3273    140   -221   -857       C
ATOM   3415  O   ALA A 446     -28.539 -30.530 -13.189  1.00 28.35           O
ANISOU 3415  O   ALA A 446     3704   3757   3309    128   -179   -850       O
ATOM   3416  CB  ALA A 446     -25.876 -30.140 -11.386  1.00 29.91           C
ANISOU 3416  CB  ALA A 446     3863   4041   3459    105   -352  -1053       C
ATOM   3417  N   VAL A 447     -27.529 -32.517 -12.847  1.00 28.19           N
ANISOU 3417  N   VAL A 447     3636   3855   3219    132   -215   -771       N
ATOM   3418  CA  VAL A 447     -28.066 -33.137 -14.058  1.00 27.59           C
ANISOU 3418  CA  VAL A 447     3547   3739   3196    107   -161   -668       C
ATOM   3419  C   VAL A 447     -29.565 -33.382 -13.923  1.00 27.07           C
ANISOU 3419  C   VAL A 447     3509   3692   3085    157   -100   -611       C
ATOM   3420  O   VAL A 447     -30.330 -33.121 -14.853  1.00 26.24           O
ANISOU 3420  O   VAL A 447     3406   3529   3035    142    -56   -571       O
ATOM   3421  CB  VAL A 447     -27.369 -34.479 -14.372  1.00 27.26           C
ANISOU 3421  CB  VAL A 447     3470   3738   3149     93   -172   -596       C
ATOM   3422  CG1 VAL A 447     -27.916 -35.059 -15.663  1.00 27.63           C
ANISOU 3422  CG1 VAL A 447     3507   3738   3253     67   -121   -504       C
ATOM   3423  CG2 VAL A 447     -25.866 -34.293 -14.466  1.00 28.70           C
ANISOU 3423  CG2 VAL A 447     3615   3914   3374     49   -231   -648       C
ATOM   3424  N   ALA A 448     -29.984 -33.874 -12.759  1.00 27.44           N
ANISOU 3424  N   ALA A 448     3572   3823   3030    219    -97   -606       N
ATOM   3425  CA  ALA A 448     -31.403 -34.082 -12.485  1.00 27.25           C
ANISOU 3425  CA  ALA A 448     3567   3825   2960    269    -37   -554       C
ATOM   3426  C   ALA A 448     -32.171 -32.761 -12.476  1.00 27.67           C
ANISOU 3426  C   ALA A 448     3650   3831   3033    287    -15   -613       C
ATOM   3427  O   ALA A 448     -33.271 -32.682 -13.021  1.00 27.63           O
ANISOU 3427  O   ALA A 448     3645   3800   3052    297     38   -564       O
ATOM   3428  CB  ALA A 448     -31.594 -34.830 -11.170  1.00 28.03           C
ANISOU 3428  CB  ALA A 448     3679   4028   2942    337    -34   -535       C
ATOM   3429  N   LYS A 449     -31.593 -31.721 -11.879  1.00 28.17           N
ANISOU 3429  N   LYS A 449     3735   3879   3087    293    -59   -722       N
ATOM   3430  CA  LYS A 449     -32.230 -30.405 -11.891  1.00 28.74           C
ANISOU 3430  CA  LYS A 449     3840   3892   3186    311    -41   -786       C
ATOM   3431  C   LYS A 449     -32.348 -29.863 -13.324  1.00 27.96           C
ANISOU 3431  C   LYS A 449     3731   3688   3206    254    -17   -759       C
ATOM   3432  O   LYS A 449     -33.361 -29.257 -13.685  1.00 27.57           O
ANISOU 3432  O   LYS A 449     3698   3598   3178    278     29   -746       O
ATOM   3433  CB  LYS A 449     -31.469 -29.418 -11.010  1.00 29.89           C
ANISOU 3433  CB  LYS A 449     4013   4033   3312    320   -100   -917       C
ATOM   3434  CG  LYS A 449     -32.183 -28.090 -10.830  1.00 30.57           C
ANISOU 3434  CG  LYS A 449     4143   4061   3413    352    -80   -991       C
ATOM   3435  CD  LYS A 449     -31.402 -27.149  -9.933  1.00 32.43           C
ANISOU 3435  CD  LYS A 449     4405   4288   3631    358   -145  -1131       C
ATOM   3436  CE  LYS A 449     -32.109 -25.819  -9.789  1.00 33.25           C
ANISOU 3436  CE  LYS A 449     4558   4321   3756    392   -123  -1207       C
ATOM   3437  NZ  LYS A 449     -32.206 -25.083 -11.082  1.00 33.22           N
ANISOU 3437  NZ  LYS A 449     4549   4189   3883    335    -94  -1184       N
ATOM   3438  N   ALA A 450     -31.313 -30.088 -14.127  1.00 27.60           N
ANISOU 3438  N   ALA A 450     3655   3603   3230    187    -45   -746       N
ATOM   3439  CA  ALA A 450     -31.324 -29.688 -15.541  1.00 27.37           C
ANISOU 3439  CA  ALA A 450     3613   3481   3304    136    -20   -709       C
ATOM   3440  C   ALA A 450     -32.445 -30.382 -16.323  1.00 26.69           C
ANISOU 3440  C   ALA A 450     3517   3404   3219    152     35   -605       C
ATOM   3441  O   ALA A 450     -33.050 -29.783 -17.213  1.00 26.64           O
ANISOU 3441  O   ALA A 450     3518   3335   3270    148     69   -583       O
ATOM   3442  CB  ALA A 450     -29.976 -29.988 -16.185  1.00 27.11           C
ANISOU 3442  CB  ALA A 450     3545   3423   3333     68    -57   -704       C
ATOM   3443  N   SER A 451     -32.719 -31.642 -15.996  1.00 26.23           N
ANISOU 3443  N   SER A 451     3441   3424   3103    171     44   -543       N
ATOM   3444  CA  SER A 451     -33.816 -32.366 -16.630  1.00 25.81           C
ANISOU 3444  CA  SER A 451     3372   3383   3051    183     91   -452       C
ATOM   3445  C   SER A 451     -35.154 -31.670 -16.383  1.00 25.67           C
ANISOU 3445  C   SER A 451     3374   3364   3016    235    135   -456       C
ATOM   3446  O   SER A 451     -35.989 -31.589 -17.281  1.00 25.67           O
ANISOU 3446  O   SER A 451     3363   3334   3057    235    169   -408       O
ATOM   3447  CB  SER A 451     -33.885 -33.811 -16.136  1.00 25.82           C
ANISOU 3447  CB  SER A 451     3353   3462   2994    195     95   -389       C
ATOM   3448  OG  SER A 451     -32.793 -34.561 -16.623  1.00 27.28           O
ANISOU 3448  OG  SER A 451     3517   3642   3206    149     63   -368       O
ATOM   3449  N   ILE A 452     -35.348 -31.167 -15.168  1.00 25.88           N
ANISOU 3449  N   ILE A 452     3427   3428   2977    286    132   -516       N
ATOM   3450  CA  ILE A 452     -36.563 -30.441 -14.828  1.00 25.93           C
ANISOU 3450  CA  ILE A 452     3454   3437   2961    345    175   -529       C
ATOM   3451  C   ILE A 452     -36.584 -29.091 -15.539  1.00 25.77           C
ANISOU 3451  C   ILE A 452     3457   3320   3016    335    177   -577       C
ATOM   3452  O   ILE A 452     -37.569 -28.747 -16.194  1.00 25.68           O
ANISOU 3452  O   ILE A 452     3441   3280   3035    356    217   -539       O
ATOM   3453  CB  ILE A 452     -36.702 -30.206 -13.308  1.00 26.72           C
ANISOU 3453  CB  ILE A 452     3584   3605   2964    410    172   -589       C
ATOM   3454  CG1 ILE A 452     -36.793 -31.538 -12.556  1.00 26.76           C
ANISOU 3454  CG1 ILE A 452     3569   3709   2889    431    181   -528       C
ATOM   3455  CG2 ILE A 452     -37.938 -29.363 -13.012  1.00 27.24           C
ANISOU 3455  CG2 ILE A 452     3671   3668   3011    477    219   -606       C
ATOM   3456  CD1 ILE A 452     -36.672 -31.391 -11.050  1.00 27.22           C
ANISOU 3456  CD1 ILE A 452     3659   3844   2840    497    169   -587       C
ATOM   3457  N   ASP A 453     -35.499 -28.333 -15.409  1.00 25.79           N
ANISOU 3457  N   ASP A 453     3480   3269   3049    304    133   -658       N
ATOM   3458  CA  ASP A 453     -35.438 -26.981 -15.976  1.00 26.14           C
ANISOU 3458  CA  ASP A 453     3553   3210   3170    293    137   -707       C
ATOM   3459  C   ASP A 453     -35.593 -26.994 -17.500  1.00 25.23           C
ANISOU 3459  C   ASP A 453     3417   3031   3137    256    162   -633       C
ATOM   3460  O   ASP A 453     -36.285 -26.145 -18.065  1.00 25.45           O
ANISOU 3460  O   ASP A 453     3463   3000   3207    280    195   -626       O
ATOM   3461  CB  ASP A 453     -34.131 -26.279 -15.590  1.00 26.73           C
ANISOU 3461  CB  ASP A 453     3644   3235   3276    252     83   -805       C
ATOM   3462  CG  ASP A 453     -34.040 -25.981 -14.098  1.00 28.32           C
ANISOU 3462  CG  ASP A 453     3875   3489   3395    300     53   -899       C
ATOM   3463  OD1 ASP A 453     -35.093 -25.788 -13.460  1.00 29.80           O
ANISOU 3463  OD1 ASP A 453     4087   3716   3520    373     87   -906       O
ATOM   3464  OD2 ASP A 453     -32.905 -25.932 -13.568  1.00 29.91           O
ANISOU 3464  OD2 ASP A 453     4074   3697   3592    267     -4   -969       O
ATOM   3465  N   GLN A 454     -34.963 -27.959 -18.159  1.00 24.62           N
ANISOU 3465  N   GLN A 454     3304   2971   3079    205    147   -577       N
ATOM   3466  CA  GLN A 454     -35.021 -28.023 -19.627  1.00 24.16           C
ANISOU 3466  CA  GLN A 454     3229   2861   3090    173    167   -509       C
ATOM   3467  C   GLN A 454     -36.387 -28.476 -20.153  1.00 23.43           C
ANISOU 3467  C   GLN A 454     3121   2801   2981    212    208   -434       C
ATOM   3468  O   GLN A 454     -36.826 -28.008 -21.204  1.00 22.59           O
ANISOU 3468  O   GLN A 454     3016   2645   2924    216    231   -399       O
ATOM   3469  CB  GLN A 454     -33.867 -28.857 -20.176  1.00 23.97           C
ANISOU 3469  CB  GLN A 454     3175   2842   3091    111    138   -481       C
ATOM   3470  CG  GLN A 454     -32.535 -28.133 -19.963  1.00 26.24           C
ANISOU 3470  CG  GLN A 454     3470   3077   3424     66    102   -553       C
ATOM   3471  CD  GLN A 454     -31.327 -28.930 -20.382  1.00 28.42           C
ANISOU 3471  CD  GLN A 454     3711   3367   3722     10     73   -530       C
ATOM   3472  OE1 GLN A 454     -31.392 -30.143 -20.567  1.00 30.20           O
ANISOU 3472  OE1 GLN A 454     3911   3651   3913     10     72   -472       O
ATOM   3473  NE2 GLN A 454     -30.198 -28.240 -20.535  1.00 31.59           N
ANISOU 3473  NE2 GLN A 454     4107   3711   4187    -38     51   -578       N
ATOM   3474  N   SER A 455     -37.066 -29.355 -19.414  1.00 23.24           N
ANISOU 3474  N   SER A 455     3078   2861   2889    242    217   -409       N
ATOM   3475  CA  SER A 455     -38.466 -29.691 -19.709  1.00 23.14           C
ANISOU 3475  CA  SER A 455     3045   2886   2863    282    256   -348       C
ATOM   3476  C   SER A 455     -39.336 -28.438 -19.747  1.00 23.13           C
ANISOU 3476  C   SER A 455     3069   2845   2877    336    287   -374       C
ATOM   3477  O   SER A 455     -40.183 -28.281 -20.629  1.00 22.58           O
ANISOU 3477  O   SER A 455     2983   2760   2836    355    311   -327       O
ATOM   3478  CB  SER A 455     -39.042 -30.657 -18.665  1.00 23.54           C
ANISOU 3478  CB  SER A 455     3075   3029   2840    310    269   -325       C
ATOM   3479  OG  SER A 455     -38.483 -31.950 -18.797  1.00 25.79           O
ANISOU 3479  OG  SER A 455     3333   3348   3117    267    250   -281       O
ATOM   3480  N   ARG A 456     -39.125 -27.552 -18.778  1.00 23.49           N
ANISOU 3480  N   ARG A 456     3152   2873   2899    365    283   -452       N
ATOM   3481  CA  ARG A 456     -39.891 -26.317 -18.684  1.00 24.10           C
ANISOU 3481  CA  ARG A 456     3262   2907   2989    424    312   -487       C
ATOM   3482  C   ARG A 456     -39.534 -25.367 -19.818  1.00 24.13           C
ANISOU 3482  C   ARG A 456     3287   2805   3078    401    313   -488       C
ATOM   3483  O   ARG A 456     -40.411 -24.746 -20.415  1.00 24.29           O
ANISOU 3483  O   ARG A 456     3312   2793   3123    444    346   -461       O
ATOM   3484  CB  ARG A 456     -39.643 -25.636 -17.339  1.00 24.74           C
ANISOU 3484  CB  ARG A 456     3385   2993   3023    459    302   -581       C
ATOM   3485  CG  ARG A 456     -40.111 -26.473 -16.159  1.00 25.14           C
ANISOU 3485  CG  ARG A 456     3420   3153   2977    499    311   -575       C
ATOM   3486  CD  ARG A 456     -39.769 -25.821 -14.844  1.00 25.63           C
ANISOU 3486  CD  ARG A 456     3529   3227   2983    539    294   -675       C
ATOM   3487  NE  ARG A 456     -40.169 -26.652 -13.713  1.00 25.57           N
ANISOU 3487  NE  ARG A 456     3510   3332   2875    583    307   -661       N
ATOM   3488  CZ  ARG A 456     -40.083 -26.276 -12.439  1.00 26.50           C
ANISOU 3488  CZ  ARG A 456     3664   3490   2915    637    299   -737       C
ATOM   3489  NH1 ARG A 456     -39.596 -25.081 -12.117  1.00 27.11           N
ANISOU 3489  NH1 ARG A 456     3793   3501   3009    648    271   -844       N
ATOM   3490  NH2 ARG A 456     -40.488 -27.100 -11.479  1.00 25.96           N
ANISOU 3490  NH2 ARG A 456     3584   3530   2752    681    320   -707       N
ATOM   3491  N   GLU A 457     -38.242 -25.263 -20.109  1.00 24.28           N
ANISOU 3491  N   GLU A 457     3315   2771   3140    337    280   -514       N
ATOM   3492  CA  GLU A 457     -37.763 -24.418 -21.202  1.00 24.84           C
ANISOU 3492  CA  GLU A 457     3403   2739   3296    308    286   -505       C
ATOM   3493  C   GLU A 457     -38.369 -24.857 -22.530  1.00 23.32           C
ANISOU 3493  C   GLU A 457     3182   2552   3124    313    309   -411       C
ATOM   3494  O   GLU A 457     -38.721 -24.018 -23.362  1.00 23.61           O
ANISOU 3494  O   GLU A 457     3238   2523   3208    336    335   -388       O
ATOM   3495  CB  GLU A 457     -36.245 -24.492 -21.293  1.00 25.37           C
ANISOU 3495  CB  GLU A 457     3468   2768   3403    232    249   -536       C
ATOM   3496  CG  GLU A 457     -35.634 -23.487 -22.244  1.00 29.01           C
ANISOU 3496  CG  GLU A 457     3950   3115   3958    200    261   -535       C
ATOM   3497  CD  GLU A 457     -34.189 -23.800 -22.552  1.00 32.80           C
ANISOU 3497  CD  GLU A 457     4408   3574   4482    120    231   -541       C
ATOM   3498  OE1 GLU A 457     -33.778 -23.555 -23.709  1.00 34.27           O
ANISOU 3498  OE1 GLU A 457     4590   3700   4731     91    250   -491       O
ATOM   3499  OE2 GLU A 457     -33.476 -24.304 -21.643  1.00 35.25           O
ANISOU 3499  OE2 GLU A 457     4704   3932   4758     93    190   -592       O
ATOM   3500  N   MET A 458     -38.498 -26.171 -22.703  1.00 21.82           N
ANISOU 3500  N   MET A 458     2950   2442   2899    294    298   -359       N
ATOM   3501  CA  MET A 458     -39.092 -26.759 -23.907  1.00 20.82           C
ANISOU 3501  CA  MET A 458     2792   2336   2784    297    310   -278       C
ATOM   3502  C   MET A 458     -40.629 -26.794 -23.863  1.00 20.80           C
ANISOU 3502  C   MET A 458     2769   2382   2751    363    338   -246       C
ATOM   3503  O   MET A 458     -41.256 -27.375 -24.748  1.00 19.72           O
ANISOU 3503  O   MET A 458     2598   2277   2617    368    341   -186       O
ATOM   3504  CB  MET A 458     -38.533 -28.170 -24.129  1.00 20.24           C
ANISOU 3504  CB  MET A 458     2682   2317   2693    246    283   -243       C
ATOM   3505  CG  MET A 458     -37.041 -28.190 -24.447  1.00 20.10           C
ANISOU 3505  CG  MET A 458     2672   2254   2711    184    259   -260       C
ATOM   3506  SD  MET A 458     -36.402 -29.815 -24.891  1.00 20.75           S
ANISOU 3506  SD  MET A 458     2715   2392   2777    135    232   -213       S
ATOM   3507  CE  MET A 458     -36.469 -30.675 -23.309  1.00 20.26           C
ANISOU 3507  CE  MET A 458     2640   2409   2647    140    215   -242       C
ATOM   3508  N   LYS A 459     -41.219 -26.167 -22.840  1.00 20.95           N
ANISOU 3508  N   LYS A 459     2807   2411   2742    414    356   -291       N
ATOM   3509  CA  LYS A 459     -42.679 -26.029 -22.696  1.00 21.44           C
ANISOU 3509  CA  LYS A 459     2849   2519   2778    484    389   -266       C
ATOM   3510  C   LYS A 459     -43.431 -27.361 -22.771  1.00 20.64           C
ANISOU 3510  C   LYS A 459     2685   2512   2646    477    389   -206       C
ATOM   3511  O   LYS A 459     -44.439 -27.491 -23.476  1.00 20.43           O
ANISOU 3511  O   LYS A 459     2621   2512   2629    507    402   -157       O
ATOM   3512  CB  LYS A 459     -43.239 -25.025 -23.718  1.00 21.83           C
ANISOU 3512  CB  LYS A 459     2914   2508   2873    528    410   -241       C
ATOM   3513  CG  LYS A 459     -42.659 -23.608 -23.617  1.00 23.16           C
ANISOU 3513  CG  LYS A 459     3146   2570   3083    542    420   -296       C
ATOM   3514  CD  LYS A 459     -42.869 -22.936 -22.256  1.00 24.85           C
ANISOU 3514  CD  LYS A 459     3395   2781   3266    585    432   -373       C
ATOM   3515  CE  LYS A 459     -44.342 -22.760 -21.877  1.00 26.03           C
ANISOU 3515  CE  LYS A 459     3526   2988   3377    673    469   -358       C
ATOM   3516  NZ  LYS A 459     -45.109 -21.828 -22.767  1.00 25.49           N
ANISOU 3516  NZ  LYS A 459     3469   2868   3348    735    498   -324       N
ATOM   3517  N   TYR A 460     -42.941 -28.349 -22.028  1.00 20.22           N
ANISOU 3517  N   TYR A 460     2617   2508   2557    439    373   -211       N
ATOM   3518  CA  TYR A 460     -43.635 -29.630 -21.917  1.00 19.95           C
ANISOU 3518  CA  TYR A 460     2526   2556   2498    429    379   -157       C
ATOM   3519  C   TYR A 460     -45.000 -29.437 -21.264  1.00 20.29           C
ANISOU 3519  C   TYR A 460     2543   2656   2511    496    420   -146       C
ATOM   3520  O   TYR A 460     -45.122 -28.710 -20.277  1.00 20.54           O
ANISOU 3520  O   TYR A 460     2606   2691   2509    543    441   -193       O
ATOM   3521  CB  TYR A 460     -42.853 -30.599 -21.040  1.00 19.96           C
ANISOU 3521  CB  TYR A 460     2526   2595   2461    389    362   -166       C
ATOM   3522  CG  TYR A 460     -41.749 -31.386 -21.704  1.00 19.65           C
ANISOU 3522  CG  TYR A 460     2485   2534   2447    320    324   -150       C
ATOM   3523  CD1 TYR A 460     -41.027 -30.883 -22.789  1.00 19.55           C
ANISOU 3523  CD1 TYR A 460     2493   2453   2484    293    305   -156       C
ATOM   3524  CD2 TYR A 460     -41.396 -32.634 -21.206  1.00 20.84           C
ANISOU 3524  CD2 TYR A 460     2615   2732   2570    287    313   -127       C
ATOM   3525  CE1 TYR A 460     -39.994 -31.618 -23.362  1.00 19.50           C
ANISOU 3525  CE1 TYR A 460     2483   2432   2496    236    275   -142       C
ATOM   3526  CE2 TYR A 460     -40.375 -33.367 -21.761  1.00 20.36           C
ANISOU 3526  CE2 TYR A 460     2554   2653   2530    232    281   -115       C
ATOM   3527  CZ  TYR A 460     -39.673 -32.866 -22.840  1.00 19.74           C
ANISOU 3527  CZ  TYR A 460     2492   2511   2497    207    261   -124       C
ATOM   3528  OH  TYR A 460     -38.652 -33.620 -23.384  1.00 19.96           O
ANISOU 3528  OH  TYR A 460     2516   2526   2542    158    234   -111       O
ATOM   3529  N   GLN A 461     -46.008 -30.115 -21.809  1.00 20.12           N
ANISOU 3529  N   GLN A 461     2460   2682   2502    499    430    -87       N
ATOM   3530  CA  GLN A 461     -47.285 -30.267 -21.142  1.00 20.67           C
ANISOU 3530  CA  GLN A 461     2484   2824   2546    549    471    -64       C
ATOM   3531  C   GLN A 461     -47.113 -31.128 -19.877  1.00 20.87           C
ANISOU 3531  C   GLN A 461     2502   2908   2520    537    487    -60       C
ATOM   3532  O   GLN A 461     -46.038 -31.680 -19.612  1.00 20.48           O
ANISOU 3532  O   GLN A 461     2478   2846   2457    488    460    -72       O
ATOM   3533  CB  GLN A 461     -48.324 -30.890 -22.087  1.00 20.62           C
ANISOU 3533  CB  GLN A 461     2405   2855   2576    543    471     -3       C
ATOM   3534  CG  GLN A 461     -48.656 -30.030 -23.298  1.00 21.40           C
ANISOU 3534  CG  GLN A 461     2507   2911   2713    573    458      0       C
ATOM   3535  CD  GLN A 461     -49.781 -30.602 -24.139  1.00 21.75           C
ANISOU 3535  CD  GLN A 461     2473   3006   2786    577    452     52       C
ATOM   3536  OE1 GLN A 461     -50.763 -31.132 -23.609  1.00 22.85           O
ANISOU 3536  OE1 GLN A 461     2548   3215   2918    590    479     80       O
ATOM   3537  NE2 GLN A 461     -49.651 -30.493 -25.461  1.00 19.81           N
ANISOU 3537  NE2 GLN A 461     2226   2728   2570    567    418     65       N
ATOM   3538  N   SER A 462     -48.181 -31.237 -19.102  1.00 21.51           N
ANISOU 3538  N   SER A 462     2545   3056   2570    585    534    -37       N
ATOM   3539  CA  SER A 462     -48.132 -31.879 -17.797  1.00 21.95           C
ANISOU 3539  CA  SER A 462     2600   3173   2566    593    562    -30       C
ATOM   3540  C   SER A 462     -48.107 -33.399 -17.879  1.00 21.55           C
ANISOU 3540  C   SER A 462     2500   3158   2529    530    558     35       C
ATOM   3541  O   SER A 462     -48.408 -33.981 -18.925  1.00 20.90           O
ANISOU 3541  O   SER A 462     2373   3064   2505    485    538     74       O
ATOM   3542  CB  SER A 462     -49.358 -31.477 -16.989  1.00 22.97           C
ANISOU 3542  CB  SER A 462     2702   3367   2660    673    623    -19       C
ATOM   3543  OG  SER A 462     -50.518 -32.102 -17.512  1.00 23.90           O
ANISOU 3543  OG  SER A 462     2734   3530   2819    665    647     50       O
ATOM   3544  N   LEU A 463     -47.779 -34.019 -16.745  1.00 21.38           N
ANISOU 3544  N   LEU A 463     2490   3180   2452    532    577     45       N
ATOM   3545  CA  LEU A 463     -47.836 -35.472 -16.575  1.00 21.06           C
ANISOU 3545  CA  LEU A 463     2407   3175   2419    483    588    113       C
ATOM   3546  C   LEU A 463     -49.157 -36.041 -17.076  1.00 21.45           C
ANISOU 3546  C   LEU A 463     2370   3257   2521    472    619    178       C
ATOM   3547  O   LEU A 463     -49.170 -36.992 -17.856  1.00 21.07           O
ANISOU 3547  O   LEU A 463     2284   3192   2530    408    596    217       O
ATOM   3548  CB  LEU A 463     -47.664 -35.841 -15.096  1.00 21.44           C
ANISOU 3548  CB  LEU A 463     2477   3284   2387    519    625    124       C
ATOM   3549  CG  LEU A 463     -48.054 -37.266 -14.678  1.00 21.74           C
ANISOU 3549  CG  LEU A 463     2465   3368   2427    489    662    211       C
ATOM   3550  CD1 LEU A 463     -47.112 -38.274 -15.324  1.00 21.47           C
ANISOU 3550  CD1 LEU A 463     2438   3288   2434    410    613    229       C
ATOM   3551  CD2 LEU A 463     -48.068 -37.399 -13.153  1.00 22.27           C
ANISOU 3551  CD2 LEU A 463     2555   3506   2400    548    712    225       C
ATOM   3552  N   ASN A 464     -50.262 -35.460 -16.619  1.00 22.30           N
ANISOU 3552  N   ASN A 464     2447   3414   2613    536    670    187       N
ATOM   3553  CA  ASN A 464     -51.585 -35.989 -16.967  1.00 22.92           C
ANISOU 3553  CA  ASN A 464     2430   3536   2743    529    704    250       C
ATOM   3554  C   ASN A 464     -51.937 -35.838 -18.451  1.00 22.64           C
ANISOU 3554  C   ASN A 464     2357   3462   2783    497    658    246       C
ATOM   3555  O   ASN A 464     -52.617 -36.695 -19.016  1.00 22.76           O
ANISOU 3555  O   ASN A 464     2296   3494   2857    452    656    293       O
ATOM   3556  CB  ASN A 464     -52.678 -35.412 -16.060  1.00 23.86           C
ANISOU 3556  CB  ASN A 464     2518   3725   2821    612    775    263       C
ATOM   3557  CG  ASN A 464     -52.791 -36.158 -14.730  1.00 24.75           C
ANISOU 3557  CG  ASN A 464     2624   3902   2878    627    837    312       C
ATOM   3558  OD1 ASN A 464     -52.240 -37.254 -14.567  1.00 24.03           O
ANISOU 3558  OD1 ASN A 464     2533   3804   2792    569    829    350       O
ATOM   3559  ND2 ASN A 464     -53.513 -35.572 -13.779  1.00 24.05           N
ANISOU 3559  ND2 ASN A 464     2529   3877   2733    712    902    314       N
ATOM   3560  N   GLU A 465     -51.464 -34.775 -19.094  1.00 22.55           N
ANISOU 3560  N   GLU A 465     2398   3398   2771    521    621    189       N
ATOM   3561  CA  GLU A 465     -51.611 -34.668 -20.545  1.00 22.30           C
ANISOU 3561  CA  GLU A 465     2344   3330   2801    494    573    187       C
ATOM   3562  C   GLU A 465     -50.830 -35.790 -21.244  1.00 21.18           C
ANISOU 3562  C   GLU A 465     2202   3152   2694    407    524    202       C
ATOM   3563  O   GLU A 465     -51.327 -36.392 -22.196  1.00 21.21           O
ANISOU 3563  O   GLU A 465     2149   3158   2751    370    498    226       O
ATOM   3564  CB  GLU A 465     -51.158 -33.297 -21.059  1.00 22.37           C
ANISOU 3564  CB  GLU A 465     2417   3281   2801    538    550    132       C
ATOM   3565  CG  GLU A 465     -52.041 -32.127 -20.622  1.00 24.82           C
ANISOU 3565  CG  GLU A 465     2725   3616   3089    630    592    115       C
ATOM   3566  CD  GLU A 465     -53.503 -32.298 -21.003  1.00 27.95           C
ANISOU 3566  CD  GLU A 465     3025   4073   3520    657    615    161       C
ATOM   3567  OE1 GLU A 465     -53.791 -32.747 -22.130  1.00 30.47           O
ANISOU 3567  OE1 GLU A 465     3297   4390   3891    620    576    184       O
ATOM   3568  OE2 GLU A 465     -54.374 -31.987 -20.169  1.00 32.16           O
ANISOU 3568  OE2 GLU A 465     3527   4663   4028    718    670    173       O
ATOM   3569  N   TYR A 466     -49.618 -36.073 -20.774  1.00 20.47           N
ANISOU 3569  N   TYR A 466     2174   3032   2572    379    510    183       N
ATOM   3570  CA  TYR A 466     -48.828 -37.182 -21.322  1.00 19.76           C
ANISOU 3570  CA  TYR A 466     2088   2910   2511    305    470    197       C
ATOM   3571  C   TYR A 466     -49.451 -38.543 -21.036  1.00 20.11           C
ANISOU 3571  C   TYR A 466     2067   2990   2583    261    492    257       C
ATOM   3572  O   TYR A 466     -49.416 -39.435 -21.887  1.00 19.85           O
ANISOU 3572  O   TYR A 466     2006   2935   2602    204    458    274       O
ATOM   3573  CB  TYR A 466     -47.369 -37.123 -20.851  1.00 19.05           C
ANISOU 3573  CB  TYR A 466     2075   2784   2380    291    450    163       C
ATOM   3574  CG  TYR A 466     -46.585 -36.157 -21.702  1.00 18.64           C
ANISOU 3574  CG  TYR A 466     2074   2671   2337    296    410    113       C
ATOM   3575  CD1 TYR A 466     -46.214 -36.502 -22.994  1.00 18.35           C
ANISOU 3575  CD1 TYR A 466     2033   2595   2343    254    367    116       C
ATOM   3576  CD2 TYR A 466     -46.277 -34.878 -21.249  1.00 18.94           C
ANISOU 3576  CD2 TYR A 466     2163   2690   2342    345    420     64       C
ATOM   3577  CE1 TYR A 466     -45.530 -35.616 -23.803  1.00 18.93           C
ANISOU 3577  CE1 TYR A 466     2151   2616   2426    261    340     81       C
ATOM   3578  CE2 TYR A 466     -45.586 -33.980 -22.053  1.00 18.74           C
ANISOU 3578  CE2 TYR A 466     2182   2603   2337    346    390     25       C
ATOM   3579  CZ  TYR A 466     -45.217 -34.355 -23.329  1.00 19.05           C
ANISOU 3579  CZ  TYR A 466     2214   2607   2418    304    353     39       C
ATOM   3580  OH  TYR A 466     -44.536 -33.475 -24.141  1.00 19.23           O
ANISOU 3580  OH  TYR A 466     2278   2569   2459    307    332     12       O
ATOM   3581  N   ARG A 467     -50.030 -38.707 -19.854  1.00 20.85           N
ANISOU 3581  N   ARG A 467     2138   3138   2646    290    551    290       N
ATOM   3582  CA  ARG A 467     -50.746 -39.943 -19.552  1.00 21.66           C
ANISOU 3582  CA  ARG A 467     2171   3272   2785    250    584    356       C
ATOM   3583  C   ARG A 467     -51.904 -40.158 -20.536  1.00 21.99           C
ANISOU 3583  C   ARG A 467     2125   3326   2903    227    571    375       C
ATOM   3584  O   ARG A 467     -52.029 -41.233 -21.128  1.00 22.20           O
ANISOU 3584  O   ARG A 467     2111   3334   2992    160    548    400       O
ATOM   3585  CB  ARG A 467     -51.212 -39.965 -18.094  1.00 22.59           C
ANISOU 3585  CB  ARG A 467     2280   3453   2851    297    659    394       C
ATOM   3586  CG  ARG A 467     -50.085 -40.335 -17.139  1.00 22.63           C
ANISOU 3586  CG  ARG A 467     2354   3452   2791    299    665    394       C
ATOM   3587  CD  ARG A 467     -50.515 -40.386 -15.684  1.00 24.10           C
ANISOU 3587  CD  ARG A 467     2537   3708   2911    354    741    434       C
ATOM   3588  NE  ARG A 467     -51.519 -41.412 -15.394  1.00 25.43           N
ANISOU 3588  NE  ARG A 467     2625   3913   3125    327    798    520       N
ATOM   3589  CZ  ARG A 467     -51.273 -42.706 -15.171  1.00 25.50           C
ANISOU 3589  CZ  ARG A 467     2622   3908   3160    274    812    581       C
ATOM   3590  NH1 ARG A 467     -50.040 -43.198 -15.227  1.00 25.28           N
ANISOU 3590  NH1 ARG A 467     2657   3835   3114    245    769    567       N
ATOM   3591  NH2 ARG A 467     -52.286 -43.523 -14.900  1.00 25.86           N
ANISOU 3591  NH2 ARG A 467     2587   3982   3255    250    872    661       N
ATOM   3592  N   LYS A 468     -52.716 -39.127 -20.750  1.00 22.46           N
ANISOU 3592  N   LYS A 468     2158   3416   2960    284    582    357       N
ATOM   3593  CA  LYS A 468     -53.807 -39.217 -21.727  1.00 23.07           C
ANISOU 3593  CA  LYS A 468     2150   3513   3104    271    562    369       C
ATOM   3594  C   LYS A 468     -53.315 -39.550 -23.136  1.00 22.44           C
ANISOU 3594  C   LYS A 468     2080   3380   3066    221    484    340       C
ATOM   3595  O   LYS A 468     -53.922 -40.365 -23.840  1.00 22.50           O
ANISOU 3595  O   LYS A 468     2017   3393   3137    171    457    357       O
ATOM   3596  CB  LYS A 468     -54.631 -37.926 -21.740  1.00 23.92           C
ANISOU 3596  CB  LYS A 468     2239   3658   3192    355    583    351       C
ATOM   3597  CG  LYS A 468     -55.513 -37.770 -20.508  1.00 25.46           C
ANISOU 3597  CG  LYS A 468     2391   3922   3362    405    665    388       C
ATOM   3598  CD  LYS A 468     -56.556 -36.694 -20.677  1.00 27.86           C
ANISOU 3598  CD  LYS A 468     2651   4269   3664    484    685    379       C
ATOM   3599  CE  LYS A 468     -55.956 -35.309 -20.625  1.00 28.52           C
ANISOU 3599  CE  LYS A 468     2830   4318   3690    557    677    321       C
ATOM   3600  NZ  LYS A 468     -57.024 -34.264 -20.651  1.00 28.77           N
ANISOU 3600  NZ  LYS A 468     2822   4392   3717    645    707    317       N
ATOM   3601  N   ARG A 469     -52.206 -38.928 -23.529  1.00 21.81           N
ANISOU 3601  N   ARG A 469     2087   3250   2950    234    448    296       N
ATOM   3602  CA  ARG A 469     -51.592 -39.147 -24.843  1.00 21.30           C
ANISOU 3602  CA  ARG A 469     2045   3136   2910    198    380    269       C
ATOM   3603  C   ARG A 469     -51.225 -40.619 -25.084  1.00 21.34           C
ANISOU 3603  C   ARG A 469     2035   3118   2957    117    355    287       C
ATOM   3604  O   ARG A 469     -51.290 -41.095 -26.219  1.00 20.81           O
ANISOU 3604  O   ARG A 469     1946   3031   2928     83    302    274       O
ATOM   3605  CB  ARG A 469     -50.362 -38.240 -24.992  1.00 20.66           C
ANISOU 3605  CB  ARG A 469     2061   3006   2783    224    362    227       C
ATOM   3606  CG  ARG A 469     -49.455 -38.541 -26.183  1.00 20.81           C
ANISOU 3606  CG  ARG A 469     2117   2974   2817    187    303    205       C
ATOM   3607  CD  ARG A 469     -50.133 -38.302 -27.522  1.00 21.97           C
ANISOU 3607  CD  ARG A 469     2226   3128   2992    201    262    197       C
ATOM   3608  NE  ARG A 469     -49.164 -38.540 -28.596  1.00 22.47           N
ANISOU 3608  NE  ARG A 469     2335   3145   3057    175    212    176       N
ATOM   3609  CZ  ARG A 469     -48.812 -39.741 -29.059  1.00 22.72           C
ANISOU 3609  CZ  ARG A 469     2357   3161   3114    116    179    177       C
ATOM   3610  NH1 ARG A 469     -49.359 -40.852 -28.575  1.00 22.22           N
ANISOU 3610  NH1 ARG A 469     2240   3117   3087     70    188    200       N
ATOM   3611  NH2 ARG A 469     -47.898 -39.834 -30.021  1.00 23.29           N
ANISOU 3611  NH2 ARG A 469     2476   3195   3179    105    139    157       N
ATOM   3612  N   PHE A 470     -50.867 -41.330 -24.014  1.00 21.49           N
ANISOU 3612  N   PHE A 470     2066   3136   2963     93    393    317       N
ATOM   3613  CA  PHE A 470     -50.531 -42.751 -24.093  1.00 21.77           C
ANISOU 3613  CA  PHE A 470     2091   3142   3039     22    379    341       C
ATOM   3614  C   PHE A 470     -51.598 -43.671 -23.485  1.00 23.09           C
ANISOU 3614  C   PHE A 470     2174   3342   3256    -12    424    398       C
ATOM   3615  O   PHE A 470     -51.298 -44.767 -23.019  1.00 22.95           O
ANISOU 3615  O   PHE A 470     2159   3302   3260    -58    441    434       O
ATOM   3616  CB  PHE A 470     -49.138 -42.974 -23.489  1.00 21.27           C
ANISOU 3616  CB  PHE A 470     2111   3044   2928     16    382    336       C
ATOM   3617  CG  PHE A 470     -48.035 -42.433 -24.356  1.00 20.26           C
ANISOU 3617  CG  PHE A 470     2049   2871   2778     23    329    285       C
ATOM   3618  CD1 PHE A 470     -47.435 -43.238 -25.315  1.00 19.66           C
ANISOU 3618  CD1 PHE A 470     1986   2751   2734    -24    280    273       C
ATOM   3619  CD2 PHE A 470     -47.632 -41.106 -24.251  1.00 20.54           C
ANISOU 3619  CD2 PHE A 470     2133   2907   2765     77    332    250       C
ATOM   3620  CE1 PHE A 470     -46.454 -42.739 -26.136  1.00 19.11           C
ANISOU 3620  CE1 PHE A 470     1972   2646   2645    -15    240    233       C
ATOM   3621  CE2 PHE A 470     -46.647 -40.596 -25.070  1.00 19.34           C
ANISOU 3621  CE2 PHE A 470     2035   2712   2602     79    291    211       C
ATOM   3622  CZ  PHE A 470     -46.047 -41.412 -26.013  1.00 19.13           C
ANISOU 3622  CZ  PHE A 470     2017   2649   2602     35    247    205       C
ATOM   3623  N   SER A 471     -52.851 -43.219 -23.532  1.00 24.22           N
ANISOU 3623  N   SER A 471     2241   3537   3424     13    445    409       N
ATOM   3624  CA  SER A 471     -54.025 -44.034 -23.185  1.00 25.93           C
ANISOU 3624  CA  SER A 471     2358   3788   3707    -24    483    462       C
ATOM   3625  C   SER A 471     -54.088 -44.440 -21.717  1.00 26.34           C
ANISOU 3625  C   SER A 471     2409   3865   3734    -17    566    524       C
ATOM   3626  O   SER A 471     -54.636 -45.497 -21.379  1.00 26.81           O
ANISOU 3626  O   SER A 471     2406   3925   3854    -69    600    579       O
ATOM   3627  CB  SER A 471     -54.112 -45.278 -24.080  1.00 26.37           C
ANISOU 3627  CB  SER A 471     2372   3799   3847   -109    432    460       C
ATOM   3628  OG  SER A 471     -53.955 -44.925 -25.442  1.00 28.40           O
ANISOU 3628  OG  SER A 471     2640   4038   4112   -108    353    400       O
ATOM   3629  N   LEU A 472     -53.550 -43.588 -20.849  1.00 25.97           N
ANISOU 3629  N   LEU A 472     2430   3839   3599     50    600    516       N
ATOM   3630  CA  LEU A 472     -53.563 -43.830 -19.411  1.00 26.51           C
ANISOU 3630  CA  LEU A 472     2508   3941   3621     76    679    570       C
ATOM   3631  C   LEU A 472     -54.556 -42.887 -18.752  1.00 27.38           C
ANISOU 3631  C   LEU A 472     2577   4126   3698    150    738    582       C
ATOM   3632  O   LEU A 472     -54.805 -41.781 -19.248  1.00 27.31           O
ANISOU 3632  O   LEU A 472     2573   4131   3673    198    714    533       O
ATOM   3633  CB  LEU A 472     -52.174 -43.604 -18.817  1.00 25.72           C
ANISOU 3633  CB  LEU A 472     2518   3817   3438    103    670    545       C
ATOM   3634  CG  LEU A 472     -51.015 -44.278 -19.553  1.00 24.14           C
ANISOU 3634  CG  LEU A 472     2371   3544   3258     48    605    520       C
ATOM   3635  CD1 LEU A 472     -49.688 -43.935 -18.891  1.00 23.63           C
ANISOU 3635  CD1 LEU A 472     2402   3468   3109     82    598    494       C
ATOM   3636  CD2 LEU A 472     -51.229 -45.779 -19.618  1.00 24.03           C
ANISOU 3636  CD2 LEU A 472     2313   3501   3317    -26    615    577       C
ATOM   3637  N   LYS A 473     -55.111 -43.323 -17.629  1.00 28.47           N
ANISOU 3637  N   LYS A 473     2679   4313   3825    163    820    650       N
ATOM   3638  CA  LYS A 473     -56.056 -42.502 -16.873  1.00 29.68           C
ANISOU 3638  CA  LYS A 473     2793   4545   3940    241    889    667       C
ATOM   3639  C   LYS A 473     -55.307 -41.419 -16.108  1.00 28.71           C
ANISOU 3639  C   LYS A 473     2770   4436   3702    328    899    620       C
ATOM   3640  O   LYS A 473     -54.332 -41.723 -15.427  1.00 28.32           O
ANISOU 3640  O   LYS A 473     2794   4371   3594    330    903    622       O
ATOM   3641  CB  LYS A 473     -56.844 -43.355 -15.876  1.00 31.21           C
ANISOU 3641  CB  LYS A 473     2917   4788   4153    231    982    762       C
ATOM   3642  CG  LYS A 473     -57.998 -44.136 -16.488  1.00 34.33           C
ANISOU 3642  CG  LYS A 473     3185   5190   4670    161    990    808       C
ATOM   3643  CD  LYS A 473     -58.691 -45.045 -15.468  1.00 37.72           C
ANISOU 3643  CD  LYS A 473     3545   5659   5127    143   1091    912       C
ATOM   3644  CE  LYS A 473     -59.221 -44.277 -14.252  1.00 40.29           C
ANISOU 3644  CE  LYS A 473     3868   6076   5365    245   1185    945       C
ATOM   3645  NZ  LYS A 473     -58.201 -44.151 -13.162  1.00 41.13           N
ANISOU 3645  NZ  LYS A 473     4088   6188   5350    303   1215    948       N
ATOM   3646  N   PRO A 474     -55.766 -40.157 -16.192  1.00 28.48           N
ANISOU 3646  N   PRO A 474     2742   4437   3642    401    902    575       N
ATOM   3647  CA  PRO A 474     -55.121 -39.117 -15.385  1.00 28.04           C
ANISOU 3647  CA  PRO A 474     2780   4392   3482    484    914    525       C
ATOM   3648  C   PRO A 474     -55.148 -39.434 -13.891  1.00 28.48           C
ANISOU 3648  C   PRO A 474     2851   4507   3462    528    994    572       C
ATOM   3649  O   PRO A 474     -56.148 -39.959 -13.391  1.00 28.66           O
ANISOU 3649  O   PRO A 474     2794   4588   3507    533   1066    646       O
ATOM   3650  CB  PRO A 474     -55.966 -37.869 -15.669  1.00 28.47           C
ANISOU 3650  CB  PRO A 474     2809   4475   3534    556    923    489       C
ATOM   3651  CG  PRO A 474     -56.613 -38.130 -16.970  1.00 28.91           C
ANISOU 3651  CG  PRO A 474     2785   4513   3687    504    879    496       C
ATOM   3652  CD  PRO A 474     -56.837 -39.608 -17.043  1.00 28.84           C
ANISOU 3652  CD  PRO A 474     2710   4504   3745    415    889    564       C
ATOM   3653  N   TYR A 475     -54.059 -39.124 -13.192  1.00 27.94           N
ANISOU 3653  N   TYR A 475     2882   4429   3306    562    981    532       N
ATOM   3654  CA  TYR A 475     -54.037 -39.229 -11.732  1.00 28.63           C
ANISOU 3654  CA  TYR A 475     2997   4582   3298    626   1052    565       C
ATOM   3655  C   TYR A 475     -54.945 -38.161 -11.131  1.00 29.49           C
ANISOU 3655  C   TYR A 475     3092   4758   3356    727   1110    547       C
ATOM   3656  O   TYR A 475     -54.969 -37.018 -11.602  1.00 28.79           O
ANISOU 3656  O   TYR A 475     3030   4646   3264    765   1075    472       O
ATOM   3657  CB  TYR A 475     -52.613 -39.080 -11.178  1.00 28.16           C
ANISOU 3657  CB  TYR A 475     3046   4499   3153    642   1010    511       C
ATOM   3658  CG  TYR A 475     -51.748 -40.309 -11.355  1.00 27.48           C
ANISOU 3658  CG  TYR A 475     2976   4371   3095    564    978    551       C
ATOM   3659  CD1 TYR A 475     -50.562 -40.256 -12.083  1.00 26.03           C
ANISOU 3659  CD1 TYR A 475     2847   4114   2927    517    892    491       C
ATOM   3660  CD2 TYR A 475     -52.113 -41.525 -10.789  1.00 28.25           C
ANISOU 3660  CD2 TYR A 475     3030   4499   3204    540   1039    651       C
ATOM   3661  CE1 TYR A 475     -49.760 -41.389 -12.243  1.00 25.13           C
ANISOU 3661  CE1 TYR A 475     2747   3962   2837    454    865    526       C
ATOM   3662  CE2 TYR A 475     -51.326 -42.658 -10.946  1.00 27.59           C
ANISOU 3662  CE2 TYR A 475     2964   4371   3148    475   1013    689       C
ATOM   3663  CZ  TYR A 475     -50.151 -42.584 -11.674  1.00 26.51           C
ANISOU 3663  CZ  TYR A 475     2884   4164   3023    434    924    623       C
ATOM   3664  OH  TYR A 475     -49.374 -43.712 -11.825  1.00 26.02           O
ANISOU 3664  OH  TYR A 475     2839   4059   2988    377    900    660       O
ATOM   3665  N   THR A 476     -55.697 -38.549 -10.100  1.00 30.64           N
ANISOU 3665  N   THR A 476     3196   4984   3462    772   1203    619       N
ATOM   3666  CA  THR A 476     -56.658 -37.659  -9.440  1.00 31.84           C
ANISOU 3666  CA  THR A 476     3324   5211   3561    875   1273    614       C
ATOM   3667  C   THR A 476     -56.121 -37.044  -8.145  1.00 32.09           C
ANISOU 3667  C   THR A 476     3450   5290   3452    975   1302    572       C
ATOM   3668  O   THR A 476     -56.752 -36.153  -7.574  1.00 32.91           O
ANISOU 3668  O   THR A 476     3557   5449   3497   1073   1351    546       O
ATOM   3669  CB  THR A 476     -57.978 -38.401  -9.133  1.00 33.01           C
ANISOU 3669  CB  THR A 476     3354   5430   3757    870   1368    725       C
ATOM   3670  OG1 THR A 476     -57.701 -39.568  -8.350  1.00 34.50           O
ANISOU 3670  OG1 THR A 476     3544   5642   3922    842   1417    809       O
ATOM   3671  CG2 THR A 476     -58.667 -38.813 -10.428  1.00 33.34           C
ANISOU 3671  CG2 THR A 476     3294   5434   3938    783   1334    749       C
ATOM   3672  N   SER A 477     -54.967 -37.519  -7.680  1.00 31.46           N
ANISOU 3672  N   SER A 477     3446   5192   3315    956   1269    561       N
ATOM   3673  CA  SER A 477     -54.309 -36.939  -6.509  1.00 31.80           C
ANISOU 3673  CA  SER A 477     3584   5277   3221   1047   1277    505       C
ATOM   3674  C   SER A 477     -52.819 -37.254  -6.518  1.00 30.78           C
ANISOU 3674  C   SER A 477     3536   5095   3062   1002   1196    460       C
ATOM   3675  O   SER A 477     -52.361 -38.137  -7.248  1.00 29.58           O
ANISOU 3675  O   SER A 477     3365   4887   2988    907   1155    496       O
ATOM   3676  CB  SER A 477     -54.929 -37.472  -5.211  1.00 33.04           C
ANISOU 3676  CB  SER A 477     3719   5541   3295   1118   1385    593       C
ATOM   3677  OG  SER A 477     -54.532 -38.814  -4.969  1.00 33.35           O
ANISOU 3677  OG  SER A 477     3747   5581   3345   1059   1401    684       O
ATOM   3678  N   PHE A 478     -52.070 -36.542  -5.685  1.00 31.01           N
ANISOU 3678  N   PHE A 478     3656   5147   2980   1075   1173    379       N
ATOM   3679  CA  PHE A 478     -50.643 -36.815  -5.530  1.00 30.70           C
ANISOU 3679  CA  PHE A 478     3690   5075   2901   1044   1098    335       C
ATOM   3680  C   PHE A 478     -50.412 -38.134  -4.796  1.00 31.25           C
ANISOU 3680  C   PHE A 478     3752   5193   2927   1036   1140    436       C
ATOM   3681  O   PHE A 478     -49.455 -38.838  -5.093  1.00 30.49           O
ANISOU 3681  O   PHE A 478     3677   5054   2854    972   1085    445       O
ATOM   3682  CB  PHE A 478     -49.937 -35.664  -4.818  1.00 31.07           C
ANISOU 3682  CB  PHE A 478     3830   5134   2843   1124   1057    212       C
ATOM   3683  CG  PHE A 478     -49.884 -34.408  -5.632  1.00 30.87           C
ANISOU 3683  CG  PHE A 478     3824   5032   2872   1118   1003    109       C
ATOM   3684  CD1 PHE A 478     -50.889 -33.456  -5.526  1.00 32.20           C
ANISOU 3684  CD1 PHE A 478     3980   5222   3033   1191   1050     82       C
ATOM   3685  CD2 PHE A 478     -48.846 -34.188  -6.525  1.00 30.61           C
ANISOU 3685  CD2 PHE A 478     3822   4906   2903   1042    910     46       C
ATOM   3686  CE1 PHE A 478     -50.848 -32.295  -6.284  1.00 31.90           C
ANISOU 3686  CE1 PHE A 478     3965   5108   3048   1190   1004     -7       C
ATOM   3687  CE2 PHE A 478     -48.800 -33.027  -7.287  1.00 30.00           C
ANISOU 3687  CE2 PHE A 478     3765   4753   2879   1037    868    -39       C
ATOM   3688  CZ  PHE A 478     -49.804 -32.081  -7.160  1.00 30.58           C
ANISOU 3688  CZ  PHE A 478     3831   4844   2944   1112    915    -65       C
ATOM   3689  N   GLU A 479     -51.298 -38.479  -3.863  1.00 32.63           N
ANISOU 3689  N   GLU A 479     3896   5459   3043   1102   1240    518       N
ATOM   3690  CA  GLU A 479     -51.220 -39.777  -3.189  1.00 33.56           C
ANISOU 3690  CA  GLU A 479     4000   5621   3129   1096   1295    634       C
ATOM   3691  C   GLU A 479     -51.431 -40.948  -4.157  1.00 33.17           C
ANISOU 3691  C   GLU A 479     3878   5505   3220    977   1296    725       C
ATOM   3692  O   GLU A 479     -50.782 -41.988  -4.015  1.00 33.01           O
ANISOU 3692  O   GLU A 479     3872   5469   3202    938   1288    784       O
ATOM   3693  CB  GLU A 479     -52.198 -39.853  -2.010  1.00 35.31           C
ANISOU 3693  CB  GLU A 479     4200   5956   3262   1195   1414    710       C
ATOM   3694  CG  GLU A 479     -51.819 -38.919  -0.863  1.00 36.67           C
ANISOU 3694  CG  GLU A 479     4458   6204   3270   1322   1413    625       C
ATOM   3695  CD  GLU A 479     -52.592 -39.177   0.421  1.00 40.13           C
ANISOU 3695  CD  GLU A 479     4887   6765   3597   1429   1533    711       C
ATOM   3696  OE1 GLU A 479     -53.514 -40.023   0.427  1.00 40.57           O
ANISOU 3696  OE1 GLU A 479     4860   6845   3709   1404   1627    843       O
ATOM   3697  OE2 GLU A 479     -52.267 -38.521   1.432  1.00 41.99           O
ANISOU 3697  OE2 GLU A 479     5198   7073   3686   1541   1533    645       O
ATOM   3698  N   GLU A 480     -52.310 -40.783  -5.148  1.00 32.93           N
ANISOU 3698  N   GLU A 480     3771   5435   3306    923   1301    732       N
ATOM   3699  CA  GLU A 480     -52.477 -41.819  -6.175  1.00 32.70           C
ANISOU 3699  CA  GLU A 480     3674   5334   3414    807   1286    797       C
ATOM   3700  C   GLU A 480     -51.196 -42.006  -6.990  1.00 31.19           C
ANISOU 3700  C   GLU A 480     3537   5055   3260    736   1178    736       C
ATOM   3701  O   GLU A 480     -50.805 -43.135  -7.281  1.00 30.99           O
ANISOU 3701  O   GLU A 480     3500   4987   3289    666   1167    795       O
ATOM   3702  CB  GLU A 480     -53.638 -41.519  -7.122  1.00 32.93           C
ANISOU 3702  CB  GLU A 480     3611   5345   3555    768   1298    802       C
ATOM   3703  CG  GLU A 480     -54.031 -42.743  -7.962  1.00 34.38           C
ANISOU 3703  CG  GLU A 480     3714   5475   3875    657   1301    883       C
ATOM   3704  CD  GLU A 480     -55.122 -42.478  -8.989  1.00 36.99           C
ANISOU 3704  CD  GLU A 480     3948   5788   4318    614   1297    879       C
ATOM   3705  OE1 GLU A 480     -55.675 -43.469  -9.507  1.00 39.86           O
ANISOU 3705  OE1 GLU A 480     4231   6124   4790    532   1314    950       O
ATOM   3706  OE2 GLU A 480     -55.419 -41.303  -9.295  1.00 37.22           O
ANISOU 3706  OE2 GLU A 480     3981   5828   4331    662   1275    805       O
ATOM   3707  N   LEU A 481     -50.559 -40.895  -7.355  1.00 30.11           N
ANISOU 3707  N   LEU A 481     3455   4887   3097    754   1103    618       N
ATOM   3708  CA  LEU A 481     -49.283 -40.924  -8.083  1.00 28.91           C
ANISOU 3708  CA  LEU A 481     3354   4658   2972    696   1003    554       C
ATOM   3709  C   LEU A 481     -48.197 -41.711  -7.345  1.00 28.94           C
ANISOU 3709  C   LEU A 481     3414   4676   2908    702    989    579       C
ATOM   3710  O   LEU A 481     -47.575 -42.603  -7.923  1.00 28.06           O
ANISOU 3710  O   LEU A 481     3299   4508   2854    631    951    608       O
ATOM   3711  CB  LEU A 481     -48.790 -39.495  -8.362  1.00 28.40           C
ANISOU 3711  CB  LEU A 481     3344   4567   2880    729    940    427       C
ATOM   3712  CG  LEU A 481     -47.346 -39.321  -8.848  1.00 27.71           C
ANISOU 3712  CG  LEU A 481     3318   4414   2796    687    843    351       C
ATOM   3713  CD1 LEU A 481     -47.105 -40.081 -10.155  1.00 25.69           C
ANISOU 3713  CD1 LEU A 481     3026   4079   2655    585    800    379       C
ATOM   3714  CD2 LEU A 481     -47.011 -37.842  -9.008  1.00 27.52           C
ANISOU 3714  CD2 LEU A 481     3342   4365   2750    723    796    233       C
ATOM   3715  N   THR A 482     -47.972 -41.380  -6.076  1.00 29.66           N
ANISOU 3715  N   THR A 482     3555   4845   2870    795   1017    566       N
ATOM   3716  CA  THR A 482     -46.843 -41.939  -5.325  1.00 29.72           C
ANISOU 3716  CA  THR A 482     3623   4876   2794    818    990    573       C
ATOM   3717  C   THR A 482     -47.171 -43.241  -4.594  1.00 30.68           C
ANISOU 3717  C   THR A 482     3722   5042   2893    829   1070    709       C
ATOM   3718  O   THR A 482     -46.274 -44.027  -4.302  1.00 30.56           O
ANISOU 3718  O   THR A 482     3742   5023   2848    822   1047    740       O
ATOM   3719  CB  THR A 482     -46.328 -40.948  -4.267  1.00 30.43           C
ANISOU 3719  CB  THR A 482     3785   5034   2744    918    970    484       C
ATOM   3720  OG1 THR A 482     -47.322 -40.781  -3.244  1.00 30.65           O
ANISOU 3720  OG1 THR A 482     3802   5154   2689   1008   1065    530       O
ATOM   3721  CG2 THR A 482     -45.996 -39.602  -4.902  1.00 29.81           C
ANISOU 3721  CG2 THR A 482     3734   4904   2690    910    897    350       C
ATOM   3722  N   GLY A 483     -48.447 -43.455  -4.280  1.00 31.72           N
ANISOU 3722  N   GLY A 483     3795   5217   3040    849   1168    792       N
ATOM   3723  CA  GLY A 483     -48.862 -44.601  -3.464  1.00 33.03           C
ANISOU 3723  CA  GLY A 483     3938   5431   3180    869   1261    929       C
ATOM   3724  C   GLY A 483     -48.455 -44.486  -2.001  1.00 34.54           C
ANISOU 3724  C   GLY A 483     4197   5724   3203    986   1295    939       C
ATOM   3725  O   GLY A 483     -48.447 -45.481  -1.268  1.00 35.06           O
ANISOU 3725  O   GLY A 483     4266   5828   3228   1011   1358   1051       O
ATOM   3726  N   GLU A 484     -48.130 -43.270  -1.569  1.00 35.01           N
ANISOU 3726  N   GLU A 484     4311   5829   3163   1062   1253    823       N
ATOM   3727  CA  GLU A 484     -47.742 -43.009  -0.182  1.00 36.33           C
ANISOU 3727  CA  GLU A 484     4546   6101   3158   1183   1273    810       C
ATOM   3728  C   GLU A 484     -48.202 -41.606   0.225  1.00 36.95           C
ANISOU 3728  C   GLU A 484     4646   6231   3160   1267   1277    706       C
ATOM   3729  O   GLU A 484     -48.890 -40.933  -0.544  1.00 36.50           O
ANISOU 3729  O   GLU A 484     4548   6131   3190   1232   1276    664       O
ATOM   3730  CB  GLU A 484     -46.228 -43.205  -0.004  1.00 36.14           C
ANISOU 3730  CB  GLU A 484     4592   6066   3074   1184   1177    754       C
ATOM   3731  CG  GLU A 484     -45.351 -42.408  -0.961  1.00 35.02           C
ANISOU 3731  CG  GLU A 484     4472   5841   2993   1121   1055    615       C
ATOM   3732  CD  GLU A 484     -45.185 -40.963  -0.540  1.00 36.00           C
ANISOU 3732  CD  GLU A 484     4645   6001   3032   1193   1012    475       C
ATOM   3733  OE1 GLU A 484     -44.389 -40.704   0.392  1.00 35.41           O
ANISOU 3733  OE1 GLU A 484     4634   5991   2828   1269    973    418       O
ATOM   3734  OE2 GLU A 484     -45.849 -40.086  -1.142  1.00 36.49           O
ANISOU 3734  OE2 GLU A 484     4683   6025   3156   1175   1014    419       O
ATOM   3735  N   LYS A 485     -47.824 -41.170   1.425  1.00 37.86           N
ANISOU 3735  N   LYS A 485     4830   6441   3113   1381   1279    662       N
ATOM   3736  CA  LYS A 485     -48.348 -39.932   1.995  1.00 38.82           C
ANISOU 3736  CA  LYS A 485     4978   6623   3148   1479   1299    574       C
ATOM   3737  C   LYS A 485     -47.342 -38.786   2.038  1.00 38.27           C
ANISOU 3737  C   LYS A 485     4985   6535   3022   1504   1184    399       C
ATOM   3738  O   LYS A 485     -47.692 -37.652   1.729  1.00 38.18           O
ANISOU 3738  O   LYS A 485     4979   6496   3032   1518   1165    301       O
ATOM   3739  CB  LYS A 485     -48.849 -40.198   3.416  1.00 40.62           C
ANISOU 3739  CB  LYS A 485     5227   6985   3222   1607   1401    649       C
ATOM   3740  CG  LYS A 485     -49.809 -41.379   3.545  1.00 42.66           C
ANISOU 3740  CG  LYS A 485     5411   7269   3529   1588   1526    834       C
ATOM   3741  CD  LYS A 485     -51.208 -41.033   3.049  1.00 44.73           C
ANISOU 3741  CD  LYS A 485     5589   7522   3886   1569   1605    869       C
ATOM   3742  CE  LYS A 485     -52.294 -41.750   3.855  1.00 47.05           C
ANISOU 3742  CE  LYS A 485     5830   7906   4143   1626   1756   1026       C
ATOM   3743  NZ  LYS A 485     -53.643 -41.156   3.600  1.00 48.81           N
ANISOU 3743  NZ  LYS A 485     5975   8146   4423   1641   1831   1037       N
ATOM   3744  N   GLU A 486     -46.102 -39.078   2.426  1.00 38.23           N
ANISOU 3744  N   GLU A 486     5035   6542   2948   1511   1109    363       N
ATOM   3745  CA  GLU A 486     -45.131 -38.025   2.754  1.00 38.34           C
ANISOU 3745  CA  GLU A 486     5122   6560   2884   1552   1006    198       C
ATOM   3746  C   GLU A 486     -44.686 -37.213   1.536  1.00 36.77           C
ANISOU 3746  C   GLU A 486     4917   6239   2815   1456    915     87       C
ATOM   3747  O   GLU A 486     -44.821 -35.988   1.526  1.00 36.83           O
ANISOU 3747  O   GLU A 486     4952   6228   2813   1488    887    -31       O
ATOM   3748  CB  GLU A 486     -43.914 -38.611   3.475  1.00 38.77           C
ANISOU 3748  CB  GLU A 486     5227   6667   2835   1584    946    192       C
ATOM   3749  CG  GLU A 486     -42.924 -37.556   3.964  1.00 39.97           C
ANISOU 3749  CG  GLU A 486     5450   6839   2897   1634    839     19       C
ATOM   3750  CD  GLU A 486     -41.842 -38.128   4.863  1.00 41.31           C
ANISOU 3750  CD  GLU A 486     5666   7090   2940   1689    787     17       C
ATOM   3751  OE1 GLU A 486     -40.652 -38.033   4.495  1.00 41.09           O
ANISOU 3751  OE1 GLU A 486     5652   7016   2945   1634    677    -63       O
ATOM   3752  OE2 GLU A 486     -42.180 -38.671   5.934  1.00 42.98           O
ANISOU 3752  OE2 GLU A 486     5898   7415   3019   1792    857     99       O
ATOM   3753  N   MET A 487     -44.149 -37.887   0.522  1.00 35.21           N
ANISOU 3753  N   MET A 487     4685   5955   2737   1343    871    126       N
ATOM   3754  CA  MET A 487     -43.755 -37.210  -0.715  1.00 33.96           C
ANISOU 3754  CA  MET A 487     4516   5681   2706   1249    795     40       C
ATOM   3755  C   MET A 487     -44.959 -36.566  -1.394  1.00 33.41           C
ANISOU 3755  C   MET A 487     4404   5569   2721   1236    847     43       C
ATOM   3756  O   MET A 487     -44.846 -35.483  -1.967  1.00 32.83           O
ANISOU 3756  O   MET A 487     4347   5430   2698   1217    799    -61       O
ATOM   3757  CB  MET A 487     -43.081 -38.179  -1.685  1.00 33.06           C
ANISOU 3757  CB  MET A 487     4369   5492   2700   1139    753     98       C
ATOM   3758  CG  MET A 487     -41.733 -38.690  -1.212  1.00 33.80           C
ANISOU 3758  CG  MET A 487     4502   5612   2729   1144    683     78       C
ATOM   3759  SD  MET A 487     -40.937 -39.722  -2.451  1.00 33.99           S
ANISOU 3759  SD  MET A 487     4488   5539   2887   1018    634    135       S
ATOM   3760  CE  MET A 487     -42.097 -41.092  -2.532  1.00 34.27           C
ANISOU 3760  CE  MET A 487     4466   5586   2967   1001    749    315       C
ATOM   3761  N   ALA A 488     -46.109 -37.233  -1.322  1.00 33.35           N
ANISOU 3761  N   ALA A 488     4340   5598   2732   1246    947    164       N
ATOM   3762  CA  ALA A 488     -47.337 -36.709  -1.915  1.00 33.06           C
ANISOU 3762  CA  ALA A 488     4253   5537   2773   1241   1002    179       C
ATOM   3763  C   ALA A 488     -47.726 -35.363  -1.313  1.00 33.78           C
ANISOU 3763  C   ALA A 488     4386   5663   2785   1340   1012     75       C
ATOM   3764  O   ALA A 488     -48.138 -34.452  -2.035  1.00 33.36           O
ANISOU 3764  O   ALA A 488     4322   5548   2804   1325    998     15       O
ATOM   3765  CB  ALA A 488     -48.470 -37.704  -1.765  1.00 33.45           C
ANISOU 3765  CB  ALA A 488     4229   5635   2846   1241   1111    328       C
ATOM   3766  N   ALA A 489     -47.594 -35.247   0.007  1.00 34.74           N
ANISOU 3766  N   ALA A 489     4560   5883   2757   1446   1036     54       N
ATOM   3767  CA  ALA A 489     -47.917 -34.011   0.715  1.00 35.67           C
ANISOU 3767  CA  ALA A 489     4729   6042   2783   1553   1046    -52       C
ATOM   3768  C   ALA A 489     -46.973 -32.876   0.337  1.00 35.12           C
ANISOU 3768  C   ALA A 489     4719   5889   2736   1530    935   -214       C
ATOM   3769  O   ALA A 489     -47.411 -31.741   0.147  1.00 35.22           O
ANISOU 3769  O   ALA A 489     4749   5865   2769   1564    934   -298       O
ATOM   3770  CB  ALA A 489     -47.900 -34.241   2.232  1.00 36.89           C
ANISOU 3770  CB  ALA A 489     4929   6327   2760   1676   1091    -38       C
ATOM   3771  N   GLU A 490     -45.684 -33.181   0.223  1.00 34.85           N
ANISOU 3771  N   GLU A 490     4714   5822   2705   1473    845   -254       N
ATOM   3772  CA  GLU A 490     -44.704 -32.179  -0.197  1.00 34.71           C
ANISOU 3772  CA  GLU A 490     4743   5718   2726   1435    739   -401       C
ATOM   3773  C   GLU A 490     -44.996 -31.722  -1.633  1.00 33.58           C
ANISOU 3773  C   GLU A 490     4561   5454   2744   1345    726   -404       C
ATOM   3774  O   GLU A 490     -44.930 -30.527  -1.937  1.00 33.37           O
ANISOU 3774  O   GLU A 490     4567   5360   2753   1351    690   -513       O
ATOM   3775  CB  GLU A 490     -43.276 -32.723  -0.090  1.00 34.68           C
ANISOU 3775  CB  GLU A 490     4763   5711   2703   1387    650   -427       C
ATOM   3776  CG  GLU A 490     -42.816 -33.111   1.326  1.00 37.03           C
ANISOU 3776  CG  GLU A 490     5106   6131   2832   1482    645   -437       C
ATOM   3777  CD  GLU A 490     -42.648 -31.927   2.278  1.00 40.07           C
ANISOU 3777  CD  GLU A 490     5564   6557   3105   1581    610   -587       C
ATOM   3778  OE1 GLU A 490     -42.460 -32.165   3.491  1.00 43.46           O
ANISOU 3778  OE1 GLU A 490     6032   7099   3380   1678    615   -596       O
ATOM   3779  OE2 GLU A 490     -42.697 -30.760   1.832  1.00 41.54           O
ANISOU 3779  OE2 GLU A 490     5770   6661   3353   1566    576   -697       O
ATOM   3780  N   LEU A 491     -45.339 -32.669  -2.504  1.00 32.57           N
ANISOU 3780  N   LEU A 491     4365   5298   2712   1265    755   -287       N
ATOM   3781  CA  LEU A 491     -45.679 -32.345  -3.892  1.00 31.64           C
ANISOU 3781  CA  LEU A 491     4207   5078   2739   1185    745   -279       C
ATOM   3782  C   LEU A 491     -46.951 -31.501  -3.987  1.00 32.42           C
ANISOU 3782  C   LEU A 491     4288   5178   2853   1245    809   -286       C
ATOM   3783  O   LEU A 491     -46.999 -30.536  -4.755  1.00 32.17           O
ANISOU 3783  O   LEU A 491     4266   5061   2895   1226    779   -352       O
ATOM   3784  CB  LEU A 491     -45.820 -33.616  -4.731  1.00 30.61           C
ANISOU 3784  CB  LEU A 491     4007   4927   2696   1095    762   -154       C
ATOM   3785  CG  LEU A 491     -44.503 -34.310  -5.088  1.00 30.27           C
ANISOU 3785  CG  LEU A 491     3976   4846   2680   1016    687   -156       C
ATOM   3786  CD1 LEU A 491     -44.770 -35.684  -5.687  1.00 29.79           C
ANISOU 3786  CD1 LEU A 491     3853   4780   2688    947    718    -27       C
ATOM   3787  CD2 LEU A 491     -43.673 -33.460  -6.052  1.00 29.59           C
ANISOU 3787  CD2 LEU A 491     3912   4653   2677    953    604   -252       C
ATOM   3788  N   LYS A 492     -47.971 -31.849  -3.205  1.00 33.38           N
ANISOU 3788  N   LYS A 492     4383   5395   2903   1323    900   -215       N
ATOM   3789  CA  LYS A 492     -49.211 -31.071  -3.203  1.00 34.27           C
ANISOU 3789  CA  LYS A 492     4474   5523   3023   1392    967   -218       C
ATOM   3790  C   LYS A 492     -48.966 -29.627  -2.764  1.00 34.82           C
ANISOU 3790  C   LYS A 492     4623   5566   3040   1468    933   -364       C
ATOM   3791  O   LYS A 492     -49.551 -28.703  -3.326  1.00 34.65           O
ANISOU 3791  O   LYS A 492     4597   5489   3078   1485    942   -403       O
ATOM   3792  CB  LYS A 492     -50.288 -31.712  -2.323  1.00 35.42           C
ANISOU 3792  CB  LYS A 492     4576   5787   3093   1468   1076   -115       C
ATOM   3793  CG  LYS A 492     -51.646 -31.009  -2.441  1.00 36.89           C
ANISOU 3793  CG  LYS A 492     4722   5992   3302   1534   1151   -103       C
ATOM   3794  CD  LYS A 492     -52.786 -31.816  -1.842  1.00 39.27           C
ANISOU 3794  CD  LYS A 492     4952   6401   3567   1582   1266     25       C
ATOM   3795  CE  LYS A 492     -54.096 -31.027  -1.874  1.00 40.65           C
ANISOU 3795  CE  LYS A 492     5086   6604   3754   1661   1339     27       C
ATOM   3796  NZ  LYS A 492     -54.395 -30.483  -3.238  1.00 40.84           N
ANISOU 3796  NZ  LYS A 492     5072   6530   3916   1598   1298      5       N
ATOM   3797  N   ALA A 493     -48.101 -29.434  -1.773  1.00 35.42           N
ANISOU 3797  N   ALA A 493     4771   5681   3007   1514    891   -446       N
ATOM   3798  CA  ALA A 493     -47.777 -28.088  -1.300  1.00 36.38           C
ANISOU 3798  CA  ALA A 493     4972   5771   3079   1582    850   -598       C
ATOM   3799  C   ALA A 493     -47.024 -27.285  -2.370  1.00 35.71           C
ANISOU 3799  C   ALA A 493     4909   5545   3114   1496    764   -685       C
ATOM   3800  O   ALA A 493     -47.235 -26.080  -2.507  1.00 36.33           O
ANISOU 3800  O   ALA A 493     5027   5561   3216   1534    755   -777       O
ATOM   3801  CB  ALA A 493     -46.974 -28.152  -0.004  1.00 37.25           C
ANISOU 3801  CB  ALA A 493     5149   5960   3042   1647    814   -668       C
ATOM   3802  N   LEU A 494     -46.163 -27.956  -3.131  1.00 34.83           N
ANISOU 3802  N   LEU A 494     4774   5383   3078   1384    707   -650       N
ATOM   3803  CA  LEU A 494     -45.396 -27.301  -4.190  1.00 34.29           C
ANISOU 3803  CA  LEU A 494     4720   5185   3126   1298    633   -716       C
ATOM   3804  C   LEU A 494     -46.236 -26.994  -5.439  1.00 33.80           C
ANISOU 3804  C   LEU A 494     4610   5047   3184   1262    667   -663       C
ATOM   3805  O   LEU A 494     -46.165 -25.886  -5.973  1.00 34.06           O
ANISOU 3805  O   LEU A 494     4675   4987   3280   1260    642   -738       O
ATOM   3806  CB  LEU A 494     -44.186 -28.156  -4.584  1.00 33.52           C
ANISOU 3806  CB  LEU A 494     4608   5065   3062   1197    565   -694       C
ATOM   3807  CG  LEU A 494     -43.079 -28.277  -3.534  1.00 34.10           C
ANISOU 3807  CG  LEU A 494     4731   5191   3035   1219    504   -770       C
ATOM   3808  CD1 LEU A 494     -42.084 -29.357  -3.919  1.00 33.13           C
ANISOU 3808  CD1 LEU A 494     4579   5067   2943   1130    456   -715       C
ATOM   3809  CD2 LEU A 494     -42.379 -26.941  -3.328  1.00 35.59           C
ANISOU 3809  CD2 LEU A 494     4986   5310   3228   1231    435   -931       C
ATOM   3810  N   TYR A 495     -47.022 -27.973  -5.892  1.00 33.23           N
ANISOU 3810  N   TYR A 495     4464   5018   3145   1237    722   -533       N
ATOM   3811  CA  TYR A 495     -47.736 -27.891  -7.180  1.00 32.45           C
ANISOU 3811  CA  TYR A 495     4309   4858   3163   1192    741   -473       C
ATOM   3812  C   TYR A 495     -49.211 -27.491  -7.084  1.00 33.59           C
ANISOU 3812  C   TYR A 495     4417   5044   3300   1275    824   -436       C
ATOM   3813  O   TYR A 495     -49.775 -27.007  -8.069  1.00 33.09           O
ANISOU 3813  O   TYR A 495     4326   4923   3325   1262    830   -421       O
ATOM   3814  CB  TYR A 495     -47.655 -29.233  -7.918  1.00 31.23           C
ANISOU 3814  CB  TYR A 495     4086   4712   3067   1099    739   -361       C
ATOM   3815  CG  TYR A 495     -46.306 -29.547  -8.527  1.00 29.39           C
ANISOU 3815  CG  TYR A 495     3872   4411   2884   1003    658   -386       C
ATOM   3816  CD1 TYR A 495     -45.371 -30.312  -7.840  1.00 28.20           C
ANISOU 3816  CD1 TYR A 495     3741   4303   2671    984    626   -386       C
ATOM   3817  CD2 TYR A 495     -45.978 -29.106  -9.809  1.00 28.09           C
ANISOU 3817  CD2 TYR A 495     3703   4144   2825    937    616   -402       C
ATOM   3818  CE1 TYR A 495     -44.135 -30.613  -8.400  1.00 27.42           C
ANISOU 3818  CE1 TYR A 495     3653   4147   2619    900    554   -407       C
ATOM   3819  CE2 TYR A 495     -44.748 -29.403 -10.378  1.00 26.71           C
ANISOU 3819  CE2 TYR A 495     3541   3913   2696    852    549   -420       C
ATOM   3820  CZ  TYR A 495     -43.828 -30.157  -9.666  1.00 26.76           C
ANISOU 3820  CZ  TYR A 495     3563   3963   2643    833    518   -424       C
ATOM   3821  OH  TYR A 495     -42.605 -30.462 -10.218  1.00 26.31           O
ANISOU 3821  OH  TYR A 495     3512   3854   2630    754    453   -440       O
ATOM   3822  N   SER A 496     -49.836 -27.748  -5.932  1.00 34.94           N
ANISOU 3822  N   SER A 496     4584   5322   3368   1361    888   -412       N
ATOM   3823  CA  SER A 496     -51.256 -27.434  -5.665  1.00 36.22           C
ANISOU 3823  CA  SER A 496     4707   5545   3511   1452    976   -372       C
ATOM   3824  C   SER A 496     -52.262 -28.328  -6.398  1.00 35.60           C
ANISOU 3824  C   SER A 496     4521   5498   3508   1409   1028   -240       C
ATOM   3825  O   SER A 496     -53.174 -28.877  -5.770  1.00 36.57           O
ANISOU 3825  O   SER A 496     4591   5719   3585   1459   1109   -162       O
ATOM   3826  CB  SER A 496     -51.582 -25.955  -5.937  1.00 36.90           C
ANISOU 3826  CB  SER A 496     4836   5560   3624   1514    971   -465       C
ATOM   3827  OG  SER A 496     -50.886 -25.111  -5.038  1.00 39.44           O
ANISOU 3827  OG  SER A 496     5253   5867   3864   1573    938   -591       O
ATOM   3828  N   ASP A 497     -52.101 -28.454  -7.714  1.00 34.21           N
ANISOU 3828  N   ASP A 497     4311   5241   3447   1318    983   -216       N
ATOM   3829  CA  ASP A 497     -53.020 -29.202  -8.566  1.00 33.60           C
ANISOU 3829  CA  ASP A 497     4131   5182   3453   1271   1016   -108       C
ATOM   3830  C   ASP A 497     -52.284 -30.368  -9.236  1.00 31.97           C
ANISOU 3830  C   ASP A 497     3898   4945   3303   1151    968    -54       C
ATOM   3831  O   ASP A 497     -51.253 -30.170  -9.886  1.00 31.00           O
ANISOU 3831  O   ASP A 497     3819   4739   3221   1089    893   -105       O
ATOM   3832  CB  ASP A 497     -53.597 -28.250  -9.622  1.00 33.70           C
ANISOU 3832  CB  ASP A 497     4127   5129   3548   1284   1005   -132       C
ATOM   3833  CG  ASP A 497     -54.670 -28.892 -10.498  1.00 34.11           C
ANISOU 3833  CG  ASP A 497     4068   5209   3683   1249   1035    -32       C
ATOM   3834  OD1 ASP A 497     -55.284 -28.139 -11.288  1.00 36.34           O
ANISOU 3834  OD1 ASP A 497     4329   5456   4022   1276   1033    -42       O
ATOM   3835  OD2 ASP A 497     -54.911 -30.116 -10.407  1.00 33.49           O
ANISOU 3835  OD2 ASP A 497     3924   5185   3616   1197   1059     54       O
ATOM   3836  N   ILE A 498     -52.822 -31.578  -9.078  1.00 31.39           N
ANISOU 3836  N   ILE A 498     3752   4937   3239   1121   1014     49       N
ATOM   3837  CA  ILE A 498     -52.257 -32.782  -9.709  1.00 29.98           C
ANISOU 3837  CA  ILE A 498     3542   4730   3119   1012    976    108       C
ATOM   3838  C   ILE A 498     -52.172 -32.650 -11.234  1.00 28.95           C
ANISOU 3838  C   ILE A 498     3386   4515   3100    938    917    101       C
ATOM   3839  O   ILE A 498     -51.281 -33.221 -11.855  1.00 27.79           O
ANISOU 3839  O   ILE A 498     3252   4314   2993    855    859    103       O
ATOM   3840  CB  ILE A 498     -53.073 -34.057  -9.332  1.00 30.29           C
ANISOU 3840  CB  ILE A 498     3498   4846   3166    994   1046    227       C
ATOM   3841  CG1 ILE A 498     -52.419 -35.340  -9.857  1.00 28.91           C
ANISOU 3841  CG1 ILE A 498     3302   4636   3046    887   1008    282       C
ATOM   3842  CG2 ILE A 498     -54.508 -33.957  -9.851  1.00 30.56           C
ANISOU 3842  CG2 ILE A 498     3435   4909   3266   1009   1097    280       C
ATOM   3843  CD1 ILE A 498     -50.998 -35.583  -9.373  1.00 27.29           C
ANISOU 3843  CD1 ILE A 498     3179   4409   2780    870    957    241       C
ATOM   3844  N   ASP A 499     -53.091 -31.892 -11.828  1.00 28.96           N
ANISOU 3844  N   ASP A 499     3351   4507   3146    974    933     95       N
ATOM   3845  CA  ASP A 499     -53.080 -31.667 -13.273  1.00 28.52           C
ANISOU 3845  CA  ASP A 499     3274   4379   3184    920    880     89       C
ATOM   3846  C   ASP A 499     -51.946 -30.754 -13.758  1.00 27.79           C
ANISOU 3846  C   ASP A 499     3269   4191   3098    907    813      1       C
ATOM   3847  O   ASP A 499     -51.796 -30.558 -14.956  1.00 27.53           O
ANISOU 3847  O   ASP A 499     3229   4096   3136    865    769     -2       O
ATOM   3848  CB  ASP A 499     -54.433 -31.114 -13.741  1.00 28.98           C
ANISOU 3848  CB  ASP A 499     3264   4463   3282    974    918    113       C
ATOM   3849  CG  ASP A 499     -55.533 -32.157 -13.714  1.00 30.03           C
ANISOU 3849  CG  ASP A 499     3286   4674   3450    952    969    209       C
ATOM   3850  OD1 ASP A 499     -55.234 -33.373 -13.798  1.00 29.56           O
ANISOU 3850  OD1 ASP A 499     3196   4620   3416    872    959    261       O
ATOM   3851  OD2 ASP A 499     -56.710 -31.750 -13.622  1.00 30.82           O
ANISOU 3851  OD2 ASP A 499     3326   4827   3558   1016   1021    232       O
ATOM   3852  N   VAL A 500     -51.155 -30.199 -12.840  1.00 28.21           N
ANISOU 3852  N   VAL A 500     3403   4235   3080    944    804    -70       N
ATOM   3853  CA  VAL A 500     -49.977 -29.408 -13.209  1.00 27.78           C
ANISOU 3853  CA  VAL A 500     3428   4089   3039    920    740   -154       C
ATOM   3854  C   VAL A 500     -48.659 -30.089 -12.793  1.00 27.00           C
ANISOU 3854  C   VAL A 500     3368   3983   2909    861    695   -173       C
ATOM   3855  O   VAL A 500     -47.578 -29.546 -13.020  1.00 25.92           O
ANISOU 3855  O   VAL A 500     3289   3776   2785    833    640   -241       O
ATOM   3856  CB  VAL A 500     -50.096 -27.974 -12.644  1.00 29.24           C
ANISOU 3856  CB  VAL A 500     3676   4249   3185   1010    753   -241       C
ATOM   3857  CG1 VAL A 500     -48.769 -27.224 -12.711  1.00 29.92           C
ANISOU 3857  CG1 VAL A 500     3846   4245   3277    982    690   -335       C
ATOM   3858  CG2 VAL A 500     -51.172 -27.216 -13.418  1.00 29.65           C
ANISOU 3858  CG2 VAL A 500     3695   4280   3291   1056    780   -225       C
ATOM   3859  N   MET A 501     -48.743 -31.290 -12.218  1.00 26.37           N
ANISOU 3859  N   MET A 501     3253   3973   2794    843    719   -108       N
ATOM   3860  CA  MET A 501     -47.546 -32.076 -11.942  1.00 25.75           C
ANISOU 3860  CA  MET A 501     3203   3890   2692    787    676   -110       C
ATOM   3861  C   MET A 501     -46.771 -32.301 -13.243  1.00 24.70           C
ANISOU 3861  C   MET A 501     3066   3675   2645    698    615   -110       C
ATOM   3862  O   MET A 501     -47.367 -32.511 -14.303  1.00 24.28           O
ANISOU 3862  O   MET A 501     2963   3598   2664    665    617    -64       O
ATOM   3863  CB  MET A 501     -47.913 -33.427 -11.316  1.00 25.78           C
ANISOU 3863  CB  MET A 501     3160   3973   2662    778    720    -19       C
ATOM   3864  CG  MET A 501     -46.727 -34.290 -10.938  1.00 25.79           C
ANISOU 3864  CG  MET A 501     3190   3977   2631    735    682    -14       C
ATOM   3865  SD  MET A 501     -45.588 -33.451  -9.822  1.00 26.08           S
ANISOU 3865  SD  MET A 501     3318   4024   2568    788    641   -124       S
ATOM   3866  CE  MET A 501     -44.286 -34.676  -9.691  1.00 23.60           C
ANISOU 3866  CE  MET A 501     3014   3713   2239    725    593    -94       C
ATOM   3867  N   GLU A 502     -45.446 -32.250 -13.146  1.00 24.37           N
ANISOU 3867  N   GLU A 502     3074   3595   2590    663    560   -162       N
ATOM   3868  CA  GLU A 502     -44.563 -32.366 -14.308  1.00 23.37           C
ANISOU 3868  CA  GLU A 502     2951   3392   2537    586    504   -169       C
ATOM   3869  C   GLU A 502     -44.185 -33.812 -14.576  1.00 22.58           C
ANISOU 3869  C   GLU A 502     2816   3309   2452    523    491   -100       C
ATOM   3870  O   GLU A 502     -44.128 -34.629 -13.651  1.00 23.15           O
ANISOU 3870  O   GLU A 502     2885   3444   2468    535    511    -67       O
ATOM   3871  CB  GLU A 502     -43.290 -31.554 -14.087  1.00 23.79           C
ANISOU 3871  CB  GLU A 502     3067   3393   2578    578    451   -261       C
ATOM   3872  CG  GLU A 502     -43.516 -30.056 -14.070  1.00 24.49           C
ANISOU 3872  CG  GLU A 502     3197   3434   2676    626    455   -337       C
ATOM   3873  CD  GLU A 502     -42.271 -29.300 -13.670  1.00 26.20           C
ANISOU 3873  CD  GLU A 502     3472   3602   2880    615    404   -434       C
ATOM   3874  OE1 GLU A 502     -41.525 -28.876 -14.577  1.00 25.50           O
ANISOU 3874  OE1 GLU A 502     3395   3431   2862    562    367   -457       O
ATOM   3875  OE2 GLU A 502     -42.027 -29.146 -12.450  1.00 27.07           O
ANISOU 3875  OE2 GLU A 502     3616   3760   2912    659    400   -487       O
ATOM   3876  N   LEU A 503     -43.898 -34.111 -15.840  1.00 21.68           N
ANISOU 3876  N   LEU A 503     2683   3140   2414    460    460    -79       N
ATOM   3877  CA  LEU A 503     -43.612 -35.473 -16.281  1.00 21.19           C
ANISOU 3877  CA  LEU A 503     2589   3083   2380    400    447    -16       C
ATOM   3878  C   LEU A 503     -42.360 -36.075 -15.636  1.00 21.12           C
ANISOU 3878  C   LEU A 503     2612   3084   2330    379    416    -29       C
ATOM   3879  O   LEU A 503     -42.428 -37.150 -15.049  1.00 20.89           O
ANISOU 3879  O   LEU A 503     2566   3101   2271    376    436     25       O
ATOM   3880  CB  LEU A 503     -43.481 -35.523 -17.811  1.00 20.58           C
ANISOU 3880  CB  LEU A 503     2493   2943   2384    346    414     -6       C
ATOM   3881  CG  LEU A 503     -43.135 -36.879 -18.436  1.00 19.87           C
ANISOU 3881  CG  LEU A 503     2375   2845   2331    284    394     47       C
ATOM   3882  CD1 LEU A 503     -44.218 -37.915 -18.112  1.00 19.97           C
ANISOU 3882  CD1 LEU A 503     2333   2909   2347    282    437    119       C
ATOM   3883  CD2 LEU A 503     -42.922 -36.738 -19.953  1.00 18.52           C
ANISOU 3883  CD2 LEU A 503     2197   2614   2226    244    359     42       C
ATOM   3884  N   TYR A 504     -41.218 -35.400 -15.746  1.00 21.22           N
ANISOU 3884  N   TYR A 504     2667   3054   2343    367    369    -97       N
ATOM   3885  CA  TYR A 504     -39.955 -36.004 -15.292  1.00 21.36           C
ANISOU 3885  CA  TYR A 504     2705   3081   2330    343    331   -109       C
ATOM   3886  C   TYR A 504     -39.922 -36.338 -13.784  1.00 21.76           C
ANISOU 3886  C   TYR A 504     2773   3210   2285    396    349   -108       C
ATOM   3887  O   TYR A 504     -39.656 -37.484 -13.420  1.00 21.67           O
ANISOU 3887  O   TYR A 504     2751   3234   2250    386    353    -54       O
ATOM   3888  CB  TYR A 504     -38.730 -35.165 -15.687  1.00 21.21           C
ANISOU 3888  CB  TYR A 504     2719   3004   2337    316    277   -185       C
ATOM   3889  CG  TYR A 504     -37.445 -35.822 -15.238  1.00 22.66           C
ANISOU 3889  CG  TYR A 504     2913   3205   2492    295    236   -196       C
ATOM   3890  CD1 TYR A 504     -37.062 -37.049 -15.765  1.00 23.59           C
ANISOU 3890  CD1 TYR A 504     3006   3321   2635    254    227   -135       C
ATOM   3891  CD2 TYR A 504     -36.642 -35.251 -14.254  1.00 25.37           C
ANISOU 3891  CD2 TYR A 504     3288   3571   2779    321    204   -269       C
ATOM   3892  CE1 TYR A 504     -35.908 -37.683 -15.349  1.00 25.01           C
ANISOU 3892  CE1 TYR A 504     3193   3521   2787    242    191   -139       C
ATOM   3893  CE2 TYR A 504     -35.468 -35.886 -13.832  1.00 26.43           C
ANISOU 3893  CE2 TYR A 504     3426   3732   2885    306    162   -277       C
ATOM   3894  CZ  TYR A 504     -35.115 -37.101 -14.389  1.00 25.55           C
ANISOU 3894  CZ  TYR A 504     3289   3618   2800    269    158   -208       C
ATOM   3895  OH  TYR A 504     -33.967 -37.756 -13.996  1.00 28.16           O
ANISOU 3895  OH  TYR A 504     3620   3976   3103    261    118   -211       O
ATOM   3896  N   PRO A 505     -40.191 -35.351 -12.908  1.00 22.28           N
ANISOU 3896  N   PRO A 505     2869   3303   2294    456    361   -168       N
ATOM   3897  CA  PRO A 505     -40.183 -35.713 -11.484  1.00 22.87           C
ANISOU 3897  CA  PRO A 505     2962   3461   2265    515    379   -163       C
ATOM   3898  C   PRO A 505     -41.222 -36.793 -11.157  1.00 22.93           C
ANISOU 3898  C   PRO A 505     2931   3526   2255    532    445    -58       C
ATOM   3899  O   PRO A 505     -40.982 -37.635 -10.298  1.00 23.48           O
ANISOU 3899  O   PRO A 505     3005   3654   2261    554    459    -16       O
ATOM   3900  CB  PRO A 505     -40.491 -34.388 -10.769  1.00 23.69           C
ANISOU 3900  CB  PRO A 505     3104   3577   2319    581    386   -248       C
ATOM   3901  CG  PRO A 505     -41.071 -33.496 -11.803  1.00 23.86           C
ANISOU 3901  CG  PRO A 505     3116   3527   2422    564    394   -268       C
ATOM   3902  CD  PRO A 505     -40.502 -33.926 -13.119  1.00 22.36           C
ANISOU 3902  CD  PRO A 505     2902   3270   2323    482    360   -239       C
ATOM   3903  N   ALA A 506     -42.346 -36.786 -11.870  1.00 22.60           N
ANISOU 3903  N   ALA A 506     2847   3466   2274    519    486    -14       N
ATOM   3904  CA  ALA A 506     -43.402 -37.773 -11.656  1.00 22.80           C
ANISOU 3904  CA  ALA A 506     2823   3537   2302    525    550     85       C
ATOM   3905  C   ALA A 506     -42.918 -39.200 -11.930  1.00 22.58           C
ANISOU 3905  C   ALA A 506     2776   3500   2305    468    540    157       C
ATOM   3906  O   ALA A 506     -43.239 -40.116 -11.179  1.00 22.83           O
ANISOU 3906  O   ALA A 506     2794   3582   2298    486    586    230       O
ATOM   3907  CB  ALA A 506     -44.610 -37.456 -12.527  1.00 22.71           C
ANISOU 3907  CB  ALA A 506     2762   3503   2363    513    581    109       C
ATOM   3908  N   LEU A 507     -42.145 -39.376 -12.999  1.00 22.03           N
ANISOU 3908  N   LEU A 507     2707   3363   2301    404    486    139       N
ATOM   3909  CA  LEU A 507     -41.608 -40.694 -13.360  1.00 21.94           C
ANISOU 3909  CA  LEU A 507     2683   3331   2324    352    471    198       C
ATOM   3910  C   LEU A 507     -40.730 -41.266 -12.251  1.00 22.84           C
ANISOU 3910  C   LEU A 507     2831   3492   2356    383    464    209       C
ATOM   3911  O   LEU A 507     -40.736 -42.474 -12.004  1.00 23.03           O
ANISOU 3911  O   LEU A 507     2841   3528   2380    372    488    287       O
ATOM   3912  CB  LEU A 507     -40.798 -40.606 -14.654  1.00 21.41           C
ANISOU 3912  CB  LEU A 507     2619   3189   2327    291    411    161       C
ATOM   3913  CG  LEU A 507     -41.575 -40.267 -15.928  1.00 21.35           C
ANISOU 3913  CG  LEU A 507     2576   3134   2402    257    411    161       C
ATOM   3914  CD1 LEU A 507     -40.604 -39.846 -17.042  1.00 21.27           C
ANISOU 3914  CD1 LEU A 507     2585   3058   2438    217    353    111       C
ATOM   3915  CD2 LEU A 507     -42.442 -41.431 -16.365  1.00 21.73           C
ANISOU 3915  CD2 LEU A 507     2573   3180   2504    221    441    241       C
ATOM   3916  N   LEU A 508     -39.987 -40.390 -11.582  1.00 23.12           N
ANISOU 3916  N   LEU A 508     2910   3552   2324    425    431    132       N
ATOM   3917  CA  LEU A 508     -39.064 -40.802 -10.528  1.00 23.76           C
ANISOU 3917  CA  LEU A 508     3025   3685   2319    463    411    129       C
ATOM   3918  C   LEU A 508     -39.710 -40.959  -9.143  1.00 24.33           C
ANISOU 3918  C   LEU A 508     3108   3847   2290    542    470    167       C
ATOM   3919  O   LEU A 508     -39.110 -41.585  -8.268  1.00 25.10           O
ANISOU 3919  O   LEU A 508     3228   3996   2313    578    466    193       O
ATOM   3920  CB  LEU A 508     -37.897 -39.811 -10.434  1.00 23.96           C
ANISOU 3920  CB  LEU A 508     3086   3698   2318    468    340     19       C
ATOM   3921  CG  LEU A 508     -36.980 -39.639 -11.652  1.00 24.72           C
ANISOU 3921  CG  LEU A 508     3175   3715   2501    397    281    -20       C
ATOM   3922  CD1 LEU A 508     -35.708 -38.898 -11.245  1.00 26.01           C
ANISOU 3922  CD1 LEU A 508     3369   3885   2629    406    215   -115       C
ATOM   3923  CD2 LEU A 508     -36.623 -40.952 -12.323  1.00 26.39           C
ANISOU 3923  CD2 LEU A 508     3364   3900   2764    349    278     55       C
ATOM   3924  N   VAL A 509     -40.899 -40.384  -8.928  1.00 24.30           N
ANISOU 3924  N   VAL A 509     3090   3866   2278    576    524    172       N
ATOM   3925  CA  VAL A 509     -41.623 -40.546  -7.648  1.00 24.93           C
ANISOU 3925  CA  VAL A 509     3175   4035   2261    656    592    218       C
ATOM   3926  C   VAL A 509     -42.820 -41.489  -7.745  1.00 25.14           C
ANISOU 3926  C   VAL A 509     3148   4073   2332    641    675    336       C
ATOM   3927  O   VAL A 509     -43.458 -41.779  -6.734  1.00 26.03           O
ANISOU 3927  O   VAL A 509     3257   4259   2373    703    744    395       O
ATOM   3928  CB  VAL A 509     -42.140 -39.197  -7.054  1.00 25.55           C
ANISOU 3928  CB  VAL A 509     3278   4151   2277    727    606    138       C
ATOM   3929  CG1 VAL A 509     -40.982 -38.239  -6.775  1.00 26.08           C
ANISOU 3929  CG1 VAL A 509     3401   4212   2298    745    526     14       C
ATOM   3930  CG2 VAL A 509     -43.194 -38.554  -7.956  1.00 24.04           C
ANISOU 3930  CG2 VAL A 509     3049   3914   2173    702    633    131       C
ATOM   3931  N   GLU A 510     -43.128 -41.956  -8.954  1.00 24.42           N
ANISOU 3931  N   GLU A 510     3011   3910   2356    561    669    370       N
ATOM   3932  CA  GLU A 510     -44.316 -42.774  -9.186  1.00 24.70           C
ANISOU 3932  CA  GLU A 510     2985   3946   2455    533    739    470       C
ATOM   3933  C   GLU A 510     -44.276 -44.061  -8.371  1.00 25.26           C
ANISOU 3933  C   GLU A 510     3055   4054   2491    546    790    574       C
ATOM   3934  O   GLU A 510     -43.216 -44.671  -8.215  1.00 25.23           O
ANISOU 3934  O   GLU A 510     3085   4038   2463    539    752    581       O
ATOM   3935  CB  GLU A 510     -44.443 -43.130 -10.672  1.00 23.89           C
ANISOU 3935  CB  GLU A 510     2840   3756   2479    442    706    474       C
ATOM   3936  CG  GLU A 510     -45.797 -43.734 -11.060  1.00 24.31           C
ANISOU 3936  CG  GLU A 510     2819   3806   2613    407    767    554       C
ATOM   3937  CD  GLU A 510     -45.986 -43.827 -12.569  1.00 24.08           C
ANISOU 3937  CD  GLU A 510     2751   3701   2699    329    723    535       C
ATOM   3938  OE1 GLU A 510     -44.995 -44.085 -13.282  1.00 24.04           O
ANISOU 3938  OE1 GLU A 510     2774   3639   2723    285    659    503       O
ATOM   3939  OE2 GLU A 510     -47.129 -43.644 -13.042  1.00 25.22           O
ANISOU 3939  OE2 GLU A 510     2836   3847   2901    315    751    551       O
ATOM   3940  N   LYS A 511     -45.436 -44.470  -7.864  1.00 26.17           N
ANISOU 3940  N   LYS A 511     3125   4211   2606    568    878    660       N
ATOM   3941  CA  LYS A 511     -45.574 -45.773  -7.222  1.00 27.06           C
ANISOU 3941  CA  LYS A 511     3228   4345   2710    570    940    779       C
ATOM   3942  C   LYS A 511     -45.030 -46.842  -8.164  1.00 26.48           C
ANISOU 3942  C   LYS A 511     3142   4182   2737    481    901    811       C
ATOM   3943  O   LYS A 511     -45.515 -46.976  -9.286  1.00 26.05           O
ANISOU 3943  O   LYS A 511     3039   4063   2794    407    885    805       O
ATOM   3944  CB  LYS A 511     -47.041 -46.076  -6.916  1.00 28.22           C
ANISOU 3944  CB  LYS A 511     3307   4526   2888    576   1042    870       C
ATOM   3945  CG  LYS A 511     -47.259 -47.361  -6.116  1.00 30.46           C
ANISOU 3945  CG  LYS A 511     3579   4834   3159    586   1122   1003       C
ATOM   3946  CD  LYS A 511     -48.733 -47.727  -6.026  1.00 32.97           C
ANISOU 3946  CD  LYS A 511     3814   5171   3541    570   1222   1096       C
ATOM   3947  CE  LYS A 511     -48.937 -48.958  -5.149  1.00 35.22           C
ANISOU 3947  CE  LYS A 511     4091   5479   3811    584   1312   1237       C
ATOM   3948  NZ  LYS A 511     -50.372 -49.233  -4.858  1.00 38.24           N
ANISOU 3948  NZ  LYS A 511     4390   5896   4244    580   1422   1333       N
ATOM   3949  N   PRO A 512     -44.008 -47.597  -7.729  1.00 26.49           N
ANISOU 3949  N   PRO A 512     3189   4182   2695    494    881    840       N
ATOM   3950  CA  PRO A 512     -43.557 -48.667  -8.613  1.00 26.03           C
ANISOU 3950  CA  PRO A 512     3120   4036   2734    415    850    874       C
ATOM   3951  C   PRO A 512     -44.584 -49.786  -8.712  1.00 26.72           C
ANISOU 3951  C   PRO A 512     3150   4092   2910    368    927    988       C
ATOM   3952  O   PRO A 512     -45.402 -49.960  -7.805  1.00 27.24           O
ANISOU 3952  O   PRO A 512     3196   4216   2939    410   1014   1066       O
ATOM   3953  CB  PRO A 512     -42.284 -49.182  -7.926  1.00 26.31           C
ANISOU 3953  CB  PRO A 512     3216   4091   2688    459    822    887       C
ATOM   3954  CG  PRO A 512     -41.860 -48.079  -7.010  1.00 26.54           C
ANISOU 3954  CG  PRO A 512     3290   4207   2587    545    801    815       C
ATOM   3955  CD  PRO A 512     -43.133 -47.447  -6.555  1.00 27.01           C
ANISOU 3955  CD  PRO A 512     3319   4320   2624    580    871    828       C
ATOM   3956  N   ARG A 513     -44.551 -50.532  -9.812  1.00 26.53           N
ANISOU 3956  N   ARG A 513     3099   3976   3004    282    898    997       N
ATOM   3957  CA  ARG A 513     -45.245 -51.818  -9.849  1.00 27.51           C
ANISOU 3957  CA  ARG A 513     3180   4054   3217    232    961   1106       C
ATOM   3958  C   ARG A 513     -44.663 -52.701  -8.736  1.00 28.47           C
ANISOU 3958  C   ARG A 513     3349   4201   3269    285   1007   1198       C
ATOM   3959  O   ARG A 513     -43.553 -52.438  -8.258  1.00 28.26           O
ANISOU 3959  O   ARG A 513     3386   4209   3143    343    964   1161       O
ATOM   3960  CB  ARG A 513     -45.104 -52.489 -11.217  1.00 26.86           C
ANISOU 3960  CB  ARG A 513     3076   3866   3265    136    907   1084       C
ATOM   3961  CG  ARG A 513     -46.279 -52.252 -12.158  1.00 26.22           C
ANISOU 3961  CG  ARG A 513     2917   3756   3289     71    908   1062       C
ATOM   3962  CD  ARG A 513     -46.446 -50.798 -12.589  1.00 25.52           C
ANISOU 3962  CD  ARG A 513     2822   3708   3166     94    864    960       C
ATOM   3963  NE  ARG A 513     -47.512 -50.710 -13.590  1.00 25.45           N
ANISOU 3963  NE  ARG A 513     2737   3669   3263     32    858    944       N
ATOM   3964  CZ  ARG A 513     -47.364 -50.928 -14.896  1.00 24.20           C
ANISOU 3964  CZ  ARG A 513     2565   3439   3189    -34    790    893       C
ATOM   3965  NH1 ARG A 513     -46.169 -51.199 -15.422  1.00 23.89           N
ANISOU 3965  NH1 ARG A 513     2584   3349   3144    -47    726    851       N
ATOM   3966  NH2 ARG A 513     -48.421 -50.834 -15.697  1.00 25.13           N
ANISOU 3966  NH2 ARG A 513     2610   3545   3393    -82    786    880       N
ATOM   3967  N   PRO A 514     -45.412 -53.731  -8.298  1.00 30.06           N
ANISOU 3967  N   PRO A 514     3515   4385   3519    267   1095   1320       N
ATOM   3968  CA  PRO A 514     -44.954 -54.561  -7.176  1.00 31.22           C
ANISOU 3968  CA  PRO A 514     3709   4561   3595    328   1151   1423       C
ATOM   3969  C   PRO A 514     -43.556 -55.136  -7.383  1.00 31.14           C
ANISOU 3969  C   PRO A 514     3762   4503   3566    333   1083   1404       C
ATOM   3970  O   PRO A 514     -43.337 -55.900  -8.321  1.00 31.09           O
ANISOU 3970  O   PRO A 514     3747   4396   3671    258   1050   1404       O
ATOM   3971  CB  PRO A 514     -46.001 -55.681  -7.116  1.00 32.28           C
ANISOU 3971  CB  PRO A 514     3784   4643   3837    272   1246   1549       C
ATOM   3972  CG  PRO A 514     -47.220 -55.084  -7.701  1.00 31.96           C
ANISOU 3972  CG  PRO A 514     3661   4606   3874    220   1262   1516       C
ATOM   3973  CD  PRO A 514     -46.760 -54.123  -8.754  1.00 30.41           C
ANISOU 3973  CD  PRO A 514     3475   4393   3687    195   1152   1372       C
ATOM   3974  N   ASP A 515     -42.620 -54.739  -6.520  1.00 31.30           N
ANISOU 3974  N   ASP A 515     3844   4600   3447    425   1058   1383       N
ATOM   3975  CA  ASP A 515     -41.219 -55.158  -6.605  1.00 31.18           C
ANISOU 3975  CA  ASP A 515     3887   4561   3399    445    990   1360       C
ATOM   3976  C   ASP A 515     -40.586 -54.894  -7.978  1.00 29.46           C
ANISOU 3976  C   ASP A 515     3664   4266   3262    374    891   1252       C
ATOM   3977  O   ASP A 515     -39.710 -55.639  -8.426  1.00 29.10           O
ANISOU 3977  O   ASP A 515     3645   4159   3252    355    850   1256       O
ATOM   3978  CB  ASP A 515     -41.086 -56.634  -6.199  1.00 32.50           C
ANISOU 3978  CB  ASP A 515     4072   4679   3597    450   1049   1494       C
ATOM   3979  CG  ASP A 515     -41.526 -56.880  -4.771  1.00 35.75           C
ANISOU 3979  CG  ASP A 515     4498   5176   3908    537   1147   1607       C
ATOM   3980  OD1 ASP A 515     -41.073 -56.135  -3.875  1.00 38.95           O
ANISOU 3980  OD1 ASP A 515     4942   5692   4167    632   1131   1573       O
ATOM   3981  OD2 ASP A 515     -42.329 -57.809  -4.539  1.00 39.13           O
ANISOU 3981  OD2 ASP A 515     4900   5564   4404    512   1240   1730       O
ATOM   3982  N   ALA A 516     -41.007 -53.802  -8.617  1.00 28.18           N
ANISOU 3982  N   ALA A 516     3473   4113   3122    343    856   1156       N
ATOM   3983  CA  ALA A 516     -40.522 -53.430  -9.941  1.00 26.76           C
ANISOU 3983  CA  ALA A 516     3286   3868   3013    280    770   1056       C
ATOM   3984  C   ALA A 516     -39.672 -52.162  -9.891  1.00 25.74           C
ANISOU 3984  C   ALA A 516     3188   3794   2799    321    698    942       C
ATOM   3985  O   ALA A 516     -39.705 -51.410  -8.915  1.00 26.08           O
ANISOU 3985  O   ALA A 516     3249   3924   2736    391    712    926       O
ATOM   3986  CB  ALA A 516     -41.689 -53.247 -10.893  1.00 26.27           C
ANISOU 3986  CB  ALA A 516     3162   3759   3061    204    784   1040       C
ATOM   3987  N   ILE A 517     -38.904 -51.940 -10.950  1.00 24.84           N
ANISOU 3987  N   ILE A 517     3080   3627   2732    279    621    864       N
ATOM   3988  CA  ILE A 517     -38.022 -50.772 -11.035  1.00 23.85           C
ANISOU 3988  CA  ILE A 517     2978   3536   2547    304    551    756       C
ATOM   3989  C   ILE A 517     -38.770 -49.505 -11.454  1.00 23.48           C
ANISOU 3989  C   ILE A 517     2905   3501   2514    288    545    684       C
ATOM   3990  O   ILE A 517     -38.346 -48.399 -11.108  1.00 22.74           O
ANISOU 3990  O   ILE A 517     2832   3453   2353    326    511    607       O
ATOM   3991  CB  ILE A 517     -36.821 -51.037 -11.980  1.00 23.37           C
ANISOU 3991  CB  ILE A 517     2933   3418   2530    270    478    709       C
ATOM   3992  CG1 ILE A 517     -35.747 -49.961 -11.807  1.00 23.14           C
ANISOU 3992  CG1 ILE A 517     2927   3432   2431    303    411    612       C
ATOM   3993  CG2 ILE A 517     -37.258 -51.118 -13.441  1.00 22.45           C
ANISOU 3993  CG2 ILE A 517     2784   3217   2529    190    460    682       C
ATOM   3994  CD1 ILE A 517     -34.443 -50.302 -12.492  1.00 23.69           C
ANISOU 3994  CD1 ILE A 517     3010   3463   2528    284    348    579       C
ATOM   3995  N   PHE A 518     -39.886 -49.676 -12.171  1.00 23.06           N
ANISOU 3995  N   PHE A 518     2807   3405   2550    235    577    708       N
ATOM   3996  CA  PHE A 518     -40.634 -48.565 -12.761  1.00 22.78           C
ANISOU 3996  CA  PHE A 518     2743   3371   2543    218    569    645       C
ATOM   3997  C   PHE A 518     -42.101 -48.594 -12.375  1.00 23.21           C
ANISOU 3997  C   PHE A 518     2751   3455   2615    222    644    702       C
ATOM   3998  O   PHE A 518     -42.644 -49.650 -12.049  1.00 23.83           O
ANISOU 3998  O   PHE A 518     2807   3524   2725    207    700    795       O
ATOM   3999  CB  PHE A 518     -40.607 -48.641 -14.295  1.00 21.86           C
ANISOU 3999  CB  PHE A 518     2603   3174   2528    145    522    606       C
ATOM   4000  CG  PHE A 518     -39.243 -48.555 -14.908  1.00 21.47           C
ANISOU 4000  CG  PHE A 518     2589   3091   2478    134    451    548       C
ATOM   4001  CD1 PHE A 518     -38.314 -47.617 -14.478  1.00 21.26           C
ANISOU 4001  CD1 PHE A 518     2597   3102   2378    175    412    481       C
ATOM   4002  CD2 PHE A 518     -38.905 -49.391 -15.965  1.00 21.44           C
ANISOU 4002  CD2 PHE A 518     2580   3016   2552     80    422    555       C
ATOM   4003  CE1 PHE A 518     -37.067 -47.537 -15.066  1.00 21.54           C
ANISOU 4003  CE1 PHE A 518     2655   3108   2421    160    351    431       C
ATOM   4004  CE2 PHE A 518     -37.658 -49.310 -16.564  1.00 21.31           C
ANISOU 4004  CE2 PHE A 518     2591   2972   2535     74    363    505       C
ATOM   4005  CZ  PHE A 518     -36.733 -48.384 -16.108  1.00 20.75           C
ANISOU 4005  CZ  PHE A 518     2548   2942   2395    112    329    446       C
ATOM   4006  N   GLY A 519     -42.744 -47.429 -12.459  1.00 22.96           N
ANISOU 4006  N   GLY A 519     2702   3452   2569    240    647    649       N
ATOM   4007  CA  GLY A 519     -44.198 -47.336 -12.402  1.00 23.26           C
ANISOU 4007  CA  GLY A 519     2682   3512   2644    235    710    691       C
ATOM   4008  C   GLY A 519     -44.829 -47.336 -13.789  1.00 22.60           C
ANISOU 4008  C   GLY A 519     2547   3368   2672    164    683    669       C
ATOM   4009  O   GLY A 519     -44.137 -47.378 -14.808  1.00 21.41           O
ANISOU 4009  O   GLY A 519     2412   3159   2565    123    619    621       O
ATOM   4010  N   GLU A 520     -46.156 -47.272 -13.817  1.00 22.97           N
ANISOU 4010  N   GLU A 520     2530   3435   2761    156    734    704       N
ATOM   4011  CA  GLU A 520     -46.941 -47.377 -15.049  1.00 22.73           C
ANISOU 4011  CA  GLU A 520     2440   3360   2838     93    713    692       C
ATOM   4012  C   GLU A 520     -46.549 -46.399 -16.156  1.00 21.80           C
ANISOU 4012  C   GLU A 520     2339   3212   2732     85    639    598       C
ATOM   4013  O   GLU A 520     -46.460 -46.787 -17.321  1.00 21.27           O
ANISOU 4013  O   GLU A 520     2256   3088   2738     28    592    578       O
ATOM   4014  CB  GLU A 520     -48.428 -47.179 -14.732  1.00 23.46           C
ANISOU 4014  CB  GLU A 520     2457   3501   2955    104    780    736       C
ATOM   4015  CG  GLU A 520     -49.343 -47.210 -15.960  1.00 23.94           C
ANISOU 4015  CG  GLU A 520     2444   3529   3122     45    755    719       C
ATOM   4016  CD  GLU A 520     -50.774 -46.810 -15.647  1.00 27.16           C
ANISOU 4016  CD  GLU A 520     2774   3997   3550     66    816    752       C
ATOM   4017  OE1 GLU A 520     -51.690 -47.299 -16.346  1.00 27.86           O
ANISOU 4017  OE1 GLU A 520     2782   4068   3736     10    816    773       O
ATOM   4018  OE2 GLU A 520     -50.986 -46.007 -14.711  1.00 28.40           O
ANISOU 4018  OE2 GLU A 520     2946   4220   3625    141    862    752       O
ATOM   4019  N   THR A 521     -46.345 -45.132 -15.801  1.00 21.88           N
ANISOU 4019  N   THR A 521     2382   3259   2672    144    632    540       N
ATOM   4020  CA  THR A 521     -46.065 -44.099 -16.799  1.00 21.15           C
ANISOU 4020  CA  THR A 521     2305   3137   2593    142    574    459       C
ATOM   4021  C   THR A 521     -44.749 -44.356 -17.539  1.00 20.49           C
ANISOU 4021  C   THR A 521     2269   2995   2522    107    507    421       C
ATOM   4022  O   THR A 521     -44.687 -44.166 -18.750  1.00 20.07           O
ANISOU 4022  O   THR A 521     2206   2898   2520     74    463    386       O
ATOM   4023  CB  THR A 521     -46.074 -42.672 -16.189  1.00 21.54           C
ANISOU 4023  CB  THR A 521     2387   3228   2570    213    583    404       C
ATOM   4024  OG1 THR A 521     -47.265 -42.485 -15.417  1.00 21.97           O
ANISOU 4024  OG1 THR A 521     2399   3344   2605    254    652    444       O
ATOM   4025  CG2 THR A 521     -46.026 -41.603 -17.291  1.00 20.23           C
ANISOU 4025  CG2 THR A 521     2228   3025   2434    210    535    336       C
ATOM   4026  N   MET A 522     -43.711 -44.802 -16.829  1.00 20.41           N
ANISOU 4026  N   MET A 522     2304   2988   2461    119    501    429       N
ATOM   4027  CA  MET A 522     -42.428 -45.086 -17.478  1.00 20.13           C
ANISOU 4027  CA  MET A 522     2308   2903   2437     90    443    397       C
ATOM   4028  C   MET A 522     -42.563 -46.183 -18.538  1.00 19.82           C
ANISOU 4028  C   MET A 522     2240   2807   2483     27    424    425       C
ATOM   4029  O   MET A 522     -42.020 -46.061 -19.628  1.00 19.32           O
ANISOU 4029  O   MET A 522     2188   2699   2453      0    374    383       O
ATOM   4030  CB  MET A 522     -41.362 -45.490 -16.457  1.00 20.55           C
ANISOU 4030  CB  MET A 522     2406   2979   2422    119    441    409       C
ATOM   4031  CG  MET A 522     -39.972 -45.652 -17.054  1.00 20.20           C
ANISOU 4031  CG  MET A 522     2397   2893   2384     98    381    371       C
ATOM   4032  SD  MET A 522     -39.193 -44.062 -17.404  1.00 21.62           S
ANISOU 4032  SD  MET A 522     2609   3069   2538    116    333    271       S
ATOM   4033  CE  MET A 522     -38.663 -43.597 -15.767  1.00 22.71           C
ANISOU 4033  CE  MET A 522     2783   3276   2569    181    343    253       C
ATOM   4034  N   VAL A 523     -43.302 -47.242 -18.224  1.00 20.57           N
ANISOU 4034  N   VAL A 523     2299   2902   2615      4    465    495       N
ATOM   4035  CA  VAL A 523     -43.427 -48.364 -19.145  1.00 20.31           C
ANISOU 4035  CA  VAL A 523     2242   2808   2666    -58    446    517       C
ATOM   4036  C   VAL A 523     -44.290 -47.991 -20.349  1.00 20.35           C
ANISOU 4036  C   VAL A 523     2200   2796   2735    -89    420    483       C
ATOM   4037  O   VAL A 523     -43.928 -48.266 -21.492  1.00 19.56           O
ANISOU 4037  O   VAL A 523     2106   2648   2678   -123    370    450       O
ATOM   4038  CB  VAL A 523     -44.017 -49.603 -18.452  1.00 21.11           C
ANISOU 4038  CB  VAL A 523     2315   2906   2801    -79    502    604       C
ATOM   4039  CG1 VAL A 523     -44.177 -50.743 -19.448  1.00 20.49           C
ANISOU 4039  CG1 VAL A 523     2212   2754   2819   -147    477    616       C
ATOM   4040  CG2 VAL A 523     -43.133 -50.025 -17.276  1.00 21.85           C
ANISOU 4040  CG2 VAL A 523     2458   3020   2822    -38    527    645       C
ATOM   4041  N   GLU A 524     -45.425 -47.350 -20.092  1.00 20.73           N
ANISOU 4041  N   GLU A 524     2202   2888   2785    -71    454    491       N
ATOM   4042  CA  GLU A 524     -46.386 -47.075 -21.153  1.00 20.98           C
ANISOU 4042  CA  GLU A 524     2179   2914   2878    -96    432    467       C
ATOM   4043  C   GLU A 524     -45.961 -45.959 -22.111  1.00 20.52           C
ANISOU 4043  C   GLU A 524     2149   2846   2801    -75    379    396       C
ATOM   4044  O   GLU A 524     -46.472 -45.879 -23.227  1.00 20.28           O
ANISOU 4044  O   GLU A 524     2087   2802   2819    -96    344    371       O
ATOM   4045  CB  GLU A 524     -47.762 -46.811 -20.546  1.00 21.82           C
ANISOU 4045  CB  GLU A 524     2219   3075   2996    -80    489    506       C
ATOM   4046  CG  GLU A 524     -48.307 -48.033 -19.792  1.00 23.20           C
ANISOU 4046  CG  GLU A 524     2354   3250   3211   -112    545    587       C
ATOM   4047  CD  GLU A 524     -48.483 -49.256 -20.692  1.00 25.15           C
ANISOU 4047  CD  GLU A 524     2567   3432   3555   -190    514    598       C
ATOM   4048  OE1 GLU A 524     -49.154 -49.136 -21.737  1.00 25.65           O
ANISOU 4048  OE1 GLU A 524     2582   3487   3678   -219    475    563       O
ATOM   4049  OE2 GLU A 524     -47.947 -50.340 -20.363  1.00 24.66           O
ANISOU 4049  OE2 GLU A 524     2530   3329   3512   -218    526    638       O
ATOM   4050  N   LEU A 525     -45.029 -45.115 -21.674  1.00 20.41           N
ANISOU 4050  N   LEU A 525     2194   2841   2719    -33    374    363       N
ATOM   4051  CA  LEU A 525     -44.381 -44.139 -22.553  1.00 19.76           C
ANISOU 4051  CA  LEU A 525     2148   2737   2624    -19    328    302       C
ATOM   4052  C   LEU A 525     -43.118 -44.727 -23.172  1.00 19.26           C
ANISOU 4052  C   LEU A 525     2126   2625   2568    -47    285    285       C
ATOM   4053  O   LEU A 525     -42.896 -44.605 -24.379  1.00 19.24           O
ANISOU 4053  O   LEU A 525     2127   2591   2591    -62    244    255       O
ATOM   4054  CB  LEU A 525     -44.033 -42.850 -21.798  1.00 19.87           C
ANISOU 4054  CB  LEU A 525     2200   2778   2573     36    343    270       C
ATOM   4055  CG  LEU A 525     -45.135 -41.790 -21.696  1.00 20.31           C
ANISOU 4055  CG  LEU A 525     2227   2868   2623     78    369    259       C
ATOM   4056  CD1 LEU A 525     -46.330 -42.298 -20.905  1.00 20.37           C
ANISOU 4056  CD1 LEU A 525     2178   2924   2638     84    424    313       C
ATOM   4057  CD2 LEU A 525     -44.589 -40.494 -21.083  1.00 20.31           C
ANISOU 4057  CD2 LEU A 525     2278   2876   2564    129    375    212       C
ATOM   4058  N   GLY A 526     -42.287 -45.356 -22.343  1.00 19.28           N
ANISOU 4058  N   GLY A 526     2159   2626   2541    -47    295    306       N
ATOM   4059  CA  GLY A 526     -40.998 -45.887 -22.792  1.00 18.66           C
ANISOU 4059  CA  GLY A 526     2119   2507   2462    -65    258    291       C
ATOM   4060  C   GLY A 526     -41.107 -46.947 -23.871  1.00 18.77           C
ANISOU 4060  C   GLY A 526     2117   2476   2539   -110    231    299       C
ATOM   4061  O   GLY A 526     -40.355 -46.926 -24.841  1.00 18.50           O
ANISOU 4061  O   GLY A 526     2106   2410   2514   -118    192    266       O
ATOM   4062  N   ALA A 527     -42.056 -47.872 -23.711  1.00 19.08           N
ANISOU 4062  N   ALA A 527     2116   2511   2624   -138    253    341       N
ATOM   4063  CA  ALA A 527     -42.158 -49.021 -24.610  1.00 18.75           C
ANISOU 4063  CA  ALA A 527     2059   2418   2646   -185    226    345       C
ATOM   4064  C   ALA A 527     -42.475 -48.631 -26.063  1.00 18.65           C
ANISOU 4064  C   ALA A 527     2032   2392   2663   -195    179    295       C
ATOM   4065  O   ALA A 527     -41.776 -49.069 -26.975  1.00 18.16           O
ANISOU 4065  O   ALA A 527     1996   2291   2612   -207    140    268       O
ATOM   4066  CB  ALA A 527     -43.166 -50.042 -24.073  1.00 19.26           C
ANISOU 4066  CB  ALA A 527     2078   2476   2764   -219    264    402       C
ATOM   4067  N   PRO A 528     -43.509 -47.791 -26.289  1.00 18.84           N
ANISOU 4067  N   PRO A 528     2015   2450   2691   -183    183    284       N
ATOM   4068  CA  PRO A 528     -43.754 -47.321 -27.658  1.00 18.82           C
ANISOU 4068  CA  PRO A 528     2004   2443   2703   -180    137    239       C
ATOM   4069  C   PRO A 528     -42.537 -46.667 -28.315  1.00 18.28           C
ANISOU 4069  C   PRO A 528     1994   2359   2593   -153    110    202       C
ATOM   4070  O   PRO A 528     -42.183 -47.026 -29.442  1.00 18.41           O
ANISOU 4070  O   PRO A 528     2023   2348   2623   -163     69    175       O
ATOM   4071  CB  PRO A 528     -44.883 -46.301 -27.483  1.00 19.24           C
ANISOU 4071  CB  PRO A 528     2014   2546   2751   -153    157    240       C
ATOM   4072  CG  PRO A 528     -45.596 -46.747 -26.271  1.00 19.81           C
ANISOU 4072  CG  PRO A 528     2048   2642   2838   -164    209    290       C
ATOM   4073  CD  PRO A 528     -44.568 -47.349 -25.365  1.00 19.60           C
ANISOU 4073  CD  PRO A 528     2068   2594   2783   -168    231    315       C
ATOM   4074  N   PHE A 529     -41.899 -45.721 -27.627  1.00 18.19           N
ANISOU 4074  N   PHE A 529     2016   2364   2533   -120    132    199       N
ATOM   4075  CA  PHE A 529     -40.719 -45.056 -28.199  1.00 17.75           C
ANISOU 4075  CA  PHE A 529     2008   2291   2447   -100    111    168       C
ATOM   4076  C   PHE A 529     -39.621 -46.078 -28.505  1.00 17.78           C
ANISOU 4076  C   PHE A 529     2040   2259   2456   -121     91    167       C
ATOM   4077  O   PHE A 529     -38.979 -46.034 -29.559  1.00 17.00           O
ANISOU 4077  O   PHE A 529     1964   2139   2357   -117     63    143       O
ATOM   4078  CB  PHE A 529     -40.130 -44.012 -27.250  1.00 17.69           C
ANISOU 4078  CB  PHE A 529     2027   2299   2394    -71    136    161       C
ATOM   4079  CG  PHE A 529     -40.986 -42.787 -27.036  1.00 17.52           C
ANISOU 4079  CG  PHE A 529     1991   2304   2361    -39    156    153       C
ATOM   4080  CD1 PHE A 529     -41.302 -42.377 -25.746  1.00 18.52           C
ANISOU 4080  CD1 PHE A 529     2115   2461   2460    -19    191    162       C
ATOM   4081  CD2 PHE A 529     -41.422 -42.012 -28.104  1.00 17.95           C
ANISOU 4081  CD2 PHE A 529     2039   2354   2425    -21    140    135       C
ATOM   4082  CE1 PHE A 529     -42.067 -41.233 -25.518  1.00 18.74           C
ANISOU 4082  CE1 PHE A 529     2133   2511   2475     18    212    151       C
ATOM   4083  CE2 PHE A 529     -42.196 -40.865 -27.886  1.00 18.69           C
ANISOU 4083  CE2 PHE A 529     2122   2468   2509     16    161    129       C
ATOM   4084  CZ  PHE A 529     -42.515 -40.477 -26.589  1.00 19.39           C
ANISOU 4084  CZ  PHE A 529     2208   2584   2575     35    197    135       C
ATOM   4085  N   SER A 530     -39.409 -46.993 -27.565  1.00 18.06           N
ANISOU 4085  N   SER A 530     2077   2289   2495   -136    109    198       N
ATOM   4086  CA  SER A 530     -38.308 -47.950 -27.644  1.00 18.30           C
ANISOU 4086  CA  SER A 530     2138   2288   2528   -147     95    202       C
ATOM   4087  C   SER A 530     -38.473 -48.935 -28.804  1.00 18.59           C
ANISOU 4087  C   SER A 530     2170   2285   2608   -171     63    189       C
ATOM   4088  O   SER A 530     -37.579 -49.080 -29.648  1.00 18.28           O
ANISOU 4088  O   SER A 530     2160   2225   2562   -163     38    165       O
ATOM   4089  CB  SER A 530     -38.182 -48.706 -26.313  1.00 18.60           C
ANISOU 4089  CB  SER A 530     2178   2331   2557   -150    126    246       C
ATOM   4090  OG  SER A 530     -37.266 -49.779 -26.409  1.00 20.33           O
ANISOU 4090  OG  SER A 530     2423   2515   2786   -157    114    257       O
ATOM   4091  N   LEU A 531     -39.613 -49.610 -28.843  1.00 19.00           N
ANISOU 4091  N   LEU A 531     2184   2328   2705   -201     64    203       N
ATOM   4092  CA  LEU A 531     -39.835 -50.673 -29.826  1.00 19.56           C
ANISOU 4092  CA  LEU A 531     2250   2357   2825   -229     30    184       C
ATOM   4093  C   LEU A 531     -39.946 -50.121 -31.249  1.00 19.50           C
ANISOU 4093  C   LEU A 531     2244   2356   2809   -214    -12    135       C
ATOM   4094  O   LEU A 531     -39.473 -50.741 -32.199  1.00 19.37           O
ANISOU 4094  O   LEU A 531     2250   2309   2800   -215    -45    106       O
ATOM   4095  CB  LEU A 531     -41.072 -51.494 -29.459  1.00 20.01           C
ANISOU 4095  CB  LEU A 531     2257   2402   2943   -272     42    210       C
ATOM   4096  CG  LEU A 531     -41.000 -52.207 -28.098  1.00 20.57           C
ANISOU 4096  CG  LEU A 531     2330   2462   3026   -285     90    270       C
ATOM   4097  CD1 LEU A 531     -42.279 -52.983 -27.817  1.00 21.77           C
ANISOU 4097  CD1 LEU A 531     2425   2598   3248   -331    109    301       C
ATOM   4098  CD2 LEU A 531     -39.782 -53.135 -28.022  1.00 21.27           C
ANISOU 4098  CD2 LEU A 531     2468   2503   3109   -280     85    279       C
ATOM   4099  N   LYS A 532     -40.552 -48.946 -31.389  1.00 19.84           N
ANISOU 4099  N   LYS A 532     2266   2441   2832   -193     -8    127       N
ATOM   4100  CA  LYS A 532     -40.629 -48.276 -32.682  1.00 20.39           C
ANISOU 4100  CA  LYS A 532     2342   2524   2882   -167    -42     90       C
ATOM   4101  C   LYS A 532     -39.227 -47.927 -33.197  1.00 20.09           C
ANISOU 4101  C   LYS A 532     2357   2473   2803   -137    -46     76       C
ATOM   4102  O   LYS A 532     -38.927 -48.120 -34.378  1.00 20.39           O
ANISOU 4102  O   LYS A 532     2413   2501   2832   -123    -77     48       O
ATOM   4103  CB  LYS A 532     -41.507 -47.022 -32.563  1.00 20.56           C
ANISOU 4103  CB  LYS A 532     2334   2590   2889   -142    -28     94       C
ATOM   4104  CG  LYS A 532     -41.497 -46.089 -33.747  1.00 21.45           C
ANISOU 4104  CG  LYS A 532     2459   2719   2971   -101    -52     69       C
ATOM   4105  CD  LYS A 532     -42.090 -46.676 -34.999  1.00 22.29           C
ANISOU 4105  CD  LYS A 532     2547   2828   3093   -104   -103     36       C
ATOM   4106  CE  LYS A 532     -42.226 -45.560 -36.041  1.00 22.75           C
ANISOU 4106  CE  LYS A 532     2617   2917   3112    -51   -119     23       C
ATOM   4107  NZ  LYS A 532     -42.552 -46.043 -37.389  1.00 22.43           N
ANISOU 4107  NZ  LYS A 532     2571   2885   3066    -39   -173    -14       N
ATOM   4108  N   GLY A 533     -38.369 -47.430 -32.310  1.00 19.92           N
ANISOU 4108  N   GLY A 533     2358   2455   2756   -127    -14     96       N
ATOM   4109  CA  GLY A 533     -37.002 -47.076 -32.673  1.00 19.72           C
ANISOU 4109  CA  GLY A 533     2373   2419   2700   -105    -13     87       C
ATOM   4110  C   GLY A 533     -36.180 -48.282 -33.098  1.00 20.04           C
ANISOU 4110  C   GLY A 533     2437   2428   2750   -112    -30     79       C
ATOM   4111  O   GLY A 533     -35.304 -48.175 -33.962  1.00 20.62           O
ANISOU 4111  O   GLY A 533     2537   2496   2804    -90    -40     64       O
ATOM   4112  N   LEU A 534     -36.470 -49.437 -32.503  1.00 19.34           N
ANISOU 4112  N   LEU A 534     2339   2317   2693   -140    -31     94       N
ATOM   4113  CA  LEU A 534     -35.727 -50.656 -32.805  1.00 19.19           C
ANISOU 4113  CA  LEU A 534     2346   2260   2688   -144    -44     89       C
ATOM   4114  C   LEU A 534     -36.194 -51.274 -34.125  1.00 19.34           C
ANISOU 4114  C   LEU A 534     2366   2257   2726   -147    -84     50       C
ATOM   4115  O   LEU A 534     -35.382 -51.557 -35.005  1.00 19.07           O
ANISOU 4115  O   LEU A 534     2363   2209   2674   -123   -100     26       O
ATOM   4116  CB  LEU A 534     -35.854 -51.662 -31.652  1.00 19.26           C
ANISOU 4116  CB  LEU A 534     2349   2245   2726   -170    -25    125       C
ATOM   4117  CG  LEU A 534     -35.159 -51.237 -30.351  1.00 18.87           C
ANISOU 4117  CG  LEU A 534     2305   2219   2644   -156      7    159       C
ATOM   4118  CD1 LEU A 534     -35.682 -52.025 -29.163  1.00 18.48           C
ANISOU 4118  CD1 LEU A 534     2243   2160   2617   -177     33    204       C
ATOM   4119  CD2 LEU A 534     -33.638 -51.383 -30.466  1.00 18.88           C
ANISOU 4119  CD2 LEU A 534     2339   2215   2620   -130      4    154       C
ATOM   4120  N   MET A 535     -37.500 -51.471 -34.268  1.00 19.35           N
ANISOU 4120  N   MET A 535     2332   2259   2762   -173   -101     40       N
ATOM   4121  CA  MET A 535     -38.036 -52.120 -35.458  1.00 19.71           C
ANISOU 4121  CA  MET A 535     2374   2287   2828   -179   -147     -5       C
ATOM   4122  C   MET A 535     -38.089 -51.198 -36.683  1.00 19.82           C
ANISOU 4122  C   MET A 535     2395   2339   2796   -138   -172    -38       C
ATOM   4123  O   MET A 535     -38.171 -51.687 -37.811  1.00 20.16           O
ANISOU 4123  O   MET A 535     2450   2373   2835   -126   -213    -82       O
ATOM   4124  CB  MET A 535     -39.424 -52.708 -35.179  1.00 20.33           C
ANISOU 4124  CB  MET A 535     2402   2354   2969   -227   -160     -6       C
ATOM   4125  CG  MET A 535     -39.465 -53.752 -34.054  1.00 20.74           C
ANISOU 4125  CG  MET A 535     2447   2360   3073   -269   -131     33       C
ATOM   4126  SD  MET A 535     -38.213 -55.053 -34.181  1.00 21.88           S
ANISOU 4126  SD  MET A 535     2650   2437   3228   -263   -136     27       S
ATOM   4127  CE  MET A 535     -38.721 -55.848 -35.708  1.00 20.89           C
ANISOU 4127  CE  MET A 535     2525   2275   3135   -274   -203    -50       C
ATOM   4128  N   GLY A 536     -38.052 -49.886 -36.464  1.00 19.34           N
ANISOU 4128  N   GLY A 536     2330   2319   2701   -114   -147    -17       N
ATOM   4129  CA  GLY A 536     -38.074 -48.914 -37.562  1.00 19.90           C
ANISOU 4129  CA  GLY A 536     2411   2424   2728    -69   -160    -34       C
ATOM   4130  C   GLY A 536     -36.779 -48.868 -38.375  1.00 19.73           C
ANISOU 4130  C   GLY A 536     2437   2396   2664    -30   -157    -43       C
ATOM   4131  O   GLY A 536     -36.733 -48.290 -39.456  1.00 20.95           O
ANISOU 4131  O   GLY A 536     2607   2575   2780     11   -169    -56       O
ATOM   4132  N   ASN A 537     -35.725 -49.475 -37.856  1.00 19.43           N
ANISOU 4132  N   ASN A 537     2421   2328   2632    -40   -138    -31       N
ATOM   4133  CA  ASN A 537     -34.425 -49.504 -38.524  1.00 18.93           C
ANISOU 4133  CA  ASN A 537     2397   2262   2535     -3   -129    -35       C
ATOM   4134  C   ASN A 537     -34.530 -50.144 -39.915  1.00 18.80           C
ANISOU 4134  C   ASN A 537     2402   2243   2497     26   -168    -80       C
ATOM   4135  O   ASN A 537     -35.248 -51.134 -40.085  1.00 18.83           O
ANISOU 4135  O   ASN A 537     2397   2225   2531      4   -206   -113       O
ATOM   4136  CB  ASN A 537     -33.442 -50.277 -37.646  1.00 18.63           C
ANISOU 4136  CB  ASN A 537     2370   2192   2515    -19   -110    -18       C
ATOM   4137  CG  ASN A 537     -32.012 -50.078 -38.057  1.00 18.52           C
ANISOU 4137  CG  ASN A 537     2383   2185   2470     16    -89    -11       C
ATOM   4138  OD1 ASN A 537     -31.572 -50.620 -39.065  1.00 19.18           O
ANISOU 4138  OD1 ASN A 537     2492   2262   2535     47   -102    -35       O
ATOM   4139  ND2 ASN A 537     -31.269 -49.294 -37.275  1.00 17.48           N
ANISOU 4139  ND2 ASN A 537     2243   2066   2334     13    -55     19       N
ATOM   4140  N   PRO A 538     -33.834 -49.582 -40.921  1.00 18.39           N
ANISOU 4140  N   PRO A 538     2377   2216   2396     77   -159    -81       N
ATOM   4141  CA  PRO A 538     -33.941 -50.188 -42.247  1.00 18.73           C
ANISOU 4141  CA  PRO A 538     2445   2266   2407    115   -197   -127       C
ATOM   4142  C   PRO A 538     -33.500 -51.647 -42.331  1.00 18.97           C
ANISOU 4142  C   PRO A 538     2498   2253   2458    108   -218   -162       C
ATOM   4143  O   PRO A 538     -33.996 -52.369 -43.193  1.00 19.64           O
ANISOU 4143  O   PRO A 538     2596   2332   2536    121   -265   -215       O
ATOM   4144  CB  PRO A 538     -33.014 -49.322 -43.113  1.00 19.13           C
ANISOU 4144  CB  PRO A 538     2523   2348   2398    174   -165   -107       C
ATOM   4145  CG  PRO A 538     -32.116 -48.670 -42.166  1.00 18.43           C
ANISOU 4145  CG  PRO A 538     2426   2252   2327    156   -112    -58       C
ATOM   4146  CD  PRO A 538     -32.938 -48.412 -40.951  1.00 18.09           C
ANISOU 4146  CD  PRO A 538     2348   2198   2328    104   -113    -44       C
ATOM   4147  N   ILE A 539     -32.597 -52.095 -41.459  1.00 18.86           N
ANISOU 4147  N   ILE A 539     2490   2207   2468     91   -188   -136       N
ATOM   4148  CA  ILE A 539     -32.177 -53.497 -41.525  1.00 19.16           C
ANISOU 4148  CA  ILE A 539     2554   2198   2529     90   -206   -165       C
ATOM   4149  C   ILE A 539     -33.339 -54.441 -41.207  1.00 19.56           C
ANISOU 4149  C   ILE A 539     2588   2206   2638     39   -246   -195       C
ATOM   4150  O   ILE A 539     -33.283 -55.615 -41.556  1.00 19.89           O
ANISOU 4150  O   ILE A 539     2653   2201   2701     39   -273   -235       O
ATOM   4151  CB  ILE A 539     -30.923 -53.847 -40.671  1.00 19.22           C
ANISOU 4151  CB  ILE A 539     2572   2184   2549     91   -167   -128       C
ATOM   4152  CG1 ILE A 539     -31.232 -53.903 -39.172  1.00 19.77           C
ANISOU 4152  CG1 ILE A 539     2611   2234   2665     38   -150    -88       C
ATOM   4153  CG2 ILE A 539     -29.772 -52.882 -40.973  1.00 19.13           C
ANISOU 4153  CG2 ILE A 539     2564   2213   2490    133   -126    -98       C
ATOM   4154  CD1 ILE A 539     -30.309 -54.857 -38.435  1.00 20.67           C
ANISOU 4154  CD1 ILE A 539     2742   2311   2802     40   -133    -68       C
ATOM   4155  N   CYS A 540     -34.389 -53.919 -40.567  1.00 19.39           N
ANISOU 4155  N   CYS A 540     2524   2198   2645     -3   -247   -176       N
ATOM   4156  CA  CYS A 540     -35.589 -54.706 -40.282  1.00 19.84           C
ANISOU 4156  CA  CYS A 540     2552   2221   2764    -56   -281   -199       C
ATOM   4157  C   CYS A 540     -36.581 -54.753 -41.444  1.00 20.32           C
ANISOU 4157  C   CYS A 540     2602   2302   2817    -48   -340   -261       C
ATOM   4158  O   CYS A 540     -37.544 -55.513 -41.398  1.00 20.53           O
ANISOU 4158  O   CYS A 540     2602   2298   2902    -93   -377   -292       O
ATOM   4159  CB  CYS A 540     -36.289 -54.180 -39.031  1.00 19.60           C
ANISOU 4159  CB  CYS A 540     2476   2203   2770   -101   -252   -149       C
ATOM   4160  SG  CYS A 540     -35.274 -54.274 -37.573  1.00 20.36           S
ANISOU 4160  SG  CYS A 540     2582   2279   2875   -111   -195    -84       S
ATOM   4161  N   SER A 541     -36.342 -53.964 -42.493  1.00 19.94           N
ANISOU 4161  N   SER A 541     2572   2307   2698     11   -349   -277       N
ATOM   4162  CA  SER A 541     -37.253 -53.935 -43.632  1.00 20.59           C
ANISOU 4162  CA  SER A 541     2645   2421   2757     31   -409   -336       C
ATOM   4163  C   SER A 541     -37.030 -55.171 -44.514  1.00 21.41           C
ANISOU 4163  C   SER A 541     2786   2487   2861     46   -457   -409       C
ATOM   4164  O   SER A 541     -35.934 -55.739 -44.529  1.00 21.04           O
ANISOU 4164  O   SER A 541     2785   2406   2805     69   -434   -408       O
ATOM   4165  CB  SER A 541     -37.091 -52.633 -44.435  1.00 20.31           C
ANISOU 4165  CB  SER A 541     2620   2457   2641     97   -398   -319       C
ATOM   4166  OG  SER A 541     -35.857 -52.591 -45.135  1.00 19.99           O
ANISOU 4166  OG  SER A 541     2632   2423   2538    157   -375   -318       O
ATOM   4167  N   PRO A 542     -38.072 -55.602 -45.240  1.00 22.07           N
ANISOU 4167  N   PRO A 542     2851   2577   2959     36   -527   -478       N
ATOM   4168  CA  PRO A 542     -37.959 -56.816 -46.053  1.00 23.26           C
ANISOU 4168  CA  PRO A 542     3038   2685   3116     47   -580   -560       C
ATOM   4169  C   PRO A 542     -36.815 -56.826 -47.072  1.00 23.68           C
ANISOU 4169  C   PRO A 542     3159   2759   3079    134   -573   -584       C
ATOM   4170  O   PRO A 542     -36.235 -57.878 -47.304  1.00 23.92           O
ANISOU 4170  O   PRO A 542     3232   2735   3123    143   -584   -626       O
ATOM   4171  CB  PRO A 542     -39.320 -56.921 -46.761  1.00 24.15           C
ANISOU 4171  CB  PRO A 542     3108   2825   3241     31   -661   -631       C
ATOM   4172  CG  PRO A 542     -40.168 -55.821 -46.237  1.00 23.53           C
ANISOU 4172  CG  PRO A 542     2969   2803   3170     10   -644   -578       C
ATOM   4173  CD  PRO A 542     -39.461 -55.118 -45.140  1.00 22.55           C
ANISOU 4173  CD  PRO A 542     2847   2674   3047      3   -559   -483       C
ATOM   4174  N   GLN A 543     -36.464 -55.687 -47.672  1.00 24.02           N
ANISOU 4174  N   GLN A 543     3214   2878   3035    200   -549   -553       N
ATOM   4175  CA  GLN A 543     -35.364 -55.713 -48.651  1.00 24.47           C
ANISOU 4175  CA  GLN A 543     3333   2958   3007    285   -534   -568       C
ATOM   4176  C   GLN A 543     -33.979 -55.827 -48.023  1.00 23.44           C
ANISOU 4176  C   GLN A 543     3229   2795   2882    293   -462   -512       C
ATOM   4177  O   GLN A 543     -33.040 -56.247 -48.699  1.00 24.22           O
ANISOU 4177  O   GLN A 543     3377   2894   2933    353   -451   -533       O
ATOM   4178  CB  GLN A 543     -35.431 -54.544 -49.644  1.00 25.24           C
ANISOU 4178  CB  GLN A 543     3438   3145   3005    361   -531   -553       C
ATOM   4179  CG  GLN A 543     -36.442 -54.745 -50.778  1.00 27.50           C
ANISOU 4179  CG  GLN A 543     3724   3475   3249    395   -616   -637       C
ATOM   4180  CD  GLN A 543     -36.127 -55.938 -51.683  1.00 31.29           C
ANISOU 4180  CD  GLN A 543     4256   3931   3701    434   -667   -731       C
ATOM   4181  OE1 GLN A 543     -36.188 -57.097 -51.259  1.00 33.50           O
ANISOU 4181  OE1 GLN A 543     4538   4132   4056    380   -693   -778       O
ATOM   4182  NE2 GLN A 543     -35.810 -55.657 -52.939  1.00 32.88           N
ANISOU 4182  NE2 GLN A 543     4502   4199   3793    531   -680   -759       N
ATOM   4183  N   TYR A 544     -33.853 -55.484 -46.742  1.00 22.03           N
ANISOU 4183  N   TYR A 544     3018   2593   2760    237   -416   -443       N
ATOM   4184  CA  TYR A 544     -32.588 -55.656 -46.014  1.00 21.11           C
ANISOU 4184  CA  TYR A 544     2917   2447   2656    239   -356   -392       C
ATOM   4185  C   TYR A 544     -32.511 -56.962 -45.227  1.00 21.23           C
ANISOU 4185  C   TYR A 544     2938   2380   2748    192   -364   -407       C
ATOM   4186  O   TYR A 544     -31.422 -57.512 -45.075  1.00 21.25           O
ANISOU 4186  O   TYR A 544     2971   2354   2749    218   -335   -396       O
ATOM   4187  CB  TYR A 544     -32.362 -54.513 -45.032  1.00 20.15           C
ANISOU 4187  CB  TYR A 544     2760   2350   2544    214   -300   -311       C
ATOM   4188  CG  TYR A 544     -31.833 -53.233 -45.638  1.00 18.99           C
ANISOU 4188  CG  TYR A 544     2619   2268   2329    268   -262   -273       C
ATOM   4189  CD1 TYR A 544     -30.535 -52.811 -45.376  1.00 18.32           C
ANISOU 4189  CD1 TYR A 544     2542   2192   2228    290   -202   -223       C
ATOM   4190  CD2 TYR A 544     -32.636 -52.424 -46.437  1.00 19.33           C
ANISOU 4190  CD2 TYR A 544     2655   2361   2327    295   -284   -283       C
ATOM   4191  CE1 TYR A 544     -30.037 -51.633 -45.911  1.00 18.22           C
ANISOU 4191  CE1 TYR A 544     2531   2228   2164    333   -161   -183       C
ATOM   4192  CE2 TYR A 544     -32.137 -51.237 -46.982  1.00 18.28           C
ANISOU 4192  CE2 TYR A 544     2531   2280   2135    346   -241   -239       C
ATOM   4193  CZ  TYR A 544     -30.836 -50.854 -46.704  1.00 18.43           C
ANISOU 4193  CZ  TYR A 544     2558   2298   2148    361   -178   -188       C
ATOM   4194  OH  TYR A 544     -30.323 -49.685 -47.218  1.00 18.70           O
ANISOU 4194  OH  TYR A 544     2596   2373   2136    404   -130   -139       O
ATOM   4195  N   TRP A 545     -33.644 -57.439 -44.708  1.00 21.19           N
ANISOU 4195  N   TRP A 545     2902   2337   2813    124   -400   -426       N
ATOM   4196  CA  TRP A 545     -33.643 -58.597 -43.799  1.00 21.18           C
ANISOU 4196  CA  TRP A 545     2902   2252   2896     72   -397   -422       C
ATOM   4197  C   TRP A 545     -33.527 -59.910 -44.567  1.00 22.08           C
ANISOU 4197  C   TRP A 545     3061   2304   3025     90   -441   -501       C
ATOM   4198  O   TRP A 545     -34.496 -60.665 -44.731  1.00 22.18           O
ANISOU 4198  O   TRP A 545     3062   2269   3096     45   -493   -557       O
ATOM   4199  CB  TRP A 545     -34.874 -58.596 -42.892  1.00 21.22           C
ANISOU 4199  CB  TRP A 545     2850   2236   2974     -9   -407   -402       C
ATOM   4200  CG  TRP A 545     -34.779 -59.603 -41.766  1.00 21.29           C
ANISOU 4200  CG  TRP A 545     2859   2165   3065    -59   -384   -370       C
ATOM   4201  CD1 TRP A 545     -35.555 -60.709 -41.592  1.00 22.21           C
ANISOU 4201  CD1 TRP A 545     2967   2207   3267   -115   -414   -402       C
ATOM   4202  CD2 TRP A 545     -33.849 -59.590 -40.675  1.00 20.61           C
ANISOU 4202  CD2 TRP A 545     2781   2066   2983    -56   -325   -297       C
ATOM   4203  NE1 TRP A 545     -35.170 -61.390 -40.459  1.00 21.88           N
ANISOU 4203  NE1 TRP A 545     2931   2103   3280   -143   -372   -346       N
ATOM   4204  CE2 TRP A 545     -34.127 -60.721 -39.875  1.00 21.13           C
ANISOU 4204  CE2 TRP A 545     2847   2050   3132   -104   -319   -282       C
ATOM   4205  CE3 TRP A 545     -32.813 -58.729 -40.291  1.00 20.45           C
ANISOU 4205  CE3 TRP A 545     2766   2098   2908    -17   -277   -243       C
ATOM   4206  CZ2 TRP A 545     -33.405 -61.014 -38.719  1.00 21.49           C
ANISOU 4206  CZ2 TRP A 545     2900   2069   3194   -106   -269   -213       C
ATOM   4207  CZ3 TRP A 545     -32.097 -59.017 -39.138  1.00 20.60           C
ANISOU 4207  CZ3 TRP A 545     2788   2093   2948    -24   -234   -183       C
ATOM   4208  CH2 TRP A 545     -32.400 -60.152 -38.363  1.00 20.90           C
ANISOU 4208  CH2 TRP A 545     2829   2055   3057    -63   -231   -167       C
ATOM   4209  N   LYS A 546     -32.315 -60.168 -45.040  1.00 22.17           N
ANISOU 4209  N   LYS A 546     3121   2315   2987    158   -418   -507       N
ATOM   4210  CA  LYS A 546     -32.000 -61.393 -45.757  1.00 23.29           C
ANISOU 4210  CA  LYS A 546     3316   2398   3135    190   -451   -581       C
ATOM   4211  C   LYS A 546     -30.505 -61.670 -45.617  1.00 22.87           C
ANISOU 4211  C   LYS A 546     3302   2335   3053    250   -399   -546       C
ATOM   4212  O   LYS A 546     -29.730 -60.753 -45.350  1.00 21.77           O
ANISOU 4212  O   LYS A 546     3148   2255   2868    277   -347   -481       O
ATOM   4213  CB  LYS A 546     -32.422 -61.300 -47.232  1.00 24.53           C
ANISOU 4213  CB  LYS A 546     3496   2598   3226    240   -509   -668       C
ATOM   4214  CG  LYS A 546     -32.000 -60.035 -47.951  1.00 24.99           C
ANISOU 4214  CG  LYS A 546     3555   2760   3180    308   -484   -641       C
ATOM   4215  CD  LYS A 546     -32.438 -60.009 -49.427  1.00 25.91           C
ANISOU 4215  CD  LYS A 546     3699   2924   3220    368   -544   -726       C
ATOM   4216  CE  LYS A 546     -33.889 -59.577 -49.626  1.00 27.09           C
ANISOU 4216  CE  LYS A 546     3803   3105   3384    325   -604   -758       C
ATOM   4217  NZ  LYS A 546     -34.194 -59.245 -51.063  1.00 27.58           N
ANISOU 4217  NZ  LYS A 546     3889   3242   3348    401   -654   -824       N
ATOM   4218  N   PRO A 547     -30.092 -62.938 -45.765  1.00 23.67           N
ANISOU 4218  N   PRO A 547     3449   2358   3186    269   -411   -589       N
ATOM   4219  CA  PRO A 547     -28.688 -63.287 -45.513  1.00 23.81           C
ANISOU 4219  CA  PRO A 547     3498   2364   3185    326   -359   -552       C
ATOM   4220  C   PRO A 547     -27.646 -62.494 -46.310  1.00 23.53           C
ANISOU 4220  C   PRO A 547     3475   2415   3048    412   -325   -538       C
ATOM   4221  O   PRO A 547     -26.603 -62.150 -45.760  1.00 22.97           O
ANISOU 4221  O   PRO A 547     3392   2372   2965    436   -269   -471       O
ATOM   4222  CB  PRO A 547     -28.617 -64.764 -45.902  1.00 24.79           C
ANISOU 4222  CB  PRO A 547     3678   2390   3350    344   -392   -625       C
ATOM   4223  CG  PRO A 547     -29.990 -65.269 -45.733  1.00 25.60           C
ANISOU 4223  CG  PRO A 547     3764   2430   3534    261   -446   -669       C
ATOM   4224  CD  PRO A 547     -30.914 -64.130 -46.042  1.00 25.03           C
ANISOU 4224  CD  PRO A 547     3643   2441   3426    232   -471   -671       C
ATOM   4225  N   SER A 548     -27.926 -62.208 -47.581  1.00 23.93           N
ANISOU 4225  N   SER A 548     3547   2514   3031    459   -356   -600       N
ATOM   4226  CA  SER A 548     -26.940 -61.548 -48.443  1.00 24.02           C
ANISOU 4226  CA  SER A 548     3576   2606   2946    549   -318   -586       C
ATOM   4227  C   SER A 548     -26.552 -60.155 -47.940  1.00 22.75           C
ANISOU 4227  C   SER A 548     3364   2518   2761    536   -261   -493       C
ATOM   4228  O   SER A 548     -25.429 -59.701 -48.170  1.00 22.83           O
ANISOU 4228  O   SER A 548     3375   2576   2723    593   -207   -451       O
ATOM   4229  CB  SER A 548     -27.428 -61.480 -49.893  1.00 24.88           C
ANISOU 4229  CB  SER A 548     3719   2757   2977    605   -364   -667       C
ATOM   4230  OG  SER A 548     -28.710 -60.886 -49.988  1.00 25.88           O
ANISOU 4230  OG  SER A 548     3813   2909   3111    554   -410   -683       O
ATOM   4231  N   THR A 549     -27.467 -59.492 -47.243  1.00 21.90           N
ANISOU 4231  N   THR A 549     3212   2418   2693    462   -273   -462       N
ATOM   4232  CA  THR A 549     -27.185 -58.175 -46.666  1.00 20.72           C
ANISOU 4232  CA  THR A 549     3017   2325   2532    443   -224   -380       C
ATOM   4233  C   THR A 549     -26.017 -58.238 -45.686  1.00 20.40           C
ANISOU 4233  C   THR A 549     2959   2273   2518    440   -170   -317       C
ATOM   4234  O   THR A 549     -25.247 -57.275 -45.554  1.00 19.74           O
ANISOU 4234  O   THR A 549     2850   2243   2409    456   -121   -261       O
ATOM   4235  CB  THR A 549     -28.412 -57.617 -45.925  1.00 20.42           C
ANISOU 4235  CB  THR A 549     2935   2283   2539    363   -247   -363       C
ATOM   4236  OG1 THR A 549     -29.514 -57.514 -46.828  1.00 21.26           O
ANISOU 4236  OG1 THR A 549     3048   2410   2621    366   -301   -421       O
ATOM   4237  CG2 THR A 549     -28.113 -56.243 -45.315  1.00 19.61           C
ANISOU 4237  CG2 THR A 549     2790   2233   2426    345   -197   -286       C
ATOM   4238  N   PHE A 550     -25.885 -59.380 -45.010  1.00 20.06           N
ANISOU 4238  N   PHE A 550     2930   2159   2532    422   -181   -327       N
ATOM   4239  CA  PHE A 550     -24.917 -59.540 -43.937  1.00 19.89           C
ANISOU 4239  CA  PHE A 550     2891   2127   2541    417   -139   -267       C
ATOM   4240  C   PHE A 550     -23.768 -60.471 -44.317  1.00 20.56           C
ANISOU 4240  C   PHE A 550     3011   2190   2611    489   -122   -282       C
ATOM   4241  O   PHE A 550     -23.071 -60.999 -43.452  1.00 20.58           O
ANISOU 4241  O   PHE A 550     3008   2165   2648    491   -101   -246       O
ATOM   4242  CB  PHE A 550     -25.649 -60.011 -42.680  1.00 19.95           C
ANISOU 4242  CB  PHE A 550     2880   2075   2623    343   -155   -246       C
ATOM   4243  CG  PHE A 550     -26.860 -59.178 -42.357  1.00 19.42           C
ANISOU 4243  CG  PHE A 550     2778   2029   2571    278   -173   -237       C
ATOM   4244  CD1 PHE A 550     -28.139 -59.640 -42.645  1.00 20.01           C
ANISOU 4244  CD1 PHE A 550     2859   2065   2679    238   -221   -287       C
ATOM   4245  CD2 PHE A 550     -26.713 -57.907 -41.810  1.00 19.61           C
ANISOU 4245  CD2 PHE A 550     2760   2112   2579    258   -142   -183       C
ATOM   4246  CE1 PHE A 550     -29.261 -58.860 -42.360  1.00 19.99           C
ANISOU 4246  CE1 PHE A 550     2818   2088   2690    184   -236   -277       C
ATOM   4247  CE2 PHE A 550     -27.821 -57.117 -41.519  1.00 19.01           C
ANISOU 4247  CE2 PHE A 550     2654   2055   2515    207   -155   -176       C
ATOM   4248  CZ  PHE A 550     -29.099 -57.590 -41.795  1.00 19.02           C
ANISOU 4248  CZ  PHE A 550     2658   2024   2546    172   -201   -220       C
ATOM   4249  N   GLY A 551     -23.545 -60.633 -45.616  1.00 21.10           N
ANISOU 4249  N   GLY A 551     3116   2278   2621    556   -128   -333       N
ATOM   4250  CA  GLY A 551     -22.470 -61.482 -46.115  1.00 21.96           C
ANISOU 4250  CA  GLY A 551     3262   2373   2707    637   -108   -353       C
ATOM   4251  C   GLY A 551     -22.777 -62.969 -46.138  1.00 22.91           C
ANISOU 4251  C   GLY A 551     3436   2398   2872    643   -147   -414       C
ATOM   4252  O   GLY A 551     -21.864 -63.784 -46.266  1.00 23.58           O
ANISOU 4252  O   GLY A 551     3550   2456   2953    706   -128   -423       O
ATOM   4253  N   GLY A 552     -24.057 -63.322 -46.045  1.00 23.34           N
ANISOU 4253  N   GLY A 552     3499   2398   2971    580   -200   -457       N
ATOM   4254  CA  GLY A 552     -24.486 -64.718 -46.141  1.00 24.42           C
ANISOU 4254  CA  GLY A 552     3686   2432   3162    575   -242   -523       C
ATOM   4255  C   GLY A 552     -24.943 -65.252 -44.799  1.00 24.55           C
ANISOU 4255  C   GLY A 552     3683   2372   3273    498   -243   -480       C
ATOM   4256  O   GLY A 552     -25.011 -64.510 -43.818  1.00 23.25           O
ANISOU 4256  O   GLY A 552     3468   2242   3125    449   -217   -406       O
ATOM   4257  N   GLU A 553     -25.247 -66.548 -44.752  1.00 25.84           N
ANISOU 4257  N   GLU A 553     3890   2429   3499    489   -271   -526       N
ATOM   4258  CA  GLU A 553     -25.817 -67.152 -43.547  1.00 26.70           C
ANISOU 4258  CA  GLU A 553     3985   2455   3704    414   -270   -485       C
ATOM   4259  C   GLU A 553     -24.908 -67.025 -42.322  1.00 26.16           C
ANISOU 4259  C   GLU A 553     3892   2401   3644    424   -214   -384       C
ATOM   4260  O   GLU A 553     -25.399 -66.911 -41.199  1.00 25.39           O
ANISOU 4260  O   GLU A 553     3762   2289   3597    359   -203   -323       O
ATOM   4261  CB  GLU A 553     -26.197 -68.622 -43.791  1.00 28.26           C
ANISOU 4261  CB  GLU A 553     4240   2523   3974    408   -305   -552       C
ATOM   4262  CG  GLU A 553     -27.326 -68.826 -44.818  1.00 30.85           C
ANISOU 4262  CG  GLU A 553     4583   2826   4313    377   -374   -658       C
ATOM   4263  CD  GLU A 553     -28.709 -68.391 -44.324  1.00 33.09           C
ANISOU 4263  CD  GLU A 553     4811   3109   4653    270   -401   -646       C
ATOM   4264  OE1 GLU A 553     -28.847 -67.975 -43.154  1.00 33.31           O
ANISOU 4264  OE1 GLU A 553     4793   3150   4713    220   -364   -555       O
ATOM   4265  OE2 GLU A 553     -29.672 -68.467 -45.122  1.00 36.42           O
ANISOU 4265  OE2 GLU A 553     5232   3522   5084    241   -462   -731       O
ATOM   4266  N   VAL A 554     -23.593 -67.010 -42.530  1.00 26.29           N
ANISOU 4266  N   VAL A 554     3921   2458   3610    508   -180   -365       N
ATOM   4267  CA  VAL A 554     -22.653 -66.877 -41.412  1.00 26.34           C
ANISOU 4267  CA  VAL A 554     3899   2490   3619    525   -133   -275       C
ATOM   4268  C   VAL A 554     -22.814 -65.522 -40.712  1.00 25.15           C
ANISOU 4268  C   VAL A 554     3680   2429   3445    475   -116   -214       C
ATOM   4269  O   VAL A 554     -22.822 -65.445 -39.482  1.00 24.76           O
ANISOU 4269  O   VAL A 554     3604   2379   3427    440    -99   -147       O
ATOM   4270  CB  VAL A 554     -21.185 -67.082 -41.865  1.00 26.79           C
ANISOU 4270  CB  VAL A 554     3972   2582   3626    629   -101   -272       C
ATOM   4271  CG1 VAL A 554     -20.215 -66.932 -40.682  1.00 27.39           C
ANISOU 4271  CG1 VAL A 554     4009   2693   3705    647    -61   -182       C
ATOM   4272  CG2 VAL A 554     -21.022 -68.449 -42.493  1.00 28.67           C
ANISOU 4272  CG2 VAL A 554     4282   2725   3888    684   -116   -334       C
ATOM   4273  N   GLY A 555     -22.962 -64.457 -41.496  1.00 24.48           N
ANISOU 4273  N   GLY A 555     3574   2423   3305    475   -121   -237       N
ATOM   4274  CA  GLY A 555     -23.200 -63.127 -40.945  1.00 23.46           C
ANISOU 4274  CA  GLY A 555     3387   2370   3158    428   -107   -189       C
ATOM   4275  C   GLY A 555     -24.565 -63.003 -40.297  1.00 22.87           C
ANISOU 4275  C   GLY A 555     3294   2264   3132    341   -131   -182       C
ATOM   4276  O   GLY A 555     -24.700 -62.446 -39.215  1.00 22.57           O
ANISOU 4276  O   GLY A 555     3217   2251   3108    300   -114   -125       O
ATOM   4277  N   PHE A 556     -25.579 -63.531 -40.972  1.00 23.09           N
ANISOU 4277  N   PHE A 556     3348   2240   3186    316   -172   -246       N
ATOM   4278  CA  PHE A 556     -26.961 -63.479 -40.493  1.00 23.21           C
ANISOU 4278  CA  PHE A 556     3340   2224   3254    233   -197   -246       C
ATOM   4279  C   PHE A 556     -27.075 -64.200 -39.143  1.00 23.51           C
ANISOU 4279  C   PHE A 556     3374   2200   3360    195   -177   -187       C
ATOM   4280  O   PHE A 556     -27.771 -63.736 -38.236  1.00 23.23           O
ANISOU 4280  O   PHE A 556     3299   2178   3348    137   -168   -142       O
ATOM   4281  CB  PHE A 556     -27.868 -64.125 -41.551  1.00 23.97           C
ANISOU 4281  CB  PHE A 556     3467   2269   3372    221   -250   -336       C
ATOM   4282  CG  PHE A 556     -29.319 -63.705 -41.500  1.00 24.39           C
ANISOU 4282  CG  PHE A 556     3482   2327   3458    145   -283   -352       C
ATOM   4283  CD1 PHE A 556     -29.698 -62.392 -41.224  1.00 24.01           C
ANISOU 4283  CD1 PHE A 556     3385   2362   3377    121   -271   -315       C
ATOM   4284  CD2 PHE A 556     -30.312 -64.630 -41.803  1.00 26.28           C
ANISOU 4284  CD2 PHE A 556     3734   2488   3765    101   -329   -412       C
ATOM   4285  CE1 PHE A 556     -31.047 -62.028 -41.212  1.00 24.48           C
ANISOU 4285  CE1 PHE A 556     3406   2428   3465     59   -301   -331       C
ATOM   4286  CE2 PHE A 556     -31.655 -64.268 -41.801  1.00 26.87           C
ANISOU 4286  CE2 PHE A 556     3765   2572   3873     33   -362   -430       C
ATOM   4287  CZ  PHE A 556     -32.018 -62.966 -41.506  1.00 25.12           C
ANISOU 4287  CZ  PHE A 556     3493   2437   3612     16   -347   -388       C
ATOM   4288  N   LYS A 557     -26.370 -65.322 -39.009  1.00 23.87           N
ANISOU 4288  N   LYS A 557     3461   2179   3431    235   -167   -184       N
ATOM   4289  CA  LYS A 557     -26.360 -66.088 -37.758  1.00 24.46           C
ANISOU 4289  CA  LYS A 557     3539   2191   3564    214   -142   -119       C
ATOM   4290  C   LYS A 557     -25.760 -65.300 -36.591  1.00 23.44           C
ANISOU 4290  C   LYS A 557     3369   2136   3401    219   -104    -35       C
ATOM   4291  O   LYS A 557     -26.209 -65.442 -35.448  1.00 23.26           O
ANISOU 4291  O   LYS A 557     3329   2094   3414    179    -87     24       O
ATOM   4292  CB  LYS A 557     -25.607 -67.416 -37.936  1.00 25.72           C
ANISOU 4292  CB  LYS A 557     3757   2265   3752    271   -137   -132       C
ATOM   4293  CG  LYS A 557     -25.255 -68.089 -36.609  1.00 28.34           C
ANISOU 4293  CG  LYS A 557     4094   2551   4124    275   -101    -47       C
ATOM   4294  CD  LYS A 557     -24.736 -69.506 -36.743  1.00 32.50           C
ANISOU 4294  CD  LYS A 557     4682   2971   4695    325    -96    -57       C
ATOM   4295  CE  LYS A 557     -24.569 -70.119 -35.344  1.00 34.08           C
ANISOU 4295  CE  LYS A 557     4885   3127   4936    325    -58     39       C
ATOM   4296  NZ  LYS A 557     -23.555 -71.206 -35.298  1.00 36.97           N
ANISOU 4296  NZ  LYS A 557     5304   3429   5315    407    -40     54       N
ATOM   4297  N   ILE A 558     -24.754 -64.471 -36.869  1.00 22.43           N
ANISOU 4297  N   ILE A 558     3223   2093   3205    269    -91    -30       N
ATOM   4298  CA  ILE A 558     -24.157 -63.643 -35.822  1.00 21.78           C
ANISOU 4298  CA  ILE A 558     3099   2086   3091    272    -64     36       C
ATOM   4299  C   ILE A 558     -25.230 -62.752 -35.198  1.00 21.07           C
ANISOU 4299  C   ILE A 558     2969   2029   3008    200    -66     57       C
ATOM   4300  O   ILE A 558     -25.272 -62.586 -33.976  1.00 20.77           O
ANISOU 4300  O   ILE A 558     2909   2008   2974    182    -47    116       O
ATOM   4301  CB  ILE A 558     -22.972 -62.791 -36.341  1.00 21.42           C
ANISOU 4301  CB  ILE A 558     3030   2126   2981    325    -51     31       C
ATOM   4302  CG1 ILE A 558     -21.798 -63.695 -36.735  1.00 21.91           C
ANISOU 4302  CG1 ILE A 558     3124   2164   3036    405    -40     24       C
ATOM   4303  CG2 ILE A 558     -22.513 -61.790 -35.276  1.00 20.67           C
ANISOU 4303  CG2 ILE A 558     2884   2109   2861    313    -32     86       C
ATOM   4304  CD1 ILE A 558     -20.718 -62.994 -37.549  1.00 22.15           C
ANISOU 4304  CD1 ILE A 558     3135   2272   3011    459    -25      9       C
ATOM   4305  N   ILE A 559     -26.114 -62.206 -36.033  1.00 20.33           N
ANISOU 4305  N   ILE A 559     2867   1946   2912    166    -89      8       N
ATOM   4306  CA  ILE A 559     -27.192 -61.356 -35.540  1.00 20.10           C
ANISOU 4306  CA  ILE A 559     2799   1948   2890    104    -91     23       C
ATOM   4307  C   ILE A 559     -28.206 -62.170 -34.752  1.00 20.27           C
ANISOU 4307  C   ILE A 559     2822   1902   2978     52    -90     49       C
ATOM   4308  O   ILE A 559     -28.564 -61.823 -33.627  1.00 19.90           O
ANISOU 4308  O   ILE A 559     2748   1877   2937     23    -68    103       O
ATOM   4309  CB  ILE A 559     -27.945 -60.650 -36.690  1.00 19.83           C
ANISOU 4309  CB  ILE A 559     2756   1940   2838     87   -119    -35       C
ATOM   4310  CG1 ILE A 559     -27.038 -59.628 -37.379  1.00 19.36           C
ANISOU 4310  CG1 ILE A 559     2689   1956   2712    133   -109    -45       C
ATOM   4311  CG2 ILE A 559     -29.217 -59.985 -36.166  1.00 19.86           C
ANISOU 4311  CG2 ILE A 559     2721   1963   2862     24   -123    -20       C
ATOM   4312  CD1 ILE A 559     -27.635 -59.051 -38.646  1.00 20.04           C
ANISOU 4312  CD1 ILE A 559     2777   2067   2771    136   -134    -98       C
ATOM   4313  N   ASN A 560     -28.672 -63.259 -35.351  1.00 21.23           N
ANISOU 4313  N   ASN A 560     2975   1939   3152     40   -112      9       N
ATOM   4314  CA  ASN A 560     -29.805 -63.985 -34.792  1.00 21.87           C
ANISOU 4314  CA  ASN A 560     3051   1950   3310    -22   -112     27       C
ATOM   4315  C   ASN A 560     -29.475 -64.853 -33.568  1.00 22.39           C
ANISOU 4315  C   ASN A 560     3131   1964   3411    -16    -74    103       C
ATOM   4316  O   ASN A 560     -30.391 -65.357 -32.910  1.00 22.99           O
ANISOU 4316  O   ASN A 560     3196   1988   3551    -69    -60    138       O
ATOM   4317  CB  ASN A 560     -30.496 -64.784 -35.898  1.00 22.72           C
ANISOU 4317  CB  ASN A 560     3180   1982   3468    -44   -154    -51       C
ATOM   4318  CG  ASN A 560     -31.262 -63.889 -36.857  1.00 23.16           C
ANISOU 4318  CG  ASN A 560     3208   2094   3497    -65   -192   -113       C
ATOM   4319  OD1 ASN A 560     -32.087 -63.079 -36.434  1.00 25.53           O
ANISOU 4319  OD1 ASN A 560     3461   2441   3797   -108   -188    -90       O
ATOM   4320  ND2 ASN A 560     -30.977 -64.013 -38.148  1.00 24.70           N
ANISOU 4320  ND2 ASN A 560     3434   2289   3663    -27   -228   -189       N
ATOM   4321  N   THR A 561     -28.183 -64.996 -33.257  1.00 22.20           N
ANISOU 4321  N   THR A 561     3130   1960   3347     50    -55    133       N
ATOM   4322  CA  THR A 561     -27.726 -65.707 -32.056  1.00 22.69           C
ANISOU 4322  CA  THR A 561     3206   1990   3425     72    -19    212       C
ATOM   4323  C   THR A 561     -27.032 -64.791 -31.034  1.00 22.05           C
ANISOU 4323  C   THR A 561     3094   2009   3275    101      4    270       C
ATOM   4324  O   THR A 561     -26.508 -65.278 -30.026  1.00 22.59           O
ANISOU 4324  O   THR A 561     3173   2071   3338    134     30    336       O
ATOM   4325  CB  THR A 561     -26.746 -66.845 -32.416  1.00 23.23           C
ANISOU 4325  CB  THR A 561     3328   1991   3508    136    -18    204       C
ATOM   4326  OG1 THR A 561     -25.523 -66.295 -32.931  1.00 22.70           O
ANISOU 4326  OG1 THR A 561     3260   1996   3371    202    -24    180       O
ATOM   4327  CG2 THR A 561     -27.370 -67.786 -33.445  1.00 24.59           C
ANISOU 4327  CG2 THR A 561     3537   2059   3748    111    -46    135       C
ATOM   4328  N   ALA A 562     -27.017 -63.484 -31.289  1.00 21.26           N
ANISOU 4328  N   ALA A 562     2957   1998   3123     92     -7    244       N
ATOM   4329  CA  ALA A 562     -26.341 -62.543 -30.397  1.00 20.81           C
ANISOU 4329  CA  ALA A 562     2869   2032   3004    115      7    283       C
ATOM   4330  C   ALA A 562     -26.992 -62.522 -29.019  1.00 20.90           C
ANISOU 4330  C   ALA A 562     2865   2053   3021     89     33    349       C
ATOM   4331  O   ALA A 562     -28.199 -62.749 -28.880  1.00 21.01           O
ANISOU 4331  O   ALA A 562     2874   2028   3082     35     41    358       O
ATOM   4332  CB  ALA A 562     -26.325 -61.129 -30.993  1.00 20.24           C
ANISOU 4332  CB  ALA A 562     2763   2038   2889    103     -8    239       C
ATOM   4333  N   SER A 563     -26.172 -62.258 -28.006  1.00 20.86           N
ANISOU 4333  N   SER A 563     2851   2107   2968    130     46    396       N
ATOM   4334  CA  SER A 563     -26.641 -62.110 -26.637  1.00 20.82           C
ANISOU 4334  CA  SER A 563     2832   2132   2946    120     72    459       C
ATOM   4335  C   SER A 563     -25.602 -61.342 -25.835  1.00 20.45           C
ANISOU 4335  C   SER A 563     2764   2180   2826    167     68    475       C
ATOM   4336  O   SER A 563     -24.431 -61.287 -26.217  1.00 20.32           O
ANISOU 4336  O   SER A 563     2747   2190   2786    211     51    454       O
ATOM   4337  CB  SER A 563     -26.893 -63.475 -25.989  1.00 21.90           C
ANISOU 4337  CB  SER A 563     3003   2191   3127    131    101    526       C
ATOM   4338  OG  SER A 563     -25.681 -64.151 -25.700  1.00 21.60           O
ANISOU 4338  OG  SER A 563     2990   2149   3067    202    103    556       O
ATOM   4339  N   ILE A 564     -26.021 -60.749 -24.722  1.00 20.26           N
ANISOU 4339  N   ILE A 564     2721   2212   2766    158     82    510       N
ATOM   4340  CA  ILE A 564     -25.068 -60.047 -23.861  1.00 20.36           C
ANISOU 4340  CA  ILE A 564     2712   2316   2707    202     71    519       C
ATOM   4341  C   ILE A 564     -23.983 -61.016 -23.361  1.00 20.82           C
ANISOU 4341  C   ILE A 564     2791   2370   2748    272     73    564       C
ATOM   4342  O   ILE A 564     -22.802 -60.656 -23.314  1.00 20.01           O
ANISOU 4342  O   ILE A 564     2670   2327   2607    315     49    546       O
ATOM   4343  CB  ILE A 564     -25.774 -59.287 -22.694  1.00 20.50           C
ANISOU 4343  CB  ILE A 564     2712   2395   2684    188     86    544       C
ATOM   4344  CG1 ILE A 564     -24.797 -58.351 -21.971  1.00 21.51           C
ANISOU 4344  CG1 ILE A 564     2815   2621   2739    225     62    527       C
ATOM   4345  CG2 ILE A 564     -26.427 -60.250 -21.718  1.00 21.42           C
ANISOU 4345  CG2 ILE A 564     2852   2478   2809    198    125    625       C
ATOM   4346  CD1 ILE A 564     -24.315 -57.178 -22.810  1.00 21.37           C
ANISOU 4346  CD1 ILE A 564     2765   2636   2718    203     32    453       C
ATOM   4347  N   GLN A 565     -24.366 -62.251 -23.030  1.00 21.71           N
ANISOU 4347  N   GLN A 565     2940   2411   2896    284    101    624       N
ATOM   4348  CA  GLN A 565     -23.382 -63.245 -22.594  1.00 22.72           C
ANISOU 4348  CA  GLN A 565     3095   2527   3012    358    105    673       C
ATOM   4349  C   GLN A 565     -22.383 -63.581 -23.701  1.00 22.72           C
ANISOU 4349  C   GLN A 565     3101   2501   3032    388     82    627       C
ATOM   4350  O   GLN A 565     -21.180 -63.678 -23.442  1.00 22.79           O
ANISOU 4350  O   GLN A 565     3100   2557   3002    454     68    637       O
ATOM   4351  CB  GLN A 565     -24.049 -64.531 -22.093  1.00 23.75           C
ANISOU 4351  CB  GLN A 565     3267   2568   3188    362    147    751       C
ATOM   4352  CG  GLN A 565     -23.048 -65.606 -21.626  1.00 26.03           C
ANISOU 4352  CG  GLN A 565     3588   2836   3464    447    155    810       C
ATOM   4353  CD  GLN A 565     -22.203 -65.173 -20.428  1.00 28.02           C
ANISOU 4353  CD  GLN A 565     3821   3202   3624    516    144    849       C
ATOM   4354  OE1 GLN A 565     -22.592 -65.393 -19.280  1.00 28.48           O
ANISOU 4354  OE1 GLN A 565     3891   3280   3649    538    173    922       O
ATOM   4355  NE2 GLN A 565     -21.032 -64.569 -20.692  1.00 25.87           N
ANISOU 4355  NE2 GLN A 565     3516   3005   3309    553    103    799       N
ATOM   4356  N   SER A 566     -22.866 -63.769 -24.926  1.00 22.49           N
ANISOU 4356  N   SER A 566     3085   2401   3059    346     78    577       N
ATOM   4357  CA  SER A 566     -21.959 -64.110 -26.028  1.00 23.11           C
ANISOU 4357  CA  SER A 566     3173   2456   3151    381     61    532       C
ATOM   4358  C   SER A 566     -21.092 -62.910 -26.439  1.00 21.99           C
ANISOU 4358  C   SER A 566     2984   2409   2963    390     36    481       C
ATOM   4359  O   SER A 566     -19.931 -63.087 -26.795  1.00 21.78           O
ANISOU 4359  O   SER A 566     2949   2404   2921    445     27    470       O
ATOM   4360  CB  SER A 566     -22.706 -64.724 -27.230  1.00 23.10           C
ANISOU 4360  CB  SER A 566     3206   2355   3218    342     61    488       C
ATOM   4361  OG  SER A 566     -23.461 -63.763 -27.930  1.00 25.91           O
ANISOU 4361  OG  SER A 566     3537   2732   3577    280     47    431       O
ATOM   4362  N   LEU A 567     -21.642 -61.697 -26.368  1.00 21.27           N
ANISOU 4362  N   LEU A 567     2859   2370   2852    338     28    453       N
ATOM   4363  CA  LEU A 567     -20.860 -60.483 -26.630  1.00 20.82           C
ANISOU 4363  CA  LEU A 567     2756   2398   2758    339      9    411       C
ATOM   4364  C   LEU A 567     -19.640 -60.429 -25.707  1.00 21.06           C
ANISOU 4364  C   LEU A 567     2759   2501   2743    398     -3    439       C
ATOM   4365  O   LEU A 567     -18.515 -60.203 -26.153  1.00 21.39           O
ANISOU 4365  O   LEU A 567     2771   2582   2774    431    -16    417       O
ATOM   4366  CB  LEU A 567     -21.714 -59.226 -26.439  1.00 20.43           C
ANISOU 4366  CB  LEU A 567     2680   2386   2695    278      5    387       C
ATOM   4367  CG  LEU A 567     -21.043 -57.886 -26.773  1.00 20.05           C
ANISOU 4367  CG  LEU A 567     2586   2409   2623    267    -11    342       C
ATOM   4368  CD1 LEU A 567     -20.762 -57.774 -28.269  1.00 20.81           C
ANISOU 4368  CD1 LEU A 567     2684   2481   2743    264    -11    299       C
ATOM   4369  CD2 LEU A 567     -21.923 -56.738 -26.284  1.00 19.88           C
ANISOU 4369  CD2 LEU A 567     2546   2420   2587    217    -12    328       C
ATOM   4370  N   ILE A 568     -19.872 -60.659 -24.422  1.00 20.94           N
ANISOU 4370  N   ILE A 568     2749   2507   2699    414      2    491       N
ATOM   4371  CA  ILE A 568     -18.792 -60.667 -23.430  1.00 21.51           C
ANISOU 4371  CA  ILE A 568     2797   2656   2720    476    -15    519       C
ATOM   4372  C   ILE A 568     -17.872 -61.881 -23.599  1.00 22.14           C
ANISOU 4372  C   ILE A 568     2897   2705   2810    551    -12    552       C
ATOM   4373  O   ILE A 568     -16.650 -61.745 -23.561  1.00 22.26           O
ANISOU 4373  O   ILE A 568     2875   2781   2801    600    -33    543       O
ATOM   4374  CB  ILE A 568     -19.367 -60.570 -21.987  1.00 21.61           C
ANISOU 4374  CB  ILE A 568     2815   2706   2687    481    -10    567       C
ATOM   4375  CG1 ILE A 568     -19.542 -59.096 -21.586  1.00 21.04           C
ANISOU 4375  CG1 ILE A 568     2702   2713   2579    440    -31    521       C
ATOM   4376  CG2 ILE A 568     -18.464 -61.272 -20.976  1.00 21.63           C
ANISOU 4376  CG2 ILE A 568     2821   2753   2645    566    -18    623       C
ATOM   4377  CD1 ILE A 568     -20.497 -58.281 -22.491  1.00 20.55           C
ANISOU 4377  CD1 ILE A 568     2637   2615   2556    362    -22    471       C
ATOM   4378  N   CYS A 569     -18.450 -63.062 -23.804  1.00 22.72           N
ANISOU 4378  N   CYS A 569     3026   2681   2925    559     15    588       N
ATOM   4379  CA  CYS A 569     -17.656 -64.289 -23.927  1.00 23.89           C
ANISOU 4379  CA  CYS A 569     3203   2787   3087    635     23    623       C
ATOM   4380  C   CYS A 569     -16.654 -64.219 -25.086  1.00 23.61           C
ANISOU 4380  C   CYS A 569     3147   2760   3064    662     10    571       C
ATOM   4381  O   CYS A 569     -15.496 -64.625 -24.947  1.00 24.05           O
ANISOU 4381  O   CYS A 569     3187   2851   3101    738      2    588       O
ATOM   4382  CB  CYS A 569     -18.573 -65.502 -24.108  1.00 24.59           C
ANISOU 4382  CB  CYS A 569     3358   2750   3234    624     56    659       C
ATOM   4383  SG  CYS A 569     -17.748 -67.081 -23.895  1.00 27.55           S
ANISOU 4383  SG  CYS A 569     3780   3061   3625    724     72    722       S
ATOM   4384  N   ASN A 570     -17.103 -63.699 -26.222  1.00 23.26           N
ANISOU 4384  N   ASN A 570     3100   2689   3049    606     11    510       N
ATOM   4385  CA  ASN A 570     -16.256 -63.597 -27.409  1.00 23.33           C
ANISOU 4385  CA  ASN A 570     3092   2706   3066    631      7    463       C
ATOM   4386  C   ASN A 570     -15.163 -62.535 -27.317  1.00 23.10           C
ANISOU 4386  C   ASN A 570     2989   2788   3001    644    -12    441       C
ATOM   4387  O   ASN A 570     -14.155 -62.631 -28.024  1.00 23.77           O
ANISOU 4387  O   ASN A 570     3051   2895   3087    689    -10    423       O
ATOM   4388  CB  ASN A 570     -17.110 -63.318 -28.648  1.00 22.95           C
ANISOU 4388  CB  ASN A 570     3065   2603   3051    572     12    407       C
ATOM   4389  CG  ASN A 570     -17.905 -64.528 -29.103  1.00 24.24           C
ANISOU 4389  CG  ASN A 570     3297   2649   3263    569     26    409       C
ATOM   4390  OD1 ASN A 570     -17.434 -65.666 -29.023  1.00 27.56           O
ANISOU 4390  OD1 ASN A 570     3754   3019   3700    630     35    436       O
ATOM   4391  ND2 ASN A 570     -19.115 -64.288 -29.595  1.00 23.49           N
ANISOU 4391  ND2 ASN A 570     3219   2508   3196    499     24    377       N
ATOM   4392  N   ASN A 571     -15.359 -61.521 -26.476  1.00 22.37           N
ANISOU 4392  N   ASN A 571     2857   2763   2879    604    -29    441       N
ATOM   4393  CA  ASN A 571     -14.492 -60.334 -26.497  1.00 22.22           C
ANISOU 4393  CA  ASN A 571     2765   2838   2839    594    -48    407       C
ATOM   4394  C   ASN A 571     -13.819 -59.964 -25.179  1.00 22.41           C
ANISOU 4394  C   ASN A 571     2742   2953   2820    621    -78    428       C
ATOM   4395  O   ASN A 571     -13.123 -58.948 -25.107  1.00 23.32           O
ANISOU 4395  O   ASN A 571     2792   3144   2926    604    -99    395       O
ATOM   4396  CB  ASN A 571     -15.290 -59.132 -26.996  1.00 21.41           C
ANISOU 4396  CB  ASN A 571     2651   2736   2748    511    -46    363       C
ATOM   4397  CG  ASN A 571     -15.819 -59.332 -28.392  1.00 21.01           C
ANISOU 4397  CG  ASN A 571     2636   2616   2732    490    -24    334       C
ATOM   4398  OD1 ASN A 571     -15.052 -59.397 -29.351  1.00 21.88           O
ANISOU 4398  OD1 ASN A 571     2731   2731   2850    519    -14    315       O
ATOM   4399  ND2 ASN A 571     -17.139 -59.434 -28.517  1.00 19.64           N
ANISOU 4399  ND2 ASN A 571     2506   2382   2574    442    -17    330       N
ATOM   4400  N   VAL A 572     -14.024 -60.761 -24.139  1.00 22.65           N
ANISOU 4400  N   VAL A 572     2805   2977   2825    662    -80    481       N
ATOM   4401  CA  VAL A 572     -13.437 -60.472 -22.839  1.00 22.63           C
ANISOU 4401  CA  VAL A 572     2764   3067   2769    698   -112    501       C
ATOM   4402  C   VAL A 572     -12.665 -61.705 -22.388  1.00 23.76           C
ANISOU 4402  C   VAL A 572     2922   3212   2895    796   -113    558       C
ATOM   4403  O   VAL A 572     -13.196 -62.816 -22.402  1.00 23.67           O
ANISOU 4403  O   VAL A 572     2977   3118   2901    823    -84    606       O
ATOM   4404  CB  VAL A 572     -14.509 -60.069 -21.802  1.00 22.32           C
ANISOU 4404  CB  VAL A 572     2748   3037   2697    661   -114    516       C
ATOM   4405  CG1 VAL A 572     -13.884 -59.864 -20.420  1.00 22.35           C
ANISOU 4405  CG1 VAL A 572     2719   3142   2633    712   -151    535       C
ATOM   4406  CG2 VAL A 572     -15.248 -58.794 -22.258  1.00 20.96           C
ANISOU 4406  CG2 VAL A 572     2559   2863   2541    571   -114    458       C
ATOM   4407  N   LYS A 573     -11.406 -61.498 -22.013  1.00 24.62           N
ANISOU 4407  N   LYS A 573     2966   3413   2976    849   -146    552       N
ATOM   4408  CA  LYS A 573     -10.511 -62.591 -21.621  1.00 25.94           C
ANISOU 4408  CA  LYS A 573     3136   3596   3123    953   -151    605       C
ATOM   4409  C   LYS A 573     -11.146 -63.443 -20.528  1.00 26.41           C
ANISOU 4409  C   LYS A 573     3259   3628   3146    996   -140    678       C
ATOM   4410  O   LYS A 573     -11.684 -62.918 -19.548  1.00 26.12           O
ANISOU 4410  O   LYS A 573     3223   3637   3065    974   -155    686       O
ATOM   4411  CB  LYS A 573      -9.160 -62.041 -21.147  1.00 26.68           C
ANISOU 4411  CB  LYS A 573     3137   3815   3184    996   -200    584       C
ATOM   4412  CG  LYS A 573      -8.071 -63.088 -20.922  1.00 29.60           C
ANISOU 4412  CG  LYS A 573     3495   4213   3538   1111   -207    631       C
ATOM   4413  CD  LYS A 573      -6.804 -62.431 -20.382  1.00 32.11           C
ANISOU 4413  CD  LYS A 573     3708   4667   3824   1144   -263    604       C
ATOM   4414  CE  LYS A 573      -5.618 -63.373 -20.396  1.00 35.39           C
ANISOU 4414  CE  LYS A 573     4096   5116   4234   1258   -269    643       C
ATOM   4415  NZ  LYS A 573      -4.383 -62.701 -19.901  1.00 37.06           N
ANISOU 4415  NZ  LYS A 573     4193   5467   4421   1285   -328    611       N
ATOM   4416  N   GLY A 574     -11.100 -64.758 -20.722  1.00 27.08           N
ANISOU 4416  N   GLY A 574     3400   3635   3252   1060   -110    734       N
ATOM   4417  CA  GLY A 574     -11.602 -65.710 -19.736  1.00 27.97           C
ANISOU 4417  CA  GLY A 574     3577   3712   3340   1111    -90    818       C
ATOM   4418  C   GLY A 574     -13.093 -65.982 -19.822  1.00 27.58           C
ANISOU 4418  C   GLY A 574     3596   3555   3326   1042    -47    839       C
ATOM   4419  O   GLY A 574     -13.611 -66.790 -19.052  1.00 28.44           O
ANISOU 4419  O   GLY A 574     3759   3621   3424   1076    -19    916       O
ATOM   4420  N   CYS A 575     -13.779 -65.323 -20.757  1.00 26.85           N
ANISOU 4420  N   CYS A 575     3501   3421   3279    948    -39    776       N
ATOM   4421  CA  CYS A 575     -15.229 -65.465 -20.935  1.00 26.49           C
ANISOU 4421  CA  CYS A 575     3508   3282   3274    874     -4    784       C
ATOM   4422  C   CYS A 575     -15.993 -65.495 -19.605  1.00 26.47           C
ANISOU 4422  C   CYS A 575     3527   3301   3228    875     10    848       C
ATOM   4423  O   CYS A 575     -16.616 -66.501 -19.259  1.00 26.96           O
ANISOU 4423  O   CYS A 575     3648   3283   3314    891     50    919       O
ATOM   4424  CB  CYS A 575     -15.543 -66.705 -21.789  1.00 27.15           C
ANISOU 4424  CB  CYS A 575     3656   3231   3430    883     32    802       C
ATOM   4425  SG  CYS A 575     -17.327 -67.118 -21.907  1.00 28.35           S
ANISOU 4425  SG  CYS A 575     3869   3260   3645    795     74    822       S
ATOM   4426  N   PRO A 576     -15.951 -64.386 -18.851  1.00 25.72           N
ANISOU 4426  N   PRO A 576     3388   3314   3071    858    -19    824       N
ATOM   4427  CA  PRO A 576     -16.644 -64.343 -17.570  1.00 25.96           C
ANISOU 4427  CA  PRO A 576     3438   3379   3047    868     -5    881       C
ATOM   4428  C   PRO A 576     -18.152 -64.385 -17.758  1.00 25.77           C
ANISOU 4428  C   PRO A 576     3453   3270   3070    788     40    894       C
ATOM   4429  O   PRO A 576     -18.660 -63.887 -18.770  1.00 24.36           O
ANISOU 4429  O   PRO A 576     3263   3046   2944    710     40    831       O
ATOM   4430  CB  PRO A 576     -16.235 -62.984 -17.000  1.00 25.57           C
ANISOU 4430  CB  PRO A 576     3327   3458   2930    857    -54    823       C
ATOM   4431  CG  PRO A 576     -16.008 -62.147 -18.200  1.00 24.95           C
ANISOU 4431  CG  PRO A 576     3207   3371   2900    789    -74    733       C
ATOM   4432  CD  PRO A 576     -15.366 -63.078 -19.193  1.00 25.38           C
ANISOU 4432  CD  PRO A 576     3275   3357   3009    822    -63    740       C
ATOM   4433  N   PHE A 577     -18.852 -64.972 -16.791  1.00 26.55           N
ANISOU 4433  N   PHE A 577     3591   3350   3148    811     79    978       N
ATOM   4434  CA  PHE A 577     -20.304 -64.952 -16.789  1.00 27.06           C
ANISOU 4434  CA  PHE A 577     3679   3349   3252    736    123    997       C
ATOM   4435  C   PHE A 577     -20.798 -63.513 -16.696  1.00 26.35           C
ANISOU 4435  C   PHE A 577     3547   3335   3129    674    101    929       C
ATOM   4436  O   PHE A 577     -20.241 -62.703 -15.955  1.00 26.12           O
ANISOU 4436  O   PHE A 577     3486   3417   3020    707     66    906       O
ATOM   4437  CB  PHE A 577     -20.869 -65.752 -15.609  1.00 28.62           C
ANISOU 4437  CB  PHE A 577     3919   3532   3422    780    174   1110       C
ATOM   4438  CG  PHE A 577     -22.355 -65.596 -15.442  1.00 30.28           C
ANISOU 4438  CG  PHE A 577     4140   3699   3666    706    221   1133       C
ATOM   4439  CD1 PHE A 577     -23.232 -66.334 -16.224  1.00 32.46           C
ANISOU 4439  CD1 PHE A 577     4443   3844   4048    642    260   1146       C
ATOM   4440  CD2 PHE A 577     -22.876 -64.684 -14.530  1.00 32.48           C
ANISOU 4440  CD2 PHE A 577     4399   4071   3872    699    225   1134       C
ATOM   4441  CE1 PHE A 577     -24.609 -66.176 -16.093  1.00 33.12           C
ANISOU 4441  CE1 PHE A 577     4525   3891   4168    570    302   1165       C
ATOM   4442  CE2 PHE A 577     -24.250 -64.524 -14.389  1.00 32.74           C
ANISOU 4442  CE2 PHE A 577     4435   4069   3937    634    272   1156       C
ATOM   4443  CZ  PHE A 577     -25.116 -65.269 -15.173  1.00 32.90           C
ANISOU 4443  CZ  PHE A 577     4473   3960   4066    568    311   1174       C
ATOM   4444  N   THR A 578     -21.849 -63.193 -17.441  1.00 25.51           N
ANISOU 4444  N   THR A 578     3442   3167   3086    587    120    893       N
ATOM   4445  CA  THR A 578     -22.501 -61.913 -17.258  1.00 25.32           C
ANISOU 4445  CA  THR A 578     3386   3202   3033    533    110    842       C
ATOM   4446  C   THR A 578     -24.002 -61.996 -17.484  1.00 25.46           C
ANISOU 4446  C   THR A 578     3418   3150   3107    461    155    859       C
ATOM   4447  O   THR A 578     -24.520 -62.978 -18.020  1.00 26.40           O
ANISOU 4447  O   THR A 578     3564   3165   3301    437    186    892       O
ATOM   4448  CB  THR A 578     -21.884 -60.813 -18.140  1.00 24.53           C
ANISOU 4448  CB  THR A 578     3242   3141   2938    500     61    741       C
ATOM   4449  OG1 THR A 578     -22.215 -59.538 -17.581  1.00 24.55           O
ANISOU 4449  OG1 THR A 578     3215   3223   2889    475     46    700       O
ATOM   4450  CG2 THR A 578     -22.387 -60.895 -19.591  1.00 22.59           C
ANISOU 4450  CG2 THR A 578     3001   2805   2778    433     68    696       C
ATOM   4451  N   SER A 579     -24.680 -60.945 -17.052  1.00 25.18           N
ANISOU 4451  N   SER A 579     3359   3173   3036    429    156    833       N
ATOM   4452  CA  SER A 579     -26.127 -60.885 -17.044  1.00 25.31           C
ANISOU 4452  CA  SER A 579     3377   3148   3092    369    199    853       C
ATOM   4453  C   SER A 579     -26.491 -59.439 -16.752  1.00 24.71           C
ANISOU 4453  C   SER A 579     3269   3155   2966    345    182    795       C
ATOM   4454  O   SER A 579     -25.635 -58.673 -16.306  1.00 23.98           O
ANISOU 4454  O   SER A 579     3160   3147   2804    382    143    755       O
ATOM   4455  CB  SER A 579     -26.672 -61.790 -15.937  1.00 26.39           C
ANISOU 4455  CB  SER A 579     3543   3272   3211    405    256    962       C
ATOM   4456  OG  SER A 579     -28.075 -61.692 -15.834  1.00 27.63           O
ANISOU 4456  OG  SER A 579     3692   3399   3406    348    302    987       O
ATOM   4457  N   PHE A 580     -27.742 -59.062 -17.006  1.00 24.22           N
ANISOU 4457  N   PHE A 580     3195   3066   2942    285    209    786       N
ATOM   4458  CA  PHE A 580     -28.240 -57.757 -16.570  1.00 24.40           C
ANISOU 4458  CA  PHE A 580     3193   3162   2916    271    204    743       C
ATOM   4459  C   PHE A 580     -28.860 -57.787 -15.165  1.00 25.83           C
ANISOU 4459  C   PHE A 580     3384   3400   3031    309    248    811       C
ATOM   4460  O   PHE A 580     -29.287 -56.749 -14.654  1.00 25.26           O
ANISOU 4460  O   PHE A 580     3296   3392   2908    310    248    779       O
ATOM   4461  CB  PHE A 580     -29.239 -57.176 -17.586  1.00 23.45           C
ANISOU 4461  CB  PHE A 580     3051   2999   2862    195    207    693       C
ATOM   4462  CG  PHE A 580     -28.613 -56.747 -18.890  1.00 21.89           C
ANISOU 4462  CG  PHE A 580     2841   2774   2702    166    161    615       C
ATOM   4463  CD1 PHE A 580     -29.216 -57.072 -20.098  1.00 20.99           C
ANISOU 4463  CD1 PHE A 580     2724   2583   2669    113    163    595       C
ATOM   4464  CD2 PHE A 580     -27.444 -55.989 -18.914  1.00 21.62           C
ANISOU 4464  CD2 PHE A 580     2796   2796   2624    193    117    561       C
ATOM   4465  CE1 PHE A 580     -28.664 -56.672 -21.300  1.00 20.44           C
ANISOU 4465  CE1 PHE A 580     2647   2495   2625     94    126    528       C
ATOM   4466  CE2 PHE A 580     -26.882 -55.588 -20.120  1.00 20.24           C
ANISOU 4466  CE2 PHE A 580     2608   2597   2485    168     84    499       C
ATOM   4467  CZ  PHE A 580     -27.487 -55.929 -21.312  1.00 20.02           C
ANISOU 4467  CZ  PHE A 580     2583   2496   2527    123     91    484       C
ATOM   4468  N  AASN A 581     -28.912 -58.964 -14.549  0.50 27.03           N
ANISOU 4468  N  AASN A 581     3564   3525   3183    346    289    906       N
ATOM   4469  N  BASN A 581     -28.886 -58.974 -14.554  0.50 27.07           N
ANISOU 4469  N  BASN A 581     3568   3529   3187    347    288    905       N
ATOM   4470  CA AASN A 581     -29.408 -59.078 -13.191  0.50 28.37           C
ANISOU 4470  CA AASN A 581     3746   3752   3282    394    337    982       C
ATOM   4471  CA BASN A 581     -29.435 -59.186 -13.218  0.50 28.46           C
ANISOU 4471  CA BASN A 581     3759   3756   3300    393    341    988       C
ATOM   4472  C  AASN A 581     -28.346 -59.675 -12.282  0.50 29.62           C
ANISOU 4472  C  AASN A 581     3933   3959   3362    486    328   1035       C
ATOM   4473  C  BASN A 581     -28.328 -59.680 -12.286  0.50 29.65           C
ANISOU 4473  C  BASN A 581     3936   3963   3365    486    327   1035       C
ATOM   4474  O  AASN A 581     -27.574 -60.539 -12.702  0.50 29.63           O
ANISOU 4474  O  AASN A 581     3951   3910   3398    504    313   1055       O
ATOM   4475  O  BASN A 581     -27.492 -60.486 -12.702  0.50 29.64           O
ANISOU 4475  O  BASN A 581     3951   3916   3394    506    308   1050       O
ATOM   4476  CB AASN A 581     -30.678 -59.923 -13.163  0.50 28.93           C
ANISOU 4476  CB AASN A 581     3819   3748   3424    354    412   1066       C
ATOM   4477  CB BASN A 581     -30.551 -60.234 -13.303  0.50 29.05           C
ANISOU 4477  CB BASN A 581     3841   3740   3456    354    412   1075       C
ATOM   4478  CG AASN A 581     -30.467 -61.301 -13.737  0.50 29.53           C
ANISOU 4478  CG AASN A 581     3919   3714   3586    341    427   1118       C
ATOM   4479  CG BASN A 581     -31.480 -60.224 -12.095  0.50 30.35           C
ANISOU 4479  CG BASN A 581     4006   3954   3570    381    480   1156       C
ATOM   4480  OD1AASN A 581     -29.916 -62.181 -13.077  0.50 31.54           O
ANISOU 4480  OD1AASN A 581     4208   3965   3812    404    447   1195       O
ATOM   4481  OD1BASN A 581     -32.665 -60.535 -12.215  0.50 31.91           O
ANISOU 4481  OD1BASN A 581     4188   4101   3835    329    536   1200       O
ATOM   4482  ND2AASN A 581     -30.916 -61.503 -14.970  0.50 29.05           N
ANISOU 4482  ND2AASN A 581     3845   3564   3631    265    416   1074       N
ATOM   4483  ND2BASN A 581     -30.950 -59.879 -10.931  0.50 31.03           N
ANISOU 4483  ND2BASN A 581     4110   4144   3537    464    476   1177       N
ATOM   4484  N   VAL A 582     -28.303 -59.196 -11.041  1.00 30.68           N
ANISOU 4484  N   VAL A 582     4073   4197   3386    549    334   1054       N
ATOM   4485  CA  VAL A 582     -27.406 -59.751 -10.024  1.00 32.59           C
ANISOU 4485  CA  VAL A 582     4343   4502   3538    648    327   1114       C
ATOM   4486  C   VAL A 582     -27.864 -61.179  -9.722  1.00 35.13           C
ANISOU 4486  C   VAL A 582     4699   4750   3900    668    401   1245       C
ATOM   4487  O   VAL A 582     -29.057 -61.464  -9.774  1.00 35.57           O
ANISOU 4487  O   VAL A 582     4753   4750   4013    619    467   1296       O
ATOM   4488  CB  VAL A 582     -27.395 -58.920  -8.714  1.00 32.95           C
ANISOU 4488  CB  VAL A 582     4391   4679   3449    716    319   1105       C
ATOM   4489  CG1 VAL A 582     -26.897 -57.516  -8.975  1.00 31.33           C
ANISOU 4489  CG1 VAL A 582     4153   4537   3213    695    245    972       C
ATOM   4490  CG2 VAL A 582     -28.776 -58.899  -8.054  1.00 33.27           C
ANISOU 4490  CG2 VAL A 582     4439   4728   3475    710    400   1171       C
ATOM   4491  N   GLN A 583     -26.921 -62.070  -9.436  1.00 37.76           N
ANISOU 4491  N   GLN A 583     5059   5079   4209    738    391   1300       N
ATOM   4492  CA  GLN A 583     -27.236 -63.491  -9.235  1.00 40.16           C
ANISOU 4492  CA  GLN A 583     5401   5294   4562    758    461   1427       C
ATOM   4493  C   GLN A 583     -27.501 -63.780  -7.766  1.00 41.86           C
ANISOU 4493  C   GLN A 583     5646   5586   4675    846    517   1536       C
ATOM   4494  O   GLN A 583     -26.572 -63.950  -6.973  1.00 43.27           O
ANISOU 4494  O   GLN A 583     5845   5844   4752    947    491   1566       O
ATOM   4495  CB  GLN A 583     -26.099 -64.387  -9.753  1.00 40.58           C
ANISOU 4495  CB  GLN A 583     5475   5293   4652    795    428   1436       C
ATOM   4496  CG  GLN A 583     -25.903 -64.352 -11.268  1.00 41.41           C
ANISOU 4496  CG  GLN A 583     5560   5307   4867    714    388   1346       C
ATOM   4497  CD  GLN A 583     -27.052 -64.997 -12.039  1.00 42.83           C
ANISOU 4497  CD  GLN A 583     5746   5352   5177    624    443   1373       C
ATOM   4498  OE1 GLN A 583     -27.439 -66.137 -11.765  1.00 46.01           O
ANISOU 4498  OE1 GLN A 583     6181   5672   5626    635    504   1476       O
ATOM   4499  NE2 GLN A 583     -27.594 -64.270 -13.016  1.00 43.66           N
ANISOU 4499  NE2 GLN A 583     5817   5432   5341    535    419   1281       N
CONECT   26   25  106
CONECT   32   31 1032
CONECT   59   58  186
CONECT  106   26  105
CONECT  186   59  185
CONECT  200  199  279
CONECT  279  200  278
CONECT 1032   32 1031
CONECT 4383 4382 4425
CONECT 4425 4383 4424
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.