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***  cd27l-for-practical  ***

elNémo ID: 191114144449142563

Job options:

ID        	=	 191114144449142563
JOBID     	=	 cd27l-for-practical
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 cd27l-for-practical

HEADER    LYASE                                   12-JAN-11   3QAY              
TITLE     CATALYTIC DOMAIN OF CD27L ENDOLYSIN TARGETING CLOSTRIDIA DIFFICILE    
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: ENDOLYSIN;                                                 
COMPND   3 CHAIN: A, B, C, D;                                                   
COMPND   4 FRAGMENT: CATALYTIC DOMAIN;                                          
COMPND   5 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: CLOSTRIDIUM PHAGE PHICD27;                      
SOURCE   3 ORGANISM_TAXID: 559189;                                              
SOURCE   4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   5 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   6 EXPRESSION_SYSTEM_STRAIN: BL21 DE3;                                  
SOURCE   7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   8 EXPRESSION_SYSTEM_PLASMID: PET15B                                    
KEYWDS    AMIDASE A/B FOLD, LYASE                                               
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    M.J.MAYER,V.GAREFALIKI,R.SPOERL,A.NARBAD,R.MEIJERS                    
REVDAT   1   28-DEC-11 3QAY    0                                                
JRNL        AUTH   M.J.MAYER,V.GAREFALAKI,R.SPOERL,A.NARBAD,R.MEIJERS           
JRNL        TITL   STRUCTURE-BASED MODIFICATION OF A CLOSTRIDIUM                
JRNL        TITL 2 DIFFICILE-TARGETING ENDOLYSIN AFFECTS ACTIVITY AND HOST      
JRNL        TITL 3 RANGE.                                                       
JRNL        REF    J.BACTERIOL.                  V. 193  5477 2011              
JRNL        REFN                   ISSN 0021-9193                               
JRNL        PMID   21803993                                                     
JRNL        DOI    10.1128/JB.00439-11                                          
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.00 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.5.0102                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.00                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 20.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 91.2                           
REMARK   3   NUMBER OF REFLECTIONS             : 41298                          
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) : 0.187                           
REMARK   3   R VALUE            (WORKING SET) : 0.184                           
REMARK   3   FREE R VALUE                     : 0.246                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2166                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.00                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.05                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 2875                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 85.75                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.1970                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 147                          
REMARK   3   BIN FREE R VALUE                    : 0.2920                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 5620                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 74                                      
REMARK   3   SOLVENT ATOMS            : 1142                                    
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 15.95                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.18000                                             
REMARK   3    B22 (A**2) : -0.99000                                             
REMARK   3    B33 (A**2) : 0.54000                                              
REMARK   3    B12 (A**2) : -0.81000                                             
REMARK   3    B13 (A**2) : -0.38000                                             
REMARK   3    B23 (A**2) : -0.11000                                             
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.270         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.210         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.143         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 10.646        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.929                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.864                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  5764 ; 0.007 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  3964 ; 0.001 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  7748 ; 0.983 ; 1.988       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  9756 ; 0.749 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   716 ; 5.620 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   240 ;36.821 ;25.167       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  1104 ;11.870 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    20 ;18.918 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   856 ; 0.055 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  6268 ; 0.003 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  1064 ; 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):  3556 ; 0.317 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  1480 ; 0.063 ; 1.500       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  5708 ; 0.602 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  2208 ; 0.988 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  2040 ; 1.620 ; 4.500       
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  : 4                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A     0        A   179                          
REMARK   3    ORIGIN FOR THE GROUP (A):   0.1420  -0.3780  -0.2990              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0067 T22:   0.0342                                     
REMARK   3      T33:   0.0128 T12:   0.0053                                     
REMARK   3      T13:   0.0063 T23:  -0.0070                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.7735 L22:   1.1458                                     
REMARK   3      L33:   1.4037 L12:  -0.2894                                     
REMARK   3      L13:  -0.0765 L23:  -0.1042                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0155 S12:  -0.0252 S13:   0.0143                       
REMARK   3      S21:  -0.0115 S22:  -0.0163 S23:   0.0155                       
REMARK   3      S31:   0.0205 S32:   0.0167 S33:   0.0318                       
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     0        B   179                          
REMARK   3    ORIGIN FOR THE GROUP (A): -20.5990 -20.3120  36.4080              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0032 T22:   0.0322                                     
REMARK   3      T33:   0.0110 T12:   0.0045                                     
REMARK   3      T13:   0.0028 T23:  -0.0061                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.7005 L22:   0.8739                                     
REMARK   3      L33:   1.2504 L12:   0.1742                                     
REMARK   3      L13:  -0.0524 L23:   0.1256                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0016 S12:  -0.0356 S13:   0.0207                       
REMARK   3      S21:   0.0080 S22:  -0.0455 S23:   0.0093                       
REMARK   3      S31:   0.0461 S32:  -0.0155 S33:   0.0438                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   C     0        C   179                          
REMARK   3    ORIGIN FOR THE GROUP (A):   1.2640 -53.4610  36.9450              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0042 T22:   0.0286                                     
REMARK   3      T33:   0.0206 T12:   0.0083                                     
REMARK   3      T13:  -0.0049 T23:  -0.0105                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.6933 L22:   1.4289                                     
REMARK   3      L33:   1.2823 L12:   0.2869                                     
REMARK   3      L13:   0.0072 L23:  -0.1322                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0077 S12:   0.0246 S13:  -0.0241                       
REMARK   3      S21:   0.0428 S22:   0.0007 S23:  -0.0245                       
REMARK   3      S31:  -0.0233 S32:  -0.0021 S33:  -0.0085                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   D     0        D   179                          
REMARK   3    ORIGIN FOR THE GROUP (A):  14.4570 -33.5010   0.4680              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0287 T22:   0.0254                                     
REMARK   3      T33:   0.0184 T12:   0.0108                                     
REMARK   3      T13:   0.0005 T23:  -0.0047                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.6932 L22:   1.6987                                     
REMARK   3      L33:   0.8347 L12:  -0.3785                                     
REMARK   3      L13:  -0.0109 L23:   0.1744                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0172 S12:   0.0180 S13:   0.0258                       
REMARK   3      S21:  -0.0457 S22:  -0.0234 S23:  -0.0426                       
REMARK   3      S31:   0.0074 S32:  -0.0058 S33:   0.0062                       
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 3QAY COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 18-JAN-11.                  
REMARK 100 THE RCSB ID CODE IS RCSB063415.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 06-JAN-10                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 8.2                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : EMBL/DESY, HAMBURG                 
REMARK 200  BEAMLINE                       : X12                                
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : NULL                               
REMARK 200  MONOCHROMATOR                  : DOUBLE CRYSTAL MONOCHROMATOR       
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARMOSAIC 225 MM CCD               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 50589                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.870                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 20.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 88.3                               
REMARK 200  DATA REDUNDANCY                : 1.800                              
REMARK 200  R MERGE                    (I) : 0.13700                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 8.9000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.87                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.90                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 69.8                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 1.50                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.31000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : 2.300                              
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: PDB ENTRY 1XOV                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 45.82                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.27                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M TRIS-HCL, 0.2 M LISO4, 20 % PEG    
REMARK 280  4000, PH 8.2, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 292K       
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1                              
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2, 3, 4                                              
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 3                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 4                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     ASN A  89    CG   OD1  ND2                                       
REMARK 470     ASN B  89    CG   OD1  ND2                                       
REMARK 470     ASN C  89    CG   OD1  ND2                                       
REMARK 470     ASN D  89    CG   OD1  ND2                                       
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   NZ   LYS D   137     O4   PO4 D   184              1.57            
REMARK 500   O3   PO4 A   181     O    HOH A  1468              2.03            
REMARK 500   O1   PO4 A   181     O    HOH A  1469              2.13            
REMARK 500   O    HOH A   184     O    HOH A  1420              2.16            
REMARK 500   O    SER A   136     O    HOH A  1420              2.17            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   NZ   LYS A    93     O    HOH A  1162     1455     2.19            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    HIS A   9     -175.15     72.33                                   
REMARK 500    SER A  88     -113.90   -144.50                                   
REMARK 500    HIS B   9     -175.88     77.03                                   
REMARK 500    SER B  88     -114.09   -146.90                                   
REMARK 500    HIS C   9     -173.89     76.08                                   
REMARK 500    GLN C  57      -50.67   -124.64                                   
REMARK 500    SER C  88     -113.72   -146.40                                   
REMARK 500    HIS D   9     -172.28     74.84                                   
REMARK 500    SER D  88     -122.97   -148.90                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH A 636        DISTANCE =  5.11 ANGSTROMS                       
REMARK 525    HOH A1006        DISTANCE =  6.20 ANGSTROMS                       
REMARK 525    HOH A1083        DISTANCE =  5.16 ANGSTROMS                       
REMARK 525    HOH A1249        DISTANCE =  6.56 ANGSTROMS                       
REMARK 525    HOH A1260        DISTANCE =  5.29 ANGSTROMS                       
REMARK 525    HOH A1314        DISTANCE =  6.89 ANGSTROMS                       
REMARK 525    HOH A1336        DISTANCE =  7.18 ANGSTROMS                       
REMARK 525    HOH A1418        DISTANCE =  5.27 ANGSTROMS                       
REMARK 525    HOH A1450        DISTANCE =  6.57 ANGSTROMS                       
REMARK 525    HOH B 681        DISTANCE =  6.19 ANGSTROMS                       
REMARK 525    HOH B1095        DISTANCE =  5.70 ANGSTROMS                       
REMARK 525    HOH B1118        DISTANCE =  8.47 ANGSTROMS                       
REMARK 525    HOH B1343        DISTANCE =  5.56 ANGSTROMS                       
REMARK 525    HOH C 385        DISTANCE =  5.89 ANGSTROMS                       
REMARK 525    HOH C 986        DISTANCE =  5.47 ANGSTROMS                       
REMARK 525    HOH C1012        DISTANCE =  5.79 ANGSTROMS                       
REMARK 525    HOH C1109        DISTANCE =  7.46 ANGSTROMS                       
REMARK 525    HOH C1389        DISTANCE =  7.59 ANGSTROMS                       
REMARK 525    HOH D 403        DISTANCE =  5.12 ANGSTROMS                       
REMARK 525    HOH D 428        DISTANCE =  7.35 ANGSTROMS                       
REMARK 525    HOH D 882        DISTANCE =  5.79 ANGSTROMS                       
REMARK 525    HOH D 907        DISTANCE =  5.31 ANGSTROMS                       
REMARK 525    HOH D1107        DISTANCE =  7.40 ANGSTROMS                       
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                              ZN C 180  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS C  84   ND1                                                    
REMARK 620 2 PO4 C 181   O1   98.0                                              
REMARK 620 3 HIS C   9   NE2 110.3 149.6                                        
REMARK 620 4 GLU C  26   OE2  98.4  95.2  91.6                                  
REMARK 620 5 HOH C1471   O    88.2  79.9  89.7 172.3                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A 180  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A  84   ND1                                                    
REMARK 620 2 HIS A   9   NE2 100.1                                              
REMARK 620 3 GLU A  26   OE2  96.5  94.9                                        
REMARK 620 4 PO4 A 181   O4   99.3 151.5 103.3                                  
REMARK 620 5 HOH A1468   O    88.6  81.4 174.2  78.5                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN D 180  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS D  84   ND1                                                    
REMARK 620 2 HIS D   9   NE2  99.0                                              
REMARK 620 3 GLU D  26   OE2  96.9  96.2                                        
REMARK 620 4 PO4 D 181   O4  109.8 147.6  94.7                                  
REMARK 620 5 PO4 D 181   O3  165.7  82.4  97.1  66.1                            
REMARK 620 6 HOH D1472   O    88.1  85.4 174.4  81.2  77.8                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN B 180  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU B  26   OE2                                                    
REMARK 620 2 HIS B  84   ND1  99.7                                              
REMARK 620 3 HIS B   9   NE2  96.0  97.5                                        
REMARK 620 4 PO4 B 181   O2  100.2 108.4 146.4                                  
REMARK 620 5 HOH B 909   O   168.2  91.7  85.3  73.2                            
REMARK 620 6 HOH B1470   O    97.1 162.3  75.1  73.8  71.8                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 180                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 A 181                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 A 182                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 A 183                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 180                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 B 181                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 B 182                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 B 183                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 B 184                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN C 180                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 C 181                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 C 182                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 C 183                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN D 180                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 D 181                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 D 182                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 D 183                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 D 184                 
DBREF  3QAY A    1   179  UNP    B6SBV8   B6SBV8_9CAUD     1    179             
DBREF  3QAY B    1   179  UNP    B6SBV8   B6SBV8_9CAUD     1    179             
DBREF  3QAY C    1   179  UNP    B6SBV8   B6SBV8_9CAUD     1    179             
DBREF  3QAY D    1   179  UNP    B6SBV8   B6SBV8_9CAUD     1    179             
SEQADV 3QAY HIS A    0  UNP  B6SBV8              EXPRESSION TAG                 
SEQADV 3QAY HIS B    0  UNP  B6SBV8              EXPRESSION TAG                 
SEQADV 3QAY HIS C    0  UNP  B6SBV8              EXPRESSION TAG                 
SEQADV 3QAY HIS D    0  UNP  B6SBV8              EXPRESSION TAG                 
SEQRES   1 A  180  HIS MET LYS ILE CYS ILE THR VAL GLY HIS SER ILE LEU          
SEQRES   2 A  180  LYS SER GLY ALA CYS THR SER ALA ASP GLY VAL VAL ASN          
SEQRES   3 A  180  GLU TYR GLN TYR ASN LYS SER LEU ALA PRO VAL LEU ALA          
SEQRES   4 A  180  ASP THR PHE ARG LYS GLU GLY HIS LYS VAL ASP VAL ILE          
SEQRES   5 A  180  ILE CYS PRO GLU LYS GLN PHE LYS THR LYS ASN GLU GLU          
SEQRES   6 A  180  LYS SER TYR LYS ILE PRO ARG VAL ASN SER GLY GLY TYR          
SEQRES   7 A  180  ASP LEU LEU ILE GLU LEU HIS LEU ASN ALA SER ASN GLY          
SEQRES   8 A  180  GLN GLY LYS GLY SER GLU VAL LEU TYR TYR SER ASN LYS          
SEQRES   9 A  180  GLY LEU GLU TYR ALA THR ARG ILE CYS ASP LYS LEU GLY          
SEQRES  10 A  180  THR VAL PHE LYS ASN ARG GLY ALA LYS LEU ASP LYS ARG          
SEQRES  11 A  180  LEU TYR ILE LEU ASN SER SER LYS PRO THR ALA VAL LEU          
SEQRES  12 A  180  ILE GLU SER PHE PHE CYS ASP ASN LYS GLU ASP TYR ASP          
SEQRES  13 A  180  LYS ALA LYS LYS LEU GLY HIS GLU GLY ILE ALA LYS LEU          
SEQRES  14 A  180  ILE VAL GLU GLY VAL LEU ASN LYS ASN ILE ASN                  
SEQRES   1 B  180  HIS MET LYS ILE CYS ILE THR VAL GLY HIS SER ILE LEU          
SEQRES   2 B  180  LYS SER GLY ALA CYS THR SER ALA ASP GLY VAL VAL ASN          
SEQRES   3 B  180  GLU TYR GLN TYR ASN LYS SER LEU ALA PRO VAL LEU ALA          
SEQRES   4 B  180  ASP THR PHE ARG LYS GLU GLY HIS LYS VAL ASP VAL ILE          
SEQRES   5 B  180  ILE CYS PRO GLU LYS GLN PHE LYS THR LYS ASN GLU GLU          
SEQRES   6 B  180  LYS SER TYR LYS ILE PRO ARG VAL ASN SER GLY GLY TYR          
SEQRES   7 B  180  ASP LEU LEU ILE GLU LEU HIS LEU ASN ALA SER ASN GLY          
SEQRES   8 B  180  GLN GLY LYS GLY SER GLU VAL LEU TYR TYR SER ASN LYS          
SEQRES   9 B  180  GLY LEU GLU TYR ALA THR ARG ILE CYS ASP LYS LEU GLY          
SEQRES  10 B  180  THR VAL PHE LYS ASN ARG GLY ALA LYS LEU ASP LYS ARG          
SEQRES  11 B  180  LEU TYR ILE LEU ASN SER SER LYS PRO THR ALA VAL LEU          
SEQRES  12 B  180  ILE GLU SER PHE PHE CYS ASP ASN LYS GLU ASP TYR ASP          
SEQRES  13 B  180  LYS ALA LYS LYS LEU GLY HIS GLU GLY ILE ALA LYS LEU          
SEQRES  14 B  180  ILE VAL GLU GLY VAL LEU ASN LYS ASN ILE ASN                  
SEQRES   1 C  180  HIS MET LYS ILE CYS ILE THR VAL GLY HIS SER ILE LEU          
SEQRES   2 C  180  LYS SER GLY ALA CYS THR SER ALA ASP GLY VAL VAL ASN          
SEQRES   3 C  180  GLU TYR GLN TYR ASN LYS SER LEU ALA PRO VAL LEU ALA          
SEQRES   4 C  180  ASP THR PHE ARG LYS GLU GLY HIS LYS VAL ASP VAL ILE          
SEQRES   5 C  180  ILE CYS PRO GLU LYS GLN PHE LYS THR LYS ASN GLU GLU          
SEQRES   6 C  180  LYS SER TYR LYS ILE PRO ARG VAL ASN SER GLY GLY TYR          
SEQRES   7 C  180  ASP LEU LEU ILE GLU LEU HIS LEU ASN ALA SER ASN GLY          
SEQRES   8 C  180  GLN GLY LYS GLY SER GLU VAL LEU TYR TYR SER ASN LYS          
SEQRES   9 C  180  GLY LEU GLU TYR ALA THR ARG ILE CYS ASP LYS LEU GLY          
SEQRES  10 C  180  THR VAL PHE LYS ASN ARG GLY ALA LYS LEU ASP LYS ARG          
SEQRES  11 C  180  LEU TYR ILE LEU ASN SER SER LYS PRO THR ALA VAL LEU          
SEQRES  12 C  180  ILE GLU SER PHE PHE CYS ASP ASN LYS GLU ASP TYR ASP          
SEQRES  13 C  180  LYS ALA LYS LYS LEU GLY HIS GLU GLY ILE ALA LYS LEU          
SEQRES  14 C  180  ILE VAL GLU GLY VAL LEU ASN LYS ASN ILE ASN                  
SEQRES   1 D  180  HIS MET LYS ILE CYS ILE THR VAL GLY HIS SER ILE LEU          
SEQRES   2 D  180  LYS SER GLY ALA CYS THR SER ALA ASP GLY VAL VAL ASN          
SEQRES   3 D  180  GLU TYR GLN TYR ASN LYS SER LEU ALA PRO VAL LEU ALA          
SEQRES   4 D  180  ASP THR PHE ARG LYS GLU GLY HIS LYS VAL ASP VAL ILE          
SEQRES   5 D  180  ILE CYS PRO GLU LYS GLN PHE LYS THR LYS ASN GLU GLU          
SEQRES   6 D  180  LYS SER TYR LYS ILE PRO ARG VAL ASN SER GLY GLY TYR          
SEQRES   7 D  180  ASP LEU LEU ILE GLU LEU HIS LEU ASN ALA SER ASN GLY          
SEQRES   8 D  180  GLN GLY LYS GLY SER GLU VAL LEU TYR TYR SER ASN LYS          
SEQRES   9 D  180  GLY LEU GLU TYR ALA THR ARG ILE CYS ASP LYS LEU GLY          
SEQRES  10 D  180  THR VAL PHE LYS ASN ARG GLY ALA LYS LEU ASP LYS ARG          
SEQRES  11 D  180  LEU TYR ILE LEU ASN SER SER LYS PRO THR ALA VAL LEU          
SEQRES  12 D  180  ILE GLU SER PHE PHE CYS ASP ASN LYS GLU ASP TYR ASP          
SEQRES  13 D  180  LYS ALA LYS LYS LEU GLY HIS GLU GLY ILE ALA LYS LEU          
SEQRES  14 D  180  ILE VAL GLU GLY VAL LEU ASN LYS ASN ILE ASN                  
HET     ZN  A 180       1                                                       
HET    PO4  A 181       5                                                       
HET    PO4  A 182       5                                                       
HET    PO4  A 183       5                                                       
HET     ZN  B 180       1                                                       
HET    PO4  B 181       5                                                       
HET    PO4  B 182       5                                                       
HET    PO4  B 183       5                                                       
HET    PO4  B 184       5                                                       
HET     ZN  C 180       1                                                       
HET    PO4  C 181       5                                                       
HET    PO4  C 182       5                                                       
HET    PO4  C 183       5                                                       
HET     ZN  D 180       1                                                       
HET    PO4  D 181       5                                                       
HET    PO4  D 182       5                                                       
HET    PO4  D 183       5                                                       
HET    PO4  D 184       5                                                       
HETNAM      ZN ZINC ION                                                         
HETNAM     PO4 PHOSPHATE ION                                                    
FORMUL   5   ZN    4(ZN 2+)                                                     
FORMUL   6  PO4    14(O4 P 3-)                                                  
FORMUL  23  HOH   *1142(H2 O)                                                   
HELIX    1   1 ASN A   25  GLU A   44  1                                  20    
HELIX    2   2 ASN A   62  GLY A   75  1                                  14    
HELIX    3   3 SER A  101  GLY A  116  1                                  16    
HELIX    4   4 LEU A  130  SER A  135  1                                   6    
HELIX    5   5 ASN A  150  ASN A  175  1                                  26    
HELIX    6   6 ASN B   25  GLU B   44  1                                  20    
HELIX    7   7 LYS B   61  GLY B   75  1                                  15    
HELIX    8   8 SER B  101  GLY B  116  1                                  16    
HELIX    9   9 LEU B  130  SER B  135  1                                   6    
HELIX   10  10 ASN B  150  ASN B  175  1                                  26    
HELIX   11  11 ASN C   25  GLU C   44  1                                  20    
HELIX   12  12 LYS C   61  ASN C   73  1                                  13    
HELIX   13  13 SER C  101  GLY C  116  1                                  16    
HELIX   14  14 LEU C  130  SER C  135  1                                   6    
HELIX   15  15 ASN C  150  ASN C  175  1                                  26    
HELIX   16  16 ASN D   25  GLU D   44  1                                  20    
HELIX   17  17 LYS D   61  GLY D   75  1                                  15    
HELIX   18  18 SER D  101  GLY D  116  1                                  16    
HELIX   19  19 LEU D  130  SER D  135  1                                   6    
HELIX   20  20 ASN D  150  ASN D  175  1                                  26    
SHEET    1   A 6 LYS A  47  ILE A  51  0                                        
SHEET    2   A 6 LYS A   2  VAL A   7  1  N  ILE A   5   O  ILE A  51           
SHEET    3   A 6 LEU A  79  ASN A  86  1  O  LEU A  79   N  CYS A   4           
SHEET    4   A 6 THR A 139  PHE A 147  1  O  ILE A 143   N  HIS A  84           
SHEET    5   A 6 SER A  95  TYR A  99 -1  N  LEU A  98   O  LEU A 142           
SHEET    6   A 6 ASN A 121  LEU A 126  1  O  LYS A 125   N  VAL A  97           
SHEET    1   B 6 LYS B  47  ILE B  51  0                                        
SHEET    2   B 6 LYS B   2  VAL B   7  1  N  ILE B   5   O  ILE B  51           
SHEET    3   B 6 LEU B  79  ASN B  86  1  O  LEU B  79   N  CYS B   4           
SHEET    4   B 6 THR B 139  PHE B 147  1  O  ILE B 143   N  HIS B  84           
SHEET    5   B 6 SER B  95  TYR B  99 -1  N  GLU B  96   O  GLU B 144           
SHEET    6   B 6 ASN B 121  LEU B 126  1  O  ARG B 122   N  SER B  95           
SHEET    1   C 6 LYS C  47  ILE C  51  0                                        
SHEET    2   C 6 LYS C   2  VAL C   7  1  N  ILE C   5   O  ILE C  51           
SHEET    3   C 6 LEU C  79  ASN C  86  1  O  LEU C  79   N  CYS C   4           
SHEET    4   C 6 ALA C 140  PHE C 147  1  O  ILE C 143   N  HIS C  84           
SHEET    5   C 6 SER C  95  TYR C  99 -1  N  GLU C  96   O  GLU C 144           
SHEET    6   C 6 ASN C 121  LEU C 126  1  O  ARG C 122   N  SER C  95           
SHEET    1   D 6 LYS D  47  ILE D  51  0                                        
SHEET    2   D 6 LYS D   2  VAL D   7  1  N  ILE D   3   O  LYS D  47           
SHEET    3   D 6 LEU D  79  ASN D  86  1  O  LEU D  79   N  CYS D   4           
SHEET    4   D 6 THR D 139  PHE D 147  1  O  PHE D 146   N  ASN D  86           
SHEET    5   D 6 SER D  95  TYR D  99 -1  N  GLU D  96   O  GLU D 144           
SHEET    6   D 6 ASN D 121  LEU D 126  1  O  LYS D 125   N  VAL D  97           
LINK         ND1 HIS C  84                ZN    ZN C 180     1555   1555  1.93  
LINK         ND1 HIS A  84                ZN    ZN A 180     1555   1555  2.00  
LINK         ND1 HIS D  84                ZN    ZN D 180     1555   1555  2.00  
LINK         NE2 HIS A   9                ZN    ZN A 180     1555   1555  2.00  
LINK         NE2 HIS D   9                ZN    ZN D 180     1555   1555  2.01  
LINK        ZN    ZN C 180                 O1  PO4 C 181     1555   1555  2.01  
LINK         OE2 GLU B  26                ZN    ZN B 180     1555   1555  2.02  
LINK         ND1 HIS B  84                ZN    ZN B 180     1555   1555  2.05  
LINK         NE2 HIS B   9                ZN    ZN B 180     1555   1555  2.07  
LINK         OE2 GLU A  26                ZN    ZN A 180     1555   1555  2.08  
LINK         NE2 HIS C   9                ZN    ZN C 180     1555   1555  2.10  
LINK         OE2 GLU D  26                ZN    ZN D 180     1555   1555  2.11  
LINK         OE2 GLU C  26                ZN    ZN C 180     1555   1555  2.18  
LINK        ZN    ZN D 180                 O4  PO4 D 181     1555   1555  2.19  
LINK        ZN    ZN A 180                 O4  PO4 A 181     1555   1555  2.20  
LINK        ZN    ZN B 180                 O2  PO4 B 181     1555   1555  2.35  
LINK        ZN    ZN D 180                 O3  PO4 D 181     1555   1555  2.36  
LINK        ZN    ZN D 180                 O   HOH D1472     1555   1555  2.24  
LINK        ZN    ZN C 180                 O   HOH C1471     1555   1555  2.30  
LINK        ZN    ZN B 180                 O   HOH B 909     1555   1555  2.39  
LINK        ZN    ZN A 180                 O   HOH A1468     1555   1555  2.43  
LINK        ZN    ZN B 180                 O   HOH B1470     1555   1555  2.68  
SITE     1 AC1  6 HIS A   9  GLU A  26  HIS A  84  PO4 A 181                    
SITE     2 AC1  6 HOH A1468  HOH A1469                                          
SITE     1 AC2  8 GLU A  26  HIS A  84  LEU A  85  ASN A  86                    
SITE     2 AC2  8 GLU A 144   ZN A 180  HOH A1468  HOH A1469                    
SITE     1 AC3  9 ARG A  42  ASP A  49  VAL A  50  LYS A  93                    
SITE     2 AC3  9 LYS A 120  HOH A 531  HOH A 619  HOH A 993                    
SITE     3 AC3  9 HOH A1162                                                     
SITE     1 AC4  8 ARG A  42  LYS A  47  VAL A  48  LYS A 120                    
SITE     2 AC4  8 HOH A 213  HOH A 220  HOH A 619  HOH A 912                    
SITE     1 AC5  6 HIS B   9  GLU B  26  HIS B  84  PO4 B 181                    
SITE     2 AC5  6 HOH B 909  HOH B1470                                          
SITE     1 AC6 11 GLU B  26  HIS B  84  LEU B  85  ASN B  86                    
SITE     2 AC6 11 ALA B  87  GLU B 144   ZN B 180  HOH B 286                    
SITE     3 AC6 11 HOH B 909  HOH B 990  HOH B1470                               
SITE     1 AC7  8 SER B 101  LYS B 103  THR B 139  HOH B 223                    
SITE     2 AC7  8 HOH B 773  HOH B1308  HOH B1372  LYS C 137                    
SITE     1 AC8  7 ARG B  42  LYS B  47  VAL B  48  LYS B 120                    
SITE     2 AC8  7 HOH B 216  HOH B1035  HOH B1148                               
SITE     1 AC9  8 ARG B  42  ASP B  49  VAL B  50  LYS B  93                    
SITE     2 AC9  8 LYS B 120  HOH B 998  HOH B1139  HOH B1161                    
SITE     1 BC1  5 HIS C   9  GLU C  26  HIS C  84  PO4 C 181                    
SITE     2 BC1  5 HOH C1471                                                     
SITE     1 BC2  8 HIS C   9  GLU C  26  HIS C  84  LEU C  85                    
SITE     2 BC2  8 ASN C  86  GLU C 144   ZN C 180  HOH C1471                    
SITE     1 BC3  9 ARG C  42  ASP C  49  VAL C  50  LYS C  93                    
SITE     2 BC3  9 LYS C 120  HOH C 227  HOH C 705  HOH C1121                    
SITE     3 BC3  9 HOH C1228                                                     
SITE     1 BC4  6 ARG C  42  LYS C  47  VAL C  48  LYS C 120                    
SITE     2 BC4  6 HOH C1122  HOH C1374                                          
SITE     1 BC5  5 HIS D   9  GLU D  26  HIS D  84  PO4 D 181                    
SITE     2 BC5  5 HOH D1472                                                     
SITE     1 BC6  9 HIS D   9  GLU D  26  HIS D  84  LEU D  85                    
SITE     2 BC6  9 GLU D 144   ZN D 180  HOH D 248  HOH D1198                    
SITE     3 BC6  9 HOH D1472                                                     
SITE     1 BC7  8 LYS A 137  SER D 101  LYS D 103  THR D 139                    
SITE     2 BC7  8 HOH D 187  HOH D 501  HOH D1074  HOH D1319                    
SITE     1 BC8  6 ARG D  42  LYS D  47  VAL D  48  LYS D 120                    
SITE     2 BC8  6 HOH D 211  HOH D1128                                          
SITE     1 BC9  7 SER A 101  LYS A 103  THR A 139  LYS D 137                    
SITE     2 BC9  7 HOH D 576  HOH D 702  HOH D1406                               
CRYST1   36.507   69.737   78.818 101.72 102.00 105.24 P 1           4          
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      0.027392  0.007463  0.008172        0.00000                         
SCALE2      0.000000  0.014862  0.004220        0.00000                         
SCALE3      0.000000  0.000000  0.013484        0.00000                         
ATOM      1  N   HIS A   0      12.938  -0.772  15.458  1.00 24.90           N  
ANISOU    1  N   HIS A   0     2882   3947   2632    276   -562   -110       N  
ATOM      2  CA  HIS A   0      12.292  -1.962  16.081  1.00 24.88           C  
ANISOU    2  CA  HIS A   0     2962   3932   2560    360   -520    -65       C  
ATOM      3  C   HIS A   0      11.899  -3.009  15.032  1.00 23.36           C  
ANISOU    3  C   HIS A   0     2767   3693   2414    392   -432    -11       C  
ATOM      4  O   HIS A   0      12.315  -4.160  15.128  1.00 23.75           O  
ANISOU    4  O   HIS A   0     2818   3762   2444    466   -426     40       O  
ATOM      5  CB  HIS A   0      11.078  -1.535  16.908  1.00 25.10           C  
ANISOU    5  CB  HIS A   0     3096   3917   2524    353   -494    -94       C  
ATOM      6  CG  HIS A   0      10.964  -2.251  18.214  1.00 27.39           C  
ANISOU    6  CG  HIS A   0     3462   4237   2708    428   -511    -70       C  
ATOM      7  ND1 HIS A   0      11.998  -2.293  19.128  1.00 30.96           N  
ANISOU    7  ND1 HIS A   0     3898   4766   3100    464   -608    -76       N  
ATOM      8  CD2 HIS A   0       9.941  -2.944  18.768  1.00 29.27           C  
ANISOU    8  CD2 HIS A   0     3794   4440   2888    473   -444    -37       C  
ATOM      9  CE1 HIS A   0      11.619  -2.990  20.184  1.00 31.67           C  
ANISOU    9  CE1 HIS A   0     4077   4865   3090    535   -599    -46       C  
ATOM     10  NE2 HIS A   0      10.374  -3.393  19.993  1.00 31.26           N  
ANISOU   10  NE2 HIS A   0     4094   4744   3040    539   -496    -20       N  
ATOM     11  N   MET A   1      11.102  -2.607  14.042  1.00 21.56           N  
ANISOU   11  N   MET A   1     2544   3403   2245    340   -369    -23       N  
ATOM     12  CA  MET A   1      10.759  -3.472  12.904  1.00 20.16           C  
ANISOU   12  CA  MET A   1     2363   3182   2117    357   -295     16       C  
ATOM     13  C   MET A   1      11.528  -3.062  11.649  1.00 19.08           C  
ANISOU   13  C   MET A   1     2135   3056   2057    321   -295     11       C  
ATOM     14  O   MET A   1      11.855  -1.887  11.470  1.00 18.67           O  
ANISOU   14  O   MET A   1     2039   3017   2036    256   -329    -26       O  
ATOM     15  CB  MET A   1       9.258  -3.405  12.591  1.00 19.53           C  
ANISOU   15  CB  MET A   1     2349   3028   2044    329   -224      9       C  
ATOM     16  CG  MET A   1       8.386  -4.371  13.373  1.00 20.21           C  
ANISOU   16  CG  MET A   1     2519   3086   2072    375   -182     41       C  
ATOM     17  SD  MET A   1       6.756  -4.567  12.605  1.00 20.90           S  
ANISOU   17  SD  MET A   1     2648   3094   2197    338    -92     44       S  
ATOM     18  CE  MET A   1       6.024  -2.990  13.038  1.00 18.47           C  
ANISOU   18  CE  MET A   1     2350   2787   1882    286   -104    -15       C  
ATOM     19  N   LYS A   2      11.800  -4.040  10.784  1.00 17.90           N  
ANISOU   19  N   LYS A   2     1968   2897   1936    363   -252     51       N  
ATOM     20  CA  LYS A   2      12.267  -3.772   9.422  1.00 17.07           C  
ANISOU   20  CA  LYS A   2     1796   2790   1899    334   -225     53       C  
ATOM     21  C   LYS A   2      11.095  -3.981   8.457  1.00 15.58           C  
ANISOU   21  C   LYS A   2     1663   2523   1732    315   -153     53       C  
ATOM     22  O   LYS A   2      10.543  -5.083   8.366  1.00 15.44           O  
ANISOU   22  O   LYS A   2     1702   2466   1697    359   -112     79       O  
ATOM     23  CB  LYS A   2      13.437  -4.680   9.041  1.00 17.72           C  
ANISOU   23  CB  LYS A   2     1818   2920   1994    403   -225     92       C  
ATOM     24  CG  LYS A   2      14.149  -4.231   7.758  1.00 18.21           C  
ANISOU   24  CG  LYS A   2     1795   3002   2120    373   -201     93       C  
ATOM     25  CD  LYS A   2      15.287  -5.156   7.357  1.00 19.24           C  
ANISOU   25  CD  LYS A   2     1863   3184   2262    453   -191    133       C  
ATOM     26  CE  LYS A   2      15.960  -4.642   6.095  1.00 19.20           C  
ANISOU   26  CE  LYS A   2     1775   3203   2318    420   -156    136       C  
ATOM     27  NZ  LYS A   2      17.094  -5.502   5.649  1.00 20.98           N  
ANISOU   27  NZ  LYS A   2     1930   3486   2556    505   -136    174       N  
ATOM     28  N   ILE A   3      10.724  -2.923   7.742  1.00 14.13           N  
ANISOU   28  N   ILE A   3     1465   2317   1588    247   -142     25       N  
ATOM     29  CA  ILE A   3       9.496  -2.912   6.962  1.00 12.66           C  
ANISOU   29  CA  ILE A   3     1330   2064   1417    223    -89     18       C  
ATOM     30  C   ILE A   3       9.804  -2.725   5.486  1.00 12.26           C  
ANISOU   30  C   ILE A   3     1242   2003   1413    205    -57     25       C  
ATOM     31  O   ILE A   3      10.666  -1.927   5.113  1.00 12.40           O  
ANISOU   31  O   ILE A   3     1197   2054   1460    174    -74     20       O  
ATOM     32  CB  ILE A   3       8.537  -1.784   7.428  1.00 12.28           C  
ANISOU   32  CB  ILE A   3     1314   1989   1363    171   -100    -19       C  
ATOM     33  CG1 ILE A   3       8.246  -1.897   8.922  1.00 12.43           C  
ANISOU   33  CG1 ILE A   3     1375   2022   1326    192   -127    -27       C  
ATOM     34  CG2 ILE A   3       7.225  -1.834   6.660  1.00 10.89           C  
ANISOU   34  CG2 ILE A   3     1180   1755   1203    155    -51    -23       C  
ATOM     35  CD1 ILE A   3       7.325  -0.804   9.456  1.00 12.21           C  
ANISOU   35  CD1 ILE A   3     1385   1971   1285    154   -133    -67       C  
ATOM     36  N   CYS A   4       9.103  -3.474   4.645  1.00 11.54           N  
ANISOU   36  N   CYS A   4     1193   1866   1325    223    -10     35       N  
ATOM     37  CA  CYS A   4       9.239  -3.325   3.202  1.00 10.98           C  
ANISOU   37  CA  CYS A   4     1106   1782   1285    211     24     39       C  
ATOM     38  C   CYS A   4       7.965  -2.708   2.675  1.00 10.21           C  
ANISOU   38  C   CYS A   4     1049   1634   1195    167     38     18       C  
ATOM     39  O   CYS A   4       6.878  -3.176   3.006  1.00  9.88           O  
ANISOU   39  O   CYS A   4     1058   1559   1139    170     47     12       O  
ATOM     40  CB  CYS A   4       9.455  -4.675   2.533  1.00 11.04           C  
ANISOU   40  CB  CYS A   4     1137   1774   1283    271     61     62       C  
ATOM     41  SG  CYS A   4       9.673  -4.582   0.727  1.00 11.76           S  
ANISOU   41  SG  CYS A   4     1221   1853   1395    269    106     66       S  
ATOM     42  N   ILE A   5       8.100  -1.648   1.878  1.00  9.62           N  
ANISOU   42  N   ILE A   5      950   1559   1147    127     41     11       N  
ATOM     43  CA  ILE A   5       6.962  -1.048   1.194  1.00  9.02           C  
ANISOU   43  CA  ILE A   5      909   1438   1078     98     53     -4       C  
ATOM     44  C   ILE A   5       7.161  -1.242  -0.301  1.00  8.98           C  
ANISOU   44  C   ILE A   5      907   1424   1080    107     86     10       C  
ATOM     45  O   ILE A   5       8.133  -0.738  -0.869  1.00  9.31           O  
ANISOU   45  O   ILE A   5      910   1491   1137     97     97     25       O  
ATOM     46  CB  ILE A   5       6.824   0.467   1.477  1.00  8.68           C  
ANISOU   46  CB  ILE A   5      857   1388   1051     49     30    -23       C  
ATOM     47  CG1 ILE A   5       6.639   0.734   2.967  1.00  8.92           C  
ANISOU   47  CG1 ILE A   5      895   1428   1066     43     -4    -44       C  
ATOM     48  CG2 ILE A   5       5.630   1.053   0.715  1.00  8.50           C  
ANISOU   48  CG2 ILE A   5      871   1322   1035     34     42    -33       C  
ATOM     49  CD1 ILE A   5       6.703   2.219   3.324  1.00  7.38           C  
ANISOU   49  CD1 ILE A   5      698   1222    886     -3    -31    -69       C  
ATOM     50  N   THR A   6       6.267  -2.001  -0.929  1.00  8.49           N  
ANISOU   50  N   THR A   6      892   1330   1004    124    103      5       N  
ATOM     51  CA  THR A   6       6.254  -2.099  -2.377  1.00  8.44           C  
ANISOU   51  CA  THR A   6      904   1310    992    132    129     11       C  
ATOM     52  C   THR A   6       5.171  -1.185  -2.936  1.00  7.93           C  
ANISOU   52  C   THR A   6      864   1219    932    101    118     -2       C  
ATOM     53  O   THR A   6       4.117  -1.022  -2.328  1.00  7.29           O  
ANISOU   53  O   THR A   6      796   1120    854     86     99    -19       O  
ATOM     54  CB  THR A   6       6.014  -3.533  -2.865  1.00  8.35           C  
ANISOU   54  CB  THR A   6      938   1277    959    171    148      9       C  
ATOM     55  OG1 THR A   6       4.769  -4.018  -2.365  1.00  9.67           O  
ANISOU   55  OG1 THR A   6     1140   1410   1124    158    132     -9       O  
ATOM     56  CG2 THR A   6       7.132  -4.453  -2.408  1.00  8.53           C  
ANISOU   56  CG2 THR A   6      943   1323    975    219    162     27       C  
ATOM     57  N   VAL A   7       5.456  -0.565  -4.080  1.00  7.88           N  
ANISOU   57  N   VAL A   7      861   1212    922     96    135     10       N  
ATOM     58  CA  VAL A   7       4.452   0.176  -4.825  1.00  7.59           C  
ANISOU   58  CA  VAL A   7      855   1149    880     82    124      3       C  
ATOM     59  C   VAL A   7       3.864  -0.762  -5.870  1.00  7.82           C  
ANISOU   59  C   VAL A   7      929   1164    879    108    130     -5       C  
ATOM     60  O   VAL A   7       4.594  -1.358  -6.664  1.00  7.36           O  
ANISOU   60  O   VAL A   7      885   1115    799    135    158      5       O  
ATOM     61  CB  VAL A   7       5.052   1.421  -5.502  1.00  8.25           C  
ANISOU   61  CB  VAL A   7      931   1233    971     62    139     26       C  
ATOM     62  CG1 VAL A   7       4.084   2.018  -6.514  1.00  7.09           C  
ANISOU   62  CG1 VAL A   7      828   1059    806     66    131     27       C  
ATOM     63  CG2 VAL A   7       5.453   2.453  -4.437  1.00  8.22           C  
ANISOU   63  CG2 VAL A   7      893   1231   1001     25    123     25       C  
ATOM     64  N   GLY A   8       2.542  -0.902  -5.848  1.00  7.47           N  
ANISOU   64  N   GLY A   8      905   1100    833    100    102    -27       N  
ATOM     65  CA  GLY A   8       1.845  -1.740  -6.798  1.00  7.66           C  
ANISOU   65  CA  GLY A   8      972   1110    830    113     92    -43       C  
ATOM     66  C   GLY A   8       1.938  -1.210  -8.215  1.00  7.94           C  
ANISOU   66  C   GLY A   8     1039   1146    832    128     97    -33       C  
ATOM     67  O   GLY A   8       2.023   0.002  -8.435  1.00  8.13           O  
ANISOU   67  O   GLY A   8     1055   1174    862    121     98    -14       O  
ATOM     68  N   HIS A   9       1.952  -2.140  -9.168  1.00  8.61           N  
ANISOU   68  N   HIS A   9     1169   1223    879    150    101    -46       N  
ATOM     69  CA  HIS A   9       1.929  -1.846 -10.601  1.00  8.98           C  
ANISOU   69  CA  HIS A   9     1263   1272    877    172    103    -41       C  
ATOM     70  C   HIS A   9       3.249  -1.275 -11.105  1.00  9.49           C  
ANISOU   70  C   HIS A   9     1323   1355    926    191    157     -3       C  
ATOM     71  O   HIS A   9       4.230  -1.227 -10.364  1.00  9.65           O  
ANISOU   71  O   HIS A   9     1298   1390    978    187    188     15       O  
ATOM     72  CB  HIS A   9       0.732  -0.955 -10.928  1.00  9.17           C  
ANISOU   72  CB  HIS A   9     1290   1293    900    160     57    -45       C  
ATOM     73  CG  HIS A   9      -0.547  -1.476 -10.357  1.00  9.31           C  
ANISOU   73  CG  HIS A   9     1291   1304    943    136     10    -78       C  
ATOM     74  ND1 HIS A   9      -1.176  -2.595 -10.857  1.00 10.66           N  
ANISOU   74  ND1 HIS A   9     1495   1463   1092    132    -19   -113       N  
ATOM     75  CD2 HIS A   9      -1.283  -1.071  -9.296  1.00  9.59           C  
ANISOU   75  CD2 HIS A   9     1278   1341   1024    113     -9    -82       C  
ATOM     76  CE1 HIS A   9      -2.265  -2.835 -10.151  1.00  9.99           C  
ANISOU   76  CE1 HIS A   9     1375   1377   1045    100    -53   -132       C  
ATOM     77  NE2 HIS A   9      -2.354  -1.925  -9.197  1.00  8.85           N  
ANISOU   77  NE2 HIS A   9     1180   1244    939     93    -44   -113       N  
ATOM     78  N   SER A  10       3.275  -0.888 -12.379  1.00 10.05           N  
ANISOU   78  N   SER A  10     1442   1430    949    213    168     11       N  
ATOM     79  CA  SER A  10       4.480  -0.368 -13.021  1.00 10.56           C  
ANISOU   79  CA  SER A  10     1505   1513    992    230    230     53       C  
ATOM     80  C   SER A  10       4.154   0.345 -14.328  1.00 11.03           C  
ANISOU   80  C   SER A  10     1624   1572    996    249    232     73       C  
ATOM     81  O   SER A  10       3.033   0.279 -14.830  1.00 10.58           O  
ANISOU   81  O   SER A  10     1611   1502    907    257    179     49       O  
ATOM     82  CB  SER A  10       5.450  -1.514 -13.319  1.00 11.07           C  
ANISOU   82  CB  SER A  10     1581   1593   1032    271    278     48       C  
ATOM     83  OG  SER A  10       4.894  -2.427 -14.252  1.00 11.26           O  
ANISOU   83  OG  SER A  10     1683   1601    993    306    262     14       O  
ATOM     84  N   ILE A  11       5.157   1.018 -14.877  1.00 11.74           N  
ANISOU   84  N   ILE A  11     1713   1677   1073    254    293    121       N  
ATOM     85  CA  ILE A  11       5.083   1.554 -16.221  1.00 12.30           C  
ANISOU   85  CA  ILE A  11     1851   1748   1074    282    313    150       C  
ATOM     86  C   ILE A  11       5.894   0.645 -17.130  1.00 13.44           C  
ANISOU   86  C   ILE A  11     2034   1916   1155    332    372    151       C  
ATOM     87  O   ILE A  11       7.117   0.546 -16.985  1.00 13.74           O  
ANISOU   87  O   ILE A  11     2028   1980   1213    336    442    179       O  
ATOM     88  CB  ILE A  11       5.622   2.987 -16.289  1.00 12.45           C  
ANISOU   88  CB  ILE A  11     1852   1762   1118    252    353    210       C  
ATOM     89  CG1 ILE A  11       4.719   3.923 -15.493  1.00 11.77           C  
ANISOU   89  CG1 ILE A  11     1747   1643   1083    216    294    205       C  
ATOM     90  CG2 ILE A  11       5.712   3.454 -17.741  1.00 12.79           C  
ANISOU   90  CG2 ILE A  11     1973   1807   1079    288    390    251       C  
ATOM     91  CD1 ILE A  11       5.158   5.361 -15.511  1.00 12.88           C  
ANISOU   91  CD1 ILE A  11     1884   1759   1250    182    326    259       C  
ATOM     92  N   LEU A  12       5.210  -0.015 -18.066  1.00 14.14           N  
ANISOU   92  N   LEU A  12     2205   1998   1167    373    342    118       N  
ATOM     93  CA  LEU A  12       5.861  -0.928 -19.007  1.00 15.32           C  
ANISOU   93  CA  LEU A  12     2414   2164   1242    431    394    108       C  
ATOM     94  C   LEU A  12       6.782  -0.189 -19.977  1.00 16.09           C  
ANISOU   94  C   LEU A  12     2535   2289   1290    457    480    172       C  
ATOM     95  O   LEU A  12       6.804   1.040 -20.023  1.00 16.35           O  
ANISOU   95  O   LEU A  12     2551   2319   1342    426    492    223       O  
ATOM     96  CB  LEU A  12       4.823  -1.742 -19.810  1.00 15.76           C  
ANISOU   96  CB  LEU A  12     2565   2202   1222    462    329     50       C  
ATOM     97  CG  LEU A  12       4.157  -3.008 -19.234  1.00 16.00           C  
ANISOU   97  CG  LEU A  12     2602   2204   1274    451    268    -20       C  
ATOM     98  CD1 LEU A  12       4.688  -3.402 -17.848  1.00 14.85           C  
ANISOU   98  CD1 LEU A  12     2369   2054   1220    424    288    -20       C  
ATOM     99  CD2 LEU A  12       2.637  -2.897 -19.240  1.00 16.43           C  
ANISOU   99  CD2 LEU A  12     2673   2242   1329    419    164    -58       C  
ATOM    100  N   LYS A  13       7.536  -0.964 -20.754  1.00 16.84           N  
ANISOU  100  N   LYS A  13     2674   2406   1320    517    546    169       N  
ATOM    101  CA  LYS A  13       8.427  -0.438 -21.786  1.00 17.71           C  
ANISOU  101  CA  LYS A  13     2813   2547   1369    551    642    229       C  
ATOM    102  C   LYS A  13       7.666   0.334 -22.865  1.00 17.48           C  
ANISOU  102  C   LYS A  13     2879   2508   1257    565    616    251       C  
ATOM    103  O   LYS A  13       8.182   1.303 -23.423  1.00 17.87           O  
ANISOU  103  O   LYS A  13     2936   2570   1284    562    682    321       O  
ATOM    104  CB  LYS A  13       9.207  -1.587 -22.425  1.00 19.04           C  
ANISOU  104  CB  LYS A  13     3024   2739   1471    628    712    209       C  
ATOM    105  CG  LYS A  13      10.318  -1.139 -23.360  1.00 21.66           C  
ANISOU  105  CG  LYS A  13     3366   3116   1749    667    834    277       C  
ATOM    106  CD  LYS A  13      11.053  -2.327 -23.952  1.00 24.41           C  
ANISOU  106  CD  LYS A  13     3757   3488   2029    756    905    251       C  
ATOM    107  CE  LYS A  13      12.373  -1.892 -24.572  1.00 27.15           C  
ANISOU  107  CE  LYS A  13     4070   3894   2354    789   1045    327       C  
ATOM    108  NZ  LYS A  13      13.273  -1.256 -23.557  1.00 28.77           N  
ANISOU  108  NZ  LYS A  13     4118   4130   2683    724   1085    381       N  
ATOM    109  N   SER A  14       6.441  -0.101 -23.143  1.00 16.46           N  
ANISOU  109  N   SER A  14     2819   2355   1082    578    519    193       N  
ATOM    110  CA  SER A  14       5.549   0.586 -24.071  1.00 16.55           C  
ANISOU  110  CA  SER A  14     2915   2359   1015    595    469    206       C  
ATOM    111  C   SER A  14       5.134   1.970 -23.581  1.00 16.00           C  
ANISOU  111  C   SER A  14     2800   2271   1008    545    442    256       C  
ATOM    112  O   SER A  14       4.673   2.792 -24.370  1.00 16.13           O  
ANISOU  112  O   SER A  14     2882   2283    964    565    427    293       O  
ATOM    113  CB  SER A  14       4.279  -0.233 -24.260  1.00 16.49           C  
ANISOU  113  CB  SER A  14     2963   2334    966    607    354    125       C  
ATOM    114  OG  SER A  14       3.489  -0.185 -23.085  1.00 14.72           O  
ANISOU  114  OG  SER A  14     2659   2090    844    548    276     95       O  
ATOM    115  N   GLY A  15       5.270   2.202 -22.277  1.00 15.16           N  
ANISOU  115  N   GLY A  15     2590   2152   1019    485    433    255       N  
ATOM    116  CA  GLY A  15       4.761   3.404 -21.636  1.00 14.72           C  
ANISOU  116  CA  GLY A  15     2495   2069   1031    438    396    285       C  
ATOM    117  C   GLY A  15       3.403   3.175 -20.992  1.00 14.10           C  
ANISOU  117  C   GLY A  15     2398   1973    987    424    284    227       C  
ATOM    118  O   GLY A  15       2.873   4.067 -20.325  1.00 13.14           O  
ANISOU  118  O   GLY A  15     2239   1828    925    392    248    241       O  
ATOM    119  N   ALA A  16       2.836   1.984 -21.186  1.00 14.22           N  
ANISOU  119  N   ALA A  16     2439   1997    965    445    232    161       N  
ATOM    120  CA  ALA A  16       1.549   1.652 -20.586  1.00 14.13           C  
ANISOU  120  CA  ALA A  16     2402   1976    992    424    130    106       C  
ATOM    121  C   ALA A  16       1.725   1.506 -19.085  1.00 13.42           C  
ANISOU  121  C   ALA A  16     2213   1874   1011    372    135     92       C  
ATOM    122  O   ALA A  16       2.663   0.850 -18.623  1.00 13.31           O  
ANISOU  122  O   ALA A  16     2168   1865   1024    364    189     87       O  
ATOM    123  CB  ALA A  16       0.988   0.369 -21.178  1.00 14.46           C  
ANISOU  123  CB  ALA A  16     2499   2025    972    448     77     38       C  
ATOM    124  N   CYS A  17       0.827   2.121 -18.322  1.00 13.15           N  
ANISOU  124  N   CYS A  17     2132   1828   1035    344     79     86       N  
ATOM    125  CA  CYS A  17       0.823   1.968 -16.869  1.00 12.48           C  
ANISOU  125  CA  CYS A  17     1964   1734   1044    299     75     68       C  
ATOM    126  C   CYS A  17      -0.168   0.874 -16.480  1.00 12.14           C  
ANISOU  126  C   CYS A  17     1906   1693   1014    286      9      6       C  
ATOM    127  O   CYS A  17      -1.314   0.887 -16.919  1.00 12.21           O  
ANISOU  127  O   CYS A  17     1932   1708   1000    295    -60    -17       O  
ATOM    128  CB  CYS A  17       0.442   3.274 -16.192  1.00 12.31           C  
ANISOU  128  CB  CYS A  17     1904   1695   1076    279     61     97       C  
ATOM    129  SG  CYS A  17       0.600   3.201 -14.409  1.00 13.21           S  
ANISOU  129  SG  CYS A  17     1929   1801   1290    228     66     78       S  
ATOM    130  N   THR A  18       0.268  -0.063 -15.645  1.00 11.47           N  
ANISOU  130  N   THR A  18     1787   1603    970    264     30    -19       N  
ATOM    131  CA  THR A  18      -0.538  -1.248 -15.358  1.00 11.12           C  
ANISOU  131  CA  THR A  18     1740   1550    935    246    -19    -74       C  
ATOM    132  C   THR A  18      -1.541  -1.028 -14.215  1.00 10.58           C  
ANISOU  132  C   THR A  18     1603   1481    938    207    -63    -88       C  
ATOM    133  O   THR A  18      -2.332  -1.923 -13.896  1.00 10.50           O  
ANISOU  133  O   THR A  18     1580   1464    946    182   -103   -128       O  
ATOM    134  CB  THR A  18       0.359  -2.450 -15.044  1.00 11.19           C  
ANISOU  134  CB  THR A  18     1758   1545    947    249     26    -91       C  
ATOM    135  OG1 THR A  18       1.120  -2.194 -13.854  1.00 10.57           O  
ANISOU  135  OG1 THR A  18     1615   1469    931    232     69    -66       O  
ATOM    136  CG2 THR A  18       1.301  -2.723 -16.218  1.00 11.08           C  
ANISOU  136  CG2 THR A  18     1814   1538    857    298     75    -81       C  
ATOM    137  N   SER A  19      -1.520   0.164 -13.618  1.00  9.92           N  
ANISOU  137  N   SER A  19     1477   1400    893    202    -51    -55       N  
ATOM    138  CA  SER A  19      -2.385   0.471 -12.481  1.00  9.31           C  
ANISOU  138  CA  SER A  19     1336   1323    878    176    -80    -65       C  
ATOM    139  C   SER A  19      -3.758   0.952 -12.931  1.00  9.78           C  
ANISOU  139  C   SER A  19     1388   1398    930    188   -145    -75       C  
ATOM    140  O   SER A  19      -3.966   1.266 -14.106  1.00  9.70           O  
ANISOU  140  O   SER A  19     1425   1397    864    220   -171    -67       O  
ATOM    141  CB  SER A  19      -1.729   1.534 -11.586  1.00  8.75           C  
ANISOU  141  CB  SER A  19     1232   1243    849    168    -40    -32       C  
ATOM    142  OG  SER A  19      -1.880   2.846 -12.100  1.00  8.65           O  
ANISOU  142  OG  SER A  19     1239   1224    823    190    -45      0       O  
ATOM    143  N   ALA A  20      -4.694   1.021 -11.985  1.00  9.69           N  
ANISOU  143  N   ALA A  20     1314   1395    971    168   -170    -90       N  
ATOM    144  CA  ALA A  20      -5.954   1.719 -12.226  1.00 10.32           C  
ANISOU  144  CA  ALA A  20     1367   1497   1056    190   -225    -91       C  
ATOM    145  C   ALA A  20      -5.670   3.205 -12.455  1.00 10.74           C  
ANISOU  145  C   ALA A  20     1444   1537   1099    230   -210    -48       C  
ATOM    146  O   ALA A  20      -4.652   3.733 -11.992  1.00 10.78           O  
ANISOU  146  O   ALA A  20     1462   1516   1118    224   -155    -23       O  
ATOM    147  CB  ALA A  20      -6.912   1.532 -11.066  1.00 10.08           C  
ANISOU  147  CB  ALA A  20     1259   1482   1089    164   -238   -110       C  
ATOM    148  N   ASP A  21      -6.568   3.861 -13.182  1.00 11.79           N  
ANISOU  148  N   ASP A  21     1584   1687   1209    272   -261    -39       N  
ATOM    149  CA  ASP A  21      -6.443   5.277 -13.524  1.00 12.31           C  
ANISOU  149  CA  ASP A  21     1686   1732   1260    318   -251      5       C  
ATOM    150  C   ASP A  21      -7.820   5.936 -13.502  1.00 12.71           C  
ANISOU  150  C   ASP A  21     1697   1807   1326    363   -309      4       C  
ATOM    151  O   ASP A  21      -8.729   5.500 -14.204  1.00 13.24           O  
ANISOU  151  O   ASP A  21     1749   1915   1367    379   -375    -15       O  
ATOM    152  CB  ASP A  21      -5.819   5.431 -14.916  1.00 13.00           C  
ANISOU  152  CB  ASP A  21     1857   1812   1269    345   -247     33       C  
ATOM    153  CG  ASP A  21      -5.394   6.860 -15.214  1.00 13.87           C  
ANISOU  153  CG  ASP A  21     2019   1884   1366    381   -216     90       C  
ATOM    154  OD1 ASP A  21      -4.684   7.454 -14.382  1.00 13.86           O  
ANISOU  154  OD1 ASP A  21     2010   1846   1410    355   -163    106       O  
ATOM    155  OD2 ASP A  21      -5.759   7.384 -16.290  1.00 16.81           O  
ANISOU  155  OD2 ASP A  21     2445   2261   1680    432   -248    117       O  
ATOM    156  N   GLY A  22      -7.972   6.982 -12.694  1.00 12.62           N  
ANISOU  156  N   GLY A  22     1668   1770   1355    384   -287     22       N  
ATOM    157  CA  GLY A  22      -9.229   7.714 -12.611  1.00 13.05           C  
ANISOU  157  CA  GLY A  22     1685   1846   1426    442   -331     25       C  
ATOM    158  C   GLY A  22      -8.995   9.204 -12.462  1.00 13.40           C  
ANISOU  158  C   GLY A  22     1779   1836   1475    491   -303     65       C  
ATOM    159  O   GLY A  22      -8.330   9.818 -13.300  1.00 13.61           O  
ANISOU  159  O   GLY A  22     1887   1825   1458    509   -289    105       O  
ATOM    160  N   VAL A  23      -9.527   9.790 -11.389  1.00 12.87           N  
ANISOU  160  N   VAL A  23     1671   1760   1460    511   -290     56       N  
ATOM    161  CA  VAL A  23      -9.252  11.193 -11.080  1.00 12.83           C  
ANISOU  161  CA  VAL A  23     1723   1687   1465    551   -258     85       C  
ATOM    162  C   VAL A  23      -7.780  11.389 -10.662  1.00 12.36           C  
ANISOU  162  C   VAL A  23     1717   1567   1414    487   -195     94       C  
ATOM    163  O   VAL A  23      -7.254  12.498 -10.727  1.00 12.34           O  
ANISOU  163  O   VAL A  23     1784   1497   1410    500   -168    125       O  
ATOM    164  CB  VAL A  23     -10.221  11.753 -10.015  1.00 13.23           C  
ANISOU  164  CB  VAL A  23     1721   1743   1563    598   -258     66       C  
ATOM    165  CG1 VAL A  23     -11.658  11.649 -10.523  1.00 13.01           C  
ANISOU  165  CG1 VAL A  23     1629   1783   1530    666   -322     64       C  
ATOM    166  CG2 VAL A  23     -10.051  11.034  -8.677  1.00 12.03           C  
ANISOU  166  CG2 VAL A  23     1510   1608   1454    539   -221     25       C  
ATOM    167  N   VAL A  24      -7.125  10.303 -10.256  1.00 11.68           N  
ANISOU  167  N   VAL A  24     1596   1504   1336    418   -174     69       N  
ATOM    168  CA  VAL A  24      -5.681  10.286 -10.057  1.00 11.42           C  
ANISOU  168  CA  VAL A  24     1599   1435   1306    358   -123     79       C  
ATOM    169  C   VAL A  24      -5.141   8.943 -10.544  1.00 11.07           C  
ANISOU  169  C   VAL A  24     1537   1431   1237    317   -121     68       C  
ATOM    170  O   VAL A  24      -5.851   7.935 -10.513  1.00 10.59           O  
ANISOU  170  O   VAL A  24     1428   1419   1176    314   -152     38       O  
ATOM    171  CB  VAL A  24      -5.311  10.502  -8.568  1.00 11.16           C  
ANISOU  171  CB  VAL A  24     1541   1378   1321    324    -92     53       C  
ATOM    172  CG1 VAL A  24      -5.823   9.344  -7.707  1.00 11.50           C  
ANISOU  172  CG1 VAL A  24     1509   1476   1386    303   -100     11       C  
ATOM    173  CG2 VAL A  24      -3.793  10.710  -8.408  1.00 11.44           C  
ANISOU  173  CG2 VAL A  24     1610   1375   1363    263    -48     67       C  
ATOM    174  N   ASN A  25      -3.900   8.928 -11.025  1.00 10.80           N  
ANISOU  174  N   ASN A  25     1544   1377   1183    285    -82     93       N  
ATOM    175  CA  ASN A  25      -3.280   7.670 -11.415  1.00 10.47           C  
ANISOU  175  CA  ASN A  25     1492   1370   1118    254    -70     81       C  
ATOM    176  C   ASN A  25      -2.823   6.934 -10.166  1.00 10.02           C  
ANISOU  176  C   ASN A  25     1381   1323   1103    209    -49     50       C  
ATOM    177  O   ASN A  25      -2.165   7.516  -9.303  1.00 10.33           O  
ANISOU  177  O   ASN A  25     1413   1335   1176    182    -21     53       O  
ATOM    178  CB  ASN A  25      -2.109   7.893 -12.374  1.00 10.79           C  
ANISOU  178  CB  ASN A  25     1587   1393   1120    245    -27    122       C  
ATOM    179  CG  ASN A  25      -1.593   6.596 -12.963  1.00 10.55           C  
ANISOU  179  CG  ASN A  25     1557   1399   1054    235    -16    109       C  
ATOM    180  OD1 ASN A  25      -2.124   6.084 -13.963  1.00 11.65           O  
ANISOU  180  OD1 ASN A  25     1726   1561   1139    266    -48    102       O  
ATOM    181  ND2 ASN A  25      -0.554   6.055 -12.353  1.00  7.97           N  
ANISOU  181  ND2 ASN A  25     1201   1077    752    196     26    102       N  
ATOM    182  N   GLU A  26      -3.184   5.659 -10.070  1.00  9.76           N  
ANISOU  182  N   GLU A  26     1316   1326   1067    198    -67     18       N  
ATOM    183  CA  GLU A  26      -2.873   4.849  -8.897  1.00  9.28           C  
ANISOU  183  CA  GLU A  26     1211   1274   1039    163    -49     -7       C  
ATOM    184  C   GLU A  26      -1.366   4.729  -8.687  1.00  9.22           C  
ANISOU  184  C   GLU A  26     1211   1258   1034    135     -3      8       C  
ATOM    185  O   GLU A  26      -0.866   5.016  -7.602  1.00  8.73           O  
ANISOU  185  O   GLU A  26     1125   1187   1004    112     14      4       O  
ATOM    186  CB  GLU A  26      -3.501   3.462  -9.033  1.00  9.23           C  
ANISOU  186  CB  GLU A  26     1184   1297   1025    155    -73    -37       C  
ATOM    187  CG  GLU A  26      -2.992   2.445  -8.038  1.00  9.08           C  
ANISOU  187  CG  GLU A  26     1139   1282   1029    123    -48    -54       C  
ATOM    188  CD  GLU A  26      -3.617   1.080  -8.206  1.00  9.84           C  
ANISOU  188  CD  GLU A  26     1228   1392   1120    108    -69    -82       C  
ATOM    189  OE1 GLU A  26      -4.349   0.851  -9.196  1.00 11.06           O  
ANISOU  189  OE1 GLU A  26     1397   1556   1250    118   -108    -93       O  
ATOM    190  OE2 GLU A  26      -3.358   0.224  -7.340  1.00 10.06           O  
ANISOU  190  OE2 GLU A  26     1239   1417   1166     86    -50    -92       O  
ATOM    191  N   TYR A  27      -0.652   4.303  -9.726  1.00  9.49           N  
ANISOU  191  N   TYR A  27     1276   1298   1031    140     16     25       N  
ATOM    192  CA  TYR A  27       0.797   4.108  -9.630  1.00  9.83           C  
ANISOU  192  CA  TYR A  27     1312   1344   1077    119     64     43       C  
ATOM    193  C   TYR A  27       1.517   5.378  -9.189  1.00  9.87           C  
ANISOU  193  C   TYR A  27     1312   1325   1113     94     87     69       C  
ATOM    194  O   TYR A  27       2.335   5.339  -8.265  1.00 10.01           O  
ANISOU  194  O   TYR A  27     1292   1348   1162     64    103     64       O  
ATOM    195  CB  TYR A  27       1.364   3.613 -10.960  1.00 10.20           C  
ANISOU  195  CB  TYR A  27     1399   1404   1073    141     89     60       C  
ATOM    196  CG  TYR A  27       2.874   3.581 -11.020  1.00 10.70           C  
ANISOU  196  CG  TYR A  27     1448   1477   1140    127    147     88       C  
ATOM    197  CD1 TYR A  27       3.592   2.516 -10.482  1.00 11.08           C  
ANISOU  197  CD1 TYR A  27     1463   1548   1199    125    166     74       C  
ATOM    198  CD2 TYR A  27       3.585   4.611 -11.627  1.00 10.91           C  
ANISOU  198  CD2 TYR A  27     1492   1494   1161    118    184    133       C  
ATOM    199  CE1 TYR A  27       4.985   2.480 -10.549  1.00 11.43           C  
ANISOU  199  CE1 TYR A  27     1479   1613   1250    119    218    101       C  
ATOM    200  CE2 TYR A  27       4.970   4.588 -11.689  1.00 11.34           C  
ANISOU  200  CE2 TYR A  27     1516   1567   1225    100    241    161       C  
ATOM    201  CZ  TYR A  27       5.664   3.524 -11.152  1.00 10.70           C  
ANISOU  201  CZ  TYR A  27     1391   1517   1157    103    256    144       C  
ATOM    202  OH  TYR A  27       7.041   3.504 -11.220  1.00 11.78           O  
ANISOU  202  OH  TYR A  27     1485   1684   1308     92    311    173       O  
ATOM    203  N   GLN A  28       1.200   6.497  -9.841  1.00 10.32           N  
ANISOU  203  N   GLN A  28     1408   1353   1159    106     84     95       N  
ATOM    204  CA  GLN A  28       1.839   7.779  -9.547  1.00 10.61           C  
ANISOU  204  CA  GLN A  28     1455   1351   1225     75    106    121       C  
ATOM    205  C   GLN A  28       1.554   8.224  -8.110  1.00 10.54           C  
ANISOU  205  C   GLN A  28     1419   1324   1261     55     85     89       C  
ATOM    206  O   GLN A  28       2.475   8.647  -7.413  1.00 10.56           O  
ANISOU  206  O   GLN A  28     1402   1314   1295     11    101     90       O  
ATOM    207  CB  GLN A  28       1.398   8.874 -10.531  1.00 11.09           C  
ANISOU  207  CB  GLN A  28     1579   1373   1261    101    106    158       C  
ATOM    208  CG  GLN A  28       1.815   8.644 -11.999  1.00 11.88           C  
ANISOU  208  CG  GLN A  28     1721   1487   1305    121    136    197       C  
ATOM    209  CD  GLN A  28       3.331   8.659 -12.223  1.00 12.68           C  
ANISOU  209  CD  GLN A  28     1808   1597   1415     79    200    231       C  
ATOM    210  OE1 GLN A  28       4.087   9.267 -11.457  1.00 14.05           O  
ANISOU  210  OE1 GLN A  28     1950   1750   1639     27    219    237       O  
ATOM    211  NE2 GLN A  28       3.777   7.978 -13.274  1.00 11.35           N  
ANISOU  211  NE2 GLN A  28     1657   1460   1194    102    233    250       N  
ATOM    212  N   TYR A  29       0.296   8.129  -7.665  1.00 10.24           N  
ANISOU  212  N   TYR A  29     1377   1288   1225     87     49     61       N  
ATOM    213  CA  TYR A  29      -0.037   8.497  -6.277  1.00 10.10           C  
ANISOU  213  CA  TYR A  29     1339   1257   1240     78     35     29       C  
ATOM    214  C   TYR A  29       0.808   7.697  -5.289  1.00  9.83           C  
ANISOU  214  C   TYR A  29     1261   1253   1221     42     45      9       C  
ATOM    215  O   TYR A  29       1.457   8.264  -4.408  1.00 10.26           O  
ANISOU  215  O   TYR A  29     1310   1290   1298      9     47      0       O  
ATOM    216  CB  TYR A  29      -1.526   8.296  -5.952  1.00  9.80           C  
ANISOU  216  CB  TYR A  29     1288   1233   1200    121      5      3       C  
ATOM    217  CG  TYR A  29      -1.848   8.735  -4.533  1.00  9.42           C  
ANISOU  217  CG  TYR A  29     1229   1173   1179    120      2    -27       C  
ATOM    218  CD1 TYR A  29      -2.081  10.070  -4.242  1.00 10.68           C  
ANISOU  218  CD1 TYR A  29     1427   1281   1350    135      0    -28       C  
ATOM    219  CD2 TYR A  29      -1.860   7.824  -3.481  1.00  9.78           C  
ANISOU  219  CD2 TYR A  29     1234   1253   1230    106      4    -54       C  
ATOM    220  CE1 TYR A  29      -2.351  10.490  -2.951  1.00 11.58           C  
ANISOU  220  CE1 TYR A  29     1541   1380   1478    139      0    -62       C  
ATOM    221  CE2 TYR A  29      -2.124   8.232  -2.178  1.00 10.06           C  
ANISOU  221  CE2 TYR A  29     1267   1279   1276    109      5    -82       C  
ATOM    222  CZ  TYR A  29      -2.369   9.565  -1.922  1.00 10.86           C  
ANISOU  222  CZ  TYR A  29     1408   1332   1386    127      2    -89       C  
ATOM    223  OH  TYR A  29      -2.629   9.985  -0.640  1.00 12.72           O  
ANISOU  223  OH  TYR A  29     1652   1557   1625    136      5   -121       O  
ATOM    224  N   ASN A  30       0.812   6.379  -5.455  1.00  9.54           N  
ANISOU  224  N   ASN A  30     1199   1258   1169     50     47      3       N  
ATOM    225  CA  ASN A  30       1.526   5.497  -4.534  1.00  9.77           C  
ANISOU  225  CA  ASN A  30     1191   1315   1207     30     54    -11       C  
ATOM    226  C   ASN A  30       3.051   5.603  -4.634  1.00  9.97           C  
ANISOU  226  C   ASN A  30     1197   1349   1240     -1     77     10       C  
ATOM    227  O   ASN A  30       3.751   5.412  -3.643  1.00  9.95           O  
ANISOU  227  O   ASN A  30     1163   1364   1252    -22     74     -1       O  
ATOM    228  CB  ASN A  30       1.043   4.048  -4.704  1.00  9.61           C  
ANISOU  228  CB  ASN A  30     1160   1323   1169     50     51    -22       C  
ATOM    229  CG  ASN A  30      -0.379   3.841  -4.177  1.00 10.09           C  
ANISOU  229  CG  ASN A  30     1214   1386   1234     65     29    -46       C  
ATOM    230  OD1 ASN A  30      -1.210   3.196  -4.824  1.00 12.87           O  
ANISOU  230  OD1 ASN A  30     1569   1746   1574     79     16    -51       O  
ATOM    231  ND2 ASN A  30      -0.662   4.391  -3.008  1.00  8.27           N  
ANISOU  231  ND2 ASN A  30      973   1149   1020     62     25    -61       N  
ATOM    232  N   LYS A  31       3.560   5.939  -5.817  1.00 10.47           N  
ANISOU  232  N   LYS A  31     1279   1407   1294     -4    102     42       N  
ATOM    233  CA  LYS A  31       4.972   6.300  -5.975  1.00 11.18           C  
ANISOU  233  CA  LYS A  31     1343   1505   1401    -40    131     69       C  
ATOM    234  C   LYS A  31       5.319   7.520  -5.099  1.00 11.41           C  
ANISOU  234  C   LYS A  31     1367   1502   1467    -89    117     61       C  
ATOM    235  O   LYS A  31       6.411   7.595  -4.528  1.00 11.91           O  
ANISOU  235  O   LYS A  31     1386   1585   1555   -129    120     62       O  
ATOM    236  CB  LYS A  31       5.287   6.569  -7.457  1.00 11.67           C  
ANISOU  236  CB  LYS A  31     1434   1561   1439    -32    169    110       C  
ATOM    237  CG  LYS A  31       6.683   7.106  -7.745  1.00 13.29           C  
ANISOU  237  CG  LYS A  31     1610   1775   1667    -76    211    147       C  
ATOM    238  CD  LYS A  31       6.898   7.344  -9.234  1.00 14.43           C  
ANISOU  238  CD  LYS A  31     1793   1913   1777    -62    257    193       C  
ATOM    239  CE  LYS A  31       8.332   7.784  -9.528  1.00 16.10           C  
ANISOU  239  CE  LYS A  31     1960   2141   2014   -109    312    236       C  
ATOM    240  NZ  LYS A  31       8.554   8.005 -10.987  1.00 17.66           N  
ANISOU  240  NZ  LYS A  31     2202   2337   2171    -91    369    287       N  
ATOM    241  N   SER A  32       4.386   8.463  -4.999  1.00 11.32           N  
ANISOU  241  N   SER A  32     1403   1441   1458    -82     98     51       N  
ATOM    242  CA  SER A  32       4.550   9.650  -4.151  1.00 11.57           C  
ANISOU  242  CA  SER A  32     1451   1427   1520   -121     81     34       C  
ATOM    243  C   SER A  32       4.344   9.364  -2.663  1.00 11.06           C  
ANISOU  243  C   SER A  32     1365   1377   1459   -122     49    -13       C  
ATOM    244  O   SER A  32       5.084   9.874  -1.836  1.00 11.54           O  
ANISOU  244  O   SER A  32     1414   1430   1541   -167     33    -30       O  
ATOM    245  CB  SER A  32       3.598  10.770  -4.593  1.00 11.90           C  
ANISOU  245  CB  SER A  32     1560   1402   1558    -99     77     41       C  
ATOM    246  OG  SER A  32       4.018  11.329  -5.822  1.00 12.99           O  
ANISOU  246  OG  SER A  32     1728   1514   1692   -112    108     90       O  
ATOM    247  N   LEU A  33       3.333   8.565  -2.330  1.00 10.63           N  
ANISOU  247  N   LEU A  33     1310   1347   1383    -73     38    -32       N  
ATOM    248  CA  LEU A  33       3.044   8.200  -0.932  1.00 10.14           C  
ANISOU  248  CA  LEU A  33     1234   1303   1315    -66     17    -71       C  
ATOM    249  C   LEU A  33       4.135   7.344  -0.264  1.00  9.80           C  
ANISOU  249  C   LEU A  33     1143   1310   1272    -87     11    -73       C  
ATOM    250  O   LEU A  33       4.455   7.537   0.908  1.00  9.35           O  
ANISOU  250  O   LEU A  33     1080   1259   1212   -103    -13   -101       O  
ATOM    251  CB  LEU A  33       1.719   7.437  -0.859  1.00  9.89           C  
ANISOU  251  CB  LEU A  33     1205   1289   1265    -15     17    -81       C  
ATOM    252  CG  LEU A  33       1.287   6.954   0.535  1.00  9.65           C  
ANISOU  252  CG  LEU A  33     1164   1281   1221     -1      8   -112       C  
ATOM    253  CD1 LEU A  33       1.151   8.137   1.477  1.00  8.65           C  
ANISOU  253  CD1 LEU A  33     1072   1118   1097     -7     -6   -142       C  
ATOM    254  CD2 LEU A  33      -0.022   6.163   0.441  1.00  8.97           C  
ANISOU  254  CD2 LEU A  33     1070   1214   1126     37     17   -113       C  
ATOM    255  N   ALA A  34       4.675   6.383  -1.008  1.00  9.35           N  
ANISOU  255  N   ALA A  34     1054   1288   1209    -79     31    -46       N  
ATOM    256  CA  ALA A  34       5.594   5.381  -0.446  1.00  9.18           C  
ANISOU  256  CA  ALA A  34      987   1319   1184    -78     27    -44       C  
ATOM    257  C   ALA A  34       6.734   5.976   0.399  1.00  9.42           C  
ANISOU  257  C   ALA A  34      984   1363   1232   -123      2    -55       C  
ATOM    258  O   ALA A  34       6.933   5.548   1.532  1.00  9.18           O  
ANISOU  258  O   ALA A  34      938   1361   1188   -116    -25    -75       O  
ATOM    259  CB  ALA A  34       6.153   4.478  -1.557  1.00  9.09           C  
ANISOU  259  CB  ALA A  34      953   1334   1166    -59     60    -12       C  
ATOM    260  N   PRO A  35       7.481   6.960  -0.146  1.00 10.23           N  
ANISOU  260  N   PRO A  35     1074   1447   1364   -173      8    -40       N  
ATOM    261  CA  PRO A  35       8.566   7.595   0.617  1.00 10.76           C  
ANISOU  261  CA  PRO A  35     1104   1526   1456   -231    -23    -54       C  
ATOM    262  C   PRO A  35       8.102   8.407   1.828  1.00 10.72           C  
ANISOU  262  C   PRO A  35     1142   1486   1444   -249    -68   -102       C  
ATOM    263  O   PRO A  35       8.815   8.476   2.822  1.00 11.08           O  
ANISOU  263  O   PRO A  35     1161   1560   1491   -277   -109   -127       O  
ATOM    264  CB  PRO A  35       9.243   8.500  -0.411  1.00 11.32           C  
ANISOU  264  CB  PRO A  35     1165   1572   1565   -285      5    -22       C  
ATOM    265  CG  PRO A  35       8.263   8.678  -1.486  1.00 11.52           C  
ANISOU  265  CG  PRO A  35     1249   1553   1575   -252     40     -1       C  
ATOM    266  CD  PRO A  35       7.455   7.437  -1.538  1.00 10.50           C  
ANISOU  266  CD  PRO A  35     1128   1453   1410   -181     46     -5       C  
ATOM    267  N   VAL A  36       6.919   9.003   1.750  1.00 10.57           N  
ANISOU  267  N   VAL A  36     1191   1409   1415   -227    -60   -117       N  
ATOM    268  CA  VAL A  36       6.333   9.698   2.898  1.00 10.77           C  
ANISOU  268  CA  VAL A  36     1269   1400   1424   -226    -93   -166       C  
ATOM    269  C   VAL A  36       5.951   8.685   3.991  1.00 10.60           C  
ANISOU  269  C   VAL A  36     1239   1427   1360   -179   -107   -187       C  
ATOM    270  O   VAL A  36       6.199   8.920   5.186  1.00 11.23           O  
ANISOU  270  O   VAL A  36     1332   1515   1419   -190   -145   -225       O  
ATOM    271  CB  VAL A  36       5.105  10.523   2.482  1.00 10.74           C  
ANISOU  271  CB  VAL A  36     1334   1327   1419   -197    -74   -172       C  
ATOM    272  CG1 VAL A  36       4.437  11.165   3.703  1.00 10.79           C  
ANISOU  272  CG1 VAL A  36     1397   1301   1402   -180    -98   -224       C  
ATOM    273  CG2 VAL A  36       5.504  11.589   1.463  1.00 10.75           C  
ANISOU  273  CG2 VAL A  36     1358   1271   1457   -242    -59   -146       C  
ATOM    274  N   LEU A  37       5.362   7.563   3.580  1.00  9.68           N  
ANISOU  274  N   LEU A  37     1109   1341   1229   -130    -78   -162       N  
ATOM    275  CA  LEU A  37       5.005   6.482   4.511  1.00  9.49           C  
ANISOU  275  CA  LEU A  37     1080   1358   1167    -88    -81   -170       C  
ATOM    276  C   LEU A  37       6.244   5.916   5.206  1.00  9.76           C  
ANISOU  276  C   LEU A  37     1071   1446   1191   -101   -113   -169       C  
ATOM    277  O   LEU A  37       6.234   5.700   6.414  1.00 10.31           O  
ANISOU  277  O   LEU A  37     1155   1537   1224    -85   -139   -191       O  
ATOM    278  CB  LEU A  37       4.261   5.354   3.781  1.00  8.44           C  
ANISOU  278  CB  LEU A  37      940   1238   1029    -47    -44   -141       C  
ATOM    279  CG  LEU A  37       3.774   4.155   4.603  1.00  7.80           C  
ANISOU  279  CG  LEU A  37      861   1187    914     -8    -36   -139       C  
ATOM    280  CD1 LEU A  37       2.881   4.608   5.765  1.00  6.77           C  
ANISOU  280  CD1 LEU A  37      770   1047    756      9    -39   -171       C  
ATOM    281  CD2 LEU A  37       3.040   3.136   3.733  1.00  6.06           C  
ANISOU  281  CD2 LEU A  37      637    967    699     16     -3   -115       C  
ATOM    282  N   ALA A  38       7.302   5.670   4.432  1.00 10.00           N  
ANISOU  282  N   ALA A  38     1046   1502   1250   -123   -108   -139       N  
ATOM    283  CA  ALA A  38       8.582   5.199   4.976  1.00 10.15           C  
ANISOU  283  CA  ALA A  38     1007   1581   1267   -132   -141   -134       C  
ATOM    284  C   ALA A  38       9.128   6.140   6.051  1.00 10.93           C  
ANISOU  284  C   ALA A  38     1109   1682   1362   -177   -200   -175       C  
ATOM    285  O   ALA A  38       9.506   5.699   7.138  1.00 10.70           O  
ANISOU  285  O   ALA A  38     1070   1696   1298   -159   -241   -190       O  
ATOM    286  CB  ALA A  38       9.612   5.021   3.851  1.00 10.45           C  
ANISOU  286  CB  ALA A  38      979   1645   1344   -151   -118    -95       C  
ATOM    287  N   ASP A  39       9.161   7.432   5.741  1.00 11.31           N  
ANISOU  287  N   ASP A  39     1176   1678   1441   -236   -207   -193       N  
ATOM    288  CA  ASP A  39       9.667   8.440   6.670  1.00 12.07           C  
ANISOU  288  CA  ASP A  39     1287   1762   1538   -291   -266   -240       C  
ATOM    289  C   ASP A  39       8.839   8.520   7.953  1.00 11.82           C  
ANISOU  289  C   ASP A  39     1328   1717   1447   -254   -292   -287       C  
ATOM    290  O   ASP A  39       9.379   8.774   9.035  1.00 12.37           O  
ANISOU  290  O   ASP A  39     1401   1809   1489   -274   -352   -326       O  
ATOM    291  CB  ASP A  39       9.701   9.820   5.998  1.00 12.65           C  
ANISOU  291  CB  ASP A  39     1388   1761   1658   -359   -258   -248       C  
ATOM    292  CG  ASP A  39      10.877   9.990   5.053  1.00 13.71           C  
ANISOU  292  CG  ASP A  39     1443   1915   1850   -421   -246   -210       C  
ATOM    293  OD1 ASP A  39      11.812   9.163   5.077  1.00 14.30           O  
ANISOU  293  OD1 ASP A  39     1432   2069   1931   -416   -256   -186       O  
ATOM    294  OD2 ASP A  39      10.864  10.975   4.287  1.00 16.51           O  
ANISOU  294  OD2 ASP A  39     1823   2207   2244   -472   -223   -199       O  
ATOM    295  N   THR A  40       7.534   8.314   7.833  1.00 10.90           N  
ANISOU  295  N   THR A  40     1265   1568   1307   -199   -247   -284       N  
ATOM    296  CA  THR A  40       6.659   8.312   9.003  1.00 11.14           C  
ANISOU  296  CA  THR A  40     1361   1592   1279   -154   -254   -320       C  
ATOM    297  C   THR A  40       6.997   7.129   9.922  1.00 11.43           C  
ANISOU  297  C   THR A  40     1376   1701   1266   -114   -273   -311       C  
ATOM    298  O   THR A  40       7.080   7.294  11.145  1.00 12.25           O  
ANISOU  298  O   THR A  40     1517   1821   1316   -104   -313   -348       O  
ATOM    299  CB  THR A  40       5.173   8.309   8.595  1.00 10.51           C  
ANISOU  299  CB  THR A  40     1325   1473   1195   -105   -195   -312       C  
ATOM    300  OG1 THR A  40       4.940   9.378   7.667  1.00 10.17           O  
ANISOU  300  OG1 THR A  40     1302   1364   1196   -134   -181   -313       O  
ATOM    301  CG2 THR A  40       4.279   8.500   9.805  1.00 10.13           C  
ANISOU  301  CG2 THR A  40     1343   1418   1090    -61   -193   -351       C  
ATOM    302  N   PHE A  41       7.226   5.954   9.334  1.00 11.06           N  
ANISOU  302  N   PHE A  41     1278   1694   1231    -87   -246   -261       N  
ATOM    303  CA  PHE A  41       7.717   4.801  10.098  1.00 11.51           C  
ANISOU  303  CA  PHE A  41     1314   1814   1245    -46   -265   -242       C  
ATOM    304  C   PHE A  41       9.088   5.080  10.709  1.00 12.47           C  
ANISOU  304  C   PHE A  41     1392   1984   1362    -80   -340   -261       C  
ATOM    305  O   PHE A  41       9.334   4.728  11.857  1.00 12.54           O  
ANISOU  305  O   PHE A  41     1418   2034   1313    -51   -381   -274       O  
ATOM    306  CB  PHE A  41       7.819   3.542   9.231  1.00 10.94           C  
ANISOU  306  CB  PHE A  41     1200   1764   1194    -13   -222   -187       C  
ATOM    307  CG  PHE A  41       6.530   2.787   9.091  1.00 10.95           C  
ANISOU  307  CG  PHE A  41     1244   1740   1178     31   -165   -168       C  
ATOM    308  CD1 PHE A  41       5.973   2.136  10.182  1.00 11.88           C  
ANISOU  308  CD1 PHE A  41     1404   1871   1239     74   -157   -167       C  
ATOM    309  CD2 PHE A  41       5.896   2.689   7.856  1.00 11.43           C  
ANISOU  309  CD2 PHE A  41     1299   1765   1279     26   -118   -149       C  
ATOM    310  CE1 PHE A  41       4.794   1.432  10.064  1.00 11.00           C  
ANISOU  310  CE1 PHE A  41     1323   1738   1119    102   -101   -147       C  
ATOM    311  CE2 PHE A  41       4.715   1.980   7.721  1.00 11.18           C  
ANISOU  311  CE2 PHE A  41     1295   1714   1237     56    -72   -135       C  
ATOM    312  CZ  PHE A  41       4.161   1.345   8.827  1.00 11.52           C  
ANISOU  312  CZ  PHE A  41     1374   1770   1233     90    -62   -132       C  
ATOM    313  N   ARG A  42       9.973   5.705   9.934  1.00 13.03           N  
ANISOU  313  N   ARG A  42     1403   2054   1493   -141   -356   -258       N  
ATOM    314  CA  ARG A  42      11.347   5.942  10.378  1.00 14.35           C  
ANISOU  314  CA  ARG A  42     1505   2277   1671   -183   -428   -271       C  
ATOM    315  C   ARG A  42      11.411   6.864  11.591  1.00 15.62           C  
ANISOU  315  C   ARG A  42     1716   2427   1790   -216   -499   -337       C  
ATOM    316  O   ARG A  42      12.228   6.657  12.495  1.00 16.37           O  
ANISOU  316  O   ARG A  42     1783   2585   1852   -215   -571   -353       O  
ATOM    317  CB  ARG A  42      12.191   6.502   9.231  1.00 14.54           C  
ANISOU  317  CB  ARG A  42     1454   2298   1775   -251   -418   -252       C  
ATOM    318  CG  ARG A  42      12.485   5.491   8.139  1.00 13.64           C  
ANISOU  318  CG  ARG A  42     1277   2215   1690   -213   -360   -190       C  
ATOM    319  CD  ARG A  42      13.301   6.104   7.015  1.00 14.38           C  
ANISOU  319  CD  ARG A  42     1301   2308   1856   -279   -339   -168       C  
ATOM    320  NE  ARG A  42      13.476   5.157   5.910  1.00 14.95           N  
ANISOU  320  NE  ARG A  42     1330   2404   1946   -232   -275   -113       N  
ATOM    321  CZ  ARG A  42      13.212   5.402   4.625  1.00 14.50           C  
ANISOU  321  CZ  ARG A  42     1280   2307   1923   -246   -211    -85       C  
ATOM    322  NH1 ARG A  42      12.777   6.588   4.218  1.00 14.16           N  
ANISOU  322  NH1 ARG A  42     1281   2195   1904   -307   -200   -100       N  
ATOM    323  NH2 ARG A  42      13.409   4.443   3.725  1.00 13.48           N  
ANISOU  323  NH2 ARG A  42     1119   2205   1797   -195   -158    -42       N  
ATOM    324  N   LYS A  43      10.534   7.866  11.618  1.00 16.17           N  
ANISOU  324  N   LYS A  43     1866   2419   1859   -239   -482   -375       N  
ATOM    325  CA  LYS A  43      10.415   8.776  12.758  1.00 17.87           C  
ANISOU  325  CA  LYS A  43     2155   2609   2026   -261   -540   -445       C  
ATOM    326  C   LYS A  43      10.149   8.023  14.068  1.00 18.32           C  
ANISOU  326  C   LYS A  43     2256   2717   1988   -189   -566   -458       C  
ATOM    327  O   LYS A  43      10.585   8.454  15.138  1.00 19.45           O  
ANISOU  327  O   LYS A  43     2431   2879   2080   -205   -641   -510       O  
ATOM    328  CB  LYS A  43       9.305   9.804  12.508  1.00 17.82           C  
ANISOU  328  CB  LYS A  43     2238   2505   2028   -268   -498   -476       C  
ATOM    329  CG  LYS A  43       9.310  10.984  13.481  1.00 20.52           C  
ANISOU  329  CG  LYS A  43     2662   2800   2334   -304   -557   -555       C  
ATOM    330  CD  LYS A  43       8.359  12.090  13.033  1.00 21.73           C  
ANISOU  330  CD  LYS A  43     2897   2848   2510   -311   -513   -580       C  
ATOM    331  CE  LYS A  43       8.650  13.412  13.745  1.00 24.65           C  
ANISOU  331  CE  LYS A  43     3345   3154   2867   -370   -576   -660       C  
ATOM    332  NZ  LYS A  43       7.793  14.530  13.227  1.00 24.63           N  
ANISOU  332  NZ  LYS A  43     3426   3039   2894   -371   -532   -679       N  
ATOM    333  N   GLU A  44       9.445   6.896  13.976  1.00 17.83           N  
ANISOU  333  N   GLU A  44     2201   2674   1900   -113   -504   -410       N  
ATOM    334  CA  GLU A  44       9.161   6.059  15.142  1.00 18.11           C  
ANISOU  334  CA  GLU A  44     2281   2755   1845    -41   -513   -406       C  
ATOM    335  C   GLU A  44      10.242   4.997  15.393  1.00 18.31           C  
ANISOU  335  C   GLU A  44     2237   2864   1855    -14   -557   -367       C  
ATOM    336  O   GLU A  44      10.072   4.138  16.255  1.00 18.44           O  
ANISOU  336  O   GLU A  44     2289   2919   1798     53   -559   -348       O  
ATOM    337  CB  GLU A  44       7.790   5.390  14.991  1.00 17.41           C  
ANISOU  337  CB  GLU A  44     2240   2638   1737     21   -420   -372       C  
ATOM    338  CG  GLU A  44       6.664   6.341  14.630  1.00 17.58           C  
ANISOU  338  CG  GLU A  44     2315   2585   1779      9   -371   -401       C  
ATOM    339  CD  GLU A  44       6.549   7.516  15.581  1.00 19.10           C  
ANISOU  339  CD  GLU A  44     2585   2748   1924     -5   -414   -474       C  
ATOM    340  OE1 GLU A  44       6.439   7.284  16.802  1.00 19.09           O  
ANISOU  340  OE1 GLU A  44     2640   2779   1835     38   -434   -496       O  
ATOM    341  OE2 GLU A  44       6.561   8.670  15.099  1.00 20.29           O  
ANISOU  341  OE2 GLU A  44     2749   2838   2120    -56   -424   -510       O  
ATOM    342  N   GLY A  45      11.336   5.048  14.634  1.00 18.48           N  
ANISOU  342  N   GLY A  45     2161   2915   1946    -60   -586   -350       N  
ATOM    343  CA  GLY A  45      12.519   4.221  14.894  1.00 18.99           C  
ANISOU  343  CA  GLY A  45     2146   3067   2001    -34   -640   -319       C  
ATOM    344  C   GLY A  45      12.630   2.941  14.083  1.00 18.44           C  
ANISOU  344  C   GLY A  45     2026   3020   1962     23   -580   -247       C  
ATOM    345  O   GLY A  45      13.542   2.144  14.306  1.00 18.71           O  
ANISOU  345  O   GLY A  45     2000   3125   1984     64   -616   -215       O  
ATOM    346  N   HIS A  46      11.717   2.736  13.136  1.00 17.33           N  
ANISOU  346  N   HIS A  46     1910   2819   1856     29   -492   -222       N  
ATOM    347  CA  HIS A  46      11.735   1.519  12.320  1.00 16.91           C  
ANISOU  347  CA  HIS A  46     1824   2773   1826     82   -433   -160       C  
ATOM    348  C   HIS A  46      12.581   1.725  11.067  1.00 16.52           C  
ANISOU  348  C   HIS A  46     1682   2737   1858     41   -420   -141       C  
ATOM    349  O   HIS A  46      12.821   2.857  10.638  1.00 16.45           O  
ANISOU  349  O   HIS A  46     1646   2707   1895    -35   -434   -169       O  
ATOM    350  CB  HIS A  46      10.305   1.098  11.965  1.00 16.28           C  
ANISOU  350  CB  HIS A  46     1818   2628   1738    108   -351   -145       C  
ATOM    351  CG  HIS A  46       9.410   1.000  13.159  1.00 17.32           C  
ANISOU  351  CG  HIS A  46     2038   2750   1795    141   -349   -161       C  
ATOM    352  ND1 HIS A  46       9.353  -0.122  13.956  1.00 18.63           N  
ANISOU  352  ND1 HIS A  46     2238   2942   1898    210   -344   -127       N  
ATOM    353  CD2 HIS A  46       8.574   1.903  13.722  1.00 18.42           C  
ANISOU  353  CD2 HIS A  46     2240   2854   1905    121   -347   -206       C  
ATOM    354  CE1 HIS A  46       8.506   0.084  14.948  1.00 18.90           C  
ANISOU  354  CE1 HIS A  46     2350   2962   1868    226   -335   -148       C  
ATOM    355  NE2 HIS A  46       8.022   1.308  14.831  1.00 19.52           N  
ANISOU  355  NE2 HIS A  46     2446   3006   1966    175   -336   -198       N  
ATOM    356  N   LYS A  47      13.064   0.625  10.503  1.00 15.92           N  
ANISOU  356  N   LYS A  47     1561   2692   1797     95   -391    -91       N  
ATOM    357  CA  LYS A  47      13.830   0.683   9.274  1.00 15.68           C  
ANISOU  357  CA  LYS A  47     1445   2677   1834     72   -363    -67       C  
ATOM    358  C   LYS A  47      12.920   0.279   8.122  1.00 14.39           C  
ANISOU  358  C   LYS A  47     1325   2450   1691     87   -277    -45       C  
ATOM    359  O   LYS A  47      12.137  -0.668   8.242  1.00 13.71           O  
ANISOU  359  O   LYS A  47     1301   2335   1571    143   -242    -27       O  
ATOM    360  CB  LYS A  47      15.058  -0.220   9.337  1.00 16.60           C  
ANISOU  360  CB  LYS A  47     1477   2875   1954    130   -386    -30       C  
ATOM    361  CG  LYS A  47      16.252   0.420  10.041  1.00 18.31           C  
ANISOU  361  CG  LYS A  47     1605   3171   2179     91   -476    -51       C  
ATOM    362  CD  LYS A  47      17.471  -0.508  10.030  1.00 20.44           C  
ANISOU  362  CD  LYS A  47     1777   3532   2457    161   -496     -9       C  
ATOM    363  CE  LYS A  47      18.118  -0.644   8.643  1.00 20.51           C  
ANISOU  363  CE  LYS A  47     1699   3559   2537    157   -432     27       C  
ATOM    364  NZ  LYS A  47      18.726   0.625   8.149  1.00 20.57           N  
ANISOU  364  NZ  LYS A  47     1623   3581   2612     47   -446      7       N  
ATOM    365  N   VAL A  48      13.029   1.012   7.016  1.00 13.67           N  
ANISOU  365  N   VAL A  48     1203   2336   1655     32   -246    -45       N  
ATOM    366  CA  VAL A  48      12.151   0.827   5.871  1.00 12.84           C  
ANISOU  366  CA  VAL A  48     1141   2171   1565     38   -176    -30       C  
ATOM    367  C   VAL A  48      12.927   0.829   4.560  1.00 12.94           C  
ANISOU  367  C   VAL A  48     1090   2202   1625     28   -135      0       C  
ATOM    368  O   VAL A  48      13.824   1.656   4.358  1.00 13.06           O  
ANISOU  368  O   VAL A  48     1036   2247   1679    -27   -152     -1       O  
ATOM    369  CB  VAL A  48      11.084   1.940   5.789  1.00 12.32           C  
ANISOU  369  CB  VAL A  48     1137   2040   1506    -16   -169    -63       C  
ATOM    370  CG1 VAL A  48      10.099   1.650   4.653  1.00 11.87           C  
ANISOU  370  CG1 VAL A  48     1124   1930   1457     -1   -107    -48       C  
ATOM    371  CG2 VAL A  48      10.351   2.078   7.100  1.00 12.54           C  
ANISOU  371  CG2 VAL A  48     1226   2054   1485     -6   -203    -96       C  
ATOM    372  N   ASP A  49      12.576  -0.119   3.693  1.00 12.34           N  
ANISOU  372  N   ASP A  49     1040   2106   1542     80    -79     25       N  
ATOM    373  CA  ASP A  49      13.012  -0.142   2.305  1.00 12.40           C  
ANISOU  373  CA  ASP A  49     1015   2116   1579     80    -25     51       C  
ATOM    374  C   ASP A  49      11.792   0.008   1.423  1.00 11.96           C  
ANISOU  374  C   ASP A  49     1038   1991   1518     70     16     45       C  
ATOM    375  O   ASP A  49      10.793  -0.688   1.612  1.00 11.59           O  
ANISOU  375  O   ASP A  49     1056   1906   1441    103     23     36       O  
ATOM    376  CB  ASP A  49      13.682  -1.475   1.954  1.00 12.62           C  
ANISOU  376  CB  ASP A  49     1018   2182   1597    163      6     83       C  
ATOM    377  CG  ASP A  49      15.008  -1.663   2.638  1.00 12.99           C  
ANISOU  377  CG  ASP A  49      971   2311   1654    186    -31     98       C  
ATOM    378  OD1 ASP A  49      15.666  -0.652   2.968  1.00 12.20           O  
ANISOU  378  OD1 ASP A  49      801   2248   1584    121    -70     88       O  
ATOM    379  OD2 ASP A  49      15.396  -2.833   2.840  1.00 12.35           O  
ANISOU  379  OD2 ASP A  49      885   2256   1551    270    -25    120       O  
ATOM    380  N   VAL A  50      11.878   0.914   0.457  1.00 12.13           N  
ANISOU  380  N   VAL A  50     1049   1996   1566     24     42     51       N  
ATOM    381  CA  VAL A  50      10.813   1.115  -0.506  1.00 12.08           C  
ANISOU  381  CA  VAL A  50     1109   1931   1551     20     75     49       C  
ATOM    382  C   VAL A  50      11.214   0.431  -1.803  1.00 12.64           C  
ANISOU  382  C   VAL A  50     1175   2013   1615     60    131     78       C  
ATOM    383  O   VAL A  50      12.310   0.675  -2.318  1.00 13.42           O  
ANISOU  383  O   VAL A  50     1211   2152   1735     51    157    103       O  
ATOM    384  CB  VAL A  50      10.563   2.614  -0.768  1.00 11.95           C  
ANISOU  384  CB  VAL A  50     1103   1878   1559    -50     68     40       C  
ATOM    385  CG1 VAL A  50       9.557   2.792  -1.899  1.00 11.83           C  
ANISOU  385  CG1 VAL A  50     1152   1813   1531    -42    101     46       C  
ATOM    386  CG2 VAL A  50      10.080   3.302   0.505  1.00 12.32           C  
ANISOU  386  CG2 VAL A  50     1171   1906   1605    -81     16      4       C  
ATOM    387  N   ILE A  51      10.333  -0.424  -2.322  1.00 12.59           N  
ANISOU  387  N   ILE A  51     1233   1971   1578    102    150     72       N  
ATOM    388  CA  ILE A  51      10.578  -1.139  -3.574  1.00 13.03           C  
ANISOU  388  CA  ILE A  51     1307   2029   1616    147    201     90       C  
ATOM    389  C   ILE A  51       9.593  -0.673  -4.627  1.00 13.03           C  
ANISOU  389  C   ILE A  51     1369   1982   1598    129    215     83       C  
ATOM    390  O   ILE A  51       8.393  -0.883  -4.494  1.00 12.88           O  
ANISOU  390  O   ILE A  51     1405   1923   1566    128    193     60       O  
ATOM    391  CB  ILE A  51      10.413  -2.676  -3.414  1.00 13.05           C  
ANISOU  391  CB  ILE A  51     1346   2023   1589    215    208     84       C  
ATOM    392  CG1 ILE A  51      11.326  -3.223  -2.313  1.00 13.72           C  
ANISOU  392  CG1 ILE A  51     1378   2153   1683    247    189     95       C  
ATOM    393  CG2 ILE A  51      10.695  -3.386  -4.738  1.00 13.54           C  
ANISOU  393  CG2 ILE A  51     1438   2081   1626    265    261     95       C  
ATOM    394  CD1 ILE A  51      12.781  -2.970  -2.543  1.00 15.62           C  
ANISOU  394  CD1 ILE A  51     1528   2461   1945    258    210    123       C  
ATOM    395  N   ILE A  52      10.103  -0.033  -5.672  1.00 13.63           N  
ANISOU  395  N   ILE A  52     1434   2068   1676    117    253    108       N  
ATOM    396  CA  ILE A  52       9.283   0.410  -6.789  1.00 13.71           C  
ANISOU  396  CA  ILE A  52     1507   2040   1661    111    267    109       C  
ATOM    397  C   ILE A  52       9.878  -0.188  -8.053  1.00 14.03           C  
ANISOU  397  C   ILE A  52     1563   2100   1668    158    324    130       C  
ATOM    398  O   ILE A  52      11.100  -0.178  -8.237  1.00 14.57           O  
ANISOU  398  O   ILE A  52     1573   2214   1749    167    366    159       O  
ATOM    399  CB  ILE A  52       9.253   1.949  -6.898  1.00 13.92           C  
ANISOU  399  CB  ILE A  52     1525   2050   1713     50    262    123       C  
ATOM    400  CG1 ILE A  52       8.929   2.571  -5.535  1.00 14.82           C  
ANISOU  400  CG1 ILE A  52     1620   2150   1861      8    210     99       C  
ATOM    401  CG2 ILE A  52       8.227   2.387  -7.940  1.00 14.05           C  
ANISOU  401  CG2 ILE A  52     1616   2025   1698     55    265    125       C  
ATOM    402  CD1 ILE A  52       8.758   4.090  -5.542  1.00 16.64           C  
ANISOU  402  CD1 ILE A  52     1861   2346   2117    -49    200    105       C  
ATOM    403  N   CYS A  53       9.022  -0.733  -8.908  1.00 13.48           N  
ANISOU  403  N   CYS A  53     1570   1999   1553    189    326    114       N  
ATOM    404  CA  CYS A  53       9.482  -1.333 -10.150  1.00 13.82           C  
ANISOU  404  CA  CYS A  53     1647   2054   1549    241    379    126       C  
ATOM    405  C   CYS A  53      10.171  -0.300 -11.038  1.00 14.12           C  
ANISOU  405  C   CYS A  53     1668   2114   1583    223    430    169       C  
ATOM    406  O   CYS A  53       9.743   0.852 -11.092  1.00 13.51           O  
ANISOU  406  O   CYS A  53     1598   2015   1520    173    413    181       O  
ATOM    407  CB  CYS A  53       8.319  -1.964 -10.912  1.00 13.59           C  
ANISOU  407  CB  CYS A  53     1712   1984   1469    267    357     93       C  
ATOM    408  SG  CYS A  53       7.720  -3.474 -10.160  1.00 13.62           S  
ANISOU  408  SG  CYS A  53     1747   1958   1472    293    321     49       S  
ATOM    409  N   PRO A  54      11.247  -0.707 -11.729  1.00 15.11           N  
ANISOU  409  N   PRO A  54     1772   2280   1689    265    498    196       N  
ATOM    410  CA  PRO A  54      11.814   0.175 -12.733  1.00 15.80           C  
ANISOU  410  CA  PRO A  54     1855   2386   1761    251    559    242       C  
ATOM    411  C   PRO A  54      10.744   0.546 -13.745  1.00 16.15           C  
ANISOU  411  C   PRO A  54     2003   2387   1748    256    546    237       C  
ATOM    412  O   PRO A  54       9.856  -0.264 -14.026  1.00 15.19           O  
ANISOU  412  O   PRO A  54     1952   2237   1581    293    511    196       O  
ATOM    413  CB  PRO A  54      12.903  -0.678 -13.398  1.00 16.59           C  
ANISOU  413  CB  PRO A  54     1936   2536   1831    321    637    262       C  
ATOM    414  CG  PRO A  54      13.127  -1.831 -12.501  1.00 16.48           C  
ANISOU  414  CG  PRO A  54     1892   2534   1837    363    612    232       C  
ATOM    415  CD  PRO A  54      11.890  -2.034 -11.716  1.00 15.32           C  
ANISOU  415  CD  PRO A  54     1791   2333   1698    338    528    186       C  
ATOM    416  N   GLU A  55      10.826   1.767 -14.267  1.00 17.31           N  
ANISOU  416  N   GLU A  55     2155   2525   1896    215    570    278       N  
ATOM    417  CA  GLU A  55       9.903   2.238 -15.292  1.00 17.86           C  
ANISOU  417  CA  GLU A  55     2321   2559   1906    227    559    284       C  
ATOM    418  C   GLU A  55      10.468   2.032 -16.700  1.00 19.27           C  
ANISOU  418  C   GLU A  55     2549   2763   2008    279    639    317       C  
ATOM    419  O   GLU A  55      11.677   2.175 -16.929  1.00 20.04           O  
ANISOU  419  O   GLU A  55     2591   2904   2120    278    719    362       O  
ATOM    420  CB  GLU A  55       9.563   3.709 -15.060  1.00 17.90           C  
ANISOU  420  CB  GLU A  55     2324   2529   1948    162    538    312       C  
ATOM    421  CG  GLU A  55       8.794   3.949 -13.767  1.00 17.42           C  
ANISOU  421  CG  GLU A  55     2237   2438   1945    124    459    272       C  
ATOM    422  CD  GLU A  55       8.578   5.416 -13.450  1.00 18.13           C  
ANISOU  422  CD  GLU A  55     2327   2486   2075     65    443    297       C  
ATOM    423  OE1 GLU A  55       8.979   6.271 -14.263  1.00 20.17           O  
ANISOU  423  OE1 GLU A  55     2612   2733   2320     49    492    348       O  
ATOM    424  OE2 GLU A  55       8.001   5.717 -12.382  1.00 17.71           O  
ANISOU  424  OE2 GLU A  55     2255   2407   2065     36    386    265       O  
ATOM    425  N   LYS A  56       9.575   1.690 -17.630  1.00 19.67           N  
ANISOU  425  N   LYS A  56     2702   2793   1979    325    615    296       N  
ATOM    426  CA  LYS A  56       9.907   1.487 -19.043  1.00 20.97           C  
ANISOU  426  CA  LYS A  56     2940   2976   2050    383    681    320       C  
ATOM    427  C   LYS A  56      10.965   0.394 -19.286  1.00 21.88           C  
ANISOU  427  C   LYS A  56     3033   3137   2142    443    755    316       C  
ATOM    428  O   LYS A  56      11.732   0.451 -20.247  1.00 22.30           O  
ANISOU  428  O   LYS A  56     3108   3224   2143    482    844    357       O  
ATOM    429  CB  LYS A  56      10.277   2.823 -19.696  1.00 21.77           C  
ANISOU  429  CB  LYS A  56     3052   3077   2141    352    737    394       C  
ATOM    430  CG  LYS A  56       9.173   3.873 -19.515  1.00 21.87           C  
ANISOU  430  CG  LYS A  56     3102   3038   2170    311    664    397       C  
ATOM    431  CD  LYS A  56       9.233   5.006 -20.532  1.00 23.72           C  
ANISOU  431  CD  LYS A  56     3401   3257   2356    308    711    467       C  
ATOM    432  CE  LYS A  56       8.015   5.924 -20.382  1.00 23.85           C  
ANISOU  432  CE  LYS A  56     3465   3218   2380    289    629    464       C  
ATOM    433  NZ  LYS A  56       8.124   7.173 -21.194  1.00 25.00           N  
ANISOU  433  NZ  LYS A  56     3672   3336   2493    279    676    541       N  
ATOM    434  N   GLN A  57      10.964  -0.613 -18.413  1.00 21.71           N  
ANISOU  434  N   GLN A  57     2975   3114   2158    456    719    268       N  
ATOM    435  CA  GLN A  57      11.867  -1.755 -18.514  1.00 22.66           C  
ANISOU  435  CA  GLN A  57     3080   3268   2261    525    778    257       C  
ATOM    436  C   GLN A  57      11.097  -3.011 -18.917  1.00 22.55           C  
ANISOU  436  C   GLN A  57     3171   3217   2180    585    736    189       C  
ATOM    437  O   GLN A  57      11.515  -3.730 -19.824  1.00 23.50           O  
ANISOU  437  O   GLN A  57     3354   3349   2225    661    793    180       O  
ATOM    438  CB  GLN A  57      12.582  -1.979 -17.176  1.00 22.36           C  
ANISOU  438  CB  GLN A  57     2923   3255   2318    501    771    259       C  
ATOM    439  CG  GLN A  57      13.689  -3.033 -17.213  1.00 24.31           C  
ANISOU  439  CG  GLN A  57     3134   3547   2558    580    840    260       C  
ATOM    440  CD  GLN A  57      14.331  -3.270 -15.849  1.00 24.58           C  
ANISOU  440  CD  GLN A  57     3051   3608   2679    563    819    263       C  
ATOM    441  OE1 GLN A  57      14.924  -2.366 -15.260  1.00 25.89           O  
ANISOU  441  OE1 GLN A  57     3114   3811   2914    500    825    301       O  
ATOM    442  NE2 GLN A  57      14.229  -4.497 -15.355  1.00 25.95           N  
ANISOU  442  NE2 GLN A  57     3247   3763   2849    618    793    221       N  
ATOM    443  N   PHE A  58       9.969  -3.255 -18.251  1.00 21.68           N  
ANISOU  443  N   PHE A  58     3081   3060   2096    548    639    141       N  
ATOM    444  CA  PHE A  58       9.199  -4.492 -18.425  1.00 21.61           C  
ANISOU  444  CA  PHE A  58     3159   3007   2043    584    589     73       C  
ATOM    445  C   PHE A  58       8.456  -4.585 -19.751  1.00 22.32           C  
ANISOU  445  C   PHE A  58     3371   3079   2031    613    569     47       C  
ATOM    446  O   PHE A  58       7.850  -3.613 -20.206  1.00 22.07           O  
ANISOU  446  O   PHE A  58     3359   3048   1978    582    540     67       O  
ATOM    447  CB  PHE A  58       8.156  -4.653 -17.308  1.00 20.67           C  
ANISOU  447  CB  PHE A  58     3017   2849   1988    524    495     36       C  
ATOM    448  CG  PHE A  58       8.728  -4.695 -15.917  1.00 19.60           C  
ANISOU  448  CG  PHE A  58     2780   2727   1941    499    498     51       C  
ATOM    449  CD1 PHE A  58      10.059  -5.034 -15.681  1.00 18.60           C  
ANISOU  449  CD1 PHE A  58     2595   2641   1833    542    569     80       C  
ATOM    450  CD2 PHE A  58       7.908  -4.415 -14.828  1.00 18.23           C  
ANISOU  450  CD2 PHE A  58     2567   2531   1829    437    428     37       C  
ATOM    451  CE1 PHE A  58      10.559  -5.075 -14.384  1.00 18.72           C  
ANISOU  451  CE1 PHE A  58     2517   2673   1924    521    559     93       C  
ATOM    452  CE2 PHE A  58       8.404  -4.458 -13.533  1.00 17.50           C  
ANISOU  452  CE2 PHE A  58     2391   2452   1806    417    426     49       C  
ATOM    453  CZ  PHE A  58       9.729  -4.790 -13.311  1.00 17.41           C  
ANISOU  453  CZ  PHE A  58     2324   2480   1809    458    486     76       C  
ATOM    454  N   LYS A  59       8.488  -5.779 -20.339  1.00 23.10           N  
ANISOU  454  N   LYS A  59     3557   3156   2064    676    580     -1       N  
ATOM    455  CA  LYS A  59       7.706  -6.102 -21.529  1.00 23.96           C  
ANISOU  455  CA  LYS A  59     3793   3241   2069    705    543    -45       C  
ATOM    456  C   LYS A  59       6.243  -6.349 -21.159  1.00 23.58           C  
ANISOU  456  C   LYS A  59     3771   3147   2042    646    422   -101       C  
ATOM    457  O   LYS A  59       5.337  -5.883 -21.851  1.00 23.51           O  
ANISOU  457  O   LYS A  59     3814   3135   1982    630    363   -114       O  
ATOM    458  CB  LYS A  59       8.282  -7.341 -22.232  1.00 25.01           C  
ANISOU  458  CB  LYS A  59     4018   3360   2125    793    595    -85       C  
ATOM    459  CG  LYS A  59       9.729  -7.177 -22.713  1.00 26.29           C  
ANISOU  459  CG  LYS A  59     4153   3577   2257    865    725    -29       C  
ATOM    460  CD  LYS A  59      10.176  -8.352 -23.590  1.00 28.26           C  
ANISOU  460  CD  LYS A  59     4517   3812   2410    967    778    -74       C  
ATOM    461  CE  LYS A  59      11.477  -8.052 -24.344  1.00 29.51           C  
ANISOU  461  CE  LYS A  59     4660   4035   2516   1044    914    -15       C  
ATOM    462  NZ  LYS A  59      11.791  -9.092 -25.373  1.00 30.95           N  
ANISOU  462  NZ  LYS A  59     4975   4202   2582   1154    967    -62       N  
ATOM    463  N   THR A  60       6.017  -7.085 -20.069  1.00 23.04           N  
ANISOU  463  N   THR A  60     3663   3044   2047    615    388   -132       N  
ATOM    464  CA  THR A  60       4.660  -7.346 -19.578  1.00 23.01           C  
ANISOU  464  CA  THR A  60     3664   3001   2078    551    284   -179       C  
ATOM    465  C   THR A  60       4.556  -7.112 -18.077  1.00 22.05           C  
ANISOU  465  C   THR A  60     3434   2877   2067    494    268   -159       C  
ATOM    466  O   THR A  60       5.571  -7.020 -17.383  1.00 21.44           O  
ANISOU  466  O   THR A  60     3290   2821   2036    509    328   -120       O  
ATOM    467  CB  THR A  60       4.204  -8.798 -19.871  1.00 23.66           C  
ANISOU  467  CB  THR A  60     3844   3023   2122    566    247   -255       C  
ATOM    468  OG1 THR A  60       4.909  -9.716 -19.021  1.00 24.10           O  
ANISOU  468  OG1 THR A  60     3881   3051   2226    587    291   -258       O  
ATOM    469  CG2 THR A  60       4.447  -9.159 -21.328  1.00 24.85           C  
ANISOU  469  CG2 THR A  60     4117   3174   2153    634    270   -283       C  
ATOM    470  N   LYS A  61       3.320  -7.037 -17.586  1.00 21.66           N  
ANISOU  470  N   LYS A  61     3367   2807   2057    431    185   -186       N  
ATOM    471  CA  LYS A  61       3.058  -6.926 -16.150  1.00 21.21           C  
ANISOU  471  CA  LYS A  61     3221   2744   2094    378    166   -174       C  
ATOM    472  C   LYS A  61       3.552  -8.150 -15.363  1.00 20.89           C  
ANISOU  472  C   LYS A  61     3185   2667   2084    392    192   -190       C  
ATOM    473  O   LYS A  61       3.717  -8.084 -14.148  1.00 20.06           O  
ANISOU  473  O   LYS A  61     3009   2565   2046    368    198   -169       O  
ATOM    474  CB  LYS A  61       1.561  -6.706 -15.878  1.00 21.22           C  
ANISOU  474  CB  LYS A  61     3205   2733   2123    315     78   -201       C  
ATOM    475  CG  LYS A  61       0.670  -7.905 -16.199  1.00 23.15           C  
ANISOU  475  CG  LYS A  61     3518   2931   2348    294     21   -266       C  
ATOM    476  CD  LYS A  61      -0.715  -7.753 -15.577  1.00 24.78           C  
ANISOU  476  CD  LYS A  61     3672   3134   2610    222    -54   -285       C  
ATOM    477  CE  LYS A  61      -1.482  -9.073 -15.600  1.00 26.30           C  
ANISOU  477  CE  LYS A  61     3916   3273   2806    182   -101   -345       C  
ATOM    478  NZ  LYS A  61      -2.951  -8.887 -15.393  1.00 26.82           N  
ANISOU  478  NZ  LYS A  61     3932   3348   2910    112   -181   -368       N  
ATOM    479  N   ASN A  62       3.786  -9.262 -16.053  1.00 21.31           N  
ANISOU  479  N   ASN A  62     3330   2684   2083    437    207   -228       N  
ATOM    480  CA  ASN A  62       4.257 -10.480 -15.394  1.00 21.45           C  
ANISOU  480  CA  ASN A  62     3371   2656   2124    462    233   -243       C  
ATOM    481  C   ASN A  62       5.602 -10.290 -14.697  1.00 20.41           C  
ANISOU  481  C   ASN A  62     3166   2563   2025    509    305   -190       C  
ATOM    482  O   ASN A  62       5.901 -10.985 -13.726  1.00 20.41           O  
ANISOU  482  O   ASN A  62     3148   2538   2067    518    316   -184       O  
ATOM    483  CB  ASN A  62       4.327 -11.641 -16.394  1.00 22.67           C  
ANISOU  483  CB  ASN A  62     3652   2757   2204    512    241   -296       C  
ATOM    484  CG  ASN A  62       2.957 -12.032 -16.930  1.00 24.44           C  
ANISOU  484  CG  ASN A  62     3946   2935   2404    453    154   -359       C  
ATOM    485  OD1 ASN A  62       2.761 -12.154 -18.141  1.00 27.97           O  
ANISOU  485  OD1 ASN A  62     4479   3377   2770    478    137   -396       O  
ATOM    486  ND2 ASN A  62       1.998 -12.219 -16.026  1.00 26.10           N  
ANISOU  486  ND2 ASN A  62     4116   3119   2683    374     99   -370       N  
ATOM    487  N   GLU A  63       6.391  -9.326 -15.170  1.00 19.54           N  
ANISOU  487  N   GLU A  63     3012   2515   1898    536    353   -147       N  
ATOM    488  CA  GLU A  63       7.700  -9.038 -14.581  1.00 18.70           C  
ANISOU  488  CA  GLU A  63     2820   2457   1827    572    417    -96       C  
ATOM    489  C   GLU A  63       7.639  -8.304 -13.219  1.00 17.50           C  
ANISOU  489  C   GLU A  63     2562   2331   1758    513    390    -64       C  
ATOM    490  O   GLU A  63       8.656  -8.195 -12.535  1.00 17.13           O  
ANISOU  490  O   GLU A  63     2440   2322   1746    535    426    -29       O  
ATOM    491  CB  GLU A  63       8.562  -8.269 -15.586  1.00 19.01           C  
ANISOU  491  CB  GLU A  63     2847   2554   1823    611    482    -59       C  
ATOM    492  CG  GLU A  63       8.880  -9.074 -16.855  1.00 19.64           C  
ANISOU  492  CG  GLU A  63     3032   2618   1813    691    527    -87       C  
ATOM    493  CD  GLU A  63       9.514  -8.237 -17.955  1.00 19.35           C  
ANISOU  493  CD  GLU A  63     2996   2636   1722    722    592    -49       C  
ATOM    494  OE1 GLU A  63      10.603  -7.671 -17.733  1.00 17.27           O  
ANISOU  494  OE1 GLU A  63     2641   2432   1491    737    658      7       O  
ATOM    495  OE2 GLU A  63       8.923  -8.164 -19.055  1.00 20.02           O  
ANISOU  495  OE2 GLU A  63     3173   2706   1729    730    576    -74       O  
ATOM    496  N   GLU A  64       6.461  -7.816 -12.825  1.00 16.34           N  
ANISOU  496  N   GLU A  64     2407   2165   1637    442    325    -79       N  
ATOM    497  CA  GLU A  64       6.300  -7.155 -11.521  1.00 15.44           C  
ANISOU  497  CA  GLU A  64     2208   2069   1591    390    299    -57       C  
ATOM    498  C   GLU A  64       6.539  -8.151 -10.377  1.00 15.47           C  
ANISOU  498  C   GLU A  64     2201   2050   1628    404    299    -60       C  
ATOM    499  O   GLU A  64       7.241  -7.846  -9.404  1.00 15.00           O  
ANISOU  499  O   GLU A  64     2068   2024   1606    406    310    -30       O  
ATOM    500  CB  GLU A  64       4.910  -6.511 -11.399  1.00 14.68           C  
ANISOU  500  CB  GLU A  64     2112   1957   1510    324    236    -75       C  
ATOM    501  CG  GLU A  64       4.667  -5.354 -12.373  1.00 14.34           C  
ANISOU  501  CG  GLU A  64     2073   1937   1438    314    231    -62       C  
ATOM    502  CD  GLU A  64       3.207  -4.879 -12.414  1.00 13.93           C  
ANISOU  502  CD  GLU A  64     2029   1870   1393    266    164    -84       C  
ATOM    503  OE1 GLU A  64       2.384  -5.331 -11.589  1.00 12.14           O  
ANISOU  503  OE1 GLU A  64     1788   1621   1202    232    126   -106       O  
ATOM    504  OE2 GLU A  64       2.885  -4.047 -13.286  1.00 14.52           O  
ANISOU  504  OE2 GLU A  64     2123   1957   1436    267    152    -75       O  
ATOM    505  N   LYS A  65       5.959  -9.341 -10.512  1.00 15.86           N  
ANISOU  505  N   LYS A  65     2328   2039   1658    414    283    -97       N  
ATOM    506  CA  LYS A  65       6.172 -10.432  -9.561  1.00 16.14           C  
ANISOU  506  CA  LYS A  65     2379   2039   1716    436    289    -97       C  
ATOM    507  C   LYS A  65       7.646 -10.836  -9.498  1.00 16.46           C  
ANISOU  507  C   LYS A  65     2399   2109   1747    521    346    -68       C  
ATOM    508  O   LYS A  65       8.236 -10.879  -8.418  1.00 16.51           O  
ANISOU  508  O   LYS A  65     2346   2139   1786    536    351    -38       O  
ATOM    509  CB  LYS A  65       5.312 -11.642  -9.950  1.00 16.85           C  
ANISOU  509  CB  LYS A  65     2572   2047   1782    427    267   -143       C  
ATOM    510  CG  LYS A  65       5.459 -12.854  -9.033  1.00 18.09           C  
ANISOU  510  CG  LYS A  65     2765   2148   1958    450    276   -140       C  
ATOM    511  CD  LYS A  65       4.463 -13.949  -9.390  1.00 19.42           C  
ANISOU  511  CD  LYS A  65     3038   2227   2116    417    249   -188       C  
ATOM    512  CE  LYS A  65       4.586 -15.126  -8.440  1.00 20.55           C  
ANISOU  512  CE  LYS A  65     3226   2303   2279    435    264   -177       C  
ATOM    513  NZ  LYS A  65       3.562 -16.172  -8.691  1.00 21.17           N  
ANISOU  513  NZ  LYS A  65     3404   2284   2357    384    236   -222       N  
ATOM    514  N   SER A  66       8.231 -11.117 -10.661  1.00 16.40           N  
ANISOU  514  N   SER A  66     2436   2104   1690    581    389    -76       N  
ATOM    515  CA  SER A  66       9.626 -11.551 -10.764  1.00 16.75           C  
ANISOU  515  CA  SER A  66     2460   2182   1723    675    452    -50       C  
ATOM    516  C   SER A  66      10.602 -10.535 -10.186  1.00 16.13           C  
ANISOU  516  C   SER A  66     2251   2192   1684    671    471      1       C  
ATOM    517  O   SER A  66      11.648 -10.909  -9.663  1.00 16.05           O  
ANISOU  517  O   SER A  66     2191   2217   1691    733    501     29       O  
ATOM    518  CB  SER A  66       9.997 -11.812 -12.227  1.00 17.49           C  
ANISOU  518  CB  SER A  66     2622   2273   1749    736    501    -68       C  
ATOM    519  OG  SER A  66       8.977 -12.526 -12.893  1.00 18.75           O  
ANISOU  519  OG  SER A  66     2902   2354   1866    720    469   -124       O  
ATOM    520  N   TYR A  67      10.263  -9.251 -10.291  1.00 15.18           N  
ANISOU  520  N   TYR A  67     2080   2107   1581    600    451     13       N  
ATOM    521  CA  TYR A  67      11.090  -8.195  -9.718  1.00 14.94           C  
ANISOU  521  CA  TYR A  67     1932   2150   1595    576    460     55       C  
ATOM    522  C   TYR A  67      10.910  -8.096  -8.201  1.00 14.21           C  
ANISOU  522  C   TYR A  67     1787   2061   1552    538    410     62       C  
ATOM    523  O   TYR A  67      11.890  -8.065  -7.462  1.00 14.44           O  
ANISOU  523  O   TYR A  67     1738   2140   1609    564    418     90       O  
ATOM    524  CB  TYR A  67      10.769  -6.845 -10.367  1.00 14.69           C  
ANISOU  524  CB  TYR A  67     1880   2140   1562    513    458     66       C  
ATOM    525  CG  TYR A  67      11.605  -5.702  -9.835  1.00 15.00           C  
ANISOU  525  CG  TYR A  67     1807   2243   1650    475    467    106       C  
ATOM    526  CD1 TYR A  67      12.917  -5.515 -10.260  1.00 16.13           C  
ANISOU  526  CD1 TYR A  67     1883   2449   1797    512    530    143       C  
ATOM    527  CD2 TYR A  67      11.086  -4.812  -8.899  1.00 14.87           C  
ANISOU  527  CD2 TYR A  67     1751   2224   1677    400    413    105       C  
ATOM    528  CE1 TYR A  67      13.686  -4.469  -9.771  1.00 16.81           C  
ANISOU  528  CE1 TYR A  67     1862   2592   1935    462    533    178       C  
ATOM    529  CE2 TYR A  67      11.848  -3.766  -8.404  1.00 15.37           C  
ANISOU  529  CE2 TYR A  67     1720   2336   1784    357    415    135       C  
ATOM    530  CZ  TYR A  67      13.144  -3.605  -8.834  1.00 16.39           C  
ANISOU  530  CZ  TYR A  67     1781   2525   1922    383    471    171       C  
ATOM    531  OH  TYR A  67      13.889  -2.563  -8.344  1.00 18.40           O  
ANISOU  531  OH  TYR A  67     1938   2826   2226    326    468    198       O  
ATOM    532  N   LYS A  68       9.660  -8.041  -7.748  1.00 13.45           N  
ANISOU  532  N   LYS A  68     1732   1916   1464    480    359     36       N  
ATOM    533  CA  LYS A  68       9.364  -7.762  -6.337  1.00 12.99           C  
ANISOU  533  CA  LYS A  68     1630   1863   1443    439    315     42       C  
ATOM    534  C   LYS A  68       9.705  -8.919  -5.393  1.00 13.27           C  
ANISOU  534  C   LYS A  68     1679   1883   1481    490    314     49       C  
ATOM    535  O   LYS A  68      10.393  -8.717  -4.397  1.00 13.74           O  
ANISOU  535  O   LYS A  68     1672   1986   1562    500    301     73       O  
ATOM    536  CB  LYS A  68       7.901  -7.340  -6.161  1.00 12.04           C  
ANISOU  536  CB  LYS A  68     1543   1703   1330    368    271     16       C  
ATOM    537  CG  LYS A  68       7.612  -5.929  -6.667  1.00 11.67           C  
ANISOU  537  CG  LYS A  68     1465   1679   1291    317    262     19       C  
ATOM    538  CD  LYS A  68       6.177  -5.499  -6.413  1.00  9.47           C  
ANISOU  538  CD  LYS A  68     1209   1368   1022    260    218     -4       C  
ATOM    539  CE  LYS A  68       5.184  -6.377  -7.169  1.00  9.60           C  
ANISOU  539  CE  LYS A  68     1302   1334   1010    262    207    -36       C  
ATOM    540  NZ  LYS A  68       3.799  -5.870  -7.100  1.00  7.72           N  
ANISOU  540  NZ  LYS A  68     1070   1080    785    209    165    -55       N  
ATOM    541  N   ILE A  69       9.242 -10.122  -5.719  1.00 13.71           N  
ANISOU  541  N   ILE A  69     1825   1872   1511    523    323     29       N  
ATOM    542  CA  ILE A  69       9.328 -11.276  -4.802  1.00 14.11           C  
ANISOU  542  CA  ILE A  69     1913   1885   1562    566    320     37       C  
ATOM    543  C   ILE A  69      10.738 -11.637  -4.273  1.00 14.69           C  
ANISOU  543  C   ILE A  69     1933   2010   1638    651    341     74       C  
ATOM    544  O   ILE A  69      10.900 -11.843  -3.068  1.00 14.68           O  
ANISOU  544  O   ILE A  69     1909   2019   1649    662    318     95       O  
ATOM    545  CB  ILE A  69       8.632 -12.526  -5.413  1.00 14.57           C  
ANISOU  545  CB  ILE A  69     2091   1851   1594    583    330      6       C  
ATOM    546  CG1 ILE A  69       7.109 -12.338  -5.403  1.00 14.20           C  
ANISOU  546  CG1 ILE A  69     2081   1757   1557    490    292    -24       C  
ATOM    547  CG2 ILE A  69       9.006 -13.812  -4.654  1.00 14.99           C  
ANISOU  547  CG2 ILE A  69     2195   1858   1642    649    343     23       C  
ATOM    548  CD1 ILE A  69       6.519 -12.074  -4.019  1.00 12.87           C  
ANISOU  548  CD1 ILE A  69     1878   1593   1419    439    262     -7       C  
ATOM    549  N   PRO A  70      11.750 -11.725  -5.156  1.00 14.95           N  
ANISOU  549  N   PRO A  70     1942   2079   1657    717    387     83       N  
ATOM    550  CA  PRO A  70      13.110 -11.999  -4.663  1.00 15.43           C  
ANISOU  550  CA  PRO A  70     1932   2205   1727    801    405    120       C  
ATOM    551  C   PRO A  70      13.649 -10.908  -3.719  1.00 15.58           C  
ANISOU  551  C   PRO A  70     1827   2310   1783    757    368    145       C  
ATOM    552  O   PRO A  70      14.342 -11.214  -2.744  1.00 15.53           O  
ANISOU  552  O   PRO A  70     1773   2342   1785    804    348    171       O  
ATOM    553  CB  PRO A  70      13.950 -12.062  -5.952  1.00 16.22           C  
ANISOU  553  CB  PRO A  70     2020   2336   1807    865    469    123       C  
ATOM    554  CG  PRO A  70      12.963 -12.351  -7.047  1.00 15.89           C  
ANISOU  554  CG  PRO A  70     2092   2216   1729    840    482     81       C  
ATOM    555  CD  PRO A  70      11.699 -11.667  -6.630  1.00 15.09           C  
ANISOU  555  CD  PRO A  70     2003   2084   1645    728    426     61       C  
ATOM    556  N   ARG A  71      13.320  -9.651  -4.012  1.00 15.27           N  
ANISOU  556  N   ARG A  71     1744   2296   1761    670    355    136       N  
ATOM    557  CA  ARG A  71      13.762  -8.515  -3.203  1.00 15.42           C  
ANISOU  557  CA  ARG A  71     1659   2385   1816    614    317    151       C  
ATOM    558  C   ARG A  71      13.029  -8.462  -1.868  1.00 14.93           C  
ANISOU  558  C   ARG A  71     1616   2299   1757    574    259    143       C  
ATOM    559  O   ARG A  71      13.643  -8.211  -0.829  1.00 15.46           O  
ANISOU  559  O   ARG A  71     1618   2420   1837    578    223    158       O  
ATOM    560  CB  ARG A  71      13.584  -7.200  -3.976  1.00 15.21           C  
ANISOU  560  CB  ARG A  71     1598   2375   1806    535    327    145       C  
ATOM    561  CG  ARG A  71      14.566  -7.080  -5.125  1.00 16.76           C  
ANISOU  561  CG  ARG A  71     1750   2618   2000    573    390    166       C  
ATOM    562  CD  ARG A  71      14.306  -5.878  -6.024  1.00 18.05           C  
ANISOU  562  CD  ARG A  71     1905   2784   2170    501    408    167       C  
ATOM    563  NE  ARG A  71      15.438  -5.665  -6.929  1.00 20.09           N  
ANISOU  563  NE  ARG A  71     2100   3103   2432    533    475    198       N  
ATOM    564  CZ  ARG A  71      15.707  -6.401  -8.009  1.00 21.89           C  
ANISOU  564  CZ  ARG A  71     2373   3325   2620    608    539    202       C  
ATOM    565  NH1 ARG A  71      14.921  -7.415  -8.365  1.00 22.20           N  
ANISOU  565  NH1 ARG A  71     2529   3294   2613    654    540    170       N  
ATOM    566  NH2 ARG A  71      16.776  -6.116  -8.750  1.00 23.59           N  
ANISOU  566  NH2 ARG A  71     2518   3606   2840    635    607    236       N  
ATOM    567  N   VAL A  72      11.720  -8.698  -1.891  1.00 14.41           N  
ANISOU  567  N   VAL A  72     1639   2159   1678    536    250    118       N  
ATOM    568  CA  VAL A  72      10.957  -8.834  -0.650  1.00 13.92           C  
ANISOU  568  CA  VAL A  72     1606   2070   1612    508    210    114       C  
ATOM    569  C   VAL A  72      11.532  -9.961   0.226  1.00 14.61           C  
ANISOU  569  C   VAL A  72     1711   2158   1682    588    206    140       C  
ATOM    570  O   VAL A  72      11.706  -9.801   1.439  1.00 14.41           O  
ANISOU  570  O   VAL A  72     1659   2164   1653    588    168    153       O  
ATOM    571  CB  VAL A  72       9.456  -9.098  -0.925  1.00 13.80           C  
ANISOU  571  CB  VAL A  72     1678   1976   1589    460    211     87       C  
ATOM    572  CG1 VAL A  72       8.736  -9.494   0.356  1.00 13.71           C  
ANISOU  572  CG1 VAL A  72     1702   1937   1571    445    187     91       C  
ATOM    573  CG2 VAL A  72       8.799  -7.867  -1.535  1.00 12.42           C  
ANISOU  573  CG2 VAL A  72     1482   1806   1429    386    202     65       C  
ATOM    574  N   ASN A  73      11.858 -11.088  -0.397  1.00 14.72           N  
ANISOU  574  N   ASN A  73     1776   2137   1680    663    244    147       N  
ATOM    575  CA  ASN A  73      12.285 -12.267   0.343  1.00 15.26           C  
ANISOU  575  CA  ASN A  73     1883   2186   1728    748    246    174       C  
ATOM    576  C   ASN A  73      13.770 -12.322   0.713  1.00 16.34           C  
ANISOU  576  C   ASN A  73     1931   2410   1869    832    239    208       C  
ATOM    577  O   ASN A  73      14.183 -13.213   1.467  1.00 17.17           O  
ANISOU  577  O   ASN A  73     2061   2510   1955    911    231    236       O  
ATOM    578  CB  ASN A  73      11.877 -13.525  -0.429  1.00 15.37           C  
ANISOU  578  CB  ASN A  73     2010   2106   1723    793    288    164       C  
ATOM    579  CG  ASN A  73      10.372 -13.726  -0.446  1.00 14.42           C  
ANISOU  579  CG  ASN A  73     1977   1898   1602    712    282    137       C  
ATOM    580  OD1 ASN A  73       9.670 -13.325   0.491  1.00 12.36           O  
ANISOU  580  OD1 ASN A  73     1710   1639   1347    653    252    140       O  
ATOM    581  ND2 ASN A  73       9.868 -14.345  -1.510  1.00 12.11           N  
ANISOU  581  ND2 ASN A  73     1767   1535   1301    711    309    108       N  
ATOM    582  N   SER A  74      14.569 -11.383   0.207  1.00 16.50           N  
ANISOU  582  N   SER A  74     1846   2511   1914    815    242    208       N  
ATOM    583  CA  SER A  74      16.001 -11.336   0.527  1.00 17.64           C  
ANISOU  583  CA  SER A  74     1879   2752   2069    883    233    239       C  
ATOM    584  C   SER A  74      16.348 -10.296   1.602  1.00 17.91           C  
ANISOU  584  C   SER A  74     1818   2866   2122    825    166    243       C  
ATOM    585  O   SER A  74      17.481 -10.256   2.084  1.00 18.91           O  
ANISOU  585  O   SER A  74     1847   3079   2259    873    139    267       O  
ATOM    586  CB  SER A  74      16.812 -11.048  -0.734  1.00 17.96           C  
ANISOU  586  CB  SER A  74     1855   2840   2129    906    288    243       C  
ATOM    587  OG  SER A  74      16.493  -9.773  -1.256  1.00 17.72           O  
ANISOU  587  OG  SER A  74     1783   2826   2122    800    287    224       O  
ATOM    588  N   GLY A  75      15.381  -9.466   1.982  1.00 17.37           N  
ANISOU  588  N   GLY A  75     1777   2768   2057    724    135    216       N  
ATOM    589  CA  GLY A  75      15.637  -8.352   2.891  1.00 17.58           C  
ANISOU  589  CA  GLY A  75     1726   2858   2098    659     72    209       C  
ATOM    590  C   GLY A  75      15.433  -8.615   4.375  1.00 17.79           C  
ANISOU  590  C   GLY A  75     1781   2889   2090    675     15    214       C  
ATOM    591  O   GLY A  75      15.699  -7.737   5.190  1.00 18.44           O  
ANISOU  591  O   GLY A  75     1807   3025   2176    628    -44    203       O  
ATOM    592  N   GLY A  76      14.963  -9.807   4.739  1.00 17.97           N  
ANISOU  592  N   GLY A  76     1899   2853   2077    740     31    232       N  
ATOM    593  CA  GLY A  76      14.716 -10.141   6.146  1.00 17.92           C  
ANISOU  593  CA  GLY A  76     1936   2846   2028    763    -15    245       C  
ATOM    594  C   GLY A  76      13.777  -9.157   6.823  1.00 17.24           C  
ANISOU  594  C   GLY A  76     1871   2747   1933    667    -46    214       C  
ATOM    595  O   GLY A  76      14.135  -8.527   7.820  1.00 17.82           O  
ANISOU  595  O   GLY A  76     1903   2879   1989    651   -106    208       O  
ATOM    596  N   TYR A  77      12.573  -9.019   6.281  1.00 16.09           N  
ANISOU  596  N   TYR A  77     1791   2527   1797    607     -7    192       N  
ATOM    597  CA  TYR A  77      11.614  -8.038   6.780  1.00 15.23           C  
ANISOU  597  CA  TYR A  77     1698   2403   1684    522    -26    161       C  
ATOM    598  C   TYR A  77      10.670  -8.650   7.806  1.00 14.87           C  
ANISOU  598  C   TYR A  77     1743   2313   1595    532    -21    173       C  
ATOM    599  O   TYR A  77      10.329  -9.826   7.727  1.00 15.01           O  
ANISOU  599  O   TYR A  77     1830   2275   1598    576     16    199       O  
ATOM    600  CB  TYR A  77      10.792  -7.452   5.631  1.00 14.69           C  
ANISOU  600  CB  TYR A  77     1640   2290   1652    454     11    132       C  
ATOM    601  CG  TYR A  77      11.608  -6.736   4.588  1.00 14.79           C  
ANISOU  601  CG  TYR A  77     1574   2341   1705    434     16    125       C  
ATOM    602  CD1 TYR A  77      12.173  -5.495   4.851  1.00 15.40           C  
ANISOU  602  CD1 TYR A  77     1577   2473   1801    383    -24    108       C  
ATOM    603  CD2 TYR A  77      11.802  -7.292   3.328  1.00 15.54           C  
ANISOU  603  CD2 TYR A  77     1676   2414   1815    463     65    133       C  
ATOM    604  CE1 TYR A  77      12.921  -4.830   3.894  1.00 15.24           C  
ANISOU  604  CE1 TYR A  77     1484   2486   1821    357    -11    108       C  
ATOM    605  CE2 TYR A  77      12.542  -6.631   2.357  1.00 15.40           C  
ANISOU  605  CE2 TYR A  77     1589   2434   1829    446     80    132       C  
ATOM    606  CZ  TYR A  77      13.106  -5.401   2.651  1.00 15.33           C  
ANISOU  606  CZ  TYR A  77     1500   2481   1844    391     45    123       C  
ATOM    607  OH  TYR A  77      13.848  -4.743   1.700  1.00 16.03           O  
ANISOU  607  OH  TYR A  77     1520   2605   1967    367     67    129       O  
ATOM    608  N   ASP A  78      10.246  -7.838   8.763  1.00 14.40           N  
ANISOU  608  N   ASP A  78     1687   2274   1512    491    -54    154       N  
ATOM    609  CA  ASP A  78       9.208  -8.238   9.705  1.00 14.17           C  
ANISOU  609  CA  ASP A  78     1740   2205   1440    489    -37    164       C  
ATOM    610  C   ASP A  78       7.827  -8.034   9.097  1.00 13.36           C  
ANISOU  610  C   ASP A  78     1672   2039   1364    425     11    143       C  
ATOM    611  O   ASP A  78       6.872  -8.692   9.504  1.00 13.62           O  
ANISOU  611  O   ASP A  78     1772   2024   1378    422     47    160       O  
ATOM    612  CB  ASP A  78       9.334  -7.444  11.005  1.00 14.51           C  
ANISOU  612  CB  ASP A  78     1776   2301   1437    481    -90    149       C  
ATOM    613  CG  ASP A  78      10.705  -7.579  11.629  1.00 15.09           C  
ANISOU  613  CG  ASP A  78     1803   2448   1481    541   -152    165       C  
ATOM    614  OD1 ASP A  78      11.181  -8.719  11.783  1.00 14.90           O  
ANISOU  614  OD1 ASP A  78     1804   2423   1436    619   -145    209       O  
ATOM    615  OD2 ASP A  78      11.312  -6.544  11.951  1.00 16.23           O  
ANISOU  615  OD2 ASP A  78     1887   2652   1627    510   -211    133       O  
ATOM    616  N   LEU A  79       7.729  -7.144   8.107  1.00 12.51           N  
ANISOU  616  N   LEU A  79     1519   1933   1302    373     11    110       N  
ATOM    617  CA  LEU A  79       6.442  -6.768   7.524  1.00 11.49           C  
ANISOU  617  CA  LEU A  79     1410   1757   1198    315     44     88       C  
ATOM    618  C   LEU A  79       6.576  -6.208   6.099  1.00 10.88           C  
ANISOU  618  C   LEU A  79     1292   1673   1167    284     50     67       C  
ATOM    619  O   LEU A  79       7.444  -5.379   5.820  1.00 10.80           O  
ANISOU  619  O   LEU A  79     1226   1705   1174    275     24     56       O  
ATOM    620  CB  LEU A  79       5.746  -5.738   8.427  1.00 11.34           C  
ANISOU  620  CB  LEU A  79     1394   1753   1160    278     29     63       C  
ATOM    621  CG  LEU A  79       4.341  -5.277   8.021  1.00 10.92           C  
ANISOU  621  CG  LEU A  79     1356   1663   1132    229     60     42       C  
ATOM    622  CD1 LEU A  79       3.366  -6.439   7.980  1.00  9.72           C  
ANISOU  622  CD1 LEU A  79     1252   1463    979    228    108     66       C  
ATOM    623  CD2 LEU A  79       3.830  -4.190   8.973  1.00 10.98           C  
ANISOU  623  CD2 LEU A  79     1366   1691   1115    209     47     15       C  
ATOM    624  N   LEU A  80       5.694  -6.662   5.212  1.00 10.21           N  
ANISOU  624  N   LEU A  80     1239   1537   1102    265     85     63       N  
ATOM    625  CA  LEU A  80       5.560  -6.110   3.866  1.00  9.54           C  
ANISOU  625  CA  LEU A  80     1132   1442   1050    235     92     43       C  
ATOM    626  C   LEU A  80       4.225  -5.386   3.725  1.00  8.72           C  
ANISOU  626  C   LEU A  80     1036   1316    960    183     96     19       C  
ATOM    627  O   LEU A  80       3.188  -5.904   4.137  1.00  8.53           O  
ANISOU  627  O   LEU A  80     1045   1264    931    170    114     22       O  
ATOM    628  CB  LEU A  80       5.647  -7.226   2.822  1.00  9.75           C  
ANISOU  628  CB  LEU A  80     1192   1430   1081    262    121     52       C  
ATOM    629  CG  LEU A  80       5.254  -6.891   1.376  1.00  9.97           C  
ANISOU  629  CG  LEU A  80     1221   1438   1130    235    132     32       C  
ATOM    630  CD1 LEU A  80       6.138  -5.787   0.802  1.00 10.58           C  
ANISOU  630  CD1 LEU A  80     1240   1560   1219    229    122     29       C  
ATOM    631  CD2 LEU A  80       5.314  -8.148   0.512  1.00 10.92           C  
ANISOU  631  CD2 LEU A  80     1393   1514   1243    267    157     35       C  
ATOM    632  N   ILE A  81       4.269  -4.186   3.152  1.00  7.72           N  
ANISOU  632  N   ILE A  81      876   1204    853    155     82      0       N  
ATOM    633  CA  ILE A  81       3.074  -3.428   2.810  1.00  7.38           C  
ANISOU  633  CA  ILE A  81      837   1143    826    118     84    -21       C  
ATOM    634  C   ILE A  81       3.153  -3.118   1.324  1.00  6.97           C  
ANISOU  634  C   ILE A  81      777   1080    791    109     87    -26       C  
ATOM    635  O   ILE A  81       4.166  -2.584   0.866  1.00  6.91           O  
ANISOU  635  O   ILE A  81      744   1092    790    112     82    -20       O  
ATOM    636  CB  ILE A  81       3.003  -2.083   3.577  1.00  7.08           C  
ANISOU  636  CB  ILE A  81      780   1124    787    100     63    -39       C  
ATOM    637  CG1 ILE A  81       2.881  -2.313   5.083  1.00  6.87           C  
ANISOU  637  CG1 ILE A  81      769   1112    728    114     59    -37       C  
ATOM    638  CG2 ILE A  81       1.830  -1.236   3.077  1.00  7.86           C  
ANISOU  638  CG2 ILE A  81      881   1203    904     76     66    -57       C  
ATOM    639  CD1 ILE A  81       3.260  -1.100   5.905  1.00  7.26           C  
ANISOU  639  CD1 ILE A  81      809   1184    767    104     29    -59       C  
ATOM    640  N   GLU A  82       2.118  -3.470   0.566  1.00  6.53           N  
ANISOU  640  N   GLU A  82      743    996    743     96     95    -35       N  
ATOM    641  CA  GLU A  82       2.028  -3.019  -0.825  1.00  6.59           C  
ANISOU  641  CA  GLU A  82      752    996    757     89     93    -41       C  
ATOM    642  C   GLU A  82       0.900  -2.011  -0.970  1.00  6.39           C  
ANISOU  642  C   GLU A  82      717    966    744     66     78    -56       C  
ATOM    643  O   GLU A  82      -0.223  -2.255  -0.543  1.00  5.96           O  
ANISOU  643  O   GLU A  82      663    905    697     54     77    -65       O  
ATOM    644  CB  GLU A  82       1.832  -4.164  -1.814  1.00  6.71           C  
ANISOU  644  CB  GLU A  82      803    984    762     99    103    -44       C  
ATOM    645  CG  GLU A  82       1.902  -3.686  -3.275  1.00  6.75           C  
ANISOU  645  CG  GLU A  82      817    988    759    101    100    -49       C  
ATOM    646  CD  GLU A  82       2.145  -4.809  -4.254  1.00  8.36           C  
ANISOU  646  CD  GLU A  82     1066   1171    941    124    112    -55       C  
ATOM    647  OE1 GLU A  82       1.151  -5.319  -4.809  1.00  9.50           O  
ANISOU  647  OE1 GLU A  82     1241   1289   1081    107     97    -76       O  
ATOM    648  OE2 GLU A  82       3.323  -5.194  -4.457  1.00  8.72           O  
ANISOU  648  OE2 GLU A  82     1114   1225    973    159    137    -40       O  
ATOM    649  N   LEU A  83       1.227  -0.887  -1.598  1.00  6.50           N  
ANISOU  649  N   LEU A  83      723    985    763     63     70    -55       N  
ATOM    650  CA  LEU A  83       0.327   0.239  -1.720  1.00  6.19           C  
ANISOU  650  CA  LEU A  83      679    938    734     54     56    -65       C  
ATOM    651  C   LEU A  83      -0.419   0.170  -3.035  1.00  6.62           C  
ANISOU  651  C   LEU A  83      749    983    783     58     46    -68       C  
ATOM    652  O   LEU A  83       0.194   0.088  -4.118  1.00  6.53           O  
ANISOU  652  O   LEU A  83      755    969    756     66     51    -58       O  
ATOM    653  CB  LEU A  83       1.114   1.553  -1.640  1.00  6.20           C  
ANISOU  653  CB  LEU A  83      674    939    743     46     52    -60       C  
ATOM    654  CG  LEU A  83       1.843   1.815  -0.320  1.00  5.95           C  
ANISOU  654  CG  LEU A  83      628    920    714     37     48    -65       C  
ATOM    655  CD1 LEU A  83       2.599   3.136  -0.380  1.00  6.28           C  
ANISOU  655  CD1 LEU A  83      666    953    769     15     40    -64       C  
ATOM    656  CD2 LEU A  83       0.853   1.810   0.831  1.00  6.23           C  
ANISOU  656  CD2 LEU A  83      667    956    745     43     45    -83       C  
ATOM    657  N   HIS A  84      -1.745   0.198  -2.922  1.00  6.71           N  
ANISOU  657  N   HIS A  84      750    994    805     54     32    -81       N  
ATOM    658  CA  HIS A  84      -2.651   0.283  -4.053  1.00  7.10           C  
ANISOU  658  CA  HIS A  84      806   1043    850     59      8    -87       C  
ATOM    659  C   HIS A  84      -3.703   1.362  -3.821  1.00  7.28           C  
ANISOU  659  C   HIS A  84      805   1071    888     71     -8    -92       C  
ATOM    660  O   HIS A  84      -3.855   1.891  -2.716  1.00  6.28           O  
ANISOU  660  O   HIS A  84      663    948    776     75      5    -96       O  
ATOM    661  CB  HIS A  84      -3.363  -1.057  -4.269  1.00  7.36           C  
ANISOU  661  CB  HIS A  84      838   1074    883     42     -1   -102       C  
ATOM    662  CG  HIS A  84      -2.481  -2.121  -4.842  1.00  8.13           C  
ANISOU  662  CG  HIS A  84      974   1157    959     42     11   -101       C  
ATOM    663  ND1 HIS A  84      -2.486  -2.451  -6.179  1.00  8.87           N  
ANISOU  663  ND1 HIS A  84     1102   1243   1026     50     -6   -110       N  
ATOM    664  CD2 HIS A  84      -1.560  -2.925  -4.260  1.00  9.07           C  
ANISOU  664  CD2 HIS A  84     1106   1265   1073     46     38    -93       C  
ATOM    665  CE1 HIS A  84      -1.611  -3.417  -6.396  1.00  9.67           C  
ANISOU  665  CE1 HIS A  84     1238   1327   1108     59     15   -109       C  
ATOM    666  NE2 HIS A  84      -1.030  -3.719  -5.249  1.00  9.54           N  
ANISOU  666  NE2 HIS A  84     1207   1310   1108     58     41    -97       N  
ATOM    667  N   LEU A  85      -4.404   1.692  -4.902  1.00  7.65           N  
ANISOU  667  N   LEU A  85      856   1122    928     86    -36    -93       N  
ATOM    668  CA  LEU A  85      -5.652   2.424  -4.839  1.00  8.19           C  
ANISOU  668  CA  LEU A  85      895   1205   1012    107    -58    -98       C  
ATOM    669  C   LEU A  85      -6.684   1.542  -5.526  1.00  9.03           C  
ANISOU  669  C   LEU A  85      977   1334   1121     95    -91   -113       C  
ATOM    670  O   LEU A  85      -6.347   0.750  -6.420  1.00  9.30           O  
ANISOU  670  O   LEU A  85     1040   1362   1130     81   -106   -118       O  
ATOM    671  CB  LEU A  85      -5.554   3.782  -5.543  1.00  8.25           C  
ANISOU  671  CB  LEU A  85      930   1196   1007    142    -70    -82       C  
ATOM    672  CG  LEU A  85      -4.700   4.888  -4.915  1.00  8.16           C  
ANISOU  672  CG  LEU A  85      945   1153   1002    147    -45    -71       C  
ATOM    673  CD1 LEU A  85      -4.855   6.193  -5.692  1.00  7.35           C  
ANISOU  673  CD1 LEU A  85      876   1024    890    182    -58    -52       C  
ATOM    674  CD2 LEU A  85      -5.030   5.119  -3.444  1.00  6.88           C  
ANISOU  674  CD2 LEU A  85      758    994    863    148    -27    -88       C  
ATOM    675  N   ASN A  86      -7.930   1.672  -5.092  1.00  9.52           N  
ANISOU  675  N   ASN A  86      983   1423   1209    100   -103   -121       N  
ATOM    676  CA  ASN A  86      -9.017   0.848  -5.578  1.00 10.50           C  
ANISOU  676  CA  ASN A  86     1066   1576   1347     76   -139   -137       C  
ATOM    677  C   ASN A  86      -9.676   1.502  -6.779  1.00 11.19           C  
ANISOU  677  C   ASN A  86     1149   1684   1418    112   -194   -137       C  
ATOM    678  O   ASN A  86      -9.359   2.640  -7.138  1.00 10.80           O  
ANISOU  678  O   ASN A  86     1131   1622   1349    159   -197   -119       O  
ATOM    679  CB  ASN A  86     -10.045   0.630  -4.456  1.00 10.82           C  
ANISOU  679  CB  ASN A  86     1034   1646   1430     61   -118   -142       C  
ATOM    680  CG  ASN A  86     -10.555  -0.801  -4.382  1.00 11.28           C  
ANISOU  680  CG  ASN A  86     1065   1711   1510     -2   -121   -155       C  
ATOM    681  OD1 ASN A  86     -10.759  -1.460  -5.405  1.00 11.06           O  
ANISOU  681  OD1 ASN A  86     1047   1681   1472    -29   -166   -171       O  
ATOM    682  ND2 ASN A  86     -10.776  -1.286  -3.157  1.00 11.53           N  
ANISOU  682  ND2 ASN A  86     1067   1745   1567    -29    -73   -149       N  
ATOM    683  N   ALA A  87     -10.585   0.762  -7.402  1.00 12.17           N  
ANISOU  683  N   ALA A  87     1238   1837   1549     87   -242   -156       N  
ATOM    684  CA  ALA A  87     -11.353   1.261  -8.524  1.00 13.24           C  
ANISOU  684  CA  ALA A  87     1361   2005   1666    122   -307   -158       C  
ATOM    685  C   ALA A  87     -12.611   0.422  -8.704  1.00 14.53           C  
ANISOU  685  C   ALA A  87     1448   2214   1860     80   -357   -184       C  
ATOM    686  O   ALA A  87     -12.638  -0.759  -8.359  1.00 14.51           O  
ANISOU  686  O   ALA A  87     1436   2200   1879     13   -345   -203       O  
ATOM    687  CB  ALA A  87     -10.510   1.237  -9.796  1.00 13.31           C  
ANISOU  687  CB  ALA A  87     1457   1989   1613    136   -331   -156       C  
ATOM    688  N   SER A  88     -13.659   1.050  -9.226  1.00 15.92           N  
ANISOU  688  N   SER A  88     1568   2439   2042    119   -413   -183       N  
ATOM    689  CA  SER A  88     -14.870   0.344  -9.607  1.00 17.28           C  
ANISOU  689  CA  SER A  88     1660   2666   2242     78   -476   -209       C  
ATOM    690  C   SER A  88     -15.419   1.028 -10.860  1.00 18.67           C  
ANISOU  690  C   SER A  88     1835   2881   2378    138   -562   -208       C  
ATOM    691  O   SER A  88     -14.769   0.999 -11.909  1.00 18.52           O  
ANISOU  691  O   SER A  88     1906   2836   2293    153   -593   -212       O  
ATOM    692  CB  SER A  88     -15.880   0.335  -8.450  1.00 17.68           C  
ANISOU  692  CB  SER A  88     1594   2761   2364     62   -444   -205       C  
ATOM    693  OG  SER A  88     -16.328   1.644  -8.126  1.00 17.98           O  
ANISOU  693  OG  SER A  88     1592   2828   2412    148   -432   -180       O  
ATOM    694  N   ASN A  89     -16.588   1.655 -10.740  1.00 20.02           N  
ANISOU  694  N   ASN A  89     1908   3116   2584    180   -595   -201       N  
ATOM    695  CA  ASN A  89     -17.203   2.410 -11.827  1.00 21.36           C  
ANISOU  695  CA  ASN A  89     2068   3330   2717    252   -678   -193       C  
ATOM    696  C   ASN A  89     -17.332   3.895 -11.459  1.00 21.84           C  
ANISOU  696  C   ASN A  89     2124   3392   2781    358   -648   -153       C  
ATOM    697  O   ASN A  89     -17.961   4.662 -12.187  1.00 22.75           O  
ANISOU  697  O   ASN A  89     2223   3547   2875    436   -711   -138       O  
ATOM    698  CB  ASN A  89     -18.573   1.820 -12.153  1.00 22.57           C  
ANISOU  698  CB  ASN A  89     2101   3568   2909    217   -762   -221       C  
ATOM    699  N   GLY A  90     -16.715   4.298 -10.346  1.00 21.36           N  
ANISOU  699  N   GLY A  90     2087   3284   2744    364   -556   -137       N  
ATOM    700  CA  GLY A  90     -16.827   5.669  -9.847  1.00 21.66           C  
ANISOU  700  CA  GLY A  90     2130   3311   2790    457   -520   -107       C  
ATOM    701  C   GLY A  90     -17.678   5.813  -8.595  1.00 22.05           C  
ANISOU  701  C   GLY A  90     2073   3399   2905    470   -473   -109       C  
ATOM    702  O   GLY A  90     -17.560   6.807  -7.875  1.00 22.10           O  
ANISOU  702  O   GLY A  90     2101   3378   2919    534   -420    -92       O  
ATOM    703  N   GLN A  91     -18.526   4.824  -8.326  1.00 22.60           N  
ANISOU  703  N   GLN A  91     2034   3532   3022    406   -488   -130       N  
ATOM    704  CA  GLN A  91     -19.428   4.866  -7.172  1.00 23.24           C  
ANISOU  704  CA  GLN A  91     2001   3664   3165    415   -437   -128       C  
ATOM    705  C   GLN A  91     -18.822   4.213  -5.924  1.00 22.16           C  
ANISOU  705  C   GLN A  91     1885   3488   3049    345   -345   -134       C  
ATOM    706  O   GLN A  91     -19.137   4.606  -4.803  1.00 22.29           O  
ANISOU  706  O   GLN A  91     1861   3517   3093    377   -276   -126       O  
ATOM    707  CB  GLN A  91     -20.760   4.203  -7.518  1.00 24.69           C  
ANISOU  707  CB  GLN A  91     2040   3944   3396    381   -499   -142       C  
ATOM    708  CG  GLN A  91     -21.513   4.870  -8.670  1.00 26.92           C  
ANISOU  708  CG  GLN A  91     2285   4284   3660    462   -598   -135       C  
ATOM    709  CD  GLN A  91     -21.988   6.284  -8.353  1.00 29.46           C  
ANISOU  709  CD  GLN A  91     2584   4623   3985    599   -576   -106       C  
ATOM    710  OE1 GLN A  91     -22.238   6.632  -7.197  1.00 31.94           O  
ANISOU  710  OE1 GLN A  91     2856   4942   4337    628   -493    -98       O  
ATOM    711  NE2 GLN A  91     -22.123   7.104  -9.389  1.00 31.04           N  
ANISOU  711  NE2 GLN A  91     2823   4830   4143    690   -649    -89       N  
ATOM    712  N   GLY A  92     -17.965   3.214  -6.117  1.00 21.19           N  
ANISOU  712  N   GLY A  92     1827   3318   2906    258   -344   -148       N  
ATOM    713  CA  GLY A  92     -17.260   2.590  -5.006  1.00 20.00           C  
ANISOU  713  CA  GLY A  92     1711   3124   2764    200   -264   -149       C  
ATOM    714  C   GLY A  92     -16.364   3.597  -4.304  1.00 19.05           C  
ANISOU  714  C   GLY A  92     1674   2950   2616    260   -206   -135       C  
ATOM    715  O   GLY A  92     -15.785   4.478  -4.942  1.00 18.58           O  
ANISOU  715  O   GLY A  92     1688   2854   2518    314   -230   -127       O  
ATOM    716  N   LYS A  93     -16.275   3.486  -2.985  1.00 18.59           N  
ANISOU  716  N   LYS A  93     1606   2886   2573    249   -130   -132       N  
ATOM    717  CA  LYS A  93     -15.435   4.385  -2.201  1.00 18.06           C  
ANISOU  717  CA  LYS A  93     1617   2767   2479    297    -79   -127       C  
ATOM    718  C   LYS A  93     -14.968   3.729  -0.913  1.00 17.08           C  
ANISOU  718  C   LYS A  93     1509   2627   2354    250     -9   -129       C  
ATOM    719  O   LYS A  93     -15.558   2.751  -0.456  1.00 16.90           O  
ANISOU  719  O   LYS A  93     1422   2639   2360    197     15   -127       O  
ATOM    720  CB  LYS A  93     -16.179   5.686  -1.883  1.00 18.87           C  
ANISOU  720  CB  LYS A  93     1691   2891   2589    397    -66   -122       C  
ATOM    721  CG  LYS A  93     -17.365   5.545  -0.936  1.00 21.08           C  
ANISOU  721  CG  LYS A  93     1863   3238   2909    414    -17   -121       C  
ATOM    722  CD  LYS A  93     -17.961   6.914  -0.632  1.00 23.92           C  
ANISOU  722  CD  LYS A  93     2212   3607   3268    530      1   -118       C  
ATOM    723  CE  LYS A  93     -19.269   6.812   0.122  1.00 25.63           C  
ANISOU  723  CE  LYS A  93     2304   3907   3527    561     48   -113       C  
ATOM    724  NZ  LYS A  93     -20.347   6.328  -0.772  1.00 27.82           N  
ANISOU  724  NZ  LYS A  93     2459   4265   3848    546    -12   -106       N  
ATOM    725  N   GLY A  94     -13.902   4.279  -0.338  1.00 16.05           N  
ANISOU  725  N   GLY A  94     1465   2442   2190    269     20   -130       N  
ATOM    726  CA  GLY A  94     -13.429   3.851   0.970  1.00 15.46           C  
ANISOU  726  CA  GLY A  94     1415   2356   2104    243     82   -131       C  
ATOM    727  C   GLY A  94     -12.131   3.073   0.957  1.00 14.54           C  
ANISOU  727  C   GLY A  94     1368   2194   1962    185     79   -130       C  
ATOM    728  O   GLY A  94     -11.511   2.872  -0.095  1.00 14.05           O  
ANISOU  728  O   GLY A  94     1340   2107   1891    164     36   -130       O  
ATOM    729  N   SER A  95     -11.744   2.626   2.150  1.00 13.84           N  
ANISOU  729  N   SER A  95     1301   2100   1859    167    130   -128       N  
ATOM    730  CA  SER A  95     -10.478   1.959   2.375  1.00 13.22           C  
ANISOU  730  CA  SER A  95     1286   1984   1754    128    132   -124       C  
ATOM    731  C   SER A  95     -10.704   0.487   2.665  1.00 13.41           C  
ANISOU  731  C   SER A  95     1288   2017   1790     69    155   -110       C  
ATOM    732  O   SER A  95     -11.746   0.097   3.186  1.00 14.04           O  
ANISOU  732  O   SER A  95     1309   2132   1893     56    190   -102       O  
ATOM    733  CB  SER A  95      -9.751   2.598   3.553  1.00 12.89           C  
ANISOU  733  CB  SER A  95     1297   1924   1677    157    163   -131       C  
ATOM    734  OG  SER A  95      -9.610   3.983   3.351  1.00 12.75           O  
ANISOU  734  OG  SER A  95     1307   1886   1652    206    145   -146       O  
ATOM    735  N   GLU A  96      -9.687  -0.306   2.365  1.00 12.93           N  
ANISOU  735  N   GLU A  96     1278   1923   1714     35    141   -106       N  
ATOM    736  CA  GLU A  96      -9.771  -1.746   2.401  1.00 13.36           C  
ANISOU  736  CA  GLU A  96     1331   1966   1780    -21    155    -94       C  
ATOM    737  C   GLU A  96      -8.344  -2.291   2.486  1.00 12.47           C  
ANISOU  737  C   GLU A  96     1291   1814   1635    -26    152    -87       C  
ATOM    738  O   GLU A  96      -7.451  -1.762   1.833  1.00 11.91           O  
ANISOU  738  O   GLU A  96     1251   1726   1547     -6    121    -96       O  
ATOM    739  CB  GLU A  96     -10.456  -2.149   1.109  1.00 14.11           C  
ANISOU  739  CB  GLU A  96     1388   2066   1905    -53    109   -104       C  
ATOM    740  CG  GLU A  96     -10.529  -3.575   0.770  1.00 15.60           C  
ANISOU  740  CG  GLU A  96     1588   2230   2108   -116    105   -102       C  
ATOM    741  CD  GLU A  96     -11.398  -3.761  -0.448  1.00 16.77           C  
ANISOU  741  CD  GLU A  96     1693   2395   2286   -146     51   -121       C  
ATOM    742  OE1 GLU A  96     -10.871  -4.110  -1.524  1.00 16.33           O  
ANISOU  742  OE1 GLU A  96     1681   2310   2212   -155      7   -137       O  
ATOM    743  OE2 GLU A  96     -12.609  -3.497  -0.330  1.00 19.11           O  
ANISOU  743  OE2 GLU A  96     1907   2738   2618   -154     51   -121       O  
ATOM    744  N   VAL A  97      -8.121  -3.317   3.306  1.00 12.26           N  
ANISOU  744  N   VAL A  97     1288   1773   1598    -49    188    -68       N  
ATOM    745  CA  VAL A  97      -6.790  -3.916   3.430  1.00 11.41           C  
ANISOU  745  CA  VAL A  97     1243   1632   1460    -43    185    -59       C  
ATOM    746  C   VAL A  97      -6.874  -5.439   3.253  1.00 11.67           C  
ANISOU  746  C   VAL A  97     1300   1630   1504    -86    198    -44       C  
ATOM    747  O   VAL A  97      -7.638  -6.112   3.953  1.00 12.02           O  
ANISOU  747  O   VAL A  97     1332   1673   1561   -117    237    -25       O  
ATOM    748  CB  VAL A  97      -6.125  -3.562   4.788  1.00 11.56           C  
ANISOU  748  CB  VAL A  97     1291   1662   1440     -9    212    -47       C  
ATOM    749  CG1 VAL A  97      -4.780  -4.268   4.939  1.00 11.23           C  
ANISOU  749  CG1 VAL A  97     1302   1596   1370      1    205    -33       C  
ATOM    750  CG2 VAL A  97      -5.966  -2.043   4.937  1.00 10.00           C  
ANISOU  750  CG2 VAL A  97     1083   1485   1231     28    195    -69       C  
ATOM    751  N   LEU A  98      -6.089  -5.968   2.313  1.00 10.91           N  
ANISOU  751  N   LEU A  98     1243   1501   1402    -88    170    -51       N  
ATOM    752  CA  LEU A  98      -6.082  -7.405   2.031  1.00 11.27           C  
ANISOU  752  CA  LEU A  98     1328   1498   1456   -123    177    -44       C  
ATOM    753  C   LEU A  98      -4.949  -8.080   2.792  1.00 10.87           C  
ANISOU  753  C   LEU A  98     1337   1420   1371    -92    202    -18       C  
ATOM    754  O   LEU A  98      -3.848  -7.529   2.901  1.00 10.42           O  
ANISOU  754  O   LEU A  98     1293   1380   1288    -44    190    -16       O  
ATOM    755  CB  LEU A  98      -5.959  -7.662   0.525  1.00 11.22           C  
ANISOU  755  CB  LEU A  98     1338   1469   1455   -134    134    -71       C  
ATOM    756  CG  LEU A  98      -6.913  -6.842  -0.353  1.00 12.06           C  
ANISOU  756  CG  LEU A  98     1389   1610   1583   -149     96    -97       C  
ATOM    757  CD1 LEU A  98      -6.816  -7.257  -1.825  1.00 11.81           C  
ANISOU  757  CD1 LEU A  98     1388   1554   1545   -160     51   -124       C  
ATOM    758  CD2 LEU A  98      -8.347  -6.969   0.141  1.00 12.69           C  
ANISOU  758  CD2 LEU A  98     1406   1713   1703   -195    110    -93       C  
ATOM    759  N   TYR A  99      -5.229  -9.258   3.342  1.00 11.08           N  
ANISOU  759  N   TYR A  99     1398   1408   1403   -119    235      6       N  
ATOM    760  CA  TYR A  99      -4.267  -9.967   4.179  1.00 11.11           C  
ANISOU  760  CA  TYR A  99     1463   1386   1372    -82    260     39       C  
ATOM    761  C   TYR A  99      -4.313 -11.472   3.902  1.00 11.55           C  
ANISOU  761  C   TYR A  99     1583   1366   1439   -110    276     52       C  
ATOM    762  O   TYR A  99      -5.222 -11.967   3.217  1.00 11.18           O  
ANISOU  762  O   TYR A  99     1530   1288   1429   -172    271     34       O  
ATOM    763  CB  TYR A  99      -4.534  -9.684   5.660  1.00 11.19           C  
ANISOU  763  CB  TYR A  99     1464   1427   1359    -70    299     69       C  
ATOM    764  CG  TYR A  99      -5.824 -10.292   6.151  1.00 12.63           C  
ANISOU  764  CG  TYR A  99     1635   1594   1569   -129    345     90       C  
ATOM    765  CD1 TYR A  99      -5.853 -11.580   6.669  1.00 13.43           C  
ANISOU  765  CD1 TYR A  99     1798   1639   1666   -150    385    128       C  
ATOM    766  CD2 TYR A  99      -7.021  -9.585   6.082  1.00 12.81           C  
ANISOU  766  CD2 TYR A  99     1584   1660   1625   -165    352     74       C  
ATOM    767  CE1 TYR A  99      -7.037 -12.149   7.111  1.00 14.43           C  
ANISOU  767  CE1 TYR A  99     1910   1750   1824   -215    434    152       C  
ATOM    768  CE2 TYR A  99      -8.212 -10.145   6.530  1.00 14.49           C  
ANISOU  768  CE2 TYR A  99     1770   1867   1869   -223    400     96       C  
ATOM    769  CZ  TYR A  99      -8.208 -11.429   7.046  1.00 15.08           C  
ANISOU  769  CZ  TYR A  99     1905   1884   1942   -254    442    136       C  
ATOM    770  OH  TYR A  99      -9.380 -11.997   7.479  1.00 16.52           O  
ANISOU  770  OH  TYR A  99     2058   2059   2159   -323    495    163       O  
ATOM    771  N   TYR A 100      -3.325 -12.179   4.450  1.00 11.46           N  
ANISOU  771  N   TYR A 100     1635   1324   1394    -62    293     82       N  
ATOM    772  CA  TYR A 100      -3.117 -13.608   4.173  1.00 12.20           C  
ANISOU  772  CA  TYR A 100     1811   1335   1492    -69    308     95       C  
ATOM    773  C   TYR A 100      -3.238 -14.498   5.402  1.00 13.10           C  
ANISOU  773  C   TYR A 100     1979   1408   1589    -69    358    149       C  
ATOM    774  O   TYR A 100      -3.612 -15.654   5.279  1.00 13.96           O  
ANISOU  774  O   TYR A 100     2151   1438   1717   -108    381    162       O  
ATOM    775  CB  TYR A 100      -1.734 -13.816   3.547  1.00 11.90           C  
ANISOU  775  CB  TYR A 100     1811   1284   1426      4    285     87       C  
ATOM    776  CG  TYR A 100      -1.491 -15.221   3.033  1.00 11.89           C  
ANISOU  776  CG  TYR A 100     1902   1190   1427      9    298     90       C  
ATOM    777  CD1 TYR A 100      -2.045 -15.641   1.842  1.00 12.17           C  
ANISOU  777  CD1 TYR A 100     1959   1178   1489    -40    279     48       C  
ATOM    778  CD2 TYR A 100      -0.717 -16.124   3.750  1.00 13.11           C  
ANISOU  778  CD2 TYR A 100     2128   1301   1552     68    324    132       C  
ATOM    779  CE1 TYR A 100      -1.842 -16.921   1.359  1.00 13.46           C  
ANISOU  779  CE1 TYR A 100     2219   1244   1650    -37    289     43       C  
ATOM    780  CE2 TYR A 100      -0.502 -17.414   3.283  1.00 14.47           C  
ANISOU  780  CE2 TYR A 100     2397   1376   1726     79    338    134       C  
ATOM    781  CZ  TYR A 100      -1.073 -17.804   2.078  1.00 14.31           C  
ANISOU  781  CZ  TYR A 100     2402   1302   1734     24    321     86       C  
ATOM    782  OH  TYR A 100      -0.871 -19.066   1.583  1.00 15.50           O  
ANISOU  782  OH  TYR A 100     2659   1347   1883     35    333     79       O  
ATOM    783  N   SER A 101      -2.917 -13.961   6.577  1.00 13.54           N  
ANISOU  783  N   SER A 101     2022   1517   1608    -27    373    179       N  
ATOM    784  CA  SER A 101      -2.818 -14.754   7.800  1.00 14.46           C  
ANISOU  784  CA  SER A 101     2202   1603   1691     -6    419    237       C  
ATOM    785  C   SER A 101      -3.506 -14.065   8.974  1.00 15.11           C  
ANISOU  785  C   SER A 101     2245   1743   1752    -19    452    258       C  
ATOM    786  O   SER A 101      -3.948 -12.920   8.871  1.00 14.11           O  
ANISOU  786  O   SER A 101     2043   1681   1637    -33    436    225       O  
ATOM    787  CB  SER A 101      -1.347 -14.951   8.147  1.00 14.39           C  
ANISOU  787  CB  SER A 101     2237   1600   1631     92    398    257       C  
ATOM    788  OG  SER A 101      -0.718 -13.693   8.330  1.00 13.08           O  
ANISOU  788  OG  SER A 101     2007   1523   1441    133    359    235       O  
ATOM    789  N   ASN A 102      -3.574 -14.766  10.100  1.00 16.72           N  
ANISOU  789  N   ASN A 102     2510   1922   1921     -6    500    315       N  
ATOM    790  CA  ASN A 102      -4.119 -14.181  11.320  1.00 17.71           C  
ANISOU  790  CA  ASN A 102     2615   2104   2010     -3    540    340       C  
ATOM    791  C   ASN A 102      -3.290 -12.986  11.799  1.00 17.45           C  
ANISOU  791  C   ASN A 102     2551   2153   1924     69    496    316       C  
ATOM    792  O   ASN A 102      -3.840 -12.021  12.331  1.00 17.93           O  
ANISOU  792  O   ASN A 102     2566   2274   1971     64    507    301       O  
ATOM    793  CB  ASN A 102      -4.236 -15.232  12.433  1.00 18.88           C  
ANISOU  793  CB  ASN A 102     2850   2205   2118      5    603    412       C  
ATOM    794  CG  ASN A 102      -5.362 -16.235  12.186  1.00 20.30           C  
ANISOU  794  CG  ASN A 102     3049   2309   2356    -90    662    439       C  
ATOM    795  OD1 ASN A 102      -6.356 -15.934  11.518  1.00 21.56           O  
ANISOU  795  OD1 ASN A 102     3133   2479   2578   -168    665    405       O  
ATOM    796  ND2 ASN A 102      -5.209 -17.432  12.737  1.00 21.94           N  
ANISOU  796  ND2 ASN A 102     3356   2439   2542    -85    707    501       N  
ATOM    797  N   LYS A 103      -1.973 -13.049  11.612  1.00 17.44           N  
ANISOU  797  N   LYS A 103     2575   2155   1897    134    445    311       N  
ATOM    798  CA  LYS A 103      -1.092 -11.941  11.989  1.00 17.33           C  
ANISOU  798  CA  LYS A 103     2527   2217   1841    191    394    285       C  
ATOM    799  C   LYS A 103      -1.355 -10.736  11.102  1.00 16.35           C  
ANISOU  799  C   LYS A 103     2321   2130   1760    157    360    225       C  
ATOM    800  O   LYS A 103      -1.464  -9.608  11.584  1.00 16.16           O  
ANISOU  800  O   LYS A 103     2262   2161   1716    165    347    200       O  
ATOM    801  CB  LYS A 103       0.379 -12.356  11.897  1.00 17.63           C  
ANISOU  801  CB  LYS A 103     2594   2253   1850    263    348    297       C  
ATOM    802  CG  LYS A 103       0.812 -13.316  13.000  1.00 19.74           C  
ANISOU  802  CG  LYS A 103     2945   2500   2055    322    369    359       C  
ATOM    803  CD  LYS A 103       2.274 -13.713  12.864  1.00 21.36           C  
ANISOU  803  CD  LYS A 103     3166   2713   2237    404    320    371       C  
ATOM    804  CE  LYS A 103       2.707 -14.637  13.992  1.00 23.46           C  
ANISOU  804  CE  LYS A 103     3517   2962   2433    474    335    437       C  
ATOM    805  NZ  LYS A 103       2.073 -15.986  13.874  1.00 25.49           N  
ANISOU  805  NZ  LYS A 103     3859   3115   2709    452    400    485       N  
ATOM    806  N   GLY A 104      -1.460 -10.994   9.804  1.00 15.82           N  
ANISOU  806  N   GLY A 104     2234   2027   1750    124    347    202       N  
ATOM    807  CA  GLY A 104      -1.829  -9.981   8.831  1.00 15.10           C  
ANISOU  807  CA  GLY A 104     2075   1962   1701     91    319    152       C  
ATOM    808  C   GLY A 104      -3.181  -9.354   9.111  1.00 14.87           C  
ANISOU  808  C   GLY A 104     2003   1956   1692     46    349    141       C  
ATOM    809  O   GLY A 104      -3.345  -8.157   8.939  1.00 14.25           O  
ANISOU  809  O   GLY A 104     1876   1920   1620     48    326    107       O  
ATOM    810  N   LEU A 105      -4.145 -10.165   9.541  1.00 15.52           N  
ANISOU  810  N   LEU A 105     2102   2009   1785      7    403    173       N  
ATOM    811  CA  LEU A 105      -5.462  -9.663   9.946  1.00 15.85           C  
ANISOU  811  CA  LEU A 105     2095   2083   1845    -31    444    171       C  
ATOM    812  C   LEU A 105      -5.379  -8.604  11.057  1.00 15.73           C  
ANISOU  812  C   LEU A 105     2074   2128   1776     17    453    166       C  
ATOM    813  O   LEU A 105      -6.112  -7.617  11.017  1.00 15.62           O  
ANISOU  813  O   LEU A 105     2004   2153   1778     11    458    138       O  
ATOM    814  CB  LEU A 105      -6.365 -10.819  10.387  1.00 16.56           C  
ANISOU  814  CB  LEU A 105     2209   2132   1951    -83    510    216       C  
ATOM    815  CG  LEU A 105      -7.728 -10.472  10.999  1.00 17.51           C  
ANISOU  815  CG  LEU A 105     2274   2291   2088   -120    571    228       C  
ATOM    816  CD1 LEU A 105      -8.616  -9.713  10.018  1.00 17.01           C  
ANISOU  816  CD1 LEU A 105     2117   2260   2087   -157    545    184       C  
ATOM    817  CD2 LEU A 105      -8.411 -11.741  11.483  1.00 17.82           C  
ANISOU  817  CD2 LEU A 105     2346   2282   2142   -176    640    284       C  
ATOM    818  N   GLU A 106      -4.490  -8.796  12.034  1.00 15.98           N  
ANISOU  818  N   GLU A 106     2165   2167   1741     69    452    190       N  
ATOM    819  CA  GLU A 106      -4.341  -7.822  13.123  1.00 16.03           C  
ANISOU  819  CA  GLU A 106     2180   2227   1685    115    452    179       C  
ATOM    820  C   GLU A 106      -3.960  -6.452  12.578  1.00 15.18           C  
ANISOU  820  C   GLU A 106     2026   2150   1590    129    394    121       C  
ATOM    821  O   GLU A 106      -4.607  -5.447  12.890  1.00 15.41           O  
ANISOU  821  O   GLU A 106     2029   2212   1615    135    407     94       O  
ATOM    822  CB  GLU A 106      -3.277  -8.261  14.126  1.00 16.61           C  
ANISOU  822  CB  GLU A 106     2324   2305   1681    172    439    209       C  
ATOM    823  CG  GLU A 106      -3.610  -9.503  14.923  1.00 18.50           C  
ANISOU  823  CG  GLU A 106     2627   2513   1888    172    502    275       C  
ATOM    824  CD  GLU A 106      -2.608  -9.730  16.040  1.00 20.62           C  
ANISOU  824  CD  GLU A 106     2968   2801   2065    243    483    303       C  
ATOM    825  OE1 GLU A 106      -1.701 -10.582  15.887  1.00 20.33           O  
ANISOU  825  OE1 GLU A 106     2971   2733   2019    272    455    331       O  
ATOM    826  OE2 GLU A 106      -2.715  -9.024  17.065  1.00 23.49           O  
ANISOU  826  OE2 GLU A 106     3350   3214   2362    276    491    295       O  
ATOM    827  N   TYR A 107      -2.896  -6.421  11.778  1.00 14.06           N  
ANISOU  827  N   TYR A 107     1880   1996   1464    137    335    104       N  
ATOM    828  CA  TYR A 107      -2.477  -5.202  11.082  1.00 13.20           C  
ANISOU  828  CA  TYR A 107     1731   1906   1378    139    282     56       C  
ATOM    829  C   TYR A 107      -3.616  -4.624  10.244  1.00 12.44           C  
ANISOU  829  C   TYR A 107     1582   1807   1338    103    296     32       C  
ATOM    830  O   TYR A 107      -3.948  -3.440  10.366  1.00 12.35           O  
ANISOU  830  O   TYR A 107     1549   1818   1324    114    288      0       O  
ATOM    831  CB  TYR A 107      -1.280  -5.484  10.164  1.00 12.72           C  
ANISOU  831  CB  TYR A 107     1666   1830   1336    144    233     52       C  
ATOM    832  CG  TYR A 107       0.031  -5.758  10.872  1.00 13.82           C  
ANISOU  832  CG  TYR A 107     1837   1988   1426    189    201     67       C  
ATOM    833  CD1 TYR A 107       0.577  -4.835  11.765  1.00 15.02           C  
ANISOU  833  CD1 TYR A 107     1994   2181   1532    213    168     46       C  
ATOM    834  CD2 TYR A 107       0.749  -6.922  10.624  1.00 14.39           C  
ANISOU  834  CD2 TYR A 107     1934   2037   1497    209    199    100       C  
ATOM    835  CE1 TYR A 107       1.790  -5.077  12.402  1.00 15.19           C  
ANISOU  835  CE1 TYR A 107     2035   2230   1509    253    127     58       C  
ATOM    836  CE2 TYR A 107       1.960  -7.174  11.261  1.00 14.92           C  
ANISOU  836  CE2 TYR A 107     2019   2129   1519    260    165    117       C  
ATOM    837  CZ  TYR A 107       2.476  -6.249  12.147  1.00 15.40           C  
ANISOU  837  CZ  TYR A 107     2075   2241   1536    280    125     96       C  
ATOM    838  OH  TYR A 107       3.676  -6.499  12.779  1.00 16.16           O  
ANISOU  838  OH  TYR A 107     2181   2372   1588    329     81    111       O  
ATOM    839  N   ALA A 108      -4.214  -5.465   9.399  1.00 11.91           N  
ANISOU  839  N   ALA A 108     1498   1711   1318     64    312     46       N  
ATOM    840  CA  ALA A 108      -5.250  -5.023   8.456  1.00 11.52           C  
ANISOU  840  CA  ALA A 108     1392   1663   1323     31    312     24       C  
ATOM    841  C   ALA A 108      -6.410  -4.296   9.142  1.00 11.58           C  
ANISOU  841  C   ALA A 108     1364   1705   1329     37    352     18       C  
ATOM    842  O   ALA A 108      -6.831  -3.226   8.688  1.00 11.52           O  
ANISOU  842  O   ALA A 108     1318   1716   1342     47    334    -12       O  
ATOM    843  CB  ALA A 108      -5.763  -6.204   7.624  1.00 11.34           C  
ANISOU  843  CB  ALA A 108     1362   1602   1343    -18    322     39       C  
ATOM    844  N   THR A 109      -6.896  -4.855  10.247  1.00 11.99           N  
ANISOU  844  N   THR A 109     1435   1768   1354     37    410     49       N  
ATOM    845  CA  THR A 109      -8.044  -4.295  10.973  1.00 12.31           C  
ANISOU  845  CA  THR A 109     1441   1847   1390     48    464     50       C  
ATOM    846  C   THR A 109      -7.732  -2.918  11.558  1.00 12.22           C  
ANISOU  846  C   THR A 109     1446   1863   1334    106    448     14       C  
ATOM    847  O   THR A 109      -8.539  -1.994  11.466  1.00 12.10           O  
ANISOU  847  O   THR A 109     1390   1872   1337    124    460    -10       O  
ATOM    848  CB  THR A 109      -8.495  -5.246  12.104  1.00 13.27           C  
ANISOU  848  CB  THR A 109     1590   1971   1479     38    539     99       C  
ATOM    849  OG1 THR A 109      -8.842  -6.523  11.544  1.00 12.97           O  
ANISOU  849  OG1 THR A 109     1543   1895   1489    -25    555    130       O  
ATOM    850  CG2 THR A 109      -9.697  -4.679  12.850  1.00 13.80           C  
ANISOU  850  CG2 THR A 109     1616   2086   1540     54    607    102       C  
ATOM    851  N   ARG A 110      -6.548  -2.781  12.143  1.00 12.17           N  
ANISOU  851  N   ARG A 110     1501   1851   1271    135    416      8       N  
ATOM    852  CA  ARG A 110      -6.141  -1.514  12.730  1.00 12.26           C  
ANISOU  852  CA  ARG A 110     1540   1879   1238    181    392    -32       C  
ATOM    853  C   ARG A 110      -5.926  -0.440  11.660  1.00 11.43           C  
ANISOU  853  C   ARG A 110     1406   1760   1178    177    338    -73       C  
ATOM    854  O   ARG A 110      -6.360   0.694  11.833  1.00 11.43           O  
ANISOU  854  O   ARG A 110     1404   1768   1173    206    340   -106       O  
ATOM    855  CB  ARG A 110      -4.889  -1.693  13.591  1.00 12.41           C  
ANISOU  855  CB  ARG A 110     1626   1901   1189    205    360    -30       C  
ATOM    856  CG  ARG A 110      -5.116  -2.547  14.841  1.00 13.58           C  
ANISOU  856  CG  ARG A 110     1820   2065   1273    225    416     11       C  
ATOM    857  CD  ARG A 110      -3.958  -2.408  15.832  1.00 14.30           C  
ANISOU  857  CD  ARG A 110     1979   2172   1281    264    373      3       C  
ATOM    858  NE  ARG A 110      -2.660  -2.675  15.200  1.00 14.86           N  
ANISOU  858  NE  ARG A 110     2048   2229   1371    254    300      1       N  
ATOM    859  CZ  ARG A 110      -1.989  -3.827  15.258  1.00 16.08           C  
ANISOU  859  CZ  ARG A 110     2224   2374   1513    258    293     44       C  
ATOM    860  NH1 ARG A 110      -2.462  -4.872  15.937  1.00 17.04           N  
ANISOU  860  NH1 ARG A 110     2383   2489   1601    267    352     96       N  
ATOM    861  NH2 ARG A 110      -0.819  -3.932  14.637  1.00 15.76           N  
ANISOU  861  NH2 ARG A 110     2169   2328   1492    257    230     38       N  
ATOM    862  N   ILE A 111      -5.279  -0.798  10.554  1.00 11.06           N  
ANISOU  862  N   ILE A 111     1344   1690   1170    147    294    -69       N  
ATOM    863  CA  ILE A 111      -5.125   0.127   9.426  1.00 10.74           C  
ANISOU  863  CA  ILE A 111     1277   1633   1170    141    250    -98       C  
ATOM    864  C   ILE A 111      -6.497   0.590   8.933  1.00 11.18           C  
ANISOU  864  C   ILE A 111     1283   1698   1266    145    275   -105       C  
ATOM    865  O   ILE A 111      -6.737   1.785   8.749  1.00 11.08           O  
ANISOU  865  O   ILE A 111     1268   1682   1261    172    262   -133       O  
ATOM    866  CB  ILE A 111      -4.370  -0.515   8.253  1.00 10.13           C  
ANISOU  866  CB  ILE A 111     1190   1534   1126    110    214    -86       C  
ATOM    867  CG1 ILE A 111      -2.909  -0.770   8.622  1.00  9.59           C  
ANISOU  867  CG1 ILE A 111     1156   1463   1024    116    182    -81       C  
ATOM    868  CG2 ILE A 111      -4.437   0.382   7.027  1.00 10.06           C  
ANISOU  868  CG2 ILE A 111     1156   1511   1156    105    181   -106       C  
ATOM    869  CD1 ILE A 111      -2.214  -1.717   7.693  1.00  9.05           C  
ANISOU  869  CD1 ILE A 111     1083   1378    978     99    166    -61       C  
ATOM    870  N   CYS A 112      -7.396  -0.370   8.735  1.00 11.62           N  
ANISOU  870  N   CYS A 112     1300   1765   1351    119    310    -78       N  
ATOM    871  CA  CYS A 112      -8.756  -0.080   8.298  1.00 12.19           C  
ANISOU  871  CA  CYS A 112     1306   1859   1465    119    332    -80       C  
ATOM    872  C   CYS A 112      -9.502   0.860   9.242  1.00 12.90           C  
ANISOU  872  C   CYS A 112     1390   1978   1532    171    374    -95       C  
ATOM    873  O   CYS A 112     -10.166   1.793   8.790  1.00 12.63           O  
ANISOU  873  O   CYS A 112     1323   1954   1524    202    367   -114       O  
ATOM    874  CB  CYS A 112      -9.540  -1.376   8.127  1.00 12.79           C  
ANISOU  874  CB  CYS A 112     1341   1944   1576     69    364    -49       C  
ATOM    875  SG  CYS A 112      -9.205  -2.164   6.557  1.00 13.22           S  
ANISOU  875  SG  CYS A 112     1385   1965   1674     17    307    -49       S  
ATOM    876  N   ASP A 113      -9.390   0.614  10.545  1.00 13.36           N  
ANISOU  876  N   ASP A 113     1489   2050   1539    189    420    -85       N  
ATOM    877  CA  ASP A 113     -10.039   1.477  11.529  1.00 14.36           C  
ANISOU  877  CA  ASP A 113     1624   2204   1630    247    467   -101       C  
ATOM    878  C   ASP A 113      -9.491   2.898  11.472  1.00 13.91           C  
ANISOU  878  C   ASP A 113     1612   2121   1551    291    423   -149       C  
ATOM    879  O   ASP A 113     -10.257   3.859  11.562  1.00 14.59           O  
ANISOU  879  O   ASP A 113     1684   2218   1643    342    444   -171       O  
ATOM    880  CB  ASP A 113      -9.897   0.912  12.944  1.00 15.19           C  
ANISOU  880  CB  ASP A 113     1780   2327   1667    260    521    -81       C  
ATOM    881  CG  ASP A 113     -10.877  -0.206  13.229  1.00 16.95           C  
ANISOU  881  CG  ASP A 113     1953   2578   1910    227    595    -32       C  
ATOM    882  OD1 ASP A 113     -11.907  -0.306  12.531  1.00 19.15           O  
ANISOU  882  OD1 ASP A 113     2145   2876   2254    206    612    -23       O  
ATOM    883  OD2 ASP A 113     -10.619  -0.985  14.168  1.00 20.63           O  
ANISOU  883  OD2 ASP A 113     2465   3047   2325    222    635     -1       O  
ATOM    884  N   LYS A 114      -8.173   3.028  11.316  1.00 12.98           N  
ANISOU  884  N   LYS A 114     1547   1970   1414    273    364   -163       N  
ATOM    885  CA  LYS A 114      -7.542   4.346  11.239  1.00 12.77           C  
ANISOU  885  CA  LYS A 114     1568   1910   1374    298    318   -207       C  
ATOM    886  C   LYS A 114      -7.946   5.103   9.976  1.00 12.01           C  
ANISOU  886  C   LYS A 114     1436   1792   1337    303    291   -216       C  
ATOM    887  O   LYS A 114      -8.416   6.234  10.050  1.00 12.39           O  
ANISOU  887  O   LYS A 114     1499   1824   1383    350    296   -243       O  
ATOM    888  CB  LYS A 114      -6.014   4.225  11.357  1.00 12.36           C  
ANISOU  888  CB  LYS A 114     1565   1836   1296    267    261   -216       C  
ATOM    889  CG  LYS A 114      -5.535   4.060  12.796  1.00 13.78           C  
ANISOU  889  CG  LYS A 114     1804   2033   1397    287    271   -225       C  
ATOM    890  CD  LYS A 114      -5.798   5.321  13.612  1.00 15.52           C  
ANISOU  890  CD  LYS A 114     2080   2243   1574    336    278   -275       C  
ATOM    891  CE  LYS A 114      -5.442   5.144  15.068  1.00 17.78           C  
ANISOU  891  CE  LYS A 114     2432   2552   1770    362    289   -287       C  
ATOM    892  NZ  LYS A 114      -5.512   6.435  15.803  1.00 18.38           N  
ANISOU  892  NZ  LYS A 114     2578   2607   1797    407    283   -347       N  
ATOM    893  N   LEU A 115      -7.783   4.473   8.819  1.00 11.20           N  
ANISOU  893  N   LEU A 115     1292   1684   1280    260    263   -192       N  
ATOM    894  CA  LEU A 115      -8.279   5.059   7.576  1.00 11.00           C  
ANISOU  894  CA  LEU A 115     1232   1646   1302    267    238   -194       C  
ATOM    895  C   LEU A 115      -9.784   5.337   7.675  1.00 11.56           C  
ANISOU  895  C   LEU A 115     1247   1751   1394    313    279   -191       C  
ATOM    896  O   LEU A 115     -10.260   6.332   7.140  1.00 11.59           O  
ANISOU  896  O   LEU A 115     1245   1742   1417    355    266   -204       O  
ATOM    897  CB  LEU A 115      -7.967   4.151   6.377  1.00 10.24           C  
ANISOU  897  CB  LEU A 115     1104   1548   1241    216    206   -169       C  
ATOM    898  CG  LEU A 115      -6.484   4.100   5.982  1.00  9.25           C  
ANISOU  898  CG  LEU A 115     1021   1390   1104    184    164   -170       C  
ATOM    899  CD1 LEU A 115      -6.212   2.959   5.007  1.00  8.64           C  
ANISOU  899  CD1 LEU A 115      919   1315   1048    142    148   -146       C  
ATOM    900  CD2 LEU A 115      -6.029   5.418   5.381  1.00  8.09           C  
ANISOU  900  CD2 LEU A 115      906   1204    965    198    131   -188       C  
ATOM    901  N   GLY A 116     -10.505   4.466   8.386  1.00 11.93           N  
ANISOU  901  N   GLY A 116     1254   1842   1436    306    333   -172       N  
ATOM    902  CA  GLY A 116     -11.946   4.592   8.603  1.00 12.76           C  
ANISOU  902  CA  GLY A 116     1290   1995   1565    345    383   -165       C  
ATOM    903  C   GLY A 116     -12.395   5.872   9.288  1.00 13.55           C  
ANISOU  903  C   GLY A 116     1418   2094   1638    429    413   -194       C  
ATOM    904  O   GLY A 116     -13.571   6.229   9.237  1.00 14.51           O  
ANISOU  904  O   GLY A 116     1475   2253   1785    478    447   -190       O  
ATOM    905  N   THR A 117     -11.459   6.560   9.931  1.00 13.39           N  
ANISOU  905  N   THR A 117     1492   2030   1566    447    399   -225       N  
ATOM    906  CA  THR A 117     -11.722   7.856  10.542  1.00 14.14           C  
ANISOU  906  CA  THR A 117     1638   2104   1629    526    418   -262       C  
ATOM    907  C   THR A 117     -11.983   8.962   9.505  1.00 14.05           C  
ANISOU  907  C   THR A 117     1625   2055   1657    566    379   -275       C  
ATOM    908  O   THR A 117     -12.564  10.005   9.833  1.00 14.61           O  
ANISOU  908  O   THR A 117     1722   2113   1717    647    403   -300       O  
ATOM    909  CB  THR A 117     -10.534   8.267  11.430  1.00 14.18           C  
ANISOU  909  CB  THR A 117     1752   2066   1570    520    396   -298       C  
ATOM    910  OG1 THR A 117     -10.968   9.225  12.404  1.00 16.93           O  
ANISOU  910  OG1 THR A 117     2156   2405   1870    598    436   -336       O  
ATOM    911  CG2 THR A 117      -9.414   8.850  10.586  1.00 12.78           C  
ANISOU  911  CG2 THR A 117     1621   1825   1412    482    319   -313       C  
ATOM    912  N   VAL A 118     -11.544   8.731   8.266  1.00 13.19           N  
ANISOU  912  N   VAL A 118     1495   1927   1589    517    321   -257       N  
ATOM    913  CA  VAL A 118     -11.689   9.691   7.166  1.00 13.24           C  
ANISOU  913  CA  VAL A 118     1508   1895   1627    549    280   -259       C  
ATOM    914  C   VAL A 118     -12.468   9.115   5.974  1.00 12.83           C  
ANISOU  914  C   VAL A 118     1361   1886   1627    537    259   -225       C  
ATOM    915  O   VAL A 118     -13.331   9.784   5.406  1.00 12.74           O  
ANISOU  915  O   VAL A 118     1317   1884   1641    599    252   -221       O  
ATOM    916  CB  VAL A 118     -10.306  10.151   6.677  1.00 12.89           C  
ANISOU  916  CB  VAL A 118     1543   1779   1574    503    224   -270       C  
ATOM    917  CG1 VAL A 118     -10.434  11.066   5.472  1.00 12.57           C  
ANISOU  917  CG1 VAL A 118     1516   1695   1564    532    187   -262       C  
ATOM    918  CG2 VAL A 118      -9.556  10.839   7.824  1.00 13.70           C  
ANISOU  918  CG2 VAL A 118     1739   1837   1628    512    231   -311       C  
ATOM    919  N   PHE A 119     -12.150   7.878   5.607  1.00 12.22           N  
ANISOU  919  N   PHE A 119     1247   1835   1563    460    245   -204       N  
ATOM    920  CA  PHE A 119     -12.814   7.178   4.514  1.00 12.21           C  
ANISOU  920  CA  PHE A 119     1162   1873   1604    434    218   -179       C  
ATOM    921  C   PHE A 119     -13.851   6.186   5.041  1.00 12.85           C  
ANISOU  921  C   PHE A 119     1152   2024   1707    416    264   -163       C  
ATOM    922  O   PHE A 119     -13.920   5.914   6.243  1.00 12.86           O  
ANISOU  922  O   PHE A 119     1161   2042   1684    419    323   -165       O  
ATOM    923  CB  PHE A 119     -11.776   6.405   3.693  1.00 11.58           C  
ANISOU  923  CB  PHE A 119     1108   1766   1524    359    172   -168       C  
ATOM    924  CG  PHE A 119     -10.686   7.264   3.135  1.00 10.84           C  
ANISOU  924  CG  PHE A 119     1095   1610   1415    361    134   -176       C  
ATOM    925  CD1 PHE A 119     -10.866   7.939   1.939  1.00 10.62           C  
ANISOU  925  CD1 PHE A 119     1071   1563   1401    388     93   -167       C  
ATOM    926  CD2 PHE A 119      -9.478   7.403   3.807  1.00 10.75           C  
ANISOU  926  CD2 PHE A 119     1152   1559   1372    335    138   -189       C  
ATOM    927  CE1 PHE A 119      -9.867   8.744   1.425  1.00 10.28           C  
ANISOU  927  CE1 PHE A 119     1103   1458   1344    385     67   -167       C  
ATOM    928  CE2 PHE A 119      -8.470   8.206   3.296  1.00 10.15           C  
ANISOU  928  CE2 PHE A 119     1141   1427   1290    327    106   -194       C  
ATOM    929  CZ  PHE A 119      -8.662   8.878   2.103  1.00 10.04           C  
ANISOU  929  CZ  PHE A 119     1134   1389   1293    349     75   -181       C  
ATOM    930  N   LYS A 120     -14.649   5.634   4.133  1.00 12.98           N  
ANISOU  930  N   LYS A 120     1083   2083   1767    394    238   -147       N  
ATOM    931  CA  LYS A 120     -15.516   4.510   4.476  1.00 13.51           C  
ANISOU  931  CA  LYS A 120     1059   2210   1864    348    274   -128       C  
ATOM    932  C   LYS A 120     -14.646   3.301   4.822  1.00 13.16           C  
ANISOU  932  C   LYS A 120     1058   2139   1802    264    285   -119       C  
ATOM    933  O   LYS A 120     -13.773   2.930   4.039  1.00 12.53           O  
ANISOU  933  O   LYS A 120     1024   2020   1717    222    235   -121       O  
ATOM    934  CB  LYS A 120     -16.427   4.165   3.300  1.00 13.86           C  
ANISOU  934  CB  LYS A 120     1009   2298   1959    328    224   -119       C  
ATOM    935  CG  LYS A 120     -17.293   2.929   3.512  1.00 13.94           C  
ANISOU  935  CG  LYS A 120      921   2365   2012    258    253   -102       C  
ATOM    936  CD  LYS A 120     -18.003   2.549   2.228  1.00 14.79           C  
ANISOU  936  CD  LYS A 120      947   2507   2164    225    182   -102       C  
ATOM    937  CE  LYS A 120     -19.030   1.465   2.460  1.00 15.29           C  
ANISOU  937  CE  LYS A 120      898   2630   2280    152    209    -86       C  
ATOM    938  NZ  LYS A 120     -20.275   1.999   3.089  1.00 15.39           N  
ANISOU  938  NZ  LYS A 120      799   2723   2326    210    263    -75       N  
ATOM    939  N   ASN A 121     -14.873   2.700   5.989  1.00 13.63           N  
ANISOU  939  N   ASN A 121     1108   2221   1850    247    354   -105       N  
ATOM    940  CA  ASN A 121     -14.163   1.476   6.364  1.00 13.59           C  
ANISOU  940  CA  ASN A 121     1143   2191   1829    175    368    -89       C  
ATOM    941  C   ASN A 121     -14.830   0.276   5.699  1.00 14.06           C  
ANISOU  941  C   ASN A 121     1131   2271   1941     98    357    -70       C  
ATOM    942  O   ASN A 121     -15.850  -0.214   6.178  1.00 14.31           O  
ANISOU  942  O   ASN A 121     1086   2349   2003     75    408    -51       O  
ATOM    943  CB  ASN A 121     -14.135   1.299   7.889  1.00 13.91           C  
ANISOU  943  CB  ASN A 121     1214   2243   1827    191    447    -77       C  
ATOM    944  CG  ASN A 121     -13.267   0.126   8.334  1.00 13.75           C  
ANISOU  944  CG  ASN A 121     1254   2192   1781    133    458    -56       C  
ATOM    945  OD1 ASN A 121     -12.887  -0.738   7.534  1.00 13.16           O  
ANISOU  945  OD1 ASN A 121     1182   2089   1729     73    418    -48       O  
ATOM    946  ND2 ASN A 121     -12.948   0.093   9.623  1.00 13.35           N  
ANISOU  946  ND2 ASN A 121     1257   2142   1674    157    511    -47       N  
ATOM    947  N   ARG A 122     -14.249  -0.184   4.593  1.00 14.15           N  
ANISOU  947  N   ARG A 122     1168   2248   1962     55    292    -78       N  
ATOM    948  CA  ARG A 122     -14.770  -1.349   3.867  1.00 14.92           C  
ANISOU  948  CA  ARG A 122     1215   2350   2103    -24    268    -70       C  
ATOM    949  C   ARG A 122     -14.411  -2.669   4.552  1.00 15.28           C  
ANISOU  949  C   ARG A 122     1299   2365   2143    -90    313    -46       C  
ATOM    950  O   ARG A 122     -14.990  -3.702   4.233  1.00 16.18           O  
ANISOU  950  O   ARG A 122     1371   2478   2296   -164    312    -37       O  
ATOM    951  CB  ARG A 122     -14.266  -1.364   2.415  1.00 14.41           C  
ANISOU  951  CB  ARG A 122     1179   2257   2041    -37    184    -90       C  
ATOM    952  CG  ARG A 122     -14.682  -0.137   1.604  1.00 14.46           C  
ANISOU  952  CG  ARG A 122     1152   2289   2052     26    136   -106       C  
ATOM    953  CD  ARG A 122     -13.897  -0.016   0.297  1.00 14.82           C  
ANISOU  953  CD  ARG A 122     1256   2297   2077     26     64   -120       C  
ATOM    954  NE  ARG A 122     -14.183  -1.104  -0.640  1.00 14.27           N  
ANISOU  954  NE  ARG A 122     1167   2226   2028    -42     19   -128       N  
ATOM    955  CZ  ARG A 122     -15.249  -1.177  -1.435  1.00 16.96           C  
ANISOU  955  CZ  ARG A 122     1430   2611   2402    -57    -30   -138       C  
ATOM    956  NH1 ARG A 122     -16.176  -0.221  -1.435  1.00 17.93           N  
ANISOU  956  NH1 ARG A 122     1478   2790   2545      1    -38   -136       N  
ATOM    957  NH2 ARG A 122     -15.394  -2.227  -2.240  1.00 17.81           N  
ANISOU  957  NH2 ARG A 122     1537   2708   2522   -127    -75   -153       N  
ATOM    958  N   GLY A 123     -13.447  -2.629   5.470  1.00 15.50           N  
ANISOU  958  N   GLY A 123     1408   2363   2119    -63    346    -37       N  
ATOM    959  CA  GLY A 123     -13.053  -3.797   6.265  1.00 15.79           C  
ANISOU  959  CA  GLY A 123     1492   2370   2138   -107    393     -8       C  
ATOM    960  C   GLY A 123     -11.827  -4.533   5.735  1.00 15.37           C  
ANISOU  960  C   GLY A 123     1521   2254   2064   -130    352    -11       C  
ATOM    961  O   GLY A 123     -11.487  -4.428   4.558  1.00 14.86           O  
ANISOU  961  O   GLY A 123     1464   2172   2012   -136    290    -34       O  
ATOM    962  N   ALA A 124     -11.159  -5.266   6.625  1.00 15.45           N  
ANISOU  962  N   ALA A 124     1598   2235   2040   -135    390     16       N  
ATOM    963  CA  ALA A 124     -10.043  -6.136   6.255  1.00 15.26           C  
ANISOU  963  CA  ALA A 124     1649   2153   1997   -150    363     20       C  
ATOM    964  C   ALA A 124     -10.588  -7.375   5.555  1.00 15.79           C  
ANISOU  964  C   ALA A 124     1706   2184   2110   -227    358     27       C  
ATOM    965  O   ALA A 124     -11.608  -7.921   5.966  1.00 16.38           O  
ANISOU  965  O   ALA A 124     1738   2269   2218   -278    402     48       O  
ATOM    966  CB  ALA A 124      -9.259  -6.543   7.490  1.00 15.42           C  
ANISOU  966  CB  ALA A 124     1738   2157   1963   -124    404     51       C  
ATOM    967  N   LYS A 125      -9.910  -7.821   4.502  1.00 15.79           N  
ANISOU  967  N   LYS A 125     1747   2141   2112   -238    306      8       N  
ATOM    968  CA  LYS A 125     -10.409  -8.931   3.689  1.00 16.64           C  
ANISOU  968  CA  LYS A 125     1856   2206   2259   -311    289      1       C  
ATOM    969  C   LYS A 125      -9.309  -9.941   3.408  1.00 16.48           C  
ANISOU  969  C   LYS A 125     1934   2114   2215   -308    279      5       C  
ATOM    970  O   LYS A 125      -8.210  -9.571   3.004  1.00 15.92           O  
ANISOU  970  O   LYS A 125     1903   2037   2109   -253    249     -8       O  
ATOM    971  CB  LYS A 125     -10.983  -8.408   2.369  1.00 16.81           C  
ANISOU  971  CB  LYS A 125     1822   2254   2311   -325    223    -40       C  
ATOM    972  CG  LYS A 125     -12.097  -7.392   2.555  1.00 17.38           C  
ANISOU  972  CG  LYS A 125     1793   2401   2411   -315    228    -44       C  
ATOM    973  CD  LYS A 125     -12.617  -6.873   1.232  1.00 18.49           C  
ANISOU  973  CD  LYS A 125     1884   2568   2573   -318    156    -79       C  
ATOM    974  CE  LYS A 125     -13.692  -5.816   1.450  1.00 19.54           C  
ANISOU  974  CE  LYS A 125     1916   2777   2732   -290    161    -80       C  
ATOM    975  NZ  LYS A 125     -14.382  -5.483   0.174  1.00 20.22           N  
ANISOU  975  NZ  LYS A 125     1946   2895   2843   -298     86   -109       N  
ATOM    976  N   LEU A 126      -9.612 -11.213   3.641  1.00 17.08           N  
ANISOU  976  N   LEU A 126     2046   2133   2310   -367    309     26       N  
ATOM    977  CA  LEU A 126      -8.685 -12.301   3.364  1.00 17.17           C  
ANISOU  977  CA  LEU A 126     2158   2066   2302   -362    305     31       C  
ATOM    978  C   LEU A 126      -8.656 -12.564   1.862  1.00 17.34           C  
ANISOU  978  C   LEU A 126     2194   2056   2337   -385    242    -17       C  
ATOM    979  O   LEU A 126      -9.711 -12.698   1.238  1.00 17.51           O  
ANISOU  979  O   LEU A 126     2166   2083   2402   -454    215    -42       O  
ATOM    980  CB  LEU A 126      -9.122 -13.566   4.106  1.00 18.04           C  
ANISOU  980  CB  LEU A 126     2311   2114   2430   -421    361     71       C  
ATOM    981  CG  LEU A 126      -8.286 -14.836   3.905  1.00 18.47           C  
ANISOU  981  CG  LEU A 126     2481   2070   2468   -416    364     81       C  
ATOM    982  CD1 LEU A 126      -6.899 -14.677   4.498  1.00 17.74           C  
ANISOU  982  CD1 LEU A 126     2448   1980   2314   -315    374    105       C  
ATOM    983  CD2 LEU A 126      -9.002 -16.040   4.504  1.00 19.31           C  
ANISOU  983  CD2 LEU A 126     2626   2107   2606   -495    418    119       C  
ATOM    984  N   ASP A 127      -7.453 -12.605   1.287  1.00 16.75           N  
ANISOU  984  N   ASP A 127     2182   1957   2224   -325    217    -31       N  
ATOM    985  CA  ASP A 127      -7.270 -13.025  -0.100  1.00 16.92           C  
ANISOU  985  CA  ASP A 127     2245   1941   2245   -336    168    -74       C  
ATOM    986  C   ASP A 127      -5.957 -13.786  -0.241  1.00 16.82           C  
ANISOU  986  C   ASP A 127     2332   1867   2192   -279    179    -67       C  
ATOM    987  O   ASP A 127      -4.883 -13.193  -0.223  1.00 16.36           O  
ANISOU  987  O   ASP A 127     2279   1840   2098   -203    179    -60       O  
ATOM    988  CB  ASP A 127      -7.305 -11.828  -1.059  1.00 16.41           C  
ANISOU  988  CB  ASP A 127     2126   1939   2170   -308    117   -108       C  
ATOM    989  CG  ASP A 127      -7.391 -12.251  -2.526  1.00 17.22           C  
ANISOU  989  CG  ASP A 127     2267   2010   2267   -329     62   -155       C  
ATOM    990  OD1 ASP A 127      -7.288 -13.463  -2.810  1.00 17.80           O  
ANISOU  990  OD1 ASP A 127     2416   2007   2341   -359     64   -168       O  
ATOM    991  OD2 ASP A 127      -7.553 -11.370  -3.403  1.00 17.78           O  
ANISOU  991  OD2 ASP A 127     2302   2129   2327   -311     18   -181       O  
ATOM    992  N   LYS A 128      -6.053 -15.103  -0.390  1.00 17.69           N  
ANISOU  992  N   LYS A 128     2521   1889   2313   -317    190    -70       N  
ATOM    993  CA  LYS A 128      -4.874 -15.950  -0.497  1.00 17.91           C  
ANISOU  993  CA  LYS A 128     2649   1850   2305   -255    206    -61       C  
ATOM    994  C   LYS A 128      -4.425 -16.165  -1.938  1.00 17.85           C  
ANISOU  994  C   LYS A 128     2693   1815   2276   -231    166   -113       C  
ATOM    995  O   LYS A 128      -3.451 -16.877  -2.180  1.00 17.97           O  
ANISOU  995  O   LYS A 128     2793   1776   2261   -171    181   -112       O  
ATOM    996  CB  LYS A 128      -5.129 -17.301   0.175  1.00 19.23           C  
ANISOU  996  CB  LYS A 128     2895   1922   2489   -295    248    -32       C  
ATOM    997  CG  LYS A 128      -5.345 -17.224   1.675  1.00 19.84           C  
ANISOU  997  CG  LYS A 128     2946   2021   2571   -298    300     29       C  
ATOM    998  CD  LYS A 128      -5.388 -18.616   2.272  1.00 22.16           C  
ANISOU  998  CD  LYS A 128     3339   2208   2872   -324    346     67       C  
ATOM    999  CE  LYS A 128      -5.311 -18.593   3.781  1.00 23.53           C  
ANISOU  999  CE  LYS A 128     3510   2402   3027   -300    402    135       C  
ATOM   1000  NZ  LYS A 128      -5.336 -19.974   4.351  1.00 25.36           N  
ANISOU 1000  NZ  LYS A 128     3852   2522   3262   -321    451    180       N  
ATOM   1001  N   ARG A 129      -5.122 -15.549  -2.890  1.00 17.45           N  
ANISOU 1001  N   ARG A 129     2593   1803   2235   -270    117   -155       N  
ATOM   1002  CA  ARG A 129      -4.821 -15.742  -4.304  1.00 17.77           C  
ANISOU 1002  CA  ARG A 129     2687   1820   2244   -252     76   -207       C  
ATOM   1003  C   ARG A 129      -3.738 -14.800  -4.818  1.00 16.29           C  
ANISOU 1003  C   ARG A 129     2483   1693   2011   -160     74   -205       C  
ATOM   1004  O   ARG A 129      -3.145 -15.055  -5.865  1.00 16.58           O  
ANISOU 1004  O   ARG A 129     2582   1709   2010   -119     62   -236       O  
ATOM   1005  CB  ARG A 129      -6.088 -15.568  -5.145  1.00 18.58           C  
ANISOU 1005  CB  ARG A 129     2750   1938   2372   -335     16   -253       C  
ATOM   1006  CG  ARG A 129      -7.164 -16.585  -4.841  1.00 21.55           C  
ANISOU 1006  CG  ARG A 129     3140   2249   2798   -441     13   -262       C  
ATOM   1007  CD  ARG A 129      -8.425 -16.311  -5.634  1.00 24.98           C  
ANISOU 1007  CD  ARG A 129     3512   2718   3261   -523    -56   -308       C  
ATOM   1008  NE  ARG A 129      -9.124 -15.118  -5.159  1.00 27.41           N  
ANISOU 1008  NE  ARG A 129     3688   3128   3596   -531    -60   -284       N  
ATOM   1009  CZ  ARG A 129     -10.256 -14.647  -5.685  1.00 30.57           C  
ANISOU 1009  CZ  ARG A 129     4005   3585   4026   -586   -118   -312       C  
ATOM   1010  NH1 ARG A 129     -10.838 -15.264  -6.715  1.00 32.07           N  
ANISOU 1010  NH1 ARG A 129     4225   3741   4218   -649   -184   -368       N  
ATOM   1011  NH2 ARG A 129     -10.810 -13.548  -5.179  1.00 31.41           N  
ANISOU 1011  NH2 ARG A 129     3999   3781   4155   -575   -112   -286       N  
ATOM   1012  N   LEU A 130      -3.482 -13.712  -4.096  1.00 14.87           N  
ANISOU 1012  N   LEU A 130     2225   1588   1835   -131     89   -171       N  
ATOM   1013  CA  LEU A 130      -2.545 -12.703  -4.566  1.00 13.76           C  
ANISOU 1013  CA  LEU A 130     2059   1508   1662    -62     86   -167       C  
ATOM   1014  C   LEU A 130      -1.120 -13.151  -4.284  1.00 13.16           C  
ANISOU 1014  C   LEU A 130     2027   1414   1557     18    126   -142       C  
ATOM   1015  O   LEU A 130      -0.798 -13.546  -3.164  1.00 12.65           O  
ANISOU 1015  O   LEU A 130     1967   1336   1501     33    156   -107       O  
ATOM   1016  CB  LEU A 130      -2.816 -11.350  -3.906  1.00 13.34           C  
ANISOU 1016  CB  LEU A 130     1910   1531   1626    -65     84   -145       C  
ATOM   1017  CG  LEU A 130      -4.221 -10.789  -4.136  1.00 14.16           C  
ANISOU 1017  CG  LEU A 130     1955   1664   1759   -128     47   -165       C  
ATOM   1018  CD1 LEU A 130      -4.424  -9.498  -3.342  1.00 14.17           C  
ANISOU 1018  CD1 LEU A 130     1876   1732   1775   -117     54   -141       C  
ATOM   1019  CD2 LEU A 130      -4.479 -10.560  -5.614  1.00 15.25           C  
ANISOU 1019  CD2 LEU A 130     2109   1809   1876   -130     -1   -204       C  
ATOM   1020  N   TYR A 131      -0.271 -13.076  -5.305  1.00 12.41           N  
ANISOU 1020  N   TYR A 131     1964   1325   1425     73    126   -158       N  
ATOM   1021  CA  TYR A 131       1.111 -13.520  -5.186  1.00 12.23           C  
ANISOU 1021  CA  TYR A 131     1975   1295   1377    157    164   -136       C  
ATOM   1022  C   TYR A 131       1.906 -12.700  -4.181  1.00 11.35           C  
ANISOU 1022  C   TYR A 131     1790   1250   1274    193    182    -92       C  
ATOM   1023  O   TYR A 131       2.802 -13.228  -3.527  1.00 11.52           O  
ANISOU 1023  O   TYR A 131     1825   1264   1287    249    208    -63       O  
ATOM   1024  CB  TYR A 131       1.821 -13.513  -6.548  1.00 12.37           C  
ANISOU 1024  CB  TYR A 131     2033   1317   1352    211    169   -161       C  
ATOM   1025  CG  TYR A 131       2.169 -12.139  -7.088  1.00 11.73           C  
ANISOU 1025  CG  TYR A 131     1883   1316   1258    224    163   -153       C  
ATOM   1026  CD1 TYR A 131       3.278 -11.436  -6.618  1.00 11.06           C  
ANISOU 1026  CD1 TYR A 131     1737   1290   1176    271    191   -115       C  
ATOM   1027  CD2 TYR A 131       1.393 -11.545  -8.083  1.00 12.31           C  
ANISOU 1027  CD2 TYR A 131     1956   1403   1318    187    127   -183       C  
ATOM   1028  CE1 TYR A 131       3.595 -10.180  -7.117  1.00 10.36           C  
ANISOU 1028  CE1 TYR A 131     1592   1264   1081    272    189   -106       C  
ATOM   1029  CE2 TYR A 131       1.704 -10.297  -8.586  1.00 10.64           C  
ANISOU 1029  CE2 TYR A 131     1694   1255   1094    200    126   -170       C  
ATOM   1030  CZ  TYR A 131       2.807  -9.621  -8.106  1.00 10.95           C  
ANISOU 1030  CZ  TYR A 131     1677   1342   1139    239    160   -131       C  
ATOM   1031  OH  TYR A 131       3.113  -8.375  -8.611  1.00 11.35           O  
ANISOU 1031  OH  TYR A 131     1685   1445   1182    243    163   -116       O  
ATOM   1032  N   ILE A 132       1.588 -11.412  -4.054  1.00 10.56           N  
ANISOU 1032  N   ILE A 132     1613   1213   1187    164    163    -88       N  
ATOM   1033  CA  ILE A 132       2.343 -10.553  -3.155  1.00  9.79           C  
ANISOU 1033  CA  ILE A 132     1449   1175   1095    189    171    -56       C  
ATOM   1034  C   ILE A 132       2.101 -10.982  -1.707  1.00  9.71           C  
ANISOU 1034  C   ILE A 132     1437   1152   1098    179    180    -30       C  
ATOM   1035  O   ILE A 132       2.941 -10.741  -0.839  1.00  9.48           O  
ANISOU 1035  O   ILE A 132     1380   1160   1063    217    187     -2       O  
ATOM   1036  CB  ILE A 132       2.016  -9.047  -3.370  1.00  9.54           C  
ANISOU 1036  CB  ILE A 132     1351   1199   1074    159    149    -61       C  
ATOM   1037  CG1 ILE A 132       3.126  -8.166  -2.781  1.00  9.16           C  
ANISOU 1037  CG1 ILE A 132     1247   1207   1027    189    157    -35       C  
ATOM   1038  CG2 ILE A 132       0.650  -8.690  -2.769  1.00  9.02           C  
ANISOU 1038  CG2 ILE A 132     1260   1132   1034     98    130    -69       C  
ATOM   1039  CD1 ILE A 132       4.495  -8.406  -3.376  1.00  8.87           C  
ANISOU 1039  CD1 ILE A 132     1211   1187    971    249    181    -23       C  
ATOM   1040  N   LEU A 133       0.969 -11.646  -1.470  1.00  9.65           N  
ANISOU 1040  N   LEU A 133     1463   1097   1107    127    179    -38       N  
ATOM   1041  CA  LEU A 133       0.624 -12.195  -0.159  1.00 10.05           C  
ANISOU 1041  CA  LEU A 133     1526   1126   1165    114    197     -9       C  
ATOM   1042  C   LEU A 133       1.007 -13.669   0.016  1.00 10.73           C  
ANISOU 1042  C   LEU A 133     1699   1139   1241    145    223      7       C  
ATOM   1043  O   LEU A 133       1.516 -14.056   1.063  1.00 11.39           O  
ANISOU 1043  O   LEU A 133     1798   1219   1310    183    242     46       O  
ATOM   1044  CB  LEU A 133      -0.876 -12.033   0.090  1.00 10.06           C  
ANISOU 1044  CB  LEU A 133     1504   1120   1196     34    191    -20       C  
ATOM   1045  CG  LEU A 133      -1.387 -10.596   0.051  1.00  9.54           C  
ANISOU 1045  CG  LEU A 133     1360   1123   1143     12    170    -33       C  
ATOM   1046  CD1 LEU A 133      -2.896 -10.561   0.234  1.00  8.60           C  
ANISOU 1046  CD1 LEU A 133     1211   1000   1057    -59    167    -42       C  
ATOM   1047  CD2 LEU A 133      -0.685  -9.761   1.111  1.00  8.87           C  
ANISOU 1047  CD2 LEU A 133     1237   1090   1042     49    176     -9       C  
ATOM   1048  N   ASN A 134       0.755 -14.496  -0.992  1.00 11.36           N  
ANISOU 1048  N   ASN A 134     1842   1153   1320    132    221    -22       N  
ATOM   1049  CA  ASN A 134       1.008 -15.939  -0.859  1.00 12.10           C  
ANISOU 1049  CA  ASN A 134     2034   1158   1407    158    246    -10       C  
ATOM   1050  C   ASN A 134       2.436 -16.393  -1.202  1.00 12.58           C  
ANISOU 1050  C   ASN A 134     2135   1212   1435    263    263      0       C  
ATOM   1051  O   ASN A 134       2.769 -17.564  -1.017  1.00 13.37           O  
ANISOU 1051  O   ASN A 134     2320   1236   1523    304    287     15       O  
ATOM   1052  CB  ASN A 134      -0.041 -16.760  -1.625  1.00 12.54           C  
ANISOU 1052  CB  ASN A 134     2154   1130   1482     84    236    -48       C  
ATOM   1053  CG  ASN A 134       0.111 -16.685  -3.146  1.00 13.28           C  
ANISOU 1053  CG  ASN A 134     2271   1217   1556     95    210   -101       C  
ATOM   1054  OD1 ASN A 134       1.219 -16.625  -3.683  1.00 13.16           O  
ANISOU 1054  OD1 ASN A 134     2272   1220   1508    178    221   -103       O  
ATOM   1055  ND2 ASN A 134      -1.021 -16.730  -3.846  1.00 13.39           N  
ANISOU 1055  ND2 ASN A 134     2290   1209   1589     12    177   -143       N  
ATOM   1056  N   SER A 135       3.274 -15.477  -1.685  1.00 12.41           N  
ANISOU 1056  N   SER A 135     2049   1266   1398    309    255     -5       N  
ATOM   1057  CA  SER A 135       4.662 -15.812  -2.034  1.00 13.06           C  
ANISOU 1057  CA  SER A 135     2147   1361   1453    412    276      7       C  
ATOM   1058  C   SER A 135       5.685 -14.969  -1.290  1.00 12.53           C  
ANISOU 1058  C   SER A 135     1990   1388   1383    461    274     43       C  
ATOM   1059  O   SER A 135       6.880 -15.013  -1.603  1.00 12.79           O  
ANISOU 1059  O   SER A 135     2004   1457   1401    541    289     54       O  
ATOM   1060  CB  SER A 135       4.878 -15.688  -3.546  1.00 13.15           C  
ANISOU 1060  CB  SER A 135     2178   1373   1447    428    278    -34       C  
ATOM   1061  OG  SER A 135       4.049 -16.604  -4.231  1.00 14.07           O  
ANISOU 1061  OG  SER A 135     2391   1396   1559    390    273    -73       O  
ATOM   1062  N   SER A 136       5.222 -14.217  -0.298  1.00 12.07           N  
ANISOU 1062  N   SER A 136     1875   1372   1339    412    254     58       N  
ATOM   1063  CA  SER A 136       6.099 -13.395   0.510  1.00 11.70           C  
ANISOU 1063  CA  SER A 136     1747   1409   1287    445    241     85       C  
ATOM   1064  C   SER A 136       6.350 -14.105   1.834  1.00 11.95           C  
ANISOU 1064  C   SER A 136     1810   1428   1304    486    245    127       C  
ATOM   1065  O   SER A 136       5.415 -14.623   2.456  1.00 11.33           O  
ANISOU 1065  O   SER A 136     1782   1295   1226    445    254    136       O  
ATOM   1066  CB  SER A 136       5.497 -11.996   0.718  1.00 10.96           C  
ANISOU 1066  CB  SER A 136     1582   1372   1212    374    215     70       C  
ATOM   1067  OG  SER A 136       4.166 -12.029   1.226  1.00 11.13           O  
ANISOU 1067  OG  SER A 136     1625   1359   1245    306    212     64       O  
ATOM   1068  N   LYS A 137       7.611 -14.165   2.254  1.00 12.49           N  
ANISOU 1068  N   LYS A 137     1844   1546   1355    568    240    155       N  
ATOM   1069  CA  LYS A 137       7.938 -14.803   3.538  1.00 13.43           C  
ANISOU 1069  CA  LYS A 137     1992   1661   1449    620    237    199       C  
ATOM   1070  C   LYS A 137       7.409 -14.005   4.728  1.00 12.84           C  
ANISOU 1070  C   LYS A 137     1882   1630   1367    568    211    207       C  
ATOM   1071  O   LYS A 137       6.741 -14.567   5.588  1.00 12.97           O  
ANISOU 1071  O   LYS A 137     1958   1602   1367    555    224    231       O  
ATOM   1072  CB  LYS A 137       9.440 -15.059   3.705  1.00 14.23           C  
ANISOU 1072  CB  LYS A 137     2056   1816   1533    728    229    228       C  
ATOM   1073  CG  LYS A 137       9.741 -16.100   4.791  1.00 15.99           C  
ANISOU 1073  CG  LYS A 137     2344   2008   1723    804    231    277       C  
ATOM   1074  CD  LYS A 137      11.221 -16.362   4.934  1.00 17.91           C  
ANISOU 1074  CD  LYS A 137     2540   2314   1951    921    218    306       C  
ATOM   1075  CE  LYS A 137      11.521 -17.737   5.516  1.00 19.95           C  
ANISOU 1075  CE  LYS A 137     2895   2508   2178   1020    236    354       C  
ATOM   1076  NZ  LYS A 137      10.600 -18.142   6.612  1.00 19.57           N  
ANISOU 1076  NZ  LYS A 137     2929   2402   2105    983    238    382       N  
ATOM   1077  N   PRO A 138       7.695 -12.692   4.786  1.00 12.67           N  
ANISOU 1077  N   PRO A 138     1770   1689   1354    538    180    188       N  
ATOM   1078  CA  PRO A 138       7.141 -11.961   5.929  1.00 12.52           C  
ANISOU 1078  CA  PRO A 138     1733   1704   1321    495    158    190       C  
ATOM   1079  C   PRO A 138       5.622 -11.839   5.883  1.00 12.07           C  
ANISOU 1079  C   PRO A 138     1709   1597   1279    413    180    172       C  
ATOM   1080  O   PRO A 138       5.012 -11.981   4.816  1.00 11.51           O  
ANISOU 1080  O   PRO A 138     1652   1483   1237    374    197    148       O  
ATOM   1081  CB  PRO A 138       7.778 -10.577   5.805  1.00 12.56           C  
ANISOU 1081  CB  PRO A 138     1642   1791   1339    475    120    166       C  
ATOM   1082  CG  PRO A 138       8.143 -10.445   4.375  1.00 12.25           C  
ANISOU 1082  CG  PRO A 138     1575   1748   1330    473    135    147       C  
ATOM   1083  CD  PRO A 138       8.494 -11.818   3.907  1.00 12.57           C  
ANISOU 1083  CD  PRO A 138     1676   1738   1363    540    166    167       C  
ATOM   1084  N   THR A 139       5.021 -11.599   7.044  1.00 12.11           N  
ANISOU 1084  N   THR A 139     1726   1614   1262    392    180    185       N  
ATOM   1085  CA  THR A 139       3.634 -11.151   7.106  1.00 11.64           C  
ANISOU 1085  CA  THR A 139     1667   1537   1221    315    198    166       C  
ATOM   1086  C   THR A 139       3.457  -9.995   6.132  1.00 10.97           C  
ANISOU 1086  C   THR A 139     1519   1480   1170    272    178    122       C  
ATOM   1087  O   THR A 139       4.304  -9.094   6.072  1.00 10.82           O  
ANISOU 1087  O   THR A 139     1447   1516   1149    288    146    109       O  
ATOM   1088  CB  THR A 139       3.264 -10.687   8.520  1.00 11.80           C  
ANISOU 1088  CB  THR A 139     1689   1591   1203    312    197    180       C  
ATOM   1089  OG1 THR A 139       3.509 -11.755   9.439  1.00 11.72           O  
ANISOU 1089  OG1 THR A 139     1745   1556   1152    360    216    229       O  
ATOM   1090  CG2 THR A 139       1.797 -10.281   8.592  1.00 11.22           C  
ANISOU 1090  CG2 THR A 139     1610   1504   1150    242    226    164       C  
ATOM   1091  N   ALA A 140       2.381 -10.033   5.348  1.00 10.52           N  
ANISOU 1091  N   ALA A 140     1466   1385   1144    218    195    101       N  
ATOM   1092  CA  ALA A 140       2.137  -9.006   4.341  1.00  9.90           C  
ANISOU 1092  CA  ALA A 140     1339   1328   1094    184    177     65       C  
ATOM   1093  C   ALA A 140       0.704  -8.499   4.380  1.00  9.98           C  
ANISOU 1093  C   ALA A 140     1334   1333   1126    125    185     47       C  
ATOM   1094  O   ALA A 140      -0.217  -9.243   4.728  1.00 10.49           O  
ANISOU 1094  O   ALA A 140     1426   1363   1196     96    212     59       O  
ATOM   1095  CB  ALA A 140       2.461  -9.532   2.962  1.00  9.90           C  
ANISOU 1095  CB  ALA A 140     1356   1296   1109    192    178     52       C  
ATOM   1096  N   VAL A 141       0.536  -7.222   4.034  1.00  9.38           N  
ANISOU 1096  N   VAL A 141     1209   1292   1062    108    164     22       N  
ATOM   1097  CA  VAL A 141      -0.780  -6.651   3.793  1.00  9.10           C  
ANISOU 1097  CA  VAL A 141     1149   1257   1051     65    167      2       C  
ATOM   1098  C   VAL A 141      -0.760  -5.813   2.520  1.00  8.74           C  
ANISOU 1098  C   VAL A 141     1076   1220   1024     56    141    -23       C  
ATOM   1099  O   VAL A 141       0.250  -5.210   2.171  1.00  8.53           O  
ANISOU 1099  O   VAL A 141     1039   1212    991     77    125    -26       O  
ATOM   1100  CB  VAL A 141      -1.295  -5.811   4.989  1.00  8.96           C  
ANISOU 1100  CB  VAL A 141     1111   1272   1020     63    176      2       C  
ATOM   1101  CG1 VAL A 141      -1.490  -6.700   6.195  1.00  9.16           C  
ANISOU 1101  CG1 VAL A 141     1171   1288   1020     71    209     32       C  
ATOM   1102  CG2 VAL A 141      -0.354  -4.669   5.310  1.00  9.68           C  
ANISOU 1102  CG2 VAL A 141     1186   1400   1094     88    147    -11       C  
ATOM   1103  N   LEU A 142      -1.880  -5.818   1.813  1.00  8.58           N  
ANISOU 1103  N   LEU A 142     1045   1188   1028     22    138    -39       N  
ATOM   1104  CA  LEU A 142      -2.033  -5.007   0.628  1.00  8.46           C  
ANISOU 1104  CA  LEU A 142     1010   1181   1023     18    112    -59       C  
ATOM   1105  C   LEU A 142      -3.037  -3.932   0.977  1.00  8.18           C  
ANISOU 1105  C   LEU A 142      934   1170   1003      7    107    -69       C  
ATOM   1106  O   LEU A 142      -4.191  -4.233   1.286  1.00  8.36           O  
ANISOU 1106  O   LEU A 142      938   1195   1044    -17    118    -71       O  
ATOM   1107  CB  LEU A 142      -2.512  -5.867  -0.533  1.00  8.56           C  
ANISOU 1107  CB  LEU A 142     1045   1163   1044     -3    101    -72       C  
ATOM   1108  CG  LEU A 142      -2.600  -5.223  -1.915  1.00  9.11           C  
ANISOU 1108  CG  LEU A 142     1110   1240   1111      0     72    -91       C  
ATOM   1109  CD1 LEU A 142      -2.747  -6.296  -2.978  1.00  9.67           C  
ANISOU 1109  CD1 LEU A 142     1223   1276   1174    -13     61   -107       C  
ATOM   1110  CD2 LEU A 142      -3.752  -4.227  -2.006  1.00  8.29           C  
ANISOU 1110  CD2 LEU A 142      962   1162   1027    -15     52   -102       C  
ATOM   1111  N   ILE A 143      -2.597  -2.679   0.950  1.00  8.06           N  
ANISOU 1111  N   ILE A 143      906   1173    983     26     94    -75       N  
ATOM   1112  CA  ILE A 143      -3.465  -1.566   1.320  1.00  8.29           C  
ANISOU 1112  CA  ILE A 143      907   1219   1022     30     91    -86       C  
ATOM   1113  C   ILE A 143      -4.066  -0.912   0.079  1.00  8.49           C  
ANISOU 1113  C   ILE A 143      919   1245   1063     31     65    -97       C  
ATOM   1114  O   ILE A 143      -3.341  -0.460  -0.825  1.00  7.70           O  
ANISOU 1114  O   ILE A 143      836   1135    954     39     49    -95       O  
ATOM   1115  CB  ILE A 143      -2.727  -0.503   2.164  1.00  8.39           C  
ANISOU 1115  CB  ILE A 143      926   1240   1020     49     90    -90       C  
ATOM   1116  CG1 ILE A 143      -2.037  -1.153   3.365  1.00  7.84           C  
ANISOU 1116  CG1 ILE A 143      874   1179    926     55    105    -79       C  
ATOM   1117  CG2 ILE A 143      -3.713   0.565   2.643  1.00  9.03           C  
ANISOU 1117  CG2 ILE A 143      991   1331   1108     62     94   -105       C  
ATOM   1118  CD1 ILE A 143      -1.200  -0.184   4.196  1.00  7.26           C  
ANISOU 1118  CD1 ILE A 143      809   1116    832     68     91    -89       C  
ATOM   1119  N   GLU A 144      -5.400  -0.899   0.037  1.00  8.74           N  
ANISOU 1119  N   GLU A 144      917   1289   1114     23     63   -104       N  
ATOM   1120  CA  GLU A 144      -6.151  -0.132  -0.942  1.00  9.34           C  
ANISOU 1120  CA  GLU A 144      972   1375   1202     36     33   -113       C  
ATOM   1121  C   GLU A 144      -6.676   1.105  -0.205  1.00  9.16           C  
ANISOU 1121  C   GLU A 144      929   1365   1186     68     43   -117       C  
ATOM   1122  O   GLU A 144      -7.776   1.083   0.357  1.00  8.89           O  
ANISOU 1122  O   GLU A 144      853   1356   1169     72     58   -120       O  
ATOM   1123  CB  GLU A 144      -7.308  -0.972  -1.499  1.00 10.22           C  
ANISOU 1123  CB  GLU A 144     1049   1499   1334      8     17   -120       C  
ATOM   1124  CG  GLU A 144      -6.866  -2.297  -2.138  1.00 12.19           C  
ANISOU 1124  CG  GLU A 144     1332   1724   1575    -26      8   -123       C  
ATOM   1125  CD  GLU A 144      -6.921  -2.296  -3.660  1.00 15.48           C  
ANISOU 1125  CD  GLU A 144     1768   2137   1978    -23    -36   -136       C  
ATOM   1126  OE1 GLU A 144      -7.473  -1.349  -4.252  1.00 17.66           O  
ANISOU 1126  OE1 GLU A 144     2023   2434   2254      1    -66   -139       O  
ATOM   1127  OE2 GLU A 144      -6.426  -3.266  -4.266  1.00 18.52           O  
ANISOU 1127  OE2 GLU A 144     2195   2496   2346    -40    -42   -143       O  
ATOM   1128  N   SER A 145      -5.875   2.170  -0.214  1.00  8.88           N  
ANISOU 1128  N   SER A 145      925   1311   1136     90     38   -117       N  
ATOM   1129  CA  SER A 145      -6.095   3.344   0.654  1.00  9.31           C  
ANISOU 1129  CA  SER A 145      984   1362   1191    121     51   -126       C  
ATOM   1130  C   SER A 145      -7.418   4.060   0.409  1.00  9.72           C  
ANISOU 1130  C   SER A 145     1003   1430   1261    158     44   -131       C  
ATOM   1131  O   SER A 145      -8.097   4.462   1.361  1.00 10.40           O  
ANISOU 1131  O   SER A 145     1071   1530   1349    185     70   -141       O  
ATOM   1132  CB  SER A 145      -4.949   4.352   0.493  1.00  9.13           C  
ANISOU 1132  CB  SER A 145     1007   1306   1156    125     40   -127       C  
ATOM   1133  OG  SER A 145      -3.732   3.849   1.018  1.00  9.10           O  
ANISOU 1133  OG  SER A 145     1020   1300   1139     99     46   -124       O  
ATOM   1134  N   PHE A 146      -7.749   4.248  -0.865  1.00  9.39           N  
ANISOU 1134  N   PHE A 146      955   1388   1225    167     11   -125       N  
ATOM   1135  CA  PHE A 146      -9.001   4.871  -1.296  1.00  9.96           C  
ANISOU 1135  CA  PHE A 146      989   1481   1313    210     -7   -125       C  
ATOM   1136  C   PHE A 146      -9.187   4.613  -2.796  1.00 10.06           C  
ANISOU 1136  C   PHE A 146     1000   1502   1322    206    -53   -117       C  
ATOM   1137  O   PHE A 146      -8.305   4.025  -3.427  1.00  9.64           O  
ANISOU 1137  O   PHE A 146      982   1431   1251    173    -63   -112       O  
ATOM   1138  CB  PHE A 146      -9.012   6.379  -0.996  1.00 10.27           C  
ANISOU 1138  CB  PHE A 146     1061   1491   1348    265     -1   -128       C  
ATOM   1139  CG  PHE A 146      -7.890   7.149  -1.651  1.00  9.61           C  
ANISOU 1139  CG  PHE A 146     1047   1355   1248    262    -15   -118       C  
ATOM   1140  CD1 PHE A 146      -8.020   7.629  -2.952  1.00 10.39           C  
ANISOU 1140  CD1 PHE A 146     1166   1443   1340    285    -48   -100       C  
ATOM   1141  CD2 PHE A 146      -6.709   7.398  -0.967  1.00  8.89           C  
ANISOU 1141  CD2 PHE A 146     1002   1231   1147    234      3   -125       C  
ATOM   1142  CE1 PHE A 146      -6.985   8.329  -3.558  1.00  9.63           C  
ANISOU 1142  CE1 PHE A 146     1134   1297   1229    277    -51    -83       C  
ATOM   1143  CE2 PHE A 146      -5.676   8.100  -1.563  1.00  8.35           C  
ANISOU 1143  CE2 PHE A 146      985   1116   1070    220     -6   -112       C  
ATOM   1144  CZ  PHE A 146      -5.812   8.564  -2.857  1.00  8.93           C  
ANISOU 1144  CZ  PHE A 146     1079   1174   1139    240    -27    -89       C  
ATOM   1145  N   PHE A 147     -10.320   5.040  -3.358  1.00 10.54           N  
ANISOU 1145  N   PHE A 147     1020   1591   1395    245    -83   -115       N  
ATOM   1146  CA  PHE A 147     -10.609   4.812  -4.781  1.00 11.03           C  
ANISOU 1146  CA  PHE A 147     1081   1666   1443    246   -137   -110       C  
ATOM   1147  C   PHE A 147     -10.029   5.913  -5.668  1.00 11.27           C  
ANISOU 1147  C   PHE A 147     1180   1659   1444    289   -155    -90       C  
ATOM   1148  O   PHE A 147     -10.328   7.093  -5.496  1.00 11.77           O  
ANISOU 1148  O   PHE A 147     1256   1706   1511    345   -152    -81       O  
ATOM   1149  CB  PHE A 147     -12.117   4.664  -5.021  1.00 11.85           C  
ANISOU 1149  CB  PHE A 147     1100   1830   1574    266   -172   -116       C  
ATOM   1150  CG  PHE A 147     -12.655   3.298  -4.678  1.00 12.08           C  
ANISOU 1150  CG  PHE A 147     1067   1895   1630    201   -168   -131       C  
ATOM   1151  CD1 PHE A 147     -13.151   2.457  -5.667  1.00 12.21           C  
ANISOU 1151  CD1 PHE A 147     1056   1937   1646    165   -223   -143       C  
ATOM   1152  CD2 PHE A 147     -12.641   2.844  -3.367  1.00 12.33           C  
ANISOU 1152  CD2 PHE A 147     1075   1927   1683    173   -110   -134       C  
ATOM   1153  CE1 PHE A 147     -13.646   1.194  -5.351  1.00 12.37           C  
ANISOU 1153  CE1 PHE A 147     1026   1978   1696     95   -220   -157       C  
ATOM   1154  CE2 PHE A 147     -13.126   1.575  -3.043  1.00 12.13           C  
ANISOU 1154  CE2 PHE A 147     1000   1925   1684    107   -100   -141       C  
ATOM   1155  CZ  PHE A 147     -13.631   0.753  -4.038  1.00 12.25           C  
ANISOU 1155  CZ  PHE A 147      988   1959   1708     65   -155   -153       C  
ATOM   1156  N   CYS A 148      -9.201   5.524  -6.629  1.00 11.43           N  
ANISOU 1156  N   CYS A 148     1250   1662   1432    264   -169    -82       N  
ATOM   1157  CA  CYS A 148      -8.591   6.490  -7.542  1.00 11.77           C  
ANISOU 1157  CA  CYS A 148     1361   1668   1442    297   -178    -56       C  
ATOM   1158  C   CYS A 148      -9.579   7.032  -8.586  1.00 12.35           C  
ANISOU 1158  C   CYS A 148     1431   1764   1498    355   -231    -43       C  
ATOM   1159  O   CYS A 148      -9.250   7.969  -9.316  1.00 13.13           O  
ANISOU 1159  O   CYS A 148     1591   1829   1568    394   -237    -14       O  
ATOM   1160  CB  CYS A 148      -7.379   5.874  -8.237  1.00 11.43           C  
ANISOU 1160  CB  CYS A 148     1370   1607   1367    258   -166    -48       C  
ATOM   1161  SG  CYS A 148      -7.808   4.741  -9.563  1.00 12.98           S  
ANISOU 1161  SG  CYS A 148     1567   1839   1525    248   -217    -60       S  
ATOM   1162  N   ASP A 149     -10.778   6.451  -8.654  1.00 12.73           N  
ANISOU 1162  N   ASP A 149     1406   1869   1563    360   -272    -62       N  
ATOM   1163  CA  ASP A 149     -11.806   6.885  -9.608  1.00 13.40           C  
ANISOU 1163  CA  ASP A 149     1471   1990   1632    418   -335    -52       C  
ATOM   1164  C   ASP A 149     -13.007   7.544  -8.915  1.00 14.28           C  
ANISOU 1164  C   ASP A 149     1507   2134   1784    475   -340    -54       C  
ATOM   1165  O   ASP A 149     -14.066   7.698  -9.520  1.00 14.72           O  
ANISOU 1165  O   ASP A 149     1513   2241   1840    521   -397    -51       O  
ATOM   1166  CB  ASP A 149     -12.255   5.704 -10.486  1.00 13.49           C  
ANISOU 1166  CB  ASP A 149     1454   2049   1624    381   -393    -74       C  
ATOM   1167  CG  ASP A 149     -12.899   4.576  -9.689  1.00 13.06           C  
ANISOU 1167  CG  ASP A 149     1310   2033   1618    319   -390   -107       C  
ATOM   1168  OD1 ASP A 149     -12.788   4.568  -8.440  1.00 12.07           O  
ANISOU 1168  OD1 ASP A 149     1156   1897   1532    301   -332   -110       O  
ATOM   1169  OD2 ASP A 149     -13.516   3.685 -10.315  1.00 12.43           O  
ANISOU 1169  OD2 ASP A 149     1194   1993   1535    285   -445   -130       O  
ATOM   1170  N   ASN A 150     -12.825   7.937  -7.654  1.00 14.19           N  
ANISOU 1170  N   ASN A 150     1488   2098   1805    476   -280    -59       N  
ATOM   1171  CA  ASN A 150     -13.864   8.604  -6.875  1.00 15.10           C  
ANISOU 1171  CA  ASN A 150     1541   2240   1955    538   -268    -61       C  
ATOM   1172  C   ASN A 150     -13.370   9.977  -6.409  1.00 15.46           C  
ANISOU 1172  C   ASN A 150     1664   2215   1994    595   -229    -47       C  
ATOM   1173  O   ASN A 150     -12.464  10.068  -5.582  1.00 14.90           O  
ANISOU 1173  O   ASN A 150     1640   2096   1926    558   -179    -56       O  
ATOM   1174  CB  ASN A 150     -14.282   7.736  -5.677  1.00 14.89           C  
ANISOU 1174  CB  ASN A 150     1434   2253   1970    490   -227    -86       C  
ATOM   1175  CG  ASN A 150     -15.435   8.348  -4.882  1.00 15.74           C  
ANISOU 1175  CG  ASN A 150     1467   2401   2113    559   -206    -88       C  
ATOM   1176  OD1 ASN A 150     -15.243   9.303  -4.131  1.00 16.43           O  
ANISOU 1176  OD1 ASN A 150     1597   2448   2199    610   -162    -87       O  
ATOM   1177  ND2 ASN A 150     -16.636   7.803  -5.054  1.00 15.29           N  
ANISOU 1177  ND2 ASN A 150     1298   2426   2087    560   -236    -92       N  
ATOM   1178  N   LYS A 151     -13.971  11.035  -6.953  1.00 16.71           N  
ANISOU 1178  N   LYS A 151     1839   2365   2143    686   -257    -25       N  
ATOM   1179  CA  LYS A 151     -13.580  12.423  -6.660  1.00 17.36           C  
ANISOU 1179  CA  LYS A 151     2011   2367   2219    746   -226    -10       C  
ATOM   1180  C   LYS A 151     -13.518  12.710  -5.170  1.00 16.84           C  
ANISOU 1180  C   LYS A 151     1940   2277   2180    746   -165    -38       C  
ATOM   1181  O   LYS A 151     -12.547  13.277  -4.674  1.00 16.20           O  
ANISOU 1181  O   LYS A 151     1944   2120   2092    722   -130    -42       O  
ATOM   1182  CB  LYS A 151     -14.586  13.401  -7.273  1.00 18.73           C  
ANISOU 1182  CB  LYS A 151     2181   2549   2387    862   -264     15       C  
ATOM   1183  CG  LYS A 151     -14.536  13.516  -8.781  1.00 20.97           C  
ANISOU 1183  CG  LYS A 151     2507   2834   2627    885   -325     51       C  
ATOM   1184  CD  LYS A 151     -13.415  14.448  -9.248  1.00 23.22           C  
ANISOU 1184  CD  LYS A 151     2930   3014   2879    885   -302     84       C  
ATOM   1185  CE  LYS A 151     -13.698  14.993 -10.643  1.00 24.71           C  
ANISOU 1185  CE  LYS A 151     3171   3198   3019    956   -357    131       C  
ATOM   1186  NZ  LYS A 151     -14.058  13.911 -11.602  1.00 26.54           N  
ANISOU 1186  NZ  LYS A 151     3345   3517   3222    929   -420    126       N  
ATOM   1187  N   GLU A 152     -14.579  12.319  -4.476  1.00 17.13           N  
ANISOU 1187  N   GLU A 152     1878   2385   2247    771   -154    -56       N  
ATOM   1188  CA  GLU A 152     -14.752  12.632  -3.062  1.00 17.32           C  
ANISOU 1188  CA  GLU A 152     1894   2398   2287    793    -93    -81       C  
ATOM   1189  C   GLU A 152     -13.628  12.002  -2.237  1.00 15.79           C  
ANISOU 1189  C   GLU A 152     1739   2176   2086    697    -54   -102       C  
ATOM   1190  O   GLU A 152     -13.057  12.658  -1.372  1.00 15.77           O  
ANISOU 1190  O   GLU A 152     1804   2114   2074    703    -17   -120       O  
ATOM   1191  CB  GLU A 152     -16.134  12.171  -2.570  1.00 18.01           C  
ANISOU 1191  CB  GLU A 152     1853   2582   2407    831    -82    -90       C  
ATOM   1192  CG  GLU A 152     -17.328  12.992  -3.108  1.00 20.72           C  
ANISOU 1192  CG  GLU A 152     2149   2960   2762    951   -112    -72       C  
ATOM   1193  CD  GLU A 152     -17.529  12.909  -4.625  1.00 23.26           C  
ANISOU 1193  CD  GLU A 152     2463   3305   3071    961   -194    -44       C  
ATOM   1194  OE1 GLU A 152     -17.195  11.862  -5.243  1.00 23.34           O  
ANISOU 1194  OE1 GLU A 152     2450   3343   3074    872   -230    -45       O  
ATOM   1195  OE2 GLU A 152     -18.028  13.903  -5.204  1.00 24.46           O  
ANISOU 1195  OE2 GLU A 152     2636   3443   3213   1066   -224    -21       O  
ATOM   1196  N   ASP A 153     -13.305  10.739  -2.524  1.00 14.94           N  
ANISOU 1196  N   ASP A 153     1590   2107   1979    613    -68   -102       N  
ATOM   1197  CA  ASP A 153     -12.175  10.059  -1.887  1.00 13.90           C  
ANISOU 1197  CA  ASP A 153     1494   1951   1837    528    -40   -115       C  
ATOM   1198  C   ASP A 153     -10.866  10.802  -2.128  1.00 13.65           C  
ANISOU 1198  C   ASP A 153     1567   1837   1784    509    -40   -109       C  
ATOM   1199  O   ASP A 153     -10.093  11.023  -1.195  1.00 13.86           O  
ANISOU 1199  O   ASP A 153     1638   1825   1803    482    -10   -127       O  
ATOM   1200  CB  ASP A 153     -12.014   8.616  -2.400  1.00 13.53           C  
ANISOU 1200  CB  ASP A 153     1401   1948   1793    451    -60   -112       C  
ATOM   1201  CG  ASP A 153     -12.762   7.586  -1.563  1.00 12.27           C  
ANISOU 1201  CG  ASP A 153     1156   1849   1657    422    -33   -124       C  
ATOM   1202  OD1 ASP A 153     -13.581   7.952  -0.702  1.00 13.66           O  
ANISOU 1202  OD1 ASP A 153     1289   2052   1848    468      2   -131       O  
ATOM   1203  OD2 ASP A 153     -12.530   6.379  -1.777  1.00 10.95           O  
ANISOU 1203  OD2 ASP A 153      967   1702   1493    353    -41   -124       O  
ATOM   1204  N   TYR A 154     -10.605  11.167  -3.378  1.00 13.71           N  
ANISOU 1204  N   TYR A 154     1612   1819   1777    518    -76    -83       N  
ATOM   1205  CA  TYR A 154      -9.351  11.839  -3.719  1.00 13.43           C  
ANISOU 1205  CA  TYR A 154     1669   1708   1725    490    -71    -69       C  
ATOM   1206  C   TYR A 154      -9.271  13.247  -3.108  1.00 13.79           C  
ANISOU 1206  C   TYR A 154     1785   1679   1774    536    -51    -77       C  
ATOM   1207  O   TYR A 154      -8.191  13.686  -2.699  1.00 13.51           O  
ANISOU 1207  O   TYR A 154     1812   1584   1737    490    -33    -85       O  
ATOM   1208  CB  TYR A 154      -9.160  11.894  -5.237  1.00 13.47           C  
ANISOU 1208  CB  TYR A 154     1703   1706   1708    494   -106    -33       C  
ATOM   1209  CG  TYR A 154      -7.821  12.453  -5.690  1.00 13.26           C  
ANISOU 1209  CG  TYR A 154     1761   1611   1667    453    -92    -11       C  
ATOM   1210  CD1 TYR A 154      -6.634  12.078  -5.071  1.00 13.09           C  
ANISOU 1210  CD1 TYR A 154     1750   1573   1651    378    -64    -24       C  
ATOM   1211  CD2 TYR A 154      -7.745  13.333  -6.761  1.00 13.52           C  
ANISOU 1211  CD2 TYR A 154     1860   1599   1680    489   -105     28       C  
ATOM   1212  CE1 TYR A 154      -5.409  12.585  -5.498  1.00 12.86           C  
ANISOU 1212  CE1 TYR A 154     1781   1489   1615    334    -49     -1       C  
ATOM   1213  CE2 TYR A 154      -6.529  13.837  -7.193  1.00 14.36           C  
ANISOU 1213  CE2 TYR A 154     2037   1643   1776    444    -83     55       C  
ATOM   1214  CZ  TYR A 154      -5.367  13.464  -6.558  1.00 13.54           C  
ANISOU 1214  CZ  TYR A 154     1930   1529   1686    364    -54     40       C  
ATOM   1215  OH  TYR A 154      -4.166  13.971  -6.994  1.00 14.09           O  
ANISOU 1215  OH  TYR A 154     2056   1546   1753    314    -31     69       O  
ATOM   1216  N   ASP A 155     -10.407  13.938  -3.038  1.00 14.20           N  
ANISOU 1216  N   ASP A 155     1826   1736   1834    626    -54    -77       N  
ATOM   1217  CA  ASP A 155     -10.473  15.231  -2.343  1.00 14.83           C  
ANISOU 1217  CA  ASP A 155     1977   1742   1916    683    -31    -92       C  
ATOM   1218  C   ASP A 155     -10.123  15.080  -0.858  1.00 14.19           C  
ANISOU 1218  C   ASP A 155     1901   1656   1836    650      7   -137       C  
ATOM   1219  O   ASP A 155      -9.420  15.919  -0.300  1.00 14.24           O  
ANISOU 1219  O   ASP A 155     1992   1583   1837    638     21   -157       O  
ATOM   1220  CB  ASP A 155     -11.859  15.871  -2.487  1.00 15.77           C  
ANISOU 1220  CB  ASP A 155     2070   1880   2043    801    -38    -85       C  
ATOM   1221  CG  ASP A 155     -12.120  16.404  -3.888  1.00 17.18           C  
ANISOU 1221  CG  ASP A 155     2279   2040   2211    852    -79    -39       C  
ATOM   1222  OD1 ASP A 155     -11.155  16.590  -4.659  1.00 18.72           O  
ANISOU 1222  OD1 ASP A 155     2543   2181   2390    802    -90    -13       O  
ATOM   1223  OD2 ASP A 155     -13.296  16.644  -4.213  1.00 18.22           O  
ANISOU 1223  OD2 ASP A 155     2362   2213   2347    946   -100    -27       O  
ATOM   1224  N   LYS A 156     -10.610  14.016  -0.226  1.00 13.77           N  
ANISOU 1224  N   LYS A 156     1761   1685   1787    634     22   -153       N  
ATOM   1225  CA  LYS A 156     -10.240  13.720   1.162  1.00 13.86           C  
ANISOU 1225  CA  LYS A 156     1778   1701   1788    602     57   -190       C  
ATOM   1226  C   LYS A 156      -8.739  13.471   1.286  1.00 13.12           C  
ANISOU 1226  C   LYS A 156     1733   1569   1684    508     49   -195       C  
ATOM   1227  O   LYS A 156      -8.108  13.961   2.215  1.00 13.04           O  
ANISOU 1227  O   LYS A 156     1780   1514   1659    491     61   -226       O  
ATOM   1228  CB  LYS A 156     -10.997  12.506   1.694  1.00 13.84           C  
ANISOU 1228  CB  LYS A 156     1674   1792   1791    594     79   -193       C  
ATOM   1229  CG  LYS A 156     -12.454  12.763   2.045  1.00 14.97           C  
ANISOU 1229  CG  LYS A 156     1758   1984   1948    684    104   -197       C  
ATOM   1230  CD  LYS A 156     -13.140  11.443   2.376  1.00 16.02           C  
ANISOU 1230  CD  LYS A 156     1782   2210   2095    652    125   -191       C  
ATOM   1231  CE  LYS A 156     -14.575  11.647   2.827  1.00 18.33           C  
ANISOU 1231  CE  LYS A 156     1997   2564   2405    736    160   -192       C  
ATOM   1232  NZ  LYS A 156     -15.221  10.355   3.141  1.00 18.92           N  
ANISOU 1232  NZ  LYS A 156     1964   2725   2499    690    184   -182       N  
ATOM   1233  N   ALA A 157      -8.180  12.723   0.337  1.00 12.60           N  
ANISOU 1233  N   ALA A 157     1641   1523   1622    451     26   -167       N  
ATOM   1234  CA  ALA A 157      -6.757  12.385   0.347  1.00 12.20           C  
ANISOU 1234  CA  ALA A 157     1619   1452   1566    367     20   -166       C  
ATOM   1235  C   ALA A 157      -5.893  13.629   0.214  1.00 12.78           C  
ANISOU 1235  C   ALA A 157     1779   1436   1641    352     14   -166       C  
ATOM   1236  O   ALA A 157      -4.923  13.796   0.955  1.00 12.81           O  
ANISOU 1236  O   ALA A 157     1814   1412   1640    300     15   -189       O  
ATOM   1237  CB  ALA A 157      -6.432  11.393  -0.779  1.00 11.78           C  
ANISOU 1237  CB  ALA A 157     1526   1437   1514    327      2   -133       C  
ATOM   1238  N   LYS A 158      -6.244  14.495  -0.734  1.00 13.40           N  
ANISOU 1238  N   LYS A 158     1896   1469   1725    394      4   -140       N  
ATOM   1239  CA  LYS A 158      -5.557  15.777  -0.901  1.00 14.24           C  
ANISOU 1239  CA  LYS A 158     2097   1477   1838    381      3   -136       C  
ATOM   1240  C   LYS A 158      -5.729  16.714   0.309  1.00 14.63           C  
ANISOU 1240  C   LYS A 158     2207   1468   1885    410     15   -183       C  
ATOM   1241  O   LYS A 158      -4.854  17.535   0.587  1.00 15.07           O  
ANISOU 1241  O   LYS A 158     2336   1443   1946    364     12   -198       O  
ATOM   1242  CB  LYS A 158      -6.010  16.467  -2.187  1.00 14.95           C  
ANISOU 1242  CB  LYS A 158     2223   1529   1927    432     -7    -90       C  
ATOM   1243  CG  LYS A 158      -5.497  15.782  -3.445  1.00 15.62           C  
ANISOU 1243  CG  LYS A 158     2282   1648   2004    391    -18    -45       C  
ATOM   1244  CD  LYS A 158      -5.790  16.592  -4.704  1.00 17.64           C  
ANISOU 1244  CD  LYS A 158     2595   1858   2249    440    -27      4       C  
ATOM   1245  CE  LYS A 158      -7.270  16.599  -5.056  1.00 18.09           C  
ANISOU 1245  CE  LYS A 158     2620   1957   2298    543    -50     11       C  
ATOM   1246  NZ  LYS A 158      -7.546  17.405  -6.276  1.00 20.25           N  
ANISOU 1246  NZ  LYS A 158     2956   2186   2552    601    -65     63       N  
ATOM   1247  N   LYS A 159      -6.840  16.584   1.029  1.00 14.69           N  
ANISOU 1247  N   LYS A 159     2184   1514   1883    484     30   -208       N  
ATOM   1248  CA  LYS A 159      -7.027  17.318   2.285  1.00 15.23           C  
ANISOU 1248  CA  LYS A 159     2310   1539   1938    519     47   -260       C  
ATOM   1249  C   LYS A 159      -6.071  16.792   3.358  1.00 14.70           C  
ANISOU 1249  C   LYS A 159     2242   1489   1854    441     45   -298       C  
ATOM   1250  O   LYS A 159      -5.362  17.571   3.993  1.00 14.91           O  
ANISOU 1250  O   LYS A 159     2347   1444   1873    409     36   -334       O  
ATOM   1251  CB  LYS A 159      -8.485  17.241   2.753  1.00 15.74           C  
ANISOU 1251  CB  LYS A 159     2331   1655   1994    624     74   -272       C  
ATOM   1252  CG  LYS A 159      -8.772  17.924   4.081  1.00 17.42           C  
ANISOU 1252  CG  LYS A 159     2605   1831   2183    675    101   -327       C  
ATOM   1253  CD  LYS A 159     -10.271  18.171   4.272  1.00 19.30           C  
ANISOU 1253  CD  LYS A 159     2808   2107   2420    801    134   -329       C  
ATOM   1254  CE  LYS A 159     -10.585  18.719   5.661  1.00 20.80           C  
ANISOU 1254  CE  LYS A 159     3056   2272   2576    859    173   -386       C  
ATOM   1255  NZ  LYS A 159     -11.901  19.446   5.689  1.00 22.14           N  
ANISOU 1255  NZ  LYS A 159     3226   2439   2747    999    206   -388       N  
ATOM   1256  N   LEU A 160      -6.035  15.472   3.535  1.00 13.99           N  
ANISOU 1256  N   LEU A 160     2067   1492   1758    409     49   -289       N  
ATOM   1257  CA  LEU A 160      -5.116  14.838   4.493  1.00 13.74           C  
ANISOU 1257  CA  LEU A 160     2028   1487   1706    343     43   -315       C  
ATOM   1258  C   LEU A 160      -3.660  15.057   4.101  1.00 13.44           C  
ANISOU 1258  C   LEU A 160     2017   1407   1683    251     13   -308       C  
ATOM   1259  O   LEU A 160      -2.807  15.288   4.959  1.00 13.47           O  
ANISOU 1259  O   LEU A 160     2055   1389   1673    204     -5   -344       O  
ATOM   1260  CB  LEU A 160      -5.367  13.328   4.588  1.00 13.08           C  
ANISOU 1260  CB  LEU A 160     1852   1500   1616    330     55   -296       C  
ATOM   1261  CG  LEU A 160      -6.321  12.814   5.657  1.00 13.66           C  
ANISOU 1261  CG  LEU A 160     1896   1631   1664    380     90   -315       C  
ATOM   1262  CD1 LEU A 160      -7.587  13.635   5.694  1.00 16.24           C  
ANISOU 1262  CD1 LEU A 160     2235   1942   1994    474    116   -324       C  
ATOM   1263  CD2 LEU A 160      -6.628  11.354   5.403  1.00 13.67           C  
ANISOU 1263  CD2 LEU A 160     1809   1712   1672    359    101   -283       C  
ATOM   1264  N   GLY A 161      -3.386  14.971   2.804  1.00 13.08           N  
ANISOU 1264  N   GLY A 161     1952   1355   1663    228      6   -261       N  
ATOM   1265  CA  GLY A 161      -2.014  14.996   2.297  1.00 13.15           C  
ANISOU 1265  CA  GLY A 161     1964   1343   1689    140    -11   -242       C  
ATOM   1266  C   GLY A 161      -1.353  13.643   2.474  1.00 12.70           C  
ANISOU 1266  C   GLY A 161     1833   1369   1625     95    -16   -234       C  
ATOM   1267  O   GLY A 161      -1.889  12.766   3.163  1.00 12.53           O  
ANISOU 1267  O   GLY A 161     1772   1406   1582    123     -7   -247       O  
ATOM   1268  N   HIS A 162      -0.186  13.459   1.862  1.00 12.78           N  
ANISOU 1268  N   HIS A 162     1823   1380   1652     28    -24   -208       N  
ATOM   1269  CA  HIS A 162       0.525  12.174   1.965  1.00 12.26           C  
ANISOU 1269  CA  HIS A 162     1690   1389   1581     -5    -27   -196       C  
ATOM   1270  C   HIS A 162       0.840  11.832   3.426  1.00 12.59           C  
ANISOU 1270  C   HIS A 162     1724   1460   1598    -16    -43   -238       C  
ATOM   1271  O   HIS A 162       0.746  10.675   3.841  1.00 12.11           O  
ANISOU 1271  O   HIS A 162     1620   1462   1518     -3    -39   -235       O  
ATOM   1272  CB  HIS A 162       1.815  12.191   1.151  1.00 12.40           C  
ANISOU 1272  CB  HIS A 162     1686   1403   1622    -71    -28   -164       C  
ATOM   1273  CG  HIS A 162       1.608  12.458  -0.307  1.00 12.48           C  
ANISOU 1273  CG  HIS A 162     1709   1389   1643    -60     -7   -118       C  
ATOM   1274  ND1 HIS A 162       0.565  11.912  -1.021  1.00 12.82           N  
ANISOU 1274  ND1 HIS A 162     1742   1458   1671     -1      3    -99       N  
ATOM   1275  CD2 HIS A 162       2.317  13.201  -1.187  1.00 13.83           C  
ANISOU 1275  CD2 HIS A 162     1904   1516   1835   -101      4    -85       C  
ATOM   1276  CE1 HIS A 162       0.642  12.304  -2.278  1.00 13.70           C  
ANISOU 1276  CE1 HIS A 162     1875   1543   1785      1     15    -58       C  
ATOM   1277  NE2 HIS A 162       1.695  13.089  -2.407  1.00 14.65           N  
ANISOU 1277  NE2 HIS A 162     2020   1620   1927    -58     21    -45       N  
ATOM   1278  N   GLU A 163       1.209  12.855   4.190  1.00 13.47           N  
ANISOU 1278  N   GLU A 163     1889   1520   1708    -40    -65   -278       N  
ATOM   1279  CA  GLU A 163       1.539  12.730   5.613  1.00 13.90           C  
ANISOU 1279  CA  GLU A 163     1955   1596   1729    -49    -89   -324       C  
ATOM   1280  C   GLU A 163       0.335  12.305   6.438  1.00 13.39           C  
ANISOU 1280  C   GLU A 163     1901   1561   1625     25    -66   -344       C  
ATOM   1281  O   GLU A 163       0.460  11.506   7.369  1.00 13.35           O  
ANISOU 1281  O   GLU A 163     1877   1610   1584     32    -71   -356       O  
ATOM   1282  CB  GLU A 163       2.055  14.076   6.108  1.00 15.17           C  
ANISOU 1282  CB  GLU A 163     2187   1681   1897    -91   -120   -368       C  
ATOM   1283  CG  GLU A 163       2.353  14.207   7.581  1.00 17.63           C  
ANISOU 1283  CG  GLU A 163     2532   2002   2166    -98   -154   -427       C  
ATOM   1284  CD  GLU A 163       2.905  15.581   7.877  1.00 19.84           C  
ANISOU 1284  CD  GLU A 163     2887   2192   2459   -152   -190   -473       C  
ATOM   1285  OE1 GLU A 163       2.152  16.445   8.380  1.00 20.76           O  
ANISOU 1285  OE1 GLU A 163     3090   2245   2554   -108   -183   -515       O  
ATOM   1286  OE2 GLU A 163       4.081  15.805   7.544  1.00 22.18           O  
ANISOU 1286  OE2 GLU A 163     3156   2481   2792   -239   -220   -464       O  
ATOM   1287  N   GLY A 164      -0.828  12.858   6.103  1.00 13.22           N  
ANISOU 1287  N   GLY A 164     1908   1506   1608     83    -39   -343       N  
ATOM   1288  CA  GLY A 164      -2.082  12.495   6.759  1.00 13.03           C  
ANISOU 1288  CA  GLY A 164     1880   1515   1554    157     -6   -355       C  
ATOM   1289  C   GLY A 164      -2.481  11.050   6.524  1.00 11.99           C  
ANISOU 1289  C   GLY A 164     1672   1461   1422    166     16   -318       C  
ATOM   1290  O   GLY A 164      -2.931  10.374   7.445  1.00 12.00           O  
ANISOU 1290  O   GLY A 164     1660   1508   1390    192     36   -327       O  
ATOM   1291  N   ILE A 165      -2.346  10.584   5.285  1.00 11.31           N  
ANISOU 1291  N   ILE A 165     1543   1386   1369    146     14   -277       N  
ATOM   1292  CA  ILE A 165      -2.603   9.179   4.952  1.00 10.57           C  
ANISOU 1292  CA  ILE A 165     1387   1353   1276    144     28   -245       C  
ATOM   1293  C   ILE A 165      -1.569   8.279   5.627  1.00 10.21           C  
ANISOU 1293  C   ILE A 165     1326   1344   1210    106     16   -245       C  
ATOM   1294  O   ILE A 165      -1.918   7.262   6.225  1.00  9.98           O  
ANISOU 1294  O   ILE A 165     1275   1358   1161    120     35   -238       O  
ATOM   1295  CB  ILE A 165      -2.548   8.940   3.423  1.00 10.41           C  
ANISOU 1295  CB  ILE A 165     1339   1330   1287    130     23   -208       C  
ATOM   1296  CG1 ILE A 165      -3.756   9.576   2.741  1.00 10.81           C  
ANISOU 1296  CG1 ILE A 165     1393   1362   1352    180     31   -201       C  
ATOM   1297  CG2 ILE A 165      -2.492   7.430   3.105  1.00  9.89           C  
ANISOU 1297  CG2 ILE A 165     1222   1316   1220    115     31   -183       C  
ATOM   1298  CD1 ILE A 165      -4.980   8.689   2.695  1.00 11.11           C  
ANISOU 1298  CD1 ILE A 165     1378   1453   1392    213     49   -192       C  
ATOM   1299  N   ALA A 166      -0.299   8.663   5.515  1.00 10.02           N  
ANISOU 1299  N   ALA A 166     1312   1302   1194     60    -14   -249       N  
ATOM   1300  CA  ALA A 166       0.805   7.918   6.118  1.00  9.91           C  
ANISOU 1300  CA  ALA A 166     1277   1326   1162     29    -34   -247       C  
ATOM   1301  C   ALA A 166       0.610   7.738   7.624  1.00 10.10           C  
ANISOU 1301  C   ALA A 166     1327   1373   1137     53    -37   -277       C  
ATOM   1302  O   ALA A 166       0.739   6.630   8.146  1.00  9.77           O  
ANISOU 1302  O   ALA A 166     1265   1377   1069     63    -30   -262       O  
ATOM   1303  CB  ALA A 166       2.133   8.616   5.837  1.00 10.15           C  
ANISOU 1303  CB  ALA A 166     1307   1336   1215    -27    -69   -252       C  
ATOM   1304  N   LYS A 167       0.281   8.825   8.312  1.00 10.46           N  
ANISOU 1304  N   LYS A 167     1427   1383   1164     67    -44   -319       N  
ATOM   1305  CA  LYS A 167       0.122   8.783   9.765  1.00 11.27           C  
ANISOU 1305  CA  LYS A 167     1569   1506   1208     93    -46   -353       C  
ATOM   1306  C   LYS A 167      -0.934   7.764  10.184  1.00 10.88           C  
ANISOU 1306  C   LYS A 167     1501   1500   1132    142      4   -330       C  
ATOM   1307  O   LYS A 167      -0.745   7.050  11.167  1.00 10.41           O  
ANISOU 1307  O   LYS A 167     1450   1479   1024    154      6   -329       O  
ATOM   1308  CB  LYS A 167      -0.222  10.168  10.315  1.00 12.02           C  
ANISOU 1308  CB  LYS A 167     1736   1545   1286    110    -54   -405       C  
ATOM   1309  CG  LYS A 167      -0.238  10.266  11.845  1.00 14.22           C  
ANISOU 1309  CG  LYS A 167     2071   1840   1491    138    -63   -450       C  
ATOM   1310  CD  LYS A 167      -0.499  11.709  12.309  1.00 16.91           C  
ANISOU 1310  CD  LYS A 167     2497   2112   1814    154    -74   -510       C  
ATOM   1311  CE  LYS A 167      -0.569  11.816  13.843  1.00 19.44           C  
ANISOU 1311  CE  LYS A 167     2886   2451   2049    189    -80   -560       C  
ATOM   1312  NZ  LYS A 167      -1.598  12.808  14.298  1.00 21.18           N  
ANISOU 1312  NZ  LYS A 167     3183   2623   2242    255    -43   -604       N  
ATOM   1313  N   LEU A 168      -2.033   7.688   9.433  1.00 10.63           N  
ANISOU 1313  N   LEU A 168     1443   1463   1133    167     44   -309       N  
ATOM   1314  CA  LEU A 168      -3.124   6.760   9.762  1.00 10.55           C  
ANISOU 1314  CA  LEU A 168     1405   1493   1111    202     95   -285       C  
ATOM   1315  C   LEU A 168      -2.688   5.305   9.578  1.00  9.99           C  
ANISOU 1315  C   LEU A 168     1295   1458   1041    175     98   -245       C  
ATOM   1316  O   LEU A 168      -2.985   4.446  10.412  1.00  9.79           O  
ANISOU 1316  O   LEU A 168     1273   1466    982    190    127   -230       O  
ATOM   1317  CB  LEU A 168      -4.370   7.061   8.921  1.00 10.54           C  
ANISOU 1317  CB  LEU A 168     1372   1483   1150    230    126   -274       C  
ATOM   1318  CG  LEU A 168      -5.109   8.366   9.248  1.00 11.33           C  
ANISOU 1318  CG  LEU A 168     1511   1552   1243    281    140   -309       C  
ATOM   1319  CD1 LEU A 168      -6.274   8.594   8.281  1.00 11.54           C  
ANISOU 1319  CD1 LEU A 168     1492   1578   1313    313    161   -291       C  
ATOM   1320  CD2 LEU A 168      -5.606   8.348  10.688  1.00 11.83           C  
ANISOU 1320  CD2 LEU A 168     1607   1640   1247    324    179   -332       C  
ATOM   1321  N   ILE A 169      -1.960   5.046   8.499  1.00  9.41           N  
ANISOU 1321  N   ILE A 169     1194   1375   1006    140     71   -226       N  
ATOM   1322  CA  ILE A 169      -1.430   3.714   8.225  1.00  8.98           C  
ANISOU 1322  CA  ILE A 169     1112   1345    955    122     71   -191       C  
ATOM   1323  C   ILE A 169      -0.414   3.301   9.277  1.00  9.18           C  
ANISOU 1323  C   ILE A 169     1159   1394    935    122     49   -192       C  
ATOM   1324  O   ILE A 169      -0.437   2.172   9.752  1.00  9.14           O  
ANISOU 1324  O   ILE A 169     1154   1412    906    133     68   -166       O  
ATOM   1325  CB  ILE A 169      -0.740   3.647   6.853  1.00  8.48           C  
ANISOU 1325  CB  ILE A 169     1022   1267    933     93     49   -174       C  
ATOM   1326  CG1 ILE A 169      -1.768   3.810   5.727  1.00  8.15           C  
ANISOU 1326  CG1 ILE A 169      960   1209    929     97     65   -166       C  
ATOM   1327  CG2 ILE A 169       0.026   2.330   6.717  1.00  8.64           C  
ANISOU 1327  CG2 ILE A 169     1025   1309    949     84     47   -144       C  
ATOM   1328  CD1 ILE A 169      -1.171   3.887   4.328  1.00  6.72           C  
ANISOU 1328  CD1 ILE A 169      764   1011    777     75     47   -151       C  
ATOM   1329  N   VAL A 170       0.481   4.218   9.628  1.00  9.71           N  
ANISOU 1329  N   VAL A 170     1245   1453    990    108      5   -223       N  
ATOM   1330  CA  VAL A 170       1.523   3.940  10.613  1.00 10.23           C  
ANISOU 1330  CA  VAL A 170     1326   1550   1011    108    -32   -230       C  
ATOM   1331  C   VAL A 170       0.926   3.715  12.011  1.00 10.86           C  
ANISOU 1331  C   VAL A 170     1453   1651   1024    147    -11   -240       C  
ATOM   1332  O   VAL A 170       1.290   2.759  12.703  1.00 11.19           O  
ANISOU 1332  O   VAL A 170     1503   1726   1024    166    -12   -216       O  
ATOM   1333  CB  VAL A 170       2.569   5.070  10.649  1.00 10.69           C  
ANISOU 1333  CB  VAL A 170     1389   1594   1078     71    -90   -266       C  
ATOM   1334  CG1 VAL A 170       3.593   4.830  11.760  1.00 10.92           C  
ANISOU 1334  CG1 VAL A 170     1429   1665   1056     72   -140   -279       C  
ATOM   1335  CG2 VAL A 170       3.261   5.185   9.296  1.00 10.51           C  
ANISOU 1335  CG2 VAL A 170     1317   1558   1117     32   -101   -245       C  
ATOM   1336  N   GLU A 171       0.001   4.579  12.420  1.00 11.21           N  
ANISOU 1336  N   GLU A 171     1532   1676   1052    168     13   -272       N  
ATOM   1337  CA  GLU A 171      -0.690   4.396  13.702  1.00 12.07           C  
ANISOU 1337  CA  GLU A 171     1687   1806   1092    212     48   -279       C  
ATOM   1338  C   GLU A 171      -1.352   3.023  13.774  1.00 12.13           C  
ANISOU 1338  C   GLU A 171     1673   1839   1095    228    105   -225       C  
ATOM   1339  O   GLU A 171      -1.283   2.343  14.806  1.00 12.51           O  
ANISOU 1339  O   GLU A 171     1755   1917   1081    253    120   -208       O  
ATOM   1340  CB  GLU A 171      -1.726   5.496  13.939  1.00 12.57           C  
ANISOU 1340  CB  GLU A 171     1783   1843   1148    242     80   -317       C  
ATOM   1341  CG  GLU A 171      -1.118   6.836  14.313  1.00 14.17           C  
ANISOU 1341  CG  GLU A 171     2040   2013   1332    234     27   -378       C  
ATOM   1342  CD  GLU A 171      -2.151   7.864  14.749  1.00 15.89           C  
ANISOU 1342  CD  GLU A 171     2308   2202   1527    281     64   -419       C  
ATOM   1343  OE1 GLU A 171      -3.347   7.714  14.413  1.00 17.72           O  
ANISOU 1343  OE1 GLU A 171     2510   2438   1783    315    127   -396       O  
ATOM   1344  OE2 GLU A 171      -1.757   8.830  15.430  1.00 15.69           O  
ANISOU 1344  OE2 GLU A 171     2351   2149   1461    286     28   -475       O  
ATOM   1345  N   GLY A 172      -1.982   2.621  12.671  1.00 11.91           N  
ANISOU 1345  N   GLY A 172     1595   1798   1131    210    135   -198       N  
ATOM   1346  CA  GLY A 172      -2.618   1.316  12.561  1.00 12.05           C  
ANISOU 1346  CA  GLY A 172     1591   1829   1161    208    185   -149       C  
ATOM   1347  C   GLY A 172      -1.639   0.168  12.692  1.00 12.26           C  
ANISOU 1347  C   GLY A 172     1624   1865   1169    202    165   -115       C  
ATOM   1348  O   GLY A 172      -1.834  -0.723  13.508  1.00 12.77           O  
ANISOU 1348  O   GLY A 172     1717   1945   1192    220    198    -83       O  
ATOM   1349  N   VAL A 173      -0.583   0.184  11.887  1.00 12.41           N  
ANISOU 1349  N   VAL A 173     1621   1876   1219    181    115   -117       N  
ATOM   1350  CA  VAL A 173       0.416  -0.896  11.918  1.00 12.62           C  
ANISOU 1350  CA  VAL A 173     1648   1913   1233    186     95    -84       C  
ATOM   1351  C   VAL A 173       1.077  -0.988  13.297  1.00 13.46           C  
ANISOU 1351  C   VAL A 173     1798   2052   1263    220     70    -85       C  
ATOM   1352  O   VAL A 173       1.197  -2.074  13.868  1.00 13.29           O  
ANISOU 1352  O   VAL A 173     1804   2042   1205    245     88    -45       O  
ATOM   1353  CB  VAL A 173       1.475  -0.710  10.811  1.00 12.37           C  
ANISOU 1353  CB  VAL A 173     1577   1876   1248    164     50    -89       C  
ATOM   1354  CG1 VAL A 173       2.646  -1.663  11.001  1.00 12.62           C  
ANISOU 1354  CG1 VAL A 173     1607   1929   1260    185     25    -60       C  
ATOM   1355  CG2 VAL A 173       0.835  -0.904   9.434  1.00 11.51           C  
ANISOU 1355  CG2 VAL A 173     1437   1737   1200    140     76    -80       C  
ATOM   1356  N   LEU A 174       1.459   0.161  13.844  1.00 14.20           N  
ANISOU 1356  N   LEU A 174     1907   2158   1328    220     28   -131       N  
ATOM   1357  CA  LEU A 174       2.195   0.201  15.102  1.00 15.55           C  
ANISOU 1357  CA  LEU A 174     2120   2365   1422    248    -15   -142       C  
ATOM   1358  C   LEU A 174       1.303   0.085  16.341  1.00 16.75           C  
ANISOU 1358  C   LEU A 174     2337   2530   1498    287     32   -139       C  
ATOM   1359  O   LEU A 174       1.810  -0.123  17.448  1.00 17.30           O  
ANISOU 1359  O   LEU A 174     2453   2632   1487    321      5   -137       O  
ATOM   1360  CB  LEU A 174       3.038   1.477  15.178  1.00 15.71           C  
ANISOU 1360  CB  LEU A 174     2135   2390   1443    223    -87   -198       C  
ATOM   1361  CG  LEU A 174       4.117   1.626  14.102  1.00 15.61           C  
ANISOU 1361  CG  LEU A 174     2056   2377   1497    183   -133   -197       C  
ATOM   1362  CD1 LEU A 174       4.887   2.926  14.316  1.00 14.55           C  
ANISOU 1362  CD1 LEU A 174     1921   2243   1364    146   -202   -253       C  
ATOM   1363  CD2 LEU A 174       5.067   0.421  14.083  1.00 14.66           C  
ANISOU 1363  CD2 LEU A 174     1907   2293   1370    207   -153   -151       C  
ATOM   1364  N   ASN A 175      -0.012   0.205  16.157  1.00 17.48           N  
ANISOU 1364  N   ASN A 175     2429   2602   1612    286    103   -135       N  
ATOM   1365  CA  ASN A 175      -0.980   0.130  17.265  1.00 19.13           C  
ANISOU 1365  CA  ASN A 175     2689   2825   1753    324    165   -129       C  
ATOM   1366  C   ASN A 175      -0.686   1.156  18.351  1.00 20.56           C  
ANISOU 1366  C   ASN A 175     2932   3025   1854    353    129   -184       C  
ATOM   1367  O   ASN A 175      -0.620   0.834  19.534  1.00 21.99           O  
ANISOU 1367  O   ASN A 175     3175   3237   1944    394    137   -174       O  
ATOM   1368  CB  ASN A 175      -1.046  -1.286  17.864  1.00 19.40           C  
ANISOU 1368  CB  ASN A 175     2751   2874   1745    346    207    -63       C  
ATOM   1369  CG  ASN A 175      -2.301  -1.514  18.722  1.00 20.16           C  
ANISOU 1369  CG  ASN A 175     2883   2981   1794    372    300    -40       C  
ATOM   1370  OD1 ASN A 175      -3.198  -0.676  18.777  1.00 19.69           O  
ANISOU 1370  OD1 ASN A 175     2816   2922   1742    377    337    -71       O  
ATOM   1371  ND2 ASN A 175      -2.358  -2.658  19.389  1.00 21.00           N  
ANISOU 1371  ND2 ASN A 175     3029   3096   1852    391    341     20       N  
ATOM   1372  N   LYS A 176      -0.502   2.397  17.934  1.00 21.56           N  
ANISOU 1372  N   LYS A 176     3050   3129   2012    333     87   -241       N  
ATOM   1373  CA  LYS A 176      -0.335   3.498  18.867  1.00 23.25           C  
ANISOU 1373  CA  LYS A 176     3330   3345   2157    355     52   -305       C  
ATOM   1374  C   LYS A 176      -0.718   4.796  18.192  1.00 23.96           C  
ANISOU 1374  C   LYS A 176     3412   3388   2304    335     47   -356       C  
ATOM   1375  O   LYS A 176      -0.904   4.843  16.975  1.00 22.88           O  
ANISOU 1375  O   LYS A 176     3213   3225   2256    303     56   -340       O  
ATOM   1376  CB  LYS A 176       1.103   3.568  19.393  1.00 23.89           C  
ANISOU 1376  CB  LYS A 176     3433   3451   2193    344    -47   -329       C  
ATOM   1377  CG  LYS A 176       2.174   3.775  18.332  1.00 23.54           C  
ANISOU 1377  CG  LYS A 176     3320   3394   2230    285   -116   -334       C  
ATOM   1378  CD  LYS A 176       3.541   3.993  18.972  1.00 24.35           C  
ANISOU 1378  CD  LYS A 176     3434   3530   2287    273   -217   -365       C  
ATOM   1379  CE  LYS A 176       4.519   4.636  17.994  1.00 24.11           C  
ANISOU 1379  CE  LYS A 176     3338   3483   2341    206   -282   -387       C  
ATOM   1380  NZ  LYS A 176       5.805   5.016  18.642  1.00 24.60           N  
ANISOU 1380  NZ  LYS A 176     3400   3580   2365    183   -386   -426       N  
ATOM   1381  N   ASN A 177      -0.851   5.843  18.998  1.00 25.60           N  
ANISOU 1381  N   ASN A 177     3691   3584   2453    361     34   -418       N  
ATOM   1382  CA  ASN A 177      -1.144   7.169  18.493  1.00 26.48           C  
ANISOU 1382  CA  ASN A 177     3815   3639   2607    351     25   -471       C  
ATOM   1383  C   ASN A 177       0.150   7.963  18.424  1.00 27.42           C  
ANISOU 1383  C   ASN A 177     3952   3733   2734    298    -77   -521       C  
ATOM   1384  O   ASN A 177       0.923   7.988  19.381  1.00 27.88           O  
ANISOU 1384  O   ASN A 177     4058   3817   2719    299   -136   -552       O  
ATOM   1385  CB  ASN A 177      -2.189   7.856  19.377  1.00 27.44           C  
ANISOU 1385  CB  ASN A 177     4010   3752   2663    418     83   -510       C  
ATOM   1386  CG  ASN A 177      -3.591   7.323  19.131  1.00 27.32           C  
ANISOU 1386  CG  ASN A 177     3950   3756   2674    458    189   -461       C  
ATOM   1387  OD1 ASN A 177      -4.088   7.358  18.007  1.00 28.53           O  
ANISOU 1387  OD1 ASN A 177     4035   3890   2916    440    210   -437       O  
ATOM   1388  ND2 ASN A 177      -4.225   6.814  20.176  1.00 28.27           N  
ANISOU 1388  ND2 ASN A 177     4106   3919   2716    511    255   -444       N  
ATOM   1389  N   ILE A 178       0.399   8.578  17.273  1.00 27.95           N  
ANISOU 1389  N   ILE A 178     3977   3752   2889    250    -99   -526       N  
ATOM   1390  CA  ILE A 178       1.642   9.302  17.040  1.00 29.07           C  
ANISOU 1390  CA  ILE A 178     4119   3868   3057    183   -189   -564       C  
ATOM   1391  C   ILE A 178       1.478  10.763  17.426  1.00 30.75           C  
ANISOU 1391  C   ILE A 178     4418   4014   3251    183   -211   -641       C  
ATOM   1392  O   ILE A 178       2.301  11.307  18.163  1.00 32.04           O  
ANISOU 1392  O   ILE A 178     4633   4172   3370    154   -285   -697       O  
ATOM   1393  CB  ILE A 178       2.084   9.212  15.566  1.00 28.27           C  
ANISOU 1393  CB  ILE A 178     3935   3748   3060    127   -195   -524       C  
ATOM   1394  CG1 ILE A 178       2.451   7.772  15.210  1.00 27.36           C  
ANISOU 1394  CG1 ILE A 178     3744   3692   2958    126   -185   -457       C  
ATOM   1395  CG2 ILE A 178       3.278  10.134  15.308  1.00 28.62           C  
ANISOU 1395  CG2 ILE A 178     3978   3758   3138     51   -275   -563       C  
ATOM   1396  CD1 ILE A 178       2.727   7.571  13.742  1.00 26.46           C  
ANISOU 1396  CD1 ILE A 178     3555   3563   2934     86   -176   -416       C  
ATOM   1397  N   ASN A 179       0.407  11.383  16.938  1.00 31.50           N  
ANISOU 1397  N   ASN A 179     4532   4059   3378    217   -150   -645       N  
ATOM   1398  CA  ASN A 179       0.169  12.810  17.130  1.00 33.21           C  
ANISOU 1398  CA  ASN A 179     4836   4195   3588    225   -163   -713       C  
ATOM   1399  C   ASN A 179       1.424  13.547  17.604  1.00 34.22           C  
ANISOU 1399  C   ASN A 179     5013   4292   3696    155   -261   -776       C  
ATOM   1400  O   ASN A 179       1.617  13.831  18.792  1.00 35.38           O  
ANISOU 1400  O   ASN A 179     5241   4444   3756    174   -297   -836       O  
ATOM   1401  CB  ASN A 179      -1.002  13.033  18.100  1.00 34.12           C  
ANISOU 1401  CB  ASN A 179     5026   4313   3624    320    -98   -743       C  
ATOM   1402  CG  ASN A 179      -1.601  14.427  17.992  1.00 35.80           C  
ANISOU 1402  CG  ASN A 179     5319   4434   3848    353    -81   -798       C  
ATOM   1403  OD1 ASN A 179      -1.166  15.251  17.181  1.00 37.36           O  
ANISOU 1403  OD1 ASN A 179     5523   4558   4112    301   -119   -812       O  
ATOM   1404  ND2 ASN A 179      -2.606  14.696  18.813  1.00 37.84           N  
ANISOU 1404  ND2 ASN A 179     5644   4695   4039    445    -20   -828       N  
ATOM   1405  OXT ASN A 179       2.290  13.851  16.779  1.00 34.33           O  
ANISOU 1405  OXT ASN A 179     4983   4277   3783     75   -309   -768       O  
TER    1406      ASN A 179                                                      
ATOM   1407  N   HIS B   0     -33.566 -20.200  20.847  1.00 22.11           N  
ANISOU 1407  N   HIS B   0     2548   3335   2517     23   -519   -161       N  
ATOM   1408  CA  HIS B   0     -33.084 -21.386  20.076  1.00 21.88           C  
ANISOU 1408  CA  HIS B   0     2588   3298   2429    -42   -501   -181       C  
ATOM   1409  C   HIS B   0     -32.644 -22.523  21.006  1.00 20.64           C  
ANISOU 1409  C   HIS B   0     2442   3107   2295    -93   -429   -213       C  
ATOM   1410  O   HIS B   0     -33.040 -23.669  20.825  1.00 20.69           O  
ANISOU 1410  O   HIS B   0     2454   3127   2280   -158   -426   -252       O  
ATOM   1411  CB  HIS B   0     -31.938 -20.972  19.166  1.00 22.04           C  
ANISOU 1411  CB  HIS B   0     2700   3277   2399    -20   -491   -142       C  
ATOM   1412  CG  HIS B   0     -31.893 -21.726  17.878  1.00 23.65           C  
ANISOU 1412  CG  HIS B   0     2964   3498   2523    -65   -513   -158       C  
ATOM   1413  ND1 HIS B   0     -33.032 -22.133  17.215  1.00 27.20           N  
ANISOU 1413  ND1 HIS B   0     3383   4011   2941    -98   -580   -185       N  
ATOM   1414  CD2 HIS B   0     -30.849 -22.125  17.114  1.00 25.27           C  
ANISOU 1414  CD2 HIS B   0     3259   3670   2672    -82   -476   -153       C  
ATOM   1415  CE1 HIS B   0     -32.691 -22.759  16.102  1.00 27.35           C  
ANISOU 1415  CE1 HIS B   0     3478   4031   2883   -137   -585   -197       C  
ATOM   1416  NE2 HIS B   0     -31.372 -22.770  16.019  1.00 26.79           N  
ANISOU 1416  NE2 HIS B   0     3481   3901   2796   -126   -519   -179       N  
ATOM   1417  N   MET B   1     -31.819 -22.190  21.991  1.00 19.28           N  
ANISOU 1417  N   MET B   1     2277   2887   2162    -65   -374   -196       N  
ATOM   1418  CA  MET B   1     -31.483 -23.107  23.079  1.00 18.61           C  
ANISOU 1418  CA  MET B   1     2195   2773   2106   -101   -311   -218       C  
ATOM   1419  C   MET B   1     -32.292 -22.738  24.318  1.00 17.65           C  
ANISOU 1419  C   MET B   1     1989   2676   2040    -92   -306   -229       C  
ATOM   1420  O   MET B   1     -32.710 -21.587  24.481  1.00 17.59           O  
ANISOU 1420  O   MET B   1     1934   2689   2059    -39   -335   -213       O  
ATOM   1421  CB  MET B   1     -29.991 -23.031  23.419  1.00 18.30           C  
ANISOU 1421  CB  MET B   1     2213   2670   2068    -77   -255   -192       C  
ATOM   1422  CG  MET B   1     -29.118 -24.010  22.645  1.00 19.65           C  
ANISOU 1422  CG  MET B   1     2464   2809   2193   -104   -226   -200       C  
ATOM   1423  SD  MET B   1     -27.426 -24.068  23.266  1.00 21.69           S  
ANISOU 1423  SD  MET B   1     2767   3006   2467    -75   -157   -176       S  
ATOM   1424  CE  MET B   1     -26.905 -22.391  22.860  1.00 20.20           C  
ANISOU 1424  CE  MET B   1     2574   2821   2280    -19   -177   -129       C  
ATOM   1425  N   LYS B   2     -32.522 -23.729  25.175  1.00 16.77           N  
ANISOU 1425  N   LYS B   2     1867   2561   1944   -145   -267   -257       N  
ATOM   1426  CA  LYS B   2     -33.001 -23.484  26.529  1.00 16.07           C  
ANISOU 1426  CA  LYS B   2     1716   2486   1903   -142   -240   -266       C  
ATOM   1427  C   LYS B   2     -31.813 -23.732  27.442  1.00 14.64           C  
ANISOU 1427  C   LYS B   2     1588   2244   1731   -136   -181   -248       C  
ATOM   1428  O   LYS B   2     -31.252 -24.828  27.461  1.00 14.36           O  
ANISOU 1428  O   LYS B   2     1609   2171   1676   -175   -149   -253       O  
ATOM   1429  CB  LYS B   2     -34.173 -24.395  26.903  1.00 16.62           C  
ANISOU 1429  CB  LYS B   2     1734   2601   1980   -213   -237   -307       C  
ATOM   1430  CG  LYS B   2     -34.947 -23.908  28.139  1.00 17.25           C  
ANISOU 1430  CG  LYS B   2     1729   2719   2105   -204   -217   -320       C  
ATOM   1431  CD  LYS B   2     -36.083 -24.859  28.537  1.00 18.01           C  
ANISOU 1431  CD  LYS B   2     1771   2864   2207   -287   -205   -360       C  
ATOM   1432  CE  LYS B   2     -36.790 -24.383  29.807  1.00 18.02           C  
ANISOU 1432  CE  LYS B   2     1690   2906   2249   -280   -173   -376       C  
ATOM   1433  NZ  LYS B   2     -37.798 -25.358  30.323  1.00 18.00           N  
ANISOU 1433  NZ  LYS B   2     1640   2950   2251   -372   -146   -413       N  
ATOM   1434  N   ILE B   3     -31.443 -22.705  28.196  1.00 13.35           N  
ANISOU 1434  N   ILE B   3     1405   2070   1597    -85   -168   -229       N  
ATOM   1435  CA  ILE B   3     -30.230 -22.715  28.993  1.00 12.09           C  
ANISOU 1435  CA  ILE B   3     1290   1861   1444    -71   -124   -209       C  
ATOM   1436  C   ILE B   3     -30.571 -22.630  30.477  1.00 11.65           C  
ANISOU 1436  C   ILE B   3     1196   1815   1417    -79    -91   -220       C  
ATOM   1437  O   ILE B   3     -31.435 -21.848  30.884  1.00 11.44           O  
ANISOU 1437  O   ILE B   3     1107   1825   1416    -59   -103   -234       O  
ATOM   1438  CB  ILE B   3     -29.340 -21.522  28.630  1.00 11.75           C  
ANISOU 1438  CB  ILE B   3     1268   1794   1404    -13   -135   -177       C  
ATOM   1439  CG1 ILE B   3     -29.036 -21.519  27.126  1.00 11.69           C  
ANISOU 1439  CG1 ILE B   3     1301   1781   1359     -6   -165   -163       C  
ATOM   1440  CG2 ILE B   3     -28.051 -21.552  29.443  1.00 11.29           C  
ANISOU 1440  CG2 ILE B   3     1246   1693   1352     -4    -94   -158       C  
ATOM   1441  CD1 ILE B   3     -28.424 -20.233  26.626  1.00 11.07           C  
ANISOU 1441  CD1 ILE B   3     1240   1686   1281     44   -182   -129       C  
ATOM   1442  N   CYS B   4     -29.887 -23.433  31.282  1.00 10.75           N  
ANISOU 1442  N   CYS B   4     1121   1667   1296   -105    -50   -214       N  
ATOM   1443  CA  CYS B   4     -29.981 -23.308  32.731  1.00 10.54           C  
ANISOU 1443  CA  CYS B   4     1074   1644   1285   -111    -17   -219       C  
ATOM   1444  C   CYS B   4     -28.700 -22.675  33.238  1.00  9.67           C  
ANISOU 1444  C   CYS B   4      996   1499   1178    -70     -5   -192       C  
ATOM   1445  O   CYS B   4     -27.608 -23.065  32.820  1.00  9.06           O  
ANISOU 1445  O   CYS B   4      969   1385   1087    -62     -1   -170       O  
ATOM   1446  CB  CYS B   4     -30.184 -24.666  33.394  1.00 10.27           C  
ANISOU 1446  CB  CYS B   4     1065   1600   1236   -174     18   -227       C  
ATOM   1447  SG  CYS B   4     -30.446 -24.587  35.176  1.00 11.93           S  
ANISOU 1447  SG  CYS B   4     1256   1826   1453   -193     61   -232       S  
ATOM   1448  N   ILE B   5     -28.849 -21.696  34.128  1.00  9.41           N  
ANISOU 1448  N   ILE B   5      932   1480   1165    -46      2   -197       N  
ATOM   1449  CA  ILE B   5     -27.728 -21.117  34.847  1.00  8.81           C  
ANISOU 1449  CA  ILE B   5      881   1376   1090    -21     15   -179       C  
ATOM   1450  C   ILE B   5     -27.936 -21.388  36.330  1.00  9.14           C  
ANISOU 1450  C   ILE B   5      917   1430   1127    -46     48   -190       C  
ATOM   1451  O   ILE B   5     -28.925 -20.937  36.914  1.00  9.06           O  
ANISOU 1451  O   ILE B   5      862   1452   1128    -49     58   -218       O  
ATOM   1452  CB  ILE B   5     -27.606 -19.594  34.650  1.00  8.50           C  
ANISOU 1452  CB  ILE B   5      825   1334   1073     27     -6   -177       C  
ATOM   1453  CG1 ILE B   5     -27.404 -19.240  33.176  1.00  9.02           C  
ANISOU 1453  CG1 ILE B   5      903   1387   1136     51    -39   -160       C  
ATOM   1454  CG2 ILE B   5     -26.425 -19.062  35.454  1.00  7.57           C  
ANISOU 1454  CG2 ILE B   5      733   1189    954     39      7   -162       C  
ATOM   1455  CD1 ILE B   5     -27.414 -17.736  32.912  1.00  7.98           C  
ANISOU 1455  CD1 ILE B   5      764   1244   1025     97    -61   -154       C  
ATOM   1456  N   THR B   6     -27.014 -22.138  36.926  1.00  8.86           N  
ANISOU 1456  N   THR B   6      927   1369   1072    -62     65   -169       N  
ATOM   1457  CA  THR B   6     -27.003 -22.324  38.366  1.00  9.23           C  
ANISOU 1457  CA  THR B   6      981   1424   1103    -83     92   -171       C  
ATOM   1458  C   THR B   6     -25.942 -21.427  38.986  1.00  8.93           C  
ANISOU 1458  C   THR B   6      954   1374   1064    -53     85   -160       C  
ATOM   1459  O   THR B   6     -24.870 -21.209  38.412  1.00  8.72           O  
ANISOU 1459  O   THR B   6      946   1324   1043    -28     67   -138       O  
ATOM   1460  CB  THR B   6     -26.739 -23.782  38.763  1.00  9.33           C  
ANISOU 1460  CB  THR B   6     1042   1416   1089   -121    110   -152       C  
ATOM   1461  OG1 THR B   6     -25.575 -24.263  38.081  1.00  9.32           O  
ANISOU 1461  OG1 THR B   6     1080   1375   1084    -98     95   -123       O  
ATOM   1462  CG2 THR B   6     -27.948 -24.668  38.420  1.00  9.86           C  
ANISOU 1462  CG2 THR B   6     1098   1497   1153   -171    124   -171       C  
ATOM   1463  N   VAL B   7     -26.261 -20.886  40.153  1.00  9.11           N  
ANISOU 1463  N   VAL B   7      965   1417   1079    -60    103   -179       N  
ATOM   1464  CA  VAL B   7     -25.300 -20.147  40.946  1.00  8.97           C  
ANISOU 1464  CA  VAL B   7      963   1391   1052    -46     98   -173       C  
ATOM   1465  C   VAL B   7     -24.672 -21.135  41.920  1.00  9.07           C  
ANISOU 1465  C   VAL B   7     1016   1402   1028    -72    107   -148       C  
ATOM   1466  O   VAL B   7     -25.369 -21.738  42.725  1.00  9.47           O  
ANISOU 1466  O   VAL B   7     1075   1470   1054   -106    134   -156       O  
ATOM   1467  CB  VAL B   7     -25.978 -18.985  41.683  1.00  9.32           C  
ANISOU 1467  CB  VAL B   7      980   1456   1104    -38    111   -212       C  
ATOM   1468  CG1 VAL B   7     -25.055 -18.389  42.748  1.00  8.33           C  
ANISOU 1468  CG1 VAL B   7      880   1327    958    -39    109   -213       C  
ATOM   1469  CG2 VAL B   7     -26.413 -17.929  40.668  1.00  9.56           C  
ANISOU 1469  CG2 VAL B   7      980   1478   1175      2     92   -227       C  
ATOM   1470  N   GLY B   8     -23.359 -21.328  41.818  1.00  8.77           N  
ANISOU 1470  N   GLY B   8     1003   1344    985    -55     86   -117       N  
ATOM   1471  CA  GLY B   8     -22.653 -22.255  42.704  1.00  9.06           C  
ANISOU 1471  CA  GLY B   8     1079   1377    987    -68     85    -87       C  
ATOM   1472  C   GLY B   8     -22.733 -21.806  44.154  1.00  9.33           C  
ANISOU 1472  C   GLY B   8     1121   1436    986    -88     94    -99       C  
ATOM   1473  O   GLY B   8     -22.817 -20.610  44.425  1.00  9.24           O  
ANISOU 1473  O   GLY B   8     1089   1440    984    -83     93   -129       O  
ATOM   1474  N   HIS B   9     -22.745 -22.773  45.071  1.00  9.61           N  
ANISOU 1474  N   HIS B   9     1196   1474    980   -114    104    -77       N  
ATOM   1475  CA  HIS B   9     -22.686 -22.529  46.518  1.00 10.15           C  
ANISOU 1475  CA  HIS B   9     1287   1570   1001   -137    110    -82       C  
ATOM   1476  C   HIS B   9     -24.026 -22.057  47.096  1.00 10.53           C  
ANISOU 1476  C   HIS B   9     1317   1647   1037   -170    153   -127       C  
ATOM   1477  O   HIS B   9     -25.039 -22.033  46.387  1.00 10.48           O  
ANISOU 1477  O   HIS B   9     1276   1643   1062   -174    175   -151       O  
ATOM   1478  CB  HIS B   9     -21.524 -21.577  46.842  1.00 10.15           C  
ANISOU 1478  CB  HIS B   9     1278   1580    999   -115     75    -83       C  
ATOM   1479  CG  HIS B   9     -20.218 -22.049  46.285  1.00  9.65           C  
ANISOU 1479  CG  HIS B   9     1218   1499    950    -83     37    -41       C  
ATOM   1480  ND1 HIS B   9     -19.597 -23.195  46.731  1.00 10.29           N  
ANISOU 1480  ND1 HIS B   9     1337   1571   1001    -76     21      4       N  
ATOM   1481  CD2 HIS B   9     -19.447 -21.571  45.283  1.00  9.43           C  
ANISOU 1481  CD2 HIS B   9     1159   1460    963    -53     17    -38       C  
ATOM   1482  CE1 HIS B   9     -18.481 -23.384  46.050  1.00  9.72           C  
ANISOU 1482  CE1 HIS B   9     1250   1488    956    -38     -8     30       C  
ATOM   1483  NE2 HIS B   9     -18.366 -22.412  45.164  1.00  9.42           N  
ANISOU 1483  NE2 HIS B   9     1169   1451    959    -27     -8      4       N  
ATOM   1484  N   SER B  10     -24.043 -21.730  48.388  1.00 10.90           N  
ANISOU 1484  N   SER B  10     1385   1722   1036   -193    166   -140       N  
ATOM   1485  CA  SER B  10     -25.271 -21.289  49.052  1.00 11.09           C  
ANISOU 1485  CA  SER B  10     1392   1780   1044   -222    215   -187       C  
ATOM   1486  C   SER B  10     -24.950 -20.562  50.346  1.00 11.69           C  
ANISOU 1486  C   SER B  10     1492   1883   1068   -235    219   -210       C  
ATOM   1487  O   SER B  10     -23.788 -20.477  50.750  1.00 11.24           O  
ANISOU 1487  O   SER B  10     1464   1820    985   -227    178   -185       O  
ATOM   1488  CB  SER B  10     -26.183 -22.490  49.346  1.00 11.58           C  
ANISOU 1488  CB  SER B  10     1472   1850   1077   -270    256   -173       C  
ATOM   1489  OG  SER B  10     -25.645 -23.344  50.345  1.00 11.26           O  
ANISOU 1489  OG  SER B  10     1500   1807    971   -300    252   -130       O  
ATOM   1490  N   ILE B  11     -25.984 -20.018  50.976  1.00 12.27           N  
ANISOU 1490  N   ILE B  11     1548   1989   1127   -255    268   -261       N  
ATOM   1491  CA  ILE B  11     -25.890 -19.539  52.356  1.00 13.00           C  
ANISOU 1491  CA  ILE B  11     1675   2112   1154   -280    285   -287       C  
ATOM   1492  C   ILE B  11     -26.697 -20.512  53.194  1.00 13.90           C  
ANISOU 1492  C   ILE B  11     1816   2255   1208   -335    336   -277       C  
ATOM   1493  O   ILE B  11     -27.905 -20.664  52.983  1.00 14.12           O  
ANISOU 1493  O   ILE B  11     1806   2304   1256   -352    388   -305       O  
ATOM   1494  CB  ILE B  11     -26.444 -18.108  52.523  1.00 13.28           C  
ANISOU 1494  CB  ILE B  11     1675   2159   1211   -259    312   -361       C  
ATOM   1495  CG1 ILE B  11     -25.572 -17.100  51.766  1.00 12.94           C  
ANISOU 1495  CG1 ILE B  11     1618   2078   1219   -214    261   -367       C  
ATOM   1496  CG2 ILE B  11     -26.498 -17.723  54.003  1.00 14.23           C  
ANISOU 1496  CG2 ILE B  11     1837   2315   1254   -293    341   -396       C  
ATOM   1497  CD1 ILE B  11     -26.112 -15.665  51.796  1.00 13.69           C  
ANISOU 1497  CD1 ILE B  11     1688   2167   1345   -185    284   -437       C  
ATOM   1498  N   LEU B  12     -26.030 -21.169  54.140  1.00 14.39           N  
ANISOU 1498  N   LEU B  12     1947   2325   1197   -366    321   -235       N  
ATOM   1499  CA  LEU B  12     -26.667 -22.179  54.989  1.00 15.20           C  
ANISOU 1499  CA  LEU B  12     2095   2449   1232   -426    367   -213       C  
ATOM   1500  C   LEU B  12     -27.528 -21.532  56.080  1.00 15.81           C  
ANISOU 1500  C   LEU B  12     2171   2580   1256   -462    432   -273       C  
ATOM   1501  O   LEU B  12     -27.497 -20.316  56.270  1.00 15.85           O  
ANISOU 1501  O   LEU B  12     2151   2599   1272   -436    435   -331       O  
ATOM   1502  CB  LEU B  12     -25.609 -23.092  55.626  1.00 15.37           C  
ANISOU 1502  CB  LEU B  12     2197   2454   1188   -438    321   -140       C  
ATOM   1503  CG  LEU B  12     -24.605 -23.776  54.684  1.00 15.61           C  
ANISOU 1503  CG  LEU B  12     2234   2433   1264   -395    257    -80       C  
ATOM   1504  CD1 LEU B  12     -23.574 -24.584  55.482  1.00 15.05           C  
ANISOU 1504  CD1 LEU B  12     2241   2354   1124   -397    210    -11       C  
ATOM   1505  CD2 LEU B  12     -25.319 -24.669  53.661  1.00 14.98           C  
ANISOU 1505  CD2 LEU B  12     2136   2320   1236   -402    282    -64       C  
ATOM   1506  N   LYS B  13     -28.285 -22.364  56.792  1.00 16.49           N  
ANISOU 1506  N   LYS B  13     2289   2692   1283   -524    489   -261       N  
ATOM   1507  CA  LYS B  13     -29.204 -21.920  57.848  1.00 17.35           C  
ANISOU 1507  CA  LYS B  13     2398   2860   1335   -567    565   -317       C  
ATOM   1508  C   LYS B  13     -28.480 -21.180  58.971  1.00 17.20           C  
ANISOU 1508  C   LYS B  13     2433   2862   1240   -567    548   -337       C  
ATOM   1509  O   LYS B  13     -29.050 -20.291  59.605  1.00 17.38           O  
ANISOU 1509  O   LYS B  13     2439   2924   1239   -574    599   -409       O  
ATOM   1510  CB  LYS B  13     -29.970 -23.122  58.420  1.00 18.35           C  
ANISOU 1510  CB  LYS B  13     2565   3008   1402   -645    625   -284       C  
ATOM   1511  CG  LYS B  13     -31.110 -22.740  59.352  1.00 20.88           C  
ANISOU 1511  CG  LYS B  13     2867   3396   1671   -695    721   -348       C  
ATOM   1512  CD  LYS B  13     -31.968 -23.948  59.734  1.00 23.30           C  
ANISOU 1512  CD  LYS B  13     3200   3723   1930   -782    787   -316       C  
ATOM   1513  CE  LYS B  13     -33.224 -23.517  60.485  1.00 25.20           C  
ANISOU 1513  CE  LYS B  13     3397   4041   2136   -829    894   -389       C  
ATOM   1514  NZ  LYS B  13     -34.057 -22.571  59.683  1.00 26.16           N  
ANISOU 1514  NZ  LYS B  13     3394   4189   2357   -775    920   -469       N  
ATOM   1515  N   SER B  14     -27.225 -21.555  59.202  1.00 16.57           N  
ANISOU 1515  N   SER B  14     2415   2758   1123   -559    474   -277       N  
ATOM   1516  CA  SER B  14     -26.355 -20.871  60.157  1.00 16.57           C  
ANISOU 1516  CA  SER B  14     2464   2778   1054   -560    437   -290       C  
ATOM   1517  C   SER B  14     -25.951 -19.465  59.708  1.00 16.00           C  
ANISOU 1517  C   SER B  14     2342   2694   1042   -509    408   -352       C  
ATOM   1518  O   SER B  14     -25.385 -18.705  60.489  1.00 16.08           O  
ANISOU 1518  O   SER B  14     2386   2724   1001   -516    387   -384       O  
ATOM   1519  CB  SER B  14     -25.072 -21.679  60.333  1.00 16.55           C  
ANISOU 1519  CB  SER B  14     2523   2753   1011   -554    353   -204       C  
ATOM   1520  OG  SER B  14     -24.278 -21.600  59.150  1.00 15.51           O  
ANISOU 1520  OG  SER B  14     2345   2576    970   -495    289   -180       O  
ATOM   1521  N   GLY B  15     -26.184 -19.153  58.436  1.00 15.51           N  
ANISOU 1521  N   GLY B  15     2210   2598   1087   -462    402   -365       N  
ATOM   1522  CA  GLY B  15     -25.661 -17.939  57.818  1.00 14.92           C  
ANISOU 1522  CA  GLY B  15     2096   2496   1076   -412    364   -406       C  
ATOM   1523  C   GLY B  15     -24.307 -18.107  57.147  1.00 14.29           C  
ANISOU 1523  C   GLY B  15     2019   2381   1030   -383    277   -350       C  
ATOM   1524  O   GLY B  15     -23.851 -17.205  56.442  1.00 13.80           O  
ANISOU 1524  O   GLY B  15     1923   2292   1030   -347    246   -373       O  
ATOM   1525  N   ALA B  16     -23.664 -19.254  57.354  1.00 14.16           N  
ANISOU 1525  N   ALA B  16     2043   2365    973   -398    240   -275       N  
ATOM   1526  CA  ALA B  16     -22.371 -19.527  56.756  1.00 13.99           C  
ANISOU 1526  CA  ALA B  16     2017   2317    981   -365    162   -221       C  
ATOM   1527  C   ALA B  16     -22.541 -19.666  55.250  1.00 13.31           C  
ANISOU 1527  C   ALA B  16     1873   2188    994   -323    160   -210       C  
ATOM   1528  O   ALA B  16     -23.470 -20.336  54.780  1.00 12.90           O  
ANISOU 1528  O   ALA B  16     1808   2126    967   -329    202   -202       O  
ATOM   1529  CB  ALA B  16     -21.771 -20.801  57.339  1.00 14.22           C  
ANISOU 1529  CB  ALA B  16     2105   2353    946   -380    127   -144       C  
ATOM   1530  N   CYS B  17     -21.660 -19.013  54.500  1.00 12.87           N  
ANISOU 1530  N   CYS B  17     1784   2112    993   -288    113   -212       N  
ATOM   1531  CA  CYS B  17     -21.673 -19.106  53.048  1.00 12.40           C  
ANISOU 1531  CA  CYS B  17     1677   2014   1020   -249    106   -198       C  
ATOM   1532  C   CYS B  17     -20.661 -20.165  52.630  1.00 12.06           C  
ANISOU 1532  C   CYS B  17     1644   1955    981   -229     57   -127       C  
ATOM   1533  O   CYS B  17     -19.537 -20.181  53.115  1.00 12.08           O  
ANISOU 1533  O   CYS B  17     1661   1973    954   -226      7   -101       O  
ATOM   1534  CB  CYS B  17     -21.346 -17.745  52.427  1.00 12.27           C  
ANISOU 1534  CB  CYS B  17     1623   1982   1059   -226     90   -240       C  
ATOM   1535  SG  CYS B  17     -21.318 -17.718  50.627  1.00 13.37           S  
ANISOU 1535  SG  CYS B  17     1711   2078   1294   -181     80   -224       S  
ATOM   1536  N   THR B  18     -21.070 -21.054  51.729  1.00 11.90           N  
ANISOU 1536  N   THR B  18     1615   1907   1000   -214     72    -99       N  
ATOM   1537  CA  THR B  18     -20.234 -22.178  51.307  1.00 11.46           C  
ANISOU 1537  CA  THR B  18     1576   1828    951   -188     36    -35       C  
ATOM   1538  C   THR B  18     -19.235 -21.805  50.207  1.00 11.06           C  
ANISOU 1538  C   THR B  18     1481   1760    962   -144     -2    -27       C  
ATOM   1539  O   THR B  18     -18.369 -22.607  49.863  1.00 11.10           O  
ANISOU 1539  O   THR B  18     1491   1751    975   -114    -34     20       O  
ATOM   1540  CB  THR B  18     -21.103 -23.339  50.815  1.00 11.56           C  
ANISOU 1540  CB  THR B  18     1607   1810    973   -197     73    -13       C  
ATOM   1541  OG1 THR B  18     -21.893 -22.906  49.697  1.00 10.93           O  
ANISOU 1541  OG1 THR B  18     1479   1718    957   -189    100    -50       O  
ATOM   1542  CG2 THR B  18     -22.024 -23.823  51.931  1.00 11.31           C  
ANISOU 1542  CG2 THR B  18     1623   1799    877   -250    115    -14       C  
ATOM   1543  N   SER B  19     -19.335 -20.589  49.673  1.00 10.64           N  
ANISOU 1543  N   SER B  19     1386   1708    950   -140      3    -71       N  
ATOM   1544  CA  SER B  19     -18.447 -20.154  48.595  1.00 10.20           C  
ANISOU 1544  CA  SER B  19     1290   1637    948   -108    -25    -64       C  
ATOM   1545  C   SER B  19     -17.086 -19.667  49.097  1.00 10.43           C  
ANISOU 1545  C   SER B  19     1308   1693    962   -108    -74    -55       C  
ATOM   1546  O   SER B  19     -16.876 -19.468  50.302  1.00 10.40           O  
ANISOU 1546  O   SER B  19     1329   1719    903   -133    -91    -62       O  
ATOM   1547  CB  SER B  19     -19.104 -19.039  47.778  1.00 10.01           C  
ANISOU 1547  CB  SER B  19     1234   1596    973   -105     -2   -110       C  
ATOM   1548  OG  SER B  19     -18.859 -17.766  48.357  1.00 10.24           O  
ANISOU 1548  OG  SER B  19     1260   1638    994   -122    -10   -149       O  
ATOM   1549  N   ALA B  20     -16.169 -19.462  48.151  1.00  9.98           N  
ANISOU 1549  N   ALA B  20     1212   1629    951    -83    -97    -41       N  
ATOM   1550  CA  ALA B  20     -14.902 -18.801  48.448  1.00 10.05           C  
ANISOU 1550  CA  ALA B  20     1195   1668    957    -90   -141    -41       C  
ATOM   1551  C   ALA B  20     -15.199 -17.332  48.717  1.00 10.27           C  
ANISOU 1551  C   ALA B  20     1220   1694    986   -127   -131    -97       C  
ATOM   1552  O   ALA B  20     -16.261 -16.822  48.343  1.00  9.62           O  
ANISOU 1552  O   ALA B  20     1146   1582    925   -129    -92   -129       O  
ATOM   1553  CB  ALA B  20     -13.919 -18.949  47.291  1.00  9.78           C  
ANISOU 1553  CB  ALA B  20     1114   1629    974    -59   -156    -16       C  
ATOM   1554  N   ASP B  21     -14.266 -16.662  49.379  1.00 10.83           N  
ANISOU 1554  N   ASP B  21     1281   1796   1036   -154   -169   -108       N  
ATOM   1555  CA  ASP B  21     -14.442 -15.266  49.757  1.00 11.47           C  
ANISOU 1555  CA  ASP B  21     1373   1870   1114   -194   -163   -164       C  
ATOM   1556  C   ASP B  21     -13.079 -14.595  49.807  1.00 11.79           C  
ANISOU 1556  C   ASP B  21     1381   1938   1162   -222   -209   -166       C  
ATOM   1557  O   ASP B  21     -12.234 -14.969  50.619  1.00 12.47           O  
ANISOU 1557  O   ASP B  21     1459   2074   1207   -234   -254   -148       O  
ATOM   1558  CB  ASP B  21     -15.129 -15.191  51.125  1.00 12.07           C  
ANISOU 1558  CB  ASP B  21     1497   1965   1123   -221   -153   -195       C  
ATOM   1559  CG  ASP B  21     -15.539 -13.771  51.510  1.00 13.19           C  
ANISOU 1559  CG  ASP B  21     1660   2088   1262   -254   -134   -263       C  
ATOM   1560  OD1 ASP B  21     -16.395 -13.175  50.830  1.00 13.51           O  
ANISOU 1560  OD1 ASP B  21     1702   2084   1347   -238    -94   -291       O  
ATOM   1561  OD2 ASP B  21     -15.023 -13.263  52.521  1.00 14.82           O  
ANISOU 1561  OD2 ASP B  21     1887   2323   1420   -295   -161   -289       O  
ATOM   1562  N   GLY B  22     -12.862 -13.605  48.944  1.00 11.58           N  
ANISOU 1562  N   GLY B  22     1336   1881   1185   -235   -198   -187       N  
ATOM   1563  CA  GLY B  22     -11.603 -12.855  48.933  1.00 11.88           C  
ANISOU 1563  CA  GLY B  22     1340   1943   1232   -276   -235   -194       C  
ATOM   1564  C   GLY B  22     -11.865 -11.362  48.947  1.00 11.85           C  
ANISOU 1564  C   GLY B  22     1365   1896   1242   -321   -219   -249       C  
ATOM   1565  O   GLY B  22     -12.462 -10.844  49.888  1.00 12.18           O  
ANISOU 1565  O   GLY B  22     1453   1928   1246   -343   -212   -293       O  
ATOM   1566  N   VAL B  23     -11.428 -10.670  47.895  1.00 11.35           N  
ANISOU 1566  N   VAL B  23     1281   1802   1229   -334   -210   -246       N  
ATOM   1567  CA  VAL B  23     -11.752  -9.263  47.718  1.00 11.19           C  
ANISOU 1567  CA  VAL B  23     1300   1722   1230   -369   -191   -292       C  
ATOM   1568  C   VAL B  23     -13.216  -9.119  47.299  1.00 10.60           C  
ANISOU 1568  C   VAL B  23     1266   1588   1176   -321   -145   -306       C  
ATOM   1569  O   VAL B  23     -13.776  -8.028  47.360  1.00 10.74           O  
ANISOU 1569  O   VAL B  23     1327   1550   1205   -333   -126   -349       O  
ATOM   1570  CB  VAL B  23     -10.811  -8.564  46.702  1.00 11.41           C  
ANISOU 1570  CB  VAL B  23     1300   1733   1304   -404   -194   -278       C  
ATOM   1571  CG1 VAL B  23      -9.377  -8.611  47.202  1.00 11.85           C  
ANISOU 1571  CG1 VAL B  23     1304   1858   1341   -458   -240   -272       C  
ATOM   1572  CG2 VAL B  23     -10.930  -9.180  45.309  1.00 10.68           C  
ANISOU 1572  CG2 VAL B  23     1179   1627   1252   -355   -169   -230       C  
ATOM   1573  N   VAL B  24     -13.822 -10.227  46.872  1.00  9.89           N  
ANISOU 1573  N   VAL B  24     1159   1509   1090   -267   -129   -272       N  
ATOM   1574  CA  VAL B  24     -15.264 -10.311  46.642  1.00  9.71           C  
ANISOU 1574  CA  VAL B  24     1161   1450   1078   -223    -91   -286       C  
ATOM   1575  C   VAL B  24     -15.766 -11.668  47.131  1.00  9.80           C  
ANISOU 1575  C   VAL B  24     1165   1502   1056   -196    -86   -264       C  
ATOM   1576  O   VAL B  24     -15.000 -12.632  47.168  1.00  9.42           O  
ANISOU 1576  O   VAL B  24     1091   1494    994   -193   -110   -224       O  
ATOM   1577  CB  VAL B  24     -15.616 -10.120  45.140  1.00  9.54           C  
ANISOU 1577  CB  VAL B  24     1131   1383   1109   -191    -72   -263       C  
ATOM   1578  CG1 VAL B  24     -15.107 -11.290  44.289  1.00  8.40           C  
ANISOU 1578  CG1 VAL B  24      947   1268    976   -168    -79   -208       C  
ATOM   1579  CG2 VAL B  24     -17.122  -9.940  44.959  1.00  9.14           C  
ANISOU 1579  CG2 VAL B  24     1102   1297   1073   -148    -40   -286       C  
ATOM   1580  N   ASN B  25     -17.038 -11.737  47.534  1.00 10.01           N  
ANISOU 1580  N   ASN B  25     1214   1518   1071   -177    -53   -291       N  
ATOM   1581  CA  ASN B  25     -17.655 -13.013  47.869  1.00  9.91           C  
ANISOU 1581  CA  ASN B  25     1199   1536   1031   -158    -40   -269       C  
ATOM   1582  C   ASN B  25     -18.102 -13.691  46.585  1.00  9.44           C  
ANISOU 1582  C   ASN B  25     1115   1458   1012   -120    -26   -235       C  
ATOM   1583  O   ASN B  25     -18.846 -13.103  45.802  1.00  9.76           O  
ANISOU 1583  O   ASN B  25     1153   1464   1092    -98     -7   -251       O  
ATOM   1584  CB  ASN B  25     -18.849 -12.838  48.802  1.00 10.03           C  
ANISOU 1584  CB  ASN B  25     1241   1556   1015   -160     -4   -314       C  
ATOM   1585  CG  ASN B  25     -19.372 -14.160  49.322  1.00 10.61           C  
ANISOU 1585  CG  ASN B  25     1318   1664   1049   -159     11   -290       C  
ATOM   1586  OD1 ASN B  25     -18.852 -14.705  50.300  1.00 13.72           O  
ANISOU 1586  OD1 ASN B  25     1732   2094   1388   -183     -8   -275       O  
ATOM   1587  ND2 ASN B  25     -20.400 -14.686  48.677  1.00  5.83           N  
ANISOU 1587  ND2 ASN B  25      697   1049    470   -133     42   -283       N  
ATOM   1588  N   GLU B  26     -17.641 -14.922  46.378  1.00  8.92           N  
ANISOU 1588  N   GLU B  26     1037   1414    937   -109    -39   -189       N  
ATOM   1589  CA  GLU B  26     -17.962 -15.698  45.190  1.00  8.65           C  
ANISOU 1589  CA  GLU B  26      987   1365    936    -78    -28   -159       C  
ATOM   1590  C   GLU B  26     -19.473 -15.829  44.972  1.00  8.39           C  
ANISOU 1590  C   GLU B  26      958   1319    912    -65      7   -180       C  
ATOM   1591  O   GLU B  26     -19.977 -15.538  43.883  1.00  8.60           O  
ANISOU 1591  O   GLU B  26      971   1320    975    -43     15   -182       O  
ATOM   1592  CB  GLU B  26     -17.306 -17.089  45.283  1.00  8.52           C  
ANISOU 1592  CB  GLU B  26      968   1369    898    -68    -43   -113       C  
ATOM   1593  CG  GLU B  26     -17.800 -18.090  44.264  1.00  8.06           C  
ANISOU 1593  CG  GLU B  26      907   1292    861    -42    -26    -89       C  
ATOM   1594  CD  GLU B  26     -17.106 -19.441  44.337  1.00  7.09           C  
ANISOU 1594  CD  GLU B  26      793   1179    723    -25    -39    -46       C  
ATOM   1595  OE1 GLU B  26     -16.427 -19.754  45.333  1.00  5.90           O  
ANISOU 1595  OE1 GLU B  26      651   1052    539    -31    -63    -30       O  
ATOM   1596  OE2 GLU B  26     -17.256 -20.217  43.377  1.00  8.71           O  
ANISOU 1596  OE2 GLU B  26      998   1364    949     -3    -28    -28       O  
ATOM   1597  N   TYR B  27     -20.191 -16.257  46.006  1.00  8.60           N  
ANISOU 1597  N   TYR B  27     1001   1367    901    -80     27   -196       N  
ATOM   1598  CA  TYR B  27     -21.634 -16.471  45.894  1.00  8.40           C  
ANISOU 1598  CA  TYR B  27      967   1341    883    -73     63   -218       C  
ATOM   1599  C   TYR B  27     -22.408 -15.170  45.606  1.00  8.63           C  
ANISOU 1599  C   TYR B  27      983   1352    946    -55     78   -264       C  
ATOM   1600  O   TYR B  27     -23.317 -15.170  44.783  1.00  8.48           O  
ANISOU 1600  O   TYR B  27      939   1323    959    -31     90   -270       O  
ATOM   1601  CB  TYR B  27     -22.180 -17.175  47.155  1.00  8.97           C  
ANISOU 1601  CB  TYR B  27     1061   1445    901   -102     87   -225       C  
ATOM   1602  CG  TYR B  27     -23.685 -17.217  47.245  1.00  8.62           C  
ANISOU 1602  CG  TYR B  27     1000   1413    862   -105    132   -259       C  
ATOM   1603  CD1 TYR B  27     -24.408 -18.237  46.641  1.00  9.68           C  
ANISOU 1603  CD1 TYR B  27     1120   1550   1008   -108    147   -241       C  
ATOM   1604  CD2 TYR B  27     -24.390 -16.225  47.920  1.00  9.29           C  
ANISOU 1604  CD2 TYR B  27     1079   1510    943   -105    160   -314       C  
ATOM   1605  CE1 TYR B  27     -25.795 -18.279  46.710  1.00  9.87           C  
ANISOU 1605  CE1 TYR B  27     1116   1596   1039   -116    187   -274       C  
ATOM   1606  CE2 TYR B  27     -25.787 -16.258  47.999  1.00  9.69           C  
ANISOU 1606  CE2 TYR B  27     1100   1581   1002   -103    204   -348       C  
ATOM   1607  CZ  TYR B  27     -26.481 -17.296  47.395  1.00 10.32           C  
ANISOU 1607  CZ  TYR B  27     1157   1671   1093   -111    216   -327       C  
ATOM   1608  OH  TYR B  27     -27.859 -17.351  47.458  1.00 10.32           O  
ANISOU 1608  OH  TYR B  27     1116   1702   1104   -115    258   -362       O  
ATOM   1609  N   GLN B  28     -22.054 -14.070  46.264  1.00  8.50           N  
ANISOU 1609  N   GLN B  28      983   1327    922    -63     74   -296       N  
ATOM   1610  CA  GLN B  28     -22.756 -12.807  46.034  1.00  9.26           C  
ANISOU 1610  CA  GLN B  28     1075   1393   1052    -38     88   -340       C  
ATOM   1611  C   GLN B  28     -22.499 -12.298  44.621  1.00  9.17           C  
ANISOU 1611  C   GLN B  28     1053   1341   1090    -10     66   -318       C  
ATOM   1612  O   GLN B  28     -23.433 -11.866  43.937  1.00  9.36           O  
ANISOU 1612  O   GLN B  28     1061   1346   1149     26     75   -331       O  
ATOM   1613  CB  GLN B  28     -22.359 -11.748  47.067  1.00  9.83           C  
ANISOU 1613  CB  GLN B  28     1179   1456   1102    -58     89   -384       C  
ATOM   1614  CG  GLN B  28     -22.787 -12.086  48.493  1.00 10.18           C  
ANISOU 1614  CG  GLN B  28     1240   1541   1089    -85    117   -415       C  
ATOM   1615  CD  GLN B  28     -24.297 -12.115  48.682  1.00 10.84           C  
ANISOU 1615  CD  GLN B  28     1300   1639   1178    -61    166   -453       C  
ATOM   1616  OE1 GLN B  28     -25.049 -11.520  47.904  1.00 10.37           O  
ANISOU 1616  OE1 GLN B  28     1215   1553   1170    -18    175   -471       O  
ATOM   1617  NE2 GLN B  28     -24.748 -12.800  49.740  1.00  9.48           N  
ANISOU 1617  NE2 GLN B  28     1136   1514    953    -90    198   -465       N  
ATOM   1618  N   TYR B  29     -21.246 -12.376  44.174  1.00  8.89           N  
ANISOU 1618  N   TYR B  29     1025   1297   1056    -27     37   -282       N  
ATOM   1619  CA  TYR B  29     -20.905 -11.951  42.815  1.00  8.98           C  
ANISOU 1619  CA  TYR B  29     1033   1273   1106     -9     21   -256       C  
ATOM   1620  C   TYR B  29     -21.696 -12.702  41.748  1.00  8.63           C  
ANISOU 1620  C   TYR B  29      965   1233   1079     21     25   -234       C  
ATOM   1621  O   TYR B  29     -22.198 -12.093  40.803  1.00  8.68           O  
ANISOU 1621  O   TYR B  29      971   1212   1117     50     20   -233       O  
ATOM   1622  CB  TYR B  29     -19.406 -12.101  42.516  1.00  9.11           C  
ANISOU 1622  CB  TYR B  29     1050   1294   1118    -36     -3   -221       C  
ATOM   1623  CG  TYR B  29     -19.090 -11.643  41.112  1.00  9.70           C  
ANISOU 1623  CG  TYR B  29     1125   1336   1226    -23    -11   -195       C  
ATOM   1624  CD1 TYR B  29     -18.968 -10.291  40.819  1.00 11.30           C  
ANISOU 1624  CD1 TYR B  29     1352   1491   1450    -28    -14   -208       C  
ATOM   1625  CD2 TYR B  29     -18.976 -12.555  40.068  1.00 11.04           C  
ANISOU 1625  CD2 TYR B  29     1278   1516   1400     -8    -12   -158       C  
ATOM   1626  CE1 TYR B  29     -18.704  -9.856  39.531  1.00 12.30           C  
ANISOU 1626  CE1 TYR B  29     1488   1585   1599    -21    -20   -179       C  
ATOM   1627  CE2 TYR B  29     -18.722 -12.133  38.771  1.00 11.96           C  
ANISOU 1627  CE2 TYR B  29     1401   1607   1537      0    -16   -134       C  
ATOM   1628  CZ  TYR B  29     -18.585 -10.778  38.510  1.00 12.21           C  
ANISOU 1628  CZ  TYR B  29     1458   1595   1588     -7    -20   -142       C  
ATOM   1629  OH  TYR B  29     -18.336 -10.341  37.231  1.00 13.47           O  
ANISOU 1629  OH  TYR B  29     1632   1726   1761     -3    -23   -113       O  
ATOM   1630  N   ASN B  30     -21.794 -14.019  41.890  1.00  8.31           N  
ANISOU 1630  N   ASN B  30      913   1227   1018     12     31   -215       N  
ATOM   1631  CA  ASN B  30     -22.481 -14.838  40.895  1.00  8.39           C  
ANISOU 1631  CA  ASN B  30      906   1242   1040     29     34   -197       C  
ATOM   1632  C   ASN B  30     -24.001 -14.736  40.972  1.00  8.48           C  
ANISOU 1632  C   ASN B  30      893   1265   1063     46     52   -229       C  
ATOM   1633  O   ASN B  30     -24.685 -14.887  39.956  1.00  8.29           O  
ANISOU 1633  O   ASN B  30      852   1240   1059     67     45   -223       O  
ATOM   1634  CB  ASN B  30     -21.987 -16.284  40.958  1.00  7.92           C  
ANISOU 1634  CB  ASN B  30      850   1203    957     12     35   -166       C  
ATOM   1635  CG  ASN B  30     -20.553 -16.409  40.495  1.00  8.55           C  
ANISOU 1635  CG  ASN B  30      937   1275   1037     10     16   -133       C  
ATOM   1636  OD1 ASN B  30     -19.697 -16.994  41.182  1.00 10.56           O  
ANISOU 1636  OD1 ASN B  30     1198   1545   1269     -2     10   -117       O  
ATOM   1637  ND2 ASN B  30     -20.268 -15.831  39.338  1.00  6.71           N  
ANISOU 1637  ND2 ASN B  30      702   1020    828     24      7   -122       N  
ATOM   1638  N   LYS B  31     -24.512 -14.453  42.168  1.00  9.14           N  
ANISOU 1638  N   LYS B  31      975   1365   1132     38     74   -265       N  
ATOM   1639  CA  LYS B  31     -25.918 -14.085  42.362  1.00  9.80           C  
ANISOU 1639  CA  LYS B  31     1028   1464   1232     59     97   -306       C  
ATOM   1640  C   LYS B  31     -26.279 -12.853  41.533  1.00 10.26           C  
ANISOU 1640  C   LYS B  31     1079   1487   1332    108     80   -317       C  
ATOM   1641  O   LYS B  31     -27.397 -12.749  41.020  1.00 10.42           O  
ANISOU 1641  O   LYS B  31     1063   1519   1378    140     81   -331       O  
ATOM   1642  CB  LYS B  31     -26.185 -13.804  43.840  1.00 10.17           C  
ANISOU 1642  CB  LYS B  31     1083   1532   1251     42    129   -347       C  
ATOM   1643  CG  LYS B  31     -27.637 -13.588  44.210  1.00 10.87           C  
ANISOU 1643  CG  LYS B  31     1130   1648   1350     61    164   -393       C  
ATOM   1644  CD  LYS B  31     -27.797 -13.461  45.718  1.00 11.75           C  
ANISOU 1644  CD  LYS B  31     1257   1786   1422     35    204   -433       C  
ATOM   1645  CE  LYS B  31     -29.228 -13.108  46.090  1.00 13.37           C  
ANISOU 1645  CE  LYS B  31     1415   2024   1643     59    247   -487       C  
ATOM   1646  NZ  LYS B  31     -29.389 -12.962  47.558  1.00 13.62           N  
ANISOU 1646  NZ  LYS B  31     1465   2083   1627     32    293   -530       N  
ATOM   1647  N   SER B  32     -25.333 -11.921  41.416  1.00 10.25           N  
ANISOU 1647  N   SER B  32     1114   1442   1339    111     62   -309       N  
ATOM   1648  CA  SER B  32     -25.539 -10.694  40.641  1.00 10.91           C  
ANISOU 1648  CA  SER B  32     1209   1477   1459    153     45   -313       C  
ATOM   1649  C   SER B  32     -25.306 -10.914  39.148  1.00 10.43           C  
ANISOU 1649  C   SER B  32     1150   1402   1412    165     15   -266       C  
ATOM   1650  O   SER B  32     -26.015 -10.343  38.326  1.00 11.03           O  
ANISOU 1650  O   SER B  32     1218   1459   1515    209     -2   -263       O  
ATOM   1651  CB  SER B  32     -24.625  -9.566  41.137  1.00 11.08           C  
ANISOU 1651  CB  SER B  32     1278   1451   1481    140     42   -325       C  
ATOM   1652  OG  SER B  32     -24.977  -9.158  42.443  1.00 12.17           O  
ANISOU 1652  OG  SER B  32     1422   1596   1607    136     69   -378       O  
ATOM   1653  N   LEU B  33     -24.316 -11.733  38.803  1.00  9.84           N  
ANISOU 1653  N   LEU B  33     1085   1338   1316    130      8   -230       N  
ATOM   1654  CA  LEU B  33     -23.970 -11.980  37.394  1.00  9.42           C  
ANISOU 1654  CA  LEU B  33     1039   1274   1267    136    -14   -188       C  
ATOM   1655  C   LEU B  33     -25.045 -12.789  36.663  1.00  9.47           C  
ANISOU 1655  C   LEU B  33     1012   1311   1274    154    -21   -185       C  
ATOM   1656  O   LEU B  33     -25.383 -12.484  35.512  1.00  9.37           O  
ANISOU 1656  O   LEU B  33     1003   1286   1272    180    -44   -167       O  
ATOM   1657  CB  LEU B  33     -22.621 -12.704  37.283  1.00  9.00           C  
ANISOU 1657  CB  LEU B  33      998   1229   1191     99    -12   -157       C  
ATOM   1658  CG  LEU B  33     -22.120 -13.050  35.865  1.00  8.84           C  
ANISOU 1658  CG  LEU B  33      988   1203   1168    100    -24   -118       C  
ATOM   1659  CD1 LEU B  33     -22.027 -11.804  34.990  1.00  7.82           C  
ANISOU 1659  CD1 LEU B  33      887   1030   1054    116    -40   -103       C  
ATOM   1660  CD2 LEU B  33     -20.778 -13.761  35.920  1.00  7.34           C  
ANISOU 1660  CD2 LEU B  33      801   1027    960     70    -16    -96       C  
ATOM   1661  N   ALA B  34     -25.567 -13.814  37.335  1.00  9.12           N  
ANISOU 1661  N   ALA B  34      941   1307   1216    135     -2   -202       N  
ATOM   1662  CA  ALA B  34     -26.488 -14.769  36.727  1.00  9.17           C  
ANISOU 1662  CA  ALA B  34      917   1347   1219    133     -6   -201       C  
ATOM   1663  C   ALA B  34     -27.653 -14.115  35.984  1.00  9.49           C  
ANISOU 1663  C   ALA B  34      927   1393   1286    176    -28   -213       C  
ATOM   1664  O   ALA B  34     -27.881 -14.431  34.820  1.00  9.57           O  
ANISOU 1664  O   ALA B  34      935   1409   1293    183    -54   -193       O  
ATOM   1665  CB  ALA B  34     -27.006 -15.760  37.784  1.00  8.90           C  
ANISOU 1665  CB  ALA B  34      862   1352   1169    100     25   -223       C  
ATOM   1666  N   PRO B  35     -28.396 -13.205  36.645  1.00 10.00           N  
ANISOU 1666  N   PRO B  35      968   1457   1374    210    -20   -247       N  
ATOM   1667  CA  PRO B  35     -29.506 -12.576  35.928  1.00 10.40           C  
ANISOU 1667  CA  PRO B  35      984   1514   1453    263    -47   -255       C  
ATOM   1668  C   PRO B  35     -29.055 -11.731  34.732  1.00 10.41           C  
ANISOU 1668  C   PRO B  35     1027   1468   1462    297    -87   -218       C  
ATOM   1669  O   PRO B  35     -29.755 -11.681  33.730  1.00 10.78           O  
ANISOU 1669  O   PRO B  35     1053   1528   1515    327   -123   -205       O  
ATOM   1670  CB  PRO B  35     -30.191 -11.711  36.996  1.00 10.85           C  
ANISOU 1670  CB  PRO B  35     1015   1572   1535    297    -23   -302       C  
ATOM   1671  CG  PRO B  35     -29.195 -11.559  38.083  1.00 10.79           C  
ANISOU 1671  CG  PRO B  35     1051   1540   1509    263      8   -311       C  
ATOM   1672  CD  PRO B  35     -28.354 -12.794  38.058  1.00 10.13           C  
ANISOU 1672  CD  PRO B  35      986   1473   1390    203     13   -282       C  
ATOM   1673  N   VAL B  36     -27.895 -11.089  34.829  1.00 10.30           N  
ANISOU 1673  N   VAL B  36     1070   1402   1444    286    -83   -199       N  
ATOM   1674  CA  VAL B  36     -27.342 -10.333  33.697  1.00 10.20           C  
ANISOU 1674  CA  VAL B  36     1104   1340   1430    304   -113   -158       C  
ATOM   1675  C   VAL B  36     -26.918 -11.274  32.553  1.00  9.64           C  
ANISOU 1675  C   VAL B  36     1043   1290   1327    275   -128   -121       C  
ATOM   1676  O   VAL B  36     -27.211 -11.004  31.380  1.00  9.22           O  
ANISOU 1676  O   VAL B  36     1004   1229   1268    300   -163    -93       O  
ATOM   1677  CB  VAL B  36     -26.158  -9.444  34.129  1.00 10.49           C  
ANISOU 1677  CB  VAL B  36     1197   1320   1469    285    -99   -150       C  
ATOM   1678  CG1 VAL B  36     -25.507  -8.767  32.914  1.00  9.96           C  
ANISOU 1678  CG1 VAL B  36     1184   1205   1394    288   -123   -102       C  
ATOM   1679  CG2 VAL B  36     -26.627  -8.394  35.153  1.00 11.04           C  
ANISOU 1679  CG2 VAL B  36     1269   1358   1567    317    -86   -191       C  
ATOM   1680  N   LEU B  37     -26.255 -12.378  32.895  1.00  8.88           N  
ANISOU 1680  N   LEU B  37      945   1220   1209    226   -103   -121       N  
ATOM   1681  CA  LEU B  37     -25.890 -13.392  31.892  1.00  8.91           C  
ANISOU 1681  CA  LEU B  37      959   1243   1183    201   -109    -96       C  
ATOM   1682  C   LEU B  37     -27.135 -13.947  31.190  1.00  9.19           C  
ANISOU 1682  C   LEU B  37      960   1317   1214    215   -136   -104       C  
ATOM   1683  O   LEU B  37     -27.155 -14.101  29.968  1.00  9.59           O  
ANISOU 1683  O   LEU B  37     1029   1370   1243    218   -162    -81       O  
ATOM   1684  CB  LEU B  37     -25.087 -14.528  32.539  1.00  8.16           C  
ANISOU 1684  CB  LEU B  37      865   1165   1071    157    -77   -100       C  
ATOM   1685  CG  LEU B  37     -24.584 -15.658  31.628  1.00  8.19           C  
ANISOU 1685  CG  LEU B  37      886   1181   1046    134    -75    -80       C  
ATOM   1686  CD1 LEU B  37     -23.662 -15.121  30.554  1.00  7.20           C  
ANISOU 1686  CD1 LEU B  37      799   1030    907    137    -81    -47       C  
ATOM   1687  CD2 LEU B  37     -23.867 -16.737  32.434  1.00  6.72           C  
ANISOU 1687  CD2 LEU B  37      699   1003    849    104    -45    -85       C  
ATOM   1688  N   ALA B  38     -28.170 -14.241  31.971  1.00  9.62           N  
ANISOU 1688  N   ALA B  38      962   1406   1285    219   -129   -140       N  
ATOM   1689  CA  ALA B  38     -29.437 -14.728  31.427  1.00 10.14           C  
ANISOU 1689  CA  ALA B  38      982   1520   1353    226   -155   -155       C  
ATOM   1690  C   ALA B  38     -29.998 -13.736  30.418  1.00 10.90           C  
ANISOU 1690  C   ALA B  38     1076   1606   1457    281   -205   -137       C  
ATOM   1691  O   ALA B  38     -30.370 -14.110  29.299  1.00 11.03           O  
ANISOU 1691  O   ALA B  38     1092   1645   1452    279   -241   -122       O  
ATOM   1692  CB  ALA B  38     -30.438 -14.962  32.551  1.00 10.52           C  
ANISOU 1692  CB  ALA B  38      967   1607   1423    222   -131   -198       C  
ATOM   1693  N   ASP B  39     -30.034 -12.462  30.805  1.00 11.14           N  
ANISOU 1693  N   ASP B  39     1116   1600   1518    329   -208   -137       N  
ATOM   1694  CA  ASP B  39     -30.556 -11.419  29.933  1.00 12.09           C  
ANISOU 1694  CA  ASP B  39     1245   1700   1650    391   -258   -115       C  
ATOM   1695  C   ASP B  39     -29.753 -11.300  28.637  1.00 11.92           C  
ANISOU 1695  C   ASP B  39     1291   1647   1591    380   -283    -63       C  
ATOM   1696  O   ASP B  39     -30.321 -11.060  27.576  1.00 11.94           O  
ANISOU 1696  O   ASP B  39     1297   1661   1580    412   -334    -40       O  
ATOM   1697  CB  ASP B  39     -30.615 -10.067  30.662  1.00 12.40           C  
ANISOU 1697  CB  ASP B  39     1296   1688   1728    444   -250   -126       C  
ATOM   1698  CG  ASP B  39     -31.780  -9.981  31.644  1.00 14.51           C  
ANISOU 1698  CG  ASP B  39     1486   1993   2033    478   -235   -178       C  
ATOM   1699  OD1 ASP B  39     -32.738 -10.786  31.522  1.00 15.18           O  
ANISOU 1699  OD1 ASP B  39     1500   2149   2117    471   -245   -199       O  
ATOM   1700  OD2 ASP B  39     -31.748  -9.096  32.529  1.00 15.05           O  
ANISOU 1700  OD2 ASP B  39     1563   2024   2130    509   -211   -202       O  
ATOM   1701  N   THR B  40     -28.440 -11.485  28.727  1.00 11.34           N  
ANISOU 1701  N   THR B  40     1268   1542   1497    335   -249    -46       N  
ATOM   1702  CA  THR B  40     -27.571 -11.396  27.555  1.00 11.39           C  
ANISOU 1702  CA  THR B  40     1339   1525   1465    317   -260     -1       C  
ATOM   1703  C   THR B  40     -27.855 -12.537  26.561  1.00 11.59           C  
ANISOU 1703  C   THR B  40     1356   1599   1448    292   -278      3       C  
ATOM   1704  O   THR B  40     -27.862 -12.316  25.351  1.00 12.10           O  
ANISOU 1704  O   THR B  40     1458   1660   1478    300   -311     36       O  
ATOM   1705  CB  THR B  40     -26.080 -11.363  27.974  1.00 11.29           C  
ANISOU 1705  CB  THR B  40     1366   1478   1445    273   -213     10       C  
ATOM   1706  OG1 THR B  40     -25.901 -10.354  28.976  1.00 10.71           O  
ANISOU 1706  OG1 THR B  40     1299   1362   1408    289   -199     -2       O  
ATOM   1707  CG2 THR B  40     -25.176 -11.060  26.771  1.00 10.23           C  
ANISOU 1707  CG2 THR B  40     1296   1317   1273    256   -217     57       C  
ATOM   1708  N   PHE B  41     -28.114 -13.741  27.073  1.00 11.57           N  
ANISOU 1708  N   PHE B  41     1312   1639   1446    258   -256    -31       N  
ATOM   1709  CA  PHE B  41     -28.600 -14.846  26.239  1.00 11.83           C  
ANISOU 1709  CA  PHE B  41     1335   1717   1444    231   -276    -39       C  
ATOM   1710  C   PHE B  41     -29.985 -14.556  25.649  1.00 12.91           C  
ANISOU 1710  C   PHE B  41     1430   1892   1583    266   -336    -44       C  
ATOM   1711  O   PHE B  41     -30.229 -14.796  24.455  1.00 13.22           O  
ANISOU 1711  O   PHE B  41     1489   1953   1581    262   -375    -27       O  
ATOM   1712  CB  PHE B  41     -28.668 -16.150  27.039  1.00 11.47           C  
ANISOU 1712  CB  PHE B  41     1257   1698   1401    185   -239    -75       C  
ATOM   1713  CG  PHE B  41     -27.360 -16.891  27.125  1.00 10.41           C  
ANISOU 1713  CG  PHE B  41     1169   1541   1247    148   -194    -67       C  
ATOM   1714  CD1 PHE B  41     -26.743 -17.366  25.980  1.00  9.43           C  
ANISOU 1714  CD1 PHE B  41     1092   1412   1080    130   -194    -49       C  
ATOM   1715  CD2 PHE B  41     -26.776 -17.150  28.359  1.00  9.17           C  
ANISOU 1715  CD2 PHE B  41     1003   1369   1111    133   -151    -79       C  
ATOM   1716  CE1 PHE B  41     -25.548 -18.060  26.052  1.00 10.01           C  
ANISOU 1716  CE1 PHE B  41     1198   1467   1138    105   -151    -45       C  
ATOM   1717  CE2 PHE B  41     -25.581 -17.847  28.449  1.00  9.38           C  
ANISOU 1717  CE2 PHE B  41     1063   1379   1123    108   -116    -70       C  
ATOM   1718  CZ  PHE B  41     -24.962 -18.305  27.294  1.00  9.92           C  
ANISOU 1718  CZ  PHE B  41     1172   1442   1155     98   -114    -54       C  
ATOM   1719  N   ARG B  42     -30.881 -14.033  26.485  1.00 13.50           N  
ANISOU 1719  N   ARG B  42     1445   1981   1704    303   -343    -67       N  
ATOM   1720  CA  ARG B  42     -32.265 -13.758  26.084  1.00 14.74           C  
ANISOU 1720  CA  ARG B  42     1540   2185   1874    345   -400    -78       C  
ATOM   1721  C   ARG B  42     -32.337 -12.756  24.943  1.00 15.96           C  
ANISOU 1721  C   ARG B  42     1737   2316   2010    399   -459    -32       C  
ATOM   1722  O   ARG B  42     -33.168 -12.889  24.040  1.00 16.31           O  
ANISOU 1722  O   ARG B  42     1757   2406   2033    414   -519    -25       O  
ATOM   1723  CB  ARG B  42     -33.085 -13.241  27.269  1.00 14.98           C  
ANISOU 1723  CB  ARG B  42     1500   2229   1962    385   -385   -114       C  
ATOM   1724  CG  ARG B  42     -33.409 -14.306  28.294  1.00 14.39           C  
ANISOU 1724  CG  ARG B  42     1371   2197   1899    331   -338   -160       C  
ATOM   1725  CD  ARG B  42     -34.205 -13.747  29.451  1.00 15.02           C  
ANISOU 1725  CD  ARG B  42     1382   2295   2029    369   -316   -198       C  
ATOM   1726  NE  ARG B  42     -34.353 -14.763  30.490  1.00 15.16           N  
ANISOU 1726  NE  ARG B  42     1365   2347   2048    306   -262   -235       N  
ATOM   1727  CZ  ARG B  42     -34.053 -14.619  31.780  1.00 14.63           C  
ANISOU 1727  CZ  ARG B  42     1298   2263   1997    299   -207   -257       C  
ATOM   1728  NH1 ARG B  42     -33.601 -13.470  32.275  1.00 15.16           N  
ANISOU 1728  NH1 ARG B  42     1396   2278   2086    348   -196   -253       N  
ATOM   1729  NH2 ARG B  42     -34.234 -15.649  32.595  1.00 14.20           N  
ANISOU 1729  NH2 ARG B  42     1219   2241   1934    236   -162   -284       N  
ATOM   1730  N   LYS B  43     -31.461 -11.758  24.993  1.00 16.57           N  
ANISOU 1730  N   LYS B  43     1880   2323   2093    422   -444      2       N  
ATOM   1731  CA  LYS B  43     -31.339 -10.776  23.918  1.00 18.09           C  
ANISOU 1731  CA  LYS B  43     2134   2477   2261    465   -492     55       C  
ATOM   1732  C   LYS B  43     -31.012 -11.430  22.567  1.00 18.07           C  
ANISOU 1732  C   LYS B  43     2180   2499   2188    424   -517     84       C  
ATOM   1733  O   LYS B  43     -31.396 -10.913  21.522  1.00 18.81           O  
ANISOU 1733  O   LYS B  43     2303   2594   2249    459   -577    122       O  
ATOM   1734  CB  LYS B  43     -30.276  -9.727  24.277  1.00 18.23           C  
ANISOU 1734  CB  LYS B  43     2223   2410   2293    473   -458     83       C  
ATOM   1735  CG  LYS B  43     -30.410  -8.421  23.524  1.00 20.90           C  
ANISOU 1735  CG  LYS B  43     2620   2694   2627    533   -507    135       C  
ATOM   1736  CD  LYS B  43     -29.392  -7.393  24.017  1.00 22.44           C  
ANISOU 1736  CD  LYS B  43     2884   2800   2842    530   -467    154       C  
ATOM   1737  CE  LYS B  43     -29.637  -6.019  23.395  1.00 24.38           C  
ANISOU 1737  CE  LYS B  43     3195   2977   3091    595   -514    205       C  
ATOM   1738  NZ  LYS B  43     -28.550  -5.042  23.734  1.00 25.17           N  
ANISOU 1738  NZ  LYS B  43     3377   2985   3203    573   -474    228       N  
ATOM   1739  N   GLU B  44     -30.317 -12.566  22.589  1.00 17.60           N  
ANISOU 1739  N   GLU B  44     2131   2457   2101    355   -471     65       N  
ATOM   1740  CA  GLU B  44     -29.992 -13.289  21.352  1.00 17.62           C  
ANISOU 1740  CA  GLU B  44     2180   2482   2033    314   -485     81       C  
ATOM   1741  C   GLU B  44     -31.050 -14.333  20.953  1.00 17.66           C  
ANISOU 1741  C   GLU B  44     2132   2561   2017    292   -524     46       C  
ATOM   1742  O   GLU B  44     -30.848 -15.071  19.983  1.00 17.89           O  
ANISOU 1742  O   GLU B  44     2200   2612   1986    251   -533     47       O  
ATOM   1743  CB  GLU B  44     -28.610 -13.948  21.461  1.00 17.10           C  
ANISOU 1743  CB  GLU B  44     2161   2390   1945    257   -414     79       C  
ATOM   1744  CG  GLU B  44     -27.485 -12.994  21.827  1.00 17.69           C  
ANISOU 1744  CG  GLU B  44     2283   2402   2037    264   -375    110       C  
ATOM   1745  CD  GLU B  44     -27.289 -11.885  20.812  1.00 19.05           C  
ANISOU 1745  CD  GLU B  44     2523   2539   2175    289   -408    166       C  
ATOM   1746  OE1 GLU B  44     -27.261 -12.179  19.600  1.00 20.42           O  
ANISOU 1746  OE1 GLU B  44     2740   2734   2284    273   -431    188       O  
ATOM   1747  OE2 GLU B  44     -27.161 -10.718  21.231  1.00 19.96           O  
ANISOU 1747  OE2 GLU B  44     2657   2603   2325    322   -410    189       O  
ATOM   1748  N   GLY B  45     -32.165 -14.394  21.690  1.00 17.18           N  
ANISOU 1748  N   GLY B  45     1983   2539   2005    314   -543     11       N  
ATOM   1749  CA  GLY B  45     -33.316 -15.229  21.322  1.00 17.35           C  
ANISOU 1749  CA  GLY B  45     1941   2637   2013    292   -588    -22       C  
ATOM   1750  C   GLY B  45     -33.496 -16.534  22.093  1.00 16.54           C  
ANISOU 1750  C   GLY B  45     1793   2565   1925    225   -542    -76       C  
ATOM   1751  O   GLY B  45     -34.400 -17.311  21.798  1.00 16.81           O  
ANISOU 1751  O   GLY B  45     1780   2661   1947    191   -573   -108       O  
ATOM   1752  N   HIS B  46     -32.655 -16.763  23.097  1.00 15.41           N  
ANISOU 1752  N   HIS B  46     1668   2379   1808    205   -470    -86       N  
ATOM   1753  CA  HIS B  46     -32.648 -18.021  23.836  1.00 14.61           C  
ANISOU 1753  CA  HIS B  46     1545   2292   1715    141   -421   -127       C  
ATOM   1754  C   HIS B  46     -33.498 -17.901  25.102  1.00 14.39           C  
ANISOU 1754  C   HIS B  46     1432   2291   1744    151   -404   -159       C  
ATOM   1755  O   HIS B  46     -33.728 -16.794  25.598  1.00 14.13           O  
ANISOU 1755  O   HIS B  46     1371   2248   1751    212   -411   -151       O  
ATOM   1756  CB  HIS B  46     -31.212 -18.397  24.182  1.00 13.70           C  
ANISOU 1756  CB  HIS B  46     1499   2119   1589    117   -356   -115       C  
ATOM   1757  CG  HIS B  46     -30.301 -18.415  22.996  1.00 13.98           C  
ANISOU 1757  CG  HIS B  46     1613   2129   1570    111   -361    -85       C  
ATOM   1758  ND1 HIS B  46     -30.155 -19.520  22.186  1.00 13.92           N  
ANISOU 1758  ND1 HIS B  46     1642   2133   1512     62   -358   -101       N  
ATOM   1759  CD2 HIS B  46     -29.511 -17.453  22.465  1.00 14.35           C  
ANISOU 1759  CD2 HIS B  46     1712   2139   1601    143   -364    -43       C  
ATOM   1760  CE1 HIS B  46     -29.308 -19.240  21.212  1.00 14.86           C  
ANISOU 1760  CE1 HIS B  46     1830   2230   1586     69   -357    -71       C  
ATOM   1761  NE2 HIS B  46     -28.896 -17.995  21.363  1.00 13.77           N  
ANISOU 1761  NE2 HIS B  46     1700   2063   1467    115   -359    -33       N  
ATOM   1762  N   LYS B  47     -33.990 -19.036  25.598  1.00 14.07           N  
ANISOU 1762  N   LYS B  47     1354   2284   1707     90   -379   -198       N  
ATOM   1763  CA  LYS B  47     -34.706 -19.079  26.876  1.00 14.24           C  
ANISOU 1763  CA  LYS B  47     1301   2333   1775     85   -347   -231       C  
ATOM   1764  C   LYS B  47     -33.760 -19.483  27.998  1.00 13.16           C  
ANISOU 1764  C   LYS B  47     1205   2148   1646     58   -276   -232       C  
ATOM   1765  O   LYS B  47     -32.895 -20.336  27.812  1.00 13.06           O  
ANISOU 1765  O   LYS B  47     1257   2101   1604     17   -250   -224       O  
ATOM   1766  CB  LYS B  47     -35.906 -20.028  26.816  1.00 15.00           C  
ANISOU 1766  CB  LYS B  47     1328   2502   1871     26   -362   -272       C  
ATOM   1767  CG  LYS B  47     -37.117 -19.419  26.120  1.00 16.54           C  
ANISOU 1767  CG  LYS B  47     1443   2766   2076     66   -435   -279       C  
ATOM   1768  CD  LYS B  47     -38.346 -20.334  26.179  1.00 17.84           C  
ANISOU 1768  CD  LYS B  47     1522   3012   2245     -1   -447   -325       C  
ATOM   1769  CE  LYS B  47     -39.079 -20.265  27.521  1.00 17.38           C  
ANISOU 1769  CE  LYS B  47     1375   2991   2238     -6   -399   -360       C  
ATOM   1770  NZ  LYS B  47     -39.576 -18.899  27.869  1.00 14.82           N  
ANISOU 1770  NZ  LYS B  47      984   2685   1961     94   -417   -356       N  
ATOM   1771  N   VAL B  48     -33.922 -18.859  29.159  1.00 12.93           N  
ANISOU 1771  N   VAL B  48     1139   2117   1656     86   -246   -243       N  
ATOM   1772  CA  VAL B  48     -33.030 -19.093  30.292  1.00 12.22           C  
ANISOU 1772  CA  VAL B  48     1087   1986   1570     67   -185   -241       C  
ATOM   1773  C   VAL B  48     -33.801 -19.200  31.611  1.00 12.73           C  
ANISOU 1773  C   VAL B  48     1089   2085   1661     50   -146   -276       C  
ATOM   1774  O   VAL B  48     -34.732 -18.426  31.861  1.00 12.77           O  
ANISOU 1774  O   VAL B  48     1025   2129   1698     90   -159   -296       O  
ATOM   1775  CB  VAL B  48     -31.978 -17.956  30.418  1.00 11.91           C  
ANISOU 1775  CB  VAL B  48     1095   1891   1539    120   -181   -210       C  
ATOM   1776  CG1 VAL B  48     -31.013 -18.233  31.556  1.00 10.11           C  
ANISOU 1776  CG1 VAL B  48      903   1628   1311     98   -128   -208       C  
ATOM   1777  CG2 VAL B  48     -31.206 -17.781  29.118  1.00 11.51           C  
ANISOU 1777  CG2 VAL B  48     1105   1809   1458    133   -213   -174       C  
ATOM   1778  N   ASP B  49     -33.407 -20.171  32.436  1.00 12.62           N  
ANISOU 1778  N   ASP B  49     1103   2059   1634     -7    -98   -281       N  
ATOM   1779  CA  ASP B  49     -33.830 -20.247  33.826  1.00 13.07           C  
ANISOU 1779  CA  ASP B  49     1126   2138   1704    -27    -50   -307       C  
ATOM   1780  C   ASP B  49     -32.617 -20.145  34.731  1.00 12.82           C  
ANISOU 1780  C   ASP B  49     1157   2053   1662    -24    -14   -287       C  
ATOM   1781  O   ASP B  49     -31.652 -20.903  34.577  1.00 12.93           O  
ANISOU 1781  O   ASP B  49     1235   2027   1650    -50     -6   -262       O  
ATOM   1782  CB  ASP B  49     -34.516 -21.574  34.120  1.00 13.39           C  
ANISOU 1782  CB  ASP B  49     1147   2211   1729   -110    -23   -328       C  
ATOM   1783  CG  ASP B  49     -35.800 -21.746  33.367  1.00 13.69           C  
ANISOU 1783  CG  ASP B  49     1109   2315   1779   -127    -57   -355       C  
ATOM   1784  OD1 ASP B  49     -36.378 -20.742  32.899  1.00 13.89           O  
ANISOU 1784  OD1 ASP B  49     1077   2372   1830    -66    -96   -362       O  
ATOM   1785  OD2 ASP B  49     -36.236 -22.906  33.260  1.00 13.22           O  
ANISOU 1785  OD2 ASP B  49     1048   2273   1701   -204    -46   -369       O  
ATOM   1786  N   VAL B  50     -32.671 -19.217  35.678  1.00 13.10           N  
ANISOU 1786  N   VAL B  50     1173   2091   1715     10      7   -301       N  
ATOM   1787  CA  VAL B  50     -31.643 -19.100  36.693  1.00 13.13           C  
ANISOU 1787  CA  VAL B  50     1227   2057   1705      7     39   -289       C  
ATOM   1788  C   VAL B  50     -32.083 -19.932  37.892  1.00 13.39           C  
ANISOU 1788  C   VAL B  50     1249   2117   1719    -50     88   -308       C  
ATOM   1789  O   VAL B  50     -33.225 -19.834  38.342  1.00 13.59           O  
ANISOU 1789  O   VAL B  50     1211   2193   1757    -60    108   -343       O  
ATOM   1790  CB  VAL B  50     -31.411 -17.628  37.102  1.00 13.20           C  
ANISOU 1790  CB  VAL B  50     1233   2048   1736     67     35   -297       C  
ATOM   1791  CG1 VAL B  50     -30.555 -17.538  38.360  1.00 12.93           C  
ANISOU 1791  CG1 VAL B  50     1239   1990   1683     51     70   -296       C  
ATOM   1792  CG2 VAL B  50     -30.764 -16.875  35.958  1.00 12.95           C  
ANISOU 1792  CG2 VAL B  50     1230   1975   1713    111     -8   -267       C  
ATOM   1793  N   ILE B  51     -31.178 -20.777  38.370  1.00 13.25           N  
ANISOU 1793  N   ILE B  51     1294   2069   1672    -86    106   -283       N  
ATOM   1794  CA  ILE B  51     -31.402 -21.571  39.561  1.00 13.67           C  
ANISOU 1794  CA  ILE B  51     1359   2137   1698   -141    151   -289       C  
ATOM   1795  C   ILE B  51     -30.398 -21.110  40.610  1.00 13.44           C  
ANISOU 1795  C   ILE B  51     1374   2083   1650   -125    165   -277       C  
ATOM   1796  O   ILE B  51     -29.182 -21.206  40.405  1.00 12.83           O  
ANISOU 1796  O   ILE B  51     1348   1964   1564   -110    146   -244       O  
ATOM   1797  CB  ILE B  51     -31.218 -23.086  39.283  1.00 13.82           C  
ANISOU 1797  CB  ILE B  51     1424   2134   1691   -199    157   -267       C  
ATOM   1798  CG1 ILE B  51     -32.108 -23.544  38.125  1.00 14.92           C  
ANISOU 1798  CG1 ILE B  51     1528   2297   1846   -220    136   -282       C  
ATOM   1799  CG2 ILE B  51     -31.512 -23.915  40.542  1.00 13.85           C  
ANISOU 1799  CG2 ILE B  51     1449   2149   1664   -260    206   -268       C  
ATOM   1800  CD1 ILE B  51     -33.557 -23.160  38.253  1.00 16.78           C  
ANISOU 1800  CD1 ILE B  51     1673   2601   2103   -233    146   -324       C  
ATOM   1801  N   ILE B  52     -30.917 -20.580  41.716  1.00 13.91           N  
ANISOU 1801  N   ILE B  52     1409   2174   1704   -129    199   -307       N  
ATOM   1802  CA  ILE B  52     -30.105 -20.201  42.867  1.00 13.93           C  
ANISOU 1802  CA  ILE B  52     1453   2162   1678   -126    214   -302       C  
ATOM   1803  C   ILE B  52     -30.679 -20.923  44.087  1.00 14.43           C  
ANISOU 1803  C   ILE B  52     1523   2258   1701   -184    265   -313       C  
ATOM   1804  O   ILE B  52     -31.896 -20.983  44.254  1.00 14.75           O  
ANISOU 1804  O   ILE B  52     1510   2345   1750   -207    298   -347       O  
ATOM   1805  CB  ILE B  52     -30.125 -18.676  43.083  1.00 14.24           C  
ANISOU 1805  CB  ILE B  52     1468   2200   1740    -72    210   -333       C  
ATOM   1806  CG1 ILE B  52     -29.882 -17.958  41.752  1.00 15.25           C  
ANISOU 1806  CG1 ILE B  52     1585   2300   1910    -20    164   -322       C  
ATOM   1807  CG2 ILE B  52     -29.082 -18.252  44.138  1.00 13.55           C  
ANISOU 1807  CG2 ILE B  52     1434   2095   1622    -74    214   -327       C  
ATOM   1808  CD1 ILE B  52     -29.552 -16.467  41.876  1.00 16.77           C  
ANISOU 1808  CD1 ILE B  52     1781   2467   2124     32    152   -340       C  
ATOM   1809  N   CYS B  53     -29.811 -21.489  44.920  1.00 14.18           N  
ANISOU 1809  N   CYS B  53     1557   2207   1625   -210    271   -282       N  
ATOM   1810  CA  CYS B  53     -30.262 -22.204  46.110  1.00 14.92           C  
ANISOU 1810  CA  CYS B  53     1672   2326   1669   -270    319   -284       C  
ATOM   1811  C   CYS B  53     -30.954 -21.247  47.093  1.00 15.26           C  
ANISOU 1811  C   CYS B  53     1680   2416   1702   -267    360   -335       C  
ATOM   1812  O   CYS B  53     -30.569 -20.080  47.192  1.00 14.67           O  
ANISOU 1812  O   CYS B  53     1597   2333   1642   -218    344   -357       O  
ATOM   1813  CB  CYS B  53     -29.087 -22.904  46.797  1.00 14.81           C  
ANISOU 1813  CB  CYS B  53     1742   2279   1607   -286    306   -235       C  
ATOM   1814  SG  CYS B  53     -28.390 -24.267  45.848  1.00 15.06           S  
ANISOU 1814  SG  CYS B  53     1823   2255   1644   -293    274   -179       S  
ATOM   1815  N   PRO B  54     -31.983 -21.735  47.813  1.00 16.36           N  
ANISOU 1815  N   PRO B  54     1799   2601   1815   -322    416   -357       N  
ATOM   1816  CA  PRO B  54     -32.612 -20.896  48.829  1.00 17.17           C  
ANISOU 1816  CA  PRO B  54     1872   2751   1900   -320    465   -410       C  
ATOM   1817  C   PRO B  54     -31.622 -20.569  49.927  1.00 17.40           C  
ANISOU 1817  C   PRO B  54     1973   2764   1874   -320    463   -399       C  
ATOM   1818  O   PRO B  54     -30.797 -21.412  50.281  1.00 17.19           O  
ANISOU 1818  O   PRO B  54     2018   2712   1803   -351    446   -347       O  
ATOM   1819  CB  PRO B  54     -33.739 -21.777  49.383  1.00 17.89           C  
ANISOU 1819  CB  PRO B  54     1941   2895   1964   -396    530   -423       C  
ATOM   1820  CG  PRO B  54     -33.922 -22.857  48.393  1.00 17.70           C  
ANISOU 1820  CG  PRO B  54     1914   2851   1962   -429    508   -389       C  
ATOM   1821  CD  PRO B  54     -32.607 -23.066  47.749  1.00 16.72           C  
ANISOU 1821  CD  PRO B  54     1852   2657   1843   -394    443   -338       C  
ATOM   1822  N   GLU B  55     -31.715 -19.358  50.461  1.00 18.08           N  
ANISOU 1822  N   GLU B  55     2041   2866   1962   -284    478   -448       N  
ATOM   1823  CA  GLU B  55     -30.780 -18.894  51.478  1.00 18.16           C  
ANISOU 1823  CA  GLU B  55     2116   2864   1918   -285    471   -447       C  
ATOM   1824  C   GLU B  55     -31.300 -19.194  52.877  1.00 19.21           C  
ANISOU 1824  C   GLU B  55     2276   3047   1976   -342    536   -469       C  
ATOM   1825  O   GLU B  55     -32.502 -19.111  53.139  1.00 19.78           O  
ANISOU 1825  O   GLU B  55     2294   3167   2052   -359    598   -515       O  
ATOM   1826  CB  GLU B  55     -30.495 -17.396  51.291  1.00 17.94           C  
ANISOU 1826  CB  GLU B  55     2072   2816   1929   -220    450   -491       C  
ATOM   1827  CG  GLU B  55     -29.707 -17.104  50.015  1.00 16.92           C  
ANISOU 1827  CG  GLU B  55     1938   2633   1858   -173    383   -458       C  
ATOM   1828  CD  GLU B  55     -29.428 -15.627  49.768  1.00 17.36           C  
ANISOU 1828  CD  GLU B  55     1987   2658   1953   -115    362   -495       C  
ATOM   1829  OE1 GLU B  55     -29.737 -14.784  50.640  1.00 17.57           O  
ANISOU 1829  OE1 GLU B  55     2018   2697   1961   -108    397   -550       O  
ATOM   1830  OE2 GLU B  55     -28.882 -15.314  48.686  1.00 16.70           O  
ANISOU 1830  OE2 GLU B  55     1898   2533   1916    -80    314   -470       O  
ATOM   1831  N   LYS B  56     -30.378 -19.568  53.761  1.00 19.56           N  
ANISOU 1831  N   LYS B  56     2401   3082   1949   -373    520   -434       N  
ATOM   1832  CA  LYS B  56     -30.676 -19.873  55.158  1.00 20.75           C  
ANISOU 1832  CA  LYS B  56     2597   3276   2011   -432    575   -444       C  
ATOM   1833  C   LYS B  56     -31.741 -20.954  55.335  1.00 21.65           C  
ANISOU 1833  C   LYS B  56     2697   3425   2103   -498    637   -434       C  
ATOM   1834  O   LYS B  56     -32.554 -20.896  56.259  1.00 22.39           O  
ANISOU 1834  O   LYS B  56     2786   3573   2148   -541    710   -472       O  
ATOM   1835  CB  LYS B  56     -31.039 -18.589  55.919  1.00 21.37           C  
ANISOU 1835  CB  LYS B  56     2660   3386   2074   -412    615   -524       C  
ATOM   1836  CG  LYS B  56     -29.913 -17.564  55.890  1.00 20.92           C  
ANISOU 1836  CG  LYS B  56     2632   3289   2026   -365    555   -533       C  
ATOM   1837  CD  LYS B  56     -30.074 -16.486  56.943  1.00 22.87           C  
ANISOU 1837  CD  LYS B  56     2899   3561   2230   -362    594   -606       C  
ATOM   1838  CE  LYS B  56     -28.839 -15.597  57.013  1.00 22.82           C  
ANISOU 1838  CE  LYS B  56     2935   3514   2221   -336    530   -610       C  
ATOM   1839  NZ  LYS B  56     -29.007 -14.473  57.984  1.00 24.98           N  
ANISOU 1839  NZ  LYS B  56     3234   3803   2456   -334    568   -691       N  
ATOM   1840  N   GLN B  57     -31.710 -21.945  54.445  1.00 21.70           N  
ANISOU 1840  N   GLN B  57     2701   3400   2143   -511    610   -383       N  
ATOM   1841  CA  GLN B  57     -32.579 -23.121  54.531  1.00 22.58           C  
ANISOU 1841  CA  GLN B  57     2813   3532   2233   -585    660   -363       C  
ATOM   1842  C   GLN B  57     -31.751 -24.379  54.771  1.00 22.75           C  
ANISOU 1842  C   GLN B  57     2935   3506   2203   -625    629   -280       C  
ATOM   1843  O   GLN B  57     -32.089 -25.198  55.629  1.00 23.28           O  
ANISOU 1843  O   GLN B  57     3056   3589   2200   -698    675   -255       O  
ATOM   1844  CB  GLN B  57     -33.389 -23.274  53.240  1.00 22.55           C  
ANISOU 1844  CB  GLN B  57     2723   3530   2315   -573    658   -379       C  
ATOM   1845  CG  GLN B  57     -34.235 -24.549  53.153  1.00 23.54           C  
ANISOU 1845  CG  GLN B  57     2847   3669   2427   -659    701   -358       C  
ATOM   1846  CD  GLN B  57     -34.986 -24.672  51.828  1.00 23.92           C  
ANISOU 1846  CD  GLN B  57     2808   3723   2556   -649    687   -377       C  
ATOM   1847  OE1 GLN B  57     -35.571 -23.703  51.341  1.00 23.59           O  
ANISOU 1847  OE1 GLN B  57     2675   3717   2572   -597    688   -432       O  
ATOM   1848  NE2 GLN B  57     -34.976 -25.873  51.246  1.00 24.10           N  
ANISOU 1848  NE2 GLN B  57     2865   3708   2583   -698    673   -333       N  
ATOM   1849  N   PHE B  58     -30.677 -24.539  53.999  1.00 22.06           N  
ANISOU 1849  N   PHE B  58     2872   3360   2150   -575    553   -236       N  
ATOM   1850  CA  PHE B  58     -29.843 -25.736  54.077  1.00 22.08           C  
ANISOU 1850  CA  PHE B  58     2963   3309   2116   -593    517   -158       C  
ATOM   1851  C   PHE B  58     -29.119 -25.852  55.420  1.00 22.83           C  
ANISOU 1851  C   PHE B  58     3145   3412   2117   -612    510   -125       C  
ATOM   1852  O   PHE B  58     -28.601 -24.867  55.942  1.00 22.59           O  
ANISOU 1852  O   PHE B  58     3111   3405   2067   -579    491   -151       O  
ATOM   1853  CB  PHE B  58     -28.796 -25.746  52.956  1.00 21.12           C  
ANISOU 1853  CB  PHE B  58     2839   3132   2055   -524    441   -128       C  
ATOM   1854  CG  PHE B  58     -29.364 -25.795  51.556  1.00 20.01           C  
ANISOU 1854  CG  PHE B  58     2631   2977   1996   -507    438   -149       C  
ATOM   1855  CD1 PHE B  58     -30.703 -26.094  51.308  1.00 20.40           C  
ANISOU 1855  CD1 PHE B  58     2632   3057   2063   -559    492   -181       C  
ATOM   1856  CD2 PHE B  58     -28.526 -25.563  50.469  1.00 19.54           C  
ANISOU 1856  CD2 PHE B  58     2556   2878   1992   -443    378   -135       C  
ATOM   1857  CE1 PHE B  58     -31.190 -26.140  50.007  1.00 20.38           C  
ANISOU 1857  CE1 PHE B  58     2567   3045   2129   -543    478   -199       C  
ATOM   1858  CE2 PHE B  58     -29.006 -25.613  49.171  1.00 18.46           C  
ANISOU 1858  CE2 PHE B  58     2365   2729   1920   -428    371   -152       C  
ATOM   1859  CZ  PHE B  58     -30.340 -25.906  48.940  1.00 19.55           C  
ANISOU 1859  CZ  PHE B  58     2458   2898   2073   -478    417   -184       C  
ATOM   1860  N   LYS B  59     -29.084 -27.065  55.970  1.00 23.66           N  
ANISOU 1860  N   LYS B  59     3334   3494   2162   -666    522    -65       N  
ATOM   1861  CA  LYS B  59     -28.299 -27.347  57.167  1.00 24.30           C  
ANISOU 1861  CA  LYS B  59     3510   3575   2149   -679    501    -17       C  
ATOM   1862  C   LYS B  59     -26.828 -27.553  56.798  1.00 23.84           C  
ANISOU 1862  C   LYS B  59     3487   3465   2107   -610    409     39       C  
ATOM   1863  O   LYS B  59     -25.932 -27.139  57.542  1.00 23.71           O  
ANISOU 1863  O   LYS B  59     3504   3465   2041   -586    365     53       O  
ATOM   1864  CB  LYS B  59     -28.837 -28.582  57.896  1.00 25.47           C  
ANISOU 1864  CB  LYS B  59     3742   3712   2222   -764    549     33       C  
ATOM   1865  CG  LYS B  59     -30.250 -28.423  58.451  1.00 26.85           C  
ANISOU 1865  CG  LYS B  59     3885   3951   2368   -845    649    -20       C  
ATOM   1866  CD  LYS B  59     -30.674 -29.670  59.239  1.00 28.89           C  
ANISOU 1866  CD  LYS B  59     4240   4194   2541   -939    697     38       C  
ATOM   1867  CE  LYS B  59     -32.080 -29.538  59.811  1.00 30.08           C  
ANISOU 1867  CE  LYS B  59     4351   4418   2659  -1027    805    -16       C  
ATOM   1868  NZ  LYS B  59     -32.482 -30.758  60.579  1.00 31.95           N  
ANISOU 1868  NZ  LYS B  59     4691   4639   2810  -1130    856     44       N  
ATOM   1869  N   THR B  60     -26.584 -28.208  55.661  1.00 23.28           N  
ANISOU 1869  N   THR B  60     3406   3337   2104   -579    380     67       N  
ATOM   1870  CA  THR B  60     -25.221 -28.436  55.164  1.00 22.93           C  
ANISOU 1870  CA  THR B  60     3381   3246   2086   -507    300    115       C  
ATOM   1871  C   THR B  60     -25.138 -28.210  53.657  1.00 22.17           C  
ANISOU 1871  C   THR B  60     3213   3121   2089   -457    280     91       C  
ATOM   1872  O   THR B  60     -26.161 -28.173  52.969  1.00 21.80           O  
ANISOU 1872  O   THR B  60     3118   3079   2087   -484    323     51       O  
ATOM   1873  CB  THR B  60     -24.718 -29.878  55.468  1.00 23.59           C  
ANISOU 1873  CB  THR B  60     3567   3269   2126   -514    277    200       C  
ATOM   1874  OG1 THR B  60     -25.354 -30.819  54.589  1.00 23.62           O  
ANISOU 1874  OG1 THR B  60     3580   3220   2174   -539    307    210       O  
ATOM   1875  CG2 THR B  60     -24.994 -30.267  56.916  1.00 24.59           C  
ANISOU 1875  CG2 THR B  60     3778   3419   2144   -578    305    232       C  
ATOM   1876  N   LYS B  61     -23.909 -28.087  53.153  1.00 21.68           N  
ANISOU 1876  N   LYS B  61     3144   3035   2060   -388    215    115       N  
ATOM   1877  CA  LYS B  61     -23.658 -27.860  51.727  1.00 21.16           C  
ANISOU 1877  CA  LYS B  61     3019   2943   2080   -338    194     97       C  
ATOM   1878  C   LYS B  61     -24.093 -29.038  50.852  1.00 20.67           C  
ANISOU 1878  C   LYS B  61     2982   2824   2048   -351    212    119       C  
ATOM   1879  O   LYS B  61     -24.262 -28.885  49.644  1.00 19.88           O  
ANISOU 1879  O   LYS B  61     2833   2709   2013   -329    210     94       O  
ATOM   1880  CB  LYS B  61     -22.168 -27.576  51.474  1.00 21.22           C  
ANISOU 1880  CB  LYS B  61     3016   2940   2106   -267    126    123       C  
ATOM   1881  CG  LYS B  61     -21.264 -28.814  51.558  1.00 23.05           C  
ANISOU 1881  CG  LYS B  61     3316   3122   2320   -235     88    195       C  
ATOM   1882  CD  LYS B  61     -19.849 -28.539  51.060  1.00 24.98           C  
ANISOU 1882  CD  LYS B  61     3527   3364   2601   -159     27    213       C  
ATOM   1883  CE  LYS B  61     -19.024 -29.829  51.071  1.00 26.55           C  
ANISOU 1883  CE  LYS B  61     3788   3509   2790   -114     -7    281       C  
ATOM   1884  NZ  LYS B  61     -17.558 -29.584  50.971  1.00 27.92           N  
ANISOU 1884  NZ  LYS B  61     3928   3699   2981    -42    -71    304       N  
ATOM   1885  N   ASN B  62     -24.234 -30.211  51.467  1.00 20.92           N  
ANISOU 1885  N   ASN B  62     3099   2820   2031   -389    226    168       N  
ATOM   1886  CA  ASN B  62     -24.700 -31.420  50.780  1.00 20.92           C  
ANISOU 1886  CA  ASN B  62     3141   2757   2051   -416    248    188       C  
ATOM   1887  C   ASN B  62     -26.066 -31.267  50.119  1.00 20.00           C  
ANISOU 1887  C   ASN B  62     2968   2662   1970   -474    300    132       C  
ATOM   1888  O   ASN B  62     -26.351 -31.955  49.149  1.00 20.28           O  
ANISOU 1888  O   ASN B  62     3009   2653   2043   -483    306    130       O  
ATOM   1889  CB  ASN B  62     -24.745 -32.600  51.758  1.00 22.02           C  
ANISOU 1889  CB  ASN B  62     3391   2855   2120   -461    262    249       C  
ATOM   1890  CG  ASN B  62     -23.379 -32.932  52.335  1.00 23.53           C  
ANISOU 1890  CG  ASN B  62     3643   3019   2279   -396    201    313       C  
ATOM   1891  OD1 ASN B  62     -23.148 -32.796  53.539  1.00 26.05           O  
ANISOU 1891  OD1 ASN B  62     4003   3369   2528   -410    191    341       O  
ATOM   1892  ND2 ASN B  62     -22.459 -33.353  51.470  1.00 24.79           N  
ANISOU 1892  ND2 ASN B  62     3805   3126   2487   -321    158    336       N  
ATOM   1893  N   GLU B  63     -26.901 -30.369  50.637  1.00 19.32           N  
ANISOU 1893  N   GLU B  63     2825   2645   1870   -510    337     84       N  
ATOM   1894  CA  GLU B  63     -28.248 -30.149  50.098  1.00 18.78           C  
ANISOU 1894  CA  GLU B  63     2688   2612   1836   -560    385     29       C  
ATOM   1895  C   GLU B  63     -28.242 -29.369  48.779  1.00 17.69           C  
ANISOU 1895  C   GLU B  63     2466   2484   1774   -506    357    -13       C  
ATOM   1896  O   GLU B  63     -29.255 -29.324  48.087  1.00 17.34           O  
ANISOU 1896  O   GLU B  63     2365   2460   1765   -536    381    -52       O  
ATOM   1897  CB  GLU B  63     -29.132 -29.431  51.133  1.00 19.26           C  
ANISOU 1897  CB  GLU B  63     2714   2748   1858   -607    437    -11       C  
ATOM   1898  CG  GLU B  63     -29.477 -30.294  52.342  1.00 19.94           C  
ANISOU 1898  CG  GLU B  63     2882   2833   1863   -685    482     25       C  
ATOM   1899  CD  GLU B  63     -30.062 -29.503  53.506  1.00 20.22           C  
ANISOU 1899  CD  GLU B  63     2893   2944   1846   -720    531    -12       C  
ATOM   1900  OE1 GLU B  63     -31.171 -28.952  53.365  1.00 19.07           O  
ANISOU 1900  OE1 GLU B  63     2665   2856   1726   -749    580    -73       O  
ATOM   1901  OE2 GLU B  63     -29.415 -29.453  54.575  1.00 20.43           O  
ANISOU 1901  OE2 GLU B  63     2985   2976   1803   -717    520     20       O  
ATOM   1902  N   GLU B  64     -27.111 -28.744  48.445  1.00 16.90           N  
ANISOU 1902  N   GLU B  64     2354   2371   1695   -429    306     -4       N  
ATOM   1903  CA  GLU B  64     -26.954 -28.059  47.160  1.00 15.88           C  
ANISOU 1903  CA  GLU B  64     2160   2242   1631   -377    277    -33       C  
ATOM   1904  C   GLU B  64     -27.148 -29.053  46.016  1.00 15.96           C  
ANISOU 1904  C   GLU B  64     2187   2204   1671   -388    274    -23       C  
ATOM   1905  O   GLU B  64     -27.872 -28.778  45.057  1.00 15.61           O  
ANISOU 1905  O   GLU B  64     2087   2176   1667   -394    278    -60       O  
ATOM   1906  CB  GLU B  64     -25.568 -27.417  47.059  1.00 15.31           C  
ANISOU 1906  CB  GLU B  64     2087   2159   1570   -305    227    -14       C  
ATOM   1907  CG  GLU B  64     -25.359 -26.246  48.021  1.00 15.02           C  
ANISOU 1907  CG  GLU B  64     2027   2169   1509   -294    224    -36       C  
ATOM   1908  CD  GLU B  64     -23.922 -25.770  48.093  1.00 13.37           C  
ANISOU 1908  CD  GLU B  64     1826   1954   1303   -239    173    -13       C  
ATOM   1909  OE1 GLU B  64     -23.088 -26.215  47.278  1.00 12.43           O  
ANISOU 1909  OE1 GLU B  64     1714   1798   1211   -199    142     15       O  
ATOM   1910  OE2 GLU B  64     -23.627 -24.940  48.979  1.00 13.57           O  
ANISOU 1910  OE2 GLU B  64     1846   2012   1299   -238    166    -27       O  
ATOM   1911  N   LYS B  65     -26.494 -30.206  46.147  1.00 16.29           N  
ANISOU 1911  N   LYS B  65     2312   2186   1692   -388    265     26       N  
ATOM   1912  CA  LYS B  65     -26.594 -31.308  45.198  1.00 16.80           C  
ANISOU 1912  CA  LYS B  65     2416   2191   1776   -402    265     36       C  
ATOM   1913  C   LYS B  65     -28.038 -31.781  45.019  1.00 16.85           C  
ANISOU 1913  C   LYS B  65     2408   2211   1782   -490    309      5       C  
ATOM   1914  O   LYS B  65     -28.534 -31.873  43.894  1.00 16.75           O  
ANISOU 1914  O   LYS B  65     2362   2197   1806   -500    305    -25       O  
ATOM   1915  CB  LYS B  65     -25.718 -32.476  45.680  1.00 17.37           C  
ANISOU 1915  CB  LYS B  65     2591   2192   1817   -388    254     97       C  
ATOM   1916  CG  LYS B  65     -25.705 -33.684  44.761  1.00 19.18           C  
ANISOU 1916  CG  LYS B  65     2879   2345   2065   -397    256    107       C  
ATOM   1917  CD  LYS B  65     -24.680 -34.715  45.201  1.00 21.16           C  
ANISOU 1917  CD  LYS B  65     3229   2518   2292   -358    238    169       C  
ATOM   1918  CE  LYS B  65     -24.606 -35.859  44.200  1.00 23.21           C  
ANISOU 1918  CE  LYS B  65     3551   2693   2575   -355    242    171       C  
ATOM   1919  NZ  LYS B  65     -23.583 -36.909  44.508  1.00 25.53           N  
ANISOU 1919  NZ  LYS B  65     3945   2901   2855   -302    223    229       N  
ATOM   1920  N   SER B  66     -28.698 -32.072  46.137  1.00 17.31           N  
ANISOU 1920  N   SER B  66     2491   2290   1797   -557    349     13       N  
ATOM   1921  CA  SER B  66     -30.075 -32.581  46.140  1.00 17.56           C  
ANISOU 1921  CA  SER B  66     2507   2343   1823   -654    398    -15       C  
ATOM   1922  C   SER B  66     -31.068 -31.581  45.565  1.00 16.64           C  
ANISOU 1922  C   SER B  66     2271   2304   1746   -659    406    -79       C  
ATOM   1923  O   SER B  66     -32.032 -31.971  44.912  1.00 16.91           O  
ANISOU 1923  O   SER B  66     2271   2352   1801   -716    423   -109       O  
ATOM   1924  CB  SER B  66     -30.504 -32.938  47.567  1.00 18.68           C  
ANISOU 1924  CB  SER B  66     2695   2500   1901   -723    446      7       C  
ATOM   1925  OG  SER B  66     -29.487 -33.655  48.239  1.00 20.04           O  
ANISOU 1925  OG  SER B  66     2976   2608   2032   -701    428     73       O  
ATOM   1926  N   TYR B  67     -30.832 -30.295  45.818  1.00 15.32           N  
ANISOU 1926  N   TYR B  67     2042   2187   1590   -600    393    -99       N  
ATOM   1927  CA  TYR B  67     -31.714 -29.227  45.336  1.00 14.55           C  
ANISOU 1927  CA  TYR B  67     1835   2161   1534   -587    396   -157       C  
ATOM   1928  C   TYR B  67     -31.588 -28.986  43.828  1.00 13.58           C  
ANISOU 1928  C   TYR B  67     1674   2024   1463   -541    351   -173       C  
ATOM   1929  O   TYR B  67     -32.588 -28.873  43.122  1.00 13.63           O  
ANISOU 1929  O   TYR B  67     1612   2069   1497   -566    353   -210       O  
ATOM   1930  CB  TYR B  67     -31.410 -27.923  46.077  1.00 14.22           C  
ANISOU 1930  CB  TYR B  67     1756   2161   1486   -533    395   -173       C  
ATOM   1931  CG  TYR B  67     -32.258 -26.762  45.627  1.00 14.20           C  
ANISOU 1931  CG  TYR B  67     1648   2221   1528   -505    397   -230       C  
ATOM   1932  CD1 TYR B  67     -33.532 -26.574  46.138  1.00 14.66           C  
ANISOU 1932  CD1 TYR B  67     1641   2345   1583   -553    448   -272       C  
ATOM   1933  CD2 TYR B  67     -31.792 -25.854  44.680  1.00 14.67           C  
ANISOU 1933  CD2 TYR B  67     1670   2271   1631   -429    349   -240       C  
ATOM   1934  CE1 TYR B  67     -34.322 -25.513  45.727  1.00 14.99           C  
ANISOU 1934  CE1 TYR B  67     1582   2443   1669   -515    447   -324       C  
ATOM   1935  CE2 TYR B  67     -32.588 -24.785  44.253  1.00 14.32           C  
ANISOU 1935  CE2 TYR B  67     1536   2277   1629   -395    346   -287       C  
ATOM   1936  CZ  TYR B  67     -33.851 -24.627  44.785  1.00 14.32           C  
ANISOU 1936  CZ  TYR B  67     1470   2341   1628   -434    393   -329       C  
ATOM   1937  OH  TYR B  67     -34.647 -23.575  44.388  1.00 14.04           O  
ANISOU 1937  OH  TYR B  67     1342   2355   1637   -390    388   -375       O  
ATOM   1938  N   LYS B  68     -30.353 -28.896  43.347  1.00 12.55           N  
ANISOU 1938  N   LYS B  68     1584   1844   1341   -475    308   -143       N  
ATOM   1939  CA  LYS B  68     -30.093 -28.443  41.986  1.00 11.66           C  
ANISOU 1939  CA  LYS B  68     1437   1725   1270   -423    267   -157       C  
ATOM   1940  C   LYS B  68     -30.387 -29.497  40.921  1.00 11.57           C  
ANISOU 1940  C   LYS B  68     1452   1678   1267   -459    260   -159       C  
ATOM   1941  O   LYS B  68     -31.044 -29.203  39.922  1.00 11.68           O  
ANISOU 1941  O   LYS B  68     1410   1720   1308   -461    243   -191       O  
ATOM   1942  CB  LYS B  68     -28.640 -28.000  41.848  1.00 11.04           C  
ANISOU 1942  CB  LYS B  68     1388   1610   1195   -346    232   -127       C  
ATOM   1943  CG  LYS B  68     -28.332 -26.675  42.505  1.00 10.62           C  
ANISOU 1943  CG  LYS B  68     1297   1594   1145   -304    226   -137       C  
ATOM   1944  CD  LYS B  68     -26.930 -26.201  42.158  1.00  9.92           C  
ANISOU 1944  CD  LYS B  68     1226   1476   1066   -237    188   -112       C  
ATOM   1945  CE  LYS B  68     -25.863 -27.060  42.819  1.00 10.14           C  
ANISOU 1945  CE  LYS B  68     1326   1464   1063   -231    183    -66       C  
ATOM   1946  NZ  LYS B  68     -24.520 -26.414  42.781  1.00  8.28           N  
ANISOU 1946  NZ  LYS B  68     1089   1221    835   -171    150    -47       N  
ATOM   1947  N   ILE B  69     -29.881 -30.707  41.135  1.00 11.36           N  
ANISOU 1947  N   ILE B  69     1514   1586   1215   -485    270   -125       N  
ATOM   1948  CA  ILE B  69     -29.844 -31.728  40.088  1.00 11.53           C  
ANISOU 1948  CA  ILE B  69     1583   1554   1244   -506    260   -125       C  
ATOM   1949  C   ILE B  69     -31.231 -32.097  39.561  1.00 11.87           C  
ANISOU 1949  C   ILE B  69     1586   1631   1295   -588    274   -167       C  
ATOM   1950  O   ILE B  69     -31.427 -32.118  38.352  1.00 11.88           O  
ANISOU 1950  O   ILE B  69     1566   1633   1314   -583    248   -191       O  
ATOM   1951  CB  ILE B  69     -29.047 -32.985  40.533  1.00 11.76           C  
ANISOU 1951  CB  ILE B  69     1726   1497   1246   -513    271    -80       C  
ATOM   1952  CG1 ILE B  69     -27.553 -32.649  40.626  1.00 11.12           C  
ANISOU 1952  CG1 ILE B  69     1670   1386   1167   -418    243    -45       C  
ATOM   1953  CG2 ILE B  69     -29.265 -34.145  39.564  1.00 11.95           C  
ANISOU 1953  CG2 ILE B  69     1806   1460   1273   -553    273    -91       C  
ATOM   1954  CD1 ILE B  69     -26.942 -32.183  39.302  1.00 10.94           C  
ANISOU 1954  CD1 ILE B  69     1619   1361   1176   -355    211    -60       C  
ATOM   1955  N   PRO B  70     -32.200 -32.361  40.454  1.00 12.56           N  
ANISOU 1955  N   PRO B  70     1655   1752   1364   -665    315   -176       N  
ATOM   1956  CA  PRO B  70     -33.535 -32.680  39.938  1.00 13.40           C  
ANISOU 1956  CA  PRO B  70     1707   1902   1482   -748    327   -219       C  
ATOM   1957  C   PRO B  70     -34.157 -31.534  39.151  1.00 13.34           C  
ANISOU 1957  C   PRO B  70     1584   1975   1510   -710    295   -261       C  
ATOM   1958  O   PRO B  70     -34.824 -31.782  38.154  1.00 13.90           O  
ANISOU 1958  O   PRO B  70     1621   2065   1595   -744    274   -292       O  
ATOM   1959  CB  PRO B  70     -34.349 -32.980  41.204  1.00 13.78           C  
ANISOU 1959  CB  PRO B  70     1748   1984   1504   -831    384   -219       C  
ATOM   1960  CG  PRO B  70     -33.333 -33.340  42.234  1.00 14.19           C  
ANISOU 1960  CG  PRO B  70     1898   1974   1520   -807    399   -165       C  
ATOM   1961  CD  PRO B  70     -32.139 -32.487  41.918  1.00 12.86           C  
ANISOU 1961  CD  PRO B  70     1727   1791   1368   -691    354   -149       C  
ATOM   1962  N   ARG B  71     -33.930 -30.299  39.598  1.00 13.28           N  
ANISOU 1962  N   ARG B  71     1522   2008   1515   -639    289   -262       N  
ATOM   1963  CA  ARG B  71     -34.445 -29.110  38.911  1.00 13.44           C  
ANISOU 1963  CA  ARG B  71     1442   2094   1571   -588    256   -295       C  
ATOM   1964  C   ARG B  71     -33.772 -28.903  37.567  1.00 12.76           C  
ANISOU 1964  C   ARG B  71     1374   1975   1498   -530    202   -288       C  
ATOM   1965  O   ARG B  71     -34.434 -28.573  36.585  1.00 13.09           O  
ANISOU 1965  O   ARG B  71     1356   2057   1559   -526    169   -316       O  
ATOM   1966  CB  ARG B  71     -34.264 -27.866  39.785  1.00 13.38           C  
ANISOU 1966  CB  ARG B  71     1392   2120   1570   -526    266   -297       C  
ATOM   1967  CG  ARG B  71     -35.134 -27.888  41.017  1.00 14.64           C  
ANISOU 1967  CG  ARG B  71     1515   2333   1717   -581    323   -317       C  
ATOM   1968  CD  ARG B  71     -34.927 -26.666  41.897  1.00 15.63           C  
ANISOU 1968  CD  ARG B  71     1608   2487   1845   -520    336   -325       C  
ATOM   1969  NE  ARG B  71     -36.068 -26.470  42.788  1.00 17.20           N  
ANISOU 1969  NE  ARG B  71     1738   2758   2038   -564    390   -362       N  
ATOM   1970  CZ  ARG B  71     -36.338 -27.214  43.861  1.00 18.54           C  
ANISOU 1970  CZ  ARG B  71     1942   2934   2167   -641    447   -355       C  
ATOM   1971  NH1 ARG B  71     -35.547 -28.226  44.217  1.00 19.17           N  
ANISOU 1971  NH1 ARG B  71     2131   2946   2206   -679    453   -307       N  
ATOM   1972  NH2 ARG B  71     -37.411 -26.937  44.594  1.00 19.67           N  
ANISOU 1972  NH2 ARG B  71     2011   3153   2307   -679    501   -395       N  
ATOM   1973  N   VAL B  72     -32.457 -29.102  37.523  1.00 12.38           N  
ANISOU 1973  N   VAL B  72     1406   1859   1438   -485    193   -252       N  
ATOM   1974  CA  VAL B  72     -31.729 -29.094  36.258  1.00 12.16           C  
ANISOU 1974  CA  VAL B  72     1408   1795   1416   -439    154   -244       C  
ATOM   1975  C   VAL B  72     -32.319 -30.125  35.295  1.00 12.80           C  
ANISOU 1975  C   VAL B  72     1511   1864   1489   -502    145   -266       C  
ATOM   1976  O   VAL B  72     -32.630 -29.805  34.154  1.00 12.90           O  
ANISOU 1976  O   VAL B  72     1490   1901   1508   -490    108   -286       O  
ATOM   1977  CB  VAL B  72     -30.221 -29.376  36.455  1.00 11.80           C  
ANISOU 1977  CB  VAL B  72     1445   1681   1359   -390    156   -203       C  
ATOM   1978  CG1 VAL B  72     -29.544 -29.686  35.114  1.00 10.89           C  
ANISOU 1978  CG1 VAL B  72     1369   1526   1243   -359    129   -201       C  
ATOM   1979  CG2 VAL B  72     -29.547 -28.196  37.155  1.00 11.52           C  
ANISOU 1979  CG2 VAL B  72     1383   1663   1332   -325    151   -187       C  
ATOM   1980  N   ASN B  73     -32.504 -31.356  35.756  1.00 13.48           N  
ANISOU 1980  N   ASN B  73     1656   1909   1555   -575    178   -262       N  
ATOM   1981  CA  ASN B  73     -32.945 -32.420  34.853  1.00 14.05           C  
ANISOU 1981  CA  ASN B  73     1767   1956   1617   -641    171   -285       C  
ATOM   1982  C   ASN B  73     -34.432 -32.347  34.459  1.00 14.89           C  
ANISOU 1982  C   ASN B  73     1786   2140   1732   -712    160   -330       C  
ATOM   1983  O   ASN B  73     -34.810 -32.854  33.403  1.00 14.80           O  
ANISOU 1983  O   ASN B  73     1784   2127   1713   -752    135   -357       O  
ATOM   1984  CB  ASN B  73     -32.579 -33.789  35.438  1.00 14.55           C  
ANISOU 1984  CB  ASN B  73     1937   1934   1657   -693    209   -263       C  
ATOM   1985  CG  ASN B  73     -31.069 -33.979  35.564  1.00 14.19           C  
ANISOU 1985  CG  ASN B  73     1975   1811   1605   -613    209   -221       C  
ATOM   1986  OD1 ASN B  73     -30.295 -33.347  34.849  1.00 13.05           O  
ANISOU 1986  OD1 ASN B  73     1820   1668   1471   -536    181   -217       O  
ATOM   1987  ND2 ASN B  73     -30.650 -34.841  36.483  1.00 14.11           N  
ANISOU 1987  ND2 ASN B  73     2046   1737   1577   -632    240   -188       N  
ATOM   1988  N   SER B  74     -35.262 -31.709  35.288  1.00 15.47           N  
ANISOU 1988  N   SER B  74     1772   2286   1819   -728    178   -342       N  
ATOM   1989  CA  SER B  74     -36.695 -31.545  34.985  1.00 16.46           C  
ANISOU 1989  CA  SER B  74     1793   2501   1959   -787    168   -387       C  
ATOM   1990  C   SER B  74     -36.971 -30.543  33.863  1.00 16.47           C  
ANISOU 1990  C   SER B  74     1718   2559   1981   -723    106   -406       C  
ATOM   1991  O   SER B  74     -38.019 -30.609  33.216  1.00 17.24           O  
ANISOU 1991  O   SER B  74     1743   2721   2085   -769     78   -442       O  
ATOM   1992  CB  SER B  74     -37.470 -31.106  36.235  1.00 16.96           C  
ANISOU 1992  CB  SER B  74     1781   2630   2033   -811    212   -397       C  
ATOM   1993  OG  SER B  74     -37.087 -29.795  36.645  1.00 17.77           O  
ANISOU 1993  OG  SER B  74     1839   2758   2154   -712    205   -386       O  
ATOM   1994  N   GLY B  75     -36.034 -29.623  33.635  1.00 15.69           N  
ANISOU 1994  N   GLY B  75     1635   2438   1889   -621     82   -380       N  
ATOM   1995  CA  GLY B  75     -36.272 -28.482  32.758  1.00 15.65           C  
ANISOU 1995  CA  GLY B  75     1560   2484   1902   -551     27   -389       C  
ATOM   1996  C   GLY B  75     -36.125 -28.708  31.266  1.00 15.56           C  
ANISOU 1996  C   GLY B  75     1578   2462   1873   -547    -25   -395       C  
ATOM   1997  O   GLY B  75     -36.556 -27.874  30.488  1.00 16.29           O  
ANISOU 1997  O   GLY B  75     1610   2605   1975   -504    -76   -403       O  
ATOM   1998  N   GLY B  76     -35.508 -29.814  30.856  1.00 15.54           N  
ANISOU 1998  N   GLY B  76     1673   2391   1842   -588    -14   -391       N  
ATOM   1999  CA  GLY B  76     -35.275 -30.079  29.435  1.00 15.47           C  
ANISOU 1999  CA  GLY B  76     1705   2366   1806   -586    -57   -400       C  
ATOM   2000  C   GLY B  76     -34.376 -29.045  28.770  1.00 14.63           C  
ANISOU 2000  C   GLY B  76     1612   2249   1698   -486    -87   -372       C  
ATOM   2001  O   GLY B  76     -34.699 -28.506  27.705  1.00 14.65           O  
ANISOU 2001  O   GLY B  76     1586   2292   1690   -464   -140   -380       O  
ATOM   2002  N   TYR B  77     -33.244 -28.758  29.401  1.00 13.56           N  
ANISOU 2002  N   TYR B  77     1521   2061   1570   -430    -56   -338       N  
ATOM   2003  CA  TYR B  77     -32.318 -27.762  28.877  1.00 12.47           C  
ANISOU 2003  CA  TYR B  77     1396   1910   1432   -345    -76   -310       C  
ATOM   2004  C   TYR B  77     -31.393 -28.344  27.819  1.00 12.20           C  
ANISOU 2004  C   TYR B  77     1447   1825   1364   -338    -78   -305       C  
ATOM   2005  O   TYR B  77     -31.128 -29.548  27.789  1.00 12.33           O  
ANISOU 2005  O   TYR B  77     1529   1792   1362   -382    -52   -316       O  
ATOM   2006  CB  TYR B  77     -31.483 -27.172  30.006  1.00 11.92           C  
ANISOU 2006  CB  TYR B  77     1330   1813   1383   -295    -43   -279       C  
ATOM   2007  CG  TYR B  77     -32.326 -26.562  31.088  1.00 11.63           C  
ANISOU 2007  CG  TYR B  77     1218   1825   1376   -298    -32   -288       C  
ATOM   2008  CD1 TYR B  77     -32.921 -25.314  30.916  1.00 11.59           C  
ANISOU 2008  CD1 TYR B  77     1138   1871   1393   -252    -65   -293       C  
ATOM   2009  CD2 TYR B  77     -32.541 -27.233  32.284  1.00 11.20           C  
ANISOU 2009  CD2 TYR B  77     1169   1761   1324   -345     12   -292       C  
ATOM   2010  CE1 TYR B  77     -33.699 -24.750  31.919  1.00 11.23           C  
ANISOU 2010  CE1 TYR B  77     1021   1869   1375   -248    -49   -308       C  
ATOM   2011  CE2 TYR B  77     -33.311 -26.682  33.280  1.00 12.07           C  
ANISOU 2011  CE2 TYR B  77     1211   1920   1456   -350     30   -304       C  
ATOM   2012  CZ  TYR B  77     -33.897 -25.444  33.095  1.00 11.83           C  
ANISOU 2012  CZ  TYR B  77     1101   1943   1450   -300      1   -316       C  
ATOM   2013  OH  TYR B  77     -34.670 -24.911  34.104  1.00 12.41           O  
ANISOU 2013  OH  TYR B  77     1106   2065   1545   -300     25   -335       O  
ATOM   2014  N   ASP B  78     -30.901 -27.467  26.955  1.00 11.72           N  
ANISOU 2014  N   ASP B  78     1388   1773   1292   -281   -107   -288       N  
ATOM   2015  CA  ASP B  78     -29.892 -27.825  25.978  1.00 11.62           C  
ANISOU 2015  CA  ASP B  78     1451   1717   1245   -263   -101   -281       C  
ATOM   2016  C   ASP B  78     -28.491 -27.563  26.529  1.00 11.03           C  
ANISOU 2016  C   ASP B  78     1410   1596   1185   -208    -63   -248       C  
ATOM   2017  O   ASP B  78     -27.511 -28.070  26.004  1.00 11.35           O  
ANISOU 2017  O   ASP B  78     1513   1596   1205   -193    -41   -244       O  
ATOM   2018  CB  ASP B  78     -30.126 -27.033  24.699  1.00 11.94           C  
ANISOU 2018  CB  ASP B  78     1480   1797   1258   -240   -152   -279       C  
ATOM   2019  CG  ASP B  78     -31.528 -27.217  24.153  1.00 12.29           C  
ANISOU 2019  CG  ASP B  78     1479   1901   1289   -290   -201   -311       C  
ATOM   2020  OD1 ASP B  78     -31.848 -28.323  23.683  1.00 12.89           O  
ANISOU 2020  OD1 ASP B  78     1593   1968   1337   -353   -200   -345       O  
ATOM   2021  OD2 ASP B  78     -32.312 -26.249  24.197  1.00 13.44           O  
ANISOU 2021  OD2 ASP B  78     1551   2102   1453   -266   -242   -305       O  
ATOM   2022  N   LEU B  79     -28.403 -26.783  27.601  1.00 10.65           N  
ANISOU 2022  N   LEU B  79     1318   1558   1170   -179    -54   -227       N  
ATOM   2023  CA  LEU B  79     -27.125 -26.415  28.187  1.00 10.02           C  
ANISOU 2023  CA  LEU B  79     1257   1445   1104   -131    -26   -196       C  
ATOM   2024  C   LEU B  79     -27.273 -26.021  29.655  1.00  9.61           C  
ANISOU 2024  C   LEU B  79     1167   1402   1084   -127    -11   -187       C  
ATOM   2025  O   LEU B  79     -28.191 -25.293  30.009  1.00  9.50           O  
ANISOU 2025  O   LEU B  79     1095   1428   1087   -129    -29   -196       O  
ATOM   2026  CB  LEU B  79     -26.531 -25.239  27.416  1.00  9.81           C  
ANISOU 2026  CB  LEU B  79     1225   1431   1073    -83    -45   -175       C  
ATOM   2027  CG  LEU B  79     -25.215 -24.672  27.950  1.00  9.84           C  
ANISOU 2027  CG  LEU B  79     1236   1411   1093    -40    -21   -145       C  
ATOM   2028  CD1 LEU B  79     -24.118 -25.706  27.861  1.00  8.85           C  
ANISOU 2028  CD1 LEU B  79     1163   1245    955    -35     15   -142       C  
ATOM   2029  CD2 LEU B  79     -24.849 -23.403  27.180  1.00  9.30           C  
ANISOU 2029  CD2 LEU B  79     1160   1356   1018     -6    -41   -124       C  
ATOM   2030  N   LEU B  80     -26.345 -26.485  30.489  1.00  9.57           N  
ANISOU 2030  N   LEU B  80     1193   1358   1083   -116     20   -169       N  
ATOM   2031  CA  LEU B  80     -26.220 -26.020  31.873  1.00  9.40           C  
ANISOU 2031  CA  LEU B  80     1145   1344   1082   -106     34   -156       C  
ATOM   2032  C   LEU B  80     -24.918 -25.239  32.023  1.00  8.99           C  
ANISOU 2032  C   LEU B  80     1098   1280   1039    -54     36   -128       C  
ATOM   2033  O   LEU B  80     -23.853 -25.714  31.617  1.00  8.44           O  
ANISOU 2033  O   LEU B  80     1065   1181    960    -34     48   -115       O  
ATOM   2034  CB  LEU B  80     -26.229 -27.201  32.846  1.00  9.50           C  
ANISOU 2034  CB  LEU B  80     1194   1327   1088   -140     63   -153       C  
ATOM   2035  CG  LEU B  80     -25.894 -26.946  34.324  1.00 10.63           C  
ANISOU 2035  CG  LEU B  80     1329   1471   1238   -133     79   -135       C  
ATOM   2036  CD1 LEU B  80     -26.841 -25.924  34.945  1.00 11.01           C  
ANISOU 2036  CD1 LEU B  80     1314   1570   1300   -141     74   -151       C  
ATOM   2037  CD2 LEU B  80     -25.938 -28.265  35.108  1.00 10.81           C  
ANISOU 2037  CD2 LEU B  80     1403   1459   1245   -170    105   -126       C  
ATOM   2038  N   ILE B  81     -25.016 -24.041  32.600  1.00  8.57           N  
ANISOU 2038  N   ILE B  81     1003   1250   1002    -36     27   -124       N  
ATOM   2039  CA  ILE B  81     -23.852 -23.269  32.998  1.00  8.31           C  
ANISOU 2039  CA  ILE B  81      970   1209    979     -1     30   -102       C  
ATOM   2040  C   ILE B  81     -23.934 -23.082  34.500  1.00  8.49           C  
ANISOU 2040  C   ILE B  81      977   1240   1008     -9     41   -103       C  
ATOM   2041  O   ILE B  81     -24.948 -22.603  35.003  1.00  8.57           O  
ANISOU 2041  O   ILE B  81      955   1274   1026    -22     39   -122       O  
ATOM   2042  CB  ILE B  81     -23.823 -21.880  32.319  1.00  8.21           C  
ANISOU 2042  CB  ILE B  81      934   1208    976     24      8    -98       C  
ATOM   2043  CG1 ILE B  81     -23.633 -22.019  30.808  1.00  8.32           C  
ANISOU 2043  CG1 ILE B  81      972   1217    974     31     -2    -93       C  
ATOM   2044  CG2 ILE B  81     -22.719 -21.027  32.903  1.00  7.21           C  
ANISOU 2044  CG2 ILE B  81      805   1074    862     45     13    -80       C  
ATOM   2045  CD1 ILE B  81     -23.893 -20.741  30.050  1.00  6.86           C  
ANISOU 2045  CD1 ILE B  81      773   1041    791     50    -28    -86       C  
ATOM   2046  N   GLU B  82     -22.891 -23.484  35.222  1.00  8.51           N  
ANISOU 2046  N   GLU B  82     1002   1226   1005      0     52    -82       N  
ATOM   2047  CA  GLU B  82     -22.784 -23.122  36.636  1.00  8.64           C  
ANISOU 2047  CA  GLU B  82     1009   1255   1020     -6     57    -80       C  
ATOM   2048  C   GLU B  82     -21.667 -22.115  36.870  1.00  8.36           C  
ANISOU 2048  C   GLU B  82      961   1223    994     20     46    -67       C  
ATOM   2049  O   GLU B  82     -20.523 -22.322  36.450  1.00  8.49           O  
ANISOU 2049  O   GLU B  82      987   1229   1011     40     43    -47       O  
ATOM   2050  CB  GLU B  82     -22.592 -24.336  37.548  1.00  8.90           C  
ANISOU 2050  CB  GLU B  82     1077   1272   1032    -23     72    -65       C  
ATOM   2051  CG  GLU B  82     -22.657 -23.928  39.025  1.00  9.69           C  
ANISOU 2051  CG  GLU B  82     1171   1393   1120    -35     76    -66       C  
ATOM   2052  CD  GLU B  82     -22.947 -25.071  39.964  1.00 10.19           C  
ANISOU 2052  CD  GLU B  82     1272   1445   1155    -66     93    -53       C  
ATOM   2053  OE1 GLU B  82     -21.984 -25.605  40.537  1.00 10.70           O  
ANISOU 2053  OE1 GLU B  82     1368   1493   1204    -50     87    -23       O  
ATOM   2054  OE2 GLU B  82     -24.134 -25.423  40.139  1.00 11.18           O  
ANISOU 2054  OE2 GLU B  82     1395   1580   1274   -106    113    -72       O  
ATOM   2055  N   LEU B  83     -22.014 -21.037  37.573  1.00  8.29           N  
ANISOU 2055  N   LEU B  83      930   1231    991     17     42    -83       N  
ATOM   2056  CA  LEU B  83     -21.122 -19.914  37.794  1.00  7.97           C  
ANISOU 2056  CA  LEU B  83      878   1190    959     30     30    -78       C  
ATOM   2057  C   LEU B  83     -20.363 -20.025  39.123  1.00  8.07           C  
ANISOU 2057  C   LEU B  83      898   1214    955     21     29    -70       C  
ATOM   2058  O   LEU B  83     -20.968 -20.176  40.189  1.00  7.99           O  
ANISOU 2058  O   LEU B  83      892   1216    927      3     38    -83       O  
ATOM   2059  CB  LEU B  83     -21.930 -18.612  37.770  1.00  8.28           C  
ANISOU 2059  CB  LEU B  83      898   1231   1015     34     25   -103       C  
ATOM   2060  CG  LEU B  83     -22.691 -18.314  36.475  1.00  8.05           C  
ANISOU 2060  CG  LEU B  83      861   1197   1002     49     16   -108       C  
ATOM   2061  CD1 LEU B  83     -23.526 -17.041  36.620  1.00  8.39           C  
ANISOU 2061  CD1 LEU B  83      885   1238   1064     65      8   -131       C  
ATOM   2062  CD2 LEU B  83     -21.717 -18.182  35.327  1.00  7.13           C  
ANISOU 2062  CD2 LEU B  83      759   1064    887     60      7    -82       C  
ATOM   2063  N   HIS B  84     -19.035 -19.951  39.033  1.00  7.91           N  
ANISOU 2063  N   HIS B  84      875   1195    937     33     17    -49       N  
ATOM   2064  CA  HIS B  84     -18.143 -19.946  40.191  1.00  7.97           C  
ANISOU 2064  CA  HIS B  84      881   1219    927     27      4    -39       C  
ATOM   2065  C   HIS B  84     -17.081 -18.859  40.045  1.00  8.09           C  
ANISOU 2065  C   HIS B  84      874   1243    957     25    -11    -38       C  
ATOM   2066  O   HIS B  84     -16.908 -18.266  38.976  1.00  7.28           O  
ANISOU 2066  O   HIS B  84      761   1129    876     30     -7    -38       O  
ATOM   2067  CB  HIS B  84     -17.435 -21.299  40.329  1.00  8.23           C  
ANISOU 2067  CB  HIS B  84      928   1250    947     45      1     -8       C  
ATOM   2068  CG  HIS B  84     -18.319 -22.397  40.815  1.00  8.61           C  
ANISOU 2068  CG  HIS B  84     1011   1286    973     35     15     -5       C  
ATOM   2069  ND1 HIS B  84     -18.264 -22.877  42.104  1.00  9.29           N  
ANISOU 2069  ND1 HIS B  84     1120   1382   1027     23      8      8       N  
ATOM   2070  CD2 HIS B  84     -19.279 -23.114  40.186  1.00  9.70           C  
ANISOU 2070  CD2 HIS B  84     1167   1404   1114     27     34    -12       C  
ATOM   2071  CE1 HIS B  84     -19.157 -23.840  42.252  1.00  9.27           C  
ANISOU 2071  CE1 HIS B  84     1151   1362   1009      7     28     11       C  
ATOM   2072  NE2 HIS B  84     -19.786 -24.005  41.102  1.00  9.67           N  
ANISOU 2072  NE2 HIS B  84     1196   1394   1082      7     43     -3       N  
ATOM   2073  N   LEU B  85     -16.380 -18.599  41.143  1.00  8.53           N  
ANISOU 2073  N   LEU B  85      923   1321    996     12    -28    -38       N  
ATOM   2074  CA  LEU B  85     -15.153 -17.812  41.116  1.00  9.05           C  
ANISOU 2074  CA  LEU B  85      963   1404   1072      1    -46    -34       C  
ATOM   2075  C   LEU B  85     -14.070 -18.681  41.720  1.00  9.48           C  
ANISOU 2075  C   LEU B  85     1002   1489   1111     15    -68     -7       C  
ATOM   2076  O   LEU B  85     -14.344 -19.519  42.573  1.00  9.79           O  
ANISOU 2076  O   LEU B  85     1063   1534   1123     22    -75      4       O  
ATOM   2077  CB  LEU B  85     -15.291 -16.502  41.897  1.00  9.11           C  
ANISOU 2077  CB  LEU B  85      976   1412   1075    -32    -55    -65       C  
ATOM   2078  CG  LEU B  85     -16.160 -15.402  41.274  1.00  9.00           C  
ANISOU 2078  CG  LEU B  85      975   1362   1083    -37    -39    -90       C  
ATOM   2079  CD1 LEU B  85     -16.146 -14.161  42.167  1.00  8.27           C  
ANISOU 2079  CD1 LEU B  85      894   1264    984    -68    -47   -125       C  
ATOM   2080  CD2 LEU B  85     -15.698 -15.049  39.871  1.00  7.88           C  
ANISOU 2080  CD2 LEU B  85      823   1203    970    -31    -33    -73       C  
ATOM   2081  N   ASN B  86     -12.839 -18.481  41.279  1.00 10.05           N  
ANISOU 2081  N   ASN B  86     1035   1582   1200     19    -78      7       N  
ATOM   2082  CA  ASN B  86     -11.745 -19.321  41.722  1.00 10.67           C  
ANISOU 2082  CA  ASN B  86     1087   1696   1271     44   -102     34       C  
ATOM   2083  C   ASN B  86     -11.123 -18.716  42.972  1.00 11.35           C  
ANISOU 2083  C   ASN B  86     1157   1822   1335     13   -140     27       C  
ATOM   2084  O   ASN B  86     -11.434 -17.580  43.343  1.00 10.99           O  
ANISOU 2084  O   ASN B  86     1120   1772   1283    -30   -142     -3       O  
ATOM   2085  CB  ASN B  86     -10.709 -19.466  40.601  1.00 10.82           C  
ANISOU 2085  CB  ASN B  86     1061   1728   1321     66    -90     48       C  
ATOM   2086  CG  ASN B  86     -10.126 -20.878  40.498  1.00 11.16           C  
ANISOU 2086  CG  ASN B  86     1096   1779   1366    125    -93     78       C  
ATOM   2087  OD1 ASN B  86      -9.897 -21.550  41.509  1.00 10.89           O  
ANISOU 2087  OD1 ASN B  86     1068   1759   1311    144   -123     96       O  
ATOM   2088  ND2 ASN B  86      -9.857 -21.320  39.262  1.00  8.86           N  
ANISOU 2088  ND2 ASN B  86      793   1475   1098    154    -62     82       N  
ATOM   2089  N   ALA B  87     -10.266 -19.497  43.624  1.00 12.22           N  
ANISOU 2089  N   ALA B  87     1246   1968   1429     39   -173     54       N  
ATOM   2090  CA  ALA B  87      -9.451 -19.023  44.737  1.00 13.09           C  
ANISOU 2090  CA  ALA B  87     1329   2128   1514     12   -219     51       C  
ATOM   2091  C   ALA B  87      -8.140 -19.808  44.788  1.00 14.05           C  
ANISOU 2091  C   ALA B  87     1396   2297   1644     56   -253     86       C  
ATOM   2092  O   ALA B  87      -8.068 -20.944  44.309  1.00 13.78           O  
ANISOU 2092  O   ALA B  87     1367   2246   1623    115   -241    114       O  
ATOM   2093  CB  ALA B  87     -10.205 -19.174  46.051  1.00 13.00           C  
ANISOU 2093  CB  ALA B  87     1373   2115   1450     -5   -236     46       C  
ATOM   2094  N   SER B  88      -7.106 -19.185  45.346  1.00 15.09           N  
ANISOU 2094  N   SER B  88     1475   2488   1772     27   -294     80       N  
ATOM   2095  CA  SER B  88      -5.869 -19.881  45.677  1.00 16.53           C  
ANISOU 2095  CA  SER B  88     1596   2729   1955     70   -340    112       C  
ATOM   2096  C   SER B  88      -5.263 -19.253  46.937  1.00 17.71           C  
ANISOU 2096  C   SER B  88     1722   2941   2066     24   -402    103       C  
ATOM   2097  O   SER B  88      -5.860 -19.341  48.012  1.00 18.04           O  
ANISOU 2097  O   SER B  88     1823   2977   2055      8   -425    102       O  
ATOM   2098  CB  SER B  88      -4.887 -19.870  44.496  1.00 16.62           C  
ANISOU 2098  CB  SER B  88     1528   2766   2021     93   -318    116       C  
ATOM   2099  OG  SER B  88      -4.404 -18.566  44.223  1.00 16.84           O  
ANISOU 2099  OG  SER B  88     1510   2822   2066     22   -313     86       O  
ATOM   2100  N   ASN B  89      -4.098 -18.621  46.800  1.00 18.83           N  
ANISOU 2100  N   ASN B  89     1779   3144   2230     -4   -427     93       N  
ATOM   2101  CA  ASN B  89      -3.439 -17.907  47.896  1.00 20.06           C  
ANISOU 2101  CA  ASN B  89     1905   3365   2352    -61   -488     76       C  
ATOM   2102  C   ASN B  89      -3.408 -16.404  47.625  1.00 20.30           C  
ANISOU 2102  C   ASN B  89     1927   3391   2397   -154   -469     27       C  
ATOM   2103  O   ASN B  89      -2.721 -15.656  48.324  1.00 21.21           O  
ANISOU 2103  O   ASN B  89     2007   3560   2493   -216   -514      5       O  
ATOM   2104  CB  ASN B  89      -2.019 -18.426  48.075  1.00 20.93           C  
ANISOU 2104  CB  ASN B  89     1916   3563   2475    -23   -544    105       C  
ATOM   2105  N   GLY B  90      -4.143 -15.969  46.605  1.00 19.85           N  
ANISOU 2105  N   GLY B  90     1905   3266   2373   -165   -403     11       N  
ATOM   2106  CA  GLY B  90      -4.103 -14.576  46.160  1.00 20.15           C  
ANISOU 2106  CA  GLY B  90     1941   3284   2431   -245   -379    -28       C  
ATOM   2107  C   GLY B  90      -3.182 -14.345  44.975  1.00 20.51           C  
ANISOU 2107  C   GLY B  90     1911   3353   2529   -255   -351    -20       C  
ATOM   2108  O   GLY B  90      -3.258 -13.300  44.325  1.00 20.85           O  
ANISOU 2108  O   GLY B  90     1965   3362   2593   -314   -317    -43       O  
ATOM   2109  N   GLN B  91      -2.317 -15.316  44.682  1.00 20.89           N  
ANISOU 2109  N   GLN B  91     1883   3456   2596   -195   -363     13       N  
ATOM   2110  CA  GLN B  91      -1.389 -15.207  43.559  1.00 21.37           C  
ANISOU 2110  CA  GLN B  91     1863   3551   2704   -199   -329     19       C  
ATOM   2111  C   GLN B  91      -1.962 -15.815  42.276  1.00 20.25           C  
ANISOU 2111  C   GLN B  91     1752   3353   2588   -141   -263     36       C  
ATOM   2112  O   GLN B  91      -1.604 -15.393  41.181  1.00 20.25           O  
ANISOU 2112  O   GLN B  91     1723   3353   2619   -165   -216     32       O  
ATOM   2113  CB  GLN B  91      -0.050 -15.861  43.910  1.00 22.63           C  
ANISOU 2113  CB  GLN B  91     1911   3812   2875   -164   -376     39       C  
ATOM   2114  CG  GLN B  91       0.590 -15.312  45.188  1.00 24.36           C  
ANISOU 2114  CG  GLN B  91     2092   4100   3063   -223   -452     23       C  
ATOM   2115  CD  GLN B  91       0.906 -13.825  45.115  1.00 25.94           C  
ANISOU 2115  CD  GLN B  91     2281   4307   3270   -345   -444    -18       C  
ATOM   2116  OE1 GLN B  91       1.107 -13.268  44.036  1.00 26.83           O  
ANISOU 2116  OE1 GLN B  91     2373   4401   3419   -382   -388    -25       O  
ATOM   2117  NE2 GLN B  91       0.967 -13.178  46.274  1.00 27.66           N  
ANISOU 2117  NE2 GLN B  91     2516   4547   3447   -411   -501    -45       N  
ATOM   2118  N   GLY B  92      -2.843 -16.801  42.412  1.00 19.26           N  
ANISOU 2118  N   GLY B  92     1688   3182   2446    -71   -260     53       N  
ATOM   2119  CA  GLY B  92      -3.559 -17.353  41.265  1.00 18.14           C  
ANISOU 2119  CA  GLY B  92     1590   2980   2321    -25   -202     63       C  
ATOM   2120  C   GLY B  92      -4.459 -16.315  40.608  1.00 17.07           C  
ANISOU 2120  C   GLY B  92     1517   2781   2188    -81   -161     41       C  
ATOM   2121  O   GLY B  92      -5.060 -15.470  41.285  1.00 16.07           O  
ANISOU 2121  O   GLY B  92     1437   2628   2042   -131   -178     19       O  
ATOM   2122  N   LYS B  93      -4.543 -16.366  39.284  1.00 16.42           N  
ANISOU 2122  N   LYS B  93     1437   2673   2127    -69   -109     46       N  
ATOM   2123  CA  LYS B  93      -5.409 -15.451  38.551  1.00 16.07           C  
ANISOU 2123  CA  LYS B  93     1456   2568   2084   -110    -75     33       C  
ATOM   2124  C   LYS B  93      -5.875 -16.006  37.203  1.00 15.15           C  
ANISOU 2124  C   LYS B  93     1367   2415   1975    -69    -25     45       C  
ATOM   2125  O   LYS B  93      -5.250 -16.897  36.636  1.00 14.82           O  
ANISOU 2125  O   LYS B  93     1284   2403   1944    -23     -5     58       O  
ATOM   2126  CB  LYS B  93      -4.698 -14.117  38.347  1.00 16.84           C  
ANISOU 2126  CB  LYS B  93     1525   2681   2194   -194    -69     20       C  
ATOM   2127  CG  LYS B  93      -3.445 -14.181  37.494  1.00 19.07           C  
ANISOU 2127  CG  LYS B  93     1727   3021   2500   -204    -39     31       C  
ATOM   2128  CD  LYS B  93      -2.734 -12.837  37.502  1.00 21.70           C  
ANISOU 2128  CD  LYS B  93     2032   3371   2841   -303    -38     17       C  
ATOM   2129  CE  LYS B  93      -1.509 -12.852  36.617  1.00 23.26           C  
ANISOU 2129  CE  LYS B  93     2145   3632   3061   -324      0     26       C  
ATOM   2130  NZ  LYS B  93      -0.407 -13.703  37.163  1.00 25.42           N  
ANISOU 2130  NZ  LYS B  93     2311   4000   3348   -284    -28     30       N  
ATOM   2131  N   GLY B  94      -6.985 -15.467  36.707  1.00 14.10           N  
ANISOU 2131  N   GLY B  94     1304   2220   1834    -85     -7     38       N  
ATOM   2132  CA  GLY B  94      -7.453 -15.769  35.357  1.00 13.36           C  
ANISOU 2132  CA  GLY B  94     1242   2095   1742    -61     35     47       C  
ATOM   2133  C   GLY B  94      -8.679 -16.652  35.311  1.00 12.48           C  
ANISOU 2133  C   GLY B  94     1185   1941   1616    -11     34     46       C  
ATOM   2134  O   GLY B  94      -9.271 -16.977  36.347  1.00 11.97           O  
ANISOU 2134  O   GLY B  94     1139   1867   1541      2      5     40       O  
ATOM   2135  N   SER B  95      -9.031 -17.059  34.094  1.00 12.03           N  
ANISOU 2135  N   SER B  95     1153   1863   1554     11     67     52       N  
ATOM   2136  CA  SER B  95     -10.291 -17.733  33.816  1.00 11.59           C  
ANISOU 2136  CA  SER B  95     1152   1765   1485     42     69     48       C  
ATOM   2137  C   SER B  95     -10.082 -19.195  33.450  1.00 11.99           C  
ANISOU 2137  C   SER B  95     1200   1822   1532     96     86     53       C  
ATOM   2138  O   SER B  95      -9.078 -19.557  32.829  1.00 12.14           O  
ANISOU 2138  O   SER B  95     1183   1870   1558    114    112     59       O  
ATOM   2139  CB  SER B  95     -11.007 -17.031  32.670  1.00 11.43           C  
ANISOU 2139  CB  SER B  95     1176   1712   1457     23     87     49       C  
ATOM   2140  OG  SER B  95     -11.119 -15.647  32.928  1.00 11.16           O  
ANISOU 2140  OG  SER B  95     1151   1662   1428    -22     74     46       O  
ATOM   2141  N   GLU B  96     -11.077 -20.006  33.794  1.00 11.85           N  
ANISOU 2141  N   GLU B  96     1223   1774   1504    120     75     48       N  
ATOM   2142  CA  GLU B  96     -11.033 -21.451  33.636  1.00 12.25           C  
ANISOU 2142  CA  GLU B  96     1288   1814   1551    168     87     51       C  
ATOM   2143  C   GLU B  96     -12.467 -21.957  33.442  1.00 11.51           C  
ANISOU 2143  C   GLU B  96     1254   1678   1442    167     86     40       C  
ATOM   2144  O   GLU B  96     -13.397 -21.361  33.962  1.00 10.99           O  
ANISOU 2144  O   GLU B  96     1204   1601   1371    139     67     33       O  
ATOM   2145  CB  GLU B  96     -10.408 -21.981  34.910  1.00 13.29           C  
ANISOU 2145  CB  GLU B  96     1393   1967   1689    192     60     63       C  
ATOM   2146  CG  GLU B  96     -10.184 -23.432  35.067  1.00 14.38           C  
ANISOU 2146  CG  GLU B  96     1546   2090   1826    248     63     73       C  
ATOM   2147  CD  GLU B  96      -9.295 -23.663  36.277  1.00 15.12           C  
ANISOU 2147  CD  GLU B  96     1601   2218   1926    272     28     92       C  
ATOM   2148  OE1 GLU B  96      -9.799 -24.101  37.331  1.00 16.12           O  
ANISOU 2148  OE1 GLU B  96     1760   2329   2037    274      1    102       O  
ATOM   2149  OE2 GLU B  96      -8.096 -23.340  36.180  1.00 15.27           O  
ANISOU 2149  OE2 GLU B  96     1553   2285   1962    282     27     97       O  
ATOM   2150  N   VAL B  97     -12.653 -23.018  32.657  1.00 11.46           N  
ANISOU 2150  N   VAL B  97     1278   1648   1426    194    108     35       N  
ATOM   2151  CA  VAL B  97     -13.980 -23.636  32.488  1.00 10.57           C  
ANISOU 2151  CA  VAL B  97     1218   1499   1298    185    106     22       C  
ATOM   2152  C   VAL B  97     -13.836 -25.157  32.566  1.00 10.83           C  
ANISOU 2152  C   VAL B  97     1283   1504   1329    222    118     23       C  
ATOM   2153  O   VAL B  97     -13.012 -25.741  31.862  1.00 10.97           O  
ANISOU 2153  O   VAL B  97     1299   1520   1350    258    144     21       O  
ATOM   2154  CB  VAL B  97     -14.646 -23.212  31.145  1.00 10.43           C  
ANISOU 2154  CB  VAL B  97     1223   1474   1265    165    119      9       C  
ATOM   2155  CG1 VAL B  97     -16.024 -23.833  30.997  1.00 10.10           C  
ANISOU 2155  CG1 VAL B  97     1224   1404   1209    150    111     -7       C  
ATOM   2156  CG2 VAL B  97     -14.746 -21.686  31.048  1.00  9.05           C  
ANISOU 2156  CG2 VAL B  97     1028   1316   1095    135    106     14       C  
ATOM   2157  N   LEU B  98     -14.605 -25.788  33.450  1.00 10.52           N  
ANISOU 2157  N   LEU B  98     1274   1440   1283    214    103     25       N  
ATOM   2158  CA  LEU B  98     -14.548 -27.235  33.618  1.00 11.29           C  
ANISOU 2158  CA  LEU B  98     1416   1497   1376    244    113     29       C  
ATOM   2159  C   LEU B  98     -15.678 -27.880  32.832  1.00 11.34           C  
ANISOU 2159  C   LEU B  98     1476   1465   1366    218    127      5       C  
ATOM   2160  O   LEU B  98     -16.802 -27.373  32.826  1.00 11.81           O  
ANISOU 2160  O   LEU B  98     1537   1532   1417    172    116     -7       O  
ATOM   2161  CB  LEU B  98     -14.641 -27.647  35.094  1.00 11.40           C  
ANISOU 2161  CB  LEU B  98     1442   1503   1386    245     89     51       C  
ATOM   2162  CG  LEU B  98     -13.658 -27.077  36.132  1.00 12.55           C  
ANISOU 2162  CG  LEU B  98     1539   1690   1540    263     63     74       C  
ATOM   2163  CD1 LEU B  98     -12.340 -26.682  35.498  1.00 12.87           C  
ANISOU 2163  CD1 LEU B  98     1524   1765   1601    298     71     77       C  
ATOM   2164  CD2 LEU B  98     -14.266 -25.923  36.915  1.00 12.96           C  
ANISOU 2164  CD2 LEU B  98     1570   1772   1584    214     43     69       C  
ATOM   2165  N   TYR B  99     -15.373 -28.998  32.180  1.00 11.81           N  
ANISOU 2165  N   TYR B  99     1578   1487   1423    247    151     -4       N  
ATOM   2166  CA  TYR B  99     -16.333 -29.714  31.330  1.00 11.98           C  
ANISOU 2166  CA  TYR B  99     1655   1470   1425    219    165    -32       C  
ATOM   2167  C   TYR B  99     -16.283 -31.220  31.597  1.00 12.41           C  
ANISOU 2167  C   TYR B  99     1777   1461   1479    240    179    -31       C  
ATOM   2168  O   TYR B  99     -15.371 -31.716  32.259  1.00 12.38           O  
ANISOU 2168  O   TYR B  99     1774   1441   1489    292    179     -7       O  
ATOM   2169  CB  TYR B  99     -16.041 -29.431  29.851  1.00 11.95           C  
ANISOU 2169  CB  TYR B  99     1649   1480   1409    225    187    -54       C  
ATOM   2170  CG  TYR B  99     -14.693 -29.943  29.389  1.00 12.40           C  
ANISOU 2170  CG  TYR B  99     1705   1532   1477    288    219    -54       C  
ATOM   2171  CD1 TYR B  99     -14.563 -31.210  28.827  1.00 13.49           C  
ANISOU 2171  CD1 TYR B  99     1902   1616   1606    316    247    -76       C  
ATOM   2172  CD2 TYR B  99     -13.545 -29.166  29.522  1.00 11.98           C  
ANISOU 2172  CD2 TYR B  99     1586   1526   1442    319    222    -36       C  
ATOM   2173  CE1 TYR B  99     -13.323 -31.692  28.402  1.00 13.57           C  
ANISOU 2173  CE1 TYR B  99     1905   1621   1628    383    281    -80       C  
ATOM   2174  CE2 TYR B  99     -12.307 -29.637  29.102  1.00 12.39           C  
ANISOU 2174  CE2 TYR B  99     1621   1581   1505    379    255    -39       C  
ATOM   2175  CZ  TYR B  99     -12.204 -30.905  28.543  1.00 13.58           C  
ANISOU 2175  CZ  TYR B  99     1831   1680   1650    416    285    -62       C  
ATOM   2176  OH  TYR B  99     -10.979 -31.379  28.132  1.00 13.78           O  
ANISOU 2176  OH  TYR B  99     1836   1711   1690    485    322    -69       O  
ATOM   2177  N   TYR B 100     -17.271 -31.934  31.065  1.00 12.87           N  
ANISOU 2177  N   TYR B 100     1892   1480   1519    200    187    -58       N  
ATOM   2178  CA  TYR B 100     -17.385 -33.385  31.225  1.00 13.61           C  
ANISOU 2178  CA  TYR B 100     2065   1498   1608    207    203    -62       C  
ATOM   2179  C   TYR B 100     -17.204 -34.150  29.918  1.00 14.08           C  
ANISOU 2179  C   TYR B 100     2177   1517   1656    222    234    -99       C  
ATOM   2180  O   TYR B 100     -16.655 -35.250  29.910  1.00 14.76           O  
ANISOU 2180  O   TYR B 100     2320   1539   1747    266    255   -101       O  
ATOM   2181  CB  TYR B 100     -18.755 -33.729  31.808  1.00 13.77           C  
ANISOU 2181  CB  TYR B 100     2118   1498   1614    131    191    -66       C  
ATOM   2182  CG  TYR B 100     -18.894 -35.170  32.224  1.00 15.58           C  
ANISOU 2182  CG  TYR B 100     2437   1644   1840    127    206    -60       C  
ATOM   2183  CD1 TYR B 100     -18.341 -35.612  33.410  1.00 18.26           C  
ANISOU 2183  CD1 TYR B 100     2795   1954   2187    163    199    -18       C  
ATOM   2184  CD2 TYR B 100     -19.569 -36.090  31.433  1.00 17.98           C  
ANISOU 2184  CD2 TYR B 100     2810   1894   2128     86    224    -97       C  
ATOM   2185  CE1 TYR B 100     -18.450 -36.925  33.811  1.00 20.06           C  
ANISOU 2185  CE1 TYR B 100     3117   2097   2410    162    211     -6       C  
ATOM   2186  CE2 TYR B 100     -19.685 -37.418  31.823  1.00 19.79           C  
ANISOU 2186  CE2 TYR B 100     3132   2034   2354     78    239    -91       C  
ATOM   2187  CZ  TYR B 100     -19.124 -37.823  33.018  1.00 20.87           C  
ANISOU 2187  CZ  TYR B 100     3291   2137   2500    118    233    -43       C  
ATOM   2188  OH  TYR B 100     -19.221 -39.127  33.440  1.00 23.95           O  
ANISOU 2188  OH  TYR B 100     3783   2430   2885    113    247    -30       O  
ATOM   2189  N   SER B 101     -17.672 -33.570  28.820  1.00 13.88           N  
ANISOU 2189  N   SER B 101     2136   1527   1610    188    235   -129       N  
ATOM   2190  CA  SER B 101     -17.765 -34.274  27.552  1.00 14.50           C  
ANISOU 2190  CA  SER B 101     2274   1572   1665    183    261   -172       C  
ATOM   2191  C   SER B 101     -17.132 -33.476  26.433  1.00 14.25           C  
ANISOU 2191  C   SER B 101     2206   1592   1619    206    276   -185       C  
ATOM   2192  O   SER B 101     -16.750 -32.320  26.620  1.00 13.68           O  
ANISOU 2192  O   SER B 101     2062   1578   1557    216    263   -160       O  
ATOM   2193  CB  SER B 101     -19.235 -34.490  27.224  1.00 14.65           C  
ANISOU 2193  CB  SER B 101     2326   1584   1658     96    243   -201       C  
ATOM   2194  OG  SER B 101     -19.860 -33.232  27.050  1.00 14.14           O  
ANISOU 2194  OG  SER B 101     2195   1593   1586     61    212   -196       O  
ATOM   2195  N   ASN B 102     -17.048 -34.096  25.261  1.00 14.74           N  
ANISOU 2195  N   ASN B 102     2322   1627   1652    209    305   -226       N  
ATOM   2196  CA  ASN B 102     -16.524 -33.438  24.073  1.00 14.76           C  
ANISOU 2196  CA  ASN B 102     2304   1676   1628    222    326   -241       C  
ATOM   2197  C   ASN B 102     -17.346 -32.207  23.693  1.00 14.15           C  
ANISOU 2197  C   ASN B 102     2185   1662   1528    165    289   -233       C  
ATOM   2198  O   ASN B 102     -16.783 -31.183  23.314  1.00 13.77           O  
ANISOU 2198  O   ASN B 102     2090   1666   1476    179    293   -216       O  
ATOM   2199  CB  ASN B 102     -16.449 -34.422  22.894  1.00 15.66           C  
ANISOU 2199  CB  ASN B 102     2498   1747   1705    226    364   -294       C  
ATOM   2200  CG  ASN B 102     -15.248 -35.348  22.975  1.00 17.09           C  
ANISOU 2200  CG  ASN B 102     2705   1879   1910    309    413   -303       C  
ATOM   2201  OD1 ASN B 102     -14.293 -35.086  23.709  1.00 17.72           O  
ANISOU 2201  OD1 ASN B 102     2727   1976   2029    369    419   -268       O  
ATOM   2202  ND2 ASN B 102     -15.285 -36.438  22.209  1.00 17.99           N  
ANISOU 2202  ND2 ASN B 102     2905   1931   1998    315    447   -352       N  
ATOM   2203  N   LYS B 103     -18.670 -32.296  23.805  1.00 13.88           N  
ANISOU 2203  N   LYS B 103     2167   1624   1481    102    252   -244       N  
ATOM   2204  CA  LYS B 103     -19.532 -31.145  23.520  1.00 13.42           C  
ANISOU 2204  CA  LYS B 103     2067   1625   1409     59    210   -234       C  
ATOM   2205  C   LYS B 103     -19.246 -30.012  24.503  1.00 12.34           C  
ANISOU 2205  C   LYS B 103     1856   1525   1309     78    192   -190       C  
ATOM   2206  O   LYS B 103     -19.138 -28.850  24.110  1.00 12.09           O  
ANISOU 2206  O   LYS B 103     1786   1538   1269     78    179   -173       O  
ATOM   2207  CB  LYS B 103     -21.014 -31.528  23.573  1.00 13.51           C  
ANISOU 2207  CB  LYS B 103     2096   1631   1406     -9    174   -257       C  
ATOM   2208  CG  LYS B 103     -21.487 -32.412  22.436  1.00 15.24           C  
ANISOU 2208  CG  LYS B 103     2386   1827   1579    -47    180   -305       C  
ATOM   2209  CD  LYS B 103     -22.938 -32.800  22.650  1.00 16.82           C  
ANISOU 2209  CD  LYS B 103     2590   2027   1772   -121    142   -326       C  
ATOM   2210  CE  LYS B 103     -23.496 -33.631  21.508  1.00 19.17           C  
ANISOU 2210  CE  LYS B 103     2956   2308   2019   -172    139   -379       C  
ATOM   2211  NZ  LYS B 103     -23.017 -35.034  21.550  1.00 22.27           N  
ANISOU 2211  NZ  LYS B 103     3434   2616   2412   -166    184   -409       N  
ATOM   2212  N   GLY B 104     -19.117 -30.357  25.780  1.00 11.81           N  
ANISOU 2212  N   GLY B 104     1775   1434   1278     91    192   -172       N  
ATOM   2213  CA  GLY B 104     -18.728 -29.391  26.793  1.00 11.29           C  
ANISOU 2213  CA  GLY B 104     1646   1399   1243    109    178   -135       C  
ATOM   2214  C   GLY B 104     -17.376 -28.759  26.511  1.00 11.28           C  
ANISOU 2214  C   GLY B 104     1612   1423   1250    156    200   -117       C  
ATOM   2215  O   GLY B 104     -17.192 -27.571  26.729  1.00 10.35           O  
ANISOU 2215  O   GLY B 104     1445   1344   1143    153    185    -96       O  
ATOM   2216  N   LEU B 105     -16.433 -29.562  26.020  1.00 12.03           N  
ANISOU 2216  N   LEU B 105     1734   1495   1342    197    239   -130       N  
ATOM   2217  CA  LEU B 105     -15.102 -29.074  25.666  1.00 12.51           C  
ANISOU 2217  CA  LEU B 105     1756   1587   1410    238    268   -118       C  
ATOM   2218  C   LEU B 105     -15.169 -27.913  24.661  1.00 12.93           C  
ANISOU 2218  C   LEU B 105     1793   1686   1436    210    268   -116       C  
ATOM   2219  O   LEU B 105     -14.482 -26.904  24.834  1.00 12.58           O  
ANISOU 2219  O   LEU B 105     1697   1678   1405    215    270    -91       O  
ATOM   2220  CB  LEU B 105     -14.241 -30.220  25.120  1.00 13.10           C  
ANISOU 2220  CB  LEU B 105     1867   1629   1481    289    316   -142       C  
ATOM   2221  CG  LEU B 105     -12.879 -29.865  24.520  1.00 13.28           C  
ANISOU 2221  CG  LEU B 105     1848   1691   1506    332    359   -140       C  
ATOM   2222  CD1 LEU B 105     -11.998 -29.133  25.522  1.00 13.04           C  
ANISOU 2222  CD1 LEU B 105     1737   1700   1517    355    347   -104       C  
ATOM   2223  CD2 LEU B 105     -12.194 -31.128  24.013  1.00 14.51           C  
ANISOU 2223  CD2 LEU B 105     2046   1808   1661    389    408   -172       C  
ATOM   2224  N   GLU B 106     -16.006 -28.052  23.631  1.00 13.82           N  
ANISOU 2224  N   GLU B 106     1953   1793   1506    177    263   -140       N  
ATOM   2225  CA  GLU B 106     -16.179 -27.003  22.616  1.00 14.25           C  
ANISOU 2225  CA  GLU B 106     2006   1886   1524    149    256   -133       C  
ATOM   2226  C   GLU B 106     -16.624 -25.684  23.240  1.00 13.42           C  
ANISOU 2226  C   GLU B 106     1854   1805   1440    129    214    -99       C  
ATOM   2227  O   GLU B 106     -16.054 -24.636  22.943  1.00 13.53           O  
ANISOU 2227  O   GLU B 106     1844   1846   1450    126    221    -76       O  
ATOM   2228  CB  GLU B 106     -17.224 -27.394  21.565  1.00 15.20           C  
ANISOU 2228  CB  GLU B 106     2183   1999   1592    113    239   -162       C  
ATOM   2229  CG  GLU B 106     -17.011 -28.707  20.825  1.00 18.05           C  
ANISOU 2229  CG  GLU B 106     2608   2328   1924    123    278   -206       C  
ATOM   2230  CD  GLU B 106     -18.093 -28.931  19.775  1.00 21.65           C  
ANISOU 2230  CD  GLU B 106     3117   2786   2321     75    252   -235       C  
ATOM   2231  OE1 GLU B 106     -19.012 -29.767  19.990  1.00 23.34           O  
ANISOU 2231  OE1 GLU B 106     3362   2971   2535     47    229   -262       O  
ATOM   2232  OE2 GLU B 106     -18.044 -28.231  18.744  1.00 24.62           O  
ANISOU 2232  OE2 GLU B 106     3506   3198   2650     61    251   -230       O  
ATOM   2233  N   TYR B 107     -17.662 -25.737  24.078  1.00 12.67           N  
ANISOU 2233  N   TYR B 107     1751   1699   1365    111    174   -100       N  
ATOM   2234  CA  TYR B 107     -18.127 -24.556  24.818  1.00 11.84           C  
ANISOU 2234  CA  TYR B 107     1603   1612   1283     99    138    -75       C  
ATOM   2235  C   TYR B 107     -17.016 -23.981  25.705  1.00 11.29           C  
ANISOU 2235  C   TYR B 107     1488   1551   1249    120    153    -51       C  
ATOM   2236  O   TYR B 107     -16.756 -22.768  25.700  1.00 10.77           O  
ANISOU 2236  O   TYR B 107     1398   1505   1191    112    144    -29       O  
ATOM   2237  CB  TYR B 107     -19.322 -24.905  25.715  1.00 11.73           C  
ANISOU 2237  CB  TYR B 107     1582   1587   1287     79    106    -86       C  
ATOM   2238  CG  TYR B 107     -20.635 -25.167  24.995  1.00 12.58           C  
ANISOU 2238  CG  TYR B 107     1714   1700   1366     47     77   -108       C  
ATOM   2239  CD1 TYR B 107     -21.236 -24.184  24.218  1.00 13.04           C  
ANISOU 2239  CD1 TYR B 107     1766   1784   1404     37     45   -100       C  
ATOM   2240  CD2 TYR B 107     -21.293 -26.383  25.129  1.00 13.17           C  
ANISOU 2240  CD2 TYR B 107     1817   1753   1436     24     78   -136       C  
ATOM   2241  CE1 TYR B 107     -22.453 -24.413  23.573  1.00 13.73           C  
ANISOU 2241  CE1 TYR B 107     1866   1886   1465      9     10   -120       C  
ATOM   2242  CE2 TYR B 107     -22.507 -26.620  24.486  1.00 13.99           C  
ANISOU 2242  CE2 TYR B 107     1933   1869   1513    -14     48   -160       C  
ATOM   2243  CZ  TYR B 107     -23.080 -25.633  23.714  1.00 13.45           C  
ANISOU 2243  CZ  TYR B 107     1849   1837   1424    -20     12   -153       C  
ATOM   2244  OH  TYR B 107     -24.283 -25.865  23.083  1.00 14.15           O  
ANISOU 2244  OH  TYR B 107     1942   1947   1487    -55    -26   -176       O  
ATOM   2245  N   ALA B 108     -16.394 -24.867  26.483  1.00 10.79           N  
ANISOU 2245  N   ALA B 108     1418   1474   1209    146    171    -54       N  
ATOM   2246  CA  ALA B 108     -15.352 -24.503  27.436  1.00 10.63           C  
ANISOU 2246  CA  ALA B 108     1350   1467   1220    167    177    -33       C  
ATOM   2247  C   ALA B 108     -14.220 -23.735  26.767  1.00 10.49           C  
ANISOU 2247  C   ALA B 108     1306   1480   1200    171    203    -21       C  
ATOM   2248  O   ALA B 108     -13.802 -22.687  27.247  1.00 10.54           O  
ANISOU 2248  O   ALA B 108     1273   1507   1223    158    193     -2       O  
ATOM   2249  CB  ALA B 108     -14.803 -25.756  28.105  1.00 10.52           C  
ANISOU 2249  CB  ALA B 108     1342   1431   1222    203    191    -37       C  
ATOM   2250  N   THR B 109     -13.730 -24.275  25.660  1.00 10.59           N  
ANISOU 2250  N   THR B 109     1342   1495   1188    185    241    -34       N  
ATOM   2251  CA  THR B 109     -12.633 -23.669  24.919  1.00 10.81           C  
ANISOU 2251  CA  THR B 109     1345   1556   1207    185    279    -25       C  
ATOM   2252  C   THR B 109     -12.965 -22.255  24.439  1.00 10.57           C  
ANISOU 2252  C   THR B 109     1317   1540   1159    141    263     -5       C  
ATOM   2253  O   THR B 109     -12.161 -21.340  24.617  1.00 10.49           O  
ANISOU 2253  O   THR B 109     1268   1554   1164    126    273     15       O  
ATOM   2254  CB  THR B 109     -12.227 -24.549  23.711  1.00 10.99           C  
ANISOU 2254  CB  THR B 109     1403   1577   1196    206    328    -51       C  
ATOM   2255  OG1 THR B 109     -11.880 -25.855  24.179  1.00 11.29           O  
ANISOU 2255  OG1 THR B 109     1444   1592   1255    254    343    -69       O  
ATOM   2256  CG2 THR B 109     -11.038 -23.955  22.973  1.00 11.91           C  
ANISOU 2256  CG2 THR B 109     1488   1737   1302    202    376    -43       C  
ATOM   2257  N   ARG B 110     -14.139 -22.086  23.835  1.00 10.48           N  
ANISOU 2257  N   ARG B 110     1352   1512   1117    121    236     -9       N  
ATOM   2258  CA  ARG B 110     -14.564 -20.784  23.319  1.00 10.75           C  
ANISOU 2258  CA  ARG B 110     1400   1551   1132     89    214     15       C  
ATOM   2259  C   ARG B 110     -14.809 -19.775  24.437  1.00 10.13           C  
ANISOU 2259  C   ARG B 110     1289   1465   1094     78    179     33       C  
ATOM   2260  O   ARG B 110     -14.497 -18.595  24.283  1.00 10.38           O  
ANISOU 2260  O   ARG B 110     1319   1500   1127     56    178     56       O  
ATOM   2261  CB  ARG B 110     -15.825 -20.916  22.454  1.00 11.24           C  
ANISOU 2261  CB  ARG B 110     1515   1603   1154     77    184      6       C  
ATOM   2262  CG  ARG B 110     -15.620 -21.728  21.171  1.00 12.15           C  
ANISOU 2262  CG  ARG B 110     1675   1725   1215     78    218    -14       C  
ATOM   2263  CD  ARG B 110     -16.732 -21.484  20.145  1.00 12.60           C  
ANISOU 2263  CD  ARG B 110     1783   1783   1219     56    181    -14       C  
ATOM   2264  NE  ARG B 110     -18.074 -21.791  20.651  1.00 12.59           N  
ANISOU 2264  NE  ARG B 110     1780   1771   1234     54    127    -28       N  
ATOM   2265  CZ  ARG B 110     -18.651 -22.992  20.636  1.00 13.46           C  
ANISOU 2265  CZ  ARG B 110     1908   1871   1335     52    123    -64       C  
ATOM   2266  NH1 ARG B 110     -18.021 -24.061  20.150  1.00 15.44           N  
ANISOU 2266  NH1 ARG B 110     2189   2113   1564     60    168    -92       N  
ATOM   2267  NH2 ARG B 110     -19.878 -23.134  21.118  1.00 13.66           N  
ANISOU 2267  NH2 ARG B 110     1922   1893   1376     41     76    -75       N  
ATOM   2268  N   ILE B 111     -15.375 -20.228  25.555  1.00  9.60           N  
ANISOU 2268  N   ILE B 111     1205   1386   1056     91    153     20       N  
ATOM   2269  CA  ILE B 111     -15.573 -19.350  26.711  1.00  9.24           C  
ANISOU 2269  CA  ILE B 111     1131   1336   1045     82    125     30       C  
ATOM   2270  C   ILE B 111     -14.213 -18.850  27.207  1.00  9.71           C  
ANISOU 2270  C   ILE B 111     1150   1414   1126     75    147     43       C  
ATOM   2271  O   ILE B 111     -14.007 -17.645  27.352  1.00  9.78           O  
ANISOU 2271  O   ILE B 111     1152   1420   1145     50    138     58       O  
ATOM   2272  CB  ILE B 111     -16.354 -20.047  27.858  1.00  8.86           C  
ANISOU 2272  CB  ILE B 111     1072   1277   1016     94    102     13       C  
ATOM   2273  CG1 ILE B 111     -17.809 -20.299  27.453  1.00  8.46           C  
ANISOU 2273  CG1 ILE B 111     1049   1217    950     89     76     -1       C  
ATOM   2274  CG2 ILE B 111     -16.346 -19.198  29.130  1.00  8.18           C  
ANISOU 2274  CG2 ILE B 111      956   1191    961     85     82     18       C  
ATOM   2275  CD1 ILE B 111     -18.486 -21.360  28.293  1.00  8.41           C  
ANISOU 2275  CD1 ILE B 111     1040   1203    953     91     69    -21       C  
ATOM   2276  N   CYS B 112     -13.284 -19.775  27.430  1.00 10.05           N  
ANISOU 2276  N   CYS B 112     1166   1474   1178     97    173     36       N  
ATOM   2277  CA  CYS B 112     -11.936 -19.424  27.882  1.00 10.93           C  
ANISOU 2277  CA  CYS B 112     1226   1616   1311     92    191     46       C  
ATOM   2278  C   CYS B 112     -11.215 -18.460  26.934  1.00 11.18           C  
ANISOU 2278  C   CYS B 112     1254   1665   1329     58    220     62       C  
ATOM   2279  O   CYS B 112     -10.506 -17.561  27.391  1.00 11.04           O  
ANISOU 2279  O   CYS B 112     1202   1663   1330     28    220     73       O  
ATOM   2280  CB  CYS B 112     -11.089 -20.682  28.069  1.00 11.13           C  
ANISOU 2280  CB  CYS B 112     1223   1659   1346    135    215     37       C  
ATOM   2281  SG  CYS B 112     -11.555 -21.667  29.491  1.00 12.23           S  
ANISOU 2281  SG  CYS B 112     1361   1780   1505    167    181     31       S  
ATOM   2282  N   ASP B 113     -11.394 -18.653  25.625  1.00 11.51           N  
ANISOU 2282  N   ASP B 113     1336   1705   1334     57    246     62       N  
ATOM   2283  CA  ASP B 113     -10.798 -17.751  24.622  1.00 12.26           C  
ANISOU 2283  CA  ASP B 113     1441   1813   1405     19    278     81       C  
ATOM   2284  C   ASP B 113     -11.353 -16.327  24.731  1.00 11.89           C  
ANISOU 2284  C   ASP B 113     1421   1736   1358    -20    246    104       C  
ATOM   2285  O   ASP B 113     -10.613 -15.353  24.628  1.00 11.72           O  
ANISOU 2285  O   ASP B 113     1390   1723   1341    -62    263    123       O  
ATOM   2286  CB  ASP B 113     -11.034 -18.266  23.196  1.00 12.89           C  
ANISOU 2286  CB  ASP B 113     1570   1894   1432     25    308     76       C  
ATOM   2287  CG  ASP B 113     -10.012 -19.304  22.758  1.00 14.84           C  
ANISOU 2287  CG  ASP B 113     1790   2175   1674     53    365     55       C  
ATOM   2288  OD1 ASP B 113      -8.884 -19.331  23.297  1.00 18.75           O  
ANISOU 2288  OD1 ASP B 113     2219   2704   2202     58    390     54       O  
ATOM   2289  OD2 ASP B 113     -10.336 -20.093  21.846  1.00 16.99           O  
ANISOU 2289  OD2 ASP B 113     2106   2443   1908     70    385     37       O  
ATOM   2290  N   LYS B 114     -12.661 -16.217  24.920  1.00 11.21           N  
ANISOU 2290  N   LYS B 114     1373   1617   1271     -7    201    101       N  
ATOM   2291  CA  LYS B 114     -13.300 -14.916  25.070  1.00 11.02           C  
ANISOU 2291  CA  LYS B 114     1379   1558   1253    -29    167    120       C  
ATOM   2292  C   LYS B 114     -12.899 -14.236  26.372  1.00 10.59           C  
ANISOU 2292  C   LYS B 114     1286   1496   1240    -46    153    116       C  
ATOM   2293  O   LYS B 114     -12.480 -13.086  26.366  1.00 10.31           O  
ANISOU 2293  O   LYS B 114     1262   1445   1212    -84    156    134       O  
ATOM   2294  CB  LYS B 114     -14.819 -15.052  24.966  1.00 10.83           C  
ANISOU 2294  CB  LYS B 114     1389   1508   1219     -1    123    113       C  
ATOM   2295  CG  LYS B 114     -15.294 -15.178  23.524  1.00 11.69           C  
ANISOU 2295  CG  LYS B 114     1550   1616   1276      0    123    126       C  
ATOM   2296  CD  LYS B 114     -15.132 -13.854  22.782  1.00 13.54           C  
ANISOU 2296  CD  LYS B 114     1829   1828   1488    -29    122    164       C  
ATOM   2297  CE  LYS B 114     -15.549 -13.951  21.322  1.00 15.15           C  
ANISOU 2297  CE  LYS B 114     2091   2036   1630    -30    120    182       C  
ATOM   2298  NZ  LYS B 114     -15.759 -12.584  20.763  1.00 16.15           N  
ANISOU 2298  NZ  LYS B 114     2273   2126   1738    -49    100    226       N  
ATOM   2299  N   LEU B 115     -13.007 -14.955  27.482  1.00  9.92           N  
ANISOU 2299  N   LEU B 115     1164   1423   1181    -22    139     94       N  
ATOM   2300  CA  LEU B 115     -12.570 -14.421  28.775  1.00  9.72           C  
ANISOU 2300  CA  LEU B 115     1104   1400   1188    -39    124     86       C  
ATOM   2301  C   LEU B 115     -11.087 -14.072  28.737  1.00 10.07           C  
ANISOU 2301  C   LEU B 115     1108   1478   1241    -76    154     96       C  
ATOM   2302  O   LEU B 115     -10.663 -13.091  29.352  1.00 10.28           O  
ANISOU 2302  O   LEU B 115     1124   1498   1285   -116    145     97       O  
ATOM   2303  CB  LEU B 115     -12.851 -15.418  29.910  1.00  9.05           C  
ANISOU 2303  CB  LEU B 115      990   1329   1118     -7    106     65       C  
ATOM   2304  CG  LEU B 115     -14.327 -15.555  30.292  1.00  8.46           C  
ANISOU 2304  CG  LEU B 115      944   1227   1043     15     76     51       C  
ATOM   2305  CD1 LEU B 115     -14.539 -16.724  31.228  1.00  7.96           C  
ANISOU 2305  CD1 LEU B 115      861   1178    985     40     69     35       C  
ATOM   2306  CD2 LEU B 115     -14.834 -14.264  30.917  1.00  7.65           C  
ANISOU 2306  CD2 LEU B 115      856   1095    956     -3     52     47       C  
ATOM   2307  N   GLY B 116     -10.319 -14.861  27.985  1.00 10.18           N  
ANISOU 2307  N   GLY B 116     1098   1528   1241    -65    192     98       N  
ATOM   2308  CA  GLY B 116      -8.878 -14.657  27.833  1.00 10.84           C  
ANISOU 2308  CA  GLY B 116     1129   1658   1334    -97    228    105       C  
ATOM   2309  C   GLY B 116      -8.453 -13.379  27.128  1.00 11.70           C  
ANISOU 2309  C   GLY B 116     1260   1755   1431   -162    251    126       C  
ATOM   2310  O   GLY B 116      -7.256 -13.078  27.042  1.00 11.60           O  
ANISOU 2310  O   GLY B 116     1199   1783   1427   -202    283    131       O  
ATOM   2311  N   THR B 117      -9.425 -12.632  26.608  1.00 12.01           N  
ANISOU 2311  N   THR B 117     1373   1739   1450   -171    234    142       N  
ATOM   2312  CA  THR B 117      -9.173 -11.304  26.059  1.00 12.89           C  
ANISOU 2312  CA  THR B 117     1525   1821   1551   -233    247    168       C  
ATOM   2313  C   THR B 117      -8.941 -10.270  27.171  1.00 13.01           C  
ANISOU 2313  C   THR B 117     1530   1813   1601   -276    221    162       C  
ATOM   2314  O   THR B 117      -8.375  -9.204  26.924  1.00 13.63           O  
ANISOU 2314  O   THR B 117     1627   1873   1678   -341    238    179       O  
ATOM   2315  CB  THR B 117     -10.339 -10.843  25.151  1.00 13.17           C  
ANISOU 2315  CB  THR B 117     1648   1801   1553   -219    228    191       C  
ATOM   2316  OG1 THR B 117      -9.966  -9.638  24.470  1.00 16.70           O  
ANISOU 2316  OG1 THR B 117     2145   2217   1983   -279    247    225       O  
ATOM   2317  CG2 THR B 117     -11.602 -10.600  25.956  1.00 11.52           C  
ANISOU 2317  CG2 THR B 117     1465   1545   1365   -181    172    178       C  
ATOM   2318  N   VAL B 118      -9.398 -10.584  28.381  1.00 12.25           N  
ANISOU 2318  N   VAL B 118     1410   1713   1529   -244    182    136       N  
ATOM   2319  CA  VAL B 118      -9.205  -9.715  29.539  1.00 12.45           C  
ANISOU 2319  CA  VAL B 118     1427   1720   1582   -281    157    120       C  
ATOM   2320  C   VAL B 118      -8.370 -10.398  30.618  1.00 12.15           C  
ANISOU 2320  C   VAL B 118     1307   1746   1565   -280    149     97       C  
ATOM   2321  O   VAL B 118      -7.466  -9.782  31.172  1.00 12.79           O  
ANISOU 2321  O   VAL B 118     1353   1847   1660   -337    148     90       O  
ATOM   2322  CB  VAL B 118     -10.558  -9.247  30.124  1.00 12.06           C  
ANISOU 2322  CB  VAL B 118     1432   1609   1541   -250    115    108       C  
ATOM   2323  CG1 VAL B 118     -10.345  -8.403  31.378  1.00 12.63           C  
ANISOU 2323  CG1 VAL B 118     1501   1663   1637   -288     93     84       C  
ATOM   2324  CG2 VAL B 118     -11.332  -8.454  29.070  1.00 12.85           C  
ANISOU 2324  CG2 VAL B 118     1612   1647   1624   -247    115    135       C  
ATOM   2325  N   PHE B 119      -8.676 -11.663  30.910  1.00 11.63           N  
ANISOU 2325  N   PHE B 119     1214   1709   1497   -217    139     87       N  
ATOM   2326  CA  PHE B 119      -7.972 -12.421  31.938  1.00 11.40           C  
ANISOU 2326  CA  PHE B 119     1114   1734   1482   -201    125     71       C  
ATOM   2327  C   PHE B 119      -6.956 -13.384  31.337  1.00 11.40           C  
ANISOU 2327  C   PHE B 119     1053   1796   1482   -179    159     79       C  
ATOM   2328  O   PHE B 119      -6.913 -13.596  30.123  1.00 11.28           O  
ANISOU 2328  O   PHE B 119     1055   1780   1451   -172    198     91       O  
ATOM   2329  CB  PHE B 119      -8.959 -13.218  32.799  1.00 10.85           C  
ANISOU 2329  CB  PHE B 119     1061   1651   1411   -146     92     57       C  
ATOM   2330  CG  PHE B 119     -10.074 -12.392  33.373  1.00 10.84           C  
ANISOU 2330  CG  PHE B 119     1114   1595   1409   -155     64     43       C  
ATOM   2331  CD1 PHE B 119      -9.913 -11.733  34.583  1.00 11.99           C  
ANISOU 2331  CD1 PHE B 119     1253   1740   1564   -187     37     24       C  
ATOM   2332  CD2 PHE B 119     -11.289 -12.291  32.716  1.00 10.57           C  
ANISOU 2332  CD2 PHE B 119     1136   1514   1366   -128     65     47       C  
ATOM   2333  CE1 PHE B 119     -10.938 -10.979  35.119  1.00 12.17           C  
ANISOU 2333  CE1 PHE B 119     1325   1711   1587   -189     19      5       C  
ATOM   2334  CE2 PHE B 119     -12.323 -11.529  33.245  1.00 11.31           C  
ANISOU 2334  CE2 PHE B 119     1272   1560   1465   -126     42     32       C  
ATOM   2335  CZ  PHE B 119     -12.146 -10.872  34.448  1.00 12.01           C  
ANISOU 2335  CZ  PHE B 119     1355   1644   1564   -155     23     10       C  
ATOM   2336  N   LYS B 120      -6.119 -13.948  32.201  1.00 11.38           N  
ANISOU 2336  N   LYS B 120      979   1848   1495   -166    144     70       N  
ATOM   2337  CA  LYS B 120      -5.285 -15.078  31.819  1.00 11.78           C  
ANISOU 2337  CA  LYS B 120      970   1954   1552   -119    170     73       C  
ATOM   2338  C   LYS B 120      -6.199 -16.242  31.465  1.00 11.23           C  
ANISOU 2338  C   LYS B 120      946   1852   1468    -48    174     72       C  
ATOM   2339  O   LYS B 120      -7.070 -16.599  32.253  1.00 10.69           O  
ANISOU 2339  O   LYS B 120      912   1754   1397    -21    138     67       O  
ATOM   2340  CB  LYS B 120      -4.368 -15.488  32.971  1.00 12.20           C  
ANISOU 2340  CB  LYS B 120      943   2067   1625   -106    138     67       C  
ATOM   2341  CG  LYS B 120      -3.517 -16.725  32.693  1.00 12.38           C  
ANISOU 2341  CG  LYS B 120      900   2144   1659    -40    159     70       C  
ATOM   2342  CD  LYS B 120      -2.780 -17.170  33.942  1.00 13.41           C  
ANISOU 2342  CD  LYS B 120      960   2329   1808    -15    112     69       C  
ATOM   2343  CE  LYS B 120      -1.825 -18.331  33.652  1.00 14.50           C  
ANISOU 2343  CE  LYS B 120     1025   2521   1963     59    132     73       C  
ATOM   2344  NZ  LYS B 120      -0.525 -17.885  33.056  1.00 13.53           N  
ANISOU 2344  NZ  LYS B 120      807   2474   1861     25    171     69       N  
ATOM   2345  N   ASN B 121      -6.010 -16.812  30.279  1.00 11.31           N  
ANISOU 2345  N   ASN B 121      961   1869   1466    -23    220     76       N  
ATOM   2346  CA  ASN B 121      -6.736 -18.009  29.875  1.00 11.19           C  
ANISOU 2346  CA  ASN B 121      988   1826   1437     40    227     70       C  
ATOM   2347  C   ASN B 121      -6.043 -19.240  30.443  1.00 11.82           C  
ANISOU 2347  C   ASN B 121     1017   1939   1535    104    224     65       C  
ATOM   2348  O   ASN B 121      -5.032 -19.688  29.905  1.00 12.44           O  
ANISOU 2348  O   ASN B 121     1044   2061   1623    128    262     62       O  
ATOM   2349  CB  ASN B 121      -6.814 -18.099  28.347  1.00 11.45           C  
ANISOU 2349  CB  ASN B 121     1057   1852   1443     38    278     71       C  
ATOM   2350  CG  ASN B 121      -7.593 -19.309  27.869  1.00 10.53           C  
ANISOU 2350  CG  ASN B 121      991   1704   1308     93    285     59       C  
ATOM   2351  OD1 ASN B 121      -7.921 -20.200  28.647  1.00  8.86           O  
ANISOU 2351  OD1 ASN B 121      781   1478   1108    136    259     52       O  
ATOM   2352  ND2 ASN B 121      -7.880 -19.350  26.573  1.00 10.69           N  
ANISOU 2352  ND2 ASN B 121     1055   1712   1293     87    320     57       N  
ATOM   2353  N   ARG B 122      -6.591 -19.784  31.530  1.00 11.69           N  
ANISOU 2353  N   ARG B 122     1016   1902   1523    133    180     65       N  
ATOM   2354  CA  ARG B 122      -6.001 -20.942  32.201  1.00 12.41           C  
ANISOU 2354  CA  ARG B 122     1071   2015   1630    197    167     67       C  
ATOM   2355  C   ARG B 122      -6.337 -22.257  31.503  1.00 12.47           C  
ANISOU 2355  C   ARG B 122     1121   1988   1629    259    196     60       C  
ATOM   2356  O   ARG B 122      -5.749 -23.288  31.820  1.00 12.94           O  
ANISOU 2356  O   ARG B 122     1156   2057   1703    323    195     63       O  
ATOM   2357  CB  ARG B 122      -6.452 -21.014  33.668  1.00 12.18           C  
ANISOU 2357  CB  ARG B 122     1053   1974   1600    198    109     74       C  
ATOM   2358  CG  ARG B 122      -6.107 -19.784  34.493  1.00 13.65           C  
ANISOU 2358  CG  ARG B 122     1203   2191   1791    137     77     74       C  
ATOM   2359  CD  ARG B 122      -6.884 -19.766  35.803  1.00 14.11           C  
ANISOU 2359  CD  ARG B 122     1297   2228   1836    130     29     75       C  
ATOM   2360  NE  ARG B 122      -6.539 -20.905  36.654  1.00 14.99           N  
ANISOU 2360  NE  ARG B 122     1395   2355   1947    188      1     89       N  
ATOM   2361  CZ  ARG B 122      -5.498 -20.946  37.484  1.00 17.05           C  
ANISOU 2361  CZ  ARG B 122     1592   2671   2216    198    -34     99       C  
ATOM   2362  NH1 ARG B 122      -4.675 -19.907  37.596  1.00 17.59           N  
ANISOU 2362  NH1 ARG B 122     1598   2791   2295    146    -43     91       N  
ATOM   2363  NH2 ARG B 122      -5.274 -22.037  38.206  1.00 17.50           N  
ANISOU 2363  NH2 ARG B 122     1649   2733   2269    259    -62    118       N  
ATOM   2364  N   GLY B 123      -7.290 -22.217  30.575  1.00 12.33           N  
ANISOU 2364  N   GLY B 123     1171   1928   1588    242    217     51       N  
ATOM   2365  CA  GLY B 123      -7.657 -23.377  29.775  1.00 12.51           C  
ANISOU 2365  CA  GLY B 123     1242   1916   1596    287    247     37       C  
ATOM   2366  C   GLY B 123      -8.958 -24.039  30.189  1.00 12.33           C  
ANISOU 2366  C   GLY B 123     1291   1835   1560    293    220     33       C  
ATOM   2367  O   GLY B 123      -9.409 -23.914  31.344  1.00 12.38           O  
ANISOU 2367  O   GLY B 123     1300   1833   1572    282    178     44       O  
ATOM   2368  N   ALA B 124      -9.568 -24.730  29.229  1.00 12.15           N  
ANISOU 2368  N   ALA B 124     1325   1776   1515    304    246     16       N  
ATOM   2369  CA  ALA B 124     -10.666 -25.647  29.492  1.00 11.98           C  
ANISOU 2369  CA  ALA B 124     1369   1701   1481    312    229      7       C  
ATOM   2370  C   ALA B 124     -10.091 -26.902  30.145  1.00 12.50           C  
ANISOU 2370  C   ALA B 124     1437   1748   1566    374    229     12       C  
ATOM   2371  O   ALA B 124      -9.062 -27.427  29.701  1.00 12.68           O  
ANISOU 2371  O   ALA B 124     1433   1784   1600    425    261      7       O  
ATOM   2372  CB  ALA B 124     -11.391 -26.004  28.191  1.00 11.78           C  
ANISOU 2372  CB  ALA B 124     1403   1648   1424    299    255    -16       C  
ATOM   2373  N   LYS B 125     -10.742 -27.372  31.204  1.00 12.30           N  
ANISOU 2373  N   LYS B 125     1440   1691   1541    373    195     24       N  
ATOM   2374  CA  LYS B 125     -10.240 -28.512  31.964  1.00 13.01           C  
ANISOU 2374  CA  LYS B 125     1542   1756   1646    432    187     38       C  
ATOM   2375  C   LYS B 125     -11.335 -29.553  32.177  1.00 13.13           C  
ANISOU 2375  C   LYS B 125     1642   1702   1644    425    182     33       C  
ATOM   2376  O   LYS B 125     -12.466 -29.224  32.553  1.00 12.31           O  
ANISOU 2376  O   LYS B 125     1565   1588   1526    369    163     31       O  
ATOM   2377  CB  LYS B 125      -9.657 -28.046  33.301  1.00 13.04           C  
ANISOU 2377  CB  LYS B 125     1492   1799   1664    438    145     67       C  
ATOM   2378  CG  LYS B 125      -8.379 -27.239  33.145  1.00 13.86           C  
ANISOU 2378  CG  LYS B 125     1506   1972   1788    449    150     71       C  
ATOM   2379  CD  LYS B 125      -7.952 -26.579  34.437  1.00 15.11           C  
ANISOU 2379  CD  LYS B 125     1614   2175   1954    434    102     94       C  
ATOM   2380  CE  LYS B 125      -6.833 -25.571  34.199  1.00 15.76           C  
ANISOU 2380  CE  LYS B 125     1605   2328   2053    419    108     92       C  
ATOM   2381  NZ  LYS B 125      -6.259 -25.078  35.488  1.00 17.21           N  
ANISOU 2381  NZ  LYS B 125     1737   2559   2243    409     57    111       N  
ATOM   2382  N   LEU B 126     -10.987 -30.809  31.912  1.00 13.74           N  
ANISOU 2382  N   LEU B 126     1762   1731   1727    480    204     27       N  
ATOM   2383  CA  LEU B 126     -11.883 -31.938  32.116  1.00 14.23           C  
ANISOU 2383  CA  LEU B 126     1913   1719   1776    473    203     23       C  
ATOM   2384  C   LEU B 126     -11.935 -32.292  33.606  1.00 14.80           C  
ANISOU 2384  C   LEU B 126     1997   1774   1850    482    165     62       C  
ATOM   2385  O   LEU B 126     -10.900 -32.582  34.208  1.00 15.05           O  
ANISOU 2385  O   LEU B 126     2001   1816   1900    546    151     88       O  
ATOM   2386  CB  LEU B 126     -11.363 -33.148  31.336  1.00 14.85           C  
ANISOU 2386  CB  LEU B 126     2040   1743   1861    536    242      4       C  
ATOM   2387  CG  LEU B 126     -12.175 -34.438  31.368  1.00 15.23           C  
ANISOU 2387  CG  LEU B 126     2192   1699   1896    528    249     -6       C  
ATOM   2388  CD1 LEU B 126     -13.473 -34.248  30.607  1.00 14.49           C  
ANISOU 2388  CD1 LEU B 126     2139   1594   1772    444    257    -40       C  
ATOM   2389  CD2 LEU B 126     -11.363 -35.610  30.789  1.00 16.44           C  
ANISOU 2389  CD2 LEU B 126     2389   1795   2063    612    286    -23       C  
ATOM   2390  N   ASP B 127     -13.128 -32.270  34.194  1.00 14.75           N  
ANISOU 2390  N   ASP B 127     2032   1748   1825    418    149     65       N  
ATOM   2391  CA  ASP B 127     -13.310 -32.772  35.550  1.00 15.77           C  
ANISOU 2391  CA  ASP B 127     2194   1853   1945    418    121    101       C  
ATOM   2392  C   ASP B 127     -14.573 -33.622  35.648  1.00 16.30           C  
ANISOU 2392  C   ASP B 127     2349   1854   1990    366    132     93       C  
ATOM   2393  O   ASP B 127     -15.683 -33.097  35.713  1.00 15.98           O  
ANISOU 2393  O   ASP B 127     2306   1831   1934    292    130     78       O  
ATOM   2394  CB  ASP B 127     -13.344 -31.635  36.574  1.00 15.26           C  
ANISOU 2394  CB  ASP B 127     2072   1854   1873    385     86    119       C  
ATOM   2395  CG  ASP B 127     -13.183 -32.135  38.006  1.00 16.28           C  
ANISOU 2395  CG  ASP B 127     2229   1969   1987    400     55    162       C  
ATOM   2396  OD1 ASP B 127     -13.312 -33.357  38.235  1.00 18.10           O  
ANISOU 2396  OD1 ASP B 127     2535   2131   2210    423     60    180       O  
ATOM   2397  OD2 ASP B 127     -12.930 -31.311  38.905  1.00 15.98           O  
ANISOU 2397  OD2 ASP B 127     2146   1986   1941    386     24    178       O  
ATOM   2398  N   LYS B 128     -14.381 -34.937  35.682  1.00 17.57           N  
ANISOU 2398  N   LYS B 128     2586   1939   2152    404    143    104       N  
ATOM   2399  CA  LYS B 128     -15.491 -35.888  35.737  1.00 18.45           C  
ANISOU 2399  CA  LYS B 128     2790   1977   2244    349    157     96       C  
ATOM   2400  C   LYS B 128     -16.033 -36.129  37.143  1.00 18.59           C  
ANISOU 2400  C   LYS B 128     2844   1980   2239    311    137    136       C  
ATOM   2401  O   LYS B 128     -17.057 -36.793  37.297  1.00 19.03           O  
ANISOU 2401  O   LYS B 128     2969   1985   2276    247    151    131       O  
ATOM   2402  CB  LYS B 128     -15.076 -37.228  35.117  1.00 19.35           C  
ANISOU 2402  CB  LYS B 128     2984   1999   2367    403    183     88       C  
ATOM   2403  CG  LYS B 128     -14.914 -37.175  33.617  1.00 20.40           C  
ANISOU 2403  CG  LYS B 128     3107   2135   2508    415    216     37       C  
ATOM   2404  CD  LYS B 128     -14.825 -38.574  33.015  1.00 22.16           C  
ANISOU 2404  CD  LYS B 128     3432   2256   2733    448    247     16       C  
ATOM   2405  CE  LYS B 128     -14.782 -38.513  31.500  1.00 22.89           C  
ANISOU 2405  CE  LYS B 128     3522   2354   2822    448    282    -41       C  
ATOM   2406  NZ  LYS B 128     -14.402 -39.830  30.906  1.00 23.79           N  
ANISOU 2406  NZ  LYS B 128     3729   2369   2942    502    316    -66       N  
ATOM   2407  N   ARG B 129     -15.354 -35.592  38.155  1.00 18.63           N  
ANISOU 2407  N   ARG B 129     2804   2033   2242    343    104    173       N  
ATOM   2408  CA  ARG B 129     -15.714 -35.833  39.551  1.00 18.93           C  
ANISOU 2408  CA  ARG B 129     2881   2061   2250    314     83    215       C  
ATOM   2409  C   ARG B 129     -16.770 -34.856  40.097  1.00 17.47           C  
ANISOU 2409  C   ARG B 129     2659   1936   2042    225     82    201       C  
ATOM   2410  O   ARG B 129     -17.270 -35.046  41.210  1.00 17.68           O  
ANISOU 2410  O   ARG B 129     2723   1958   2036    184     75    228       O  
ATOM   2411  CB  ARG B 129     -14.468 -35.744  40.434  1.00 19.85           C  
ANISOU 2411  CB  ARG B 129     2970   2205   2368    391     43    262       C  
ATOM   2412  CG  ARG B 129     -13.388 -36.775  40.149  1.00 23.01           C  
ANISOU 2412  CG  ARG B 129     3405   2547   2791    493     39    285       C  
ATOM   2413  CD  ARG B 129     -12.141 -36.481  40.996  1.00 26.23           C  
ANISOU 2413  CD  ARG B 129     3757   3006   3202    568    -11    328       C  
ATOM   2414  NE  ARG B 129     -11.434 -35.279  40.539  1.00 28.40           N  
ANISOU 2414  NE  ARG B 129     3913   3375   3502    582    -18    302       N  
ATOM   2415  CZ  ARG B 129     -10.410 -34.706  41.174  1.00 30.72           C  
ANISOU 2415  CZ  ARG B 129     4133   3739   3801    625    -61    326       C  
ATOM   2416  NH1 ARG B 129      -9.945 -35.210  42.316  1.00 32.12           N  
ANISOU 2416  NH1 ARG B 129     4339   3909   3957    666   -107    379       N  
ATOM   2417  NH2 ARG B 129      -9.846 -33.613  40.663  1.00 31.34           N  
ANISOU 2417  NH2 ARG B 129     4110   3897   3903    622    -60    298       N  
ATOM   2418  N   LEU B 130     -17.097 -33.813  39.335  1.00 15.51           N  
ANISOU 2418  N   LEU B 130     2341   1744   1809    198     90    160       N  
ATOM   2419  CA  LEU B 130     -18.035 -32.792  39.797  1.00 14.16           C  
ANISOU 2419  CA  LEU B 130     2127   1631   1624    130     89    142       C  
ATOM   2420  C   LEU B 130     -19.452 -33.249  39.508  1.00 13.30           C  
ANISOU 2420  C   LEU B 130     2056   1494   1502     53    117    115       C  
ATOM   2421  O   LEU B 130     -19.802 -33.499  38.355  1.00 12.80           O  
ANISOU 2421  O   LEU B 130     1999   1410   1454     42    133     83       O  
ATOM   2422  CB  LEU B 130     -17.774 -31.450  39.109  1.00 13.42           C  
ANISOU 2422  CB  LEU B 130     1946   1601   1552    139     82    113       C  
ATOM   2423  CG  LEU B 130     -16.375 -30.860  39.296  1.00 13.92           C  
ANISOU 2423  CG  LEU B 130     1957   1703   1630    202     57    132       C  
ATOM   2424  CD1 LEU B 130     -16.199 -29.616  38.452  1.00 13.32           C  
ANISOU 2424  CD1 LEU B 130     1809   1676   1575    199     58    102       C  
ATOM   2425  CD2 LEU B 130     -16.101 -30.563  40.763  1.00 13.97           C  
ANISOU 2425  CD2 LEU B 130     1957   1738   1611    198     28    162       C  
ATOM   2426  N   TYR B 131     -20.263 -33.350  40.557  1.00 12.58           N  
ANISOU 2426  N   TYR B 131     1989   1410   1383     -5    123    127       N  
ATOM   2427  CA  TYR B 131     -21.630 -33.823  40.405  1.00 12.43           C  
ANISOU 2427  CA  TYR B 131     1998   1373   1352    -87    152    103       C  
ATOM   2428  C   TYR B 131     -22.422 -32.935  39.446  1.00 11.44           C  
ANISOU 2428  C   TYR B 131     1802   1298   1247   -117    157     52       C  
ATOM   2429  O   TYR B 131     -23.225 -33.443  38.682  1.00 11.11           O  
ANISOU 2429  O   TYR B 131     1778   1234   1208   -162    173     24       O  
ATOM   2430  CB  TYR B 131     -22.347 -33.950  41.757  1.00 12.63           C  
ANISOU 2430  CB  TYR B 131     2049   1410   1339   -148    165    123       C  
ATOM   2431  CG  TYR B 131     -22.664 -32.631  42.411  1.00 12.34           C  
ANISOU 2431  CG  TYR B 131     1938   1457   1296   -163    159    107       C  
ATOM   2432  CD1 TYR B 131     -23.772 -31.884  42.011  1.00 11.94           C  
ANISOU 2432  CD1 TYR B 131     1824   1456   1258   -211    175     60       C  
ATOM   2433  CD2 TYR B 131     -21.860 -32.124  43.424  1.00 12.68           C  
ANISOU 2433  CD2 TYR B 131     1971   1527   1318   -128    136    137       C  
ATOM   2434  CE1 TYR B 131     -24.067 -30.671  42.597  1.00 12.22           C  
ANISOU 2434  CE1 TYR B 131     1795   1558   1289   -217    173     42       C  
ATOM   2435  CE2 TYR B 131     -22.151 -30.905  44.027  1.00 12.50           C  
ANISOU 2435  CE2 TYR B 131     1888   1575   1288   -144    133    116       C  
ATOM   2436  CZ  TYR B 131     -23.255 -30.185  43.605  1.00 12.19           C  
ANISOU 2436  CZ  TYR B 131     1793   1575   1265   -186    155     68       C  
ATOM   2437  OH  TYR B 131     -23.559 -28.973  44.176  1.00 14.35           O  
ANISOU 2437  OH  TYR B 131     2011   1909   1533   -194    156     43       O  
ATOM   2438  N   ILE B 132     -22.191 -31.619  39.477  1.00 10.94           N  
ANISOU 2438  N   ILE B 132     1663   1299   1196    -94    140     41       N  
ATOM   2439  CA  ILE B 132     -22.964 -30.696  38.634  1.00 10.21           C  
ANISOU 2439  CA  ILE B 132     1507   1253   1122   -115    140     -1       C  
ATOM   2440  C   ILE B 132     -22.767 -30.995  37.145  1.00 10.57           C  
ANISOU 2440  C   ILE B 132     1560   1273   1183    -95    138    -21       C  
ATOM   2441  O   ILE B 132     -23.650 -30.724  36.330  1.00 10.46           O  
ANISOU 2441  O   ILE B 132     1520   1281   1175   -128    138    -54       O  
ATOM   2442  CB  ILE B 132     -22.636 -29.205  38.935  1.00  9.88           C  
ANISOU 2442  CB  ILE B 132     1395   1270   1091    -87    122     -6       C  
ATOM   2443  CG1 ILE B 132     -23.702 -28.279  38.333  1.00  8.86           C  
ANISOU 2443  CG1 ILE B 132     1207   1183    975   -113    121    -45       C  
ATOM   2444  CG2 ILE B 132     -21.244 -28.825  38.439  1.00  8.83           C  
ANISOU 2444  CG2 ILE B 132     1247   1133    973    -21    103     10       C  
ATOM   2445  CD1 ILE B 132     -25.101 -28.496  38.903  1.00  8.79           C  
ANISOU 2445  CD1 ILE B 132     1190   1196    955   -179    142    -65       C  
ATOM   2446  N   LEU B 133     -21.612 -31.563  36.806  1.00 10.71           N  
ANISOU 2446  N   LEU B 133     1613   1250   1206    -40    136     -1       N  
ATOM   2447  CA  LEU B 133     -21.311 -31.968  35.447  1.00 11.12           C  
ANISOU 2447  CA  LEU B 133     1684   1274   1267    -18    142    -21       C  
ATOM   2448  C   LEU B 133     -21.727 -33.410  35.162  1.00 12.10           C  
ANISOU 2448  C   LEU B 133     1891   1328   1380    -48    162    -30       C  
ATOM   2449  O   LEU B 133     -22.312 -33.688  34.115  1.00 12.76           O  
ANISOU 2449  O   LEU B 133     1988   1402   1459    -80    168    -64       O  
ATOM   2450  CB  LEU B 133     -19.817 -31.802  35.178  1.00 11.24           C  
ANISOU 2450  CB  LEU B 133     1689   1287   1296     61    137     -2       C  
ATOM   2451  CG  LEU B 133     -19.235 -30.407  35.427  1.00 10.64           C  
ANISOU 2451  CG  LEU B 133     1537   1274   1232     87    119      6       C  
ATOM   2452  CD1 LEU B 133     -17.747 -30.407  35.120  1.00 11.48           C  
ANISOU 2452  CD1 LEU B 133     1630   1380   1354    157    118     23       C  
ATOM   2453  CD2 LEU B 133     -19.958 -29.346  34.609  1.00  9.77           C  
ANISOU 2453  CD2 LEU B 133     1381   1206   1126     58    113    -23       C  
ATOM   2454  N   ASN B 134     -21.437 -34.330  36.080  1.00 12.37           N  
ANISOU 2454  N   ASN B 134     1986   1310   1404    -42    169      2       N  
ATOM   2455  CA  ASN B 134     -21.667 -35.752  35.799  1.00 13.04           C  
ANISOU 2455  CA  ASN B 134     2165   1310   1480    -65    190     -2       C  
ATOM   2456  C   ASN B 134     -23.086 -36.240  36.086  1.00 13.37           C  
ANISOU 2456  C   ASN B 134     2235   1341   1504   -167    205    -19       C  
ATOM   2457  O   ASN B 134     -23.453 -37.315  35.641  1.00 13.36           O  
ANISOU 2457  O   ASN B 134     2308   1273   1495   -204    222    -35       O  
ATOM   2458  CB  ASN B 134     -20.632 -36.642  36.505  1.00 13.18           C  
ANISOU 2458  CB  ASN B 134     2249   1261   1498     -2    190     43       C  
ATOM   2459  CG  ASN B 134     -20.780 -36.644  38.007  1.00 13.24           C  
ANISOU 2459  CG  ASN B 134     2269   1275   1486    -22    182     87       C  
ATOM   2460  OD1 ASN B 134     -21.889 -36.701  38.535  1.00 12.61           O  
ANISOU 2460  OD1 ASN B 134     2199   1206   1387   -106    194     82       O  
ATOM   2461  ND2 ASN B 134     -19.656 -36.589  38.705  1.00 11.98           N  
ANISOU 2461  ND2 ASN B 134     2107   1116   1328     52    161    130       N  
ATOM   2462  N   SER B 135     -23.873 -35.464  36.832  1.00 13.78           N  
ANISOU 2462  N   SER B 135     2228   1457   1548   -214    201    -18       N  
ATOM   2463  CA  SER B 135     -25.254 -35.846  37.154  1.00 14.50           C  
ANISOU 2463  CA  SER B 135     2329   1555   1625   -316    219    -37       C  
ATOM   2464  C   SER B 135     -26.296 -35.015  36.396  1.00 14.55           C  
ANISOU 2464  C   SER B 135     2252   1636   1641   -360    211    -85       C  
ATOM   2465  O   SER B 135     -27.496 -35.201  36.590  1.00 14.52           O  
ANISOU 2465  O   SER B 135     2232   1656   1629   -443    224   -106       O  
ATOM   2466  CB  SER B 135     -25.504 -35.730  38.663  1.00 15.03           C  
ANISOU 2466  CB  SER B 135     2398   1642   1672   -344    230     -3       C  
ATOM   2467  OG  SER B 135     -24.676 -36.625  39.392  1.00 15.80           O  
ANISOU 2467  OG  SER B 135     2584   1667   1754   -311    233     46       O  
ATOM   2468  N   SER B 136     -25.838 -34.105  35.537  1.00 14.35           N  
ANISOU 2468  N   SER B 136     2171   1649   1632   -303    188    -99       N  
ATOM   2469  CA  SER B 136     -26.736 -33.245  34.769  1.00 14.58           C  
ANISOU 2469  CA  SER B 136     2124   1747   1670   -329    171   -137       C  
ATOM   2470  C   SER B 136     -26.926 -33.789  33.352  1.00 14.53           C  
ANISOU 2470  C   SER B 136     2146   1718   1658   -346    163   -171       C  
ATOM   2471  O   SER B 136     -25.946 -34.040  32.649  1.00 14.21           O  
ANISOU 2471  O   SER B 136     2146   1638   1617   -292    163   -168       O  
ATOM   2472  CB  SER B 136     -26.193 -31.812  34.730  1.00 13.86           C  
ANISOU 2472  CB  SER B 136     1960   1711   1594   -263    149   -129       C  
ATOM   2473  OG  SER B 136     -24.896 -31.757  34.147  1.00 16.13           O  
ANISOU 2473  OG  SER B 136     2272   1971   1887   -192    142   -114       O  
ATOM   2474  N   LYS B 137     -28.186 -33.956  32.942  1.00 14.63           N  
ANISOU 2474  N   LYS B 137     2135   1761   1665   -423    158   -207       N  
ATOM   2475  CA  LYS B 137     -28.516 -34.541  31.629  1.00 15.25           C  
ANISOU 2475  CA  LYS B 137     2245   1822   1729   -455    147   -246       C  
ATOM   2476  C   LYS B 137     -28.030 -33.672  30.446  1.00 14.64           C  
ANISOU 2476  C   LYS B 137     2134   1779   1651   -395    118   -256       C  
ATOM   2477  O   LYS B 137     -27.461 -34.215  29.503  1.00 14.80           O  
ANISOU 2477  O   LYS B 137     2213   1756   1655   -377    121   -270       O  
ATOM   2478  CB  LYS B 137     -30.029 -34.881  31.504  1.00 15.77           C  
ANISOU 2478  CB  LYS B 137     2279   1925   1787   -560    142   -284       C  
ATOM   2479  CG  LYS B 137     -30.360 -36.251  30.795  1.00 18.20           C  
ANISOU 2479  CG  LYS B 137     2672   2169   2073   -633    152   -317       C  
ATOM   2480  CD  LYS B 137     -31.892 -36.469  30.483  1.00 18.62           C  
ANISOU 2480  CD  LYS B 137     2677   2278   2120   -744    137   -362       C  
ATOM   2481  CE  LYS B 137     -32.315 -37.957  30.090  1.00 19.99           C  
ANISOU 2481  CE  LYS B 137     2945   2379   2271   -843    155   -395       C  
ATOM   2482  NZ  LYS B 137     -32.720 -38.265  28.680  1.00 16.11           N  
ANISOU 2482  NZ  LYS B 137     2468   1896   1755   -884    124   -448       N  
ATOM   2483  N   PRO B 138     -28.236 -32.330  30.488  1.00 13.91           N  
ANISOU 2483  N   PRO B 138     1955   1759   1572   -363     93   -249       N  
ATOM   2484  CA  PRO B 138     -27.719 -31.507  29.389  1.00 13.46           C  
ANISOU 2484  CA  PRO B 138     1880   1726   1509   -308     68   -250       C  
ATOM   2485  C   PRO B 138     -26.201 -31.376  29.396  1.00 12.94           C  
ANISOU 2485  C   PRO B 138     1848   1622   1447   -232     86   -221       C  
ATOM   2486  O   PRO B 138     -25.571 -31.593  30.437  1.00 12.05           O  
ANISOU 2486  O   PRO B 138     1751   1480   1348   -208    107   -193       O  
ATOM   2487  CB  PRO B 138     -28.342 -30.132  29.661  1.00 13.23           C  
ANISOU 2487  CB  PRO B 138     1758   1771   1498   -293     41   -245       C  
ATOM   2488  CG  PRO B 138     -28.600 -30.113  31.095  1.00 13.12           C  
ANISOU 2488  CG  PRO B 138     1721   1762   1502   -308     63   -231       C  
ATOM   2489  CD  PRO B 138     -28.976 -31.506  31.462  1.00 13.84           C  
ANISOU 2489  CD  PRO B 138     1869   1809   1581   -375     89   -242       C  
ATOM   2490  N   THR B 139     -25.619 -31.020  28.246  1.00 12.79           N  
ANISOU 2490  N   THR B 139     1838   1608   1413   -196     77   -226       N  
ATOM   2491  CA  THR B 139     -24.215 -30.589  28.209  1.00 12.50           C  
ANISOU 2491  CA  THR B 139     1807   1558   1384   -124     92   -199       C  
ATOM   2492  C   THR B 139     -24.008 -29.498  29.250  1.00 12.02           C  
ANISOU 2492  C   THR B 139     1686   1531   1351    -96     84   -168       C  
ATOM   2493  O   THR B 139     -24.787 -28.537  29.307  1.00 12.24           O  
ANISOU 2493  O   THR B 139     1658   1607   1385   -108     59   -171       O  
ATOM   2494  CB  THR B 139     -23.806 -30.036  26.835  1.00 12.54           C  
ANISOU 2494  CB  THR B 139     1814   1585   1366    -99     83   -207       C  
ATOM   2495  OG1 THR B 139     -24.051 -31.028  25.830  1.00 13.73           O  
ANISOU 2495  OG1 THR B 139     2025   1707   1483   -129     90   -243       O  
ATOM   2496  CG2 THR B 139     -22.326 -29.661  26.825  1.00 12.00           C  
ANISOU 2496  CG2 THR B 139     1746   1506   1307    -34    107   -181       C  
ATOM   2497  N   ALA B 140     -22.974 -29.656  30.077  1.00 11.46           N  
ANISOU 2497  N   ALA B 140     1625   1434   1294    -57    104   -141       N  
ATOM   2498  CA  ALA B 140     -22.730 -28.749  31.190  1.00 10.80           C  
ANISOU 2498  CA  ALA B 140     1494   1379   1232    -38     97   -116       C  
ATOM   2499  C   ALA B 140     -21.303 -28.212  31.205  1.00 10.26           C  
ANISOU 2499  C   ALA B 140     1413   1312   1174     20    103    -91       C  
ATOM   2500  O   ALA B 140     -20.345 -28.916  30.855  1.00 10.24           O  
ANISOU 2500  O   ALA B 140     1444   1278   1169     53    122    -86       O  
ATOM   2501  CB  ALA B 140     -23.040 -29.438  32.509  1.00 10.87           C  
ANISOU 2501  CB  ALA B 140     1521   1367   1244    -62    108   -105       C  
ATOM   2502  N   VAL B 141     -21.181 -26.953  31.612  1.00  9.85           N  
ANISOU 2502  N   VAL B 141     1311   1297   1135     31     88    -79       N  
ATOM   2503  CA  VAL B 141     -19.883 -26.330  31.868  1.00  9.29           C  
ANISOU 2503  CA  VAL B 141     1218   1236   1077     72     91    -56       C  
ATOM   2504  C   VAL B 141     -19.925 -25.608  33.216  1.00  8.90           C  
ANISOU 2504  C   VAL B 141     1135   1207   1040     67     79    -43       C  
ATOM   2505  O   VAL B 141     -20.980 -25.133  33.638  1.00  8.44           O  
ANISOU 2505  O   VAL B 141     1059   1166    983     39     68    -55       O  
ATOM   2506  CB  VAL B 141     -19.463 -25.350  30.743  1.00  9.27           C  
ANISOU 2506  CB  VAL B 141     1196   1255   1072     85     88    -55       C  
ATOM   2507  CG1 VAL B 141     -19.210 -26.122  29.443  1.00  9.49           C  
ANISOU 2507  CG1 VAL B 141     1262   1265   1079     93    107    -69       C  
ATOM   2508  CG2 VAL B 141     -20.503 -24.237  30.549  1.00  8.96           C  
ANISOU 2508  CG2 VAL B 141     1131   1241   1034     63     63    -63       C  
ATOM   2509  N   LEU B 142     -18.779 -25.561  33.890  1.00  8.42           N  
ANISOU 2509  N   LEU B 142     1065   1149    987     95     80    -21       N  
ATOM   2510  CA  LEU B 142     -18.643 -24.869  35.166  1.00  8.32           C  
ANISOU 2510  CA  LEU B 142     1026   1158    979     90     66    -11       C  
ATOM   2511  C   LEU B 142     -17.647 -23.763  34.902  1.00  8.40           C  
ANISOU 2511  C   LEU B 142      998   1191   1002    107     59     -3       C  
ATOM   2512  O   LEU B 142     -16.489 -24.039  34.590  1.00  8.30           O  
ANISOU 2512  O   LEU B 142      978   1181    995    136     67     10       O  
ATOM   2513  CB  LEU B 142     -18.150 -25.820  36.270  1.00  8.30           C  
ANISOU 2513  CB  LEU B 142     1046   1140    968    102     66     10       C  
ATOM   2514  CG  LEU B 142     -18.184 -25.320  37.729  1.00  8.33           C  
ANISOU 2514  CG  LEU B 142     1036   1167    962     87     51     18       C  
ATOM   2515  CD1 LEU B 142     -18.135 -26.488  38.718  1.00  8.42           C  
ANISOU 2515  CD1 LEU B 142     1090   1155    953     89     51     41       C  
ATOM   2516  CD2 LEU B 142     -17.059 -24.326  38.041  1.00  8.94           C  
ANISOU 2516  CD2 LEU B 142     1071   1275   1049    105     34     28       C  
ATOM   2517  N   ILE B 143     -18.109 -22.518  34.979  1.00  8.31           N  
ANISOU 2517  N   ILE B 143      964   1197    998     89     48    -13       N  
ATOM   2518  CA  ILE B 143     -17.257 -21.375  34.685  1.00  8.68           C  
ANISOU 2518  CA  ILE B 143      983   1258   1056     93     43     -7       C  
ATOM   2519  C   ILE B 143     -16.645 -20.831  35.972  1.00  8.59           C  
ANISOU 2519  C   ILE B 143      951   1265   1048     86     30     -2       C  
ATOM   2520  O   ILE B 143     -17.355 -20.471  36.908  1.00  8.31           O  
ANISOU 2520  O   ILE B 143      917   1232   1007     69     21    -14       O  
ATOM   2521  CB  ILE B 143     -18.014 -20.248  33.952  1.00  8.38           C  
ANISOU 2521  CB  ILE B 143      943   1217   1023     80     37    -18       C  
ATOM   2522  CG1 ILE B 143     -18.797 -20.802  32.756  1.00  9.67           C  
ANISOU 2522  CG1 ILE B 143     1129   1369   1175     82     41    -25       C  
ATOM   2523  CG2 ILE B 143     -17.044 -19.176  33.475  1.00  9.03           C  
ANISOU 2523  CG2 ILE B 143     1011   1305   1114     77     38     -6       C  
ATOM   2524  CD1 ILE B 143     -19.650 -19.750  32.039  1.00 10.18           C  
ANISOU 2524  CD1 ILE B 143     1193   1434   1242     77     25    -31       C  
ATOM   2525  N   GLU B 144     -15.315 -20.812  36.003  1.00  8.92           N  
ANISOU 2525  N   GLU B 144      970   1324   1097     99     28     14       N  
ATOM   2526  CA  GLU B 144     -14.555 -20.135  37.034  1.00  9.39           C  
ANISOU 2526  CA  GLU B 144     1002   1408   1158     86     10     17       C  
ATOM   2527  C   GLU B 144     -14.040 -18.847  36.387  1.00  9.23           C  
ANISOU 2527  C   GLU B 144      960   1394   1152     65     12     14       C  
ATOM   2528  O   GLU B 144     -12.913 -18.799  35.895  1.00  8.92           O  
ANISOU 2528  O   GLU B 144      893   1375   1122     69     20     26       O  
ATOM   2529  CB  GLU B 144     -13.394 -21.020  37.511  1.00  9.96           C  
ANISOU 2529  CB  GLU B 144     1054   1501   1228    114      2     39       C  
ATOM   2530  CG  GLU B 144     -13.816 -22.388  38.063  1.00 11.29           C  
ANISOU 2530  CG  GLU B 144     1258   1652   1381    137      0     50       C  
ATOM   2531  CD  GLU B 144     -13.764 -22.496  39.587  1.00 13.37           C  
ANISOU 2531  CD  GLU B 144     1526   1930   1622    129    -27     58       C  
ATOM   2532  OE1 GLU B 144     -12.928 -21.832  40.228  1.00 15.41           O  
ANISOU 2532  OE1 GLU B 144     1750   2224   1879    120    -50     61       O  
ATOM   2533  OE2 GLU B 144     -14.555 -23.278  40.151  1.00 17.45           O  
ANISOU 2533  OE2 GLU B 144     2084   2427   2119    126    -24     63       O  
ATOM   2534  N   SER B 145     -14.895 -17.826  36.374  1.00  9.07           N  
ANISOU 2534  N   SER B 145      957   1356   1135     44      9     -2       N  
ATOM   2535  CA  SER B 145     -14.680 -16.591  35.600  1.00  8.99           C  
ANISOU 2535  CA  SER B 145      946   1333   1137     24     13     -2       C  
ATOM   2536  C   SER B 145     -13.396 -15.847  35.946  1.00  9.42           C  
ANISOU 2536  C   SER B 145      972   1409   1200     -5      8      3       C  
ATOM   2537  O   SER B 145     -12.701 -15.361  35.055  1.00 10.08           O  
ANISOU 2537  O   SER B 145     1045   1493   1290    -20     22     15       O  
ATOM   2538  CB  SER B 145     -15.859 -15.644  35.805  1.00  8.90           C  
ANISOU 2538  CB  SER B 145      960   1293   1129     16      4    -22       C  
ATOM   2539  OG  SER B 145     -17.035 -16.181  35.241  1.00  8.31           O  
ANISOU 2539  OG  SER B 145      902   1206   1050     37      8    -26       O  
ATOM   2540  N   PHE B 146     -13.117 -15.727  37.241  1.00  9.27           N  
ANISOU 2540  N   PHE B 146      939   1408   1176    -19    -13     -8       N  
ATOM   2541  CA  PHE B 146     -11.868 -15.140  37.719  1.00  9.70           C  
ANISOU 2541  CA  PHE B 146      958   1493   1235    -51    -25     -7       C  
ATOM   2542  C   PHE B 146     -11.654 -15.504  39.195  1.00 10.00           C  
ANISOU 2542  C   PHE B 146      984   1561   1256    -53    -54    -14       C  
ATOM   2543  O   PHE B 146     -12.488 -16.176  39.792  1.00  9.45           O  
ANISOU 2543  O   PHE B 146      939   1483   1169    -32    -58    -18       O  
ATOM   2544  CB  PHE B 146     -11.834 -13.616  37.491  1.00  9.89           C  
ANISOU 2544  CB  PHE B 146      999   1489   1271    -97    -24    -19       C  
ATOM   2545  CG  PHE B 146     -12.953 -12.858  38.161  1.00  9.10           C  
ANISOU 2545  CG  PHE B 146      941   1350   1167   -103    -33    -47       C  
ATOM   2546  CD1 PHE B 146     -12.808 -12.370  39.456  1.00  9.84           C  
ANISOU 2546  CD1 PHE B 146     1036   1453   1249   -131    -53    -72       C  
ATOM   2547  CD2 PHE B 146     -14.140 -12.604  37.483  1.00  8.54           C  
ANISOU 2547  CD2 PHE B 146      907   1237   1102    -80    -22    -50       C  
ATOM   2548  CE1 PHE B 146     -13.840 -11.663  40.074  1.00  8.89           C  
ANISOU 2548  CE1 PHE B 146      956   1298   1126   -133    -54   -104       C  
ATOM   2549  CE2 PHE B 146     -15.181 -11.894  38.090  1.00  7.70           C  
ANISOU 2549  CE2 PHE B 146      831   1098    998    -76    -27    -79       C  
ATOM   2550  CZ  PHE B 146     -15.033 -11.427  39.385  1.00  7.98           C  
ANISOU 2550  CZ  PHE B 146      870   1140   1023   -102    -39   -108       C  
ATOM   2551  N   PHE B 147     -10.527 -15.078  39.759  1.00 10.88           N  
ANISOU 2551  N   PHE B 147     1057   1709   1367    -84    -75    -15       N  
ATOM   2552  CA  PHE B 147     -10.192 -15.365  41.155  1.00 11.64           C  
ANISOU 2552  CA  PHE B 147     1142   1842   1439    -90   -111    -20       C  
ATOM   2553  C   PHE B 147     -10.766 -14.315  42.107  1.00 11.86           C  
ANISOU 2553  C   PHE B 147     1205   1851   1449   -132   -123    -55       C  
ATOM   2554  O   PHE B 147     -10.446 -13.136  41.998  1.00 12.06           O  
ANISOU 2554  O   PHE B 147     1231   1864   1486   -179   -124    -74       O  
ATOM   2555  CB  PHE B 147      -8.672 -15.472  41.324  1.00 12.37           C  
ANISOU 2555  CB  PHE B 147     1167   1995   1538   -100   -134     -6       C  
ATOM   2556  CG  PHE B 147      -8.127 -16.810  40.940  1.00 12.89           C  
ANISOU 2556  CG  PHE B 147     1200   2087   1611    -41   -131     25       C  
ATOM   2557  CD1 PHE B 147      -7.633 -17.682  41.903  1.00 14.07           C  
ANISOU 2557  CD1 PHE B 147     1329   2276   1742    -10   -168     42       C  
ATOM   2558  CD2 PHE B 147      -8.153 -17.228  39.614  1.00 13.42           C  
ANISOU 2558  CD2 PHE B 147     1263   2135   1700    -11    -92     37       C  
ATOM   2559  CE1 PHE B 147      -7.149 -18.936  41.550  1.00 13.82           C  
ANISOU 2559  CE1 PHE B 147     1273   2257   1719     55   -166     71       C  
ATOM   2560  CE2 PHE B 147      -7.668 -18.481  39.258  1.00 13.29           C  
ANISOU 2560  CE2 PHE B 147     1223   2135   1690     49    -85     60       C  
ATOM   2561  CZ  PHE B 147      -7.166 -19.331  40.224  1.00 13.44           C  
ANISOU 2561  CZ  PHE B 147     1221   2187   1697     85   -121     77       C  
ATOM   2562  N   CYS B 148     -11.610 -14.753  43.045  1.00 12.04           N  
ANISOU 2562  N   CYS B 148     1262   1871   1443   -119   -130    -65       N  
ATOM   2563  CA  CYS B 148     -12.252 -13.841  43.999  1.00 12.25           C  
ANISOU 2563  CA  CYS B 148     1325   1880   1448   -153   -134   -105       C  
ATOM   2564  C   CYS B 148     -11.291 -13.310  45.074  1.00 13.00           C  
ANISOU 2564  C   CYS B 148     1405   2016   1517   -199   -172   -121       C  
ATOM   2565  O   CYS B 148     -11.626 -12.370  45.810  1.00 13.04           O  
ANISOU 2565  O   CYS B 148     1443   2007   1506   -237   -175   -161       O  
ATOM   2566  CB  CYS B 148     -13.456 -14.514  44.670  1.00 12.16           C  
ANISOU 2566  CB  CYS B 148     1351   1861   1408   -129   -122   -113       C  
ATOM   2567  SG  CYS B 148     -13.044 -15.817  45.874  1.00 13.22           S  
ANISOU 2567  SG  CYS B 148     1485   2046   1493   -116   -152    -85       S  
ATOM   2568  N   ASP B 149     -10.104 -13.906  45.158  1.00 13.34           N  
ANISOU 2568  N   ASP B 149     1398   2113   1559   -196   -202    -93       N  
ATOM   2569  CA  ASP B 149      -9.097 -13.486  46.124  1.00 14.03           C  
ANISOU 2569  CA  ASP B 149     1458   2253   1621   -241   -247   -105       C  
ATOM   2570  C   ASP B 149      -7.923 -12.773  45.448  1.00 14.47           C  
ANISOU 2570  C   ASP B 149     1458   2329   1711   -281   -254   -104       C  
ATOM   2571  O   ASP B 149      -6.835 -12.677  46.021  1.00 14.72           O  
ANISOU 2571  O   ASP B 149     1441   2421   1731   -313   -296   -104       O  
ATOM   2572  CB  ASP B 149      -8.605 -14.697  46.916  1.00 14.50           C  
ANISOU 2572  CB  ASP B 149     1496   2368   1647   -206   -286    -72       C  
ATOM   2573  CG  ASP B 149      -7.943 -15.743  46.041  1.00 14.26           C  
ANISOU 2573  CG  ASP B 149     1414   2356   1648   -150   -283    -27       C  
ATOM   2574  OD1 ASP B 149      -7.959 -15.599  44.800  1.00 13.68           O  
ANISOU 2574  OD1 ASP B 149     1326   2255   1617   -140   -246    -22       O  
ATOM   2575  OD2 ASP B 149      -7.416 -16.722  46.599  1.00 15.71           O  
ANISOU 2575  OD2 ASP B 149     1578   2582   1811   -113   -318      5       O  
ATOM   2576  N   ASN B 150      -8.153 -12.272  44.237  1.00 14.09           N  
ANISOU 2576  N   ASN B 150     1417   2235   1703   -284   -213   -103       N  
ATOM   2577  CA  ASN B 150      -7.133 -11.560  43.476  1.00 14.63           C  
ANISOU 2577  CA  ASN B 150     1440   2316   1802   -330   -207   -101       C  
ATOM   2578  C   ASN B 150      -7.656 -10.179  43.056  1.00 14.76           C  
ANISOU 2578  C   ASN B 150     1512   2262   1835   -379   -181   -129       C  
ATOM   2579  O   ASN B 150      -8.611 -10.081  42.282  1.00 14.36           O  
ANISOU 2579  O   ASN B 150     1506   2151   1799   -347   -146   -124       O  
ATOM   2580  CB  ASN B 150      -6.706 -12.407  42.268  1.00 14.32           C  
ANISOU 2580  CB  ASN B 150     1355   2294   1792   -283   -180    -62       C  
ATOM   2581  CG  ASN B 150      -5.559 -11.782  41.482  1.00 15.14           C  
ANISOU 2581  CG  ASN B 150     1402   2425   1924   -333   -167    -57       C  
ATOM   2582  OD1 ASN B 150      -5.762 -10.831  40.726  1.00 14.95           O  
ANISOU 2582  OD1 ASN B 150     1411   2353   1918   -373   -136    -64       O  
ATOM   2583  ND2 ASN B 150      -4.346 -12.313  41.661  1.00 15.56           N  
ANISOU 2583  ND2 ASN B 150     1369   2558   1983   -330   -190    -43       N  
ATOM   2584  N   LYS B 151      -7.033  -9.125  43.587  1.00 15.63           N  
ANISOU 2584  N   LYS B 151     1621   2377   1940   -456   -200   -159       N  
ATOM   2585  CA  LYS B 151      -7.453  -7.731  43.352  1.00 16.16           C  
ANISOU 2585  CA  LYS B 151     1753   2367   2020   -507   -180   -190       C  
ATOM   2586  C   LYS B 151      -7.457  -7.342  41.875  1.00 15.49           C  
ANISOU 2586  C   LYS B 151     1677   2236   1972   -508   -139   -163       C  
ATOM   2587  O   LYS B 151      -8.360  -6.649  41.414  1.00 15.01           O  
ANISOU 2587  O   LYS B 151     1685   2095   1922   -498   -115   -171       O  
ATOM   2588  CB  LYS B 151      -6.513  -6.750  44.072  1.00 17.29           C  
ANISOU 2588  CB  LYS B 151     1885   2529   2153   -602   -209   -224       C  
ATOM   2589  CG  LYS B 151      -6.496  -6.830  45.596  1.00 19.81           C  
ANISOU 2589  CG  LYS B 151     2212   2888   2426   -620   -254   -260       C  
ATOM   2590  CD  LYS B 151      -7.489  -5.868  46.256  1.00 21.89           C  
ANISOU 2590  CD  LYS B 151     2570   3075   2672   -637   -243   -313       C  
ATOM   2591  CE  LYS B 151      -7.100  -5.565  47.705  1.00 24.00           C  
ANISOU 2591  CE  LYS B 151     2846   3384   2890   -694   -288   -359       C  
ATOM   2592  NZ  LYS B 151      -6.703  -6.782  48.485  1.00 24.12           N  
ANISOU 2592  NZ  LYS B 151     2806   3494   2865   -661   -330   -336       N  
ATOM   2593  N   GLU B 152      -6.422  -7.765  41.153  1.00 15.56           N  
ANISOU 2593  N   GLU B 152     1617   2299   1997   -519   -131   -132       N  
ATOM   2594  CA  GLU B 152      -6.246  -7.389  39.748  1.00 15.57           C  
ANISOU 2594  CA  GLU B 152     1625   2268   2024   -533    -89   -105       C  
ATOM   2595  C   GLU B 152      -7.367  -7.971  38.892  1.00 14.18           C  
ANISOU 2595  C   GLU B 152     1490   2048   1851   -453    -62    -81       C  
ATOM   2596  O   GLU B 152      -7.935  -7.271  38.061  1.00 13.82           O  
ANISOU 2596  O   GLU B 152     1503   1935   1815   -457    -37    -73       O  
ATOM   2597  CB  GLU B 152      -4.875  -7.828  39.215  1.00 16.24           C  
ANISOU 2597  CB  GLU B 152     1616   2434   2121   -558    -80    -81       C  
ATOM   2598  CG  GLU B 152      -3.705  -6.965  39.702  1.00 19.32           C  
ANISOU 2598  CG  GLU B 152     1963   2862   2515   -660    -99   -102       C  
ATOM   2599  CD  GLU B 152      -3.436  -7.087  41.198  1.00 22.49           C  
ANISOU 2599  CD  GLU B 152     2339   3313   2894   -676   -156   -133       C  
ATOM   2600  OE1 GLU B 152      -3.571  -8.208  41.759  1.00 24.26           O  
ANISOU 2600  OE1 GLU B 152     2530   3585   3101   -605   -182   -124       O  
ATOM   2601  OE2 GLU B 152      -3.088  -6.057  41.817  1.00 24.22           O  
ANISOU 2601  OE2 GLU B 152     2576   3521   3107   -762   -176   -168       O  
ATOM   2602  N   ASP B 153      -7.675  -9.248  39.112  1.00 13.22           N  
ANISOU 2602  N   ASP B 153     1340   1964   1718   -383    -70    -70       N  
ATOM   2603  CA  ASP B 153      -8.824  -9.906  38.474  1.00 12.26           C  
ANISOU 2603  CA  ASP B 153     1255   1807   1595   -312    -51    -55       C  
ATOM   2604  C   ASP B 153     -10.134  -9.184  38.773  1.00 11.88           C  
ANISOU 2604  C   ASP B 153     1282   1688   1545   -301    -52    -79       C  
ATOM   2605  O   ASP B 153     -10.911  -8.888  37.865  1.00 11.56           O  
ANISOU 2605  O   ASP B 153     1283   1595   1513   -278    -33    -68       O  
ATOM   2606  CB  ASP B 153      -8.954 -11.360  38.949  1.00 11.74           C  
ANISOU 2606  CB  ASP B 153     1158   1788   1516   -251    -64    -46       C  
ATOM   2607  CG  ASP B 153      -8.219 -12.349  38.061  1.00 11.71           C  
ANISOU 2607  CG  ASP B 153     1102   1827   1521   -219    -45    -15       C  
ATOM   2608  OD1 ASP B 153      -7.432 -11.948  37.173  1.00 13.30           O  
ANISOU 2608  OD1 ASP B 153     1277   2040   1736   -250    -21     -3       O  
ATOM   2609  OD2 ASP B 153      -8.442 -13.558  38.257  1.00 10.96           O  
ANISOU 2609  OD2 ASP B 153      996   1751   1417   -162    -50     -5       O  
ATOM   2610  N   TYR B 154     -10.379  -8.903  40.048  1.00 11.97           N  
ANISOU 2610  N   TYR B 154     1308   1700   1541   -315    -76   -113       N  
ATOM   2611  CA  TYR B 154     -11.637  -8.287  40.446  1.00 11.85           C  
ANISOU 2611  CA  TYR B 154     1354   1623   1523   -297    -73   -143       C  
ATOM   2612  C   TYR B 154     -11.774  -6.859  39.900  1.00 12.00           C  
ANISOU 2612  C   TYR B 154     1428   1567   1563   -331    -61   -152       C  
ATOM   2613  O   TYR B 154     -12.867  -6.440  39.510  1.00 11.51           O  
ANISOU 2613  O   TYR B 154     1414   1446   1512   -292    -49   -157       O  
ATOM   2614  CB  TYR B 154     -11.800  -8.315  41.971  1.00 12.06           C  
ANISOU 2614  CB  TYR B 154     1386   1673   1522   -308    -95   -181       C  
ATOM   2615  CG  TYR B 154     -13.166  -7.866  42.437  1.00 12.97           C  
ANISOU 2615  CG  TYR B 154     1557   1738   1634   -278    -84   -217       C  
ATOM   2616  CD1 TYR B 154     -14.323  -8.312  41.800  1.00 13.35           C  
ANISOU 2616  CD1 TYR B 154     1616   1763   1694   -216    -64   -204       C  
ATOM   2617  CD2 TYR B 154     -13.306  -6.999  43.519  1.00 14.38           C  
ANISOU 2617  CD2 TYR B 154     1772   1895   1796   -311    -91   -266       C  
ATOM   2618  CE1 TYR B 154     -15.572  -7.903  42.214  1.00 14.17           C  
ANISOU 2618  CE1 TYR B 154     1755   1830   1799   -185    -52   -239       C  
ATOM   2619  CE2 TYR B 154     -14.559  -6.583  43.939  1.00 15.41           C  
ANISOU 2619  CE2 TYR B 154     1947   1982   1926   -276    -74   -303       C  
ATOM   2620  CZ  TYR B 154     -15.690  -7.042  43.285  1.00 15.25           C  
ANISOU 2620  CZ  TYR B 154     1926   1946   1922   -211    -54   -288       C  
ATOM   2621  OH  TYR B 154     -16.943  -6.642  43.698  1.00 16.54           O  
ANISOU 2621  OH  TYR B 154     2120   2077   2089   -173    -35   -327       O  
ATOM   2622  N   ASP B 155     -10.665  -6.127  39.859  1.00 12.45           N  
ANISOU 2622  N   ASP B 155     1477   1626   1626   -403    -64   -153       N  
ATOM   2623  CA  ASP B 155     -10.644  -4.802  39.235  1.00 13.25           C  
ANISOU 2623  CA  ASP B 155     1638   1650   1747   -445    -50   -154       C  
ATOM   2624  C   ASP B 155     -11.015  -4.868  37.753  1.00 13.11           C  
ANISOU 2624  C   ASP B 155     1640   1600   1742   -410    -26   -109       C  
ATOM   2625  O   ASP B 155     -11.779  -4.029  37.263  1.00 13.36           O  
ANISOU 2625  O   ASP B 155     1740   1552   1786   -394    -18   -106       O  
ATOM   2626  CB  ASP B 155      -9.279  -4.126  39.429  1.00 14.23           C  
ANISOU 2626  CB  ASP B 155     1741   1793   1872   -542    -55   -161       C  
ATOM   2627  CG  ASP B 155      -9.108  -3.549  40.829  1.00 14.67           C  
ANISOU 2627  CG  ASP B 155     1813   1848   1913   -590    -82   -214       C  
ATOM   2628  OD1 ASP B 155     -10.124  -3.396  41.538  1.00 16.18           O  
ANISOU 2628  OD1 ASP B 155     2049   2002   2095   -549    -86   -248       O  
ATOM   2629  OD2 ASP B 155      -7.967  -3.243  41.221  1.00 15.90           O  
ANISOU 2629  OD2 ASP B 155     1933   2044   2064   -670    -97   -226       O  
ATOM   2630  N   LYS B 156     -10.500  -5.875  37.055  1.00 12.91           N  
ANISOU 2630  N   LYS B 156     1558   1636   1712   -395    -15    -74       N  
ATOM   2631  CA  LYS B 156     -10.875  -6.120  35.663  1.00 12.85           C  
ANISOU 2631  CA  LYS B 156     1567   1608   1705   -359      7    -34       C  
ATOM   2632  C   LYS B 156     -12.362  -6.448  35.535  1.00 12.35           C  
ANISOU 2632  C   LYS B 156     1538   1512   1641   -280      0    -38       C  
ATOM   2633  O   LYS B 156     -12.995  -6.071  34.558  1.00 12.24           O  
ANISOU 2633  O   LYS B 156     1570   1451   1630   -256      7    -15       O  
ATOM   2634  CB  LYS B 156     -10.059  -7.274  35.068  1.00 12.74           C  
ANISOU 2634  CB  LYS B 156     1485   1671   1683   -351     23     -8       C  
ATOM   2635  CG  LYS B 156      -8.595  -6.965  34.812  1.00 14.11           C  
ANISOU 2635  CG  LYS B 156     1615   1886   1862   -425     40      4       C  
ATOM   2636  CD  LYS B 156      -7.840  -8.251  34.515  1.00 14.33           C  
ANISOU 2636  CD  LYS B 156     1562   1998   1885   -398     53     19       C  
ATOM   2637  CE  LYS B 156      -6.431  -7.971  34.039  1.00 16.81           C  
ANISOU 2637  CE  LYS B 156     1822   2360   2205   -465     79     32       C  
ATOM   2638  NZ  LYS B 156      -5.741  -9.229  33.662  1.00 16.49           N  
ANISOU 2638  NZ  LYS B 156     1704   2398   2163   -425     96     44       N  
ATOM   2639  N   ALA B 157     -12.909  -7.152  36.525  1.00 12.02           N  
ANISOU 2639  N   ALA B 157     1473   1502   1594   -244    -15    -65       N  
ATOM   2640  CA  ALA B 157     -14.323  -7.516  36.536  1.00 11.42           C  
ANISOU 2640  CA  ALA B 157     1415   1406   1517   -177    -19    -74       C  
ATOM   2641  C   ALA B 157     -15.227  -6.298  36.707  1.00 11.88           C  
ANISOU 2641  C   ALA B 157     1534   1389   1591   -163    -24    -97       C  
ATOM   2642  O   ALA B 157     -16.215  -6.141  35.978  1.00 11.73           O  
ANISOU 2642  O   ALA B 157     1542   1335   1581   -114    -26    -84       O  
ATOM   2643  CB  ALA B 157     -14.594  -8.532  37.632  1.00 10.93           C  
ANISOU 2643  CB  ALA B 157     1316   1396   1441   -155    -28    -97       C  
ATOM   2644  N   LYS B 158     -14.884  -5.437  37.662  1.00 12.51           N  
ANISOU 2644  N   LYS B 158     1636   1444   1675   -204    -29   -131       N  
ATOM   2645  CA  LYS B 158     -15.629  -4.191  37.886  1.00 13.17           C  
ANISOU 2645  CA  LYS B 158     1784   1444   1775   -191    -30   -158       C  
ATOM   2646  C   LYS B 158     -15.459  -3.203  36.730  1.00 13.53           C  
ANISOU 2646  C   LYS B 158     1887   1418   1837   -205    -26   -123       C  
ATOM   2647  O   LYS B 158     -16.345  -2.381  36.476  1.00 13.50           O  
ANISOU 2647  O   LYS B 158     1939   1340   1850   -163    -30   -128       O  
ATOM   2648  CB  LYS B 158     -15.209  -3.526  39.198  1.00 13.69           C  
ANISOU 2648  CB  LYS B 158     1868   1499   1836   -240    -34   -209       C  
ATOM   2649  CG  LYS B 158     -15.548  -4.338  40.427  1.00 14.12           C  
ANISOU 2649  CG  LYS B 158     1883   1614   1867   -223    -39   -245       C  
ATOM   2650  CD  LYS B 158     -15.244  -3.594  41.720  1.00 15.99           C  
ANISOU 2650  CD  LYS B 158     2149   1837   2091   -270    -44   -300       C  
ATOM   2651  CE  LYS B 158     -13.777  -3.680  42.090  1.00 16.77           C  
ANISOU 2651  CE  LYS B 158     2217   1983   2171   -351    -60   -296       C  
ATOM   2652  NZ  LYS B 158     -13.500  -3.079  43.425  1.00 18.09           N  
ANISOU 2652  NZ  LYS B 158     2409   2149   2315   -401    -72   -353       N  
ATOM   2653  N   LYS B 159     -14.324  -3.278  36.040  1.00 13.68           N  
ANISOU 2653  N   LYS B 159     1892   1458   1848   -262    -17    -88       N  
ATOM   2654  CA  LYS B 159     -14.093  -2.470  34.844  1.00 14.26           C  
ANISOU 2654  CA  LYS B 159     2021   1470   1926   -284     -8    -45       C  
ATOM   2655  C   LYS B 159     -15.017  -2.957  33.729  1.00 13.64           C  
ANISOU 2655  C   LYS B 159     1950   1391   1843   -212    -12     -8       C  
ATOM   2656  O   LYS B 159     -15.716  -2.163  33.107  1.00 13.77           O  
ANISOU 2656  O   LYS B 159     2030   1334   1868   -179    -20     10       O  
ATOM   2657  CB  LYS B 159     -12.626  -2.551  34.410  1.00 14.77           C  
ANISOU 2657  CB  LYS B 159     2056   1576   1981   -368     11    -20       C  
ATOM   2658  CG  LYS B 159     -12.330  -1.845  33.111  1.00 16.26           C  
ANISOU 2658  CG  LYS B 159     2301   1712   2165   -400     28     30       C  
ATOM   2659  CD  LYS B 159     -10.847  -1.548  32.944  1.00 18.89           C  
ANISOU 2659  CD  LYS B 159     2612   2072   2493   -503     52     42       C  
ATOM   2660  CE  LYS B 159     -10.550  -1.014  31.553  1.00 20.45           C  
ANISOU 2660  CE  LYS B 159     2863   2229   2677   -537     78     98       C  
ATOM   2661  NZ  LYS B 159      -9.344  -0.129  31.562  1.00 23.00           N  
ANISOU 2661  NZ  LYS B 159     3201   2535   3003   -653    101    102       N  
ATOM   2662  N   LEU B 160     -15.009  -4.267  33.495  1.00 13.07           N  
ANISOU 2662  N   LEU B 160     1814   1397   1755   -188     -9      2       N  
ATOM   2663  CA  LEU B 160     -15.911  -4.924  32.540  1.00 12.90           C  
ANISOU 2663  CA  LEU B 160     1791   1388   1723   -124    -16     28       C  
ATOM   2664  C   LEU B 160     -17.385  -4.755  32.892  1.00 12.91           C  
ANISOU 2664  C   LEU B 160     1806   1360   1740    -51    -38      4       C  
ATOM   2665  O   LEU B 160     -18.223  -4.634  32.002  1.00 13.19           O  
ANISOU 2665  O   LEU B 160     1866   1372   1773     -2    -53     28       O  
ATOM   2666  CB  LEU B 160     -15.615  -6.433  32.457  1.00 12.47           C  
ANISOU 2666  CB  LEU B 160     1667   1420   1650   -115     -7     31       C  
ATOM   2667  CG  LEU B 160     -14.784  -6.949  31.280  1.00 13.70           C  
ANISOU 2667  CG  LEU B 160     1812   1609   1783   -140     14     70       C  
ATOM   2668  CD1 LEU B 160     -13.568  -6.102  31.083  1.00 16.47           C  
ANISOU 2668  CD1 LEU B 160     2179   1943   2134   -214     35     86       C  
ATOM   2669  CD2 LEU B 160     -14.387  -8.423  31.476  1.00 13.65           C  
ANISOU 2669  CD2 LEU B 160     1739   1680   1766   -129     25     62       C  
ATOM   2670  N   GLY B 161     -17.695  -4.769  34.185  1.00 12.62           N  
ANISOU 2670  N   GLY B 161     1747   1331   1715    -43    -39    -44       N  
ATOM   2671  CA  GLY B 161     -19.072  -4.841  34.645  1.00 12.66           C  
ANISOU 2671  CA  GLY B 161     1745   1332   1735     25    -51    -75       C  
ATOM   2672  C   GLY B 161     -19.655  -6.224  34.445  1.00 12.14           C  
ANISOU 2672  C   GLY B 161     1621   1337   1654     58    -53    -71       C  
ATOM   2673  O   GLY B 161     -19.025  -7.101  33.834  1.00 11.56           O  
ANISOU 2673  O   GLY B 161     1524   1307   1560     36    -47    -43       O  
ATOM   2674  N   HIS B 162     -20.866  -6.426  34.957  1.00 12.38           N  
ANISOU 2674  N   HIS B 162     1629   1379   1696    109    -59   -102       N  
ATOM   2675  CA  HIS B 162     -21.552  -7.707  34.810  1.00 12.17           C  
ANISOU 2675  CA  HIS B 162     1551   1416   1658    133    -60   -103       C  
ATOM   2676  C   HIS B 162     -21.861  -7.993  33.346  1.00 12.11           C  
ANISOU 2676  C   HIS B 162     1550   1411   1641    155    -78    -62       C  
ATOM   2677  O   HIS B 162     -21.752  -9.130  32.890  1.00 11.15           O  
ANISOU 2677  O   HIS B 162     1401   1337   1498    145    -75    -48       O  
ATOM   2678  CB  HIS B 162     -22.844  -7.744  35.631  1.00 12.39           C  
ANISOU 2678  CB  HIS B 162     1550   1458   1701    177    -58   -147       C  
ATOM   2679  CG  HIS B 162     -22.625  -7.603  37.105  1.00 13.18           C  
ANISOU 2679  CG  HIS B 162     1646   1565   1798    153    -37   -191       C  
ATOM   2680  ND1 HIS B 162     -21.627  -8.275  37.775  1.00 14.00           N  
ANISOU 2680  ND1 HIS B 162     1738   1703   1877    101    -26   -191       N  
ATOM   2681  CD2 HIS B 162     -23.273  -6.866  38.038  1.00 14.16           C  
ANISOU 2681  CD2 HIS B 162     1777   1666   1937    177    -26   -238       C  
ATOM   2682  CE1 HIS B 162     -21.666  -7.954  39.056  1.00 14.43           C  
ANISOU 2682  CE1 HIS B 162     1796   1760   1926     88    -13   -234       C  
ATOM   2683  NE2 HIS B 162     -22.656  -7.101  39.242  1.00 14.30           N  
ANISOU 2683  NE2 HIS B 162     1793   1708   1933    132     -9   -266       N  
ATOM   2684  N   GLU B 163     -22.259  -6.951  32.621  1.00 13.12           N  
ANISOU 2684  N   GLU B 163     1721   1485   1781    186    -98    -42       N  
ATOM   2685  CA  GLU B 163     -22.589  -7.050  31.199  1.00 13.43           C  
ANISOU 2685  CA  GLU B 163     1777   1522   1804    209   -122      0       C  
ATOM   2686  C   GLU B 163     -21.357  -7.429  30.356  1.00 13.20           C  
ANISOU 2686  C   GLU B 163     1769   1504   1743    155   -106     39       C  
ATOM   2687  O   GLU B 163     -21.460  -8.224  29.410  1.00 12.83           O  
ANISOU 2687  O   GLU B 163     1713   1493   1669    158   -113     61       O  
ATOM   2688  CB  GLU B 163     -23.210  -5.720  30.758  1.00 14.83           C  
ANISOU 2688  CB  GLU B 163     2004   1629   2001    257   -149     15       C  
ATOM   2689  CG  GLU B 163     -23.213  -5.359  29.295  1.00 16.52           C  
ANISOU 2689  CG  GLU B 163     2268   1816   2192    269   -175     71       C  
ATOM   2690  CD  GLU B 163     -23.676  -3.913  29.102  1.00 19.04           C  
ANISOU 2690  CD  GLU B 163     2650   2049   2535    316   -200     88       C  
ATOM   2691  OE1 GLU B 163     -22.834  -3.035  28.783  1.00 18.20           O  
ANISOU 2691  OE1 GLU B 163     2615   1877   2423    280   -191    119       O  
ATOM   2692  OE2 GLU B 163     -24.878  -3.649  29.324  1.00 21.46           O  
ANISOU 2692  OE2 GLU B 163     2933   2351   2869    389   -227     67       O  
ATOM   2693  N   GLY B 164     -20.198  -6.873  30.703  1.00 12.76           N  
ANISOU 2693  N   GLY B 164     1736   1421   1689    105    -85     44       N  
ATOM   2694  CA  GLY B 164     -18.958  -7.177  29.984  1.00 12.36           C  
ANISOU 2694  CA  GLY B 164     1694   1388   1612     52    -62     76       C  
ATOM   2695  C   GLY B 164     -18.570  -8.635  30.128  1.00 11.54           C  
ANISOU 2695  C   GLY B 164     1535   1357   1493     40    -45     65       C  
ATOM   2696  O   GLY B 164     -18.232  -9.296  29.146  1.00 11.52           O  
ANISOU 2696  O   GLY B 164     1533   1382   1463     32    -36     89       O  
ATOM   2697  N   ILE B 165     -18.619  -9.131  31.360  1.00 10.83           N  
ANISOU 2697  N   ILE B 165     1404   1294   1417     40    -40     29       N  
ATOM   2698  CA  ILE B 165     -18.344 -10.534  31.651  1.00 10.17           C  
ANISOU 2698  CA  ILE B 165     1275   1269   1321     36    -27     19       C  
ATOM   2699  C   ILE B 165     -19.365 -11.426  30.934  1.00  9.55           C  
ANISOU 2699  C   ILE B 165     1188   1212   1228     71    -39     21       C  
ATOM   2700  O   ILE B 165     -18.989 -12.343  30.211  1.00  8.49           O  
ANISOU 2700  O   ILE B 165     1049   1105   1071     65    -28     34       O  
ATOM   2701  CB  ILE B 165     -18.370 -10.808  33.171  1.00 10.17           C  
ANISOU 2701  CB  ILE B 165     1243   1286   1333     31    -25    -17       C  
ATOM   2702  CG1 ILE B 165     -17.159 -10.161  33.847  1.00 11.28           C  
ANISOU 2702  CG1 ILE B 165     1384   1421   1480    -15    -16    -21       C  
ATOM   2703  CG2 ILE B 165     -18.410 -12.330  33.468  1.00  9.37           C  
ANISOU 2703  CG2 ILE B 165     1106   1235   1218     39    -17    -24       C  
ATOM   2704  CD1 ILE B 165     -15.879 -10.968  33.743  1.00 11.10           C  
ANISOU 2704  CD1 ILE B 165     1329   1443   1445    -42     -1     -5       C  
ATOM   2705  N   ALA B 166     -20.650 -11.130  31.122  1.00  9.29           N  
ANISOU 2705  N   ALA B 166     1153   1167   1208    108    -61      4       N  
ATOM   2706  CA  ALA B 166     -21.726 -11.867  30.455  1.00  8.97           C  
ANISOU 2706  CA  ALA B 166     1100   1152   1156    136    -79      2       C  
ATOM   2707  C   ALA B 166     -21.542 -11.938  28.945  1.00  9.41           C  
ANISOU 2707  C   ALA B 166     1187   1206   1181    135    -88     37       C  
ATOM   2708  O   ALA B 166     -21.694 -13.011  28.356  1.00  8.79           O  
ANISOU 2708  O   ALA B 166     1100   1161   1080    131    -87     37       O  
ATOM   2709  CB  ALA B 166     -23.086 -11.265  30.782  1.00  8.76           C  
ANISOU 2709  CB  ALA B 166     1061   1116   1153    178   -104    -18       C  
ATOM   2710  N   LYS B 167     -21.225 -10.802  28.327  1.00  9.96           N  
ANISOU 2710  N   LYS B 167     1301   1235   1249    134    -96     67       N  
ATOM   2711  CA  LYS B 167     -21.064 -10.734  26.878  1.00 11.04           C  
ANISOU 2711  CA  LYS B 167     1479   1368   1348    131   -105    104       C  
ATOM   2712  C   LYS B 167     -20.005 -11.727  26.383  1.00 10.88           C  
ANISOU 2712  C   LYS B 167     1454   1382   1297     94    -68    111       C  
ATOM   2713  O   LYS B 167     -20.220 -12.417  25.383  1.00 10.49           O  
ANISOU 2713  O   LYS B 167     1417   1357   1212     96    -73    119       O  
ATOM   2714  CB  LYS B 167     -20.712  -9.306  26.435  1.00 11.75           C  
ANISOU 2714  CB  LYS B 167     1626   1400   1439    126   -111    140       C  
ATOM   2715  CG  LYS B 167     -20.633  -9.114  24.922  1.00 14.08           C  
ANISOU 2715  CG  LYS B 167     1974   1688   1686    122   -122    185       C  
ATOM   2716  CD  LYS B 167     -20.199  -7.700  24.559  1.00 16.38           C  
ANISOU 2716  CD  LYS B 167     2332   1914   1977    108   -124    225       C  
ATOM   2717  CE  LYS B 167     -20.217  -7.483  23.053  1.00 18.64           C  
ANISOU 2717  CE  LYS B 167     2681   2194   2208    105   -138    276       C  
ATOM   2718  NZ  LYS B 167     -19.343  -6.352  22.635  1.00 19.77           N  
ANISOU 2718  NZ  LYS B 167     2893   2279   2338     63   -117    319       N  
ATOM   2719  N   LEU B 168     -18.883 -11.813  27.097  1.00 10.77           N  
ANISOU 2719  N   LEU B 168     1421   1373   1298     63    -34    104       N  
ATOM   2720  CA  LEU B 168     -17.773 -12.683  26.679  1.00 10.91           C  
ANISOU 2720  CA  LEU B 168     1427   1424   1293     37      3    108       C  
ATOM   2721  C   LEU B 168     -18.171 -14.154  26.768  1.00 10.45           C  
ANISOU 2721  C   LEU B 168     1343   1402   1227     55      6     83       C  
ATOM   2722  O   LEU B 168     -17.839 -14.954  25.889  1.00 10.28           O  
ANISOU 2722  O   LEU B 168     1331   1400   1173     51     25     86       O  
ATOM   2723  CB  LEU B 168     -16.529 -12.422  27.535  1.00 10.67           C  
ANISOU 2723  CB  LEU B 168     1370   1398   1286      5     31    104       C  
ATOM   2724  CG  LEU B 168     -15.825 -11.083  27.308  1.00 11.26           C  
ANISOU 2724  CG  LEU B 168     1474   1440   1364    -32     40    129       C  
ATOM   2725  CD1 LEU B 168     -14.789 -10.822  28.405  1.00 10.27           C  
ANISOU 2725  CD1 LEU B 168     1311   1324   1266    -66     56    115       C  
ATOM   2726  CD2 LEU B 168     -15.172 -11.035  25.943  1.00 10.51           C  
ANISOU 2726  CD2 LEU B 168     1410   1353   1231    -56     68    161       C  
ATOM   2727  N   ILE B 169     -18.882 -14.490  27.844  1.00  9.96           N  
ANISOU 2727  N   ILE B 169     1251   1343   1190     70     -9     56       N  
ATOM   2728  CA  ILE B 169     -19.409 -15.837  28.063  1.00  9.43           C  
ANISOU 2728  CA  ILE B 169     1165   1301   1118     80     -8     33       C  
ATOM   2729  C   ILE B 169     -20.411 -16.205  26.972  1.00  9.50           C  
ANISOU 2729  C   ILE B 169     1194   1317   1098     91    -31     32       C  
ATOM   2730  O   ILE B 169     -20.331 -17.280  26.381  1.00  9.20           O  
ANISOU 2730  O   ILE B 169     1166   1295   1035     85    -18     24       O  
ATOM   2731  CB  ILE B 169     -20.081 -15.951  29.462  1.00  9.24           C  
ANISOU 2731  CB  ILE B 169     1110   1279   1122     87    -19      7       C  
ATOM   2732  CG1 ILE B 169     -19.014 -15.912  30.562  1.00  9.23           C  
ANISOU 2732  CG1 ILE B 169     1089   1280   1137     74      1      5       C  
ATOM   2733  CG2 ILE B 169     -20.897 -17.225  29.570  1.00  9.14           C  
ANISOU 2733  CG2 ILE B 169     1086   1285   1101     90    -21    -14       C  
ATOM   2734  CD1 ILE B 169     -19.565 -15.756  31.974  1.00  8.85           C  
ANISOU 2734  CD1 ILE B 169     1020   1233   1109     75     -8    -18       C  
ATOM   2735  N   VAL B 170     -21.340 -15.292  26.703  1.00  9.32           N  
ANISOU 2735  N   VAL B 170     1179   1282   1079    107    -66     39       N  
ATOM   2736  CA  VAL B 170     -22.364 -15.504  25.690  1.00  9.66           C  
ANISOU 2736  CA  VAL B 170     1236   1339   1095    119   -100     41       C  
ATOM   2737  C   VAL B 170     -21.753 -15.685  24.303  1.00  9.88           C  
ANISOU 2737  C   VAL B 170     1310   1371   1073    105    -90     63       C  
ATOM   2738  O   VAL B 170     -22.071 -16.642  23.590  1.00  9.52           O  
ANISOU 2738  O   VAL B 170     1275   1349    995     97    -93     50       O  
ATOM   2739  CB  VAL B 170     -23.358 -14.333  25.657  1.00  9.89           C  
ANISOU 2739  CB  VAL B 170     1264   1353   1141    150   -143     50       C  
ATOM   2740  CG1 VAL B 170     -24.301 -14.476  24.470  1.00 10.59           C  
ANISOU 2740  CG1 VAL B 170     1366   1463   1196    164   -187     58       C  
ATOM   2741  CG2 VAL B 170     -24.132 -14.263  26.974  1.00  9.85           C  
ANISOU 2741  CG2 VAL B 170     1210   1353   1181    167   -148     19       C  
ATOM   2742  N   GLU B 171     -20.875 -14.761  23.932  1.00 10.24           N  
ANISOU 2742  N   GLU B 171     1385   1395   1111     96    -74     95       N  
ATOM   2743  CA  GLU B 171     -20.161 -14.834  22.660  1.00 10.80           C  
ANISOU 2743  CA  GLU B 171     1501   1472   1131     77    -53    119       C  
ATOM   2744  C   GLU B 171     -19.443 -16.174  22.494  1.00 10.57           C  
ANISOU 2744  C   GLU B 171     1464   1469   1084     62    -10     95       C  
ATOM   2745  O   GLU B 171     -19.435 -16.751  21.402  1.00 10.29           O  
ANISOU 2745  O   GLU B 171     1461   1449    998     54     -2     93       O  
ATOM   2746  CB  GLU B 171     -19.162 -13.683  22.543  1.00 11.18           C  
ANISOU 2746  CB  GLU B 171     1575   1492   1181     57    -30    154       C  
ATOM   2747  CG  GLU B 171     -19.810 -12.362  22.185  1.00 12.98           C  
ANISOU 2747  CG  GLU B 171     1842   1683   1407     72    -72    187       C  
ATOM   2748  CD  GLU B 171     -18.814 -11.255  21.935  1.00 14.51           C  
ANISOU 2748  CD  GLU B 171     2075   1842   1595     41    -46    225       C  
ATOM   2749  OE1 GLU B 171     -17.676 -11.332  22.457  1.00 16.93           O  
ANISOU 2749  OE1 GLU B 171     2358   2156   1921      9      0    217       O  
ATOM   2750  OE2 GLU B 171     -19.187 -10.293  21.228  1.00 14.48           O  
ANISOU 2750  OE2 GLU B 171     2127   1805   1569     48    -75    264       O  
ATOM   2751  N   GLY B 172     -18.847 -16.653  23.585  1.00 10.30           N  
ANISOU 2751  N   GLY B 172     1389   1436   1088     62     17     76       N  
ATOM   2752  CA  GLY B 172     -18.178 -17.952  23.607  1.00 10.46           C  
ANISOU 2752  CA  GLY B 172     1400   1473   1102     60     56     53       C  
ATOM   2753  C   GLY B 172     -19.136 -19.108  23.390  1.00 10.75           C  
ANISOU 2753  C   GLY B 172     1445   1517   1121     66     39     24       C  
ATOM   2754  O   GLY B 172     -18.901 -19.964  22.540  1.00 11.01           O  
ANISOU 2754  O   GLY B 172     1507   1557   1117     61     61     10       O  
ATOM   2755  N   VAL B 173     -20.231 -19.125  24.145  1.00 10.89           N  
ANISOU 2755  N   VAL B 173     1440   1532   1165     71      4     10       N  
ATOM   2756  CA  VAL B 173     -21.223 -20.200  24.032  1.00 11.18           C  
ANISOU 2756  CA  VAL B 173     1480   1578   1189     64    -13    -20       C  
ATOM   2757  C   VAL B 173     -21.887 -20.247  22.653  1.00 12.08           C  
ANISOU 2757  C   VAL B 173     1630   1707   1253     55    -41    -21       C  
ATOM   2758  O   VAL B 173     -22.060 -21.323  22.071  1.00 11.88           O  
ANISOU 2758  O   VAL B 173     1631   1688   1197     39    -33    -47       O  
ATOM   2759  CB  VAL B 173     -22.314 -20.071  25.116  1.00 11.03           C  
ANISOU 2759  CB  VAL B 173     1420   1562   1207     66    -43    -33       C  
ATOM   2760  CG1 VAL B 173     -23.521 -20.944  24.782  1.00 10.77           C  
ANISOU 2760  CG1 VAL B 173     1387   1547   1159     48    -68    -62       C  
ATOM   2761  CG2 VAL B 173     -21.738 -20.429  26.475  1.00 10.08           C  
ANISOU 2761  CG2 VAL B 173     1275   1431   1123     68    -15    -39       C  
ATOM   2762  N   LEU B 174     -22.243 -19.080  22.128  1.00 12.77           N  
ANISOU 2762  N   LEU B 174     1726   1798   1329     64    -74      7       N  
ATOM   2763  CA  LEU B 174     -23.009 -18.998  20.888  1.00 13.86           C  
ANISOU 2763  CA  LEU B 174     1896   1955   1415     59   -115     11       C  
ATOM   2764  C   LEU B 174     -22.120 -19.033  19.645  1.00 14.93           C  
ANISOU 2764  C   LEU B 174     2089   2092   1490     45    -86     27       C  
ATOM   2765  O   LEU B 174     -22.627 -19.087  18.522  1.00 15.51           O  
ANISOU 2765  O   LEU B 174     2200   2185   1506     36   -116     29       O  
ATOM   2766  CB  LEU B 174     -23.870 -17.731  20.889  1.00 13.91           C  
ANISOU 2766  CB  LEU B 174     1888   1961   1435     83   -170     38       C  
ATOM   2767  CG  LEU B 174     -24.946 -17.675  21.977  1.00 13.77           C  
ANISOU 2767  CG  LEU B 174     1809   1953   1471     99   -199     16       C  
ATOM   2768  CD1 LEU B 174     -25.707 -16.364  21.906  1.00 12.94           C  
ANISOU 2768  CD1 LEU B 174     1693   1843   1381    136   -250     42       C  
ATOM   2769  CD2 LEU B 174     -25.903 -18.857  21.858  1.00 12.85           C  
ANISOU 2769  CD2 LEU B 174     1672   1869   1341     76   -218    -24       C  
ATOM   2770  N   ASN B 175     -20.805 -19.015  19.858  1.00 15.83           N  
ANISOU 2770  N   ASN B 175     2208   2194   1615     43    -28     35       N  
ATOM   2771  CA  ASN B 175     -19.811 -18.933  18.787  1.00 17.38           C  
ANISOU 2771  CA  ASN B 175     2449   2396   1758     30     13     50       C  
ATOM   2772  C   ASN B 175     -20.078 -17.792  17.807  1.00 19.22           C  
ANISOU 2772  C   ASN B 175     2727   2630   1945     24    -19     93       C  
ATOM   2773  O   ASN B 175     -20.072 -17.988  16.591  1.00 19.94           O  
ANISOU 2773  O   ASN B 175     2871   2739   1966      9    -17     97       O  
ATOM   2774  CB  ASN B 175     -19.687 -20.261  18.035  1.00 17.29           C  
ANISOU 2774  CB  ASN B 175     2470   2398   1700     18     41     12       C  
ATOM   2775  CG  ASN B 175     -18.359 -20.389  17.281  1.00 17.48           C  
ANISOU 2775  CG  ASN B 175     2524   2430   1687     10    109     16       C  
ATOM   2776  OD1 ASN B 175     -17.547 -19.457  17.252  1.00 16.28           O  
ANISOU 2776  OD1 ASN B 175     2368   2278   1541      5    134     50       O  
ATOM   2777  ND2 ASN B 175     -18.135 -21.546  16.674  1.00 16.68           N  
ANISOU 2777  ND2 ASN B 175     2454   2336   1549      6    143    -23       N  
ATOM   2778  N   LYS B 176     -20.309 -16.600  18.344  1.00 20.99           N  
ANISOU 2778  N   LYS B 176     2936   2833   2206     37    -48    126       N  
ATOM   2779  CA  LYS B 176     -20.480 -15.409  17.514  1.00 22.98           C  
ANISOU 2779  CA  LYS B 176     3238   3073   2421     37    -78    175       C  
ATOM   2780  C   LYS B 176     -20.136 -14.144  18.296  1.00 24.04           C  
ANISOU 2780  C   LYS B 176     3361   3167   2607     44    -77    207       C  
ATOM   2781  O   LYS B 176     -20.012 -14.176  19.522  1.00 23.49           O  
ANISOU 2781  O   LYS B 176     3239   3086   2601     53    -67    186       O  
ATOM   2782  CB  LYS B 176     -21.912 -15.333  16.969  1.00 23.48           C  
ANISOU 2782  CB  LYS B 176     3314   3150   2456     57   -156    178       C  
ATOM   2783  CG  LYS B 176     -22.992 -15.012  17.991  1.00 24.00           C  
ANISOU 2783  CG  LYS B 176     3323   3209   2588     92   -207    167       C  
ATOM   2784  CD  LYS B 176     -24.353 -14.900  17.317  1.00 25.62           C  
ANISOU 2784  CD  LYS B 176     3532   3439   2763    114   -286    172       C  
ATOM   2785  CE  LYS B 176     -25.416 -14.363  18.279  1.00 26.36           C  
ANISOU 2785  CE  LYS B 176     3565   3528   2924    157   -334    165       C  
ATOM   2786  NZ  LYS B 176     -26.666 -13.936  17.564  1.00 27.29           N  
ANISOU 2786  NZ  LYS B 176     3683   3669   3016    190   -417    182       N  
ATOM   2787  N   ASN B 177     -19.972 -13.039  17.575  1.00 25.88           N  
ANISOU 2787  N   ASN B 177     3650   3376   2806     36    -88    257       N  
ATOM   2788  CA  ASN B 177     -19.747 -11.735  18.187  1.00 27.06           C  
ANISOU 2788  CA  ASN B 177     3805   3476   2999     40    -93    289       C  
ATOM   2789  C   ASN B 177     -21.075 -10.982  18.281  1.00 28.37           C  
ANISOU 2789  C   ASN B 177     3980   3617   3183     88   -170    305       C  
ATOM   2790  O   ASN B 177     -21.818 -10.916  17.303  1.00 28.76           O  
ANISOU 2790  O   ASN B 177     4068   3678   3182    105   -218    327       O  
ATOM   2791  CB  ASN B 177     -18.724 -10.931  17.374  1.00 27.66           C  
ANISOU 2791  CB  ASN B 177     3945   3532   3031     -2    -54    337       C  
ATOM   2792  CG  ASN B 177     -17.315 -11.500  17.467  1.00 27.49           C  
ANISOU 2792  CG  ASN B 177     3898   3538   3009    -47     28    318       C  
ATOM   2793  OD1 ASN B 177     -17.025 -12.366  18.296  1.00 27.51           O  
ANISOU 2793  OD1 ASN B 177     3836   3564   3053    -40     52    274       O  
ATOM   2794  ND2 ASN B 177     -16.428 -11.010  16.610  1.00 28.01           N  
ANISOU 2794  ND2 ASN B 177     4013   3602   3026    -91     72    354       N  
ATOM   2795  N   ILE B 178     -21.372 -10.431  19.459  1.00 29.39           N  
ANISOU 2795  N   ILE B 178     4071   3715   3382    113   -182    292       N  
ATOM   2796  CA  ILE B 178     -22.654  -9.759  19.710  1.00 30.90           C  
ANISOU 2796  CA  ILE B 178     4254   3885   3602    170   -249    298       C  
ATOM   2797  C   ILE B 178     -22.653  -8.304  19.233  1.00 32.65           C  
ANISOU 2797  C   ILE B 178     4549   4043   3815    186   -275    356       C  
ATOM   2798  O   ILE B 178     -23.387  -7.955  18.301  1.00 33.77           O  
ANISOU 2798  O   ILE B 178     4733   4182   3916    217   -330    391       O  
ATOM   2799  CB  ILE B 178     -23.045  -9.805  21.206  1.00 30.44           C  
ANISOU 2799  CB  ILE B 178     4126   3821   3620    194   -247    253       C  
ATOM   2800  CG1 ILE B 178     -23.315 -11.245  21.642  1.00 30.00           C  
ANISOU 2800  CG1 ILE B 178     4005   3823   3569    184   -233    202       C  
ATOM   2801  CG2 ILE B 178     -24.277  -8.948  21.466  1.00 31.13           C  
ANISOU 2801  CG2 ILE B 178     4205   3883   3741    258   -307    258       C  
ATOM   2802  CD1 ILE B 178     -23.679 -11.377  23.106  1.00 30.06           C  
ANISOU 2802  CD1 ILE B 178     3949   3832   3642    199   -225    160       C  
ATOM   2803  N   ASN B 179     -21.839  -7.463  19.869  1.00 33.58           N  
ANISOU 2803  N   ASN B 179     4685   4106   3967    163   -239    366       N  
ATOM   2804  CA  ASN B 179     -21.755  -6.037  19.514  1.00 35.27           C  
ANISOU 2804  CA  ASN B 179     4980   4243   4177    171   -257    420       C  
ATOM   2805  C   ASN B 179     -21.631  -5.848  18.005  1.00 36.23           C  
ANISOU 2805  C   ASN B 179     5184   4365   4217    154   -271    480       C  
ATOM   2806  O   ASN B 179     -22.447  -5.159  17.390  1.00 37.38           O  
ANISOU 2806  O   ASN B 179     5381   4480   4342    202   -332    521       O  
ATOM   2807  CB  ASN B 179     -20.565  -5.389  20.235  1.00 35.36           C  
ANISOU 2807  CB  ASN B 179     5006   4209   4222    116   -199    420       C  
ATOM   2808  CG  ASN B 179     -20.470  -3.879  20.023  1.00 37.19           C  
ANISOU 2808  CG  ASN B 179     5326   4345   4458    117   -213    471       C  
ATOM   2809  OD1 ASN B 179     -21.056  -3.310  19.096  1.00 39.80           O  
ANISOU 2809  OD1 ASN B 179     5726   4644   4752    150   -259    522       O  
ATOM   2810  ND2 ASN B 179     -19.719  -3.223  20.902  1.00 37.88           N  
ANISOU 2810  ND2 ASN B 179     5418   4385   4589     78   -176    458       N  
ATOM   2811  OXT ASN B 179     -20.726  -6.397  17.370  1.00 36.64           O  
ANISOU 2811  OXT ASN B 179     5252   4452   4218     96   -222    486       O  
TER    2812      ASN B 179                                                      
ATOM   2813  N   HIS C   0      14.274 -52.830  21.362  1.00 27.17           N  
ANISOU 2813  N   HIS C   0     3142   3870   3312   -113    793   -277       N  
ATOM   2814  CA  HIS C   0      13.554 -51.657  20.787  1.00 26.94           C  
ANISOU 2814  CA  HIS C   0     3211   3835   3191   -182    763   -236       C  
ATOM   2815  C   HIS C   0      13.252 -50.623  21.871  1.00 25.35           C  
ANISOU 2815  C   HIS C   0     2987   3616   3028   -206    669   -184       C  
ATOM   2816  O   HIS C   0      13.756 -49.506  21.815  1.00 25.72           O  
ANISOU 2816  O   HIS C   0     3024   3675   3072   -266    684   -147       O  
ATOM   2817  CB  HIS C   0      12.265 -52.112  20.095  1.00 27.04           C  
ANISOU 2817  CB  HIS C   0     3344   3821   3111   -173    726   -253       C  
ATOM   2818  CG  HIS C   0      12.102 -51.569  18.712  1.00 29.35           C  
ANISOU 2818  CG  HIS C   0     3740   4126   3287   -230    775   -243       C  
ATOM   2819  ND1 HIS C   0      13.140 -51.526  17.806  1.00 32.50           N  
ANISOU 2819  ND1 HIS C   0     4134   4559   3655   -260    897   -259       N  
ATOM   2820  CD2 HIS C   0      11.020 -51.069  18.070  1.00 30.64           C  
ANISOU 2820  CD2 HIS C   0     4015   4272   3354   -262    718   -217       C  
ATOM   2821  CE1 HIS C   0      12.708 -51.013  16.668  1.00 33.93           C  
ANISOU 2821  CE1 HIS C   0     4432   4742   3717   -314    914   -243       C  
ATOM   2822  NE2 HIS C   0      11.425 -50.724  16.802  1.00 33.13           N  
ANISOU 2822  NE2 HIS C   0     4403   4610   3575   -315    800   -215       N  
ATOM   2823  N   MET C   1      12.438 -51.007  22.850  1.00 23.61           N  
ANISOU 2823  N   MET C   1     2764   3365   2841   -162    579   -185       N  
ATOM   2824  CA  MET C   1      12.086 -50.141  23.973  1.00 22.39           C  
ANISOU 2824  CA  MET C   1     2597   3189   2722   -176    494   -146       C  
ATOM   2825  C   MET C   1      12.893 -50.531  25.200  1.00 21.32           C  
ANISOU 2825  C   MET C   1     2355   3062   2686   -148    473   -152       C  
ATOM   2826  O   MET C   1      13.286 -51.682  25.341  1.00 21.00           O  
ANISOU 2826  O   MET C   1     2262   3029   2689    -97    496   -185       O  
ATOM   2827  CB  MET C   1      10.595 -50.258  24.304  1.00 21.80           C  
ANISOU 2827  CB  MET C   1     2590   3078   2615   -148    410   -141       C  
ATOM   2828  CG  MET C   1       9.694 -49.325  23.519  1.00 23.15           C  
ANISOU 2828  CG  MET C   1     2858   3234   2704   -183    387   -110       C  
ATOM   2829  SD  MET C   1       8.052 -49.179  24.268  1.00 24.96           S  
ANISOU 2829  SD  MET C   1     3128   3426   2929   -148    282    -92       S  
ATOM   2830  CE  MET C   1       7.335 -50.738  23.764  1.00 23.59           C  
ANISOU 2830  CE  MET C   1     2973   3259   2732   -110    280   -137       C  
ATOM   2831  N   LYS C   2      13.154 -49.559  26.074  1.00 20.25           N  
ANISOU 2831  N   LYS C   2     2192   2920   2583   -184    426   -118       N  
ATOM   2832  CA  LYS C   2      13.626 -49.848  27.424  1.00 19.42           C  
ANISOU 2832  CA  LYS C   2     2009   2814   2558   -161    374   -117       C  
ATOM   2833  C   LYS C   2      12.439 -49.645  28.365  1.00 17.89           C  
ANISOU 2833  C   LYS C   2     1874   2577   2347   -144    286   -106       C  
ATOM   2834  O   LYS C   2      11.814 -48.576  28.366  1.00 17.51           O  
ANISOU 2834  O   LYS C   2     1891   2504   2258   -178    259    -82       O  
ATOM   2835  CB  LYS C   2      14.792 -48.947  27.828  1.00 20.29           C  
ANISOU 2835  CB  LYS C   2     2048   2947   2714   -222    378    -92       C  
ATOM   2836  CG  LYS C   2      15.515 -49.439  29.091  1.00 20.62           C  
ANISOU 2836  CG  LYS C   2     1992   3000   2841   -197    326    -92       C  
ATOM   2837  CD  LYS C   2      16.716 -48.582  29.469  1.00 21.56           C  
ANISOU 2837  CD  LYS C   2     2032   3150   3010   -267    321    -66       C  
ATOM   2838  CE  LYS C   2      17.485 -49.224  30.629  1.00 21.63           C  
ANISOU 2838  CE  LYS C   2     1937   3177   3105   -236    263    -65       C  
ATOM   2839  NZ  LYS C   2      18.536 -48.339  31.216  1.00 22.75           N  
ANISOU 2839  NZ  LYS C   2     2004   3346   3294   -313    230    -37       N  
ATOM   2840  N   ILE C   3      12.127 -50.670  29.153  1.00 16.30           N  
ANISOU 2840  N   ILE C   3     1652   2364   2179    -89    248   -123       N  
ATOM   2841  CA  ILE C   3      10.896 -50.690  29.926  1.00 15.05           C  
ANISOU 2841  CA  ILE C   3     1550   2170   2000    -67    183   -118       C  
ATOM   2842  C   ILE C   3      11.206 -50.864  31.407  1.00 13.87           C  
ANISOU 2842  C   ILE C   3     1360   2011   1900    -56    124   -110       C  
ATOM   2843  O   ILE C   3      12.091 -51.629  31.778  1.00 13.70           O  
ANISOU 2843  O   ILE C   3     1268   2006   1932    -33    125   -118       O  
ATOM   2844  CB  ILE C   3       9.967 -51.843  29.476  1.00 14.67           C  
ANISOU 2844  CB  ILE C   3     1537   2110   1928    -21    189   -144       C  
ATOM   2845  CG1 ILE C   3       9.619 -51.720  27.992  1.00 15.86           C  
ANISOU 2845  CG1 ILE C   3     1740   2271   2017    -36    238   -153       C  
ATOM   2846  CG2 ILE C   3       8.695 -51.840  30.282  1.00 14.36           C  
ANISOU 2846  CG2 ILE C   3     1542   2041   1873     -5    130   -136       C  
ATOM   2847  CD1 ILE C   3       8.886 -52.933  27.439  1.00 15.82           C  
ANISOU 2847  CD1 ILE C   3     1768   2256   1986     -2    246   -184       C  
ATOM   2848  N   CYS C   4      10.464 -50.154  32.249  1.00 12.48           N  
ANISOU 2848  N   CYS C   4     1233   1807   1703    -69     74    -96       N  
ATOM   2849  CA  CYS C   4      10.562 -50.339  33.689  1.00 11.56           C  
ANISOU 2849  CA  CYS C   4     1103   1677   1614    -60     15    -90       C  
ATOM   2850  C   CYS C   4       9.276 -50.963  34.180  1.00 10.60           C  
ANISOU 2850  C   CYS C   4     1031   1529   1469    -21     -8    -97       C  
ATOM   2851  O   CYS C   4       8.187 -50.509  33.818  1.00 10.16           O  
ANISOU 2851  O   CYS C   4     1029   1458   1373    -20     -1    -96       O  
ATOM   2852  CB  CYS C   4      10.799 -49.009  34.393  1.00 11.77           C  
ANISOU 2852  CB  CYS C   4     1154   1688   1630   -113    -18    -72       C  
ATOM   2853  SG  CYS C   4      11.134 -49.152  36.167  1.00 11.86           S  
ANISOU 2853  SG  CYS C   4     1157   1687   1663   -118    -94    -65       S  
ATOM   2854  N   ILE C   5       9.406 -52.015  34.985  1.00 10.10           N  
ANISOU 2854  N   ILE C   5      944   1461   1433     10    -35   -101       N  
ATOM   2855  CA  ILE C   5       8.273 -52.607  35.676  1.00  9.75           C  
ANISOU 2855  CA  ILE C   5      943   1392   1368     35    -58   -103       C  
ATOM   2856  C   ILE C   5       8.482 -52.426  37.178  1.00  9.70           C  
ANISOU 2856  C   ILE C   5      949   1373   1365     24   -111    -89       C  
ATOM   2857  O   ILE C   5       9.442 -52.957  37.743  1.00  9.81           O  
ANISOU 2857  O   ILE C   5      920   1393   1414     30   -142    -81       O  
ATOM   2858  CB  ILE C   5       8.106 -54.107  35.345  1.00  9.67           C  
ANISOU 2858  CB  ILE C   5      921   1378   1376     76    -45   -118       C  
ATOM   2859  CG1 ILE C   5       7.838 -54.303  33.851  1.00  9.45           C  
ANISOU 2859  CG1 ILE C   5      898   1360   1331     81      6   -138       C  
ATOM   2860  CG2 ILE C   5       6.951 -54.711  36.148  1.00  9.04           C  
ANISOU 2860  CG2 ILE C   5      886   1273   1278     89    -68   -116       C  
ATOM   2861  CD1 ILE C   5       8.114 -55.706  33.357  1.00  8.30           C  
ANISOU 2861  CD1 ILE C   5      736   1207   1209    118     29   -161       C  
ATOM   2862  N   THR C   6       7.620 -51.631  37.812  1.00  9.23           N  
ANISOU 2862  N   THR C   6      947   1293   1268      8   -122    -86       N  
ATOM   2863  CA  THR C   6       7.595 -51.567  39.260  1.00  9.04           C  
ANISOU 2863  CA  THR C   6      956   1252   1229     -2   -166    -77       C  
ATOM   2864  C   THR C   6       6.513 -52.494  39.803  1.00  8.86           C  
ANISOU 2864  C   THR C   6      966   1214   1188     26   -163    -79       C  
ATOM   2865  O   THR C   6       5.449 -52.665  39.187  1.00  8.28           O  
ANISOU 2865  O   THR C   6      904   1139   1103     42   -128    -87       O  
ATOM   2866  CB  THR C   6       7.382 -50.128  39.803  1.00  9.36           C  
ANISOU 2866  CB  THR C   6     1051   1272   1233    -38   -174    -78       C  
ATOM   2867  OG1 THR C   6       6.177 -49.561  39.268  1.00  8.58           O  
ANISOU 2867  OG1 THR C   6      990   1159   1110    -22   -134    -85       O  
ATOM   2868  CG2 THR C   6       8.575 -49.237  39.459  1.00 10.14           C  
ANISOU 2868  CG2 THR C   6     1120   1381   1350    -82   -186    -72       C  
ATOM   2869  N   VAL C   7       6.818 -53.114  40.942  1.00  8.91           N  
ANISOU 2869  N   VAL C   7      985   1210   1191     25   -203    -67       N  
ATOM   2870  CA  VAL C   7       5.854 -53.877  41.723  1.00  8.93           C  
ANISOU 2870  CA  VAL C   7     1032   1194   1167     37   -201    -62       C  
ATOM   2871  C   VAL C   7       5.245 -52.947  42.762  1.00  8.85           C  
ANISOU 2871  C   VAL C   7     1088   1170   1106     13   -201    -64       C  
ATOM   2872  O   VAL C   7       5.963 -52.358  43.569  1.00  9.38           O  
ANISOU 2872  O   VAL C   7     1179   1230   1154    -15   -241    -59       O  
ATOM   2873  CB  VAL C   7       6.533 -55.041  42.453  1.00  9.46           C  
ANISOU 2873  CB  VAL C   7     1092   1252   1251     48   -247    -42       C  
ATOM   2874  CG1 VAL C   7       5.595 -55.662  43.492  1.00  9.67           C  
ANISOU 2874  CG1 VAL C   7     1182   1255   1236     45   -248    -31       C  
ATOM   2875  CG2 VAL C   7       7.024 -56.082  41.437  1.00  9.87           C  
ANISOU 2875  CG2 VAL C   7     1086   1307   1356     84   -236    -46       C  
ATOM   2876  N   GLY C   8       3.924 -52.819  42.751  1.00  8.38           N  
ANISOU 2876  N   GLY C   8     1057   1104   1023     23   -157    -74       N  
ATOM   2877  CA  GLY C   8       3.238 -51.975  43.722  1.00  8.34           C  
ANISOU 2877  CA  GLY C   8     1115   1081    970     10   -139    -81       C  
ATOM   2878  C   GLY C   8       3.383 -52.506  45.134  1.00  8.79           C  
ANISOU 2878  C   GLY C   8     1227   1126    988     -9   -167    -69       C  
ATOM   2879  O   GLY C   8       3.458 -53.714  45.338  1.00  8.57           O  
ANISOU 2879  O   GLY C   8     1190   1098    968     -3   -184    -52       O  
ATOM   2880  N   HIS C   9       3.435 -51.589  46.100  1.00  9.19           N  
ANISOU 2880  N   HIS C   9     1345   1159    988    -33   -172    -79       N  
ATOM   2881  CA  HIS C   9       3.442 -51.911  47.528  1.00  9.86           C  
ANISOU 2881  CA  HIS C   9     1504   1229   1013    -58   -194    -70       C  
ATOM   2882  C   HIS C   9       4.787 -52.431  48.035  1.00 10.22           C  
ANISOU 2882  C   HIS C   9     1547   1277   1060    -82   -281    -44       C  
ATOM   2883  O   HIS C   9       5.786 -52.406  47.319  1.00  9.63           O  
ANISOU 2883  O   HIS C   9     1405   1217   1037    -79   -321    -38       O  
ATOM   2884  CB  HIS C   9       2.292 -52.863  47.867  1.00  9.86           C  
ANISOU 2884  CB  HIS C   9     1519   1230    997    -45   -145    -62       C  
ATOM   2885  CG  HIS C   9       0.969 -52.366  47.391  1.00 10.36           C  
ANISOU 2885  CG  HIS C   9     1567   1299   1069    -21    -65    -83       C  
ATOM   2886  ND1 HIS C   9       0.308 -51.324  48.002  1.00 10.95           N  
ANISOU 2886  ND1 HIS C   9     1699   1360   1103    -20    -16   -107       N  
ATOM   2887  CD2 HIS C   9       0.206 -52.732  46.335  1.00 10.63           C  
ANISOU 2887  CD2 HIS C   9     1535   1352   1153      6    -30    -83       C  
ATOM   2888  CE1 HIS C   9      -0.824 -51.090  47.362  1.00 11.20           C  
ANISOU 2888  CE1 HIS C   9     1689   1403   1165     13     47   -117       C  
ATOM   2889  NE2 HIS C   9      -0.905 -51.924  46.342  1.00 10.88           N  
ANISOU 2889  NE2 HIS C   9     1572   1384   1177     25     34   -102       N  
ATOM   2890  N   SER C  10       4.813 -52.856  49.292  1.00 11.05           N  
ANISOU 2890  N   SER C  10     1724   1369   1105   -105   -312    -29       N  
ATOM   2891  CA  SER C  10       6.040 -53.325  49.910  1.00 11.91           C  
ANISOU 2891  CA  SER C  10     1836   1479   1210   -127   -408      2       C  
ATOM   2892  C   SER C  10       5.730 -54.142  51.150  1.00 12.57           C  
ANISOU 2892  C   SER C  10     2004   1545   1226   -143   -428     28       C  
ATOM   2893  O   SER C  10       4.582 -54.251  51.564  1.00 12.84           O  
ANISOU 2893  O   SER C  10     2096   1568   1213   -145   -359     19       O  
ATOM   2894  CB  SER C  10       6.943 -52.140  50.284  1.00 12.16           C  
ANISOU 2894  CB  SER C  10     1892   1510   1219   -171   -462    -10       C  
ATOM   2895  OG  SER C  10       6.411 -51.380  51.360  1.00 12.22           O  
ANISOU 2895  OG  SER C  10     2015   1493   1134   -207   -444    -31       O  
ATOM   2896  N   ILE C  11       6.770 -54.732  51.715  1.00 13.18           N  
ANISOU 2896  N   ILE C  11     2083   1621   1302   -154   -524     66       N  
ATOM   2897  CA  ILE C  11       6.698 -55.339  53.029  1.00 14.16           C  
ANISOU 2897  CA  ILE C  11     2307   1726   1347   -182   -566     98       C  
ATOM   2898  C   ILE C  11       7.531 -54.421  53.907  1.00 15.01           C  
ANISOU 2898  C   ILE C  11     2474   1836   1395   -235   -646     95       C  
ATOM   2899  O   ILE C  11       8.719 -54.259  53.664  1.00 15.47           O  
ANISOU 2899  O   ILE C  11     2465   1910   1502   -240   -730    109       O  
ATOM   2900  CB  ILE C  11       7.285 -56.761  53.029  1.00 14.38           C  
ANISOU 2900  CB  ILE C  11     2299   1745   1419   -151   -632    150       C  
ATOM   2901  CG1 ILE C  11       6.472 -57.677  52.104  1.00 14.04           C  
ANISOU 2901  CG1 ILE C  11     2206   1693   1434   -107   -556    147       C  
ATOM   2902  CG2 ILE C  11       7.306 -57.323  54.441  1.00 14.89           C  
ANISOU 2902  CG2 ILE C  11     2480   1787   1393   -185   -690    192       C  
ATOM   2903  CD1 ILE C  11       7.052 -59.080  51.951  1.00 13.47           C  
ANISOU 2903  CD1 ILE C  11     2101   1600   1417    -68   -612    191       C  
ATOM   2904  N   LEU C  12       6.901 -53.807  54.903  1.00 15.85           N  
ANISOU 2904  N   LEU C  12     2702   1924   1395   -277   -614     74       N  
ATOM   2905  CA  LEU C  12       7.579 -52.849  55.772  1.00 16.52           C  
ANISOU 2905  CA  LEU C  12     2866   2003   1407   -338   -684     62       C  
ATOM   2906  C   LEU C  12       8.486 -53.567  56.762  1.00 17.33           C  
ANISOU 2906  C   LEU C  12     3014   2106   1466   -369   -812    117       C  
ATOM   2907  O   LEU C  12       8.473 -54.796  56.852  1.00 16.97           O  
ANISOU 2907  O   LEU C  12     2952   2057   1439   -338   -836    164       O  
ATOM   2908  CB  LEU C  12       6.556 -51.995  56.536  1.00 17.03           C  
ANISOU 2908  CB  LEU C  12     3062   2043   1365   -369   -597     17       C  
ATOM   2909  CG  LEU C  12       5.506 -51.250  55.711  1.00 16.74           C  
ANISOU 2909  CG  LEU C  12     2995   2001   1365   -332   -469    -34       C  
ATOM   2910  CD1 LEU C  12       4.585 -50.452  56.628  1.00 17.72           C  
ANISOU 2910  CD1 LEU C  12     3253   2096   1382   -356   -386    -78       C  
ATOM   2911  CD2 LEU C  12       6.164 -50.346  54.686  1.00 16.35           C  
ANISOU 2911  CD2 LEU C  12     2859   1959   1394   -326   -489    -56       C  
ATOM   2912  N   LYS C  13       9.265 -52.783  57.506  1.00 18.09           N  
ANISOU 2912  N   LYS C  13     3170   2202   1501   -431   -901    112       N  
ATOM   2913  CA  LYS C  13      10.146 -53.303  58.551  1.00 19.21           C  
ANISOU 2913  CA  LYS C  13     3366   2345   1587   -470  -1040    165       C  
ATOM   2914  C   LYS C  13       9.368 -54.071  59.613  1.00 19.19           C  
ANISOU 2914  C   LYS C  13     3501   2317   1474   -482  -1018    191       C  
ATOM   2915  O   LYS C  13       9.865 -55.048  60.164  1.00 19.95           O  
ANISOU 2915  O   LYS C  13     3615   2411   1556   -480  -1113    254       O  
ATOM   2916  CB  LYS C  13      10.924 -52.162  59.209  1.00 20.22           C  
ANISOU 2916  CB  LYS C  13     3558   2475   1651   -551  -1129    143       C  
ATOM   2917  CG  LYS C  13      12.050 -52.635  60.105  1.00 22.63           C  
ANISOU 2917  CG  LYS C  13     3885   2793   1921   -593  -1300    204       C  
ATOM   2918  CD  LYS C  13      12.760 -51.478  60.785  1.00 24.53           C  
ANISOU 2918  CD  LYS C  13     4198   3034   2088   -687  -1392    179       C  
ATOM   2919  CE  LYS C  13      14.019 -51.957  61.498  1.00 26.91           C  
ANISOU 2919  CE  LYS C  13     4483   3360   2381   -725  -1584    246       C  
ATOM   2920  NZ  LYS C  13      14.970 -52.637  60.562  1.00 27.91           N  
ANISOU 2920  NZ  LYS C  13     4404   3527   2672   -663  -1647    294       N  
ATOM   2921  N   SER C  14       8.148 -53.618  59.886  1.00 18.53           N  
ANISOU 2921  N   SER C  14     3512   2215   1315   -492   -889    144       N  
ATOM   2922  CA  SER C  14       7.253 -54.285  60.826  1.00 18.75           C  
ANISOU 2922  CA  SER C  14     3667   2220   1236   -508   -836    163       C  
ATOM   2923  C   SER C  14       6.840 -55.676  60.342  1.00 18.16           C  
ANISOU 2923  C   SER C  14     3525   2144   1231   -453   -805    211       C  
ATOM   2924  O   SER C  14       6.360 -56.491  61.126  1.00 18.29           O  
ANISOU 2924  O   SER C  14     3636   2141   1170   -470   -793    248       O  
ATOM   2925  CB  SER C  14       5.994 -53.448  61.018  1.00 18.58           C  
ANISOU 2925  CB  SER C  14     3727   2185   1147   -518   -683     97       C  
ATOM   2926  OG  SER C  14       5.258 -53.373  59.805  1.00 16.90           O  
ANISOU 2926  OG  SER C  14     3395   1983   1043   -456   -572     67       O  
ATOM   2927  N   GLY C  15       7.006 -55.927  59.045  1.00 17.14           N  
ANISOU 2927  N   GLY C  15     3242   2031   1241   -392   -788    207       N  
ATOM   2928  CA  GLY C  15       6.506 -57.141  58.420  1.00 16.74           C  
ANISOU 2928  CA  GLY C  15     3127   1972   1262   -341   -742    237       C  
ATOM   2929  C   GLY C  15       5.130 -56.931  57.817  1.00 16.17           C  
ANISOU 2929  C   GLY C  15     3035   1903   1207   -322   -586    191       C  
ATOM   2930  O   GLY C  15       4.617 -57.808  57.118  1.00 15.48           O  
ANISOU 2930  O   GLY C  15     2883   1811   1186   -285   -538    204       O  
ATOM   2931  N   ALA C  16       4.531 -55.766  58.070  1.00 16.28           N  
ANISOU 2931  N   ALA C  16     3101   1922   1163   -346   -510    136       N  
ATOM   2932  CA  ALA C  16       3.242 -55.435  57.483  1.00 15.90           C  
ANISOU 2932  CA  ALA C  16     3020   1881   1140   -321   -368     92       C  
ATOM   2933  C   ALA C  16       3.404 -55.262  55.968  1.00 15.09           C  
ANISOU 2933  C   ALA C  16     2767   1797   1168   -268   -357     74       C  
ATOM   2934  O   ALA C  16       4.350 -54.619  55.506  1.00 14.79           O  
ANISOU 2934  O   ALA C  16     2679   1768   1174   -263   -421     62       O  
ATOM   2935  CB  ALA C  16       2.671 -54.168  58.120  1.00 16.23           C  
ANISOU 2935  CB  ALA C  16     3154   1916   1095   -349   -294     37       C  
ATOM   2936  N   CYS C  17       2.505 -55.878  55.206  1.00 14.74           N  
ANISOU 2936  N   CYS C  17     2656   1760   1183   -235   -279     73       N  
ATOM   2937  CA  CYS C  17       2.477 -55.719  53.755  1.00 13.93           C  
ANISOU 2937  CA  CYS C  17     2428   1676   1191   -189   -257     53       C  
ATOM   2938  C   CYS C  17       1.463 -54.640  53.422  1.00 13.46           C  
ANISOU 2938  C   CYS C  17     2358   1626   1129   -176   -155      3       C  
ATOM   2939  O   CYS C  17       0.326 -54.702  53.892  1.00 14.10           O  
ANISOU 2939  O   CYS C  17     2480   1708   1170   -184    -68     -7       O  
ATOM   2940  CB  CYS C  17       2.080 -57.031  53.090  1.00 13.85           C  
ANISOU 2940  CB  CYS C  17     2356   1663   1242   -164   -241     80       C  
ATOM   2941  SG  CYS C  17       2.094 -56.982  51.290  1.00 13.60           S  
ANISOU 2941  SG  CYS C  17     2185   1653   1331   -114   -222     56       S  
ATOM   2942  N   THR C  18       1.866 -53.655  52.620  1.00 12.47           N  
ANISOU 2942  N   THR C  18     2179   1508   1052   -157   -165    -26       N  
ATOM   2943  CA  THR C  18       1.014 -52.499  52.323  1.00 11.98           C  
ANISOU 2943  CA  THR C  18     2116   1446    990   -138    -80    -70       C  
ATOM   2944  C   THR C  18      -0.038 -52.756  51.231  1.00 11.34           C  
ANISOU 2944  C   THR C  18     1942   1385    982    -96     -8    -77       C  
ATOM   2945  O   THR C  18      -0.882 -51.891  50.964  1.00 10.76           O  
ANISOU 2945  O   THR C  18     1859   1313    917    -71     63   -107       O  
ATOM   2946  CB  THR C  18       1.859 -51.297  51.883  1.00 12.05           C  
ANISOU 2946  CB  THR C  18     2114   1445   1018   -140   -122    -94       C  
ATOM   2947  OG1 THR C  18       2.632 -51.655  50.724  1.00 11.07           O  
ANISOU 2947  OG1 THR C  18     1888   1340    979   -121   -174    -77       O  
ATOM   2948  CG2 THR C  18       2.790 -50.850  53.006  1.00 12.02           C  
ANISOU 2948  CG2 THR C  18     2208   1422    937   -192   -193    -95       C  
ATOM   2949  N   SER C  19       0.017 -53.927  50.595  1.00 10.48           N  
ANISOU 2949  N   SER C  19     1768   1289    925    -87    -31    -48       N  
ATOM   2950  CA  SER C  19      -0.888 -54.233  49.491  1.00  9.98           C  
ANISOU 2950  CA  SER C  19     1618   1247    928    -57     20    -53       C  
ATOM   2951  C   SER C  19      -2.241 -54.714  49.990  1.00 10.30           C  
ANISOU 2951  C   SER C  19     1671   1296    946    -67    101    -50       C  
ATOM   2952  O   SER C  19      -2.426 -54.986  51.181  1.00 10.72           O  
ANISOU 2952  O   SER C  19     1805   1339    931    -98    121    -40       O  
ATOM   2953  CB  SER C  19      -0.273 -55.288  48.561  1.00  9.45           C  
ANISOU 2953  CB  SER C  19     1486   1184    922    -48    -34    -31       C  
ATOM   2954  OG  SER C  19      -0.456 -56.607  49.058  1.00  9.89           O  
ANISOU 2954  OG  SER C  19     1566   1227    964    -68    -42     -1       O  
ATOM   2955  N   ALA C  20      -3.184 -54.816  49.060  1.00 10.21           N  
ANISOU 2955  N   ALA C  20     1578   1308    992    -45    146    -57       N  
ATOM   2956  CA  ALA C  20      -4.445 -55.505  49.311  1.00 10.90           C  
ANISOU 2956  CA  ALA C  20     1648   1414   1081    -61    215    -48       C  
ATOM   2957  C   ALA C  20      -4.160 -56.988  49.539  1.00 11.11           C  
ANISOU 2957  C   ALA C  20     1695   1425   1100    -98    178    -12       C  
ATOM   2958  O   ALA C  20      -3.132 -57.501  49.104  1.00 10.74           O  
ANISOU 2958  O   ALA C  20     1644   1360   1075    -94    103      1       O  
ATOM   2959  CB  ALA C  20      -5.408 -55.314  48.125  1.00 10.69           C  
ANISOU 2959  CB  ALA C  20     1517   1419   1127    -32    249    -58       C  
ATOM   2960  N   ASP C  21      -5.068 -57.657  50.236  1.00 11.95           N  
ANISOU 2960  N   ASP C  21     1825   1536   1178   -135    236      4       N  
ATOM   2961  CA  ASP C  21      -4.916 -59.069  50.577  1.00 12.61           C  
ANISOU 2961  CA  ASP C  21     1947   1595   1249   -176    208     42       C  
ATOM   2962  C   ASP C  21      -6.284 -59.747  50.569  1.00 13.19           C  
ANISOU 2962  C   ASP C  21     1983   1689   1338   -213    284     52       C  
ATOM   2963  O   ASP C  21      -7.146 -59.403  51.370  1.00 13.75           O  
ANISOU 2963  O   ASP C  21     2074   1780   1370   -233    368     48       O  
ATOM   2964  CB  ASP C  21      -4.271 -59.212  51.960  1.00 13.40           C  
ANISOU 2964  CB  ASP C  21     2166   1666   1260   -205    185     65       C  
ATOM   2965  CG  ASP C  21      -3.879 -60.640  52.278  1.00 13.78           C  
ANISOU 2965  CG  ASP C  21     2263   1676   1296   -238    135    112       C  
ATOM   2966  OD1 ASP C  21      -3.097 -61.229  51.505  1.00 12.04           O  
ANISOU 2966  OD1 ASP C  21     2010   1435   1131   -214     62    122       O  
ATOM   2967  OD2 ASP C  21      -4.347 -61.170  53.308  1.00 16.56           O  
ANISOU 2967  OD2 ASP C  21     2694   2016   1584   -286    172    140       O  
ATOM   2968  N   GLY C  22      -6.479 -60.701  49.659  1.00 13.23           N  
ANISOU 2968  N   GLY C  22     1934   1689   1401   -226    258     64       N  
ATOM   2969  CA  GLY C  22      -7.744 -61.429  49.551  1.00 13.72           C  
ANISOU 2969  CA  GLY C  22     1954   1772   1487   -274    318     75       C  
ATOM   2970  C   GLY C  22      -7.549 -62.929  49.441  1.00 14.01           C  
ANISOU 2970  C   GLY C  22     2027   1764   1533   -321    277    108       C  
ATOM   2971  O   GLY C  22      -7.001 -63.559  50.344  1.00 14.64           O  
ANISOU 2971  O   GLY C  22     2204   1801   1560   -345    255    140       O  
ATOM   2972  N   VAL C  23      -8.012 -63.510  48.337  1.00 13.96           N  
ANISOU 2972  N   VAL C  23     1951   1763   1590   -334    263    101       N  
ATOM   2973  CA  VAL C  23      -7.748 -64.922  48.046  1.00 14.19           C  
ANISOU 2973  CA  VAL C  23     2020   1738   1634   -372    218    123       C  
ATOM   2974  C   VAL C  23      -6.301 -65.103  47.571  1.00 13.65           C  
ANISOU 2974  C   VAL C  23     1985   1623   1578   -317    132    118       C  
ATOM   2975  O   VAL C  23      -5.780 -66.222  47.528  1.00 14.15           O  
ANISOU 2975  O   VAL C  23     2103   1626   1648   -328     89    138       O  
ATOM   2976  CB  VAL C  23      -8.729 -65.496  47.012  1.00 14.34           C  
ANISOU 2976  CB  VAL C  23     1963   1774   1711   -414    229    113       C  
ATOM   2977  CG1 VAL C  23     -10.142 -65.444  47.564  1.00 15.06           C  
ANISOU 2977  CG1 VAL C  23     2011   1914   1799   -474    315    125       C  
ATOM   2978  CG2 VAL C  23      -8.628 -64.748  45.680  1.00 14.12           C  
ANISOU 2978  CG2 VAL C  23     1848   1782   1733   -362    198     74       C  
ATOM   2979  N   VAL C  24      -5.664 -63.995  47.214  1.00 12.87           N  
ANISOU 2979  N   VAL C  24     1851   1552   1487   -256    112     91       N  
ATOM   2980  CA  VAL C  24      -4.230 -63.957  47.008  1.00 12.61           C  
ANISOU 2980  CA  VAL C  24     1843   1488   1460   -205     42     89       C  
ATOM   2981  C   VAL C  24      -3.724 -62.619  47.526  1.00 12.43           C  
ANISOU 2981  C   VAL C  24     1822   1495   1406   -170     42     78       C  
ATOM   2982  O   VAL C  24      -4.472 -61.638  47.581  1.00 12.27           O  
ANISOU 2982  O   VAL C  24     1767   1518   1377   -169     94     58       O  
ATOM   2983  CB  VAL C  24      -3.866 -64.117  45.523  1.00 12.13           C  
ANISOU 2983  CB  VAL C  24     1724   1426   1460   -173     10     60       C  
ATOM   2984  CG1 VAL C  24      -4.232 -62.850  44.730  1.00 11.99           C  
ANISOU 2984  CG1 VAL C  24     1627   1467   1461   -147     32     27       C  
ATOM   2985  CG2 VAL C  24      -2.393 -64.446  45.368  1.00 12.19           C  
ANISOU 2985  CG2 VAL C  24     1757   1392   1483   -125    -54     64       C  
ATOM   2986  N   ASN C  25      -2.460 -62.582  47.930  1.00 12.45           N  
ANISOU 2986  N   ASN C  25     1867   1470   1393   -142    -19     90       N  
ATOM   2987  CA  ASN C  25      -1.843 -61.333  48.333  1.00 12.02           C  
ANISOU 2987  CA  ASN C  25     1817   1438   1310   -118    -32     77       C  
ATOM   2988  C   ASN C  25      -1.359 -60.591  47.099  1.00 11.17           C  
ANISOU 2988  C   ASN C  25     1633   1355   1256    -75    -49     44       C  
ATOM   2989  O   ASN C  25      -0.669 -61.156  46.253  1.00 11.30           O  
ANISOU 2989  O   ASN C  25     1619   1356   1319    -51    -88     42       O  
ATOM   2990  CB  ASN C  25      -0.685 -61.576  49.291  1.00 12.43           C  
ANISOU 2990  CB  ASN C  25     1940   1459   1325   -115   -101    108       C  
ATOM   2991  CG  ASN C  25      -0.112 -60.296  49.837  1.00 12.55           C  
ANISOU 2991  CG  ASN C  25     1973   1494   1301   -106   -118     94       C  
ATOM   2992  OD1 ASN C  25      -0.629 -59.725  50.805  1.00 15.30           O  
ANISOU 2992  OD1 ASN C  25     2379   1851   1582   -134    -79     92       O  
ATOM   2993  ND2 ASN C  25       0.963 -59.830  49.224  1.00  9.45           N  
ANISOU 2993  ND2 ASN C  25     1535   1109    949    -73   -171     82       N  
ATOM   2994  N   GLU C  26      -1.731 -59.323  47.000  1.00 10.65           N  
ANISOU 2994  N   GLU C  26     1543   1323   1182    -65    -14     19       N  
ATOM   2995  CA  GLU C  26      -1.417 -58.522  45.821  1.00 10.02           C  
ANISOU 2995  CA  GLU C  26     1398   1265   1145    -32    -23     -8       C  
ATOM   2996  C   GLU C  26       0.090 -58.377  45.596  1.00  9.89           C  
ANISOU 2996  C   GLU C  26     1377   1236   1144     -9    -87     -6       C  
ATOM   2997  O   GLU C  26       0.565 -58.577  44.480  1.00  9.81           O  
ANISOU 2997  O   GLU C  26     1318   1230   1181     12   -103    -17       O  
ATOM   2998  CB  GLU C  26      -2.058 -57.146  45.930  1.00  9.67           C  
ANISOU 2998  CB  GLU C  26     1343   1246   1083    -23     23    -29       C  
ATOM   2999  CG  GLU C  26      -1.527 -56.149  44.925  1.00  8.92           C  
ANISOU 2999  CG  GLU C  26     1206   1164   1020      7      5    -49       C  
ATOM   3000  CD  GLU C  26      -2.104 -54.768  45.104  1.00  8.84           C  
ANISOU 3000  CD  GLU C  26     1201   1164    993     22     46    -68       C  
ATOM   3001  OE1 GLU C  26      -2.759 -54.516  46.126  1.00  8.60           O  
ANISOU 3001  OE1 GLU C  26     1213   1132    925     12     89    -70       O  
ATOM   3002  OE2 GLU C  26      -1.878 -53.918  44.226  1.00 10.03           O  
ANISOU 3002  OE2 GLU C  26     1321   1322   1169     44     38    -80       O  
ATOM   3003  N   TYR C  27       0.829 -58.008  46.642  1.00 10.12           N  
ANISOU 3003  N   TYR C  27     1457   1255   1134    -18   -121      7       N  
ATOM   3004  CA  TYR C  27       2.280 -57.838  46.531  1.00 10.32           C  
ANISOU 3004  CA  TYR C  27     1466   1276   1179     -2   -188     12       C  
ATOM   3005  C   TYR C  27       2.963 -59.136  46.083  1.00 10.62           C  
ANISOU 3005  C   TYR C  27     1479   1292   1265     20   -227     30       C  
ATOM   3006  O   TYR C  27       3.757 -59.123  45.145  1.00 10.66           O  
ANISOU 3006  O   TYR C  27     1425   1305   1320     48   -243     19       O  
ATOM   3007  CB  TYR C  27       2.884 -57.339  47.853  1.00 10.68           C  
ANISOU 3007  CB  TYR C  27     1577   1313   1168    -26   -230     27       C  
ATOM   3008  CG  TYR C  27       4.404 -57.301  47.877  1.00 10.33           C  
ANISOU 3008  CG  TYR C  27     1507   1268   1149    -17   -312     42       C  
ATOM   3009  CD1 TYR C  27       5.113 -56.204  47.380  1.00 10.26           C  
ANISOU 3009  CD1 TYR C  27     1456   1280   1161    -17   -326     22       C  
ATOM   3010  CD2 TYR C  27       5.130 -58.354  48.408  1.00 11.18           C  
ANISOU 3010  CD2 TYR C  27     1630   1355   1265     -9   -376     79       C  
ATOM   3011  CE1 TYR C  27       6.512 -56.170  47.418  1.00 10.30           C  
ANISOU 3011  CE1 TYR C  27     1423   1293   1198    -15   -399     38       C  
ATOM   3012  CE2 TYR C  27       6.517 -58.335  48.435  1.00 11.59           C  
ANISOU 3012  CE2 TYR C  27     1641   1412   1352      5   -453     96       C  
ATOM   3013  CZ  TYR C  27       7.203 -57.241  47.943  1.00 10.49           C  
ANISOU 3013  CZ  TYR C  27     1449   1302   1236     -1   -463     74       C  
ATOM   3014  OH  TYR C  27       8.580 -57.240  47.989  1.00 11.93           O  
ANISOU 3014  OH  TYR C  27     1577   1496   1459      6   -539     93       O  
ATOM   3015  N   GLN C  28       2.637 -60.247  46.741  1.00 11.08           N  
ANISOU 3015  N   GLN C  28     1585   1318   1305      9   -234     58       N  
ATOM   3016  CA  GLN C  28       3.269 -61.534  46.446  1.00 11.52           C  
ANISOU 3016  CA  GLN C  28     1634   1338   1404     35   -272     77       C  
ATOM   3017  C   GLN C  28       3.000 -61.982  45.020  1.00 11.06           C  
ANISOU 3017  C   GLN C  28     1521   1280   1401     57   -237     48       C  
ATOM   3018  O   GLN C  28       3.903 -62.492  44.346  1.00 11.34           O  
ANISOU 3018  O   GLN C  28     1521   1301   1487     96   -262     44       O  
ATOM   3019  CB  GLN C  28       2.801 -62.628  47.418  1.00 12.05           C  
ANISOU 3019  CB  GLN C  28     1779   1362   1436     11   -281    115       C  
ATOM   3020  CG  GLN C  28       3.252 -62.429  48.860  1.00 12.77           C  
ANISOU 3020  CG  GLN C  28     1942   1445   1465     -9   -331    151       C  
ATOM   3021  CD  GLN C  28       4.760 -62.454  49.027  1.00 13.02           C  
ANISOU 3021  CD  GLN C  28     1949   1470   1526     27   -420    172       C  
ATOM   3022  OE1 GLN C  28       5.478 -63.047  48.221  1.00 13.48           O  
ANISOU 3022  OE1 GLN C  28     1951   1515   1658     74   -443    171       O  
ATOM   3023  NE2 GLN C  28       5.247 -61.806  50.082  1.00 11.66           N  
ANISOU 3023  NE2 GLN C  28     1821   1310   1300      3   -470    191       N  
ATOM   3024  N   TYR C  29       1.764 -61.797  44.560  1.00 10.70           N  
ANISOU 3024  N   TYR C  29     1469   1252   1344     31   -181     28       N  
ATOM   3025  CA  TYR C  29       1.414 -62.165  43.186  1.00  9.98           C  
ANISOU 3025  CA  TYR C  29     1336   1164   1293     41   -154     -1       C  
ATOM   3026  C   TYR C  29       2.234 -61.390  42.174  1.00  9.35           C  
ANISOU 3026  C   TYR C  29     1197   1112   1242     73   -158    -26       C  
ATOM   3027  O   TYR C  29       2.783 -61.975  41.238  1.00  9.23           O  
ANISOU 3027  O   TYR C  29     1159   1083   1264     99   -159    -42       O  
ATOM   3028  CB  TYR C  29      -0.063 -61.919  42.872  1.00  9.99           C  
ANISOU 3028  CB  TYR C  29     1326   1190   1278      6   -104    -14       C  
ATOM   3029  CG  TYR C  29      -0.390 -62.351  41.463  1.00  9.84           C  
ANISOU 3029  CG  TYR C  29     1274   1174   1291      8    -91    -42       C  
ATOM   3030  CD1 TYR C  29      -0.619 -63.688  41.168  1.00 11.86           C  
ANISOU 3030  CD1 TYR C  29     1557   1387   1563     -7    -95    -42       C  
ATOM   3031  CD2 TYR C  29      -0.402 -61.443  40.418  1.00  9.96           C  
ANISOU 3031  CD2 TYR C  29     1241   1227   1316     22    -80    -67       C  
ATOM   3032  CE1 TYR C  29      -0.893 -64.103  39.877  1.00 11.88           C  
ANISOU 3032  CE1 TYR C  29     1542   1387   1584    -11    -87    -72       C  
ATOM   3033  CE2 TYR C  29      -0.668 -61.850  39.113  1.00 11.13           C  
ANISOU 3033  CE2 TYR C  29     1371   1378   1481     19    -73    -92       C  
ATOM   3034  CZ  TYR C  29      -0.911 -63.180  38.855  1.00 11.96           C  
ANISOU 3034  CZ  TYR C  29     1506   1442   1597      1    -77    -97       C  
ATOM   3035  OH  TYR C  29      -1.183 -63.598  37.573  1.00 13.78           O  
ANISOU 3035  OH  TYR C  29     1731   1671   1834     -8    -73   -127       O  
ATOM   3036  N   ASN C  30       2.273 -60.073  42.344  1.00  8.35           N  
ANISOU 3036  N   ASN C  30     1055   1021   1096     67   -152    -32       N  
ATOM   3037  CA  ASN C  30       2.958 -59.195  41.408  1.00  8.24           C  
ANISOU 3037  CA  ASN C  30      992   1035   1103     85   -149    -52       C  
ATOM   3038  C   ASN C  30       4.480 -59.278  41.517  1.00  8.75           C  
ANISOU 3038  C   ASN C  30     1031   1095   1198    111   -189    -43       C  
ATOM   3039  O   ASN C  30       5.178 -59.048  40.532  1.00  8.93           O  
ANISOU 3039  O   ASN C  30     1007   1134   1253    129   -180    -60       O  
ATOM   3040  CB  ASN C  30       2.460 -57.751  41.562  1.00  8.12           C  
ANISOU 3040  CB  ASN C  30      977   1048   1059     70   -129    -59       C  
ATOM   3041  CG  ASN C  30       0.995 -57.595  41.164  1.00  7.74           C  
ANISOU 3041  CG  ASN C  30      927   1014    999     58    -88    -69       C  
ATOM   3042  OD1 ASN C  30       0.211 -56.972  41.871  1.00  8.79           O  
ANISOU 3042  OD1 ASN C  30     1081   1154   1105     46    -66    -65       O  
ATOM   3043  ND2 ASN C  30       0.627 -58.171  40.036  1.00  7.36           N  
ANISOU 3043  ND2 ASN C  30      854    969    971     60    -77    -82       N  
ATOM   3044  N   LYS C  31       4.987 -59.601  42.707  1.00  9.36           N  
ANISOU 3044  N   LYS C  31     1138   1154   1266    109   -235    -15       N  
ATOM   3045  CA  LYS C  31       6.390 -59.996  42.880  1.00 10.22           C  
ANISOU 3045  CA  LYS C  31     1214   1254   1415    139   -285      2       C  
ATOM   3046  C   LYS C  31       6.720 -61.194  41.975  1.00 10.62           C  
ANISOU 3046  C   LYS C  31     1238   1279   1519    183   -271     -9       C  
ATOM   3047  O   LYS C  31       7.784 -61.240  41.340  1.00 10.66           O  
ANISOU 3047  O   LYS C  31     1182   1294   1573    217   -274    -17       O  
ATOM   3048  CB  LYS C  31       6.667 -60.338  44.361  1.00 10.77           C  
ANISOU 3048  CB  LYS C  31     1335   1302   1457    129   -346     42       C  
ATOM   3049  CG  LYS C  31       8.127 -60.627  44.696  1.00 11.50           C  
ANISOU 3049  CG  LYS C  31     1386   1392   1593    160   -415     67       C  
ATOM   3050  CD  LYS C  31       8.325 -60.922  46.174  1.00 11.54           C  
ANISOU 3050  CD  LYS C  31     1454   1375   1558    144   -486    112       C  
ATOM   3051  CE  LYS C  31       9.717 -61.486  46.449  1.00 12.14           C  
ANISOU 3051  CE  LYS C  31     1480   1442   1689    186   -566    146       C  
ATOM   3052  NZ  LYS C  31       9.943 -61.720  47.897  1.00 12.58           N  
ANISOU 3052  NZ  LYS C  31     1604   1479   1697    166   -649    195       N  
ATOM   3053  N   SER C  32       5.792 -62.145  41.894  1.00 10.99           N  
ANISOU 3053  N   SER C  32     1331   1291   1555    178   -249    -11       N  
ATOM   3054  CA  SER C  32       5.974 -63.330  41.045  1.00 11.67           C  
ANISOU 3054  CA  SER C  32     1414   1339   1683    213   -232    -27       C  
ATOM   3055  C   SER C  32       5.786 -63.050  39.546  1.00 11.23           C  
ANISOU 3055  C   SER C  32     1324   1306   1637    216   -179    -72       C  
ATOM   3056  O   SER C  32       6.511 -63.600  38.720  1.00 11.43           O  
ANISOU 3056  O   SER C  32     1323   1317   1702    257   -162    -93       O  
ATOM   3057  CB  SER C  32       5.047 -64.464  41.487  1.00 11.88           C  
ANISOU 3057  CB  SER C  32     1512   1312   1691    195   -232    -14       C  
ATOM   3058  OG  SER C  32       5.474 -65.006  42.726  1.00 13.94           O  
ANISOU 3058  OG  SER C  32     1812   1537   1948    204   -285     31       O  
ATOM   3059  N   LEU C  33       4.823 -62.194  39.205  1.00 10.80           N  
ANISOU 3059  N   LEU C  33     1273   1288   1544    176   -151    -86       N  
ATOM   3060  CA  LEU C  33       4.500 -61.886  37.808  1.00 10.53           C  
ANISOU 3060  CA  LEU C  33     1218   1276   1505    170   -110   -121       C  
ATOM   3061  C   LEU C  33       5.559 -61.043  37.095  1.00 10.87           C  
ANISOU 3061  C   LEU C  33     1208   1355   1567    189    -95   -134       C  
ATOM   3062  O   LEU C  33       5.824 -61.257  35.908  1.00 10.96           O  
ANISOU 3062  O   LEU C  33     1207   1371   1587    203    -60   -164       O  
ATOM   3063  CB  LEU C  33       3.160 -61.142  37.735  1.00  9.89           C  
ANISOU 3063  CB  LEU C  33     1151   1224   1383    127    -96   -122       C  
ATOM   3064  CG  LEU C  33       2.653 -60.668  36.376  1.00  8.83           C  
ANISOU 3064  CG  LEU C  33     1003   1119   1235    115    -67   -149       C  
ATOM   3065  CD1 LEU C  33       2.586 -61.818  35.377  1.00  8.44           C  
ANISOU 3065  CD1 LEU C  33      974   1040   1192    119    -52   -179       C  
ATOM   3066  CD2 LEU C  33       1.283 -60.001  36.546  1.00  6.78           C  
ANISOU 3066  CD2 LEU C  33      747    884    946     81    -65   -140       C  
ATOM   3067  N   ALA C  34       6.132 -60.075  37.812  1.00 10.81           N  
ANISOU 3067  N   ALA C  34     1175   1373   1559    183   -119   -113       N  
ATOM   3068  CA  ALA C  34       7.027 -59.078  37.219  1.00 10.92           C  
ANISOU 3068  CA  ALA C  34     1138   1425   1586    183   -105   -120       C  
ATOM   3069  C   ALA C  34       8.163 -59.676  36.387  1.00 11.45           C  
ANISOU 3069  C   ALA C  34     1158   1492   1701    222    -80   -138       C  
ATOM   3070  O   ALA C  34       8.351 -59.267  35.239  1.00 11.50           O  
ANISOU 3070  O   ALA C  34     1146   1523   1702    217    -34   -161       O  
ATOM   3071  CB  ALA C  34       7.579 -58.133  38.288  1.00 10.81           C  
ANISOU 3071  CB  ALA C  34     1110   1427   1569    164   -146    -93       C  
ATOM   3072  N   PRO C  35       8.923 -60.636  36.953  1.00 12.23           N  
ANISOU 3072  N   PRO C  35     1239   1563   1846    264   -106   -125       N  
ATOM   3073  CA  PRO C  35      10.021 -61.224  36.180  1.00 12.65           C  
ANISOU 3073  CA  PRO C  35     1237   1614   1953    313    -73   -145       C  
ATOM   3074  C   PRO C  35       9.537 -61.996  34.951  1.00 12.62           C  
ANISOU 3074  C   PRO C  35     1272   1587   1937    328    -13   -188       C  
ATOM   3075  O   PRO C  35      10.227 -62.025  33.938  1.00 12.85           O  
ANISOU 3075  O   PRO C  35     1266   1631   1985    350     42   -216       O  
ATOM   3076  CB  PRO C  35      10.700 -62.164  37.180  1.00 13.45           C  
ANISOU 3076  CB  PRO C  35     1324   1680   2106    361   -125   -116       C  
ATOM   3077  CG  PRO C  35       9.714 -62.362  38.275  1.00 13.54           C  
ANISOU 3077  CG  PRO C  35     1409   1663   2075    331   -174    -89       C  
ATOM   3078  CD  PRO C  35       8.908 -61.126  38.342  1.00 12.17           C  
ANISOU 3078  CD  PRO C  35     1256   1526   1843    270   -167    -90       C  
ATOM   3079  N   VAL C  36       8.356 -62.602  35.050  1.00 12.19           N  
ANISOU 3079  N   VAL C  36     1290   1496   1846    309    -22   -193       N  
ATOM   3080  CA  VAL C  36       7.752 -63.318  33.933  1.00 12.05           C  
ANISOU 3080  CA  VAL C  36     1321   1453   1806    307     22   -235       C  
ATOM   3081  C   VAL C  36       7.345 -62.321  32.847  1.00 11.72           C  
ANISOU 3081  C   VAL C  36     1279   1459   1715    267     58   -255       C  
ATOM   3082  O   VAL C  36       7.621 -62.536  31.658  1.00 11.53           O  
ANISOU 3082  O   VAL C  36     1264   1438   1680    276    110   -292       O  
ATOM   3083  CB  VAL C  36       6.537 -64.153  34.392  1.00 12.16           C  
ANISOU 3083  CB  VAL C  36     1407   1420   1795    281     -5   -230       C  
ATOM   3084  CG1 VAL C  36       5.903 -64.880  33.218  1.00 12.11           C  
ANISOU 3084  CG1 VAL C  36     1455   1386   1761    267     31   -275       C  
ATOM   3085  CG2 VAL C  36       6.958 -65.152  35.484  1.00 11.93           C  
ANISOU 3085  CG2 VAL C  36     1390   1334   1807    319    -43   -202       C  
ATOM   3086  N   LEU C  37       6.714 -61.221  33.259  1.00 10.71           N  
ANISOU 3086  N   LEU C  37     1148   1366   1555    225     32   -230       N  
ATOM   3087  CA  LEU C  37       6.399 -60.136  32.330  1.00 10.54           C  
ANISOU 3087  CA  LEU C  37     1126   1387   1491    191     56   -237       C  
ATOM   3088  C   LEU C  37       7.673 -59.574  31.692  1.00 10.80           C  
ANISOU 3088  C   LEU C  37     1110   1451   1543    204     98   -245       C  
ATOM   3089  O   LEU C  37       7.720 -59.357  30.481  1.00 11.10           O  
ANISOU 3089  O   LEU C  37     1163   1507   1549    192    143   -269       O  
ATOM   3090  CB  LEU C  37       5.598 -59.024  33.025  1.00  9.69           C  
ANISOU 3090  CB  LEU C  37     1022   1302   1358    156     22   -206       C  
ATOM   3091  CG  LEU C  37       5.125 -57.880  32.125  1.00  9.63           C  
ANISOU 3091  CG  LEU C  37     1024   1328   1308    126     36   -206       C  
ATOM   3092  CD1 LEU C  37       4.173 -58.386  31.048  1.00  7.90           C  
ANISOU 3092  CD1 LEU C  37      847   1105   1049    110     46   -229       C  
ATOM   3093  CD2 LEU C  37       4.468 -56.778  32.948  1.00  7.66           C  
ANISOU 3093  CD2 LEU C  37      776   1090   1046    107      6   -176       C  
ATOM   3094  N   ALA C  38       8.705 -59.350  32.503  1.00 11.17           N  
ANISOU 3094  N   ALA C  38     1099   1506   1638    224     81   -224       N  
ATOM   3095  CA  ALA C  38       9.995 -58.885  31.991  1.00 11.60           C  
ANISOU 3095  CA  ALA C  38     1088   1594   1724    233    122   -228       C  
ATOM   3096  C   ALA C  38      10.562 -59.835  30.920  1.00 12.24           C  
ANISOU 3096  C   ALA C  38     1165   1665   1822    273    190   -269       C  
ATOM   3097  O   ALA C  38      10.949 -59.400  29.847  1.00 12.22           O  
ANISOU 3097  O   ALA C  38     1154   1691   1797    259    251   -289       O  
ATOM   3098  CB  ALA C  38      10.989 -58.722  33.137  1.00 11.91           C  
ANISOU 3098  CB  ALA C  38     1059   1643   1823    249     78   -197       C  
ATOM   3099  N   ASP C  39      10.587 -61.132  31.210  1.00 12.61           N  
ANISOU 3099  N   ASP C  39     1226   1663   1901    322    183   -283       N  
ATOM   3100  CA  ASP C  39      11.129 -62.111  30.262  1.00 13.70           C  
ANISOU 3100  CA  ASP C  39     1369   1777   2058    370    252   -328       C  
ATOM   3101  C   ASP C  39      10.300 -62.172  28.977  1.00 13.46           C  
ANISOU 3101  C   ASP C  39     1421   1744   1950    335    297   -369       C  
ATOM   3102  O   ASP C  39      10.852 -62.383  27.895  1.00 14.19           O  
ANISOU 3102  O   ASP C  39     1517   1842   2031    351    374   -408       O  
ATOM   3103  CB  ASP C  39      11.218 -63.512  30.887  1.00 14.15           C  
ANISOU 3103  CB  ASP C  39     1443   1768   2165    431    228   -333       C  
ATOM   3104  CG  ASP C  39      12.351 -63.644  31.900  1.00 15.41           C  
ANISOU 3104  CG  ASP C  39     1514   1930   2411    483    193   -298       C  
ATOM   3105  OD1 ASP C  39      13.296 -62.821  31.903  1.00 16.72           O  
ANISOU 3105  OD1 ASP C  39     1591   2152   2609    480    205   -283       O  
ATOM   3106  OD2 ASP C  39      12.299 -64.595  32.699  1.00 15.71           O  
ANISOU 3106  OD2 ASP C  39     1572   1913   2483    523    147   -283       O  
ATOM   3107  N   THR C  40       8.987 -61.980  29.090  1.00 12.56           N  
ANISOU 3107  N   THR C  40     1369   1622   1780    287    250   -359       N  
ATOM   3108  CA  THR C  40       8.126 -61.985  27.913  1.00 12.47           C  
ANISOU 3108  CA  THR C  40     1434   1613   1692    247    273   -390       C  
ATOM   3109  C   THR C  40       8.459 -60.805  26.985  1.00 12.76           C  
ANISOU 3109  C   THR C  40     1458   1704   1684    213    315   -387       C  
ATOM   3110  O   THR C  40       8.537 -60.973  25.765  1.00 12.75           O  
ANISOU 3110  O   THR C  40     1503   1708   1634    203    371   -424       O  
ATOM   3111  CB  THR C  40       6.628 -61.980  28.300  1.00 11.87           C  
ANISOU 3111  CB  THR C  40     1407   1524   1577    202    207   -372       C  
ATOM   3112  OG1 THR C  40       6.361 -63.072  29.186  1.00 11.35           O  
ANISOU 3112  OG1 THR C  40     1357   1405   1550    225    174   -370       O  
ATOM   3113  CG2 THR C  40       5.748 -62.111  27.059  1.00 11.36           C  
ANISOU 3113  CG2 THR C  40     1417   1461   1437    159    217   -403       C  
ATOM   3114  N   PHE C  41       8.680 -59.629  27.569  1.00 12.67           N  
ANISOU 3114  N   PHE C  41     1396   1731   1687    193    289   -345       N  
ATOM   3115  CA  PHE C  41       9.124 -58.455  26.805  1.00 13.13           C  
ANISOU 3115  CA  PHE C  41     1441   1835   1711    158    328   -334       C  
ATOM   3116  C   PHE C  41      10.502 -58.676  26.190  1.00 14.26           C  
ANISOU 3116  C   PHE C  41     1536   1996   1884    185    414   -359       C  
ATOM   3117  O   PHE C  41      10.761 -58.258  25.055  1.00 14.89           O  
ANISOU 3117  O   PHE C  41     1642   2102   1914    158    477   -375       O  
ATOM   3118  CB  PHE C  41       9.194 -57.208  27.692  1.00 12.53           C  
ANISOU 3118  CB  PHE C  41     1323   1784   1655    132    282   -285       C  
ATOM   3119  CG  PHE C  41       7.890 -56.474  27.834  1.00 12.15           C  
ANISOU 3119  CG  PHE C  41     1325   1733   1558     96    227   -260       C  
ATOM   3120  CD1 PHE C  41       7.294 -55.865  26.732  1.00 11.76           C  
ANISOU 3120  CD1 PHE C  41     1331   1699   1439     61    238   -259       C  
ATOM   3121  CD2 PHE C  41       7.289 -56.339  29.083  1.00 11.15           C  
ANISOU 3121  CD2 PHE C  41     1188   1591   1455    100    164   -235       C  
ATOM   3122  CE1 PHE C  41       6.097 -55.171  26.863  1.00 11.03           C  
ANISOU 3122  CE1 PHE C  41     1274   1605   1312     38    184   -232       C  
ATOM   3123  CE2 PHE C  41       6.099 -55.641  29.224  1.00 11.09           C  
ANISOU 3123  CE2 PHE C  41     1218   1585   1413     76    123   -214       C  
ATOM   3124  CZ  PHE C  41       5.500 -55.057  28.110  1.00 11.39           C  
ANISOU 3124  CZ  PHE C  41     1299   1636   1392     50    131   -211       C  
ATOM   3125  N   ARG C  42      11.384 -59.323  26.948  1.00 14.93           N  
ANISOU 3125  N   ARG C  42     1551   2069   2053    238    416   -361       N  
ATOM   3126  CA  ARG C  42      12.758 -59.555  26.507  1.00 16.14           C  
ANISOU 3126  CA  ARG C  42     1632   2243   2256    275    498   -381       C  
ATOM   3127  C   ARG C  42      12.843 -60.488  25.298  1.00 17.31           C  
ANISOU 3127  C   ARG C  42     1837   2370   2371    303    585   -441       C  
ATOM   3128  O   ARG C  42      13.731 -60.332  24.448  1.00 17.79           O  
ANISOU 3128  O   ARG C  42     1866   2461   2430    308    679   -464       O  
ATOM   3129  CB  ARG C  42      13.597 -60.098  27.661  1.00 16.33           C  
ANISOU 3129  CB  ARG C  42     1565   2256   2384    334    464   -363       C  
ATOM   3130  CG  ARG C  42      13.884 -59.069  28.739  1.00 15.54           C  
ANISOU 3130  CG  ARG C  42     1400   2189   2317    300    395   -309       C  
ATOM   3131  CD  ARG C  42      14.682 -59.682  29.868  1.00 15.73           C  
ANISOU 3131  CD  ARG C  42     1342   2201   2436    356    348   -288       C  
ATOM   3132  NE  ARG C  42      14.843 -58.758  30.991  1.00 13.66           N  
ANISOU 3132  NE  ARG C  42     1036   1963   2191    316    268   -239       N  
ATOM   3133  CZ  ARG C  42      14.589 -59.041  32.268  1.00 13.21           C  
ANISOU 3133  CZ  ARG C  42      985   1880   2156    329    179   -210       C  
ATOM   3134  NH1 ARG C  42      14.164 -60.243  32.647  1.00 12.86           N  
ANISOU 3134  NH1 ARG C  42      983   1781   2124    382    155   -218       N  
ATOM   3135  NH2 ARG C  42      14.790 -58.107  33.190  1.00 12.73           N  
ANISOU 3135  NH2 ARG C  42      896   1843   2100    285    114   -171       N  
ATOM   3136  N   LYS C  43      11.919 -61.443  25.214  1.00 17.62           N  
ANISOU 3136  N   LYS C  43     1961   2355   2378    315    558   -469       N  
ATOM   3137  CA  LYS C  43      11.878 -62.380  24.085  1.00 19.05           C  
ANISOU 3137  CA  LYS C  43     2220   2504   2515    335    632   -533       C  
ATOM   3138  C   LYS C  43      11.621 -61.643  22.767  1.00 19.10           C  
ANISOU 3138  C   LYS C  43     2292   2548   2418    272    684   -548       C  
ATOM   3139  O   LYS C  43      12.018 -62.109  21.697  1.00 20.07           O  
ANISOU 3139  O   LYS C  43     2460   2665   2500    284    776   -601       O  
ATOM   3140  CB  LYS C  43      10.810 -63.461  24.314  1.00 19.33           C  
ANISOU 3140  CB  LYS C  43     2343   2470   2531    341    577   -554       C  
ATOM   3141  CG  LYS C  43      11.040 -64.758  23.533  1.00 21.62           C  
ANISOU 3141  CG  LYS C  43     2702   2702   2812    386    648   -624       C  
ATOM   3142  CD  LYS C  43      10.022 -65.839  23.916  1.00 23.51           C  
ANISOU 3142  CD  LYS C  43     3025   2866   3043    383    584   -639       C  
ATOM   3143  CE  LYS C  43      10.349 -67.186  23.273  1.00 25.62           C  
ANISOU 3143  CE  LYS C  43     3364   3057   3312    436    654   -710       C  
ATOM   3144  NZ  LYS C  43       9.267 -68.210  23.457  1.00 26.41           N  
ANISOU 3144  NZ  LYS C  43     3566   3079   3387    411    594   -729       N  
ATOM   3145  N   GLU C  44      10.967 -60.487  22.852  1.00 18.34           N  
ANISOU 3145  N   GLU C  44     2206   2487   2276    208    627   -502       N  
ATOM   3146  CA  GLU C  44      10.727 -59.643  21.682  1.00 18.54           C  
ANISOU 3146  CA  GLU C  44     2294   2549   2202    146    662   -502       C  
ATOM   3147  C   GLU C  44      11.836 -58.603  21.467  1.00 18.70           C  
ANISOU 3147  C   GLU C  44     2242   2624   2240    128    727   -476       C  
ATOM   3148  O   GLU C  44      11.750 -57.791  20.549  1.00 19.19           O  
ANISOU 3148  O   GLU C  44     2354   2716   2222     72    759   -466       O  
ATOM   3149  CB  GLU C  44       9.361 -58.962  21.796  1.00 17.79           C  
ANISOU 3149  CB  GLU C  44     2255   2456   2048     91    564   -463       C  
ATOM   3150  CG  GLU C  44       8.208 -59.929  22.089  1.00 17.97           C  
ANISOU 3150  CG  GLU C  44     2334   2433   2062     97    495   -481       C  
ATOM   3151  CD  GLU C  44       8.074 -61.014  21.040  1.00 19.26           C  
ANISOU 3151  CD  GLU C  44     2590   2564   2166     98    543   -546       C  
ATOM   3152  OE1 GLU C  44       8.148 -60.684  19.836  1.00 19.76           O  
ANISOU 3152  OE1 GLU C  44     2717   2649   2141     62    592   -565       O  
ATOM   3153  OE2 GLU C  44       7.896 -62.196  21.421  1.00 19.12           O  
ANISOU 3153  OE2 GLU C  44     2588   2493   2183    132    531   -578       O  
ATOM   3154  N   GLY C  45      12.876 -58.636  22.298  1.00 18.56           N  
ANISOU 3154  N   GLY C  45     2108   2618   2325    169    742   -463       N  
ATOM   3155  CA  GLY C  45      14.074 -57.815  22.090  1.00 19.14           C  
ANISOU 3155  CA  GLY C  45     2097   2746   2430    151    813   -445       C  
ATOM   3156  C   GLY C  45      14.176 -56.542  22.917  1.00 18.31           C  
ANISOU 3156  C   GLY C  45     1933   2669   2354    104    748   -381       C  
ATOM   3157  O   GLY C  45      15.153 -55.796  22.796  1.00 19.11           O  
ANISOU 3157  O   GLY C  45     1963   2815   2485     75    798   -361       O  
ATOM   3158  N   HIS C  46      13.176 -56.288  23.755  1.00 16.87           N  
ANISOU 3158  N   HIS C  46     1782   2460   2166     93    640   -351       N  
ATOM   3159  CA  HIS C  46      13.141 -55.083  24.572  1.00 15.96           C  
ANISOU 3159  CA  HIS C  46     1634   2361   2071     50    575   -298       C  
ATOM   3160  C   HIS C  46      13.984 -55.285  25.819  1.00 15.91           C  
ANISOU 3160  C   HIS C  46     1517   2360   2170     84    541   -282       C  
ATOM   3161  O   HIS C  46      14.189 -56.411  26.261  1.00 15.79           O  
ANISOU 3161  O   HIS C  46     1470   2323   2209    148    536   -304       O  
ATOM   3162  CB  HIS C  46      11.695 -54.737  24.932  1.00 15.09           C  
ANISOU 3162  CB  HIS C  46     1603   2221   1911     31    485   -276       C  
ATOM   3163  CG  HIS C  46      10.794 -54.680  23.741  1.00 15.03           C  
ANISOU 3163  CG  HIS C  46     1699   2208   1803      4    499   -289       C  
ATOM   3164  ND1 HIS C  46      10.784 -53.615  22.869  1.00 15.79           N  
ANISOU 3164  ND1 HIS C  46     1842   2326   1833    -52    525   -265       N  
ATOM   3165  CD2 HIS C  46       9.917 -55.582  23.242  1.00 15.20           C  
ANISOU 3165  CD2 HIS C  46     1792   2205   1779     20    488   -321       C  
ATOM   3166  CE1 HIS C  46       9.918 -53.851  21.899  1.00 15.95           C  
ANISOU 3166  CE1 HIS C  46     1956   2336   1767    -66    523   -280       C  
ATOM   3167  NE2 HIS C  46       9.383 -55.042  22.099  1.00 14.73           N  
ANISOU 3167  NE2 HIS C  46     1816   2157   1624    -26    500   -316       N  
ATOM   3168  N   LYS C  47      14.506 -54.192  26.357  1.00 15.81           N  
ANISOU 3168  N   LYS C  47     1451   2372   2183     38    516   -242       N  
ATOM   3169  CA  LYS C  47      15.264 -54.243  27.598  1.00 16.12           C  
ANISOU 3169  CA  LYS C  47     1391   2419   2313     56    465   -221       C  
ATOM   3170  C   LYS C  47      14.334 -53.879  28.740  1.00 14.83           C  
ANISOU 3170  C   LYS C  47     1275   2224   2137     45    359   -195       C  
ATOM   3171  O   LYS C  47      13.540 -52.954  28.623  1.00 14.49           O  
ANISOU 3171  O   LYS C  47     1302   2169   2034      0    335   -177       O  
ATOM   3172  CB  LYS C  47      16.469 -53.302  27.547  1.00 17.11           C  
ANISOU 3172  CB  LYS C  47     1429   2594   2479      4    498   -197       C  
ATOM   3173  CG  LYS C  47      17.688 -53.919  26.862  1.00 19.20           C  
ANISOU 3173  CG  LYS C  47     1596   2898   2799     36    598   -222       C  
ATOM   3174  CD  LYS C  47      18.936 -53.051  27.006  1.00 21.78           C  
ANISOU 3174  CD  LYS C  47     1810   3280   3186    -21    621   -192       C  
ATOM   3175  CE  LYS C  47      19.503 -53.031  28.442  1.00 22.04           C  
ANISOU 3175  CE  LYS C  47     1746   3319   3308    -12    521   -162       C  
ATOM   3176  NZ  LYS C  47      20.191 -54.299  28.849  1.00 22.15           N  
ANISOU 3176  NZ  LYS C  47     1660   3339   3416     82    521   -177       N  
ATOM   3177  N   VAL C  48      14.414 -54.627  29.835  1.00 14.44           N  
ANISOU 3177  N   VAL C  48     1189   2155   2142     91    300   -191       N  
ATOM   3178  CA  VAL C  48      13.517 -54.430  30.960  1.00 13.16           C  
ANISOU 3178  CA  VAL C  48     1077   1961   1963     85    211   -170       C  
ATOM   3179  C   VAL C  48      14.293 -54.452  32.269  1.00 13.65           C  
ANISOU 3179  C   VAL C  48     1067   2029   2090     91    145   -145       C  
ATOM   3180  O   VAL C  48      15.239 -55.238  32.428  1.00 13.65           O  
ANISOU 3180  O   VAL C  48      986   2041   2159    136    153   -148       O  
ATOM   3181  CB  VAL C  48      12.420 -55.519  30.999  1.00 12.74           C  
ANISOU 3181  CB  VAL C  48     1091   1867   1883    130    196   -191       C  
ATOM   3182  CG1 VAL C  48      11.411 -55.226  32.096  1.00 11.54           C  
ANISOU 3182  CG1 VAL C  48      990   1687   1707    116    120   -169       C  
ATOM   3183  CG2 VAL C  48      11.723 -55.624  29.652  1.00 11.56           C  
ANISOU 3183  CG2 VAL C  48     1009   1715   1670    122    253   -218       C  
ATOM   3184  N   ASP C  49      13.890 -53.565  33.182  1.00 13.16           N  
ANISOU 3184  N   ASP C  49     1040   1957   2004     48     80   -120       N  
ATOM   3185  CA  ASP C  49      14.369 -53.551  34.562  1.00 13.54           C  
ANISOU 3185  CA  ASP C  49     1053   2003   2091     45      0    -95       C  
ATOM   3186  C   ASP C  49      13.175 -53.730  35.482  1.00 12.83           C  
ANISOU 3186  C   ASP C  49     1049   1870   1954     54    -55    -90       C  
ATOM   3187  O   ASP C  49      12.193 -53.002  35.367  1.00 12.25           O  
ANISOU 3187  O   ASP C  49     1050   1781   1824     26    -50    -93       O  
ATOM   3188  CB  ASP C  49      15.041 -52.217  34.902  1.00 13.88           C  
ANISOU 3188  CB  ASP C  49     1068   2070   2137    -29    -26    -73       C  
ATOM   3189  CG  ASP C  49      16.327 -51.986  34.127  1.00 15.60           C  
ANISOU 3189  CG  ASP C  49     1184   2336   2408    -51     27    -71       C  
ATOM   3190  OD1 ASP C  49      16.947 -52.972  33.671  1.00 17.44           O  
ANISOU 3190  OD1 ASP C  49     1344   2589   2694      5     68    -84       O  
ATOM   3191  OD2 ASP C  49      16.722 -50.810  33.981  1.00 15.69           O  
ANISOU 3191  OD2 ASP C  49     1188   2364   2409   -125     32    -57       O  
ATOM   3192  N   VAL C  50      13.257 -54.692  36.395  1.00 13.01           N  
ANISOU 3192  N   VAL C  50     1062   1876   2005     95   -105    -81       N  
ATOM   3193  CA  VAL C  50      12.208 -54.893  37.382  1.00 12.78           C  
ANISOU 3193  CA  VAL C  50     1113   1810   1932     97   -152    -73       C  
ATOM   3194  C   VAL C  50      12.642 -54.192  38.664  1.00 13.18           C  
ANISOU 3194  C   VAL C  50     1166   1864   1979     56   -226    -47       C  
ATOM   3195  O   VAL C  50      13.723 -54.470  39.188  1.00 14.03           O  
ANISOU 3195  O   VAL C  50     1206   1988   2135     63   -273    -28       O  
ATOM   3196  CB  VAL C  50      11.955 -56.386  37.650  1.00 12.66           C  
ANISOU 3196  CB  VAL C  50     1108   1764   1937    156   -162    -75       C  
ATOM   3197  CG1 VAL C  50      10.956 -56.559  38.770  1.00 12.25           C  
ANISOU 3197  CG1 VAL C  50     1135   1680   1840    147   -208    -62       C  
ATOM   3198  CG2 VAL C  50      11.467 -57.078  36.377  1.00 13.04           C  
ANISOU 3198  CG2 VAL C  50     1170   1803   1981    187    -91   -108       C  
ATOM   3199  N   ILE C  51      11.805 -53.275  39.145  1.00 12.87           N  
ANISOU 3199  N   ILE C  51     1202   1807   1879     16   -238    -48       N  
ATOM   3200  CA  ILE C  51      12.051 -52.542  40.384  1.00 13.23           C  
ANISOU 3200  CA  ILE C  51     1279   1847   1902    -29   -304    -31       C  
ATOM   3201  C   ILE C  51      11.054 -53.027  41.440  1.00 13.29           C  
ANISOU 3201  C   ILE C  51     1368   1821   1861    -14   -332    -27       C  
ATOM   3202  O   ILE C  51       9.835 -52.852  41.291  1.00 12.34           O  
ANISOU 3202  O   ILE C  51     1310   1680   1698     -9   -292    -41       O  
ATOM   3203  CB  ILE C  51      11.896 -51.014  40.187  1.00 13.30           C  
ANISOU 3203  CB  ILE C  51     1326   1852   1875    -88   -289    -38       C  
ATOM   3204  CG1 ILE C  51      12.777 -50.511  39.039  1.00 14.17           C  
ANISOU 3204  CG1 ILE C  51     1365   1995   2025   -111   -249    -40       C  
ATOM   3205  CG2 ILE C  51      12.251 -50.258  41.457  1.00 13.60           C  
ANISOU 3205  CG2 ILE C  51     1403   1879   1886   -141   -359    -28       C  
ATOM   3206  CD1 ILE C  51      14.257 -50.588  39.306  1.00 16.20           C  
ANISOU 3206  CD1 ILE C  51     1525   2289   2343   -135   -291    -22       C  
ATOM   3207  N   ILE C  52      11.582 -53.661  42.482  1.00 13.85           N  
ANISOU 3207  N   ILE C  52     1434   1887   1941     -8   -399     -4       N  
ATOM   3208  CA  ILE C  52      10.796 -54.111  43.626  1.00 14.47           C  
ANISOU 3208  CA  ILE C  52     1595   1935   1967     -5   -429      6       C  
ATOM   3209  C   ILE C  52      11.388 -53.481  44.884  1.00 15.26           C  
ANISOU 3209  C   ILE C  52     1729   2035   2034    -55   -509     24       C  
ATOM   3210  O   ILE C  52      12.610 -53.475  45.062  1.00 15.74           O  
ANISOU 3210  O   ILE C  52     1724   2120   2138    -67   -569     43       O  
ATOM   3211  CB  ILE C  52      10.832 -55.655  43.785  1.00 14.90           C  
ANISOU 3211  CB  ILE C  52     1636   1973   2051     49   -446     24       C  
ATOM   3212  CG1 ILE C  52      10.400 -56.348  42.488  1.00 15.30           C  
ANISOU 3212  CG1 ILE C  52     1656   2021   2136     93   -373      2       C  
ATOM   3213  CG2 ILE C  52       9.933 -56.102  44.934  1.00 14.48           C  
ANISOU 3213  CG2 ILE C  52     1679   1888   1936     42   -466     38       C  
ATOM   3214  CD1 ILE C  52      10.294 -57.872  42.599  1.00 16.67           C  
ANISOU 3214  CD1 ILE C  52     1835   2164   2335    144   -382     15       C  
ATOM   3215  N   CYS C  53      10.526 -52.964  45.750  1.00 15.25           N  
ANISOU 3215  N   CYS C  53     1829   2008   1956    -84   -507     16       N  
ATOM   3216  CA  CYS C  53      10.969 -52.409  47.021  1.00 16.12           C  
ANISOU 3216  CA  CYS C  53     1997   2112   2016   -136   -582     28       C  
ATOM   3217  C   CYS C  53      11.640 -53.478  47.875  1.00 17.01           C  
ANISOU 3217  C   CYS C  53     2099   2227   2138   -122   -667     67       C  
ATOM   3218  O   CYS C  53      11.166 -54.616  47.928  1.00 16.83           O  
ANISOU 3218  O   CYS C  53     2087   2188   2120    -76   -653     81       O  
ATOM   3219  CB  CYS C  53       9.794 -51.807  47.791  1.00 15.96           C  
ANISOU 3219  CB  CYS C  53     2098   2059   1907   -159   -547      7       C  
ATOM   3220  SG  CYS C  53       9.110 -50.344  47.016  1.00 15.79           S  
ANISOU 3220  SG  CYS C  53     2102   2024   1872   -175   -468    -34       S  
ATOM   3221  N   PRO C  54      12.754 -53.117  48.543  1.00 18.04           N  
ANISOU 3221  N   PRO C  54     2209   2374   2271   -164   -762     88       N  
ATOM   3222  CA  PRO C  54      13.343 -54.022  49.520  1.00 18.98           C  
ANISOU 3222  CA  PRO C  54     2334   2491   2386   -155   -859    132       C  
ATOM   3223  C   PRO C  54      12.325 -54.352  50.594  1.00 19.09           C  
ANISOU 3223  C   PRO C  54     2484   2467   2301   -164   -856    138       C  
ATOM   3224  O   PRO C  54      11.507 -53.499  50.946  1.00 18.80           O  
ANISOU 3224  O   PRO C  54     2541   2413   2189   -203   -810    106       O  
ATOM   3225  CB  PRO C  54      14.503 -53.214  50.121  1.00 19.99           C  
ANISOU 3225  CB  PRO C  54     2438   2646   2513   -222   -961    146       C  
ATOM   3226  CG  PRO C  54      14.750 -52.098  49.178  1.00 19.63           C  
ANISOU 3226  CG  PRO C  54     2337   2619   2502   -255   -909    113       C  
ATOM   3227  CD  PRO C  54      13.473 -51.835  48.464  1.00 18.44           C  
ANISOU 3227  CD  PRO C  54     2239   2443   2325   -230   -789     75       C  
ATOM   3228  N   GLU C  55      12.379 -55.578  51.099  1.00 19.58           N  
ANISOU 3228  N   GLU C  55     2561   2514   2366   -127   -900    178       N  
ATOM   3229  CA  GLU C  55      11.434 -56.043  52.098  1.00 19.74           C  
ANISOU 3229  CA  GLU C  55     2709   2498   2293   -139   -892    190       C  
ATOM   3230  C   GLU C  55      12.011 -55.853  53.496  1.00 21.06           C  
ANISOU 3230  C   GLU C  55     2957   2662   2382   -193  -1005    222       C  
ATOM   3231  O   GLU C  55      13.215 -56.002  53.704  1.00 21.69           O  
ANISOU 3231  O   GLU C  55     2972   2762   2505   -195  -1114    257       O  
ATOM   3232  CB  GLU C  55      11.103 -57.515  51.862  1.00 19.60           C  
ANISOU 3232  CB  GLU C  55     2679   2455   2313    -76   -874    219       C  
ATOM   3233  CG  GLU C  55      10.399 -57.776  50.536  1.00 18.75           C  
ANISOU 3233  CG  GLU C  55     2512   2346   2265    -31   -764    184       C  
ATOM   3234  CD  GLU C  55      10.094 -59.243  50.287  1.00 18.54           C  
ANISOU 3234  CD  GLU C  55     2483   2285   2274     23   -749    208       C  
ATOM   3235  OE1 GLU C  55      10.547 -60.104  51.066  1.00 19.46           O  
ANISOU 3235  OE1 GLU C  55     2632   2378   2385     37   -826    257       O  
ATOM   3236  OE2 GLU C  55       9.399 -59.535  49.294  1.00 18.50           O  
ANISOU 3236  OE2 GLU C  55     2449   2275   2304     50   -663    180       O  
ATOM   3237  N   LYS C  56      11.140 -55.518  54.446  1.00 21.41           N  
ANISOU 3237  N   LYS C  56     3141   2682   2310   -238   -979    210       N  
ATOM   3238  CA  LYS C  56      11.524 -55.354  55.846  1.00 22.57           C  
ANISOU 3238  CA  LYS C  56     3397   2821   2357   -298  -1079    237       C  
ATOM   3239  C   LYS C  56      12.637 -54.321  56.024  1.00 23.29           C  
ANISOU 3239  C   LYS C  56     3456   2940   2454   -355  -1173    229       C  
ATOM   3240  O   LYS C  56      13.585 -54.530  56.785  1.00 23.98           O  
ANISOU 3240  O   LYS C  56     3549   3039   2525   -383  -1306    273       O  
ATOM   3241  CB  LYS C  56      11.909 -56.704  56.463  1.00 23.47           C  
ANISOU 3241  CB  LYS C  56     3526   2919   2471   -268  -1167    306       C  
ATOM   3242  CG  LYS C  56      10.866 -57.787  56.224  1.00 23.44           C  
ANISOU 3242  CG  LYS C  56     3551   2883   2470   -220  -1078    316       C  
ATOM   3243  CD  LYS C  56      10.810 -58.835  57.338  1.00 24.73           C  
ANISOU 3243  CD  LYS C  56     3821   3013   2563   -227  -1146    380       C  
ATOM   3244  CE  LYS C  56       9.602 -59.762  57.134  1.00 25.12           C  
ANISOU 3244  CE  LYS C  56     3914   3026   2603   -199  -1039    382       C  
ATOM   3245  NZ  LYS C  56       9.522 -60.902  58.099  1.00 26.03           N  
ANISOU 3245  NZ  LYS C  56     4132   3099   2658   -204  -1097    450       N  
ATOM   3246  N   GLN C  57      12.501 -53.203  55.311  1.00 22.77           N  
ANISOU 3246  N   GLN C  57     3357   2883   2411   -374  -1106    177       N  
ATOM   3247  CA  GLN C  57      13.432 -52.083  55.419  1.00 23.49           C  
ANISOU 3247  CA  GLN C  57     3428   2993   2503   -442  -1178    162       C  
ATOM   3248  C   GLN C  57      12.697 -50.793  55.759  1.00 23.17           C  
ANISOU 3248  C   GLN C  57     3512   2923   2370   -500  -1112    103       C  
ATOM   3249  O   GLN C  57      13.085 -50.086  56.690  1.00 23.66           O  
ANISOU 3249  O   GLN C  57     3667   2974   2348   -577  -1186     94       O  
ATOM   3250  CB  GLN C  57      14.212 -51.905  54.119  1.00 23.26           C  
ANISOU 3250  CB  GLN C  57     3229   3000   2607   -415  -1167    159       C  
ATOM   3251  CG  GLN C  57      15.233 -50.785  54.161  1.00 24.76           C  
ANISOU 3251  CG  GLN C  57     3385   3214   2811   -495  -1241    149       C  
ATOM   3252  CD  GLN C  57      15.940 -50.606  52.846  1.00 25.92           C  
ANISOU 3252  CD  GLN C  57     3366   3398   3084   -473  -1212    146       C  
ATOM   3253  OE1 GLN C  57      16.484 -51.559  52.284  1.00 28.15           O  
ANISOU 3253  OE1 GLN C  57     3524   3711   3461   -409  -1225    180       O  
ATOM   3254  NE2 GLN C  57      15.936 -49.384  52.338  1.00 26.37           N  
ANISOU 3254  NE2 GLN C  57     3428   3450   3140   -524  -1166    107       N  
ATOM   3255  N   PHE C  58      11.646 -50.486  54.999  1.00 21.92           N  
ANISOU 3255  N   PHE C  58     3355   2747   2226   -460   -977     62       N  
ATOM   3256  CA  PHE C  58      10.898 -49.240  55.179  1.00 21.72           C  
ANISOU 3256  CA  PHE C  58     3435   2687   2131   -495   -901      4       C  
ATOM   3257  C   PHE C  58      10.236 -49.120  56.554  1.00 22.25           C  
ANISOU 3257  C   PHE C  58     3676   2719   2058   -533   -895    -11       C  
ATOM   3258  O   PHE C  58       9.654 -50.076  57.058  1.00 21.77           O  
ANISOU 3258  O   PHE C  58     3658   2656   1958   -505   -875     13       O  
ATOM   3259  CB  PHE C  58       9.807 -49.092  54.107  1.00 20.52           C  
ANISOU 3259  CB  PHE C  58     3243   2525   2027   -432   -762    -28       C  
ATOM   3260  CG  PHE C  58      10.314 -49.083  52.681  1.00 19.52           C  
ANISOU 3260  CG  PHE C  58     2967   2427   2021   -398   -748    -22       C  
ATOM   3261  CD1 PHE C  58      11.631 -48.754  52.364  1.00 19.84           C  
ANISOU 3261  CD1 PHE C  58     2924   2495   2118   -437   -832     -6       C  
ATOM   3262  CD2 PHE C  58       9.437 -49.367  51.642  1.00 18.78           C  
ANISOU 3262  CD2 PHE C  58     2819   2336   1980   -333   -645    -33       C  
ATOM   3263  CE1 PHE C  58      12.066 -48.740  51.037  1.00 19.11           C  
ANISOU 3263  CE1 PHE C  58     2701   2430   2129   -409   -802     -2       C  
ATOM   3264  CE2 PHE C  58       9.863 -49.347  50.310  1.00 17.82           C  
ANISOU 3264  CE2 PHE C  58     2576   2239   1954   -306   -626    -30       C  
ATOM   3265  CZ  PHE C  58      11.176 -49.035  50.008  1.00 18.14           C  
ANISOU 3265  CZ  PHE C  58     2540   2306   2047   -343   -698    -15       C  
ATOM   3266  N   LYS C  59      10.312 -47.924  57.134  1.00 23.31           N  
ANISOU 3266  N   LYS C  59     3918   2824   2115   -599   -906    -53       N  
ATOM   3267  CA  LYS C  59       9.595 -47.593  58.367  1.00 24.33           C  
ANISOU 3267  CA  LYS C  59     4229   2914   2103   -636   -874    -84       C  
ATOM   3268  C   LYS C  59       8.108 -47.350  58.093  1.00 23.79           C  
ANISOU 3268  C   LYS C  59     4201   2818   2020   -578   -708   -127       C  
ATOM   3269  O   LYS C  59       7.254 -47.755  58.890  1.00 24.00           O  
ANISOU 3269  O   LYS C  59     4327   2832   1961   -571   -649   -132       O  
ATOM   3270  CB  LYS C  59      10.210 -46.359  59.040  1.00 25.52           C  
ANISOU 3270  CB  LYS C  59     4487   3033   2175   -729   -940   -121       C  
ATOM   3271  CG  LYS C  59      11.616 -46.577  59.598  1.00 27.28           C  
ANISOU 3271  CG  LYS C  59     4691   3286   2388   -802  -1118    -76       C  
ATOM   3272  CD  LYS C  59      12.004 -45.481  60.597  1.00 29.48           C  
ANISOU 3272  CD  LYS C  59     5126   3526   2548   -908  -1184   -117       C  
ATOM   3273  CE  LYS C  59      13.441 -45.633  61.084  1.00 30.72           C  
ANISOU 3273  CE  LYS C  59     5247   3720   2705   -989  -1375    -70       C  
ATOM   3274  NZ  LYS C  59      13.832 -44.584  62.076  1.00 32.44           N  
ANISOU 3274  NZ  LYS C  59     5627   3899   2799  -1106  -1452   -110       N  
ATOM   3275  N   THR C  60       7.808 -46.678  56.977  1.00 23.06           N  
ANISOU 3275  N   THR C  60     4032   2718   2010   -539   -635   -156       N  
ATOM   3276  CA  THR C  60       6.424 -46.420  56.550  1.00 22.48           C  
ANISOU 3276  CA  THR C  60     3970   2625   1948   -475   -487   -192       C  
ATOM   3277  C   THR C  60       6.287 -46.542  55.031  1.00 21.28           C  
ANISOU 3277  C   THR C  60     3664   2497   1925   -412   -445   -181       C  
ATOM   3278  O   THR C  60       7.287 -46.580  54.313  1.00 20.66           O  
ANISOU 3278  O   THR C  60     3487   2442   1920   -425   -517   -158       O  
ATOM   3279  CB  THR C  60       5.919 -45.014  56.999  1.00 23.31           C  
ANISOU 3279  CB  THR C  60     4206   2670   1981   -496   -421   -258       C  
ATOM   3280  OG1 THR C  60       6.399 -44.001  56.103  1.00 23.04           O  
ANISOU 3280  OG1 THR C  60     4123   2616   2014   -504   -434   -277       O  
ATOM   3281  CG2 THR C  60       6.368 -44.689  58.422  1.00 24.43           C  
ANISOU 3281  CG2 THR C  60     4509   2784   1988   -579   -486   -276       C  
ATOM   3282  N   LYS C  61       5.045 -46.595  54.548  1.00 20.97           N  
ANISOU 3282  N   LYS C  61     3605   2453   1911   -348   -329   -198       N  
ATOM   3283  CA  LYS C  61       4.771 -46.735  53.113  1.00 20.15           C  
ANISOU 3283  CA  LYS C  61     3369   2371   1916   -290   -288   -188       C  
ATOM   3284  C   LYS C  61       5.228 -45.519  52.294  1.00 19.66           C  
ANISOU 3284  C   LYS C  61     3285   2287   1899   -300   -294   -210       C  
ATOM   3285  O   LYS C  61       5.376 -45.611  51.077  1.00 18.83           O  
ANISOU 3285  O   LYS C  61     3073   2203   1879   -270   -288   -194       O  
ATOM   3286  CB  LYS C  61       3.279 -47.008  52.864  1.00 20.26           C  
ANISOU 3286  CB  LYS C  61     3370   2387   1941   -225   -170   -201       C  
ATOM   3287  CG  LYS C  61       2.361 -45.816  53.115  1.00 22.43           C  
ANISOU 3287  CG  LYS C  61     3727   2617   2180   -204    -79   -251       C  
ATOM   3288  CD  LYS C  61       0.911 -46.134  52.779  1.00 24.21           C  
ANISOU 3288  CD  LYS C  61     3908   2856   2436   -136     32   -256       C  
ATOM   3289  CE  LYS C  61       0.060 -44.866  52.799  1.00 25.65           C  
ANISOU 3289  CE  LYS C  61     4145   2992   2608    -97    121   -304       C  
ATOM   3290  NZ  LYS C  61      -1.388 -45.140  52.573  1.00 26.61           N  
ANISOU 3290  NZ  LYS C  61     4216   3133   2763    -30    229   -308       N  
ATOM   3291  N   ASN C  62       5.451 -44.387  52.958  1.00 20.08           N  
ANISOU 3291  N   ASN C  62     3449   2291   1888   -347   -305   -246       N  
ATOM   3292  CA  ASN C  62       5.953 -43.185  52.279  1.00 20.02           C  
ANISOU 3292  CA  ASN C  62     3439   2251   1915   -370   -318   -264       C  
ATOM   3293  C   ASN C  62       7.277 -43.431  51.555  1.00 19.17           C  
ANISOU 3293  C   ASN C  62     3222   2184   1877   -410   -409   -227       C  
ATOM   3294  O   ASN C  62       7.595 -42.738  50.593  1.00 19.04           O  
ANISOU 3294  O   ASN C  62     3159   2158   1916   -415   -402   -228       O  
ATOM   3295  CB  ASN C  62       6.125 -42.017  53.261  1.00 21.13           C  
ANISOU 3295  CB  ASN C  62     3733   2327   1967   -430   -330   -309       C  
ATOM   3296  CG  ASN C  62       4.843 -41.668  54.002  1.00 22.21           C  
ANISOU 3296  CG  ASN C  62     3986   2420   2034   -387   -225   -354       C  
ATOM   3297  OD1 ASN C  62       4.884 -41.300  55.172  1.00 26.16           O  
ANISOU 3297  OD1 ASN C  62     4622   2883   2433   -434   -234   -386       O  
ATOM   3298  ND2 ASN C  62       3.706 -41.789  53.331  1.00 22.84           N  
ANISOU 3298  ND2 ASN C  62     4008   2504   2164   -301   -126   -356       N  
ATOM   3299  N   GLU C  63       8.038 -44.419  52.016  1.00 18.67           N  
ANISOU 3299  N   GLU C  63     3117   2165   1812   -436   -490   -192       N  
ATOM   3300  CA  GLU C  63       9.333 -44.740  51.424  1.00 18.22           C  
ANISOU 3300  CA  GLU C  63     2945   2152   1827   -467   -575   -156       C  
ATOM   3301  C   GLU C  63       9.230 -45.503  50.110  1.00 17.03           C  
ANISOU 3301  C   GLU C  63     2656   2043   1773   -402   -534   -131       C  
ATOM   3302  O   GLU C  63      10.232 -45.666  49.422  1.00 16.63           O  
ANISOU 3302  O   GLU C  63     2502   2027   1790   -418   -579   -107       O  
ATOM   3303  CB  GLU C  63      10.194 -45.528  52.414  1.00 18.81           C  
ANISOU 3303  CB  GLU C  63     3022   2256   1870   -508   -683   -125       C  
ATOM   3304  CG  GLU C  63      10.682 -44.693  53.579  1.00 19.79           C  
ANISOU 3304  CG  GLU C  63     3269   2346   1902   -597   -755   -146       C  
ATOM   3305  CD  GLU C  63      11.343 -45.529  54.642  1.00 19.70           C  
ANISOU 3305  CD  GLU C  63     3277   2361   1845   -631   -865   -111       C  
ATOM   3306  OE1 GLU C  63      12.423 -46.098  54.378  1.00 19.93           O  
ANISOU 3306  OE1 GLU C  63     3191   2438   1943   -643   -955    -67       O  
ATOM   3307  OE2 GLU C  63      10.773 -45.625  55.741  1.00 21.16           O  
ANISOU 3307  OE2 GLU C  63     3594   2520   1925   -644   -859   -124       O  
ATOM   3308  N   GLU C  64       8.031 -45.977  49.766  1.00 16.33           N  
ANISOU 3308  N   GLU C  64     2565   1952   1689   -332   -449   -137       N  
ATOM   3309  CA  GLU C  64       7.802 -46.594  48.458  1.00 15.31           C  
ANISOU 3309  CA  GLU C  64     2323   1854   1640   -275   -405   -121       C  
ATOM   3310  C   GLU C  64       8.052 -45.570  47.345  1.00 15.17           C  
ANISOU 3310  C   GLU C  64     2271   1827   1666   -285   -380   -130       C  
ATOM   3311  O   GLU C  64       8.767 -45.854  46.381  1.00 14.70           O  
ANISOU 3311  O   GLU C  64     2113   1801   1671   -284   -394   -110       O  
ATOM   3312  CB  GLU C  64       6.378 -47.167  48.365  1.00 14.64           C  
ANISOU 3312  CB  GLU C  64     2251   1766   1545   -211   -323   -128       C  
ATOM   3313  CG  GLU C  64       6.112 -48.294  49.373  1.00 14.44           C  
ANISOU 3313  CG  GLU C  64     2258   1751   1479   -206   -341   -111       C  
ATOM   3314  CD  GLU C  64       4.698 -48.858  49.314  1.00 13.27           C  
ANISOU 3314  CD  GLU C  64     2116   1602   1323   -156   -256   -117       C  
ATOM   3315  OE1 GLU C  64       3.858 -48.351  48.544  1.00 12.71           O  
ANISOU 3315  OE1 GLU C  64     2024   1526   1279   -120   -189   -134       O  
ATOM   3316  OE2 GLU C  64       4.426 -49.821  50.053  1.00 14.24           O  
ANISOU 3316  OE2 GLU C  64     2266   1731   1414   -155   -262   -100       O  
ATOM   3317  N   LYS C  65       7.476 -44.378  47.495  1.00 15.46           N  
ANISOU 3317  N   LYS C  65     2396   1812   1665   -294   -341   -160       N  
ATOM   3318  CA  LYS C  65       7.669 -43.288  46.526  1.00 15.39           C  
ANISOU 3318  CA  LYS C  65     2380   1780   1688   -308   -319   -166       C  
ATOM   3319  C   LYS C  65       9.136 -42.875  46.434  1.00 15.98           C  
ANISOU 3319  C   LYS C  65     2420   1868   1785   -389   -392   -152       C  
ATOM   3320  O   LYS C  65       9.699 -42.798  45.343  1.00 16.05           O  
ANISOU 3320  O   LYS C  65     2346   1901   1850   -397   -387   -134       O  
ATOM   3321  CB  LYS C  65       6.816 -42.070  46.904  1.00 15.76           C  
ANISOU 3321  CB  LYS C  65     2546   1756   1688   -301   -271   -201       C  
ATOM   3322  CG  LYS C  65       6.996 -40.859  45.982  1.00 15.77           C  
ANISOU 3322  CG  LYS C  65     2560   1716   1714   -319   -253   -203       C  
ATOM   3323  CD  LYS C  65       6.018 -39.736  46.306  1.00 16.01           C  
ANISOU 3323  CD  LYS C  65     2709   1668   1708   -289   -198   -236       C  
ATOM   3324  CE  LYS C  65       6.306 -38.486  45.474  1.00 16.21           C  
ANISOU 3324  CE  LYS C  65     2766   1639   1755   -315   -192   -233       C  
ATOM   3325  NZ  LYS C  65       5.461 -37.311  45.856  1.00 16.23           N  
ANISOU 3325  NZ  LYS C  65     2895   1549   1723   -285   -143   -268       N  
ATOM   3326  N   SER C  66       9.748 -42.628  47.589  1.00 16.79           N  
ANISOU 3326  N   SER C  66     2585   1956   1839   -452   -459   -161       N  
ATOM   3327  CA  SER C  66      11.137 -42.179  47.661  1.00 17.57           C  
ANISOU 3327  CA  SER C  66     2651   2068   1957   -542   -539   -149       C  
ATOM   3328  C   SER C  66      12.099 -43.188  47.063  1.00 17.11           C  
ANISOU 3328  C   SER C  66     2442   2085   1975   -536   -578   -110       C  
ATOM   3329  O   SER C  66      13.130 -42.806  46.501  1.00 17.36           O  
ANISOU 3329  O   SER C  66     2400   2139   2055   -590   -606    -95       O  
ATOM   3330  CB  SER C  66      11.524 -41.914  49.113  1.00 18.52           C  
ANISOU 3330  CB  SER C  66     2869   2165   2002   -609   -616   -163       C  
ATOM   3331  OG  SER C  66      10.612 -41.009  49.696  1.00 20.56           O  
ANISOU 3331  OG  SER C  66     3276   2350   2186   -607   -568   -206       O  
ATOM   3332  N   TYR C  67      11.764 -44.471  47.185  1.00 16.36           N  
ANISOU 3332  N   TYR C  67     2300   2023   1891   -471   -573    -94       N  
ATOM   3333  CA  TYR C  67      12.599 -45.535  46.637  1.00 16.13           C  
ANISOU 3333  CA  TYR C  67     2134   2056   1938   -448   -601    -61       C  
ATOM   3334  C   TYR C  67      12.450 -45.669  45.118  1.00 15.04           C  
ANISOU 3334  C   TYR C  67     1912   1939   1862   -404   -524    -57       C  
ATOM   3335  O   TYR C  67      13.445 -45.769  44.408  1.00 15.45           O  
ANISOU 3335  O   TYR C  67     1860   2031   1977   -423   -535    -40       O  
ATOM   3336  CB  TYR C  67      12.297 -46.881  47.316  1.00 15.99           C  
ANISOU 3336  CB  TYR C  67     2112   2055   1908   -394   -626    -44       C  
ATOM   3337  CG  TYR C  67      13.112 -48.026  46.753  1.00 16.18           C  
ANISOU 3337  CG  TYR C  67     2002   2131   2014   -356   -650    -13       C  
ATOM   3338  CD1 TYR C  67      14.439 -48.215  47.128  1.00 18.17           C  
ANISOU 3338  CD1 TYR C  67     2177   2419   2306   -395   -742     15       C  
ATOM   3339  CD2 TYR C  67      12.562 -48.910  45.830  1.00 15.88           C  
ANISOU 3339  CD2 TYR C  67     1911   2105   2016   -282   -581    -11       C  
ATOM   3340  CE1 TYR C  67      15.191 -49.263  46.599  1.00 17.58           C  
ANISOU 3340  CE1 TYR C  67     1975   2389   2317   -347   -756     43       C  
ATOM   3341  CE2 TYR C  67      13.302 -49.946  45.296  1.00 15.07           C  
ANISOU 3341  CE2 TYR C  67     1697   2040   1988   -241   -594     11       C  
ATOM   3342  CZ  TYR C  67      14.614 -50.119  45.677  1.00 17.20           C  
ANISOU 3342  CZ  TYR C  67     1889   2344   2304   -268   -677     38       C  
ATOM   3343  OH  TYR C  67      15.342 -51.160  45.143  1.00 17.51           O  
ANISOU 3343  OH  TYR C  67     1812   2417   2425   -215   -682     58       O  
ATOM   3344  N   LYS C  68      11.215 -45.679  44.627  1.00 13.91           N  
ANISOU 3344  N   LYS C  68     1813   1772   1700   -348   -447    -73       N  
ATOM   3345  CA  LYS C  68      10.955 -45.955  43.207  1.00 13.07           C  
ANISOU 3345  CA  LYS C  68     1640   1687   1641   -303   -381    -69       C  
ATOM   3346  C   LYS C  68      11.223 -44.771  42.260  1.00 13.12           C  
ANISOU 3346  C   LYS C  68     1648   1678   1659   -344   -348    -71       C  
ATOM   3347  O   LYS C  68      11.853 -44.932  41.210  1.00 12.96           O  
ANISOU 3347  O   LYS C  68     1545   1694   1686   -348   -325    -58       O  
ATOM   3348  CB  LYS C  68       9.509 -46.425  43.019  1.00 12.18           C  
ANISOU 3348  CB  LYS C  68     1566   1557   1504   -233   -322    -80       C  
ATOM   3349  CG  LYS C  68       9.172 -47.743  43.711  1.00 11.25           C  
ANISOU 3349  CG  LYS C  68     1441   1454   1381   -193   -339    -73       C  
ATOM   3350  CD  LYS C  68       7.749 -48.190  43.407  1.00  9.26           C  
ANISOU 3350  CD  LYS C  68     1213   1191   1113   -135   -277    -83       C  
ATOM   3351  CE  LYS C  68       6.711 -47.227  43.968  1.00  8.63           C  
ANISOU 3351  CE  LYS C  68     1229   1070    981   -136   -245   -104       C  
ATOM   3352  NZ  LYS C  68       5.349 -47.831  44.052  1.00  8.55           N  
ANISOU 3352  NZ  LYS C  68     1235   1057    958    -85   -195   -109       N  
ATOM   3353  N   ILE C  69      10.729 -43.593  42.617  1.00 13.06           N  
ANISOU 3353  N   ILE C  69     1741   1615   1605   -372   -341    -87       N  
ATOM   3354  CA  ILE C  69      10.769 -42.438  41.704  1.00 13.31           C  
ANISOU 3354  CA  ILE C  69     1798   1617   1642   -404   -305    -85       C  
ATOM   3355  C   ILE C  69      12.171 -42.106  41.166  1.00 13.93           C  
ANISOU 3355  C   ILE C  69     1803   1727   1763   -479   -328    -66       C  
ATOM   3356  O   ILE C  69      12.333 -41.948  39.954  1.00 13.54           O  
ANISOU 3356  O   ILE C  69     1710   1693   1739   -480   -281    -53       O  
ATOM   3357  CB  ILE C  69      10.095 -41.191  42.339  1.00 13.34           C  
ANISOU 3357  CB  ILE C  69     1935   1542   1591   -421   -300   -108       C  
ATOM   3358  CG1 ILE C  69       8.580 -41.405  42.413  1.00 12.76           C  
ANISOU 3358  CG1 ILE C  69     1912   1444   1493   -334   -248   -123       C  
ATOM   3359  CG2 ILE C  69      10.423 -39.925  41.560  1.00 14.00           C  
ANISOU 3359  CG2 ILE C  69     2054   1584   1680   -473   -282   -101       C  
ATOM   3360  CD1 ILE C  69       7.912 -41.666  41.064  1.00 12.65           C  
ANISOU 3360  CD1 ILE C  69     1851   1449   1508   -276   -194   -107       C  
ATOM   3361  N   PRO C  70      13.185 -42.019  42.045  1.00 14.75           N  
ANISOU 3361  N   PRO C  70     1887   1845   1873   -546   -399    -63       N  
ATOM   3362  CA  PRO C  70      14.532 -41.760  41.519  1.00 15.71           C  
ANISOU 3362  CA  PRO C  70     1916   2007   2046   -620   -417    -43       C  
ATOM   3363  C   PRO C  70      15.065 -42.872  40.608  1.00 15.74           C  
ANISOU 3363  C   PRO C  70     1781   2085   2116   -576   -385    -24       C  
ATOM   3364  O   PRO C  70      15.825 -42.591  39.691  1.00 16.06           O  
ANISOU 3364  O   PRO C  70     1751   2155   2196   -616   -353     -9       O  
ATOM   3365  CB  PRO C  70      15.393 -41.627  42.784  1.00 16.62           C  
ANISOU 3365  CB  PRO C  70     2032   2129   2155   -692   -515    -42       C  
ATOM   3366  CG  PRO C  70      14.414 -41.327  43.892  1.00 16.53           C  
ANISOU 3366  CG  PRO C  70     2161   2054   2065   -675   -534    -70       C  
ATOM   3367  CD  PRO C  70      13.180 -42.091  43.516  1.00 15.35           C  
ANISOU 3367  CD  PRO C  70     2024   1902   1905   -566   -467    -77       C  
ATOM   3368  N   ARG C  71      14.665 -44.115  40.859  1.00 15.82           N  
ANISOU 3368  N   ARG C  71     1759   2119   2134   -496   -388    -26       N  
ATOM   3369  CA  ARG C  71      15.089 -45.245  40.033  1.00 16.27           C  
ANISOU 3369  CA  ARG C  71     1699   2233   2249   -443   -353    -16       C  
ATOM   3370  C   ARG C  71      14.357 -45.253  38.690  1.00 15.92           C  
ANISOU 3370  C   ARG C  71     1669   2183   2196   -401   -263    -22       C  
ATOM   3371  O   ARG C  71      14.975 -45.443  37.646  1.00 16.75           O  
ANISOU 3371  O   ARG C  71     1698   2327   2340   -404   -214    -15       O  
ATOM   3372  CB  ARG C  71      14.897 -46.565  40.786  1.00 16.26           C  
ANISOU 3372  CB  ARG C  71     1674   2245   2257   -375   -391    -14       C  
ATOM   3373  CG  ARG C  71      15.877 -46.709  41.939  1.00 17.96           C  
ANISOU 3373  CG  ARG C  71     1851   2481   2493   -416   -489      2       C  
ATOM   3374  CD  ARG C  71      15.600 -47.916  42.831  1.00 18.89           C  
ANISOU 3374  CD  ARG C  71     1974   2599   2605   -355   -537     10       C  
ATOM   3375  NE  ARG C  71      16.725 -48.150  43.737  1.00 20.66           N  
ANISOU 3375  NE  ARG C  71     2136   2853   2860   -389   -638     35       N  
ATOM   3376  CZ  ARG C  71      17.027 -47.393  44.791  1.00 22.53           C  
ANISOU 3376  CZ  ARG C  71     2432   3075   3055   -465   -719     38       C  
ATOM   3377  NH1 ARG C  71      16.283 -46.337  45.120  1.00 22.55           N  
ANISOU 3377  NH1 ARG C  71     2562   3025   2980   -510   -704     13       N  
ATOM   3378  NH2 ARG C  71      18.084 -47.700  45.536  1.00 24.72           N  
ANISOU 3378  NH2 ARG C  71     2641   3387   3366   -494   -821     67       N  
ATOM   3379  N   VAL C  72      13.049 -45.028  38.709  1.00 15.35           N  
ANISOU 3379  N   VAL C  72     1695   2065   2072   -363   -240    -35       N  
ATOM   3380  CA  VAL C  72      12.302 -44.838  37.467  1.00 14.98           C  
ANISOU 3380  CA  VAL C  72     1674   2009   2008   -334   -170    -37       C  
ATOM   3381  C   VAL C  72      12.905 -43.700  36.634  1.00 15.69           C  
ANISOU 3381  C   VAL C  72     1770   2093   2099   -403   -142    -23       C  
ATOM   3382  O   VAL C  72      13.132 -43.840  35.430  1.00 16.16           O  
ANISOU 3382  O   VAL C  72     1791   2180   2169   -401    -86    -15       O  
ATOM   3383  CB  VAL C  72      10.822 -44.515  37.742  1.00 14.49           C  
ANISOU 3383  CB  VAL C  72     1714   1897   1896   -291   -162    -48       C  
ATOM   3384  CG1 VAL C  72      10.117 -44.115  36.451  1.00 14.91           C  
ANISOU 3384  CG1 VAL C  72     1797   1938   1932   -271   -107    -42       C  
ATOM   3385  CG2 VAL C  72      10.129 -45.705  38.385  1.00 12.91           C  
ANISOU 3385  CG2 VAL C  72     1507   1705   1693   -227   -174    -59       C  
ATOM   3386  N   ASN C  73      13.184 -42.581  37.286  1.00 15.76           N  
ANISOU 3386  N   ASN C  73     1835   2063   2092   -470   -178    -20       N  
ATOM   3387  CA  ASN C  73      13.620 -41.383  36.587  1.00 16.32           C  
ANISOU 3387  CA  ASN C  73     1935   2110   2155   -544   -153     -4       C  
ATOM   3388  C   ASN C  73      15.116 -41.326  36.229  1.00 17.37           C  
ANISOU 3388  C   ASN C  73     1964   2297   2339   -621   -150     12       C  
ATOM   3389  O   ASN C  73      15.560 -40.350  35.634  1.00 18.35           O  
ANISOU 3389  O   ASN C  73     2109   2404   2458   -695   -126     29       O  
ATOM   3390  CB  ASN C  73      13.202 -40.157  37.401  1.00 16.33           C  
ANISOU 3390  CB  ASN C  73     2056   2032   2115   -584   -189    -12       C  
ATOM   3391  CG  ASN C  73      11.696 -39.963  37.415  1.00 15.16           C  
ANISOU 3391  CG  ASN C  73     2006   1829   1924   -507   -167    -24       C  
ATOM   3392  OD1 ASN C  73      10.992 -40.461  36.538  1.00 14.10           O  
ANISOU 3392  OD1 ASN C  73     1858   1713   1788   -444   -125    -18       O  
ATOM   3393  ND2 ASN C  73      11.198 -39.229  38.398  1.00 13.24           N  
ANISOU 3393  ND2 ASN C  73     1863   1522   1648   -513   -195    -42       N  
ATOM   3394  N   SER C  74      15.883 -42.359  36.569  1.00 17.83           N  
ANISOU 3394  N   SER C  74     1909   2417   2448   -604   -173     11       N  
ATOM   3395  CA  SER C  74      17.316 -42.411  36.232  1.00 19.09           C  
ANISOU 3395  CA  SER C  74     1944   2639   2670   -666   -166     28       C  
ATOM   3396  C   SER C  74      17.665 -43.444  35.148  1.00 19.26           C  
ANISOU 3396  C   SER C  74     1862   2722   2732   -611    -91     28       C  
ATOM   3397  O   SER C  74      18.795 -43.471  34.654  1.00 20.23           O  
ANISOU 3397  O   SER C  74     1878   2901   2909   -655    -60     41       O  
ATOM   3398  CB  SER C  74      18.141 -42.701  37.489  1.00 19.54           C  
ANISOU 3398  CB  SER C  74     1936   2722   2767   -696   -257     31       C  
ATOM   3399  OG  SER C  74      17.903 -44.015  37.962  1.00 19.15           O  
ANISOU 3399  OG  SER C  74     1844   2697   2736   -604   -281     23       O  
ATOM   3400  N   GLY C  75      16.700 -44.278  34.771  1.00 18.47           N  
ANISOU 3400  N   GLY C  75     1797   2615   2607   -518    -59     12       N  
ATOM   3401  CA  GLY C  75      16.954 -45.393  33.857  1.00 18.53           C  
ANISOU 3401  CA  GLY C  75     1723   2670   2646   -458      7      4       C  
ATOM   3402  C   GLY C  75      16.804 -45.078  32.382  1.00 18.55           C  
ANISOU 3402  C   GLY C  75     1752   2680   2616   -471     99      6       C  
ATOM   3403  O   GLY C  75      17.184 -45.886  31.542  1.00 18.92           O  
ANISOU 3403  O   GLY C  75     1734   2769   2685   -435    165     -5       O  
ATOM   3404  N   GLY C  76      16.243 -43.915  32.062  1.00 18.42           N  
ANISOU 3404  N   GLY C  76     1839   2617   2543   -519    105     19       N  
ATOM   3405  CA  GLY C  76      16.007 -43.526  30.674  1.00 18.38           C  
ANISOU 3405  CA  GLY C  76     1881   2610   2492   -536    183     29       C  
ATOM   3406  C   GLY C  76      15.028 -44.453  29.981  1.00 17.50           C  
ANISOU 3406  C   GLY C  76     1806   2500   2344   -451    214     10       C  
ATOM   3407  O   GLY C  76      15.295 -44.940  28.886  1.00 17.54           O  
ANISOU 3407  O   GLY C  76     1786   2540   2340   -441    287      3       O  
ATOM   3408  N   TYR C  77      13.891 -44.696  30.624  1.00 16.28           N  
ANISOU 3408  N   TYR C  77     1712   2306   2167   -394    161      0       N  
ATOM   3409  CA  TYR C  77      12.920 -45.659  30.117  1.00 15.40           C  
ANISOU 3409  CA  TYR C  77     1628   2196   2028   -318    177    -19       C  
ATOM   3410  C   TYR C  77      11.982 -45.024  29.105  1.00 15.16           C  
ANISOU 3410  C   TYR C  77     1695   2137   1928   -322    198     -4       C  
ATOM   3411  O   TYR C  77      11.737 -43.826  29.140  1.00 15.06           O  
ANISOU 3411  O   TYR C  77     1749   2084   1889   -363    181     20       O  
ATOM   3412  CB  TYR C  77      12.104 -46.255  31.265  1.00 14.73           C  
ANISOU 3412  CB  TYR C  77     1557   2088   1954   -261    114    -34       C  
ATOM   3413  CG  TYR C  77      12.940 -46.973  32.292  1.00 14.06           C  
ANISOU 3413  CG  TYR C  77     1387   2025   1928   -250     81    -43       C  
ATOM   3414  CD1 TYR C  77      13.526 -48.201  32.006  1.00 13.82           C  
ANISOU 3414  CD1 TYR C  77     1277   2034   1940   -208    110    -59       C  
ATOM   3415  CD2 TYR C  77      13.144 -46.427  33.550  1.00 14.15           C  
ANISOU 3415  CD2 TYR C  77     1405   2016   1953   -279     17    -34       C  
ATOM   3416  CE1 TYR C  77      14.301 -48.866  32.949  1.00 13.36           C  
ANISOU 3416  CE1 TYR C  77     1140   1993   1941   -191     70    -60       C  
ATOM   3417  CE2 TYR C  77      13.905 -47.086  34.505  1.00 14.67           C  
ANISOU 3417  CE2 TYR C  77     1399   2105   2070   -271    -28    -36       C  
ATOM   3418  CZ  TYR C  77      14.486 -48.300  34.200  1.00 13.93           C  
ANISOU 3418  CZ  TYR C  77     1218   2050   2024   -224     -4    -46       C  
ATOM   3419  OH  TYR C  77      15.250 -48.934  35.156  1.00 14.76           O  
ANISOU 3419  OH  TYR C  77     1250   2174   2182   -210    -57    -40       O  
ATOM   3420  N   ASP C  78      11.458 -45.848  28.206  1.00 15.00           N  
ANISOU 3420  N   ASP C  78     1688   2134   1878   -280    231    -19       N  
ATOM   3421  CA  ASP C  78      10.437 -45.423  27.254  1.00 14.70           C  
ANISOU 3421  CA  ASP C  78     1741   2074   1771   -276    234     -4       C  
ATOM   3422  C   ASP C  78       9.047 -45.681  27.809  1.00 13.61           C  
ANISOU 3422  C   ASP C  78     1642   1906   1624   -217    176     -9       C  
ATOM   3423  O   ASP C  78       8.069 -45.110  27.331  1.00 13.84           O  
ANISOU 3423  O   ASP C  78     1742   1908   1609   -208    155     12       O  
ATOM   3424  CB  ASP C  78      10.608 -46.170  25.933  1.00 15.34           C  
ANISOU 3424  CB  ASP C  78     1823   2191   1814   -271    298    -19       C  
ATOM   3425  CG  ASP C  78      11.982 -45.980  25.344  1.00 16.68           C  
ANISOU 3425  CG  ASP C  78     1946   2398   1995   -326    374    -16       C  
ATOM   3426  OD1 ASP C  78      12.364 -44.812  25.095  1.00 18.58           O  
ANISOU 3426  OD1 ASP C  78     2218   2625   2216   -391    386     18       O  
ATOM   3427  OD2 ASP C  78      12.686 -46.989  25.154  1.00 17.11           O  
ANISOU 3427  OD2 ASP C  78     1929   2491   2080   -304    423    -48       O  
ATOM   3428  N   LEU C  79       8.960 -46.539  28.820  1.00 12.76           N  
ANISOU 3428  N   LEU C  79     1485   1803   1559   -178    148    -33       N  
ATOM   3429  CA  LEU C  79       7.680 -46.902  29.407  1.00 11.82           C  
ANISOU 3429  CA  LEU C  79     1392   1662   1436   -127    103    -39       C  
ATOM   3430  C   LEU C  79       7.862 -47.432  30.824  1.00 11.31           C  
ANISOU 3430  C   LEU C  79     1284   1594   1418   -107     72    -54       C  
ATOM   3431  O   LEU C  79       8.705 -48.297  31.070  1.00 11.14           O  
ANISOU 3431  O   LEU C  79     1203   1599   1433   -102     83    -70       O  
ATOM   3432  CB  LEU C  79       6.988 -47.964  28.550  1.00 11.62           C  
ANISOU 3432  CB  LEU C  79     1374   1657   1385    -94    115    -57       C  
ATOM   3433  CG  LEU C  79       5.616 -48.481  29.006  1.00 10.93           C  
ANISOU 3433  CG  LEU C  79     1300   1556   1295    -50     73    -63       C  
ATOM   3434  CD1 LEU C  79       4.590 -47.365  29.083  1.00 10.47           C  
ANISOU 3434  CD1 LEU C  79     1292   1468   1217    -42     40    -34       C  
ATOM   3435  CD2 LEU C  79       5.134 -49.590  28.069  1.00 10.14           C  
ANISOU 3435  CD2 LEU C  79     1206   1477   1169    -35     84    -83       C  
ATOM   3436  N   LEU C  80       7.059 -46.904  31.744  1.00 10.58           N  
ANISOU 3436  N   LEU C  80     1228   1468   1323    -92     34    -48       N  
ATOM   3437  CA  LEU C  80       6.931 -47.459  33.089  1.00 10.05           C  
ANISOU 3437  CA  LEU C  80     1142   1395   1282    -71      3    -61       C  
ATOM   3438  C   LEU C  80       5.580 -48.176  33.212  1.00  9.59           C  
ANISOU 3438  C   LEU C  80     1098   1332   1213    -23     -7    -69       C  
ATOM   3439  O   LEU C  80       4.544 -47.627  32.818  1.00  9.49           O  
ANISOU 3439  O   LEU C  80     1124   1306   1178     -8    -10    -59       O  
ATOM   3440  CB  LEU C  80       7.035 -46.345  34.138  1.00 10.27           C  
ANISOU 3440  CB  LEU C  80     1207   1387   1309    -96    -25    -53       C  
ATOM   3441  CG  LEU C  80       6.647 -46.709  35.577  1.00  9.59           C  
ANISOU 3441  CG  LEU C  80     1129   1285   1228    -76    -56    -65       C  
ATOM   3442  CD1 LEU C  80       7.484 -47.877  36.082  1.00  8.87           C  
ANISOU 3442  CD1 LEU C  80      978   1224   1168    -73    -72    -73       C  
ATOM   3443  CD2 LEU C  80       6.794 -45.493  36.496  1.00 10.00           C  
ANISOU 3443  CD2 LEU C  80     1236   1296   1267   -107    -77    -63       C  
ATOM   3444  N   ILE C  81       5.613 -49.405  33.736  1.00  8.82           N  
ANISOU 3444  N   ILE C  81      967   1248   1136     -2    -14    -85       N  
ATOM   3445  CA  ILE C  81       4.425 -50.182  34.069  1.00  8.29           C  
ANISOU 3445  CA  ILE C  81      908   1177   1065     31    -24    -92       C  
ATOM   3446  C   ILE C  81       4.505 -50.516  35.553  1.00  7.96           C  
ANISOU 3446  C   ILE C  81      866   1122   1038     35    -47    -94       C  
ATOM   3447  O   ILE C  81       5.496 -51.100  35.985  1.00  7.54           O  
ANISOU 3447  O   ILE C  81      783   1075   1006     30    -58    -97       O  
ATOM   3448  CB  ILE C  81       4.394 -51.531  33.306  1.00  8.40           C  
ANISOU 3448  CB  ILE C  81      898   1210   1085     45    -10   -108       C  
ATOM   3449  CG1 ILE C  81       4.378 -51.314  31.796  1.00  8.13           C  
ANISOU 3449  CG1 ILE C  81      876   1191   1024     34     13   -109       C  
ATOM   3450  CG2 ILE C  81       3.190 -52.376  33.740  1.00  7.78           C  
ANISOU 3450  CG2 ILE C  81      826   1125   1005     65    -24   -113       C  
ATOM   3451  CD1 ILE C  81       4.626 -52.572  31.016  1.00  8.93           C  
ANISOU 3451  CD1 ILE C  81      964   1305   1124     42     35   -133       C  
ATOM   3452  N   GLU C  82       3.495 -50.141  36.337  1.00  7.57           N  
ANISOU 3452  N   GLU C  82      848   1055    974     47    -53    -92       N  
ATOM   3453  CA  GLU C  82       3.435 -50.601  37.727  1.00  7.68           C  
ANISOU 3453  CA  GLU C  82      873   1057    987     49    -69    -94       C  
ATOM   3454  C   GLU C  82       2.322 -51.619  37.889  1.00  7.54           C  
ANISOU 3454  C   GLU C  82      851   1045    969     69    -59    -97       C  
ATOM   3455  O   GLU C  82       1.189 -51.386  37.471  1.00  7.27           O  
ANISOU 3455  O   GLU C  82      818   1014    929     84    -44    -96       O  
ATOM   3456  CB  GLU C  82       3.257 -49.467  38.742  1.00  7.96           C  
ANISOU 3456  CB  GLU C  82      957   1065   1000     39    -73    -94       C  
ATOM   3457  CG  GLU C  82       3.335 -49.985  40.198  1.00  8.67           C  
ANISOU 3457  CG  GLU C  82     1072   1146   1077     32    -91    -96       C  
ATOM   3458  CD  GLU C  82       3.638 -48.914  41.240  1.00 10.19           C  
ANISOU 3458  CD  GLU C  82     1322   1310   1239      8   -104   -101       C  
ATOM   3459  OE1 GLU C  82       2.680 -48.465  41.897  1.00 11.38           O  
ANISOU 3459  OE1 GLU C  82     1519   1440   1364     22    -79   -110       O  
ATOM   3460  OE2 GLU C  82       4.821 -48.533  41.420  1.00 11.07           O  
ANISOU 3460  OE2 GLU C  82     1433   1420   1355    -27   -138    -98       O  
ATOM   3461  N   LEU C  83       2.660 -52.738  38.526  1.00  7.59           N  
ANISOU 3461  N   LEU C  83      850   1049    985     69    -73    -97       N  
ATOM   3462  CA  LEU C  83       1.741 -53.848  38.693  1.00  7.56           C  
ANISOU 3462  CA  LEU C  83      846   1045    982     76    -65    -98       C  
ATOM   3463  C   LEU C  83       0.994 -53.768  40.015  1.00  7.98           C  
ANISOU 3463  C   LEU C  83      933   1087   1013     72    -58    -92       C  
ATOM   3464  O   LEU C  83       1.608 -53.656  41.087  1.00  8.07           O  
ANISOU 3464  O   LEU C  83      973   1083   1008     61    -77    -86       O  
ATOM   3465  CB  LEU C  83       2.496 -55.173  38.621  1.00  7.46           C  
ANISOU 3465  CB  LEU C  83      818   1026    991     80    -81    -99       C  
ATOM   3466  CG  LEU C  83       3.178 -55.490  37.291  1.00  6.74           C  
ANISOU 3466  CG  LEU C  83      695    945    919     89    -73   -112       C  
ATOM   3467  CD1 LEU C  83       3.918 -56.819  37.405  1.00  6.80           C  
ANISOU 3467  CD1 LEU C  83      693    936    955    105    -84   -115       C  
ATOM   3468  CD2 LEU C  83       2.182 -55.505  36.147  1.00  4.36           C  
ANISOU 3468  CD2 LEU C  83      394    657    607     87    -53   -122       C  
ATOM   3469  N   HIS C  84      -0.333 -53.825  39.917  1.00  7.94           N  
ANISOU 3469  N   HIS C  84      921   1090   1005     78    -31    -92       N  
ATOM   3470  CA  HIS C  84      -1.212 -53.941  41.064  1.00  8.52           C  
ANISOU 3470  CA  HIS C  84     1019   1159   1060     72     -7    -88       C  
ATOM   3471  C   HIS C  84      -2.249 -55.043  40.840  1.00  8.74           C  
ANISOU 3471  C   HIS C  84     1021   1198   1101     62      8    -84       C  
ATOM   3472  O   HIS C  84      -2.393 -55.567  39.735  1.00  8.35           O  
ANISOU 3472  O   HIS C  84      939   1160   1072     61     -3    -87       O  
ATOM   3473  CB  HIS C  84      -1.944 -52.614  41.303  1.00  9.00           C  
ANISOU 3473  CB  HIS C  84     1090   1220   1110     91     24    -94       C  
ATOM   3474  CG  HIS C  84      -1.069 -51.531  41.855  1.00  9.42           C  
ANISOU 3474  CG  HIS C  84     1189   1249   1140     89     13   -100       C  
ATOM   3475  ND1 HIS C  84      -1.170 -51.083  43.155  1.00 10.30           N  
ANISOU 3475  ND1 HIS C  84     1358   1342   1215     81     30   -107       N  
ATOM   3476  CD2 HIS C  84      -0.079 -50.807  41.284  1.00  9.00           C  
ANISOU 3476  CD2 HIS C  84     1139   1188   1093     84    -13   -102       C  
ATOM   3477  CE1 HIS C  84      -0.275 -50.132  43.362  1.00  9.66           C  
ANISOU 3477  CE1 HIS C  84     1314   1238   1117     71      8   -114       C  
ATOM   3478  NE2 HIS C  84       0.400 -49.944  42.243  1.00 10.01           N  
ANISOU 3478  NE2 HIS C  84     1322   1290   1190     71    -18   -109       N  
ATOM   3479  N   LEU C  85      -2.964 -55.380  41.910  1.00  9.25           N  
ANISOU 3479  N   LEU C  85     1106   1261   1149     48     36    -76       N  
ATOM   3480  CA  LEU C  85      -4.214 -56.138  41.835  1.00  9.67           C  
ANISOU 3480  CA  LEU C  85     1128   1330   1215     31     63    -70       C  
ATOM   3481  C   LEU C  85      -5.252 -55.281  42.540  1.00 10.36           C  
ANISOU 3481  C   LEU C  85     1209   1434   1294     43    116    -72       C  
ATOM   3482  O   LEU C  85      -4.914 -54.544  43.466  1.00 10.88           O  
ANISOU 3482  O   LEU C  85     1323   1483   1327     53    133    -77       O  
ATOM   3483  CB  LEU C  85      -4.104 -57.512  42.514  1.00  9.54           C  
ANISOU 3483  CB  LEU C  85     1145   1293   1188     -4     57    -57       C  
ATOM   3484  CG  LEU C  85      -3.216 -58.580  41.853  1.00  9.82           C  
ANISOU 3484  CG  LEU C  85     1188   1304   1240     -9     13    -57       C  
ATOM   3485  CD1 LEU C  85      -3.306 -59.895  42.620  1.00  7.99           C  
ANISOU 3485  CD1 LEU C  85      997   1041    998    -41     11    -38       C  
ATOM   3486  CD2 LEU C  85      -3.598 -58.794  40.390  1.00  7.92           C  
ANISOU 3486  CD2 LEU C  85      900   1080   1029     -9      3    -71       C  
ATOM   3487  N   ASN C  86      -6.505 -55.369  42.096  1.00 11.03           N  
ANISOU 3487  N   ASN C  86     1233   1549   1408     42    141    -69       N  
ATOM   3488  CA  ASN C  86      -7.585 -54.534  42.620  1.00 11.95           C  
ANISOU 3488  CA  ASN C  86     1323   1685   1531     67    199    -71       C  
ATOM   3489  C   ASN C  86      -8.225 -55.177  43.847  1.00 12.61           C  
ANISOU 3489  C   ASN C  86     1425   1773   1593     33    256    -64       C  
ATOM   3490  O   ASN C  86      -7.900 -56.311  44.207  1.00 12.72           O  
ANISOU 3490  O   ASN C  86     1471   1772   1588    -11    241    -52       O  
ATOM   3491  CB  ASN C  86      -8.642 -54.286  41.523  1.00 12.35           C  
ANISOU 3491  CB  ASN C  86     1285   1774   1633     85    194    -65       C  
ATOM   3492  CG  ASN C  86      -9.202 -52.858  41.533  1.00 13.13           C  
ANISOU 3492  CG  ASN C  86     1361   1879   1750    146    225    -70       C  
ATOM   3493  OD1 ASN C  86      -9.328 -52.233  42.585  1.00 13.36           O  
ANISOU 3493  OD1 ASN C  86     1425   1892   1758    167    281    -81       O  
ATOM   3494  ND2 ASN C  86      -9.549 -52.345  40.345  1.00 12.58           N  
ANISOU 3494  ND2 ASN C  86     1239   1827   1716    175    189    -62       N  
ATOM   3495  N   ALA C  87      -9.133 -54.446  44.484  1.00 13.31           N  
ANISOU 3495  N   ALA C  87     1495   1878   1683     57    324    -70       N  
ATOM   3496  CA  ALA C  87      -9.896 -54.968  45.610  1.00 14.39           C  
ANISOU 3496  CA  ALA C  87     1642   2027   1798     25    396    -64       C  
ATOM   3497  C   ALA C  87     -11.163 -54.148  45.802  1.00 15.33           C  
ANISOU 3497  C   ALA C  87     1694   2180   1950     65    474    -72       C  
ATOM   3498  O   ALA C  87     -11.217 -52.982  45.414  1.00 15.51           O  
ANISOU 3498  O   ALA C  87     1700   2198   1995    127    475    -86       O  
ATOM   3499  CB  ALA C  87      -9.055 -54.936  46.883  1.00 14.49           C  
ANISOU 3499  CB  ALA C  87     1769   2001   1736      7    409    -68       C  
ATOM   3500  N   SER C  88     -12.185 -54.765  46.386  1.00 16.48           N  
ANISOU 3500  N   SER C  88     1800   2358   2105     30    542    -61       N  
ATOM   3501  CA  SER C  88     -13.389 -54.043  46.801  1.00 17.62           C  
ANISOU 3501  CA  SER C  88     1878   2536   2280     70    637    -70       C  
ATOM   3502  C   SER C  88     -13.937 -54.699  48.072  1.00 18.71           C  
ANISOU 3502  C   SER C  88     2045   2686   2376     17    730    -64       C  
ATOM   3503  O   SER C  88     -13.285 -54.642  49.115  1.00 18.69           O  
ANISOU 3503  O   SER C  88     2161   2648   2294      1    755    -74       O  
ATOM   3504  CB  SER C  88     -14.417 -53.983  45.662  1.00 17.97           C  
ANISOU 3504  CB  SER C  88     1779   2633   2416     92    617    -56       C  
ATOM   3505  OG  SER C  88     -14.863 -55.272  45.282  1.00 17.95           O  
ANISOU 3505  OG  SER C  88     1722   2661   2438     17    591    -32       O  
ATOM   3506  N   ASN C  89     -15.117 -55.310  47.991  1.00 19.74           N  
ANISOU 3506  N   ASN C  89     2073   2870   2556    -17    778    -46       N  
ATOM   3507  CA  ASN C  89     -15.644 -56.150  49.069  1.00 20.69           C  
ANISOU 3507  CA  ASN C  89     2217   3005   2638    -88    863    -33       C  
ATOM   3508  C   ASN C  89     -15.860 -57.584  48.559  1.00 20.80           C  
ANISOU 3508  C   ASN C  89     2193   3034   2679   -178    813      1       C  
ATOM   3509  O   ASN C  89     -16.652 -58.339  49.120  1.00 21.52           O  
ANISOU 3509  O   ASN C  89     2255   3152   2769   -245    881     20       O  
ATOM   3510  CB  ASN C  89     -16.947 -55.563  49.608  1.00 21.93           C  
ANISOU 3510  CB  ASN C  89     2287   3214   2833    -57    992    -42       C  
ATOM   3511  N   GLY C  90     -15.159 -57.944  47.483  1.00 20.19           N  
ANISOU 3511  N   GLY C  90     2117   2933   2621   -181    698      5       N  
ATOM   3512  CA  GLY C  90     -15.190 -59.306  46.946  1.00 20.24           C  
ANISOU 3512  CA  GLY C  90     2112   2935   2643   -263    640     29       C  
ATOM   3513  C   GLY C  90     -16.060 -59.481  45.713  1.00 20.64           C  
ANISOU 3513  C   GLY C  90     2028   3035   2779   -274    598     36       C  
ATOM   3514  O   GLY C  90     -15.900 -60.458  44.976  1.00 20.14           O  
ANISOU 3514  O   GLY C  90     1967   2958   2729   -331    527     46       O  
ATOM   3515  N   GLN C  91     -16.975 -58.540  45.486  1.00 21.25           N  
ANISOU 3515  N   GLN C  91     1992   3167   2914   -219    639     30       N  
ATOM   3516  CA  GLN C  91     -17.915 -58.618  44.370  1.00 21.96           C  
ANISOU 3516  CA  GLN C  91     1943   3314   3088   -228    594     42       C  
ATOM   3517  C   GLN C  91     -17.390 -57.946  43.103  1.00 20.87           C  
ANISOU 3517  C   GLN C  91     1793   3165   2969   -165    493     31       C  
ATOM   3518  O   GLN C  91     -17.799 -58.301  41.995  1.00 20.67           O  
ANISOU 3518  O   GLN C  91     1696   3169   2989   -192    418     42       O  
ATOM   3519  CB  GLN C  91     -19.256 -57.990  44.767  1.00 23.40           C  
ANISOU 3519  CB  GLN C  91     1991   3566   3334   -197    688     48       C  
ATOM   3520  CG  GLN C  91     -19.932 -58.677  45.954  1.00 25.83           C  
ANISOU 3520  CG  GLN C  91     2294   3897   3626   -271    801     60       C  
ATOM   3521  CD  GLN C  91     -20.268 -60.134  45.677  1.00 28.20           C  
ANISOU 3521  CD  GLN C  91     2574   4204   3936   -396    764     86       C  
ATOM   3522  OE1 GLN C  91     -20.801 -60.470  44.615  1.00 30.12           O  
ANISOU 3522  OE1 GLN C  91     2718   4484   4243   -428    690     98       O  
ATOM   3523  NE2 GLN C  91     -19.950 -61.009  46.628  1.00 29.19           N  
ANISOU 3523  NE2 GLN C  91     2805   4291   3995   -472    811     97       N  
ATOM   3524  N   GLY C  92     -16.512 -56.959  43.269  1.00 19.89           N  
ANISOU 3524  N   GLY C  92     1746   3002   2810    -87    492     12       N  
ATOM   3525  CA  GLY C  92     -15.837 -56.345  42.137  1.00 18.86           C  
ANISOU 3525  CA  GLY C  92     1630   2853   2684    -36    402      5       C  
ATOM   3526  C   GLY C  92     -14.957 -57.366  41.432  1.00 18.13           C  
ANISOU 3526  C   GLY C  92     1604   2726   2560    -94    318      4       C  
ATOM   3527  O   GLY C  92     -14.396 -58.264  42.070  1.00 17.53           O  
ANISOU 3527  O   GLY C  92     1607   2613   2440   -146    330      3       O  
ATOM   3528  N   LYS C  93     -14.849 -57.229  40.112  1.00 17.59           N  
ANISOU 3528  N   LYS C  93     1506   2666   2512    -82    234      5       N  
ATOM   3529  CA  LYS C  93     -14.044 -58.127  39.305  1.00 16.76           C  
ANISOU 3529  CA  LYS C  93     1462   2528   2378   -129    160     -3       C  
ATOM   3530  C   LYS C  93     -13.613 -57.450  38.002  1.00 16.00           C  
ANISOU 3530  C   LYS C  93     1366   2432   2282    -86     87     -8       C  
ATOM   3531  O   LYS C  93     -14.245 -56.494  37.553  1.00 16.17           O  
ANISOU 3531  O   LYS C  93     1318   2488   2338    -36     76      3       O  
ATOM   3532  CB  LYS C  93     -14.820 -59.408  39.006  1.00 17.65           C  
ANISOU 3532  CB  LYS C  93     1531   2661   2512   -221    140      7       C  
ATOM   3533  CG  LYS C  93     -16.151 -59.208  38.283  1.00 19.30           C  
ANISOU 3533  CG  LYS C  93     1609   2940   2783   -233    113     24       C  
ATOM   3534  CD  LYS C  93     -16.773 -60.559  37.973  1.00 20.92           C  
ANISOU 3534  CD  LYS C  93     1788   3158   3003   -341     83     31       C  
ATOM   3535  CE  LYS C  93     -18.071 -60.459  37.200  1.00 22.83           C  
ANISOU 3535  CE  LYS C  93     1894   3473   3309   -368     39     50       C  
ATOM   3536  NZ  LYS C  93     -19.281 -60.308  38.078  1.00 24.52           N  
ANISOU 3536  NZ  LYS C  93     1989   3747   3582   -379    117     72       N  
ATOM   3537  N   GLY C  94     -12.520 -57.935  37.421  1.00 14.74           N  
ANISOU 3537  N   GLY C  94     1286   2231   2083   -102     41    -23       N  
ATOM   3538  CA  GLY C  94     -12.076 -57.477  36.111  1.00 14.17           C  
ANISOU 3538  CA  GLY C  94     1226   2159   2001    -77    -25    -29       C  
ATOM   3539  C   GLY C  94     -10.758 -56.726  36.097  1.00 13.40           C  
ANISOU 3539  C   GLY C  94     1204   2022   1867    -26    -23    -41       C  
ATOM   3540  O   GLY C  94     -10.101 -56.560  37.134  1.00 12.44           O  
ANISOU 3540  O   GLY C  94     1130   1870   1729     -9     21    -47       O  
ATOM   3541  N   SER C  95     -10.400 -56.258  34.899  1.00 13.13           N  
ANISOU 3541  N   SER C  95     1181   1990   1820     -9    -73    -43       N  
ATOM   3542  CA  SER C  95      -9.115 -55.629  34.630  1.00 12.67           C  
ANISOU 3542  CA  SER C  95     1188   1897   1727     25    -77    -53       C  
ATOM   3543  C   SER C  95      -9.291 -54.152  34.310  1.00 13.07           C  
ANISOU 3543  C   SER C  95     1222   1957   1787     83    -83    -37       C  
ATOM   3544  O   SER C  95     -10.284 -53.734  33.705  1.00 13.24           O  
ANISOU 3544  O   SER C  95     1186   2011   1832     97   -113    -17       O  
ATOM   3545  CB  SER C  95      -8.421 -56.323  33.455  1.00 12.63           C  
ANISOU 3545  CB  SER C  95     1226   1880   1691     -7   -120    -70       C  
ATOM   3546  OG  SER C  95      -8.243 -57.705  33.718  1.00 12.44           O  
ANISOU 3546  OG  SER C  95     1227   1836   1662    -55   -114    -86       O  
ATOM   3547  N   GLU C  96      -8.283 -53.380  34.683  1.00 12.77           N  
ANISOU 3547  N   GLU C  96     1238   1885   1729    114    -62    -43       N  
ATOM   3548  CA  GLU C  96      -8.346 -51.938  34.661  1.00 13.24           C  
ANISOU 3548  CA  GLU C  96     1301   1935   1795    169    -56    -29       C  
ATOM   3549  C   GLU C  96      -6.916 -51.429  34.550  1.00 12.20           C  
ANISOU 3549  C   GLU C  96     1240   1766   1628    172    -55    -39       C  
ATOM   3550  O   GLU C  96      -6.011 -52.012  35.148  1.00 11.67           O  
ANISOU 3550  O   GLU C  96     1208   1681   1546    148    -38    -57       O  
ATOM   3551  CB  GLU C  96      -8.981 -51.503  35.974  1.00 14.04           C  
ANISOU 3551  CB  GLU C  96     1381   2033   1922    200      0    -30       C  
ATOM   3552  CG  GLU C  96      -9.052 -50.032  36.262  1.00 16.34           C  
ANISOU 3552  CG  GLU C  96     1689   2299   2222    262     22    -23       C  
ATOM   3553  CD  GLU C  96      -9.898 -49.772  37.500  1.00 18.02           C  
ANISOU 3553  CD  GLU C  96     1873   2513   2459    292     87    -29       C  
ATOM   3554  OE1 GLU C  96      -9.373 -49.223  38.494  1.00 18.78           O  
ANISOU 3554  OE1 GLU C  96     2030   2572   2533    307    131    -47       O  
ATOM   3555  OE2 GLU C  96     -11.090 -50.150  37.474  1.00 19.13           O  
ANISOU 3555  OE2 GLU C  96     1931   2696   2640    296     97    -18       O  
ATOM   3556  N   VAL C  97      -6.712 -50.372  33.768  1.00 11.55           N  
ANISOU 3556  N   VAL C  97     1178   1673   1537    197    -76    -24       N  
ATOM   3557  CA  VAL C  97      -5.391 -49.757  33.620  1.00 10.74           C  
ANISOU 3557  CA  VAL C  97     1138   1538   1406    193    -72    -30       C  
ATOM   3558  C   VAL C  97      -5.500 -48.245  33.751  1.00 10.87           C  
ANISOU 3558  C   VAL C  97     1180   1523   1428    236    -65    -13       C  
ATOM   3559  O   VAL C  97      -6.262 -47.600  33.020  1.00 11.02           O  
ANISOU 3559  O   VAL C  97     1183   1547   1457    267    -91     12       O  
ATOM   3560  CB  VAL C  97      -4.743 -50.087  32.268  1.00 10.67           C  
ANISOU 3560  CB  VAL C  97     1150   1540   1366    163   -103    -29       C  
ATOM   3561  CG1 VAL C  97      -3.402 -49.356  32.120  1.00 10.39           C  
ANISOU 3561  CG1 VAL C  97     1165   1475   1306    154    -90    -30       C  
ATOM   3562  CG2 VAL C  97      -4.556 -51.595  32.122  1.00  9.78           C  
ANISOU 3562  CG2 VAL C  97     1025   1444   1246    124   -105    -51       C  
ATOM   3563  N   LEU C  98      -4.718 -47.690  34.671  1.00 10.04           N  
ANISOU 3563  N   LEU C  98     1119   1382   1315    237    -36    -27       N  
ATOM   3564  CA  LEU C  98      -4.731 -46.265  34.935  1.00 10.27           C  
ANISOU 3564  CA  LEU C  98     1189   1367   1346    272    -24    -18       C  
ATOM   3565  C   LEU C  98      -3.581 -45.589  34.198  1.00 10.19           C  
ANISOU 3565  C   LEU C  98     1233   1331   1309    245    -42     -9       C  
ATOM   3566  O   LEU C  98      -2.480 -46.139  34.096  1.00  9.97           O  
ANISOU 3566  O   LEU C  98     1214   1312   1262    200    -43    -21       O  
ATOM   3567  CB  LEU C  98      -4.641 -45.998  36.436  1.00 10.19           C  
ANISOU 3567  CB  LEU C  98     1207   1328   1336    281     19    -42       C  
ATOM   3568  CG  LEU C  98      -5.542 -46.869  37.311  1.00 11.03           C  
ANISOU 3568  CG  LEU C  98     1268   1463   1458    289     49    -54       C  
ATOM   3569  CD1 LEU C  98      -5.381 -46.499  38.796  1.00 11.91           C  
ANISOU 3569  CD1 LEU C  98     1429   1543   1554    293     95    -78       C  
ATOM   3570  CD2 LEU C  98      -6.996 -46.740  36.876  1.00 10.72           C  
ANISOU 3570  CD2 LEU C  98     1163   1451   1460    336     50    -35       C  
ATOM   3571  N   TYR C  99      -3.844 -44.393  33.685  1.00 10.61           N  
ANISOU 3571  N   TYR C  99     1319   1349   1362    275    -53     15       N  
ATOM   3572  CA  TYR C  99      -2.868 -43.666  32.888  1.00 10.98           C  
ANISOU 3572  CA  TYR C  99     1420   1369   1381    244    -67     31       C  
ATOM   3573  C   TYR C  99      -2.912 -42.190  33.217  1.00 11.28           C  
ANISOU 3573  C   TYR C  99     1523   1340   1424    273    -58     43       C  
ATOM   3574  O   TYR C  99      -3.821 -41.730  33.904  1.00 11.43           O  
ANISOU 3574  O   TYR C  99     1539   1334   1469    330    -42     39       O  
ATOM   3575  CB  TYR C  99      -3.142 -43.876  31.398  1.00 11.24           C  
ANISOU 3575  CB  TYR C  99     1443   1433   1396    238   -103     60       C  
ATOM   3576  CG  TYR C  99      -4.457 -43.296  30.938  1.00 13.23           C  
ANISOU 3576  CG  TYR C  99     1680   1678   1667    298   -134     93       C  
ATOM   3577  CD1 TYR C  99      -4.534 -41.989  30.457  1.00 13.76           C  
ANISOU 3577  CD1 TYR C  99     1805   1694   1730    325   -150    128       C  
ATOM   3578  CD2 TYR C  99      -5.624 -44.048  30.985  1.00 13.67           C  
ANISOU 3578  CD2 TYR C  99     1663   1779   1753    326   -149     93       C  
ATOM   3579  CE1 TYR C  99      -5.737 -41.449  30.038  1.00 14.42           C  
ANISOU 3579  CE1 TYR C  99     1871   1770   1840    390   -185    164       C  
ATOM   3580  CE2 TYR C  99      -6.826 -43.519  30.565  1.00 14.71           C  
ANISOU 3580  CE2 TYR C  99     1764   1911   1912    384   -183    127       C  
ATOM   3581  CZ  TYR C  99      -6.873 -42.218  30.092  1.00 14.81           C  
ANISOU 3581  CZ  TYR C  99     1832   1871   1922    421   -203    164       C  
ATOM   3582  OH  TYR C  99      -8.064 -41.691  29.675  1.00 16.24           O  
ANISOU 3582  OH  TYR C  99     1980   2053   2139    488   -244    203       O  
ATOM   3583  N   TYR C 100      -1.921 -41.466  32.705  1.00 11.46           N  
ANISOU 3583  N   TYR C 100     1604   1330   1421    232    -64     56       N  
ATOM   3584  CA  TYR C 100      -1.728 -40.045  32.984  1.00 11.74           C  
ANISOU 3584  CA  TYR C 100     1718   1288   1455    242    -58     66       C  
ATOM   3585  C   TYR C 100      -1.910 -39.151  31.768  1.00 12.41           C  
ANISOU 3585  C   TYR C 100     1850   1340   1526    253    -85    114       C  
ATOM   3586  O   TYR C 100      -2.338 -38.006  31.905  1.00 12.50           O  
ANISOU 3586  O   TYR C 100     1919   1281   1549    296    -87    130       O  
ATOM   3587  CB  TYR C 100      -0.309 -39.825  33.515  1.00 11.64           C  
ANISOU 3587  CB  TYR C 100     1746   1255   1423    169    -44     46       C  
ATOM   3588  CG  TYR C 100      -0.045 -38.425  34.034  1.00 11.62           C  
ANISOU 3588  CG  TYR C 100     1834   1165   1416    164    -36     45       C  
ATOM   3589  CD1 TYR C 100      -0.549 -38.019  35.259  1.00 11.48           C  
ANISOU 3589  CD1 TYR C 100     1848   1103   1410    203    -15     15       C  
ATOM   3590  CD2 TYR C 100       0.713 -37.518  33.303  1.00 11.66           C  
ANISOU 3590  CD2 TYR C 100     1901   1127   1401    116    -46     73       C  
ATOM   3591  CE1 TYR C 100      -0.303 -36.748  35.755  1.00 12.64           C  
ANISOU 3591  CE1 TYR C 100     2092   1161   1549    197     -6      8       C  
ATOM   3592  CE2 TYR C 100       0.964 -36.232  33.786  1.00 12.04           C  
ANISOU 3592  CE2 TYR C 100     2044   1085   1445    104    -41     72       C  
ATOM   3593  CZ  TYR C 100       0.451 -35.856  35.016  1.00 12.99           C  
ANISOU 3593  CZ  TYR C 100     2201   1158   1578    146    -22     37       C  
ATOM   3594  OH  TYR C 100       0.686 -34.588  35.513  1.00 13.65           O  
ANISOU 3594  OH  TYR C 100     2391   1143   1653    134    -16     29       O  
ATOM   3595  N   SER C 101      -1.568 -39.680  30.593  1.00 12.64           N  
ANISOU 3595  N   SER C 101     1862   1415   1526    215   -105    135       N  
ATOM   3596  CA  SER C 101      -1.388 -38.893  29.384  1.00 13.35           C  
ANISOU 3596  CA  SER C 101     2013   1477   1584    199   -128    182       C  
ATOM   3597  C   SER C 101      -2.056 -39.563  28.185  1.00 13.97           C  
ANISOU 3597  C   SER C 101     2057   1610   1640    211   -166    209       C  
ATOM   3598  O   SER C 101      -2.516 -40.696  28.274  1.00 13.70           O  
ANISOU 3598  O   SER C 101     1951   1636   1617    221   -171    187       O  
ATOM   3599  CB  SER C 101       0.111 -38.755  29.102  1.00 13.44           C  
ANISOU 3599  CB  SER C 101     2061   1486   1561    109   -103    179       C  
ATOM   3600  OG  SER C 101       0.649 -39.975  28.606  1.00 11.95           O  
ANISOU 3600  OG  SER C 101     1816   1372   1354     68    -92    161       O  
ATOM   3601  N   ASN C 102      -2.077 -38.868  27.054  1.00 15.13           N  
ANISOU 3601  N   ASN C 102     2265   1733   1749    202   -196    259       N  
ATOM   3602  CA  ASN C 102      -2.645 -39.429  25.824  1.00 15.99           C  
ANISOU 3602  CA  ASN C 102     2361   1893   1822    203   -240    287       C  
ATOM   3603  C   ASN C 102      -1.849 -40.631  25.291  1.00 15.39           C  
ANISOU 3603  C   ASN C 102     2259   1884   1704    134   -216    257       C  
ATOM   3604  O   ASN C 102      -2.442 -41.602  24.839  1.00 15.10           O  
ANISOU 3604  O   ASN C 102     2178   1903   1657    140   -242    248       O  
ATOM   3605  CB  ASN C 102      -2.791 -38.348  24.753  1.00 17.08           C  
ANISOU 3605  CB  ASN C 102     2587   1983   1919    205   -280    353       C  
ATOM   3606  CG  ASN C 102      -3.868 -37.320  25.094  1.00 18.82           C  
ANISOU 3606  CG  ASN C 102     2823   2140   2187    296   -319    389       C  
ATOM   3607  OD1 ASN C 102      -4.889 -37.647  25.700  1.00 20.34           O  
ANISOU 3607  OD1 ASN C 102     2939   2352   2436    365   -333    375       O  
ATOM   3608  ND2 ASN C 102      -3.650 -36.076  24.682  1.00 20.77           N  
ANISOU 3608  ND2 ASN C 102     3168   2309   2415    298   -332    437       N  
ATOM   3609  N   LYS C 103      -0.518 -40.587  25.379  1.00 15.37           N  
ANISOU 3609  N   LYS C 103     2281   1877   1683     70   -164    238       N  
ATOM   3610  CA  LYS C 103       0.312 -41.748  24.994  1.00 15.21           C  
ANISOU 3610  CA  LYS C 103     2227   1917   1636     17   -128    202       C  
ATOM   3611  C   LYS C 103       0.026 -42.942  25.903  1.00 14.07           C  
ANISOU 3611  C   LYS C 103     1998   1811   1536     42   -121    153       C  
ATOM   3612  O   LYS C 103      -0.103 -44.071  25.436  1.00 13.84           O  
ANISOU 3612  O   LYS C 103     1938   1830   1490     32   -123    132       O  
ATOM   3613  CB  LYS C 103       1.806 -41.411  25.030  1.00 15.51           C  
ANISOU 3613  CB  LYS C 103     2287   1944   1661    -50    -71    194       C  
ATOM   3614  CG  LYS C 103       2.255 -40.439  23.955  1.00 17.57           C  
ANISOU 3614  CG  LYS C 103     2634   2177   1865    -97    -65    241       C  
ATOM   3615  CD  LYS C 103       3.740 -40.132  24.080  1.00 19.45           C  
ANISOU 3615  CD  LYS C 103     2877   2412   2102   -171     -3    232       C  
ATOM   3616  CE  LYS C 103       4.117 -38.870  23.332  1.00 21.33           C  
ANISOU 3616  CE  LYS C 103     3210   2600   2294   -220      3    286       C  
ATOM   3617  NZ  LYS C 103       3.581 -37.648  24.021  1.00 23.19           N  
ANISOU 3617  NZ  LYS C 103     3498   2751   2561   -186    -35    313       N  
ATOM   3618  N   GLY C 104      -0.077 -42.682  27.203  1.00 13.80           N  
ANISOU 3618  N   GLY C 104     1939   1750   1555     70   -112    136       N  
ATOM   3619  CA  GLY C 104      -0.482 -43.698  28.170  1.00 12.89           C  
ANISOU 3619  CA  GLY C 104     1755   1662   1479     96   -108     98       C  
ATOM   3620  C   GLY C 104      -1.828 -44.323  27.827  1.00 12.96           C  
ANISOU 3620  C   GLY C 104     1726   1703   1495    135   -147    105       C  
ATOM   3621  O   GLY C 104      -2.000 -45.533  27.946  1.00 12.78           O  
ANISOU 3621  O   GLY C 104     1656   1721   1479    127   -145     76       O  
ATOM   3622  N   LEU C 105      -2.778 -43.501  27.387  1.00 13.53           N  
ANISOU 3622  N   LEU C 105     1818   1756   1568    175   -187    145       N  
ATOM   3623  CA  LEU C 105      -4.114 -43.984  27.035  1.00 13.92           C  
ANISOU 3623  CA  LEU C 105     1820   1839   1631    210   -235    158       C  
ATOM   3624  C   LEU C 105      -4.033 -45.081  25.985  1.00 13.99           C  
ANISOU 3624  C   LEU C 105     1823   1899   1592    164   -255    148       C  
ATOM   3625  O   LEU C 105      -4.661 -46.126  26.133  1.00 13.84           O  
ANISOU 3625  O   LEU C 105     1749   1918   1590    163   -270    127       O  
ATOM   3626  CB  LEU C 105      -4.997 -42.841  26.532  1.00 14.68           C  
ANISOU 3626  CB  LEU C 105     1941   1904   1733    261   -284    212       C  
ATOM   3627  CG  LEU C 105      -6.408 -43.202  26.048  1.00 15.24           C  
ANISOU 3627  CG  LEU C 105     1953   2015   1823    299   -348    237       C  
ATOM   3628  CD1 LEU C 105      -7.193 -43.923  27.140  1.00 14.34           C  
ANISOU 3628  CD1 LEU C 105     1747   1930   1773    328   -329    205       C  
ATOM   3629  CD2 LEU C 105      -7.145 -41.954  25.578  1.00 16.19           C  
ANISOU 3629  CD2 LEU C 105     2101   2096   1955    359   -399    296       C  
ATOM   3630  N   GLU C 106      -3.245 -44.834  24.941  1.00 14.54           N  
ANISOU 3630  N   GLU C 106     1959   1966   1600    121   -252    162       N  
ATOM   3631  CA  GLU C 106      -3.013 -45.819  23.881  1.00 14.97           C  
ANISOU 3631  CA  GLU C 106     2031   2062   1596     73   -258    146       C  
ATOM   3632  C   GLU C 106      -2.599 -47.163  24.465  1.00 13.84           C  
ANISOU 3632  C   GLU C 106     1840   1945   1475     54   -219     89       C  
ATOM   3633  O   GLU C 106      -3.247 -48.175  24.213  1.00 14.09           O  
ANISOU 3633  O   GLU C 106     1845   2007   1501     46   -246     71       O  
ATOM   3634  CB  GLU C 106      -1.930 -45.346  22.907  1.00 15.54           C  
ANISOU 3634  CB  GLU C 106     2182   2123   1599     25   -228    159       C  
ATOM   3635  CG  GLU C 106      -2.180 -43.997  22.263  1.00 18.64           C  
ANISOU 3635  CG  GLU C 106     2641   2479   1960     34   -264    221       C  
ATOM   3636  CD  GLU C 106      -1.257 -43.749  21.090  1.00 21.75           C  
ANISOU 3636  CD  GLU C 106     3120   2875   2270    -27   -236    236       C  
ATOM   3637  OE1 GLU C 106      -0.260 -43.011  21.252  1.00 23.32           O  
ANISOU 3637  OE1 GLU C 106     3351   3042   2466    -54   -184    244       O  
ATOM   3638  OE2 GLU C 106      -1.521 -44.314  20.006  1.00 25.34           O  
ANISOU 3638  OE2 GLU C 106     3609   3363   2655    -55   -262    239       O  
ATOM   3639  N   TYR C 107      -1.523 -47.173  25.251  1.00 12.99           N  
ANISOU 3639  N   TYR C 107     1723   1821   1392     45   -160     64       N  
ATOM   3640  CA  TYR C 107      -1.082 -48.401  25.920  1.00 12.23           C  
ANISOU 3640  CA  TYR C 107     1583   1740   1322     36   -127     16       C  
ATOM   3641  C   TYR C 107      -2.199 -49.000  26.772  1.00 11.64           C  
ANISOU 3641  C   TYR C 107     1453   1674   1295     66   -154      8       C  
ATOM   3642  O   TYR C 107      -2.457 -50.196  26.697  1.00 11.31           O  
ANISOU 3642  O   TYR C 107     1390   1654   1254     51   -159    -19       O  
ATOM   3643  CB  TYR C 107       0.126 -48.151  26.821  1.00 11.60           C  
ANISOU 3643  CB  TYR C 107     1493   1641   1273     30    -78      1       C  
ATOM   3644  CG  TYR C 107       1.416 -47.878  26.095  1.00 12.72           C  
ANISOU 3644  CG  TYR C 107     1667   1784   1381     -9    -35      0       C  
ATOM   3645  CD1 TYR C 107       2.045 -48.874  25.345  1.00 13.28           C  
ANISOU 3645  CD1 TYR C 107     1741   1882   1424    -33     -1    -31       C  
ATOM   3646  CD2 TYR C 107       2.032 -46.634  26.177  1.00 13.41           C  
ANISOU 3646  CD2 TYR C 107     1784   1845   1467    -25    -21     26       C  
ATOM   3647  CE1 TYR C 107       3.244 -48.627  24.692  1.00 13.84           C  
ANISOU 3647  CE1 TYR C 107     1831   1959   1468    -68     52    -33       C  
ATOM   3648  CE2 TYR C 107       3.221 -46.380  25.519  1.00 13.54           C  
ANISOU 3648  CE2 TYR C 107     1821   1867   1455    -69     25     27       C  
ATOM   3649  CZ  TYR C 107       3.823 -47.380  24.787  1.00 13.74           C  
ANISOU 3649  CZ  TYR C 107     1838   1927   1456    -89     65     -2       C  
ATOM   3650  OH  TYR C 107       5.004 -47.123  24.149  1.00 16.39           O  
ANISOU 3650  OH  TYR C 107     2186   2275   1768   -132    123     -2       O  
ATOM   3651  N   ALA C 108      -2.849 -48.166  27.582  1.00 11.67           N  
ANISOU 3651  N   ALA C 108     1437   1660   1338    105   -166     30       N  
ATOM   3652  CA  ALA C 108      -3.866 -48.639  28.528  1.00 11.55           C  
ANISOU 3652  CA  ALA C 108     1364   1655   1371    132   -175     22       C  
ATOM   3653  C   ALA C 108      -5.049 -49.323  27.833  1.00 12.02           C  
ANISOU 3653  C   ALA C 108     1391   1751   1426    127   -224     30       C  
ATOM   3654  O   ALA C 108      -5.478 -50.397  28.252  1.00 12.45           O  
ANISOU 3654  O   ALA C 108     1406   1825   1501    113   -223      8       O  
ATOM   3655  CB  ALA C 108      -4.356 -47.495  29.412  1.00 11.59           C  
ANISOU 3655  CB  ALA C 108     1361   1630   1412    181   -169     42       C  
ATOM   3656  N   THR C 109      -5.562 -48.715  26.771  1.00 12.61           N  
ANISOU 3656  N   THR C 109     1486   1833   1472    132   -273     64       N  
ATOM   3657  CA  THR C 109      -6.682 -49.292  26.030  1.00 13.25           C  
ANISOU 3657  CA  THR C 109     1535   1953   1545    120   -336     76       C  
ATOM   3658  C   THR C 109      -6.343 -50.673  25.459  1.00 13.22           C  
ANISOU 3658  C   THR C 109     1551   1970   1502     61   -335     38       C  
ATOM   3659  O   THR C 109      -7.131 -51.608  25.588  1.00 13.69           O  
ANISOU 3659  O   THR C 109     1566   2054   1581     41   -360     24       O  
ATOM   3660  CB  THR C 109      -7.122 -48.357  24.902  1.00 13.82           C  
ANISOU 3660  CB  THR C 109     1642   2027   1582    132   -397    125       C  
ATOM   3661  OG1 THR C 109      -7.397 -47.070  25.458  1.00 14.07           O  
ANISOU 3661  OG1 THR C 109     1665   2026   1655    194   -393    159       O  
ATOM   3662  CG2 THR C 109      -8.371 -48.887  24.200  1.00 15.08           C  
ANISOU 3662  CG2 THR C 109     1759   2231   1739    119   -478    143       C  
ATOM   3663  N   ARG C 110      -5.165 -50.801  24.852  1.00 13.14           N  
ANISOU 3663  N   ARG C 110     1607   1947   1439     32   -302     18       N  
ATOM   3664  CA  ARG C 110      -4.738 -52.070  24.256  1.00 13.14           C  
ANISOU 3664  CA  ARG C 110     1638   1957   1399    -16   -290    -25       C  
ATOM   3665  C   ARG C 110      -4.530 -53.170  25.301  1.00 12.36           C  
ANISOU 3665  C   ARG C 110     1502   1848   1347    -18   -251    -64       C  
ATOM   3666  O   ARG C 110      -4.896 -54.324  25.076  1.00 12.41           O  
ANISOU 3666  O   ARG C 110     1509   1862   1345    -51   -266    -91       O  
ATOM   3667  CB  ARG C 110      -3.459 -51.878  23.437  1.00 13.39           C  
ANISOU 3667  CB  ARG C 110     1742   1977   1370    -37   -245    -38       C  
ATOM   3668  CG  ARG C 110      -3.649 -50.994  22.214  1.00 14.42           C  
ANISOU 3668  CG  ARG C 110     1931   2115   1432    -50   -284      1       C  
ATOM   3669  CD  ARG C 110      -2.547 -51.199  21.186  1.00 15.41           C  
ANISOU 3669  CD  ARG C 110     2135   2240   1481    -90   -236    -22       C  
ATOM   3670  NE  ARG C 110      -1.210 -50.945  21.734  1.00 15.75           N  
ANISOU 3670  NE  ARG C 110     2171   2264   1549    -81   -153    -38       N  
ATOM   3671  CZ  ARG C 110      -0.554 -49.785  21.683  1.00 16.83           C  
ANISOU 3671  CZ  ARG C 110     2329   2386   1678    -79   -127     -7       C  
ATOM   3672  NH1 ARG C 110      -1.090 -48.707  21.112  1.00 18.38           N  
ANISOU 3672  NH1 ARG C 110     2566   2577   1841    -78   -174     46       N  
ATOM   3673  NH2 ARG C 110       0.661 -49.697  22.217  1.00 16.98           N  
ANISOU 3673  NH2 ARG C 110     2330   2394   1727    -81    -57    -25       N  
ATOM   3674  N   ILE C 111      -3.945 -52.803  26.438  1.00 11.74           N  
ANISOU 3674  N   ILE C 111     1399   1749   1313     12   -206    -65       N  
ATOM   3675  CA  ILE C 111      -3.773 -53.727  27.566  1.00 11.19           C  
ANISOU 3675  CA  ILE C 111     1298   1666   1287     14   -176    -91       C  
ATOM   3676  C   ILE C 111      -5.128 -54.226  28.085  1.00 11.41           C  
ANISOU 3676  C   ILE C 111     1275   1712   1350      9   -208    -84       C  
ATOM   3677  O   ILE C 111      -5.319 -55.423  28.307  1.00 11.29           O  
ANISOU 3677  O   ILE C 111     1254   1692   1343    -19   -206   -108       O  
ATOM   3678  CB  ILE C 111      -2.996 -53.056  28.725  1.00 10.58           C  
ANISOU 3678  CB  ILE C 111     1210   1567   1244     44   -136    -86       C  
ATOM   3679  CG1 ILE C 111      -1.526 -52.849  28.334  1.00 10.63           C  
ANISOU 3679  CG1 ILE C 111     1252   1561   1228     37    -98    -99       C  
ATOM   3680  CG2 ILE C 111      -3.086 -53.891  30.001  1.00 10.54           C  
ANISOU 3680  CG2 ILE C 111     1175   1550   1279     47   -118   -101       C  
ATOM   3681  CD1 ILE C 111      -0.780 -51.831  29.207  1.00  9.23           C  
ANISOU 3681  CD1 ILE C 111     1069   1365   1073     55    -75    -85       C  
ATOM   3682  N   CYS C 112      -6.057 -53.296  28.279  1.00 11.64           N  
ANISOU 3682  N   CYS C 112     1264   1756   1402     37   -234    -49       N  
ATOM   3683  CA  CYS C 112      -7.402 -53.624  28.723  1.00 12.17           C  
ANISOU 3683  CA  CYS C 112     1266   1848   1510     35   -259    -37       C  
ATOM   3684  C   CYS C 112      -8.121 -54.533  27.733  1.00 12.83           C  
ANISOU 3684  C   CYS C 112     1345   1959   1571    -16   -314    -43       C  
ATOM   3685  O   CYS C 112      -8.767 -55.502  28.133  1.00 12.20           O  
ANISOU 3685  O   CYS C 112     1230   1890   1516    -49   -320    -54       O  
ATOM   3686  CB  CYS C 112      -8.217 -52.354  28.937  1.00 12.74           C  
ANISOU 3686  CB  CYS C 112     1295   1932   1614     86   -275      2       C  
ATOM   3687  SG  CYS C 112      -7.808 -51.501  30.463  1.00 13.33           S  
ANISOU 3687  SG  CYS C 112     1366   1973   1726    137   -208      2       S  
ATOM   3688  N   ASP C 113      -7.990 -54.225  26.443  1.00 13.26           N  
ANISOU 3688  N   ASP C 113     1444   2023   1571    -30   -356    -35       N  
ATOM   3689  CA  ASP C 113      -8.601 -55.048  25.400  1.00 14.14           C  
ANISOU 3689  CA  ASP C 113     1570   2157   1645    -86   -417    -44       C  
ATOM   3690  C   ASP C 113      -8.059 -56.484  25.448  1.00 13.47           C  
ANISOU 3690  C   ASP C 113     1527   2048   1542   -134   -386    -95       C  
ATOM   3691  O   ASP C 113      -8.823 -57.434  25.334  1.00 14.20           O  
ANISOU 3691  O   ASP C 113     1603   2152   1641   -184   -421   -108       O  
ATOM   3692  CB  ASP C 113      -8.399 -54.421  24.009  1.00 14.78           C  
ANISOU 3692  CB  ASP C 113     1714   2248   1655    -95   -461    -27       C  
ATOM   3693  CG  ASP C 113      -9.366 -53.259  23.731  1.00 16.84           C  
ANISOU 3693  CG  ASP C 113     1929   2536   1934    -58   -525     31       C  
ATOM   3694  OD1 ASP C 113     -10.494 -53.262  24.264  1.00 19.77           O  
ANISOU 3694  OD1 ASP C 113     2210   2934   2368    -45   -557     53       O  
ATOM   3695  OD2 ASP C 113      -9.006 -52.348  22.957  1.00 18.36           O  
ANISOU 3695  OD2 ASP C 113     2175   2722   2080    -42   -544     58       O  
ATOM   3696  N   LYS C 114      -6.757 -56.639  25.671  1.00 12.53           N  
ANISOU 3696  N   LYS C 114     1458   1894   1410   -118   -323   -123       N  
ATOM   3697  CA  LYS C 114      -6.153 -57.969  25.750  1.00 12.19           C  
ANISOU 3697  CA  LYS C 114     1457   1817   1358   -147   -290   -171       C  
ATOM   3698  C   LYS C 114      -6.547 -58.724  27.019  1.00 11.62           C  
ANISOU 3698  C   LYS C 114     1339   1729   1345   -152   -272   -174       C  
ATOM   3699  O   LYS C 114      -6.954 -59.877  26.948  1.00 11.57           O  
ANISOU 3699  O   LYS C 114     1348   1709   1338   -199   -287   -197       O  
ATOM   3700  CB  LYS C 114      -4.633 -57.886  25.610  1.00 11.93           C  
ANISOU 3700  CB  LYS C 114     1475   1754   1302   -121   -227   -195       C  
ATOM   3701  CG  LYS C 114      -4.171 -57.765  24.167  1.00 12.99           C  
ANISOU 3701  CG  LYS C 114     1681   1894   1360   -142   -230   -212       C  
ATOM   3702  CD  LYS C 114      -4.291 -59.093  23.417  1.00 13.96           C  
ANISOU 3702  CD  LYS C 114     1865   1999   1442   -191   -239   -259       C  
ATOM   3703  CE  LYS C 114      -3.965 -58.930  21.937  1.00 15.17           C  
ANISOU 3703  CE  LYS C 114     2101   2162   1503   -218   -243   -276       C  
ATOM   3704  NZ  LYS C 114      -4.075 -60.217  21.199  1.00 15.42           N  
ANISOU 3704  NZ  LYS C 114     2206   2167   1485   -268   -249   -331       N  
ATOM   3705  N   LEU C 115      -6.429 -58.075  28.174  1.00 11.22           N  
ANISOU 3705  N   LEU C 115     1245   1678   1340   -109   -240   -151       N  
ATOM   3706  CA  LEU C 115      -6.880 -58.674  29.436  1.00 10.84           C  
ANISOU 3706  CA  LEU C 115     1158   1620   1340   -115   -220   -147       C  
ATOM   3707  C   LEU C 115      -8.382 -58.979  29.393  1.00 11.56           C  
ANISOU 3707  C   LEU C 115     1193   1747   1454   -157   -263   -131       C  
ATOM   3708  O   LEU C 115      -8.843 -59.940  30.015  1.00 11.56           O  
ANISOU 3708  O   LEU C 115     1180   1736   1478   -195   -255   -137       O  
ATOM   3709  CB  LEU C 115      -6.545 -57.766  30.629  1.00 10.22           C  
ANISOU 3709  CB  LEU C 115     1052   1538   1293    -65   -181   -127       C  
ATOM   3710  CG  LEU C 115      -5.058 -57.682  31.011  1.00  9.18           C  
ANISOU 3710  CG  LEU C 115      962   1371   1153    -35   -141   -141       C  
ATOM   3711  CD1 LEU C 115      -4.814 -56.578  32.010  1.00  7.99           C  
ANISOU 3711  CD1 LEU C 115      793   1221   1022      6   -116   -120       C  
ATOM   3712  CD2 LEU C 115      -4.560 -59.003  31.563  1.00  8.66           C  
ANISOU 3712  CD2 LEU C 115      925   1267   1097    -52   -122   -163       C  
ATOM   3713  N   GLY C 116      -9.127 -58.167  28.642  1.00 12.25           N  
ANISOU 3713  N   GLY C 116     1245   1876   1535   -151   -311   -106       N  
ATOM   3714  CA  GLY C 116     -10.573 -58.325  28.482  1.00 13.21           C  
ANISOU 3714  CA  GLY C 116     1294   2042   1685   -187   -362    -84       C  
ATOM   3715  C   GLY C 116     -11.005 -59.597  27.775  1.00 14.06           C  
ANISOU 3715  C   GLY C 116     1427   2148   1769   -270   -407   -108       C  
ATOM   3716  O   GLY C 116     -12.179 -59.964  27.812  1.00 14.80           O  
ANISOU 3716  O   GLY C 116     1453   2276   1893   -316   -447    -93       O  
ATOM   3717  N   THR C 117     -10.053 -60.270  27.134  1.00 14.09           N  
ANISOU 3717  N   THR C 117     1526   2109   1719   -290   -399   -148       N  
ATOM   3718  CA  THR C 117     -10.307 -61.552  26.506  1.00 15.39           C  
ANISOU 3718  CA  THR C 117     1740   2254   1855   -368   -432   -182       C  
ATOM   3719  C   THR C 117     -10.547 -62.660  27.541  1.00 15.35           C  
ANISOU 3719  C   THR C 117     1725   2215   1892   -405   -400   -192       C  
ATOM   3720  O   THR C 117     -11.105 -63.703  27.210  1.00 15.83           O  
ANISOU 3720  O   THR C 117     1808   2263   1944   -483   -434   -211       O  
ATOM   3721  CB  THR C 117      -9.140 -61.956  25.577  1.00 15.45           C  
ANISOU 3721  CB  THR C 117     1860   2217   1792   -368   -414   -228       C  
ATOM   3722  OG1 THR C 117      -9.582 -62.976  24.681  1.00 18.87           O  
ANISOU 3722  OG1 THR C 117     2350   2637   2183   -447   -463   -261       O  
ATOM   3723  CG2 THR C 117      -7.953 -62.468  26.376  1.00 13.95           C  
ANISOU 3723  CG2 THR C 117     1711   1968   1620   -329   -336   -253       C  
ATOM   3724  N   VAL C 118     -10.113 -62.431  28.783  1.00 14.89           N  
ANISOU 3724  N   VAL C 118     1644   2140   1873   -357   -338   -179       N  
ATOM   3725  CA  VAL C 118     -10.277 -63.402  29.872  1.00 14.83           C  
ANISOU 3725  CA  VAL C 118     1637   2098   1900   -388   -303   -180       C  
ATOM   3726  C   VAL C 118     -11.044 -62.819  31.066  1.00 14.99           C  
ANISOU 3726  C   VAL C 118     1565   2157   1972   -371   -274   -140       C  
ATOM   3727  O   VAL C 118     -11.858 -63.514  31.677  1.00 15.46           O  
ANISOU 3727  O   VAL C 118     1591   2220   2062   -427   -267   -128       O  
ATOM   3728  CB  VAL C 118      -8.902 -63.925  30.351  1.00 14.44           C  
ANISOU 3728  CB  VAL C 118     1668   1980   1840   -350   -251   -205       C  
ATOM   3729  CG1 VAL C 118      -9.057 -64.840  31.559  1.00 14.08           C  
ANISOU 3729  CG1 VAL C 118     1631   1895   1826   -378   -220   -195       C  
ATOM   3730  CG2 VAL C 118      -8.188 -64.657  29.212  1.00 14.77           C  
ANISOU 3730  CG2 VAL C 118     1801   1978   1834   -366   -265   -251       C  
ATOM   3731  N   PHE C 119     -10.763 -61.558  31.396  1.00 14.59           N  
ANISOU 3731  N   PHE C 119     1481   2131   1931   -297   -250   -120       N  
ATOM   3732  CA  PHE C 119     -11.407 -60.850  32.500  1.00 14.71           C  
ANISOU 3732  CA  PHE C 119     1420   2179   1989   -268   -212    -89       C  
ATOM   3733  C   PHE C 119     -12.409 -59.826  31.982  1.00 14.95           C  
ANISOU 3733  C   PHE C 119     1362   2273   2045   -246   -247    -61       C  
ATOM   3734  O   PHE C 119     -12.456 -59.529  30.791  1.00 15.48           O  
ANISOU 3734  O   PHE C 119     1436   2357   2088   -247   -307    -62       O  
ATOM   3735  CB  PHE C 119     -10.354 -60.119  33.349  1.00 13.88           C  
ANISOU 3735  CB  PHE C 119     1351   2046   1876   -198   -159    -88       C  
ATOM   3736  CG  PHE C 119      -9.293 -61.023  33.914  1.00 14.00           C  
ANISOU 3736  CG  PHE C 119     1444   2000   1873   -205   -131   -107       C  
ATOM   3737  CD1 PHE C 119      -9.503 -61.695  35.106  1.00 14.01           C  
ANISOU 3737  CD1 PHE C 119     1453   1982   1889   -231    -94    -97       C  
ATOM   3738  CD2 PHE C 119      -8.089 -61.204  33.250  1.00 13.61           C  
ANISOU 3738  CD2 PHE C 119     1463   1916   1794   -185   -141   -132       C  
ATOM   3739  CE1 PHE C 119      -8.536 -62.532  35.621  1.00 14.50           C  
ANISOU 3739  CE1 PHE C 119     1589   1985   1937   -233    -79   -107       C  
ATOM   3740  CE2 PHE C 119      -7.113 -62.043  33.763  1.00 13.63           C  
ANISOU 3740  CE2 PHE C 119     1527   1863   1791   -182   -120   -146       C  
ATOM   3741  CZ  PHE C 119      -7.330 -62.707  34.945  1.00 13.46           C  
ANISOU 3741  CZ  PHE C 119     1514   1816   1784   -203    -95   -132       C  
ATOM   3742  N   LYS C 120     -13.204 -59.275  32.890  1.00 15.15           N  
ANISOU 3742  N   LYS C 120     1307   2331   2117   -221   -209    -36       N  
ATOM   3743  CA  LYS C 120     -14.081 -58.165  32.555  1.00 15.44           C  
ANISOU 3743  CA  LYS C 120     1255   2422   2190   -176   -234     -7       C  
ATOM   3744  C   LYS C 120     -13.229 -56.933  32.274  1.00 14.77           C  
ANISOU 3744  C   LYS C 120     1216   2317   2080    -96   -232     -6       C  
ATOM   3745  O   LYS C 120     -12.404 -56.535  33.100  1.00 13.67           O  
ANISOU 3745  O   LYS C 120     1124   2141   1928    -56   -175    -15       O  
ATOM   3746  CB  LYS C 120     -15.050 -57.879  33.697  1.00 16.12           C  
ANISOU 3746  CB  LYS C 120     1248   2542   2334   -160   -173     13       C  
ATOM   3747  CG  LYS C 120     -16.046 -56.774  33.397  1.00 16.34           C  
ANISOU 3747  CG  LYS C 120     1170   2624   2414   -103   -194     44       C  
ATOM   3748  CD  LYS C 120     -16.742 -56.321  34.657  1.00 16.83           C  
ANISOU 3748  CD  LYS C 120     1158   2708   2528    -64   -107     56       C  
ATOM   3749  CE  LYS C 120     -17.751 -55.231  34.367  1.00 18.05           C  
ANISOU 3749  CE  LYS C 120     1200   2913   2746      6   -124     87       C  
ATOM   3750  NZ  LYS C 120     -18.959 -55.749  33.675  1.00 17.04           N  
ANISOU 3750  NZ  LYS C 120      953   2852   2668    -48   -190    112       N  
ATOM   3751  N   ASN C 121     -13.422 -56.347  31.098  1.00 15.08           N  
ANISOU 3751  N   ASN C 121     1246   2377   2107    -81   -299      9       N  
ATOM   3752  CA  ASN C 121     -12.715 -55.127  30.729  1.00 15.10           C  
ANISOU 3752  CA  ASN C 121     1292   2360   2085    -13   -301     17       C  
ATOM   3753  C   ASN C 121     -13.399 -53.914  31.356  1.00 15.55           C  
ANISOU 3753  C   ASN C 121     1280   2434   2196     63   -274     46       C  
ATOM   3754  O   ASN C 121     -14.384 -53.406  30.827  1.00 15.96           O  
ANISOU 3754  O   ASN C 121     1257   2525   2283     86   -322     78       O  
ATOM   3755  CB  ASN C 121     -12.641 -54.994  29.206  1.00 15.43           C  
ANISOU 3755  CB  ASN C 121     1367   2414   2083    -30   -383     26       C  
ATOM   3756  CG  ASN C 121     -11.830 -53.794  28.757  1.00 15.12           C  
ANISOU 3756  CG  ASN C 121     1387   2348   2011     27   -383     37       C  
ATOM   3757  OD1 ASN C 121     -11.325 -53.023  29.571  1.00 14.60           O  
ANISOU 3757  OD1 ASN C 121     1335   2254   1960     80   -327     38       O  
ATOM   3758  ND2 ASN C 121     -11.706 -53.632  27.451  1.00 15.82           N  
ANISOU 3758  ND2 ASN C 121     1517   2444   2050     10   -447     47       N  
ATOM   3759  N   ARG C 122     -12.863 -53.462  32.490  1.00 15.41           N  
ANISOU 3759  N   ARG C 122     1290   2382   2182    103   -198     34       N  
ATOM   3760  CA  ARG C 122     -13.392 -52.288  33.184  1.00 16.14           C  
ANISOU 3760  CA  ARG C 122     1339   2476   2319    180   -157     51       C  
ATOM   3761  C   ARG C 122     -12.962 -50.988  32.515  1.00 16.13           C  
ANISOU 3761  C   ARG C 122     1379   2447   2302    242   -187     69       C  
ATOM   3762  O   ARG C 122     -13.526 -49.940  32.800  1.00 17.21           O  
ANISOU 3762  O   ARG C 122     1480   2581   2479    313   -170     88       O  
ATOM   3763  CB  ARG C 122     -12.944 -52.267  34.645  1.00 15.85           C  
ANISOU 3763  CB  ARG C 122     1337   2408   2279    192    -67     29       C  
ATOM   3764  CG  ARG C 122     -13.381 -53.480  35.447  1.00 16.67           C  
ANISOU 3764  CG  ARG C 122     1408   2530   2393    132    -29     18       C  
ATOM   3765  CD  ARG C 122     -12.582 -53.605  36.724  1.00 17.20           C  
ANISOU 3765  CD  ARG C 122     1548   2557   2430    130     41     -4       C  
ATOM   3766  NE  ARG C 122     -12.879 -52.526  37.661  1.00 18.83           N  
ANISOU 3766  NE  ARG C 122     1747   2754   2653    195    106     -5       N  
ATOM   3767  CZ  ARG C 122     -13.939 -52.483  38.471  1.00 21.38           C  
ANISOU 3767  CZ  ARG C 122     2002   3107   3016    209    169     -1       C  
ATOM   3768  NH1 ARG C 122     -14.840 -53.463  38.478  1.00 22.34           N  
ANISOU 3768  NH1 ARG C 122     2046   3274   3168    154    172     10       N  
ATOM   3769  NH2 ARG C 122     -14.101 -51.444  39.283  1.00 22.49           N  
ANISOU 3769  NH2 ARG C 122     2153   3229   3164    274    234     -9       N  
ATOM   3770  N   GLY C 123     -11.949 -51.054  31.655  1.00 15.73           N  
ANISOU 3770  N   GLY C 123     1410   2372   2194    215   -224     62       N  
ATOM   3771  CA  GLY C 123     -11.539 -49.908  30.848  1.00 15.59           C  
ANISOU 3771  CA  GLY C 123     1440   2330   2153    257   -258     84       C  
ATOM   3772  C   GLY C 123     -10.334 -49.143  31.366  1.00 15.02           C  
ANISOU 3772  C   GLY C 123     1453   2201   2053    280   -209     69       C  
ATOM   3773  O   GLY C 123      -9.961 -49.240  32.542  1.00 14.25           O  
ANISOU 3773  O   GLY C 123     1369   2083   1963    283   -147     45       O  
ATOM   3774  N   ALA C 124      -9.726 -48.378  30.464  1.00 14.76           N  
ANISOU 3774  N   ALA C 124     1480   2143   1983    290   -242     86       N  
ATOM   3775  CA  ALA C 124      -8.648 -47.467  30.815  1.00 14.34           C  
ANISOU 3775  CA  ALA C 124     1503   2036   1908    307   -205     80       C  
ATOM   3776  C   ALA C 124      -9.228 -46.251  31.542  1.00 14.65           C  
ANISOU 3776  C   ALA C 124     1532   2043   1990    381   -179     95       C  
ATOM   3777  O   ALA C 124     -10.287 -45.754  31.172  1.00 15.16           O  
ANISOU 3777  O   ALA C 124     1548   2121   2092    431   -211    126       O  
ATOM   3778  CB  ALA C 124      -7.903 -47.038  29.562  1.00 14.26           C  
ANISOU 3778  CB  ALA C 124     1560   2012   1845    286   -244     98       C  
ATOM   3779  N   LYS C 125      -8.543 -45.782  32.584  1.00 14.38           N  
ANISOU 3779  N   LYS C 125     1546   1966   1953    391   -122     71       N  
ATOM   3780  CA  LYS C 125      -9.031 -44.641  33.370  1.00 15.18           C  
ANISOU 3780  CA  LYS C 125     1655   2024   2088    460    -85     74       C  
ATOM   3781  C   LYS C 125      -7.921 -43.633  33.666  1.00 15.05           C  
ANISOU 3781  C   LYS C 125     1739   1940   2042    458    -64     65       C  
ATOM   3782  O   LYS C 125      -6.807 -44.012  34.031  1.00 13.98           O  
ANISOU 3782  O   LYS C 125     1646   1795   1870    403    -47     40       O  
ATOM   3783  CB  LYS C 125      -9.665 -45.129  34.673  1.00 15.36           C  
ANISOU 3783  CB  LYS C 125     1628   2064   2142    474    -24     47       C  
ATOM   3784  CG  LYS C 125     -10.839 -46.086  34.468  1.00 16.32           C  
ANISOU 3784  CG  LYS C 125     1643   2254   2303    469    -39     57       C  
ATOM   3785  CD  LYS C 125     -11.260 -46.749  35.767  1.00 17.33           C  
ANISOU 3785  CD  LYS C 125     1735   2401   2448    459     30     30       C  
ATOM   3786  CE  LYS C 125     -12.369 -47.762  35.541  1.00 17.75           C  
ANISOU 3786  CE  LYS C 125     1682   2523   2540    436     15     42       C  
ATOM   3787  NZ  LYS C 125     -12.903 -48.226  36.842  1.00 19.89           N  
ANISOU 3787  NZ  LYS C 125     1918   2810   2831    432     95     21       N  
ATOM   3788  N   LEU C 126      -8.231 -42.349  33.488  1.00 15.79           N  
ANISOU 3788  N   LEU C 126     1867   1982   2152    518    -69     87       N  
ATOM   3789  CA  LEU C 126      -7.288 -41.275  33.777  1.00 15.76           C  
ANISOU 3789  CA  LEU C 126     1964   1903   2122    513    -50     80       C  
ATOM   3790  C   LEU C 126      -7.227 -41.053  35.284  1.00 16.01           C  
ANISOU 3790  C   LEU C 126     2022   1900   2159    527     16     37       C  
ATOM   3791  O   LEU C 126      -8.262 -40.971  35.945  1.00 16.37           O  
ANISOU 3791  O   LEU C 126     2025   1951   2245    587     54     28       O  
ATOM   3792  CB  LEU C 126      -7.712 -39.983  33.064  1.00 16.78           C  
ANISOU 3792  CB  LEU C 126     2132   1977   2267    573    -80    122       C  
ATOM   3793  CG  LEU C 126      -6.835 -38.740  33.254  1.00 16.52           C  
ANISOU 3793  CG  LEU C 126     2214   1852   2209    566    -65    120       C  
ATOM   3794  CD1 LEU C 126      -5.438 -38.977  32.717  1.00 14.23           C  
ANISOU 3794  CD1 LEU C 126     1974   1569   1865    472    -82    120       C  
ATOM   3795  CD2 LEU C 126      -7.479 -37.514  32.592  1.00 18.32           C  
ANISOU 3795  CD2 LEU C 126     2479   2019   2463    641    -96    167       C  
ATOM   3796  N   ASP C 127      -6.013 -40.981  35.826  1.00 15.84           N  
ANISOU 3796  N   ASP C 127     2071   1851   2098    469     31     12       N  
ATOM   3797  CA  ASP C 127      -5.818 -40.632  37.236  1.00 16.20           C  
ANISOU 3797  CA  ASP C 127     2167   1855   2133    472     84    -29       C  
ATOM   3798  C   ASP C 127      -4.507 -39.880  37.419  1.00 16.14           C  
ANISOU 3798  C   ASP C 127     2258   1788   2086    418     76    -40       C  
ATOM   3799  O   ASP C 127      -3.431 -40.486  37.482  1.00 15.59           O  
ANISOU 3799  O   ASP C 127     2193   1745   1988    345     58    -49       O  
ATOM   3800  CB  ASP C 127      -5.851 -41.872  38.138  1.00 16.05           C  
ANISOU 3800  CB  ASP C 127     2104   1890   2104    439    111    -57       C  
ATOM   3801  CG  ASP C 127      -6.032 -41.516  39.610  1.00 17.08           C  
ANISOU 3801  CG  ASP C 127     2285   1984   2220    457    172    -95       C  
ATOM   3802  OD1 ASP C 127      -5.602 -40.422  40.026  1.00 18.41           O  
ANISOU 3802  OD1 ASP C 127     2544   2082   2371    463    185   -111       O  
ATOM   3803  OD2 ASP C 127      -6.611 -42.329  40.357  1.00 19.58           O  
ANISOU 3803  OD2 ASP C 127     2559   2340   2540    459    209   -111       O  
ATOM   3804  N   LYS C 128      -4.621 -38.558  37.515  1.00 16.69           N  
ANISOU 3804  N   LYS C 128     2404   1778   2160    456     87    -38       N  
ATOM   3805  CA  LYS C 128      -3.468 -37.670  37.646  1.00 17.18           C  
ANISOU 3805  CA  LYS C 128     2567   1773   2188    400     77    -46       C  
ATOM   3806  C   LYS C 128      -3.000 -37.499  39.093  1.00 17.29           C  
ANISOU 3806  C   LYS C 128     2646   1751   2171    370    110    -95       C  
ATOM   3807  O   LYS C 128      -1.990 -36.843  39.349  1.00 17.47           O  
ANISOU 3807  O   LYS C 128     2751   1724   2164    310     97   -106       O  
ATOM   3808  CB  LYS C 128      -3.792 -36.299  37.042  1.00 18.04           C  
ANISOU 3808  CB  LYS C 128     2745   1798   2313    449     69    -18       C  
ATOM   3809  CG  LYS C 128      -3.978 -36.327  35.533  1.00 18.58           C  
ANISOU 3809  CG  LYS C 128     2775   1892   2393    458     21     38       C  
ATOM   3810  CD  LYS C 128      -3.868 -34.929  34.933  1.00 19.61           C  
ANISOU 3810  CD  LYS C 128     3001   1928   2522    476      4     71       C  
ATOM   3811  CE  LYS C 128      -3.778 -34.990  33.427  1.00 20.11           C  
ANISOU 3811  CE  LYS C 128     3048   2019   2576    459    -48    129       C  
ATOM   3812  NZ  LYS C 128      -3.384 -33.679  32.841  1.00 21.16           N  
ANISOU 3812  NZ  LYS C 128     3290   2056   2693    449    -66    165       N  
ATOM   3813  N   ARG C 129      -3.722 -38.104  40.030  1.00 17.40           N  
ANISOU 3813  N   ARG C 129     2627   1794   2188    403    152   -123       N  
ATOM   3814  CA  ARG C 129      -3.430 -37.951  41.452  1.00 17.77           C  
ANISOU 3814  CA  ARG C 129     2748   1809   2195    379    188   -171       C  
ATOM   3815  C   ARG C 129      -2.334 -38.902  41.930  1.00 16.65           C  
ANISOU 3815  C   ARG C 129     2596   1716   2015    289    156   -181       C  
ATOM   3816  O   ARG C 129      -1.700 -38.649  42.946  1.00 16.93           O  
ANISOU 3816  O   ARG C 129     2709   1719   2006    242    157   -212       O  
ATOM   3817  CB  ARG C 129      -4.707 -38.175  42.267  1.00 18.51           C  
ANISOU 3817  CB  ARG C 129     2817   1914   2304    453    257   -195       C  
ATOM   3818  CG  ARG C 129      -5.836 -37.218  41.902  1.00 20.97           C  
ANISOU 3818  CG  ARG C 129     3127   2176   2664    557    293   -186       C  
ATOM   3819  CD  ARG C 129      -7.088 -37.468  42.725  1.00 23.82           C  
ANISOU 3819  CD  ARG C 129     3447   2557   3047    630    373   -211       C  
ATOM   3820  NE  ARG C 129      -7.780 -38.687  42.308  1.00 26.36           N  
ANISOU 3820  NE  ARG C 129     3633   2978   3404    637    367   -184       N  
ATOM   3821  CZ  ARG C 129      -8.882 -39.166  42.883  1.00 28.58           C  
ANISOU 3821  CZ  ARG C 129     3847   3302   3712    684    432   -196       C  
ATOM   3822  NH1 ARG C 129      -9.444 -38.537  43.917  1.00 30.64           N  
ANISOU 3822  NH1 ARG C 129     4161   3516   3966    738    519   -237       N  
ATOM   3823  NH2 ARG C 129      -9.426 -40.285  42.421  1.00 28.85           N  
ANISOU 3823  NH2 ARG C 129     3761   3423   3777    674    415   -169       N  
ATOM   3824  N   LEU C 130      -2.110 -39.990  41.195  1.00 15.40           N  
ANISOU 3824  N   LEU C 130     2346   1632   1873    265    123   -154       N  
ATOM   3825  CA  LEU C 130      -1.153 -41.020  41.603  1.00 14.41           C  
ANISOU 3825  CA  LEU C 130     2197   1556   1724    196     93   -159       C  
ATOM   3826  C   LEU C 130       0.292 -40.589  41.344  1.00 13.97           C  
ANISOU 3826  C   LEU C 130     2176   1480   1652    121     45   -153       C  
ATOM   3827  O   LEU C 130       0.640 -40.248  40.213  1.00 13.72           O  
ANISOU 3827  O   LEU C 130     2127   1448   1640    111     25   -127       O  
ATOM   3828  CB  LEU C 130      -1.454 -42.327  40.865  1.00 13.93           C  
ANISOU 3828  CB  LEU C 130     2031   1570   1690    203     80   -136       C  
ATOM   3829  CG  LEU C 130      -2.812 -42.938  41.229  1.00 13.93           C  
ANISOU 3829  CG  LEU C 130     1984   1600   1707    258    123   -140       C  
ATOM   3830  CD1 LEU C 130      -3.102 -44.151  40.390  1.00 13.03           C  
ANISOU 3830  CD1 LEU C 130     1778   1553   1620    255    103   -118       C  
ATOM   3831  CD2 LEU C 130      -2.863 -43.294  42.707  1.00 14.46           C  
ANISOU 3831  CD2 LEU C 130     2093   1664   1738    242    155   -169       C  
ATOM   3832  N   TYR C 131       1.130 -40.623  42.385  1.00 13.42           N  
ANISOU 3832  N   TYR C 131     2155   1400   1546     64     26   -175       N  
ATOM   3833  CA  TYR C 131       2.529 -40.179  42.266  1.00 13.30           C  
ANISOU 3833  CA  TYR C 131     2164   1370   1520    -15    -22   -170       C  
ATOM   3834  C   TYR C 131       3.334 -40.982  41.237  1.00 12.19           C  
ANISOU 3834  C   TYR C 131     1928   1292   1410    -45    -53   -140       C  
ATOM   3835  O   TYR C 131       4.194 -40.430  40.566  1.00 12.07           O  
ANISOU 3835  O   TYR C 131     1914   1267   1404    -92    -74   -125       O  
ATOM   3836  CB  TYR C 131       3.246 -40.187  43.634  1.00 13.75           C  
ANISOU 3836  CB  TYR C 131     2281   1413   1531    -74    -49   -197       C  
ATOM   3837  CG  TYR C 131       3.624 -41.564  44.149  1.00 13.81           C  
ANISOU 3837  CG  TYR C 131     2228   1487   1534    -91    -77   -191       C  
ATOM   3838  CD1 TYR C 131       4.734 -42.243  43.643  1.00 14.39           C  
ANISOU 3838  CD1 TYR C 131     2223   1609   1634   -134   -126   -167       C  
ATOM   3839  CD2 TYR C 131       2.880 -42.182  45.151  1.00 14.18           C  
ANISOU 3839  CD2 TYR C 131     2296   1542   1548    -63    -51   -207       C  
ATOM   3840  CE1 TYR C 131       5.076 -43.502  44.109  1.00 14.95           C  
ANISOU 3840  CE1 TYR C 131     2243   1731   1706   -140   -154   -158       C  
ATOM   3841  CE2 TYR C 131       3.218 -43.432  45.628  1.00 14.15           C  
ANISOU 3841  CE2 TYR C 131     2250   1589   1539    -79    -80   -196       C  
ATOM   3842  CZ  TYR C 131       4.315 -44.091  45.105  1.00 14.58           C  
ANISOU 3842  CZ  TYR C 131     2230   1685   1625   -114   -135   -171       C  
ATOM   3843  OH  TYR C 131       4.656 -45.338  45.574  1.00 14.91           O  
ANISOU 3843  OH  TYR C 131     2233   1768   1666   -121   -167   -156       O  
ATOM   3844  N   ILE C 132       3.059 -42.281  41.118  1.00 11.25           N  
ANISOU 3844  N   ILE C 132     1733   1234   1306    -21    -51   -133       N  
ATOM   3845  CA  ILE C 132       3.797 -43.128  40.183  1.00 10.60           C  
ANISOU 3845  CA  ILE C 132     1568   1207   1253    -41    -72   -111       C  
ATOM   3846  C   ILE C 132       3.532 -42.689  38.740  1.00 10.52           C  
ANISOU 3846  C   ILE C 132     1540   1196   1260    -24    -56    -90       C  
ATOM   3847  O   ILE C 132       4.361 -42.900  37.856  1.00 10.75           O  
ANISOU 3847  O   ILE C 132     1527   1253   1302    -56    -66    -74       O  
ATOM   3848  CB  ILE C 132       3.457 -44.631  40.369  1.00 10.14           C  
ANISOU 3848  CB  ILE C 132     1448   1201   1205    -15    -71   -111       C  
ATOM   3849  CG1 ILE C 132       4.562 -45.508  39.775  1.00  9.51           C  
ANISOU 3849  CG1 ILE C 132     1296   1166   1150    -44    -96    -99       C  
ATOM   3850  CG2 ILE C 132       2.094 -44.970  39.755  1.00 10.01           C  
ANISOU 3850  CG2 ILE C 132     1405   1197   1202     44    -37   -106       C  
ATOM   3851  CD1 ILE C 132       5.920 -45.314  40.439  1.00  8.46           C  
ANISOU 3851  CD1 ILE C 132     1166   1032   1016   -102   -138    -99       C  
ATOM   3852  N   LEU C 133       2.386 -42.047  38.523  1.00 10.71           N  
ANISOU 3852  N   LEU C 133     1598   1187   1283     28    -32    -87       N  
ATOM   3853  CA  LEU C 133       2.039 -41.477  37.225  1.00 10.77           C  
ANISOU 3853  CA  LEU C 133     1607   1185   1301     48    -27    -60       C  
ATOM   3854  C   LEU C 133       2.425 -40.001  37.089  1.00 11.48           C  
ANISOU 3854  C   LEU C 133     1779   1205   1380     22    -30    -52       C  
ATOM   3855  O   LEU C 133       2.935 -39.585  36.042  1.00 11.44           O  
ANISOU 3855  O   LEU C 133     1777   1196   1372     -9    -36    -25       O  
ATOM   3856  CB  LEU C 133       0.536 -41.654  36.973  1.00 10.47           C  
ANISOU 3856  CB  LEU C 133     1548   1153   1277    124    -10    -54       C  
ATOM   3857  CG  LEU C 133       0.032 -43.100  37.010  1.00  9.75           C  
ANISOU 3857  CG  LEU C 133     1380   1126   1197    142     -7    -59       C  
ATOM   3858  CD1 LEU C 133      -1.452 -43.148  36.621  1.00  8.99           C  
ANISOU 3858  CD1 LEU C 133     1255   1040   1122    207      4    -48       C  
ATOM   3859  CD2 LEU C 133       0.870 -44.006  36.094  1.00  8.29           C  
ANISOU 3859  CD2 LEU C 133     1146    990   1013    103    -25    -50       C  
ATOM   3860  N   ASN C 134       2.168 -39.202  38.125  1.00 12.13           N  
ANISOU 3860  N   ASN C 134     1934   1226   1449     31    -20    -74       N  
ATOM   3861  CA  ASN C 134       2.410 -37.755  38.029  1.00 12.74           C  
ANISOU 3861  CA  ASN C 134     2106   1221   1516     11    -21    -69       C  
ATOM   3862  C   ASN C 134       3.853 -37.303  38.310  1.00 12.99           C  
ANISOU 3862  C   ASN C 134     2170   1233   1531    -89    -47    -74       C  
ATOM   3863  O   ASN C 134       4.191 -36.147  38.061  1.00 13.57           O  
ANISOU 3863  O   ASN C 134     2321   1240   1597   -124    -51    -64       O  
ATOM   3864  CB  ASN C 134       1.386 -36.953  38.854  1.00 13.34           C  
ANISOU 3864  CB  ASN C 134     2258   1225   1588     76      8    -93       C  
ATOM   3865  CG  ASN C 134       1.579 -37.071  40.363  1.00 13.82           C  
ANISOU 3865  CG  ASN C 134     2361   1271   1619     54     17   -138       C  
ATOM   3866  OD1 ASN C 134       2.697 -37.135  40.868  1.00 13.58           O  
ANISOU 3866  OD1 ASN C 134     2348   1246   1567    -27    -14   -150       O  
ATOM   3867  ND2 ASN C 134       0.465 -37.068  41.092  1.00 15.02           N  
ANISOU 3867  ND2 ASN C 134     2532   1406   1770    126     59   -162       N  
ATOM   3868  N   SER C 135       4.698 -38.211  38.801  1.00 12.95           N  
ANISOU 3868  N   SER C 135     2108   1288   1526   -137    -69    -86       N  
ATOM   3869  CA  SER C 135       6.097 -37.890  39.120  1.00 13.36           C  
ANISOU 3869  CA  SER C 135     2169   1337   1571   -235   -102    -88       C  
ATOM   3870  C   SER C 135       7.114 -38.790  38.410  1.00 12.94           C  
ANISOU 3870  C   SER C 135     2008   1364   1544   -277   -115    -67       C  
ATOM   3871  O   SER C 135       8.304 -38.749  38.731  1.00 12.57           O  
ANISOU 3871  O   SER C 135     1938   1334   1503   -354   -146    -68       O  
ATOM   3872  CB  SER C 135       6.321 -37.952  40.631  1.00 13.68           C  
ANISOU 3872  CB  SER C 135     2252   1362   1585   -261   -127   -123       C  
ATOM   3873  OG  SER C 135       5.506 -37.001  41.293  1.00 15.54           O  
ANISOU 3873  OG  SER C 135     2598   1514   1791   -229   -105   -149       O  
ATOM   3874  N   SER C 136       6.648 -39.587  37.448  1.00 12.17           N  
ANISOU 3874  N   SER C 136     1846   1316   1462   -227    -92    -51       N  
ATOM   3875  CA  SER C 136       7.530 -40.367  36.582  1.00 12.25           C  
ANISOU 3875  CA  SER C 136     1766   1394   1495   -257    -88    -35       C  
ATOM   3876  C   SER C 136       7.722 -39.654  35.242  1.00 12.65           C  
ANISOU 3876  C   SER C 136     1834   1432   1540   -283    -64     -4       C  
ATOM   3877  O   SER C 136       6.746 -39.190  34.634  1.00 12.91           O  
ANISOU 3877  O   SER C 136     1916   1432   1558   -237    -49     10       O  
ATOM   3878  CB  SER C 136       6.942 -41.760  36.343  1.00 11.44           C  
ANISOU 3878  CB  SER C 136     1594   1349   1404   -194    -77    -40       C  
ATOM   3879  OG  SER C 136       5.631 -41.676  35.813  1.00 11.39           O  
ANISOU 3879  OG  SER C 136     1614   1326   1387   -130    -57    -34       O  
ATOM   3880  N   LYS C 137       8.968 -39.566  34.776  1.00 13.03           N  
ANISOU 3880  N   LYS C 137     1841   1509   1602   -357    -59      8       N  
ATOM   3881  CA  LYS C 137       9.259 -38.891  33.504  1.00 13.40           C  
ANISOU 3881  CA  LYS C 137     1909   1546   1635   -395    -28     40       C  
ATOM   3882  C   LYS C 137       8.735 -39.661  32.292  1.00 12.88           C  
ANISOU 3882  C   LYS C 137     1811   1526   1558   -346      4     53       C  
ATOM   3883  O   LYS C 137       8.051 -39.083  31.453  1.00 12.47           O  
ANISOU 3883  O   LYS C 137     1820   1441   1477   -327     14     78       O  
ATOM   3884  CB  LYS C 137      10.755 -38.599  33.333  1.00 14.30           C  
ANISOU 3884  CB  LYS C 137     1979   1685   1768   -495    -22     51       C  
ATOM   3885  CG  LYS C 137      11.044 -37.561  32.243  1.00 15.22           C  
ANISOU 3885  CG  LYS C 137     2152   1769   1861   -555     10     87       C  
ATOM   3886  CD  LYS C 137      12.532 -37.311  32.078  1.00 16.68           C  
ANISOU 3886  CD  LYS C 137     2279   1988   2072   -662     24     99       C  
ATOM   3887  CE  LYS C 137      12.829 -35.985  31.406  1.00 17.99           C  
ANISOU 3887  CE  LYS C 137     2529   2094   2211   -743     44    135       C  
ATOM   3888  NZ  LYS C 137      11.833 -35.576  30.369  1.00 16.53           N  
ANISOU 3888  NZ  LYS C 137     2434   1867   1979   -696     67    164       N  
ATOM   3889  N   PRO C 138       9.041 -40.966  32.198  1.00 12.61           N  
ANISOU 3889  N   PRO C 138     1687   1560   1544   -324     15     36       N  
ATOM   3890  CA  PRO C 138       8.501 -41.677  31.042  1.00 12.57           C  
ANISOU 3890  CA  PRO C 138     1667   1590   1520   -283     43     42       C  
ATOM   3891  C   PRO C 138       6.981 -41.821  31.090  1.00 12.06           C  
ANISOU 3891  C   PRO C 138     1642   1503   1438   -207     23     40       C  
ATOM   3892  O   PRO C 138       6.359 -41.637  32.143  1.00 11.81           O  
ANISOU 3892  O   PRO C 138     1631   1438   1417   -174     -4     28       O  
ATOM   3893  CB  PRO C 138       9.185 -43.045  31.106  1.00 12.52           C  
ANISOU 3893  CB  PRO C 138     1563   1650   1545   -273     59     18       C  
ATOM   3894  CG  PRO C 138       9.688 -43.181  32.493  1.00 12.74           C  
ANISOU 3894  CG  PRO C 138     1557   1675   1608   -284     22      1       C  
ATOM   3895  CD  PRO C 138       9.919 -41.819  33.023  1.00 12.57           C  
ANISOU 3895  CD  PRO C 138     1598   1600   1578   -337      0     14       C  
ATOM   3896  N   THR C 139       6.397 -42.118  29.937  1.00 12.04           N  
ANISOU 3896  N   THR C 139     1649   1518   1407   -183     36     54       N  
ATOM   3897  CA  THR C 139       5.007 -42.543  29.858  1.00 11.48           C  
ANISOU 3897  CA  THR C 139     1588   1447   1328   -114     13     53       C  
ATOM   3898  C   THR C 139       4.810 -43.723  30.806  1.00 10.72           C  
ANISOU 3898  C   THR C 139     1430   1380   1263    -81      5     18       C  
ATOM   3899  O   THR C 139       5.644 -44.625  30.874  1.00 10.63           O  
ANISOU 3899  O   THR C 139     1364   1407   1268    -98     21     -1       O  
ATOM   3900  CB  THR C 139       4.661 -42.988  28.432  1.00 11.63           C  
ANISOU 3900  CB  THR C 139     1613   1497   1308   -109     23     67       C  
ATOM   3901  OG1 THR C 139       4.936 -41.914  27.528  1.00 12.35           O  
ANISOU 3901  OG1 THR C 139     1769   1561   1361   -148     32    105       O  
ATOM   3902  CG2 THR C 139       3.193 -43.403  28.322  1.00 11.43           C  
ANISOU 3902  CG2 THR C 139     1589   1476   1279    -47    -12     69       C  
ATOM   3903  N   ALA C 140       3.705 -43.717  31.530  1.00 10.29           N  
ANISOU 3903  N   ALA C 140     1385   1306   1219    -31    -17     13       N  
ATOM   3904  CA  ALA C 140       3.523 -44.640  32.631  1.00  9.80           C  
ANISOU 3904  CA  ALA C 140     1283   1260   1182     -9    -23    -15       C  
ATOM   3905  C   ALA C 140       2.093 -45.134  32.685  1.00  9.53           C  
ANISOU 3905  C   ALA C 140     1237   1233   1150     46    -33    -16       C  
ATOM   3906  O   ALA C 140       1.158 -44.362  32.482  1.00  9.95           O  
ANISOU 3906  O   ALA C 140     1321   1261   1199     77    -42      2       O  
ATOM   3907  CB  ALA C 140       3.902 -43.967  33.945  1.00  9.78           C  
ANISOU 3907  CB  ALA C 140     1306   1220   1189    -24    -32    -25       C  
ATOM   3908  N   VAL C 141       1.940 -46.431  32.940  1.00  9.00           N  
ANISOU 3908  N   VAL C 141     1124   1200   1095     56    -33    -35       N  
ATOM   3909  CA  VAL C 141       0.638 -47.031  33.181  1.00  8.65           C  
ANISOU 3909  CA  VAL C 141     1059   1167   1060     94    -41    -39       C  
ATOM   3910  C   VAL C 141       0.693 -47.872  34.452  1.00  8.52           C  
ANISOU 3910  C   VAL C 141     1021   1156   1060     97    -36    -60       C  
ATOM   3911  O   VAL C 141       1.733 -48.444  34.794  1.00  8.47           O  
ANISOU 3911  O   VAL C 141     1003   1157   1060     72    -36    -71       O  
ATOM   3912  CB  VAL C 141       0.151 -47.893  31.991  1.00  8.52           C  
ANISOU 3912  CB  VAL C 141     1019   1186   1032     96    -50    -37       C  
ATOM   3913  CG1 VAL C 141      -0.060 -47.029  30.756  1.00  8.79           C  
ANISOU 3913  CG1 VAL C 141     1086   1215   1038     94    -62    -10       C  
ATOM   3914  CG2 VAL C 141       1.119 -49.032  31.687  1.00  8.26           C  
ANISOU 3914  CG2 VAL C 141      964   1176    997     69    -37    -58       C  
ATOM   3915  N   LEU C 142      -0.427 -47.907  35.163  1.00  8.70           N  
ANISOU 3915  N   LEU C 142     1041   1174   1092    127    -32    -61       N  
ATOM   3916  CA  LEU C 142      -0.572 -48.709  36.357  1.00  8.46           C  
ANISOU 3916  CA  LEU C 142      999   1146   1068    126    -23    -76       C  
ATOM   3917  C   LEU C 142      -1.609 -49.767  36.009  1.00  8.77           C  
ANISOU 3917  C   LEU C 142      998   1215   1119    137    -24    -76       C  
ATOM   3918  O   LEU C 142      -2.766 -49.435  35.736  1.00  9.08           O  
ANISOU 3918  O   LEU C 142     1019   1262   1168    162    -22    -66       O  
ATOM   3919  CB  LEU C 142      -1.025 -47.828  37.529  1.00  8.86           C  
ANISOU 3919  CB  LEU C 142     1087   1166   1114    144     -5    -81       C  
ATOM   3920  CG  LEU C 142      -1.077 -48.450  38.929  1.00  8.92           C  
ANISOU 3920  CG  LEU C 142     1106   1171   1111    136      7    -94       C  
ATOM   3921  CD1 LEU C 142      -1.067 -47.382  40.023  1.00  9.36           C  
ANISOU 3921  CD1 LEU C 142     1223   1188   1147    141     25   -106       C  
ATOM   3922  CD2 LEU C 142      -2.304 -49.338  39.071  1.00  8.91           C  
ANISOU 3922  CD2 LEU C 142     1067   1196   1124    153     26    -93       C  
ATOM   3923  N   ILE C 143      -1.178 -51.026  35.970  1.00  8.40           N  
ANISOU 3923  N   ILE C 143      934   1183   1075    116    -30    -85       N  
ATOM   3924  CA  ILE C 143      -2.033 -52.121  35.567  1.00  8.47           C  
ANISOU 3924  CA  ILE C 143      912   1213   1092    112    -34    -88       C  
ATOM   3925  C   ILE C 143      -2.627 -52.777  36.805  1.00  8.51           C  
ANISOU 3925  C   ILE C 143      914   1216   1105    109    -19    -90       C  
ATOM   3926  O   ILE C 143      -1.895 -53.289  37.644  1.00  8.19           O  
ANISOU 3926  O   ILE C 143      893   1160   1059     98    -18    -94       O  
ATOM   3927  CB  ILE C 143      -1.259 -53.177  34.746  1.00  8.51           C  
ANISOU 3927  CB  ILE C 143      915   1224   1094     92    -44   -100       C  
ATOM   3928  CG1 ILE C 143      -0.602 -52.544  33.517  1.00  8.77           C  
ANISOU 3928  CG1 ILE C 143      958   1263   1110     89    -48    -99       C  
ATOM   3929  CG2 ILE C 143      -2.192 -54.307  34.309  1.00  8.92           C  
ANISOU 3929  CG2 ILE C 143      949   1290   1150     79    -53   -106       C  
ATOM   3930  CD1 ILE C 143       0.186 -53.550  32.641  1.00  7.92           C  
ANISOU 3930  CD1 ILE C 143      852   1161    997     74    -43   -118       C  
ATOM   3931  N   GLU C 144      -3.955 -52.724  36.914  1.00  8.89           N  
ANISOU 3931  N   GLU C 144      932   1279   1164    119     -7    -83       N  
ATOM   3932  CA  GLU C 144      -4.706 -53.475  37.916  1.00  9.56           C  
ANISOU 3932  CA  GLU C 144     1007   1370   1256    107     17    -82       C  
ATOM   3933  C   GLU C 144      -5.230 -54.726  37.201  1.00  9.47           C  
ANISOU 3933  C   GLU C 144      965   1377   1257     77     -2    -83       C  
ATOM   3934  O   GLU C 144      -6.324 -54.704  36.637  1.00  9.78           O  
ANISOU 3934  O   GLU C 144      959   1444   1314     76     -8    -75       O  
ATOM   3935  CB  GLU C 144      -5.882 -52.637  38.460  1.00 10.16           C  
ANISOU 3935  CB  GLU C 144     1059   1457   1346    136     51    -75       C  
ATOM   3936  CG  GLU C 144      -5.481 -51.309  39.141  1.00 12.01           C  
ANISOU 3936  CG  GLU C 144     1337   1663   1565    167     72    -81       C  
ATOM   3937  CD  GLU C 144      -5.534 -51.348  40.673  1.00 15.09           C  
ANISOU 3937  CD  GLU C 144     1766   2037   1932    161    115    -90       C  
ATOM   3938  OE1 GLU C 144      -5.960 -52.365  41.243  1.00 17.70           O  
ANISOU 3938  OE1 GLU C 144     2085   2379   2259    135    132    -87       O  
ATOM   3939  OE2 GLU C 144      -5.160 -50.345  41.314  1.00 18.20           O  
ANISOU 3939  OE2 GLU C 144     2210   2401   2305    178    131   -100       O  
ATOM   3940  N   SER C 145      -4.450 -55.807  37.221  1.00  9.19           N  
ANISOU 3940  N   SER C 145      955   1322   1214     53    -13    -91       N  
ATOM   3941  CA  SER C 145      -4.696 -56.963  36.340  1.00  9.02           C  
ANISOU 3941  CA  SER C 145      925   1304   1197     23    -34   -100       C  
ATOM   3942  C   SER C 145      -6.001 -57.695  36.615  1.00  9.40           C  
ANISOU 3942  C   SER C 145      942   1368   1261    -10    -27    -92       C  
ATOM   3943  O   SER C 145      -6.696 -58.098  35.687  1.00  9.34           O  
ANISOU 3943  O   SER C 145      908   1380   1261    -34    -51    -95       O  
ATOM   3944  CB  SER C 145      -3.525 -57.942  36.400  1.00  8.89           C  
ANISOU 3944  CB  SER C 145      948   1253   1176     16    -42   -112       C  
ATOM   3945  OG  SER C 145      -2.387 -57.387  35.771  1.00  8.79           O  
ANISOU 3945  OG  SER C 145      946   1238   1157     39    -49   -121       O  
ATOM   3946  N   PHE C 146      -6.312 -57.886  37.890  1.00  9.57           N  
ANISOU 3946  N   PHE C 146      970   1382   1284    -18      5    -81       N  
ATOM   3947  CA  PHE C 146      -7.581 -58.465  38.309  1.00 10.32           C  
ANISOU 3947  CA  PHE C 146     1029   1498   1395    -54     25    -70       C  
ATOM   3948  C   PHE C 146      -7.756 -58.191  39.798  1.00 10.77           C  
ANISOU 3948  C   PHE C 146     1103   1549   1440    -49     75    -59       C  
ATOM   3949  O   PHE C 146      -6.859 -57.615  40.422  1.00 10.86           O  
ANISOU 3949  O   PHE C 146     1160   1538   1428    -21     81    -62       O  
ATOM   3950  CB  PHE C 146      -7.646 -59.976  38.011  1.00 10.35           C  
ANISOU 3950  CB  PHE C 146     1053   1479   1401   -109      6    -75       C  
ATOM   3951  CG  PHE C 146      -6.557 -60.779  38.661  1.00 10.26           C  
ANISOU 3951  CG  PHE C 146     1112   1414   1372   -111      5    -76       C  
ATOM   3952  CD1 PHE C 146      -6.709 -61.270  39.956  1.00 11.37           C  
ANISOU 3952  CD1 PHE C 146     1283   1535   1501   -133     33    -57       C  
ATOM   3953  CD2 PHE C 146      -5.384 -61.060  37.978  1.00  9.85           C  
ANISOU 3953  CD2 PHE C 146     1095   1332   1314    -90    -24    -93       C  
ATOM   3954  CE1 PHE C 146      -5.704 -62.017  40.560  1.00 10.87           C  
ANISOU 3954  CE1 PHE C 146     1287   1421   1422   -131     20    -51       C  
ATOM   3955  CE2 PHE C 146      -4.379 -61.812  38.568  1.00 10.09           C  
ANISOU 3955  CE2 PHE C 146     1179   1315   1340    -82    -30    -90       C  
ATOM   3956  CZ  PHE C 146      -4.533 -62.283  39.862  1.00 10.94           C  
ANISOU 3956  CZ  PHE C 146     1319   1401   1437   -101    -14    -67       C  
ATOM   3957  N   PHE C 147      -8.893 -58.612  40.356  1.00 11.30           N  
ANISOU 3957  N   PHE C 147     1136   1638   1521    -83    112    -47       N  
ATOM   3958  CA  PHE C 147      -9.191 -58.420  41.782  1.00 11.62           C  
ANISOU 3958  CA  PHE C 147     1199   1677   1541    -85    172    -38       C  
ATOM   3959  C   PHE C 147      -8.638 -59.563  42.627  1.00 11.76           C  
ANISOU 3959  C   PHE C 147     1289   1652   1526   -128    173    -27       C  
ATOM   3960  O   PHE C 147      -8.973 -60.719  42.399  1.00 11.92           O  
ANISOU 3960  O   PHE C 147     1309   1662   1558   -179    161    -18       O  
ATOM   3961  CB  PHE C 147     -10.702 -58.286  42.007  1.00 12.28           C  
ANISOU 3961  CB  PHE C 147     1202   1808   1657   -100    224    -28       C  
ATOM   3962  CG  PHE C 147     -11.241 -56.928  41.679  1.00 11.85           C  
ANISOU 3962  CG  PHE C 147     1087   1787   1630    -39    240    -33       C  
ATOM   3963  CD1 PHE C 147     -11.673 -56.073  42.685  1.00 12.27           C  
ANISOU 3963  CD1 PHE C 147     1140   1848   1676     -4    312    -36       C  
ATOM   3964  CD2 PHE C 147     -11.308 -56.494  40.361  1.00 11.84           C  
ANISOU 3964  CD2 PHE C 147     1040   1803   1658    -13    184    -35       C  
ATOM   3965  CE1 PHE C 147     -12.180 -54.814  42.384  1.00 11.83           C  
ANISOU 3965  CE1 PHE C 147     1033   1811   1651     63    329    -42       C  
ATOM   3966  CE2 PHE C 147     -11.818 -55.236  40.049  1.00 11.45           C  
ANISOU 3966  CE2 PHE C 147      939   1775   1636     49    193    -33       C  
ATOM   3967  CZ  PHE C 147     -12.253 -54.396  41.062  1.00 11.86           C  
ANISOU 3967  CZ  PHE C 147      987   1829   1690     91    265    -37       C  
ATOM   3968  N   CYS C 148      -7.804 -59.223  43.612  1.00 11.92           N  
ANISOU 3968  N   CYS C 148     1379   1645   1505   -110    182    -25       N  
ATOM   3969  CA  CYS C 148      -7.164 -60.220  44.470  1.00 12.22           C  
ANISOU 3969  CA  CYS C 148     1495   1639   1509   -142    170     -7       C  
ATOM   3970  C   CYS C 148      -8.127 -60.789  45.511  1.00 12.93           C  
ANISOU 3970  C   CYS C 148     1601   1734   1576   -194    230     14       C  
ATOM   3971  O   CYS C 148      -7.823 -61.802  46.133  1.00 13.13           O  
ANISOU 3971  O   CYS C 148     1692   1721   1575   -232    220     36       O  
ATOM   3972  CB  CYS C 148      -5.911 -59.646  45.150  1.00 11.73           C  
ANISOU 3972  CB  CYS C 148     1500   1551   1408   -110    145     -8       C  
ATOM   3973  SG  CYS C 148      -6.217 -58.444  46.472  1.00 13.21           S  
ANISOU 3973  SG  CYS C 148     1726   1752   1543    -97    205    -13       S  
ATOM   3974  N   ASP C 149      -9.279 -60.137  45.690  1.00 13.45           N  
ANISOU 3974  N   ASP C 149     1607   1847   1655   -193    294      9       N  
ATOM   3975  CA  ASP C 149     -10.316 -60.608  46.609  1.00 14.30           C  
ANISOU 3975  CA  ASP C 149     1713   1972   1749   -246    368     27       C  
ATOM   3976  C   ASP C 149     -11.512 -61.261  45.903  1.00 14.87           C  
ANISOU 3976  C   ASP C 149     1693   2080   1877   -294    382     35       C  
ATOM   3977  O   ASP C 149     -12.575 -61.420  46.498  1.00 15.21           O  
ANISOU 3977  O   ASP C 149     1699   2156   1925   -334    454     48       O  
ATOM   3978  CB  ASP C 149     -10.784 -59.464  47.532  1.00 14.91           C  
ANISOU 3978  CB  ASP C 149     1791   2076   1798   -214    448     16       C  
ATOM   3979  CG  ASP C 149     -11.366 -58.274  46.771  1.00 14.50           C  
ANISOU 3979  CG  ASP C 149     1646   2067   1799   -152    464     -7       C  
ATOM   3980  OD1 ASP C 149     -11.183 -58.182  45.537  1.00 13.14           O  
ANISOU 3980  OD1 ASP C 149     1421   1900   1671   -130    400    -13       O  
ATOM   3981  OD2 ASP C 149     -12.011 -57.418  47.422  1.00 16.15           O  
ANISOU 3981  OD2 ASP C 149     1838   2299   2001   -123    542    -18       O  
ATOM   3982  N   ASN C 150     -11.322 -61.678  44.652  1.00 14.73           N  
ANISOU 3982  N   ASN C 150     1641   2057   1898   -296    313     27       N  
ATOM   3983  CA  ASN C 150     -12.381 -62.311  43.867  1.00 15.45           C  
ANISOU 3983  CA  ASN C 150     1649   2180   2039   -350    306     32       C  
ATOM   3984  C   ASN C 150     -11.924 -63.703  43.417  1.00 15.80           C  
ANISOU 3984  C   ASN C 150     1753   2171   2081   -406    250     38       C  
ATOM   3985  O   ASN C 150     -11.006 -63.823  42.600  1.00 14.72           O  
ANISOU 3985  O   ASN C 150     1649   2001   1944   -376    186     21       O  
ATOM   3986  CB  ASN C 150     -12.724 -61.426  42.662  1.00 15.07           C  
ANISOU 3986  CB  ASN C 150     1510   2178   2039   -303    271     15       C  
ATOM   3987  CG  ASN C 150     -13.918 -61.935  41.866  1.00 16.09           C  
ANISOU 3987  CG  ASN C 150     1541   2352   2220   -359    255     22       C  
ATOM   3988  OD1 ASN C 150     -13.756 -62.649  40.877  1.00 15.48           O  
ANISOU 3988  OD1 ASN C 150     1472   2258   2152   -394    188     15       O  
ATOM   3989  ND2 ASN C 150     -15.127 -61.564  42.297  1.00 15.64           N  
ANISOU 3989  ND2 ASN C 150     1390   2354   2198   -369    317     35       N  
ATOM   3990  N   LYS C 151     -12.555 -64.743  43.971  1.00 17.26           N  
ANISOU 3990  N   LYS C 151     1955   2342   2262   -488    280     61       N  
ATOM   3991  CA  LYS C 151     -12.231 -66.143  43.654  1.00 18.11           C  
ANISOU 3991  CA  LYS C 151     2131   2385   2367   -548    235     68       C  
ATOM   3992  C   LYS C 151     -12.172 -66.402  42.149  1.00 17.88           C  
ANISOU 3992  C   LYS C 151     2068   2353   2372   -550    164     41       C  
ATOM   3993  O   LYS C 151     -11.195 -66.946  41.639  1.00 17.53           O  
ANISOU 3993  O   LYS C 151     2095   2248   2316   -530    113     26       O  
ATOM   3994  CB  LYS C 151     -13.278 -67.088  44.257  1.00 19.56           C  
ANISOU 3994  CB  LYS C 151     2309   2568   2553   -652    282     98       C  
ATOM   3995  CG  LYS C 151     -13.197 -67.291  45.772  1.00 21.90           C  
ANISOU 3995  CG  LYS C 151     2683   2842   2797   -675    346    131       C  
ATOM   3996  CD  LYS C 151     -12.013 -68.177  46.171  1.00 24.14           C  
ANISOU 3996  CD  LYS C 151     3106   3029   3038   -671    300    147       C  
ATOM   3997  CE  LYS C 151     -12.184 -68.780  47.561  1.00 25.64           C  
ANISOU 3997  CE  LYS C 151     3382   3186   3173   -730    354    192       C  
ATOM   3998  NZ  LYS C 151     -12.456 -67.748  48.608  1.00 26.96           N  
ANISOU 3998  NZ  LYS C 151     3537   3408   3299   -704    431    197       N  
ATOM   3999  N   GLU C 152     -13.225 -65.996  41.450  1.00 18.07           N  
ANISOU 3999  N   GLU C 152     1985   2445   2437   -570    163     34       N  
ATOM   4000  CA  GLU C 152     -13.366 -66.275  40.021  1.00 18.39           C  
ANISOU 4000  CA  GLU C 152     1996   2490   2501   -589     93     11       C  
ATOM   4001  C   GLU C 152     -12.250 -65.613  39.197  1.00 16.86           C  
ANISOU 4001  C   GLU C 152     1833   2281   2292   -503     47    -18       C  
ATOM   4002  O   GLU C 152     -11.738 -66.212  38.250  1.00 16.00           O  
ANISOU 4002  O   GLU C 152     1771   2133   2176   -513     -5    -41       O  
ATOM   4003  CB  GLU C 152     -14.757 -65.843  39.526  1.00 19.28           C  
ANISOU 4003  CB  GLU C 152     1976   2688   2662   -624     93     17       C  
ATOM   4004  CG  GLU C 152     -15.936 -66.650  40.145  1.00 21.85           C  
ANISOU 4004  CG  GLU C 152     2256   3034   3012   -730    136     45       C  
ATOM   4005  CD  GLU C 152     -16.174 -66.394  41.643  1.00 23.95           C  
ANISOU 4005  CD  GLU C 152     2524   3313   3264   -725    234     71       C  
ATOM   4006  OE1 GLU C 152     -15.754 -65.332  42.170  1.00 24.89           O  
ANISOU 4006  OE1 GLU C 152     2644   3448   3367   -637    271     68       O  
ATOM   4007  OE2 GLU C 152     -16.791 -67.264  42.300  1.00 25.34           O  
ANISOU 4007  OE2 GLU C 152     2708   3480   3442   -816    276     96       O  
ATOM   4008  N   ASP C 153     -11.868 -64.390  39.572  1.00 16.01           N  
ANISOU 4008  N   ASP C 153     1704   2201   2176   -424     72    -17       N  
ATOM   4009  CA  ASP C 153     -10.729 -63.709  38.943  1.00 15.14           C  
ANISOU 4009  CA  ASP C 153     1627   2076   2050   -349     38    -38       C  
ATOM   4010  C   ASP C 153      -9.441 -64.491  39.182  1.00 14.58           C  
ANISOU 4010  C   ASP C 153     1658   1929   1952   -337     23    -46       C  
ATOM   4011  O   ASP C 153      -8.701 -64.771  38.249  1.00 14.25           O  
ANISOU 4011  O   ASP C 153     1649   1858   1905   -319    -17    -70       O  
ATOM   4012  CB  ASP C 153     -10.554 -62.270  39.480  1.00 14.88           C  
ANISOU 4012  CB  ASP C 153     1565   2077   2013   -276     71    -34       C  
ATOM   4013  CG  ASP C 153     -11.291 -61.217  38.646  1.00 14.73           C  
ANISOU 4013  CG  ASP C 153     1456   2118   2021   -245     56    -36       C  
ATOM   4014  OD1 ASP C 153     -12.082 -61.575  37.746  1.00 13.34           O  
ANISOU 4014  OD1 ASP C 153     1228   1972   1871   -286     20    -37       O  
ATOM   4015  OD2 ASP C 153     -11.070 -60.007  38.900  1.00 14.64           O  
ANISOU 4015  OD2 ASP C 153     1433   2123   2008   -181     77    -36       O  
ATOM   4016  N   TYR C 154      -9.176 -64.844  40.437  1.00 14.73           N  
ANISOU 4016  N   TYR C 154     1728   1916   1952   -344     55    -24       N  
ATOM   4017  CA  TYR C 154      -7.934 -65.534  40.772  1.00 14.50           C  
ANISOU 4017  CA  TYR C 154     1790   1816   1904   -322     34    -23       C  
ATOM   4018  C   TYR C 154      -7.897 -66.927  40.135  1.00 14.95           C  
ANISOU 4018  C   TYR C 154     1896   1814   1972   -369      4    -33       C  
ATOM   4019  O   TYR C 154      -6.853 -67.370  39.663  1.00 14.38           O  
ANISOU 4019  O   TYR C 154     1874   1690   1899   -332    -26    -51       O  
ATOM   4020  CB  TYR C 154      -7.748 -65.617  42.291  1.00 14.53           C  
ANISOU 4020  CB  TYR C 154     1845   1799   1878   -326     67     10       C  
ATOM   4021  CG  TYR C 154      -6.395 -66.151  42.721  1.00 14.14           C  
ANISOU 4021  CG  TYR C 154     1879   1682   1811   -290     33     19       C  
ATOM   4022  CD1 TYR C 154      -5.220 -65.656  42.169  1.00 12.99           C  
ANISOU 4022  CD1 TYR C 154     1731   1531   1673   -222     -1     -1       C  
ATOM   4023  CD2 TYR C 154      -6.292 -67.143  43.687  1.00 14.59           C  
ANISOU 4023  CD2 TYR C 154     2013   1682   1847   -325     35     52       C  
ATOM   4024  CE1 TYR C 154      -3.984 -66.143  42.555  1.00 13.63           C  
ANISOU 4024  CE1 TYR C 154     1870   1557   1751   -184    -34     10       C  
ATOM   4025  CE2 TYR C 154      -5.053 -67.630  44.085  1.00 14.64           C  
ANISOU 4025  CE2 TYR C 154     2090   1627   1845   -283     -5     67       C  
ATOM   4026  CZ  TYR C 154      -3.907 -67.126  43.513  1.00 14.16           C  
ANISOU 4026  CZ  TYR C 154     2011   1568   1801   -211    -40     44       C  
ATOM   4027  OH  TYR C 154      -2.678 -67.604  43.895  1.00 15.28           O  
ANISOU 4027  OH  TYR C 154     2205   1655   1945   -166    -83     61       O  
ATOM   4028  N   ASP C 155      -9.040 -67.607  40.110  1.00 15.84           N  
ANISOU 4028  N   ASP C 155     1992   1932   2095   -450     14    -24       N  
ATOM   4029  CA  ASP C 155      -9.128 -68.884  39.402  1.00 16.61           C  
ANISOU 4029  CA  ASP C 155     2140   1970   2201   -505    -17    -39       C  
ATOM   4030  C   ASP C 155      -8.740 -68.707  37.928  1.00 16.06           C  
ANISOU 4030  C   ASP C 155     2060   1906   2136   -476    -58    -84       C  
ATOM   4031  O   ASP C 155      -8.022 -69.538  37.375  1.00 16.46           O  
ANISOU 4031  O   ASP C 155     2184   1888   2184   -468    -81   -108       O  
ATOM   4032  CB  ASP C 155     -10.525 -69.504  39.547  1.00 17.77           C  
ANISOU 4032  CB  ASP C 155     2255   2134   2361   -611     -2    -23       C  
ATOM   4033  CG  ASP C 155     -10.754 -70.133  40.920  1.00 18.89           C  
ANISOU 4033  CG  ASP C 155     2447   2241   2489   -658     40     20       C  
ATOM   4034  OD1 ASP C 155      -9.772 -70.380  41.650  1.00 20.23           O  
ANISOU 4034  OD1 ASP C 155     2698   2351   2635   -614     40     36       O  
ATOM   4035  OD2 ASP C 155     -11.925 -70.384  41.275  1.00 21.13           O  
ANISOU 4035  OD2 ASP C 155     2687   2557   2784   -742     72     42       O  
ATOM   4036  N   LYS C 156      -9.181 -67.615  37.309  1.00 15.50           N  
ANISOU 4036  N   LYS C 156     1907   1913   2071   -456    -64    -93       N  
ATOM   4037  CA  LYS C 156      -8.824 -67.334  35.911  1.00 15.49           C  
ANISOU 4037  CA  LYS C 156     1903   1923   2062   -431   -102   -130       C  
ATOM   4038  C   LYS C 156      -7.326 -67.066  35.758  1.00 14.54           C  
ANISOU 4038  C   LYS C 156     1830   1767   1929   -347   -100   -148       C  
ATOM   4039  O   LYS C 156      -6.710 -67.505  34.791  1.00 14.21           O  
ANISOU 4039  O   LYS C 156     1833   1690   1876   -335   -118   -182       O  
ATOM   4040  CB  LYS C 156      -9.607 -66.138  35.364  1.00 15.39           C  
ANISOU 4040  CB  LYS C 156     1793   1997   2056   -422   -113   -125       C  
ATOM   4041  CG  LYS C 156     -11.048 -66.435  34.994  1.00 17.05           C  
ANISOU 4041  CG  LYS C 156     1942   2251   2286   -506   -136   -117       C  
ATOM   4042  CD  LYS C 156     -11.787 -65.135  34.738  1.00 17.86           C  
ANISOU 4042  CD  LYS C 156     1940   2440   2407   -476   -142   -101       C  
ATOM   4043  CE  LYS C 156     -13.173 -65.357  34.153  1.00 19.88           C  
ANISOU 4043  CE  LYS C 156     2117   2749   2688   -552   -182    -92       C  
ATOM   4044  NZ  LYS C 156     -13.757 -64.061  33.687  1.00 19.75           N  
ANISOU 4044  NZ  LYS C 156     2003   2810   2691   -506   -202    -76       N  
ATOM   4045  N   ALA C 157      -6.753 -66.349  36.720  1.00 13.70           N  
ANISOU 4045  N   ALA C 157     1711   1671   1822   -293    -75   -125       N  
ATOM   4046  CA  ALA C 157      -5.326 -66.035  36.704  1.00 13.23           C  
ANISOU 4046  CA  ALA C 157     1681   1587   1758   -219    -75   -135       C  
ATOM   4047  C   ALA C 157      -4.458 -67.289  36.832  1.00 13.57           C  
ANISOU 4047  C   ALA C 157     1802   1545   1807   -208    -82   -143       C  
ATOM   4048  O   ALA C 157      -3.412 -67.386  36.203  1.00 13.34           O  
ANISOU 4048  O   ALA C 157     1795   1492   1783   -158    -87   -169       O  
ATOM   4049  CB  ALA C 157      -4.992 -65.048  37.818  1.00 12.69           C  
ANISOU 4049  CB  ALA C 157     1589   1546   1685   -179    -56   -107       C  
ATOM   4050  N   LYS C 158      -4.891 -68.237  37.660  1.00 14.20           N  
ANISOU 4050  N   LYS C 158     1925   1580   1891   -252    -79   -120       N  
ATOM   4051  CA  LYS C 158      -4.142 -69.476  37.871  1.00 14.63           C  
ANISOU 4051  CA  LYS C 158     2063   1542   1956   -239    -90   -121       C  
ATOM   4052  C   LYS C 158      -4.291 -70.437  36.690  1.00 14.89           C  
ANISOU 4052  C   LYS C 158     2142   1525   1991   -269   -101   -163       C  
ATOM   4053  O   LYS C 158      -3.380 -71.209  36.387  1.00 14.65           O  
ANISOU 4053  O   LYS C 158     2171   1421   1973   -227   -105   -184       O  
ATOM   4054  CB  LYS C 158      -4.566 -70.142  39.176  1.00 15.38           C  
ANISOU 4054  CB  LYS C 158     2201   1598   2045   -282    -83    -75       C  
ATOM   4055  CG  LYS C 158      -4.089 -69.380  40.409  1.00 15.83           C  
ANISOU 4055  CG  LYS C 158     2245   1681   2088   -242    -76    -37       C  
ATOM   4056  CD  LYS C 158      -4.213 -70.213  41.675  1.00 18.41           C  
ANISOU 4056  CD  LYS C 158     2644   1953   2400   -276    -75     11       C  
ATOM   4057  CE  LYS C 158      -5.650 -70.427  42.076  1.00 19.00           C  
ANISOU 4057  CE  LYS C 158     2709   2050   2460   -370    -42     30       C  
ATOM   4058  NZ  LYS C 158      -5.742 -71.405  43.180  1.00 21.07           N  
ANISOU 4058  NZ  LYS C 158     3057   2245   2702   -413    -39     76       N  
ATOM   4059  N   LYS C 159      -5.437 -70.376  36.021  1.00 15.11           N  
ANISOU 4059  N   LYS C 159     2140   1592   2008   -340   -108   -178       N  
ATOM   4060  CA  LYS C 159      -5.625 -71.080  34.760  1.00 15.66           C  
ANISOU 4060  CA  LYS C 159     2254   1628   2069   -376   -126   -225       C  
ATOM   4061  C   LYS C 159      -4.629 -70.545  33.717  1.00 15.15           C  
ANISOU 4061  C   LYS C 159     2187   1577   1993   -304   -121   -266       C  
ATOM   4062  O   LYS C 159      -3.857 -71.312  33.142  1.00 15.26           O  
ANISOU 4062  O   LYS C 159     2270   1522   2007   -274   -114   -303       O  
ATOM   4063  CB  LYS C 159      -7.071 -70.916  34.283  1.00 15.98           C  
ANISOU 4063  CB  LYS C 159     2245   1726   2099   -469   -146   -225       C  
ATOM   4064  CG  LYS C 159      -7.433 -71.694  33.034  1.00 17.80           C  
ANISOU 4064  CG  LYS C 159     2529   1924   2311   -528   -176   -273       C  
ATOM   4065  CD  LYS C 159      -8.936 -71.603  32.752  1.00 19.51           C  
ANISOU 4065  CD  LYS C 159     2685   2201   2526   -631   -208   -261       C  
ATOM   4066  CE  LYS C 159      -9.318 -72.204  31.402  1.00 20.46           C  
ANISOU 4066  CE  LYS C 159     2857   2301   2616   -697   -251   -311       C  
ATOM   4067  NZ  LYS C 159      -9.823 -73.614  31.514  1.00 22.16           N  
ANISOU 4067  NZ  LYS C 159     3153   2433   2836   -793   -265   -321       N  
ATOM   4068  N   LEU C 160      -4.645 -69.231  33.499  1.00 14.51           N  
ANISOU 4068  N   LEU C 160     2030   1581   1903   -276   -119   -259       N  
ATOM   4069  CA  LEU C 160      -3.728 -68.562  32.552  1.00 14.46           C  
ANISOU 4069  CA  LEU C 160     2015   1598   1882   -216   -108   -290       C  
ATOM   4070  C   LEU C 160      -2.245 -68.760  32.888  1.00 14.31           C  
ANISOU 4070  C   LEU C 160     2020   1533   1886   -132    -83   -295       C  
ATOM   4071  O   LEU C 160      -1.410 -68.877  31.991  1.00 14.58           O  
ANISOU 4071  O   LEU C 160     2078   1548   1912    -92    -64   -334       O  
ATOM   4072  CB  LEU C 160      -3.993 -67.051  32.510  1.00 14.04           C  
ANISOU 4072  CB  LEU C 160     1880   1635   1820   -200   -111   -268       C  
ATOM   4073  CG  LEU C 160      -4.815 -66.463  31.368  1.00 14.61           C  
ANISOU 4073  CG  LEU C 160     1925   1765   1861   -238   -136   -281       C  
ATOM   4074  CD1 LEU C 160      -6.171 -67.098  31.302  1.00 17.04           C  
ANISOU 4074  CD1 LEU C 160     2229   2076   2169   -324   -168   -277       C  
ATOM   4075  CD2 LEU C 160      -4.937 -64.958  31.556  1.00 14.71           C  
ANISOU 4075  CD2 LEU C 160     1864   1850   1875   -205   -135   -252       C  
ATOM   4076  N   GLY C 161      -1.928 -68.765  34.177  1.00 13.80           N  
ANISOU 4076  N   GLY C 161     1944   1453   1846   -106    -83   -254       N  
ATOM   4077  CA  GLY C 161      -0.539 -68.754  34.627  1.00 14.00           C  
ANISOU 4077  CA  GLY C 161     1968   1451   1899    -26    -72   -247       C  
ATOM   4078  C   GLY C 161       0.073 -67.372  34.490  1.00 13.37           C  
ANISOU 4078  C   GLY C 161     1820   1444   1817     15    -63   -242       C  
ATOM   4079  O   GLY C 161      -0.504 -66.486  33.853  1.00 13.16           O  
ANISOU 4079  O   GLY C 161     1759   1478   1764    -10    -61   -250       O  
ATOM   4080  N   HIS C 162       1.248 -67.179  35.084  1.00 13.37           N  
ANISOU 4080  N   HIS C 162     1799   1435   1844     77    -62   -226       N  
ATOM   4081  CA  HIS C 162       1.934 -65.882  35.013  1.00 13.01           C  
ANISOU 4081  CA  HIS C 162     1691   1453   1800    108    -54   -219       C  
ATOM   4082  C   HIS C 162       2.226 -65.498  33.557  1.00 13.05           C  
ANISOU 4082  C   HIS C 162     1685   1485   1788    116    -24   -261       C  
ATOM   4083  O   HIS C 162       2.099 -64.339  33.176  1.00 12.10           O  
ANISOU 4083  O   HIS C 162     1527   1423   1646    105    -19   -258       O  
ATOM   4084  CB  HIS C 162       3.231 -65.895  35.830  1.00 13.24           C  
ANISOU 4084  CB  HIS C 162     1698   1466   1867    167    -66   -196       C  
ATOM   4085  CG  HIS C 162       3.025 -66.177  37.288  1.00 14.02           C  
ANISOU 4085  CG  HIS C 162     1819   1540   1968    158   -101   -150       C  
ATOM   4086  ND1 HIS C 162       2.137 -65.465  38.068  1.00 15.44           N  
ANISOU 4086  ND1 HIS C 162     1994   1757   2116    113   -109   -124       N  
ATOM   4087  CD2 HIS C 162       3.590 -67.094  38.106  1.00 15.35           C  
ANISOU 4087  CD2 HIS C 162     2019   1650   2163    188   -127   -125       C  
ATOM   4088  CE1 HIS C 162       2.167 -65.934  39.305  1.00 14.25           C  
ANISOU 4088  CE1 HIS C 162     1877   1573   1964    109   -135    -86       C  
ATOM   4089  NE2 HIS C 162       3.041 -66.922  39.354  1.00 14.91           N  
ANISOU 4089  NE2 HIS C 162     1985   1598   2082    154   -152    -83       N  
ATOM   4090  N   GLU C 163       2.585 -66.497  32.757  1.00 13.64           N  
ANISOU 4090  N   GLU C 163     1802   1510   1868    133     -3   -301       N  
ATOM   4091  CA  GLU C 163       2.897 -66.329  31.340  1.00 14.47           C  
ANISOU 4091  CA  GLU C 163     1917   1632   1948    138     34   -346       C  
ATOM   4092  C   GLU C 163       1.674 -65.959  30.490  1.00 13.98           C  
ANISOU 4092  C   GLU C 163     1876   1605   1830     71     21   -359       C  
ATOM   4093  O   GLU C 163       1.794 -65.195  29.540  1.00 14.16           O  
ANISOU 4093  O   GLU C 163     1889   1673   1819     65     38   -374       O  
ATOM   4094  CB  GLU C 163       3.552 -67.622  30.836  1.00 15.73           C  
ANISOU 4094  CB  GLU C 163     2131   1717   2128    177     65   -389       C  
ATOM   4095  CG  GLU C 163       3.692 -67.790  29.355  1.00 18.00           C  
ANISOU 4095  CG  GLU C 163     2461   2003   2376    173    110   -447       C  
ATOM   4096  CD  GLU C 163       4.223 -69.164  29.030  1.00 20.86           C  
ANISOU 4096  CD  GLU C 163     2889   2276   2760    214    142   -491       C  
ATOM   4097  OE1 GLU C 163       3.423 -70.026  28.589  1.00 22.47           O  
ANISOU 4097  OE1 GLU C 163     3176   2429   2932    167    132   -522       O  
ATOM   4098  OE2 GLU C 163       5.431 -69.384  29.260  1.00 22.98           O  
ANISOU 4098  OE2 GLU C 163     3124   2524   3083    293    175   -493       O  
ATOM   4099  N   GLY C 164       0.506 -66.497  30.827  1.00 13.78           N  
ANISOU 4099  N   GLY C 164     1878   1563   1796     17    -12   -349       N  
ATOM   4100  CA  GLY C 164      -0.731 -66.131  30.139  1.00 13.47           C  
ANISOU 4100  CA  GLY C 164     1841   1564   1713    -48    -38   -353       C  
ATOM   4101  C   GLY C 164      -1.081 -64.673  30.376  1.00 12.58           C  
ANISOU 4101  C   GLY C 164     1661   1526   1594    -49    -51   -316       C  
ATOM   4102  O   GLY C 164      -1.421 -63.946  29.443  1.00 12.65           O  
ANISOU 4102  O   GLY C 164     1663   1579   1566    -66    -59   -322       O  
ATOM   4103  N   ILE C 165      -0.983 -64.258  31.634  1.00 11.75           N  
ANISOU 4103  N   ILE C 165     1516   1429   1520    -28    -54   -278       N  
ATOM   4104  CA  ILE C 165      -1.234 -62.877  32.045  1.00 11.11           C  
ANISOU 4104  CA  ILE C 165     1379   1404   1436    -21    -60   -246       C  
ATOM   4105  C   ILE C 165      -0.206 -61.971  31.389  1.00 10.48           C  
ANISOU 4105  C   ILE C 165     1286   1349   1347     15    -39   -254       C  
ATOM   4106  O   ILE C 165      -0.562 -60.973  30.754  1.00 10.01           O  
ANISOU 4106  O   ILE C 165     1211   1332   1261      5    -45   -247       O  
ATOM   4107  CB  ILE C 165      -1.130 -62.714  33.587  1.00 10.85           C  
ANISOU 4107  CB  ILE C 165     1327   1364   1432     -5    -62   -211       C  
ATOM   4108  CG1 ILE C 165      -2.250 -63.482  34.291  1.00 11.41           C  
ANISOU 4108  CG1 ILE C 165     1409   1418   1508    -50    -73   -196       C  
ATOM   4109  CG2 ILE C 165      -1.179 -61.232  33.984  1.00 11.36           C  
ANISOU 4109  CG2 ILE C 165     1348   1476   1492      9    -60   -186       C  
ATOM   4110  CD1 ILE C 165      -3.606 -62.857  34.146  1.00 12.09           C  
ANISOU 4110  CD1 ILE C 165     1455   1553   1584    -88    -84   -182       C  
ATOM   4111  N   ALA C 166       1.067 -62.341  31.530  1.00 10.09           N  
ANISOU 4111  N   ALA C 166     1241   1272   1320     55    -15   -266       N  
ATOM   4112  CA  ALA C 166       2.171 -61.592  30.923  1.00  9.95           C  
ANISOU 4112  CA  ALA C 166     1203   1278   1299     84     15   -275       C  
ATOM   4113  C   ALA C 166       1.975 -61.389  29.423  1.00 10.21           C  
ANISOU 4113  C   ALA C 166     1265   1332   1284     62     32   -302       C  
ATOM   4114  O   ALA C 166       2.123 -60.272  28.917  1.00  9.93           O  
ANISOU 4114  O   ALA C 166     1215   1336   1224     57     39   -291       O  
ATOM   4115  CB  ALA C 166       3.500 -62.293  31.186  1.00 10.06           C  
ANISOU 4115  CB  ALA C 166     1209   1259   1355    132     41   -288       C  
ATOM   4116  N   LYS C 167       1.643 -62.466  28.721  1.00 10.76           N  
ANISOU 4116  N   LYS C 167     1387   1370   1333     45     36   -338       N  
ATOM   4117  CA  LYS C 167       1.477 -62.422  27.268  1.00 11.74           C  
ANISOU 4117  CA  LYS C 167     1557   1508   1397     19     49   -369       C  
ATOM   4118  C   LYS C 167       0.441 -61.375  26.841  1.00 11.51           C  
ANISOU 4118  C   LYS C 167     1517   1528   1327    -20      8   -341       C  
ATOM   4119  O   LYS C 167       0.659 -60.640  25.876  1.00 11.68           O  
ANISOU 4119  O   LYS C 167     1555   1580   1303    -29     20   -343       O  
ATOM   4120  CB  LYS C 167       1.074 -63.800  26.742  1.00 12.52           C  
ANISOU 4120  CB  LYS C 167     1724   1556   1476     -5     47   -413       C  
ATOM   4121  CG  LYS C 167       0.955 -63.912  25.226  1.00 15.25           C  
ANISOU 4121  CG  LYS C 167     2137   1909   1749    -37     61   -454       C  
ATOM   4122  CD  LYS C 167       0.717 -65.372  24.823  1.00 18.14           C  
ANISOU 4122  CD  LYS C 167     2582   2210   2099    -58     65   -505       C  
ATOM   4123  CE  LYS C 167       0.534 -65.537  23.322  1.00 20.71           C  
ANISOU 4123  CE  LYS C 167     2992   2539   2338    -99     74   -551       C  
ATOM   4124  NZ  LYS C 167      -0.005 -66.892  22.969  1.00 22.26           N  
ANISOU 4124  NZ  LYS C 167     3275   2670   2512   -140     58   -599       N  
ATOM   4125  N   LEU C 168      -0.672 -61.314  27.564  1.00 10.87           N  
ANISOU 4125  N   LEU C 168     1410   1457   1265    -43    -39   -313       N  
ATOM   4126  CA  LEU C 168      -1.762 -60.389  27.237  1.00 10.67           C  
ANISOU 4126  CA  LEU C 168     1364   1476   1214    -70    -83   -283       C  
ATOM   4127  C   LEU C 168      -1.320 -58.939  27.413  1.00 10.16           C  
ANISOU 4127  C   LEU C 168     1265   1442   1153    -40    -72   -250       C  
ATOM   4128  O   LEU C 168      -1.596 -58.084  26.571  1.00  9.55           O  
ANISOU 4128  O   LEU C 168     1199   1394   1037    -51    -89   -236       O  
ATOM   4129  CB  LEU C 168      -2.992 -60.685  28.107  1.00 10.47           C  
ANISOU 4129  CB  LEU C 168     1303   1455   1222    -94   -121   -260       C  
ATOM   4130  CG  LEU C 168      -3.736 -61.985  27.774  1.00 11.48           C  
ANISOU 4130  CG  LEU C 168     1464   1557   1338   -145   -147   -286       C  
ATOM   4131  CD1 LEU C 168      -4.805 -62.275  28.816  1.00 11.61           C  
ANISOU 4131  CD1 LEU C 168     1435   1579   1396   -171   -169   -259       C  
ATOM   4132  CD2 LEU C 168      -4.356 -61.959  26.374  1.00 11.58           C  
ANISOU 4132  CD2 LEU C 168     1513   1595   1293   -191   -187   -301       C  
ATOM   4133  N   ILE C 169      -0.608 -58.680  28.505  1.00  9.65           N  
ANISOU 4133  N   ILE C 169     1168   1366   1132     -7    -48   -237       N  
ATOM   4134  CA  ILE C 169      -0.077 -57.358  28.781  1.00  9.17           C  
ANISOU 4134  CA  ILE C 169     1083   1324   1078     15    -37   -211       C  
ATOM   4135  C   ILE C 169       0.932 -56.937  27.710  1.00  9.61           C  
ANISOU 4135  C   ILE C 169     1164   1389   1100     15     -3   -223       C  
ATOM   4136  O   ILE C 169       0.889 -55.806  27.216  1.00  9.13           O  
ANISOU 4136  O   ILE C 169     1108   1349   1012      8     -8   -200       O  
ATOM   4137  CB  ILE C 169       0.597 -57.298  30.168  1.00  9.03           C  
ANISOU 4137  CB  ILE C 169     1034   1289   1107     41    -24   -200       C  
ATOM   4138  CG1 ILE C 169      -0.430 -57.568  31.275  1.00  8.63           C  
ANISOU 4138  CG1 ILE C 169      967   1233   1080     37    -48   -183       C  
ATOM   4139  CG2 ILE C 169       1.260 -55.936  30.362  1.00  8.45           C  
ANISOU 4139  CG2 ILE C 169      945   1229   1035     53    -14   -178       C  
ATOM   4140  CD1 ILE C 169       0.154 -57.543  32.682  1.00  7.41           C  
ANISOU 4140  CD1 ILE C 169      797   1060    958     56    -42   -171       C  
ATOM   4141  N   VAL C 170       1.829 -57.852  27.354  1.00 10.30           N  
ANISOU 4141  N   VAL C 170     1267   1458   1188     23     36   -259       N  
ATOM   4142  CA  VAL C 170       2.857 -57.597  26.336  1.00 11.00           C  
ANISOU 4142  CA  VAL C 170     1375   1558   1247     23     87   -277       C  
ATOM   4143  C   VAL C 170       2.260 -57.349  24.945  1.00 11.96           C  
ANISOU 4143  C   VAL C 170     1555   1697   1291    -13     78   -282       C  
ATOM   4144  O   VAL C 170       2.664 -56.415  24.226  1.00 12.16           O  
ANISOU 4144  O   VAL C 170     1597   1745   1278    -25     98   -268       O  
ATOM   4145  CB  VAL C 170       3.855 -58.775  26.262  1.00 11.40           C  
ANISOU 4145  CB  VAL C 170     1428   1580   1322     50    137   -319       C  
ATOM   4146  CG1 VAL C 170       4.807 -58.616  25.065  1.00 11.58           C  
ANISOU 4146  CG1 VAL C 170     1474   1618   1306     48    204   -344       C  
ATOM   4147  CG2 VAL C 170       4.627 -58.893  27.575  1.00 10.72           C  
ANISOU 4147  CG2 VAL C 170     1283   1482   1310     87    139   -304       C  
ATOM   4148  N   GLU C 171       1.304 -58.188  24.557  1.00 12.60           N  
ANISOU 4148  N   GLU C 171     1673   1769   1346    -36     43   -302       N  
ATOM   4149  CA  GLU C 171       0.630 -58.015  23.274  1.00 13.34           C  
ANISOU 4149  CA  GLU C 171     1827   1881   1361    -76     16   -305       C  
ATOM   4150  C   GLU C 171      -0.074 -56.666  23.214  1.00 13.42           C  
ANISOU 4150  C   GLU C 171     1820   1923   1357    -84    -33   -250       C  
ATOM   4151  O   GLU C 171      -0.096 -56.016  22.168  1.00 13.82           O  
ANISOU 4151  O   GLU C 171     1918   1992   1342   -106    -39   -237       O  
ATOM   4152  CB  GLU C 171      -0.361 -59.151  23.024  1.00 13.82           C  
ANISOU 4152  CB  GLU C 171     1922   1926   1404   -108    -27   -332       C  
ATOM   4153  CG  GLU C 171       0.302 -60.493  22.757  1.00 14.80           C  
ANISOU 4153  CG  GLU C 171     2093   2007   1524   -104     23   -392       C  
ATOM   4154  CD  GLU C 171      -0.684 -61.602  22.438  1.00 15.53           C  
ANISOU 4154  CD  GLU C 171     2234   2074   1591   -149    -23   -421       C  
ATOM   4155  OE1 GLU C 171      -1.880 -61.480  22.784  1.00 17.51           O  
ANISOU 4155  OE1 GLU C 171     2455   2344   1856   -179    -94   -390       O  
ATOM   4156  OE2 GLU C 171      -0.253 -62.603  21.832  1.00 15.68           O  
ANISOU 4156  OE2 GLU C 171     2322   2056   1581   -156     15   -476       O  
ATOM   4157  N   GLY C 172      -0.639 -56.247  24.345  1.00 13.32           N  
ANISOU 4157  N   GLY C 172     1747   1910   1403    -63    -65   -219       N  
ATOM   4158  CA  GLY C 172      -1.267 -54.938  24.458  1.00 13.39           C  
ANISOU 4158  CA  GLY C 172     1736   1939   1413    -55   -104   -168       C  
ATOM   4159  C   GLY C 172      -0.277 -53.802  24.288  1.00 13.59           C  
ANISOU 4159  C   GLY C 172     1772   1963   1426    -45    -66   -148       C  
ATOM   4160  O   GLY C 172      -0.491 -52.892  23.484  1.00 13.86           O  
ANISOU 4160  O   GLY C 172     1843   2010   1415    -57    -86   -118       O  
ATOM   4161  N   VAL C 173       0.809 -53.847  25.052  1.00 13.58           N  
ANISOU 4161  N   VAL C 173     1743   1949   1468    -27    -15   -161       N  
ATOM   4162  CA  VAL C 173       1.819 -52.794  25.008  1.00 13.68           C  
ANISOU 4162  CA  VAL C 173     1756   1962   1478    -28     22   -142       C  
ATOM   4163  C   VAL C 173       2.484 -52.736  23.630  1.00 14.63           C  
ANISOU 4163  C   VAL C 173     1931   2096   1532    -57     63   -153       C  
ATOM   4164  O   VAL C 173       2.655 -51.663  23.061  1.00 14.69           O  
ANISOU 4164  O   VAL C 173     1970   2109   1503    -76     66   -121       O  
ATOM   4165  CB  VAL C 173       2.895 -52.984  26.119  1.00 13.63           C  
ANISOU 4165  CB  VAL C 173     1699   1945   1535     -9     58   -155       C  
ATOM   4166  CG1 VAL C 173       4.078 -52.045  25.898  1.00 13.04           C  
ANISOU 4166  CG1 VAL C 173     1622   1876   1457    -24    101   -141       C  
ATOM   4167  CG2 VAL C 173       2.282 -52.775  27.496  1.00 11.82           C  
ANISOU 4167  CG2 VAL C 173     1434   1702   1356     14     22   -138       C  
ATOM   4168  N   LEU C 174       2.827 -53.897  23.083  1.00 15.62           N  
ANISOU 4168  N   LEU C 174     2075   2222   1637    -63     97   -198       N  
ATOM   4169  CA  LEU C 174       3.558 -53.950  21.816  1.00 16.55           C  
ANISOU 4169  CA  LEU C 174     2248   2352   1688    -90    155   -218       C  
ATOM   4170  C   LEU C 174       2.676 -53.850  20.567  1.00 17.55           C  
ANISOU 4170  C   LEU C 174     2457   2490   1721   -126    116   -211       C  
ATOM   4171  O   LEU C 174       3.198 -53.712  19.461  1.00 18.00           O  
ANISOU 4171  O   LEU C 174     2576   2559   1705   -155    162   -220       O  
ATOM   4172  CB  LEU C 174       4.414 -55.216  21.755  1.00 16.90           C  
ANISOU 4172  CB  LEU C 174     2282   2386   1751    -72    221   -276       C  
ATOM   4173  CG  LEU C 174       5.460 -55.333  22.864  1.00 16.34           C  
ANISOU 4173  CG  LEU C 174     2129   2309   1770    -36    258   -279       C  
ATOM   4174  CD1 LEU C 174       6.267 -56.612  22.687  1.00 16.53           C  
ANISOU 4174  CD1 LEU C 174     2146   2318   1816     -7    322   -334       C  
ATOM   4175  CD2 LEU C 174       6.371 -54.118  22.889  1.00 15.67           C  
ANISOU 4175  CD2 LEU C 174     2015   2245   1695    -51    293   -247       C  
ATOM   4176  N   ASN C 175       1.357 -53.911  20.742  1.00 17.84           N  
ANISOU 4176  N   ASN C 175     2493   2527   1759   -126     31   -192       N  
ATOM   4177  CA  ASN C 175       0.401 -53.792  19.631  1.00 19.15           C  
ANISOU 4177  CA  ASN C 175     2727   2707   1841   -161    -30   -177       C  
ATOM   4178  C   ASN C 175       0.627 -54.843  18.544  1.00 20.46           C  
ANISOU 4178  C   ASN C 175     2971   2874   1930   -196      1   -231       C  
ATOM   4179  O   ASN C 175       0.650 -54.530  17.342  1.00 21.25           O  
ANISOU 4179  O   ASN C 175     3154   2987   1933   -234      2   -225       O  
ATOM   4180  CB  ASN C 175       0.438 -52.379  19.029  1.00 19.27           C  
ANISOU 4180  CB  ASN C 175     2782   2733   1809   -175    -44   -120       C  
ATOM   4181  CG  ASN C 175      -0.779 -52.069  18.172  1.00 19.86           C  
ANISOU 4181  CG  ASN C 175     2907   2821   1818   -198   -138    -84       C  
ATOM   4182  OD1 ASN C 175      -1.815 -52.727  18.268  1.00 18.36           O  
ANISOU 4182  OD1 ASN C 175     2698   2640   1640   -201   -205    -92       O  
ATOM   4183  ND2 ASN C 175      -0.652 -51.053  17.323  1.00 21.35           N  
ANISOU 4183  ND2 ASN C 175     3160   3013   1937   -219   -147    -40       N  
ATOM   4184  N   LYS C 176       0.803 -56.086  18.982  1.00 20.91           N  
ANISOU 4184  N   LYS C 176     3010   2911   2026   -183     28   -283       N  
ATOM   4185  CA  LYS C 176       0.985 -57.215  18.081  1.00 22.55           C  
ANISOU 4185  CA  LYS C 176     3295   3105   2168   -210     61   -345       C  
ATOM   4186  C   LYS C 176       0.659 -58.512  18.809  1.00 22.95           C  
ANISOU 4186  C   LYS C 176     3320   3122   2278   -196     49   -386       C  
ATOM   4187  O   LYS C 176       0.672 -58.557  20.042  1.00 21.99           O  
ANISOU 4187  O   LYS C 176     3117   2990   2249   -159     43   -370       O  
ATOM   4188  CB  LYS C 176       2.427 -57.267  17.560  1.00 23.18           C  
ANISOU 4188  CB  LYS C 176     3403   3182   2222   -200    179   -380       C  
ATOM   4189  CG  LYS C 176       3.466 -57.632  18.619  1.00 23.13           C  
ANISOU 4189  CG  LYS C 176     3312   3158   2320   -145    247   -398       C  
ATOM   4190  CD  LYS C 176       4.867 -57.719  18.033  1.00 24.72           C  
ANISOU 4190  CD  LYS C 176     3526   3364   2503   -134    366   -433       C  
ATOM   4191  CE  LYS C 176       5.854 -58.251  19.058  1.00 24.70           C  
ANISOU 4191  CE  LYS C 176     3433   3343   2610    -74    420   -453       C  
ATOM   4192  NZ  LYS C 176       7.207 -58.510  18.492  1.00 26.13           N  
ANISOU 4192  NZ  LYS C 176     3610   3530   2787    -55    542   -493       N  
ATOM   4193  N   ASN C 177       0.376 -59.565  18.047  1.00 24.10           N  
ANISOU 4193  N   ASN C 177     3545   3247   2364   -230     46   -438       N  
ATOM   4194  CA  ASN C 177       0.211 -60.891  18.629  1.00 24.84           C  
ANISOU 4194  CA  ASN C 177     3634   3296   2508   -222     47   -482       C  
ATOM   4195  C   ASN C 177       1.572 -61.575  18.717  1.00 25.87           C  
ANISOU 4195  C   ASN C 177     3772   3390   2666   -174    157   -534       C  
ATOM   4196  O   ASN C 177       2.398 -61.427  17.819  1.00 26.49           O  
ANISOU 4196  O   ASN C 177     3902   3476   2686   -173    232   -562       O  
ATOM   4197  CB  ASN C 177      -0.782 -61.720  17.809  1.00 25.38           C  
ANISOU 4197  CB  ASN C 177     3789   3352   2503   -287    -16   -515       C  
ATOM   4198  CG  ASN C 177      -2.203 -61.182  17.900  1.00 24.94           C  
ANISOU 4198  CG  ASN C 177     3697   3334   2445   -327   -134   -460       C  
ATOM   4199  OD1 ASN C 177      -2.549 -60.470  18.844  1.00 23.92           O  
ANISOU 4199  OD1 ASN C 177     3471   3227   2389   -298   -164   -406       O  
ATOM   4200  ND2 ASN C 177      -3.033 -61.519  16.919  1.00 24.81           N  
ANISOU 4200  ND2 ASN C 177     3757   3327   2344   -395   -203   -474       N  
ATOM   4201  N   ILE C 178       1.807 -62.300  19.809  1.00 26.53           N  
ANISOU 4201  N   ILE C 178     3802   3437   2842   -132    168   -544       N  
ATOM   4202  CA  ILE C 178       3.079 -62.995  20.029  1.00 27.85           C  
ANISOU 4202  CA  ILE C 178     3960   3566   3056    -74    262   -586       C  
ATOM   4203  C   ILE C 178       2.952 -64.491  19.792  1.00 29.43           C  
ANISOU 4203  C   ILE C 178     4236   3698   3247    -76    277   -651       C  
ATOM   4204  O   ILE C 178       3.811 -65.098  19.152  1.00 30.63           O  
ANISOU 4204  O   ILE C 178     4442   3819   3378    -48    362   -709       O  
ATOM   4205  CB  ILE C 178       3.591 -62.786  21.467  1.00 27.01           C  
ANISOU 4205  CB  ILE C 178     3745   3457   3061    -18    263   -548       C  
ATOM   4206  CG1 ILE C 178       3.877 -61.305  21.716  1.00 26.50           C  
ANISOU 4206  CG1 ILE C 178     3613   3450   3006    -16    259   -492       C  
ATOM   4207  CG2 ILE C 178       4.853 -63.613  21.712  1.00 27.58           C  
ANISOU 4207  CG2 ILE C 178     3801   3489   3191     48    346   -588       C  
ATOM   4208  CD1 ILE C 178       4.315 -61.003  23.124  1.00 25.20           C  
ANISOU 4208  CD1 ILE C 178     3352   3285   2937     27    249   -454       C  
ATOM   4209  N   ASN C 179       1.880 -65.077  20.316  1.00 30.19           N  
ANISOU 4209  N   ASN C 179     4340   3769   3363   -109    198   -643       N  
ATOM   4210  CA  ASN C 179       1.672 -66.522  20.275  1.00 31.73           C  
ANISOU 4210  CA  ASN C 179     4608   3887   3560   -118    201   -698       C  
ATOM   4211  C   ASN C 179       2.958 -67.265  20.660  1.00 32.30           C  
ANISOU 4211  C   ASN C 179     4672   3902   3698    -33    291   -734       C  
ATOM   4212  O   ASN C 179       3.391 -67.181  21.814  1.00 31.90           O  
ANISOU 4212  O   ASN C 179     4534   3848   3739     19    290   -696       O  
ATOM   4213  CB  ASN C 179       1.125 -66.960  18.903  1.00 32.87           C  
ANISOU 4213  CB  ASN C 179     4879   4020   3591   -187    188   -751       C  
ATOM   4214  CG  ASN C 179       0.178 -68.157  18.999  1.00 34.52           C  
ANISOU 4214  CG  ASN C 179     5154   4167   3796   -242    129   -781       C  
ATOM   4215  OD1 ASN C 179       0.147 -68.862  20.013  1.00 35.89           O  
ANISOU 4215  OD1 ASN C 179     5297   4290   4051   -217    122   -774       O  
ATOM   4216  ND2 ASN C 179      -0.601 -68.387  17.940  1.00 35.37           N  
ANISOU 4216  ND2 ASN C 179     5359   4276   3804   -324     82   -812       N  
ATOM   4217  OXT ASN C 179       3.611 -67.930  19.850  1.00 33.69           O  
ANISOU 4217  OXT ASN C 179     4924   4038   3839    -12    366   -799       O  
TER    4218      ASN C 179                                                      
ATOM   4219  N   HIS D   0       2.321 -33.222  16.800  1.00 23.97           N  
ANISOU 4219  N   HIS D   0     3349   3048   2708    188    806    -42       N  
ATOM   4220  CA  HIS D   0       2.949 -32.064  17.493  1.00 23.85           C  
ANISOU 4220  CA  HIS D   0     3420   3035   2606    245    766    -74       C  
ATOM   4221  C   HIS D   0       3.395 -30.992  16.499  1.00 22.53           C  
ANISOU 4221  C   HIS D   0     3191   2881   2488    254    659   -113       C  
ATOM   4222  O   HIS D   0       3.208 -29.799  16.736  1.00 22.92           O  
ANISOU 4222  O   HIS D   0     3248   2933   2527    294    657   -149       O  
ATOM   4223  CB  HIS D   0       4.132 -32.536  18.330  1.00 24.46           C  
ANISOU 4223  CB  HIS D   0     3633   3094   2568    264    721    -58       C  
ATOM   4224  CG  HIS D   0       4.264 -31.823  19.635  1.00 25.79           C  
ANISOU 4224  CG  HIS D   0     3923   3253   2624    323    749    -78       C  
ATOM   4225  ND1 HIS D   0       3.187 -31.580  20.459  1.00 29.44           N  
ANISOU 4225  ND1 HIS D   0     4411   3715   3060    349    880    -77       N  
ATOM   4226  CD2 HIS D   0       5.346 -31.320  20.271  1.00 27.56           C  
ANISOU 4226  CD2 HIS D   0     4252   3466   2753    364    663   -103       C  
ATOM   4227  CE1 HIS D   0       3.596 -30.942  21.541  1.00 29.57           C  
ANISOU 4227  CE1 HIS D   0     4556   3720   2960    407    874   -102       C  
ATOM   4228  NE2 HIS D   0       4.902 -30.772  21.452  1.00 29.62           N  
ANISOU 4228  NE2 HIS D   0     4611   3719   2924    415    736   -120       N  
ATOM   4229  N   MET D   1       3.981 -31.422  15.389  1.00 20.91           N  
ANISOU 4229  N   MET D   1     2933   2679   2333    219    576   -105       N  
ATOM   4230  CA  MET D   1       4.317 -30.525  14.291  1.00 19.79           C  
ANISOU 4230  CA  MET D   1     2730   2547   2245    221    489   -131       C  
ATOM   4231  C   MET D   1       3.480 -30.901  13.072  1.00 18.71           C  
ANISOU 4231  C   MET D   1     2477   2423   2209    188    492   -125       C  
ATOM   4232  O   MET D   1       3.206 -32.079  12.840  1.00 18.21           O  
ANISOU 4232  O   MET D   1     2387   2357   2174    150    518   -100       O  
ATOM   4233  CB  MET D   1       5.805 -30.622  13.942  1.00 19.26           C  
ANISOU 4233  CB  MET D   1     2701   2470   2146    214    387   -130       C  
ATOM   4234  CG  MET D   1       6.733 -29.741  14.782  1.00 20.45           C  
ANISOU 4234  CG  MET D   1     2938   2607   2225    250    339   -156       C  
ATOM   4235  SD  MET D   1       8.328 -29.457  13.953  1.00 21.85           S  
ANISOU 4235  SD  MET D   1     3106   2776   2421    236    216   -166       S  
ATOM   4236  CE  MET D   1       8.980 -31.134  13.965  1.00 20.46           C  
ANISOU 4236  CE  MET D   1     2952   2599   2224    210    204   -126       C  
ATOM   4237  N   LYS D   2       3.058 -29.892  12.314  1.00 17.80           N  
ANISOU 4237  N   LYS D   2     2298   2316   2148    206    461   -150       N  
ATOM   4238  CA  LYS D   2       2.522 -30.117  10.973  1.00 17.24           C  
ANISOU 4238  CA  LYS D   2     2131   2257   2163    184    425   -150       C  
ATOM   4239  C   LYS D   2       3.676 -29.911   9.995  1.00 15.73           C  
ANISOU 4239  C   LYS D   2     1956   2060   1959    178    327   -149       C  
ATOM   4240  O   LYS D   2       4.274 -28.827   9.936  1.00 15.59           O  
ANISOU 4240  O   LYS D   2     1969   2035   1921    204    286   -163       O  
ATOM   4241  CB  LYS D   2       1.358 -29.168  10.666  1.00 17.81           C  
ANISOU 4241  CB  LYS D   2     2128   2339   2300    215    444   -176       C  
ATOM   4242  CG  LYS D   2       0.493 -29.623   9.483  1.00 18.47           C  
ANISOU 4242  CG  LYS D   2     2105   2435   2477    193    417   -178       C  
ATOM   4243  CD  LYS D   2      -0.521 -28.558   9.058  1.00 19.23           C  
ANISOU 4243  CD  LYS D   2     2128   2540   2640    236    409   -206       C  
ATOM   4244  CE  LYS D   2      -1.381 -29.051   7.897  1.00 19.49           C  
ANISOU 4244  CE  LYS D   2     2056   2584   2764    219    366   -213       C  
ATOM   4245  NZ  LYS D   2      -2.379 -28.032   7.448  1.00 20.23           N  
ANISOU 4245  NZ  LYS D   2     2075   2686   2927    269    345   -241       N  
ATOM   4246  N   ILE D   3       3.997 -30.957   9.242  1.00 14.76           N  
ANISOU 4246  N   ILE D   3     1816   1939   1854    142    296   -131       N  
ATOM   4247  CA  ILE D   3       5.177 -30.965   8.385  1.00 13.45           C  
ANISOU 4247  CA  ILE D   3     1672   1768   1672    135    222   -125       C  
ATOM   4248  C   ILE D   3       4.800 -31.112   6.919  1.00 12.81           C  
ANISOU 4248  C   ILE D   3     1531   1694   1643    125    177   -128       C  
ATOM   4249  O   ILE D   3       3.920 -31.903   6.567  1.00 13.22           O  
ANISOU 4249  O   ILE D   3     1532   1751   1740    104    191   -129       O  
ATOM   4250  CB  ILE D   3       6.120 -32.115   8.762  1.00 13.40           C  
ANISOU 4250  CB  ILE D   3     1716   1752   1625    111    218   -104       C  
ATOM   4251  CG1 ILE D   3       6.601 -31.963  10.207  1.00 14.35           C  
ANISOU 4251  CG1 ILE D   3     1911   1863   1679    129    245   -102       C  
ATOM   4252  CG2 ILE D   3       7.309 -32.172   7.809  1.00 12.60           C  
ANISOU 4252  CG2 ILE D   3     1622   1645   1519    106    151   -100       C  
ATOM   4253  CD1 ILE D   3       7.347 -33.185  10.720  1.00 14.25           C  
ANISOU 4253  CD1 ILE D   3     1951   1838   1626    115    245    -78       C  
ATOM   4254  N   CYS D   4       5.474 -30.342   6.070  1.00 11.69           N  
ANISOU 4254  N   CYS D   4     1401   1547   1494    141    123   -130       N  
ATOM   4255  CA  CYS D   4       5.296 -30.428   4.635  1.00 10.94           C  
ANISOU 4255  CA  CYS D   4     1274   1455   1426    141     75   -130       C  
ATOM   4256  C   CYS D   4       6.542 -31.030   4.028  1.00 10.13           C  
ANISOU 4256  C   CYS D   4     1209   1345   1294    124     46   -115       C  
ATOM   4257  O   CYS D   4       7.653 -30.608   4.337  1.00 10.07           O  
ANISOU 4257  O   CYS D   4     1241   1327   1257    128     41   -108       O  
ATOM   4258  CB  CYS D   4       5.060 -29.041   4.040  1.00 11.07           C  
ANISOU 4258  CB  CYS D   4     1286   1467   1454    178     46   -138       C  
ATOM   4259  SG  CYS D   4       4.661 -29.047   2.276  1.00 10.41           S  
ANISOU 4259  SG  CYS D   4     1179   1386   1390    192    -18   -138       S  
ATOM   4260  N   ILE D   5       6.363 -32.026   3.173  1.00  9.89           N  
ANISOU 4260  N   ILE D   5     1163   1318   1277    107     26   -114       N  
ATOM   4261  CA  ILE D   5       7.483 -32.616   2.449  1.00  9.43           C  
ANISOU 4261  CA  ILE D   5     1139   1252   1192     99      3   -103       C  
ATOM   4262  C   ILE D   5       7.238 -32.383   0.974  1.00  9.37           C  
ANISOU 4262  C   ILE D   5     1127   1246   1188    115    -40   -107       C  
ATOM   4263  O   ILE D   5       6.281 -32.923   0.426  1.00  9.83           O  
ANISOU 4263  O   ILE D   5     1155   1308   1271    111    -63   -123       O  
ATOM   4264  CB  ILE D   5       7.613 -34.138   2.688  1.00  9.13           C  
ANISOU 4264  CB  ILE D   5     1107   1208   1156     69     15    -99       C  
ATOM   4265  CG1 ILE D   5       7.809 -34.448   4.173  1.00  9.86           C  
ANISOU 4265  CG1 ILE D   5     1218   1295   1232     59     57    -89       C  
ATOM   4266  CG2 ILE D   5       8.777 -34.684   1.880  1.00  8.41           C  
ANISOU 4266  CG2 ILE D   5     1048   1107   1039     70     -6    -91       C  
ATOM   4267  CD1 ILE D   5       7.791 -35.935   4.500  1.00  8.57           C  
ANISOU 4267  CD1 ILE D   5     1068   1117   1072     32     76    -80       C  
ATOM   4268  N   THR D   6       8.071 -31.560   0.341  1.00  9.16           N  
ANISOU 4268  N   THR D   6     1134   1211   1137    135    -52    -95       N  
ATOM   4269  CA  THR D   6       7.991 -31.375  -1.104  1.00  9.49           C  
ANISOU 4269  CA  THR D   6     1194   1249   1161    156    -87    -93       C  
ATOM   4270  C   THR D   6       9.046 -32.244  -1.790  1.00  9.65           C  
ANISOU 4270  C   THR D   6     1251   1263   1152    148    -82    -84       C  
ATOM   4271  O   THR D   6      10.153 -32.436  -1.277  1.00  9.69           O  
ANISOU 4271  O   THR D   6     1267   1262   1152    135    -53    -72       O  
ATOM   4272  CB  THR D   6       8.184 -29.905  -1.539  1.00  9.78           C  
ANISOU 4272  CB  THR D   6     1256   1274   1187    187    -92    -79       C  
ATOM   4273  OG1 THR D   6       9.482 -29.447  -1.149  1.00  8.94           O  
ANISOU 4273  OG1 THR D   6     1174   1153   1072    176    -59    -61       O  
ATOM   4274  CG2 THR D   6       7.108 -28.994  -0.933  1.00  9.13           C  
ANISOU 4274  CG2 THR D   6     1140   1194   1135    205    -97    -91       C  
ATOM   4275  N   VAL D   7       8.682 -32.796  -2.935  1.00  9.76           N  
ANISOU 4275  N   VAL D   7     1283   1278   1149    160   -115    -94       N  
ATOM   4276  CA  VAL D   7       9.614 -33.548  -3.749  1.00  9.88           C  
ANISOU 4276  CA  VAL D   7     1342   1284   1129    162   -108    -90       C  
ATOM   4277  C   VAL D   7      10.179 -32.584  -4.777  1.00 10.07           C  
ANISOU 4277  C   VAL D   7     1415   1298   1113    194   -101    -68       C  
ATOM   4278  O   VAL D   7       9.429 -31.957  -5.531  1.00 10.88           O  
ANISOU 4278  O   VAL D   7     1537   1400   1197    223   -137    -70       O  
ATOM   4279  CB  VAL D   7       8.934 -34.742  -4.429  1.00 10.35           C  
ANISOU 4279  CB  VAL D   7     1407   1343   1185    159   -148   -118       C  
ATOM   4280  CG1 VAL D   7       9.839 -35.342  -5.503  1.00 10.68           C  
ANISOU 4280  CG1 VAL D   7     1509   1373   1177    176   -142   -116       C  
ATOM   4281  CG2 VAL D   7       8.574 -35.789  -3.390  1.00 10.13           C  
ANISOU 4281  CG2 VAL D   7     1337   1313   1199    120   -138   -131       C  
ATOM   4282  N   GLY D   8      11.501 -32.442  -4.789  1.00  9.46           N  
ANISOU 4282  N   GLY D   8     1357   1212   1027    191    -53    -46       N  
ATOM   4283  CA  GLY D   8      12.161 -31.552  -5.737  1.00  9.84           C  
ANISOU 4283  CA  GLY D   8     1453   1243   1042    215    -25    -18       C  
ATOM   4284  C   GLY D   8      11.959 -31.988  -7.181  1.00  9.99           C  
ANISOU 4284  C   GLY D   8     1537   1258    999    248    -43    -21       C  
ATOM   4285  O   GLY D   8      11.846 -33.174  -7.456  1.00  9.83           O  
ANISOU 4285  O   GLY D   8     1524   1244    966    247    -61    -46       O  
ATOM   4286  N   HIS D   9      11.897 -31.015  -8.091  1.00 10.33           N  
ANISOU 4286  N   HIS D   9     1636   1287   1002    281    -39      3       N  
ATOM   4287  CA  HIS D   9      11.882 -31.266  -9.536  1.00 10.99           C  
ANISOU 4287  CA  HIS D   9     1806   1363   1008    322    -47      6       C  
ATOM   4288  C   HIS D   9      10.532 -31.794 -10.030  1.00 11.34           C  
ANISOU 4288  C   HIS D   9     1862   1418   1027    346   -141    -32       C  
ATOM   4289  O   HIS D   9       9.560 -31.796  -9.282  1.00 11.49           O  
ANISOU 4289  O   HIS D   9     1816   1451   1099    329   -191    -55       O  
ATOM   4290  CB  HIS D   9      13.048 -32.186  -9.924  1.00 10.99           C  
ANISOU 4290  CB  HIS D   9     1830   1359    988    319     13      8       C  
ATOM   4291  CG  HIS D   9      14.366 -31.718  -9.398  1.00 11.15           C  
ANISOU 4291  CG  HIS D   9     1816   1368   1051    293     97     39       C  
ATOM   4292  ND1 HIS D   9      14.983 -30.578  -9.864  1.00 12.54           N  
ANISOU 4292  ND1 HIS D   9     2027   1520   1218    302    156     81       N  
ATOM   4293  CD2 HIS D   9      15.167 -32.210  -8.424  1.00 10.92           C  
ANISOU 4293  CD2 HIS D   9     1720   1345   1083    259    126     32       C  
ATOM   4294  CE1 HIS D   9      16.118 -30.398  -9.214  1.00 12.34           C  
ANISOU 4294  CE1 HIS D   9     1946   1487   1255    269    217     95       C  
ATOM   4295  NE2 HIS D   9      16.251 -31.373  -8.331  1.00 11.93           N  
ANISOU 4295  NE2 HIS D   9     1833   1455   1244    247    194     64       N  
ATOM   4296  N   SER D  10      10.466 -32.202 -11.299  1.00 11.95           N  
ANISOU 4296  N   SER D  10     2025   1489   1027    386   -165    -41       N  
ATOM   4297  CA  SER D  10       9.212 -32.681 -11.894  1.00 12.34           C  
ANISOU 4297  CA  SER D  10     2091   1545   1053    412   -269    -84       C  
ATOM   4298  C   SER D  10       9.469 -33.340 -13.236  1.00 12.98           C  
ANISOU 4298  C   SER D  10     2280   1615   1039    454   -284    -98       C  
ATOM   4299  O   SER D  10      10.600 -33.341 -13.724  1.00 13.01           O  
ANISOU 4299  O   SER D  10     2345   1606    991    467   -201    -69       O  
ATOM   4300  CB  SER D  10       8.237 -31.519 -12.094  1.00 12.65           C  
ANISOU 4300  CB  SER D  10     2136   1583   1090    447   -329    -74       C  
ATOM   4301  OG  SER D  10       8.779 -30.549 -12.972  1.00 13.29           O  
ANISOU 4301  OG  SER D  10     2315   1640   1095    492   -292    -27       O  
ATOM   4302  N   ILE D  11       8.417 -33.917 -13.812  1.00 13.41           N  
ANISOU 4302  N   ILE D  11     2352   1672   1072    475   -390   -147       N  
ATOM   4303  CA  ILE D  11       8.448 -34.400 -15.192  1.00 14.44           C  
ANISOU 4303  CA  ILE D  11     2603   1788   1096    529   -428   -168       C  
ATOM   4304  C   ILE D  11       7.589 -33.473 -16.045  1.00 15.26           C  
ANISOU 4304  C   ILE D  11     2774   1887   1138    591   -513   -163       C  
ATOM   4305  O   ILE D  11       6.373 -33.408 -15.872  1.00 15.54           O  
ANISOU 4305  O   ILE D  11     2751   1932   1222    593   -620   -199       O  
ATOM   4306  CB  ILE D  11       7.920 -35.848 -15.316  1.00 14.57           C  
ANISOU 4306  CB  ILE D  11     2604   1803   1129    511   -503   -237       C  
ATOM   4307  CG1 ILE D  11       8.860 -36.820 -14.594  1.00 13.64           C  
ANISOU 4307  CG1 ILE D  11     2443   1683   1058    462   -418   -239       C  
ATOM   4308  CG2 ILE D  11       7.781 -36.239 -16.790  1.00 14.93           C  
ANISOU 4308  CG2 ILE D  11     2786   1833   1055    575   -566   -269       C  
ATOM   4309  CD1 ILE D  11       8.261 -38.180 -14.334  1.00 13.58           C  
ANISOU 4309  CD1 ILE D  11     2392   1667   1102    425   -482   -300       C  
ATOM   4310  N   LEU D  12       8.231 -32.754 -16.961  1.00 16.13           N  
ANISOU 4310  N   LEU D  12     3005   1978   1144    644   -463   -116       N  
ATOM   4311  CA  LEU D  12       7.545 -31.792 -17.814  1.00 17.05           C  
ANISOU 4311  CA  LEU D  12     3208   2082   1187    714   -535   -100       C  
ATOM   4312  C   LEU D  12       6.676 -32.474 -18.869  1.00 18.27           C  
ANISOU 4312  C   LEU D  12     3442   2235   1265    768   -671   -160       C  
ATOM   4313  O   LEU D  12       6.770 -33.684 -19.095  1.00 18.59           O  
ANISOU 4313  O   LEU D  12     3493   2278   1294    754   -693   -212       O  
ATOM   4314  CB  LEU D  12       8.556 -30.882 -18.520  1.00 17.53           C  
ANISOU 4314  CB  LEU D  12     3393   2116   1153    754   -426    -26       C  
ATOM   4315  CG  LEU D  12       9.565 -30.095 -17.680  1.00 16.81           C  
ANISOU 4315  CG  LEU D  12     3244   2017   1128    705   -289     36       C  
ATOM   4316  CD1 LEU D  12      10.549 -29.388 -18.612  1.00 17.23           C  
ANISOU 4316  CD1 LEU D  12     3431   2034   1080    745   -180    104       C  
ATOM   4317  CD2 LEU D  12       8.862 -29.106 -16.767  1.00 15.88           C  
ANISOU 4317  CD2 LEU D  12     3032   1901   1101    686   -327     48       C  
ATOM   4318  N   LYS D  13       5.841 -31.666 -19.517  1.00 19.17           N  
ANISOU 4318  N   LYS D  13     3616   2341   1328    834   -769   -156       N  
ATOM   4319  CA  LYS D  13       4.934 -32.120 -20.566  1.00 20.36           C  
ANISOU 4319  CA  LYS D  13     3847   2487   1401    897   -922   -214       C  
ATOM   4320  C   LYS D  13       5.673 -32.860 -21.683  1.00 20.50           C  
ANISOU 4320  C   LYS D  13     4025   2487   1277    938   -893   -226       C  
ATOM   4321  O   LYS D  13       5.185 -33.865 -22.203  1.00 21.23           O  
ANISOU 4321  O   LYS D  13     4147   2579   1342    952   -997   -300       O  
ATOM   4322  CB  LYS D  13       4.180 -30.922 -21.136  1.00 21.55           C  
ANISOU 4322  CB  LYS D  13     4062   2625   1500    976  -1010   -188       C  
ATOM   4323  CG  LYS D  13       3.020 -31.295 -22.016  1.00 24.43           C  
ANISOU 4323  CG  LYS D  13     4475   2989   1817   1040  -1202   -258       C  
ATOM   4324  CD  LYS D  13       2.102 -30.100 -22.260  1.00 27.12           C  
ANISOU 4324  CD  LYS D  13     4829   3323   2152   1111  -1304   -238       C  
ATOM   4325  CE  LYS D  13       0.791 -30.554 -22.879  1.00 29.49           C  
ANISOU 4325  CE  LYS D  13     5122   3629   2453   1161  -1518   -324       C  
ATOM   4326  NZ  LYS D  13       0.152 -31.625 -22.041  1.00 29.61           N  
ANISOU 4326  NZ  LYS D  13     4952   3671   2628   1076  -1570   -404       N  
ATOM   4327  N   SER D  14       6.861 -32.369 -22.025  1.00 19.70           N  
ANISOU 4327  N   SER D  14     4022   2368   1093    956   -745   -155       N  
ATOM   4328  CA  SER D  14       7.724 -33.025 -23.005  1.00 19.86           C  
ANISOU 4328  CA  SER D  14     4191   2372    983    994   -680   -157       C  
ATOM   4329  C   SER D  14       8.184 -34.413 -22.570  1.00 18.85           C  
ANISOU 4329  C   SER D  14     3995   2254    913    936   -644   -211       C  
ATOM   4330  O   SER D  14       8.662 -35.184 -23.387  1.00 19.09           O  
ANISOU 4330  O   SER D  14     4140   2270    843    971   -623   -237       O  
ATOM   4331  CB  SER D  14       8.968 -32.173 -23.258  1.00 19.86           C  
ANISOU 4331  CB  SER D  14     4275   2351    920   1008   -501    -64       C  
ATOM   4332  OG  SER D  14       9.786 -32.131 -22.102  1.00 17.82           O  
ANISOU 4332  OG  SER D  14     3878   2104    790    924   -375    -33       O  
ATOM   4333  N   GLY D  15       8.075 -34.704 -21.278  1.00 17.67           N  
ANISOU 4333  N   GLY D  15     3669   2124    919    851   -631   -223       N  
ATOM   4334  CA  GLY D  15       8.603 -35.930 -20.704  1.00 17.04           C  
ANISOU 4334  CA  GLY D  15     3519   2049    906    793   -582   -260       C  
ATOM   4335  C   GLY D  15       9.987 -35.744 -20.111  1.00 16.21           C  
ANISOU 4335  C   GLY D  15     3378   1945    836    756   -406   -199       C  
ATOM   4336  O   GLY D  15      10.505 -36.646 -19.461  1.00 15.57           O  
ANISOU 4336  O   GLY D  15     3223   1867    824    707   -357   -219       O  
ATOM   4337  N   ALA D  16      10.589 -34.576 -20.326  1.00 16.65           N  
ANISOU 4337  N   ALA D  16     3483   1994    851    779   -313   -125       N  
ATOM   4338  CA  ALA D  16      11.875 -34.252 -19.721  1.00 16.03           C  
ANISOU 4338  CA  ALA D  16     3351   1913    825    739   -153    -68       C  
ATOM   4339  C   ALA D  16      11.707 -34.174 -18.211  1.00 14.97           C  
ANISOU 4339  C   ALA D  16     3044   1800    845    661   -159    -69       C  
ATOM   4340  O   ALA D  16      10.745 -33.586 -17.726  1.00 14.34           O  
ANISOU 4340  O   ALA D  16     2904   1730    816    649   -241    -73       O  
ATOM   4341  CB  ALA D  16      12.397 -32.929 -20.256  1.00 16.71           C  
ANISOU 4341  CB  ALA D  16     3522   1979    848    774    -64     11       C  
ATOM   4342  N   CYS D  17      12.625 -34.801 -17.481  1.00 14.65           N  
ANISOU 4342  N   CYS D  17     2926   1764    874    614    -74    -69       N  
ATOM   4343  CA  CYS D  17      12.666 -34.706 -16.031  1.00 13.96           C  
ANISOU 4343  CA  CYS D  17     2692   1693    918    545    -64    -64       C  
ATOM   4344  C   CYS D  17      13.745 -33.690 -15.650  1.00 13.61           C  
ANISOU 4344  C   CYS D  17     2620   1642    909    526     56      1       C  
ATOM   4345  O   CYS D  17      14.864 -33.751 -16.151  1.00 14.06           O  
ANISOU 4345  O   CYS D  17     2722   1685    933    541    161     28       O  
ATOM   4346  CB  CYS D  17      12.959 -36.075 -15.417  1.00 13.80           C  
ANISOU 4346  CB  CYS D  17     2609   1680    956    508    -62   -106       C  
ATOM   4347  SG  CYS D  17      12.987 -36.093 -13.617  1.00 14.07           S  
ANISOU 4347  SG  CYS D  17     2483   1731   1133    432    -54   -102       S  
ATOM   4348  N   THR D  18      13.401 -32.759 -14.763  1.00 13.04           N  
ANISOU 4348  N   THR D  18     2471   1575    910    494     41     23       N  
ATOM   4349  CA  THR D  18      14.287 -31.645 -14.414  1.00 12.67           C  
ANISOU 4349  CA  THR D  18     2400   1512    901    474    137     80       C  
ATOM   4350  C   THR D  18      15.353 -31.995 -13.370  1.00 12.31           C  
ANISOU 4350  C   THR D  18     2252   1474    952    420    207     83       C  
ATOM   4351  O   THR D  18      16.251 -31.191 -13.111  1.00 12.36           O  
ANISOU 4351  O   THR D  18     2231   1464   1001    399    289    123       O  
ATOM   4352  CB  THR D  18      13.467 -30.453 -13.885  1.00 12.55           C  
ANISOU 4352  CB  THR D  18     2352   1493    922    466     85     98       C  
ATOM   4353  OG1 THR D  18      12.707 -30.862 -12.738  1.00 10.64           O  
ANISOU 4353  OG1 THR D  18     2007   1277    760    428     13     57       O  
ATOM   4354  CG2 THR D  18      12.521 -29.938 -14.966  1.00 13.07           C  
ANISOU 4354  CG2 THR D  18     2525   1547    895    528     17    104       C  
ATOM   4355  N   SER D  19      15.254 -33.181 -12.777  1.00 11.98           N  
ANISOU 4355  N   SER D  19     2153   1450    946    399    170     39       N  
ATOM   4356  CA  SER D  19      16.161 -33.603 -11.705  1.00 11.68           C  
ANISOU 4356  CA  SER D  19     2021   1420    997    357    215     36       C  
ATOM   4357  C   SER D  19      17.483 -34.150 -12.229  1.00 12.23           C  
ANISOU 4357  C   SER D  19     2109   1480   1058    371    311     46       C  
ATOM   4358  O   SER D  19      17.622 -34.457 -13.408  1.00 13.08           O  
ANISOU 4358  O   SER D  19     2310   1578   1084    415    342     46       O  
ATOM   4359  CB  SER D  19      15.502 -34.698 -10.858  1.00 10.83           C  
ANISOU 4359  CB  SER D  19     1857   1329    928    333    140    -10       C  
ATOM   4360  OG  SER D  19      15.659 -35.973 -11.469  1.00 11.50           O  
ANISOU 4360  OG  SER D  19     1985   1410    973    355    137    -41       O  
ATOM   4361  N   ALA D  20      18.441 -34.300 -11.324  1.00 12.19           N  
ANISOU 4361  N   ALA D  20     2015   1478   1139    339    353     50       N  
ATOM   4362  CA  ALA D  20      19.690 -34.986 -11.629  1.00 12.50           C  
ANISOU 4362  CA  ALA D  20     2044   1511   1194    353    437     51       C  
ATOM   4363  C   ALA D  20      19.405 -36.462 -11.925  1.00 12.49           C  
ANISOU 4363  C   ALA D  20     2080   1514   1152    380    398      6       C  
ATOM   4364  O   ALA D  20      18.380 -37.006 -11.516  1.00 11.48           O  
ANISOU 4364  O   ALA D  20     1950   1394   1018    369    307    -26       O  
ATOM   4365  CB  ALA D  20      20.668 -34.851 -10.456  1.00 12.20           C  
ANISOU 4365  CB  ALA D  20     1892   1476   1269    314    463     57       C  
ATOM   4366  N   ASP D  21      20.316 -37.103 -12.646  1.00 13.46           N  
ANISOU 4366  N   ASP D  21     2236   1627   1252    414    475      2       N  
ATOM   4367  CA  ASP D  21      20.148 -38.499 -13.021  1.00 13.85           C  
ANISOU 4367  CA  ASP D  21     2331   1671   1261    445    446    -43       C  
ATOM   4368  C   ASP D  21      21.491 -39.187 -13.148  1.00 14.74           C  
ANISOU 4368  C   ASP D  21     2417   1775   1408    470    538    -45       C  
ATOM   4369  O   ASP D  21      22.409 -38.633 -13.737  1.00 15.35           O  
ANISOU 4369  O   ASP D  21     2500   1846   1485    488    644    -14       O  
ATOM   4370  CB  ASP D  21      19.418 -38.593 -14.361  1.00 14.47           C  
ANISOU 4370  CB  ASP D  21     2542   1741   1217    491    426    -57       C  
ATOM   4371  CG  ASP D  21      18.968 -40.001 -14.678  1.00 14.92           C  
ANISOU 4371  CG  ASP D  21     2650   1786   1234    514    367   -115       C  
ATOM   4372  OD1 ASP D  21      18.144 -40.549 -13.919  1.00 14.58           O  
ANISOU 4372  OD1 ASP D  21     2564   1745   1230    481    273   -145       O  
ATOM   4373  OD2 ASP D  21      19.430 -40.553 -15.693  1.00 16.92           O  
ANISOU 4373  OD2 ASP D  21     2989   2023   1415    566    419   -131       O  
ATOM   4374  N   GLY D  22      21.592 -40.405 -12.619  1.00 14.90           N  
ANISOU 4374  N   GLY D  22     2409   1791   1462    473    500    -81       N  
ATOM   4375  CA  GLY D  22      22.824 -41.187 -12.709  1.00 15.67           C  
ANISOU 4375  CA  GLY D  22     2479   1878   1599    506    576    -90       C  
ATOM   4376  C   GLY D  22      22.546 -42.667 -12.578  1.00 15.81           C  
ANISOU 4376  C   GLY D  22     2525   1877   1605    526    521   -138       C  
ATOM   4377  O   GLY D  22      21.883 -43.254 -13.436  1.00 16.10           O  
ANISOU 4377  O   GLY D  22     2663   1899   1557    554    491   -171       O  
ATOM   4378  N   VAL D  23      23.043 -43.276 -11.503  1.00 15.74           N  
ANISOU 4378  N   VAL D  23     2434   1865   1684    514    499   -144       N  
ATOM   4379  CA  VAL D  23      22.713 -44.669 -11.209  1.00 16.05           C  
ANISOU 4379  CA  VAL D  23     2498   1877   1722    526    440   -184       C  
ATOM   4380  C   VAL D  23      21.261 -44.775 -10.701  1.00 15.62           C  
ANISOU 4380  C   VAL D  23     2464   1821   1649    479    332   -197       C  
ATOM   4381  O   VAL D  23      20.653 -45.846 -10.756  1.00 16.19           O  
ANISOU 4381  O   VAL D  23     2584   1865   1703    481    279   -233       O  
ATOM   4382  CB  VAL D  23      23.725 -45.319 -10.231  1.00 16.12           C  
ANISOU 4382  CB  VAL D  23     2423   1878   1824    537    450   -183       C  
ATOM   4383  CG1 VAL D  23      25.122 -45.298 -10.834  1.00 16.50           C  
ANISOU 4383  CG1 VAL D  23     2442   1926   1900    589    559   -177       C  
ATOM   4384  CG2 VAL D  23      23.715 -44.631  -8.866  1.00 16.04           C  
ANISOU 4384  CG2 VAL D  23     2318   1888   1887    488    404   -154       C  
ATOM   4385  N   VAL D  24      20.717 -43.660 -10.218  1.00 14.98           N  
ANISOU 4385  N   VAL D  24     2344   1767   1582    436    306   -169       N  
ATOM   4386  CA  VAL D  24      19.287 -43.544  -9.923  1.00 14.66           C  
ANISOU 4386  CA  VAL D  24     2319   1730   1523    395    218   -180       C  
ATOM   4387  C   VAL D  24      18.798 -42.178 -10.401  1.00 14.17           C  
ANISOU 4387  C   VAL D  24     2269   1692   1424    386    222   -156       C  
ATOM   4388  O   VAL D  24      19.580 -41.227 -10.500  1.00 14.16           O  
ANISOU 4388  O   VAL D  24     2240   1704   1435    391    287   -122       O  
ATOM   4389  CB  VAL D  24      19.002 -43.701  -8.418  1.00 14.10           C  
ANISOU 4389  CB  VAL D  24     2174   1660   1522    351    171   -170       C  
ATOM   4390  CG1 VAL D  24      19.619 -42.559  -7.633  1.00 14.35           C  
ANISOU 4390  CG1 VAL D  24     2131   1719   1603    333    199   -132       C  
ATOM   4391  CG2 VAL D  24      17.487 -43.795  -8.146  1.00 14.28           C  
ANISOU 4391  CG2 VAL D  24     2210   1680   1535    311     93   -186       C  
ATOM   4392  N   ASN D  25      17.512 -42.083 -10.710  1.00 13.58           N  
ANISOU 4392  N   ASN D  25     2234   1618   1310    372    151   -175       N  
ATOM   4393  CA  ASN D  25      16.910 -40.797 -11.013  1.00 13.11           C  
ANISOU 4393  CA  ASN D  25     2182   1578   1222    365    137   -153       C  
ATOM   4394  C   ASN D  25      16.503 -40.114  -9.719  1.00 12.18           C  
ANISOU 4394  C   ASN D  25     1978   1477   1172    317    109   -131       C  
ATOM   4395  O   ASN D  25      15.770 -40.692  -8.922  1.00 11.85           O  
ANISOU 4395  O   ASN D  25     1904   1432   1167    286     54   -149       O  
ATOM   4396  CB  ASN D  25      15.697 -40.948 -11.923  1.00 13.33           C  
ANISOU 4396  CB  ASN D  25     2284   1599   1181    379     63   -186       C  
ATOM   4397  CG  ASN D  25      15.148 -39.614 -12.373  1.00 13.55           C  
ANISOU 4397  CG  ASN D  25     2334   1643   1172    387     49   -160       C  
ATOM   4398  OD1 ASN D  25      15.676 -38.988 -13.289  1.00 17.19           O  
ANISOU 4398  OD1 ASN D  25     2858   2102   1570    425    104   -137       O  
ATOM   4399  ND2 ASN D  25      14.084 -39.176 -11.740  1.00 11.14           N  
ANISOU 4399  ND2 ASN D  25     1979   1350    904    355    -19   -163       N  
ATOM   4400  N   GLU D  26      16.975 -38.883  -9.533  1.00 11.83           N  
ANISOU 4400  N   GLU D  26     1904   1447   1145    311    151    -93       N  
ATOM   4401  CA  GLU D  26      16.706 -38.101  -8.324  1.00 11.45           C  
ANISOU 4401  CA  GLU D  26     1782   1412   1155    272    130    -75       C  
ATOM   4402  C   GLU D  26      15.212 -37.941  -8.043  1.00 11.18           C  
ANISOU 4402  C   GLU D  26     1745   1386   1118    252     54    -91       C  
ATOM   4403  O   GLU D  26      14.765 -38.181  -6.927  1.00 11.05           O  
ANISOU 4403  O   GLU D  26     1676   1373   1147    220     25    -97       O  
ATOM   4404  CB  GLU D  26      17.371 -36.720  -8.441  1.00 11.52           C  
ANISOU 4404  CB  GLU D  26     1777   1425   1176    272    185    -37       C  
ATOM   4405  CG  GLU D  26      16.906 -35.699  -7.416  1.00 10.80           C  
ANISOU 4405  CG  GLU D  26     1633   1343   1129    239    156    -23       C  
ATOM   4406  CD  GLU D  26      17.568 -34.335  -7.592  1.00 11.26           C  
ANISOU 4406  CD  GLU D  26     1683   1393   1203    236    209     12       C  
ATOM   4407  OE1 GLU D  26      18.090 -34.031  -8.690  1.00 10.57           O  
ANISOU 4407  OE1 GLU D  26     1644   1293   1078    261    267     33       O  
ATOM   4408  OE2 GLU D  26      17.562 -33.559  -6.619  1.00 12.47           O  
ANISOU 4408  OE2 GLU D  26     1786   1547   1405    209    196     20       O  
ATOM   4409  N   TYR D  27      14.448 -37.532  -9.052  1.00 11.56           N  
ANISOU 4409  N   TYR D  27     1847   1434   1110    275     24    -98       N  
ATOM   4410  CA  TYR D  27      13.003 -37.336  -8.884  1.00 11.33           C  
ANISOU 4410  CA  TYR D  27     1804   1412   1088    261    -53   -117       C  
ATOM   4411  C   TYR D  27      12.290 -38.637  -8.530  1.00 11.07           C  
ANISOU 4411  C   TYR D  27     1752   1370   1083    238   -103   -157       C  
ATOM   4412  O   TYR D  27      11.473 -38.661  -7.615  1.00 11.15           O  
ANISOU 4412  O   TYR D  27     1705   1387   1145    204   -132   -163       O  
ATOM   4413  CB  TYR D  27      12.382 -36.716 -10.142  1.00 11.96           C  
ANISOU 4413  CB  TYR D  27     1953   1491   1099    301    -88   -120       C  
ATOM   4414  CG  TYR D  27      10.866 -36.652 -10.134  1.00 11.37           C  
ANISOU 4414  CG  TYR D  27     1859   1424   1039    295   -180   -149       C  
ATOM   4415  CD1 TYR D  27      10.198 -35.651  -9.442  1.00 11.13           C  
ANISOU 4415  CD1 TYR D  27     1772   1406   1051    282   -197   -135       C  
ATOM   4416  CD2 TYR D  27      10.100 -37.584 -10.837  1.00 12.44           C  
ANISOU 4416  CD2 TYR D  27     2027   1549   1151    305   -252   -196       C  
ATOM   4417  CE1 TYR D  27       8.798 -35.575  -9.448  1.00 11.25           C  
ANISOU 4417  CE1 TYR D  27     1756   1429   1091    282   -278   -164       C  
ATOM   4418  CE2 TYR D  27       8.698 -37.521 -10.843  1.00 12.20           C  
ANISOU 4418  CE2 TYR D  27     1961   1524   1150    298   -341   -228       C  
ATOM   4419  CZ  TYR D  27       8.056 -36.506 -10.146  1.00 11.92           C  
ANISOU 4419  CZ  TYR D  27     1862   1506   1163    288   -351   -210       C  
ATOM   4420  OH  TYR D  27       6.673 -36.429 -10.133  1.00 12.37           O  
ANISOU 4420  OH  TYR D  27     1870   1569   1262    285   -434   -242       O  
ATOM   4421  N   GLN D  28      12.588 -39.716  -9.249  1.00 11.70           N  
ANISOU 4421  N   GLN D  28     1884   1431   1130    255   -106   -183       N  
ATOM   4422  CA  GLN D  28      11.934 -41.002  -8.996  1.00 12.03           C  
ANISOU 4422  CA  GLN D  28     1916   1453   1201    230   -153   -222       C  
ATOM   4423  C   GLN D  28      12.248 -41.489  -7.594  1.00 11.47           C  
ANISOU 4423  C   GLN D  28     1783   1377   1197    192   -123   -207       C  
ATOM   4424  O   GLN D  28      11.359 -41.975  -6.899  1.00 11.29           O  
ANISOU 4424  O   GLN D  28     1721   1345   1221    154   -155   -221       O  
ATOM   4425  CB  GLN D  28      12.351 -42.068 -10.011  1.00 12.71           C  
ANISOU 4425  CB  GLN D  28     2079   1512   1239    260   -156   -256       C  
ATOM   4426  CG  GLN D  28      11.876 -41.801 -11.426  1.00 13.60           C  
ANISOU 4426  CG  GLN D  28     2272   1623   1272    302   -202   -281       C  
ATOM   4427  CD  GLN D  28      10.366 -41.794 -11.568  1.00 14.42           C  
ANISOU 4427  CD  GLN D  28     2356   1727   1396    283   -304   -318       C  
ATOM   4428  OE1 GLN D  28       9.645 -42.426 -10.792  1.00 15.06           O  
ANISOU 4428  OE1 GLN D  28     2374   1797   1551    235   -338   -338       O  
ATOM   4429  NE2 GLN D  28       9.881 -41.078 -12.570  1.00 15.59           N  
ANISOU 4429  NE2 GLN D  28     2559   1885   1481    323   -351   -325       N  
ATOM   4430  N   TYR D  29      13.506 -41.343  -7.179  1.00 11.37           N  
ANISOU 4430  N   TYR D  29     1763   1369   1189    203    -62   -178       N  
ATOM   4431  CA  TYR D  29      13.921 -41.819  -5.867  1.00 11.30           C  
ANISOU 4431  CA  TYR D  29     1710   1353   1232    179    -42   -163       C  
ATOM   4432  C   TYR D  29      13.202 -41.058  -4.742  1.00 10.94           C  
ANISOU 4432  C   TYR D  29     1609   1326   1223    145    -53   -146       C  
ATOM   4433  O   TYR D  29      12.711 -41.667  -3.797  1.00 11.18           O  
ANISOU 4433  O   TYR D  29     1616   1344   1287    115    -62   -147       O  
ATOM   4434  CB  TYR D  29      15.445 -41.743  -5.671  1.00 11.29           C  
ANISOU 4434  CB  TYR D  29     1702   1354   1236    204     14   -140       C  
ATOM   4435  CG  TYR D  29      15.818 -42.204  -4.279  1.00 11.20           C  
ANISOU 4435  CG  TYR D  29     1652   1335   1270    186     16   -126       C  
ATOM   4436  CD1 TYR D  29      15.920 -43.562  -3.980  1.00 12.88           C  
ANISOU 4436  CD1 TYR D  29     1884   1514   1494    187      8   -139       C  
ATOM   4437  CD2 TYR D  29      15.993 -41.294  -3.247  1.00 11.33           C  
ANISOU 4437  CD2 TYR D  29     1623   1370   1311    171     22   -102       C  
ATOM   4438  CE1 TYR D  29      16.217 -43.995  -2.692  1.00 11.62           C  
ANISOU 4438  CE1 TYR D  29     1706   1344   1367    176      7   -121       C  
ATOM   4439  CE2 TYR D  29      16.283 -41.720  -1.950  1.00 11.57           C  
ANISOU 4439  CE2 TYR D  29     1635   1393   1369    161     16    -91       C  
ATOM   4440  CZ  TYR D  29      16.395 -43.068  -1.686  1.00 11.61           C  
ANISOU 4440  CZ  TYR D  29     1665   1367   1381    166      9    -97       C  
ATOM   4441  OH  TYR D  29      16.685 -43.494  -0.415  1.00 12.29           O  
ANISOU 4441  OH  TYR D  29     1746   1439   1483    163      2    -81       O  
ATOM   4442  N   ASN D  30      13.132 -39.737  -4.850  1.00 10.91           N  
ANISOU 4442  N   ASN D  30     1590   1346   1210    152    -47   -129       N  
ATOM   4443  CA  ASN D  30      12.467 -38.928  -3.817  1.00 10.91           C  
ANISOU 4443  CA  ASN D  30     1542   1362   1240    128    -54   -116       C  
ATOM   4444  C   ASN D  30      10.932 -39.016  -3.851  1.00 11.33           C  
ANISOU 4444  C   ASN D  30     1575   1417   1312    108    -96   -138       C  
ATOM   4445  O   ASN D  30      10.273 -38.813  -2.830  1.00 11.68           O  
ANISOU 4445  O   ASN D  30     1579   1467   1391     83    -93   -133       O  
ATOM   4446  CB  ASN D  30      12.965 -37.482  -3.879  1.00 10.67           C  
ANISOU 4446  CB  ASN D  30     1503   1347   1202    142    -32    -93       C  
ATOM   4447  CG  ASN D  30      14.424 -37.359  -3.474  1.00 10.37           C  
ANISOU 4447  CG  ASN D  30     1457   1307   1176    149      9    -74       C  
ATOM   4448  OD1 ASN D  30      15.219 -36.680  -4.132  1.00 10.66           O  
ANISOU 4448  OD1 ASN D  30     1505   1344   1202    167     40    -59       O  
ATOM   4449  ND2 ASN D  30      14.789 -38.029  -2.387  1.00  9.88           N  
ANISOU 4449  ND2 ASN D  30     1376   1240   1140    136     10    -73       N  
ATOM   4450  N   LYS D  31      10.374 -39.358  -5.011  1.00 11.78           N  
ANISOU 4450  N   LYS D  31     1661   1467   1347    120   -137   -165       N  
ATOM   4451  CA  LYS D  31       8.951 -39.700  -5.129  1.00 12.30           C  
ANISOU 4451  CA  LYS D  31     1698   1528   1446     99   -189   -196       C  
ATOM   4452  C   LYS D  31       8.636 -40.944  -4.288  1.00 12.33           C  
ANISOU 4452  C   LYS D  31     1679   1508   1499     56   -180   -205       C  
ATOM   4453  O   LYS D  31       7.589 -41.025  -3.648  1.00 12.34           O  
ANISOU 4453  O   LYS D  31     1627   1508   1553     23   -186   -212       O  
ATOM   4454  CB  LYS D  31       8.596 -39.940  -6.604  1.00 12.89           C  
ANISOU 4454  CB  LYS D  31     1821   1595   1480    126   -247   -229       C  
ATOM   4455  CG  LYS D  31       7.123 -40.149  -6.911  1.00 13.82           C  
ANISOU 4455  CG  LYS D  31     1902   1709   1638    110   -321   -269       C  
ATOM   4456  CD  LYS D  31       6.903 -40.343  -8.421  1.00 14.76           C  
ANISOU 4456  CD  LYS D  31     2088   1819   1701    148   -391   -305       C  
ATOM   4457  CE  LYS D  31       5.536 -40.935  -8.727  1.00 15.84           C  
ANISOU 4457  CE  LYS D  31     2184   1942   1892    124   -478   -358       C  
ATOM   4458  NZ  LYS D  31       5.362 -41.234 -10.176  1.00 15.80           N  
ANISOU 4458  NZ  LYS D  31     2256   1924   1824    164   -560   -402       N  
ATOM   4459  N   SER D  32       9.553 -41.907  -4.284  1.00 12.33           N  
ANISOU 4459  N   SER D  32     1718   1483   1483     59   -157   -203       N  
ATOM   4460  CA  SER D  32       9.405 -43.110  -3.468  1.00 12.59           C  
ANISOU 4460  CA  SER D  32     1745   1483   1557     23   -142   -204       C  
ATOM   4461  C   SER D  32       9.687 -42.838  -1.988  1.00 12.05           C  
ANISOU 4461  C   SER D  32     1650   1422   1505      9    -93   -165       C  
ATOM   4462  O   SER D  32       8.977 -43.334  -1.117  1.00 12.48           O  
ANISOU 4462  O   SER D  32     1682   1459   1600    -28    -77   -160       O  
ATOM   4463  CB  SER D  32      10.325 -44.227  -3.981  1.00 13.00           C  
ANISOU 4463  CB  SER D  32     1855   1501   1584     42   -138   -215       C  
ATOM   4464  OG  SER D  32      10.003 -44.567  -5.328  1.00 14.08           O  
ANISOU 4464  OG  SER D  32     2028   1626   1696     57   -186   -256       O  
ATOM   4465  N   LEU D  33      10.723 -42.054  -1.709  1.00 11.46           N  
ANISOU 4465  N   LEU D  33     1583   1370   1400     38    -69   -141       N  
ATOM   4466  CA  LEU D  33      11.125 -41.776  -0.335  1.00 11.12           C  
ANISOU 4466  CA  LEU D  33     1529   1333   1363     33    -36   -111       C  
ATOM   4467  C   LEU D  33      10.112 -40.932   0.460  1.00 10.85           C  
ANISOU 4467  C   LEU D  33     1455   1319   1349     13    -25   -104       C  
ATOM   4468  O   LEU D  33       9.902 -41.188   1.646  1.00 10.60           O  
ANISOU 4468  O   LEU D  33     1423   1279   1328     -4      4    -87       O  
ATOM   4469  CB  LEU D  33      12.501 -41.100  -0.304  1.00 10.65           C  
ANISOU 4469  CB  LEU D  33     1478   1290   1278     67    -24    -94       C  
ATOM   4470  CG  LEU D  33      13.045 -40.725   1.082  1.00 11.10           C  
ANISOU 4470  CG  LEU D  33     1529   1353   1336     69     -8    -71       C  
ATOM   4471  CD1 LEU D  33      13.075 -41.936   2.011  1.00 10.45           C  
ANISOU 4471  CD1 LEU D  33     1474   1240   1257     59      1    -59       C  
ATOM   4472  CD2 LEU D  33      14.433 -40.091   0.961  1.00 10.94           C  
ANISOU 4472  CD2 LEU D  33     1504   1344   1309     98     -6    -63       C  
ATOM   4473  N   ALA D  34       9.498 -39.940  -0.182  1.00 10.74           N  
ANISOU 4473  N   ALA D  34     1414   1329   1337     21    -45   -117       N  
ATOM   4474  CA  ALA D  34       8.624 -38.984   0.518  1.00 10.92           C  
ANISOU 4474  CA  ALA D  34     1397   1372   1381     13    -33   -113       C  
ATOM   4475  C   ALA D  34       7.512 -39.626   1.354  1.00 11.38           C  
ANISOU 4475  C   ALA D  34     1425   1417   1483    -24     -7   -115       C  
ATOM   4476  O   ALA D  34       7.373 -39.307   2.532  1.00 11.29           O  
ANISOU 4476  O   ALA D  34     1409   1411   1472    -29     34    -97       O  
ATOM   4477  CB  ALA D  34       8.033 -37.961  -0.463  1.00 11.10           C  
ANISOU 4477  CB  ALA D  34     1399   1415   1405     33    -68   -129       C  
ATOM   4478  N   PRO D  35       6.709 -40.523   0.755  1.00 12.25           N  
ANISOU 4478  N   PRO D  35     1515   1507   1632    -51    -28   -137       N  
ATOM   4479  CA  PRO D  35       5.657 -41.189   1.542  1.00 12.72           C  
ANISOU 4479  CA  PRO D  35     1538   1547   1748    -94      8   -137       C  
ATOM   4480  C   PRO D  35       6.178 -42.032   2.716  1.00 12.86           C  
ANISOU 4480  C   PRO D  35     1600   1536   1751   -110     64   -103       C  
ATOM   4481  O   PRO D  35       5.494 -42.143   3.736  1.00 13.25           O  
ANISOU 4481  O   PRO D  35     1633   1577   1826   -135    120    -87       O  
ATOM   4482  CB  PRO D  35       4.938 -42.070   0.508  1.00 13.16           C  
ANISOU 4482  CB  PRO D  35     1571   1579   1853   -121    -40   -173       C  
ATOM   4483  CG  PRO D  35       5.883 -42.201  -0.625  1.00 12.92           C  
ANISOU 4483  CG  PRO D  35     1593   1546   1768    -88    -89   -186       C  
ATOM   4484  CD  PRO D  35       6.664 -40.928  -0.661  1.00 12.39           C  
ANISOU 4484  CD  PRO D  35     1544   1516   1647    -43    -86   -168       C  
ATOM   4485  N   VAL D  36       7.377 -42.602   2.588  1.00 12.55           N  
ANISOU 4485  N   VAL D  36     1620   1480   1669    -91     52    -92       N  
ATOM   4486  CA  VAL D  36       7.982 -43.352   3.697  1.00 12.34           C  
ANISOU 4486  CA  VAL D  36     1645   1424   1618    -93     92    -59       C  
ATOM   4487  C   VAL D  36       8.464 -42.398   4.796  1.00 11.92           C  
ANISOU 4487  C   VAL D  36     1610   1398   1520    -66    118    -35       C  
ATOM   4488  O   VAL D  36       8.270 -42.663   5.981  1.00 12.11           O  
ANISOU 4488  O   VAL D  36     1663   1407   1531    -74    165     -9       O  
ATOM   4489  CB  VAL D  36       9.156 -44.236   3.223  1.00 12.40           C  
ANISOU 4489  CB  VAL D  36     1706   1405   1600    -72     65    -58       C  
ATOM   4490  CG1 VAL D  36       9.767 -44.993   4.401  1.00 12.09           C  
ANISOU 4490  CG1 VAL D  36     1725   1333   1535    -65     97    -22       C  
ATOM   4491  CG2 VAL D  36       8.684 -45.220   2.156  1.00 12.86           C  
ANISOU 4491  CG2 VAL D  36     1761   1431   1696    -97     38    -88       C  
ATOM   4492  N   LEU D  37       9.096 -41.291   4.401  1.00 11.06           N  
ANISOU 4492  N   LEU D  37     1492   1325   1388    -33     87    -45       N  
ATOM   4493  CA  LEU D  37       9.482 -40.256   5.358  1.00 10.44           C  
ANISOU 4493  CA  LEU D  37     1425   1268   1274    -10     99    -32       C  
ATOM   4494  C   LEU D  37       8.251 -39.722   6.096  1.00 10.45           C  
ANISOU 4494  C   LEU D  37     1399   1280   1292    -25    145    -31       C  
ATOM   4495  O   LEU D  37       8.298 -39.496   7.297  1.00 10.10           O  
ANISOU 4495  O   LEU D  37     1388   1234   1214    -16    179    -15       O  
ATOM   4496  CB  LEU D  37      10.210 -39.107   4.657  1.00 10.02           C  
ANISOU 4496  CB  LEU D  37     1355   1243   1210     18     62    -46       C  
ATOM   4497  CG  LEU D  37      10.736 -37.987   5.555  1.00  9.76           C  
ANISOU 4497  CG  LEU D  37     1335   1226   1149     41     63    -41       C  
ATOM   4498  CD1 LEU D  37      11.655 -38.538   6.639  1.00  9.26           C  
ANISOU 4498  CD1 LEU D  37     1322   1146   1049     55     61    -24       C  
ATOM   4499  CD2 LEU D  37      11.448 -36.918   4.720  1.00  9.15           C  
ANISOU 4499  CD2 LEU D  37     1238   1165   1075     59     32    -52       C  
ATOM   4500  N   ALA D  38       7.161 -39.530   5.362  1.00 10.54           N  
ANISOU 4500  N   ALA D  38     1351   1301   1354    -44    142    -52       N  
ATOM   4501  CA  ALA D  38       5.915 -39.018   5.932  1.00 11.18           C  
ANISOU 4501  CA  ALA D  38     1387   1392   1467    -57    188    -56       C  
ATOM   4502  C   ALA D  38       5.373 -39.968   6.993  1.00 11.55           C  
ANISOU 4502  C   ALA D  38     1454   1410   1524    -87    260    -32       C  
ATOM   4503  O   ALA D  38       5.081 -39.556   8.113  1.00 11.51           O  
ANISOU 4503  O   ALA D  38     1468   1409   1495    -78    317    -17       O  
ATOM   4504  CB  ALA D  38       4.879 -38.804   4.836  1.00 11.31           C  
ANISOU 4504  CB  ALA D  38     1329   1420   1548    -69    157    -86       C  
ATOM   4505  N   ASP D  39       5.262 -41.241   6.633  1.00 12.02           N  
ANISOU 4505  N   ASP D  39     1518   1435   1615   -121    259    -28       N  
ATOM   4506  CA  ASP D  39       4.784 -42.269   7.551  1.00 13.18           C  
ANISOU 4506  CA  ASP D  39     1690   1541   1776   -156    332      1       C  
ATOM   4507  C   ASP D  39       5.630 -42.344   8.818  1.00 13.20           C  
ANISOU 4507  C   ASP D  39     1787   1533   1694   -126    366     39       C  
ATOM   4508  O   ASP D  39       5.092 -42.559   9.911  1.00 13.85           O  
ANISOU 4508  O   ASP D  39     1900   1598   1765   -137    447     67       O  
ATOM   4509  CB  ASP D  39       4.765 -43.642   6.865  1.00 13.50           C  
ANISOU 4509  CB  ASP D  39     1735   1536   1860   -194    312     -2       C  
ATOM   4510  CG  ASP D  39       3.557 -43.839   5.974  1.00 15.39           C  
ANISOU 4510  CG  ASP D  39     1881   1770   2196   -237    297    -38       C  
ATOM   4511  OD1 ASP D  39       2.600 -43.031   6.047  1.00 18.82           O  
ANISOU 4511  OD1 ASP D  39     2243   2233   2673   -241    317    -53       O  
ATOM   4512  OD2 ASP D  39       3.554 -44.824   5.209  1.00 16.06           O  
ANISOU 4512  OD2 ASP D  39     1966   1819   2316   -265    260    -55       O  
ATOM   4513  N   THR D  40       6.942 -42.156   8.676  1.00 12.88           N  
ANISOU 4513  N   THR D  40     1795   1501   1597    -87    306     39       N  
ATOM   4514  CA  THR D  40       7.848 -42.236   9.822  1.00 12.99           C  
ANISOU 4514  CA  THR D  40     1898   1505   1532    -52    313     68       C  
ATOM   4515  C   THR D  40       7.593 -41.095  10.815  1.00 13.28           C  
ANISOU 4515  C   THR D  40     1952   1570   1525    -26    346     68       C  
ATOM   4516  O   THR D  40       7.593 -41.326  12.024  1.00 13.65           O  
ANISOU 4516  O   THR D  40     2073   1599   1515    -12    395     97       O  
ATOM   4517  CB  THR D  40       9.329 -42.262   9.393  1.00 12.55           C  
ANISOU 4517  CB  THR D  40     1871   1454   1444    -15    234     61       C  
ATOM   4518  OG1 THR D  40       9.527 -43.290   8.413  1.00 12.77           O  
ANISOU 4518  OG1 THR D  40     1887   1455   1511    -33    209     56       O  
ATOM   4519  CG2 THR D  40      10.220 -42.538  10.591  1.00 12.63           C  
ANISOU 4519  CG2 THR D  40     1972   1446   1381     23    229     89       C  
ATOM   4520  N   PHE D  41       7.374 -39.879  10.307  1.00 12.95           N  
ANISOU 4520  N   PHE D  41     1850   1566   1503    -16    321     37       N  
ATOM   4521  CA  PHE D  41       6.956 -38.751  11.155  1.00 13.40           C  
ANISOU 4521  CA  PHE D  41     1916   1646   1530      8    357     29       C  
ATOM   4522  C   PHE D  41       5.571 -38.983  11.754  1.00 14.51           C  
ANISOU 4522  C   PHE D  41     2036   1777   1700    -17    457     42       C  
ATOM   4523  O   PHE D  41       5.332 -38.675  12.925  1.00 14.59           O  
ANISOU 4523  O   PHE D  41     2101   1786   1658      3    518     55       O  
ATOM   4524  CB  PHE D  41       6.912 -37.436  10.367  1.00 12.95           C  
ANISOU 4524  CB  PHE D  41     1796   1623   1501     23    311     -6       C  
ATOM   4525  CG  PHE D  41       8.253 -36.798  10.162  1.00 12.21           C  
ANISOU 4525  CG  PHE D  41     1729   1538   1371     53    236    -17       C  
ATOM   4526  CD1 PHE D  41       8.978 -36.318  11.244  1.00 12.09           C  
ANISOU 4526  CD1 PHE D  41     1781   1521   1290     86    225    -17       C  
ATOM   4527  CD2 PHE D  41       8.776 -36.638   8.880  1.00 11.96           C  
ANISOU 4527  CD2 PHE D  41     1654   1515   1374     50    179    -31       C  
ATOM   4528  CE1 PHE D  41      10.213 -35.717  11.064  1.00 12.23           C  
ANISOU 4528  CE1 PHE D  41     1810   1544   1294    108    153    -32       C  
ATOM   4529  CE2 PHE D  41      10.016 -36.033   8.687  1.00 11.08           C  
ANISOU 4529  CE2 PHE D  41     1557   1409   1244     72    123    -40       C  
ATOM   4530  CZ  PHE D  41      10.735 -35.574   9.777  1.00 11.56           C  
ANISOU 4530  CZ  PHE D  41     1671   1466   1256     98    108    -42       C  
ATOM   4531  N   ARG D  42       4.654 -39.500  10.941  1.00 15.21           N  
ANISOU 4531  N   ARG D  42     2044   1860   1876    -60    474     34       N  
ATOM   4532  CA  ARG D  42       3.300 -39.782  11.408  1.00 16.52           C  
ANISOU 4532  CA  ARG D  42     2166   2014   2096    -93    572     44       C  
ATOM   4533  C   ARG D  42       3.335 -40.747  12.595  1.00 17.82           C  
ANISOU 4533  C   ARG D  42     2421   2137   2211   -104    656     91       C  
ATOM   4534  O   ARG D  42       2.599 -40.571  13.566  1.00 18.43           O  
ANISOU 4534  O   ARG D  42     2515   2211   2276   -102    756    108       O  
ATOM   4535  CB  ARG D  42       2.429 -40.327  10.267  1.00 16.68           C  
ANISOU 4535  CB  ARG D  42     2082   2027   2228   -142    555     23       C  
ATOM   4536  CG  ARG D  42       2.031 -39.272   9.234  1.00 15.89           C  
ANISOU 4536  CG  ARG D  42     1894   1967   2178   -126    491    -21       C  
ATOM   4537  CD  ARG D  42       1.132 -39.839   8.128  1.00 16.62           C  
ANISOU 4537  CD  ARG D  42     1887   2050   2376   -170    460    -47       C  
ATOM   4538  NE  ARG D  42       0.943 -38.862   7.049  1.00 15.20           N  
ANISOU 4538  NE  ARG D  42     1646   1906   2223   -142    378    -86       N  
ATOM   4539  CZ  ARG D  42       1.229 -39.051   5.757  1.00 15.22           C  
ANISOU 4539  CZ  ARG D  42     1634   1910   2240   -143    285   -109       C  
ATOM   4540  NH1 ARG D  42       1.710 -40.212   5.305  1.00 14.68           N  
ANISOU 4540  NH1 ARG D  42     1599   1810   2169   -172    258   -105       N  
ATOM   4541  NH2 ARG D  42       1.021 -38.059   4.892  1.00 13.24           N  
ANISOU 4541  NH2 ARG D  42     1342   1688   2001   -109    220   -137       N  
ATOM   4542  N   LYS D  43       4.222 -41.740  12.525  1.00 18.42           N  
ANISOU 4542  N   LYS D  43     2564   2181   2255   -108    618    114       N  
ATOM   4543  CA  LYS D  43       4.400 -42.716  13.605  1.00 19.72           C  
ANISOU 4543  CA  LYS D  43     2832   2298   2361   -110    685    164       C  
ATOM   4544  C   LYS D  43       4.771 -42.028  14.928  1.00 20.22           C  
ANISOU 4544  C   LYS D  43     2996   2373   2312    -55    717    180       C  
ATOM   4545  O   LYS D  43       4.407 -42.505  16.004  1.00 21.31           O  
ANISOU 4545  O   LYS D  43     3214   2481   2404    -54    812    222       O  
ATOM   4546  CB  LYS D  43       5.475 -43.737  13.204  1.00 19.73           C  
ANISOU 4546  CB  LYS D  43     2888   2266   2343   -107    614    178       C  
ATOM   4547  CG  LYS D  43       5.503 -45.028  14.008  1.00 21.70           C  
ANISOU 4547  CG  LYS D  43     3234   2451   2561   -121    677    233       C  
ATOM   4548  CD  LYS D  43       6.487 -46.014  13.379  1.00 22.89           C  
ANISOU 4548  CD  LYS D  43     3416   2566   2713   -117    598    237       C  
ATOM   4549  CE  LYS D  43       6.492 -47.373  14.067  1.00 24.54           C  
ANISOU 4549  CE  LYS D  43     3723   2700   2901   -132    657    293       C  
ATOM   4550  NZ  LYS D  43       7.378 -48.356  13.344  1.00 24.67           N  
ANISOU 4550  NZ  LYS D  43     3762   2679   2933   -126    580    291       N  
ATOM   4551  N   GLU D  44       5.480 -40.902  14.844  1.00 19.66           N  
ANISOU 4551  N   GLU D  44     2927   2343   2198     -9    640    147       N  
ATOM   4552  CA  GLU D  44       5.871 -40.140  16.032  1.00 19.97           C  
ANISOU 4552  CA  GLU D  44     3061   2394   2132     47    650    149       C  
ATOM   4553  C   GLU D  44       4.852 -39.059  16.429  1.00 20.03           C  
ANISOU 4553  C   GLU D  44     3031   2429   2150     56    724    127       C  
ATOM   4554  O   GLU D  44       5.157 -38.191  17.254  1.00 20.52           O  
ANISOU 4554  O   GLU D  44     3161   2504   2131    106    719    113       O  
ATOM   4555  CB  GLU D  44       7.259 -39.519  15.828  1.00 19.27           C  
ANISOU 4555  CB  GLU D  44     2999   2325   1997     90    525    121       C  
ATOM   4556  CG  GLU D  44       8.344 -40.517  15.448  1.00 19.66           C  
ANISOU 4556  CG  GLU D  44     3079   2350   2041     91    451    138       C  
ATOM   4557  CD  GLU D  44       8.487 -41.661  16.438  1.00 21.60           C  
ANISOU 4557  CD  GLU D  44     3440   2548   2218    103    495    189       C  
ATOM   4558  OE1 GLU D  44       8.541 -41.398  17.656  1.00 23.25           O  
ANISOU 4558  OE1 GLU D  44     3752   2751   2333    143    524    204       O  
ATOM   4559  OE2 GLU D  44       8.557 -42.826  15.996  1.00 22.43           O  
ANISOU 4559  OE2 GLU D  44     3544   2618   2361     75    498    214       O  
ATOM   4560  N   GLY D  45       3.650 -39.113  15.854  1.00 19.70           N  
ANISOU 4560  N   GLY D  45     2880   2392   2211     13    787    120       N  
ATOM   4561  CA  GLY D  45       2.536 -38.265  16.291  1.00 20.07           C  
ANISOU 4561  CA  GLY D  45     2884   2460   2281     22    877    104       C  
ATOM   4562  C   GLY D  45       2.316 -36.996  15.484  1.00 19.14           C  
ANISOU 4562  C   GLY D  45     2670   2383   2219     39    817     53       C  
ATOM   4563  O   GLY D  45       1.396 -36.231  15.767  1.00 19.58           O  
ANISOU 4563  O   GLY D  45     2681   2455   2302     54    883     35       O  
ATOM   4564  N   HIS D  46       3.140 -36.782  14.466  1.00 17.73           N  
ANISOU 4564  N   HIS D  46     2462   2217   2057     40    697     32       N  
ATOM   4565  CA  HIS D  46       3.089 -35.554  13.690  1.00 17.22           C  
ANISOU 4565  CA  HIS D  46     2328   2184   2030     61    634    -11       C  
ATOM   4566  C   HIS D  46       2.143 -35.725  12.502  1.00 17.15           C  
ANISOU 4566  C   HIS D  46     2192   2186   2140     24    625    -26       C  
ATOM   4567  O   HIS D  46       1.819 -36.849  12.108  1.00 16.98           O  
ANISOU 4567  O   HIS D  46     2137   2145   2170    -22    640    -10       O  
ATOM   4568  CB  HIS D  46       4.501 -35.176  13.227  1.00 16.50           C  
ANISOU 4568  CB  HIS D  46     2277   2099   1895     82    518    -23       C  
ATOM   4569  CG  HIS D  46       5.495 -35.127  14.345  1.00 16.42           C  
ANISOU 4569  CG  HIS D  46     2385   2076   1779    116    505    -13       C  
ATOM   4570  ND1 HIS D  46       5.567 -34.073  15.230  1.00 16.36           N  
ANISOU 4570  ND1 HIS D  46     2433   2074   1710    160    515    -34       N  
ATOM   4571  CD2 HIS D  46       6.432 -36.017  14.744  1.00 16.71           C  
ANISOU 4571  CD2 HIS D  46     2498   2091   1759    118    475     12       C  
ATOM   4572  CE1 HIS D  46       6.516 -34.311  16.118  1.00 17.06           C  
ANISOU 4572  CE1 HIS D  46     2628   2147   1707    186    485    -25       C  
ATOM   4573  NE2 HIS D  46       7.056 -35.485  15.845  1.00 16.99           N  
ANISOU 4573  NE2 HIS D  46     2632   2123   1701    163    460      5       N  
ATOM   4574  N   LYS D  47       1.678 -34.599  11.970  1.00 16.89           N  
ANISOU 4574  N   LYS D  47     2092   2177   2148     48    598    -59       N  
ATOM   4575  CA  LYS D  47       0.847 -34.573  10.775  1.00 16.99           C  
ANISOU 4575  CA  LYS D  47     1988   2201   2265     28    564    -81       C  
ATOM   4576  C   LYS D  47       1.704 -34.125   9.602  1.00 15.49           C  
ANISOU 4576  C   LYS D  47     1799   2022   2067     40    448    -96       C  
ATOM   4577  O   LYS D  47       2.503 -33.197   9.728  1.00 15.11           O  
ANISOU 4577  O   LYS D  47     1800   1978   1961     76    409   -104       O  
ATOM   4578  CB  LYS D  47      -0.350 -33.638  10.962  1.00 17.88           C  
ANISOU 4578  CB  LYS D  47     2025   2331   2435     54    615   -106       C  
ATOM   4579  CG  LYS D  47      -1.476 -34.252  11.791  1.00 20.66           C  
ANISOU 4579  CG  LYS D  47     2337   2675   2838     28    742    -92       C  
ATOM   4580  CD  LYS D  47      -2.742 -33.398  11.791  1.00 23.68           C  
ANISOU 4580  CD  LYS D  47     2617   3077   3305     54    789   -122       C  
ATOM   4581  CE  LYS D  47      -3.482 -33.431  10.440  1.00 25.19           C  
ANISOU 4581  CE  LYS D  47     2677   3279   3615     37    712   -150       C  
ATOM   4582  NZ  LYS D  47      -4.137 -34.750  10.153  1.00 27.02           N  
ANISOU 4582  NZ  LYS D  47     2835   3493   3940    -32    740   -142       N  
ATOM   4583  N   VAL D  48       1.546 -34.798   8.467  1.00 14.93           N  
ANISOU 4583  N   VAL D  48     1674   1947   2050     10    395   -102       N  
ATOM   4584  CA  VAL D  48       2.402 -34.578   7.308  1.00 13.76           C  
ANISOU 4584  CA  VAL D  48     1539   1804   1885     20    298   -110       C  
ATOM   4585  C   VAL D  48       1.584 -34.527   6.020  1.00 13.92           C  
ANISOU 4585  C   VAL D  48     1476   1834   1980     15    243   -136       C  
ATOM   4586  O   VAL D  48       0.693 -35.356   5.814  1.00 14.09           O  
ANISOU 4586  O   VAL D  48     1435   1847   2070    -20    258   -144       O  
ATOM   4587  CB  VAL D  48       3.444 -35.714   7.159  1.00 13.67           C  
ANISOU 4587  CB  VAL D  48     1586   1772   1834     -5    275    -90       C  
ATOM   4588  CG1 VAL D  48       4.402 -35.428   5.992  1.00 11.99           C  
ANISOU 4588  CG1 VAL D  48     1391   1566   1601     11    190    -98       C  
ATOM   4589  CG2 VAL D  48       4.211 -35.921   8.464  1.00 13.02           C  
ANISOU 4589  CG2 VAL D  48     1590   1679   1680      3    319    -65       C  
ATOM   4590  N   ASP D  49       1.886 -33.539   5.178  1.00 13.38           N  
ANISOU 4590  N   ASP D  49     1409   1776   1897     51    176   -149       N  
ATOM   4591  CA  ASP D  49       1.393 -33.488   3.801  1.00 13.50           C  
ANISOU 4591  CA  ASP D  49     1375   1798   1957     58    101   -170       C  
ATOM   4592  C   ASP D  49       2.584 -33.624   2.869  1.00 13.02           C  
ANISOU 4592  C   ASP D  49     1379   1731   1839     63     41   -161       C  
ATOM   4593  O   ASP D  49       3.606 -32.959   3.053  1.00 12.44           O  
ANISOU 4593  O   ASP D  49     1362   1655   1708     84     41   -146       O  
ATOM   4594  CB  ASP D  49       0.681 -32.164   3.502  1.00 13.73           C  
ANISOU 4594  CB  ASP D  49     1362   1841   2014    105     77   -188       C  
ATOM   4595  CG  ASP D  49      -0.590 -31.975   4.312  1.00 14.11           C  
ANISOU 4595  CG  ASP D  49     1333   1898   2132    107    140   -202       C  
ATOM   4596  OD1 ASP D  49      -1.209 -32.982   4.716  1.00 14.90           O  
ANISOU 4596  OD1 ASP D  49     1385   1992   2283     64    187   -203       O  
ATOM   4597  OD2 ASP D  49      -0.972 -30.807   4.538  1.00 13.06           O  
ANISOU 4597  OD2 ASP D  49     1184   1772   2007    153    147   -212       O  
ATOM   4598  N   VAL D  50       2.452 -34.504   1.883  1.00 13.31           N  
ANISOU 4598  N   VAL D  50     1404   1761   1894     44     -7   -173       N  
ATOM   4599  CA  VAL D  50       3.459 -34.663   0.846  1.00 13.12           C  
ANISOU 4599  CA  VAL D  50     1437   1730   1817     55    -59   -168       C  
ATOM   4600  C   VAL D  50       3.007 -33.901  -0.391  1.00 13.41           C  
ANISOU 4600  C   VAL D  50     1463   1776   1857     93   -130   -185       C  
ATOM   4601  O   VAL D  50       1.879 -34.075  -0.856  1.00 14.11           O  
ANISOU 4601  O   VAL D  50     1491   1868   2001     93   -170   -213       O  
ATOM   4602  CB  VAL D  50       3.664 -36.150   0.510  1.00 13.12           C  
ANISOU 4602  CB  VAL D  50     1451   1712   1823     18    -69   -173       C  
ATOM   4603  CG1 VAL D  50       4.614 -36.315  -0.661  1.00 13.74           C  
ANISOU 4603  CG1 VAL D  50     1589   1785   1848     37   -117   -174       C  
ATOM   4604  CG2 VAL D  50       4.185 -36.884   1.732  1.00 12.75           C  
ANISOU 4604  CG2 VAL D  50     1431   1651   1764    -11     -2   -150       C  
ATOM   4605  N   ILE D  51       3.877 -33.040  -0.909  1.00 13.52           N  
ANISOU 4605  N   ILE D  51     1533   1788   1814    127   -146   -169       N  
ATOM   4606  CA  ILE D  51       3.587 -32.278  -2.131  1.00 14.07           C  
ANISOU 4606  CA  ILE D  51     1619   1860   1869    170   -210   -176       C  
ATOM   4607  C   ILE D  51       4.504 -32.741  -3.257  1.00 14.20           C  
ANISOU 4607  C   ILE D  51     1705   1865   1823    177   -238   -168       C  
ATOM   4608  O   ILE D  51       5.719 -32.510  -3.226  1.00 13.95           O  
ANISOU 4608  O   ILE D  51     1727   1827   1747    179   -203   -142       O  
ATOM   4609  CB  ILE D  51       3.778 -30.755  -1.929  1.00 13.98           C  
ANISOU 4609  CB  ILE D  51     1625   1846   1840    209   -197   -158       C  
ATOM   4610  CG1 ILE D  51       3.002 -30.253  -0.703  1.00 14.76           C  
ANISOU 4610  CG1 ILE D  51     1666   1953   1989    208   -156   -167       C  
ATOM   4611  CG2 ILE D  51       3.353 -29.998  -3.167  1.00 14.07           C  
ANISOU 4611  CG2 ILE D  51     1659   1853   1834    259   -264   -161       C  
ATOM   4612  CD1 ILE D  51       1.524 -30.385  -0.812  1.00 15.93           C  
ANISOU 4612  CD1 ILE D  51     1731   2113   2207    217   -185   -196       C  
ATOM   4613  N   ILE D  52       3.927 -33.419  -4.244  1.00 15.08           N  
ANISOU 4613  N   ILE D  52     1816   1976   1939    182   -301   -195       N  
ATOM   4614  CA  ILE D  52       4.662 -33.796  -5.446  1.00 15.41           C  
ANISOU 4614  CA  ILE D  52     1936   2007   1913    201   -330   -193       C  
ATOM   4615  C   ILE D  52       4.002 -33.125  -6.645  1.00 15.79           C  
ANISOU 4615  C   ILE D  52     2010   2055   1934    253   -409   -206       C  
ATOM   4616  O   ILE D  52       2.770 -33.143  -6.775  1.00 16.01           O  
ANISOU 4616  O   ILE D  52     1979   2090   2014    261   -471   -238       O  
ATOM   4617  CB  ILE D  52       4.681 -35.324  -5.651  1.00 15.69           C  
ANISOU 4617  CB  ILE D  52     1973   2031   1958    166   -344   -220       C  
ATOM   4618  CG1 ILE D  52       5.091 -36.038  -4.367  1.00 16.03           C  
ANISOU 4618  CG1 ILE D  52     1986   2069   2035    118   -274   -207       C  
ATOM   4619  CG2 ILE D  52       5.634 -35.707  -6.771  1.00 15.85           C  
ANISOU 4619  CG2 ILE D  52     2083   2039   1899    190   -354   -216       C  
ATOM   4620  CD1 ILE D  52       5.196 -37.563  -4.520  1.00 16.62           C  
ANISOU 4620  CD1 ILE D  52     2071   2123   2120     84   -281   -228       C  
ATOM   4621  N   CYS D  53       4.816 -32.518  -7.504  1.00 15.53           N  
ANISOU 4621  N   CYS D  53     2065   2013   1824    291   -404   -179       N  
ATOM   4622  CA  CYS D  53       4.306 -31.797  -8.663  1.00 16.37           C  
ANISOU 4622  CA  CYS D  53     2221   2114   1885    351   -476   -181       C  
ATOM   4623  C   CYS D  53       3.609 -32.751  -9.632  1.00 16.76           C  
ANISOU 4623  C   CYS D  53     2284   2162   1922    363   -568   -228       C  
ATOM   4624  O   CYS D  53       4.061 -33.882  -9.817  1.00 15.91           O  
ANISOU 4624  O   CYS D  53     2199   2048   1798    336   -558   -245       O  
ATOM   4625  CB  CYS D  53       5.443 -31.079  -9.395  1.00 16.54           C  
ANISOU 4625  CB  CYS D  53     2347   2117   1820    384   -433   -136       C  
ATOM   4626  SG  CYS D  53       6.183 -29.713  -8.483  1.00 17.40           S  
ANISOU 4626  SG  CYS D  53     2447   2215   1947    377   -347    -87       S  
ATOM   4627  N   PRO D  54       2.494 -32.306 -10.239  1.00 17.61           N  
ANISOU 4627  N   PRO D  54     2379   2273   2041    407   -664   -253       N  
ATOM   4628  CA  PRO D  54       1.869 -33.097 -11.292  1.00 18.63           C  
ANISOU 4628  CA  PRO D  54     2533   2397   2148    427   -770   -302       C  
ATOM   4629  C   PRO D  54       2.883 -33.445 -12.377  1.00 18.78           C  
ANISOU 4629  C   PRO D  54     2689   2400   2047    455   -761   -290       C  
ATOM   4630  O   PRO D  54       3.757 -32.636 -12.683  1.00 18.56           O  
ANISOU 4630  O   PRO D  54     2743   2364   1945    486   -701   -239       O  
ATOM   4631  CB  PRO D  54       0.796 -32.158 -11.859  1.00 19.47           C  
ANISOU 4631  CB  PRO D  54     2630   2507   2261    491   -872   -316       C  
ATOM   4632  CG  PRO D  54       0.523 -31.178 -10.792  1.00 19.08           C  
ANISOU 4632  CG  PRO D  54     2501   2467   2282    485   -817   -289       C  
ATOM   4633  CD  PRO D  54       1.782 -31.040  -9.997  1.00 17.99           C  
ANISOU 4633  CD  PRO D  54     2388   2325   2121    445   -687   -240       C  
ATOM   4634  N   GLU D  55       2.763 -34.639 -12.941  1.00 19.61           N  
ANISOU 4634  N   GLU D  55     2817   2495   2137    443   -813   -337       N  
ATOM   4635  CA  GLU D  55       3.639 -35.072 -14.028  1.00 20.29           C  
ANISOU 4635  CA  GLU D  55     3038   2565   2105    477   -805   -334       C  
ATOM   4636  C   GLU D  55       3.008 -34.763 -15.384  1.00 21.74           C  
ANISOU 4636  C   GLU D  55     3314   2741   2205    553   -925   -360       C  
ATOM   4637  O   GLU D  55       1.792 -34.859 -15.544  1.00 22.36           O  
ANISOU 4637  O   GLU D  55     3335   2823   2338    563  -1045   -410       O  
ATOM   4638  CB  GLU D  55       3.955 -36.567 -13.898  1.00 20.17           C  
ANISOU 4638  CB  GLU D  55     3015   2538   2111    428   -792   -373       C  
ATOM   4639  CG  GLU D  55       4.862 -36.883 -12.703  1.00 19.06           C  
ANISOU 4639  CG  GLU D  55     2820   2400   2021    369   -668   -338       C  
ATOM   4640  CD  GLU D  55       5.046 -38.375 -12.442  1.00 19.47           C  
ANISOU 4640  CD  GLU D  55     2856   2434   2109    320   -660   -374       C  
ATOM   4641  OE1 GLU D  55       4.668 -39.197 -13.304  1.00 20.76           O  
ANISOU 4641  OE1 GLU D  55     3066   2578   2244    333   -739   -427       O  
ATOM   4642  OE2 GLU D  55       5.582 -38.729 -11.369  1.00 18.14           O  
ANISOU 4642  OE2 GLU D  55     2634   2265   1993    272   -577   -351       O  
ATOM   4643  N   LYS D  56       3.847 -34.369 -16.340  1.00 22.31           N  
ANISOU 4643  N   LYS D  56     3529   2799   2147    609   -891   -325       N  
ATOM   4644  CA  LYS D  56       3.426 -34.072 -17.714  1.00 23.81           C  
ANISOU 4644  CA  LYS D  56     3844   2977   2225    693   -995   -342       C  
ATOM   4645  C   LYS D  56       2.355 -32.975 -17.804  1.00 24.68           C  
ANISOU 4645  C   LYS D  56     3924   3094   2361    741  -1091   -338       C  
ATOM   4646  O   LYS D  56       1.474 -33.007 -18.670  1.00 25.76           O  
ANISOU 4646  O   LYS D  56     4103   3225   2459    798  -1234   -382       O  
ATOM   4647  CB  LYS D  56       3.003 -35.357 -18.437  1.00 24.55           C  
ANISOU 4647  CB  LYS D  56     3975   3059   2292    697  -1099   -421       C  
ATOM   4648  CG  LYS D  56       4.138 -36.380 -18.511  1.00 24.42           C  
ANISOU 4648  CG  LYS D  56     4016   3031   2234    668  -1002   -423       C  
ATOM   4649  CD  LYS D  56       3.873 -37.494 -19.511  1.00 25.44           C  
ANISOU 4649  CD  LYS D  56     4232   3137   2296    694  -1102   -497       C  
ATOM   4650  CE  LYS D  56       5.085 -38.407 -19.639  1.00 25.60           C  
ANISOU 4650  CE  LYS D  56     4322   3142   2265    679   -993   -494       C  
ATOM   4651  NZ  LYS D  56       4.795 -39.646 -20.415  1.00 26.62           N  
ANISOU 4651  NZ  LYS D  56     4519   3243   2351    692  -1088   -577       N  
ATOM   4652  N   GLN D  57       2.461 -31.994 -16.911  1.00 24.25           N  
ANISOU 4652  N   GLN D  57     3798   3046   2368    723  -1017   -287       N  
ATOM   4653  CA  GLN D  57       1.566 -30.839 -16.903  1.00 24.82           C  
ANISOU 4653  CA  GLN D  57     3842   3120   2469    773  -1087   -275       C  
ATOM   4654  C   GLN D  57       2.321 -29.534 -17.171  1.00 24.67           C  
ANISOU 4654  C   GLN D  57     3926   3079   2368    819  -1005   -194       C  
ATOM   4655  O   GLN D  57       1.825 -28.685 -17.912  1.00 25.70           O  
ANISOU 4655  O   GLN D  57     4133   3194   2438    897  -1081   -178       O  
ATOM   4656  CB  GLN D  57       0.821 -30.761 -15.570  1.00 24.39           C  
ANISOU 4656  CB  GLN D  57     3607   3087   2572    716  -1080   -294       C  
ATOM   4657  CG  GLN D  57      -0.189 -29.623 -15.478  1.00 25.75           C  
ANISOU 4657  CG  GLN D  57     3731   3261   2791    770  -1153   -289       C  
ATOM   4658  CD  GLN D  57      -0.882 -29.560 -14.134  1.00 25.59           C  
ANISOU 4658  CD  GLN D  57     3536   3263   2925    716  -1125   -308       C  
ATOM   4659  OE1 GLN D  57      -1.567 -30.500 -13.728  1.00 26.36           O  
ANISOU 4659  OE1 GLN D  57     3524   3377   3117    668  -1165   -364       O  
ATOM   4660  NE2 GLN D  57      -0.712 -28.443 -13.433  1.00 26.89           N  
ANISOU 4660  NE2 GLN D  57     3680   3423   3116    724  -1053   -261       N  
ATOM   4661  N   PHE D  58       3.507 -29.377 -16.580  1.00 23.55           N  
ANISOU 4661  N   PHE D  58     3787   2932   2228    770   -856   -143       N  
ATOM   4662  CA  PHE D  58       4.297 -28.150 -16.734  1.00 23.43           C  
ANISOU 4662  CA  PHE D  58     3857   2889   2158    798   -764    -65       C  
ATOM   4663  C   PHE D  58       4.962 -28.053 -18.104  1.00 24.59           C  
ANISOU 4663  C   PHE D  58     4186   3008   2151    859   -745    -31       C  
ATOM   4664  O   PHE D  58       5.509 -29.038 -18.612  1.00 24.80           O  
ANISOU 4664  O   PHE D  58     4268   3039   2118    851   -722    -52       O  
ATOM   4665  CB  PHE D  58       5.397 -28.038 -15.666  1.00 22.15           C  
ANISOU 4665  CB  PHE D  58     3632   2727   2058    723   -617    -28       C  
ATOM   4666  CG  PHE D  58       4.903 -28.078 -14.236  1.00 20.85           C  
ANISOU 4666  CG  PHE D  58     3308   2586   2028    664   -613    -53       C  
ATOM   4667  CD1 PHE D  58       3.613 -27.686 -13.892  1.00 20.63           C  
ANISOU 4667  CD1 PHE D  58     3201   2569   2067    685   -705    -84       C  
ATOM   4668  CD2 PHE D  58       5.768 -28.472 -13.224  1.00 19.71           C  
ANISOU 4668  CD2 PHE D  58     3097   2450   1940    592   -511    -45       C  
ATOM   4669  CE1 PHE D  58       3.184 -27.719 -12.572  1.00 20.41           C  
ANISOU 4669  CE1 PHE D  58     3036   2562   2157    634   -684   -104       C  
ATOM   4670  CE2 PHE D  58       5.351 -28.511 -11.900  1.00 19.30           C  
ANISOU 4670  CE2 PHE D  58     2918   2418   1997    543   -501    -65       C  
ATOM   4671  CZ  PHE D  58       4.055 -28.128 -11.569  1.00 19.73           C  
ANISOU 4671  CZ  PHE D  58     2901   2484   2114    563   -580    -93       C  
ATOM   4672  N   LYS D  59       4.919 -26.855 -18.688  1.00 25.39           N  
ANISOU 4672  N   LYS D  59     4386   3076   2184    924   -747     23       N  
ATOM   4673  CA  LYS D  59       5.630 -26.557 -19.937  1.00 26.44           C  
ANISOU 4673  CA  LYS D  59     4708   3175   2165    985   -700     73       C  
ATOM   4674  C   LYS D  59       7.114 -26.284 -19.667  1.00 25.80           C  
ANISOU 4674  C   LYS D  59     4649   3073   2081    934   -514    138       C  
ATOM   4675  O   LYS D  59       7.971 -26.605 -20.499  1.00 26.22           O  
ANISOU 4675  O   LYS D  59     4820   3110   2031    953   -437    163       O  
ATOM   4676  CB  LYS D  59       5.019 -25.335 -20.633  1.00 27.58           C  
ANISOU 4676  CB  LYS D  59     4956   3283   2238   1074   -768    114       C  
ATOM   4677  CG  LYS D  59       3.577 -25.509 -21.097  1.00 28.89           C  
ANISOU 4677  CG  LYS D  59     5116   3464   2395   1142   -966     52       C  
ATOM   4678  CD  LYS D  59       3.110 -24.288 -21.885  1.00 30.58           C  
ANISOU 4678  CD  LYS D  59     5460   3637   2523   1245  -1029    101       C  
ATOM   4679  CE  LYS D  59       1.781 -24.539 -22.590  1.00 32.33           C  
ANISOU 4679  CE  LYS D  59     5703   3871   2711   1328  -1239     37       C  
ATOM   4680  NZ  LYS D  59       1.491 -23.521 -23.642  1.00 33.84           N  
ANISOU 4680  NZ  LYS D  59     6071   4016   2772   1446  -1306     89       N  
ATOM   4681  N   THR D  60       7.408 -25.670 -18.518  1.00 24.52           N  
ANISOU 4681  N   THR D  60     4374   2909   2034    873   -443    162       N  
ATOM   4682  CA  THR D  60       8.783 -25.367 -18.118  1.00 23.95           C  
ANISOU 4682  CA  THR D  60     4295   2817   1989    817   -280    215       C  
ATOM   4683  C   THR D  60       8.975 -25.582 -16.617  1.00 22.74           C  
ANISOU 4683  C   THR D  60     3971   2690   1980    731   -246    190       C  
ATOM   4684  O   THR D  60       8.006 -25.637 -15.859  1.00 22.07           O  
ANISOU 4684  O   THR D  60     3785   2630   1972    720   -332    147       O  
ATOM   4685  CB  THR D  60       9.164 -23.909 -18.450  1.00 24.66           C  
ANISOU 4685  CB  THR D  60     4475   2850   2046    846   -211    296       C  
ATOM   4686  OG1 THR D  60       8.497 -23.011 -17.551  1.00 24.28           O  
ANISOU 4686  OG1 THR D  60     4339   2794   2093    835   -256    295       O  
ATOM   4687  CG2 THR D  60       8.798 -23.558 -19.893  1.00 26.08           C  
ANISOU 4687  CG2 THR D  60     4838   2998   2074    944   -259    326       C  
ATOM   4688  N   LYS D  61      10.232 -25.679 -16.195  1.00 22.44           N  
ANISOU 4688  N   LYS D  61     3904   2644   1977    674   -119    216       N  
ATOM   4689  CA  LYS D  61      10.560 -25.891 -14.784  1.00 21.67           C  
ANISOU 4689  CA  LYS D  61     3662   2568   2004    598    -86    195       C  
ATOM   4690  C   LYS D  61      10.185 -24.698 -13.898  1.00 21.33           C  
ANISOU 4690  C   LYS D  61     3560   2506   2038    584    -95    211       C  
ATOM   4691  O   LYS D  61      10.114 -24.830 -12.673  1.00 20.22           O  
ANISOU 4691  O   LYS D  61     3305   2387   1992    533    -97    183       O  
ATOM   4692  CB  LYS D  61      12.046 -26.228 -14.609  1.00 21.68           C  
ANISOU 4692  CB  LYS D  61     3648   2563   2027    549     43    218       C  
ATOM   4693  CG  LYS D  61      13.008 -25.099 -14.954  1.00 23.57           C  
ANISOU 4693  CG  LYS D  61     3948   2751   2258    545    154    288       C  
ATOM   4694  CD  LYS D  61      14.376 -25.320 -14.325  1.00 25.20           C  
ANISOU 4694  CD  LYS D  61     4078   2955   2542    480    265    299       C  
ATOM   4695  CE  LYS D  61      15.194 -24.034 -14.337  1.00 27.09           C  
ANISOU 4695  CE  LYS D  61     4339   3138   2817    457    364    361       C  
ATOM   4696  NZ  LYS D  61      16.664 -24.285 -14.205  1.00 28.24           N  
ANISOU 4696  NZ  LYS D  61     4438   3274   3018    408    486    379       N  
ATOM   4697  N   ASN D  62       9.950 -23.542 -14.519  1.00 21.98           N  
ANISOU 4697  N   ASN D  62     3731   2546   2076    632    -98    256       N  
ATOM   4698  CA  ASN D  62       9.523 -22.341 -13.794  1.00 22.23           C  
ANISOU 4698  CA  ASN D  62     3724   2549   2173    631   -113    271       C  
ATOM   4699  C   ASN D  62       8.203 -22.531 -13.051  1.00 21.48           C  
ANISOU 4699  C   ASN D  62     3533   2492   2137    642   -222    213       C  
ATOM   4700  O   ASN D  62       7.951 -21.858 -12.058  1.00 21.18           O  
ANISOU 4700  O   ASN D  62     3424   2446   2178    622   -221    206       O  
ATOM   4701  CB  ASN D  62       9.397 -21.145 -14.748  1.00 23.70           C  
ANISOU 4701  CB  ASN D  62     4040   2676   2287    695   -108    331       C  
ATOM   4702  CG  ASN D  62      10.723 -20.743 -15.371  1.00 25.49           C  
ANISOU 4702  CG  ASN D  62     4357   2854   2473    677     25    398       C  
ATOM   4703  OD1 ASN D  62      10.811 -20.525 -16.584  1.00 28.94           O  
ANISOU 4703  OD1 ASN D  62     4934   3261   2802    733     41    442       O  
ATOM   4704  ND2 ASN D  62      11.765 -20.642 -14.545  1.00 26.41           N  
ANISOU 4704  ND2 ASN D  62     4396   2962   2678    600    120    405       N  
ATOM   4705  N   GLU D  63       7.368 -23.449 -13.533  1.00 21.36           N  
ANISOU 4705  N   GLU D  63     3515   2514   2088    673   -314    169       N  
ATOM   4706  CA  GLU D  63       6.079 -23.731 -12.902  1.00 20.88           C  
ANISOU 4706  CA  GLU D  63     3352   2489   2094    680   -413    113       C  
ATOM   4707  C   GLU D  63       6.187 -24.546 -11.612  1.00 19.91           C  
ANISOU 4707  C   GLU D  63     3098   2403   2062    605   -383     72       C  
ATOM   4708  O   GLU D  63       5.207 -24.661 -10.879  1.00 19.87           O  
ANISOU 4708  O   GLU D  63     2999   2422   2127    601   -436     32       O  
ATOM   4709  CB  GLU D  63       5.151 -24.437 -13.890  1.00 21.77           C  
ANISOU 4709  CB  GLU D  63     3501   2622   2149    734   -529     76       C  
ATOM   4710  CG  GLU D  63       4.724 -23.559 -15.057  1.00 22.41           C  
ANISOU 4710  CG  GLU D  63     3708   2667   2141    825   -590    108       C  
ATOM   4711  CD  GLU D  63       4.071 -24.351 -16.167  1.00 23.42           C  
ANISOU 4711  CD  GLU D  63     3897   2811   2189    879   -703     71       C  
ATOM   4712  OE1 GLU D  63       3.085 -25.066 -15.890  1.00 23.56           O  
ANISOU 4712  OE1 GLU D  63     3818   2865   2268    874   -800      6       O  
ATOM   4713  OE2 GLU D  63       4.545 -24.258 -17.319  1.00 24.57           O  
ANISOU 4713  OE2 GLU D  63     4192   2931   2213    927   -693    106       O  
ATOM   4714  N   GLU D  64       7.355 -25.123 -11.334  1.00 19.17           N  
ANISOU 4714  N   GLU D  64     3001   2313   1968    551   -297     83       N  
ATOM   4715  CA  GLU D  64       7.576 -25.805 -10.052  1.00 18.22           C  
ANISOU 4715  CA  GLU D  64     2773   2222   1928    485   -264     53       C  
ATOM   4716  C   GLU D  64       7.399 -24.814  -8.891  1.00 17.88           C  
ANISOU 4716  C   GLU D  64     2669   2167   1957    469   -243     57       C  
ATOM   4717  O   GLU D  64       6.684 -25.098  -7.938  1.00 17.28           O  
ANISOU 4717  O   GLU D  64     2507   2117   1942    451   -267     21       O  
ATOM   4718  CB  GLU D  64       8.959 -26.462 -10.007  1.00 17.57           C  
ANISOU 4718  CB  GLU D  64     2704   2139   1833    440   -179     68       C  
ATOM   4719  CG  GLU D  64       9.088 -27.662 -10.951  1.00 17.89           C  
ANISOU 4719  CG  GLU D  64     2792   2195   1811    453   -198     51       C  
ATOM   4720  CD  GLU D  64      10.505 -28.206 -11.073  1.00 16.95           C  
ANISOU 4720  CD  GLU D  64     2694   2069   1676    423   -106     70       C  
ATOM   4721  OE1 GLU D  64      11.398 -27.766 -10.322  1.00 15.22           O  
ANISOU 4721  OE1 GLU D  64     2436   1840   1507    385    -36     92       O  
ATOM   4722  OE2 GLU D  64      10.723 -29.089 -11.935  1.00 17.75           O  
ANISOU 4722  OE2 GLU D  64     2850   2176   1716    441   -109     59       O  
ATOM   4723  N   LYS D  65       8.035 -23.649  -9.016  1.00 18.27           N  
ANISOU 4723  N   LYS D  65     2772   2173   1997    477   -195    101       N  
ATOM   4724  CA  LYS D  65       7.963 -22.563  -8.030  1.00 18.21           C  
ANISOU 4724  CA  LYS D  65     2728   2140   2050    467   -175    105       C  
ATOM   4725  C   LYS D  65       6.531 -22.057  -7.819  1.00 18.45           C  
ANISOU 4725  C   LYS D  65     2725   2178   2108    516   -249     79       C  
ATOM   4726  O   LYS D  65       6.078 -21.890  -6.687  1.00 18.13           O  
ANISOU 4726  O   LYS D  65     2610   2149   2130    501   -248     51       O  
ATOM   4727  CB  LYS D  65       8.869 -21.410  -8.496  1.00 18.90           C  
ANISOU 4727  CB  LYS D  65     2895   2167   2118    471   -115    159       C  
ATOM   4728  CG  LYS D  65       8.822 -20.140  -7.652  1.00 20.09           C  
ANISOU 4728  CG  LYS D  65     3030   2277   2326    467   -100    164       C  
ATOM   4729  CD  LYS D  65       9.982 -19.204  -7.985  1.00 21.85           C  
ANISOU 4729  CD  LYS D  65     3318   2435   2549    446    -24    216       C  
ATOM   4730  CE  LYS D  65       9.960 -17.957  -7.103  1.00 23.52           C  
ANISOU 4730  CE  LYS D  65     3516   2598   2823    437    -14    214       C  
ATOM   4731  NZ  LYS D  65      11.233 -17.163  -7.092  1.00 25.13           N  
ANISOU 4731  NZ  LYS D  65     3752   2738   3060    391     64    251       N  
ATOM   4732  N   SER D  66       5.837 -21.801  -8.922  1.00 18.75           N  
ANISOU 4732  N   SER D  66     2822   2205   2097    580   -313     90       N  
ATOM   4733  CA  SER D  66       4.451 -21.344  -8.892  1.00 19.22           C  
ANISOU 4733  CA  SER D  66     2847   2271   2186    638   -395     65       C  
ATOM   4734  C   SER D  66       3.519 -22.364  -8.250  1.00 18.43           C  
ANISOU 4734  C   SER D  66     2633   2226   2145    618   -438      6       C  
ATOM   4735  O   SER D  66       2.612 -21.996  -7.508  1.00 18.46           O  
ANISOU 4735  O   SER D  66     2560   2238   2215    634   -459    -21       O  
ATOM   4736  CB  SER D  66       3.977 -21.051 -10.313  1.00 20.25           C  
ANISOU 4736  CB  SER D  66     3071   2381   2241    714   -469     86       C  
ATOM   4737  OG  SER D  66       4.900 -20.206 -10.971  1.00 22.10           O  
ANISOU 4737  OG  SER D  66     3423   2561   2414    727   -413    148       O  
ATOM   4738  N   TYR D  67       3.758 -23.644  -8.531  1.00 17.80           N  
ANISOU 4738  N   TYR D  67     2542   2177   2045    584   -443    -12       N  
ATOM   4739  CA  TYR D  67       2.925 -24.719  -8.000  1.00 17.29           C  
ANISOU 4739  CA  TYR D  67     2375   2156   2039    557   -478    -64       C  
ATOM   4740  C   TYR D  67       3.112 -24.916  -6.496  1.00 16.26           C  
ANISOU 4740  C   TYR D  67     2163   2041   1975    499   -406    -77       C  
ATOM   4741  O   TYR D  67       2.139 -25.048  -5.755  1.00 16.47           O  
ANISOU 4741  O   TYR D  67     2099   2088   2070    497   -420   -111       O  
ATOM   4742  CB  TYR D  67       3.234 -26.036  -8.719  1.00 17.39           C  
ANISOU 4742  CB  TYR D  67     2413   2187   2008    534   -499    -78       C  
ATOM   4743  CG  TYR D  67       2.404 -27.181  -8.205  1.00 17.13           C  
ANISOU 4743  CG  TYR D  67     2278   2188   2042    498   -531   -130       C  
ATOM   4744  CD1 TYR D  67       1.123 -27.405  -8.691  1.00 18.44           C  
ANISOU 4744  CD1 TYR D  67     2396   2366   2242    532   -631   -170       C  
ATOM   4745  CD2 TYR D  67       2.888 -28.029  -7.214  1.00 16.96           C  
ANISOU 4745  CD2 TYR D  67     2207   2182   2057    431   -464   -138       C  
ATOM   4746  CE1 TYR D  67       0.347 -28.452  -8.214  1.00 18.53           C  
ANISOU 4746  CE1 TYR D  67     2306   2403   2331    491   -654   -217       C  
ATOM   4747  CE2 TYR D  67       2.116 -29.074  -6.727  1.00 17.16           C  
ANISOU 4747  CE2 TYR D  67     2144   2229   2146    394   -483   -179       C  
ATOM   4748  CZ  TYR D  67       0.844 -29.273  -7.230  1.00 17.74           C  
ANISOU 4748  CZ  TYR D  67     2165   2312   2263    421   -573   -218       C  
ATOM   4749  OH  TYR D  67       0.077 -30.305  -6.760  1.00 18.38           O  
ANISOU 4749  OH  TYR D  67     2152   2409   2422    377   -585   -258       O  
ATOM   4750  N   LYS D  68       4.366 -24.941  -6.052  1.00 15.19           N  
ANISOU 4750  N   LYS D  68     2059   1893   1818    455   -330    -52       N  
ATOM   4751  CA  LYS D  68       4.692 -25.352  -4.684  1.00 14.26           C  
ANISOU 4751  CA  LYS D  68     1882   1791   1745    401   -271    -66       C  
ATOM   4752  C   LYS D  68       4.474 -24.265  -3.638  1.00 13.92           C  
ANISOU 4752  C   LYS D  68     1814   1733   1743    410   -241    -68       C  
ATOM   4753  O   LYS D  68       3.906 -24.523  -2.572  1.00 13.71           O  
ANISOU 4753  O   LYS D  68     1721   1726   1763    394   -221    -95       O  
ATOM   4754  CB  LYS D  68       6.151 -25.821  -4.601  1.00 13.88           C  
ANISOU 4754  CB  LYS D  68     1873   1736   1665    356   -214    -44       C  
ATOM   4755  CG  LYS D  68       6.446 -27.134  -5.313  1.00 13.65           C  
ANISOU 4755  CG  LYS D  68     1858   1724   1603    339   -227    -50       C  
ATOM   4756  CD  LYS D  68       7.878 -27.595  -5.058  1.00 12.81           C  
ANISOU 4756  CD  LYS D  68     1775   1613   1481    299   -165    -32       C  
ATOM   4757  CE  LYS D  68       8.907 -26.695  -5.730  1.00 12.96           C  
ANISOU 4757  CE  LYS D  68     1862   1598   1465    312   -128      8       C  
ATOM   4758  NZ  LYS D  68      10.240 -27.355  -5.860  1.00 12.39           N  
ANISOU 4758  NZ  LYS D  68     1806   1523   1378    281    -76     22       N  
ATOM   4759  N   ILE D  69       4.955 -23.062  -3.925  1.00 13.69           N  
ANISOU 4759  N   ILE D  69     1845   1663   1694    436   -230    -39       N  
ATOM   4760  CA  ILE D  69       5.052 -22.022  -2.893  1.00 13.54           C  
ANISOU 4760  CA  ILE D  69     1818   1618   1707    437   -195    -43       C  
ATOM   4761  C   ILE D  69       3.700 -21.649  -2.268  1.00 13.96           C  
ANISOU 4761  C   ILE D  69     1809   1684   1811    475   -216    -76       C  
ATOM   4762  O   ILE D  69       3.594 -21.603  -1.041  1.00 14.01           O  
ANISOU 4762  O   ILE D  69     1778   1698   1848    457   -176    -98       O  
ATOM   4763  CB  ILE D  69       5.813 -20.777  -3.409  1.00 13.68           C  
ANISOU 4763  CB  ILE D  69     1917   1579   1704    454   -180     -5       C  
ATOM   4764  CG1 ILE D  69       7.302 -21.108  -3.585  1.00 12.81           C  
ANISOU 4764  CG1 ILE D  69     1843   1455   1568    401   -132     22       C  
ATOM   4765  CG2 ILE D  69       5.640 -19.586  -2.450  1.00 13.89           C  
ANISOU 4765  CG2 ILE D  69     1940   1570   1769    468   -162    -17       C  
ATOM   4766  CD1 ILE D  69       8.039 -21.383  -2.284  1.00 11.44           C  
ANISOU 4766  CD1 ILE D  69     1632   1290   1426    348    -92      1       C  
ATOM   4767  N   PRO D  70       2.663 -21.402  -3.093  1.00 14.12           N  
ANISOU 4767  N   PRO D  70     1818   1706   1839    531   -278    -80       N  
ATOM   4768  CA  PRO D  70       1.347 -21.089  -2.521  1.00 14.63           C  
ANISOU 4768  CA  PRO D  70     1807   1785   1967    571   -295   -115       C  
ATOM   4769  C   PRO D  70       0.750 -22.231  -1.700  1.00 14.48           C  
ANISOU 4769  C   PRO D  70     1694   1813   1994    532   -270   -150       C  
ATOM   4770  O   PRO D  70       0.059 -21.983  -0.712  1.00 14.82           O  
ANISOU 4770  O   PRO D  70     1679   1865   2088    542   -235   -175       O  
ATOM   4771  CB  PRO D  70       0.480 -20.813  -3.756  1.00 15.34           C  
ANISOU 4771  CB  PRO D  70     1904   1870   2056    637   -383   -113       C  
ATOM   4772  CG  PRO D  70       1.426 -20.510  -4.836  1.00 15.30           C  
ANISOU 4772  CG  PRO D  70     2008   1832   1974    644   -397    -68       C  
ATOM   4773  CD  PRO D  70       2.640 -21.335  -4.559  1.00 14.38           C  
ANISOU 4773  CD  PRO D  70     1912   1726   1826    569   -337    -56       C  
ATOM   4774  N   ARG D  71       1.014 -23.468  -2.112  1.00 14.54           N  
ANISOU 4774  N   ARG D  71     1693   1846   1984    489   -282   -150       N  
ATOM   4775  CA  ARG D  71       0.538 -24.641  -1.385  1.00 14.50           C  
ANISOU 4775  CA  ARG D  71     1610   1877   2022    444   -253   -177       C  
ATOM   4776  C   ARG D  71       1.281 -24.802  -0.060  1.00 14.07           C  
ANISOU 4776  C   ARG D  71     1567   1822   1956    399   -169   -172       C  
ATOM   4777  O   ARG D  71       0.671 -25.097   0.969  1.00 14.34           O  
ANISOU 4777  O   ARG D  71     1544   1873   2031    386   -121   -192       O  
ATOM   4778  CB  ARG D  71       0.686 -25.896  -2.252  1.00 14.63           C  
ANISOU 4778  CB  ARG D  71     1629   1910   2020    413   -294   -179       C  
ATOM   4779  CG  ARG D  71      -0.278 -25.941  -3.430  1.00 15.97           C  
ANISOU 4779  CG  ARG D  71     1774   2086   2210    456   -390   -197       C  
ATOM   4780  CD  ARG D  71      -0.096 -27.217  -4.255  1.00 17.35           C  
ANISOU 4780  CD  ARG D  71     1961   2271   2360    425   -433   -207       C  
ATOM   4781  NE  ARG D  71      -1.248 -27.475  -5.117  1.00 18.98           N  
ANISOU 4781  NE  ARG D  71     2118   2488   2607    458   -531   -242       N  
ATOM   4782  CZ  ARG D  71      -1.540 -26.796  -6.223  1.00 20.25           C  
ANISOU 4782  CZ  ARG D  71     2325   2636   2734    524   -618   -240       C  
ATOM   4783  NH1 ARG D  71      -0.764 -25.796  -6.643  1.00 20.55           N  
ANISOU 4783  NH1 ARG D  71     2466   2647   2696    562   -606   -198       N  
ATOM   4784  NH2 ARG D  71      -2.622 -27.127  -6.924  1.00 22.13           N  
ANISOU 4784  NH2 ARG D  71     2509   2885   3016    553   -719   -279       N  
ATOM   4785  N   VAL D  72       2.598 -24.610  -0.082  1.00 13.60           N  
ANISOU 4785  N   VAL D  72     1582   1742   1841    378   -150   -146       N  
ATOM   4786  CA  VAL D  72       3.391 -24.597   1.154  1.00 13.35           C  
ANISOU 4786  CA  VAL D  72     1571   1705   1794    345    -89   -145       C  
ATOM   4787  C   VAL D  72       2.861 -23.549   2.132  1.00 13.88           C  
ANISOU 4787  C   VAL D  72     1630   1760   1886    377    -58   -163       C  
ATOM   4788  O   VAL D  72       2.627 -23.839   3.304  1.00 14.40           O  
ANISOU 4788  O   VAL D  72     1674   1838   1960    364     -8   -180       O  
ATOM   4789  CB  VAL D  72       4.871 -24.278   0.876  1.00 12.71           C  
ANISOU 4789  CB  VAL D  72     1563   1598   1669    325    -85   -119       C  
ATOM   4790  CG1 VAL D  72       5.621 -23.971   2.184  1.00 12.13           C  
ANISOU 4790  CG1 VAL D  72     1510   1511   1586    303    -42   -126       C  
ATOM   4791  CG2 VAL D  72       5.513 -25.410   0.121  1.00 12.04           C  
ANISOU 4791  CG2 VAL D  72     1490   1527   1558    293    -97   -104       C  
ATOM   4792  N   ASN D  73       2.661 -22.336   1.636  1.00 14.33           N  
ANISOU 4792  N   ASN D  73     1710   1786   1949    424    -86   -159       N  
ATOM   4793  CA  ASN D  73       2.286 -21.212   2.494  1.00 14.75           C  
ANISOU 4793  CA  ASN D  73     1768   1816   2021    461    -59   -178       C  
ATOM   4794  C   ASN D  73       0.840 -21.228   2.995  1.00 15.33           C  
ANISOU 4794  C   ASN D  73     1763   1914   2149    498    -40   -209       C  
ATOM   4795  O   ASN D  73       0.546 -20.622   4.020  1.00 15.78           O  
ANISOU 4795  O   ASN D  73     1820   1959   2216    520      6   -231       O  
ATOM   4796  CB  ASN D  73       2.620 -19.890   1.792  1.00 14.82           C  
ANISOU 4796  CB  ASN D  73     1837   1773   2020    500    -92   -160       C  
ATOM   4797  CG  ASN D  73       4.115 -19.650   1.722  1.00 14.45           C  
ANISOU 4797  CG  ASN D  73     1861   1694   1936    458    -83   -136       C  
ATOM   4798  OD1 ASN D  73       4.870 -20.224   2.505  1.00 13.93           O  
ANISOU 4798  OD1 ASN D  73     1800   1640   1854    412    -53   -143       O  
ATOM   4799  ND2 ASN D  73       4.552 -18.818   0.787  1.00 14.56           N  
ANISOU 4799  ND2 ASN D  73     1930   1664   1939    476   -107   -107       N  
ATOM   4800  N   SER D  74      -0.046 -21.929   2.293  1.00 15.74           N  
ANISOU 4800  N   SER D  74     1746   1995   2240    504    -74   -214       N  
ATOM   4801  CA  SER D  74      -1.452 -22.041   2.707  1.00 16.60           C  
ANISOU 4801  CA  SER D  74     1759   2128   2422    533    -54   -245       C  
ATOM   4802  C   SER D  74      -1.677 -23.077   3.815  1.00 16.39           C  
ANISOU 4802  C   SER D  74     1687   2130   2409    485     25   -257       C  
ATOM   4803  O   SER D  74      -2.648 -22.986   4.572  1.00 16.64           O  
ANISOU 4803  O   SER D  74     1654   2175   2494    505     80   -280       O  
ATOM   4804  CB  SER D  74      -2.321 -22.412   1.510  1.00 16.86           C  
ANISOU 4804  CB  SER D  74     1727   2177   2501    555   -133   -251       C  
ATOM   4805  OG  SER D  74      -1.914 -23.660   0.998  1.00 17.56           O  
ANISOU 4805  OG  SER D  74     1816   2286   2570    498   -154   -241       O  
ATOM   4806  N   GLY D  75      -0.783 -24.060   3.905  1.00 15.92           N  
ANISOU 4806  N   GLY D  75     1666   2080   2305    424     36   -238       N  
ATOM   4807  CA  GLY D  75      -0.977 -25.197   4.802  1.00 16.00           C  
ANISOU 4807  CA  GLY D  75     1643   2111   2324    377    104   -241       C  
ATOM   4808  C   GLY D  75      -0.780 -24.933   6.288  1.00 16.21           C  
ANISOU 4808  C   GLY D  75     1709   2133   2318    378    191   -247       C  
ATOM   4809  O   GLY D  75      -1.257 -25.706   7.120  1.00 16.77           O  
ANISOU 4809  O   GLY D  75     1749   2219   2404    354    263   -250       O  
ATOM   4810  N   GLY D  76      -0.071 -23.865   6.633  1.00 15.81           N  
ANISOU 4810  N   GLY D  76     1733   2055   2220    406    185   -249       N  
ATOM   4811  CA  GLY D  76       0.224 -23.570   8.038  1.00 15.97           C  
ANISOU 4811  CA  GLY D  76     1809   2065   2193    412    253   -261       C  
ATOM   4812  C   GLY D  76       1.157 -24.593   8.663  1.00 15.40           C  
ANISOU 4812  C   GLY D  76     1790   1999   2062    360    275   -243       C  
ATOM   4813  O   GLY D  76       0.883 -25.132   9.743  1.00 15.83           O  
ANISOU 4813  O   GLY D  76     1856   2063   2095    352    348   -245       O  
ATOM   4814  N   TYR D  77       2.264 -24.860   7.977  1.00 14.29           N  
ANISOU 4814  N   TYR D  77     1686   1851   1893    330    214   -224       N  
ATOM   4815  CA  TYR D  77       3.252 -25.814   8.447  1.00 13.59           C  
ANISOU 4815  CA  TYR D  77     1645   1765   1753    288    219   -207       C  
ATOM   4816  C   TYR D  77       4.233 -25.190   9.438  1.00 13.45           C  
ANISOU 4816  C   TYR D  77     1712   1724   1674    297    218   -218       C  
ATOM   4817  O   TYR D  77       4.471 -23.978   9.424  1.00 13.22           O  
ANISOU 4817  O   TYR D  77     1709   1670   1644    325    194   -236       O  
ATOM   4818  CB  TYR D  77       4.020 -26.387   7.266  1.00 13.05           C  
ANISOU 4818  CB  TYR D  77     1572   1698   1688    256    158   -185       C  
ATOM   4819  CG  TYR D  77       3.121 -27.054   6.273  1.00 13.14           C  
ANISOU 4819  CG  TYR D  77     1512   1728   1752    247    144   -180       C  
ATOM   4820  CD1 TYR D  77       2.512 -28.266   6.568  1.00 13.35           C  
ANISOU 4820  CD1 TYR D  77     1500   1772   1801    217    182   -177       C  
ATOM   4821  CD2 TYR D  77       2.863 -26.470   5.041  1.00 14.36           C  
ANISOU 4821  CD2 TYR D  77     1643   1879   1934    270     88   -181       C  
ATOM   4822  CE1 TYR D  77       1.676 -28.885   5.651  1.00 13.93           C  
ANISOU 4822  CE1 TYR D  77     1503   1857   1932    204    158   -181       C  
ATOM   4823  CE2 TYR D  77       2.030 -27.081   4.118  1.00 14.03           C  
ANISOU 4823  CE2 TYR D  77     1540   1853   1938    266     58   -184       C  
ATOM   4824  CZ  TYR D  77       1.437 -28.284   4.430  1.00 14.12           C  
ANISOU 4824  CZ  TYR D  77     1504   1881   1981    231     90   -188       C  
ATOM   4825  OH  TYR D  77       0.596 -28.883   3.521  1.00 14.46           O  
ANISOU 4825  OH  TYR D  77     1480   1935   2078    224     50   -199       O  
ATOM   4826  N   ASP D  78       4.779 -26.041  10.298  1.00 13.03           N  
ANISOU 4826  N   ASP D  78     1703   1676   1571    275    240   -210       N  
ATOM   4827  CA  ASP D  78       5.845 -25.674  11.215  1.00 13.01           C  
ANISOU 4827  CA  ASP D  78     1783   1654   1507    281    220   -223       C  
ATOM   4828  C   ASP D  78       7.208 -25.987  10.608  1.00 12.14           C  
ANISOU 4828  C   ASP D  78     1685   1535   1393    250    152   -209       C  
ATOM   4829  O   ASP D  78       8.222 -25.460  11.053  1.00 12.64           O  
ANISOU 4829  O   ASP D  78     1796   1576   1431    252    111   -224       O  
ATOM   4830  CB  ASP D  78       5.678 -26.438  12.527  1.00 13.29           C  
ANISOU 4830  CB  ASP D  78     1870   1696   1483    285    277   -221       C  
ATOM   4831  CG  ASP D  78       4.306 -26.248  13.130  1.00 14.39           C  
ANISOU 4831  CG  ASP D  78     1991   1846   1632    313    366   -232       C  
ATOM   4832  OD1 ASP D  78       3.954 -25.092  13.445  1.00 14.86           O  
ANISOU 4832  OD1 ASP D  78     2064   1891   1690    354    376   -262       O  
ATOM   4833  OD2 ASP D  78       3.576 -27.251  13.275  1.00 15.51           O  
ANISOU 4833  OD2 ASP D  78     2101   2005   1788    295    429   -210       O  
ATOM   4834  N   LEU D  79       7.224 -26.834   9.584  1.00 11.38           N  
ANISOU 4834  N   LEU D  79     1541   1454   1328    222    139   -183       N  
ATOM   4835  CA  LEU D  79       8.456 -27.253   8.943  1.00 10.85           C  
ANISOU 4835  CA  LEU D  79     1479   1381   1262    196     90   -168       C  
ATOM   4836  C   LEU D  79       8.195 -27.690   7.507  1.00 10.27           C  
ANISOU 4836  C   LEU D  79     1354   1319   1229    181     77   -148       C  
ATOM   4837  O   LEU D  79       7.207 -28.373   7.222  1.00 10.64           O  
ANISOU 4837  O   LEU D  79     1363   1384   1295    176    101   -142       O  
ATOM   4838  CB  LEU D  79       9.087 -28.411   9.722  1.00 10.92           C  
ANISOU 4838  CB  LEU D  79     1524   1396   1229    181     92   -157       C  
ATOM   4839  CG  LEU D  79      10.389 -29.022   9.180  1.00 10.63           C  
ANISOU 4839  CG  LEU D  79     1486   1355   1197    159     46   -143       C  
ATOM   4840  CD1 LEU D  79      11.553 -28.051   9.280  1.00 11.00           C  
ANISOU 4840  CD1 LEU D  79     1549   1379   1250    162     -4   -160       C  
ATOM   4841  CD2 LEU D  79      10.694 -30.299   9.939  1.00 11.58           C  
ANISOU 4841  CD2 LEU D  79     1641   1480   1279    153     54   -129       C  
ATOM   4842  N   LEU D  80       9.088 -27.277   6.615  1.00  9.70           N  
ANISOU 4842  N   LEU D  80     1282   1233   1170    174     39   -140       N  
ATOM   4843  CA  LEU D  80       9.102 -27.731   5.232  1.00  8.83           C  
ANISOU 4843  CA  LEU D  80     1145   1130   1080    163     23   -121       C  
ATOM   4844  C   LEU D  80      10.400 -28.471   4.996  1.00  8.65           C  
ANISOU 4844  C   LEU D  80     1135   1104   1047    141      7   -108       C  
ATOM   4845  O   LEU D  80      11.467 -28.003   5.395  1.00  8.18           O  
ANISOU 4845  O   LEU D  80     1094   1028    987    136     -8   -112       O  
ATOM   4846  CB  LEU D  80       9.023 -26.542   4.277  1.00  8.76           C  
ANISOU 4846  CB  LEU D  80     1136   1103   1091    182      5   -117       C  
ATOM   4847  CG  LEU D  80       9.333 -26.807   2.799  1.00  7.63           C  
ANISOU 4847  CG  LEU D  80      990    959    951    178    -13    -95       C  
ATOM   4848  CD1 LEU D  80       8.344 -27.799   2.188  1.00  6.86           C  
ANISOU 4848  CD1 LEU D  80      863    887    857    180    -20    -96       C  
ATOM   4849  CD2 LEU D  80       9.328 -25.506   2.031  1.00  7.86           C  
ANISOU 4849  CD2 LEU D  80     1037    959    990    201    -25    -85       C  
ATOM   4850  N   ILE D  81      10.297 -29.630   4.352  1.00  8.41           N  
ANISOU 4850  N   ILE D  81     1090   1088   1016    128      9    -96       N  
ATOM   4851  CA  ILE D  81      11.448 -30.417   3.943  1.00  8.34           C  
ANISOU 4851  CA  ILE D  81     1089   1076   1003    114     -2    -84       C  
ATOM   4852  C   ILE D  81      11.296 -30.688   2.454  1.00  8.35           C  
ANISOU 4852  C   ILE D  81     1082   1080   1009    116     -8    -73       C  
ATOM   4853  O   ILE D  81      10.289 -31.252   2.028  1.00  8.65           O  
ANISOU 4853  O   ILE D  81     1106   1130   1050    117    -11    -77       O  
ATOM   4854  CB  ILE D  81      11.508 -31.771   4.681  1.00  8.25           C  
ANISOU 4854  CB  ILE D  81     1087   1072    975    103      7    -81       C  
ATOM   4855  CG1 ILE D  81      11.786 -31.568   6.172  1.00  9.06           C  
ANISOU 4855  CG1 ILE D  81     1217   1169   1055    108      9    -90       C  
ATOM   4856  CG2 ILE D  81      12.579 -32.672   4.073  1.00  7.99           C  
ANISOU 4856  CG2 ILE D  81     1057   1035    943     96     -4    -71       C  
ATOM   4857  CD1 ILE D  81      11.502 -32.807   7.017  1.00  8.44           C  
ANISOU 4857  CD1 ILE D  81     1163   1094    951    103     28    -81       C  
ATOM   4858  N   GLU D  82      12.266 -30.261   1.659  1.00  8.09           N  
ANISOU 4858  N   GLU D  82     1058   1035    980    118     -9    -61       N  
ATOM   4859  CA  GLU D  82      12.278 -30.632   0.257  1.00  8.37           C  
ANISOU 4859  CA  GLU D  82     1104   1071   1004    126    -10    -50       C  
ATOM   4860  C   GLU D  82      13.367 -31.668   0.042  1.00  8.50           C  
ANISOU 4860  C   GLU D  82     1124   1087   1017    117      1    -44       C  
ATOM   4861  O   GLU D  82      14.490 -31.517   0.524  1.00  8.17           O  
ANISOU 4861  O   GLU D  82     1074   1036    994    109      9    -41       O  
ATOM   4862  CB  GLU D  82      12.482 -29.436  -0.676  1.00  8.43           C  
ANISOU 4862  CB  GLU D  82     1131   1061   1011    141     -4    -34       C  
ATOM   4863  CG  GLU D  82      12.330 -29.839  -2.143  1.00  9.19           C  
ANISOU 4863  CG  GLU D  82     1256   1158   1077    158     -7    -23       C  
ATOM   4864  CD  GLU D  82      11.934 -28.703  -3.054  1.00 10.86           C  
ANISOU 4864  CD  GLU D  82     1501   1354   1273    185    -12     -7       C  
ATOM   4865  OE1 GLU D  82      12.839 -28.127  -3.690  1.00 11.13           O  
ANISOU 4865  OE1 GLU D  82     1563   1364   1300    187     21     19       O  
ATOM   4866  OE2 GLU D  82      10.718 -28.390  -3.140  1.00 11.72           O  
ANISOU 4866  OE2 GLU D  82     1606   1469   1379    205    -46    -17       O  
ATOM   4867  N   LEU D  83      13.013 -32.724  -0.676  1.00  8.89           N  
ANISOU 4867  N   LEU D  83     1184   1144   1050    120     -5    -48       N  
ATOM   4868  CA  LEU D  83      13.906 -33.846  -0.891  1.00  9.13           C  
ANISOU 4868  CA  LEU D  83     1221   1170   1077    119      6    -47       C  
ATOM   4869  C   LEU D  83      14.604 -33.711  -2.243  1.00  9.52           C  
ANISOU 4869  C   LEU D  83     1294   1212   1110    136     27    -35       C  
ATOM   4870  O   LEU D  83      13.952 -33.548  -3.285  1.00  9.15           O  
ANISOU 4870  O   LEU D  83     1276   1165   1034    151     19    -36       O  
ATOM   4871  CB  LEU D  83      13.121 -35.159  -0.817  1.00  9.21           C  
ANISOU 4871  CB  LEU D  83     1236   1184   1080    111     -9    -61       C  
ATOM   4872  CG  LEU D  83      12.481 -35.473   0.536  1.00  9.21           C  
ANISOU 4872  CG  LEU D  83     1219   1186   1092     93    -12    -65       C  
ATOM   4873  CD1 LEU D  83      11.637 -36.735   0.429  1.00  9.37           C  
ANISOU 4873  CD1 LEU D  83     1242   1200   1117     78    -19    -76       C  
ATOM   4874  CD2 LEU D  83      13.535 -35.611   1.641  1.00  8.75           C  
ANISOU 4874  CD2 LEU D  83     1164   1122   1038     93     -5    -58       C  
ATOM   4875  N   HIS D  84      15.934 -33.758  -2.198  1.00  9.62           N  
ANISOU 4875  N   HIS D  84     1295   1216   1143    136     55    -26       N  
ATOM   4876  CA  HIS D  84      16.781 -33.832  -3.373  1.00 10.13           C  
ANISOU 4876  CA  HIS D  84     1379   1273   1197    152     96    -14       C  
ATOM   4877  C   HIS D  84      17.833 -34.937  -3.229  1.00 10.58           C  
ANISOU 4877  C   HIS D  84     1419   1327   1273    158    113    -20       C  
ATOM   4878  O   HIS D  84      18.016 -35.511  -2.153  1.00 10.43           O  
ANISOU 4878  O   HIS D  84     1375   1310   1277    150     88    -30       O  
ATOM   4879  CB  HIS D  84      17.495 -32.499  -3.580  1.00 10.45           C  
ANISOU 4879  CB  HIS D  84     1408   1298   1263    146    131      8       C  
ATOM   4880  CG  HIS D  84      16.601 -31.400  -4.046  1.00  9.83           C  
ANISOU 4880  CG  HIS D  84     1362   1214   1160    152    123     20       C  
ATOM   4881  ND1 HIS D  84      16.626 -30.922  -5.335  1.00 10.87           N  
ANISOU 4881  ND1 HIS D  84     1544   1332   1255    173    156     42       N  
ATOM   4882  CD2 HIS D  84      15.659 -30.680  -3.393  1.00  9.77           C  
ANISOU 4882  CD2 HIS D  84     1347   1207   1156    146     87     13       C  
ATOM   4883  CE1 HIS D  84      15.736 -29.953  -5.459  1.00 10.83           C  
ANISOU 4883  CE1 HIS D  84     1562   1320   1234    181    132     50       C  
ATOM   4884  NE2 HIS D  84      15.134 -29.789  -4.295  1.00 10.83           N  
ANISOU 4884  NE2 HIS D  84     1523   1329   1263    165     92     30       N  
ATOM   4885  N   LEU D  85      18.495 -35.245  -4.340  1.00 11.29           N  
ANISOU 4885  N   LEU D  85     1532   1410   1348    179    157    -14       N  
ATOM   4886  CA  LEU D  85      19.750 -35.993  -4.336  1.00 12.07           C  
ANISOU 4886  CA  LEU D  85     1603   1502   1479    193    189    -16       C  
ATOM   4887  C   LEU D  85      20.756 -35.115  -5.054  1.00 13.02           C  
ANISOU 4887  C   LEU D  85     1708   1613   1625    196    258      6       C  
ATOM   4888  O   LEU D  85      20.373 -34.235  -5.830  1.00 13.46           O  
ANISOU 4888  O   LEU D  85     1802   1663   1648    196    283     24       O  
ATOM   4889  CB  LEU D  85      19.628 -37.349  -5.045  1.00 12.16           C  
ANISOU 4889  CB  LEU D  85     1659   1510   1452    220    193    -33       C  
ATOM   4890  CG  LEU D  85      18.682 -38.398  -4.463  1.00 11.87           C  
ANISOU 4890  CG  LEU D  85     1640   1472   1399    212    136    -54       C  
ATOM   4891  CD1 LEU D  85      18.851 -39.721  -5.205  1.00 10.73           C  
ANISOU 4891  CD1 LEU D  85     1537   1312   1228    240    145    -73       C  
ATOM   4892  CD2 LEU D  85      18.905 -38.591  -2.961  1.00 11.64           C  
ANISOU 4892  CD2 LEU D  85     1566   1444   1412    195    104    -54       C  
ATOM   4893  N   ASN D  86      22.039 -35.342  -4.786  1.00 13.86           N  
ANISOU 4893  N   ASN D  86     1758   1715   1794    199    289      5       N  
ATOM   4894  CA  ASN D  86      23.103 -34.491  -5.315  1.00 14.60           C  
ANISOU 4894  CA  ASN D  86     1815   1794   1937    193    363     27       C  
ATOM   4895  C   ASN D  86      23.731 -35.118  -6.562  1.00 15.44           C  
ANISOU 4895  C   ASN D  86     1951   1895   2020    228    445     33       C  
ATOM   4896  O   ASN D  86      23.403 -36.247  -6.946  1.00 14.59           O  
ANISOU 4896  O   ASN D  86     1890   1793   1861    259    433     16       O  
ATOM   4897  CB  ASN D  86      24.162 -34.241  -4.229  1.00 14.79           C  
ANISOU 4897  CB  ASN D  86     1743   1815   2061    172    344     17       C  
ATOM   4898  CG  ASN D  86      24.739 -32.825  -4.265  1.00 15.71           C  
ANISOU 4898  CG  ASN D  86     1816   1911   2242    138    383     36       C  
ATOM   4899  OD1 ASN D  86      24.918 -32.230  -5.327  1.00 16.47           O  
ANISOU 4899  OD1 ASN D  86     1939   1991   2328    137    463     64       O  
ATOM   4900  ND2 ASN D  86      25.049 -32.289  -3.090  1.00 16.95           N  
ANISOU 4900  ND2 ASN D  86     1913   2063   2464    110    325     20       N  
ATOM   4901  N   ALA D  87      24.609 -34.357  -7.204  1.00 16.38           N  
ANISOU 4901  N   ALA D  87     2047   1999   2178    223    532     59       N  
ATOM   4902  CA  ALA D  87      25.297 -34.810  -8.406  1.00 17.56           C  
ANISOU 4902  CA  ALA D  87     2226   2141   2307    259    632     69       C  
ATOM   4903  C   ALA D  87      26.566 -33.994  -8.601  1.00 18.71           C  
ANISOU 4903  C   ALA D  87     2296   2267   2546    239    728     94       C  
ATOM   4904  O   ALA D  87      26.628 -32.837  -8.186  1.00 18.64           O  
ANISOU 4904  O   ALA D  87     2251   2244   2589    196    724    112       O  
ATOM   4905  CB  ALA D  87      24.385 -34.677  -9.616  1.00 17.34           C  
ANISOU 4905  CB  ALA D  87     2321   2109   2160    284    655     84       C  
ATOM   4906  N   SER D  88      27.575 -34.612  -9.211  1.00 19.84           N  
ANISOU 4906  N   SER D  88     2411   2406   2719    270    816     94       N  
ATOM   4907  CA  SER D  88      28.803 -33.925  -9.586  1.00 21.36           C  
ANISOU 4907  CA  SER D  88     2530   2578   3008    253    932    119       C  
ATOM   4908  C   SER D  88      29.362 -34.588 -10.852  1.00 22.66           C  
ANISOU 4908  C   SER D  88     2742   2738   3129    305   1056    129       C  
ATOM   4909  O   SER D  88      28.655 -34.672 -11.857  1.00 22.57           O  
ANISOU 4909  O   SER D  88     2860   2724   2992    336   1088    143       O  
ATOM   4910  CB  SER D  88      29.806 -33.928  -8.425  1.00 21.45           C  
ANISOU 4910  CB  SER D  88     2391   2591   3168    226    891     95       C  
ATOM   4911  OG  SER D  88      30.268 -35.237  -8.139  1.00 22.02           O  
ANISOU 4911  OG  SER D  88     2425   2680   3261    270    864     61       O  
ATOM   4912  N   ASN D  89      30.604 -35.074 -10.806  1.00 24.01           N  
ANISOU 4912  N   ASN D  89     2813   2909   3403    321   1123    117       N  
ATOM   4913  CA  ASN D  89      31.210 -35.768 -11.949  1.00 25.34           C  
ANISOU 4913  CA  ASN D  89     3020   3071   3536    378   1251    121       C  
ATOM   4914  C   ASN D  89      31.400 -37.255 -11.658  1.00 25.67           C  
ANISOU 4914  C   ASN D  89     3046   3130   3578    433   1200     74       C  
ATOM   4915  O   ASN D  89      32.148 -37.936 -12.362  1.00 26.64           O  
ANISOU 4915  O   ASN D  89     3166   3248   3708    484   1301     66       O  
ATOM   4916  CB  ASN D  89      32.544 -35.122 -12.312  1.00 26.63           C  
ANISOU 4916  CB  ASN D  89     3080   3214   3824    360   1398    149       C  
ATOM   4917  N   GLY D  90      30.713 -37.751 -10.629  1.00 24.98           N  
ANISOU 4917  N   GLY D  90     2955   3057   3480    424   1052     44       N  
ATOM   4918  CA  GLY D  90      30.791 -39.155 -10.239  1.00 25.18           C  
ANISOU 4918  CA  GLY D  90     2975   3089   3503    471    991      3       C  
ATOM   4919  C   GLY D  90      31.676 -39.416  -9.032  1.00 25.33           C  
ANISOU 4919  C   GLY D  90     2851   3113   3661    466    930    -18       C  
ATOM   4920  O   GLY D  90      31.601 -40.492  -8.436  1.00 25.60           O  
ANISOU 4920  O   GLY D  90     2885   3149   3693    499    851    -48       O  
ATOM   4921  N   GLN D  91      32.518 -38.447  -8.670  1.00 25.84           N  
ANISOU 4921  N   GLN D  91     2797   3174   3846    425    963     -4       N  
ATOM   4922  CA  GLN D  91      33.424 -38.587  -7.522  1.00 26.05           C  
ANISOU 4922  CA  GLN D  91     2680   3205   4014    421    893    -28       C  
ATOM   4923  C   GLN D  91      32.859 -37.983  -6.234  1.00 24.83           C  
ANISOU 4923  C   GLN D  91     2506   3056   3871    370    753    -34       C  
ATOM   4924  O   GLN D  91      33.251 -38.382  -5.137  1.00 24.96           O  
ANISOU 4924  O   GLN D  91     2451   3077   3954    380    653    -61       O  
ATOM   4925  CB  GLN D  91      34.788 -37.969  -7.846  1.00 27.50           C  
ANISOU 4925  CB  GLN D  91     2727   3377   4344    408   1005    -19       C  
ATOM   4926  CG  GLN D  91      35.466 -38.583  -9.067  1.00 29.38           C  
ANISOU 4926  CG  GLN D  91     2973   3609   4579    466   1159    -14       C  
ATOM   4927  CD  GLN D  91      35.576 -40.094  -8.978  1.00 30.58           C  
ANISOU 4927  CD  GLN D  91     3148   3767   4705    544   1119    -50       C  
ATOM   4928  OE1 GLN D  91      35.969 -40.639  -7.944  1.00 31.31           O  
ANISOU 4928  OE1 GLN D  91     3158   3863   4874    562   1013    -79       O  
ATOM   4929  NE2 GLN D  91      35.225 -40.781 -10.061  1.00 31.83           N  
ANISOU 4929  NE2 GLN D  91     3426   3920   4748    596   1200    -49       N  
ATOM   4930  N   GLY D  92      31.946 -37.024  -6.368  1.00 23.70           N  
ANISOU 4930  N   GLY D  92     2434   2911   3660    322    747    -10       N  
ATOM   4931  CA  GLY D  92      31.253 -36.448  -5.218  1.00 22.39           C  
ANISOU 4931  CA  GLY D  92     2272   2750   3486    279    624    -17       C  
ATOM   4932  C   GLY D  92      30.412 -37.485  -4.495  1.00 21.09           C  
ANISOU 4932  C   GLY D  92     2175   2598   3241    307    515    -38       C  
ATOM   4933  O   GLY D  92      29.845 -38.383  -5.119  1.00 20.73           O  
ANISOU 4933  O   GLY D  92     2216   2554   3105    343    534    -39       O  
ATOM   4934  N   LYS D  93      30.346 -37.369  -3.173  1.00 20.14           N  
ANISOU 4934  N   LYS D  93     2017   2481   3152    291    402    -56       N  
ATOM   4935  CA  LYS D  93      29.630 -38.334  -2.348  1.00 19.26           C  
ANISOU 4935  CA  LYS D  93     1967   2377   2974    315    305    -70       C  
ATOM   4936  C   LYS D  93      29.256 -37.729  -1.007  1.00 18.23           C  
ANISOU 4936  C   LYS D  93     1828   2250   2849    283    199    -79       C  
ATOM   4937  O   LYS D  93      29.935 -36.829  -0.514  1.00 18.43           O  
ANISOU 4937  O   LYS D  93     1772   2270   2960    255    177    -88       O  
ATOM   4938  CB  LYS D  93      30.484 -39.585  -2.117  1.00 19.97           C  
ANISOU 4938  CB  LYS D  93     2016   2463   3110    374    286    -90       C  
ATOM   4939  CG  LYS D  93      31.779 -39.344  -1.328  1.00 22.12           C  
ANISOU 4939  CG  LYS D  93     2157   2732   3514    381    242   -110       C  
ATOM   4940  CD  LYS D  93      32.614 -40.621  -1.225  1.00 24.65           C  
ANISOU 4940  CD  LYS D  93     2439   3046   3881    452    227   -129       C  
ATOM   4941  CE  LYS D  93      33.825 -40.439  -0.308  1.00 26.49           C  
ANISOU 4941  CE  LYS D  93     2541   3277   4246    466    154   -154       C  
ATOM   4942  NZ  LYS D  93      34.870 -39.542  -0.892  1.00 28.26           N  
ANISOU 4942  NZ  LYS D  93     2636   3500   4600    439    236   -157       N  
ATOM   4943  N   GLY D  94      28.178 -38.242  -0.421  1.00 16.80           N  
ANISOU 4943  N   GLY D  94     1732   2073   2578    287    136    -80       N  
ATOM   4944  CA  GLY D  94      27.801 -37.885   0.935  1.00 16.25           C  
ANISOU 4944  CA  GLY D  94     1670   2005   2497    270     39    -89       C  
ATOM   4945  C   GLY D  94      26.532 -37.067   1.006  1.00 15.25           C  
ANISOU 4945  C   GLY D  94     1610   1885   2300    230     37    -78       C  
ATOM   4946  O   GLY D  94      25.848 -36.863  -0.006  1.00 14.57           O  
ANISOU 4946  O   GLY D  94     1569   1801   2167    217     99    -61       O  
ATOM   4947  N   SER D  95      26.255 -36.576   2.211  1.00 14.85           N  
ANISOU 4947  N   SER D  95     1566   1835   2242    215    -39    -89       N  
ATOM   4948  CA  SER D  95      24.998 -35.928   2.550  1.00 14.08           C  
ANISOU 4948  CA  SER D  95     1531   1741   2076    186    -52    -82       C  
ATOM   4949  C   SER D  95      25.194 -34.472   2.934  1.00 14.59           C  
ANISOU 4949  C   SER D  95     1561   1799   2184    151    -69    -92       C  
ATOM   4950  O   SER D  95      26.233 -34.088   3.476  1.00 15.19           O  
ANISOU 4950  O   SER D  95     1571   1866   2337    148   -109   -112       O  
ATOM   4951  CB  SER D  95      24.337 -36.672   3.705  1.00 13.75           C  
ANISOU 4951  CB  SER D  95     1550   1702   1972    204   -116    -87       C  
ATOM   4952  OG  SER D  95      24.124 -38.030   3.363  1.00 12.69           O  
ANISOU 4952  OG  SER D  95     1454   1565   1805    232   -100    -77       O  
ATOM   4953  N   GLU D  96      24.148 -33.685   2.705  1.00 14.37           N  
ANISOU 4953  N   GLU D  96     1579   1772   2109    126    -47    -82       N  
ATOM   4954  CA  GLU D  96      24.224 -32.239   2.743  1.00 14.69           C  
ANISOU 4954  CA  GLU D  96     1597   1797   2188     92    -43    -86       C  
ATOM   4955  C   GLU D  96      22.809 -31.693   2.920  1.00 13.83           C  
ANISOU 4955  C   GLU D  96     1557   1692   2006     83    -46    -80       C  
ATOM   4956  O   GLU D  96      21.867 -32.216   2.314  1.00 13.36           O  
ANISOU 4956  O   GLU D  96     1544   1645   1886     93    -16    -63       O  
ATOM   4957  CB  GLU D  96      24.838 -31.793   1.415  1.00 15.54           C  
ANISOU 4957  CB  GLU D  96     1666   1892   2347     78     41    -65       C  
ATOM   4958  CG  GLU D  96      25.000 -30.326   1.174  1.00 16.89           C  
ANISOU 4958  CG  GLU D  96     1816   2035   2565     39     67    -59       C  
ATOM   4959  CD  GLU D  96      25.782 -30.072  -0.105  1.00 19.24           C  
ANISOU 4959  CD  GLU D  96     2076   2316   2917     28    163    -33       C  
ATOM   4960  OE1 GLU D  96      25.238 -29.430  -1.028  1.00 20.69           O  
ANISOU 4960  OE1 GLU D  96     2307   2487   3065     19    224     -4       O  
ATOM   4961  OE2 GLU D  96      26.936 -30.536  -0.192  1.00 20.05           O  
ANISOU 4961  OE2 GLU D  96     2105   2418   3094     34    180    -41       O  
ATOM   4962  N   VAL D  97      22.651 -30.679   3.774  1.00 13.41           N  
ANISOU 4962  N   VAL D  97     1507   1626   1962     66    -87    -98       N  
ATOM   4963  CA  VAL D  97      21.343 -30.066   4.025  1.00 12.47           C  
ANISOU 4963  CA  VAL D  97     1446   1509   1785     62    -88    -97       C  
ATOM   4964  C   VAL D  97      21.472 -28.546   3.969  1.00 12.59           C  
ANISOU 4964  C   VAL D  97     1448   1493   1842     35    -83   -103       C  
ATOM   4965  O   VAL D  97      22.335 -27.947   4.626  1.00 12.38           O  
ANISOU 4965  O   VAL D  97     1386   1444   1874     20   -124   -129       O  
ATOM   4966  CB  VAL D  97      20.747 -30.494   5.384  1.00 12.40           C  
ANISOU 4966  CB  VAL D  97     1481   1512   1720     80   -142   -116       C  
ATOM   4967  CG1 VAL D  97      19.401 -29.801   5.638  1.00 11.50           C  
ANISOU 4967  CG1 VAL D  97     1415   1399   1556     79   -131   -117       C  
ATOM   4968  CG2 VAL D  97      20.575 -32.012   5.431  1.00 12.99           C  
ANISOU 4968  CG2 VAL D  97     1575   1606   1754    103   -141   -104       C  
ATOM   4969  N   LEU D  98      20.628 -27.932   3.151  1.00 11.92           N  
ANISOU 4969  N   LEU D  98     1395   1403   1733     32    -39    -82       N  
ATOM   4970  CA  LEU D  98      20.685 -26.503   2.945  1.00 12.32           C  
ANISOU 4970  CA  LEU D  98     1444   1415   1821      9    -25    -80       C  
ATOM   4971  C   LEU D  98      19.618 -25.870   3.826  1.00 11.90           C  
ANISOU 4971  C   LEU D  98     1437   1359   1725     20    -61   -101       C  
ATOM   4972  O   LEU D  98      18.563 -26.458   4.051  1.00 11.12           O  
ANISOU 4972  O   LEU D  98     1373   1290   1563     43    -64   -100       O  
ATOM   4973  CB  LEU D  98      20.480 -26.164   1.466  1.00 12.32           C  
ANISOU 4973  CB  LEU D  98     1460   1404   1817      8     45    -40       C  
ATOM   4974  CG  LEU D  98      21.274 -27.044   0.486  1.00 13.72           C  
ANISOU 4974  CG  LEU D  98     1611   1593   2008     11     96    -18       C  
ATOM   4975  CD1 LEU D  98      20.974 -26.661  -0.964  1.00 14.39           C  
ANISOU 4975  CD1 LEU D  98     1735   1665   2067     18    166     22       C  
ATOM   4976  CD2 LEU D  98      22.760 -26.982   0.762  1.00 14.15           C  
ANISOU 4976  CD2 LEU D  98     1590   1629   2156    -13     97    -30       C  
ATOM   4977  N   TYR D  99      19.910 -24.682   4.341  1.00 12.38           N  
ANISOU 4977  N   TYR D  99     1495   1381   1827      2    -84   -122       N  
ATOM   4978  CA  TYR D  99      18.994 -23.973   5.223  1.00 12.20           C  
ANISOU 4978  CA  TYR D  99     1518   1349   1767     16   -114   -148       C  
ATOM   4979  C   TYR D  99      19.042 -22.484   4.941  1.00 12.67           C  
ANISOU 4979  C   TYR D  99     1587   1353   1873     -3   -103   -149       C  
ATOM   4980  O   TYR D  99      19.947 -22.008   4.258  1.00 12.78           O  
ANISOU 4980  O   TYR D  99     1566   1333   1955    -34    -77   -134       O  
ATOM   4981  CB  TYR D  99      19.368 -24.231   6.678  1.00 12.32           C  
ANISOU 4981  CB  TYR D  99     1540   1369   1771     23   -181   -192       C  
ATOM   4982  CG  TYR D  99      20.723 -23.699   7.066  1.00 12.83           C  
ANISOU 4982  CG  TYR D  99     1560   1397   1916     -7   -228   -221       C  
ATOM   4983  CD1 TYR D  99      20.866 -22.405   7.562  1.00 13.94           C  
ANISOU 4983  CD1 TYR D  99     1714   1489   2095    -24   -259   -254       C  
ATOM   4984  CD2 TYR D  99      21.867 -24.483   6.936  1.00 13.93           C  
ANISOU 4984  CD2 TYR D  99     1640   1548   2104    -17   -244   -219       C  
ATOM   4985  CE1 TYR D  99      22.108 -21.910   7.926  1.00 14.91           C  
ANISOU 4985  CE1 TYR D  99     1788   1574   2305    -57   -311   -287       C  
ATOM   4986  CE2 TYR D  99      23.119 -23.995   7.300  1.00 13.99           C  
ANISOU 4986  CE2 TYR D  99     1590   1522   2202    -46   -293   -251       C  
ATOM   4987  CZ  TYR D  99      23.232 -22.707   7.793  1.00 15.89           C  
ANISOU 4987  CZ  TYR D  99     1842   1713   2484    -69   -328   -286       C  
ATOM   4988  OH  TYR D  99      24.469 -22.208   8.157  1.00 16.68           O  
ANISOU 4988  OH  TYR D  99     1876   1773   2686   -103   -385   -324       O  
ATOM   4989  N   TYR D 100      18.066 -21.760   5.479  1.00 13.11           N  
ANISOU 4989  N   TYR D 100     1689   1397   1894     18   -115   -167       N  
ATOM   4990  CA  TYR D 100      17.960 -20.310   5.294  1.00 13.78           C  
ANISOU 4990  CA  TYR D 100     1796   1423   2017      8   -108   -171       C  
ATOM   4991  C   TYR D 100      18.264 -19.553   6.570  1.00 14.27           C  
ANISOU 4991  C   TYR D 100     1874   1448   2098      1   -167   -227       C  
ATOM   4992  O   TYR D 100      18.928 -18.518   6.534  1.00 14.96           O  
ANISOU 4992  O   TYR D 100     1953   1474   2255    -31   -178   -240       O  
ATOM   4993  CB  TYR D 100      16.548 -19.930   4.852  1.00 13.78           C  
ANISOU 4993  CB  TYR D 100     1840   1428   1968     46    -80   -153       C  
ATOM   4994  CG  TYR D 100      16.433 -18.502   4.386  1.00 14.72           C  
ANISOU 4994  CG  TYR D 100     1987   1480   2124     42    -64   -143       C  
ATOM   4995  CD1 TYR D 100      16.825 -18.146   3.104  1.00 16.25           C  
ANISOU 4995  CD1 TYR D 100     2179   1644   2350     25    -18    -95       C  
ATOM   4996  CD2 TYR D 100      15.938 -17.510   5.219  1.00 16.49           C  
ANISOU 4996  CD2 TYR D 100     2249   1668   2349     59    -91   -181       C  
ATOM   4997  CE1 TYR D 100      16.732 -16.830   2.657  1.00 17.25           C  
ANISOU 4997  CE1 TYR D 100     2343   1701   2510     23      0    -80       C  
ATOM   4998  CE2 TYR D 100      15.839 -16.185   4.784  1.00 18.18           C  
ANISOU 4998  CE2 TYR D 100     2495   1811   2601     58    -77   -171       C  
ATOM   4999  CZ  TYR D 100      16.237 -15.859   3.495  1.00 17.87           C  
ANISOU 4999  CZ  TYR D 100     2456   1740   2596     39    -32   -118       C  
ATOM   5000  OH  TYR D 100      16.151 -14.564   3.044  1.00 19.85           O  
ANISOU 5000  OH  TYR D 100     2748   1913   2882     38    -14   -101       O  
ATOM   5001  N   SER D 101      17.761 -20.070   7.689  1.00 14.28           N  
ANISOU 5001  N   SER D 101     1905   1484   2036     31   -202   -260       N  
ATOM   5002  CA  SER D 101      17.751 -19.348   8.955  1.00 14.87           C  
ANISOU 5002  CA  SER D 101     2022   1528   2100     42   -256   -317       C  
ATOM   5003  C   SER D 101      18.488 -20.095  10.058  1.00 15.15           C  
ANISOU 5003  C   SER D 101     2057   1585   2114     44   -322   -354       C  
ATOM   5004  O   SER D 101      18.942 -21.228   9.877  1.00 14.53           O  
ANISOU 5004  O   SER D 101     1943   1546   2030     40   -323   -333       O  
ATOM   5005  CB  SER D 101      16.301 -19.113   9.387  1.00 14.72           C  
ANISOU 5005  CB  SER D 101     2060   1523   2008     90   -231   -325       C  
ATOM   5006  OG  SER D 101      15.708 -20.328   9.825  1.00 14.77           O  
ANISOU 5006  OG  SER D 101     2077   1592   1943    118   -217   -316       O  
ATOM   5007  N   ASN D 102      18.594 -19.450  11.214  1.00 15.85           N  
ANISOU 5007  N   ASN D 102     2192   1642   2186     55   -382   -411       N  
ATOM   5008  CA  ASN D 102      19.198 -20.083  12.385  1.00 16.56           C  
ANISOU 5008  CA  ASN D 102     2305   1750   2238     70   -457   -451       C  
ATOM   5009  C   ASN D 102      18.400 -21.300  12.858  1.00 15.96           C  
ANISOU 5009  C   ASN D 102     2271   1736   2059    113   -429   -429       C  
ATOM   5010  O   ASN D 102      18.984 -22.296  13.278  1.00 15.72           O  
ANISOU 5010  O   ASN D 102     2235   1732   2006    121   -467   -429       O  
ATOM   5011  CB  ASN D 102      19.376 -19.065  13.522  1.00 17.47           C  
ANISOU 5011  CB  ASN D 102     2480   1815   2343     80   -530   -522       C  
ATOM   5012  CG  ASN D 102      20.590 -18.165  13.321  1.00 19.59           C  
ANISOU 5012  CG  ASN D 102     2694   2019   2730     27   -590   -555       C  
ATOM   5013  OD1 ASN D 102      21.487 -18.465  12.527  1.00 20.79           O  
ANISOU 5013  OD1 ASN D 102     2758   2170   2969    -15   -584   -528       O  
ATOM   5014  ND2 ASN D 102      20.638 -17.066  14.069  1.00 22.22           N  
ANISOU 5014  ND2 ASN D 102     3078   2293   3070     28   -645   -617       N  
ATOM   5015  N   LYS D 103      17.069 -21.230  12.777  1.00 15.70           N  
ANISOU 5015  N   LYS D 103     2275   1720   1970    142   -361   -411       N  
ATOM   5016  CA  LYS D 103      16.232 -22.375  13.142  1.00 15.38           C  
ANISOU 5016  CA  LYS D 103     2266   1733   1847    174   -318   -386       C  
ATOM   5017  C   LYS D 103      16.448 -23.535  12.162  1.00 14.37           C  
ANISOU 5017  C   LYS D 103     2075   1641   1743    154   -288   -334       C  
ATOM   5018  O   LYS D 103      16.512 -24.697  12.569  1.00 13.93           O  
ANISOU 5018  O   LYS D 103     2034   1616   1642    166   -291   -320       O  
ATOM   5019  CB  LYS D 103      14.753 -21.980  13.205  1.00 15.48           C  
ANISOU 5019  CB  LYS D 103     2311   1753   1817    205   -248   -381       C  
ATOM   5020  CG  LYS D 103      14.413 -21.070  14.373  1.00 17.95           C  
ANISOU 5020  CG  LYS D 103     2703   2035   2081    240   -266   -435       C  
ATOM   5021  CD  LYS D 103      12.946 -20.692  14.377  1.00 19.80           C  
ANISOU 5021  CD  LYS D 103     2957   2278   2286    276   -187   -430       C  
ATOM   5022  CE  LYS D 103      12.540 -19.987  15.663  1.00 22.10           C  
ANISOU 5022  CE  LYS D 103     3339   2546   2510    321   -191   -484       C  
ATOM   5023  NZ  LYS D 103      13.050 -18.587  15.745  1.00 25.41           N  
ANISOU 5023  NZ  LYS D 103     3780   2902   2973    316   -246   -533       N  
ATOM   5024  N   GLY D 104      16.555 -23.211  10.874  1.00 13.85           N  
ANISOU 5024  N   GLY D 104     1951   1567   1745    125   -257   -305       N  
ATOM   5025  CA  GLY D 104      16.873 -24.199   9.839  1.00 13.39           C  
ANISOU 5025  CA  GLY D 104     1839   1536   1712    107   -230   -262       C  
ATOM   5026  C   GLY D 104      18.233 -24.849  10.053  1.00 13.80           C  
ANISOU 5026  C   GLY D 104     1860   1589   1796     93   -283   -269       C  
ATOM   5027  O   GLY D 104      18.394 -26.065   9.856  1.00 13.46           O  
ANISOU 5027  O   GLY D 104     1802   1576   1735     99   -273   -245       O  
ATOM   5028  N   LEU D 105      19.203 -24.045  10.483  1.00 14.51           N  
ANISOU 5028  N   LEU D 105     1937   1642   1937     76   -342   -306       N  
ATOM   5029  CA  LEU D 105      20.531 -24.545  10.812  1.00 15.28           C  
ANISOU 5029  CA  LEU D 105     1993   1735   2076     67   -407   -324       C  
ATOM   5030  C   LEU D 105      20.474 -25.661  11.858  1.00 15.81           C  
ANISOU 5030  C   LEU D 105     2111   1834   2063    106   -447   -331       C  
ATOM   5031  O   LEU D 105      21.183 -26.662  11.719  1.00 15.74           O  
ANISOU 5031  O   LEU D 105     2068   1843   2070    111   -466   -317       O  
ATOM   5032  CB  LEU D 105      21.433 -23.408  11.293  1.00 16.04           C  
ANISOU 5032  CB  LEU D 105     2071   1782   2241     43   -476   -374       C  
ATOM   5033  CG  LEU D 105      22.856 -23.770  11.721  1.00 16.23           C  
ANISOU 5033  CG  LEU D 105     2040   1797   2328     34   -562   -404       C  
ATOM   5034  CD1 LEU D 105      23.609 -24.505  10.620  1.00 15.39           C  
ANISOU 5034  CD1 LEU D 105     1844   1709   2296     13   -520   -364       C  
ATOM   5035  CD2 LEU D 105      23.600 -22.514  12.151  1.00 16.79           C  
ANISOU 5035  CD2 LEU D 105     2090   1811   2479      3   -631   -460       C  
ATOM   5036  N   GLU D 106      19.636 -25.498  12.887  1.00 16.51           N  
ANISOU 5036  N   GLU D 106     2285   1925   2064    138   -454   -351       N  
ATOM   5037  CA  GLU D 106      19.485 -26.528  13.941  1.00 17.00           C  
ANISOU 5037  CA  GLU D 106     2415   2009   2034    179   -480   -351       C  
ATOM   5038  C   GLU D 106      19.067 -27.866  13.343  1.00 16.00           C  
ANISOU 5038  C   GLU D 106     2275   1918   1887    183   -419   -297       C  
ATOM   5039  O   GLU D 106      19.663 -28.907  13.630  1.00 16.12           O  
ANISOU 5039  O   GLU D 106     2295   1944   1887    199   -453   -287       O  
ATOM   5040  CB  GLU D 106      18.404 -26.163  14.968  1.00 17.78           C  
ANISOU 5040  CB  GLU D 106     2614   2108   2035    213   -459   -369       C  
ATOM   5041  CG  GLU D 106      18.596 -24.922  15.796  1.00 19.86           C  
ANISOU 5041  CG  GLU D 106     2924   2333   2289    223   -518   -429       C  
ATOM   5042  CD  GLU D 106      17.438 -24.734  16.776  1.00 23.34           C  
ANISOU 5042  CD  GLU D 106     3469   2778   2621    266   -476   -441       C  
ATOM   5043  OE1 GLU D 106      16.720 -23.707  16.690  1.00 23.08           O  
ANISOU 5043  OE1 GLU D 106     3448   2727   2595    267   -437   -459       O  
ATOM   5044  OE2 GLU D 106      17.231 -25.640  17.624  1.00 26.03           O  
ANISOU 5044  OE2 GLU D 106     3883   3138   2870    303   -473   -430       O  
ATOM   5045  N   TYR D 107      18.002 -27.829  12.544  1.00 15.05           N  
ANISOU 5045  N   TYR D 107     2142   1812   1765    170   -334   -267       N  
ATOM   5046  CA  TYR D 107      17.492 -29.026  11.878  1.00 14.10           C  
ANISOU 5046  CA  TYR D 107     2006   1719   1633    168   -277   -222       C  
ATOM   5047  C   TYR D 107      18.550 -29.619  10.959  1.00 13.66           C  
ANISOU 5047  C   TYR D 107     1882   1666   1643    151   -293   -206       C  
ATOM   5048  O   TYR D 107      18.787 -30.826  10.976  1.00 13.63           O  
ANISOU 5048  O   TYR D 107     1883   1674   1622    163   -295   -186       O  
ATOM   5049  CB  TYR D 107      16.248 -28.705  11.046  1.00 13.62           C  
ANISOU 5049  CB  TYR D 107     1928   1668   1577    156   -201   -201       C  
ATOM   5050  CG  TYR D 107      14.987 -28.446  11.842  1.00 14.01           C  
ANISOU 5050  CG  TYR D 107     2034   1724   1567    177   -161   -208       C  
ATOM   5051  CD1 TYR D 107      14.415 -29.447  12.628  1.00 14.30           C  
ANISOU 5051  CD1 TYR D 107     2121   1774   1538    195   -132   -193       C  
ATOM   5052  CD2 TYR D 107      14.345 -27.215  11.782  1.00 13.56           C  
ANISOU 5052  CD2 TYR D 107     1978   1654   1521    180   -142   -227       C  
ATOM   5053  CE1 TYR D 107      13.249 -29.218  13.348  1.00 14.63           C  
ANISOU 5053  CE1 TYR D 107     2209   1820   1531    214    -77   -197       C  
ATOM   5054  CE2 TYR D 107      13.174 -26.980  12.496  1.00 14.34           C  
ANISOU 5054  CE2 TYR D 107     2119   1757   1570    205    -96   -236       C  
ATOM   5055  CZ  TYR D 107      12.634 -27.986  13.274  1.00 14.67           C  
ANISOU 5055  CZ  TYR D 107     2206   1817   1552    220    -59   -220       C  
ATOM   5056  OH  TYR D 107      11.476 -27.757  13.979  1.00 15.24           O  
ANISOU 5056  OH  TYR D 107     2316   1894   1581    244      3   -227       O  
ATOM   5057  N   ALA D 108      19.177 -28.759  10.160  1.00 13.18           N  
ANISOU 5057  N   ALA D 108     1761   1588   1657    124   -297   -214       N  
ATOM   5058  CA  ALA D 108      20.149 -29.184   9.159  1.00 12.78           C  
ANISOU 5058  CA  ALA D 108     1641   1539   1677    108   -291   -197       C  
ATOM   5059  C   ALA D 108      21.324 -29.935   9.785  1.00 12.99           C  
ANISOU 5059  C   ALA D 108     1651   1564   1721    125   -359   -212       C  
ATOM   5060  O   ALA D 108      21.700 -31.016   9.314  1.00 12.74           O  
ANISOU 5060  O   ALA D 108     1596   1545   1699    135   -345   -190       O  
ATOM   5061  CB  ALA D 108      20.643 -27.989   8.362  1.00 12.57           C  
ANISOU 5061  CB  ALA D 108     1562   1485   1728     75   -277   -203       C  
ATOM   5062  N   THR D 109      21.887 -29.368  10.848  1.00 13.15           N  
ANISOU 5062  N   THR D 109     1686   1566   1744    134   -437   -252       N  
ATOM   5063  CA  THR D 109      23.034 -29.972  11.531  1.00 13.80           C  
ANISOU 5063  CA  THR D 109     1751   1645   1846    158   -522   -273       C  
ATOM   5064  C   THR D 109      22.737 -31.386  12.034  1.00 13.67           C  
ANISOU 5064  C   THR D 109     1795   1649   1752    199   -525   -249       C  
ATOM   5065  O   THR D 109      23.576 -32.281  11.920  1.00 13.92           O  
ANISOU 5065  O   THR D 109     1792   1682   1813    218   -556   -242       O  
ATOM   5066  CB  THR D 109      23.485 -29.127  12.746  1.00 14.46           C  
ANISOU 5066  CB  THR D 109     1865   1705   1924    168   -620   -328       C  
ATOM   5067  OG1 THR D 109      23.669 -27.762  12.349  1.00 14.84           O  
ANISOU 5067  OG1 THR D 109     1868   1725   2047    126   -615   -352       O  
ATOM   5068  CG2 THR D 109      24.792 -29.669  13.323  1.00 15.44           C  
ANISOU 5068  CG2 THR D 109     1954   1824   2090    193   -724   -355       C  
ATOM   5069  N   ARG D 110      21.550 -31.580  12.598  1.00 13.45           N  
ANISOU 5069  N   ARG D 110     1855   1629   1627    213   -490   -235       N  
ATOM   5070  CA  ARG D 110      21.189 -32.869  13.186  1.00 13.90           C  
ANISOU 5070  CA  ARG D 110     1982   1693   1605    248   -485   -207       C  
ATOM   5071  C   ARG D 110      20.874 -33.906  12.119  1.00 13.40           C  
ANISOU 5071  C   ARG D 110     1888   1642   1561    236   -414   -166       C  
ATOM   5072  O   ARG D 110      21.220 -35.080  12.264  1.00 13.95           O  
ANISOU 5072  O   ARG D 110     1976   1709   1615    262   -429   -147       O  
ATOM   5073  CB  ARG D 110      20.004 -32.717  14.132  1.00 13.96           C  
ANISOU 5073  CB  ARG D 110     2091   1702   1512    263   -453   -204       C  
ATOM   5074  CG  ARG D 110      20.327 -31.936  15.391  1.00 14.98           C  
ANISOU 5074  CG  ARG D 110     2282   1815   1593    291   -531   -248       C  
ATOM   5075  CD  ARG D 110      19.245 -32.117  16.433  1.00 15.44           C  
ANISOU 5075  CD  ARG D 110     2457   1874   1534    319   -490   -237       C  
ATOM   5076  NE  ARG D 110      17.924 -31.792  15.905  1.00 15.10           N  
ANISOU 5076  NE  ARG D 110     2405   1844   1489    292   -383   -217       N  
ATOM   5077  CZ  ARG D 110      17.325 -30.606  15.981  1.00 14.69           C  
ANISOU 5077  CZ  ARG D 110     2357   1788   1438    283   -359   -244       C  
ATOM   5078  NH1 ARG D 110      17.906 -29.571  16.586  1.00 16.55           N  
ANISOU 5078  NH1 ARG D 110     2611   2004   1671    295   -433   -294       N  
ATOM   5079  NH2 ARG D 110      16.121 -30.459  15.446  1.00 13.95           N  
ANISOU 5079  NH2 ARG D 110     2244   1707   1349    265   -266   -223       N  
ATOM   5080  N   ILE D 111      20.223 -33.469  11.048  1.00 12.89           N  
ANISOU 5080  N   ILE D 111     1782   1586   1528    201   -344   -153       N  
ATOM   5081  CA  ILE D 111      19.951 -34.349   9.918  1.00 12.36           C  
ANISOU 5081  CA  ILE D 111     1687   1529   1482    190   -285   -123       C  
ATOM   5082  C   ILE D 111      21.278 -34.851   9.333  1.00 12.86           C  
ANISOU 5082  C   ILE D 111     1688   1587   1611    199   -313   -125       C  
ATOM   5083  O   ILE D 111      21.448 -36.052   9.089  1.00 13.03           O  
ANISOU 5083  O   ILE D 111     1717   1607   1627    217   -304   -106       O  
ATOM   5084  CB  ILE D 111      19.098 -33.641   8.848  1.00 11.58           C  
ANISOU 5084  CB  ILE D 111     1559   1439   1403    158   -221   -115       C  
ATOM   5085  CG1 ILE D 111      17.705 -33.322   9.407  1.00 10.93           C  
ANISOU 5085  CG1 ILE D 111     1528   1361   1263    155   -187   -112       C  
ATOM   5086  CG2 ILE D 111      18.941 -34.518   7.596  1.00 10.99           C  
ANISOU 5086  CG2 ILE D 111     1459   1370   1347    150   -174    -91       C  
ATOM   5087  CD1 ILE D 111      16.970 -32.260   8.613  1.00  9.39           C  
ANISOU 5087  CD1 ILE D 111     1306   1171   1091    134   -149   -115       C  
ATOM   5088  N   CYS D 112      22.223 -33.935   9.143  1.00 13.41           N  
ANISOU 5088  N   CYS D 112     1694   1650   1750    187   -344   -149       N  
ATOM   5089  CA  CYS D 112      23.533 -34.292   8.615  1.00 14.05           C  
ANISOU 5089  CA  CYS D 112     1699   1727   1911    195   -364   -154       C  
ATOM   5090  C   CYS D 112      24.276 -35.277   9.509  1.00 14.83           C  
ANISOU 5090  C   CYS D 112     1815   1821   1999    241   -437   -162       C  
ATOM   5091  O   CYS D 112      24.834 -36.257   9.014  1.00 14.67           O  
ANISOU 5091  O   CYS D 112     1767   1800   2008    263   -428   -149       O  
ATOM   5092  CB  CYS D 112      24.375 -33.046   8.388  1.00 14.57           C  
ANISOU 5092  CB  CYS D 112     1690   1781   2065    168   -382   -181       C  
ATOM   5093  SG  CYS D 112      23.912 -32.174   6.895  1.00 14.09           S  
ANISOU 5093  SG  CYS D 112     1596   1719   2038    124   -282   -159       S  
ATOM   5094  N   ASP D 113      24.276 -35.017  10.817  1.00 15.45           N  
ANISOU 5094  N   ASP D 113     1948   1892   2031    262   -512   -182       N  
ATOM   5095  CA  ASP D 113      24.913 -35.911  11.787  1.00 16.28           C  
ANISOU 5095  CA  ASP D 113     2090   1988   2108    314   -595   -188       C  
ATOM   5096  C   ASP D 113      24.368 -37.339  11.688  1.00 15.88           C  
ANISOU 5096  C   ASP D 113     2101   1935   1997    340   -552   -147       C  
ATOM   5097  O   ASP D 113      25.127 -38.301  11.705  1.00 15.72           O  
ANISOU 5097  O   ASP D 113     2069   1905   1998    379   -587   -141       O  
ATOM   5098  CB  ASP D 113      24.729 -35.384  13.218  1.00 17.05           C  
ANISOU 5098  CB  ASP D 113     2269   2078   2133    336   -672   -213       C  
ATOM   5099  CG  ASP D 113      25.781 -34.355  13.610  1.00 19.42           C  
ANISOU 5099  CG  ASP D 113     2506   2368   2506    332   -766   -266       C  
ATOM   5100  OD1 ASP D 113      26.983 -34.582  13.346  1.00 22.03           O  
ANISOU 5100  OD1 ASP D 113     2746   2693   2929    344   -819   -283       O  
ATOM   5101  OD2 ASP D 113      25.407 -33.327  14.215  1.00 21.46           O  
ANISOU 5101  OD2 ASP D 113     2802   2619   2732    318   -790   -294       O  
ATOM   5102  N   LYS D 114      23.049 -37.461  11.571  1.00 15.24           N  
ANISOU 5102  N   LYS D 114     2082   1859   1850    317   -477   -120       N  
ATOM   5103  CA  LYS D 114      22.401 -38.762  11.457  1.00 14.73           C  
ANISOU 5103  CA  LYS D 114     2076   1784   1738    329   -430    -83       C  
ATOM   5104  C   LYS D 114      22.690 -39.436  10.116  1.00 14.17           C  
ANISOU 5104  C   LYS D 114     1943   1714   1728    320   -382    -72       C  
ATOM   5105  O   LYS D 114      22.995 -40.622  10.081  1.00 13.88           O  
ANISOU 5105  O   LYS D 114     1929   1659   1688    351   -388    -55       O  
ATOM   5106  CB  LYS D 114      20.892 -38.639  11.696  1.00 14.48           C  
ANISOU 5106  CB  LYS D 114     2110   1755   1635    301   -361    -63       C  
ATOM   5107  CG  LYS D 114      20.520 -38.529  13.169  1.00 15.69           C  
ANISOU 5107  CG  LYS D 114     2362   1899   1700    327   -391    -61       C  
ATOM   5108  CD  LYS D 114      20.622 -39.881  13.873  1.00 17.09           C  
ANISOU 5108  CD  LYS D 114     2623   2048   1820    368   -406    -29       C  
ATOM   5109  CE  LYS D 114      20.385 -39.763  15.369  1.00 18.54           C  
ANISOU 5109  CE  LYS D 114     2922   2221   1903    404   -438    -25       C  
ATOM   5110  NZ  LYS D 114      20.176 -41.106  15.986  1.00 19.70           N  
ANISOU 5110  NZ  LYS D 114     3168   2333   1982    437   -424     20       N  
ATOM   5111  N   LEU D 115      22.596 -38.686   9.021  1.00 13.75           N  
ANISOU 5111  N   LEU D 115     1823   1677   1726    283   -334    -80       N  
ATOM   5112  CA  LEU D 115      22.976 -39.215   7.710  1.00 13.49           C  
ANISOU 5112  CA  LEU D 115     1737   1643   1744    280   -288    -74       C  
ATOM   5113  C   LEU D 115      24.468 -39.551   7.670  1.00 14.26           C  
ANISOU 5113  C   LEU D 115     1772   1734   1911    317   -334    -89       C  
ATOM   5114  O   LEU D 115      24.878 -40.477   6.964  1.00 13.77           O  
ANISOU 5114  O   LEU D 115     1694   1664   1875    339   -309    -82       O  
ATOM   5115  CB  LEU D 115      22.621 -38.232   6.591  1.00 13.03           C  
ANISOU 5115  CB  LEU D 115     1633   1601   1716    239   -230    -78       C  
ATOM   5116  CG  LEU D 115      21.133 -38.071   6.264  1.00 12.44           C  
ANISOU 5116  CG  LEU D 115     1604   1533   1589    209   -179    -64       C  
ATOM   5117  CD1 LEU D 115      20.936 -37.004   5.190  1.00 12.48           C  
ANISOU 5117  CD1 LEU D 115     1568   1550   1623    180   -136    -68       C  
ATOM   5118  CD2 LEU D 115      20.515 -39.388   5.827  1.00 12.77           C  
ANISOU 5118  CD2 LEU D 115     1686   1564   1601    214   -147    -47       C  
ATOM   5119  N   GLY D 116      25.263 -38.806   8.444  1.00 14.80           N  
ANISOU 5119  N   GLY D 116     1805   1804   2014    326   -405   -114       N  
ATOM   5120  CA  GLY D 116      26.714 -39.005   8.532  1.00 15.97           C  
ANISOU 5120  CA  GLY D 116     1876   1947   2245    362   -463   -135       C  
ATOM   5121  C   GLY D 116      27.143 -40.301   9.207  1.00 16.78           C  
ANISOU 5121  C   GLY D 116     2021   2032   2323    424   -521   -127       C  
ATOM   5122  O   GLY D 116      28.321 -40.667   9.181  1.00 17.05           O  
ANISOU 5122  O   GLY D 116     1987   2059   2431    463   -567   -143       O  
ATOM   5123  N   THR D 117      26.187 -40.987   9.828  1.00 17.04           N  
ANISOU 5123  N   THR D 117     2166   2052   2258    434   -518   -101       N  
ATOM   5124  CA  THR D 117      26.417 -42.315  10.372  1.00 17.86           C  
ANISOU 5124  CA  THR D 117     2331   2128   2325    491   -556    -82       C  
ATOM   5125  C   THR D 117      26.653 -43.339   9.252  1.00 17.70           C  
ANISOU 5125  C   THR D 117     2282   2095   2347    505   -497    -71       C  
ATOM   5126  O   THR D 117      27.288 -44.367   9.470  1.00 18.52           O  
ANISOU 5126  O   THR D 117     2401   2175   2462    562   -536    -65       O  
ATOM   5127  CB  THR D 117      25.220 -42.765  11.233  1.00 17.92           C  
ANISOU 5127  CB  THR D 117     2470   2119   2218    488   -542    -50       C  
ATOM   5128  OG1 THR D 117      25.564 -43.950  11.957  1.00 20.66           O  
ANISOU 5128  OG1 THR D 117     2891   2432   2528    549   -592    -29       O  
ATOM   5129  CG2 THR D 117      24.003 -43.043  10.369  1.00 16.25           C  
ANISOU 5129  CG2 THR D 117     2283   1908   1984    438   -436    -27       C  
ATOM   5130  N   VAL D 118      26.130 -43.046   8.060  1.00 17.01           N  
ANISOU 5130  N   VAL D 118     2163   2022   2277    459   -408    -69       N  
ATOM   5131  CA  VAL D 118      26.227 -43.936   6.900  1.00 16.62           C  
ANISOU 5131  CA  VAL D 118     2100   1960   2255    469   -345    -63       C  
ATOM   5132  C   VAL D 118      26.996 -43.296   5.745  1.00 16.64           C  
ANISOU 5132  C   VAL D 118     1997   1984   2341    458   -298    -83       C  
ATOM   5133  O   VAL D 118      27.820 -43.958   5.110  1.00 16.80           O  
ANISOU 5133  O   VAL D 118     1974   1995   2414    496   -279    -91       O  
ATOM   5134  CB  VAL D 118      24.826 -44.345   6.417  1.00 16.00           C  
ANISOU 5134  CB  VAL D 118     2096   1873   2111    430   -278    -43       C  
ATOM   5135  CG1 VAL D 118      24.893 -45.110   5.099  1.00 15.65           C  
ANISOU 5135  CG1 VAL D 118     2041   1816   2090    437   -216    -46       C  
ATOM   5136  CG2 VAL D 118      24.134 -45.183   7.490  1.00 16.42           C  
ANISOU 5136  CG2 VAL D 118     2252   1895   2092    442   -305    -16       C  
ATOM   5137  N   PHE D 119      26.727 -42.015   5.485  1.00 16.10           N  
ANISOU 5137  N   PHE D 119     1892   1941   2284    408   -273    -90       N  
ATOM   5138  CA  PHE D 119      27.317 -41.292   4.366  1.00 16.30           C  
ANISOU 5138  CA  PHE D 119     1832   1982   2380    389   -212   -101       C  
ATOM   5139  C   PHE D 119      28.415 -40.323   4.833  1.00 17.25           C  
ANISOU 5139  C   PHE D 119     1855   2110   2589    386   -259   -124       C  
ATOM   5140  O   PHE D 119      28.633 -40.142   6.037  1.00 17.79           O  
ANISOU 5140  O   PHE D 119     1931   2175   2654    398   -351   -136       O  
ATOM   5141  CB  PHE D 119      26.230 -40.497   3.641  1.00 15.67           C  
ANISOU 5141  CB  PHE D 119     1783   1915   2255    335   -148    -90       C  
ATOM   5142  CG  PHE D 119      25.106 -41.344   3.089  1.00 14.92           C  
ANISOU 5142  CG  PHE D 119     1770   1811   2086    331   -108    -75       C  
ATOM   5143  CD1 PHE D 119      25.250 -42.009   1.880  1.00 14.40           C  
ANISOU 5143  CD1 PHE D 119     1707   1738   2025    348    -47    -75       C  
ATOM   5144  CD2 PHE D 119      23.900 -41.453   3.768  1.00 13.89           C  
ANISOU 5144  CD2 PHE D 119     1712   1678   1887    310   -128    -63       C  
ATOM   5145  CE1 PHE D 119      24.216 -42.777   1.364  1.00 14.00           C  
ANISOU 5145  CE1 PHE D 119     1730   1675   1913    341    -23    -70       C  
ATOM   5146  CE2 PHE D 119      22.857 -42.215   3.255  1.00 13.41           C  
ANISOU 5146  CE2 PHE D 119     1713   1606   1776    299    -95    -54       C  
ATOM   5147  CZ  PHE D 119      23.016 -42.880   2.054  1.00 13.60           C  
ANISOU 5147  CZ  PHE D 119     1739   1620   1807    313    -49    -60       C  
ATOM   5148  N   LYS D 120      29.110 -39.702   3.882  1.00 17.67           N  
ANISOU 5148  N   LYS D 120     1822   2170   2722    368   -197   -130       N  
ATOM   5149  CA  LYS D 120      30.019 -38.605   4.224  1.00 18.41           C  
ANISOU 5149  CA  LYS D 120     1817   2266   2912    346   -230   -152       C  
ATOM   5150  C   LYS D 120      29.164 -37.428   4.647  1.00 17.59           C  
ANISOU 5150  C   LYS D 120     1754   2166   2763    294   -246   -151       C  
ATOM   5151  O   LYS D 120      28.243 -37.040   3.932  1.00 16.47           O  
ANISOU 5151  O   LYS D 120     1661   2029   2568    261   -176   -131       O  
ATOM   5152  CB  LYS D 120      30.920 -38.181   3.059  1.00 19.17           C  
ANISOU 5152  CB  LYS D 120     1812   2362   3109    333   -139   -153       C  
ATOM   5153  CG  LYS D 120      31.845 -37.017   3.459  1.00 20.81           C  
ANISOU 5153  CG  LYS D 120     1910   2564   3434    299   -174   -178       C  
ATOM   5154  CD  LYS D 120      32.757 -36.543   2.358  1.00 22.60           C  
ANISOU 5154  CD  LYS D 120     2031   2785   3771    279    -71   -174       C  
ATOM   5155  CE  LYS D 120      33.644 -35.387   2.865  1.00 24.06           C  
ANISOU 5155  CE  LYS D 120     2101   2955   4085    237   -115   -202       C  
ATOM   5156  NZ  LYS D 120      34.630 -35.809   3.926  1.00 23.83           N  
ANISOU 5156  NZ  LYS D 120     1990   2924   4141    277   -241   -244       N  
ATOM   5157  N   ASN D 121      29.459 -36.872   5.817  1.00 17.67           N  
ANISOU 5157  N   ASN D 121     1750   2172   2792    291   -343   -177       N  
ATOM   5158  CA  ASN D 121      28.775 -35.674   6.274  1.00 17.20           C  
ANISOU 5158  CA  ASN D 121     1725   2111   2701    246   -360   -183       C  
ATOM   5159  C   ASN D 121      29.458 -34.457   5.655  1.00 17.66           C  
ANISOU 5159  C   ASN D 121     1687   2159   2865    199   -320   -194       C  
ATOM   5160  O   ASN D 121      30.541 -34.059   6.089  1.00 18.61           O  
ANISOU 5160  O   ASN D 121     1716   2267   3087    196   -379   -226       O  
ATOM   5161  CB  ASN D 121      28.790 -35.591   7.803  1.00 17.42           C  
ANISOU 5161  CB  ASN D 121     1792   2133   2692    267   -481   -210       C  
ATOM   5162  CG  ASN D 121      27.989 -34.418   8.331  1.00 16.91           C  
ANISOU 5162  CG  ASN D 121     1778   2065   2582    228   -496   -220       C  
ATOM   5163  OD1 ASN D 121      27.505 -33.581   7.566  1.00 14.78           O  
ANISOU 5163  OD1 ASN D 121     1500   1794   2321    184   -423   -208       O  
ATOM   5164  ND2 ASN D 121      27.842 -34.352   9.649  1.00 17.02           N  
ANISOU 5164  ND2 ASN D 121     1852   2074   2540    251   -591   -242       N  
ATOM   5165  N   ARG D 122      28.831 -33.889   4.628  1.00 17.13           N  
ANISOU 5165  N   ARG D 122     1639   2091   2777    163   -223   -168       N  
ATOM   5166  CA  ARG D 122      29.332 -32.671   3.999  1.00 17.64           C  
ANISOU 5166  CA  ARG D 122     1634   2137   2930    114   -170   -168       C  
ATOM   5167  C   ARG D 122      28.882 -31.424   4.759  1.00 17.60           C  
ANISOU 5167  C   ARG D 122     1655   2115   2917     76   -222   -187       C  
ATOM   5168  O   ARG D 122      29.386 -30.331   4.510  1.00 17.83           O  
ANISOU 5168  O   ARG D 122     1625   2118   3033     32   -201   -195       O  
ATOM   5169  CB  ARG D 122      28.885 -32.590   2.538  1.00 17.40           C  
ANISOU 5169  CB  ARG D 122     1630   2109   2872    100    -43   -128       C  
ATOM   5170  CG  ARG D 122      29.362 -33.765   1.682  1.00 18.10           C  
ANISOU 5170  CG  ARG D 122     1700   2209   2967    140     19   -114       C  
ATOM   5171  CD  ARG D 122      28.499 -33.950   0.445  1.00 18.09           C  
ANISOU 5171  CD  ARG D 122     1776   2214   2882    142    115    -80       C  
ATOM   5172  NE  ARG D 122      28.640 -32.851  -0.506  1.00 19.24           N  
ANISOU 5172  NE  ARG D 122     1906   2342   3062    104    204    -57       N  
ATOM   5173  CZ  ARG D 122      29.666 -32.684  -1.335  1.00 21.39           C  
ANISOU 5173  CZ  ARG D 122     2107   2601   3418     99    292    -46       C  
ATOM   5174  NH1 ARG D 122      30.685 -33.539  -1.350  1.00 22.57           N  
ANISOU 5174  NH1 ARG D 122     2182   2756   3635    132    300    -61       N  
ATOM   5175  NH2 ARG D 122      29.676 -31.642  -2.157  1.00 22.79           N  
ANISOU 5175  NH2 ARG D 122     2290   2757   3614     63    377    -18       N  
ATOM   5176  N   GLY D 123      27.929 -31.587   5.675  1.00 17.10           N  
ANISOU 5176  N   GLY D 123     1683   2062   2753     93   -283   -194       N  
ATOM   5177  CA  GLY D 123      27.565 -30.523   6.608  1.00 17.30           C  
ANISOU 5177  CA  GLY D 123     1740   2071   2764     71   -347   -222       C  
ATOM   5178  C   GLY D 123      26.395 -29.652   6.190  1.00 16.54           C  
ANISOU 5178  C   GLY D 123     1707   1967   2608     43   -289   -202       C  
ATOM   5179  O   GLY D 123      25.964 -29.662   5.032  1.00 16.19           O  
ANISOU 5179  O   GLY D 123     1673   1929   2550     33   -198   -165       O  
ATOM   5180  N   ALA D 124      25.881 -28.897   7.156  1.00 16.39           N  
ANISOU 5180  N   ALA D 124     1737   1936   2553     37   -347   -228       N  
ATOM   5181  CA  ALA D 124      24.807 -27.944   6.917  1.00 16.03           C  
ANISOU 5181  CA  ALA D 124     1748   1879   2462     17   -305   -217       C  
ATOM   5182  C   ALA D 124      25.354 -26.747   6.143  1.00 16.59           C  
ANISOU 5182  C   ALA D 124     1762   1912   2629    -30   -261   -213       C  
ATOM   5183  O   ALA D 124      26.417 -26.223   6.478  1.00 17.17           O  
ANISOU 5183  O   ALA D 124     1767   1956   2800    -55   -305   -244       O  
ATOM   5184  CB  ALA D 124      24.205 -27.486   8.234  1.00 15.88           C  
ANISOU 5184  CB  ALA D 124     1798   1855   2382     31   -377   -251       C  
ATOM   5185  N   LYS D 125      24.631 -26.312   5.116  1.00 16.08           N  
ANISOU 5185  N   LYS D 125     1728   1842   2539    -42   -177   -175       N  
ATOM   5186  CA  LYS D 125      25.085 -25.201   4.283  1.00 16.90           C  
ANISOU 5186  CA  LYS D 125     1794   1902   2723    -84   -120   -160       C  
ATOM   5187  C   LYS D 125      23.999 -24.145   4.092  1.00 16.61           C  
ANISOU 5187  C   LYS D 125     1829   1843   2641    -90    -96   -147       C  
ATOM   5188  O   LYS D 125      22.875 -24.460   3.720  1.00 15.77           O  
ANISOU 5188  O   LYS D 125     1784   1762   2447    -63    -67   -124       O  
ATOM   5189  CB  LYS D 125      25.576 -25.728   2.936  1.00 16.97           C  
ANISOU 5189  CB  LYS D 125     1768   1920   2761    -86    -26   -117       C  
ATOM   5190  CG  LYS D 125      26.787 -26.647   3.068  1.00 18.26           C  
ANISOU 5190  CG  LYS D 125     1846   2099   2993    -78    -43   -132       C  
ATOM   5191  CD  LYS D 125      27.245 -27.207   1.733  1.00 19.08           C  
ANISOU 5191  CD  LYS D 125     1922   2211   3117    -73     61    -92       C  
ATOM   5192  CE  LYS D 125      28.338 -28.243   1.939  1.00 19.54           C  
ANISOU 5192  CE  LYS D 125     1899   2288   3237    -52     40   -110       C  
ATOM   5193  NZ  LYS D 125      28.845 -28.782   0.649  1.00 20.46           N  
ANISOU 5193  NZ  LYS D 125     1988   2411   3376    -41    150    -76       N  
ATOM   5194  N   LEU D 126      24.346 -22.891   4.370  1.00 17.47           N  
ANISOU 5194  N   LEU D 126     1923   1897   2817   -126   -113   -167       N  
ATOM   5195  CA  LEU D 126      23.442 -21.758   4.145  1.00 17.59           C  
ANISOU 5195  CA  LEU D 126     2001   1877   2804   -131    -88   -156       C  
ATOM   5196  C   LEU D 126      23.264 -21.502   2.642  1.00 17.65           C  
ANISOU 5196  C   LEU D 126     2024   1871   2812   -138     14    -95       C  
ATOM   5197  O   LEU D 126      24.241 -21.458   1.899  1.00 18.21           O  
ANISOU 5197  O   LEU D 126     2040   1920   2958   -168     71    -72       O  
ATOM   5198  CB  LEU D 126      24.007 -20.507   4.836  1.00 18.41           C  
ANISOU 5198  CB  LEU D 126     2086   1917   2993   -171   -136   -197       C  
ATOM   5199  CG  LEU D 126      23.182 -19.215   4.819  1.00 18.80           C  
ANISOU 5199  CG  LEU D 126     2202   1915   3025   -174   -125   -196       C  
ATOM   5200  CD1 LEU D 126      21.868 -19.378   5.570  1.00 17.11           C  
ANISOU 5200  CD1 LEU D 126     2066   1735   2699   -123   -163   -216       C  
ATOM   5201  CD2 LEU D 126      24.003 -18.070   5.406  1.00 20.00           C  
ANISOU 5201  CD2 LEU D 126     2322   1993   3282   -223   -172   -240       C  
ATOM   5202  N   ASP D 127      22.019 -21.366   2.187  1.00 17.54           N  
ANISOU 5202  N   ASP D 127     2084   1869   2712   -106     38    -70       N  
ATOM   5203  CA  ASP D 127      21.753 -20.907   0.820  1.00 18.07           C  
ANISOU 5203  CA  ASP D 127     2187   1912   2767   -105    120    -15       C  
ATOM   5204  C   ASP D 127      20.462 -20.072   0.752  1.00 18.51           C  
ANISOU 5204  C   ASP D 127     2320   1949   2765    -77    112     -7       C  
ATOM   5205  O   ASP D 127      19.357 -20.614   0.709  1.00 18.15           O  
ANISOU 5205  O   ASP D 127     2312   1946   2636    -34     96     -5       O  
ATOM   5206  CB  ASP D 127      21.698 -22.092  -0.155  1.00 17.88           C  
ANISOU 5206  CB  ASP D 127     2167   1936   2690    -78    169     19       C  
ATOM   5207  CG  ASP D 127      21.775 -21.657  -1.617  1.00 17.90           C  
ANISOU 5207  CG  ASP D 127     2207   1909   2685    -78    260     76       C  
ATOM   5208  OD1 ASP D 127      21.568 -20.462  -1.911  1.00 18.46           O  
ANISOU 5208  OD1 ASP D 127     2317   1925   2773    -90    283     96       O  
ATOM   5209  OD2 ASP D 127      22.045 -22.513  -2.477  1.00 18.25           O  
ANISOU 5209  OD2 ASP D 127     2252   1981   2701    -63    310    101       O  
ATOM   5210  N   LYS D 128      20.621 -18.750   0.728  1.00 19.70           N  
ANISOU 5210  N   LYS D 128     2488   2030   2968   -101    123     -3       N  
ATOM   5211  CA  LYS D 128      19.484 -17.829   0.700  1.00 19.97           C  
ANISOU 5211  CA  LYS D 128     2593   2036   2960    -71    113      2       C  
ATOM   5212  C   LYS D 128      18.908 -17.617  -0.703  1.00 20.20           C  
ANISOU 5212  C   LYS D 128     2681   2053   2939    -42    174     64       C  
ATOM   5213  O   LYS D 128      17.839 -17.016  -0.851  1.00 20.32           O  
ANISOU 5213  O   LYS D 128     2755   2055   2911     -3    160     71       O  
ATOM   5214  CB  LYS D 128      19.875 -16.476   1.309  1.00 20.79           C  
ANISOU 5214  CB  LYS D 128     2700   2059   3140   -106     93    -23       C  
ATOM   5215  CG  LYS D 128      20.240 -16.540   2.793  1.00 21.33           C  
ANISOU 5215  CG  LYS D 128     2732   2134   3238   -121     13    -94       C  
ATOM   5216  CD  LYS D 128      20.319 -15.151   3.411  1.00 22.12           C  
ANISOU 5216  CD  LYS D 128     2858   2152   3395   -143    -18   -128       C  
ATOM   5217  CE  LYS D 128      20.373 -15.212   4.926  1.00 22.74           C  
ANISOU 5217  CE  LYS D 128     2930   2241   3468   -138   -108   -204       C  
ATOM   5218  NZ  LYS D 128      20.456 -13.845   5.538  1.00 23.13           N  
ANISOU 5218  NZ  LYS D 128     3011   2204   3571   -158   -144   -246       N  
ATOM   5219  N   ARG D 129      19.603 -18.116  -1.724  1.00 20.45           N  
ANISOU 5219  N   ARG D 129     2703   2092   2976    -55    239    105       N  
ATOM   5220  CA  ARG D 129      19.192 -17.913  -3.111  1.00 20.93           C  
ANISOU 5220  CA  ARG D 129     2834   2137   2981    -25    299    166       C  
ATOM   5221  C   ARG D 129      18.050 -18.827  -3.540  1.00 19.87           C  
ANISOU 5221  C   ARG D 129     2737   2069   2744     35    269    168       C  
ATOM   5222  O   ARG D 129      17.379 -18.540  -4.517  1.00 20.78           O  
ANISOU 5222  O   ARG D 129     2925   2173   2800     74    286    206       O  
ATOM   5223  CB  ARG D 129      20.376 -18.131  -4.058  1.00 21.92           C  
ANISOU 5223  CB  ARG D 129     2943   2244   3143    -56    390    208       C  
ATOM   5224  CG  ARG D 129      21.545 -17.191  -3.831  1.00 24.80           C  
ANISOU 5224  CG  ARG D 129     3262   2534   3627   -122    434    213       C  
ATOM   5225  CD  ARG D 129      22.699 -17.478  -4.804  1.00 28.28           C  
ANISOU 5225  CD  ARG D 129     3677   2960   4110   -152    542    258       C  
ATOM   5226  NE  ARG D 129      23.435 -18.704  -4.466  1.00 30.32           N  
ANISOU 5226  NE  ARG D 129     3846   3279   4395   -161    533    226       N  
ATOM   5227  CZ  ARG D 129      24.489 -19.174  -5.140  1.00 32.47           C  
ANISOU 5227  CZ  ARG D 129     4073   3551   4711   -181    621    251       C  
ATOM   5228  NH1 ARG D 129      24.958 -18.532  -6.210  1.00 34.37           N  
ANISOU 5228  NH1 ARG D 129     4352   3735   4971   -198    736    312       N  
ATOM   5229  NH2 ARG D 129      25.082 -20.295  -4.741  1.00 32.78           N  
ANISOU 5229  NH2 ARG D 129     4033   3646   4777   -181    600    217       N  
ATOM   5230  N   LEU D 130      17.839 -19.928  -2.823  1.00 18.51           N  
ANISOU 5230  N   LEU D 130     2519   1962   2553     41    222    127       N  
ATOM   5231  CA  LEU D 130      16.859 -20.940  -3.233  1.00 17.36           C  
ANISOU 5231  CA  LEU D 130     2395   1876   2326     86    197    126       C  
ATOM   5232  C   LEU D 130      15.447 -20.535  -2.846  1.00 16.22           C  
ANISOU 5232  C   LEU D 130     2278   1740   2146    126    141    107       C  
ATOM   5233  O   LEU D 130      15.161 -20.324  -1.673  1.00 15.74           O  
ANISOU 5233  O   LEU D 130     2188   1683   2110    119    103     68       O  
ATOM   5234  CB  LEU D 130      17.198 -22.296  -2.609  1.00 16.82           C  
ANISOU 5234  CB  LEU D 130     2270   1864   2258     74    175     94       C  
ATOM   5235  CG  LEU D 130      18.544 -22.856  -3.062  1.00 17.27           C  
ANISOU 5235  CG  LEU D 130     2291   1919   2350     46    229    109       C  
ATOM   5236  CD1 LEU D 130      18.920 -24.070  -2.239  1.00 16.76           C  
ANISOU 5236  CD1 LEU D 130     2170   1900   2296     38    196     74       C  
ATOM   5237  CD2 LEU D 130      18.510 -23.191  -4.545  1.00 18.10           C  
ANISOU 5237  CD2 LEU D 130     2451   2026   2398     73    285    151       C  
ATOM   5238  N   TYR D 131      14.563 -20.453  -3.836  1.00 15.64           N  
ANISOU 5238  N   TYR D 131     2259   1669   2015    171    136    133       N  
ATOM   5239  CA  TYR D 131      13.187 -20.007  -3.601  1.00 14.90           C  
ANISOU 5239  CA  TYR D 131     2183   1580   1899    216     85    117       C  
ATOM   5240  C   TYR D 131      12.428 -20.892  -2.601  1.00 13.60           C  
ANISOU 5240  C   TYR D 131     1963   1473   1731    220     40     69       C  
ATOM   5241  O   TYR D 131      11.607 -20.398  -1.838  1.00 13.37           O  
ANISOU 5241  O   TYR D 131     1922   1443   1714    240     11     43       O  
ATOM   5242  CB  TYR D 131      12.409 -19.902  -4.926  1.00 15.44           C  
ANISOU 5242  CB  TYR D 131     2317   1645   1904    270     74    150       C  
ATOM   5243  CG  TYR D 131      12.041 -21.230  -5.555  1.00 14.97           C  
ANISOU 5243  CG  TYR D 131     2254   1643   1792    287     53    143       C  
ATOM   5244  CD1 TYR D 131      10.918 -21.933  -5.134  1.00 15.38           C  
ANISOU 5244  CD1 TYR D 131     2266   1743   1836    308     -5    105       C  
ATOM   5245  CD2 TYR D 131      12.808 -21.774  -6.585  1.00 15.94           C  
ANISOU 5245  CD2 TYR D 131     2416   1766   1876    283     96    174       C  
ATOM   5246  CE1 TYR D 131      10.577 -23.153  -5.702  1.00 14.97           C  
ANISOU 5246  CE1 TYR D 131     2209   1734   1744    318    -28     94       C  
ATOM   5247  CE2 TYR D 131      12.471 -22.994  -7.165  1.00 15.11           C  
ANISOU 5247  CE2 TYR D 131     2314   1705   1720    301     73    161       C  
ATOM   5248  CZ  TYR D 131      11.353 -23.676  -6.720  1.00 15.22           C  
ANISOU 5248  CZ  TYR D 131     2286   1763   1732    316      6    119       C  
ATOM   5249  OH  TYR D 131      11.003 -24.881  -7.275  1.00 15.74           O  
ANISOU 5249  OH  TYR D 131     2357   1867   1758    328    -23    102       O  
ATOM   5250  N   ILE D 132      12.697 -22.196  -2.598  1.00 12.42           N  
ANISOU 5250  N   ILE D 132     1784   1371   1566    204     41     59       N  
ATOM   5251  CA  ILE D 132      11.973 -23.096  -1.704  1.00 11.53           C  
ANISOU 5251  CA  ILE D 132     1625   1306   1449    205      9     22       C  
ATOM   5252  C   ILE D 132      12.311 -22.780  -0.248  1.00 11.56           C  
ANISOU 5252  C   ILE D 132     1601   1303   1489    181      6     -8       C  
ATOM   5253  O   ILE D 132      11.516 -23.055   0.640  1.00 11.18           O  
ANISOU 5253  O   ILE D 132     1531   1279   1437    191    -12    -37       O  
ATOM   5254  CB  ILE D 132      12.255 -24.593  -2.005  1.00 11.14           C  
ANISOU 5254  CB  ILE D 132     1558   1298   1377    192     12     19       C  
ATOM   5255  CG1 ILE D 132      11.182 -25.492  -1.380  1.00 10.24           C  
ANISOU 5255  CG1 ILE D 132     1411   1225   1256    199    -18    -11       C  
ATOM   5256  CG2 ILE D 132      13.625 -25.004  -1.479  1.00 10.29           C  
ANISOU 5256  CG2 ILE D 132     1426   1187   1297    153     38     17       C  
ATOM   5257  CD1 ILE D 132       9.758 -25.194  -1.808  1.00 10.58           C  
ANISOU 5257  CD1 ILE D 132     1455   1276   1290    238    -52    -18       C  
ATOM   5258  N   LEU D 133      13.486 -22.193  -0.018  1.00 11.97           N  
ANISOU 5258  N   LEU D 133     1654   1318   1577    150     25     -3       N  
ATOM   5259  CA  LEU D 133      13.888 -21.755   1.318  1.00 12.28           C  
ANISOU 5259  CA  LEU D 133     1676   1341   1648    130      9    -37       C  
ATOM   5260  C   LEU D 133      13.507 -20.301   1.613  1.00 12.68           C  
ANISOU 5260  C   LEU D 133     1756   1342   1720    144      2    -46       C  
ATOM   5261  O   LEU D 133      13.048 -19.998   2.713  1.00 12.97           O  
ANISOU 5261  O   LEU D 133     1793   1378   1756    155    -20    -83       O  
ATOM   5262  CB  LEU D 133      15.397 -21.934   1.499  1.00 12.33           C  
ANISOU 5262  CB  LEU D 133     1655   1332   1696     87     18    -38       C  
ATOM   5263  CG  LEU D 133      15.958 -23.340   1.257  1.00 12.39           C  
ANISOU 5263  CG  LEU D 133     1634   1382   1691     77     27    -31       C  
ATOM   5264  CD1 LEU D 133      17.461 -23.356   1.473  1.00 12.31           C  
ANISOU 5264  CD1 LEU D 133     1586   1352   1740     40     33    -35       C  
ATOM   5265  CD2 LEU D 133      15.282 -24.377   2.158  1.00 10.14           C  
ANISOU 5265  CD2 LEU D 133     1341   1144   1369     91     -2    -56       C  
ATOM   5266  N   ASN D 134      13.706 -19.400   0.652  1.00 13.33           N  
ANISOU 5266  N   ASN D 134     1870   1375   1818    147     23    -13       N  
ATOM   5267  CA  ASN D 134      13.497 -17.973   0.911  1.00 13.82           C  
ANISOU 5267  CA  ASN D 134     1966   1375   1909    157     18    -19       C  
ATOM   5268  C   ASN D 134      12.053 -17.485   0.700  1.00 14.17           C  
ANISOU 5268  C   ASN D 134     2039   1421   1924    217      2    -19       C  
ATOM   5269  O   ASN D 134      11.704 -16.398   1.163  1.00 14.11           O  
ANISOU 5269  O   ASN D 134     2057   1367   1937    236     -8    -36       O  
ATOM   5270  CB  ASN D 134      14.503 -17.106   0.136  1.00 14.15           C  
ANISOU 5270  CB  ASN D 134     2033   1349   1995    125     55     18       C  
ATOM   5271  CG  ASN D 134      14.253 -17.087  -1.369  1.00 14.40           C  
ANISOU 5271  CG  ASN D 134     2108   1373   1990    151     89     75       C  
ATOM   5272  OD1 ASN D 134      13.113 -17.080  -1.826  1.00 13.42           O  
ANISOU 5272  OD1 ASN D 134     2013   1266   1819    204     68     84       O  
ATOM   5273  ND2 ASN D 134      15.329 -17.063  -2.140  1.00 13.22           N  
ANISOU 5273  ND2 ASN D 134     1965   1195   1863    116    141    113       N  
ATOM   5274  N   SER D 135      11.231 -18.278   0.009  1.00 14.04           N  
ANISOU 5274  N   SER D 135     2015   1453   1866    249     -6     -5       N  
ATOM   5275  CA  SER D 135       9.825 -17.931  -0.243  1.00 14.89           C  
ANISOU 5275  CA  SER D 135     2133   1567   1956    309    -31     -8       C  
ATOM   5276  C   SER D 135       8.832 -18.766   0.564  1.00 14.63           C  
ANISOU 5276  C   SER D 135     2048   1595   1914    325    -48    -47       C  
ATOM   5277  O   SER D 135       7.624 -18.537   0.473  1.00 14.92           O  
ANISOU 5277  O   SER D 135     2074   1643   1952    374    -68    -57       O  
ATOM   5278  CB  SER D 135       9.501 -18.069  -1.734  1.00 14.99           C  
ANISOU 5278  CB  SER D 135     2180   1582   1934    340    -39     34       C  
ATOM   5279  OG  SER D 135      10.363 -17.246  -2.493  1.00 16.98           O  
ANISOU 5279  OG  SER D 135     2489   1771   2189    328     -8     77       O  
ATOM   5280  N   SER D 136       9.334 -19.722   1.346  1.00 14.62           N  
ANISOU 5280  N   SER D 136     2015   1630   1909    287    -38    -66       N  
ATOM   5281  CA  SER D 136       8.484 -20.595   2.149  1.00 14.67           C  
ANISOU 5281  CA  SER D 136     1979   1689   1907    295    -39    -96       C  
ATOM   5282  C   SER D 136       8.371 -20.053   3.565  1.00 14.73           C  
ANISOU 5282  C   SER D 136     1992   1684   1923    300    -29   -133       C  
ATOM   5283  O   SER D 136       9.362 -19.683   4.195  1.00 14.46           O  
ANISOU 5283  O   SER D 136     1980   1620   1893    272    -29   -145       O  
ATOM   5284  CB  SER D 136       9.021 -22.030   2.180  1.00 14.65           C  
ANISOU 5284  CB  SER D 136     1952   1728   1887    257    -32    -91       C  
ATOM   5285  OG  SER D 136      10.198 -22.143   2.978  1.00 16.42           O  
ANISOU 5285  OG  SER D 136     2184   1942   2114    220    -25   -101       O  
ATOM   5286  N   LYS D 137       7.150 -20.034   4.067  1.00 14.49           N  
ANISOU 5286  N   LYS D 137     1937   1673   1894    336    -20   -156       N  
ATOM   5287  CA  LYS D 137       6.879 -19.441   5.355  1.00 15.06           C  
ANISOU 5287  CA  LYS D 137     2025   1732   1966    354     -2   -193       C  
ATOM   5288  C   LYS D 137       7.408 -20.213   6.575  1.00 14.05           C  
ANISOU 5288  C   LYS D 137     1905   1626   1807    325     14   -214       C  
ATOM   5289  O   LYS D 137       8.028 -19.619   7.452  1.00 13.90           O  
ANISOU 5289  O   LYS D 137     1928   1577   1777    320      8   -240       O  
ATOM   5290  CB  LYS D 137       5.388 -19.208   5.491  1.00 15.86           C  
ANISOU 5290  CB  LYS D 137     2093   1849   2085    407     14   -210       C  
ATOM   5291  CG  LYS D 137       5.116 -17.980   6.231  1.00 19.01           C  
ANISOU 5291  CG  LYS D 137     2525   2206   2491    446     24   -241       C  
ATOM   5292  CD  LYS D 137       3.739 -17.471   5.982  1.00 22.02           C  
ANISOU 5292  CD  LYS D 137     2870   2589   2906    509     30   -251       C  
ATOM   5293  CE  LYS D 137       3.842 -16.003   5.831  1.00 24.35           C  
ANISOU 5293  CE  LYS D 137     3217   2818   3218    546     12   -257       C  
ATOM   5294  NZ  LYS D 137       4.529 -15.374   7.008  1.00 25.60           N  
ANISOU 5294  NZ  LYS D 137     3434   2937   3356    536     27   -293       N  
ATOM   5295  N   PRO D 138       7.156 -21.531   6.644  1.00 13.10           N  
ANISOU 5295  N   PRO D 138     1751   1554   1671    307     30   -204       N  
ATOM   5296  CA  PRO D 138       7.746 -22.284   7.754  1.00 12.62           C  
ANISOU 5296  CA  PRO D 138     1713   1509   1574    283     42   -217       C  
ATOM   5297  C   PRO D 138       9.265 -22.360   7.644  1.00 11.91           C  
ANISOU 5297  C   PRO D 138     1645   1399   1480    246      6   -209       C  
ATOM   5298  O   PRO D 138       9.817 -22.150   6.566  1.00 11.39           O  
ANISOU 5298  O   PRO D 138     1568   1318   1441    230    -13   -186       O  
ATOM   5299  CB  PRO D 138       7.152 -23.682   7.580  1.00 12.28           C  
ANISOU 5299  CB  PRO D 138     1628   1511   1526    269     66   -199       C  
ATOM   5300  CG  PRO D 138       6.837 -23.759   6.126  1.00 12.62           C  
ANISOU 5300  CG  PRO D 138     1633   1560   1601    269     44   -176       C  
ATOM   5301  CD  PRO D 138       6.346 -22.402   5.774  1.00 12.84           C  
ANISOU 5301  CD  PRO D 138     1667   1558   1653    308     33   -185       C  
ATOM   5302  N   THR D 139       9.928 -22.647   8.756  1.00 11.41           N  
ANISOU 5302  N   THR D 139     1616   1335   1386    236     -4   -230       N  
ATOM   5303  CA  THR D 139      11.329 -23.039   8.717  1.00 10.76           C  
ANISOU 5303  CA  THR D 139     1536   1244   1307    201    -41   -224       C  
ATOM   5304  C   THR D 139      11.496 -24.125   7.652  1.00 10.36           C  
ANISOU 5304  C   THR D 139     1445   1222   1269    179    -33   -187       C  
ATOM   5305  O   THR D 139      10.756 -25.107   7.652  1.00  9.72           O  
ANISOU 5305  O   THR D 139     1350   1175   1169    183     -8   -175       O  
ATOM   5306  CB  THR D 139      11.777 -23.593  10.075  1.00 11.22           C  
ANISOU 5306  CB  THR D 139     1635   1311   1317    204    -56   -247       C  
ATOM   5307  OG1 THR D 139      11.527 -22.610  11.091  1.00 10.58           O  
ANISOU 5307  OG1 THR D 139     1604   1204   1212    231    -62   -288       O  
ATOM   5308  CG2 THR D 139      13.260 -23.976  10.037  1.00 10.11           C  
ANISOU 5308  CG2 THR D 139     1486   1161   1193    174   -106   -246       C  
ATOM   5309  N   ALA D 140      12.446 -23.935   6.737  1.00 10.23           N  
ANISOU 5309  N   ALA D 140     1411   1188   1286    156    -50   -169       N  
ATOM   5310  CA  ALA D 140      12.628 -24.851   5.612  1.00  9.80           C  
ANISOU 5310  CA  ALA D 140     1329   1155   1240    142    -40   -137       C  
ATOM   5311  C   ALA D 140      14.044 -25.394   5.547  1.00  9.81           C  
ANISOU 5311  C   ALA D 140     1317   1153   1258    115    -57   -131       C  
ATOM   5312  O   ALA D 140      15.016 -24.677   5.826  1.00  9.72           O  
ANISOU 5312  O   ALA D 140     1305   1110   1279    100    -78   -144       O  
ATOM   5313  CB  ALA D 140      12.270 -24.157   4.282  1.00 10.03           C  
ANISOU 5313  CB  ALA D 140     1353   1168   1289    151    -29   -114       C  
ATOM   5314  N   VAL D 141      14.143 -26.676   5.196  1.00  9.43           N  
ANISOU 5314  N   VAL D 141     1255   1134   1196    110    -49   -115       N  
ATOM   5315  CA  VAL D 141      15.421 -27.311   4.874  1.00  9.68           C  
ANISOU 5315  CA  VAL D 141     1265   1163   1249     93    -57   -106       C  
ATOM   5316  C   VAL D 141      15.311 -28.104   3.577  1.00  9.39           C  
ANISOU 5316  C   VAL D 141     1218   1143   1209     93    -31    -79       C  
ATOM   5317  O   VAL D 141      14.251 -28.650   3.250  1.00  9.31           O  
ANISOU 5317  O   VAL D 141     1215   1153   1171    104    -20    -73       O  
ATOM   5318  CB  VAL D 141      15.925 -28.259   5.989  1.00  9.67           C  
ANISOU 5318  CB  VAL D 141     1270   1175   1228     95    -85   -120       C  
ATOM   5319  CG1 VAL D 141      16.250 -27.473   7.253  1.00 10.21           C  
ANISOU 5319  CG1 VAL D 141     1361   1225   1294     99   -123   -152       C  
ATOM   5320  CG2 VAL D 141      14.913 -29.354   6.261  1.00  9.52           C  
ANISOU 5320  CG2 VAL D 141     1270   1182   1164    106    -66   -112       C  
ATOM   5321  N   LEU D 142      16.416 -28.151   2.845  1.00  9.37           N  
ANISOU 5321  N   LEU D 142     1195   1128   1237     81    -19    -65       N  
ATOM   5322  CA  LEU D 142      16.512 -28.912   1.612  1.00  9.31           C  
ANISOU 5322  CA  LEU D 142     1187   1131   1219     86      9    -43       C  
ATOM   5323  C   LEU D 142      17.532 -30.012   1.860  1.00  9.58           C  
ANISOU 5323  C   LEU D 142     1198   1174   1267     83      4    -47       C  
ATOM   5324  O   LEU D 142      18.695 -29.728   2.140  1.00 10.01           O  
ANISOU 5324  O   LEU D 142     1222   1214   1368     72     -1    -52       O  
ATOM   5325  CB  LEU D 142      16.948 -27.993   0.469  1.00  9.37           C  
ANISOU 5325  CB  LEU D 142     1198   1113   1247     82     44    -21       C  
ATOM   5326  CG  LEU D 142      16.843 -28.493  -0.972  1.00  9.18           C  
ANISOU 5326  CG  LEU D 142     1199   1096   1194     97     78      3       C  
ATOM   5327  CD1 LEU D 142      16.858 -27.302  -1.920  1.00  9.62           C  
ANISOU 5327  CD1 LEU D 142     1283   1121   1252    100    110     30       C  
ATOM   5328  CD2 LEU D 142      17.967 -29.472  -1.323  1.00  8.43           C  
ANISOU 5328  CD2 LEU D 142     1081   1006   1114     94    103      7       C  
ATOM   5329  N   ILE D 143      17.094 -31.266   1.784  1.00  9.60           N  
ANISOU 5329  N   ILE D 143     1213   1197   1238     93      2    -46       N  
ATOM   5330  CA  ILE D 143      17.971 -32.400   2.071  1.00  9.72           C  
ANISOU 5330  CA  ILE D 143     1214   1215   1263     98     -6    -50       C  
ATOM   5331  C   ILE D 143      18.510 -32.985   0.769  1.00 10.19           C  
ANISOU 5331  C   ILE D 143     1270   1274   1327    107     31    -36       C  
ATOM   5332  O   ILE D 143      17.740 -33.454  -0.073  1.00  9.92           O  
ANISOU 5332  O   ILE D 143     1265   1246   1257    115     45    -31       O  
ATOM   5333  CB  ILE D 143      17.240 -33.508   2.874  1.00  9.58           C  
ANISOU 5333  CB  ILE D 143     1222   1209   1209    105    -25    -55       C  
ATOM   5334  CG1 ILE D 143      16.712 -32.947   4.198  1.00  9.32           C  
ANISOU 5334  CG1 ILE D 143     1205   1177   1160    102    -49    -67       C  
ATOM   5335  CG2 ILE D 143      18.180 -34.674   3.176  1.00  9.22           C  
ANISOU 5335  CG2 ILE D 143     1171   1160   1172    117    -38    -56       C  
ATOM   5336  CD1 ILE D 143      15.774 -33.893   4.923  1.00  9.77           C  
ANISOU 5336  CD1 ILE D 143     1292   1240   1178    105    -47    -65       C  
ATOM   5337  N   GLU D 144      19.831 -32.925   0.611  1.00 10.83           N  
ANISOU 5337  N   GLU D 144     1314   1345   1456    107     45    -35       N  
ATOM   5338  CA  GLU D 144      20.535 -33.631  -0.448  1.00 11.76           C  
ANISOU 5338  CA  GLU D 144     1425   1461   1581    122     88    -25       C  
ATOM   5339  C   GLU D 144      21.075 -34.926   0.176  1.00 11.73           C  
ANISOU 5339  C   GLU D 144     1409   1462   1587    140     62    -38       C  
ATOM   5340  O   GLU D 144      22.222 -34.980   0.622  1.00 11.79           O  
ANISOU 5340  O   GLU D 144     1367   1463   1649    145     51    -45       O  
ATOM   5341  CB  GLU D 144      21.675 -32.771  -1.001  1.00 12.65           C  
ANISOU 5341  CB  GLU D 144     1495   1558   1754    112    134    -14       C  
ATOM   5342  CG  GLU D 144      21.255 -31.395  -1.537  1.00 14.65           C  
ANISOU 5342  CG  GLU D 144     1767   1795   2003     94    161      3       C  
ATOM   5343  CD  GLU D 144      21.118 -31.341  -3.053  1.00 17.78           C  
ANISOU 5343  CD  GLU D 144     2207   2186   2361    109    226     29       C  
ATOM   5344  OE1 GLU D 144      21.768 -32.145  -3.750  1.00 20.44           O  
ANISOU 5344  OE1 GLU D 144     2542   2526   2697    128    269     33       O  
ATOM   5345  OE2 GLU D 144      20.363 -30.483  -3.552  1.00 18.70           O  
ANISOU 5345  OE2 GLU D 144     2368   2293   2445    108    234     45       O  
ATOM   5346  N   SER D 145      20.232 -35.958   0.215  1.00 11.58           N  
ANISOU 5346  N   SER D 145     1432   1448   1520    150     48    -41       N  
ATOM   5347  CA  SER D 145      20.501 -37.175   1.007  1.00 11.71           C  
ANISOU 5347  CA  SER D 145     1454   1461   1536    167     16    -48       C  
ATOM   5348  C   SER D 145      21.763 -37.935   0.597  1.00 12.14           C  
ANISOU 5348  C   SER D 145     1479   1506   1628    195     33    -51       C  
ATOM   5349  O   SER D 145      22.486 -38.444   1.449  1.00 12.12           O  
ANISOU 5349  O   SER D 145     1456   1497   1652    213     -3    -57       O  
ATOM   5350  CB  SER D 145      19.303 -38.123   0.951  1.00 11.68           C  
ANISOU 5350  CB  SER D 145     1502   1454   1482    165     10    -48       C  
ATOM   5351  OG  SER D 145      18.168 -37.557   1.579  1.00 10.94           O  
ANISOU 5351  OG  SER D 145     1423   1368   1364    143     -5    -48       O  
ATOM   5352  N   PHE D 146      22.006 -38.030  -0.705  1.00 12.36           N  
ANISOU 5352  N   PHE D 146     1510   1532   1653    205     87    -47       N  
ATOM   5353  CA  PHE D 146      23.239 -38.636  -1.223  1.00 12.75           C  
ANISOU 5353  CA  PHE D 146     1526   1574   1745    236    122    -51       C  
ATOM   5354  C   PHE D 146      23.387 -38.278  -2.702  1.00 13.08           C  
ANISOU 5354  C   PHE D 146     1581   1615   1774    242    198    -42       C  
ATOM   5355  O   PHE D 146      22.540 -37.574  -3.255  1.00 12.75           O  
ANISOU 5355  O   PHE D 146     1578   1578   1688    224    211    -32       O  
ATOM   5356  CB  PHE D 146      23.277 -40.164  -0.984  1.00 12.85           C  
ANISOU 5356  CB  PHE D 146     1567   1573   1742    268     99    -61       C  
ATOM   5357  CG  PHE D 146      22.133 -40.920  -1.611  1.00 11.95           C  
ANISOU 5357  CG  PHE D 146     1526   1450   1562    266    104    -65       C  
ATOM   5358  CD1 PHE D 146      22.223 -41.381  -2.918  1.00 11.06           C  
ANISOU 5358  CD1 PHE D 146     1446   1331   1426    288    152    -72       C  
ATOM   5359  CD2 PHE D 146      20.977 -41.189  -0.889  1.00 10.84           C  
ANISOU 5359  CD2 PHE D 146     1423   1307   1387    243     61    -64       C  
ATOM   5360  CE1 PHE D 146      21.174 -42.067  -3.502  1.00 10.91           C  
ANISOU 5360  CE1 PHE D 146     1494   1301   1352    285    142    -84       C  
ATOM   5361  CE2 PHE D 146      19.924 -41.885  -1.466  1.00 10.81           C  
ANISOU 5361  CE2 PHE D 146     1474   1292   1341    235     61    -73       C  
ATOM   5362  CZ  PHE D 146      20.019 -42.320  -2.771  1.00 10.95           C  
ANISOU 5362  CZ  PHE D 146     1522   1301   1337    256     93    -86       C  
ATOM   5363  N   PHE D 147      24.466 -38.733  -3.335  1.00 13.37           N  
ANISOU 5363  N   PHE D 147     1589   1645   1846    272    250    -44       N  
ATOM   5364  CA  PHE D 147      24.692 -38.440  -4.750  1.00 13.59           C  
ANISOU 5364  CA  PHE D 147     1641   1669   1852    284    337    -33       C  
ATOM   5365  C   PHE D 147      24.065 -39.497  -5.655  1.00 13.84           C  
ANISOU 5365  C   PHE D 147     1759   1695   1806    315    348    -45       C  
ATOM   5366  O   PHE D 147      24.397 -40.684  -5.560  1.00 13.69           O  
ANISOU 5366  O   PHE D 147     1744   1665   1792    346    339    -64       O  
ATOM   5367  CB  PHE D 147      26.183 -38.283  -5.040  1.00 14.41           C  
ANISOU 5367  CB  PHE D 147     1667   1767   2039    300    405    -29       C  
ATOM   5368  CG  PHE D 147      26.740 -36.959  -4.598  1.00 14.54           C  
ANISOU 5368  CG  PHE D 147     1609   1783   2131    260    414    -16       C  
ATOM   5369  CD1 PHE D 147      27.117 -36.003  -5.530  1.00 14.60           C  
ANISOU 5369  CD1 PHE D 147     1611   1781   2155    245    505      9       C  
ATOM   5370  CD2 PHE D 147      26.872 -36.660  -3.243  1.00 14.30           C  
ANISOU 5370  CD2 PHE D 147     1524   1756   2154    238    330    -28       C  
ATOM   5371  CE1 PHE D 147      27.625 -34.774  -5.128  1.00 14.80           C  
ANISOU 5371  CE1 PHE D 147     1568   1794   2260    203    513     21       C  
ATOM   5372  CE2 PHE D 147      27.382 -35.426  -2.830  1.00 14.21           C  
ANISOU 5372  CE2 PHE D 147     1446   1736   2216    199    329    -24       C  
ATOM   5373  CZ  PHE D 147      27.758 -34.486  -3.779  1.00 15.10           C  
ANISOU 5373  CZ  PHE D 147     1545   1835   2357    178    421      0       C  
ATOM   5374  N   CYS D 148      23.164 -39.053  -6.538  1.00 13.76           N  
ANISOU 5374  N   CYS D 148     1819   1687   1724    309    362    -38       N  
ATOM   5375  CA  CYS D 148      22.453 -39.949  -7.456  1.00 14.07           C  
ANISOU 5375  CA  CYS D 148     1945   1717   1683    336    358    -57       C  
ATOM   5376  C   CYS D 148      23.330 -40.470  -8.605  1.00 14.69           C  
ANISOU 5376  C   CYS D 148     2054   1784   1743    384    442    -63       C  
ATOM   5377  O   CYS D 148      22.886 -41.318  -9.375  1.00 14.73           O  
ANISOU 5377  O   CYS D 148     2137   1777   1682    413    438    -86       O  
ATOM   5378  CB  CYS D 148      21.211 -39.259  -8.035  1.00 13.79           C  
ANISOU 5378  CB  CYS D 148     1974   1688   1579    321    332    -52       C  
ATOM   5379  SG  CYS D 148      21.559 -37.992  -9.294  1.00 14.78           S  
ANISOU 5379  SG  CYS D 148     2139   1813   1666    334    418    -19       S  
ATOM   5380  N   ASP D 149      24.552 -39.951  -8.719  1.00 15.38           N  
ANISOU 5380  N   ASP D 149     2080   1872   1891    391    520    -44       N  
ATOM   5381  CA  ASP D 149      25.506 -40.374  -9.753  1.00 16.42           C  
ANISOU 5381  CA  ASP D 149     2228   1993   2017    439    621    -46       C  
ATOM   5382  C   ASP D 149      26.725 -41.074  -9.137  1.00 17.07           C  
ANISOU 5382  C   ASP D 149     2218   2071   2196    462    638    -59       C  
ATOM   5383  O   ASP D 149      27.790 -41.156  -9.755  1.00 18.06           O  
ANISOU 5383  O   ASP D 149     2313   2191   2358    495    735    -55       O  
ATOM   5384  CB  ASP D 149      25.931 -39.173 -10.625  1.00 16.81           C  
ANISOU 5384  CB  ASP D 149     2287   2043   2059    433    721     -9       C  
ATOM   5385  CG  ASP D 149      26.662 -38.075  -9.837  1.00 16.85           C  
ANISOU 5385  CG  ASP D 149     2178   2051   2173    388    738     16       C  
ATOM   5386  OD1 ASP D 149      26.584 -38.052  -8.590  1.00 15.32           O  
ANISOU 5386  OD1 ASP D 149     1915   1865   2039    358    653      5       O  
ATOM   5387  OD2 ASP D 149      27.321 -37.221 -10.478  1.00 17.49           O  
ANISOU 5387  OD2 ASP D 149     2245   2123   2278    382    839     47       O  
ATOM   5388  N   ASN D 150      26.552 -41.592  -7.924  1.00 16.86           N  
ANISOU 5388  N   ASN D 150     2151   2046   2211    449    545    -73       N  
ATOM   5389  CA  ASN D 150      27.613 -42.271  -7.206  1.00 17.51           C  
ANISOU 5389  CA  ASN D 150     2150   2123   2382    476    536    -86       C  
ATOM   5390  C   ASN D 150      27.126 -43.652  -6.753  1.00 17.31           C  
ANISOU 5390  C   ASN D 150     2174   2078   2324    501    464   -111       C  
ATOM   5391  O   ASN D 150      26.295 -43.759  -5.848  1.00 16.26           O  
ANISOU 5391  O   ASN D 150     2059   1945   2175    471    378   -111       O  
ATOM   5392  CB  ASN D 150      28.069 -41.417  -6.021  1.00 17.36           C  
ANISOU 5392  CB  ASN D 150     2028   2116   2452    437    489    -74       C  
ATOM   5393  CG  ASN D 150      29.275 -42.001  -5.299  1.00 18.86           C  
ANISOU 5393  CG  ASN D 150     2122   2300   2743    471    471    -89       C  
ATOM   5394  OD1 ASN D 150      29.192 -43.064  -4.679  1.00 19.84           O  
ANISOU 5394  OD1 ASN D 150     2264   2412   2861    501    406   -105       O  
ATOM   5395  ND2 ASN D 150      30.395 -41.291  -5.352  1.00 20.77           N  
ANISOU 5395  ND2 ASN D 150     2259   2548   3085    466    524    -83       N  
ATOM   5396  N   LYS D 151      27.644 -44.693  -7.408  1.00 18.03           N  
ANISOU 5396  N   LYS D 151     2293   2149   2409    558    509   -132       N  
ATOM   5397  CA  LYS D 151      27.304 -46.096  -7.111  1.00 18.29           C  
ANISOU 5397  CA  LYS D 151     2381   2151   2419    588    453   -158       C  
ATOM   5398  C   LYS D 151      27.339 -46.425  -5.625  1.00 17.50           C  
ANISOU 5398  C   LYS D 151     2234   2044   2370    577    361   -152       C  
ATOM   5399  O   LYS D 151      26.401 -47.007  -5.084  1.00 16.57           O  
ANISOU 5399  O   LYS D 151     2175   1909   2212    557    293   -155       O  
ATOM   5400  CB  LYS D 151      28.280 -47.038  -7.815  1.00 19.55           C  
ANISOU 5400  CB  LYS D 151     2543   2288   2599    661    521   -181       C  
ATOM   5401  CG  LYS D 151      28.086 -47.159  -9.305  1.00 21.90           C  
ANISOU 5401  CG  LYS D 151     2930   2578   2814    689    603   -196       C  
ATOM   5402  CD  LYS D 151      26.983 -48.147  -9.673  1.00 23.22           C  
ANISOU 5402  CD  LYS D 151     3219   2712   2893    694    548   -227       C  
ATOM   5403  CE  LYS D 151      27.074 -48.543 -11.147  1.00 24.92           C  
ANISOU 5403  CE  LYS D 151     3528   2910   3029    746    627   -255       C  
ATOM   5404  NZ  LYS D 151      27.329 -47.368 -12.040  1.00 25.31           N  
ANISOU 5404  NZ  LYS D 151     3579   2990   3045    742    719   -230       N  
ATOM   5405  N   GLU D 152      28.437 -46.047  -4.980  1.00 17.68           N  
ANISOU 5405  N   GLU D 152     2153   2080   2483    589    360   -144       N  
ATOM   5406  CA  GLU D 152      28.690 -46.407  -3.591  1.00 17.62           C  
ANISOU 5406  CA  GLU D 152     2106   2065   2524    596    270   -141       C  
ATOM   5407  C   GLU D 152      27.632 -45.795  -2.673  1.00 16.08           C  
ANISOU 5407  C   GLU D 152     1939   1882   2288    535    198   -124       C  
ATOM   5408  O   GLU D 152      27.128 -46.470  -1.789  1.00 15.24           O  
ANISOU 5408  O   GLU D 152     1876   1756   2159    535    130   -121       O  
ATOM   5409  CB  GLU D 152      30.104 -45.983  -3.166  1.00 18.65           C  
ANISOU 5409  CB  GLU D 152     2111   2209   2767    621    276   -143       C  
ATOM   5410  CG  GLU D 152      31.231 -46.785  -3.836  1.00 21.32           C  
ANISOU 5410  CG  GLU D 152     2408   2531   3162    694    340   -162       C  
ATOM   5411  CD  GLU D 152      31.243 -46.682  -5.363  1.00 24.13           C  
ANISOU 5411  CD  GLU D 152     2800   2889   3480    705    463   -167       C  
ATOM   5412  OE1 GLU D 152      30.877 -45.609  -5.901  1.00 25.25           O  
ANISOU 5412  OE1 GLU D 152     2948   3053   3593    656    512   -150       O  
ATOM   5413  OE2 GLU D 152      31.618 -47.675  -6.031  1.00 25.38           O  
ANISOU 5413  OE2 GLU D 152     2990   3022   3630    767    511   -188       O  
ATOM   5414  N   ASP D 153      27.299 -44.523  -2.906  1.00 15.16           N  
ANISOU 5414  N   ASP D 153     1802   1794   2164    486    222   -112       N  
ATOM   5415  CA  ASP D 153      26.202 -43.848  -2.194  1.00 14.05           C  
ANISOU 5415  CA  ASP D 153     1691   1666   1980    431    168    -98       C  
ATOM   5416  C   ASP D 153      24.870 -44.563  -2.395  1.00 13.39           C  
ANISOU 5416  C   ASP D 153     1704   1565   1816    416    149   -101       C  
ATOM   5417  O   ASP D 153      24.119 -44.756  -1.450  1.00 12.81           O  
ANISOU 5417  O   ASP D 153     1660   1486   1722    393     92    -94       O  
ATOM   5418  CB  ASP D 153      26.040 -42.393  -2.674  1.00 13.77           C  
ANISOU 5418  CB  ASP D 153     1629   1656   1946    389    208    -86       C  
ATOM   5419  CG  ASP D 153      26.858 -41.396  -1.867  1.00 13.63           C  
ANISOU 5419  CG  ASP D 153     1520   1652   2007    372    185    -81       C  
ATOM   5420  OD1 ASP D 153      27.713 -41.813  -1.064  1.00 14.06           O  
ANISOU 5420  OD1 ASP D 153     1520   1700   2121    399    140    -91       O  
ATOM   5421  OD2 ASP D 153      26.634 -40.174  -2.042  1.00 13.14           O  
ANISOU 5421  OD2 ASP D 153     1441   1602   1948    332    205    -70       O  
ATOM   5422  N   TYR D 154      24.564 -44.934  -3.632  1.00 13.40           N  
ANISOU 5422  N   TYR D 154     1757   1557   1775    428    197   -114       N  
ATOM   5423  CA  TYR D 154      23.270 -45.552  -3.924  1.00 13.22           C  
ANISOU 5423  CA  TYR D 154     1818   1516   1687    408    172   -124       C  
ATOM   5424  C   TYR D 154      23.169 -46.968  -3.343  1.00 13.22           C  
ANISOU 5424  C   TYR D 154     1857   1475   1690    428    133   -134       C  
ATOM   5425  O   TYR D 154      22.091 -47.383  -2.922  1.00 12.74           O  
ANISOU 5425  O   TYR D 154     1841   1396   1602    395     94   -133       O  
ATOM   5426  CB  TYR D 154      22.989 -45.543  -5.433  1.00 13.50           C  
ANISOU 5426  CB  TYR D 154     1908   1551   1670    421    223   -141       C  
ATOM   5427  CG  TYR D 154      21.606 -46.029  -5.810  1.00 13.97           C  
ANISOU 5427  CG  TYR D 154     2043   1594   1671    396    184   -160       C  
ATOM   5428  CD1 TYR D 154      20.473 -45.573  -5.139  1.00 14.23           C  
ANISOU 5428  CD1 TYR D 154     2073   1638   1697    344    134   -149       C  
ATOM   5429  CD2 TYR D 154      21.427 -46.930  -6.853  1.00 15.83           C  
ANISOU 5429  CD2 TYR D 154     2350   1800   1864    425    196   -192       C  
ATOM   5430  CE1 TYR D 154      19.206 -46.014  -5.485  1.00 14.06           C  
ANISOU 5430  CE1 TYR D 154     2103   1599   1639    318     97   -170       C  
ATOM   5431  CE2 TYR D 154      20.160 -47.375  -7.207  1.00 16.09           C  
ANISOU 5431  CE2 TYR D 154     2445   1813   1855    398    149   -216       C  
ATOM   5432  CZ  TYR D 154      19.058 -46.910  -6.520  1.00 15.35           C  
ANISOU 5432  CZ  TYR D 154     2333   1733   1768    343     99   -204       C  
ATOM   5433  OH  TYR D 154      17.805 -47.351  -6.866  1.00 17.12           O  
ANISOU 5433  OH  TYR D 154     2600   1936   1967    314     51   -231       O  
ATOM   5434  N   ASP D 155      24.293 -47.687  -3.309  1.00 13.76           N  
ANISOU 5434  N   ASP D 155     1905   1524   1799    483    147   -141       N  
ATOM   5435  CA  ASP D 155      24.355 -49.011  -2.676  1.00 14.30           C  
ANISOU 5435  CA  ASP D 155     2012   1545   1876    511    109   -144       C  
ATOM   5436  C   ASP D 155      24.104 -48.918  -1.172  1.00 13.86           C  
ANISOU 5436  C   ASP D 155     1946   1488   1831    488     46   -118       C  
ATOM   5437  O   ASP D 155      23.371 -49.730  -0.627  1.00 13.67           O  
ANISOU 5437  O   ASP D 155     1984   1427   1784    474     15   -111       O  
ATOM   5438  CB  ASP D 155      25.693 -49.709  -2.958  1.00 15.05           C  
ANISOU 5438  CB  ASP D 155     2079   1622   2019    585    136   -158       C  
ATOM   5439  CG  ASP D 155      25.766 -50.294  -4.366  1.00 16.05           C  
ANISOU 5439  CG  ASP D 155     2255   1728   2116    618    197   -190       C  
ATOM   5440  OD1 ASP D 155      24.703 -50.565  -4.968  1.00 15.16           O  
ANISOU 5440  OD1 ASP D 155     2218   1599   1943    588    192   -205       O  
ATOM   5441  OD2 ASP D 155      26.891 -50.485  -4.870  1.00 17.86           O  
ANISOU 5441  OD2 ASP D 155     2446   1956   2383    676    248   -202       O  
ATOM   5442  N   LYS D 156      24.680 -47.910  -0.520  1.00 13.71           N  
ANISOU 5442  N   LYS D 156     1857   1506   1845    483     31   -104       N  
ATOM   5443  CA  LYS D 156      24.396 -47.643   0.893  1.00 13.64           C  
ANISOU 5443  CA  LYS D 156     1851   1501   1832    464    -29    -82       C  
ATOM   5444  C   LYS D 156      22.918 -47.303   1.126  1.00 13.04           C  
ANISOU 5444  C   LYS D 156     1822   1429   1702    401    -33    -71       C  
ATOM   5445  O   LYS D 156      22.337 -47.710   2.132  1.00 12.86           O  
ANISOU 5445  O   LYS D 156     1844   1386   1657    388    -65    -53       O  
ATOM   5446  CB  LYS D 156      25.268 -46.499   1.414  1.00 13.83           C  
ANISOU 5446  CB  LYS D 156     1790   1563   1902    466    -49    -79       C  
ATOM   5447  CG  LYS D 156      26.755 -46.827   1.489  1.00 14.71           C  
ANISOU 5447  CG  LYS D 156     1835   1669   2085    528    -61    -91       C  
ATOM   5448  CD  LYS D 156      27.552 -45.576   1.813  1.00 15.02           C  
ANISOU 5448  CD  LYS D 156     1778   1744   2185    517    -75    -95       C  
ATOM   5449  CE  LYS D 156      28.986 -45.892   2.192  1.00 16.40           C  
ANISOU 5449  CE  LYS D 156     1874   1912   2444    577   -111   -109       C  
ATOM   5450  NZ  LYS D 156      29.694 -44.651   2.611  1.00 16.99           N  
ANISOU 5450  NZ  LYS D 156     1851   2016   2587    557   -138   -118       N  
ATOM   5451  N   ALA D 157      22.316 -46.565   0.197  1.00 12.69           N  
ANISOU 5451  N   ALA D 157     1770   1411   1641    367      3    -81       N  
ATOM   5452  CA  ALA D 157      20.900 -46.204   0.301  1.00 12.50           C  
ANISOU 5452  CA  ALA D 157     1777   1394   1578    312     -2    -75       C  
ATOM   5453  C   ALA D 157      20.005 -47.431   0.152  1.00 12.44           C  
ANISOU 5453  C   ALA D 157     1836   1341   1550    299     -6    -82       C  
ATOM   5454  O   ALA D 157      19.064 -47.614   0.926  1.00 12.25           O  
ANISOU 5454  O   ALA D 157     1837   1303   1513    263    -20    -67       O  
ATOM   5455  CB  ALA D 157      20.533 -45.148  -0.736  1.00 12.11           C  
ANISOU 5455  CB  ALA D 157     1706   1378   1516    290     29    -85       C  
ATOM   5456  N   LYS D 158      20.309 -48.271  -0.836  1.00 12.92           N  
ANISOU 5456  N   LYS D 158     1924   1375   1611    327     12   -104       N  
ATOM   5457  CA  LYS D 158      19.569 -49.519  -1.045  1.00 13.12           C  
ANISOU 5457  CA  LYS D 158     2013   1346   1626    315      3   -118       C  
ATOM   5458  C   LYS D 158      19.749 -50.520   0.104  1.00 13.36           C  
ANISOU 5458  C   LYS D 158     2078   1328   1669    328    -18    -94       C  
ATOM   5459  O   LYS D 158      18.889 -51.377   0.330  1.00 13.16           O  
ANISOU 5459  O   LYS D 158     2104   1255   1641    298    -24    -92       O  
ATOM   5460  CB  LYS D 158      19.954 -50.160  -2.381  1.00 13.48           C  
ANISOU 5460  CB  LYS D 158     2088   1369   1663    351     25   -153       C  
ATOM   5461  CG  LYS D 158      19.397 -49.398  -3.588  1.00 14.33           C  
ANISOU 5461  CG  LYS D 158     2197   1510   1738    333     40   -177       C  
ATOM   5462  CD  LYS D 158      19.568 -50.167  -4.890  1.00 15.61           C  
ANISOU 5462  CD  LYS D 158     2415   1642   1875    368     56   -217       C  
ATOM   5463  CE  LYS D 158      21.014 -50.203  -5.335  1.00 16.10           C  
ANISOU 5463  CE  LYS D 158     2460   1711   1946    435    105   -219       C  
ATOM   5464  NZ  LYS D 158      21.153 -50.845  -6.667  1.00 16.35           N  
ANISOU 5464  NZ  LYS D 158     2556   1717   1940    474    131   -261       N  
ATOM   5465  N   LYS D 159      20.864 -50.409   0.820  1.00 13.44           N  
ANISOU 5465  N   LYS D 159     2062   1347   1696    374    -32    -77       N  
ATOM   5466  CA  LYS D 159      21.104 -51.215   2.016  1.00 14.07           C  
ANISOU 5466  CA  LYS D 159     2183   1385   1779    396    -61    -49       C  
ATOM   5467  C   LYS D 159      20.203 -50.718   3.149  1.00 13.85           C  
ANISOU 5467  C   LYS D 159     2170   1367   1724    349    -71    -18       C  
ATOM   5468  O   LYS D 159      19.508 -51.503   3.783  1.00 13.23           O  
ANISOU 5468  O   LYS D 159     2153   1240   1632    328    -69      4       O  
ATOM   5469  CB  LYS D 159      22.583 -51.150   2.413  1.00 14.55           C  
ANISOU 5469  CB  LYS D 159     2203   1456   1868    465    -87    -45       C  
ATOM   5470  CG  LYS D 159      22.947 -51.963   3.650  1.00 16.03           C  
ANISOU 5470  CG  LYS D 159     2441   1599   2051    504   -130    -16       C  
ATOM   5471  CD  LYS D 159      24.460 -52.108   3.801  1.00 17.49           C  
ANISOU 5471  CD  LYS D 159     2580   1787   2279    584   -164    -23       C  
ATOM   5472  CE  LYS D 159      24.852 -52.506   5.223  1.00 19.21           C  
ANISOU 5472  CE  LYS D 159     2839   1976   2481    626   -228      9       C  
ATOM   5473  NZ  LYS D 159      26.166 -53.227   5.255  1.00 20.96           N  
ANISOU 5473  NZ  LYS D 159     3042   2173   2751    716   -266      0       N  
ATOM   5474  N   LEU D 160      20.215 -49.402   3.369  1.00 13.70           N  
ANISOU 5474  N   LEU D 160     2098   1408   1701    332    -75    -17       N  
ATOM   5475  CA  LEU D 160      19.349 -48.746   4.356  1.00 13.53           C  
ANISOU 5475  CA  LEU D 160     2086   1403   1651    290    -76      6       C  
ATOM   5476  C   LEU D 160      17.864 -48.926   4.046  1.00 13.31           C  
ANISOU 5476  C   LEU D 160     2079   1361   1616    228    -44      4       C  
ATOM   5477  O   LEU D 160      17.042 -49.061   4.956  1.00 12.96           O  
ANISOU 5477  O   LEU D 160     2069   1300   1555    198    -30     29       O  
ATOM   5478  CB  LEU D 160      19.658 -47.240   4.430  1.00 13.27           C  
ANISOU 5478  CB  LEU D 160     1989   1433   1622    285    -85     -2       C  
ATOM   5479  CG  LEU D 160      20.546 -46.720   5.567  1.00 14.38           C  
ANISOU 5479  CG  LEU D 160     2118   1588   1758    320   -130      9       C  
ATOM   5480  CD1 LEU D 160      21.748 -47.592   5.791  1.00 16.35           C  
ANISOU 5480  CD1 LEU D 160     2375   1809   2029    382   -166     11       C  
ATOM   5481  CD2 LEU D 160      20.983 -45.288   5.291  1.00 13.66           C  
ANISOU 5481  CD2 LEU D 160     1952   1548   1689    311   -135     -8       C  
ATOM   5482  N   GLY D 161      17.522 -48.905   2.760  1.00 13.14           N  
ANISOU 5482  N   GLY D 161     2036   1347   1609    211    -30    -27       N  
ATOM   5483  CA  GLY D 161      16.129 -48.857   2.344  1.00 12.91           C  
ANISOU 5483  CA  GLY D 161     2006   1315   1585    153    -14    -38       C  
ATOM   5484  C   GLY D 161      15.550 -47.479   2.607  1.00 12.37           C  
ANISOU 5484  C   GLY D 161     1891   1301   1508    126     -8    -35       C  
ATOM   5485  O   GLY D 161      16.153 -46.661   3.315  1.00 12.20           O  
ANISOU 5485  O   GLY D 161     1851   1311   1474    147    -16    -20       O  
ATOM   5486  N   HIS D 162      14.375 -47.219   2.041  1.00 12.23           N  
ANISOU 5486  N   HIS D 162     1854   1292   1502     84     -1    -52       N  
ATOM   5487  CA  HIS D 162      13.678 -45.941   2.246  1.00 11.81           C  
ANISOU 5487  CA  HIS D 162     1756   1285   1445     61      5    -50       C  
ATOM   5488  C   HIS D 162      13.392 -45.662   3.723  1.00 11.89           C  
ANISOU 5488  C   HIS D 162     1777   1298   1444     50     24    -19       C  
ATOM   5489  O   HIS D 162      13.451 -44.523   4.172  1.00 11.29           O  
ANISOU 5489  O   HIS D 162     1676   1261   1354     56     25    -14       O  
ATOM   5490  CB  HIS D 162      12.361 -45.923   1.476  1.00 11.97           C  
ANISOU 5490  CB  HIS D 162     1754   1305   1489     20      1    -76       C  
ATOM   5491  CG  HIS D 162      12.524 -46.144   0.007  1.00 12.47           C  
ANISOU 5491  CG  HIS D 162     1823   1365   1549     34    -24   -111       C  
ATOM   5492  ND1 HIS D 162      13.416 -45.422  -0.752  1.00 13.73           N  
ANISOU 5492  ND1 HIS D 162     1978   1557   1682     74    -29   -117       N  
ATOM   5493  CD2 HIS D 162      11.923 -47.011  -0.839  1.00 12.57           C  
ANISOU 5493  CD2 HIS D 162     1853   1344   1579     16    -45   -142       C  
ATOM   5494  CE1 HIS D 162      13.356 -45.832  -2.005  1.00 12.89           C  
ANISOU 5494  CE1 HIS D 162     1894   1438   1565     85    -46   -149       C  
ATOM   5495  NE2 HIS D 162      12.457 -46.795  -2.086  1.00 13.33           N  
ANISOU 5495  NE2 HIS D 162     1965   1455   1646     52    -63   -168       N  
ATOM   5496  N   GLU D 163      13.088 -46.719   4.467  1.00 12.25           N  
ANISOU 5496  N   GLU D 163     1866   1296   1491     36     44      3       N  
ATOM   5497  CA  GLU D 163      12.771 -46.628   5.892  1.00 12.41           C  
ANISOU 5497  CA  GLU D 163     1917   1309   1487     29     73     37       C  
ATOM   5498  C   GLU D 163      14.013 -46.255   6.715  1.00 12.30           C  
ANISOU 5498  C   GLU D 163     1932   1310   1432     82     45     54       C  
ATOM   5499  O   GLU D 163      13.921 -45.485   7.681  1.00 12.17           O  
ANISOU 5499  O   GLU D 163     1925   1316   1383     89     52     67       O  
ATOM   5500  CB  GLU D 163      12.181 -47.971   6.323  1.00 13.45           C  
ANISOU 5500  CB  GLU D 163     2100   1375   1634      0    107     60       C  
ATOM   5501  CG  GLU D 163      11.978 -48.246   7.796  1.00 15.47           C  
ANISOU 5501  CG  GLU D 163     2419   1606   1855      1    148    106       C  
ATOM   5502  CD  GLU D 163      11.577 -49.707   8.004  1.00 18.07           C  
ANISOU 5502  CD  GLU D 163     2805   1857   2205    -26    182    130       C  
ATOM   5503  OE1 GLU D 163      12.419 -50.501   8.490  1.00 18.58           O  
ANISOU 5503  OE1 GLU D 163     2942   1879   2238     13    166    156       O  
ATOM   5504  OE2 GLU D 163      10.440 -50.064   7.613  1.00 19.05           O  
ANISOU 5504  OE2 GLU D 163     2897   1957   2385    -86    217    120       O  
ATOM   5505  N   GLY D 164      15.167 -46.797   6.328  1.00 12.09           N  
ANISOU 5505  N   GLY D 164     1917   1269   1408    122     11     48       N  
ATOM   5506  CA  GLY D 164      16.441 -46.495   6.982  1.00 12.08           C  
ANISOU 5506  CA  GLY D 164     1926   1280   1384    175    -30     56       C  
ATOM   5507  C   GLY D 164      16.875 -45.053   6.802  1.00 11.80           C  
ANISOU 5507  C   GLY D 164     1831   1300   1354    182    -50     35       C  
ATOM   5508  O   GLY D 164      17.366 -44.414   7.745  1.00 11.72           O  
ANISOU 5508  O   GLY D 164     1828   1305   1319    205    -78     41       O  
ATOM   5509  N   ILE D 165      16.697 -44.545   5.587  1.00 11.32           N  
ANISOU 5509  N   ILE D 165     1716   1263   1321    165    -40     11       N  
ATOM   5510  CA  ILE D 165      17.008 -43.162   5.274  1.00 11.17           C  
ANISOU 5510  CA  ILE D 165     1645   1288   1312    165    -49     -5       C  
ATOM   5511  C   ILE D 165      16.014 -42.253   5.984  1.00 10.63           C  
ANISOU 5511  C   ILE D 165     1578   1240   1224    138    -34      0       C  
ATOM   5512  O   ILE D 165      16.415 -41.284   6.624  1.00 10.62           O  
ANISOU 5512  O   ILE D 165     1566   1258   1212    149    -53     -3       O  
ATOM   5513  CB  ILE D 165      16.972 -42.901   3.751  1.00 11.07           C  
ANISOU 5513  CB  ILE D 165     1594   1290   1324    156    -34    -25       C  
ATOM   5514  CG1 ILE D 165      18.130 -43.629   3.063  1.00 12.48           C  
ANISOU 5514  CG1 ILE D 165     1768   1452   1521    192    -40    -33       C  
ATOM   5515  CG2 ILE D 165      17.042 -41.395   3.442  1.00 10.95           C  
ANISOU 5515  CG2 ILE D 165     1534   1311   1315    149    -33    -34       C  
ATOM   5516  CD1 ILE D 165      19.480 -42.941   3.207  1.00 13.47           C  
ANISOU 5516  CD1 ILE D 165     1850   1597   1672    223    -57    -36       C  
ATOM   5517  N   ALA D 166      14.724 -42.574   5.881  1.00 10.34           N  
ANISOU 5517  N   ALA D 166     1549   1193   1187    103      0      4       N  
ATOM   5518  CA  ALA D 166      13.683 -41.800   6.562  1.00 10.03           C  
ANISOU 5518  CA  ALA D 166     1506   1171   1135     81     26      7       C  
ATOM   5519  C   ALA D 166      13.937 -41.712   8.066  1.00 10.47           C  
ANISOU 5519  C   ALA D 166     1613   1219   1145    101     25     26       C  
ATOM   5520  O   ALA D 166      13.836 -40.631   8.659  1.00  9.79           O  
ANISOU 5520  O   ALA D 166     1524   1157   1041    107     23     19       O  
ATOM   5521  CB  ALA D 166      12.310 -42.397   6.292  1.00 10.05           C  
ANISOU 5521  CB  ALA D 166     1501   1157   1159     41     65      8       C  
ATOM   5522  N   LYS D 167      14.270 -42.852   8.670  1.00 10.96           N  
ANISOU 5522  N   LYS D 167     1733   1245   1186    115     25     49       N  
ATOM   5523  CA  LYS D 167      14.512 -42.932  10.104  1.00 12.24           C  
ANISOU 5523  CA  LYS D 167     1965   1394   1291    142     20     72       C  
ATOM   5524  C   LYS D 167      15.618 -41.978  10.538  1.00 12.04           C  
ANISOU 5524  C   LYS D 167     1933   1393   1248    181    -42     53       C  
ATOM   5525  O   LYS D 167      15.491 -41.309  11.554  1.00 12.58           O  
ANISOU 5525  O   LYS D 167     2039   1471   1271    194    -46     53       O  
ATOM   5526  CB  LYS D 167      14.858 -44.368  10.526  1.00 12.90           C  
ANISOU 5526  CB  LYS D 167     2118   1428   1356    160     19    102       C  
ATOM   5527  CG  LYS D 167      15.208 -44.516  12.015  1.00 15.29           C  
ANISOU 5527  CG  LYS D 167     2514   1712   1585    200      5    129       C  
ATOM   5528  CD  LYS D 167      15.254 -45.976  12.456  1.00 17.33           C  
ANISOU 5528  CD  LYS D 167     2854   1910   1820    212     21    169       C  
ATOM   5529  CE  LYS D 167      15.486 -46.082  13.948  1.00 19.82           C  
ANISOU 5529  CE  LYS D 167     3279   2206   2047    256     11    200       C  
ATOM   5530  NZ  LYS D 167      15.597 -47.495  14.399  1.00 20.91           N  
ANISOU 5530  NZ  LYS D 167     3510   2278   2158    276     24    245       N  
ATOM   5531  N   LEU D 168      16.692 -41.918   9.757  1.00 11.70           N  
ANISOU 5531  N   LEU D 168     1842   1359   1245    197    -87     35       N  
ATOM   5532  CA  LEU D 168      17.817 -41.031  10.051  1.00 11.50           C  
ANISOU 5532  CA  LEU D 168     1791   1353   1227    227   -149     14       C  
ATOM   5533  C   LEU D 168      17.403 -39.558   9.963  1.00 10.96           C  
ANISOU 5533  C   LEU D 168     1684   1315   1166    204   -140     -8       C  
ATOM   5534  O   LEU D 168      17.717 -38.745  10.853  1.00 11.04           O  
ANISOU 5534  O   LEU D 168     1712   1331   1151    221   -177    -23       O  
ATOM   5535  CB  LEU D 168      18.986 -41.340   9.106  1.00 11.47           C  
ANISOU 5535  CB  LEU D 168     1730   1349   1281    244   -179      1       C  
ATOM   5536  CG  LEU D 168      19.694 -42.674   9.378  1.00 11.96           C  
ANISOU 5536  CG  LEU D 168     1830   1378   1338    284   -207     17       C  
ATOM   5537  CD1 LEU D 168      20.625 -43.046   8.240  1.00 11.96           C  
ANISOU 5537  CD1 LEU D 168     1767   1376   1399    299   -213      3       C  
ATOM   5538  CD2 LEU D 168      20.461 -42.635  10.698  1.00 12.22           C  
ANISOU 5538  CD2 LEU D 168     1907   1401   1334    330   -277     18       C  
ATOM   5539  N   ILE D 169      16.672 -39.224   8.901  1.00  9.91           N  
ANISOU 5539  N   ILE D 169     1504   1195   1065    171    -98    -13       N  
ATOM   5540  CA  ILE D 169      16.144 -37.882   8.733  1.00  9.19           C  
ANISOU 5540  CA  ILE D 169     1382   1126    983    153    -85    -30       C  
ATOM   5541  C   ILE D 169      15.211 -37.494   9.895  1.00  9.20           C  
ANISOU 5541  C   ILE D 169     1433   1129    935    153    -61    -27       C  
ATOM   5542  O   ILE D 169      15.305 -36.387  10.425  1.00  9.13           O  
ANISOU 5542  O   ILE D 169     1427   1128    913    162    -79    -46       O  
ATOM   5543  CB  ILE D 169      15.403 -37.726   7.389  1.00  8.67           C  
ANISOU 5543  CB  ILE D 169     1270   1071    952    126    -49    -33       C  
ATOM   5544  CG1 ILE D 169      16.406 -37.758   6.233  1.00  8.31           C  
ANISOU 5544  CG1 ILE D 169     1183   1028    947    132    -64    -39       C  
ATOM   5545  CG2 ILE D 169      14.624 -36.413   7.359  1.00  7.97           C  
ANISOU 5545  CG2 ILE D 169     1162   1000    866    114    -33    -45       C  
ATOM   5546  CD1 ILE D 169      15.772 -37.978   4.873  1.00  7.53           C  
ANISOU 5546  CD1 ILE D 169     1064    933    865    115    -36    -40       C  
ATOM   5547  N   VAL D 170      14.330 -38.406  10.295  1.00  9.23           N  
ANISOU 5547  N   VAL D 170     1477   1118    912    144    -15     -4       N  
ATOM   5548  CA  VAL D 170      13.347 -38.103  11.329  1.00  9.57           C  
ANISOU 5548  CA  VAL D 170     1565   1161    911    143     30      3       C  
ATOM   5549  C   VAL D 170      14.001 -37.957  12.715  1.00 10.45           C  
ANISOU 5549  C   VAL D 170     1755   1262    952    183     -5      3       C  
ATOM   5550  O   VAL D 170      13.644 -37.064  13.481  1.00 10.36           O  
ANISOU 5550  O   VAL D 170     1773   1259    904    195      5    -11       O  
ATOM   5551  CB  VAL D 170      12.224 -39.157  11.370  1.00  9.63           C  
ANISOU 5551  CB  VAL D 170     1587   1150    920    116    100     30       C  
ATOM   5552  CG1 VAL D 170      11.343 -38.953  12.597  1.00  9.79           C  
ANISOU 5552  CG1 VAL D 170     1664   1167    890    121    161     43       C  
ATOM   5553  CG2 VAL D 170      11.396 -39.090  10.095  1.00  8.66           C  
ANISOU 5553  CG2 VAL D 170     1386   1039    864     80    123     18       C  
ATOM   5554  N   GLU D 171      14.964 -38.820  13.017  1.00 11.17           N  
ANISOU 5554  N   GLU D 171     1885   1335   1026    208    -51     16       N  
ATOM   5555  CA  GLU D 171      15.710 -38.730  14.273  1.00 12.39           C  
ANISOU 5555  CA  GLU D 171     2118   1478   1112    254   -107     13       C  
ATOM   5556  C   GLU D 171      16.470 -37.402  14.353  1.00 12.43           C  
ANISOU 5556  C   GLU D 171     2089   1501   1133    267   -176    -31       C  
ATOM   5557  O   GLU D 171      16.556 -36.792  15.423  1.00 12.72           O  
ANISOU 5557  O   GLU D 171     2188   1535   1109    295   -205    -48       O  
ATOM   5558  CB  GLU D 171      16.671 -39.922  14.420  1.00 12.90           C  
ANISOU 5558  CB  GLU D 171     2217   1516   1167    285   -156     33       C  
ATOM   5559  CG  GLU D 171      15.972 -41.250  14.748  1.00 14.51           C  
ANISOU 5559  CG  GLU D 171     2491   1686   1335    281    -93     80       C  
ATOM   5560  CD  GLU D 171      16.942 -42.402  14.982  1.00 15.65           C  
ANISOU 5560  CD  GLU D 171     2684   1797   1466    322   -147    101       C  
ATOM   5561  OE1 GLU D 171      18.120 -42.301  14.584  1.00 16.67           O  
ANISOU 5561  OE1 GLU D 171     2763   1935   1636    347   -227     77       O  
ATOM   5562  OE2 GLU D 171      16.521 -43.414  15.577  1.00 17.38           O  
ANISOU 5562  OE2 GLU D 171     2990   1978   1636    330   -106    143       O  
ATOM   5563  N   GLY D 172      16.995 -36.952  13.213  1.00 12.15           N  
ANISOU 5563  N   GLY D 172     1959   1479   1178    246   -197    -50       N  
ATOM   5564  CA  GLY D 172      17.671 -35.658  13.115  1.00 12.48           C  
ANISOU 5564  CA  GLY D 172     1955   1530   1255    245   -250    -89       C  
ATOM   5565  C   GLY D 172      16.745 -34.465  13.322  1.00 12.65           C  
ANISOU 5565  C   GLY D 172     1983   1561   1262    231   -213   -107       C  
ATOM   5566  O   GLY D 172      17.081 -33.514  14.029  1.00 12.65           O  
ANISOU 5566  O   GLY D 172     2007   1556   1243    246   -259   -139       O  
ATOM   5567  N   VAL D 173      15.573 -34.513  12.705  1.00 12.71           N  
ANISOU 5567  N   VAL D 173     1969   1579   1282    205   -136    -90       N  
ATOM   5568  CA  VAL D 173      14.606 -33.428  12.826  1.00 13.21           C  
ANISOU 5568  CA  VAL D 173     2030   1650   1338    198    -96   -106       C  
ATOM   5569  C   VAL D 173      14.027 -33.367  14.235  1.00 14.42           C  
ANISOU 5569  C   VAL D 173     2274   1797   1408    225    -72   -108       C  
ATOM   5570  O   VAL D 173      13.948 -32.288  14.831  1.00 14.91           O  
ANISOU 5570  O   VAL D 173     2363   1856   1445    242    -86   -139       O  
ATOM   5571  CB  VAL D 173      13.476 -33.567  11.783  1.00 12.62           C  
ANISOU 5571  CB  VAL D 173     1901   1588   1305    168    -29    -89       C  
ATOM   5572  CG1 VAL D 173      12.286 -32.677  12.141  1.00 12.71           C  
ANISOU 5572  CG1 VAL D 173     1919   1606   1304    171     22   -102       C  
ATOM   5573  CG2 VAL D 173      14.010 -33.225  10.395  1.00 12.27           C  
ANISOU 5573  CG2 VAL D 173     1784   1550   1329    149    -52    -94       C  
ATOM   5574  N   LEU D 174      13.654 -34.530  14.769  1.00 15.32           N  
ANISOU 5574  N   LEU D 174     2443   1903   1475    233    -33    -75       N  
ATOM   5575  CA  LEU D 174      13.007 -34.617  16.077  1.00 16.74           C  
ANISOU 5575  CA  LEU D 174     2720   2074   1567    260     13    -67       C  
ATOM   5576  C   LEU D 174      13.991 -34.617  17.256  1.00 18.44           C  
ANISOU 5576  C   LEU D 174     3032   2273   1701    307    -63    -80       C  
ATOM   5577  O   LEU D 174      13.575 -34.488  18.402  1.00 19.50           O  
ANISOU 5577  O   LEU D 174     3265   2399   1746    340    -35    -80       O  
ATOM   5578  CB  LEU D 174      12.120 -35.864  16.139  1.00 16.73           C  
ANISOU 5578  CB  LEU D 174     2740   2063   1554    242    101    -20       C  
ATOM   5579  CG  LEU D 174      11.023 -35.964  15.077  1.00 15.19           C  
ANISOU 5579  CG  LEU D 174     2452   1880   1438    197    170    -11       C  
ATOM   5580  CD1 LEU D 174      10.278 -37.278  15.201  1.00 14.27           C  
ANISOU 5580  CD1 LEU D 174     2357   1745   1321    174    246     32       C  
ATOM   5581  CD2 LEU D 174      10.065 -34.797  15.183  1.00 14.67           C  
ANISOU 5581  CD2 LEU D 174     2359   1831   1382    198    218    -36       C  
ATOM   5582  N   ASN D 175      15.283 -34.747  16.961  1.00 19.50           N  
ANISOU 5582  N   ASN D 175     3139   2404   1868    315   -161    -94       N  
ATOM   5583  CA  ASN D 175      16.339 -34.804  17.967  1.00 21.28           C  
ANISOU 5583  CA  ASN D 175     3439   2613   2031    363   -258   -112       C  
ATOM   5584  C   ASN D 175      16.082 -35.862  19.038  1.00 23.06           C  
ANISOU 5584  C   ASN D 175     3790   2819   2151    401   -232    -73       C  
ATOM   5585  O   ASN D 175      16.172 -35.594  20.232  1.00 23.73           O  
ANISOU 5585  O   ASN D 175     3985   2892   2138    447   -262    -87       O  
ATOM   5586  CB  ASN D 175      16.570 -33.431  18.619  1.00 21.72           C  
ANISOU 5586  CB  ASN D 175     3523   2668   2062    382   -313   -167       C  
ATOM   5587  CG  ASN D 175      17.923 -33.337  19.315  1.00 22.23           C  
ANISOU 5587  CG  ASN D 175     3624   2717   2104    422   -448   -202       C  
ATOM   5588  OD1 ASN D 175      18.741 -34.259  19.239  1.00 22.87           O  
ANISOU 5588  OD1 ASN D 175     3699   2793   2199    437   -503   -184       O  
ATOM   5589  ND2 ASN D 175      18.169 -32.221  19.984  1.00 22.51           N  
ANISOU 5589  ND2 ASN D 175     3696   2744   2112    441   -509   -255       N  
ATOM   5590  N   LYS D 176      15.743 -37.063  18.591  1.00 24.34           N  
ANISOU 5590  N   LYS D 176     3944   2973   2332    382   -175    -24       N  
ATOM   5591  CA  LYS D 176      15.597 -38.205  19.483  1.00 26.23           C  
ANISOU 5591  CA  LYS D 176     4300   3183   2482    415   -147     22       C  
ATOM   5592  C   LYS D 176      15.798 -39.465  18.667  1.00 27.05           C  
ANISOU 5592  C   LYS D 176     4361   3272   2645    394   -135     60       C  
ATOM   5593  O   LYS D 176      15.678 -39.435  17.445  1.00 26.23           O  
ANISOU 5593  O   LYS D 176     4144   3183   2638    348   -117     52       O  
ATOM   5594  CB  LYS D 176      14.219 -38.219  20.158  1.00 26.66           C  
ANISOU 5594  CB  LYS D 176     4429   3232   2470    408    -20     50       C  
ATOM   5595  CG  LYS D 176      13.034 -38.483  19.234  1.00 26.64           C  
ANISOU 5595  CG  LYS D 176     4336   3237   2548    345     95     72       C  
ATOM   5596  CD  LYS D 176      11.733 -38.597  20.024  1.00 28.11           C  
ANISOU 5596  CD  LYS D 176     4592   3413   2676    341    227    102       C  
ATOM   5597  CE  LYS D 176      10.583 -39.071  19.145  1.00 28.61           C  
ANISOU 5597  CE  LYS D 176     4561   3478   2833    277    331    126       C  
ATOM   5598  NZ  LYS D 176       9.409 -39.533  19.949  1.00 30.53           N  
ANISOU 5598  NZ  LYS D 176     4871   3699   3031    269    470    167       N  
ATOM   5599  N   ASN D 177      16.104 -40.565  19.346  1.00 29.11           N  
ANISOU 5599  N   ASN D 177     4721   3498   2841    431   -147     99       N  
ATOM   5600  CA  ASN D 177      16.191 -41.862  18.691  1.00 30.11           C  
ANISOU 5600  CA  ASN D 177     4827   3598   3015    414   -126    138       C  
ATOM   5601  C   ASN D 177      14.809 -42.494  18.585  1.00 31.13           C  
ANISOU 5601  C   ASN D 177     4973   3708   3147    366     12    182       C  
ATOM   5602  O   ASN D 177      14.002 -42.411  19.510  1.00 31.99           O  
ANISOU 5602  O   ASN D 177     5169   3805   3179    372     88    205       O  
ATOM   5603  CB  ASN D 177      17.170 -42.775  19.430  1.00 30.98           C  
ANISOU 5603  CB  ASN D 177     5036   3672   3064    479   -206    161       C  
ATOM   5604  CG  ASN D 177      18.584 -42.231  19.414  1.00 31.27           C  
ANISOU 5604  CG  ASN D 177     5028   3727   3127    523   -350    113       C  
ATOM   5605  OD1 ASN D 177      18.956 -41.469  18.523  1.00 32.15           O  
ANISOU 5605  OD1 ASN D 177     5015   3871   3329    493   -380     70       O  
ATOM   5606  ND2 ASN D 177      19.375 -42.606  20.407  1.00 32.85           N  
ANISOU 5606  ND2 ASN D 177     5330   3903   3248    594   -441    119       N  
ATOM   5607  N   ILE D 178      14.539 -43.103  17.438  1.00 31.82           N  
ANISOU 5607  N   ILE D 178     4973   3790   3326    318     44    189       N  
ATOM   5608  CA  ILE D 178      13.233 -43.684  17.146  1.00 32.94           C  
ANISOU 5608  CA  ILE D 178     5102   3913   3501    262    163    221       C  
ATOM   5609  C   ILE D 178      13.197 -45.138  17.583  1.00 34.39           C  
ANISOU 5609  C   ILE D 178     5380   4034   3652    269    199    277       C  
ATOM   5610  O   ILE D 178      12.271 -45.555  18.285  1.00 35.43           O  
ANISOU 5610  O   ILE D 178     5582   4134   3743    252    300    319       O  
ATOM   5611  CB  ILE D 178      12.907 -43.587  15.637  1.00 32.19           C  
ANISOU 5611  CB  ILE D 178     4871   3840   3521    206    170    193       C  
ATOM   5612  CG1 ILE D 178      12.233 -42.252  15.328  1.00 31.96           C  
ANISOU 5612  CG1 ILE D 178     4765   3859   3521    183    194    157       C  
ATOM   5613  CG2 ILE D 178      12.011 -44.742  15.196  1.00 33.00           C  
ANISOU 5613  CG2 ILE D 178     4965   3901   3671    156    251    226       C  
ATOM   5614  CD1 ILE D 178      12.022 -42.014  13.847  1.00 31.31           C  
ANISOU 5614  CD1 ILE D 178     4560   3799   3536    142    183    128       C  
ATOM   5615  N   ASN D 179      14.222 -45.888  17.175  1.00 35.08           N  
ANISOU 5615  N   ASN D 179     5468   4100   3761    296    121    279       N  
ATOM   5616  CA  ASN D 179      14.340 -47.328  17.442  1.00 36.49           C  
ANISOU 5616  CA  ASN D 179     5733   4211   3920    308    139    330       C  
ATOM   5617  C   ASN D 179      13.069 -47.950  18.030  1.00 37.36           C  
ANISOU 5617  C   ASN D 179     5915   4275   4004    267    272    384       C  
ATOM   5618  O   ASN D 179      12.915 -48.147  19.239  1.00 38.47           O  
ANISOU 5618  O   ASN D 179     6186   4387   4046    301    311    426       O  
ATOM   5619  CB  ASN D 179      15.566 -47.609  18.329  1.00 37.27           C  
ANISOU 5619  CB  ASN D 179     5935   4289   3936    395     40    343       C  
ATOM   5620  CG  ASN D 179      16.193 -48.966  18.047  1.00 38.48           C  
ANISOU 5620  CG  ASN D 179     6124   4384   4111    420      8    372       C  
ATOM   5621  OD1 ASN D 179      15.506 -49.910  17.653  1.00 39.64           O  
ANISOU 5621  OD1 ASN D 179     6280   4484   4299    374     86    404       O  
ATOM   5622  ND2 ASN D 179      17.507 -49.066  18.244  1.00 39.39           N  
ANISOU 5622  ND2 ASN D 179     6258   4500   4209    493   -111    358       N  
ATOM   5623  OXT ASN D 179      12.144 -48.247  17.271  1.00 37.38           O  
ANISOU 5623  OXT ASN D 179     5842   4269   4091    197    345    383       O  
TER    5624      ASN D 179                                                      
HETATM 5625 ZN    ZN A 180      -3.647  -1.813  -7.670  1.00  9.00          ZN  
HETATM 5626  P   PO4 A 181      -6.562  -2.841  -7.769  1.00 29.85           P  
HETATM 5627  O1  PO4 A 181      -6.636  -1.973  -9.011  1.00 28.47           O  
HETATM 5628  O2  PO4 A 181      -7.951  -2.994  -7.173  1.00 27.13           O  
HETATM 5629  O3  PO4 A 181      -6.045  -4.208  -8.163  1.00 26.65           O  
HETATM 5630  O4  PO4 A 181      -5.616  -2.195  -6.775  1.00 26.64           O  
HETATM 5631  P   PO4 A 182      14.440   3.669   0.464  1.00 21.60           P  
HETATM 5632  O1  PO4 A 182      14.635   4.130  -0.957  1.00 22.50           O  
HETATM 5633  O2  PO4 A 182      13.183   4.310   1.001  1.00 22.52           O  
HETATM 5634  O3  PO4 A 182      14.352   2.164   0.509  1.00 21.36           O  
HETATM 5635  O4  PO4 A 182      15.619   4.082   1.312  1.00 23.92           O  
HETATM 5636  P   PO4 A 183     -20.273   2.966   6.739  1.00 18.11           P  
HETATM 5637  O1  PO4 A 183     -20.147   3.703   5.425  1.00 17.58           O  
HETATM 5638  O2  PO4 A 183     -21.713   3.019   7.214  1.00 18.26           O  
HETATM 5639  O3  PO4 A 183     -19.840   1.527   6.605  1.00 18.11           O  
HETATM 5640  O4  PO4 A 183     -19.400   3.659   7.759  1.00 19.41           O  
HETATM 5641 ZN    ZN B 180     -17.027 -22.215  43.602  1.00  9.64          ZN  
HETATM 5642  P   PO4 B 181     -13.536 -23.139  43.375  1.00 49.21           P  
HETATM 5643  O1  PO4 B 181     -12.924 -24.016  42.306  1.00 47.99           O  
HETATM 5644  O2  PO4 B 181     -14.801 -22.462  42.889  1.00 48.07           O  
HETATM 5645  O3  PO4 B 181     -13.905 -23.988  44.570  1.00 48.94           O  
HETATM 5646  O4  PO4 B 181     -12.515 -22.100  43.779  1.00 48.51           O  
HETATM 5647  P   PO4 B 182     -23.037 -34.396  26.808  1.00 17.88           P  
HETATM 5648  O1  PO4 B 182     -22.483 -33.050  26.434  1.00 18.15           O  
HETATM 5649  O2  PO4 B 182     -24.430 -34.501  26.258  1.00 19.67           O  
HETATM 5650  O3  PO4 B 182     -22.199 -35.510  26.252  1.00 18.42           O  
HETATM 5651  O4  PO4 B 182     -23.053 -34.529  28.305  1.00 20.24           O  
HETATM 5652  P   PO4 B 183     -37.057 -16.853  29.455  1.00 17.45           P  
HETATM 5653  O1  PO4 B 183     -35.651 -16.616  28.972  1.00 18.16           O  
HETATM 5654  O2  PO4 B 183     -38.009 -16.138  28.528  1.00 18.36           O  
HETATM 5655  O3  PO4 B 183     -37.335 -18.336  29.453  1.00 17.74           O  
HETATM 5656  O4  PO4 B 183     -37.184 -16.318  30.863  1.00 18.55           O  
HETATM 5657  P   PO4 B 184     -35.346 -16.501  35.954  1.00 22.53           P  
HETATM 5658  O1  PO4 B 184     -34.047 -15.867  35.506  1.00 22.96           O  
HETATM 5659  O2  PO4 B 184     -36.454 -16.023  35.048  1.00 23.45           O  
HETATM 5660  O3  PO4 B 184     -35.251 -18.005  35.897  1.00 22.70           O  
HETATM 5661  O4  PO4 B 184     -35.639 -16.099  37.380  1.00 23.08           O  
HETATM 5662 ZN    ZN C 180      -2.148 -51.802  44.655  1.00 10.70          ZN  
HETATM 5663  P   PO4 C 181      -4.930 -51.409  45.019  1.00 47.05           P  
HETATM 5664  O1  PO4 C 181      -3.997 -51.689  43.865  1.00 46.08           O  
HETATM 5665  O2  PO4 C 181      -5.016 -49.916  45.239  1.00 47.13           O  
HETATM 5666  O3  PO4 C 181      -6.314 -51.924  44.691  1.00 47.25           O  
HETATM 5667  O4  PO4 C 181      -4.403 -52.066  46.277  1.00 46.15           O  
HETATM 5668  P   PO4 C 182     -20.671 -57.359  36.631  1.00 26.36           P  
HETATM 5669  O1  PO4 C 182     -19.570 -57.870  35.735  1.00 27.10           O  
HETATM 5670  O2  PO4 C 182     -21.983 -57.941  36.148  1.00 26.60           O  
HETATM 5671  O3  PO4 C 182     -20.412 -57.783  38.052  1.00 25.75           O  
HETATM 5672  O4  PO4 C 182     -20.703 -55.856  36.566  1.00 25.78           O  
HETATM 5673  P   PO4 C 183      17.638 -56.601  30.284  1.00 23.85           P  
HETATM 5674  O1  PO4 C 183      17.950 -55.128  30.399  1.00 23.58           O  
HETATM 5675  O2  PO4 C 183      16.254 -56.772  29.697  1.00 23.34           O  
HETATM 5676  O3  PO4 C 183      18.641 -57.287  29.385  1.00 23.42           O  
HETATM 5677  O4  PO4 C 183      17.688 -57.228  31.648  1.00 22.73           O  
HETATM 5678 ZN    ZN D 180      17.696 -31.476  -6.934  1.00 13.44          ZN  
HETATM 5679  P   PO4 D 181      20.181 -31.057  -7.913  1.00 51.16           P  
HETATM 5680  O1  PO4 D 181      21.486 -31.718  -8.297  1.00 50.55           O  
HETATM 5681  O2  PO4 D 181      20.314 -29.557  -8.069  1.00 50.37           O  
HETATM 5682  O3  PO4 D 181      19.092 -31.559  -8.835  1.00 50.19           O  
HETATM 5683  O4  PO4 D 181      19.836 -31.363  -6.472  1.00 49.99           O  
HETATM 5684  P   PO4 D 182      12.535 -19.224   9.997  1.00 18.63           P  
HETATM 5685  O1  PO4 D 182      12.348 -18.976   8.524  1.00 17.87           O  
HETATM 5686  O2  PO4 D 182      11.197 -19.256  10.696  1.00 18.04           O  
HETATM 5687  O3  PO4 D 182      13.225 -20.552  10.196  1.00 18.35           O  
HETATM 5688  O4  PO4 D 182      13.388 -18.127  10.577  1.00 18.53           O  
HETATM 5689  P   PO4 D 183      -1.823 -36.675   8.023  1.00 23.07           P  
HETATM 5690  O1  PO4 D 183      -0.415 -36.766   8.561  1.00 20.94           O  
HETATM 5691  O2  PO4 D 183      -2.270 -35.231   7.975  1.00 21.64           O  
HETATM 5692  O3  PO4 D 183      -1.869 -37.235   6.620  1.00 22.25           O  
HETATM 5693  O4  PO4 D 183      -2.740 -37.478   8.919  1.00 23.25           O  
HETATM 5694  P   PO4 D 184       2.272 -14.822   8.265  1.00 16.14           P  
HETATM 5695  O1  PO4 D 184       1.544 -15.007   6.957  1.00 16.79           O  
HETATM 5696  O2  PO4 D 184       1.655 -13.656   9.005  1.00 15.66           O  
HETATM 5697  O3  PO4 D 184       2.137 -16.076   9.078  1.00 15.44           O  
HETATM 5698  O4  PO4 D 184       3.716 -14.522   8.043  1.00 16.70           O  
HETATM 5699  O   HOH A 184       2.601 -13.045   3.229  1.00  2.00           O  
HETATM 5700  O   HOH A 185     -15.233   4.059  -7.573  1.00  4.72           O  
HETATM 5701  O   HOH A 186       0.098   1.267  -6.746  1.00  5.64           O  
HETATM 5702  O   HOH A 187      11.220  -8.860 -13.222  1.00 12.78           O  
HETATM 5703  O   HOH A 188       9.107  -1.474 -16.351  1.00  2.00           O  
HETATM 5704  O   HOH A 189      -2.183  11.201 -11.209  1.00 16.20           O  
HETATM 5705  O   HOH A 190      -3.507  11.378  10.062  1.00  6.77           O  
HETATM 5706  O   HOH A 191       1.621  -7.765 -10.687  1.00  5.71           O  
HETATM 5707  O   HOH A 192      -0.192  -9.909  -5.842  1.00  8.57           O  
HETATM 5708  O   HOH A 193      -7.476 -14.633  14.081  1.00 26.23           O  
HETATM 5709  O   HOH A 194       3.443  -9.627 -11.977  1.00  5.42           O  
HETATM 5710  O   HOH A 195     -14.739   7.064   1.585  1.00  4.72           O  
HETATM 5711  O   HOH A 196      -9.351  -4.820  -3.419  1.00 14.56           O  
HETATM 5712  O   HOH A 197      -1.746 -10.185  -8.538  1.00 14.20           O  
HETATM 5713  O   HOH A 198       1.908  -4.889  -8.716  1.00  7.71           O  
HETATM 5714  O   HOH A 199     -11.977  -4.663   9.328  1.00 11.62           O  
HETATM 5715  O   HOH A 200      -5.547  10.032 -13.359  1.00 18.20           O  
HETATM 5716  O   HOH A 201      -1.587  15.493  -1.240  1.00 11.79           O  
HETATM 5717  O   HOH A 202      18.429  -9.684   5.179  1.00 13.94           O  
HETATM 5718  O   HOH A 203       6.951 -11.429   9.352  1.00  5.80           O  
HETATM 5719  O   HOH A 204      -2.678  12.535  -0.374  1.00  9.10           O  
HETATM 5720  O   HOH A 205       4.559  -3.384  -8.507  1.00  9.88           O  
HETATM 5721  O   HOH A 206      -9.989  14.367   4.613  1.00 20.47           O  
HETATM 5722  O   HOH A 207       6.458   8.339 -14.246  1.00  8.36           O  
HETATM 5723  O   HOH A 208      -2.801   3.308 -15.561  1.00  8.92           O  
HETATM 5724  O   HOH A 209     -15.642   7.619   7.489  1.00 16.51           O  
HETATM 5725  O   HOH A 210       0.140  -9.222  13.906  1.00 11.19           O  
HETATM 5726  O   HOH A 211      -0.179  -4.759 -12.182  1.00  9.04           O  
HETATM 5727  O   HOH A 212      11.853   7.475  17.572  1.00 16.76           O  
HETATM 5728  O   HOH A 213      16.105  -0.848   5.773  1.00 12.71           O  
HETATM 5729  O   HOH A 214      -2.549  14.204   9.866  1.00  9.33           O  
HETATM 5730  O   HOH A 215      12.829   3.661 -13.052  1.00 17.87           O  
HETATM 5731  O   HOH A 216       1.029  -7.344  -6.561  1.00 14.18           O  
HETATM 5732  O   HOH A 217     -10.237   0.701  -1.209  1.00  8.25           O  
HETATM 5733  O   HOH A 218      -1.441 -19.743  -0.904  1.00  7.70           O  
HETATM 5734  O   HOH A 219      13.163  -9.869  10.295  1.00 25.65           O  
HETATM 5735  O   HOH A 220     -16.845   3.746   7.669  1.00  8.57           O  
HETATM 5736  O   HOH A 221      -1.189 -11.453   5.822  1.00  7.66           O  
HETATM 5737  O   HOH A 222       1.604   6.545 -14.443  1.00  5.40           O  
HETATM 5738  O   HOH A 223     -15.268   9.660   0.206  1.00 24.72           O  
HETATM 5739  O   HOH A 224      10.011   8.323 -13.360  1.00 23.50           O  
HETATM 5740  O   HOH A 225       8.749   6.319 -16.934  1.00 10.88           O  
HETATM 5741  O   HOH A 226      11.752  10.173   9.196  1.00 14.51           O  
HETATM 5742  O   HOH A 227       6.969  11.018  -7.948  1.00 17.27           O  
HETATM 5743  O   HOH A 228       5.645   9.130  12.749  1.00  8.32           O  
HETATM 5744  O   HOH A 229     -10.234  -2.572 -10.672  1.00 19.31           O  
HETATM 5745  O   HOH A 238     -16.335  14.863   4.257  1.00 25.85           O  
HETATM 5746  O   HOH A 245      -8.496  -1.139  15.768  1.00 13.20           O  
HETATM 5747  O   HOH A 246      10.683   3.388 -10.680  1.00 21.64           O  
HETATM 5748  O   HOH A 247      12.663  -7.657 -16.038  1.00 24.98           O  
HETATM 5749  O   HOH A 250      15.224  -6.109  -0.236  1.00 12.22           O  
HETATM 5750  O   HOH A 255       2.712  -9.905  14.082  1.00 11.72           O  
HETATM 5751  O   HOH A 257      12.218 -10.848   3.989  1.00  5.87           O  
HETATM 5752  O   HOH A 258       4.202 -10.917  12.046  1.00  9.76           O  
HETATM 5753  O   HOH A 274       1.810  -2.239 -23.253  1.00 15.31           O  
HETATM 5754  O   HOH A 277      13.203 -14.931   3.086  1.00  5.48           O  
HETATM 5755  O   HOH A 279       6.767  11.912  -2.046  1.00 12.39           O  
HETATM 5756  O   HOH A 280       0.052   9.132 -15.273  1.00 14.92           O  
HETATM 5757  O   HOH A 283       5.796  -3.179 -22.779  1.00 15.65           O  
HETATM 5758  O   HOH A 285      -6.420  -5.763  15.197  1.00 17.29           O  
HETATM 5759  O   HOH A 291       8.370   3.610 -25.023  1.00 20.47           O  
HETATM 5760  O   HOH A 297      17.686  -3.953   3.662  1.00 22.02           O  
HETATM 5761  O   HOH A 298      -8.475 -16.660  -0.319  1.00  7.65           O  
HETATM 5762  O   HOH A 304     -17.944  -1.751   5.645  1.00 15.90           O  
HETATM 5763  O   HOH A 308      -0.934  -4.637  19.209  1.00 17.57           O  
HETATM 5764  O   HOH A 309       4.557   0.167  18.139  1.00 26.05           O  
HETATM 5765  O   HOH A 313      -3.265  14.759  12.726  1.00 25.37           O  
HETATM 5766  O   HOH A 315      13.761   9.816   7.460  1.00 16.52           O  
HETATM 5767  O   HOH A 317      -6.733   0.788  15.080  1.00 25.96           O  
HETATM 5768  O   HOH A 318       5.206   8.484  19.041  1.00  9.41           O  
HETATM 5769  O   HOH A 325      -3.908  -3.167 -15.767  1.00 15.68           O  
HETATM 5770  O   HOH A 326      18.370  -1.688   2.357  1.00 18.35           O  
HETATM 5771  O   HOH A 329      19.653 -11.841   2.163  1.00 16.54           O  
HETATM 5772  O   HOH A 337       4.031  -5.326  15.374  1.00 17.88           O  
HETATM 5773  O   HOH A 341      16.384  -2.802  -8.911  1.00 26.06           O  
HETATM 5774  O   HOH A 342     -11.429   5.339 -14.045  1.00 18.19           O  
HETATM 5775  O   HOH A 347      13.291  -1.048  -6.121  1.00 18.17           O  
HETATM 5776  O   HOH A 354      -2.931  -8.453 -12.439  1.00 34.93           O  
HETATM 5777  O   HOH A 358      -5.659 -17.268   7.252  1.00 18.24           O  
HETATM 5778  O   HOH A 361     -12.835   3.916  12.537  1.00 14.65           O  
HETATM 5779  O   HOH A 363     -14.097   6.460  13.167  1.00 14.46           O  
HETATM 5780  O   HOH A 367      11.032   2.398 -23.477  1.00 17.83           O  
HETATM 5781  O   HOH A 368       4.144   1.411  21.802  1.00 24.20           O  
HETATM 5782  O   HOH A 370      13.044   3.426  -3.574  1.00 26.27           O  
HETATM 5783  O   HOH A 386      15.619  -4.151  -2.382  1.00 17.13           O  
HETATM 5784  O   HOH A 390       1.991 -17.068  -6.237  1.00 23.64           O  
HETATM 5785  O   HOH A 400       2.650  -3.235  16.084  1.00 13.18           O  
HETATM 5786  O   HOH A 401     -10.485  15.603  -9.140  1.00 14.03           O  
HETATM 5787  O   HOH A 415       9.369   9.789  17.505  1.00 21.03           O  
HETATM 5788  O   HOH A 418     -16.604  -4.287   2.133  1.00 29.94           O  
HETATM 5789  O   HOH A 427      -4.966  -2.549 -12.436  1.00 18.23           O  
HETATM 5790  O   HOH A 430     -11.391   6.618  15.644  1.00 20.34           O  
HETATM 5791  O   HOH A 434       5.470 -13.097  13.344  1.00 21.83           O  
HETATM 5792  O   HOH A 441      14.663   5.181  11.965  1.00 11.78           O  
HETATM 5793  O   HOH A 443      11.081  12.690   9.386  1.00 26.96           O  
HETATM 5794  O   HOH A 445     -14.625  14.574  -0.404  1.00 23.41           O  
HETATM 5795  O   HOH A 446       2.319  -6.253 -22.223  1.00 21.51           O  
HETATM 5796  O   HOH A 448       9.602 -11.776   9.658  1.00 19.96           O  
HETATM 5797  O   HOH A 452      -9.323 -14.401   8.549  1.00 18.52           O  
HETATM 5798  O   HOH A 453       9.213  -6.352  16.767  1.00 30.78           O  
HETATM 5799  O   HOH A 457       6.333  12.699  -5.317  1.00 21.77           O  
HETATM 5800  O   HOH A 459      12.211  -6.919 -19.897  1.00 17.66           O  
HETATM 5801  O   HOH A 466      -4.452  -4.928  18.346  1.00 28.82           O  
HETATM 5802  O   HOH A 468       7.867 -14.784   7.902  1.00 20.36           O  
HETATM 5803  O   HOH A 469      -6.386  -3.353  19.126  1.00 25.88           O  
HETATM 5804  O   HOH A 470      -7.929  -8.985  -4.681  1.00 41.36           O  
HETATM 5805  O   HOH A 473       4.117 -16.900  12.280  1.00 35.88           O  
HETATM 5806  O   HOH A 478      14.850  -0.645  -3.165  1.00 39.21           O  
HETATM 5807  O   HOH A 486      15.988   7.764   8.581  1.00 13.67           O  
HETATM 5808  O   HOH A 490      -9.122 -14.831  11.905  1.00 33.58           O  
HETATM 5809  O   HOH A 492       8.596   9.486  -5.376  1.00 26.06           O  
HETATM 5810  O   HOH A 495       4.184  12.720  -8.253  1.00 20.41           O  
HETATM 5811  O   HOH A 497       8.710   4.077  18.355  1.00 24.95           O  
HETATM 5812  O   HOH A 507      -2.663 -18.897  -5.960  1.00 27.13           O  
HETATM 5813  O   HOH A 511      14.903 -10.819 -24.265  1.00 13.85           O  
HETATM 5814  O   HOH A 518      -9.155 -13.532  15.728  1.00 21.91           O  
HETATM 5815  O   HOH A 525      12.671  12.422  13.177  1.00 26.70           O  
HETATM 5816  O   HOH A 528     -14.253  -7.516   6.141  1.00 16.18           O  
HETATM 5817  O   HOH A 529     -10.784  16.975  -6.953  1.00 25.21           O  
HETATM 5818  O   HOH A 531     -20.226   3.079  -2.805  1.00 23.24           O  
HETATM 5819  O   HOH A 534       9.460 -10.625  12.787  1.00 29.46           O  
HETATM 5820  O   HOH A 535      -3.893  10.438  16.493  1.00 18.00           O  
HETATM 5821  O   HOH A 536      20.227  -1.766  -5.776  1.00 28.48           O  
HETATM 5822  O   HOH A 537       7.178   5.171  21.121  1.00 24.20           O  
HETATM 5823  O   HOH A 540       0.994  14.809  12.236  1.00 23.38           O  
HETATM 5824  O   HOH A 545     -12.304  -9.373   9.587  1.00 23.83           O  
HETATM 5825  O   HOH A 546       5.291  18.632   9.277  1.00 28.78           O  
HETATM 5826  O   HOH A 549      -7.883  -7.930  14.420  1.00 28.13           O  
HETATM 5827  O   HOH A 557     -14.537  -7.681  -1.523  1.00 24.51           O  
HETATM 5828  O   HOH A 566      -0.824  -8.518 -10.890  1.00 18.27           O  
HETATM 5829  O   HOH A 569     -12.573  14.537   5.374  1.00 11.96           O  
HETATM 5830  O   HOH A 571       4.866  11.535  18.909  1.00 38.80           O  
HETATM 5831  O   HOH A 574      -8.179   6.613  15.854  1.00 21.24           O  
HETATM 5832  O   HOH A 575      -0.993  -6.319  -8.415  1.00 14.48           O  
HETATM 5833  O   HOH A 579      -4.075  -5.473 -12.137  1.00 13.08           O  
HETATM 5834  O   HOH A 583       4.207   7.412 -17.749  1.00 31.72           O  
HETATM 5835  O   HOH A 590      16.115  -5.347 -12.879  1.00 25.74           O  
HETATM 5836  O   HOH A 592       6.748   1.652  17.395  1.00  9.36           O  
HETATM 5837  O   HOH A 595     -14.217   2.026  11.139  1.00  6.76           O  
HETATM 5838  O   HOH A 597      10.607   6.424  -6.667  1.00 14.44           O  
HETATM 5839  O   HOH A 600     -17.111   8.048   2.739  1.00  9.86           O  
HETATM 5840  O   HOH A 602      -7.431 -18.941   9.383  1.00 32.15           O  
HETATM 5841  O   HOH A 604     -10.532  -7.448  15.193  1.00 18.41           O  
HETATM 5842  O   HOH A 606      -8.113  -4.368  16.536  1.00 23.49           O  
HETATM 5843  O   HOH A 609     -15.250  15.994  -2.645  1.00 26.07           O  
HETATM 5844  O   HOH A 611      -0.991 -15.052  -8.779  1.00 42.84           O  
HETATM 5845  O   HOH A 619     -19.747   5.803   3.405  1.00 38.63           O  
HETATM 5846  O   HOH A 626       0.171  12.610  -5.216  1.00 17.00           O  
HETATM 5847  O   HOH A 628      18.779  -2.534  -7.889  1.00 41.62           O  
HETATM 5848  O   HOH A 630      -3.986 -19.106   8.677  1.00 18.53           O  
HETATM 5849  O   HOH A 632      -6.891 -15.339   8.560  1.00 24.11           O  
HETATM 5850  O   HOH A 635       6.754 -13.882 -12.587  1.00 39.97           O  
HETATM 5851  O   HOH A 636      -7.754  -9.409  17.839  1.00 28.00           O  
HETATM 5852  O   HOH A 638      17.984  -0.733  -5.637  1.00 31.13           O  
HETATM 5853  O   HOH A 644       6.488  10.834  16.608  1.00 22.93           O  
HETATM 5854  O   HOH A 653     -11.599 -10.668   7.535  1.00 15.16           O  
HETATM 5855  O   HOH A 654      10.859   6.067  -3.012  1.00 17.35           O  
HETATM 5856  O   HOH A 655      15.302  -0.685 -24.915  1.00 25.24           O  
HETATM 5857  O   HOH A 658     -24.982   6.917 -10.763  1.00 22.91           O  
HETATM 5858  O   HOH A 664      15.348  -3.334 -25.300  1.00 20.28           O  
HETATM 5859  O   HOH A 668      16.711   0.389  -7.689  1.00 16.94           O  
HETATM 5860  O   HOH A 693       4.561  10.265  -8.747  1.00  7.62           O  
HETATM 5861  O   HOH A 694      -3.917  -6.113  -6.860  1.00 17.42           O  
HETATM 5862  O   HOH A 696      -2.172   3.192  -1.034  1.00  3.48           O  
HETATM 5863  O   HOH A 712       1.179  -6.917 -19.510  1.00 14.41           O  
HETATM 5864  O   HOH A 724       8.677  12.269   3.342  1.00 12.17           O  
HETATM 5865  O   HOH A 726      -3.449  10.107 -14.905  1.00 15.96           O  
HETATM 5866  O   HOH A 734      -7.145  20.116  -5.789  1.00 35.67           O  
HETATM 5867  O   HOH A 736     -11.268  -6.768  10.702  1.00 16.94           O  
HETATM 5868  O   HOH A 738       0.008  -6.469  15.166  1.00 16.44           O  
HETATM 5869  O   HOH A 753      14.340   9.868   4.228  1.00 30.92           O  
HETATM 5870  O   HOH A 759      -1.764 -12.666  -7.919  1.00 18.37           O  
HETATM 5871  O   HOH A 765     -12.840  -3.917  -3.322  1.00 25.00           O  
HETATM 5872  O   HOH A 766       1.379 -15.446  -9.931  1.00 36.93           O  
HETATM 5873  O   HOH A 768     -12.333  16.472   1.324  1.00 29.69           O  
HETATM 5874  O   HOH A 776     -11.815  -2.906  15.298  1.00 15.99           O  
HETATM 5875  O   HOH A 779       1.882 -18.731  -8.270  1.00 19.48           O  
HETATM 5876  O   HOH A 793       7.782 -15.281 -10.620  1.00 18.73           O  
HETATM 5877  O   HOH A 794      -4.267  13.843 -10.340  1.00 28.85           O  
HETATM 5878  O   HOH A 800      14.302 -10.503  -9.801  1.00 26.78           O  
HETATM 5879  O   HOH A 808     -23.402   9.136 -10.504  1.00 25.24           O  
HETATM 5880  O   HOH A 811      -1.690  15.827  21.093  1.00 29.67           O  
HETATM 5881  O   HOH A 816      -4.006 -11.279 -15.818  1.00 29.53           O  
HETATM 5882  O   HOH A 829      19.102  -4.295   7.634  1.00 18.61           O  
HETATM 5883  O   HOH A 832      -8.317  15.056 -10.585  1.00 24.21           O  
HETATM 5884  O   HOH A 839      -5.722   9.765 -17.508  1.00 22.85           O  
HETATM 5885  O   HOH A 858     -12.255   8.272 -12.708  1.00 14.53           O  
HETATM 5886  O   HOH A 870       7.710 -10.893 -22.093  1.00 10.00           O  
HETATM 5887  O   HOH A 873     -20.008  16.150  -4.324  1.00 23.14           O  
HETATM 5888  O   HOH A 880      16.626 -10.083  -5.397  1.00 24.50           O  
HETATM 5889  O   HOH A 886      -0.655   5.217  21.852  1.00  9.18           O  
HETATM 5890  O   HOH A 893     -17.114   7.721   5.327  1.00 27.98           O  
HETATM 5891  O   HOH A 895      -0.962 -15.310 -13.360  1.00 37.87           O  
HETATM 5892  O   HOH A 899      17.610 -13.076  -4.319  1.00 27.65           O  
HETATM 5893  O   HOH A 902      13.466   1.620  -9.229  1.00 28.71           O  
HETATM 5894  O   HOH A 912      16.038   5.321   9.763  1.00 23.14           O  
HETATM 5895  O   HOH A 914       4.913  11.606  12.464  1.00 19.61           O  
HETATM 5896  O   HOH A 915      16.938  -7.893 -14.075  1.00 23.52           O  
HETATM 5897  O   HOH A 917      12.021  14.823   3.340  1.00 24.06           O  
HETATM 5898  O   HOH A 918     -18.359  11.791 -12.679  1.00 22.41           O  
HETATM 5899  O   HOH A 922      -2.046 -13.085 -12.281  1.00 30.02           O  
HETATM 5900  O   HOH A 925     -13.455  -5.979  12.816  1.00 19.99           O  
HETATM 5901  O   HOH A 931     -11.619  10.371 -14.498  1.00 17.06           O  
HETATM 5902  O   HOH A 935      17.560   2.390  12.191  1.00 16.19           O  
HETATM 5903  O   HOH A 945       0.483  15.588  15.290  1.00 39.90           O  
HETATM 5904  O   HOH A 947       6.649  10.056 -11.419  1.00 16.50           O  
HETATM 5905  O   HOH A 949      -5.463  -5.558  -4.878  1.00 16.76           O  
HETATM 5906  O   HOH A 950       9.264 -12.566 -15.364  1.00 12.36           O  
HETATM 5907  O   HOH A 954       4.490 -18.068  -6.593  1.00 29.98           O  
HETATM 5908  O   HOH A 955       8.111 -12.200 -17.685  1.00 21.03           O  
HETATM 5909  O   HOH A 956     -14.900   5.147 -13.525  1.00 26.35           O  
HETATM 5910  O   HOH A 959      -2.986  16.078   7.467  1.00 16.17           O  
HETATM 5911  O   HOH A 963      11.103  -6.553  14.821  1.00 32.40           O  
HETATM 5912  O   HOH A 966      -7.435   5.894  18.366  1.00 28.43           O  
HETATM 5913  O   HOH A 967      16.672  -7.616 -11.499  1.00 38.21           O  
HETATM 5914  O   HOH A 969      15.272 -13.767  -2.636  1.00 22.91           O  
HETATM 5915  O   HOH A 970      12.083  13.002   5.432  1.00 30.44           O  
HETATM 5916  O   HOH A 984     -11.388  -2.535  10.973  1.00 21.74           O  
HETATM 5917  O   HOH A 985      11.834  10.531   1.796  1.00 28.72           O  
HETATM 5918  O   HOH A 987      -1.201 -17.503  13.821  1.00 25.54           O  
HETATM 5919  O   HOH A 992      19.810 -13.328  -0.233  1.00 20.17           O  
HETATM 5920  O   HOH A 993      15.678   0.449  -0.962  1.00 26.67           O  
HETATM 5921  O   HOH A 994     -13.877  12.280   6.204  1.00 24.61           O  
HETATM 5922  O   HOH A1000     -15.653   8.162  10.604  1.00 28.22           O  
HETATM 5923  O   HOH A1002       5.238  -8.222  11.647  1.00 12.14           O  
HETATM 5924  O   HOH A1006     -15.249  19.971 -11.089  1.00 34.37           O  
HETATM 5925  O   HOH A1014     -11.703 -11.862  12.951  1.00 19.14           O  
HETATM 5926  O   HOH A1015       4.110  -3.919  18.672  1.00 18.30           O  
HETATM 5927  O   HOH A1033      -2.547   8.380 -16.802  1.00 40.94           O  
HETATM 5928  O   HOH A1037      10.702  14.600  11.040  1.00 22.09           O  
HETATM 5929  O   HOH A1042     -12.790  -0.871 -12.028  1.00 26.06           O  
HETATM 5930  O   HOH A1043      -2.680  17.951  -1.160  1.00 15.33           O  
HETATM 5931  O   HOH A1048     -15.455   1.411 -14.489  1.00 14.92           O  
HETATM 5932  O   HOH A1052     -15.128   7.408 -11.906  1.00 27.88           O  
HETATM 5933  O   HOH A1058      19.790   1.770  10.453  1.00 26.88           O  
HETATM 5934  O   HOH A1073      16.583  -8.366   8.813  1.00 16.31           O  
HETATM 5935  O   HOH A1079      -8.229  11.106  11.508  1.00 11.67           O  
HETATM 5936  O   HOH A1081      15.824  -6.737  11.978  1.00 17.40           O  
HETATM 5937  O   HOH A1082      -8.532   2.816  15.837  1.00 14.61           O  
HETATM 5938  O   HOH A1083      16.949  -3.832  10.974  1.00 21.83           O  
HETATM 5939  O   HOH A1090      -3.393  10.586  12.511  1.00 19.22           O  
HETATM 5940  O   HOH A1091     -10.940   1.586  16.155  1.00 26.07           O  
HETATM 5941  O   HOH A1094       7.154  -3.049 -25.217  1.00 19.16           O  
HETATM 5942  O   HOH A1114      -0.569  10.823 -13.155  1.00 20.51           O  
HETATM 5943  O   HOH A1135     -12.749  21.346   3.799  1.00 14.96           O  
HETATM 5944  O   HOH A1145     -18.370   9.657  -3.772  1.00 23.28           O  
HETATM 5945  O   HOH A1153      15.826  16.378  13.971  1.00 23.30           O  
HETATM 5946  O   HOH A1160       2.384 -18.640  13.401  1.00 28.70           O  
HETATM 5947  O   HOH A1162      14.248   6.760  -1.740  1.00 20.20           O  
HETATM 5948  O   HOH A1163      -5.609  -7.254  -9.037  1.00 32.24           O  
HETATM 5949  O   HOH A1178      -0.427  -8.846 -19.749  1.00 19.48           O  
HETATM 5950  O   HOH A1185      11.347 -10.346 -29.046  1.00 34.36           O  
HETATM 5951  O   HOH A1186      15.142  13.926  14.297  1.00 22.26           O  
HETATM 5952  O   HOH A1193     -14.152  -6.621  -5.054  1.00 20.79           O  
HETATM 5953  O   HOH A1197      11.648  10.900  -1.359  1.00 29.53           O  
HETATM 5954  O   HOH A1199      18.979  -9.083  -9.452  1.00 23.71           O  
HETATM 5955  O   HOH A1201      -6.148  12.366  10.382  1.00 20.54           O  
HETATM 5956  O   HOH A1210      -0.306 -13.807 -15.609  1.00 28.74           O  
HETATM 5957  O   HOH A1213       4.375 -13.900 -13.746  1.00 25.38           O  
HETATM 5958  O   HOH A1214      13.307   9.915  11.372  1.00 34.69           O  
HETATM 5959  O   HOH A1216       6.621 -16.965  11.668  1.00 29.09           O  
HETATM 5960  O   HOH A1230     -11.135  -9.838  14.346  1.00 30.40           O  
HETATM 5961  O   HOH A1232       2.255  -0.935  20.538  1.00 29.35           O  
HETATM 5962  O   HOH A1246      -3.047 -21.738   8.792  1.00 22.67           O  
HETATM 5963  O   HOH A1249      12.536 -15.574 -24.724  1.00 34.13           O  
HETATM 5964  O   HOH A1254     -17.647  13.887 -11.342  1.00 22.08           O  
HETATM 5965  O   HOH A1256     -16.443   9.477 -13.493  1.00 29.27           O  
HETATM 5966  O   HOH A1260      14.320 -12.579 -22.295  1.00 26.52           O  
HETATM 5967  O   HOH A1266      -7.023 -21.516   8.425  1.00 23.02           O  
HETATM 5968  O   HOH A1271     -15.725  17.208   6.657  1.00 30.37           O  
HETATM 5969  O   HOH A1272       1.765   6.938 -17.053  1.00 23.89           O  
HETATM 5970  O   HOH A1282     -17.266  18.321   4.206  1.00 18.83           O  
HETATM 5971  O   HOH A1285     -13.124  19.472  -4.317  1.00 19.67           O  
HETATM 5972  O   HOH A1290       7.133 -16.934  -6.450  1.00 23.77           O  
HETATM 5973  O   HOH A1295       8.406  12.592   9.536  1.00 31.35           O  
HETATM 5974  O   HOH A1302      -7.224  12.142 -14.448  1.00 16.53           O  
HETATM 5975  O   HOH A1305     -10.975  -2.868  -8.051  1.00 22.55           O  
HETATM 5976  O   HOH A1313     -13.492  16.686   3.707  1.00 24.61           O  
HETATM 5977  O   HOH A1314     -16.851  19.886 -13.589  1.00 30.51           O  
HETATM 5978  O   HOH A1322     -11.750  13.256  10.399  1.00 24.52           O  
HETATM 5979  O   HOH A1330     -18.484   7.195  10.384  1.00 29.02           O  
HETATM 5980  O   HOH A1336     -15.932  19.239 -16.036  1.00 41.20           O  
HETATM 5981  O   HOH A1352      15.704   0.778  13.541  1.00 35.70           O  
HETATM 5982  O   HOH A1375      -2.604  -6.728 -10.334  1.00 31.78           O  
HETATM 5983  O   HOH A1376       5.442  17.847   6.547  1.00 20.57           O  
HETATM 5984  O   HOH A1382      -4.938   9.667  14.269  1.00 14.10           O  
HETATM 5985  O   HOH A1385      22.199 -11.709   3.368  1.00 15.97           O  
HETATM 5986  O   HOH A1388      17.367  -1.270  -2.360  1.00 38.26           O  
HETATM 5987  O   HOH A1418     -21.151  11.534  -0.500  1.00 26.24           O  
HETATM 5988  O   HOH A1419     -10.501  12.781 -14.544  1.00 19.82           O  
HETATM 5989  O   HOH A1420       3.947 -14.521   4.050  1.00 24.54           O  
HETATM 5990  O   HOH A1426      -0.843 -16.783  -6.752  1.00 31.91           O  
HETATM 5991  O   HOH A1444     -15.690   4.147   9.990  1.00 25.51           O  
HETATM 5992  O   HOH A1450      15.501  12.363   9.478  1.00 21.48           O  
HETATM 5993  O   HOH A1456     -15.026  -9.821   5.171  1.00 25.39           O  
HETATM 5994  O   HOH A1458      13.722  -8.376 -12.542  1.00 34.90           O  
HETATM 5995  O   HOH A1459     -11.896  -5.589  -6.897  1.00 36.42           O  
HETATM 5996  O   HOH A1463      -4.273   1.532  15.576  1.00 18.63           O  
HETATM 5997  O   HOH A1467      16.856 -10.570  -9.789  1.00 24.28           O  
HETATM 5998  O   HOH A1468      -4.018  -4.130  -8.292  1.00 13.81           O  
HETATM 5999  O   HOH A1469      -4.957  -1.406 -10.185  1.00 33.12           O  
HETATM 6000  O   HOH B 185      -9.175 -26.255  24.739  1.00  8.41           O  
HETATM 6001  O   HOH B 186     -28.235 -19.946  49.125  1.00  5.93           O  
HETATM 6002  O   HOH B 187      -5.611 -16.168  43.775  1.00  6.60           O  
HETATM 6003  O   HOH B 188      -6.599 -16.940  25.351  1.00 12.14           O  
HETATM 6004  O   HOH B 189     -17.260  -7.812  26.821  1.00  6.28           O  
HETATM 6005  O   HOH B 190     -27.050 -21.215  44.752  1.00  3.82           O  
HETATM 6006  O   HOH B 191     -18.508  -7.902  36.876  1.00 13.19           O  
HETATM 6007  O   HOH B 192     -21.627 -28.154  54.895  1.00 16.60           O  
HETATM 6008  O   HOH B 193     -20.313 -30.158  41.241  1.00  7.19           O  
HETATM 6009  O   HOH B 194     -10.574 -19.166  37.309  1.00  6.75           O  
HETATM 6010  O   HOH B 195      -3.585  -9.960  44.387  1.00 26.20           O  
HETATM 6011  O   HOH B 196      -4.142 -23.769  34.423  1.00 17.61           O  
HETATM 6012  O   HOH B 197     -22.560 -25.591  44.808  1.00  8.12           O  
HETATM 6013  O   HOH B 198     -23.478 -32.877  31.743  1.00  5.29           O  
HETATM 6014  O   HOH B 199     -29.790 -14.896  53.408  1.00 10.68           O  
HETATM 6015  O   HOH B 200      -6.779  -4.749  37.310  1.00 13.99           O  
HETATM 6016  O   HOH B 201     -26.690 -10.425  24.008  1.00 12.44           O  
HETATM 6017  O   HOH B 202     -18.632  -5.232  26.964  1.00  6.76           O  
HETATM 6018  O   HOH B 203     -20.534 -28.303  21.898  1.00 11.04           O  
HETATM 6019  O   HOH B 204     -12.095  -1.404  37.885  1.00 12.70           O  
HETATM 6020  O   HOH B 205     -25.296 -10.487  45.257  1.00  5.89           O  
HETATM 6021  O   HOH B 206     -20.451 -25.440  48.004  1.00  9.70           O  
HETATM 6022  O   HOH B 207     -27.340 -31.005  25.678  1.00  4.38           O  
HETATM 6023  O   HOH B 208     -25.329 -24.095  44.268  1.00  9.20           O  
HETATM 6024  O   HOH B 209     -12.672  -8.272  25.389  1.00  8.26           O  
HETATM 6025  O   HOH B 210      -9.467 -21.829  25.246  1.00 11.88           O  
HETATM 6026  O   HOH B 211      -2.969 -21.709  30.460  1.00 17.18           O  
HETATM 6027  O   HOH B 212     -18.013 -17.434  51.755  1.00 12.68           O  
HETATM 6028  O   HOH B 213      -8.137  -3.138  35.749  1.00 11.52           O  
HETATM 6029  O   HOH B 214     -15.398 -10.315  50.231  1.00 14.64           O  
HETATM 6030  O   HOH B 215     -33.685 -21.061  41.984  1.00 17.72           O  
HETATM 6031  O   HOH B 216      -4.024 -15.781  28.447  1.00  8.29           O  
HETATM 6032  O   HOH B 217     -23.418 -22.548  20.159  1.00 10.50           O  
HETATM 6033  O   HOH B 218     -27.516  -8.177  38.812  1.00 12.41           O  
HETATM 6034  O   HOH B 219      -6.046 -12.916  34.949  1.00  3.86           O  
HETATM 6035  O   HOH B 220     -22.087 -38.907  33.813  1.00 11.64           O  
HETATM 6036  O   HOH B 221     -32.490 -30.730  31.480  1.00  6.15           O  
HETATM 6037  O   HOH B 222     -24.738 -24.735  20.559  1.00 13.75           O  
HETATM 6038  O   HOH B 223     -21.638 -32.490  29.605  1.00 10.60           O  
HETATM 6039  O   HOH B 224     -11.274 -24.861  39.290  1.00 13.51           O  
HETATM 6040  O   HOH B 225     -11.334  -5.105  32.441  1.00 19.63           O  
HETATM 6041  O   HOH B 226     -20.821 -19.050  43.013  1.00  8.81           O  
HETATM 6042  O   HOH B 227     -21.752  -7.208  41.907  1.00 11.12           O  
HETATM 6043  O   HOH B 228     -18.468  -6.228  38.833  1.00  9.33           O  
HETATM 6044  O   HOH B 229     -23.794 -30.488  47.355  1.00 12.92           O  
HETATM 6045  O   HOH B 230     -28.888 -10.953  42.080  1.00 22.28           O  
HETATM 6046  O   HOH B 231     -34.741 -31.599  45.275  1.00 11.49           O  
HETATM 6047  O   HOH B 232     -22.191 -28.671  46.329  1.00  8.90           O  
HETATM 6048  O   HOH B 233     -22.480 -14.277  50.979  1.00 10.26           O  
HETATM 6049  O   HOH B 234     -15.732 -21.913  15.129  1.00  8.50           O  
HETATM 6050  O   HOH B 235     -26.377 -24.538  58.898  1.00 11.49           O  
HETATM 6051  O   HOH B 236     -29.837  -7.810  33.402  1.00 14.21           O  
HETATM 6052  O   HOH B 239      -4.006  -3.207  41.529  1.00 32.64           O  
HETATM 6053  O   HOH B 242     -12.106 -34.323  23.422  1.00 26.47           O  
HETATM 6054  O   HOH B 249     -20.893 -25.892  20.754  1.00 15.28           O  
HETATM 6055  O   HOH B 252      -5.543  -9.977  36.356  1.00 23.23           O  
HETATM 6056  O   HOH B 253     -33.351 -17.448  49.163  1.00 17.98           O  
HETATM 6057  O   HOH B 259     -22.903 -14.846  53.461  1.00 14.46           O  
HETATM 6058  O   HOH B 265     -11.576 -35.694  37.394  1.00 25.42           O  
HETATM 6059  O   HOH B 273     -19.920 -26.478  44.333  1.00 16.99           O  
HETATM 6060  O   HOH B 281     -12.437 -27.286  21.318  1.00 31.64           O  
HETATM 6061  O   HOH B 286      -9.757 -22.946  44.259  1.00 20.83           O  
HETATM 6062  O   HOH B 287      -8.622 -24.132  26.572  1.00 11.11           O  
HETATM 6063  O   HOH B 289     -21.050 -36.400  44.078  1.00 18.93           O  
HETATM 6064  O   HOH B 290     -15.172 -26.067  40.612  1.00 12.37           O  
HETATM 6065  O   HOH B 292     -26.509 -25.118  61.444  1.00  9.52           O  
HETATM 6066  O   HOH B 293     -16.977 -23.852  54.568  1.00 16.76           O  
HETATM 6067  O   HOH B 294     -37.043 -33.410  31.890  1.00 13.48           O  
HETATM 6068  O   HOH B 300     -17.793 -37.059  25.059  1.00  8.46           O  
HETATM 6069  O   HOH B 301     -32.865 -34.699  45.395  1.00 10.09           O  
HETATM 6070  O   HOH B 305      -8.862  -5.129  31.689  1.00 18.26           O  
HETATM 6071  O   HOH B 310     -19.397 -31.139  29.583  1.00 10.37           O  
HETATM 6072  O   HOH B 312     -33.343 -33.314  31.271  1.00 22.09           O  
HETATM 6073  O   HOH B 323     -32.290 -14.497  54.451  1.00 17.92           O  
HETATM 6074  O   HOH B 330     -32.209  -7.549  20.569  1.00 21.97           O  
HETATM 6075  O   HOH B 332      -3.196  -8.095  31.954  1.00 20.40           O  
HETATM 6076  O   HOH B 339     -19.313  -6.242  41.403  1.00 23.16           O  
HETATM 6077  O   HOH B 340     -24.322 -36.416  23.556  1.00 27.89           O  
HETATM 6078  O   HOH B 343     -28.666 -10.158  52.477  1.00 28.84           O  
HETATM 6079  O   HOH B 344      -7.947 -31.269  31.283  1.00 11.69           O  
HETATM 6080  O   HOH B 346     -12.592 -41.748  28.650  1.00 22.23           O  
HETATM 6081  O   HOH B 349     -31.758 -17.638  46.971  1.00 17.15           O  
HETATM 6082  O   HOH B 351      -7.709  -2.878  32.631  1.00 22.61           O  
HETATM 6083  O   HOH B 352      -4.500 -25.538  31.064  1.00 14.71           O  
HETATM 6084  O   HOH B 353      -3.712 -23.712  28.603  1.00 27.15           O  
HETATM 6085  O   HOH B 359     -21.723 -27.735  42.021  1.00 13.84           O  
HETATM 6086  O   HOH B 364     -38.977 -21.323  33.930  1.00 16.81           O  
HETATM 6087  O   HOH B 365     -13.549 -25.043  20.505  1.00 23.72           O  
HETATM 6088  O   HOH B 374     -13.239 -38.231  21.551  1.00 29.75           O  
HETATM 6089  O   HOH B 376     -17.914 -12.108  52.987  1.00 19.84           O  
HETATM 6090  O   HOH B 377     -14.382 -38.499  18.732  1.00 14.17           O  
HETATM 6091  O   HOH B 381     -10.734 -23.165  46.908  1.00 12.16           O  
HETATM 6092  O   HOH B 382     -33.285 -35.604  48.056  1.00 18.72           O  
HETATM 6093  O   HOH B 383     -27.293  -8.195  20.807  1.00 24.57           O  
HETATM 6094  O   HOH B 389     -14.774  -7.203  26.474  1.00 19.28           O  
HETATM 6095  O   HOH B 391     -12.797  -5.259  47.284  1.00 14.70           O  
HETATM 6096  O   HOH B 392     -20.011 -39.851  39.396  1.00 19.31           O  
HETATM 6097  O   HOH B 404     -33.952  -9.029  25.370  1.00 23.73           O  
HETATM 6098  O   HOH B 409     -37.210 -28.033  27.083  1.00 18.37           O  
HETATM 6099  O   HOH B 412     -20.113 -23.609  55.840  1.00 38.01           O  
HETATM 6100  O   HOH B 413     -15.573 -25.011  18.781  1.00 16.06           O  
HETATM 6101  O   HOH B 416     -32.525  -9.465  27.416  1.00 22.70           O  
HETATM 6102  O   HOH B 419     -30.747 -36.620  48.503  1.00 16.92           O  
HETATM 6103  O   HOH B 420     -16.857 -24.127  52.066  1.00 21.29           O  
HETATM 6104  O   HOH B 435     -14.574 -36.619  28.179  1.00 16.67           O  
HETATM 6105  O   HOH B 436      -6.953  -6.937  30.512  1.00 10.80           O  
HETATM 6106  O   HOH B 458       2.718 -18.027  44.778  1.00 24.53           O  
HETATM 6107  O   HOH B 461      -2.592 -17.593  37.506  1.00 20.63           O  
HETATM 6108  O   HOH B 464     -36.060 -27.044  48.841  1.00 22.89           O  
HETATM 6109  O   HOH B 471     -17.032  -8.710  24.076  1.00 20.18           O  
HETATM 6110  O   HOH B 476      -5.897 -27.558  37.248  1.00 22.56           O  
HETATM 6111  O   HOH B 477     -31.395 -11.665  43.497  1.00 17.80           O  
HETATM 6112  O   HOH B 481      -8.767 -26.563  38.173  1.00 27.35           O  
HETATM 6113  O   HOH B 493     -36.247 -15.189  25.950  1.00 16.40           O  
HETATM 6114  O   HOH B 499     -19.660 -30.390  54.902  1.00 23.45           O  
HETATM 6115  O   HOH B 506     -38.698 -23.673  32.708  1.00 14.76           O  
HETATM 6116  O   HOH B 521      -9.410 -15.267  50.540  1.00 21.78           O  
HETATM 6117  O   HOH B 524     -27.195  -7.618  42.265  1.00 33.97           O  
HETATM 6118  O   HOH B 530      -2.290 -20.906  38.908  1.00 13.00           O  
HETATM 6119  O   HOH B 532     -35.894 -26.267  36.136  1.00 16.73           O  
HETATM 6120  O   HOH B 538      -4.629  -5.008  35.790  1.00 19.35           O  
HETATM 6121  O   HOH B 542     -15.464 -36.978  43.623  1.00 54.04           O  
HETATM 6122  O   HOH B 544     -38.462 -27.612  35.465  1.00 29.58           O  
HETATM 6123  O   HOH B 548     -27.947 -10.062  44.743  1.00 21.09           O  
HETATM 6124  O   HOH B 552     -15.700 -23.455  48.565  1.00 26.87           O  
HETATM 6125  O   HOH B 558     -13.848 -29.384  20.393  1.00 18.76           O  
HETATM 6126  O   HOH B 568     -37.032 -26.709  24.914  1.00 21.01           O  
HETATM 6127  O   HOH B 577     -34.645 -35.675  29.788  1.00 10.31           O  
HETATM 6128  O   HOH B 578     -18.579 -27.244  46.655  1.00 16.61           O  
HETATM 6129  O   HOH B 586     -20.915 -11.996  51.507  1.00 22.58           O  
HETATM 6130  O   HOH B 589     -11.749 -23.350  19.204  1.00 17.84           O  
HETATM 6131  O   HOH B 594     -37.467 -27.917  46.901  1.00 38.41           O  
HETATM 6132  O   HOH B 598     -25.970 -27.756  23.810  1.00  6.80           O  
HETATM 6133  O   HOH B 599      -5.690 -23.849  26.651  1.00 22.50           O  
HETATM 6134  O   HOH B 601      -7.850 -21.603  47.917  1.00 17.29           O  
HETATM 6135  O   HOH B 605     -38.582 -17.046  23.972  1.00 22.69           O  
HETATM 6136  O   HOH B 607     -31.524 -14.078  39.289  1.00 17.40           O  
HETATM 6137  O   HOH B 617     -17.041 -26.351  42.582  1.00 13.57           O  
HETATM 6138  O   HOH B 623     -15.752 -14.864  54.789  1.00 16.68           O  
HETATM 6139  O   HOH B 624     -31.332 -14.247  43.134  1.00 22.54           O  
HETATM 6140  O   HOH B 631       2.851 -16.259  41.702  1.00 27.62           O  
HETATM 6141  O   HOH B 633     -10.054  -5.407  43.609  1.00 31.34           O  
HETATM 6142  O   HOH B 637     -30.822 -30.449  62.674  1.00 20.62           O  
HETATM 6143  O   HOH B 641     -26.451  -5.817  21.238  1.00 21.24           O  
HETATM 6144  O   HOH B 642     -16.553 -25.856  47.837  1.00 17.37           O  
HETATM 6145  O   HOH B 646     -27.867  -6.758  44.753  1.00 25.28           O  
HETATM 6146  O   HOH B 651     -27.134 -34.390  48.760  1.00 11.60           O  
HETATM 6147  O   HOH B 657      -6.071 -29.651  30.388  1.00 38.05           O  
HETATM 6148  O   HOH B 672     -24.821 -30.174  23.476  1.00  8.10           O  
HETATM 6149  O   HOH B 673      -2.799  -9.515  37.582  1.00 16.41           O  
HETATM 6150  O   HOH B 675      -8.911 -29.794  27.763  1.00 12.85           O  
HETATM 6151  O   HOH B 677      -2.218 -10.113  40.393  1.00 22.20           O  
HETATM 6152  O   HOH B 680     -12.450 -16.205  20.546  1.00 16.68           O  
HETATM 6153  O   HOH B 681      -7.385 -24.763  19.056  1.00 25.18           O  
HETATM 6154  O   HOH B 683      -8.287 -30.499  23.869  1.00 14.97           O  
HETATM 6155  O   HOH B 684     -10.134  -7.947  51.005  1.00 28.21           O  
HETATM 6156  O   HOH B 706     -18.979  -9.490  47.702  1.00 13.03           O  
HETATM 6157  O   HOH B 711     -38.177 -28.900  39.259  1.00 16.14           O  
HETATM 6158  O   HOH B 717       4.185 -13.287  47.114  1.00 20.34           O  
HETATM 6159  O   HOH B 718     -33.107 -10.186  35.477  1.00 30.76           O  
HETATM 6160  O   HOH B 723     -17.248 -16.878  16.538  1.00 16.70           O  
HETATM 6161  O   HOH B 725     -12.518 -14.419  53.955  1.00 15.04           O  
HETATM 6162  O   HOH B 727      -9.898 -33.448  24.319  1.00 30.94           O  
HETATM 6163  O   HOH B 729     -27.769 -10.728  48.262  1.00 13.08           O  
HETATM 6164  O   HOH B 741     -34.798 -25.992  23.250  1.00 21.24           O  
HETATM 6165  O   HOH B 752     -14.352 -17.739  21.367  1.00 25.83           O  
HETATM 6166  O   HOH B 754     -15.207 -31.773  20.989  1.00 22.78           O  
HETATM 6167  O   HOH B 757     -34.036 -20.478  45.748  1.00 21.23           O  
HETATM 6168  O   HOH B 761     -14.859 -19.734  17.543  1.00 29.51           O  
HETATM 6169  O   HOH B 762     -32.277 -12.531  34.386  1.00 23.97           O  
HETATM 6170  O   HOH B 764     -28.379 -32.107  57.615  1.00 16.95           O  
HETATM 6171  O   HOH B 773     -26.003 -32.875  24.265  1.00 19.29           O  
HETATM 6172  O   HOH B 774     -22.306 -38.413  40.494  1.00  8.97           O  
HETATM 6173  O   HOH B 782     -32.998  -6.438  31.793  1.00 27.36           O  
HETATM 6174  O   HOH B 791     -36.360 -20.618  19.231  1.00 29.09           O  
HETATM 6175  O   HOH B 795     -11.813 -14.039  21.822  1.00 20.13           O  
HETATM 6176  O   HOH B 807     -26.275 -31.660  21.859  1.00 22.44           O  
HETATM 6177  O   HOH B 812     -35.950 -19.446  22.196  1.00 22.70           O  
HETATM 6178  O   HOH B 827     -35.604 -23.755  21.547  1.00 33.40           O  
HETATM 6179  O   HOH B 834      -8.030  -6.403  26.976  1.00 22.23           O  
HETATM 6180  O   HOH B 840      -5.311 -11.045  26.075  1.00 26.22           O  
HETATM 6181  O   HOH B 841      -8.948 -29.436  37.084  1.00 27.51           O  
HETATM 6182  O   HOH B 842      -9.038  -8.658  22.022  1.00 29.83           O  
HETATM 6183  O   HOH B 846     -24.899  -7.933  45.529  1.00 26.91           O  
HETATM 6184  O   HOH B 848     -34.008 -29.277  25.126  1.00 16.90           O  
HETATM 6185  O   HOH B 854     -25.522  -5.373  45.575  1.00 37.95           O  
HETATM 6186  O   HOH B 865     -17.533 -17.187  54.544  1.00  7.92           O  
HETATM 6187  O   HOH B 871      -3.688 -11.589  34.110  1.00 17.43           O  
HETATM 6188  O   HOH B 877     -17.769  -8.644  19.944  1.00 13.50           O  
HETATM 6189  O   HOH B 879      -9.619  -1.267  36.859  1.00 19.99           O  
HETATM 6190  O   HOH B 883      -7.370  -8.940  24.407  1.00 38.67           O  
HETATM 6191  O   HOH B 891     -16.805  -6.759  47.401  1.00 24.56           O  
HETATM 6192  O   HOH B 894      -0.824  -7.214  35.539  1.00 30.37           O  
HETATM 6193  O   HOH B 909     -16.370 -24.449  44.145  1.00 11.26           O  
HETATM 6194  O   HOH B 911      -8.571 -11.975  49.293  1.00 13.04           O  
HETATM 6195  O   HOH B 913     -31.827 -15.502  45.546  1.00 25.41           O  
HETATM 6196  O   HOH B 941     -18.763 -30.337  43.859  1.00 20.58           O  
HETATM 6197  O   HOH B 962     -18.896 -37.229  22.463  1.00 25.27           O  
HETATM 6198  O   HOH B 968      -8.017 -35.011  44.591  1.00 22.90           O  
HETATM 6199  O   HOH B 974     -13.494 -35.324  44.475  1.00 27.96           O  
HETATM 6200  O   HOH B 975     -17.930 -39.231  37.461  1.00 25.78           O  
HETATM 6201  O   HOH B 989     -22.648 -32.977  48.046  1.00 21.08           O  
HETATM 6202  O   HOH B 990      -9.951 -24.357  41.559  1.00 26.88           O  
HETATM 6203  O   HOH B 991      -1.523 -19.107  44.034  1.00 31.08           O  
HETATM 6204  O   HOH B 997       1.460 -18.905  42.503  1.00 21.31           O  
HETATM 6205  O   HOH B 998     -32.821 -13.995  36.889  1.00  9.27           O  
HETATM 6206  O   HOH B1005      -6.113 -11.725  48.239  1.00 30.02           O  
HETATM 6207  O   HOH B1013     -27.133 -12.732  53.468  1.00 29.23           O  
HETATM 6208  O   HOH B1018     -19.622 -26.135  53.644  1.00 29.12           O  
HETATM 6209  O   HOH B1021       0.600 -10.526  35.259  1.00 24.23           O  
HETATM 6210  O   HOH B1023      -1.221  -4.694  33.853  1.00 21.16           O  
HETATM 6211  O   HOH B1035     -36.961 -20.730  30.301  1.00 12.63           O  
HETATM 6212  O   HOH B1044     -35.769 -16.561  19.533  1.00 20.40           O  
HETATM 6213  O   HOH B1045     -15.598 -33.285  42.888  1.00 20.66           O  
HETATM 6214  O   HOH B1050     -10.518  -5.673  49.554  1.00 35.31           O  
HETATM 6215  O   HOH B1054      -8.221 -21.864  20.960  1.00 26.97           O  
HETATM 6216  O   HOH B1062     -29.934 -33.905  50.767  1.00 16.08           O  
HETATM 6217  O   HOH B1075     -15.111 -40.813  39.553  1.00 25.73           O  
HETATM 6218  O   HOH B1080     -22.852 -23.762  59.559  1.00 19.54           O  
HETATM 6219  O   HOH B1088     -21.801 -38.825  23.697  1.00 25.97           O  
HETATM 6220  O   HOH B1095     -17.321 -40.985  41.485  1.00 29.54           O  
HETATM 6221  O   HOH B1098       0.558  -7.170  32.312  1.00 20.75           O  
HETATM 6222  O   HOH B1105     -28.732 -34.354  24.491  1.00 26.66           O  
HETATM 6223  O   HOH B1108      -8.966 -14.522  21.807  1.00 16.56           O  
HETATM 6224  O   HOH B1117     -22.645 -11.340  54.064  1.00 32.67           O  
HETATM 6225  O   HOH B1118      -5.895 -28.354  18.735  1.00 29.98           O  
HETATM 6226  O   HOH B1120      -5.230 -14.970  26.128  1.00 24.19           O  
HETATM 6227  O   HOH B1123     -27.602 -17.328  18.880  1.00 12.78           O  
HETATM 6228  O   HOH B1127     -28.362 -38.125  29.040  1.00 19.73           O  
HETATM 6229  O   HOH B1130     -34.252 -31.415  58.089  1.00 19.97           O  
HETATM 6230  O   HOH B1132     -23.655 -36.566  47.616  1.00 39.96           O  
HETATM 6231  O   HOH B1134     -36.985 -22.083  53.757  1.00 27.05           O  
HETATM 6232  O   HOH B1136     -35.625 -21.829  23.422  1.00 19.94           O  
HETATM 6233  O   HOH B1139      -1.021 -13.902  33.769  1.00 33.51           O  
HETATM 6234  O   HOH B1140      -1.604 -22.987  36.746  1.00 29.04           O  
HETATM 6235  O   HOH B1148     -37.465 -13.769  31.436  1.00 13.83           O  
HETATM 6236  O   HOH B1155     -34.091 -20.300  58.404  1.00 37.73           O  
HETATM 6237  O   HOH B1159      -6.385 -27.112  29.853  1.00 20.82           O  
HETATM 6238  O   HOH B1161     -33.778 -15.371  39.226  1.00 36.18           O  
HETATM 6239  O   HOH B1167     -35.273 -30.086  47.314  1.00 36.91           O  
HETATM 6240  O   HOH B1180     -20.558  -9.094  45.598  1.00 26.94           O  
HETATM 6241  O   HOH B1182     -19.406 -35.127  45.548  1.00 26.87           O  
HETATM 6242  O   HOH B1183     -27.905  -7.839  29.384  1.00 35.36           O  
HETATM 6243  O   HOH B1187       0.596 -13.220  39.532  1.00 29.10           O  
HETATM 6244  O   HOH B1192     -26.173  -7.719  24.856  1.00 25.30           O  
HETATM 6245  O   HOH B1195     -35.338 -18.069  56.083  1.00 25.25           O  
HETATM 6246  O   HOH B1207      -8.072 -15.371  24.141  1.00 16.18           O  
HETATM 6247  O   HOH B1219      -5.317  -9.900  46.438  1.00 43.67           O  
HETATM 6248  O   HOH B1222     -39.234 -24.152  44.125  1.00 31.98           O  
HETATM 6249  O   HOH B1227      -1.042 -12.719  47.597  1.00 21.45           O  
HETATM 6250  O   HOH B1234     -24.964  -9.623  51.584  1.00 35.87           O  
HETATM 6251  O   HOH B1235     -29.635 -36.368  27.484  1.00 33.71           O  
HETATM 6252  O   HOH B1241     -13.074  -7.873  19.134  1.00 21.00           O  
HETATM 6253  O   HOH B1267     -26.635 -10.918  15.681  1.00 29.19           O  
HETATM 6254  O   HOH B1275     -30.162  -5.271  34.931  1.00 27.70           O  
HETATM 6255  O   HOH B1291     -23.460 -39.014  26.019  1.00 28.12           O  
HETATM 6256  O   HOH B1293     -23.894 -11.554  15.347  1.00 22.42           O  
HETATM 6257  O   HOH B1298      -8.992 -34.279  33.739  1.00 21.67           O  
HETATM 6258  O   HOH B1307     -18.722 -33.749  43.088  1.00 22.15           O  
HETATM 6259  O   HOH B1308     -27.022 -35.090  27.187  1.00 20.46           O  
HETATM 6260  O   HOH B1309      -5.904  -3.764  39.719  1.00 19.01           O  
HETATM 6261  O   HOH B1312     -12.617 -19.386  20.139  1.00 16.15           O  
HETATM 6262  O   HOH B1324      -1.984  -9.719  35.215  1.00 36.26           O  
HETATM 6263  O   HOH B1329     -31.773  -6.891  27.537  1.00 23.24           O  
HETATM 6264  O   HOH B1331     -36.586 -14.219  22.435  1.00 36.15           O  
HETATM 6265  O   HOH B1332     -34.637 -35.219  26.725  1.00 18.85           O  
HETATM 6266  O   HOH B1335     -11.325 -12.800  19.413  1.00 35.34           O  
HETATM 6267  O   HOH B1342     -37.584 -31.626  44.807  1.00 30.84           O  
HETATM 6268  O   HOH B1343     -10.645 -32.921  20.112  1.00 29.92           O  
HETATM 6269  O   HOH B1367     -21.406 -14.817  55.522  1.00 17.79           O  
HETATM 6270  O   HOH B1372     -20.430 -34.920  24.292  1.00 13.73           O  
HETATM 6271  O   HOH B1373     -15.249  -7.141  20.675  1.00 38.97           O  
HETATM 6272  O   HOH B1381     -36.478 -11.493  30.664  1.00 14.84           O  
HETATM 6273  O   HOH B1393      -1.174 -15.967  50.556  1.00 28.98           O  
HETATM 6274  O   HOH B1396      -6.358 -12.567  24.159  1.00 42.62           O  
HETATM 6275  O   HOH B1407     -23.363 -29.073  21.650  1.00  9.06           O  
HETATM 6276  O   HOH B1410     -10.460  -4.704  46.078  1.00 23.58           O  
HETATM 6277  O   HOH B1421     -25.715 -35.855  41.564  1.00 12.12           O  
HETATM 6278  O   HOH B1431      -7.195  -2.515  43.519  1.00 21.61           O  
HETATM 6279  O   HOH B1432     -10.958  -2.924  43.944  1.00 24.85           O  
HETATM 6280  O   HOH B1442     -12.903 -11.229  21.159  1.00 15.36           O  
HETATM 6281  O   HOH B1464      -6.459 -34.224  39.900  1.00 37.03           O  
HETATM 6282  O   HOH B1470     -15.518 -22.129  45.816  1.00 19.94           O  
HETATM 6283  O   HOH C 184       1.460 -44.351  22.955  1.00  6.97           O  
HETATM 6284  O   HOH C 185      -0.721 -56.742  38.021  1.00  5.36           O  
HETATM 6285  O   HOH C 186       8.989 -54.799  49.858  1.00 11.04           O  
HETATM 6286  O   HOH C 187       0.969 -38.034  25.977  1.00 14.11           O  
HETATM 6287  O   HOH C 188     -13.671 -57.659  44.800  1.00  7.39           O  
HETATM 6288  O   HOH C 189       2.369 -40.937  31.494  1.00  2.00           O  
HETATM 6289  O   HOH C 190      -0.565 -35.802  30.504  1.00 11.26           O  
HETATM 6290  O   HOH C 191     -12.961 -68.631  37.520  1.00 18.41           O  
HETATM 6291  O   HOH C 192      10.810 -60.213  53.610  1.00 14.21           O  
HETATM 6292  O   HOH C 193      -6.789 -64.797  25.546  1.00 14.68           O  
HETATM 6293  O   HOH C 194      -3.389 -51.254  49.498  1.00  6.73           O  
HETATM 6294  O   HOH C 195      -0.503 -64.695  48.252  1.00  8.98           O  
HETATM 6295  O   HOH C 196       5.992 -50.312  45.386  1.00  8.44           O  
HETATM 6296  O   HOH C 197      -7.232 -37.220  37.358  1.00 12.75           O  
HETATM 6297  O   HOH C 198       6.317 -36.077  43.492  1.00 13.57           O  
HETATM 6298  O   HOH C 199       7.653 -53.184  45.538  1.00  4.11           O  
HETATM 6299  O   HOH C 200      -8.807 -54.494  38.106  1.00  7.16           O  
HETATM 6300  O   HOH C 201      13.530 -42.998  32.889  1.00  7.51           O  
HETATM 6301  O   HOH C 202       0.017 -42.007  30.955  1.00  7.75           O  
HETATM 6302  O   HOH C 203       8.289 -42.229  27.472  1.00  9.61           O  
HETATM 6303  O   HOH C 204     -13.320 -60.685  35.387  1.00  2.36           O  
HETATM 6304  O   HOH C 205       3.941 -50.698  20.831  1.00 12.94           O  
HETATM 6305  O   HOH C 206       8.256 -55.700  19.698  1.00  4.98           O  
HETATM 6306  O   HOH C 207      -1.240 -66.129  37.184  1.00 14.13           O  
HETATM 6307  O   HOH C 208     -10.003 -51.263  26.369  1.00 16.63           O  
HETATM 6308  O   HOH C 209       3.774 -40.800  33.742  1.00  6.36           O  
HETATM 6309  O   HOH C 210      -2.449 -47.563  43.723  1.00 13.64           O  
HETATM 6310  O   HOH C 211      -1.371 -57.053  52.546  1.00 11.45           O  
HETATM 6311  O   HOH C 212       4.687 -43.956  48.915  1.00  9.70           O  
HETATM 6312  O   HOH C 213       1.670 -55.071  43.641  1.00  7.38           O  
HETATM 6313  O   HOH C 214       3.227 -60.235  51.434  1.00 10.69           O  
HETATM 6314  O   HOH C 215      -2.325 -65.195  27.269  1.00  8.03           O  
HETATM 6315  O   HOH C 216      -4.097 -47.858  41.721  1.00 14.35           O  
HETATM 6316  O   HOH C 217       6.038 -68.356  40.497  1.00 21.81           O  
HETATM 6317  O   HOH C 218       8.184 -63.933  48.337  1.00 10.41           O  
HETATM 6318  O   HOH C 219      -4.188 -36.549  30.211  1.00 11.15           O  
HETATM 6319  O   HOH C 220       0.698 -57.862  56.569  1.00 11.28           O  
HETATM 6320  O   HOH C 221       3.323 -48.648  45.918  1.00  6.20           O  
HETATM 6321  O   HOH C 222      -0.506 -40.755  44.897  1.00 23.20           O  
HETATM 6322  O   HOH C 223      13.146 -63.793  27.762  1.00 15.36           O  
HETATM 6323  O   HOH C 224     -13.981 -63.769  36.884  1.00 21.93           O  
HETATM 6324  O   HOH C 225      -4.148 -63.995  50.398  1.00 32.53           O  
HETATM 6325  O   HOH C 226       8.010 -62.256  51.192  1.00 11.69           O  
HETATM 6326  O   HOH C 227      16.597 -53.879  37.856  1.00 13.10           O  
HETATM 6327  O   HOH C 228       1.219 -43.851  42.795  1.00  7.23           O  
HETATM 6328  O   HOH C 229       1.272 -48.874  49.367  1.00  6.80           O  
HETATM 6329  O   HOH C 230       2.600 -46.291  43.415  1.00 10.73           O  
HETATM 6330  O   HOH C 231      18.921 -49.775  33.453  1.00 19.49           O  
HETATM 6331  O   HOH C 232      -5.089 -54.731  22.157  1.00 12.88           O  
HETATM 6332  O   HOH C 233      12.939 -56.581  47.255  1.00 13.34           O  
HETATM 6333  O   HOH C 234       5.942 -63.904  45.565  1.00 15.71           O  
HETATM 6334  O   HOH C 235       2.918 -36.924  43.759  1.00 13.03           O  
HETATM 6335  O   HOH C 236       0.071 -34.082  38.031  1.00  2.00           O  
HETATM 6336  O   HOH C 237      -2.489 -55.652  20.753  1.00 15.42           O  
HETATM 6337  O   HOH C 238       3.187 -45.842  48.019  1.00 18.06           O  
HETATM 6338  O   HOH C 239       0.609 -47.805  45.766  1.00 14.60           O  
HETATM 6339  O   HOH C 240      13.764 -40.636  31.891  1.00 16.63           O  
HETATM 6340  O   HOH C 241      -0.100 -46.465  18.982  1.00 25.57           O  
HETATM 6341  O   HOH C 242     -11.066 -70.157  35.837  1.00 15.80           O  
HETATM 6342  O   HOH C 256      -1.939 -57.609  55.345  1.00  6.66           O  
HETATM 6343  O   HOH C 260      -7.923 -38.233  24.884  1.00 21.69           O  
HETATM 6344  O   HOH C 262     -11.401 -66.557  28.166  1.00 30.34           O  
HETATM 6345  O   HOH C 263      15.713 -43.295  46.817  1.00 20.18           O  
HETATM 6346  O   HOH C 264       5.335 -60.248  56.758  1.00 11.26           O  
HETATM 6347  O   HOH C 267       1.618 -47.002  21.869  1.00 17.21           O  
HETATM 6348  O   HOH C 278     -10.494 -48.791  27.794  1.00 16.92           O  
HETATM 6349  O   HOH C 288     -21.529 -63.007  47.578  1.00 21.11           O  
HETATM 6350  O   HOH C 295      -0.338 -43.361  45.463  1.00 25.42           O  
HETATM 6351  O   HOH C 302      13.203 -55.570  19.612  1.00 32.40           O  
HETATM 6352  O   HOH C 307      18.884 -45.056  40.209  1.00 10.15           O  
HETATM 6353  O   HOH C 311      -9.782 -46.681  26.235  1.00  8.70           O  
HETATM 6354  O   HOH C 314      -9.330 -51.111  45.811  1.00 19.15           O  
HETATM 6355  O   HOH C 316      -7.925 -72.449  40.862  1.00 22.90           O  
HETATM 6356  O   HOH C 321      13.287 -64.557  20.839  1.00 37.26           O  
HETATM 6357  O   HOH C 322      -0.732 -44.160  56.491  1.00 19.92           O  
HETATM 6358  O   HOH C 324      10.365 -61.822  41.937  1.00 18.08           O  
HETATM 6359  O   HOH C 335       3.658 -47.539  59.247  1.00 13.72           O  
HETATM 6360  O   HOH C 350      -7.285 -35.726  25.575  1.00 36.87           O  
HETATM 6361  O   HOH C 355      -0.327 -57.893  14.532  1.00 32.51           O  
HETATM 6362  O   HOH C 356       0.772 -64.929  50.568  1.00  8.70           O  
HETATM 6363  O   HOH C 360      -3.855 -31.459  34.212  1.00 15.92           O  
HETATM 6364  O   HOH C 371       0.418 -37.259  44.132  1.00 23.41           O  
HETATM 6365  O   HOH C 373      -5.554 -43.386  22.074  1.00 15.13           O  
HETATM 6366  O   HOH C 380       7.963 -66.292  42.545  1.00 21.53           O  
HETATM 6367  O   HOH C 385      -1.687 -68.872  50.836  1.00 28.46           O  
HETATM 6368  O   HOH C 387       7.605 -50.784  59.677  1.00 11.73           O  
HETATM 6369  O   HOH C 388      -5.162 -57.892  18.952  1.00 25.10           O  
HETATM 6370  O   HOH C 394      13.845 -63.856  34.715  1.00 18.11           O  
HETATM 6371  O   HOH C 396      21.013 -41.713  35.248  1.00 26.64           O  
HETATM 6372  O   HOH C 397      17.542 -45.851  27.932  1.00 18.06           O  
HETATM 6373  O   HOH C 402     -12.945 -55.631  25.902  1.00 14.95           O  
HETATM 6374  O   HOH C 405      -1.427 -71.558  38.180  1.00 15.52           O  
HETATM 6375  O   HOH C 414      -0.893 -67.600  27.082  1.00 12.11           O  
HETATM 6376  O   HOH C 422     -18.386 -60.603  49.065  1.00 12.10           O  
HETATM 6377  O   HOH C 424       7.482 -40.065  50.627  1.00 25.23           O  
HETATM 6378  O   HOH C 425       1.758 -60.035  55.567  1.00 20.94           O  
HETATM 6379  O   HOH C 431       0.432 -71.214  29.372  1.00 15.04           O  
HETATM 6380  O   HOH C 432      -7.170 -49.156  20.826  1.00 34.18           O  
HETATM 6381  O   HOH C 449      17.080 -56.028  20.800  1.00 29.78           O  
HETATM 6382  O   HOH C 450      16.570 -47.780  37.219  1.00 18.07           O  
HETATM 6383  O   HOH C 455      -2.158 -33.356  39.339  1.00 14.74           O  
HETATM 6384  O   HOH C 462     -13.155 -49.962  27.653  1.00 31.28           O  
HETATM 6385  O   HOH C 463      -2.218 -45.395  17.705  1.00 25.03           O  
HETATM 6386  O   HOH C 482      -6.956 -68.697  47.534  1.00 25.25           O  
HETATM 6387  O   HOH C 485      16.036 -58.952  25.182  1.00 19.68           O  
HETATM 6388  O   HOH C 489      -3.596 -48.285  19.375  1.00 31.18           O  
HETATM 6389  O   HOH C 494      17.528 -58.073  22.494  1.00 32.72           O  
HETATM 6390  O   HOH C 500       8.087 -65.716  38.947  1.00 21.45           O  
HETATM 6391  O   HOH C 502       7.175 -62.712  24.207  1.00 20.62           O  
HETATM 6392  O   HOH C 503      -2.792 -45.363  45.362  1.00 23.44           O  
HETATM 6393  O   HOH C 504      20.628 -45.775  33.615  1.00 17.94           O  
HETATM 6394  O   HOH C 513      -2.776 -69.631  15.750  1.00 34.10           O  
HETATM 6395  O   HOH C 520      12.365 -59.057  46.375  1.00 17.16           O  
HETATM 6396  O   HOH C 523      16.664 -51.138  41.718  1.00 30.42           O  
HETATM 6397  O   HOH C 543      -4.721 -32.138  36.655  1.00 23.56           O  
HETATM 6398  O   HOH C 547     -14.633 -44.313  37.582  1.00 33.52           O  
HETATM 6399  O   HOH C 550     -16.453 -51.523  31.256  1.00 19.68           O  
HETATM 6400  O   HOH C 551      -1.181 -68.642  24.627  1.00 26.35           O  
HETATM 6401  O   HOH C 556       5.783 -53.670  18.791  1.00 19.62           O  
HETATM 6402  O   HOH C 561       1.490 -62.674  51.891  1.00 13.84           O  
HETATM 6403  O   HOH C 564      -6.712 -56.480  21.032  1.00  9.41           O  
HETATM 6404  O   HOH C 565      -2.228 -64.294  24.368  1.00 16.50           O  
HETATM 6405  O   HOH C 570       0.019 -69.074  38.216  1.00 13.53           O  
HETATM 6406  O   HOH C 572       3.899 -60.221  53.915  1.00 27.77           O  
HETATM 6407  O   HOH C 588     -15.760 -62.890  45.410  1.00 17.49           O  
HETATM 6408  O   HOH C 591     -10.920 -38.548  38.961  1.00 30.53           O  
HETATM 6409  O   HOH C 593      17.855 -48.844  49.891  1.00 29.74           O  
HETATM 6410  O   HOH C 603     -16.619 -52.334  35.058  1.00 21.99           O  
HETATM 6411  O   HOH C 608     -14.722 -51.934  26.358  1.00 35.04           O  
HETATM 6412  O   HOH C 610      -9.080 -69.139  45.880  1.00 17.31           O  
HETATM 6413  O   HOH C 613       6.885 -65.401  24.818  1.00 19.06           O  
HETATM 6414  O   HOH C 614      -7.835 -72.594  37.877  1.00 23.96           O  
HETATM 6415  O   HOH C 616       8.970 -50.867  61.872  1.00  8.20           O  
HETATM 6416  O   HOH C 618      14.306 -58.621  41.552  1.00 27.84           O  
HETATM 6417  O   HOH C 621      -1.574 -35.920  27.342  1.00 10.91           O  
HETATM 6418  O   HOH C 625      16.947 -49.127  39.815  1.00 21.03           O  
HETATM 6419  O   HOH C 627      19.188 -46.967  36.683  1.00 15.59           O  
HETATM 6420  O   HOH C 640      -1.559 -32.151  27.736  1.00 19.33           O  
HETATM 6421  O   HOH C 648     -15.766 -62.132  49.838  1.00 26.22           O  
HETATM 6422  O   HOH C 656      10.463 -71.699  23.751  1.00 24.02           O  
HETATM 6423  O   HOH C 663      12.782 -66.695  29.037  1.00 27.83           O  
HETATM 6424  O   HOH C 665      16.904 -61.693  26.423  1.00 19.52           O  
HETATM 6425  O   HOH C 674      12.004 -69.396  29.513  1.00 24.18           O  
HETATM 6426  O   HOH C 678      -1.873 -31.703  30.369  1.00 16.18           O  
HETATM 6427  O   HOH C 687      -1.343 -30.199  24.248  1.00 22.74           O  
HETATM 6428  O   HOH C 688      -5.022 -34.112  30.695  1.00 20.02           O  
HETATM 6429  O   HOH C 691     -17.939 -55.878  47.006  1.00 11.14           O  
HETATM 6430  O   HOH C 700      -8.514 -68.176  32.566  1.00 20.65           O  
HETATM 6431  O   HOH C 701      16.565 -41.144  32.481  1.00 29.02           O  
HETATM 6432  O   HOH C 705     -19.918 -60.629  34.858  1.00 17.17           O  
HETATM 6433  O   HOH C 707      -6.553 -61.358  21.653  1.00 12.35           O  
HETATM 6434  O   HOH C 708       3.544 -51.376  60.213  1.00 14.50           O  
HETATM 6435  O   HOH C 709     -10.719 -62.234  49.967  1.00 16.16           O  
HETATM 6436  O   HOH C 710       2.863 -46.727  56.710  1.00 10.20           O  
HETATM 6437  O   HOH C 713      -5.306 -62.150  18.530  1.00 13.91           O  
HETATM 6438  O   HOH C 714     -13.641 -70.295  39.444  1.00 16.66           O  
HETATM 6439  O   HOH C 715     -10.939 -68.436  31.884  1.00 15.40           O  
HETATM 6440  O   HOH C 730      14.272 -57.461  49.520  1.00 20.79           O  
HETATM 6441  O   HOH C 732      14.553 -55.259  46.028  1.00 16.05           O  
HETATM 6442  O   HOH C 733     -15.387 -60.022  29.897  1.00 34.99           O  
HETATM 6443  O   HOH C 739       6.864 -61.874  18.053  1.00 20.83           O  
HETATM 6444  O   HOH C 747      15.941 -62.916  32.466  1.00 23.14           O  
HETATM 6445  O   HOH C 755       8.845 -43.746  56.325  1.00 21.79           O  
HETATM 6446  O   HOH C 758      10.187 -65.999  33.579  1.00 19.94           O  
HETATM 6447  O   HOH C 770      -3.398 -67.579  47.464  1.00 21.39           O  
HETATM 6448  O   HOH C 775      -6.956 -45.629  23.272  1.00 19.07           O  
HETATM 6449  O   HOH C 781      19.208 -42.118  32.019  1.00 16.74           O  
HETATM 6450  O   HOH C 787      19.921 -44.331  30.976  1.00 22.83           O  
HETATM 6451  O   HOH C 790     -10.100 -43.065  29.163  1.00 21.85           O  
HETATM 6452  O   HOH C 797      -8.149 -49.154  40.663  1.00 18.75           O  
HETATM 6453  O   HOH C 799      14.796 -52.880  42.663  1.00 24.83           O  
HETATM 6454  O   HOH C 801     -16.770 -55.465  38.563  1.00 27.39           O  
HETATM 6455  O   HOH C 802     -22.393 -58.203  44.122  1.00 25.50           O  
HETATM 6456  O   HOH C 814      -9.347 -38.056  36.159  1.00 12.50           O  
HETATM 6457  O   HOH C 817      12.325 -59.693  40.126  1.00 11.03           O  
HETATM 6458  O   HOH C 819      14.024 -40.555  47.286  1.00 22.05           O  
HETATM 6459  O   HOH C 822      -8.953 -66.569  25.671  1.00 20.08           O  
HETATM 6460  O   HOH C 823     -17.316 -62.919  40.410  1.00 22.74           O  
HETATM 6461  O   HOH C 828       6.704 -65.466  27.454  1.00 30.65           O  
HETATM 6462  O   HOH C 830       6.467 -71.668  29.566  1.00 24.78           O  
HETATM 6463  O   HOH C 836      16.500 -44.110  26.213  1.00 22.39           O  
HETATM 6464  O   HOH C 838      13.163 -49.062  62.889  1.00 13.63           O  
HETATM 6465  O   HOH C 845      10.737 -63.060  50.361  1.00 25.46           O  
HETATM 6466  O   HOH C 852       7.179 -51.418  19.273  1.00 24.97           O  
HETATM 6467  O   HOH C 857     -14.581 -62.397  26.404  1.00 27.55           O  
HETATM 6468  O   HOH C 860      -7.637 -58.379  22.478  1.00 20.62           O  
HETATM 6469  O   HOH C 864     -11.646 -52.554  49.150  1.00  7.65           O  
HETATM 6470  O   HOH C 875      13.239 -38.763  49.341  1.00 22.28           O  
HETATM 6471  O   HOH C 878      -8.610 -51.060  48.244  1.00  6.09           O  
HETATM 6472  O   HOH C 887       5.719 -61.956  54.684  1.00 26.58           O  
HETATM 6473  O   HOH C 896     -16.723 -64.065  37.249  1.00 25.07           O  
HETATM 6474  O   HOH C 901     -11.106 -44.643  27.413  1.00 22.67           O  
HETATM 6475  O   HOH C 905      -2.563 -32.872  25.401  1.00 24.48           O  
HETATM 6476  O   HOH C 921       3.649 -41.580  49.505  1.00 16.41           O  
HETATM 6477  O   HOH C 927     -13.353 -41.550  23.793  1.00 16.78           O  
HETATM 6478  O   HOH C 928     -17.238 -63.779  30.760  1.00 19.66           O  
HETATM 6479  O   HOH C 929     -19.286 -64.802  37.416  1.00 32.89           O  
HETATM 6480  O   HOH C 932      -7.216 -51.721  21.458  1.00 17.67           O  
HETATM 6481  O   HOH C 933      -7.603 -34.285  31.163  1.00 16.88           O  
HETATM 6482  O   HOH C 951      -2.993 -70.814  45.432  1.00 31.54           O  
HETATM 6483  O   HOH C 952       2.004 -44.173  56.698  1.00 27.12           O  
HETATM 6484  O   HOH C 953     -11.337 -57.589  24.651  1.00 13.45           O  
HETATM 6485  O   HOH C 957       5.291 -49.607  60.265  1.00  9.38           O  
HETATM 6486  O   HOH C 964       4.700 -66.490  46.209  1.00 35.52           O  
HETATM 6487  O   HOH C 965       7.315 -62.743  58.065  1.00 17.02           O  
HETATM 6488  O   HOH C 978      16.434 -53.158  63.287  1.00 23.06           O  
HETATM 6489  O   HOH C 980       5.675 -49.660  62.834  1.00 23.53           O  
HETATM 6490  O   HOH C 983     -12.068 -51.017  43.419  1.00 22.17           O  
HETATM 6491  O   HOH C 986     -15.451 -66.894  28.127  1.00 32.65           O  
HETATM 6492  O   HOH C 999       0.539 -45.087  47.868  1.00 16.21           O  
HETATM 6493  O   HOH C1003       9.423 -42.772  59.001  1.00 34.25           O  
HETATM 6494  O   HOH C1007     -10.024 -42.820  37.999  1.00 29.09           O  
HETATM 6495  O   HOH C1010      10.751 -40.990  52.142  1.00 14.83           O  
HETATM 6496  O   HOH C1012     -17.577 -67.747  31.369  1.00 31.19           O  
HETATM 6497  O   HOH C1025      -7.803 -68.814  30.045  1.00 18.43           O  
HETATM 6498  O   HOH C1026       7.098 -40.726  23.384  1.00 25.28           O  
HETATM 6499  O   HOH C1027       5.437 -42.715  25.165  1.00 16.98           O  
HETATM 6500  O   HOH C1028       3.563 -51.313  15.715  1.00 39.19           O  
HETATM 6501  O   HOH C1029      -0.134 -46.457  43.505  1.00 25.29           O  
HETATM 6502  O   HOH C1040      -3.164 -59.809  55.568  1.00 22.23           O  
HETATM 6503  O   HOH C1047       6.399 -45.281  25.224  1.00 13.57           O  
HETATM 6504  O   HOH C1049       8.753 -65.224  28.978  1.00 38.46           O  
HETATM 6505  O   HOH C1051      11.740 -62.382  57.676  1.00 22.33           O  
HETATM 6506  O   HOH C1059     -16.162 -68.859  44.370  1.00 15.80           O  
HETATM 6507  O   HOH C1060     -12.127 -43.486  41.023  1.00 38.64           O  
HETATM 6508  O   HOH C1061      14.987 -63.324  25.613  1.00 27.93           O  
HETATM 6509  O   HOH C1066      -1.257 -64.125  55.080  1.00 38.34           O  
HETATM 6510  O   HOH C1072       1.230 -50.575  14.560  1.00 20.97           O  
HETATM 6511  O   HOH C1076      -8.866 -42.940  44.030  1.00 27.26           O  
HETATM 6512  O   HOH C1077       3.927 -71.865  26.729  1.00 16.91           O  
HETATM 6513  O   HOH C1086     -16.159 -66.474  47.221  1.00 16.70           O  
HETATM 6514  O   HOH C1109      -5.471 -30.859  19.674  1.00 36.37           O  
HETATM 6515  O   HOH C1110       8.031 -52.766  15.174  1.00 45.67           O  
HETATM 6516  O   HOH C1115      -4.709 -65.772  26.313  1.00 18.87           O  
HETATM 6517  O   HOH C1116     -22.059 -66.056  47.255  1.00 18.76           O  
HETATM 6518  O   HOH C1121     -23.325 -59.925  37.392  1.00 16.39           O  
HETATM 6519  O   HOH C1122      17.991 -59.756  32.122  1.00  9.23