CNRS Nantes University UFIP UFIP
home |  start a new run |  job status |  references&downloads |  examples |  help  

Should you encounter any unexpected behaviour,
please let us know.


***  aaasert  ***

elNémo ID: 21062508481244774

Job options:

ID        	=	 21062508481244774
JOBID     	=	 aaasert
USERID    	=	 aaasert
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 aaasert

HEADER    PROTEIN BINDING                         10-FEB-17   5N48              
TITLE     STRUCTURE OF ANTICALIN N9B IN COMPLEX WITH EXTRA-DOMAIN B OF HUMAN    
TITLE    2 ONCOFETAL FIBRONECTIN                                                
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: NEUTROPHIL GELATINASE-ASSOCIATED LIPOCALIN;                
COMPND   3 CHAIN: A, C;                                                         
COMPND   4 SYNONYM: NGAL,25 KDA ALPHA-2-MICROGLOBULIN-RELATED SUBUNIT OF MMP-9, 
COMPND   5 LIPOCALIN-2,ONCOGENE 24P3,SIDEROCALIN LCN2,P25;                      
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MUTATION: YES;                                                       
COMPND   8 MOL_ID: 2;                                                           
COMPND   9 MOLECULE: FIBRONECTIN;                                               
COMPND  10 CHAIN: B, D;                                                         
COMPND  11 SYNONYM: FN,COLD-INSOLUBLE GLOBULIN,CIG;                             
COMPND  12 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: LCN2, HNL, NGAL;                                               
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: TG1;                                       
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PNGAL98-N9B;                              
SOURCE  11 MOL_ID: 2;                                                           
SOURCE  12 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  13 ORGANISM_COMMON: HUMAN;                                              
SOURCE  14 ORGANISM_TAXID: 9606;                                                
SOURCE  15 GENE: FN1, FN;                                                       
SOURCE  16 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  17 EXPRESSION_SYSTEM_TAXID: 511693;                                     
SOURCE  18 EXPRESSION_SYSTEM_STRAIN: BL21;                                      
SOURCE  19 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  20 EXPRESSION_SYSTEM_PLASMID: PASK35(+)-EDB                             
KEYWDS    LIPOCALIN, ANTICALIN, LIPOCALIN-BASED BINDING PROTEIN, PROTEIN        
KEYWDS   2 BINDING, HUMAN FIBRONECTIN, ONCOFETAL SPLICE VARIANT, FN TYPE III    
KEYWDS   3 DOMAIN, EXTRA-DOMAIN B, EIIIB, ED-B, EXTRACELLULAR MATRIX            
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    A.SCHIEFNER,A.SKERRA                                                  
REVDAT   3   11-APR-18 5N48    1       JRNL                                     
REVDAT   2   21-MAR-18 5N48    1       JRNL                                     
REVDAT   1   14-FEB-18 5N48    0                                                
JRNL        AUTH   A.SCHIEFNER,M.GEBAUER,A.RICHTER,A.SKERRA                     
JRNL        TITL   ANTICALINS REVEAL HIGH PLASTICITY IN THE MODE OF COMPLEX     
JRNL        TITL 2 FORMATION WITH A COMMON TUMOR ANTIGEN.                       
JRNL        REF    STRUCTURE                     V.  26   649 2018              
JRNL        REFN                   ISSN 1878-4186                               
JRNL        PMID   29526433                                                     
JRNL        DOI    10.1016/J.STR.2018.02.003                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.60 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.8.0155                                      
REMARK   3   AUTHORS     : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,              
REMARK   3               : NICHOLLS,WINN,LONG,VAGIN                             
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : NULL                                          
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.60                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 28.47                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.4                           
REMARK   3   NUMBER OF REFLECTIONS             : 67277                          
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) : 0.171                           
REMARK   3   R VALUE            (WORKING SET) : 0.169                           
REMARK   3   FREE R VALUE                     : 0.208                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 3545                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 1.60                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.64                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 4769                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 96.25                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2130                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 240                          
REMARK   3   BIN FREE R VALUE                    : 0.2720                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 4217                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 0                                       
REMARK   3   SOLVENT ATOMS            : 296                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 25.45                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 22.80                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -10.75000                                            
REMARK   3    B22 (A**2) : 27.05000                                             
REMARK   3    B33 (A**2) : -16.31000                                            
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 1.05000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.018         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.019         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.044         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.449         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.962                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.942                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  4321 ; 0.019 ; 0.019       
REMARK   3   BOND LENGTHS OTHERS               (A):  4097 ; 0.002 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  5873 ; 1.918 ; 1.958       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  9459 ; 1.136 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   530 ; 7.508 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   190 ;36.343 ;24.421       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   721 ;16.063 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    20 ;14.642 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   666 ; 0.117 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  4828 ; 0.011 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):   972 ; 0.003 ; 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):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TWIN DETAILS                                                        
REMARK   3   NUMBER OF TWIN DOMAINS  : 2                                        
REMARK   3      TWIN DOMAIN   : 1                                               
REMARK   3      TWIN OPERATOR : H, K, L                                         
REMARK   3      TWIN FRACTION : 0.510                                           
REMARK   3      TWIN DOMAIN   : 2                                               
REMARK   3      TWIN OPERATOR : H,-K,-L                                         
REMARK   3      TWIN FRACTION : 0.490                                           
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     3        A   177                          
REMARK   3    ORIGIN FOR THE GROUP (A):  53.5829   4.5418  37.1738              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1642 T22:   0.0022                                     
REMARK   3      T33:   0.1455 T12:   0.0068                                     
REMARK   3      T13:   0.0014 T23:  -0.0081                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.4069 L22:   0.0953                                     
REMARK   3      L33:   0.4289 L12:  -0.0116                                     
REMARK   3      L13:   0.1581 L23:  -0.1886                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0208 S12:   0.0051 S13:  -0.0092                       
REMARK   3      S21:  -0.0015 S22:   0.0048 S23:   0.0187                       
REMARK   3      S31:   0.0175 S32:  -0.0039 S33:  -0.0256                       
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  1266        B  1357                          
REMARK   3    ORIGIN FOR THE GROUP (A):  70.0174   1.4894  54.6294              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1405 T22:   0.0422                                     
REMARK   3      T33:   0.1123 T12:  -0.0150                                     
REMARK   3      T13:   0.0136 T23:  -0.0116                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.8966 L22:   0.3445                                     
REMARK   3      L33:   1.5876 L12:  -0.0423                                     
REMARK   3      L13:  -0.2122 L23:  -0.7138                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0917 S12:  -0.0929 S13:   0.0243                       
REMARK   3      S21:  -0.0494 S22:  -0.0635 S23:   0.0216                       
REMARK   3      S31:   0.0616 S32:   0.1662 S33:  -0.0282                       
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     4        C   177                          
REMARK   3    ORIGIN FOR THE GROUP (A):  41.0993   2.0944  -1.3041              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1461 T22:   0.0259                                     
REMARK   3      T33:   0.1211 T12:   0.0085                                     
REMARK   3      T13:   0.0180 T23:   0.0014                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.3444 L22:   0.0403                                     
REMARK   3      L33:   0.9903 L12:   0.0142                                     
REMARK   3      L13:  -0.1851 L23:   0.1641                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0159 S12:   0.0192 S13:   0.0102                       
REMARK   3      S21:   0.0104 S22:   0.0076 S23:  -0.0187                       
REMARK   3      S31:  -0.0027 S32:  -0.0309 S33:  -0.0236                       
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  1265        D  1357                          
REMARK   3    ORIGIN FOR THE GROUP (A):  24.5501   5.4235  16.3733              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1299 T22:   0.0824                                     
REMARK   3      T33:   0.0886 T12:  -0.0072                                     
REMARK   3      T13:   0.0185 T23:  -0.0015                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.7770 L22:   0.2582                                     
REMARK   3      L33:   1.5504 L12:  -0.0636                                     
REMARK   3      L13:   0.0474 L23:   0.6169                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1177 S12:   0.0049 S13:  -0.0029                       
REMARK   3      S21:  -0.0045 S22:  -0.0731 S23:  -0.0319                       
REMARK   3      S31:   0.0121 S32:  -0.2089 S33:  -0.0446                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : NULL                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS U VALUES : WITH TLS ADDED                                 
REMARK   4                                                                      
REMARK   4 5N48 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 10-FEB-17.                  
REMARK 100 THE DEPOSITION ID IS D_1200003266.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 07-DEC-11                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : BESSY                              
REMARK 200  BEAMLINE                       : 14.2                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.91741                            
REMARK 200  MONOCHROMATOR                  : SI111                              
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARMOSAIC 225 MM CCD               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XSCALE                             
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 70827                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.600                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 28.470                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.7                               
REMARK 200  DATA REDUNDANCY                : 4.180                              
REMARK 200  R MERGE                    (I) : 0.05700                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 14.8500                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.60                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.70                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.8                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.17                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.42300                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : 3.330                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: 4GH7                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 40.57                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.07                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 29 % (W/V) PEG4000, 0.1 M NA-MALONATE,   
REMARK 280  PH 6.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 298K             
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y+1/2,-Z                                             
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000       33.90050            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 2100 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 13330 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -7.0 KCAL/MOL                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 2130 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 13260 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -6.0 KCAL/MOL                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     GLN A     1                                                      
REMARK 465     ASP A     2                                                      
REMARK 465     GLY A   178                                                      
REMARK 465     SER A   179                                                      
REMARK 465     ALA A   180                                                      
REMARK 465     TRP A   181                                                      
REMARK 465     SER A   182                                                      
REMARK 465     HIS A   183                                                      
REMARK 465     PRO A   184                                                      
REMARK 465     GLN A   185                                                      
REMARK 465     PHE A   186                                                      
REMARK 465     GLU A   187                                                      
REMARK 465     LYS A   188                                                      
REMARK 465     MET B  1252                                                      
REMARK 465     ALA B  1253                                                      
REMARK 465     SER B  1254                                                      
REMARK 465     ARG B  1255                                                      
REMARK 465     GLY B  1256                                                      
REMARK 465     SER B  1257                                                      
REMARK 465     HIS B  1258                                                      
REMARK 465     HIS B  1259                                                      
REMARK 465     HIS B  1260                                                      
REMARK 465     HIS B  1261                                                      
REMARK 465     HIS B  1262                                                      
REMARK 465     HIS B  1263                                                      
REMARK 465     GLY B  1264                                                      
REMARK 465     ALA B  1265                                                      
REMARK 465     GLN C     1                                                      
REMARK 465     ASP C     2                                                      
REMARK 465     SER C     3                                                      
REMARK 465     GLY C   178                                                      
REMARK 465     SER C   179                                                      
REMARK 465     ALA C   180                                                      
REMARK 465     TRP C   181                                                      
REMARK 465     SER C   182                                                      
REMARK 465     HIS C   183                                                      
REMARK 465     PRO C   184                                                      
REMARK 465     GLN C   185                                                      
REMARK 465     PHE C   186                                                      
REMARK 465     GLU C   187                                                      
REMARK 465     LYS C   188                                                      
REMARK 465     MET D  1252                                                      
REMARK 465     ALA D  1253                                                      
REMARK 465     SER D  1254                                                      
REMARK 465     ARG D  1255                                                      
REMARK 465     GLY D  1256                                                      
REMARK 465     SER D  1257                                                      
REMARK 465     HIS D  1258                                                      
REMARK 465     HIS D  1259                                                      
REMARK 465     HIS D  1260                                                      
REMARK 465     HIS D  1261                                                      
REMARK 465     HIS D  1262                                                      
REMARK 465     HIS D  1263                                                      
REMARK 465     GLY D  1264                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    TRP A  31   CG    TRP A  31   CD1     0.086                       
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    ARG B1299   NE  -  CZ  -  NH1 ANGL. DEV. =   3.7 DEGREES          
REMARK 500    ARG B1299   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.1 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ASP A  47       66.25   -157.80                                   
REMARK 500    LYS A  62        7.60     84.25                                   
REMARK 500    ARG A  73       55.60     37.15                                   
REMARK 500    TYR A 115      -40.67     71.04                                   
REMARK 500    GLN A 117      -59.65   -128.44                                   
REMARK 500    GLN A 128     -105.11     54.17                                   
REMARK 500    THR A 145      144.95    -38.35                                   
REMARK 500    CYS A 175       -6.97     78.39                                   
REMARK 500    ASP B1272       34.25   -142.45                                   
REMARK 500    ASP C  45       73.73   -168.50                                   
REMARK 500    LYS C  62        2.26     82.30                                   
REMARK 500    ARG C  73       65.16     23.22                                   
REMARK 500    LYS C  74      -29.12     80.06                                   
REMARK 500    TYR C 115      -37.81     70.46                                   
REMARK 500    GLN C 117      -55.97   -131.02                                   
REMARK 500    GLN C 128      -92.14     50.77                                   
REMARK 500    CYS C 175      -43.65     81.95                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 5N47   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4GH7   RELATED DB: PDB                                   
DBREF  5N48 A    1   178  UNP    P80188   NGAL_HUMAN      21    198             
DBREF  5N48 B 1266  1357  UNP    P02751   FINC_HUMAN    1266   1357             
DBREF  5N48 C    1   178  UNP    P80188   NGAL_HUMAN      21    198             
DBREF  5N48 D 1266  1357  UNP    P02751   FINC_HUMAN    1266   1357             
SEQADV 5N48 HIS A   28  UNP  P80188    GLN    48 ENGINEERED MUTATION            
SEQADV 5N48 ARG A   36  UNP  P80188    LEU    56 ENGINEERED MUTATION            
SEQADV 5N48 MET A   40  UNP  P80188    ALA    60 ENGINEERED MUTATION            
SEQADV 5N48 ARG A   41  UNP  P80188    ILE    61 ENGINEERED MUTATION            
SEQADV 5N48 ALA A   49  UNP  P80188    GLN    69 ENGINEERED MUTATION            
SEQADV 5N48 VAL A   52  UNP  P80188    TYR    72 ENGINEERED MUTATION            
SEQADV 5N48 LYS A   68  UNP  P80188    SER    88 ENGINEERED MUTATION            
SEQADV 5N48 MET A   70  UNP  P80188    LEU    90 ENGINEERED MUTATION            
SEQADV 5N48 GLN A   72  UNP  P80188    ARG    92 ENGINEERED MUTATION            
SEQADV 5N48 ARG A   73  UNP  P80188    LYS    93 ENGINEERED MUTATION            
SEQADV 5N48 LYS A   77  UNP  P80188    ASP    97 ENGINEERED MUTATION            
SEQADV 5N48 MET A   79  UNP  P80188    TRP    99 ENGINEERED MUTATION            
SEQADV 5N48 ASN A   81  UNP  P80188    ARG   101 ENGINEERED MUTATION            
SEQADV 5N48 SER A   87  UNP  P80188    CYS   107 ENGINEERED MUTATION            
SEQADV 5N48 ALA A   96  UNP  P80188    ASN   116 ENGINEERED MUTATION            
SEQADV 5N48 PRO A  100  UNP  P80188    TYR   120 ENGINEERED MUTATION            
SEQADV 5N48 PRO A  103  UNP  P80188    LEU   123 ENGINEERED MUTATION            
SEQADV 5N48 THR A  106  UNP  P80188    TYR   126 ENGINEERED MUTATION            
SEQADV 5N48 HIS A  125  UNP  P80188    LYS   145 ENGINEERED MUTATION            
SEQADV 5N48 PHE A  127  UNP  P80188    SER   147 ENGINEERED MUTATION            
SEQADV 5N48 HIS A  134  UNP  P80188    LYS   154 ENGINEERED MUTATION            
SEQADV 5N48 SER A  179  UNP  P80188              EXPRESSION TAG                 
SEQADV 5N48 ALA A  180  UNP  P80188              EXPRESSION TAG                 
SEQADV 5N48 TRP A  181  UNP  P80188              EXPRESSION TAG                 
SEQADV 5N48 SER A  182  UNP  P80188              EXPRESSION TAG                 
SEQADV 5N48 HIS A  183  UNP  P80188              EXPRESSION TAG                 
SEQADV 5N48 PRO A  184  UNP  P80188              EXPRESSION TAG                 
SEQADV 5N48 GLN A  185  UNP  P80188              EXPRESSION TAG                 
SEQADV 5N48 PHE A  186  UNP  P80188              EXPRESSION TAG                 
SEQADV 5N48 GLU A  187  UNP  P80188              EXPRESSION TAG                 
SEQADV 5N48 LYS A  188  UNP  P80188              EXPRESSION TAG                 
SEQADV 5N48 MET B 1252  UNP  P02751              INITIATING METHIONINE          
SEQADV 5N48 ALA B 1253  UNP  P02751              EXPRESSION TAG                 
SEQADV 5N48 SER B 1254  UNP  P02751              EXPRESSION TAG                 
SEQADV 5N48 ARG B 1255  UNP  P02751              EXPRESSION TAG                 
SEQADV 5N48 GLY B 1256  UNP  P02751              EXPRESSION TAG                 
SEQADV 5N48 SER B 1257  UNP  P02751              EXPRESSION TAG                 
SEQADV 5N48 HIS B 1258  UNP  P02751              EXPRESSION TAG                 
SEQADV 5N48 HIS B 1259  UNP  P02751              EXPRESSION TAG                 
SEQADV 5N48 HIS B 1260  UNP  P02751              EXPRESSION TAG                 
SEQADV 5N48 HIS B 1261  UNP  P02751              EXPRESSION TAG                 
SEQADV 5N48 HIS B 1262  UNP  P02751              EXPRESSION TAG                 
SEQADV 5N48 HIS B 1263  UNP  P02751              EXPRESSION TAG                 
SEQADV 5N48 GLY B 1264  UNP  P02751              EXPRESSION TAG                 
SEQADV 5N48 ALA B 1265  UNP  P02751              EXPRESSION TAG                 
SEQADV 5N48 HIS C   28  UNP  P80188    GLN    48 ENGINEERED MUTATION            
SEQADV 5N48 ARG C   36  UNP  P80188    LEU    56 ENGINEERED MUTATION            
SEQADV 5N48 MET C   40  UNP  P80188    ALA    60 ENGINEERED MUTATION            
SEQADV 5N48 ARG C   41  UNP  P80188    ILE    61 ENGINEERED MUTATION            
SEQADV 5N48 ALA C   49  UNP  P80188    GLN    69 ENGINEERED MUTATION            
SEQADV 5N48 VAL C   52  UNP  P80188    TYR    72 ENGINEERED MUTATION            
SEQADV 5N48 LYS C   68  UNP  P80188    SER    88 ENGINEERED MUTATION            
SEQADV 5N48 MET C   70  UNP  P80188    LEU    90 ENGINEERED MUTATION            
SEQADV 5N48 GLN C   72  UNP  P80188    ARG    92 ENGINEERED MUTATION            
SEQADV 5N48 ARG C   73  UNP  P80188    LYS    93 ENGINEERED MUTATION            
SEQADV 5N48 LYS C   77  UNP  P80188    ASP    97 ENGINEERED MUTATION            
SEQADV 5N48 MET C   79  UNP  P80188    TRP    99 ENGINEERED MUTATION            
SEQADV 5N48 ASN C   81  UNP  P80188    ARG   101 ENGINEERED MUTATION            
SEQADV 5N48 SER C   87  UNP  P80188    CYS   107 ENGINEERED MUTATION            
SEQADV 5N48 ALA C   96  UNP  P80188    ASN   116 ENGINEERED MUTATION            
SEQADV 5N48 PRO C  100  UNP  P80188    TYR   120 ENGINEERED MUTATION            
SEQADV 5N48 PRO C  103  UNP  P80188    LEU   123 ENGINEERED MUTATION            
SEQADV 5N48 THR C  106  UNP  P80188    TYR   126 ENGINEERED MUTATION            
SEQADV 5N48 HIS C  125  UNP  P80188    LYS   145 ENGINEERED MUTATION            
SEQADV 5N48 PHE C  127  UNP  P80188    SER   147 ENGINEERED MUTATION            
SEQADV 5N48 HIS C  134  UNP  P80188    LYS   154 ENGINEERED MUTATION            
SEQADV 5N48 SER C  179  UNP  P80188              EXPRESSION TAG                 
SEQADV 5N48 ALA C  180  UNP  P80188              EXPRESSION TAG                 
SEQADV 5N48 TRP C  181  UNP  P80188              EXPRESSION TAG                 
SEQADV 5N48 SER C  182  UNP  P80188              EXPRESSION TAG                 
SEQADV 5N48 HIS C  183  UNP  P80188              EXPRESSION TAG                 
SEQADV 5N48 PRO C  184  UNP  P80188              EXPRESSION TAG                 
SEQADV 5N48 GLN C  185  UNP  P80188              EXPRESSION TAG                 
SEQADV 5N48 PHE C  186  UNP  P80188              EXPRESSION TAG                 
SEQADV 5N48 GLU C  187  UNP  P80188              EXPRESSION TAG                 
SEQADV 5N48 LYS C  188  UNP  P80188              EXPRESSION TAG                 
SEQADV 5N48 MET D 1252  UNP  P02751              INITIATING METHIONINE          
SEQADV 5N48 ALA D 1253  UNP  P02751              EXPRESSION TAG                 
SEQADV 5N48 SER D 1254  UNP  P02751              EXPRESSION TAG                 
SEQADV 5N48 ARG D 1255  UNP  P02751              EXPRESSION TAG                 
SEQADV 5N48 GLY D 1256  UNP  P02751              EXPRESSION TAG                 
SEQADV 5N48 SER D 1257  UNP  P02751              EXPRESSION TAG                 
SEQADV 5N48 HIS D 1258  UNP  P02751              EXPRESSION TAG                 
SEQADV 5N48 HIS D 1259  UNP  P02751              EXPRESSION TAG                 
SEQADV 5N48 HIS D 1260  UNP  P02751              EXPRESSION TAG                 
SEQADV 5N48 HIS D 1261  UNP  P02751              EXPRESSION TAG                 
SEQADV 5N48 HIS D 1262  UNP  P02751              EXPRESSION TAG                 
SEQADV 5N48 HIS D 1263  UNP  P02751              EXPRESSION TAG                 
SEQADV 5N48 GLY D 1264  UNP  P02751              EXPRESSION TAG                 
SEQADV 5N48 ALA D 1265  UNP  P02751              EXPRESSION TAG                 
SEQRES   1 A  188  GLN ASP SER THR SER ASP LEU ILE PRO ALA PRO PRO LEU          
SEQRES   2 A  188  SER LYS VAL PRO LEU GLN GLN ASN PHE GLN ASP ASN GLN          
SEQRES   3 A  188  PHE HIS GLY LYS TRP TYR VAL VAL GLY ARG ALA GLY ASN          
SEQRES   4 A  188  MET ARG LEU ARG GLU ASP LYS ASP PRO ALA LYS MET VAL          
SEQRES   5 A  188  ALA THR ILE TYR GLU LEU LYS GLU ASP LYS SER TYR ASN          
SEQRES   6 A  188  VAL THR LYS VAL MET PHE GLN ARG LYS LYS CYS LYS TYR          
SEQRES   7 A  188  MET ILE ASN THR PHE VAL PRO GLY SER GLN PRO GLY GLU          
SEQRES   8 A  188  PHE THR LEU GLY ALA ILE LYS SER PRO PRO GLY PRO THR          
SEQRES   9 A  188  SER THR LEU VAL ARG VAL VAL SER THR ASN TYR ASN GLN          
SEQRES  10 A  188  HIS ALA MET VAL PHE PHE LYS HIS VAL PHE GLN ASN ARG          
SEQRES  11 A  188  GLU TYR PHE HIS ILE THR LEU TYR GLY ARG THR LYS GLU          
SEQRES  12 A  188  LEU THR SER GLU LEU LYS GLU ASN PHE ILE ARG PHE SER          
SEQRES  13 A  188  LYS SER LEU GLY LEU PRO GLU ASN HIS ILE VAL PHE PRO          
SEQRES  14 A  188  VAL PRO ILE ASP GLN CYS ILE ASP GLY SER ALA TRP SER          
SEQRES  15 A  188  HIS PRO GLN PHE GLU LYS                                      
SEQRES   1 B  106  MET ALA SER ARG GLY SER HIS HIS HIS HIS HIS HIS GLY          
SEQRES   2 B  106  ALA GLU VAL PRO GLN LEU THR ASP LEU SER PHE VAL ASP          
SEQRES   3 B  106  ILE THR ASP SER SER ILE GLY LEU ARG TRP THR PRO LEU          
SEQRES   4 B  106  ASN SER SER THR ILE ILE GLY TYR ARG ILE THR VAL VAL          
SEQRES   5 B  106  ALA ALA GLY GLU GLY ILE PRO ILE PHE GLU ASP PHE VAL          
SEQRES   6 B  106  ASP SER SER VAL GLY TYR TYR THR VAL THR GLY LEU GLU          
SEQRES   7 B  106  PRO GLY ILE ASP TYR ASP ILE SER VAL ILE THR LEU ILE          
SEQRES   8 B  106  ASN GLY GLY GLU SER ALA PRO THR THR LEU THR GLN GLN          
SEQRES   9 B  106  THR ALA                                                      
SEQRES   1 C  188  GLN ASP SER THR SER ASP LEU ILE PRO ALA PRO PRO LEU          
SEQRES   2 C  188  SER LYS VAL PRO LEU GLN GLN ASN PHE GLN ASP ASN GLN          
SEQRES   3 C  188  PHE HIS GLY LYS TRP TYR VAL VAL GLY ARG ALA GLY ASN          
SEQRES   4 C  188  MET ARG LEU ARG GLU ASP LYS ASP PRO ALA LYS MET VAL          
SEQRES   5 C  188  ALA THR ILE TYR GLU LEU LYS GLU ASP LYS SER TYR ASN          
SEQRES   6 C  188  VAL THR LYS VAL MET PHE GLN ARG LYS LYS CYS LYS TYR          
SEQRES   7 C  188  MET ILE ASN THR PHE VAL PRO GLY SER GLN PRO GLY GLU          
SEQRES   8 C  188  PHE THR LEU GLY ALA ILE LYS SER PRO PRO GLY PRO THR          
SEQRES   9 C  188  SER THR LEU VAL ARG VAL VAL SER THR ASN TYR ASN GLN          
SEQRES  10 C  188  HIS ALA MET VAL PHE PHE LYS HIS VAL PHE GLN ASN ARG          
SEQRES  11 C  188  GLU TYR PHE HIS ILE THR LEU TYR GLY ARG THR LYS GLU          
SEQRES  12 C  188  LEU THR SER GLU LEU LYS GLU ASN PHE ILE ARG PHE SER          
SEQRES  13 C  188  LYS SER LEU GLY LEU PRO GLU ASN HIS ILE VAL PHE PRO          
SEQRES  14 C  188  VAL PRO ILE ASP GLN CYS ILE ASP GLY SER ALA TRP SER          
SEQRES  15 C  188  HIS PRO GLN PHE GLU LYS                                      
SEQRES   1 D  106  MET ALA SER ARG GLY SER HIS HIS HIS HIS HIS HIS GLY          
SEQRES   2 D  106  ALA GLU VAL PRO GLN LEU THR ASP LEU SER PHE VAL ASP          
SEQRES   3 D  106  ILE THR ASP SER SER ILE GLY LEU ARG TRP THR PRO LEU          
SEQRES   4 D  106  ASN SER SER THR ILE ILE GLY TYR ARG ILE THR VAL VAL          
SEQRES   5 D  106  ALA ALA GLY GLU GLY ILE PRO ILE PHE GLU ASP PHE VAL          
SEQRES   6 D  106  ASP SER SER VAL GLY TYR TYR THR VAL THR GLY LEU GLU          
SEQRES   7 D  106  PRO GLY ILE ASP TYR ASP ILE SER VAL ILE THR LEU ILE          
SEQRES   8 D  106  ASN GLY GLY GLU SER ALA PRO THR THR LEU THR GLN GLN          
SEQRES   9 D  106  THR ALA                                                      
FORMUL   5  HOH   *296(H2 O)                                                    
HELIX    1 AA1 PRO A   12  VAL A   16  5                                   5    
HELIX    2 AA2 GLN A   23  HIS A   28  1                                   6    
HELIX    3 AA3 THR A  145  LEU A  159  1                                  15    
HELIX    4 AA4 PRO A  162  ASN A  164  5                                   3    
HELIX    5 AA5 PRO C   12  VAL C   16  5                                   5    
HELIX    6 AA6 GLN C   23  HIS C   28  1                                   6    
HELIX    7 AA7 THR C  145  LEU C  159  1                                  15    
HELIX    8 AA8 PRO C  162  ASN C  164  5                                   3    
SHEET    1 AA110 ILE A 166  VAL A 167  0                                        
SHEET    2 AA110 GLY A  29  GLY A  38 -1  N  ARG A  36   O  VAL A 167           
SHEET    3 AA110 ARG A 130  GLY A 139 -1  O  LEU A 137   N  VAL A  34           
SHEET    4 AA110 HIS A 118  PHE A 127 -1  N  ALA A 119   O  TYR A 138           
SHEET    5 AA110 SER A 105  THR A 113 -1  N  ARG A 109   O  PHE A 122           
SHEET    6 AA110 GLU A  91  LEU A  94 -1  N  PHE A  92   O  VAL A 108           
SHEET    7 AA110 LYS A  75  PRO A  85 -1  N  VAL A  84   O  THR A  93           
SHEET    8 AA110 TYR A  64  GLN A  72 -1  N  VAL A  66   O  ASN A  81           
SHEET    9 AA110 LYS A  50  LEU A  58 -1  N  GLU A  57   O  ASN A  65           
SHEET   10 AA110 GLY A  29  GLY A  38 -1  N  GLY A  29   O  TYR A  56           
SHEET    1 AA2 3 SER B1274  VAL B1276  0                                        
SHEET    2 AA2 3 SER B1282  ARG B1286 -1  O  ARG B1286   N  SER B1274           
SHEET    3 AA2 3 TYR B1322  THR B1326 -1  O  TYR B1323   N  LEU B1285           
SHEET    1 AA3 4 PHE B1312  ASP B1317  0                                        
SHEET    2 AA3 4 ILE B1295  ALA B1304 -1  N  VAL B1302   O  PHE B1312           
SHEET    3 AA3 4 ASP B1333  ILE B1342 -1  O  ASP B1335   N  VAL B1303           
SHEET    4 AA3 4 GLY B1345  GLU B1346 -1  O  GLY B1345   N  ILE B1342           
SHEET    1 AA4 4 PHE B1312  ASP B1317  0                                        
SHEET    2 AA4 4 ILE B1295  ALA B1304 -1  N  VAL B1302   O  PHE B1312           
SHEET    3 AA4 4 ASP B1333  ILE B1342 -1  O  ASP B1335   N  VAL B1303           
SHEET    4 AA4 4 THR B1350  GLN B1355 -1  O  LEU B1352   N  ILE B1336           
SHEET    1 AA510 ILE C 166  VAL C 167  0                                        
SHEET    2 AA510 GLY C  29  GLY C  38 -1  N  ARG C  36   O  VAL C 167           
SHEET    3 AA510 ARG C 130  GLY C 139 -1  O  GLY C 139   N  TYR C  32           
SHEET    4 AA510 HIS C 118  PHE C 127 -1  N  ALA C 119   O  TYR C 138           
SHEET    5 AA510 SER C 105  THR C 113 -1  N  ARG C 109   O  PHE C 122           
SHEET    6 AA510 GLU C  91  THR C  93 -1  N  PHE C  92   O  VAL C 108           
SHEET    7 AA510 LYS C  75  PRO C  85 -1  N  VAL C  84   O  THR C  93           
SHEET    8 AA510 TYR C  64  GLN C  72 -1  N  LYS C  68   O  MET C  79           
SHEET    9 AA510 LYS C  50  LEU C  58 -1  N  VAL C  52   O  VAL C  69           
SHEET   10 AA510 GLY C  29  GLY C  38 -1  N  GLY C  29   O  TYR C  56           
SHEET    1 AA6 3 SER D1274  VAL D1276  0                                        
SHEET    2 AA6 3 SER D1282  ARG D1286 -1  O  ARG D1286   N  SER D1274           
SHEET    3 AA6 3 TYR D1322  THR D1326 -1  O  VAL D1325   N  ILE D1283           
SHEET    1 AA7 4 PHE D1312  ASP D1317  0                                        
SHEET    2 AA7 4 ILE D1295  ALA D1304 -1  N  TYR D1298   O  VAL D1316           
SHEET    3 AA7 4 ASP D1333  ILE D1342 -1  O  ASP D1335   N  VAL D1303           
SHEET    4 AA7 4 GLY D1345  GLU D1346 -1  O  GLY D1345   N  ILE D1342           
SHEET    1 AA8 4 PHE D1312  ASP D1317  0                                        
SHEET    2 AA8 4 ILE D1295  ALA D1304 -1  N  TYR D1298   O  VAL D1316           
SHEET    3 AA8 4 ASP D1333  ILE D1342 -1  O  ASP D1335   N  VAL D1303           
SHEET    4 AA8 4 THR D1350  GLN D1355 -1  O  GLN D1354   N  TYR D1334           
SSBOND   1 CYS A   76    CYS A  175                          1555   1555  2.02  
SSBOND   2 CYS C   76    CYS C  175                          1555   1555  2.04  
CISPEP   1 SER A   99    PRO A  100          0       -10.28                     
CISPEP   2 PRO A  100    PRO A  101          0         8.18                     
CISPEP   3 SER C   99    PRO C  100          0       -10.76                     
CISPEP   4 PRO C  100    PRO C  101          0         2.92                     
CRYST1   52.456   67.801   76.806  90.00  90.06  90.00 P 1 21 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      0.019064  0.000000  0.000019        0.00000                         
SCALE2      0.000000  0.014749  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.013020        0.00000                         
ATOM      1  N   SER A   3      57.427  -6.467  62.814  1.00 41.81           N  
ANISOU    1  N   SER A   3     5667   4657   5563   -113    -42    264       N  
ATOM      2  CA  SER A   3      57.600  -6.987  61.404  1.00 41.30           C  
ANISOU    2  CA  SER A   3     5625   4530   5534   -104    -54    256       C  
ATOM      3  C   SER A   3      56.335  -7.041  60.533  1.00 39.67           C  
ANISOU    3  C   SER A   3     5425   4303   5342   -102    -57    253       C  
ATOM      4  O   SER A   3      56.455  -7.177  59.321  1.00 38.28           O  
ANISOU    4  O   SER A   3     5271   4082   5189    -93    -63    236       O  
ATOM      5  CB  SER A   3      58.289  -8.363  61.379  1.00 44.12           C  
ANISOU    5  CB  SER A   3     5982   4863   5919   -109    -77    288       C  
ATOM      6  OG  SER A   3      58.954  -8.565  60.132  1.00 46.72           O  
ANISOU    6  OG  SER A   3     6337   5141   6273    -93    -82    266       O  
ATOM      7  N   THR A   4      55.135  -6.987  61.118  1.00 38.02           N  
ANISOU    7  N   THR A   4     5196   4128   5119   -112    -55    272       N  
ATOM      8  CA  THR A   4      53.934  -6.634  60.347  1.00 33.74           C  
ANISOU    8  CA  THR A   4     4659   3578   4583   -108    -51    263       C  
ATOM      9  C   THR A   4      54.212  -5.302  59.676  1.00 31.37           C  
ANISOU    9  C   THR A   4     4379   3266   4272    -88    -31    214       C  
ATOM     10  O   THR A   4      54.703  -4.372  60.301  1.00 32.29           O  
ANISOU   10  O   THR A   4     4495   3408   4363    -81    -14    192       O  
ATOM     11  CB  THR A   4      52.660  -6.488  61.221  1.00 34.90           C  
ANISOU   11  CB  THR A   4     4776   3777   4705   -117    -45    287       C  
ATOM     12  OG1 THR A   4      52.193  -7.771  61.654  1.00 34.42           O  
ANISOU   12  OG1 THR A   4     4696   3724   4659   -139    -68    338       O  
ATOM     13  CG2 THR A   4      51.515  -5.856  60.448  1.00 35.04           C  
ANISOU   13  CG2 THR A   4     4798   3790   4722   -108    -36    272       C  
ATOM     14  N   SER A   5      53.904  -5.220  58.395  1.00 27.45           N  
ANISOU   14  N   SER A   5     3902   2730   3797    -80    -34    197       N  
ATOM     15  CA  SER A   5      54.071  -3.971  57.666  1.00 24.39           C  
ANISOU   15  CA  SER A   5     3533   2329   3402    -62    -16    155       C  
ATOM     16  C   SER A   5      53.122  -2.882  58.176  1.00 22.52           C  
ANISOU   16  C   SER A   5     3286   2130   3139    -55      2    143       C  
ATOM     17  O   SER A   5      51.930  -3.159  58.386  1.00 22.30           O  
ANISOU   17  O   SER A   5     3240   2123   3107    -60      0    166       O  
ATOM     18  CB  SER A   5      53.770  -4.299  56.207  1.00 23.46           C  
ANISOU   18  CB  SER A   5     3433   2166   3312    -58    -26    148       C  
ATOM     19  OG  SER A   5      53.583  -3.147  55.505  1.00 22.36           O  
ANISOU   19  OG  SER A   5     3306   2020   3167    -44    -11    116       O  
ATOM     20  N   ASP A   6      53.613  -1.649  58.342  1.00 20.63           N  
ANISOU   20  N   ASP A   6     3057   1898   2881    -42     19    109       N  
ATOM     21  CA  ASP A   6      52.780  -0.490  58.777  1.00 20.79           C  
ANISOU   21  CA  ASP A   6     3073   1948   2876    -29     38     91       C  
ATOM     22  C   ASP A   6      52.256   0.344  57.595  1.00 18.99           C  
ANISOU   22  C   ASP A   6     2863   1693   2660    -14     45     65       C  
ATOM     23  O   ASP A   6      51.598   1.414  57.760  1.00 18.33           O  
ANISOU   23  O   ASP A   6     2780   1625   2559      1     61     46       O  
ATOM     24  CB  ASP A   6      53.512   0.382  59.791  1.00 21.53           C  
ANISOU   24  CB  ASP A   6     3170   2069   2942    -24     49     68       C  
ATOM     25  CG  ASP A   6      54.749   1.079  59.205  1.00 22.58           C  
ANISOU   25  CG  ASP A   6     3329   2168   3082    -21     50     37       C  
ATOM     26  OD1 ASP A   6      54.815   1.185  57.953  1.00 22.15           O  
ANISOU   26  OD1 ASP A   6     3290   2074   3050    -16     47     27       O  
ATOM     27  OD2 ASP A   6      55.659   1.439  60.002  1.00 23.55           O  
ANISOU   27  OD2 ASP A   6     3454   2307   3187    -25     51     27       O  
ATOM     28  N   LEU A   7      52.564  -0.105  56.376  1.00 17.56           N  
ANISOU   28  N   LEU A   7     2696   1469   2507    -16     34     65       N  
ATOM     29  CA  LEU A   7      52.117   0.584  55.153  1.00 16.16           C  
ANISOU   29  CA  LEU A   7     2533   1265   2342     -4     39     45       C  
ATOM     30  C   LEU A   7      50.644   0.537  54.971  1.00 15.82           C  
ANISOU   30  C   LEU A   7     2476   1236   2298     -1     42     60       C  
ATOM     31  O   LEU A   7      50.016  -0.418  55.376  1.00 15.75           O  
ANISOU   31  O   LEU A   7     2448   1245   2291    -14     32     92       O  
ATOM     32  CB  LEU A   7      52.698  -0.046  53.876  1.00 15.37           C  
ANISOU   32  CB  LEU A   7     2449   1122   2269     -8     25     44       C  
ATOM     33  CG  LEU A   7      54.236  -0.044  53.872  1.00 15.46           C  
ANISOU   33  CG  LEU A   7     2473   1118   2282     -9     22     31       C  
ATOM     34  CD1 LEU A   7      54.854  -0.942  52.875  1.00 15.60           C  
ANISOU   34  CD1 LEU A   7     2500   1102   2323    -10      8     36       C  
ATOM     35  CD2 LEU A   7      54.785   1.376  53.743  1.00 15.46           C  
ANISOU   35  CD2 LEU A   7     2486   1115   2270      1     36      0       C  
ATOM     36  N   ILE A   8      50.098   1.524  54.247  1.00 14.95           N  
ANISOU   36  N   ILE A   8     2374   1116   2189     13     53     40       N  
ATOM     37  CA  ILE A   8      48.765   1.413  53.730  1.00 15.21           C  
ANISOU   37  CA  ILE A   8     2395   1156   2226     15     53     55       C  
ATOM     38  C   ILE A   8      48.700   0.088  52.898  1.00 15.19           C  
ANISOU   38  C   ILE A   8     2393   1127   2249     -3     30     79       C  
ATOM     39  O   ILE A   8      49.556  -0.134  52.042  1.00 14.80           O  
ANISOU   39  O   ILE A   8     2364   1042   2217     -4     22     66       O  
ATOM     40  CB  ILE A   8      48.336   2.583  52.811  1.00 15.32           C  
ANISOU   40  CB  ILE A   8     2421   1154   2244     34     65     31       C  
ATOM     41  CG1 ILE A   8      48.280   3.899  53.614  1.00 15.52           C  
ANISOU   41  CG1 ILE A   8     2450   1201   2246     55     84      6       C  
ATOM     42  CG2 ILE A   8      46.984   2.319  52.147  1.00 15.67           C  
ANISOU   42  CG2 ILE A   8     2452   1205   2296     33     62     52       C  
ATOM     43  CD1 ILE A   8      48.190   5.111  52.665  1.00 15.36           C  
ANISOU   43  CD1 ILE A   8     2447   1154   2233     73     93    -19       C  
ATOM     44  N   PRO A   9      47.717  -0.745  53.161  1.00 15.62           N  
ANISOU   44  N   PRO A   9     2427   1201   2305    -16     21    113       N  
ATOM     45  CA  PRO A   9      47.739  -2.077  52.453  1.00 15.88           C  
ANISOU   45  CA  PRO A   9     2465   1204   2363    -36     -4    135       C  
ATOM     46  C   PRO A   9      47.501  -1.916  50.967  1.00 15.60           C  
ANISOU   46  C   PRO A   9     2446   1135   2345    -32     -9    121       C  
ATOM     47  O   PRO A   9      46.773  -0.973  50.517  1.00 15.33           O  
ANISOU   47  O   PRO A   9     2409   1110   2304    -19      4    110       O  
ATOM     48  CB  PRO A   9      46.535  -2.819  53.041  1.00 16.40           C  
ANISOU   48  CB  PRO A   9     2503   1303   2425    -53    -14    177       C  
ATOM     49  CG  PRO A   9      46.102  -2.082  54.203  1.00 16.59           C  
ANISOU   49  CG  PRO A   9     2505   1377   2419    -42      5    180       C  
ATOM     50  CD  PRO A   9      46.649  -0.662  54.156  1.00 16.04           C  
ANISOU   50  CD  PRO A   9     2452   1305   2337    -16     29    137       C  
ATOM     51  N   ALA A  10      48.115  -2.781  50.179  1.00 15.19           N  
ANISOU   51  N   ALA A  10     2412   1046   2314    -41    -28    119       N  
ATOM     52  CA  ALA A  10      47.849  -2.781  48.746  1.00 14.79           C  
ANISOU   52  CA  ALA A  10     2375    965   2277    -39    -36    107       C  
ATOM     53  C   ALA A  10      46.392  -3.155  48.481  1.00 15.24           C  
ANISOU   53  C   ALA A  10     2416   1035   2338    -53    -46    135       C  
ATOM     54  O   ALA A  10      45.784  -3.984  49.247  1.00 16.16           O  
ANISOU   54  O   ALA A  10     2515   1170   2453    -72    -59    170       O  
ATOM     55  CB  ALA A  10      48.781  -3.709  48.029  1.00 15.07           C  
ANISOU   55  CB  ALA A  10     2433    961   2332    -43    -55     99       C  
ATOM     56  N   PRO A  11      45.775  -2.615  47.436  1.00 15.00           N  
ANISOU   56  N   PRO A  11     2390    998   2311    -48    -43    126       N  
ATOM     57  CA  PRO A  11      44.341  -2.844  47.195  1.00 15.53           C  
ANISOU   57  CA  PRO A  11     2438   1083   2377    -61    -51    154       C  
ATOM     58  C   PRO A  11      44.173  -4.229  46.603  1.00 16.12           C  
ANISOU   58  C   PRO A  11     2523   1130   2472    -86    -84    172       C  
ATOM     59  O   PRO A  11      45.110  -4.743  45.961  1.00 16.28           O  
ANISOU   59  O   PRO A  11     2567   1111   2505    -85    -96    152       O  
ATOM     60  CB  PRO A  11      43.972  -1.828  46.098  1.00 15.65           C  
ANISOU   60  CB  PRO A  11     2460   1094   2392    -45    -38    134       C  
ATOM     61  CG  PRO A  11      45.339  -1.452  45.452  1.00 15.23           C  
ANISOU   61  CG  PRO A  11     2433   1007   2345    -31    -33     97       C  
ATOM     62  CD  PRO A  11      46.307  -1.528  46.561  1.00 14.73           C  
ANISOU   62  CD  PRO A  11     2372    948   2275    -27    -27     92       C  
ATOM     63  N   PRO A  12      42.981  -4.823  46.824  1.00 17.48           N  
ANISOU   63  N   PRO A  12     2674   1322   2645   -108    -99    210       N  
ATOM     64  CA  PRO A  12      42.747  -6.065  46.072  1.00 18.26           C  
ANISOU   64  CA  PRO A  12     2786   1387   2763   -134   -134    224       C  
ATOM     65  C   PRO A  12      42.774  -5.794  44.568  1.00 18.97           C  
ANISOU   65  C   PRO A  12     2896   1448   2860   -127   -137    197       C  
ATOM     66  O   PRO A  12      42.403  -4.678  44.118  1.00 18.69           O  
ANISOU   66  O   PRO A  12     2854   1431   2814   -111   -115    184       O  
ATOM     67  CB  PRO A  12      41.320  -6.501  46.512  1.00 18.54           C  
ANISOU   67  CB  PRO A  12     2791   1457   2795   -160   -147    272       C  
ATOM     68  CG  PRO A  12      40.735  -5.352  47.238  1.00 18.46           C  
ANISOU   68  CG  PRO A  12     2752   1499   2761   -142   -115    278       C  
ATOM     69  CD  PRO A  12      41.799  -4.327  47.512  1.00 18.05           C  
ANISOU   69  CD  PRO A  12     2712   1444   2698   -109    -86    238       C  
ATOM     70  N   LEU A  13      43.182  -6.778  43.792  1.00 19.58           N  
ANISOU   70  N   LEU A  13     2999   1483   2955   -138   -165    188       N  
ATOM     71  CA  LEU A  13      43.242  -6.575  42.329  1.00 20.81           C  
ANISOU   71  CA  LEU A  13     3175   1615   3115   -131   -169    162       C  
ATOM     72  C   LEU A  13      41.890  -6.353  41.703  1.00 21.14           C  
ANISOU   72  C   LEU A  13     3201   1675   3152   -146   -175    181       C  
ATOM     73  O   LEU A  13      41.817  -5.801  40.620  1.00 21.09           O  
ANISOU   73  O   LEU A  13     3203   1664   3144   -137   -169    161       O  
ATOM     74  CB  LEU A  13      44.022  -7.672  41.580  1.00 22.84           C  
ANISOU   74  CB  LEU A  13     3465   1823   3388   -135   -197    142       C  
ATOM     75  CG  LEU A  13      45.515  -7.649  41.906  1.00 23.68           C  
ANISOU   75  CG  LEU A  13     3587   1913   3495   -111   -185    116       C  
ATOM     76  CD1 LEU A  13      46.215  -8.725  41.104  1.00 24.30           C  
ANISOU   76  CD1 LEU A  13     3698   1945   3589   -110   -212     96       C  
ATOM     77  CD2 LEU A  13      46.202  -6.287  41.721  1.00 23.77           C  
ANISOU   77  CD2 LEU A  13     3597   1941   3493    -82   -151     87       C  
ATOM     78  N   SER A  14      40.836  -6.790  42.370  1.00 21.51           N  
ANISOU   78  N   SER A  14     3224   1747   3199   -171   -187    223       N  
ATOM     79  CA  SER A  14      39.491  -6.553  41.947  1.00 22.40           C  
ANISOU   79  CA  SER A  14     3316   1887   3305   -186   -191    248       C  
ATOM     80  C   SER A  14      39.198  -5.070  41.808  1.00 21.56           C  
ANISOU   80  C   SER A  14     3193   1813   3183   -158   -155    237       C  
ATOM     81  O   SER A  14      38.417  -4.678  40.931  1.00 24.45           O  
ANISOU   81  O   SER A  14     3552   2189   3546   -161   -155    241       O  
ATOM     82  CB  SER A  14      38.486  -7.150  42.927  1.00 22.48           C  
ANISOU   82  CB  SER A  14     3297   1930   3314   -214   -205    300       C  
ATOM     83  OG  SER A  14      38.800  -6.809  44.257  1.00 23.46           O  
ANISOU   83  OG  SER A  14     3402   2082   3427   -200   -183    308       O  
ATOM     84  N   LYS A  15      39.882  -4.268  42.629  1.00 21.14           N  
ANISOU   84  N   LYS A  15     3137   1774   3120   -132   -126    220       N  
ATOM     85  CA  LYS A  15      39.794  -2.786  42.562  1.00 21.10           C  
ANISOU   85  CA  LYS A  15     3122   1792   3102   -101    -91    203       C  
ATOM     86  C   LYS A  15      40.752  -2.147  41.531  1.00 19.51           C  
ANISOU   86  C   LYS A  15     2947   1560   2906    -81    -82    162       C  
ATOM     87  O   LYS A  15      40.802  -0.867  41.414  1.00 18.52           O  
ANISOU   87  O   LYS A  15     2817   1446   2771    -56    -56    146       O  
ATOM     88  CB  LYS A  15      40.031  -2.216  43.947  1.00 22.12           C  
ANISOU   88  CB  LYS A  15     3236   1949   3217    -84    -68    205       C  
ATOM     89  CG  LYS A  15      39.125  -2.790  45.026  1.00 23.97           C  
ANISOU   89  CG  LYS A  15     3440   2222   3443   -102    -74    248       C  
ATOM     90  CD  LYS A  15      38.871  -1.791  46.149  1.00 24.74           C  
ANISOU   90  CD  LYS A  15     3516   2365   3519    -76    -44    250       C  
ATOM     91  CE  LYS A  15      37.688  -0.933  45.820  1.00 25.27           C  
ANISOU   91  CE  LYS A  15     3559   2465   3575    -63    -28    262       C  
ATOM     92  NZ  LYS A  15      37.884   0.499  46.194  1.00 24.71           N  
ANISOU   92  NZ  LYS A  15     3488   2410   3490    -24      4    235       N  
ATOM     93  N   VAL A  16      41.506  -2.931  40.790  1.00 18.04           N  
ANISOU   93  N   VAL A  16     2787   1336   2731    -89   -102    144       N  
ATOM     94  CA  VAL A  16      42.455  -2.364  39.798  1.00 17.29           C  
ANISOU   94  CA  VAL A  16     2713   1217   2636    -70    -93    107       C  
ATOM     95  C   VAL A  16      42.138  -2.864  38.362  1.00 17.21           C  
ANISOU   95  C   VAL A  16     2716   1188   2632    -82   -115    102       C  
ATOM     96  O   VAL A  16      42.745  -3.817  37.876  1.00 16.96           O  
ANISOU   96  O   VAL A  16     2707   1126   2609    -89   -137     88       O  
ATOM     97  CB  VAL A  16      43.904  -2.605  40.237  1.00 16.32           C  
ANISOU   97  CB  VAL A  16     2610   1073   2517    -58    -90     84       C  
ATOM     98  CG1 VAL A  16      44.942  -2.009  39.274  1.00 16.16           C  
ANISOU   98  CG1 VAL A  16     2607   1035   2496    -38    -81     50       C  
ATOM     99  CG2 VAL A  16      44.036  -2.168  41.666  1.00 16.13           C  
ANISOU   99  CG2 VAL A  16     2570   1072   2485    -51    -72     93       C  
ATOM    100  N   PRO A  17      41.185  -2.201  37.680  1.00 17.43           N  
ANISOU  100  N   PRO A  17     2730   1236   2656    -83   -109    112       N  
ATOM    101  CA  PRO A  17      40.819  -2.526  36.320  1.00 17.90           C  
ANISOU  101  CA  PRO A  17     2799   1285   2717    -94   -128    108       C  
ATOM    102  C   PRO A  17      41.937  -2.449  35.321  1.00 17.47           C  
ANISOU  102  C   PRO A  17     2769   1205   2663    -79   -128     72       C  
ATOM    103  O   PRO A  17      43.011  -1.899  35.621  1.00 16.61           O  
ANISOU  103  O   PRO A  17     2667   1090   2551    -58   -109     50       O  
ATOM    104  CB  PRO A  17      39.852  -1.403  35.973  1.00 18.09           C  
ANISOU  104  CB  PRO A  17     2799   1340   2733    -87   -110    122       C  
ATOM    105  CG  PRO A  17      39.372  -0.878  37.261  1.00 18.20           C  
ANISOU  105  CG  PRO A  17     2789   1382   2741    -79    -90    143       C  
ATOM    106  CD  PRO A  17      40.628  -0.877  38.028  1.00 17.73           C  
ANISOU  106  CD  PRO A  17     2745   1306   2684    -65    -81    120       C  
ATOM    107  N   LEU A  18      41.667  -3.085  34.171  1.00 17.71           N  
ANISOU  107  N   LEU A  18     2812   1222   2694    -93   -151     66       N  
ATOM    108  CA  LEU A  18      42.488  -3.048  32.999  1.00 17.60           C  
ANISOU  108  CA  LEU A  18     2818   1193   2675    -80   -154     34       C  
ATOM    109  C   LEU A  18      41.686  -2.423  31.896  1.00 17.76           C  
ANISOU  109  C   LEU A  18     2827   1233   2688    -84   -152     40       C  
ATOM    110  O   LEU A  18      40.486  -2.680  31.759  1.00 17.42           O  
ANISOU  110  O   LEU A  18     2771   1202   2645   -106   -166     66       O  
ATOM    111  CB  LEU A  18      42.867  -4.468  32.587  1.00 18.43           C  
ANISOU  111  CB  LEU A  18     2950   1265   2786    -92   -186     20       C  
ATOM    112  CG  LEU A  18      43.984  -4.961  33.445  1.00 18.52           C  
ANISOU  112  CG  LEU A  18     2975   1255   2804    -79   -184      7       C  
ATOM    113  CD1 LEU A  18      43.974  -6.516  33.312  1.00 18.66           C  
ANISOU  113  CD1 LEU A  18     3018   1238   2832    -97   -222      4       C  
ATOM    114  CD2 LEU A  18      45.385  -4.445  33.112  1.00 19.41           C  
ANISOU  114  CD2 LEU A  18     3100   1365   2910    -49   -165    -24       C  
ATOM    115  N   GLN A  19      42.356  -1.539  31.146  1.00 17.56           N  
ANISOU  115  N   GLN A  19     2803   1212   2655    -63   -135     21       N  
ATOM    116  CA  GLN A  19      41.784  -0.963  29.947  1.00 18.01           C  
ANISOU  116  CA  GLN A  19     2851   1287   2703    -64   -134     24       C  
ATOM    117  C   GLN A  19      41.313  -2.072  29.082  1.00 18.96           C  
ANISOU  117  C   GLN A  19     2985   1396   2821    -86   -167     21       C  
ATOM    118  O   GLN A  19      42.083  -2.935  28.722  1.00 18.92           O  
ANISOU  118  O   GLN A  19     3006   1368   2815    -84   -183     -4       O  
ATOM    119  CB  GLN A  19      42.817  -0.078  29.225  1.00 17.57           C  
ANISOU  119  CB  GLN A  19     2799   1234   2640    -40   -116      1       C  
ATOM    120  CG  GLN A  19      42.388   0.408  27.848  1.00 17.66           C  
ANISOU  120  CG  GLN A  19     2803   1263   2641    -42   -118      2       C  
ATOM    121  CD  GLN A  19      41.211   1.397  27.901  1.00 17.98           C  
ANISOU  121  CD  GLN A  19     2816   1330   2683    -46   -106     33       C  
ATOM    122  OE1 GLN A  19      41.149   2.241  28.793  1.00 17.87           O  
ANISOU  122  OE1 GLN A  19     2789   1322   2676    -34    -84     44       O  
ATOM    123  NE2 GLN A  19      40.260   1.241  26.963  1.00 18.55           N  
ANISOU  123  NE2 GLN A  19     2880   1417   2749    -62   -120     47       N  
ATOM    124  N   GLN A  20      40.033  -2.018  28.728  1.00 20.75           N  
ANISOU  124  N   GLN A  20     3196   1642   3046   -107   -176     47       N  
ATOM    125  CA  GLN A  20      39.472  -3.116  27.916  1.00 21.84           C  
ANISOU  125  CA  GLN A  20     3347   1769   3180   -133   -212     46       C  
ATOM    126  C   GLN A  20      39.917  -2.888  26.491  1.00 21.47           C  
ANISOU  126  C   GLN A  20     3311   1726   3119   -123   -214     20       C  
ATOM    127  O   GLN A  20      40.132  -1.752  26.071  1.00 21.39           O  
ANISOU  127  O   GLN A  20     3287   1738   3103   -105   -189     19       O  
ATOM    128  CB  GLN A  20      37.962  -3.226  28.007  1.00 25.10           C  
ANISOU  128  CB  GLN A  20     3738   2203   3594   -163   -225     85       C  
ATOM    129  CG  GLN A  20      37.124  -2.048  27.604  1.00 26.52           C  
ANISOU  129  CG  GLN A  20     3887   2421   3767   -159   -205    109       C  
ATOM    130  CD  GLN A  20      35.637  -2.385  27.552  1.00 28.97           C  
ANISOU  130  CD  GLN A  20     4176   2753   4076   -191   -224    148       C  
ATOM    131  OE1 GLN A  20      35.209  -3.519  27.879  1.00 31.25           O  
ANISOU  131  OE1 GLN A  20     4474   3028   4371   -220   -254    160       O  
ATOM    132  NE2 GLN A  20      34.838  -1.423  27.090  1.00 27.88           N  
ANISOU  132  NE2 GLN A  20     4011   2650   3932   -187   -210    171       N  
ATOM    133  N   ASN A  21      40.169  -4.002  25.794  1.00 21.03           N  
ANISOU  133  N   ASN A  21     3283   1647   3058   -133   -244     -2       N  
ATOM    134  CA  ASN A  21      40.701  -3.987  24.429  1.00 21.06           C  
ANISOU  134  CA  ASN A  21     3301   1655   3045   -121   -249    -32       C  
ATOM    135  C   ASN A  21      42.055  -3.270  24.313  1.00 19.69           C  
ANISOU  135  C   ASN A  21     3129   1485   2865    -85   -221    -57       C  
ATOM    136  O   ASN A  21      42.366  -2.668  23.311  1.00 19.54           O  
ANISOU  136  O   ASN A  21     3104   1487   2830    -72   -212    -68       O  
ATOM    137  CB  ASN A  21      39.666  -3.411  23.443  1.00 21.65           C  
ANISOU  137  CB  ASN A  21     3355   1762   3108   -137   -251    -13       C  
ATOM    138  CG  ASN A  21      38.338  -4.138  23.509  1.00 23.78           C  
ANISOU  138  CG  ASN A  21     3620   2031   3381   -175   -281     13       C  
ATOM    139  OD1 ASN A  21      37.268  -3.531  23.542  1.00 25.53           O  
ANISOU  139  OD1 ASN A  21     3813   2281   3604   -189   -275     48       O  
ATOM    140  ND2 ASN A  21      38.407  -5.453  23.483  1.00 24.25           N  
ANISOU  140  ND2 ASN A  21     3711   2058   3445   -192   -315     -2       N  
ATOM    141  N   PHE A  22      42.856  -3.403  25.353  1.00 18.89           N  
ANISOU  141  N   PHE A  22     3035   1366   2775    -71   -210    -63       N  
ATOM    142  CA  PHE A  22      44.197  -2.789  25.425  1.00 18.24           C  
ANISOU  142  CA  PHE A  22     2954   1288   2689    -40   -186    -83       C  
ATOM    143  C   PHE A  22      44.968  -3.105  24.143  1.00 18.32           C  
ANISOU  143  C   PHE A  22     2980   1300   2678    -24   -194   -115       C  
ATOM    144  O   PHE A  22      44.997  -4.272  23.672  1.00 18.09           O  
ANISOU  144  O   PHE A  22     2976   1250   2644    -28   -221   -137       O  
ATOM    145  CB  PHE A  22      44.987  -3.235  26.647  1.00 17.74           C  
ANISOU  145  CB  PHE A  22     2902   1200   2638    -30   -181    -89       C  
ATOM    146  CG  PHE A  22      46.379  -2.738  26.666  1.00 17.03           C  
ANISOU  146  CG  PHE A  22     2813   1114   2541     -1   -161   -108       C  
ATOM    147  CD1 PHE A  22      46.622  -1.365  26.991  1.00 16.42           C  
ANISOU  147  CD1 PHE A  22     2714   1059   2465      8   -131    -94       C  
ATOM    148  CD2 PHE A  22      47.433  -3.480  26.256  1.00 16.52           C  
ANISOU  148  CD2 PHE A  22     2770   1036   2468     17   -169   -138       C  
ATOM    149  CE1 PHE A  22      47.925  -0.857  27.013  1.00 16.29           C  
ANISOU  149  CE1 PHE A  22     2697   1048   2442     32   -114   -108       C  
ATOM    150  CE2 PHE A  22      48.701  -3.000  26.250  1.00 16.70           C  
ANISOU  150  CE2 PHE A  22     2791   1069   2484     43   -150   -151       C  
ATOM    151  CZ  PHE A  22      48.972  -1.644  26.622  1.00 16.41           C  
ANISOU  151  CZ  PHE A  22     2730   1054   2448     48   -122   -135       C  
ATOM    152  N   GLN A  23      45.534  -2.065  23.547  1.00 17.67           N  
ANISOU  152  N   GLN A  23     2883   1245   2584     -6   -172   -118       N  
ATOM    153  CA  GLN A  23      46.283  -2.104  22.285  1.00 18.32           C  
ANISOU  153  CA  GLN A  23     2972   1343   2643     12   -174   -144       C  
ATOM    154  C   GLN A  23      47.720  -1.802  22.575  1.00 18.20           C  
ANISOU  154  C   GLN A  23     2959   1332   2625     40   -154   -158       C  
ATOM    155  O   GLN A  23      48.133  -0.613  22.744  1.00 17.81           O  
ANISOU  155  O   GLN A  23     2887   1302   2576     49   -130   -144       O  
ATOM    156  CB  GLN A  23      45.771  -1.050  21.262  1.00 18.41           C  
ANISOU  156  CB  GLN A  23     2959   1392   2641      7   -164   -128       C  
ATOM    157  CG  GLN A  23      44.339  -1.190  20.868  1.00 18.66           C  
ANISOU  157  CG  GLN A  23     2984   1431   2674    -20   -180   -109       C  
ATOM    158  CD  GLN A  23      44.082  -2.461  20.087  1.00 19.49           C  
ANISOU  158  CD  GLN A  23     3114   1523   2765    -30   -213   -134       C  
ATOM    159  OE1 GLN A  23      44.606  -2.644  18.981  1.00 19.09           O  
ANISOU  159  OE1 GLN A  23     3072   1488   2692    -17   -219   -159       O  
ATOM    160  NE2 GLN A  23      43.246  -3.322  20.652  1.00 20.72           N  
ANISOU  160  NE2 GLN A  23     3283   1654   2936    -55   -236   -126       N  
ATOM    161  N   ASP A  24      48.536  -2.827  22.625  1.00 18.04           N  
ANISOU  161  N   ASP A  24     2962   1291   2600     56   -166   -186       N  
ATOM    162  CA  ASP A  24      49.917  -2.665  22.978  1.00 17.62           C  
ANISOU  162  CA  ASP A  24     2909   1241   2544     83   -150   -198       C  
ATOM    163  C   ASP A  24      50.681  -1.753  21.958  1.00 17.38           C  
ANISOU  163  C   ASP A  24     2861   1252   2490    102   -132   -202       C  
ATOM    164  O   ASP A  24      51.575  -0.990  22.339  1.00 16.90           O  
ANISOU  164  O   ASP A  24     2786   1205   2430    114   -111   -194       O  
ATOM    165  CB  ASP A  24      50.570  -4.031  23.242  1.00 18.60           C  
ANISOU  165  CB  ASP A  24     3063   1334   2669     98   -167   -226       C  
ATOM    166  CG  ASP A  24      50.622  -4.922  22.060  1.00 19.31           C  
ANISOU  166  CG  ASP A  24     3175   1423   2739    108   -189   -258       C  
ATOM    167  OD1 ASP A  24      50.061  -4.576  20.945  1.00 19.11           O  
ANISOU  167  OD1 ASP A  24     3141   1423   2696    101   -193   -259       O  
ATOM    168  OD2 ASP A  24      51.255  -6.050  22.270  1.00 19.61           O  
ANISOU  168  OD2 ASP A  24     3239   1432   2778    126   -204   -283       O  
ATOM    169  N   ASN A  25      50.302  -1.815  20.680  1.00 17.09           N  
ANISOU  169  N   ASN A  25     2823   1236   2432    101   -142   -211       N  
ATOM    170  CA  ASN A  25      50.961  -1.039  19.676  1.00 17.63           C  
ANISOU  170  CA  ASN A  25     2872   1346   2477    116   -128   -211       C  
ATOM    171  C   ASN A  25      50.670   0.432  19.858  1.00 16.82           C  
ANISOU  171  C   ASN A  25     2741   1265   2385    104   -108   -176       C  
ATOM    172  O   ASN A  25      51.464   1.246  19.392  1.00 16.91           O  
ANISOU  172  O   ASN A  25     2734   1307   2383    117    -93   -169       O  
ATOM    173  CB  ASN A  25      50.482  -1.441  18.261  1.00 18.60           C  
ANISOU  173  CB  ASN A  25     3001   1491   2575    115   -145   -227       C  
ATOM    174  CG  ASN A  25      48.968  -1.496  18.131  1.00 19.28           C  
ANISOU  174  CG  ASN A  25     3087   1568   2671     83   -160   -212       C  
ATOM    175  OD1 ASN A  25      48.280  -2.180  18.898  1.00 20.82           O  
ANISOU  175  OD1 ASN A  25     3297   1727   2885     66   -175   -210       O  
ATOM    176  ND2 ASN A  25      48.416  -0.701  17.230  1.00 19.83           N  
ANISOU  176  ND2 ASN A  25     3134   1671   2727     73   -156   -194       N  
ATOM    177  N   GLN A  26      49.524   0.750  20.444  1.00 16.29           N  
ANISOU  177  N   GLN A  26     2669   1182   2339     80   -109   -153       N  
ATOM    178  CA  GLN A  26      49.204   2.218  20.568  1.00 15.53           C  
ANISOU  178  CA  GLN A  26     2544   1102   2252     72    -90   -120       C  
ATOM    179  C   GLN A  26      49.764   2.808  21.849  1.00 15.79           C  
ANISOU  179  C   GLN A  26     2574   1118   2304     76    -73   -110       C  
ATOM    180  O   GLN A  26      49.941   4.033  21.917  1.00 15.71           O  
ANISOU  180  O   GLN A  26     2546   1122   2300     76    -58    -89       O  
ATOM    181  CB  GLN A  26      47.703   2.428  20.518  1.00 15.44           C  
ANISOU  181  CB  GLN A  26     2525   1089   2251     48    -97    -99       C  
ATOM    182  CG  GLN A  26      47.178   2.164  19.115  1.00 15.81           C  
ANISOU  182  CG  GLN A  26     2569   1161   2276     42   -111   -104       C  
ATOM    183  CD  GLN A  26      45.740   2.499  18.940  1.00 16.32           C  
ANISOU  183  CD  GLN A  26     2620   1231   2348     19   -117    -78       C  
ATOM    184  OE1 GLN A  26      44.873   1.602  18.886  1.00 17.47           O  
ANISOU  184  OE1 GLN A  26     2778   1365   2494      2   -138    -82       O  
ATOM    185  NE2 GLN A  26      45.444   3.815  18.896  1.00 16.02           N  
ANISOU  185  NE2 GLN A  26     2556   1210   2318     18   -100    -48       N  
ATOM    186  N   PHE A  27      49.868   2.033  22.900  1.00 15.73           N  
ANISOU  186  N   PHE A  27     2583   1082   2309     76    -78   -120       N  
ATOM    187  CA  PHE A  27      50.451   2.467  24.149  1.00 14.98           C  
ANISOU  187  CA  PHE A  27     2487    973   2230     80    -64   -113       C  
ATOM    188  C   PHE A  27      51.924   2.859  24.005  1.00 15.68           C  
ANISOU  188  C   PHE A  27     2570   1077   2307     98    -52   -120       C  
ATOM    189  O   PHE A  27      52.463   3.709  24.742  1.00 15.08           O  
ANISOU  189  O   PHE A  27     2486   1000   2241     99    -38   -107       O  
ATOM    190  CB  PHE A  27      50.274   1.386  25.217  1.00 15.02           C  
ANISOU  190  CB  PHE A  27     2511    947   2249     75    -74   -122       C  
ATOM    191  CG  PHE A  27      50.643   1.873  26.587  1.00 14.63           C  
ANISOU  191  CG  PHE A  27     2457    884   2214     75    -60   -112       C  
ATOM    192  CD1 PHE A  27      49.831   2.792  27.296  1.00 14.44           C  
ANISOU  192  CD1 PHE A  27     2421    859   2204     64    -49    -89       C  
ATOM    193  CD2 PHE A  27      51.820   1.478  27.167  1.00 14.72           C  
ANISOU  193  CD2 PHE A  27     2477    888   2224     89    -57   -124       C  
ATOM    194  CE1 PHE A  27      50.209   3.208  28.575  1.00 13.92           C  
ANISOU  194  CE1 PHE A  27     2354    783   2150     66    -37    -84       C  
ATOM    195  CE2 PHE A  27      52.186   1.938  28.419  1.00 14.90           C  
ANISOU  195  CE2 PHE A  27     2498    903   2260     88    -45   -115       C  
ATOM    196  CZ  PHE A  27      51.380   2.826  29.089  1.00 14.07           C  
ANISOU  196  CZ  PHE A  27     2382    796   2166     76    -35    -96       C  
ATOM    197  N   HIS A  28      52.597   2.180  23.084  1.00 16.09           N  
ANISOU  197  N   HIS A  28     2629   1145   2339    114    -60   -140       N  
ATOM    198  CA  HIS A  28      53.916   2.443  22.709  1.00 16.06           C  
ANISOU  198  CA  HIS A  28     2617   1165   2318    133    -51   -145       C  
ATOM    199  C   HIS A  28      54.221   3.960  22.534  1.00 15.66           C  
ANISOU  199  C   HIS A  28     2541   1138   2269    127    -35   -118       C  
ATOM    200  O   HIS A  28      53.367   4.693  21.952  1.00 16.91           O  
ANISOU  200  O   HIS A  28     2687   1307   2429    114    -34   -101       O  
ATOM    201  CB  HIS A  28      54.211   1.659  21.406  1.00 18.10           C  
ANISOU  201  CB  HIS A  28     2882   1446   2549    150    -61   -168       C  
ATOM    202  CG  HIS A  28      55.442   2.104  20.709  1.00 19.18           C  
ANISOU  202  CG  HIS A  28     3002   1623   2663    169    -51   -168       C  
ATOM    203  ND1 HIS A  28      56.660   1.490  20.888  1.00 20.95           N  
ANISOU  203  ND1 HIS A  28     3231   1852   2874    194    -48   -184       N  
ATOM    204  CD2 HIS A  28      55.641   3.055  19.754  1.00 20.55           C  
ANISOU  204  CD2 HIS A  28     3151   1836   2820    169    -43   -150       C  
ATOM    205  CE1 HIS A  28      57.575   2.094  20.146  1.00 21.21           C  
ANISOU  205  CE1 HIS A  28     3243   1930   2885    207    -38   -176       C  
ATOM    206  NE2 HIS A  28      56.972   3.019  19.416  1.00 21.78           N  
ANISOU  206  NE2 HIS A  28     3297   2023   2954    191    -36   -155       N  
ATOM    207  N   GLY A  29      55.373   4.369  23.023  1.00 15.28           N  
ANISOU  207  N   GLY A  29     2486   1097   2220    135    -25   -113       N  
ATOM    208  CA  GLY A  29      55.880   5.736  22.852  1.00 15.11           C  
ANISOU  208  CA  GLY A  29     2443   1097   2199    129    -14    -88       C  
ATOM    209  C   GLY A  29      56.136   6.457  24.125  1.00 14.43           C  
ANISOU  209  C   GLY A  29     2358    989   2134    119     -6    -75       C  
ATOM    210  O   GLY A  29      56.250   5.897  25.205  1.00 13.99           O  
ANISOU  210  O   GLY A  29     2317    909   2089    120     -6    -85       O  
ATOM    211  N   LYS A  30      56.161   7.801  24.004  1.00 14.39           N  
ANISOU  211  N   LYS A  30     2338    992   2137    108      0    -50       N  
ATOM    212  CA  LYS A  30      56.544   8.641  25.131  1.00 14.38           C  
ANISOU  212  CA  LYS A  30     2337    972   2153     99      6    -38       C  
ATOM    213  C   LYS A  30      55.338   9.134  25.877  1.00 13.22           C  
ANISOU  213  C   LYS A  30     2198    795   2030     88      7    -33       C  
ATOM    214  O   LYS A  30      54.366   9.556  25.279  1.00 13.49           O  
ANISOU  214  O   LYS A  30     2225    830   2068     83      6    -23       O  
ATOM    215  CB  LYS A  30      57.319   9.856  24.626  1.00 15.70           C  
ANISOU  215  CB  LYS A  30     2485   1161   2317     92      8    -14       C  
ATOM    216  CG  LYS A  30      57.846  10.732  25.738  1.00 17.03           C  
ANISOU  216  CG  LYS A  30     2657   1310   2502     80     11     -3       C  
ATOM    217  CD  LYS A  30      58.527  12.006  25.163  1.00 18.22           C  
ANISOU  217  CD  LYS A  30     2789   1480   2652     69      9     25       C  
ATOM    218  CE  LYS A  30      59.274  12.759  26.237  1.00 20.14           C  
ANISOU  218  CE  LYS A  30     3038   1705   2908     56      8     33       C  
ATOM    219  NZ  LYS A  30      60.500  12.106  26.741  1.00 20.89           N  
ANISOU  219  NZ  LYS A  30     3132   1814   2989     61      9     25       N  
ATOM    220  N   TRP A  31      55.466   9.063  27.184  1.00 12.64           N  
ANISOU  220  N   TRP A  31     2137    697   1969     85     11    -40       N  
ATOM    221  CA  TRP A  31      54.441   9.443  28.144  1.00 12.56           C  
ANISOU  221  CA  TRP A  31     2134    659   1977     79     14    -37       C  
ATOM    222  C   TRP A  31      55.046  10.374  29.212  1.00 12.23           C  
ANISOU  222  C   TRP A  31     2096    602   1946     73     19    -32       C  
ATOM    223  O   TRP A  31      56.083  10.066  29.773  1.00 12.24           O  
ANISOU  223  O   TRP A  31     2101    606   1942     74     19    -39       O  
ATOM    224  CB  TRP A  31      53.869   8.172  28.743  1.00 12.30           C  
ANISOU  224  CB  TRP A  31     2113    614   1945     82     11    -54       C  
ATOM    225  CG  TRP A  31      52.965   7.428  27.777  1.00 12.31           C  
ANISOU  225  CG  TRP A  31     2114    623   1939     82      3    -57       C  
ATOM    226  CD1 TRP A  31      53.186   6.139  27.152  1.00 12.55           C  
ANISOU  226  CD1 TRP A  31     2151    661   1955     89     -6    -73       C  
ATOM    227  CD2 TRP A  31      51.623   7.733  27.478  1.00 12.29           C  
ANISOU  227  CD2 TRP A  31     2106    619   1945     76      2    -46       C  
ATOM    228  NE1 TRP A  31      52.105   5.787  26.474  1.00 12.37           N  
ANISOU  228  NE1 TRP A  31     2127    640   1930     84    -14    -72       N  
ATOM    229  CE2 TRP A  31      51.122   6.752  26.622  1.00 12.55           C  
ANISOU  229  CE2 TRP A  31     2140    659   1966     75     -8    -53       C  
ATOM    230  CE3 TRP A  31      50.793   8.821  27.761  1.00 12.21           C  
ANISOU  230  CE3 TRP A  31     2088    602   1948     72      9    -29       C  
ATOM    231  CZ2 TRP A  31      49.810   6.790  26.124  1.00 12.68           C  
ANISOU  231  CZ2 TRP A  31     2151    680   1986     67    -13    -43       C  
ATOM    232  CZ3 TRP A  31      49.511   8.852  27.254  1.00 12.35           C  
ANISOU  232  CZ3 TRP A  31     2099    625   1969     68      6    -18       C  
ATOM    233  CH2 TRP A  31      49.018   7.857  26.441  1.00 12.82           C  
ANISOU  233  CH2 TRP A  31     2158    694   2017     64     -4    -23       C  
ATOM    234  N   TYR A  32      54.538  11.625  29.361  1.00 12.40           N  
ANISOU  234  N   TYR A  32     2115    611   1982     68     22    -19       N  
ATOM    235  CA  TYR A  32      54.948  12.520  30.415  1.00 12.56           C  
ANISOU  235  CA  TYR A  32     2144    613   2014     62     24    -18       C  
ATOM    236  C   TYR A  32      54.254  12.292  31.705  1.00 11.73           C  
ANISOU  236  C   TYR A  32     2052    488   1916     66     29    -30       C  
ATOM    237  O   TYR A  32      53.056  12.007  31.707  1.00 11.76           O  
ANISOU  237  O   TYR A  32     2055    488   1924     71     32    -31       O  
ATOM    238  CB  TYR A  32      54.703  13.972  29.972  1.00 12.80           C  
ANISOU  238  CB  TYR A  32     2170    636   2058     57     23      0       C  
ATOM    239  CG  TYR A  32      55.575  14.417  28.833  1.00 13.82           C  
ANISOU  239  CG  TYR A  32     2285    787   2179     50     16     18       C  
ATOM    240  CD1 TYR A  32      56.835  14.987  29.096  1.00 14.99           C  
ANISOU  240  CD1 TYR A  32     2432    937   2326     39     11     26       C  
ATOM    241  CD2 TYR A  32      55.079  14.478  27.562  1.00 14.22           C  
ANISOU  241  CD2 TYR A  32     2320    856   2225     51     15     31       C  
ATOM    242  CE1 TYR A  32      57.628  15.450  28.071  1.00 15.46           C  
ANISOU  242  CE1 TYR A  32     2474   1021   2377     31      5     47       C  
ATOM    243  CE2 TYR A  32      55.887  14.964  26.501  1.00 14.97           C  
ANISOU  243  CE2 TYR A  32     2397    976   2311     44      9     52       C  
ATOM    244  CZ  TYR A  32      57.163  15.449  26.778  1.00 15.46           C  
ANISOU  244  CZ  TYR A  32     2458   1043   2372     34      4     61       C  
ATOM    245  OH  TYR A  32      57.978  15.861  25.732  1.00 17.40           O  
ANISOU  245  OH  TYR A  32     2683   1320   2606     26     -1     84       O  
ATOM    246  N   VAL A  33      54.980  12.349  32.798  1.00 11.63           N  
ANISOU  246  N   VAL A  33     2048    466   1903     62     30    -39       N  
ATOM    247  CA  VAL A  33      54.377  12.176  34.128  1.00 11.70           C  
ANISOU  247  CA  VAL A  33     2068    460   1917     66     36    -51       C  
ATOM    248  C   VAL A  33      53.590  13.369  34.472  1.00 12.10           C  
ANISOU  248  C   VAL A  33     2123    493   1981     69     40    -47       C  
ATOM    249  O   VAL A  33      54.188  14.492  34.510  1.00 12.21           O  
ANISOU  249  O   VAL A  33     2142    495   2001     64     36    -43       O  
ATOM    250  CB  VAL A  33      55.376  11.837  35.223  1.00 11.38           C  
ANISOU  250  CB  VAL A  33     2035    418   1870     61     35    -61       C  
ATOM    251  CG1 VAL A  33      54.710  11.710  36.507  1.00 11.20           C  
ANISOU  251  CG1 VAL A  33     2021    385   1850     65     41    -71       C  
ATOM    252  CG2 VAL A  33      56.198  10.569  34.865  1.00 11.39           C  
ANISOU  252  CG2 VAL A  33     2031    436   1859     62     31    -64       C  
ATOM    253  N   VAL A  34      52.305  13.256  34.796  1.00 11.86           N  
ANISOU  253  N   VAL A  34     2092    459   1954     79     46    -49       N  
ATOM    254  CA  VAL A  34      51.463  14.442  35.178  1.00 11.90           C  
ANISOU  254  CA  VAL A  34     2102    448   1971     89     51    -47       C  
ATOM    255  C   VAL A  34      50.986  14.357  36.615  1.00 12.00           C  
ANISOU  255  C   VAL A  34     2123    455   1981     97     59    -60       C  
ATOM    256  O   VAL A  34      50.991  15.310  37.353  1.00 12.97           O  
ANISOU  256  O   VAL A  34     2257    562   2109    104     61    -69       O  
ATOM    257  CB  VAL A  34      50.287  14.649  34.238  1.00 11.88           C  
ANISOU  257  CB  VAL A  34     2087    451   1975     96     53    -32       C  
ATOM    258  CG1 VAL A  34      49.268  15.726  34.685  1.00 11.99           C  
ANISOU  258  CG1 VAL A  34     2103    449   2000    112     60    -30       C  
ATOM    259  CG2 VAL A  34      50.820  14.851  32.833  1.00 11.78           C  
ANISOU  259  CG2 VAL A  34     2065    446   1962     87     46    -18       C  
ATOM    260  N   GLY A  35      50.608  13.132  37.065  1.00 11.85           N  
ANISOU  260  N   GLY A  35     2097    450   1952     97     61    -63       N  
ATOM    261  CA  GLY A  35      50.205  12.927  38.441  1.00 12.19           C  
ANISOU  261  CA  GLY A  35     2145    496   1989    104     68    -73       C  
ATOM    262  C   GLY A  35      50.912  11.686  38.953  1.00 12.50           C  
ANISOU  262  C   GLY A  35     2184    545   2018     93     64    -78       C  
ATOM    263  O   GLY A  35      51.154  10.795  38.148  1.00 13.16           O  
ANISOU  263  O   GLY A  35     2263    636   2101     86     57    -72       O  
ATOM    264  N   ARG A  36      51.209  11.667  40.248  1.00 12.76           N  
ANISOU  264  N   ARG A  36     2224    579   2044     93     67    -88       N  
ATOM    265  CA  ARG A  36      51.797  10.437  40.901  1.00 12.60           C  
ANISOU  265  CA  ARG A  36     2202    569   2015     84     64    -90       C  
ATOM    266  C   ARG A  36      51.140  10.232  42.227  1.00 12.67           C  
ANISOU  266  C   ARG A  36     2209    589   2015     90     71    -93       C  
ATOM    267  O   ARG A  36      50.821  11.120  42.982  1.00 12.63           O  
ANISOU  267  O   ARG A  36     2209    583   2007    100     78   -102       O  
ATOM    268  CB  ARG A  36      53.316  10.491  40.991  1.00 13.59           C  
ANISOU  268  CB  ARG A  36     2336    691   2137     74     58    -96       C  
ATOM    269  CG  ARG A  36      53.858  11.898  41.152  1.00 15.16           C  
ANISOU  269  CG  ARG A  36     2545    875   2338     73     58   -104       C  
ATOM    270  CD  ARG A  36      55.376  11.902  41.108  1.00 16.26           C  
ANISOU  270  CD  ARG A  36     2688   1014   2473     60     50   -105       C  
ATOM    271  NE  ARG A  36      55.964  11.036  42.152  1.00 17.47           N  
ANISOU  271  NE  ARG A  36     2842   1179   2616     55     49   -109       N  
ATOM    272  CZ  ARG A  36      57.234  10.748  42.326  1.00 18.86           C  
ANISOU  272  CZ  ARG A  36     3018   1362   2786     44     44   -108       C  
ATOM    273  NH1 ARG A  36      58.175  11.222  41.528  1.00 19.91           N  
ANISOU  273  NH1 ARG A  36     3150   1494   2921     37     37   -102       N  
ATOM    274  NH2 ARG A  36      57.556   9.963  43.372  1.00 19.95           N  
ANISOU  274  NH2 ARG A  36     3153   1510   2914     41     44   -110       N  
ATOM    275  N   ALA A  37      50.867   8.974  42.588  1.00 11.99           N  
ANISOU  275  N   ALA A  37     2114    516   1924     84     67    -84       N  
ATOM    276  CA  ALA A  37      50.345   8.726  43.881  1.00 12.08           C  
ANISOU  276  CA  ALA A  37     2120    544   1925     87     73    -83       C  
ATOM    277  C   ALA A  37      50.834   7.380  44.374  1.00 12.53           C  
ANISOU  277  C   ALA A  37     2172    609   1978     74     65    -76       C  
ATOM    278  O   ALA A  37      50.912   6.558  43.615  1.00 13.04           O  
ANISOU  278  O   ALA A  37     2236    669   2050     67     56    -68       O  
ATOM    279  CB  ALA A  37      48.841   8.671  43.801  1.00 12.01           C  
ANISOU  279  CB  ALA A  37     2098    549   1917     95     79    -70       C  
ATOM    280  N   GLY A  38      51.222   7.212  45.633  1.00 12.94           N  
ANISOU  280  N   GLY A  38     2224    672   2019     71     68    -79       N  
ATOM    281  CA  GLY A  38      51.599   5.845  46.085  1.00 13.24           C  
ANISOU  281  CA  GLY A  38     2256    718   2055     59     58    -67       C  
ATOM    282  C   GLY A  38      51.694   5.713  47.573  1.00 13.46           C  
ANISOU  282  C   GLY A  38     2279    766   2068     57     63    -66       C  
ATOM    283  O   GLY A  38      51.407   6.652  48.284  1.00 14.33           O  
ANISOU  283  O   GLY A  38     2390    886   2167     67     73    -77       O  
ATOM    284  N   ASN A  39      51.952   4.491  48.078  1.00 13.39           N  
ANISOU  284  N   ASN A  39     2263    765   2059     46     54    -51       N  
ATOM    285  CA  ASN A  39      51.981   4.362  49.542  1.00 13.90           C  
ANISOU  285  CA  ASN A  39     2319    854   2107     43     58    -47       C  
ATOM    286  C   ASN A  39      53.325   4.465  50.195  1.00 14.33           C  
ANISOU  286  C   ASN A  39     2380    909   2153     38     57    -57       C  
ATOM    287  O   ASN A  39      53.367   4.438  51.410  1.00 14.79           O  
ANISOU  287  O   ASN A  39     2431    990   2196     35     60    -55       O  
ATOM    288  CB  ASN A  39      51.271   3.061  49.949  1.00 13.59           C  
ANISOU  288  CB  ASN A  39     2262    830   2069     33     49    -20       C  
ATOM    289  CG  ASN A  39      52.053   1.845  49.562  1.00 13.54           C  
ANISOU  289  CG  ASN A  39     2261    807   2077     21     33     -9       C  
ATOM    290  OD1 ASN A  39      52.884   1.867  48.671  1.00 13.04           O  
ANISOU  290  OD1 ASN A  39     2211    721   2023     23     28    -21       O  
ATOM    291  ND2 ASN A  39      51.743   0.723  50.238  1.00 13.69           N  
ANISOU  291  ND2 ASN A  39     2266    837   2095      9     23     14       N  
ATOM    292  N   MET A  40      54.421   4.687  49.461  1.00 15.91           N  
ANISOU  292  N   MET A  40     2593   1089   2361     36     52    -67       N  
ATOM    293  CA  MET A  40      55.680   4.848  50.102  1.00 17.13           C  
ANISOU  293  CA  MET A  40     2752   1248   2507     29     51    -74       C  
ATOM    294  C   MET A  40      55.628   6.203  50.785  1.00 18.93           C  
ANISOU  294  C   MET A  40     2987   1483   2721     34     60    -93       C  
ATOM    295  O   MET A  40      54.946   7.105  50.286  1.00 21.46           O  
ANISOU  295  O   MET A  40     3315   1794   3045     44     66   -104       O  
ATOM    296  CB  MET A  40      56.825   4.785  49.073  1.00 18.50           C  
ANISOU  296  CB  MET A  40     2934   1403   2691     27     44    -77       C  
ATOM    297  CG  MET A  40      58.182   4.568  49.681  1.00 19.76           C  
ANISOU  297  CG  MET A  40     3093   1572   2843     19     39    -75       C  
ATOM    298  SD  MET A  40      59.503   4.733  48.511  1.00 21.10           S  
ANISOU  298  SD  MET A  40     3268   1728   3020     20     34    -78       S  
ATOM    299  CE  MET A  40      59.408   6.498  48.160  1.00 20.47           C  
ANISOU  299  CE  MET A  40     3201   1639   2938     19     39    -96       C  
ATOM    300  N   ARG A  41      56.194   6.294  51.976  1.00 20.49           N  
ANISOU  300  N   ARG A  41     3184   1698   2901     27     61    -96       N  
ATOM    301  CA  ARG A  41      56.293   7.601  52.645  1.00 24.05           C  
ANISOU  301  CA  ARG A  41     3647   2153   3338     31     67   -119       C  
ATOM    302  C   ARG A  41      57.535   8.294  52.106  1.00 26.00           C  
ANISOU  302  C   ARG A  41     3908   2379   3589     22     59   -130       C  
ATOM    303  O   ARG A  41      58.633   7.710  52.087  1.00 26.67           O  
ANISOU  303  O   ARG A  41     3989   2468   3675     10     52   -119       O  
ATOM    304  CB  ARG A  41      56.312   7.391  54.137  1.00 25.63           C  
ANISOU  304  CB  ARG A  41     3838   2383   3514     27     69   -119       C  
ATOM    305  CG  ARG A  41      55.015   6.693  54.606  1.00 25.80           C  
ANISOU  305  CG  ARG A  41     3841   2429   3530     35     76   -103       C  
ATOM    306  CD  ARG A  41      54.914   6.642  56.110  1.00 26.05           C  
ANISOU  306  CD  ARG A  41     3863   2497   3534     34     80   -103       C  
ATOM    307  NE  ARG A  41      53.702   5.991  56.574  1.00 26.54           N  
ANISOU  307  NE  ARG A  41     3904   2589   3589     40     86    -84       N  
ATOM    308  CZ  ARG A  41      53.611   4.676  56.821  1.00 25.70           C  
ANISOU  308  CZ  ARG A  41     3779   2498   3487     27     79    -52       C  
ATOM    309  NH1 ARG A  41      54.650   3.875  56.627  1.00 25.25           N  
ANISOU  309  NH1 ARG A  41     3723   2428   3442     12     67    -40       N  
ATOM    310  NH2 ARG A  41      52.465   4.176  57.251  1.00 25.50           N  
ANISOU  310  NH2 ARG A  41     3732   2500   3454     31     82    -32       N  
ATOM    311  N   LEU A  42      57.363   9.540  51.696  1.00 31.10           N  
ANISOU  311  N   LEU A  42     4570   3007   4240     28     61   -147       N  
ATOM    312  CA  LEU A  42      58.368  10.273  50.957  1.00 32.09           C  
ANISOU  312  CA  LEU A  42     4707   3111   4373     18     53   -153       C  
ATOM    313  C   LEU A  42      58.838  11.421  51.814  1.00 34.34           C  
ANISOU  313  C   LEU A  42     5009   3394   4645     12     49   -173       C  
ATOM    314  O   LEU A  42      58.029  12.232  52.231  1.00 32.73           O  
ANISOU  314  O   LEU A  42     4815   3184   4435     25     55   -191       O  
ATOM    315  CB  LEU A  42      57.743  10.816  49.660  1.00 32.90           C  
ANISOU  315  CB  LEU A  42     4815   3191   4495     29     55   -153       C  
ATOM    316  CG  LEU A  42      56.919   9.789  48.859  1.00 31.80           C  
ANISOU  316  CG  LEU A  42     4660   3054   4366     38     58   -137       C  
ATOM    317  CD1 LEU A  42      55.510  10.319  48.569  1.00 31.96           C  
ANISOU  317  CD1 LEU A  42     4682   3069   4392     54     67   -142       C  
ATOM    318  CD2 LEU A  42      57.612   9.326  47.571  1.00 31.81           C  
ANISOU  318  CD2 LEU A  42     4659   3046   4381     32     51   -125       C  
ATOM    319  N   ARG A  43      60.141  11.496  52.059  1.00 36.12           N  
ANISOU  319  N   ARG A  43     5237   3622   4864     -6     39   -170       N  
ATOM    320  CA  ARG A  43      60.694  12.534  52.901  1.00 37.52           C  
ANISOU  320  CA  ARG A  43     5431   3796   5027    -18     31   -189       C  
ATOM    321  C   ARG A  43      60.269  13.915  52.351  1.00 38.31           C  
ANISOU  321  C   ARG A  43     5553   3864   5139    -11     28   -207       C  
ATOM    322  O   ARG A  43      60.260  14.136  51.125  1.00 38.34           O  
ANISOU  322  O   ARG A  43     5556   3847   5162    -10     26   -198       O  
ATOM    323  CB  ARG A  43      62.216  12.399  53.043  1.00 38.56           C  
ANISOU  323  CB  ARG A  43     5560   3937   5154    -43     18   -178       C  
ATOM    324  CG  ARG A  43      62.995  12.553  51.748  1.00 38.36           C  
ANISOU  324  CG  ARG A  43     5531   3896   5145    -52     10   -162       C  
ATOM    325  CD  ARG A  43      64.477  12.300  51.951  1.00 38.83           C  
ANISOU  325  CD  ARG A  43     5583   3974   5196    -74      0   -147       C  
ATOM    326  NE  ARG A  43      65.268  12.944  50.906  1.00 37.73           N  
ANISOU  326  NE  ARG A  43     5444   3821   5067    -87    -10   -136       N  
ATOM    327  CZ  ARG A  43      66.574  12.803  50.689  1.00 38.43           C  
ANISOU  327  CZ  ARG A  43     5522   3926   5153   -105    -20   -116       C  
ATOM    328  NH1 ARG A  43      67.315  11.966  51.406  1.00 39.35           N  
ANISOU  328  NH1 ARG A  43     5625   4071   5255   -112    -21   -104       N  
ATOM    329  NH2 ARG A  43      67.142  13.489  49.690  1.00 38.15           N  
ANISOU  329  NH2 ARG A  43     5488   3881   5127   -116    -30   -105       N  
ATOM    330  N   GLU A  44      59.874  14.812  53.247  1.00 40.09           N  
ANISOU  330  N   GLU A  44     5797   4083   5351     -4     28   -233       N  
ATOM    331  CA  GLU A  44      59.504  16.180  52.843  1.00 40.65           C  
ANISOU  331  CA  GLU A  44     5891   4118   5433      3     22   -252       C  
ATOM    332  C   GLU A  44      60.764  16.796  52.267  1.00 38.84           C  
ANISOU  332  C   GLU A  44     5672   3869   5214    -24      3   -245       C  
ATOM    333  O   GLU A  44      61.775  16.862  52.956  1.00 40.16           O  
ANISOU  333  O   GLU A  44     5843   4045   5367    -46     -7   -246       O  
ATOM    334  CB  GLU A  44      59.018  17.017  54.034  1.00 44.15           C  
ANISOU  334  CB  GLU A  44     6356   4559   5857     15     23   -285       C  
ATOM    335  CG  GLU A  44      57.767  16.492  54.757  1.00 46.41           C  
ANISOU  335  CG  GLU A  44     6631   4874   6129     44     43   -293       C  
ATOM    336  CD  GLU A  44      56.450  16.769  54.031  1.00 49.25           C  
ANISOU  336  CD  GLU A  44     6988   5219   6502     73     55   -293       C  
ATOM    337  OE1 GLU A  44      56.393  17.695  53.175  1.00 48.87           O  
ANISOU  337  OE1 GLU A  44     6956   5135   6475     76     48   -298       O  
ATOM    338  OE2 GLU A  44      55.455  16.060  54.335  1.00 49.24           O  
ANISOU  338  OE2 GLU A  44     6969   5248   6493     92     71   -286       O  
ATOM    339  N   ASP A  45      60.741  17.174  50.990  1.00 36.60           N  
ANISOU  339  N   ASP A  45     5388   3562   4953    -24      0   -232       N  
ATOM    340  CA  ASP A  45      61.931  17.712  50.378  1.00 32.68           C  
ANISOU  340  CA  ASP A  45     4896   3053   4466    -51    -18   -218       C  
ATOM    341  C   ASP A  45      61.617  19.015  49.685  1.00 31.61           C  
ANISOU  341  C   ASP A  45     4781   2878   4350    -49    -29   -225       C  
ATOM    342  O   ASP A  45      60.693  19.117  48.911  1.00 30.54           O  
ANISOU  342  O   ASP A  45     4643   2730   4229    -29    -19   -222       O  
ATOM    343  CB  ASP A  45      62.572  16.791  49.340  1.00 34.11           C  
ANISOU  343  CB  ASP A  45     5051   3252   4654    -60    -17   -187       C  
ATOM    344  CG  ASP A  45      63.919  17.312  48.923  1.00 34.93           C  
ANISOU  344  CG  ASP A  45     5156   3354   4762    -89    -36   -170       C  
ATOM    345  OD1 ASP A  45      64.632  17.786  49.817  1.00 38.83           O  
ANISOU  345  OD1 ASP A  45     5661   3847   5243   -109    -49   -179       O  
ATOM    346  OD2 ASP A  45      64.248  17.334  47.736  1.00 37.25           O  
ANISOU  346  OD2 ASP A  45     5437   3645   5068    -94    -39   -149       O  
ATOM    347  N   LYS A  46      62.475  19.979  49.911  1.00 30.33           N  
ANISOU  347  N   LYS A  46     4638   2695   4188    -74    -50   -230       N  
ATOM    348  CA  LYS A  46      62.264  21.306  49.354  1.00 29.64           C  
ANISOU  348  CA  LYS A  46     4574   2565   4121    -75    -64   -236       C  
ATOM    349  C   LYS A  46      62.858  21.414  47.929  1.00 28.67           C  
ANISOU  349  C   LYS A  46     4436   2439   4018    -92    -74   -201       C  
ATOM    350  O   LYS A  46      62.754  22.457  47.287  1.00 27.33           O  
ANISOU  350  O   LYS A  46     4280   2235   3868    -97    -87   -197       O  
ATOM    351  CB  LYS A  46      62.811  22.325  50.345  1.00 31.56           C  
ANISOU  351  CB  LYS A  46     4849   2786   4357    -94    -86   -259       C  
ATOM    352  CG  LYS A  46      62.127  22.199  51.706  1.00 32.99           C  
ANISOU  352  CG  LYS A  46     5043   2975   4514    -72    -75   -295       C  
ATOM    353  CD  LYS A  46      62.257  23.420  52.613  1.00 33.72           C  
ANISOU  353  CD  LYS A  46     5175   3035   4600    -78    -95   -329       C  
ATOM    354  CE  LYS A  46      61.077  23.614  53.590  1.00 34.11           C  
ANISOU  354  CE  LYS A  46     5242   3084   4634    -39    -80   -368       C  
ATOM    355  NZ  LYS A  46      60.662  25.066  53.755  1.00 34.31           N  
ANISOU  355  NZ  LYS A  46     5308   3056   4670    -26    -96   -400       N  
ATOM    356  N   ASP A  47      63.400  20.311  47.389  1.00 26.34           N  
ANISOU  356  N   ASP A  47     4110   2178   3717    -98    -65   -175       N  
ATOM    357  CA  ASP A  47      63.895  20.295  46.018  1.00 26.16           C  
ANISOU  357  CA  ASP A  47     4068   2161   3708   -109    -70   -144       C  
ATOM    358  C   ASP A  47      63.933  18.857  45.499  1.00 24.04           C  
ANISOU  358  C   ASP A  47     3770   1931   3432    -97    -53   -127       C  
ATOM    359  O   ASP A  47      64.994  18.361  45.186  1.00 23.89           O  
ANISOU  359  O   ASP A  47     3732   1938   3406   -113    -57   -106       O  
ATOM    360  CB  ASP A  47      65.262  20.965  45.891  1.00 28.26           C  
ANISOU  360  CB  ASP A  47     4336   2425   3974   -147    -96   -124       C  
ATOM    361  CG  ASP A  47      65.658  21.248  44.444  1.00 29.63           C  
ANISOU  361  CG  ASP A  47     4493   2602   4163   -157   -103    -91       C  
ATOM    362  OD1 ASP A  47      64.855  21.026  43.511  1.00 31.23           O  
ANISOU  362  OD1 ASP A  47     4685   2803   4376   -136    -90    -85       O  
ATOM    363  OD2 ASP A  47      66.803  21.699  44.235  1.00 33.65           O  
ANISOU  363  OD2 ASP A  47     4997   3118   4671   -189   -123    -68       O  
ATOM    364  N   PRO A  48      62.767  18.267  45.355  1.00 23.42           N  
ANISOU  364  N   PRO A  48     3687   1855   3357    -69    -34   -136       N  
ATOM    365  CA  PRO A  48      62.716  16.820  45.055  1.00 21.66           C  
ANISOU  365  CA  PRO A  48     3439   1663   3125    -57    -19   -126       C  
ATOM    366  C   PRO A  48      63.159  16.435  43.642  1.00 20.82           C  
ANISOU  366  C   PRO A  48     3312   1571   3026    -58    -20   -100       C  
ATOM    367  O   PRO A  48      63.001  17.191  42.711  1.00 22.08           O  
ANISOU  367  O   PRO A  48     3473   1716   3198    -61    -25    -91       O  
ATOM    368  CB  PRO A  48      61.251  16.493  45.287  1.00 23.05           C  
ANISOU  368  CB  PRO A  48     3619   1833   3305    -29     -3   -142       C  
ATOM    369  CG  PRO A  48      60.515  17.709  44.978  1.00 23.35           C  
ANISOU  369  CG  PRO A  48     3674   1839   3357    -22     -7   -151       C  
ATOM    370  CD  PRO A  48      61.417  18.850  45.391  1.00 24.20           C  
ANISOU  370  CD  PRO A  48     3800   1926   3465    -45    -26   -155       C  
ATOM    371  N   ALA A  49      63.719  15.219  43.511  1.00 18.46           N  
ANISOU  371  N   ALA A  49     2995   1302   2717    -55    -14    -90       N  
ATOM    372  CA  ALA A  49      63.944  14.674  42.176  1.00 17.98           C  
ANISOU  372  CA  ALA A  49     2914   1257   2657    -49    -11    -71       C  
ATOM    373  C   ALA A  49      62.648  14.363  41.530  1.00 16.55           C  
ANISOU  373  C   ALA A  49     2733   1068   2487    -27      0    -77       C  
ATOM    374  O   ALA A  49      61.633  14.107  42.188  1.00 17.14           O  
ANISOU  374  O   ALA A  49     2816   1132   2562    -14      8    -93       O  
ATOM    375  CB  ALA A  49      64.841  13.438  42.246  1.00 17.48           C  
ANISOU  375  CB  ALA A  49     2833   1226   2580    -46     -8    -61       C  
ATOM    376  N   LYS A  50      62.642  14.417  40.221  1.00 16.66           N  
ANISOU  376  N   LYS A  50     2736   1088   2506    -24      0    -63       N  
ATOM    377  CA  LYS A  50      61.382  14.311  39.470  1.00 17.27           C  
ANISOU  377  CA  LYS A  50     2812   1155   2593     -7      7    -66       C  
ATOM    378  C   LYS A  50      61.433  13.078  38.493  1.00 16.53           C  
ANISOU  378  C   LYS A  50     2701   1086   2493      5     12    -59       C  
ATOM    379  O   LYS A  50      62.487  12.744  37.950  1.00 15.15           O  
ANISOU  379  O   LYS A  50     2513    932   2308      2      8    -47       O  
ATOM    380  CB  LYS A  50      61.061  15.619  38.786  1.00 18.54           C  
ANISOU  380  CB  LYS A  50     2978   1297   2768    -12      0    -58       C  
ATOM    381  CG  LYS A  50      60.336  16.598  39.760  1.00 19.07           C  
ANISOU  381  CG  LYS A  50     3067   1332   2844    -11      0    -75       C  
ATOM    382  CD  LYS A  50      60.247  17.982  39.209  1.00 20.23           C  
ANISOU  382  CD  LYS A  50     3223   1455   3007    -19    -11    -66       C  
ATOM    383  CE  LYS A  50      59.706  18.914  40.285  1.00 21.24           C  
ANISOU  383  CE  LYS A  50     3376   1551   3142    -16    -14    -87       C  
ATOM    384  NZ  LYS A  50      58.295  18.629  40.622  1.00 22.00           N  
ANISOU  384  NZ  LYS A  50     3476   1641   3240      9      0   -103       N  
ATOM    385  N   MET A  51      60.293  12.438  38.305  1.00 16.38           N  
ANISOU  385  N   MET A  51     2683   1062   2478     21     20    -67       N  
ATOM    386  CA  MET A  51      60.098  11.448  37.279  1.00 18.10           C  
ANISOU  386  CA  MET A  51     2889   1294   2691     33     23    -64       C  
ATOM    387  C   MET A  51      59.430  12.225  36.166  1.00 16.64           C  
ANISOU  387  C   MET A  51     2701   1104   2515     34     22    -55       C  
ATOM    388  O   MET A  51      58.258  12.712  36.302  1.00 16.17           O  
ANISOU  388  O   MET A  51     2648   1027   2466     39     26    -59       O  
ATOM    389  CB  MET A  51      59.247  10.272  37.789  1.00 19.94           C  
ANISOU  389  CB  MET A  51     3125   1524   2924     44     28    -75       C  
ATOM    390  CG  MET A  51      59.011   9.189  36.729  1.00 22.63           C  
ANISOU  390  CG  MET A  51     3459   1876   3261     56     27    -74       C  
ATOM    391  SD  MET A  51      60.470   8.356  35.975  1.00 26.30           S  
ANISOU  391  SD  MET A  51     3913   2367   3711     63     23    -70       S  
ATOM    392  CE  MET A  51      59.671   7.445  34.665  1.00 27.94           C  
ANISOU  392  CE  MET A  51     4119   2578   3917     77     21    -75       C  
ATOM    393  N   VAL A  52      60.199  12.428  35.105  1.00 15.60           N  
ANISOU  393  N   VAL A  52     2556    990   2378     31     17    -41       N  
ATOM    394  CA  VAL A  52      59.823  13.261  34.027  1.00 15.83           C  
ANISOU  394  CA  VAL A  52     2579   1020   2414     28     15    -28       C  
ATOM    395  C   VAL A  52      58.895  12.611  33.036  1.00 14.76           C  
ANISOU  395  C   VAL A  52     2437    892   2277     42     19    -29       C  
ATOM    396  O   VAL A  52      57.893  13.205  32.588  1.00 14.53           O  
ANISOU  396  O   VAL A  52     2408    852   2259     43     20    -24       O  
ATOM    397  CB  VAL A  52      61.024  13.825  33.192  1.00 16.56           C  
ANISOU  397  CB  VAL A  52     2657   1135   2500     17      7     -6       C  
ATOM    398  CG1 VAL A  52      60.533  14.665  32.026  1.00 17.12           C  
ANISOU  398  CG1 VAL A  52     2718   1206   2577     14      3     10       C  
ATOM    399  CG2 VAL A  52      62.029  14.543  34.096  1.00 16.73           C  
ANISOU  399  CG2 VAL A  52     2683   1149   2521     -1      0     -1       C  
ATOM    400  N   ALA A  53      59.203  11.349  32.656  1.00 14.21           N  
ANISOU  400  N   ALA A  53     2362    842   2194     52     20    -36       N  
ATOM    401  CA  ALA A  53      58.515  10.758  31.559  1.00 13.64           C  
ANISOU  401  CA  ALA A  53     2284    781   2118     62     20    -37       C  
ATOM    402  C   ALA A  53      58.926   9.275  31.520  1.00 13.39           C  
ANISOU  402  C   ALA A  53     2253    761   2073     75     19    -51       C  
ATOM    403  O   ALA A  53      59.868   8.924  32.139  1.00 13.40           O  
ANISOU  403  O   ALA A  53     2255    767   2068     76     19    -54       O  
ATOM    404  CB  ALA A  53      58.809  11.381  30.247  1.00 13.97           C  
ANISOU  404  CB  ALA A  53     2311    844   2154     60     17    -20       C  
ATOM    405  N   THR A  54      58.198   8.506  30.743  1.00 13.20           N  
ANISOU  405  N   THR A  54     2230    740   2044     84     18    -58       N  
ATOM    406  CA  THR A  54      58.437   7.042  30.642  1.00 13.40           C  
ANISOU  406  CA  THR A  54     2261    770   2060     98     14    -74       C  
ATOM    407  C   THR A  54      58.282   6.806  29.191  1.00 13.78           C  
ANISOU  407  C   THR A  54     2301    838   2095    107     10    -75       C  
ATOM    408  O   THR A  54      57.360   7.286  28.564  1.00 13.61           O  
ANISOU  408  O   THR A  54     2275    815   2077    101     10    -68       O  
ATOM    409  CB  THR A  54      57.506   6.183  31.468  1.00 13.36           C  
ANISOU  409  CB  THR A  54     2269    741   2064     97     11    -85       C  
ATOM    410  OG1 THR A  54      57.510   6.469  32.854  1.00 13.79           O  
ANISOU  410  OG1 THR A  54     2329    780   2129     89     15    -83       O  
ATOM    411  CG2 THR A  54      57.981   4.767  31.369  1.00 13.53           C  
ANISOU  411  CG2 THR A  54     2297    764   2077    111      5    -99       C  
ATOM    412  N   ILE A  55      59.214   6.022  28.634  1.00 14.35           N  
ANISOU  412  N   ILE A  55     2370    931   2149    122      8    -83       N  
ATOM    413  CA  ILE A  55      59.156   5.781  27.212  1.00 14.75           C  
ANISOU  413  CA  ILE A  55     2413   1006   2183    133      5    -86       C  
ATOM    414  C   ILE A  55      58.904   4.254  27.147  1.00 15.05           C  
ANISOU  414  C   ILE A  55     2468   1032   2216    149     -3   -111       C  
ATOM    415  O   ILE A  55      59.728   3.504  27.675  1.00 15.60           O  
ANISOU  415  O   ILE A  55     2544   1100   2282    162     -3   -121       O  
ATOM    416  CB  ILE A  55      60.460   6.083  26.433  1.00 15.49           C  
ANISOU  416  CB  ILE A  55     2489   1141   2256    144      8    -77       C  
ATOM    417  CG1 ILE A  55      60.931   7.530  26.658  1.00 16.17           C  
ANISOU  417  CG1 ILE A  55     2559   1235   2348    125     12    -50       C  
ATOM    418  CG2 ILE A  55      60.193   5.928  24.955  1.00 15.78           C  
ANISOU  418  CG2 ILE A  55     2516   1204   2273    154      5    -80       C  
ATOM    419  CD1 ILE A  55      62.388   7.695  26.394  1.00 16.92           C  
ANISOU  419  CD1 ILE A  55     2636   1366   2424    132     15    -38       C  
ATOM    420  N   TYR A  56      57.816   3.847  26.547  1.00 15.47           N  
ANISOU  420  N   TYR A  56     2529   1077   2270    147    -10   -119       N  
ATOM    421  CA  TYR A  56      57.467   2.396  26.348  1.00 15.75           C  
ANISOU  421  CA  TYR A  56     2584   1098   2302    158    -23   -143       C  
ATOM    422  C   TYR A  56      57.775   1.990  24.899  1.00 17.03           C  
ANISOU  422  C   TYR A  56     2742   1287   2438    176    -28   -157       C  
ATOM    423  O   TYR A  56      57.093   2.448  23.979  1.00 17.04           O  
ANISOU  423  O   TYR A  56     2736   1303   2433    169    -30   -151       O  
ATOM    424  CB  TYR A  56      55.999   2.144  26.708  1.00 15.91           C  
ANISOU  424  CB  TYR A  56     2615   1090   2340    140    -31   -142       C  
ATOM    425  CG  TYR A  56      55.690   2.313  28.171  1.00 15.47           C  
ANISOU  425  CG  TYR A  56     2562   1009   2304    127    -27   -132       C  
ATOM    426  CD1 TYR A  56      55.377   3.543  28.700  1.00 15.31           C  
ANISOU  426  CD1 TYR A  56     2530    989   2295    113    -16   -113       C  
ATOM    427  CD2 TYR A  56      55.604   1.254  29.024  1.00 15.67           C  
ANISOU  427  CD2 TYR A  56     2604   1010   2340    127    -35   -141       C  
ATOM    428  CE1 TYR A  56      55.079   3.707  30.022  1.00 14.93           C  
ANISOU  428  CE1 TYR A  56     2487    923   2263    104    -12   -107       C  
ATOM    429  CE2 TYR A  56      55.309   1.398  30.347  1.00 15.39           C  
ANISOU  429  CE2 TYR A  56     2569    958   2320    115    -31   -130       C  
ATOM    430  CZ  TYR A  56      54.987   2.654  30.880  1.00 15.26           C  
ANISOU  430  CZ  TYR A  56     2541    946   2311    103    -19   -114       C  
ATOM    431  OH  TYR A  56      54.701   2.818  32.232  1.00 15.35           O  
ANISOU  431  OH  TYR A  56     2553    944   2334     94    -14   -106       O  
ATOM    432  N   GLU A  57      58.730   1.058  24.670  1.00 18.50           N  
ANISOU  432  N   GLU A  57     2936   1483   2609    202    -31   -176       N  
ATOM    433  CA  GLU A  57      59.064   0.620  23.334  1.00 19.38           C  
ANISOU  433  CA  GLU A  57     3045   1623   2692    224    -35   -193       C  
ATOM    434  C   GLU A  57      58.602  -0.834  23.163  1.00 19.38           C  
ANISOU  434  C   GLU A  57     3075   1595   2692    237    -54   -224       C  
ATOM    435  O   GLU A  57      59.102  -1.696  23.817  1.00 19.41           O  
ANISOU  435  O   GLU A  57     3094   1579   2702    251    -58   -236       O  
ATOM    436  CB  GLU A  57      60.575   0.652  23.098  1.00 21.62           C  
ANISOU  436  CB  GLU A  57     3314   1943   2954    251    -26   -193       C  
ATOM    437  CG  GLU A  57      60.979   0.073  21.765  1.00 23.54           C  
ANISOU  437  CG  GLU A  57     3557   2221   3165    280    -30   -214       C  
ATOM    438  CD  GLU A  57      62.470   0.128  21.474  1.00 25.42           C  
ANISOU  438  CD  GLU A  57     3776   2503   3377    309    -18   -211       C  
ATOM    439  OE1 GLU A  57      63.325  -0.028  22.395  1.00 27.78           O  
ANISOU  439  OE1 GLU A  57     4074   2796   3684    316    -13   -205       O  
ATOM    440  OE2 GLU A  57      62.803   0.225  20.303  1.00 27.54           O  
ANISOU  440  OE2 GLU A  57     4030   2816   3616    326    -16   -215       O  
ATOM    441  N   LEU A  58      57.667  -1.070  22.285  1.00 19.92           N  
ANISOU  441  N   LEU A  58     3151   1663   2754    230    -65   -234       N  
ATOM    442  CA  LEU A  58      57.121  -2.401  22.136  1.00 20.39           C  
ANISOU  442  CA  LEU A  58     3240   1691   2815    236    -87   -262       C  
ATOM    443  C   LEU A  58      58.093  -3.195  21.306  1.00 22.38           C  
ANISOU  443  C   LEU A  58     3501   1962   3039    275    -91   -291       C  
ATOM    444  O   LEU A  58      58.459  -2.745  20.195  1.00 22.44           O  
ANISOU  444  O   LEU A  58     3492   2015   3018    288    -84   -294       O  
ATOM    445  CB  LEU A  58      55.782  -2.332  21.443  1.00 20.20           C  
ANISOU  445  CB  LEU A  58     3219   1663   2791    214    -99   -261       C  
ATOM    446  CG  LEU A  58      55.068  -3.674  21.181  1.00 20.11           C  
ANISOU  446  CG  LEU A  58     3240   1617   2781    213   -127   -288       C  
ATOM    447  CD1 LEU A  58      54.864  -4.410  22.469  1.00 19.62           C  
ANISOU  447  CD1 LEU A  58     3197   1509   2748    203   -136   -286       C  
ATOM    448  CD2 LEU A  58      53.780  -3.476  20.385  1.00 20.41           C  
ANISOU  448  CD2 LEU A  58     3277   1661   2816    188   -138   -283       C  
ATOM    449  N   LYS A  59      58.407  -4.407  21.788  1.00 23.02           N  
ANISOU  449  N   LYS A  59     3608   2010   3127    293   -103   -314       N  
ATOM    450  CA  LYS A  59      59.346  -5.320  21.115  1.00 25.78           C  
ANISOU  450  CA  LYS A  59     3971   2371   3451    336   -109   -347       C  
ATOM    451  C   LYS A  59      58.562  -6.350  20.330  1.00 26.08           C  
ANISOU  451  C   LYS A  59     4040   2385   3483    339   -135   -380       C  
ATOM    452  O   LYS A  59      57.361  -6.488  20.481  1.00 24.13           O  
ANISOU  452  O   LYS A  59     3806   2108   3254    307   -151   -375       O  
ATOM    453  CB  LYS A  59      60.221  -6.011  22.166  1.00 26.77           C  
ANISOU  453  CB  LYS A  59     4107   2472   3591    355   -108   -350       C  
ATOM    454  CG  LYS A  59      61.118  -5.083  23.018  1.00 28.30           C  
ANISOU  454  CG  LYS A  59     4272   2690   3790    352    -84   -319       C  
ATOM    455  CD  LYS A  59      62.230  -5.923  23.651  1.00 29.57           C  
ANISOU  455  CD  LYS A  59     4441   2841   3952    384    -83   -329       C  
ATOM    456  CE  LYS A  59      63.334  -5.089  24.282  1.00 31.34           C  
ANISOU  456  CE  LYS A  59     4635   3099   4174    387    -61   -301       C  
ATOM    457  NZ  LYS A  59      63.116  -4.765  25.747  1.00 32.08           N  
ANISOU  457  NZ  LYS A  59     4726   3163   4298    356    -58   -276       N  
ATOM    458  N   GLU A  60      59.276  -7.082  19.492  1.00 29.43           N  
ANISOU  458  N   GLU A  60     4477   2824   3878    380   -140   -414       N  
ATOM    459  CA  GLU A  60      58.705  -8.156  18.645  1.00 31.48           C  
ANISOU  459  CA  GLU A  60     4771   3061   4126    391   -168   -453       C  
ATOM    460  C   GLU A  60      58.105  -9.276  19.504  1.00 30.40           C  
ANISOU  460  C   GLU A  60     4672   2854   4024    377   -195   -463       C  
ATOM    461  O   GLU A  60      57.107  -9.875  19.129  1.00 29.96           O  
ANISOU  461  O   GLU A  60     4641   2767   3972    358   -221   -478       O  
ATOM    462  CB  GLU A  60      59.776  -8.759  17.717  1.00 34.32           C  
ANISOU  462  CB  GLU A  60     5139   3451   4449    446   -166   -490       C  
ATOM    463  CG  GLU A  60      60.511  -7.755  16.838  1.00 38.18           C  
ANISOU  463  CG  GLU A  60     5589   4016   4900    464   -141   -479       C  
ATOM    464  CD  GLU A  60      61.548  -6.910  17.569  1.00 40.95           C  
ANISOU  464  CD  GLU A  60     5905   4397   5256    469   -113   -445       C  
ATOM    465  OE1 GLU A  60      61.632  -6.935  18.844  1.00 40.60           O  
ANISOU  465  OE1 GLU A  60     5863   4317   5245    454   -111   -426       O  
ATOM    466  OE2 GLU A  60      62.270  -6.171  16.856  1.00 45.16           O  
ANISOU  466  OE2 GLU A  60     6406   4994   5758    486    -94   -434       O  
ATOM    467  N   ASP A  61      58.693  -9.529  20.664  1.00 28.52           N  
ANISOU  467  N   ASP A  61     4435   2591   3808    383   -189   -451       N  
ATOM    468  CA  ASP A  61      58.183 -10.537  21.569  1.00 29.67           C  
ANISOU  468  CA  ASP A  61     4612   2674   3988    368   -214   -454       C  
ATOM    469  C   ASP A  61      57.002 -10.109  22.443  1.00 29.49           C  
ANISOU  469  C   ASP A  61     4581   2627   3996    315   -218   -418       C  
ATOM    470  O   ASP A  61      56.538 -10.928  23.256  1.00 31.33           O  
ANISOU  470  O   ASP A  61     4836   2809   4257    298   -239   -415       O  
ATOM    471  CB  ASP A  61      59.316 -11.116  22.442  1.00 29.04           C  
ANISOU  471  CB  ASP A  61     4537   2577   3917    400   -208   -456       C  
ATOM    472  CG  ASP A  61      59.954 -10.091  23.376  1.00 29.61           C  
ANISOU  472  CG  ASP A  61     4572   2678   3997    392   -178   -418       C  
ATOM    473  OD1 ASP A  61      59.398  -8.979  23.462  1.00 26.51           O  
ANISOU  473  OD1 ASP A  61     4155   2309   3608    359   -164   -391       O  
ATOM    474  OD2 ASP A  61      61.009 -10.414  24.014  1.00 29.10           O  
ANISOU  474  OD2 ASP A  61     4505   2613   3936    419   -169   -416       O  
ATOM    475  N   LYS A  62      56.573  -8.847  22.269  1.00 29.31           N  
ANISOU  475  N   LYS A  62     4527   2642   3967    291   -199   -392       N  
ATOM    476  CA  LYS A  62      55.383  -8.216  22.868  1.00 28.20           C  
ANISOU  476  CA  LYS A  62     4374   2492   3849    244   -199   -359       C  
ATOM    477  C   LYS A  62      55.639  -7.661  24.287  1.00 25.75           C  
ANISOU  477  C   LYS A  62     4044   2176   3562    231   -180   -326       C  
ATOM    478  O   LYS A  62      54.723  -7.226  24.990  1.00 24.08           O  
ANISOU  478  O   LYS A  62     3822   1954   3369    197   -180   -299       O  
ATOM    479  CB  LYS A  62      54.167  -9.127  22.804  1.00 29.46           C  
ANISOU  479  CB  LYS A  62     4560   2608   4023    217   -232   -365       C  
ATOM    480  CG  LYS A  62      53.829  -9.473  21.349  1.00 31.43           C  
ANISOU  480  CG  LYS A  62     4825   2869   4247    225   -249   -396       C  
ATOM    481  CD  LYS A  62      52.896 -10.662  21.266  1.00 32.56           C  
ANISOU  481  CD  LYS A  62     5005   2963   4404    205   -289   -411       C  
ATOM    482  CE  LYS A  62      51.678 -10.386  20.391  1.00 33.64           C  
ANISOU  482  CE  LYS A  62     5138   3113   4529    173   -303   -406       C  
ATOM    483  NZ  LYS A  62      51.933  -9.700  19.077  1.00 33.87           N  
ANISOU  483  NZ  LYS A  62     5152   3195   4523    191   -289   -421       N  
ATOM    484  N   SER A  63      56.911  -7.697  24.670  1.00 24.86           N  
ANISOU  484  N   SER A  63     3926   2074   3444    260   -166   -330       N  
ATOM    485  CA  SER A  63      57.365  -7.095  25.912  1.00 22.70           C  
ANISOU  485  CA  SER A  63     3633   1803   3186    252   -147   -303       C  
ATOM    486  C   SER A  63      57.632  -5.626  25.523  1.00 21.96           C  
ANISOU  486  C   SER A  63     3507   1759   3077    248   -121   -285       C  
ATOM    487  O   SER A  63      57.670  -5.285  24.331  1.00 21.23           O  
ANISOU  487  O   SER A  63     3407   1696   2961    258   -118   -296       O  
ATOM    488  CB  SER A  63      58.645  -7.754  26.406  1.00 23.80           C  
ANISOU  488  CB  SER A  63     3780   1938   3325    285   -144   -313       C  
ATOM    489  OG  SER A  63      59.794  -7.199  25.797  1.00 24.96           O  
ANISOU  489  OG  SER A  63     3907   2129   3445    315   -124   -318       O  
ATOM    490  N   TYR A  64      57.853  -4.824  26.560  1.00 20.52           N  
ANISOU  490  N   TYR A  64     3306   1582   2908    234   -104   -259       N  
ATOM    491  CA  TYR A  64      58.270  -3.433  26.401  1.00 20.07           C  
ANISOU  491  CA  TYR A  64     3220   1564   2841    230    -81   -240       C  
ATOM    492  C   TYR A  64      59.682  -3.192  26.938  1.00 19.46           C  
ANISOU  492  C   TYR A  64     3129   1506   2757    249    -66   -233       C  
ATOM    493  O   TYR A  64      60.053  -3.608  28.016  1.00 19.67           O  
ANISOU  493  O   TYR A  64     3161   1513   2798    249    -66   -228       O  
ATOM    494  CB  TYR A  64      57.333  -2.464  27.139  1.00 20.48           C  
ANISOU  494  CB  TYR A  64     3259   1609   2911    195    -74   -213       C  
ATOM    495  CG  TYR A  64      56.000  -2.178  26.470  1.00 19.79           C  
ANISOU  495  CG  TYR A  64     3172   1520   2825    175    -81   -209       C  
ATOM    496  CD1 TYR A  64      55.919  -1.349  25.369  1.00 19.92           C  
ANISOU  496  CD1 TYR A  64     3173   1569   2825    176    -74   -206       C  
ATOM    497  CD2 TYR A  64      54.818  -2.753  26.941  1.00 20.16           C  
ANISOU  497  CD2 TYR A  64     3232   1536   2890    153    -97   -205       C  
ATOM    498  CE1 TYR A  64      54.708  -1.082  24.764  1.00 19.38           C  
ANISOU  498  CE1 TYR A  64     3103   1502   2758    157    -81   -200       C  
ATOM    499  CE2 TYR A  64      53.615  -2.522  26.334  1.00 19.77           C  
ANISOU  499  CE2 TYR A  64     3180   1489   2841    134   -104   -199       C  
ATOM    500  CZ  TYR A  64      53.560  -1.676  25.237  1.00 19.18           C  
ANISOU  500  CZ  TYR A  64     3089   1446   2749    137    -96   -197       C  
ATOM    501  OH  TYR A  64      52.327  -1.425  24.750  1.00 19.36           O  
ANISOU  501  OH  TYR A  64     3108   1471   2774    116   -103   -187       O  
ATOM    502  N   ASN A  65      60.414  -2.348  26.230  1.00 19.36           N  
ANISOU  502  N   ASN A  65     3095   1536   2723    259    -52   -227       N  
ATOM    503  CA  ASN A  65      61.626  -1.851  26.719  1.00 20.04           C  
ANISOU  503  CA  ASN A  65     3163   1645   2803    268    -37   -213       C  
ATOM    504  C   ASN A  65      61.172  -0.519  27.275  1.00 18.95           C  
ANISOU  504  C   ASN A  65     3009   1510   2679    236    -27   -186       C  
ATOM    505  O   ASN A  65      60.645   0.271  26.510  1.00 19.91           O  
ANISOU  505  O   ASN A  65     3121   1648   2795    224    -24   -178       O  
ATOM    506  CB  ASN A  65      62.579  -1.657  25.598  1.00 22.16           C  
ANISOU  506  CB  ASN A  65     3416   1961   3042    295    -29   -218       C  
ATOM    507  CG  ASN A  65      63.956  -1.272  26.059  1.00 24.87           C  
ANISOU  507  CG  ASN A  65     3739   2334   3376    307    -16   -202       C  
ATOM    508  OD1 ASN A  65      64.710  -2.103  26.661  1.00 29.27           O  
ANISOU  508  OD1 ASN A  65     4303   2882   3934    327    -18   -209       O  
ATOM    509  ND2 ASN A  65      64.327  -0.036  25.781  1.00 26.22           N  
ANISOU  509  ND2 ASN A  65     3883   2539   3537    293     -5   -177       N  
ATOM    510  N   VAL A  66      61.358  -0.351  28.584  1.00 17.82           N  
ANISOU  510  N   VAL A  66     2866   1350   2553    223    -22   -173       N  
ATOM    511  CA  VAL A  66      60.860   0.852  29.282  1.00 17.88           C  
ANISOU  511  CA  VAL A  66     2863   1353   2575    193    -14   -152       C  
ATOM    512  C   VAL A  66      61.996   1.766  29.644  1.00 17.68           C  
ANISOU  512  C   VAL A  66     2820   1354   2544    191     -3   -134       C  
ATOM    513  O   VAL A  66      62.907   1.348  30.332  1.00 18.69           O  
ANISOU  513  O   VAL A  66     2946   1484   2669    200     -1   -133       O  
ATOM    514  CB  VAL A  66      60.091   0.401  30.537  1.00 17.83           C  
ANISOU  514  CB  VAL A  66     2871   1310   2591    178    -20   -150       C  
ATOM    515  CG1 VAL A  66      59.542   1.619  31.273  1.00 17.57           C  
ANISOU  515  CG1 VAL A  66     2830   1274   2571    152    -11   -132       C  
ATOM    516  CG2 VAL A  66      58.953  -0.504  30.140  1.00 17.85           C  
ANISOU  516  CG2 VAL A  66     2891   1289   2601    176    -34   -164       C  
ATOM    517  N   THR A  67      61.948   3.055  29.287  1.00 17.82           N  
ANISOU  517  N   THR A  67     2821   1389   2559    176      3   -117       N  
ATOM    518  CA  THR A  67      63.011   3.986  29.721  1.00 18.24           C  
ANISOU  518  CA  THR A  67     2858   1463   2608    168     11    -97       C  
ATOM    519  C   THR A  67      62.392   4.979  30.667  1.00 18.09           C  
ANISOU  519  C   THR A  67     2841   1420   2609    141     13    -85       C  
ATOM    520  O   THR A  67      61.456   5.660  30.261  1.00 18.56           O  
ANISOU  520  O   THR A  67     2902   1473   2676    129     13    -81       O  
ATOM    521  CB  THR A  67      63.672   4.666  28.573  1.00 19.00           C  
ANISOU  521  CB  THR A  67     2933   1599   2685    172     14    -84       C  
ATOM    522  OG1 THR A  67      64.231   3.692  27.691  1.00 19.79           O  
ANISOU  522  OG1 THR A  67     3030   1723   2763    203     13    -99       O  
ATOM    523  CG2 THR A  67      64.748   5.657  29.031  1.00 19.00           C  
ANISOU  523  CG2 THR A  67     2916   1620   2683    159     18    -60       C  
ATOM    524  N   LYS A  68      62.867   5.006  31.902  1.00 18.11           N  
ANISOU  524  N   LYS A  68     2848   1413   2619    133     15    -81       N  
ATOM    525  CA  LYS A  68      62.434   6.018  32.844  1.00 18.46           C  
ANISOU  525  CA  LYS A  68     2896   1440   2678    110     17    -72       C  
ATOM    526  C   LYS A  68      63.353   7.226  32.736  1.00 17.34           C  
ANISOU  526  C   LYS A  68     2738   1317   2530     97     18    -53       C  
ATOM    527  O   LYS A  68      64.544   7.103  32.966  1.00 16.98           O  
ANISOU  527  O   LYS A  68     2684   1292   2474     99     18    -45       O  
ATOM    528  CB  LYS A  68      62.446   5.443  34.247  1.00 19.20           C  
ANISOU  528  CB  LYS A  68     2999   1514   2779    107     17    -78       C  
ATOM    529  CG  LYS A  68      61.620   4.141  34.368  1.00 19.71           C  
ANISOU  529  CG  LYS A  68     3078   1560   2851    117     12    -93       C  
ATOM    530  CD  LYS A  68      61.524   3.686  35.816  1.00 20.20           C  
ANISOU  530  CD  LYS A  68     3147   1605   2921    110     11    -94       C  
ATOM    531  CE  LYS A  68      62.895   3.349  36.372  1.00 20.30           C  
ANISOU  531  CE  LYS A  68     3154   1633   2925    116     12    -89       C  
ATOM    532  NZ  LYS A  68      62.996   1.879  36.519  1.00 20.27           N  
ANISOU  532  NZ  LYS A  68     3157   1620   2922    133      5    -97       N  
ATOM    533  N   VAL A  69      62.784   8.424  32.499  1.00 17.10           N  
ANISOU  533  N   VAL A  69     2707   1279   2510     81     18    -43       N  
ATOM    534  CA  VAL A  69      63.498   9.676  32.435  1.00 17.36           C  
ANISOU  534  CA  VAL A  69     2730   1323   2543     64     15    -23       C  
ATOM    535  C   VAL A  69      63.310  10.410  33.764  1.00 16.75           C  
ANISOU  535  C   VAL A  69     2666   1218   2480     46     14    -24       C  
ATOM    536  O   VAL A  69      62.197  10.704  34.138  1.00 15.53           O  
ANISOU  536  O   VAL A  69     2523   1036   2338     43     15    -33       O  
ATOM    537  CB  VAL A  69      62.968  10.576  31.319  1.00 17.85           C  
ANISOU  537  CB  VAL A  69     2784   1389   2608     58     13    -11       C  
ATOM    538  CG1 VAL A  69      63.726  11.918  31.378  1.00 17.73           C  
ANISOU  538  CG1 VAL A  69     2760   1379   2596     36      7     12       C  
ATOM    539  CG2 VAL A  69      63.070   9.920  29.943  1.00 17.96           C  
ANISOU  539  CG2 VAL A  69     2784   1434   2605     76     14    -11       C  
ATOM    540  N   MET A  70      64.406  10.674  34.444  1.00 17.90           N  
ANISOU  540  N   MET A  70     2807   1373   2620     35     10    -16       N  
ATOM    541  CA  MET A  70      64.404  11.280  35.761  1.00 17.29           C  
ANISOU  541  CA  MET A  70     2744   1274   2552     18      8    -19       C  
ATOM    542  C   MET A  70      65.182  12.619  35.663  1.00 16.75           C  
ANISOU  542  C   MET A  70     2669   1209   2484     -5     -1      0       C  
ATOM    543  O   MET A  70      66.076  12.803  34.818  1.00 16.15           O  
ANISOU  543  O   MET A  70     2574   1162   2397     -9     -6     20       O  
ATOM    544  CB  MET A  70      65.108  10.430  36.759  1.00 19.35           C  
ANISOU  544  CB  MET A  70     3005   1542   2804     21      9    -25       C  
ATOM    545  CG  MET A  70      64.791   8.976  36.619  1.00 20.33           C  
ANISOU  545  CG  MET A  70     3130   1670   2924     44     15    -37       C  
ATOM    546  SD  MET A  70      63.117   8.674  37.175  1.00 23.55           S  
ANISOU  546  SD  MET A  70     3555   2044   3346     48     19    -56       S  
ATOM    547  CE  MET A  70      63.329   8.677  38.927  1.00 23.56           C  
ANISOU  547  CE  MET A  70     3566   2035   3348     36     19    -61       C  
ATOM    548  N   PHE A  71      64.866  13.502  36.600  1.00 16.10           N  
ANISOU  548  N   PHE A  71     2603   1098   2413    -20     -6     -5       N  
ATOM    549  CA  PHE A  71      65.625  14.727  36.810  1.00 16.35           C  
ANISOU  549  CA  PHE A  71     2636   1125   2448    -47    -20     10       C  
ATOM    550  C   PHE A  71      66.138  14.702  38.245  1.00 15.60           C  
ANISOU  550  C   PHE A  71     2553   1024   2350    -59    -24      1       C  
ATOM    551  O   PHE A  71      65.379  14.816  39.165  1.00 15.71           O  
ANISOU  551  O   PHE A  71     2586   1012   2370    -56    -21    -19       O  
ATOM    552  CB  PHE A  71      64.710  15.953  36.529  1.00 16.55           C  
ANISOU  552  CB  PHE A  71     2676   1119   2494    -54    -25     10       C  
ATOM    553  CG  PHE A  71      65.448  17.261  36.247  1.00 17.44           C  
ANISOU  553  CG  PHE A  71     2786   1227   2612    -81    -43     34       C  
ATOM    554  CD1 PHE A  71      66.498  17.327  35.337  1.00 17.73           C  
ANISOU  554  CD1 PHE A  71     2798   1299   2638    -92    -50     64       C  
ATOM    555  CD2 PHE A  71      65.029  18.419  36.866  1.00 18.71           C  
ANISOU  555  CD2 PHE A  71     2970   1348   2790    -94    -54     27       C  
ATOM    556  CE1 PHE A  71      67.131  18.539  35.079  1.00 18.42           C  
ANISOU  556  CE1 PHE A  71     2883   1382   2733   -120    -69     90       C  
ATOM    557  CE2 PHE A  71      65.633  19.644  36.620  1.00 18.28           C  
ANISOU  557  CE2 PHE A  71     2917   1282   2745   -121    -74     49       C  
ATOM    558  CZ  PHE A  71      66.680  19.693  35.717  1.00 18.58           C  
ANISOU  558  CZ  PHE A  71     2929   1356   2773   -136    -82     82       C  
ATOM    559  N   GLN A  72      67.436  14.560  38.391  1.00 16.50           N  
ANISOU  559  N   GLN A  72     2653   1165   2450    -71    -30     17       N  
ATOM    560  CA  GLN A  72      68.092  14.442  39.706  1.00 17.73           C  
ANISOU  560  CA  GLN A  72     2815   1322   2598    -84    -34     12       C  
ATOM    561  C   GLN A  72      69.142  15.513  39.839  1.00 19.46           C  
ANISOU  561  C   GLN A  72     3031   1546   2815   -117    -53     34       C  
ATOM    562  O   GLN A  72      70.043  15.547  39.032  1.00 19.43           O  
ANISOU  562  O   GLN A  72     3005   1574   2803   -123    -58     60       O  
ATOM    563  CB  GLN A  72      68.741  13.082  39.858  1.00 17.21           C  
ANISOU  563  CB  GLN A  72     2733   1288   2516    -68    -25     15       C  
ATOM    564  CG  GLN A  72      67.785  11.909  39.746  1.00 16.74           C  
ANISOU  564  CG  GLN A  72     2677   1222   2459    -39    -11     -4       C  
ATOM    565  CD  GLN A  72      68.485  10.590  39.981  1.00 16.09           C  
ANISOU  565  CD  GLN A  72     2583   1166   2364    -23     -5     -1       C  
ATOM    566  OE1 GLN A  72      69.688  10.393  39.644  1.00 15.94           O  
ANISOU  566  OE1 GLN A  72     2544   1180   2331    -24     -8     17       O  
ATOM    567  NE2 GLN A  72      67.722   9.662  40.586  1.00 16.42           N  
ANISOU  567  NE2 GLN A  72     2634   1194   2410     -8      1    -19       N  
ATOM    568  N   ARG A  73      69.034  16.325  40.899  1.00 22.22           N  
ANISOU  568  N   ARG A  73     3403   1867   3170   -136    -63     21       N  
ATOM    569  CA  ARG A  73      69.948  17.451  41.131  1.00 24.70           C  
ANISOU  569  CA  ARG A  73     3720   2178   3484   -172    -86     40       C  
ATOM    570  C   ARG A  73      70.322  18.122  39.800  1.00 25.05           C  
ANISOU  570  C   ARG A  73     3748   2234   3535   -184    -96     71       C  
ATOM    571  O   ARG A  73      71.495  18.264  39.422  1.00 26.33           O  
ANISOU  571  O   ARG A  73     3888   2429   3686   -203   -107    102       O  
ATOM    572  CB  ARG A  73      71.159  17.015  41.969  1.00 27.06           C  
ANISOU  572  CB  ARG A  73     4008   2507   3764   -188    -92     50       C  
ATOM    573  CG  ARG A  73      70.719  16.412  43.306  1.00 28.97           C  
ANISOU  573  CG  ARG A  73     4266   2739   4001   -178    -82     21       C  
ATOM    574  CD  ARG A  73      71.595  16.667  44.511  1.00 32.35           C  
ANISOU  574  CD  ARG A  73     4699   3173   4416   -205    -96     22       C  
ATOM    575  NE  ARG A  73      71.106  17.830  45.275  1.00 36.06           N  
ANISOU  575  NE  ARG A  73     5203   3603   4896   -223   -111      1       N  
ATOM    576  CZ  ARG A  73      71.505  18.181  46.502  1.00 36.57           C  
ANISOU  576  CZ  ARG A  73     5282   3662   4949   -245   -123    -10       C  
ATOM    577  NH1 ARG A  73      72.426  17.473  47.150  1.00 37.65           N  
ANISOU  577  NH1 ARG A  73     5402   3834   5067   -254   -123      1       N  
ATOM    578  NH2 ARG A  73      70.987  19.262  47.084  1.00 38.37           N  
ANISOU  578  NH2 ARG A  73     5543   3849   5186   -256   -136    -33       N  
ATOM    579  N   LYS A  74      69.303  18.531  39.074  1.00 25.50           N  
ANISOU  579  N   LYS A  74     3814   2267   3608   -171    -92     65       N  
ATOM    580  CA  LYS A  74      69.491  19.358  37.853  1.00 27.15           C  
ANISOU  580  CA  LYS A  74     4009   2480   3826   -184   -104     94       C  
ATOM    581  C   LYS A  74      70.033  18.640  36.613  1.00 25.60           C  
ANISOU  581  C   LYS A  74     3777   2334   3614   -172    -95    120       C  
ATOM    582  O   LYS A  74      70.294  19.285  35.584  1.00 24.94           O  
ANISOU  582  O   LYS A  74     3677   2263   3534   -184   -104    150       O  
ATOM    583  CB  LYS A  74      70.313  20.678  38.188  1.00 29.98           C  
ANISOU  583  CB  LYS A  74     4376   2822   4191   -227   -133    116       C  
ATOM    584  CG  LYS A  74      71.295  21.195  37.117  1.00 33.12           C  
ANISOU  584  CG  LYS A  74     4745   3253   4586   -251   -149    163       C  
ATOM    585  CD  LYS A  74      72.029  22.484  37.486  1.00 35.16           C  
ANISOU  585  CD  LYS A  74     5014   3490   4853   -297   -181    185       C  
ATOM    586  CE  LYS A  74      72.631  23.159  36.268  1.00 36.68           C  
ANISOU  586  CE  LYS A  74     5179   3707   5048   -320   -198    233       C  
ATOM    587  NZ  LYS A  74      73.920  23.827  36.611  1.00 39.07           N  
ANISOU  587  NZ  LYS A  74     5474   4023   5345   -366   -226    267       N  
ATOM    588  N   LYS A  75      70.126  17.299  36.662  1.00 24.17           N  
ANISOU  588  N   LYS A  75     3584   2181   3417   -145    -76    109       N  
ATOM    589  CA  LYS A  75      70.642  16.500  35.559  1.00 23.23           C  
ANISOU  589  CA  LYS A  75     3434   2111   3280   -127    -67    126       C  
ATOM    590  C   LYS A  75      69.637  15.402  35.126  1.00 21.20           C  
ANISOU  590  C   LYS A  75     3180   1851   3023    -89    -46    101       C  
ATOM    591  O   LYS A  75      69.027  14.720  35.967  1.00 18.90           O  
ANISOU  591  O   LYS A  75     2906   1539   2734    -75    -37     72       O  
ATOM    592  CB  LYS A  75      71.949  15.854  35.967  1.00 24.33           C  
ANISOU  592  CB  LYS A  75     3553   2291   3398   -130    -67    141       C  
ATOM    593  CG  LYS A  75      73.082  16.834  36.064  1.00 27.01           C  
ANISOU  593  CG  LYS A  75     3880   2647   3734   -168    -88    176       C  
ATOM    594  CD  LYS A  75      74.355  16.135  36.508  1.00 28.29           C  
ANISOU  594  CD  LYS A  75     4020   2854   3873   -169    -87    192       C  
ATOM    595  CE  LYS A  75      75.512  16.599  35.643  1.00 29.02           C  
ANISOU  595  CE  LYS A  75     4077   2997   3950   -187    -98    238       C  
ATOM    596  NZ  LYS A  75      76.759  15.806  35.859  1.00 30.62           N  
ANISOU  596  NZ  LYS A  75     4251   3254   4127   -180    -94    257       N  
ATOM    597  N   CYS A  76      69.421  15.315  33.826  1.00 20.44           N  
ANISOU  597  N   CYS A  76     3068   1776   2922    -76    -42    112       N  
ATOM    598  CA  CYS A  76      68.620  14.255  33.271  1.00 20.18           C  
ANISOU  598  CA  CYS A  76     3035   1746   2885    -43    -26     90       C  
ATOM    599  C   CYS A  76      69.304  12.904  33.451  1.00 19.28           C  
ANISOU  599  C   CYS A  76     2911   1663   2752    -20    -17     83       C  
ATOM    600  O   CYS A  76      70.502  12.758  33.180  1.00 20.52           O  
ANISOU  600  O   CYS A  76     3045   1861   2891    -21    -19    104       O  
ATOM    601  CB  CYS A  76      68.363  14.464  31.763  1.00 20.48           C  
ANISOU  601  CB  CYS A  76     3056   1807   2919    -35    -25    106       C  
ATOM    602  SG  CYS A  76      67.746  16.108  31.409  1.00 22.50           S  
ANISOU  602  SG  CYS A  76     3318   2031   3197    -63    -39    124       S  
ATOM    603  N   LYS A  77      68.525  11.918  33.877  1.00 18.91           N  
ANISOU  603  N   LYS A  77     2880   1596   2709      0     -7     54       N  
ATOM    604  CA  LYS A  77      68.994  10.532  34.010  1.00 18.50           C  
ANISOU  604  CA  LYS A  77     2821   1563   2642     26      1     43       C  
ATOM    605  C   LYS A  77      68.022   9.577  33.328  1.00 19.32           C  
ANISOU  605  C   LYS A  77     2934   1659   2747     54      9     21       C  
ATOM    606  O   LYS A  77      66.856   9.880  33.165  1.00 18.15           O  
ANISOU  606  O   LYS A  77     2798   1482   2612     51      9     10       O  
ATOM    607  CB  LYS A  77      69.010  10.186  35.505  1.00 18.26           C  
ANISOU  607  CB  LYS A  77     2807   1511   2618     19      1     30       C  
ATOM    608  CG  LYS A  77      69.739  11.109  36.403  1.00 18.82           C  
ANISOU  608  CG  LYS A  77     2877   1580   2690    -10     -8     45       C  
ATOM    609  CD  LYS A  77      71.193  11.124  36.048  1.00 19.25           C  
ANISOU  609  CD  LYS A  77     2905   1681   2725    -14    -12     73       C  
ATOM    610  CE  LYS A  77      72.015  11.765  37.092  1.00 20.20           C  
ANISOU  610  CE  LYS A  77     3026   1804   2845    -44    -23     87       C  
ATOM    611  NZ  LYS A  77      73.425  11.787  36.690  1.00 21.26           N  
ANISOU  611  NZ  LYS A  77     3130   1988   2959    -49    -28    119       N  
ATOM    612  N   TYR A  78      68.519   8.433  32.877  1.00 19.17           N  
ANISOU  612  N   TYR A  78     2906   1665   2712     81     14     15       N  
ATOM    613  CA  TYR A  78      67.734   7.514  32.088  1.00 19.63           C  
ANISOU  613  CA  TYR A  78     2971   1718   2768    107     18     -4       C  
ATOM    614  C   TYR A  78      67.919   6.091  32.626  1.00 20.39           C  
ANISOU  614  C   TYR A  78     3076   1808   2861    131     21    -23       C  
ATOM    615  O   TYR A  78      69.053   5.562  32.588  1.00 22.61           O  
ANISOU  615  O   TYR A  78     3344   2120   3127    147     22    -16       O  
ATOM    616  CB  TYR A  78      68.171   7.511  30.642  1.00 20.36           C  
ANISOU  616  CB  TYR A  78     3043   1851   2840    122     20      4       C  
ATOM    617  CG  TYR A  78      67.979   8.808  30.030  1.00 20.92           C  
ANISOU  617  CG  TYR A  78     3104   1929   2915    100     16     25       C  
ATOM    618  CD1 TYR A  78      68.994   9.797  30.144  1.00 21.09           C  
ANISOU  618  CD1 TYR A  78     3106   1974   2931     78     10     55       C  
ATOM    619  CD2 TYR A  78      66.768   9.155  29.438  1.00 21.54           C  
ANISOU  619  CD2 TYR A  78     3191   1986   3004     96     15     17       C  
ATOM    620  CE1 TYR A  78      68.830  11.066  29.674  1.00 21.74           C  
ANISOU  620  CE1 TYR A  78     3181   2057   3021     53      3     78       C  
ATOM    621  CE2 TYR A  78      66.617  10.442  28.897  1.00 21.61           C  
ANISOU  621  CE2 TYR A  78     3190   2000   3019     75     10     40       C  
ATOM    622  CZ  TYR A  78      67.643  11.381  29.018  1.00 22.04           C  
ANISOU  622  CZ  TYR A  78     3227   2075   3070     53      4     70       C  
ATOM    623  OH  TYR A  78      67.508  12.661  28.560  1.00 23.66           O  
ANISOU  623  OH  TYR A  78     3425   2280   3285     29     -3     95       O  
ATOM    624  N   MET A  79      66.834   5.473  33.040  1.00 21.46           N  
ANISOU  624  N   MET A  79     3234   1908   3012    134     20    -43       N  
ATOM    625  CA  MET A  79      66.871   4.069  33.563  1.00 22.55           C  
ANISOU  625  CA  MET A  79     3382   2033   3151    155     19    -59       C  
ATOM    626  C   MET A  79      66.084   3.092  32.708  1.00 23.37           C  
ANISOU  626  C   MET A  79     3499   2126   3255    177     16    -80       C  
ATOM    627  O   MET A  79      65.085   3.448  32.115  1.00 22.79           O  
ANISOU  627  O   MET A  79     3431   2040   3186    169     15    -85       O  
ATOM    628  CB  MET A  79      66.342   4.043  34.988  1.00 23.75           C  
ANISOU  628  CB  MET A  79     3549   2154   3321    137     18    -62       C  
ATOM    629  CG  MET A  79      67.298   4.670  35.983  1.00 24.57           C  
ANISOU  629  CG  MET A  79     3643   2269   3420    120     18    -45       C  
ATOM    630  SD  MET A  79      66.819   4.661  37.728  1.00 27.68           S  
ANISOU  630  SD  MET A  79     4051   2636   3830    100     17    -49       S  
ATOM    631  CE  MET A  79      65.263   5.523  37.725  1.00 27.59           C  
ANISOU  631  CE  MET A  79     4054   2594   3834     84     18    -58       C  
ATOM    632  N   ILE A  80      66.572   1.857  32.597  1.00 24.45           N  
ANISOU  632  N   ILE A  80     3640   2266   3384    204     14    -92       N  
ATOM    633  CA  ILE A  80      65.946   0.854  31.716  1.00 25.22           C  
ANISOU  633  CA  ILE A  80     3752   2351   3479    227      8   -115       C  
ATOM    634  C   ILE A  80      65.349  -0.277  32.531  1.00 23.76           C  
ANISOU  634  C   ILE A  80     3589   2127   3311    230      0   -128       C  
ATOM    635  O   ILE A  80      65.920  -0.678  33.504  1.00 26.20           O  
ANISOU  635  O   ILE A  80     3897   2431   3625    232      0   -122       O  
ATOM    636  CB  ILE A  80      66.956   0.291  30.694  1.00 26.80           C  
ANISOU  636  CB  ILE A  80     3940   2586   3653    262     10   -121       C  
ATOM    637  CG1 ILE A  80      67.419   1.403  29.754  1.00 27.48           C  
ANISOU  637  CG1 ILE A  80     4002   2716   3721    257     17   -105       C  
ATOM    638  CG2 ILE A  80      66.340  -0.879  29.940  1.00 27.97           C  
ANISOU  638  CG2 ILE A  80     4109   2716   3800    287      1   -150       C  
ATOM    639  CD1 ILE A  80      68.667   1.112  28.934  1.00 28.90           C  
ANISOU  639  CD1 ILE A  80     4163   2945   3872    289     22   -102       C  
ATOM    640  N   ASN A  81      64.125  -0.655  32.199  1.00 22.71           N  
ANISOU  640  N   ASN A  81     3472   1966   3188    225     -8   -142       N  
ATOM    641  CA  ASN A  81      63.411  -1.869  32.735  1.00 22.97           C  
ANISOU  641  CA  ASN A  81     3528   1961   3238    227    -21   -154       C  
ATOM    642  C   ASN A  81      62.856  -2.600  31.518  1.00 21.15           C  
ANISOU  642  C   ASN A  81     3312   1723   3002    244    -32   -176       C  
ATOM    643  O   ASN A  81      62.670  -2.034  30.442  1.00 20.27           O  
ANISOU  643  O   ASN A  81     3193   1631   2877    246    -28   -179       O  
ATOM    644  CB  ASN A  81      62.178  -1.507  33.587  1.00 24.10           C  
ANISOU  644  CB  ASN A  81     3676   2078   3400    196    -23   -146       C  
ATOM    645  CG  ASN A  81      62.483  -1.181  35.065  1.00 25.44           C  
ANISOU  645  CG  ASN A  81     3841   2245   3580    180    -17   -129       C  
ATOM    646  OD1 ASN A  81      61.925  -0.225  35.642  1.00 26.99           O  
ANISOU  646  OD1 ASN A  81     4031   2440   3781    157    -11   -119       O  
ATOM    647  ND2 ASN A  81      63.254  -2.027  35.703  1.00 27.10           N  
ANISOU  647  ND2 ASN A  81     4053   2452   3791    192    -21   -128       N  
ATOM    648  N   THR A  82      62.579  -3.898  31.690  1.00 20.82           N  
ANISOU  648  N   THR A  82     3291   1650   2969    255    -47   -190       N  
ATOM    649  CA  THR A  82      61.717  -4.619  30.763  1.00 20.72           C  
ANISOU  649  CA  THR A  82     3297   1617   2956    261    -63   -211       C  
ATOM    650  C   THR A  82      60.392  -4.988  31.413  1.00 19.93           C  
ANISOU  650  C   THR A  82     3212   1480   2880    233    -76   -206       C  
ATOM    651  O   THR A  82      60.380  -5.317  32.590  1.00 20.34           O  
ANISOU  651  O   THR A  82     3266   1514   2948    222    -79   -193       O  
ATOM    652  CB  THR A  82      62.414  -5.907  30.234  1.00 21.96           C  
ANISOU  652  CB  THR A  82     3472   1766   3105    299    -74   -235       C  
ATOM    653  OG1 THR A  82      63.522  -5.540  29.413  1.00 23.34           O  
ANISOU  653  OG1 THR A  82     3631   1983   3253    328    -61   -240       O  
ATOM    654  CG2 THR A  82      61.464  -6.903  29.385  1.00 23.07           C  
ANISOU  654  CG2 THR A  82     3641   1875   3248    304    -98   -261       C  
ATOM    655  N   PHE A  83      59.299  -4.775  30.667  1.00 19.94           N  
ANISOU  655  N   PHE A  83     3217   1476   2880    218    -83   -210       N  
ATOM    656  CA  PHE A  83      57.924  -5.119  31.076  1.00 19.66           C  
ANISOU  656  CA  PHE A  83     3193   1411   2864    191    -97   -203       C  
ATOM    657  C   PHE A  83      57.517  -6.339  30.228  1.00 19.83           C  
ANISOU  657  C   PHE A  83     3240   1408   2885    201   -122   -227       C  
ATOM    658  O   PHE A  83      57.446  -6.246  28.987  1.00 19.80           O  
ANISOU  658  O   PHE A  83     3239   1418   2864    212   -124   -243       O  
ATOM    659  CB  PHE A  83      56.961  -3.959  30.850  1.00 20.11           C  
ANISOU  659  CB  PHE A  83     3236   1484   2921    167    -88   -189       C  
ATOM    660  CG  PHE A  83      57.011  -2.877  31.900  1.00 19.74           C  
ANISOU  660  CG  PHE A  83     3170   1449   2881    151    -69   -167       C  
ATOM    661  CD1 PHE A  83      58.091  -2.711  32.789  1.00 19.35           C  
ANISOU  661  CD1 PHE A  83     3113   1407   2831    158    -59   -161       C  
ATOM    662  CD2 PHE A  83      55.980  -1.988  31.936  1.00 20.28           C  
ANISOU  662  CD2 PHE A  83     3229   1523   2955    130    -64   -154       C  
ATOM    663  CE1 PHE A  83      58.108  -1.664  33.756  1.00 19.68           C  
ANISOU  663  CE1 PHE A  83     3140   1459   2878    143    -44   -143       C  
ATOM    664  CE2 PHE A  83      55.961  -0.974  32.890  1.00 18.40           C  
ANISOU  664  CE2 PHE A  83     2976   1292   2721    118    -48   -137       C  
ATOM    665  CZ  PHE A  83      57.047  -0.799  33.750  1.00 19.13           C  
ANISOU  665  CZ  PHE A  83     3064   1391   2812    124    -39   -133       C  
ATOM    666  N   VAL A  84      57.354  -7.448  30.904  1.00 19.21           N  
ANISOU  666  N   VAL A  84     3180   1294   2824    198   -141   -227       N  
ATOM    667  CA  VAL A  84      56.952  -8.747  30.299  1.00 19.62           C  
ANISOU  667  CA  VAL A  84     3262   1311   2881    205   -170   -249       C  
ATOM    668  C   VAL A  84      55.458  -8.912  30.483  1.00 19.58           C  
ANISOU  668  C   VAL A  84     3263   1285   2891    168   -187   -234       C  
ATOM    669  O   VAL A  84      54.974  -8.722  31.572  1.00 18.62           O  
ANISOU  669  O   VAL A  84     3130   1159   2785    144   -185   -208       O  
ATOM    670  CB  VAL A  84      57.672  -9.897  31.007  1.00 20.72           C  
ANISOU  670  CB  VAL A  84     3419   1420   3033    223   -183   -253       C  
ATOM    671  CG1 VAL A  84      57.118 -11.228  30.519  1.00 20.94           C  
ANISOU  671  CG1 VAL A  84     3480   1403   3070    224   -218   -273       C  
ATOM    672  CG2 VAL A  84      59.186  -9.771  30.856  1.00 21.32           C  
ANISOU  672  CG2 VAL A  84     3487   1521   3092    262   -166   -264       C  
ATOM    673  N   PRO A  85      54.707  -9.269  29.440  1.00 20.78           N  
ANISOU  673  N   PRO A  85     3429   1428   3037    162   -206   -250       N  
ATOM    674  CA  PRO A  85      53.256  -9.369  29.622  1.00 20.60           C  
ANISOU  674  CA  PRO A  85     3408   1391   3028    123   -223   -231       C  
ATOM    675  C   PRO A  85      52.785 -10.388  30.678  1.00 21.40           C  
ANISOU  675  C   PRO A  85     3522   1453   3155    103   -246   -214       C  
ATOM    676  O   PRO A  85      53.474 -11.415  30.902  1.00 21.36           O  
ANISOU  676  O   PRO A  85     3538   1417   3158    121   -262   -227       O  
ATOM    677  CB  PRO A  85      52.735  -9.683  28.226  1.00 21.93           C  
ANISOU  677  CB  PRO A  85     3592   1557   3183    124   -241   -255       C  
ATOM    678  CG  PRO A  85      53.821  -9.268  27.287  1.00 22.04           C  
ANISOU  678  CG  PRO A  85     3603   1599   3170    161   -223   -281       C  
ATOM    679  CD  PRO A  85      55.109  -9.430  28.038  1.00 21.84           C  
ANISOU  679  CD  PRO A  85     3576   1574   3148    188   -210   -282       C  
ATOM    680  N   GLY A  86      51.625 -10.111  31.276  1.00 20.80           N  
ANISOU  680  N   GLY A  86     3432   1379   3091     67   -250   -184       N  
ATOM    681  CA  GLY A  86      51.048 -10.822  32.401  1.00 21.83           C  
ANISOU  681  CA  GLY A  86     3564   1485   3244     41   -268   -157       C  
ATOM    682  C   GLY A  86      49.924 -11.730  31.882  1.00 21.39           C  
ANISOU  682  C   GLY A  86     3527   1400   3197     13   -305   -155       C  
ATOM    683  O   GLY A  86      49.926 -12.116  30.726  1.00 24.17           O  
ANISOU  683  O   GLY A  86     3901   1741   3540     23   -321   -183       O  
ATOM    684  N   SER A  87      48.936 -12.037  32.724  1.00 22.14           N  
ANISOU  684  N   SER A  87     3614   1488   3309    -21   -320   -120       N  
ATOM    685  CA  SER A  87      47.861 -12.978  32.347  1.00 22.11           C  
ANISOU  685  CA  SER A  87     3628   1454   3316    -53   -360   -112       C  
ATOM    686  C   SER A  87      46.762 -12.357  31.457  1.00 22.42           C  
ANISOU  686  C   SER A  87     3656   1519   3343    -73   -361   -107       C  
ATOM    687  O   SER A  87      46.214 -13.003  30.604  1.00 22.91           O  
ANISOU  687  O   SER A  87     3738   1560   3404    -87   -391   -119       O  
ATOM    688  CB  SER A  87      47.294 -13.672  33.595  1.00 21.43           C  
ANISOU  688  CB  SER A  87     3535   1351   3253    -84   -380    -73       C  
ATOM    689  OG  SER A  87      48.369 -14.170  34.380  1.00 20.72           O  
ANISOU  689  OG  SER A  87     3455   1242   3175    -63   -378    -77       O  
ATOM    690  N   GLN A  88      46.553 -11.031  31.583  1.00 21.52           N  
ANISOU  690  N   GLN A  88     3509   1449   3216    -71   -325    -94       N  
ATOM    691  CA  GLN A  88      45.572 -10.311  30.805  1.00 21.37           C  
ANISOU  691  CA  GLN A  88     3475   1459   3185    -86   -321    -86       C  
ATOM    692  C   GLN A  88      46.254  -9.211  29.961  1.00 20.52           C  
ANISOU  692  C   GLN A  88     3359   1381   3057    -56   -290   -111       C  
ATOM    693  O   GLN A  88      47.360  -8.772  30.324  1.00 19.36           O  
ANISOU  693  O   GLN A  88     3208   1242   2906    -28   -265   -123       O  
ATOM    694  CB  GLN A  88      44.516  -9.693  31.741  1.00 21.61           C  
ANISOU  694  CB  GLN A  88     3471   1517   3221   -113   -309    -42       C  
ATOM    695  CG  GLN A  88      43.796 -10.769  32.557  1.00 23.10           C  
ANISOU  695  CG  GLN A  88     3664   1683   3429   -146   -341    -12       C  
ATOM    696  CD  GLN A  88      42.731 -10.258  33.485  1.00 23.09           C  
ANISOU  696  CD  GLN A  88     3627   1715   3430   -171   -331     33       C  
ATOM    697  OE1 GLN A  88      42.885 -10.289  34.724  1.00 24.56           O  
ANISOU  697  OE1 GLN A  88     3799   1907   3624   -172   -322     54       O  
ATOM    698  NE2 GLN A  88      41.632  -9.780  32.915  1.00 24.69           N  
ANISOU  698  NE2 GLN A  88     3813   1943   3624   -189   -332     50       N  
ATOM    699  N   PRO A  89      45.606  -8.769  28.840  1.00 20.13           N  
ANISOU  699  N   PRO A  89     3305   1350   2993    -63   -292   -115       N  
ATOM    700  CA  PRO A  89      46.176  -7.610  28.059  1.00 19.23           C  
ANISOU  700  CA  PRO A  89     3176   1269   2858    -37   -261   -131       C  
ATOM    701  C   PRO A  89      46.237  -6.281  28.854  1.00 17.51           C  
ANISOU  701  C   PRO A  89     2927   1082   2642    -32   -225   -109       C  
ATOM    702  O   PRO A  89      45.283  -5.925  29.551  1.00 17.39           O  
ANISOU  702  O   PRO A  89     2893   1079   2635    -52   -221    -78       O  
ATOM    703  CB  PRO A  89      45.236  -7.467  26.880  1.00 19.46           C  
ANISOU  703  CB  PRO A  89     3204   1313   2876    -54   -274   -131       C  
ATOM    704  CG  PRO A  89      44.681  -8.917  26.703  1.00 19.98           C  
ANISOU  704  CG  PRO A  89     3298   1340   2950    -77   -319   -137       C  
ATOM    705  CD  PRO A  89      44.423  -9.286  28.150  1.00 20.39           C  
ANISOU  705  CD  PRO A  89     3343   1377   3024    -94   -322   -107       C  
ATOM    706  N   GLY A  90      47.395  -5.654  28.837  1.00 16.67           N  
ANISOU  706  N   GLY A  90     2817    987   2527     -3   -201   -125       N  
ATOM    707  CA  GLY A  90      47.561  -4.349  29.601  1.00 15.68           C  
ANISOU  707  CA  GLY A  90     2666    886   2403      2   -168   -107       C  
ATOM    708  C   GLY A  90      48.161  -4.556  30.961  1.00 15.70           C  
ANISOU  708  C   GLY A  90     2669    878   2418      7   -160   -100       C  
ATOM    709  O   GLY A  90      48.517  -3.597  31.692  1.00 15.00           O  
ANISOU  709  O   GLY A  90     2564    805   2329     14   -135    -91       O  
ATOM    710  N   GLU A  91      48.417  -5.847  31.297  1.00 15.78           N  
ANISOU  710  N   GLU A  91     2699    857   2436      4   -183   -107       N  
ATOM    711  CA  GLU A  91      49.066  -6.280  32.492  1.00 16.07           C  
ANISOU  711  CA  GLU A  91     2739    881   2485      8   -182   -102       C  
ATOM    712  C   GLU A  91      50.504  -6.772  32.175  1.00 15.89           C  
ANISOU  712  C   GLU A  91     2735    845   2457     38   -182   -131       C  
ATOM    713  O   GLU A  91      50.709  -7.506  31.167  1.00 17.14           O  
ANISOU  713  O   GLU A  91     2915    988   2610     48   -200   -154       O  
ATOM    714  CB  GLU A  91      48.298  -7.477  33.088  1.00 16.87           C  
ANISOU  714  CB  GLU A  91     2850    955   2602    -16   -211    -85       C  
ATOM    715  CG  GLU A  91      48.674  -7.804  34.456  1.00 17.29           C  
ANISOU  715  CG  GLU A  91     2899   1001   2667    -18   -208    -69       C  
ATOM    716  CD  GLU A  91      47.810  -8.909  35.019  1.00 17.92           C  
ANISOU  716  CD  GLU A  91     2985   1059   2764    -47   -239    -45       C  
ATOM    717  OE1 GLU A  91      47.904 -10.059  34.504  1.00 19.27           O  
ANISOU  717  OE1 GLU A  91     3183   1196   2943    -50   -270    -58       O  
ATOM    718  OE2 GLU A  91      47.048  -8.597  35.987  1.00 18.31           O  
ANISOU  718  OE2 GLU A  91     3011   1128   2817    -66   -232    -13       O  
ATOM    719  N   PHE A  92      51.464  -6.442  33.026  1.00 15.10           N  
ANISOU  719  N   PHE A  92     2627    752   2357     52   -164   -129       N  
ATOM    720  CA  PHE A  92      52.872  -6.740  32.906  1.00 14.92           C  
ANISOU  720  CA  PHE A  92     2614    724   2328     81   -159   -149       C  
ATOM    721  C   PHE A  92      53.515  -6.985  34.237  1.00 14.50           C  
ANISOU  721  C   PHE A  92     2557    665   2285     83   -154   -137       C  
ATOM    722  O   PHE A  92      52.949  -6.720  35.234  1.00 14.21           O  
ANISOU  722  O   PHE A  92     2507    634   2257     64   -149   -114       O  
ATOM    723  CB  PHE A  92      53.727  -5.682  32.249  1.00 14.85           C  
ANISOU  723  CB  PHE A  92     2594    746   2301    102   -135   -161       C  
ATOM    724  CG  PHE A  92      53.144  -5.196  31.019  1.00 14.58           C  
ANISOU  724  CG  PHE A  92     2556    726   2255    100   -135   -169       C  
ATOM    725  CD1 PHE A  92      52.199  -4.188  31.080  1.00 14.42           C  
ANISOU  725  CD1 PHE A  92     2519    724   2236     80   -124   -150       C  
ATOM    726  CD2 PHE A  92      53.464  -5.727  29.795  1.00 14.75           C  
ANISOU  726  CD2 PHE A  92     2593    746   2263    117   -147   -194       C  
ATOM    727  CE1 PHE A  92      51.587  -3.802  29.950  1.00 14.69           C  
ANISOU  727  CE1 PHE A  92     2549    771   2260     76   -126   -154       C  
ATOM    728  CE2 PHE A  92      52.838  -5.363  28.645  1.00 15.22           C  
ANISOU  728  CE2 PHE A  92     2650    820   2311    112   -150   -200       C  
ATOM    729  CZ  PHE A  92      51.923  -4.277  28.717  1.00 15.33           C  
ANISOU  729  CZ  PHE A  92     2644    853   2327     91   -137   -177       C  
ATOM    730  N   THR A  93      54.692  -7.627  34.189  1.00 15.56           N  
ANISOU  730  N   THR A  93     2704    790   2418    108   -157   -153       N  
ATOM    731  CA  THR A  93      55.570  -7.802  35.334  1.00 15.97           C  
ANISOU  731  CA  THR A  93     2750    841   2476    115   -149   -142       C  
ATOM    732  C   THR A  93      56.941  -7.265  34.853  1.00 16.84           C  
ANISOU  732  C   THR A  93     2855    975   2568    146   -130   -159       C  
ATOM    733  O   THR A  93      57.184  -7.137  33.661  1.00 17.05           O  
ANISOU  733  O   THR A  93     2886   1009   2580    163   -129   -179       O  
ATOM    734  CB  THR A  93      55.636  -9.216  35.931  1.00 16.88           C  
ANISOU  734  CB  THR A  93     2883    920   2608    114   -175   -138       C  
ATOM    735  OG1 THR A  93      56.233 -10.072  34.978  1.00 17.01           O  
ANISOU  735  OG1 THR A  93     2923    916   2621    141   -190   -165       O  
ATOM    736  CG2 THR A  93      54.267  -9.777  36.331  1.00 16.71           C  
ANISOU  736  CG2 THR A  93     2866    878   2604     81   -197   -118       C  
ATOM    737  N   LEU A  94      57.790  -6.868  35.787  1.00 18.14           N  
ANISOU  737  N   LEU A  94     3005   1154   2731    150   -115   -147       N  
ATOM    738  CA  LEU A  94      59.152  -6.461  35.463  1.00 18.49           C  
ANISOU  738  CA  LEU A  94     3042   1222   2759    176    -99   -157       C  
ATOM    739  C   LEU A  94      59.966  -7.692  35.116  1.00 20.37           C  
ANISOU  739  C   LEU A  94     3298   1443   2999    206   -113   -173       C  
ATOM    740  O   LEU A  94      59.592  -8.825  35.521  1.00 21.57           O  
ANISOU  740  O   LEU A  94     3467   1560   3168    203   -135   -172       O  
ATOM    741  CB  LEU A  94      59.807  -5.669  36.592  1.00 18.22           C  
ANISOU  741  CB  LEU A  94     2988   1209   2723    169    -81   -139       C  
ATOM    742  CG  LEU A  94      59.579  -4.134  36.493  1.00 18.47           C  
ANISOU  742  CG  LEU A  94     3002   1268   2745    155    -61   -133       C  
ATOM    743  CD1 LEU A  94      58.129  -3.753  36.606  1.00 18.18           C  
ANISOU  743  CD1 LEU A  94     2966   1224   2718    130    -64   -125       C  
ATOM    744  CD2 LEU A  94      60.371  -3.538  37.605  1.00 18.71           C  
ANISOU  744  CD2 LEU A  94     3018   1315   2772    150    -48   -119       C  
ATOM    745  N   GLY A  95      60.993  -7.443  34.327  1.00 21.67           N  
ANISOU  745  N   GLY A  95     3457   1630   3144    235   -103   -188       N  
ATOM    746  CA  GLY A  95      61.933  -8.495  33.887  1.00 24.83           C  
ANISOU  746  CA  GLY A  95     3872   2022   3539    272   -112   -206       C  
ATOM    747  C   GLY A  95      62.489  -9.135  35.113  1.00 27.54           C  
ANISOU  747  C   GLY A  95     4215   2351   3897    275   -116   -191       C  
ATOM    748  O   GLY A  95      62.596  -8.476  36.176  1.00 31.03           O  
ANISOU  748  O   GLY A  95     4638   2807   4343    254   -103   -167       O  
ATOM    749  N   ALA A  96      62.808 -10.427  34.979  1.00 29.94           N  
ANISOU  749  N   ALA A  96     4541   2624   4210    300   -135   -204       N  
ATOM    750  CA  ALA A  96      63.361 -11.213  36.060  1.00 31.00           C  
ANISOU  750  CA  ALA A  96     4676   2740   4359    306   -142   -189       C  
ATOM    751  C   ALA A  96      64.488 -10.365  36.640  1.00 31.58           C  
ANISOU  751  C   ALA A  96     4722   2858   4419    312   -117   -172       C  
ATOM    752  O   ALA A  96      65.310  -9.803  35.905  1.00 34.10           O  
ANISOU  752  O   ALA A  96     5028   3212   4715    334   -101   -181       O  
ATOM    753  CB  ALA A  96      63.857 -12.553  35.533  1.00 31.78           C  
ANISOU  753  CB  ALA A  96     4802   2809   4463    345   -162   -211       C  
ATOM    754  N   ILE A  97      64.461 -10.197  37.956  1.00 30.88           N  
ANISOU  754  N   ILE A  97     4620   2771   4341    288   -114   -145       N  
ATOM    755  CA  ILE A  97      65.500  -9.432  38.671  1.00 27.60           C  
ANISOU  755  CA  ILE A  97     4178   2394   3913    288    -93   -127       C  
ATOM    756  C   ILE A  97      65.710 -10.108  40.028  1.00 25.71           C  
ANISOU  756  C   ILE A  97     3937   2141   3691    279   -101   -104       C  
ATOM    757  O   ILE A  97      64.808 -10.694  40.597  1.00 27.11           O  
ANISOU  757  O   ILE A  97     4125   2288   3888    259   -117    -95       O  
ATOM    758  CB  ILE A  97      65.163  -7.925  38.828  1.00 28.91           C  
ANISOU  758  CB  ILE A  97     4325   2591   4068    258    -74   -118       C  
ATOM    759  CG1 ILE A  97      63.826  -7.790  39.523  1.00 28.74           C  
ANISOU  759  CG1 ILE A  97     4307   2549   4062    221    -81   -107       C  
ATOM    760  CG2 ILE A  97      65.251  -7.178  37.486  1.00 29.73           C  
ANISOU  760  CG2 ILE A  97     4425   2717   4153    269    -64   -135       C  
ATOM    761  CD1 ILE A  97      63.982  -7.602  40.999  1.00 26.69           C  
ANISOU  761  CD1 ILE A  97     4034   2299   3808    201    -77    -83       C  
ATOM    762  N   LYS A  98      66.928 -10.026  40.513  1.00 24.66           N  
ANISOU  762  N   LYS A  98     3786   2033   3547    294    -90    -91       N  
ATOM    763  CA  LYS A  98      67.351 -10.773  41.660  1.00 23.92           C  
ANISOU  763  CA  LYS A  98     3689   1931   3467    294    -98    -70       C  
ATOM    764  C   LYS A  98      66.649 -10.367  42.959  1.00 22.56           C  
ANISOU  764  C   LYS A  98     3506   1761   3304    252    -97    -45       C  
ATOM    765  O   LYS A  98      66.675  -9.204  43.331  1.00 19.85           O  
ANISOU  765  O   LYS A  98     3145   1449   2947    230    -81    -38       O  
ATOM    766  CB  LYS A  98      68.850 -10.666  41.810  1.00 26.06           C  
ANISOU  766  CB  LYS A  98     3940   2236   3722    320    -85    -61       C  
ATOM    767  CG  LYS A  98      69.410 -11.472  42.962  1.00 27.66           C  
ANISOU  767  CG  LYS A  98     4137   2433   3937    324    -93    -36       C  
ATOM    768  CD  LYS A  98      70.939 -11.539  42.967  1.00 30.29           C  
ANISOU  768  CD  LYS A  98     4452   2801   4256    357    -82    -27       C  
ATOM    769  CE  LYS A  98      71.471 -12.544  41.947  1.00 31.47           C  
ANISOU  769  CE  LYS A  98     4617   2932   4405    409    -90    -48       C  
ATOM    770  NZ  LYS A  98      72.944 -12.418  41.735  1.00 32.77           N  
ANISOU  770  NZ  LYS A  98     4759   3141   4548    444    -75    -41       N  
ATOM    771  N   SER A  99      65.990 -11.316  43.615  1.00 19.99           N  
ANISOU  771  N   SER A  99     3192   1402   3000    240   -117    -33       N  
ATOM    772  CA  SER A  99      65.259 -11.076  44.854  1.00 19.14           C  
ANISOU  772  CA  SER A  99     3073   1299   2899    202   -118     -8       C  
ATOM    773  C   SER A  99      65.510 -12.215  45.849  1.00 20.38           C  
ANISOU  773  C   SER A  99     3229   1438   3074    203   -135     16       C  
ATOM    774  O   SER A  99      65.478 -13.366  45.397  1.00 21.16           O  
ANISOU  774  O   SER A  99     3350   1499   3191    222   -155     10       O  
ATOM    775  CB  SER A  99      63.780 -10.937  44.558  1.00 19.25           C  
ANISOU  775  CB  SER A  99     3097   1293   2921    177   -126    -14       C  
ATOM    776  OG  SER A  99      63.027 -10.588  45.711  1.00 20.68           O  
ANISOU  776  OG  SER A  99     3265   1487   3105    143   -124      8       O  
ATOM    777  N   PRO A 100      65.830 -11.931  47.130  1.00 20.29           N  
ANISOU  777  N   PRO A 100     3197   1454   3058    184   -127     43       N  
ATOM    778  CA  PRO A 100      66.181 -10.526  47.602  1.00 19.93           C  
ANISOU  778  CA  PRO A 100     3129   1455   2988    167   -103     45       C  
ATOM    779  C   PRO A 100      67.475 -10.023  46.971  1.00 19.44           C  
ANISOU  779  C   PRO A 100     3059   1418   2907    194    -88     33       C  
ATOM    780  O   PRO A 100      68.293 -10.805  46.514  1.00 19.13           O  
ANISOU  780  O   PRO A 100     3025   1370   2873    226    -94     30       O  
ATOM    781  CB  PRO A 100      66.428 -10.733  49.092  1.00 20.35           C  
ANISOU  781  CB  PRO A 100     3164   1526   3042    149   -104     76       C  
ATOM    782  CG  PRO A 100      66.927 -12.139  49.180  1.00 20.70           C  
ANISOU  782  CG  PRO A 100     3216   1543   3105    171   -123     90       C  
ATOM    783  CD  PRO A 100      66.149 -12.918  48.177  1.00 21.29           C  
ANISOU  783  CD  PRO A 100     3318   1571   3199    182   -141     72       C  
ATOM    784  N   PRO A 101      67.704  -8.692  46.935  1.00 17.66           N  
ANISOU  784  N   PRO A 101     2821   1227   2662    181    -69     27       N  
ATOM    785  CA  PRO A 101      66.915  -7.675  47.587  1.00 17.25           C  
ANISOU  785  CA  PRO A 101     2762   1189   2603    147    -61     30       C  
ATOM    786  C   PRO A 101      65.891  -6.999  46.644  1.00 15.82           C  
ANISOU  786  C   PRO A 101     2593    996   2421    140    -57      8       C  
ATOM    787  O   PRO A 101      65.208  -6.062  47.051  1.00 15.13           O  
ANISOU  787  O   PRO A 101     2501    920   2327    116    -49      7       O  
ATOM    788  CB  PRO A 101      67.981  -6.642  47.964  1.00 17.53           C  
ANISOU  788  CB  PRO A 101     2778   1264   2616    141    -45     35       C  
ATOM    789  CG  PRO A 101      68.946  -6.713  46.846  1.00 17.10           C  
ANISOU  789  CG  PRO A 101     2724   1216   2555    171    -42     25       C  
ATOM    790  CD  PRO A 101      69.037  -8.236  46.580  1.00 18.28           C  
ANISOU  790  CD  PRO A 101     2885   1336   2722    200    -57     26       C  
ATOM    791  N   GLY A 102      65.796  -7.394  45.387  1.00 15.03           N  
ANISOU  791  N   GLY A 102     2507    876   2326    162    -62     -9       N  
ATOM    792  CA  GLY A 102      64.717  -6.998  44.568  1.00 14.10           C  
ANISOU  792  CA  GLY A 102     2401    745   2212    154    -63    -26       C  
ATOM    793  C   GLY A 102      63.359  -7.470  45.017  1.00 14.11           C  
ANISOU  793  C   GLY A 102     2409    722   2228    133    -75    -18       C  
ATOM    794  O   GLY A 102      63.237  -8.304  45.983  1.00 14.38           O  
ANISOU  794  O   GLY A 102     2442    747   2274    125    -87      1       O  
ATOM    795  N   PRO A 103      62.322  -7.017  44.361  1.00 13.95           N  
ANISOU  795  N   PRO A 103     2396    694   2209    124    -75    -30       N  
ATOM    796  CA  PRO A 103      60.991  -7.430  44.714  1.00 13.50           C  
ANISOU  796  CA  PRO A 103     2344    619   2165    103    -87    -20       C  
ATOM    797  C   PRO A 103      60.734  -8.932  44.357  1.00 13.71           C  
ANISOU  797  C   PRO A 103     2388    608   2211    112   -112    -18       C  
ATOM    798  O   PRO A 103      61.225  -9.413  43.343  1.00 13.77           O  
ANISOU  798  O   PRO A 103     2410    598   2220    136   -119    -36       O  
ATOM    799  CB  PRO A 103      60.112  -6.440  43.938  1.00 13.58           C  
ANISOU  799  CB  PRO A 103     2355    635   2169     95    -77    -34       C  
ATOM    800  CG  PRO A 103      60.887  -6.075  42.785  1.00 13.53           C  
ANISOU  800  CG  PRO A 103     2353    633   2152    117    -70    -54       C  
ATOM    801  CD  PRO A 103      62.252  -5.910  43.386  1.00 13.73           C  
ANISOU  801  CD  PRO A 103     2368    679   2168    127    -61    -48       C  
ATOM    802  N   THR A 104      59.970  -9.586  45.208  1.00 13.76           N  
ANISOU  802  N   THR A 104     2393    603   2231     91   -127      4       N  
ATOM    803  CA  THR A 104      59.602 -11.005  44.907  1.00 14.21           C  
ANISOU  803  CA  THR A 104     2470    619   2311     93   -156      8       C  
ATOM    804  C   THR A 104      58.527 -11.088  43.862  1.00 14.50           C  
ANISOU  804  C   THR A 104     2522    635   2353     87   -168     -5       C  
ATOM    805  O   THR A 104      58.365 -12.139  43.126  1.00 15.36           O  
ANISOU  805  O   THR A 104     2653    704   2476     95   -192    -14       O  
ATOM    806  CB  THR A 104      59.158 -11.749  46.141  1.00 14.66           C  
ANISOU  806  CB  THR A 104     2517    669   2381     71   -171     42       C  
ATOM    807  OG1 THR A 104      58.262 -10.959  46.943  1.00 14.77           O  
ANISOU  807  OG1 THR A 104     2511    713   2385     43   -159     59       O  
ATOM    808  CG2 THR A 104      60.342 -12.144  46.949  1.00 14.73           C  
ANISOU  808  CG2 THR A 104     2518    685   2390     84   -169     55       C  
ATOM    809  N   SER A 105      57.701 -10.030  43.779  1.00 14.45           N  
ANISOU  809  N   SER A 105     2504    651   2335     70   -153     -5       N  
ATOM    810  CA  SER A 105      56.791  -9.936  42.653  1.00 14.67           C  
ANISOU  810  CA  SER A 105     2543    666   2364     66   -160    -20       C  
ATOM    811  C   SER A 105      56.617  -8.458  42.269  1.00 14.14           C  
ANISOU  811  C   SER A 105     2463    630   2278     65   -134    -32       C  
ATOM    812  O   SER A 105      56.695  -7.645  43.096  1.00 14.24           O  
ANISOU  812  O   SER A 105     2458    669   2282     58   -116    -22       O  
ATOM    813  CB  SER A 105      55.430 -10.487  42.944  1.00 15.06           C  
ANISOU  813  CB  SER A 105     2592    701   2426     36   -180      0       C  
ATOM    814  OG  SER A 105      54.828  -9.936  44.106  1.00 15.13           O  
ANISOU  814  OG  SER A 105     2578    740   2431     14   -169     26       O  
ATOM    815  N   THR A 106      56.266  -8.291  41.017  1.00 14.67           N  
ANISOU  815  N   THR A 106     2541    689   2342     72   -137    -52       N  
ATOM    816  CA  THR A 106      55.810  -6.985  40.543  1.00 14.65           C  
ANISOU  816  CA  THR A 106     2528    711   2327     68   -117    -59       C  
ATOM    817  C   THR A 106      54.552  -7.155  39.729  1.00 14.61           C  
ANISOU  817  C   THR A 106     2529    694   2326     55   -130    -60       C  
ATOM    818  O   THR A 106      54.246  -8.238  39.165  1.00 15.43           O  
ANISOU  818  O   THR A 106     2652    769   2441     53   -155    -64       O  
ATOM    819  CB  THR A 106      56.876  -6.291  39.671  1.00 15.07           C  
ANISOU  819  CB  THR A 106     2581    777   2365     92   -101    -81       C  
ATOM    820  OG1 THR A 106      57.186  -7.068  38.497  1.00 15.75           O  
ANISOU  820  OG1 THR A 106     2687    845   2452    111   -116   -102       O  
ATOM    821  CG2 THR A 106      58.179  -6.060  40.442  1.00 14.88           C  
ANISOU  821  CG2 THR A 106     2549    770   2335    104    -88    -78       C  
ATOM    822  N   LEU A 107      53.867  -6.055  39.517  1.00 14.22           N  
ANISOU  822  N   LEU A 107     2467    666   2268     46   -115    -58       N  
ATOM    823  CA  LEU A 107      52.708  -6.005  38.702  1.00 14.11           C  
ANISOU  823  CA  LEU A 107     2456    648   2256     34   -124    -58       C  
ATOM    824  C   LEU A 107      52.540  -4.617  38.097  1.00 13.49           C  
ANISOU  824  C   LEU A 107     2366    594   2165     39   -102    -66       C  
ATOM    825  O   LEU A 107      52.660  -3.660  38.846  1.00 14.04           O  
ANISOU  825  O   LEU A 107     2421    683   2228     39    -82    -59       O  
ATOM    826  CB  LEU A 107      51.476  -6.411  39.428  1.00 14.91           C  
ANISOU  826  CB  LEU A 107     2549    749   2367      8   -136    -31       C  
ATOM    827  CG  LEU A 107      50.151  -6.403  38.687  1.00 15.25           C  
ANISOU  827  CG  LEU A 107     2590    791   2410     -8   -147    -24       C  
ATOM    828  CD1 LEU A 107      50.111  -7.303  37.463  1.00 15.78           C  
ANISOU  828  CD1 LEU A 107     2681    831   2484     -6   -172    -41       C  
ATOM    829  CD2 LEU A 107      48.997  -6.655  39.618  1.00 15.79           C  
ANISOU  829  CD2 LEU A 107     2643    869   2486    -34   -155      8       C  
ATOM    830  N   VAL A 108      52.146  -4.566  36.846  1.00 13.11           N  
ANISOU  830  N   VAL A 108     2325    542   2113     42   -108    -78       N  
ATOM    831  CA  VAL A 108      51.795  -3.281  36.135  1.00 12.70           C  
ANISOU  831  CA  VAL A 108     2261    511   2050     44    -91    -81       C  
ATOM    832  C   VAL A 108      50.431  -3.499  35.525  1.00 13.20           C  
ANISOU  832  C   VAL A 108     2324    572   2117     27   -104    -72       C  
ATOM    833  O   VAL A 108      50.206  -4.536  34.798  1.00 13.26           O  
ANISOU  833  O   VAL A 108     2348    560   2129     23   -128    -80       O  
ATOM    834  CB  VAL A 108      52.787  -2.956  35.026  1.00 12.23           C  
ANISOU  834  CB  VAL A 108     2208    457   1980     65    -85   -103       C  
ATOM    835  CG1 VAL A 108      52.524  -1.462  34.592  1.00 12.00           C  
ANISOU  835  CG1 VAL A 108     2163    452   1943     65    -65   -100       C  
ATOM    836  CG2 VAL A 108      54.149  -2.988  35.523  1.00 12.30           C  
ANISOU  836  CG2 VAL A 108     2219    469   1986     81    -76   -110       C  
ATOM    837  N   ARG A 109      49.499  -2.569  35.702  1.00 12.72           N  
ANISOU  837  N   ARG A 109     2247    530   2056     18    -92    -57       N  
ATOM    838  CA  ARG A 109      48.176  -2.655  35.082  1.00 12.48           C  
ANISOU  838  CA  ARG A 109     2211    503   2026      2   -103    -45       C  
ATOM    839  C   ARG A 109      47.949  -1.331  34.449  1.00 12.07           C  
ANISOU  839  C   ARG A 109     2146    472   1966     10    -84    -46       C  
ATOM    840  O   ARG A 109      47.894  -0.367  35.196  1.00 12.29           O  
ANISOU  840  O   ARG A 109     2161    513   1993     14    -64    -38       O  
ATOM    841  CB  ARG A 109      47.098  -2.915  36.094  1.00 12.81           C  
ANISOU  841  CB  ARG A 109     2239    551   2075    -17   -108    -17       C  
ATOM    842  CG  ARG A 109      47.116  -4.420  36.456  1.00 13.10           C  
ANISOU  842  CG  ARG A 109     2290    563   2122    -31   -135    -11       C  
ATOM    843  CD  ARG A 109      45.757  -4.830  36.887  1.00 13.64           C  
ANISOU  843  CD  ARG A 109     2345    639   2196    -57   -149     18       C  
ATOM    844  NE  ARG A 109      45.569  -6.278  36.749  1.00 14.63           N  
ANISOU  844  NE  ARG A 109     2488    736   2333    -75   -184     24       N  
ATOM    845  CZ  ARG A 109      44.444  -6.876  37.052  1.00 15.14           C  
ANISOU  845  CZ  ARG A 109     2544    803   2404   -103   -203     53       C  
ATOM    846  NH1 ARG A 109      43.420  -6.226  37.574  1.00 15.79           N  
ANISOU  846  NH1 ARG A 109     2599    919   2482   -114   -191     81       N  
ATOM    847  NH2 ARG A 109      44.384  -8.251  36.910  1.00 15.78           N  
ANISOU  847  NH2 ARG A 109     2645    850   2498   -121   -239     57       N  
ATOM    848  N   VAL A 110      47.752  -1.311  33.150  1.00 12.23           N  
ANISOU  848  N   VAL A 110     2171    494   1981     11    -91    -55       N  
ATOM    849  CA  VAL A 110      47.266  -0.045  32.506  1.00 11.97           C  
ANISOU  849  CA  VAL A 110     2123    482   1943     14    -75    -49       C  
ATOM    850  C   VAL A 110      45.754  -0.010  32.762  1.00 12.09           C  
ANISOU  850  C   VAL A 110     2123    506   1962     -3    -80    -24       C  
ATOM    851  O   VAL A 110      44.936  -0.783  32.161  1.00 12.40           O  
ANISOU  851  O   VAL A 110     2165    543   2001    -19   -100    -17       O  
ATOM    852  CB  VAL A 110      47.593  -0.014  30.985  1.00 11.87           C  
ANISOU  852  CB  VAL A 110     2117    473   1920     21    -81    -65       C  
ATOM    853  CG1 VAL A 110      47.021   1.286  30.403  1.00 11.84           C  
ANISOU  853  CG1 VAL A 110     2094    490   1912     23    -66    -53       C  
ATOM    854  CG2 VAL A 110      49.100  -0.043  30.755  1.00 11.70           C  
ANISOU  854  CG2 VAL A 110     2105    448   1891     41    -76    -87       C  
ATOM    855  N   VAL A 111      45.378   0.858  33.703  1.00 12.00           N  
ANISOU  855  N   VAL A 111     2096    509   1953      0    -61     -9       N  
ATOM    856  CA  VAL A 111      44.000   0.968  34.126  1.00 12.42           C  
ANISOU  856  CA  VAL A 111     2131    578   2008    -11    -61     16       C  
ATOM    857  C   VAL A 111      43.140   1.544  33.008  1.00 12.58           C  
ANISOU  857  C   VAL A 111     2140    612   2024    -13    -61     25       C  
ATOM    858  O   VAL A 111      42.062   1.040  32.677  1.00 13.10           O  
ANISOU  858  O   VAL A 111     2198    687   2090    -31    -76     44       O  
ATOM    859  CB  VAL A 111      43.880   1.727  35.463  1.00 12.16           C  
ANISOU  859  CB  VAL A 111     2086    558   1976     -1    -41     26       C  
ATOM    860  CG1 VAL A 111      42.454   1.883  35.871  1.00 12.18           C  
ANISOU  860  CG1 VAL A 111     2066    583   1977     -9    -39     54       C  
ATOM    861  CG2 VAL A 111      44.677   1.073  36.597  1.00 12.42           C  
ANISOU  861  CG2 VAL A 111     2127    579   2010     -2    -43     20       C  
ATOM    862  N   SER A 112      43.575   2.737  32.507  1.00 12.69           N  
ANISOU  862  N   SER A 112     2151    632   2036      3    -43     17       N  
ATOM    863  CA  SER A 112      42.810   3.419  31.462  1.00 12.92           C  
ANISOU  863  CA  SER A 112     2168    677   2062      3    -41     28       C  
ATOM    864  C   SER A 112      43.740   4.165  30.553  1.00 12.80           C  
ANISOU  864  C   SER A 112     2158    660   2044     16    -34     12       C  
ATOM    865  O   SER A 112      44.755   4.731  31.004  1.00 12.73           O  
ANISOU  865  O   SER A 112     2156    644   2037     29    -21      0       O  
ATOM    866  CB  SER A 112      41.837   4.446  32.055  1.00 13.06           C  
ANISOU  866  CB  SER A 112     2165    713   2083     11    -24     50       C  
ATOM    867  OG  SER A 112      42.384   5.058  33.201  1.00 13.47           O  
ANISOU  867  OG  SER A 112     2218    760   2137     26     -7     42       O  
ATOM    868  N   THR A 113      43.401   4.190  29.253  1.00 12.90           N  
ANISOU  868  N   THR A 113     2167    682   2050     10    -42     15       N  
ATOM    869  CA  THR A 113      44.154   5.054  28.331  1.00 13.16           C  
ANISOU  869  CA  THR A 113     2199    721   2078     22    -34      6       C  
ATOM    870  C   THR A 113      43.360   5.204  27.069  1.00 13.51           C  
ANISOU  870  C   THR A 113     2233    784   2117     14    -42     19       C  
ATOM    871  O   THR A 113      42.554   4.310  26.717  1.00 14.16           O  
ANISOU  871  O   THR A 113     2315    870   2194     -1    -59     24       O  
ATOM    872  CB  THR A 113      45.540   4.492  27.945  1.00 12.65           C  
ANISOU  872  CB  THR A 113     2152    647   2006     28    -40    -18       C  
ATOM    873  OG1 THR A 113      46.206   5.282  27.008  1.00 12.76           O  
ANISOU  873  OG1 THR A 113     2161    673   2012     38    -33    -22       O  
ATOM    874  CG2 THR A 113      45.492   2.999  27.363  1.00 12.62           C  
ANISOU  874  CG2 THR A 113     2164    637   1994     18    -64    -33       C  
ATOM    875  N   ASN A 114      43.512   6.381  26.439  1.00 13.67           N  
ANISOU  875  N   ASN A 114     2241    816   2137     24    -30     26       N  
ATOM    876  CA  ASN A 114      43.022   6.587  25.080  1.00 13.95           C  
ANISOU  876  CA  ASN A 114     2265    872   2163     18    -37     37       C  
ATOM    877  C   ASN A 114      44.131   6.724  24.070  1.00 13.63           C  
ANISOU  877  C   ASN A 114     2228    838   2109     24    -38     22       C  
ATOM    878  O   ASN A 114      43.902   7.235  22.942  1.00 13.57           O  
ANISOU  878  O   ASN A 114     2208    852   2094     23    -39     34       O  
ATOM    879  CB  ASN A 114      42.032   7.734  25.033  1.00 13.88           C  
ANISOU  879  CB  ASN A 114     2235    875   2163     22    -25     65       C  
ATOM    880  CG  ASN A 114      42.672   9.035  25.264  1.00 13.90           C  
ANISOU  880  CG  ASN A 114     2233    871   2174     39     -8     68       C  
ATOM    881  OD1 ASN A 114      43.924   9.110  25.366  1.00 13.97           O  
ANISOU  881  OD1 ASN A 114     2255    870   2182     45     -5     50       O  
ATOM    882  ND2 ASN A 114      41.854  10.088  25.344  1.00 14.42           N  
ANISOU  882  ND2 ASN A 114     2284    943   2251     47      2     91       N  
ATOM    883  N   TYR A 115      45.318   6.234  24.425  1.00 13.91           N  
ANISOU  883  N   TYR A 115     2281    861   2142     32    -38      0       N  
ATOM    884  CA  TYR A 115      46.457   6.087  23.492  1.00 13.93           C  
ANISOU  884  CA  TYR A 115     2288    876   2129     39    -42    -16       C  
ATOM    885  C   TYR A 115      47.081   7.422  23.083  1.00 13.52           C  
ANISOU  885  C   TYR A 115     2222    837   2077     48    -28     -4       C  
ATOM    886  O   TYR A 115      48.302   7.515  23.047  1.00 13.39           O  
ANISOU  886  O   TYR A 115     2209    823   2055     57    -24    -14       O  
ATOM    887  CB  TYR A 115      46.083   5.266  22.281  1.00 14.33           C  
ANISOU  887  CB  TYR A 115     2341    942   2161     32    -59    -25       C  
ATOM    888  CG  TYR A 115      45.566   3.903  22.715  1.00 14.65           C  
ANISOU  888  CG  TYR A 115     2399    963   2202     21    -77    -38       C  
ATOM    889  CD1 TYR A 115      46.386   3.083  23.450  1.00 15.05           C  
ANISOU  889  CD1 TYR A 115     2469    993   2255     28    -80    -59       C  
ATOM    890  CD2 TYR A 115      44.222   3.582  22.626  1.00 14.98           C  
ANISOU  890  CD2 TYR A 115     2435   1007   2247      3    -88    -22       C  
ATOM    891  CE1 TYR A 115      45.923   1.869  23.930  1.00 15.14           C  
ANISOU  891  CE1 TYR A 115     2496    982   2271     17    -98    -67       C  
ATOM    892  CE2 TYR A 115      43.735   2.322  23.142  1.00 15.78           C  
ANISOU  892  CE2 TYR A 115     2554   1089   2353    -10   -108    -30       C  
ATOM    893  CZ  TYR A 115      44.570   1.559  23.834  1.00 15.25           C  
ANISOU  893  CZ  TYR A 115     2506    999   2290     -3   -111    -51       C  
ATOM    894  OH  TYR A 115      44.090   0.339  24.334  1.00 15.79           O  
ANISOU  894  OH  TYR A 115     2589   1044   2363    -18   -132    -55       O  
ATOM    895  N   ASN A 116      46.241   8.425  22.837  1.00 13.96           N  
ANISOU  895  N   ASN A 116     2261    901   2142     44    -22     21       N  
ATOM    896  CA  ASN A 116      46.768   9.672  22.213  1.00 13.88           C  
ANISOU  896  CA  ASN A 116     2236    904   2133     49    -14     37       C  
ATOM    897  C   ASN A 116      46.758  10.850  23.114  1.00 13.87           C  
ANISOU  897  C   ASN A 116     2232    883   2152     55     -1     50       C  
ATOM    898  O   ASN A 116      47.320  11.903  22.698  1.00 13.83           O  
ANISOU  898  O   ASN A 116     2217    883   2151     58      2     64       O  
ATOM    899  CB  ASN A 116      45.979   9.958  20.939  1.00 14.07           C  
ANISOU  899  CB  ASN A 116     2242    955   2148     43    -19     56       C  
ATOM    900  CG  ASN A 116      46.196   8.892  19.869  1.00 14.02           C  
ANISOU  900  CG  ASN A 116     2239    971   2115     39    -33     39       C  
ATOM    901  OD1 ASN A 116      47.320   8.585  19.533  1.00 14.42           O  
ANISOU  901  OD1 ASN A 116     2295   1031   2151     46    -35     22       O  
ATOM    902  ND2 ASN A 116      45.128   8.401  19.312  1.00 14.56           N  
ANISOU  902  ND2 ASN A 116     2303   1051   2177     28    -44     44       N  
ATOM    903  N   GLN A 117      46.193  10.717  24.318  1.00 13.60           N  
ANISOU  903  N   GLN A 117     2205    828   2131     57      3     47       N  
ATOM    904  CA  GLN A 117      46.086  11.824  25.282  1.00 13.68           C  
ANISOU  904  CA  GLN A 117     2217    819   2161     66     15     56       C  
ATOM    905  C   GLN A 117      46.624  11.451  26.669  1.00 13.41           C  
ANISOU  905  C   GLN A 117     2200    763   2132     70     20     37       C  
ATOM    906  O   GLN A 117      47.530  12.107  27.234  1.00 13.59           O  
ANISOU  906  O   GLN A 117     2230    772   2161     74     25     32       O  
ATOM    907  CB  GLN A 117      44.673  12.242  25.387  1.00 13.61           C  
ANISOU  907  CB  GLN A 117     2196    811   2161     68     19     75       C  
ATOM    908  CG  GLN A 117      44.474  13.526  26.173  1.00 13.92           C  
ANISOU  908  CG  GLN A 117     2236    832   2220     82     31     85       C  
ATOM    909  CD  GLN A 117      42.989  13.783  26.515  1.00 14.50           C  
ANISOU  909  CD  GLN A 117     2297    909   2301     90     37    101       C  
ATOM    910  OE1 GLN A 117      42.119  12.905  26.444  1.00 15.05           O  
ANISOU  910  OE1 GLN A 117     2360    995   2363     83     32    106       O  
ATOM    911  NE2 GLN A 117      42.696  15.011  26.903  1.00 15.47           N  
ANISOU  911  NE2 GLN A 117     2419   1018   2440    106     46    112       N  
ATOM    912  N   HIS A 118      46.029  10.422  27.280  1.00 13.41           N  
ANISOU  912  N   HIS A 118     2205    761   2128     66     16     29       N  
ATOM    913  CA  HIS A 118      46.249  10.164  28.701  1.00 12.90           C  
ANISOU  913  CA  HIS A 118     2152    679   2069     70     22     17       C  
ATOM    914  C   HIS A 118      46.423   8.663  28.928  1.00 12.69           C  
ANISOU  914  C   HIS A 118     2135    652   2033     62     11      2       C  
ATOM    915  O   HIS A 118      45.904   7.898  28.137  1.00 12.95           O  
ANISOU  915  O   HIS A 118     2165    695   2059     53      0      4       O  
ATOM    916  CB  HIS A 118      45.101  10.652  29.532  1.00 13.72           C  
ANISOU  916  CB  HIS A 118     2249    779   2182     77     31     29       C  
ATOM    917  CG  HIS A 118      43.833   9.932  29.297  1.00 14.26           C  
ANISOU  917  CG  HIS A 118     2306    862   2247     69     25     42       C  
ATOM    918  ND1 HIS A 118      43.525   8.737  29.923  1.00 14.92           N  
ANISOU  918  ND1 HIS A 118     2395    947   2327     60     17     37       N  
ATOM    919  CD2 HIS A 118      42.870  10.114  28.374  1.00 15.01           C  
ANISOU  919  CD2 HIS A 118     2386    974   2341     66     21     61       C  
ATOM    920  CE1 HIS A 118      42.358   8.310  29.498  1.00 15.12           C  
ANISOU  920  CE1 HIS A 118     2407    987   2348     51     10     54       C  
ATOM    921  NE2 HIS A 118      41.971   9.062  28.517  1.00 15.92           N  
ANISOU  921  NE2 HIS A 118     2497   1100   2451     53     12     68       N  
ATOM    922  N   ALA A 119      46.960   8.327  30.076  1.00 11.96           N  
ANISOU  922  N   ALA A 119     2054    547   1943     64     14     -8       N  
ATOM    923  CA  ALA A 119      47.003   6.883  30.489  1.00 11.91           C  
ANISOU  923  CA  ALA A 119     2056    535   1931     56      3    -19       C  
ATOM    924  C   ALA A 119      47.151   6.946  31.993  1.00 11.88           C  
ANISOU  924  C   ALA A 119     2057    521   1933     60     12    -22       C  
ATOM    925  O   ALA A 119      47.796   7.910  32.508  1.00 11.99           O  
ANISOU  925  O   ALA A 119     2074    530   1952     68     23    -26       O  
ATOM    926  CB  ALA A 119      48.137   6.175  29.908  1.00 11.90           C  
ANISOU  926  CB  ALA A 119     2065    533   1921     57     -4    -36       C  
ATOM    927  N   MET A 120      46.666   5.895  32.717  1.00 11.75           N  
ANISOU  927  N   MET A 120     2044    503   1918     52      4    -20       N  
ATOM    928  CA  MET A 120      46.799   5.818  34.141  1.00 11.63           C  
ANISOU  928  CA  MET A 120     2031    483   1905     54     11    -22       C  
ATOM    929  C   MET A 120      47.253   4.389  34.416  1.00 11.82           C  
ANISOU  929  C   MET A 120     2065    498   1926     45     -3    -29       C  
ATOM    930  O   MET A 120      46.680   3.503  33.833  1.00 12.38           O  
ANISOU  930  O   MET A 120     2137    569   1997     34    -18    -24       O  
ATOM    931  CB  MET A 120      45.471   6.124  34.810  1.00 12.11           C  
ANISOU  931  CB  MET A 120     2077    555   1967     54     18     -4       C  
ATOM    932  CG  MET A 120      45.543   6.145  36.323  1.00 12.38           C  
ANISOU  932  CG  MET A 120     2112    590   2000     58     26     -5       C  
ATOM    933  SD  MET A 120      44.028   6.779  37.055  1.00 13.81           S  
ANISOU  933  SD  MET A 120     2273    792   2180     67     39     14       S  
ATOM    934  CE  MET A 120      42.799   5.644  36.547  1.00 14.02           C  
ANISOU  934  CE  MET A 120     2286    833   2206     48     22     37       C  
ATOM    935  N   VAL A 121      48.365   4.271  35.102  1.00 11.51           N  
ANISOU  935  N   VAL A 121     2034    451   1886     49      0    -41       N  
ATOM    936  CA  VAL A 121      49.023   2.963  35.240  1.00 11.31           C  
ANISOU  936  CA  VAL A 121     2021    415   1859     45    -13    -49       C  
ATOM    937  C   VAL A 121      49.130   2.702  36.733  1.00 11.28           C  
ANISOU  937  C   VAL A 121     2017    411   1858     42    -10    -45       C  
ATOM    938  O   VAL A 121      49.612   3.524  37.512  1.00 11.30           O  
ANISOU  938  O   VAL A 121     2017    417   1859     49      3    -48       O  
ATOM    939  CB  VAL A 121      50.356   2.959  34.510  1.00 11.14           C  
ANISOU  939  CB  VAL A 121     2008    390   1832     54    -14    -66       C  
ATOM    940  CG1 VAL A 121      51.048   1.634  34.746  1.00 11.40           C  
ANISOU  940  CG1 VAL A 121     2053    411   1865     55    -28    -75       C  
ATOM    941  CG2 VAL A 121      50.140   3.161  33.043  1.00 11.10           C  
ANISOU  941  CG2 VAL A 121     2002    392   1823     56    -19    -68       C  
ATOM    942  N   PHE A 122      48.863   1.412  37.118  1.00 11.33           N  
ANISOU  942  N   PHE A 122     2026    409   1867     32    -25    -39       N  
ATOM    943  CA  PHE A 122      49.015   0.988  38.480  1.00 11.49           C  
ANISOU  943  CA  PHE A 122     2045    431   1889     27    -24    -31       C  
ATOM    944  C   PHE A 122      50.312   0.118  38.545  1.00 11.92           C  
ANISOU  944  C   PHE A 122     2112    470   1944     31    -34    -44       C  
ATOM    945  O   PHE A 122      50.565  -0.685  37.592  1.00 12.28           O  
ANISOU  945  O   PHE A 122     2171    502   1993     32    -49    -53       O  
ATOM    946  CB  PHE A 122      47.746   0.195  38.920  1.00 11.73           C  
ANISOU  946  CB  PHE A 122     2066    466   1923     11    -37     -9       C  
ATOM    947  CG  PHE A 122      47.911  -0.493  40.191  1.00 11.65           C  
ANISOU  947  CG  PHE A 122     2053    457   1914      4    -41      1       C  
ATOM    948  CD1 PHE A 122      47.707   0.076  41.383  1.00 11.86           C  
ANISOU  948  CD1 PHE A 122     2067    503   1934      6    -26      9       C  
ATOM    949  CD2 PHE A 122      48.268  -1.873  40.184  1.00 11.88           C  
ANISOU  949  CD2 PHE A 122     2094    468   1952     -5    -63      3       C  
ATOM    950  CE1 PHE A 122      47.909  -0.514  42.585  1.00 12.11           C  
ANISOU  950  CE1 PHE A 122     2094    541   1964      0    -29     20       C  
ATOM    951  CE2 PHE A 122      48.441  -2.497  41.376  1.00 12.17           C  
ANISOU  951  CE2 PHE A 122     2126    506   1990    -12    -67     16       C  
ATOM    952  CZ  PHE A 122      48.164  -1.916  42.578  1.00 12.22           C  
ANISOU  952  CZ  PHE A 122     2117    538   1989    -12    -52     28       C  
ATOM    953  N   PHE A 123      51.113   0.343  39.587  1.00 12.30           N  
ANISOU  953  N   PHE A 123     2160    522   1989     35    -24    -46       N  
ATOM    954  CA  PHE A 123      52.349  -0.477  39.833  1.00 12.87           C  
ANISOU  954  CA  PHE A 123     2242    584   2062     40    -32    -54       C  
ATOM    955  C   PHE A 123      52.327  -1.045  41.193  1.00 13.38           C  
ANISOU  955  C   PHE A 123     2302    652   2129     32    -34    -40       C  
ATOM    956  O   PHE A 123      51.955  -0.369  42.170  1.00 14.01           O  
ANISOU  956  O   PHE A 123     2370    748   2203     28    -22    -32       O  
ATOM    957  CB  PHE A 123      53.616   0.372  39.716  1.00 12.81           C  
ANISOU  957  CB  PHE A 123     2235    582   2046     53    -19    -67       C  
ATOM    958  CG  PHE A 123      53.719   1.100  38.443  1.00 12.81           C  
ANISOU  958  CG  PHE A 123     2237    585   2044     60    -14    -77       C  
ATOM    959  CD1 PHE A 123      52.947   2.271  38.225  1.00 12.86           C  
ANISOU  959  CD1 PHE A 123     2236    600   2050     58     -3    -73       C  
ATOM    960  CD2 PHE A 123      54.638   0.668  37.453  1.00 12.89           C  
ANISOU  960  CD2 PHE A 123     2255    593   2050     72    -20    -89       C  
ATOM    961  CE1 PHE A 123      53.063   2.939  37.033  1.00 12.87           C  
ANISOU  961  CE1 PHE A 123     2236    604   2047     64      0    -79       C  
ATOM    962  CE2 PHE A 123      54.718   1.346  36.260  1.00 13.39           C  
ANISOU  962  CE2 PHE A 123     2316    663   2108     78    -16    -95       C  
ATOM    963  CZ  PHE A 123      53.966   2.531  36.092  1.00 12.98           C  
ANISOU  963  CZ  PHE A 123     2255    618   2056     72     -6    -89       C  
ATOM    964  N   LYS A 124      52.645  -2.356  41.316  1.00 14.54           N  
ANISOU  964  N   LYS A 124     2457    782   2283     29    -52    -36       N  
ATOM    965  CA  LYS A 124      52.885  -2.911  42.622  1.00 15.94           C  
ANISOU  965  CA  LYS A 124     2629    964   2462     22    -55    -21       C  
ATOM    966  C   LYS A 124      54.275  -3.636  42.661  1.00 16.29           C  
ANISOU  966  C   LYS A 124     2684    996   2509     33    -62    -30       C  
ATOM    967  O   LYS A 124      54.652  -4.364  41.736  1.00 16.80           O  
ANISOU  967  O   LYS A 124     2763   1041   2580     43    -75    -40       O  
ATOM    968  CB  LYS A 124      51.779  -3.856  42.988  1.00 16.36           C  
ANISOU  968  CB  LYS A 124     2678   1012   2525      4    -73      0       C  
ATOM    969  CG  LYS A 124      51.808  -4.415  44.393  1.00 17.61           C  
ANISOU  969  CG  LYS A 124     2826   1180   2684     -6    -76     22       C  
ATOM    970  CD  LYS A 124      50.473  -5.052  44.759  1.00 18.67           C  
ANISOU  970  CD  LYS A 124     2949   1318   2824    -27    -91     50       C  
ATOM    971  CE  LYS A 124      50.574  -6.326  45.556  1.00 19.69           C  
ANISOU  971  CE  LYS A 124     3078   1438   2965    -41   -112     73       C  
ATOM    972  NZ  LYS A 124      49.474  -6.536  46.520  1.00 20.64           N  
ANISOU  972  NZ  LYS A 124     3177   1583   3082    -62   -116    107       N  
ATOM    973  N   HIS A 125      54.983  -3.470  43.766  1.00 16.41           N  
ANISOU  973  N   HIS A 125     2692   1024   2519     33    -53    -24       N  
ATOM    974  CA  HIS A 125      56.287  -4.130  44.012  1.00 16.64           C  
ANISOU  974  CA  HIS A 125     2725   1046   2549     44    -58    -26       C  
ATOM    975  C   HIS A 125      56.103  -4.718  45.381  1.00 16.18           C  
ANISOU  975  C   HIS A 125     2658    995   2494     30    -64     -3       C  
ATOM    976  O   HIS A 125      55.930  -4.026  46.372  1.00 15.80           O  
ANISOU  976  O   HIS A 125     2596    970   2434     22    -51      4       O  
ATOM    977  CB  HIS A 125      57.513  -3.197  44.042  1.00 17.54           C  
ANISOU  977  CB  HIS A 125     2836   1177   2650     55    -42    -38       C  
ATOM    978  CG  HIS A 125      57.896  -2.597  42.713  1.00 17.27           C  
ANISOU  978  CG  HIS A 125     2808   1141   2611     69    -36    -57       C  
ATOM    979  ND1 HIS A 125      58.875  -1.611  42.599  1.00 18.37           N  
ANISOU  979  ND1 HIS A 125     2942   1296   2739     75    -23    -65       N  
ATOM    980  CD2 HIS A 125      57.382  -2.765  41.468  1.00 17.09           C  
ANISOU  980  CD2 HIS A 125     2794   1106   2593     74    -43    -67       C  
ATOM    981  CE1 HIS A 125      58.992  -1.271  41.313  1.00 18.25           C  
ANISOU  981  CE1 HIS A 125     2931   1280   2721     86    -21    -77       C  
ATOM    982  NE2 HIS A 125      58.128  -1.984  40.612  1.00 18.53           N  
ANISOU  982  NE2 HIS A 125     2975   1298   2765     87    -33    -80       N  
ATOM    983  N   VAL A 126      56.233  -6.063  45.480  1.00 15.19           N  
ANISOU  983  N   VAL A 126     2539    848   2382     29    -84      7       N  
ATOM    984  CA  VAL A 126      56.165  -6.705  46.757  1.00 15.76           C  
ANISOU  984  CA  VAL A 126     2602    928   2459     16    -92     33       C  
ATOM    985  C   VAL A 126      57.557  -7.209  47.080  1.00 15.47           C  
ANISOU  985  C   VAL A 126     2568    887   2423     30    -94     32       C  
ATOM    986  O   VAL A 126      58.198  -7.837  46.222  1.00 15.39           O  
ANISOU  986  O   VAL A 126     2573    853   2421     48   -104     20       O  
ATOM    987  CB  VAL A 126      55.250  -7.987  46.786  1.00 15.67           C  
ANISOU  987  CB  VAL A 126     2594    892   2465      1   -119     54       C  
ATOM    988  CG1 VAL A 126      55.316  -8.646  48.154  1.00 16.12           C  
ANISOU  988  CG1 VAL A 126     2638    960   2525    -12   -127     85       C  
ATOM    989  CG2 VAL A 126      53.818  -7.686  46.400  1.00 16.05           C  
ANISOU  989  CG2 VAL A 126     2638    944   2513    -14   -121     60       C  
ATOM    990  N   PHE A 127      57.987  -6.963  48.308  1.00 15.66           N  
ANISOU  990  N   PHE A 127     2576    936   2437     23    -85     47       N  
ATOM    991  CA  PHE A 127      59.235  -7.414  48.877  1.00 16.97           C  
ANISOU  991  CA  PHE A 127     2739   1106   2602     32    -87     54       C  
ATOM    992  C   PHE A 127      58.845  -8.294  50.073  1.00 18.30           C  
ANISOU  992  C   PHE A 127     2896   1278   2778     14   -100     86       C  
ATOM    993  O   PHE A 127      58.740  -7.795  51.209  1.00 19.38           O  
ANISOU  993  O   PHE A 127     3014   1447   2900      1    -89     99       O  
ATOM    994  CB  PHE A 127      60.156  -6.249  49.340  1.00 16.23           C  
ANISOU  994  CB  PHE A 127     2634   1043   2487     35    -65     44       C  
ATOM    995  CG  PHE A 127      60.560  -5.290  48.232  1.00 15.65           C  
ANISOU  995  CG  PHE A 127     2569    970   2406     49    -53     18       C  
ATOM    996  CD1 PHE A 127      59.654  -4.328  47.750  1.00 15.82           C  
ANISOU  996  CD1 PHE A 127     2593    995   2423     43    -43      5       C  
ATOM    997  CD2 PHE A 127      61.829  -5.317  47.691  1.00 15.33           C  
ANISOU  997  CD2 PHE A 127     2531    929   2362     67    -50      8       C  
ATOM    998  CE1 PHE A 127      60.027  -3.454  46.740  1.00 16.12           C  
ANISOU  998  CE1 PHE A 127     2636   1032   2454     53    -33    -15       C  
ATOM    999  CE2 PHE A 127      62.232  -4.440  46.673  1.00 15.78           C  
ANISOU  999  CE2 PHE A 127     2592    990   2410     78    -40    -11       C  
ATOM   1000  CZ  PHE A 127      61.322  -3.500  46.191  1.00 15.74           C  
ANISOU 1000  CZ  PHE A 127     2591    987   2403     70    -32    -22       C  
ATOM   1001  N   GLN A 128      58.666  -9.621  49.824  1.00 20.45           N  
ANISOU 1001  N   GLN A 128     3179   1517   3073     15   -125     99       N  
ATOM   1002  CA  GLN A 128      58.199 -10.535  50.826  1.00 22.69           C  
ANISOU 1002  CA  GLN A 128     3452   1800   3366     -3   -142    134       C  
ATOM   1003  C   GLN A 128      56.863 -10.029  51.441  1.00 21.05           C  
ANISOU 1003  C   GLN A 128     3228   1620   3149    -29   -137    150       C  
ATOM   1004  O   GLN A 128      55.842 -10.086  50.756  1.00 21.76           O  
ANISOU 1004  O   GLN A 128     3324   1695   3246    -36   -145    148       O  
ATOM   1005  CB  GLN A 128      59.309 -10.850  51.859  1.00 25.33           C  
ANISOU 1005  CB  GLN A 128     3774   2151   3697      0   -140    152       C  
ATOM   1006  CG  GLN A 128      59.077 -12.119  52.667  1.00 27.82           C  
ANISOU 1006  CG  GLN A 128     4084   2454   4031    -14   -165    190       C  
ATOM   1007  CD  GLN A 128      60.371 -12.698  53.231  1.00 29.75           C  
ANISOU 1007  CD  GLN A 128     4324   2699   4279     -1   -168    202       C  
ATOM   1008  OE1 GLN A 128      61.392 -12.000  53.306  1.00 32.21           O  
ANISOU 1008  OE1 GLN A 128     4631   3033   4574     12   -149    187       O  
ATOM   1009  NE2 GLN A 128      60.337 -13.965  53.633  1.00 31.66           N  
ANISOU 1009  NE2 GLN A 128     4568   2917   4544     -7   -194    232       N  
ATOM   1010  N   ASN A 129      56.881  -9.498  52.661  1.00 22.41           N  
ANISOU 1010  N   ASN A 129     3378   1833   3304    -39   -123    165       N  
ATOM   1011  CA  ASN A 129      55.705  -9.171  53.454  1.00 22.91           C  
ANISOU 1011  CA  ASN A 129     3420   1928   3354    -60   -118    185       C  
ATOM   1012  C   ASN A 129      55.129  -7.803  53.051  1.00 21.87           C  
ANISOU 1012  C   ASN A 129     3288   1815   3204    -54    -96    159       C  
ATOM   1013  O   ASN A 129      53.886  -7.521  53.101  1.00 23.29           O  
ANISOU 1013  O   ASN A 129     3458   2011   3379    -65    -93    168       O  
ATOM   1014  CB  ASN A 129      56.051  -9.103  54.971  1.00 24.20           C  
ANISOU 1014  CB  ASN A 129     3560   2133   3501    -70   -111    209       C  
ATOM   1015  CG  ASN A 129      56.460 -10.440  55.593  1.00 26.52           C  
ANISOU 1015  CG  ASN A 129     3848   2415   3811    -79   -135    244       C  
ATOM   1016  OD1 ASN A 129      56.392 -11.519  54.966  1.00 27.87           O  
ANISOU 1016  OD1 ASN A 129     4034   2544   4010    -80   -159    253       O  
ATOM   1017  ND2 ASN A 129      56.914 -10.371  56.850  1.00 27.59           N  
ANISOU 1017  ND2 ASN A 129     3963   2588   3930    -87   -128    263       N  
ATOM   1018  N   ARG A 130      56.051  -6.950  52.598  1.00 18.97           N  
ANISOU 1018  N   ARG A 130     2932   1447   2829    -37    -79    128       N  
ATOM   1019  CA  ARG A 130      55.810  -5.515  52.408  1.00 18.04           C  
ANISOU 1019  CA  ARG A 130     2814   1348   2693    -30    -57    103       C  
ATOM   1020  C   ARG A 130      55.363  -5.213  50.968  1.00 17.32           C  
ANISOU 1020  C   ARG A 130     2738   1230   2611    -21    -57     82       C  
ATOM   1021  O   ARG A 130      56.034  -5.594  50.008  1.00 17.52           O  
ANISOU 1021  O   ARG A 130     2780   1228   2649     -9    -64     69       O  
ATOM   1022  CB  ARG A 130      57.083  -4.777  52.716  1.00 18.38           C  
ANISOU 1022  CB  ARG A 130     2858   1402   2720    -20    -43     86       C  
ATOM   1023  CG  ARG A 130      57.364  -4.751  54.202  1.00 19.01           C  
ANISOU 1023  CG  ARG A 130     2921   1518   2784    -31    -38    103       C  
ATOM   1024  CD  ARG A 130      58.673  -4.088  54.487  1.00 18.96           C  
ANISOU 1024  CD  ARG A 130     2916   1522   2763    -25    -28     87       C  
ATOM   1025  NE  ARG A 130      58.610  -2.641  54.253  1.00 19.30           N  
ANISOU 1025  NE  ARG A 130     2965   1574   2791    -20    -11     59       N  
ATOM   1026  CZ  ARG A 130      58.109  -1.755  55.114  1.00 19.11           C  
ANISOU 1026  CZ  ARG A 130     2934   1579   2746    -24      0     53       C  
ATOM   1027  NH1 ARG A 130      57.656  -2.112  56.336  1.00 19.34           N  
ANISOU 1027  NH1 ARG A 130     2946   1639   2762    -35      0     74       N  
ATOM   1028  NH2 ARG A 130      58.081  -0.463  54.792  1.00 19.27           N  
ANISOU 1028  NH2 ARG A 130     2965   1599   2757    -18     13     26       N  
ATOM   1029  N   GLU A 131      54.232  -4.527  50.830  1.00 16.84           N  
ANISOU 1029  N   GLU A 131     2671   1182   2543    -24    -48     80       N  
ATOM   1030  CA  GLU A 131      53.677  -4.298  49.485  1.00 15.87           C  
ANISOU 1030  CA  GLU A 131     2561   1037   2429    -18    -50     64       C  
ATOM   1031  C   GLU A 131      53.609  -2.804  49.159  1.00 14.83           C  
ANISOU 1031  C   GLU A 131     2432    918   2285     -7    -28     40       C  
ATOM   1032  O   GLU A 131      52.820  -2.137  49.736  1.00 14.63           O  
ANISOU 1032  O   GLU A 131     2394    916   2247     -9    -17     44       O  
ATOM   1033  CB  GLU A 131      52.301  -4.865  49.353  1.00 17.74           C  
ANISOU 1033  CB  GLU A 131     2790   1273   2674    -33    -63     86       C  
ATOM   1034  CG  GLU A 131      52.299  -6.340  49.756  1.00 19.09           C  
ANISOU 1034  CG  GLU A 131     2961   1431   2862    -47    -88    114       C  
ATOM   1035  CD  GLU A 131      51.110  -7.134  49.320  1.00 20.57           C  
ANISOU 1035  CD  GLU A 131     3147   1606   3063    -64   -109    135       C  
ATOM   1036  OE1 GLU A 131      49.985  -6.748  49.645  1.00 22.36           O  
ANISOU 1036  OE1 GLU A 131     3356   1859   3280    -75   -104    151       O  
ATOM   1037  OE2 GLU A 131      51.320  -8.326  48.847  1.00 23.29           O  
ANISOU 1037  OE2 GLU A 131     3506   1913   3428    -70   -135    142       O  
ATOM   1038  N   TYR A 132      54.420  -2.380  48.232  1.00 13.79           N  
ANISOU 1038  N   TYR A 132     2314    770   2156      4    -25     18       N  
ATOM   1039  CA  TYR A 132      54.394  -0.940  47.798  1.00 13.02           C  
ANISOU 1039  CA  TYR A 132     2219    678   2048     13     -7     -2       C  
ATOM   1040  C   TYR A 132      53.571  -0.810  46.533  1.00 13.00           C  
ANISOU 1040  C   TYR A 132     2222    661   2055     17    -10     -8       C  
ATOM   1041  O   TYR A 132      53.621  -1.658  45.640  1.00 13.41           O  
ANISOU 1041  O   TYR A 132     2283    693   2119     17    -24     -8       O  
ATOM   1042  CB  TYR A 132      55.817  -0.411  47.525  1.00 12.92           C  
ANISOU 1042  CB  TYR A 132     2215    662   2031     22     -1    -20       C  
ATOM   1043  CG  TYR A 132      56.708  -0.295  48.748  1.00 13.28           C  
ANISOU 1043  CG  TYR A 132     2254    725   2065     18      2    -16       C  
ATOM   1044  CD1 TYR A 132      56.706   0.802  49.584  1.00 13.70           C  
ANISOU 1044  CD1 TYR A 132     2303    797   2101     16     15    -24       C  
ATOM   1045  CD2 TYR A 132      57.603  -1.349  49.071  1.00 13.47           C  
ANISOU 1045  CD2 TYR A 132     2278    746   2094     17     -8     -5       C  
ATOM   1046  CE1 TYR A 132      57.498   0.875  50.689  1.00 13.77           C  
ANISOU 1046  CE1 TYR A 132     2308    825   2098     10     17    -21       C  
ATOM   1047  CE2 TYR A 132      58.384  -1.307  50.226  1.00 13.62           C  
ANISOU 1047  CE2 TYR A 132     2289    785   2101     12     -5      1       C  
ATOM   1048  CZ  TYR A 132      58.378  -0.172  51.024  1.00 13.90           C  
ANISOU 1048  CZ  TYR A 132     2320    842   2119      7      7     -7       C  
ATOM   1049  OH  TYR A 132      59.165  -0.073  52.126  1.00 14.47           O  
ANISOU 1049  OH  TYR A 132     2386    935   2177      0      9     -2       O  
ATOM   1050  N   PHE A 133      52.845   0.315  46.383  1.00 12.24           N  
ANISOU 1050  N   PHE A 133     2122    575   1951     21      2    -15       N  
ATOM   1051  CA  PHE A 133      52.103   0.498  45.143  1.00 11.87           C  
ANISOU 1051  CA  PHE A 133     2079    517   1913     24      0    -19       C  
ATOM   1052  C   PHE A 133      52.086   1.953  44.741  1.00 11.62           C  
ANISOU 1052  C   PHE A 133     2050    488   1875     34     16    -35       C  
ATOM   1053  O   PHE A 133      52.291   2.776  45.560  1.00 11.95           O  
ANISOU 1053  O   PHE A 133     2089    542   1907     37     27    -41       O  
ATOM   1054  CB  PHE A 133      50.693  -0.040  45.148  1.00 12.02           C  
ANISOU 1054  CB  PHE A 133     2087    541   1935     14     -7      0       C  
ATOM   1055  CG  PHE A 133      49.741   0.608  46.100  1.00 12.02           C  
ANISOU 1055  CG  PHE A 133     2071    569   1924     14      5     10       C  
ATOM   1056  CD1 PHE A 133      49.729   0.298  47.428  1.00 12.18           C  
ANISOU 1056  CD1 PHE A 133     2080    610   1935      8      7     23       C  
ATOM   1057  CD2 PHE A 133      48.844   1.626  45.671  1.00 12.14           C  
ANISOU 1057  CD2 PHE A 133     2082    594   1936     23     17      6       C  
ATOM   1058  CE1 PHE A 133      48.781   0.852  48.346  1.00 12.23           C  
ANISOU 1058  CE1 PHE A 133     2070    649   1927     11     19     33       C  
ATOM   1059  CE2 PHE A 133      47.946   2.155  46.540  1.00 11.80           C  
ANISOU 1059  CE2 PHE A 133     2023    578   1880     27     29     16       C  
ATOM   1060  CZ  PHE A 133      47.904   1.808  47.877  1.00 12.27           C  
ANISOU 1060  CZ  PHE A 133     2070    661   1928     23     31     28       C  
ATOM   1061  N   HIS A 134      51.810   2.120  43.467  1.00 11.49           N  
ANISOU 1061  N   HIS A 134     2038    460   1866     38     13    -40       N  
ATOM   1062  CA  HIS A 134      51.956   3.489  42.865  1.00 11.30           C  
ANISOU 1062  CA  HIS A 134     2018    435   1839     47     25    -54       C  
ATOM   1063  C   HIS A 134      50.988   3.614  41.704  1.00 11.44           C  
ANISOU 1063  C   HIS A 134     2033    449   1864     48     22    -50       C  
ATOM   1064  O   HIS A 134      50.746   2.693  40.962  1.00 11.48           O  
ANISOU 1064  O   HIS A 134     2040    446   1875     43      9    -45       O  
ATOM   1065  CB  HIS A 134      53.416   3.659  42.408  1.00 11.39           C  
ANISOU 1065  CB  HIS A 134     2039    438   1850     51     24    -66       C  
ATOM   1066  CG  HIS A 134      53.717   5.069  42.001  1.00 11.67           C  
ANISOU 1066  CG  HIS A 134     2077    472   1883     56     33    -76       C  
ATOM   1067  ND1 HIS A 134      54.154   6.030  42.843  1.00 12.41           N  
ANISOU 1067  ND1 HIS A 134     2174    570   1971     56     42    -83       N  
ATOM   1068  CD2 HIS A 134      53.645   5.602  40.785  1.00 11.74           C  
ANISOU 1068  CD2 HIS A 134     2088    476   1897     60     33    -79       C  
ATOM   1069  CE1 HIS A 134      54.298   7.164  42.180  1.00 11.76           C  
ANISOU 1069  CE1 HIS A 134     2095    481   1891     60     46    -89       C  
ATOM   1070  NE2 HIS A 134      53.948   6.948  40.931  1.00 11.98           N  
ANISOU 1070  NE2 HIS A 134     2121    505   1926     62     42    -85       N  
ATOM   1071  N   ILE A 135      50.451   4.819  41.473  1.00 11.23           N  
ANISOU 1071  N   ILE A 135     2004    426   1836     56     34    -52       N  
ATOM   1072  CA  ILE A 135      49.652   5.026  40.363  1.00 11.20           C  
ANISOU 1072  CA  ILE A 135     1997    421   1838     57     32    -48       C  
ATOM   1073  C   ILE A 135      50.229   6.224  39.677  1.00 11.38           C  
ANISOU 1073  C   ILE A 135     2024    436   1861     66     39    -58       C  
ATOM   1074  O   ILE A 135      50.522   7.187  40.351  1.00 11.48           O  
ANISOU 1074  O   ILE A 135     2040    449   1871     71     49    -65       O  
ATOM   1075  CB  ILE A 135      48.165   5.340  40.694  1.00 11.58           C  
ANISOU 1075  CB  ILE A 135     2030    483   1884     60     38    -33       C  
ATOM   1076  CG1 ILE A 135      47.568   4.349  41.729  1.00 11.77           C  
ANISOU 1076  CG1 ILE A 135     2045    520   1904     51     33    -18       C  
ATOM   1077  CG2 ILE A 135      47.360   5.343  39.396  1.00 11.82           C  
ANISOU 1077  CG2 ILE A 135     2057    513   1921     58     32    -25       C  
ATOM   1078  CD1 ILE A 135      47.556   4.704  43.148  1.00 11.91           C  
ANISOU 1078  CD1 ILE A 135     2058    554   1913     56     44    -18       C  
ATOM   1079  N   THR A 136      50.367   6.119  38.361  1.00 11.09           N  
ANISOU 1079  N   THR A 136     1989    395   1828     65     32    -59       N  
ATOM   1080  CA  THR A 136      50.922   7.273  37.608  1.00 11.31           C  
ANISOU 1080  CA  THR A 136     2020    419   1858     70     37    -64       C  
ATOM   1081  C   THR A 136      49.894   7.688  36.583  1.00 11.16           C  
ANISOU 1081  C   THR A 136     1993    403   1843     73     38    -55       C  
ATOM   1082  O   THR A 136      49.305   6.880  35.939  1.00 11.48           O  
ANISOU 1082  O   THR A 136     2029    447   1883     68     29    -49       O  
ATOM   1083  CB  THR A 136      52.225   6.866  36.961  1.00 11.11           C  
ANISOU 1083  CB  THR A 136     1999    391   1828     69     31    -71       C  
ATOM   1084  OG1 THR A 136      53.222   6.696  37.962  1.00 11.33           O  
ANISOU 1084  OG1 THR A 136     2033    418   1852     67     32    -78       O  
ATOM   1085  CG2 THR A 136      52.650   7.892  35.948  1.00 11.45           C  
ANISOU 1085  CG2 THR A 136     2041    436   1873     72     33    -70       C  
ATOM   1086  N   LEU A 137      49.647   9.017  36.511  1.00 11.09           N  
ANISOU 1086  N   LEU A 137     1983    392   1839     80     47    -53       N  
ATOM   1087  CA  LEU A 137      48.828   9.634  35.454  1.00 11.28           C  
ANISOU 1087  CA  LEU A 137     1998    418   1868     84     48    -42       C  
ATOM   1088  C   LEU A 137      49.807  10.219  34.474  1.00 11.37           C  
ANISOU 1088  C   LEU A 137     2012    426   1881     82     44    -43       C  
ATOM   1089  O   LEU A 137      50.672  11.049  34.870  1.00 11.35           O  
ANISOU 1089  O   LEU A 137     2017    415   1880     83     47    -49       O  
ATOM   1090  CB  LEU A 137      47.922  10.758  36.029  1.00 11.64           C  
ANISOU 1090  CB  LEU A 137     2040    462   1920     96     59    -37       C  
ATOM   1091  CG  LEU A 137      47.131  11.443  34.901  1.00 11.59           C  
ANISOU 1091  CG  LEU A 137     2024    458   1920    101     59    -22       C  
ATOM   1092  CD1 LEU A 137      46.100  10.588  34.262  1.00 11.76           C  
ANISOU 1092  CD1 LEU A 137     2032    495   1938     95     54     -9       C  
ATOM   1093  CD2 LEU A 137      46.400  12.804  35.357  1.00 11.95           C  
ANISOU 1093  CD2 LEU A 137     2068    496   1973    119     71    -19       C  
ATOM   1094  N   TYR A 138      49.660   9.835  33.200  1.00 11.22           N  
ANISOU 1094  N   TYR A 138     1986    417   1859     78     37    -37       N  
ATOM   1095  CA  TYR A 138      50.577  10.149  32.130  1.00 11.50           C  
ANISOU 1095  CA  TYR A 138     2019    457   1890     76     33    -36       C  
ATOM   1096  C   TYR A 138      49.822  10.942  31.053  1.00 11.29           C  
ANISOU 1096  C   TYR A 138     1982    437   1869     78     33    -20       C  
ATOM   1097  O   TYR A 138      48.631  10.691  30.818  1.00 11.31           O  
ANISOU 1097  O   TYR A 138     1978    445   1873     78     33    -12       O  
ATOM   1098  CB  TYR A 138      51.052   8.859  31.488  1.00 11.93           C  
ANISOU 1098  CB  TYR A 138     2076    522   1933     74     24    -44       C  
ATOM   1099  CG  TYR A 138      52.098   8.049  32.205  1.00 11.82           C  
ANISOU 1099  CG  TYR A 138     2072    505   1914     74     21    -57       C  
ATOM   1100  CD1 TYR A 138      53.416   8.436  32.255  1.00 12.12           C  
ANISOU 1100  CD1 TYR A 138     2111    546   1948     75     23    -61       C  
ATOM   1101  CD2 TYR A 138      51.813   6.711  32.555  1.00 12.23           C  
ANISOU 1101  CD2 TYR A 138     2129    553   1963     72     14    -64       C  
ATOM   1102  CE1 TYR A 138      54.422   7.662  32.792  1.00 12.30           C  
ANISOU 1102  CE1 TYR A 138     2140    569   1964     77     20    -70       C  
ATOM   1103  CE2 TYR A 138      52.807   5.912  33.075  1.00 12.48           C  
ANISOU 1103  CE2 TYR A 138     2169    581   1990     75     10    -75       C  
ATOM   1104  CZ  TYR A 138      54.091   6.315  33.133  1.00 12.51           C  
ANISOU 1104  CZ  TYR A 138     2173    590   1989     78     14    -78       C  
ATOM   1105  OH  TYR A 138      55.041   5.537  33.690  1.00 13.27           O  
ANISOU 1105  OH  TYR A 138     2274    685   2080     82     11    -86       O  
ATOM   1106  N   GLY A 139      50.505  11.872  30.347  1.00 11.55           N  
ANISOU 1106  N   GLY A 139     2011    472   1903     77     33    -13       N  
ATOM   1107  CA  GLY A 139      49.911  12.422  29.089  1.00 11.58           C  
ANISOU 1107  CA  GLY A 139     2001    487   1908     76     31      4       C  
ATOM   1108  C   GLY A 139      50.858  12.335  27.942  1.00 11.31           C  
ANISOU 1108  C   GLY A 139     1960    473   1863     71     24      8       C  
ATOM   1109  O   GLY A 139      52.062  12.277  28.144  1.00 11.51           O  
ANISOU 1109  O   GLY A 139     1990    500   1883     70     23      1       O  
ATOM   1110  N   ARG A 140      50.349  12.437  26.719  1.00 11.78           N  
ANISOU 1110  N   ARG A 140     2006    550   1918     70     20     21       N  
ATOM   1111  CA  ARG A 140      51.243  12.504  25.594  1.00 12.11           C  
ANISOU 1111  CA  ARG A 140     2037    615   1946     67     15     27       C  
ATOM   1112  C   ARG A 140      51.920  13.883  25.605  1.00 12.56           C  
ANISOU 1112  C   ARG A 140     2090    666   2014     63     16     45       C  
ATOM   1113  O   ARG A 140      53.047  13.999  25.103  1.00 12.91           O  
ANISOU 1113  O   ARG A 140     2128    728   2048     59     13     50       O  
ATOM   1114  CB  ARG A 140      50.576  12.225  24.252  1.00 12.05           C  
ANISOU 1114  CB  ARG A 140     2016    634   1927     65     10     36       C  
ATOM   1115  CG  ARG A 140      50.173  10.763  24.040  1.00 12.12           C  
ANISOU 1115  CG  ARG A 140     2031    650   1921     66      4     17       C  
ATOM   1116  CD  ARG A 140      51.349   9.895  23.972  1.00 12.02           C  
ANISOU 1116  CD  ARG A 140     2027    647   1893     72      1     -1       C  
ATOM   1117  NE  ARG A 140      50.891   8.534  23.528  1.00 12.29           N  
ANISOU 1117  NE  ARG A 140     2069    686   1912     73     -8    -19       N  
ATOM   1118  CZ  ARG A 140      51.648   7.455  23.496  1.00 12.25           C  
ANISOU 1118  CZ  ARG A 140     2075    685   1894     81    -14    -42       C  
ATOM   1119  NH1 ARG A 140      52.906   7.476  23.872  1.00 12.05           N  
ANISOU 1119  NH1 ARG A 140     2052    662   1864     89     -9    -48       N  
ATOM   1120  NH2 ARG A 140      51.108   6.327  23.052  1.00 12.41           N  
ANISOU 1120  NH2 ARG A 140     2104    705   1904     81    -26    -57       N  
ATOM   1121  N   THR A 141      51.253  14.879  26.170  1.00 13.37           N  
ANISOU 1121  N   THR A 141     2197    745   2137     64     20     54       N  
ATOM   1122  CA  THR A 141      51.903  16.138  26.529  1.00 13.79           C  
ANISOU 1122  CA  THR A 141     2253    780   2204     59     18     65       C  
ATOM   1123  C   THR A 141      51.937  16.354  28.024  1.00 14.04           C  
ANISOU 1123  C   THR A 141     2305    781   2248     63     23     49       C  
ATOM   1124  O   THR A 141      51.354  15.657  28.804  1.00 13.96           O  
ANISOU 1124  O   THR A 141     2303    765   2236     71     28     32       O  
ATOM   1125  CB  THR A 141      51.219  17.396  25.911  1.00 13.70           C  
ANISOU 1125  CB  THR A 141     2233    761   2210     59     16     92       C  
ATOM   1126  OG1 THR A 141      49.988  17.634  26.560  1.00 13.99           O  
ANISOU 1126  OG1 THR A 141     2276    777   2261     71     22     88       O  
ATOM   1127  CG2 THR A 141      50.982  17.247  24.505  1.00 14.22           C  
ANISOU 1127  CG2 THR A 141     2278    858   2265     55     12    110       C  
ATOM   1128  N   LYS A 142      52.493  17.481  28.478  1.00 14.83           N  
ANISOU 1128  N   LYS A 142     2413    859   2362     58     19     55       N  
ATOM   1129  CA  LYS A 142      52.489  17.740  29.918  1.00 15.26           C  
ANISOU 1129  CA  LYS A 142     2488    885   2425     63     22     37       C  
ATOM   1130  C   LYS A 142      51.106  18.203  30.443  1.00 15.15           C  
ANISOU 1130  C   LYS A 142     2479    851   2424     80     30     34       C  
ATOM   1131  O   LYS A 142      50.882  18.302  31.654  1.00 15.38           O  
ANISOU 1131  O   LYS A 142     2524    862   2457     88     35     16       O  
ATOM   1132  CB  LYS A 142      53.568  18.788  30.237  1.00 16.74           C  
ANISOU 1132  CB  LYS A 142     2684   1054   2621     50     12     43       C  
ATOM   1133  CG  LYS A 142      54.965  18.254  29.980  1.00 17.96           C  
ANISOU 1133  CG  LYS A 142     2832   1232   2760     36      7     45       C  
ATOM   1134  CD  LYS A 142      56.125  19.172  30.306  1.00 19.54           C  
ANISOU 1134  CD  LYS A 142     3039   1419   2966     19     -4     54       C  
ATOM   1135  CE  LYS A 142      57.391  18.776  29.543  1.00 20.48           C  
ANISOU 1135  CE  LYS A 142     3140   1574   3068      5    -10     69       C  
ATOM   1136  NZ  LYS A 142      58.599  19.643  29.843  1.00 21.72           N  
ANISOU 1136  NZ  LYS A 142     3300   1723   3229    -15    -24     83       N  
ATOM   1137  N   GLU A 143      50.185  18.477  29.529  1.00 15.52           N  
ANISOU 1137  N   GLU A 143     2512    906   2476     85     31     52       N  
ATOM   1138  CA  GLU A 143      48.884  19.087  29.799  1.00 16.43           C  
ANISOU 1138  CA  GLU A 143     2628   1007   2605    103     37     56       C  
ATOM   1139  C   GLU A 143      47.779  18.043  29.791  1.00 16.05           C  
ANISOU 1139  C   GLU A 143     2570    980   2547    111     46     53       C  
ATOM   1140  O   GLU A 143      47.570  17.407  28.767  1.00 15.83           O  
ANISOU 1140  O   GLU A 143     2527    978   2510    103     43     64       O  
ATOM   1141  CB  GLU A 143      48.598  20.156  28.731  1.00 16.89           C  
ANISOU 1141  CB  GLU A 143     2676   1061   2679    103     31     84       C  
ATOM   1142  CG  GLU A 143      49.558  21.347  28.682  1.00 17.42           C  
ANISOU 1142  CG  GLU A 143     2753   1104   2761     92     19     94       C  
ATOM   1143  CD  GLU A 143      49.792  22.003  30.066  1.00 16.71           C  
ANISOU 1143  CD  GLU A 143     2690    976   2682    100     19     72       C  
ATOM   1144  OE1 GLU A 143      50.929  22.190  30.452  1.00 17.81           O  
ANISOU 1144  OE1 GLU A 143     2841   1105   2820     85     10     66       O  
ATOM   1145  OE2 GLU A 143      48.849  22.147  30.801  1.00 16.74           O  
ANISOU 1145  OE2 GLU A 143     2701    966   2690    121     28     60       O  
ATOM   1146  N   LEU A 144      47.039  17.945  30.888  1.00 15.75           N  
ANISOU 1146  N   LEU A 144     2539    933   2510    126     55     41       N  
ATOM   1147  CA  LEU A 144      45.820  17.177  30.910  1.00 15.89           C  
ANISOU 1147  CA  LEU A 144     2544    972   2521    133     62     45       C  
ATOM   1148  C   LEU A 144      44.619  18.026  31.413  1.00 15.72           C  
ANISOU 1148  C   LEU A 144     2521    941   2511    157     71     51       C  
ATOM   1149  O   LEU A 144      44.810  19.013  32.205  1.00 15.80           O  
ANISOU 1149  O   LEU A 144     2547    925   2532    171     74     41       O  
ATOM   1150  CB  LEU A 144      45.917  15.876  31.754  1.00 15.35           C  
ANISOU 1150  CB  LEU A 144     2480    914   2438    128     64     27       C  
ATOM   1151  CG  LEU A 144      46.885  14.863  31.172  1.00 15.07           C  
ANISOU 1151  CG  LEU A 144     2445    890   2390    109     55     22       C  
ATOM   1152  CD1 LEU A 144      47.062  13.705  32.236  1.00 14.36           C  
ANISOU 1152  CD1 LEU A 144     2362    803   2289    106     56      4       C  
ATOM   1153  CD2 LEU A 144      46.431  14.356  29.815  1.00 15.08           C  
ANISOU 1153  CD2 LEU A 144     2430    913   2385    101     49     37       C  
ATOM   1154  N   THR A 145      43.467  17.724  30.852  1.00 16.03           N  
ANISOU 1154  N   THR A 145     2541   1002   2548    162     74     69       N  
ATOM   1155  CA  THR A 145      42.084  17.961  31.314  1.00 17.28           C  
ANISOU 1155  CA  THR A 145     2687   1168   2707    184     85     79       C  
ATOM   1156  C   THR A 145      41.806  17.795  32.809  1.00 17.17           C  
ANISOU 1156  C   THR A 145     2683   1152   2687    200     96     60       C  
ATOM   1157  O   THR A 145      42.325  16.882  33.426  1.00 17.49           O  
ANISOU 1157  O   THR A 145     2729   1197   2716    187     94     45       O  
ATOM   1158  CB  THR A 145      41.281  16.793  30.648  1.00 17.54           C  
ANISOU 1158  CB  THR A 145     2699   1236   2728    170     82     95       C  
ATOM   1159  OG1 THR A 145      41.184  17.007  29.257  1.00 18.64           O  
ANISOU 1159  OG1 THR A 145     2825   1384   2870    160     75    116       O  
ATOM   1160  CG2 THR A 145      39.878  16.373  31.231  1.00 18.08           C  
ANISOU 1160  CG2 THR A 145     2751   1328   2789    182     91    106       C  
ATOM   1161  N   SER A 146      40.906  18.615  33.373  1.00 17.28           N  
ANISOU 1161  N   SER A 146     2695   1163   2708    229    107     63       N  
ATOM   1162  CA  SER A 146      40.616  18.592  34.807  1.00 16.62           C  
ANISOU 1162  CA  SER A 146     2619   1081   2615    248    118     45       C  
ATOM   1163  C   SER A 146      39.923  17.237  35.209  1.00 17.04           C  
ANISOU 1163  C   SER A 146     2652   1171   2649    239    122     53       C  
ATOM   1164  O   SER A 146      40.214  16.732  36.247  1.00 17.67           O  
ANISOU 1164  O   SER A 146     2739   1254   2718    238    125     37       O  
ATOM   1165  CB  SER A 146      39.767  19.864  35.256  1.00 17.63           C  
ANISOU 1165  CB  SER A 146     2748   1198   2753    288    130     46       C  
ATOM   1166  OG  SER A 146      38.661  19.994  34.410  1.00 17.64           O  
ANISOU 1166  OG  SER A 146     2725   1218   2758    297    133     75       O  
ATOM   1167  N   GLU A 147      38.996  16.798  34.384  1.00 17.66           N  
ANISOU 1167  N   GLU A 147     2708   1275   2726    233    120     80       N  
ATOM   1168  CA  GLU A 147      38.244  15.579  34.634  1.00 18.33           C  
ANISOU 1168  CA  GLU A 147     2773   1394   2795    220    119     93       C  
ATOM   1169  C   GLU A 147      39.195  14.390  34.678  1.00 16.92           C  
ANISOU 1169  C   GLU A 147     2605   1211   2610    190    107     80       C  
ATOM   1170  O   GLU A 147      38.979  13.444  35.483  1.00 16.81           O  
ANISOU 1170  O   GLU A 147     2587   1215   2584    182    106     79       O  
ATOM   1171  CB  GLU A 147      37.172  15.372  33.576  1.00 20.17           C  
ANISOU 1171  CB  GLU A 147     2981   1652   3029    214    115    125       C  
ATOM   1172  CG  GLU A 147      35.936  16.244  33.821  1.00 23.51           C  
ANISOU 1172  CG  GLU A 147     3385   2091   3454    248    130    143       C  
ATOM   1173  CD  GLU A 147      34.962  15.537  34.729  1.00 25.62           C  
ANISOU 1173  CD  GLU A 147     3632   2395   3704    253    137    156       C  
ATOM   1174  OE1 GLU A 147      33.775  15.410  34.355  1.00 30.76           O  
ANISOU 1174  OE1 GLU A 147     4256   3080   4352    257    139    187       O  
ATOM   1175  OE2 GLU A 147      35.409  15.036  35.792  1.00 27.57           O  
ANISOU 1175  OE2 GLU A 147     3889   2642   3942    250    139    137       O  
ATOM   1176  N   LEU A 148      40.208  14.399  33.845  1.00 16.10           N  
ANISOU 1176  N   LEU A 148     2515   1089   2512    173     96     71       N  
ATOM   1177  CA  LEU A 148      41.160  13.267  33.745  1.00 15.18           C  
ANISOU 1177  CA  LEU A 148     2408    969   2389    148     84     59       C  
ATOM   1178  C   LEU A 148      42.000  13.224  34.971  1.00 15.73           C  
ANISOU 1178  C   LEU A 148     2495   1025   2455    152     89     36       C  
ATOM   1179  O   LEU A 148      42.268  12.176  35.515  1.00 15.08           O  
ANISOU 1179  O   LEU A 148     2415    950   2364    138     84     30       O  
ATOM   1180  CB  LEU A 148      42.011  13.348  32.504  1.00 14.97           C  
ANISOU 1180  CB  LEU A 148     2387    932   2366    134     74     57       C  
ATOM   1181  CG  LEU A 148      41.319  13.188  31.170  1.00 15.14           C  
ANISOU 1181  CG  LEU A 148     2393    971   2388    125     66     79       C  
ATOM   1182  CD1 LEU A 148      42.204  13.451  29.942  1.00 15.18           C  
ANISOU 1182  CD1 LEU A 148     2401    970   2394    115     58     78       C  
ATOM   1183  CD2 LEU A 148      40.744  11.739  31.132  1.00 15.15           C  
ANISOU 1183  CD2 LEU A 148     2385    992   2377    106     56     85       C  
ATOM   1184  N   LYS A 149      42.466  14.387  35.436  1.00 15.06           N  
ANISOU 1184  N   LYS A 149     2424    920   2377    168     96     22       N  
ATOM   1185  CA  LYS A 149      43.109  14.554  36.709  1.00 15.18           C  
ANISOU 1185  CA  LYS A 149     2454    923   2387    175    101      0       C  
ATOM   1186  C   LYS A 149      42.232  14.229  37.893  1.00 15.79           C  
ANISOU 1186  C   LYS A 149     2523   1023   2454    189    112      1       C  
ATOM   1187  O   LYS A 149      42.668  13.547  38.853  1.00 14.88           O  
ANISOU 1187  O   LYS A 149     2412    912   2327    182    111     -9       O  
ATOM   1188  CB  LYS A 149      43.629  16.062  36.813  1.00 15.57           C  
ANISOU 1188  CB  LYS A 149     2522    943   2449    191    104    -11       C  
ATOM   1189  CG  LYS A 149      44.927  16.270  36.027  1.00 15.68           C  
ANISOU 1189  CG  LYS A 149     2548    938   2471    172     92    -15       C  
ATOM   1190  CD  LYS A 149      45.505  17.693  36.042  1.00 16.45           C  
ANISOU 1190  CD  LYS A 149     2662   1004   2582    181     90    -23       C  
ATOM   1191  CE  LYS A 149      44.432  18.597  35.545  1.00 17.13           C  
ANISOU 1191  CE  LYS A 149     2740   1086   2680    202     95     -8       C  
ATOM   1192  NZ  LYS A 149      44.940  19.974  35.229  1.00 17.84           N  
ANISOU 1192  NZ  LYS A 149     2846   1142   2789    207     88     -9       N  
ATOM   1193  N   GLU A 150      40.957  14.696  37.888  1.00 15.70           N  
ANISOU 1193  N   GLU A 150     2495   1027   2442    210    121     17       N  
ATOM   1194  CA  GLU A 150      40.014  14.391  38.942  1.00 17.11           C  
ANISOU 1194  CA  GLU A 150     2659   1235   2607    224    132     23       C  
ATOM   1195  C   GLU A 150      39.713  12.842  39.007  1.00 16.47           C  
ANISOU 1195  C   GLU A 150     2561   1180   2515    198    123     40       C  
ATOM   1196  O   GLU A 150      39.530  12.281  40.110  1.00 16.36           O  
ANISOU 1196  O   GLU A 150     2542   1186   2488    198    127     39       O  
ATOM   1197  CB  GLU A 150      38.748  15.261  38.797  1.00 19.17           C  
ANISOU 1197  CB  GLU A 150     2903   1510   2869    255    144     39       C  
ATOM   1198  CG  GLU A 150      39.005  16.644  39.356  1.00 22.35           C  
ANISOU 1198  CG  GLU A 150     3325   1887   3278    286    154     16       C  
ATOM   1199  CD  GLU A 150      38.196  17.751  38.753  1.00 25.53           C  
ANISOU 1199  CD  GLU A 150     3722   2285   3692    314    161     28       C  
ATOM   1200  OE1 GLU A 150      37.119  17.508  38.114  1.00 29.00           O  
ANISOU 1200  OE1 GLU A 150     4135   2752   4132    317    163     57       O  
ATOM   1201  OE2 GLU A 150      38.670  18.915  38.870  1.00 28.14           O  
ANISOU 1201  OE2 GLU A 150     4075   2580   4034    333    162      8       O  
ATOM   1202  N   ASN A 151      39.694  12.221  37.859  1.00 16.68           N  
ANISOU 1202  N   ASN A 151     2583   1206   2547    175    110     53       N  
ATOM   1203  CA  ASN A 151      39.558  10.748  37.893  1.00 17.42           C  
ANISOU 1203  CA  ASN A 151     2668   1316   2634    148     97     66       C  
ATOM   1204  C   ASN A 151      40.689  10.039  38.591  1.00 16.61           C  
ANISOU 1204  C   ASN A 151     2582   1199   2527    135     91     47       C  
ATOM   1205  O   ASN A 151      40.505   9.025  39.337  1.00 15.88           O  
ANISOU 1205  O   ASN A 151     2482   1122   2426    122     86     54       O  
ATOM   1206  CB  ASN A 151      39.431  10.226  36.493  1.00 18.51           C  
ANISOU 1206  CB  ASN A 151     2802   1452   2778    127     82     78       C  
ATOM   1207  CG  ASN A 151      38.083   9.825  36.216  1.00 20.95           C  
ANISOU 1207  CG  ASN A 151     3086   1790   3082    122     79    108       C  
ATOM   1208  OD1 ASN A 151      37.265  10.660  35.917  1.00 21.78           O  
ANISOU 1208  OD1 ASN A 151     3177   1908   3190    140     89    122       O  
ATOM   1209  ND2 ASN A 151      37.772   8.524  36.458  1.00 20.48           N  
ANISOU 1209  ND2 ASN A 151     3019   1745   3017     98     65    121       N  
ATOM   1210  N   PHE A 152      41.901  10.463  38.268  1.00 15.59           N  
ANISOU 1210  N   PHE A 152     2474   1043   2405    133     89     25       N  
ATOM   1211  CA  PHE A 152      43.100   9.953  38.910  1.00 15.16           C  
ANISOU 1211  CA  PHE A 152     2435    975   2347    123     84      7       C  
ATOM   1212  C   PHE A 152      43.090  10.174  40.422  1.00 14.82           C  
ANISOU 1212  C   PHE A 152     2393    942   2294    136     95     -1       C  
ATOM   1213  O   PHE A 152      43.428   9.275  41.185  1.00 14.28           O  
ANISOU 1213  O   PHE A 152     2325    881   2219    124     90     -2       O  
ATOM   1214  CB  PHE A 152      44.316  10.574  38.216  1.00 14.68           C  
ANISOU 1214  CB  PHE A 152     2392    888   2295    122     81     -9       C  
ATOM   1215  CG  PHE A 152      45.578  10.461  38.976  1.00 14.81           C  
ANISOU 1215  CG  PHE A 152     2425    893   2308    117     80    -29       C  
ATOM   1216  CD1 PHE A 152      46.289   9.244  38.961  1.00 14.44           C  
ANISOU 1216  CD1 PHE A 152     2382    845   2259    100     68    -31       C  
ATOM   1217  CD2 PHE A 152      46.109  11.541  39.673  1.00 14.79           C  
ANISOU 1217  CD2 PHE A 152     2434    877   2305    130     88    -45       C  
ATOM   1218  CE1 PHE A 152      47.433   9.090  39.720  1.00 14.74           C  
ANISOU 1218  CE1 PHE A 152     2431    875   2291     96     68    -45       C  
ATOM   1219  CE2 PHE A 152      47.289  11.422  40.366  1.00 14.95           C  
ANISOU 1219  CE2 PHE A 152     2468    889   2321    123     85    -60       C  
ATOM   1220  CZ  PHE A 152      47.950  10.182  40.416  1.00 15.00           C  
ANISOU 1220  CZ  PHE A 152     2475    900   2324    106     76    -59       C  
ATOM   1221  N   ILE A 153      42.728  11.381  40.872  1.00 15.61           N  
ANISOU 1221  N   ILE A 153     2495   1042   2394    161    109     -9       N  
ATOM   1222  CA  ILE A 153      42.493  11.606  42.280  1.00 16.06           C  
ANISOU 1222  CA  ILE A 153     2549   1114   2435    177    121    -17       C  
ATOM   1223  C   ILE A 153      41.508  10.561  42.909  1.00 17.22           C  
ANISOU 1223  C   ILE A 153     2672   1300   2570    171    121      6       C  
ATOM   1224  O   ILE A 153      41.783   9.942  43.914  1.00 16.59           O  
ANISOU 1224  O   ILE A 153     2591   1233   2479    164    121      4       O  
ATOM   1225  CB  ILE A 153      42.037  13.096  42.574  1.00 16.64           C  
ANISOU 1225  CB  ILE A 153     2629   1183   2510    211    136    -29       C  
ATOM   1226  CG1 ILE A 153      43.145  14.033  42.213  1.00 16.45           C  
ANISOU 1226  CG1 ILE A 153     2631   1121   2498    211    131    -51       C  
ATOM   1227  CG2 ILE A 153      41.694  13.166  44.049  1.00 16.54           C  
ANISOU 1227  CG2 ILE A 153     2612   1195   2478    229    148    -37       C  
ATOM   1228  CD1 ILE A 153      42.683  15.488  42.221  1.00 16.30           C  
ANISOU 1228  CD1 ILE A 153     2619   1087   2485    242    141    -61       C  
ATOM   1229  N   ARG A 154      40.362  10.385  42.273  1.00 17.16           N  
ANISOU 1229  N   ARG A 154     2644   1310   2564    171    121     31       N  
ATOM   1230  CA  ARG A 154      39.284   9.520  42.812  1.00 17.73           C  
ANISOU 1230  CA  ARG A 154     2689   1422   2624    165    120     59       C  
ATOM   1231  C   ARG A 154      39.773   8.066  42.829  1.00 17.05           C  
ANISOU 1231  C   ARG A 154     2604   1333   2540    131    101     68       C  
ATOM   1232  O   ARG A 154      39.561   7.328  43.803  1.00 16.85           O  
ANISOU 1232  O   ARG A 154     2567   1331   2503    123     99     81       O  
ATOM   1233  CB  ARG A 154      38.025   9.642  41.986  1.00 19.94           C  
ANISOU 1233  CB  ARG A 154     2947   1721   2906    169    121     86       C  
ATOM   1234  CG  ARG A 154      36.944  10.547  42.573  1.00 22.31           C  
ANISOU 1234  CG  ARG A 154     3228   2051   3195    204    141     95       C  
ATOM   1235  CD  ARG A 154      36.481  11.593  41.582  1.00 23.98           C  
ANISOU 1235  CD  ARG A 154     3440   2253   3419    224    147     97       C  
ATOM   1236  NE  ARG A 154      36.131  11.021  40.261  1.00 25.25           N  
ANISOU 1236  NE  ARG A 154     3590   2411   3590    198    131    120       N  
ATOM   1237  CZ  ARG A 154      36.040  11.747  39.151  1.00 25.69           C  
ANISOU 1237  CZ  ARG A 154     3650   2450   3659    205    131    121       C  
ATOM   1238  NH1 ARG A 154      36.295  13.085  39.181  1.00 27.00           N  
ANISOU 1238  NH1 ARG A 154     3830   2596   3832    236    144    102       N  
ATOM   1239  NH2 ARG A 154      35.688  11.168  38.002  1.00 27.11           N  
ANISOU 1239  NH2 ARG A 154     3820   2633   3845    181    116    141       N  
ATOM   1240  N   PHE A 155      40.501   7.691  41.790  1.00 15.14           N  
ANISOU 1240  N   PHE A 155     2378   1062   2311    113     87     61       N  
ATOM   1241  CA  PHE A 155      40.981   6.281  41.709  1.00 14.82           C  
ANISOU 1241  CA  PHE A 155     2342   1013   2274     83     67     67       C  
ATOM   1242  C   PHE A 155      41.986   6.053  42.820  1.00 14.86           C  
ANISOU 1242  C   PHE A 155     2359   1013   2274     83     69     51       C  
ATOM   1243  O   PHE A 155      41.966   4.969  43.465  1.00 14.45           O  
ANISOU 1243  O   PHE A 155     2300    972   2218     66     59     65       O  
ATOM   1244  CB  PHE A 155      41.568   6.013  40.341  1.00 14.22           C  
ANISOU 1244  CB  PHE A 155     2281    909   2210     70     53     59       C  
ATOM   1245  CG  PHE A 155      42.098   4.639  40.183  1.00 13.93           C  
ANISOU 1245  CG  PHE A 155     2254    860   2178     46     32     61       C  
ATOM   1246  CD1 PHE A 155      41.233   3.636  40.200  1.00 14.21           C  
ANISOU 1246  CD1 PHE A 155     2276    909   2214     26     17     86       C  
ATOM   1247  CD2 PHE A 155      43.454   4.427  40.063  1.00 13.84           C  
ANISOU 1247  CD2 PHE A 155     2263    823   2171     44     27     38       C  
ATOM   1248  CE1 PHE A 155      41.711   2.336  40.036  1.00 14.09           C  
ANISOU 1248  CE1 PHE A 155     2271    875   2204      4     -4     87       C  
ATOM   1249  CE2 PHE A 155      43.944   3.165  39.897  1.00 13.68           C  
ANISOU 1249  CE2 PHE A 155     2253    789   2156     25      8     38       C  
ATOM   1250  CZ  PHE A 155      43.056   2.124  39.894  1.00 14.19           C  
ANISOU 1250  CZ  PHE A 155     2307    862   2222      6     -8     62       C  
ATOM   1251  N   SER A 156      42.960   6.973  42.962  1.00 14.21           N  
ANISOU 1251  N   SER A 156     2295    911   2192     97     79     24       N  
ATOM   1252  CA  SER A 156      43.987   6.861  43.973  1.00 14.03           C  
ANISOU 1252  CA  SER A 156     2283    884   2162     96     81      7       C  
ATOM   1253  C   SER A 156      43.330   6.741  45.344  1.00 14.38           C  
ANISOU 1253  C   SER A 156     2311    963   2190    103     90     18       C  
ATOM   1254  O   SER A 156      43.786   5.957  46.211  1.00 14.42           O  
ANISOU 1254  O   SER A 156     2313    975   2187     91     84     22       O  
ATOM   1255  CB  SER A 156      44.981   8.081  43.938  1.00 14.20           C  
ANISOU 1255  CB  SER A 156     2325    882   2185    111     90    -21       C  
ATOM   1256  OG  SER A 156      45.671   8.020  42.726  1.00 13.77           O  
ANISOU 1256  OG  SER A 156     2282    803   2144    102     80    -26       O  
ATOM   1257  N   LYS A 157      42.279   7.512  45.580  1.00 14.57           N  
ANISOU 1257  N   LYS A 157     2321   1009   2205    124    104     24       N  
ATOM   1258  CA  LYS A 157      41.547   7.426  46.852  1.00 15.23           C  
ANISOU 1258  CA  LYS A 157     2383   1133   2268    134    114     37       C  
ATOM   1259  C   LYS A 157      40.830   6.105  47.019  1.00 15.46           C  
ANISOU 1259  C   LYS A 157     2390   1189   2296    111    101     73       C  
ATOM   1260  O   LYS A 157      40.789   5.585  48.151  1.00 15.71           O  
ANISOU 1260  O   LYS A 157     2408   1247   2311    106    102     83       O  
ATOM   1261  CB  LYS A 157      40.552   8.582  47.030  1.00 16.35           C  
ANISOU 1261  CB  LYS A 157     2514   1295   2400    168    133     34       C  
ATOM   1262  CG  LYS A 157      41.172   9.916  47.283  1.00 16.57           C  
ANISOU 1262  CG  LYS A 157     2566   1302   2427    194    146      0       C  
ATOM   1263  CD  LYS A 157      40.151  11.013  47.320  1.00 17.47           C  
ANISOU 1263  CD  LYS A 157     2672   1431   2534    229    163     -2       C  
ATOM   1264  CE  LYS A 157      40.784  12.371  47.406  1.00 17.80           C  
ANISOU 1264  CE  LYS A 157     2741   1441   2579    253    170    -38       C  
ATOM   1265  NZ  LYS A 157      39.676  13.403  47.400  1.00 18.98           N  
ANISOU 1265  NZ  LYS A 157     2882   1605   2725    292    186    -38       N  
ATOM   1266  N   SER A 158      40.257   5.595  45.959  1.00 15.48           N  
ANISOU 1266  N   SER A 158     2385   1184   2310     96     89     92       N  
ATOM   1267  CA  SER A 158      39.561   4.308  45.984  1.00 15.78           C  
ANISOU 1267  CA  SER A 158     2403   1242   2349     68     71    128       C  
ATOM   1268  C   SER A 158      40.491   3.218  46.374  1.00 16.24           C  
ANISOU 1268  C   SER A 158     2474   1284   2413     44     54    128       C  
ATOM   1269  O   SER A 158      39.975   2.105  46.703  1.00 16.44           O  
ANISOU 1269  O   SER A 158     2482   1326   2438     21     38    160       O  
ATOM   1270  CB  SER A 158      38.889   3.977  44.605  1.00 16.15           C  
ANISOU 1270  CB  SER A 158     2447   1278   2410     53     57    145       C  
ATOM   1271  OG  SER A 158      39.841   3.469  43.714  1.00 16.38           O  
ANISOU 1271  OG  SER A 158     2501   1265   2455     37     40    128       O  
ATOM   1272  N   LEU A 159      41.814   3.420  46.164  1.00 15.76           N  
ANISOU 1272  N   LEU A 159     2440   1187   2360     47     54     97       N  
ATOM   1273  CA  LEU A 159      42.843   2.429  46.594  1.00 15.70           C  
ANISOU 1273  CA  LEU A 159     2443   1162   2357     29     39     94       C  
ATOM   1274  C   LEU A 159      43.358   2.651  48.010  1.00 15.97           C  
ANISOU 1274  C   LEU A 159     2474   1216   2375     37     51     87       C  
ATOM   1275  O   LEU A 159      44.327   2.008  48.428  1.00 17.19           O  
ANISOU 1275  O   LEU A 159     2638   1358   2532     26     42     83       O  
ATOM   1276  CB  LEU A 159      44.006   2.358  45.602  1.00 15.64           C  
ANISOU 1276  CB  LEU A 159     2464   1113   2366     26     31     69       C  
ATOM   1277  CG  LEU A 159      43.517   2.169  44.173  1.00 15.79           C  
ANISOU 1277  CG  LEU A 159     2486   1115   2397     18     19     74       C  
ATOM   1278  CD1 LEU A 159      44.688   1.951  43.208  1.00 15.76           C  
ANISOU 1278  CD1 LEU A 159     2507   1074   2405     16     10     51       C  
ATOM   1279  CD2 LEU A 159      42.321   1.182  43.986  1.00 16.07           C  
ANISOU 1279  CD2 LEU A 159     2504   1165   2435     -2      2    108       C  
ATOM   1280  N   GLY A 160      42.716   3.552  48.756  1.00 16.32           N  
ANISOU 1280  N   GLY A 160     2505   1294   2401     59     71     86       N  
ATOM   1281  CA  GLY A 160      43.118   3.866  50.126  1.00 16.27           C  
ANISOU 1281  CA  GLY A 160     2494   1310   2374     69     83     76       C  
ATOM   1282  C   GLY A 160      44.176   4.930  50.375  1.00 16.26           C  
ANISOU 1282  C   GLY A 160     2517   1290   2368     87     95     37       C  
ATOM   1283  O   GLY A 160      44.687   5.048  51.513  1.00 16.21           O  
ANISOU 1283  O   GLY A 160     2510   1300   2345     90    102     28       O  
ATOM   1284  N   LEU A 161      44.432   5.774  49.376  1.00 16.02           N  
ANISOU 1284  N   LEU A 161     2505   1229   2351     98     99     16       N  
ATOM   1285  CA  LEU A 161      45.516   6.778  49.457  1.00 16.02           C  
ANISOU 1285  CA  LEU A 161     2530   1205   2351    109    106    -18       C  
ATOM   1286  C   LEU A 161      44.855   8.091  49.899  1.00 16.99           C  
ANISOU 1286  C   LEU A 161     2653   1342   2460    139    124    -34       C  
ATOM   1287  O   LEU A 161      43.914   8.492  49.273  1.00 17.76           O  
ANISOU 1287  O   LEU A 161     2742   1443   2562    152    129    -26       O  
ATOM   1288  CB  LEU A 161      46.251   6.929  48.133  1.00 15.29           C  
ANISOU 1288  CB  LEU A 161     2457   1072   2279    102     97    -29       C  
ATOM   1289  CG  LEU A 161      47.059   5.703  47.706  1.00 14.76           C  
ANISOU 1289  CG  LEU A 161     2395    989   2225     78     79    -20       C  
ATOM   1290  CD1 LEU A 161      47.745   5.911  46.365  1.00 14.32           C  
ANISOU 1290  CD1 LEU A 161     2355    899   2185     75     72    -31       C  
ATOM   1291  CD2 LEU A 161      48.082   5.384  48.761  1.00 15.07           C  
ANISOU 1291  CD2 LEU A 161     2438   1032   2254     71     77    -27       C  
ATOM   1292  N   PRO A 162      45.350   8.660  51.001  1.00 17.43           N  
ANISOU 1292  N   PRO A 162     2717   1408   2498    150    132    -55       N  
ATOM   1293  CA  PRO A 162      44.952  10.009  51.440  1.00 18.08           C  
ANISOU 1293  CA  PRO A 162     2807   1495   2568    182    148    -79       C  
ATOM   1294  C   PRO A 162      45.352  11.079  50.476  1.00 18.95           C  
ANISOU 1294  C   PRO A 162     2941   1561   2695    191    147   -101       C  
ATOM   1295  O   PRO A 162      46.181  10.852  49.575  1.00 17.97           O  
ANISOU 1295  O   PRO A 162     2829   1406   2590    171    135   -100       O  
ATOM   1296  CB  PRO A 162      45.645  10.106  52.812  1.00 18.48           C  
ANISOU 1296  CB  PRO A 162     2864   1562   2595    183    151    -97       C  
ATOM   1297  CG  PRO A 162      46.874   9.315  52.675  1.00 18.53           C  
ANISOU 1297  CG  PRO A 162     2879   1550   2612    153    136    -93       C  
ATOM   1298  CD  PRO A 162      46.509   8.189  51.771  1.00 17.31           C  
ANISOU 1298  CD  PRO A 162     2709   1391   2475    134    126    -62       C  
ATOM   1299  N   GLU A 163      44.811  12.293  50.663  1.00 20.31           N  
ANISOU 1299  N   GLU A 163     3122   1733   2862    222    159   -119       N  
ATOM   1300  CA  GLU A 163      45.053  13.333  49.632  1.00 21.41           C  
ANISOU 1300  CA  GLU A 163     3281   1829   3022    230    156   -134       C  
ATOM   1301  C   GLU A 163      46.523  13.720  49.541  1.00 20.50           C  
ANISOU 1301  C   GLU A 163     3194   1678   2915    212    144   -155       C  
ATOM   1302  O   GLU A 163      47.060  13.995  48.430  1.00 19.76           O  
ANISOU 1302  O   GLU A 163     3112   1552   2844    201    135   -154       O  
ATOM   1303  CB  GLU A 163      44.141  14.562  49.826  1.00 24.41           C  
ANISOU 1303  CB  GLU A 163     3665   2210   3396    269    170   -148       C  
ATOM   1304  CG  GLU A 163      44.420  15.649  48.774  1.00 27.59           C  
ANISOU 1304  CG  GLU A 163     4091   2567   3824    275    164   -160       C  
ATOM   1305  CD  GLU A 163      45.331  16.757  49.256  1.00 30.92           C  
ANISOU 1305  CD  GLU A 163     4546   2956   4246    282    160   -195       C  
ATOM   1306  OE1 GLU A 163      45.071  17.267  50.348  1.00 34.95           O  
ANISOU 1306  OE1 GLU A 163     5063   3479   4735    306    168   -217       O  
ATOM   1307  OE2 GLU A 163      46.299  17.151  48.550  1.00 33.82           O  
ANISOU 1307  OE2 GLU A 163     4932   3285   4631    263    146   -201       O  
ATOM   1308  N   ASN A 164      47.208  13.728  50.678  1.00 21.17           N  
ANISOU 1308  N   ASN A 164     3287   1772   2982    209    144   -172       N  
ATOM   1309  CA  ASN A 164      48.617  14.106  50.712  1.00 21.39           C  
ANISOU 1309  CA  ASN A 164     3340   1771   3016    190    132   -191       C  
ATOM   1310  C   ASN A 164      49.585  13.152  50.008  1.00 20.42           C  
ANISOU 1310  C   ASN A 164     3213   1638   2907    159    119   -174       C  
ATOM   1311  O   ASN A 164      50.710  13.535  49.713  1.00 21.45           O  
ANISOU 1311  O   ASN A 164     3360   1743   3045    144    109   -183       O  
ATOM   1312  CB  ASN A 164      49.146  14.478  52.123  1.00 22.92           C  
ANISOU 1312  CB  ASN A 164     3546   1976   3185    194    134   -216       C  
ATOM   1313  CG  ASN A 164      48.990  13.416  53.170  1.00 23.50           C  
ANISOU 1313  CG  ASN A 164     3598   2093   3236    188    138   -203       C  
ATOM   1314  OD1 ASN A 164      48.645  12.239  52.931  1.00 23.07           O  
ANISOU 1314  OD1 ASN A 164     3519   2059   3184    175    138   -174       O  
ATOM   1315  ND2 ASN A 164      49.239  13.843  54.411  1.00 23.68           N  
ANISOU 1315  ND2 ASN A 164     3630   2132   3233    196    142   -226       N  
ATOM   1316  N   HIS A 165      49.135  11.939  49.721  1.00 18.90           N  
ANISOU 1316  N   HIS A 165     2998   1465   2716    149    119   -148       N  
ATOM   1317  CA  HIS A 165      49.945  11.047  48.952  1.00 18.73           C  
ANISOU 1317  CA  HIS A 165     2975   1431   2707    125    107   -134       C  
ATOM   1318  C   HIS A 165      49.635  11.144  47.451  1.00 18.24           C  
ANISOU 1318  C   HIS A 165     2912   1350   2667    125    103   -123       C  
ATOM   1319  O   HIS A 165      50.073  10.266  46.663  1.00 17.67           O  
ANISOU 1319  O   HIS A 165     2836   1272   2605    109     94   -110       O  
ATOM   1320  CB  HIS A 165      49.666   9.608  49.412  1.00 18.06           C  
ANISOU 1320  CB  HIS A 165     2870   1375   2616    113    104   -111       C  
ATOM   1321  CG  HIS A 165      50.349   9.215  50.683  1.00 18.49           C  
ANISOU 1321  CG  HIS A 165     2924   1447   2653    105    103   -115       C  
ATOM   1322  ND1 HIS A 165      51.283   8.220  50.723  1.00 18.89           N  
ANISOU 1322  ND1 HIS A 165     2972   1496   2707     84     93   -105       N  
ATOM   1323  CD2 HIS A 165      50.301   9.725  51.949  1.00 19.45           C  
ANISOU 1323  CD2 HIS A 165     3046   1589   2753    114    111   -130       C  
ATOM   1324  CE1 HIS A 165      51.706   8.051  51.965  1.00 19.39           C  
ANISOU 1324  CE1 HIS A 165     3033   1582   2753     80     94   -108       C  
ATOM   1325  NE2 HIS A 165      51.146   8.965  52.726  1.00 20.30           N  
ANISOU 1325  NE2 HIS A 165     3150   1711   2851     97    105   -124       N  
ATOM   1326  N   ILE A 166      48.919  12.209  47.054  1.00 17.14           N  
ANISOU 1326  N   ILE A 166     2777   1200   2533    144    110   -130       N  
ATOM   1327  CA  ILE A 166      48.439  12.318  45.654  1.00 16.25           C  
ANISOU 1327  CA  ILE A 166     2661   1075   2439    145    107   -117       C  
ATOM   1328  C   ILE A 166      48.883  13.606  45.138  1.00 16.37           C  
ANISOU 1328  C   ILE A 166     2694   1061   2465    151    105   -131       C  
ATOM   1329  O   ILE A 166      48.328  14.626  45.589  1.00 17.41           O  
ANISOU 1329  O   ILE A 166     2834   1187   2594    173    113   -143       O  
ATOM   1330  CB  ILE A 166      46.900  12.198  45.542  1.00 16.86           C  
ANISOU 1330  CB  ILE A 166     2719   1173   2514    161    116   -101       C  
ATOM   1331  CG1 ILE A 166      46.411  10.882  46.164  1.00 16.06           C  
ANISOU 1331  CG1 ILE A 166     2598   1103   2401    151    116    -83       C  
ATOM   1332  CG2 ILE A 166      46.452  12.238  44.108  1.00 16.82           C  
ANISOU 1332  CG2 ILE A 166     2707   1156   2524    159    112    -86       C  
ATOM   1333  CD1 ILE A 166      44.879  10.721  46.295  1.00 17.02           C  
ANISOU 1333  CD1 ILE A 166     2696   1254   2516    165    125    -64       C  
ATOM   1334  N   VAL A 167      49.917  13.603  44.275  1.00 15.72           N  
ANISOU 1334  N   VAL A 167     2619    959   2393    134     94   -129       N  
ATOM   1335  CA  VAL A 167      50.607  14.875  43.826  1.00 14.98           C  
ANISOU 1335  CA  VAL A 167     2543    837   2311    133     88   -139       C  
ATOM   1336  C   VAL A 167      50.640  15.044  42.293  1.00 14.38           C  
ANISOU 1336  C   VAL A 167     2462    749   2251    127     82   -123       C  
ATOM   1337  O   VAL A 167      50.746  14.135  41.529  1.00 14.33           O  
ANISOU 1337  O   VAL A 167     2444    753   2247    116     78   -110       O  
ATOM   1338  CB  VAL A 167      52.054  14.991  44.393  1.00 15.89           C  
ANISOU 1338  CB  VAL A 167     2673    943   2420    115     79   -151       C  
ATOM   1339  CG1 VAL A 167      52.561  16.438  44.210  1.00 16.40           C  
ANISOU 1339  CG1 VAL A 167     2757    977   2494    115     71   -162       C  
ATOM   1340  CG2 VAL A 167      52.018  14.738  45.877  1.00 15.88           C  
ANISOU 1340  CG2 VAL A 167     2674    958   2400    119     84   -165       C  
ATOM   1341  N   PHE A 168      50.686  16.313  41.873  1.00 13.92           N  
ANISOU 1341  N   PHE A 168     2416    666   2205    133     78   -127       N  
ATOM   1342  CA  PHE A 168      50.805  16.665  40.479  1.00 13.68           C  
ANISOU 1342  CA  PHE A 168     2381    626   2190    127     72   -111       C  
ATOM   1343  C   PHE A 168      52.054  17.478  40.405  1.00 13.81           C  
ANISOU 1343  C   PHE A 168     2413    621   2212    111     59   -115       C  
ATOM   1344  O   PHE A 168      51.980  18.750  40.573  1.00 13.85           O  
ANISOU 1344  O   PHE A 168     2434    599   2227    119     55   -123       O  
ATOM   1345  CB  PHE A 168      49.594  17.474  40.070  1.00 14.04           C  
ANISOU 1345  CB  PHE A 168     2424    663   2246    148     78   -105       C  
ATOM   1346  CG  PHE A 168      48.346  16.723  40.005  1.00 13.67           C  
ANISOU 1346  CG  PHE A 168     2359    641   2194    160     88    -94       C  
ATOM   1347  CD1 PHE A 168      48.102  15.944  38.892  1.00 13.50           C  
ANISOU 1347  CD1 PHE A 168     2320    634   2175    150     86    -75       C  
ATOM   1348  CD2 PHE A 168      47.459  16.704  41.100  1.00 13.98           C  
ANISOU 1348  CD2 PHE A 168     2395    691   2222    180    100   -103       C  
ATOM   1349  CE1 PHE A 168      46.961  15.208  38.821  1.00 13.85           C  
ANISOU 1349  CE1 PHE A 168     2347    701   2214    157     92    -63       C  
ATOM   1350  CE2 PHE A 168      46.279  16.022  41.006  1.00 14.11           C  
ANISOU 1350  CE2 PHE A 168     2391    734   2233    189    109    -89       C  
ATOM   1351  CZ  PHE A 168      46.034  15.277  39.845  1.00 14.11           C  
ANISOU 1351  CZ  PHE A 168     2376    745   2239    175    103    -68       C  
ATOM   1352  N   PRO A 169      53.220  16.902  40.274  1.00 13.38           N  
ANISOU 1352  N   PRO A 169     2356    575   2151     91     52   -112       N  
ATOM   1353  CA  PRO A 169      54.453  17.630  40.263  1.00 14.25           C  
ANISOU 1353  CA  PRO A 169     2477    670   2265     74     39   -113       C  
ATOM   1354  C   PRO A 169      54.528  18.681  39.161  1.00 14.77           C  
ANISOU 1354  C   PRO A 169     2545    717   2349     69     29    -98       C  
ATOM   1355  O   PRO A 169      54.127  18.476  38.016  1.00 14.39           O  
ANISOU 1355  O   PRO A 169     2482    679   2307     71     31    -80       O  
ATOM   1356  CB  PRO A 169      55.549  16.682  40.209  1.00 13.97           C  
ANISOU 1356  CB  PRO A 169     2434    655   2219     56     35   -107       C  
ATOM   1357  CG  PRO A 169      54.901  15.360  40.511  1.00 13.05           C  
ANISOU 1357  CG  PRO A 169     2305    560   2092     66     45   -109       C  
ATOM   1358  CD  PRO A 169      53.443  15.417  40.191  1.00 12.87           C  
ANISOU 1358  CD  PRO A 169     2276    536   2075     84     54   -107       C  
ATOM   1359  N   VAL A 170      55.075  19.847  39.530  1.00 16.15           N  
ANISOU 1359  N   VAL A 170     2738    864   2531     61     17   -103       N  
ATOM   1360  CA  VAL A 170      55.391  20.768  38.504  1.00 16.94           C  
ANISOU 1360  CA  VAL A 170     2839    949   2648     51      5    -84       C  
ATOM   1361  C   VAL A 170      56.475  20.218  37.592  1.00 17.24           C  
ANISOU 1361  C   VAL A 170     2859   1012   2680     29     -1    -63       C  
ATOM   1362  O   VAL A 170      57.517  19.820  38.061  1.00 17.66           O  
ANISOU 1362  O   VAL A 170     2911   1075   2721     13     -6    -65       O  
ATOM   1363  CB  VAL A 170      55.815  22.171  39.126  1.00 17.79           C  
ANISOU 1363  CB  VAL A 170     2974   1017   2768     43    -10    -94       C  
ATOM   1364  CG1 VAL A 170      55.968  23.196  38.027  1.00 18.70           C  
ANISOU 1364  CG1 VAL A 170     3088   1111   2903     33    -25    -70       C  
ATOM   1365  CG2 VAL A 170      54.820  22.618  40.208  1.00 18.48           C  
ANISOU 1365  CG2 VAL A 170     3081   1083   2855     70     -2   -122       C  
ATOM   1366  N   PRO A 171      56.196  20.121  36.291  1.00 18.40           N  
ANISOU 1366  N   PRO A 171     2987   1170   2832     30      0    -41       N  
ATOM   1367  CA  PRO A 171      57.159  19.574  35.313  1.00 20.09           C  
ANISOU 1367  CA  PRO A 171     3181   1414   3037     14     -6    -21       C  
ATOM   1368  C   PRO A 171      58.366  20.412  34.970  1.00 22.92           C  
ANISOU 1368  C   PRO A 171     3538   1768   3399    -10    -23     -2       C  
ATOM   1369  O   PRO A 171      58.351  21.642  35.142  1.00 22.27           O  
ANISOU 1369  O   PRO A 171     3472   1653   3334    -18    -36      1       O  
ATOM   1370  CB  PRO A 171      56.332  19.461  34.057  1.00 20.05           C  
ANISOU 1370  CB  PRO A 171     3159   1421   3037     24     -1     -5       C  
ATOM   1371  CG  PRO A 171      55.261  20.437  34.215  1.00 19.71           C  
ANISOU 1371  CG  PRO A 171     3128   1347   3012     37      0     -7       C  
ATOM   1372  CD  PRO A 171      54.916  20.437  35.645  1.00 19.17           C  
ANISOU 1372  CD  PRO A 171     3080   1261   2942     48      5    -34       C  
ATOM   1373  N   ILE A 172      59.383  19.734  34.434  1.00 24.18           N  
ANISOU 1373  N   ILE A 172     3680   1961   3544    -22    -25     11       N  
ATOM   1374  CA  ILE A 172      60.602  20.335  33.952  1.00 27.87           C  
ANISOU 1374  CA  ILE A 172     4139   2439   4011    -47    -42     36       C  
ATOM   1375  C   ILE A 172      60.392  20.786  32.508  1.00 29.71           C  
ANISOU 1375  C   ILE A 172     4353   2684   4251    -49    -46     64       C  
ATOM   1376  O   ILE A 172      59.408  20.399  31.864  1.00 29.84           O  
ANISOU 1376  O   ILE A 172     4362   2707   4269    -31    -35     63       O  
ATOM   1377  CB  ILE A 172      61.791  19.340  33.992  1.00 28.39           C  
ANISOU 1377  CB  ILE A 172     4189   2543   4054    -54    -40     40       C  
ATOM   1378  CG1 ILE A 172      61.499  18.074  33.174  1.00 26.43           C  
ANISOU 1378  CG1 ILE A 172     3921   2329   3791    -35    -25     38       C  
ATOM   1379  CG2 ILE A 172      62.110  18.892  35.413  1.00 29.30           C  
ANISOU 1379  CG2 ILE A 172     4319   2650   4161    -54    -37     16       C  
ATOM   1380  CD1 ILE A 172      62.770  17.370  32.800  1.00 26.24           C  
ANISOU 1380  CD1 ILE A 172     3878   2346   3747    -40    -27     50       C  
ATOM   1381  N   ASP A 173      61.334  21.589  32.014  1.00 31.26           N  
ANISOU 1381  N   ASP A 173     4540   2884   4450    -73    -63     93       N  
ATOM   1382  CA  ASP A 173      61.377  22.010  30.606  1.00 31.84           C  
ANISOU 1382  CA  ASP A 173     4591   2978   4526    -80    -70    127       C  
ATOM   1383  C   ASP A 173      62.547  21.286  29.898  1.00 31.13           C  
ANISOU 1383  C   ASP A 173     4472   2944   4412    -88    -69    146       C  
ATOM   1384  O   ASP A 173      63.133  21.801  28.925  1.00 31.39           O  
ANISOU 1384  O   ASP A 173     4483   3000   4442   -104    -80    181       O  
ATOM   1385  CB  ASP A 173      61.619  23.530  30.497  1.00 31.94           C  
ANISOU 1385  CB  ASP A 173     4613   2959   4563   -104    -93    152       C  
ATOM   1386  CG  ASP A 173      60.937  24.352  31.589  1.00 31.51           C  
ANISOU 1386  CG  ASP A 173     4594   2846   4531    -99    -98    128       C  
ATOM   1387  OD1 ASP A 173      59.759  24.681  31.499  1.00 30.72           O  
ANISOU 1387  OD1 ASP A 173     4503   2721   4447    -80    -92    119       O  
ATOM   1388  OD2 ASP A 173      61.613  24.721  32.545  1.00 34.11           O  
ANISOU 1388  OD2 ASP A 173     4941   3155   4862   -115   -110    119       O  
ATOM   1389  N   GLN A 174      62.901  20.098  30.391  1.00 30.78           N  
ANISOU 1389  N   GLN A 174     4426   2920   4347    -76    -57    125       N  
ATOM   1390  CA  GLN A 174      64.220  19.501  30.113  1.00 32.19           C  
ANISOU 1390  CA  GLN A 174     4582   3145   4502    -83    -58    139       C  
ATOM   1391  C   GLN A 174      64.088  18.033  29.749  1.00 30.75           C  
ANISOU 1391  C   GLN A 174     4389   2996   4298    -57    -40    122       C  
ATOM   1392  O   GLN A 174      63.021  17.478  29.864  1.00 32.12           O  
ANISOU 1392  O   GLN A 174     4574   3153   4476    -37    -29     98       O  
ATOM   1393  CB  GLN A 174      65.154  19.579  31.345  1.00 34.86           C  
ANISOU 1393  CB  GLN A 174     4933   3474   4838   -100    -66    133       C  
ATOM   1394  CG  GLN A 174      65.151  20.863  32.176  1.00 37.34           C  
ANISOU 1394  CG  GLN A 174     5270   3741   5174   -123    -84    135       C  
ATOM   1395  CD  GLN A 174      66.473  21.571  32.188  1.00 38.58           C  
ANISOU 1395  CD  GLN A 174     5417   3911   5327   -157   -104    166       C  
ATOM   1396  OE1 GLN A 174      67.508  20.990  31.847  1.00 41.76           O  
ANISOU 1396  OE1 GLN A 174     5794   4362   5708   -161   -103    184       O  
ATOM   1397  NE2 GLN A 174      66.456  22.836  32.583  1.00 40.94           N  
ANISOU 1397  NE2 GLN A 174     5736   4170   5649   -181   -125    174       N  
ATOM   1398  N   CYS A 175      65.211  17.443  29.339  1.00 30.13           N  
ANISOU 1398  N   CYS A 175     4288   2962   4195    -56    -40    134       N  
ATOM   1399  CA  CYS A 175      65.429  15.973  29.223  1.00 27.43           C  
ANISOU 1399  CA  CYS A 175     3939   2651   3832    -30    -26    115       C  
ATOM   1400  C   CYS A 175      64.879  15.200  28.050  1.00 31.01           C  
ANISOU 1400  C   CYS A 175     4380   3130   4271     -7    -16    109       C  
ATOM   1401  O   CYS A 175      65.211  14.019  27.891  1.00 30.60           O  
ANISOU 1401  O   CYS A 175     4323   3103   4200     14     -8     94       O  
ATOM   1402  CB  CYS A 175      64.978  15.259  30.475  1.00 25.62           C  
ANISOU 1402  CB  CYS A 175     3733   2390   3608    -20    -18     82       C  
ATOM   1403  SG  CYS A 175      65.796  15.922  31.914  1.00 23.40           S  
ANISOU 1403  SG  CYS A 175     3467   2089   3336    -45    -29     85       S  
ATOM   1404  N   ILE A 176      64.091  15.873  27.236  1.00 34.32           N  
ANISOU 1404  N   ILE A 176     4795   3543   4700    -11    -19    121       N  
ATOM   1405  CA  ILE A 176      63.251  15.240  26.202  1.00 35.76           C  
ANISOU 1405  CA  ILE A 176     4971   3742   4874      8    -11    112       C  
ATOM   1406  C   ILE A 176      63.734  15.683  24.807  1.00 39.46           C  
ANISOU 1406  C   ILE A 176     5410   4257   5326      4    -16    144       C  
ATOM   1407  O   ILE A 176      64.167  14.863  24.005  1.00 41.28           O  
ANISOU 1407  O   ILE A 176     5623   4531   5530     21    -11    141       O  
ATOM   1408  CB  ILE A 176      61.733  15.580  26.454  1.00 35.76           C  
ANISOU 1408  CB  ILE A 176     4991   3698   4898      9    -10     99       C  
ATOM   1409  CG1 ILE A 176      61.463  17.116  26.479  1.00 36.57           C  
ANISOU 1409  CG1 ILE A 176     5095   3774   5024    -11    -20    124       C  
ATOM   1410  CG2 ILE A 176      61.279  14.939  27.769  1.00 35.38           C  
ANISOU 1410  CG2 ILE A 176     4968   3616   4859     17     -3     68       C  
ATOM   1411  CD1 ILE A 176      60.149  17.601  27.059  1.00 35.17           C  
ANISOU 1411  CD1 ILE A 176     4940   3550   4872     -9    -18    111       C  
ATOM   1412  N   ASP A 177      63.744  16.990  24.545  1.00 43.67           N  
ANISOU 1412  N   ASP A 177     5935   4781   5874    -19    -27    175       N  
ATOM   1413  CA  ASP A 177      63.935  17.511  23.185  1.00 45.96           C  
ANISOU 1413  CA  ASP A 177     6196   5113   6153    -25    -33    209       C  
ATOM   1414  C   ASP A 177      65.409  17.777  22.905  1.00 45.04           C  
ANISOU 1414  C   ASP A 177     6053   5042   6017    -38    -40    241       C  
ATOM   1415  O   ASP A 177      65.795  17.926  21.756  1.00 45.66           O  
ANISOU 1415  O   ASP A 177     6100   5170   6075    -39    -42    268       O  
ATOM   1416  CB  ASP A 177      63.110  18.795  22.966  1.00 45.41           C  
ANISOU 1416  CB  ASP A 177     6130   5011   6112    -44    -43    231       C  
ATOM   1417  CG  ASP A 177      61.683  18.515  22.525  1.00 46.98           C  
ANISOU 1417  CG  ASP A 177     6337   5194   6318    -28    -35    215       C  
ATOM   1418  OD1 ASP A 177      61.102  17.497  22.958  1.00 46.05           O  
ANISOU 1418  OD1 ASP A 177     6236   5064   6195     -8    -24    179       O  
ATOM   1419  OD2 ASP A 177      61.138  19.325  21.735  1.00 48.10           O  
ANISOU 1419  OD2 ASP A 177     6468   5338   6470    -36    -41    241       O  
TER    1420      ASP A 177                                                      
ATOM   1421  N   GLU B1266      59.579   6.333  71.493  1.00 36.60           N  
ANISOU 1421  N   GLU B1266     4871   4533   4502   -247    510   -261       N  
ATOM   1422  CA  GLU B1266      59.736   6.175  70.013  1.00 35.40           C  
ANISOU 1422  CA  GLU B1266     4729   4300   4421   -251    479   -236       C  
ATOM   1423  C   GLU B1266      61.146   5.637  69.691  1.00 35.17           C  
ANISOU 1423  C   GLU B1266     4697   4272   4394   -315    426   -260       C  
ATOM   1424  O   GLU B1266      62.111   5.914  70.414  1.00 35.18           O  
ANISOU 1424  O   GLU B1266     4711   4310   4344   -362    431   -319       O  
ATOM   1425  CB  GLU B1266      59.470   7.518  69.324  1.00 36.84           C  
ANISOU 1425  CB  GLU B1266     4982   4387   4626   -220    540   -280       C  
ATOM   1426  CG  GLU B1266      60.711   8.394  69.124  1.00 37.42           C  
ANISOU 1426  CG  GLU B1266     5125   4402   4688   -275    554   -373       C  
ATOM   1427  CD  GLU B1266      60.395   9.878  68.980  1.00 39.27           C  
ANISOU 1427  CD  GLU B1266     5445   4549   4923   -245    633   -429       C  
ATOM   1428  OE1 GLU B1266      61.307  10.651  68.618  1.00 39.91           O  
ANISOU 1428  OE1 GLU B1266     5588   4567   5008   -294    644   -495       O  
ATOM   1429  OE2 GLU B1266      59.241  10.276  69.226  1.00 41.37           O  
ANISOU 1429  OE2 GLU B1266     5719   4811   5187   -171    686   -403       O  
ATOM   1430  N   VAL B1267      61.254   4.914  68.577  1.00 31.92           N  
ANISOU 1430  N   VAL B1267     4270   3822   4034   -315    380   -213       N  
ATOM   1431  CA  VAL B1267      62.396   4.071  68.301  1.00 30.04           C  
ANISOU 1431  CA  VAL B1267     4016   3600   3797   -353    328   -207       C  
ATOM   1432  C   VAL B1267      63.582   4.926  67.796  1.00 28.98           C  
ANISOU 1432  C   VAL B1267     3926   3426   3657   -390    341   -275       C  
ATOM   1433  O   VAL B1267      63.387   5.773  66.937  1.00 28.03           O  
ANISOU 1433  O   VAL B1267     3849   3229   3570   -378    367   -298       O  
ATOM   1434  CB  VAL B1267      62.030   2.939  67.294  1.00 28.48           C  
ANISOU 1434  CB  VAL B1267     3799   3370   3650   -335    276   -133       C  
ATOM   1435  CG1 VAL B1267      63.218   2.015  67.008  1.00 27.17           C  
ANISOU 1435  CG1 VAL B1267     3625   3217   3482   -357    231   -123       C  
ATOM   1436  CG2 VAL B1267      60.852   2.120  67.827  1.00 28.82           C  
ANISOU 1436  CG2 VAL B1267     3797   3456   3697   -315    259    -59       C  
ATOM   1437  N   PRO B1268      64.810   4.688  68.314  1.00 28.07           N  
ANISOU 1437  N   PRO B1268     3794   3372   3499   -437    322   -298       N  
ATOM   1438  CA  PRO B1268      65.988   5.464  67.906  1.00 27.63           C  
ANISOU 1438  CA  PRO B1268     3769   3297   3431   -485    329   -353       C  
ATOM   1439  C   PRO B1268      66.430   5.197  66.483  1.00 26.73           C  
ANISOU 1439  C   PRO B1268     3663   3127   3366   -470    304   -326       C  
ATOM   1440  O   PRO B1268      66.499   4.029  66.088  1.00 25.19           O  
ANISOU 1440  O   PRO B1268     3437   2945   3188   -442    264   -269       O  
ATOM   1441  CB  PRO B1268      67.086   4.987  68.854  1.00 27.76           C  
ANISOU 1441  CB  PRO B1268     3741   3423   3384   -533    305   -356       C  
ATOM   1442  CG  PRO B1268      66.666   3.628  69.233  1.00 27.49           C  
ANISOU 1442  CG  PRO B1268     3653   3439   3353   -494    273   -283       C  
ATOM   1443  CD  PRO B1268      65.180   3.630  69.281  1.00 28.40           C  
ANISOU 1443  CD  PRO B1268     3777   3512   3499   -448    290   -261       C  
ATOM   1444  N   GLN B1269      66.720   6.284  65.768  1.00 27.86           N  
ANISOU 1444  N   GLN B1269     3851   3204   3527   -487    331   -368       N  
ATOM   1445  CA  GLN B1269      67.318   6.263  64.420  1.00 28.03           C  
ANISOU 1445  CA  GLN B1269     3882   3181   3585   -480    314   -351       C  
ATOM   1446  C   GLN B1269      68.830   6.136  64.519  1.00 28.03           C  
ANISOU 1446  C   GLN B1269     3856   3247   3545   -529    293   -358       C  
ATOM   1447  O   GLN B1269      69.444   6.598  65.499  1.00 28.90           O  
ANISOU 1447  O   GLN B1269     3959   3418   3602   -591    302   -397       O  
ATOM   1448  CB  GLN B1269      67.079   7.606  63.720  1.00 28.50           C  
ANISOU 1448  CB  GLN B1269     3999   3152   3676   -485    357   -390       C  
ATOM   1449  CG  GLN B1269      65.642   7.949  63.380  1.00 27.94           C  
ANISOU 1449  CG  GLN B1269     3953   3014   3647   -427    388   -374       C  
ATOM   1450  CD  GLN B1269      65.535   9.174  62.459  1.00 26.97           C  
ANISOU 1450  CD  GLN B1269     3882   2801   3561   -420    430   -395       C  
ATOM   1451  OE1 GLN B1269      64.885  10.153  62.828  1.00 29.18           O  
ANISOU 1451  OE1 GLN B1269     4207   3034   3844   -408    484   -425       O  
ATOM   1452  NE2 GLN B1269      66.171   9.126  61.265  1.00 26.56           N  
ANISOU 1452  NE2 GLN B1269     3828   2726   3537   -421    409   -375       N  
ATOM   1453  N   LEU B1270      69.431   5.558  63.491  1.00 28.94           N  
ANISOU 1453  N   LEU B1270     3957   3358   3680   -504    266   -318       N  
ATOM   1454  CA  LEU B1270      70.898   5.573  63.364  1.00 29.39           C  
ANISOU 1454  CA  LEU B1270     3985   3481   3701   -542    252   -313       C  
ATOM   1455  C   LEU B1270      71.335   7.013  63.133  1.00 30.34           C  
ANISOU 1455  C   LEU B1270     4140   3568   3820   -606    281   -364       C  
ATOM   1456  O   LEU B1270      70.721   7.739  62.362  1.00 28.92           O  
ANISOU 1456  O   LEU B1270     4006   3294   3686   -589    306   -380       O  
ATOM   1457  CB  LEU B1270      71.344   4.644  62.234  1.00 29.15           C  
ANISOU 1457  CB  LEU B1270     3939   3445   3690   -483    226   -257       C  
ATOM   1458  CG  LEU B1270      71.027   3.149  62.473  1.00 27.76           C  
ANISOU 1458  CG  LEU B1270     3742   3292   3512   -425    197   -205       C  
ATOM   1459  CD1 LEU B1270      71.004   2.369  61.176  1.00 27.30           C  
ANISOU 1459  CD1 LEU B1270     3706   3181   3486   -358    179   -167       C  
ATOM   1460  CD2 LEU B1270      71.932   2.486  63.488  1.00 27.66           C  
ANISOU 1460  CD2 LEU B1270     3674   3392   3442   -439    184   -177       C  
ATOM   1461  N   THR B1271      72.350   7.447  63.872  1.00 32.02           N  
ANISOU 1461  N   THR B1271     4331   3858   3975   -686    279   -388       N  
ATOM   1462  CA  THR B1271      72.823   8.836  63.787  1.00 32.71           C  
ANISOU 1462  CA  THR B1271     4460   3912   4054   -768    303   -440       C  
ATOM   1463  C   THR B1271      74.174   8.933  63.074  1.00 32.79           C  
ANISOU 1463  C   THR B1271     4431   3977   4048   -806    283   -405       C  
ATOM   1464  O   THR B1271      74.751  10.017  63.012  1.00 34.84           O  
ANISOU 1464  O   THR B1271     4716   4224   4295   -891    295   -438       O  
ATOM   1465  CB  THR B1271      72.960   9.518  65.168  1.00 33.62           C  
ANISOU 1465  CB  THR B1271     4595   4068   4108   -858    316   -504       C  
ATOM   1466  OG1 THR B1271      73.881   8.790  65.974  1.00 33.83           O  
ANISOU 1466  OG1 THR B1271     4548   4238   4067   -895    281   -476       O  
ATOM   1467  CG2 THR B1271      71.629   9.605  65.890  1.00 32.77           C  
ANISOU 1467  CG2 THR B1271     4531   3909   4011   -818    345   -540       C  
ATOM   1468  N   ASP B1272      74.670   7.827  62.524  1.00 32.29           N  
ANISOU 1468  N   ASP B1272     4311   3972   3983   -744    255   -337       N  
ATOM   1469  CA  ASP B1272      75.969   7.818  61.857  1.00 33.57           C  
ANISOU 1469  CA  ASP B1272     4425   4205   4122   -763    240   -290       C  
ATOM   1470  C   ASP B1272      76.040   6.938  60.606  1.00 32.00           C  
ANISOU 1470  C   ASP B1272     4211   3989   3955   -658    230   -228       C  
ATOM   1471  O   ASP B1272      77.084   6.360  60.320  1.00 33.82           O  
ANISOU 1471  O   ASP B1272     4385   4312   4150   -636    215   -170       O  
ATOM   1472  CB  ASP B1272      77.030   7.364  62.838  1.00 35.18           C  
ANISOU 1472  CB  ASP B1272     4555   4563   4247   -813    216   -261       C  
ATOM   1473  CG  ASP B1272      77.028   5.876  63.057  1.00 36.03           C  
ANISOU 1473  CG  ASP B1272     4615   4732   4341   -721    199   -201       C  
ATOM   1474  OD1 ASP B1272      75.948   5.232  63.088  1.00 36.06           O  
ANISOU 1474  OD1 ASP B1272     4652   4664   4384   -651    201   -207       O  
ATOM   1475  OD2 ASP B1272      78.127   5.323  63.202  1.00 37.48           O  
ANISOU 1475  OD2 ASP B1272     4727   5041   4473   -719    183   -140       O  
ATOM   1476  N   LEU B1273      74.951   6.852  59.861  1.00 30.07           N  
ANISOU 1476  N   LEU B1273     4019   3634   3772   -592    241   -239       N  
ATOM   1477  CA  LEU B1273      74.950   6.167  58.575  1.00 29.77           C  
ANISOU 1477  CA  LEU B1273     3983   3566   3761   -503    232   -193       C  
ATOM   1478  C   LEU B1273      75.990   6.839  57.666  1.00 30.85           C  
ANISOU 1478  C   LEU B1273     4099   3731   3890   -526    239   -168       C  
ATOM   1479  O   LEU B1273      75.988   8.061  57.528  1.00 31.52           O  
ANISOU 1479  O   LEU B1273     4208   3774   3993   -593    258   -200       O  
ATOM   1480  CB  LEU B1273      73.564   6.264  57.940  1.00 28.41           C  
ANISOU 1480  CB  LEU B1273     3869   3274   3650   -455    242   -214       C  
ATOM   1481  CG  LEU B1273      73.360   5.772  56.510  1.00 26.98           C  
ANISOU 1481  CG  LEU B1273     3705   3046   3497   -376    235   -180       C  
ATOM   1482  CD1 LEU B1273      73.773   4.320  56.312  1.00 26.98           C  
ANISOU 1482  CD1 LEU B1273     3689   3091   3470   -304    209   -136       C  
ATOM   1483  CD2 LEU B1273      71.922   6.016  56.094  1.00 26.61           C  
ANISOU 1483  CD2 LEU B1273     3706   2901   3503   -351    243   -200       C  
ATOM   1484  N   SER B1274      76.841   6.025  57.061  1.00 30.54           N  
ANISOU 1484  N   SER B1274     4019   3760   3823   -465    226   -109       N  
ATOM   1485  CA  SER B1274      77.909   6.495  56.170  1.00 31.21           C  
ANISOU 1485  CA  SER B1274     4069   3895   3892   -473    231    -68       C  
ATOM   1486  C   SER B1274      77.952   5.653  54.908  1.00 30.81           C  
ANISOU 1486  C   SER B1274     4029   3828   3850   -358    229    -24       C  
ATOM   1487  O   SER B1274      77.500   4.498  54.898  1.00 29.01           O  
ANISOU 1487  O   SER B1274     3822   3578   3621   -277    219    -15       O  
ATOM   1488  CB  SER B1274      79.266   6.407  56.878  1.00 32.16           C  
ANISOU 1488  CB  SER B1274     4110   4166   3942   -525    221    -24       C  
ATOM   1489  OG  SER B1274      79.230   7.142  58.087  1.00 33.93           O  
ANISOU 1489  OG  SER B1274     4333   4410   4148   -640    218    -72       O  
ATOM   1490  N   PHE B1275      78.456   6.253  53.826  1.00 29.53           N  
ANISOU 1490  N   PHE B1275     3857   3670   3693   -352    240      1       N  
ATOM   1491  CA  PHE B1275      78.647   5.536  52.571  1.00 30.46           C  
ANISOU 1491  CA  PHE B1275     3982   3786   3805   -242    242     44       C  
ATOM   1492  C   PHE B1275      80.132   5.355  52.325  1.00 32.07           C  
ANISOU 1492  C   PHE B1275     4111   4124   3948   -222    246    117       C  
ATOM   1493  O   PHE B1275      80.943   6.278  52.559  1.00 34.99           O  
ANISOU 1493  O   PHE B1275     4427   4566   4300   -311    249    137       O  
ATOM   1494  CB  PHE B1275      78.015   6.271  51.371  1.00 28.73           C  
ANISOU 1494  CB  PHE B1275     3804   3477   3634   -230    254     29       C  
ATOM   1495  CG  PHE B1275      76.538   6.521  51.527  1.00 26.31           C  
ANISOU 1495  CG  PHE B1275     3559   3051   3383   -244    254    -28       C  
ATOM   1496  CD1 PHE B1275      75.655   5.452  51.587  1.00 26.44           C  
ANISOU 1496  CD1 PHE B1275     3617   3020   3408   -183    237    -43       C  
ATOM   1497  CD2 PHE B1275      76.008   7.824  51.615  1.00 26.64           C  
ANISOU 1497  CD2 PHE B1275     3623   3029   3470   -318    274    -61       C  
ATOM   1498  CE1 PHE B1275      74.294   5.655  51.761  1.00 25.07           C  
ANISOU 1498  CE1 PHE B1275     3489   2756   3281   -197    236    -82       C  
ATOM   1499  CE2 PHE B1275      74.639   8.014  51.771  1.00 25.75           C  
ANISOU 1499  CE2 PHE B1275     3560   2819   3402   -315    280   -102       C  
ATOM   1500  CZ  PHE B1275      73.790   6.936  51.846  1.00 26.41           C  
ANISOU 1500  CZ  PHE B1275     3669   2875   3490   -257    259   -109       C  
ATOM   1501  N   VAL B1276      80.473   4.159  51.863  1.00 32.49           N  
ANISOU 1501  N   VAL B1276     4164   4211   3967   -106    247    160       N  
ATOM   1502  CA  VAL B1276      81.858   3.757  51.657  1.00 34.91           C  
ANISOU 1502  CA  VAL B1276     4398   4656   4207    -55    257    242       C  
ATOM   1503  C   VAL B1276      81.947   2.923  50.375  1.00 34.84           C  
ANISOU 1503  C   VAL B1276     4428   4627   4183     86    271    273       C  
ATOM   1504  O   VAL B1276      80.990   2.274  49.983  1.00 36.32           O  
ANISOU 1504  O   VAL B1276     4698   4704   4397    145    265    231       O  
ATOM   1505  CB  VAL B1276      82.425   2.969  52.886  1.00 35.70           C  
ANISOU 1505  CB  VAL B1276     4450   4855   4259    -51    252    276       C  
ATOM   1506  CG1 VAL B1276      82.181   3.722  54.177  1.00 36.66           C  
ANISOU 1506  CG1 VAL B1276     4549   4987   4391   -190    236    231       C  
ATOM   1507  CG2 VAL B1276      81.877   1.541  52.992  1.00 34.95           C  
ANISOU 1507  CG2 VAL B1276     4415   4700   4162     60    252    271       C  
ATOM   1508  N   ASP B1277      83.101   2.942  49.713  1.00 36.38           N  
ANISOU 1508  N   ASP B1277     4562   4932   4327    137    289    349       N  
ATOM   1509  CA  ASP B1277      83.329   2.045  48.586  1.00 36.16           C  
ANISOU 1509  CA  ASP B1277     4571   4901   4265    287    309    382       C  
ATOM   1510  C   ASP B1277      82.252   2.173  47.510  1.00 34.45           C  
ANISOU 1510  C   ASP B1277     4445   4549   4095    313    303    322       C  
ATOM   1511  O   ASP B1277      81.646   1.172  47.067  1.00 35.94           O  
ANISOU 1511  O   ASP B1277     4719   4655   4281    404    301    293       O  
ATOM   1512  CB  ASP B1277      83.440   0.610  49.093  1.00 37.52           C  
ANISOU 1512  CB  ASP B1277     4775   5080   4401    389    316    399       C  
ATOM   1513  CG  ASP B1277      84.611   0.430  50.035  1.00 39.71           C  
ANISOU 1513  CG  ASP B1277     4949   5515   4620    382    326    478       C  
ATOM   1514  OD1 ASP B1277      85.734   0.854  49.671  1.00 40.50           O  
ANISOU 1514  OD1 ASP B1277     4962   5752   4674    390    343    556       O  
ATOM   1515  OD2 ASP B1277      84.413  -0.121  51.119  1.00 38.51           O  
ANISOU 1515  OD2 ASP B1277     4799   5364   4469    366    318    470       O  
ATOM   1516  N   ILE B1278      81.991   3.429  47.144  1.00 32.71           N  
ANISOU 1516  N   ILE B1278     4206   4305   3916    224    299    305       N  
ATOM   1517  CA  ILE B1278      81.077   3.760  46.070  1.00 31.12           C  
ANISOU 1517  CA  ILE B1278     4067   4003   3755    241    297    266       C  
ATOM   1518  C   ILE B1278      81.716   3.400  44.742  1.00 31.27           C  
ANISOU 1518  C   ILE B1278     4085   4072   3723    356    317    316       C  
ATOM   1519  O   ILE B1278      82.826   3.871  44.400  1.00 31.77           O  
ANISOU 1519  O   ILE B1278     4069   4252   3750    362    336    387       O  
ATOM   1520  CB  ILE B1278      80.623   5.242  46.118  1.00 30.35           C  
ANISOU 1520  CB  ILE B1278     3951   3862   3717    119    295    241       C  
ATOM   1521  CG1 ILE B1278      79.828   5.492  47.404  1.00 29.95           C  
ANISOU 1521  CG1 ILE B1278     3922   3746   3710     25    280    181       C  
ATOM   1522  CG2 ILE B1278      79.747   5.601  44.908  1.00 28.29           C  
ANISOU 1522  CG2 ILE B1278     3741   3516   3491    149    297    219       C  
ATOM   1523  CD1 ILE B1278      80.100   6.854  48.011  1.00 30.92           C  
ANISOU 1523  CD1 ILE B1278     4002   3885   3859   -105    286    178       C  
ATOM   1524  N   THR B1279      81.029   2.533  44.022  1.00 29.95           N  
ANISOU 1524  N   THR B1279     4006   3825   3547    445    312    280       N  
ATOM   1525  CA  THR B1279      81.430   2.195  42.669  1.00 30.86           C  
ANISOU 1525  CA  THR B1279     4141   3971   3613    558    331    311       C  
ATOM   1526  C   THR B1279      80.306   2.601  41.726  1.00 31.32           C  
ANISOU 1526  C   THR B1279     4257   3932   3708    542    316    262       C  
ATOM   1527  O   THR B1279      79.283   3.202  42.126  1.00 29.56           O  
ANISOU 1527  O   THR B1279     4050   3628   3551    448    296    215       O  
ATOM   1528  CB  THR B1279      81.775   0.682  42.542  1.00 30.71           C  
ANISOU 1528  CB  THR B1279     4186   3953   3529    694    344    318       C  
ATOM   1529  OG1 THR B1279      80.587  -0.061  42.303  1.00 30.51           O  
ANISOU 1529  OG1 THR B1279     4275   3794   3521    712    320    244       O  
ATOM   1530  CG2 THR B1279      82.493   0.118  43.815  1.00 31.64           C  
ANISOU 1530  CG2 THR B1279     4260   4136   3624    698    352    354       C  
ATOM   1531  N   ASP B1280      80.503   2.318  40.451  1.00 30.81           N  
ANISOU 1531  N   ASP B1280     4222   3887   3598    637    329    279       N  
ATOM   1532  CA  ASP B1280      79.456   2.503  39.462  1.00 31.29           C  
ANISOU 1532  CA  ASP B1280     4341   3870   3677    637    313    237       C  
ATOM   1533  C   ASP B1280      78.224   1.601  39.638  1.00 29.92           C  
ANISOU 1533  C   ASP B1280     4273   3576   3517    634    280    162       C  
ATOM   1534  O   ASP B1280      77.183   1.930  39.124  1.00 29.90           O  
ANISOU 1534  O   ASP B1280     4302   3513   3544    596    259    128       O  
ATOM   1535  CB  ASP B1280      80.010   2.302  38.061  1.00 32.33           C  
ANISOU 1535  CB  ASP B1280     4483   4061   3740    747    335    272       C  
ATOM   1536  CG  ASP B1280      80.751   1.006  37.915  1.00 33.34           C  
ANISOU 1536  CG  ASP B1280     4660   4219   3786    878    354    283       C  
ATOM   1537  OD1 ASP B1280      81.682   0.749  38.738  1.00 34.28           O  
ANISOU 1537  OD1 ASP B1280     4729   4407   3886    897    373    328       O  
ATOM   1538  OD2 ASP B1280      80.388   0.265  36.986  1.00 35.38           O  
ANISOU 1538  OD2 ASP B1280     5011   4434   3997    960    351    248       O  
ATOM   1539  N   SER B1281      78.348   0.464  40.339  1.00 30.01           N  
ANISOU 1539  N   SER B1281     4336   3561   3505    673    275    143       N  
ATOM   1540  CA  SER B1281      77.226  -0.453  40.547  1.00 29.28           C  
ANISOU 1540  CA  SER B1281     4345   3356   3424    661    240     79       C  
ATOM   1541  C   SER B1281      76.962  -0.845  42.016  1.00 28.86           C  
ANISOU 1541  C   SER B1281     4289   3266   3407    604    226     63       C  
ATOM   1542  O   SER B1281      76.115  -1.721  42.297  1.00 28.09           O  
ANISOU 1542  O   SER B1281     4274   3080   3318    595    198     20       O  
ATOM   1543  CB  SER B1281      77.448  -1.709  39.706  1.00 30.07           C  
ANISOU 1543  CB  SER B1281     4549   3429   3447    781    245     63       C  
ATOM   1544  OG  SER B1281      78.372  -2.549  40.351  1.00 29.75           O  
ANISOU 1544  OG  SER B1281     4515   3418   3369    855    271     92       O  
ATOM   1545  N   SER B1282      77.685  -0.253  42.955  1.00 27.67           N  
ANISOU 1545  N   SER B1282     4048   3188   3275    563    244    101       N  
ATOM   1546  CA  SER B1282      77.454  -0.607  44.368  1.00 28.89           C  
ANISOU 1546  CA  SER B1282     4196   3321   3459    509    232     88       C  
ATOM   1547  C   SER B1282      77.816   0.518  45.321  1.00 27.41           C  
ANISOU 1547  C   SER B1282     3909   3198   3308    414    240    108       C  
ATOM   1548  O   SER B1282      78.691   1.330  45.031  1.00 30.08           O  
ANISOU 1548  O   SER B1282     4174   3620   3632    406    261    151       O  
ATOM   1549  CB  SER B1282      78.197  -1.912  44.730  1.00 29.72           C  
ANISOU 1549  CB  SER B1282     4336   3445   3510    606    247    113       C  
ATOM   1550  OG  SER B1282      79.591  -1.714  44.740  1.00 31.23           O  
ANISOU 1550  OG  SER B1282     4449   3760   3655    660    283    181       O  
ATOM   1551  N   ILE B1283      77.150   0.516  46.486  1.00 26.69           N  
ANISOU 1551  N   ILE B1283     3817   3066   3257    339    222     78       N  
ATOM   1552  CA  ILE B1283      77.342   1.504  47.551  1.00 25.51           C  
ANISOU 1552  CA  ILE B1283     3592   2961   3138    239    227     82       C  
ATOM   1553  C   ILE B1283      77.435   0.733  48.846  1.00 25.59           C  
ANISOU 1553  C   ILE B1283     3597   2986   3138    230    219     82       C  
ATOM   1554  O   ILE B1283      76.606  -0.100  49.101  1.00 24.78           O  
ANISOU 1554  O   ILE B1283     3556   2811   3049    245    200     55       O  
ATOM   1555  CB  ILE B1283      76.150   2.502  47.623  1.00 24.98           C  
ANISOU 1555  CB  ILE B1283     3536   2818   3136    150    217     37       C  
ATOM   1556  CG1 ILE B1283      76.112   3.398  46.371  1.00 25.31           C  
ANISOU 1556  CG1 ILE B1283     3571   2854   3190    156    229     47       C  
ATOM   1557  CG2 ILE B1283      76.220   3.319  48.901  1.00 25.29           C  
ANISOU 1557  CG2 ILE B1283     3525   2882   3200     52    222     25       C  
ATOM   1558  CD1 ILE B1283      74.782   4.098  46.184  1.00 23.78           C  
ANISOU 1558  CD1 ILE B1283     3404   2576   3053    105    222     13       C  
ATOM   1559  N   GLY B1284      78.434   1.040  49.658  1.00 25.93           N  
ANISOU 1559  N   GLY B1284     3563   3132   3156    199    232    119       N  
ATOM   1560  CA  GLY B1284      78.606   0.359  50.946  1.00 25.36           C  
ANISOU 1560  CA  GLY B1284     3472   3095   3068    190    227    129       C  
ATOM   1561  C   GLY B1284      78.008   1.209  52.043  1.00 24.53           C  
ANISOU 1561  C   GLY B1284     3340   2977   3002     70    216     89       C  
ATOM   1562  O   GLY B1284      78.182   2.431  52.065  1.00 24.87           O  
ANISOU 1562  O   GLY B1284     3346   3043   3061     -8    223     78       O  
ATOM   1563  N   LEU B1285      77.245   0.571  52.930  1.00 24.44           N  
ANISOU 1563  N   LEU B1285     3357   2921   3006     58    200     65       N  
ATOM   1564  CA  LEU B1285      76.635   1.234  54.068  1.00 24.24           C  
ANISOU 1564  CA  LEU B1285     3313   2888   3008    -39    193     27       C  
ATOM   1565  C   LEU B1285      77.307   0.766  55.338  1.00 25.47           C  
ANISOU 1565  C   LEU B1285     3414   3138   3123    -54    193     56       C  
ATOM   1566  O   LEU B1285      77.508  -0.443  55.531  1.00 25.64           O  
ANISOU 1566  O   LEU B1285     3447   3174   3121     19    191     92       O  
ATOM   1567  CB  LEU B1285      75.130   0.920  54.150  1.00 23.07           C  
ANISOU 1567  CB  LEU B1285     3229   2628   2908    -45    175    -15       C  
ATOM   1568  CG  LEU B1285      74.355   0.949  52.860  1.00 22.66           C  
ANISOU 1568  CG  LEU B1285     3236   2486   2886    -11    169    -32       C  
ATOM   1569  CD1 LEU B1285      72.879   0.713  53.219  1.00 22.20           C  
ANISOU 1569  CD1 LEU B1285     3220   2347   2869    -39    148    -63       C  
ATOM   1570  CD2 LEU B1285      74.567   2.230  52.123  1.00 22.75           C  
ANISOU 1570  CD2 LEU B1285     3228   2502   2914    -43    186    -40       C  
ATOM   1571  N   ARG B1286      77.638   1.732  56.172  1.00 25.58           N  
ANISOU 1571  N   ARG B1286     3376   3216   3128   -150    196     42       N  
ATOM   1572  CA  ARG B1286      78.210   1.502  57.478  1.00 27.80           C  
ANISOU 1572  CA  ARG B1286     3597   3600   3365   -189    193     64       C  
ATOM   1573  C   ARG B1286      77.438   2.317  58.517  1.00 27.33           C  
ANISOU 1573  C   ARG B1286     3543   3514   3326   -291    188      2       C  
ATOM   1574  O   ARG B1286      77.025   3.479  58.274  1.00 25.43           O  
ANISOU 1574  O   ARG B1286     3327   3217   3116   -356    196    -46       O  
ATOM   1575  CB  ARG B1286      79.701   1.915  57.454  1.00 30.97           C  
ANISOU 1575  CB  ARG B1286     3916   4141   3708   -213    201    118       C  
ATOM   1576  CG  ARG B1286      80.392   1.968  58.806  1.00 33.90           C  
ANISOU 1576  CG  ARG B1286     4210   4644   4023   -282    195    141       C  
ATOM   1577  CD  ARG B1286      81.919   2.000  58.664  1.00 36.84           C  
ANISOU 1577  CD  ARG B1286     4491   5175   4328   -278    201    223       C  
ATOM   1578  NE  ARG B1286      82.482   3.345  58.408  1.00 39.25           N  
ANISOU 1578  NE  ARG B1286     4764   5521   4625   -388    198    212       N  
ATOM   1579  CZ  ARG B1286      83.684   3.584  57.859  1.00 40.58           C  
ANISOU 1579  CZ  ARG B1286     4862   5806   4750   -388    203    283       C  
ATOM   1580  NH1 ARG B1286      84.489   2.591  57.484  1.00 41.21           N  
ANISOU 1580  NH1 ARG B1286     4894   5977   4784   -271    217    374       N  
ATOM   1581  NH2 ARG B1286      84.086   4.834  57.671  1.00 41.35           N  
ANISOU 1581  NH2 ARG B1286     4938   5925   4845   -503    197    269       N  
ATOM   1582  N   TRP B1287      77.322   1.742  59.710  1.00 26.12           N  
ANISOU 1582  N   TRP B1287     3365   3408   3148   -303    180      9       N  
ATOM   1583  CA  TRP B1287      76.655   2.372  60.846  1.00 25.92           C  
ANISOU 1583  CA  TRP B1287     3343   3377   3126   -388    179    -44       C  
ATOM   1584  C   TRP B1287      77.055   1.603  62.094  1.00 26.14           C  
ANISOU 1584  C   TRP B1287     3316   3513   3103   -390    170     -8       C  
ATOM   1585  O   TRP B1287      77.433   0.404  62.016  1.00 26.20           O  
ANISOU 1585  O   TRP B1287     3305   3554   3093   -306    167     55       O  
ATOM   1586  CB  TRP B1287      75.117   2.416  60.693  1.00 24.04           C  
ANISOU 1586  CB  TRP B1287     3174   3008   2950   -374    179    -91       C  
ATOM   1587  CG  TRP B1287      74.430   1.031  60.698  1.00 22.63           C  
ANISOU 1587  CG  TRP B1287     3020   2787   2789   -295    164    -59       C  
ATOM   1588  CD1 TRP B1287      74.076   0.312  61.795  1.00 23.35           C  
ANISOU 1588  CD1 TRP B1287     3094   2911   2866   -293    155    -44       C  
ATOM   1589  CD2 TRP B1287      74.048   0.239  59.579  1.00 21.89           C  
ANISOU 1589  CD2 TRP B1287     2978   2613   2727   -215    155    -39       C  
ATOM   1590  NE1 TRP B1287      73.463  -0.859  61.447  1.00 22.18           N  
ANISOU 1590  NE1 TRP B1287     2983   2698   2743   -224    141    -14       N  
ATOM   1591  CE2 TRP B1287      73.454  -0.953  60.090  1.00 21.86           C  
ANISOU 1591  CE2 TRP B1287     2990   2586   2728   -177    139    -13       C  
ATOM   1592  CE3 TRP B1287      74.127   0.400  58.188  1.00 23.09           C  
ANISOU 1592  CE3 TRP B1287     3165   2707   2899   -176    158    -40       C  
ATOM   1593  CZ2 TRP B1287      72.955  -1.942  59.267  1.00 21.41           C  
ANISOU 1593  CZ2 TRP B1287     2993   2445   2695   -111    124      4       C  
ATOM   1594  CZ3 TRP B1287      73.640  -0.584  57.395  1.00 22.53           C  
ANISOU 1594  CZ3 TRP B1287     3150   2564   2846   -106    144    -24       C  
ATOM   1595  CH2 TRP B1287      73.061  -1.748  57.907  1.00 21.82           C  
ANISOU 1595  CH2 TRP B1287     3085   2443   2760    -77    126     -4       C  
ATOM   1596  N   THR B1288      76.869   2.229  63.240  1.00 26.99           N  
ANISOU 1596  N   THR B1288     3405   3661   3186   -477    170    -48       N  
ATOM   1597  CA  THR B1288      77.146   1.581  64.503  1.00 26.99           C  
ANISOU 1597  CA  THR B1288     3349   3769   3134   -487    161    -17       C  
ATOM   1598  C   THR B1288      75.864   0.906  65.015  1.00 25.68           C  
ANISOU 1598  C   THR B1288     3220   3531   3004   -448    158    -29       C  
ATOM   1599  O   THR B1288      74.895   1.587  65.274  1.00 25.83           O  
ANISOU 1599  O   THR B1288     3281   3481   3051   -489    165    -91       O  
ATOM   1600  CB  THR B1288      77.653   2.600  65.552  1.00 29.46           C  
ANISOU 1600  CB  THR B1288     3623   4182   3388   -610    160    -56       C  
ATOM   1601  OG1 THR B1288      78.744   3.363  64.994  1.00 30.79           O  
ANISOU 1601  OG1 THR B1288     3762   4406   3529   -665    159    -46       O  
ATOM   1602  CG2 THR B1288      78.115   1.874  66.815  1.00 29.54           C  
ANISOU 1602  CG2 THR B1288     3558   4333   3330   -617    149     -9       C  
ATOM   1603  N   PRO B1289      75.851  -0.434  65.140  1.00 25.23           N  
ANISOU 1603  N   PRO B1289     3151   3488   2946   -367    151     34       N  
ATOM   1604  CA  PRO B1289      74.620  -1.034  65.708  1.00 24.55           C  
ANISOU 1604  CA  PRO B1289     3095   3341   2892   -347    144     29       C  
ATOM   1605  C   PRO B1289      74.180  -0.385  67.016  1.00 25.22           C  
ANISOU 1605  C   PRO B1289     3153   3480   2946   -425    148    -13       C  
ATOM   1606  O   PRO B1289      75.054  -0.078  67.864  1.00 25.76           O  
ANISOU 1606  O   PRO B1289     3161   3676   2948   -479    148     -7       O  
ATOM   1607  CB  PRO B1289      75.013  -2.501  65.920  1.00 25.48           C  
ANISOU 1607  CB  PRO B1289     3188   3498   2994   -266    138    114       C  
ATOM   1608  CG  PRO B1289      76.050  -2.741  64.907  1.00 25.22           C  
ANISOU 1608  CG  PRO B1289     3154   3478   2949   -210    146    152       C  
ATOM   1609  CD  PRO B1289      76.856  -1.455  64.855  1.00 25.97           C  
ANISOU 1609  CD  PRO B1289     3208   3648   3010   -289    152    118       C  
ATOM   1610  N   LEU B1290      72.870  -0.091  67.124  1.00 23.80           N  
ANISOU 1610  N   LEU B1290     3020   3212   2809   -434    151    -56       N  
ATOM   1611  CA  LEU B1290      72.250   0.352  68.395  1.00 25.16           C  
ANISOU 1611  CA  LEU B1290     3178   3429   2954   -485    160    -91       C  
ATOM   1612  C   LEU B1290      72.151  -0.814  69.339  1.00 25.04           C  
ANISOU 1612  C   LEU B1290     3115   3485   2914   -452    147    -26       C  
ATOM   1613  O   LEU B1290      71.983  -1.938  68.924  1.00 25.17           O  
ANISOU 1613  O   LEU B1290     3138   3461   2961   -386    134     33       O  
ATOM   1614  CB  LEU B1290      70.896   0.988  68.129  1.00 25.65           C  
ANISOU 1614  CB  LEU B1290     3298   3380   3066   -486    174   -141       C  
ATOM   1615  CG  LEU B1290      71.029   2.336  67.417  1.00 26.19           C  
ANISOU 1615  CG  LEU B1290     3412   3387   3149   -527    194   -207       C  
ATOM   1616  CD1 LEU B1290      69.702   2.715  66.745  1.00 25.65           C  
ANISOU 1616  CD1 LEU B1290     3400   3198   3145   -497    209   -229       C  
ATOM   1617  CD2 LEU B1290      71.499   3.415  68.397  1.00 27.81           C  
ANISOU 1617  CD2 LEU B1290     3610   3662   3293   -613    212   -268       C  
ATOM   1618  N   ASN B1291      72.220  -0.517  70.630  1.00 26.26           N  
ANISOU 1618  N   ASN B1291     3225   3742   3009   -502    153    -41       N  
ATOM   1619  CA  ASN B1291      72.479  -1.513  71.667  1.00 27.31           C  
ANISOU 1619  CA  ASN B1291     3292   3985   3099   -482    143     27       C  
ATOM   1620  C   ASN B1291      71.263  -2.004  72.459  1.00 28.49           C  
ANISOU 1620  C   ASN B1291     3439   4122   3262   -463    143     45       C  
ATOM   1621  O   ASN B1291      71.288  -3.065  73.079  1.00 28.41           O  
ANISOU 1621  O   ASN B1291     3384   4170   3239   -428    134    120       O  
ATOM   1622  CB  ASN B1291      73.504  -0.905  72.635  1.00 27.29           C  
ANISOU 1622  CB  ASN B1291     3228   4136   3004   -556    145      9       C  
ATOM   1623  CG  ASN B1291      74.863  -0.663  72.000  1.00 28.23           C  
ANISOU 1623  CG  ASN B1291     3321   4307   3096   -574    140     23       C  
ATOM   1624  OD1 ASN B1291      75.499  -1.579  71.529  1.00 28.19           O  
ANISOU 1624  OD1 ASN B1291     3288   4323   3098   -508    135    101       O  
ATOM   1625  ND2 ASN B1291      75.286   0.587  71.964  1.00 28.42           N  
ANISOU 1625  ND2 ASN B1291     3360   4347   3089   -662    145    -48       N  
ATOM   1626  N   SER B1292      70.195  -1.235  72.443  1.00 28.87           N  
ANISOU 1626  N   SER B1292     3532   4100   3337   -483    157    -13       N  
ATOM   1627  CA  SER B1292      69.024  -1.564  73.273  1.00 29.54           C  
ANISOU 1627  CA  SER B1292     3604   4192   3425   -469    160      6       C  
ATOM   1628  C   SER B1292      68.494  -2.940  72.898  1.00 29.77           C  
ANISOU 1628  C   SER B1292     3633   4168   3510   -408    137     94       C  
ATOM   1629  O   SER B1292      68.369  -3.285  71.715  1.00 26.95           O  
ANISOU 1629  O   SER B1292     3323   3703   3211   -377    124    105       O  
ATOM   1630  CB  SER B1292      67.928  -0.512  73.111  1.00 31.23           C  
ANISOU 1630  CB  SER B1292     3872   4330   3664   -482    185    -62       C  
ATOM   1631  OG  SER B1292      66.833  -0.821  73.988  1.00 31.95           O  
ANISOU 1631  OG  SER B1292     3939   4452   3748   -465    191    -33       O  
ATOM   1632  N   SER B1293      68.199  -3.754  73.908  1.00 30.53           N  
ANISOU 1632  N   SER B1293     3679   4338   3584   -395    130    157       N  
ATOM   1633  CA  SER B1293      67.636  -5.056  73.660  1.00 30.91           C  
ANISOU 1633  CA  SER B1293     3733   4329   3683   -350    108    242       C  
ATOM   1634  C   SER B1293      66.224  -4.965  73.063  1.00 29.66           C  
ANISOU 1634  C   SER B1293     3620   4061   3586   -347    100    236       C  
ATOM   1635  O   SER B1293      65.613  -5.994  72.793  1.00 33.65           O  
ANISOU 1635  O   SER B1293     4140   4509   4136   -326     76    303       O  
ATOM   1636  CB  SER B1293      67.661  -5.914  74.933  1.00 32.39           C  
ANISOU 1636  CB  SER B1293     3849   4626   3830   -339    105    320       C  
ATOM   1637  OG  SER B1293      66.809  -5.368  75.900  1.00 35.58           O  
ANISOU 1637  OG  SER B1293     4222   5092   4203   -366    118    300       O  
ATOM   1638  N   THR B1294      65.695  -3.753  72.863  1.00 27.57           N  
ANISOU 1638  N   THR B1294     3381   3771   3324   -371    121    162       N  
ATOM   1639  CA  THR B1294      64.422  -3.615  72.178  1.00 25.82           C  
ANISOU 1639  CA  THR B1294     3195   3456   3157   -363    117    164       C  
ATOM   1640  C   THR B1294      64.585  -3.823  70.693  1.00 25.15           C  
ANISOU 1640  C   THR B1294     3172   3256   3128   -350     97    158       C  
ATOM   1641  O   THR B1294      63.596  -4.013  70.025  1.00 25.48           O  
ANISOU 1641  O   THR B1294     3240   3223   3215   -346     81    179       O  
ATOM   1642  CB  THR B1294      63.743  -2.233  72.372  1.00 26.70           C  
ANISOU 1642  CB  THR B1294     3319   3570   3254   -377    155     95       C  
ATOM   1643  OG1 THR B1294      64.596  -1.176  71.881  1.00 27.74           O  
ANISOU 1643  OG1 THR B1294     3488   3678   3372   -396    176     12       O  
ATOM   1644  CG2 THR B1294      63.444  -1.968  73.869  1.00 28.37           C  
ANISOU 1644  CG2 THR B1294     3479   3896   3402   -385    179     94       C  
ATOM   1645  N   ILE B1295      65.811  -3.803  70.189  1.00 24.23           N  
ANISOU 1645  N   ILE B1295     3071   3134   3000   -343     97    135       N  
ATOM   1646  CA  ILE B1295      66.022  -3.706  68.750  1.00 24.38           C  
ANISOU 1646  CA  ILE B1295     3148   3052   3060   -328     87    112       C  
ATOM   1647  C   ILE B1295      66.144  -5.099  68.169  1.00 24.86           C  
ANISOU 1647  C   ILE B1295     3239   3054   3150   -294     55    175       C  
ATOM   1648  O   ILE B1295      66.931  -5.888  68.651  1.00 26.32           O  
ANISOU 1648  O   ILE B1295     3402   3286   3309   -272     52    219       O  
ATOM   1649  CB  ILE B1295      67.203  -2.764  68.403  1.00 25.20           C  
ANISOU 1649  CB  ILE B1295     3258   3179   3136   -340    109     51       C  
ATOM   1650  CG1 ILE B1295      66.780  -1.334  68.794  1.00 26.49           C  
ANISOU 1650  CG1 ILE B1295     3422   3359   3284   -378    141    -18       C  
ATOM   1651  CG2 ILE B1295      67.562  -2.813  66.923  1.00 23.98           C  
ANISOU 1651  CG2 ILE B1295     3156   2934   3018   -315     99     40       C  
ATOM   1652  CD1 ILE B1295      67.880  -0.409  69.131  1.00 27.74           C  
ANISOU 1652  CD1 ILE B1295     3567   3578   3392   -417    162    -73       C  
ATOM   1653  N   ILE B1296      65.369  -5.376  67.119  1.00 24.53           N  
ANISOU 1653  N   ILE B1296     3253   2910   3157   -291     33    181       N  
ATOM   1654  CA  ILE B1296      65.351  -6.703  66.466  1.00 25.36           C  
ANISOU 1654  CA  ILE B1296     3410   2935   3289   -266      0    232       C  
ATOM   1655  C   ILE B1296      66.132  -6.745  65.171  1.00 24.53           C  
ANISOU 1655  C   ILE B1296     3366   2761   3191   -233      0    203       C  
ATOM   1656  O   ILE B1296      66.481  -7.838  64.724  1.00 25.63           O  
ANISOU 1656  O   ILE B1296     3556   2844   3337   -198    -16    237       O  
ATOM   1657  CB  ILE B1296      63.916  -7.207  66.232  1.00 25.63           C  
ANISOU 1657  CB  ILE B1296     3466   2907   3361   -297    -33    269       C  
ATOM   1658  CG1 ILE B1296      63.130  -6.278  65.315  1.00 25.57           C  
ANISOU 1658  CG1 ILE B1296     3480   2857   3379   -317    -34    226       C  
ATOM   1659  CG2 ILE B1296      63.211  -7.336  67.577  1.00 26.50           C  
ANISOU 1659  CG2 ILE B1296     3510   3098   3460   -320    -30    315       C  
ATOM   1660  CD1 ILE B1296      61.702  -6.708  65.051  1.00 25.26           C  
ANISOU 1660  CD1 ILE B1296     3449   2777   3371   -355    -70    271       C  
ATOM   1661  N   GLY B1297      66.474  -5.566  64.606  1.00 23.51           N  
ANISOU 1661  N   GLY B1297     3236   2639   3058   -238     20    141       N  
ATOM   1662  CA  GLY B1297      67.155  -5.505  63.309  1.00 22.05           C  
ANISOU 1662  CA  GLY B1297     3102   2396   2878   -206     20    116       C  
ATOM   1663  C   GLY B1297      66.996  -4.141  62.645  1.00 20.60           C  
ANISOU 1663  C   GLY B1297     2919   2202   2705   -227     37     57       C  
ATOM   1664  O   GLY B1297      66.534  -3.157  63.242  1.00 20.49           O  
ANISOU 1664  O   GLY B1297     2868   2226   2690   -262     57     30       O  
ATOM   1665  N   TYR B1298      67.433  -4.100  61.399  1.00 20.40           N  
ANISOU 1665  N   TYR B1298     2938   2122   2687   -199     34     40       N  
ATOM   1666  CA  TYR B1298      67.317  -2.939  60.516  1.00 19.05           C  
ANISOU 1666  CA  TYR B1298     2778   1927   2532   -211     49     -4       C  
ATOM   1667  C   TYR B1298      66.813  -3.320  59.157  1.00 18.26           C  
ANISOU 1667  C   TYR B1298     2739   1741   2455   -193     24     -3       C  
ATOM   1668  O   TYR B1298      67.197  -4.361  58.597  1.00 18.73           O  
ANISOU 1668  O   TYR B1298     2848   1760   2506   -155      5     15       O  
ATOM   1669  CB  TYR B1298      68.647  -2.238  60.299  1.00 18.52           C  
ANISOU 1669  CB  TYR B1298     2690   1907   2437   -199     76    -28       C  
ATOM   1670  CG  TYR B1298      69.260  -1.855  61.590  1.00 18.87           C  
ANISOU 1670  CG  TYR B1298     2675   2047   2447   -228     96    -32       C  
ATOM   1671  CD1 TYR B1298      68.995  -0.629  62.179  1.00 19.19           C  
ANISOU 1671  CD1 TYR B1298     2689   2115   2484   -279    120    -74       C  
ATOM   1672  CD2 TYR B1298      70.170  -2.700  62.190  1.00 19.88           C  
ANISOU 1672  CD2 TYR B1298     2775   2238   2538   -202     94      7       C  
ATOM   1673  CE1 TYR B1298      69.555  -0.281  63.409  1.00 19.65           C  
ANISOU 1673  CE1 TYR B1298     2699   2266   2500   -316    135    -84       C  
ATOM   1674  CE2 TYR B1298      70.752  -2.386  63.393  1.00 20.12           C  
ANISOU 1674  CE2 TYR B1298     2745   2372   2528   -234    108      8       C  
ATOM   1675  CZ  TYR B1298      70.424  -1.202  64.022  1.00 20.09           C  
ANISOU 1675  CZ  TYR B1298     2718   2397   2517   -296    125    -40       C  
ATOM   1676  OH  TYR B1298      71.031  -0.962  65.227  1.00 21.85           O  
ANISOU 1676  OH  TYR B1298     2885   2727   2688   -334    135    -41       O  
ATOM   1677  N   ARG B1299      65.916  -2.506  58.641  1.00 17.08           N  
ANISOU 1677  N   ARG B1299     2592   1564   2332   -217     26    -21       N  
ATOM   1678  CA  ARG B1299      65.523  -2.585  57.239  1.00 16.26           C  
ANISOU 1678  CA  ARG B1299     2538   1396   2243   -205      6    -26       C  
ATOM   1679  C   ARG B1299      66.336  -1.613  56.383  1.00 16.40           C  
ANISOU 1679  C   ARG B1299     2555   1419   2256   -183     35    -58       C  
ATOM   1680  O   ARG B1299      66.412  -0.433  56.732  1.00 16.02           O  
ANISOU 1680  O   ARG B1299     2470   1401   2215   -203     68    -80       O  
ATOM   1681  CB  ARG B1299      64.057  -2.246  57.125  1.00 16.66           C  
ANISOU 1681  CB  ARG B1299     2579   1430   2321   -241     -6    -12       C  
ATOM   1682  CG  ARG B1299      63.500  -2.520  55.739  1.00 16.76           C  
ANISOU 1682  CG  ARG B1299     2639   1387   2342   -240    -37     -7       C  
ATOM   1683  CD  ARG B1299      62.014  -2.462  55.717  1.00 18.21           C  
ANISOU 1683  CD  ARG B1299     2804   1570   2543   -281    -59     25       C  
ATOM   1684  NE  ARG B1299      61.480  -1.147  56.013  1.00 20.08           N  
ANISOU 1684  NE  ARG B1299     2987   1844   2796   -282    -18     23       N  
ATOM   1685  CZ  ARG B1299      60.699  -0.868  57.068  1.00 19.07           C  
ANISOU 1685  CZ  ARG B1299     2812   1758   2676   -299     -3     47       C  
ATOM   1686  NH1 ARG B1299      60.370  -1.758  58.011  1.00 19.60           N  
ANISOU 1686  NH1 ARG B1299     2865   1844   2736   -322    -27     78       N  
ATOM   1687  NH2 ARG B1299      60.285   0.366  57.195  1.00 19.35           N  
ANISOU 1687  NH2 ARG B1299     2815   1814   2723   -286     42     40       N  
ATOM   1688  N   ILE B1300      66.823  -2.049  55.258  1.00 16.05           N  
ANISOU 1688  N   ILE B1300     2557   1341   2201   -147     23    -60       N  
ATOM   1689  CA  ILE B1300      67.485  -1.164  54.271  1.00 15.15           C  
ANISOU 1689  CA  ILE B1300     2442   1232   2083   -125     46    -80       C  
ATOM   1690  C   ILE B1300      66.524  -1.037  53.086  1.00 14.56           C  
ANISOU 1690  C   ILE B1300     2399   1105   2024   -128     26    -80       C  
ATOM   1691  O   ILE B1300      66.078  -2.093  52.560  1.00 14.57           O  
ANISOU 1691  O   ILE B1300     2455   1063   2017   -122    -12    -70       O  
ATOM   1692  CB  ILE B1300      68.856  -1.699  53.749  1.00 15.99           C  
ANISOU 1692  CB  ILE B1300     2568   1354   2152    -67     53    -75       C  
ATOM   1693  CG1 ILE B1300      69.787  -1.951  54.919  1.00 17.04           C  
ANISOU 1693  CG1 ILE B1300     2659   1551   2261    -63     69    -60       C  
ATOM   1694  CG2 ILE B1300      69.465  -0.772  52.676  1.00 16.34           C  
ANISOU 1694  CG2 ILE B1300     2605   1410   2193    -47     75    -87       C  
ATOM   1695  CD1 ILE B1300      69.721  -3.363  55.430  1.00 17.58           C  
ANISOU 1695  CD1 ILE B1300     2760   1600   2316    -37     48    -32       C  
ATOM   1696  N   THR B1301      66.134   0.179  52.721  1.00 13.60           N  
ANISOU 1696  N   THR B1301     2251    989   1925   -143     50    -89       N  
ATOM   1697  CA  THR B1301      65.274   0.423  51.578  1.00 13.63           C  
ANISOU 1697  CA  THR B1301     2273    964   1941   -143     35    -80       C  
ATOM   1698  C   THR B1301      66.046   1.389  50.634  1.00 13.23           C  
ANISOU 1698  C   THR B1301     2215    923   1889   -115     67    -91       C  
ATOM   1699  O   THR B1301      66.630   2.443  51.059  1.00 12.90           O  
ANISOU 1699  O   THR B1301     2137    905   1859   -123    109   -102       O  
ATOM   1700  CB  THR B1301      63.903   1.030  52.025  1.00 14.15           C  
ANISOU 1700  CB  THR B1301     2304   1034   2037   -179     41    -61       C  
ATOM   1701  OG1 THR B1301      63.314   0.222  53.065  1.00 14.52           O  
ANISOU 1701  OG1 THR B1301     2345   1088   2084   -207     17    -45       O  
ATOM   1702  CG2 THR B1301      62.928   1.163  50.904  1.00 14.50           C  
ANISOU 1702  CG2 THR B1301     2356   1065   2087   -182     21    -37       C  
ATOM   1703  N   VAL B1302      66.016   1.099  49.352  1.00 12.74           N  
ANISOU 1703  N   VAL B1302     2186    843   1811    -89     48    -86       N  
ATOM   1704  CA  VAL B1302      66.758   1.862  48.370  1.00 12.88           C  
ANISOU 1704  CA  VAL B1302     2196    874   1821    -57     74    -88       C  
ATOM   1705  C   VAL B1302      65.810   2.285  47.272  1.00 12.86           C  
ANISOU 1705  C   VAL B1302     2196    860   1828    -58     65    -71       C  
ATOM   1706  O   VAL B1302      65.075   1.483  46.674  1.00 13.17           O  
ANISOU 1706  O   VAL B1302     2271    882   1849    -64     22    -65       O  
ATOM   1707  CB  VAL B1302      67.939   1.122  47.753  1.00 13.74           C  
ANISOU 1707  CB  VAL B1302     2338    993   1887     -5     68    -93       C  
ATOM   1708  CG1 VAL B1302      68.616   1.985  46.741  1.00 13.46           C  
ANISOU 1708  CG1 VAL B1302     2284    983   1845     24     95    -85       C  
ATOM   1709  CG2 VAL B1302      68.900   0.712  48.823  1.00 13.76           C  
ANISOU 1709  CG2 VAL B1302     2328   1024   1876      1     79    -97       C  
ATOM   1710  N   VAL B1303      65.800   3.596  47.007  1.00 12.24           N  
ANISOU 1710  N   VAL B1303     2079    792   1777    -58    105    -60       N  
ATOM   1711  CA  VAL B1303      64.934   4.142  46.007  1.00 12.61           C  
ANISOU 1711  CA  VAL B1303     2117    840   1835    -53    106    -32       C  
ATOM   1712  C   VAL B1303      65.756   4.976  45.033  1.00 12.38           C  
ANISOU 1712  C   VAL B1303     2075    825   1803    -20    138    -23       C  
ATOM   1713  O   VAL B1303      66.530   5.837  45.491  1.00 12.19           O  
ANISOU 1713  O   VAL B1303     2027    804   1799    -25    179    -29       O  
ATOM   1714  CB  VAL B1303      63.786   5.044  46.650  1.00 12.80           C  
ANISOU 1714  CB  VAL B1303     2102    859   1901    -78    134     -8       C  
ATOM   1715  CG1 VAL B1303      62.779   5.412  45.575  1.00 13.43           C  
ANISOU 1715  CG1 VAL B1303     2165    953   1983    -67    129     34       C  
ATOM   1716  CG2 VAL B1303      63.091   4.314  47.852  1.00 12.98           C  
ANISOU 1716  CG2 VAL B1303     2125    880   1927   -111    111    -12       C  
ATOM   1717  N   ALA B1304      65.535   4.821  43.717  1.00 12.02           N  
ANISOU 1717  N   ALA B1304     2041    793   1732      5    119     -5       N  
ATOM   1718  CA  ALA B1304      66.266   5.645  42.787  1.00 12.48           C  
ANISOU 1718  CA  ALA B1304     2080    873   1789     38    151     12       C  
ATOM   1719  C   ALA B1304      65.500   6.970  42.914  1.00 12.50           C  
ANISOU 1719  C   ALA B1304     2041    864   1843     23    193     45       C  
ATOM   1720  O   ALA B1304      64.287   6.959  42.903  1.00 12.91           O  
ANISOU 1720  O   ALA B1304     2084    915   1905     12    182     67       O  
ATOM   1721  CB  ALA B1304      66.200   5.067  41.395  1.00 12.72           C  
ANISOU 1721  CB  ALA B1304     2136    926   1769     73    119     21       C  
ATOM   1722  N   ALA B1305      66.212   8.074  43.144  1.00 12.99           N  
ANISOU 1722  N   ALA B1305     2082    917   1936     21    244     50       N  
ATOM   1723  CA  ALA B1305      65.602   9.278  43.634  1.00 13.94           C  
ANISOU 1723  CA  ALA B1305     2182   1004   2107      6    293     68       C  
ATOM   1724  C   ALA B1305      64.623   9.837  42.531  1.00 14.24           C  
ANISOU 1724  C   ALA B1305     2199   1055   2157     37    306    125       C  
ATOM   1725  O   ALA B1305      64.950   9.965  41.342  1.00 14.62           O  
ANISOU 1725  O   ALA B1305     2235   1131   2186     66    303    153       O  
ATOM   1726  CB  ALA B1305      66.631  10.364  43.962  1.00 14.53           C  
ANISOU 1726  CB  ALA B1305     2252   1058   2208    -11    343     62       C  
ATOM   1727  N   GLY B1306      63.394  10.134  42.964  1.00 15.54           N  
ANISOU 1727  N   GLY B1306     2350   1207   2346     35    320    149       N  
ATOM   1728  CA  GLY B1306      62.254  10.490  42.106  1.00 16.61           C  
ANISOU 1728  CA  GLY B1306     2454   1372   2485     64    327    214       C  
ATOM   1729  C   GLY B1306      61.277   9.382  41.728  1.00 18.10           C  
ANISOU 1729  C   GLY B1306     2635   1610   2632     52    262    230       C  
ATOM   1730  O   GLY B1306      60.157   9.659  41.271  1.00 20.00           O  
ANISOU 1730  O   GLY B1306     2838   1887   2873     65    266    291       O  
ATOM   1731  N   GLU B1307      61.732   8.145  41.899  1.00 17.32           N  
ANISOU 1731  N   GLU B1307     2570   1513   2494     26    205    181       N  
ATOM   1732  CA  GLU B1307      60.853   6.959  41.742  1.00 18.44           C  
ANISOU 1732  CA  GLU B1307     2722   1685   2596     -5    136    185       C  
ATOM   1733  C   GLU B1307      59.850   6.872  42.893  1.00 18.36           C  
ANISOU 1733  C   GLU B1307     2691   1672   2609    -33    137    200       C  
ATOM   1734  O   GLU B1307      60.097   7.296  44.007  1.00 18.08           O  
ANISOU 1734  O   GLU B1307     2657   1603   2608    -33    176    179       O  
ATOM   1735  CB  GLU B1307      61.644   5.665  41.588  1.00 17.79           C  
ANISOU 1735  CB  GLU B1307     2699   1592   2467    -18     82    129       C  
ATOM   1736  CG  GLU B1307      62.533   5.578  40.391  1.00 18.97           C  
ANISOU 1736  CG  GLU B1307     2871   1757   2579     16     76    118       C  
ATOM   1737  CD  GLU B1307      62.433   4.225  39.724  1.00 20.83           C  
ANISOU 1737  CD  GLU B1307     3164   1999   2748      2      8     90       C  
ATOM   1738  OE1 GLU B1307      62.942   3.232  40.242  1.00 21.24           O  
ANISOU 1738  OE1 GLU B1307     3270   2016   2781     -5    -17     44       O  
ATOM   1739  OE2 GLU B1307      61.739   4.182  38.703  1.00 23.16           O  
ANISOU 1739  OE2 GLU B1307     3452   2336   3011     -3    -18    119       O  
ATOM   1740  N   GLY B1308      58.724   6.245  42.605  1.00 19.28           N  
ANISOU 1740  N   GLY B1308     2791   1833   2699    -63     89    238       N  
ATOM   1741  CA  GLY B1308      57.652   6.185  43.622  1.00 19.62           C  
ANISOU 1741  CA  GLY B1308     2801   1893   2761    -86     90    271       C  
ATOM   1742  C   GLY B1308      57.610   4.942  44.463  1.00 19.00           C  
ANISOU 1742  C   GLY B1308     2755   1798   2665   -138     36    236       C  
ATOM   1743  O   GLY B1308      56.686   4.753  45.237  1.00 19.73           O  
ANISOU 1743  O   GLY B1308     2816   1915   2765   -163     28    270       O  
ATOM   1744  N   ILE B1309      58.496   3.988  44.170  1.00 18.58           N  
ANISOU 1744  N   ILE B1309     2764   1712   2581   -154     -6    179       N  
ATOM   1745  CA  ILE B1309      58.538   2.650  44.831  1.00 18.45           C  
ANISOU 1745  CA  ILE B1309     2794   1671   2546   -201    -61    147       C  
ATOM   1746  C   ILE B1309      60.021   2.341  44.965  1.00 17.30           C  
ANISOU 1746  C   ILE B1309     2703   1476   2394   -171    -49     81       C  
ATOM   1747  O   ILE B1309      60.796   2.790  44.106  1.00 17.46           O  
ANISOU 1747  O   ILE B1309     2732   1494   2404   -131    -28     67       O  
ATOM   1748  CB  ILE B1309      57.886   1.527  43.997  1.00 19.53           C  
ANISOU 1748  CB  ILE B1309     2966   1823   2631   -256   -141    158       C  
ATOM   1749  CG1 ILE B1309      56.416   1.747  43.808  1.00 20.14           C  
ANISOU 1749  CG1 ILE B1309     2979   1969   2704   -296   -162    234       C  
ATOM   1750  CG2 ILE B1309      58.000   0.179  44.693  1.00 19.87           C  
ANISOU 1750  CG2 ILE B1309     3069   1821   2660   -303   -192    125       C  
ATOM   1751  CD1 ILE B1309      55.702   0.664  43.012  1.00 20.32           C  
ANISOU 1751  CD1 ILE B1309     3034   2014   2669   -372   -248    248       C  
ATOM   1752  N   PRO B1310      60.442   1.679  46.045  1.00 16.41           N  
ANISOU 1752  N   PRO B1310     2613   1333   2287   -184    -56     52       N  
ATOM   1753  CA  PRO B1310      61.813   1.152  46.161  1.00 15.66           C  
ANISOU 1753  CA  PRO B1310     2568   1204   2175   -155    -52      2       C  
ATOM   1754  C   PRO B1310      62.166   0.132  45.086  1.00 16.29           C  
ANISOU 1754  C   PRO B1310     2720   1262   2205   -147    -97    -20       C  
ATOM   1755  O   PRO B1310      61.249  -0.555  44.631  1.00 17.57           O  
ANISOU 1755  O   PRO B1310     2909   1422   2343   -191   -150     -6       O  
ATOM   1756  CB  PRO B1310      61.822   0.490  47.526  1.00 16.30           C  
ANISOU 1756  CB  PRO B1310     2653   1270   2268   -180    -60     -6       C  
ATOM   1757  CG  PRO B1310      60.667   1.015  48.259  1.00 16.46           C  
ANISOU 1757  CG  PRO B1310     2617   1319   2319   -211    -50     31       C  
ATOM   1758  CD  PRO B1310      59.647   1.399  47.251  1.00 17.05           C  
ANISOU 1758  CD  PRO B1310     2667   1422   2387   -222    -65     73       C  
ATOM   1759  N   ILE B1311      63.454   0.031  44.810  1.00 16.14           N  
ANISOU 1759  N   ILE B1311     2732   1231   2167    -95    -76    -51       N  
ATOM   1760  CA  ILE B1311      64.037  -0.983  43.876  1.00 17.73           C  
ANISOU 1760  CA  ILE B1311     3017   1406   2313    -64   -106    -80       C  
ATOM   1761  C   ILE B1311      64.532  -2.163  44.714  1.00 18.00           C  
ANISOU 1761  C   ILE B1311     3107   1394   2335    -59   -121   -102       C  
ATOM   1762  O   ILE B1311      64.508  -3.310  44.245  1.00 18.85           O  
ANISOU 1762  O   ILE B1311     3304   1457   2401    -58   -159   -123       O  
ATOM   1763  CB  ILE B1311      65.213  -0.507  42.982  1.00 19.07           C  
ANISOU 1763  CB  ILE B1311     3189   1598   2458      6    -70    -91       C  
ATOM   1764  CG1 ILE B1311      66.191   0.434  43.715  1.00 18.25           C  
ANISOU 1764  CG1 ILE B1311     3021   1522   2388     33    -13    -84       C  
ATOM   1765  CG2 ILE B1311      64.671   0.050  41.688  1.00 20.21           C  
ANISOU 1765  CG2 ILE B1311     3320   1772   2584      7    -78    -73       C  
ATOM   1766  CD1 ILE B1311      67.606   0.337  43.207  1.00 19.08           C  
ANISOU 1766  CD1 ILE B1311     3143   1648   2458    102     12    -92       C  
ATOM   1767  N   PHE B1312      65.031  -1.881  45.906  1.00 16.97           N  
ANISOU 1767  N   PHE B1312     2933   1277   2237    -54    -88    -98       N  
ATOM   1768  CA  PHE B1312      65.715  -2.792  46.788  1.00 16.81           C  
ANISOU 1768  CA  PHE B1312     2945   1233   2208    -35    -87   -107       C  
ATOM   1769  C   PHE B1312      65.189  -2.637  48.179  1.00 17.11           C  
ANISOU 1769  C   PHE B1312     2931   1284   2286    -82    -84    -90       C  
ATOM   1770  O   PHE B1312      64.970  -1.497  48.658  1.00 15.28           O  
ANISOU 1770  O   PHE B1312     2626   1092   2088   -100    -52    -80       O  
ATOM   1771  CB  PHE B1312      67.237  -2.630  46.741  1.00 18.24           C  
ANISOU 1771  CB  PHE B1312     3119   1441   2367     37    -44   -115       C  
ATOM   1772  CG  PHE B1312      67.867  -2.938  45.397  1.00 19.31           C  
ANISOU 1772  CG  PHE B1312     3312   1570   2454    101    -43   -129       C  
ATOM   1773  CD1 PHE B1312      67.428  -4.020  44.582  1.00 20.26           C  
ANISOU 1773  CD1 PHE B1312     3533   1631   2533    106    -84   -149       C  
ATOM   1774  CD2 PHE B1312      68.977  -2.205  44.952  1.00 20.29           C  
ANISOU 1774  CD2 PHE B1312     3396   1747   2564    156      0   -120       C  
ATOM   1775  CE1 PHE B1312      67.999  -4.279  43.372  1.00 20.70           C  
ANISOU 1775  CE1 PHE B1312     3646   1682   2534    169    -80   -166       C  
ATOM   1776  CE2 PHE B1312      69.566  -2.489  43.712  1.00 21.00           C  
ANISOU 1776  CE2 PHE B1312     3534   1840   2602    224      3   -128       C  
ATOM   1777  CZ  PHE B1312      69.103  -3.563  42.949  1.00 21.02           C  
ANISOU 1777  CZ  PHE B1312     3641   1784   2562    237    -33   -154       C  
ATOM   1778  N   GLU B1313      64.979  -3.758  48.860  1.00 16.25           N  
ANISOU 1778  N   GLU B1313     2862   1140   2171   -101   -112    -86       N  
ATOM   1779  CA  GLU B1313      64.679  -3.699  50.268  1.00 16.31           C  
ANISOU 1779  CA  GLU B1313     2818   1169   2208   -134   -104    -67       C  
ATOM   1780  C   GLU B1313      65.089  -5.014  50.892  1.00 17.16           C  
ANISOU 1780  C   GLU B1313     2979   1240   2300   -121   -120    -62       C  
ATOM   1781  O   GLU B1313      64.858  -6.057  50.288  1.00 18.17           O  
ANISOU 1781  O   GLU B1313     3193   1305   2405   -124   -157    -67       O  
ATOM   1782  CB  GLU B1313      63.207  -3.401  50.488  1.00 16.41           C  
ANISOU 1782  CB  GLU B1313     2795   1192   2248   -201   -129    -41       C  
ATOM   1783  CG  GLU B1313      62.851  -3.175  51.927  1.00 16.44           C  
ANISOU 1783  CG  GLU B1313     2738   1231   2278   -228   -113    -20       C  
ATOM   1784  CD  GLU B1313      61.447  -2.708  52.008  1.00 17.06           C  
ANISOU 1784  CD  GLU B1313     2771   1334   2378   -277   -126     13       C  
ATOM   1785  OE1 GLU B1313      60.559  -3.535  52.154  1.00 18.00           O  
ANISOU 1785  OE1 GLU B1313     2904   1439   2493   -326   -172     44       O  
ATOM   1786  OE2 GLU B1313      61.285  -1.518  51.824  1.00 17.34           O  
ANISOU 1786  OE2 GLU B1313     2759   1399   2428   -264    -90     13       O  
ATOM   1787  N   ASP B1314      65.733  -4.932  52.050  1.00 17.91           N  
ANISOU 1787  N   ASP B1314     3027   1373   2402   -106    -91    -52       N  
ATOM   1788  CA  ASP B1314      66.278  -6.131  52.683  1.00 18.67           C  
ANISOU 1788  CA  ASP B1314     3165   1444   2482    -78    -96    -37       C  
ATOM   1789  C   ASP B1314      66.369  -5.912  54.171  1.00 19.75           C  
ANISOU 1789  C   ASP B1314     3228   1640   2635    -97    -76    -14       C  
ATOM   1790  O   ASP B1314      66.188  -4.798  54.666  1.00 19.28           O  
ANISOU 1790  O   ASP B1314     3094   1636   2593   -125    -54    -21       O  
ATOM   1791  CB  ASP B1314      67.680  -6.372  52.114  1.00 19.90           C  
ANISOU 1791  CB  ASP B1314     3355   1603   2600      7    -66    -47       C  
ATOM   1792  CG  ASP B1314      68.091  -7.872  52.143  1.00 22.24           C  
ANISOU 1792  CG  ASP B1314     3744   1834   2870     56    -75    -33       C  
ATOM   1793  OD1 ASP B1314      67.305  -8.669  52.682  1.00 22.70           O  
ANISOU 1793  OD1 ASP B1314     3835   1844   2944     11   -107    -16       O  
ATOM   1794  OD2 ASP B1314      69.167  -8.183  51.601  1.00 23.53           O  
ANISOU 1794  OD2 ASP B1314     3945   1997   2997    140    -48    -36       O  
ATOM   1795  N   PHE B1315      66.726  -6.961  54.897  1.00 20.49           N  
ANISOU 1795  N   PHE B1315     3346   1720   2718    -78    -80     11       N  
ATOM   1796  CA  PHE B1315      66.760  -6.946  56.339  1.00 21.14           C  
ANISOU 1796  CA  PHE B1315     3361   1861   2809    -97    -67     38       C  
ATOM   1797  C   PHE B1315      68.063  -7.477  56.845  1.00 22.69           C  
ANISOU 1797  C   PHE B1315     3552   2093   2976    -32    -38     59       C  
ATOM   1798  O   PHE B1315      68.612  -8.434  56.296  1.00 23.39           O  
ANISOU 1798  O   PHE B1315     3714   2127   3042     26    -38     69       O  
ATOM   1799  CB  PHE B1315      65.615  -7.833  56.831  1.00 23.83           C  
ANISOU 1799  CB  PHE B1315     3727   2156   3170   -149   -108     71       C  
ATOM   1800  CG  PHE B1315      64.266  -7.232  56.604  1.00 24.59           C  
ANISOU 1800  CG  PHE B1315     3798   2252   3291   -217   -133     69       C  
ATOM   1801  CD1 PHE B1315      63.676  -7.263  55.353  1.00 25.33           C  
ANISOU 1801  CD1 PHE B1315     3946   2290   3385   -237   -163     52       C  
ATOM   1802  CD2 PHE B1315      63.586  -6.602  57.638  1.00 25.41           C  
ANISOU 1802  CD2 PHE B1315     3821   2421   3413   -257   -124     87       C  
ATOM   1803  CE1 PHE B1315      62.418  -6.702  55.147  1.00 25.65           C  
ANISOU 1803  CE1 PHE B1315     3952   2347   3445   -297   -185     64       C  
ATOM   1804  CE2 PHE B1315      62.330  -6.041  57.449  1.00 25.86           C  
ANISOU 1804  CE2 PHE B1315     3848   2486   3489   -308   -140     98       C  
ATOM   1805  CZ  PHE B1315      61.744  -6.090  56.188  1.00 26.04           C  
ANISOU 1805  CZ  PHE B1315     3917   2461   3514   -327   -171     91       C  
ATOM   1806  N   VAL B1316      68.544  -6.905  57.951  1.00 21.82           N  
ANISOU 1806  N   VAL B1316     3356   2075   2858    -41    -11     70       N  
ATOM   1807  CA  VAL B1316      69.648  -7.528  58.685  1.00 22.75           C  
ANISOU 1807  CA  VAL B1316     3451   2247   2944     11     11    108       C  
ATOM   1808  C   VAL B1316      69.257  -7.588  60.146  1.00 23.52           C  
ANISOU 1808  C   VAL B1316     3484   2404   3046    -31     10    136       C  
ATOM   1809  O   VAL B1316      68.506  -6.723  60.642  1.00 23.92           O  
ANISOU 1809  O   VAL B1316     3486   2487   3114    -93      6    115       O  
ATOM   1810  CB  VAL B1316      70.955  -6.770  58.442  1.00 21.92           C  
ANISOU 1810  CB  VAL B1316     3298   2223   2805     48     47     99       C  
ATOM   1811  CG1 VAL B1316      71.265  -6.683  56.959  1.00 21.65           C  
ANISOU 1811  CG1 VAL B1316     3325   2135   2765     93     49     75       C  
ATOM   1812  CG2 VAL B1316      70.872  -5.354  59.016  1.00 21.81           C  
ANISOU 1812  CG2 VAL B1316     3204   2286   2797    -18     60     68       C  
ATOM   1813  N   ASP B1317      69.708  -8.652  60.837  1.00 25.41           N  
ANISOU 1813  N   ASP B1317     3727   2657   3269      8     14    190       N  
ATOM   1814  CA  ASP B1317      69.404  -8.752  62.248  1.00 27.48           C  
ANISOU 1814  CA  ASP B1317     3923   2989   3530    -27     14    224       C  
ATOM   1815  C   ASP B1317      70.183  -7.696  63.009  1.00 26.30           C  
ANISOU 1815  C   ASP B1317     3677   2970   3346    -44     43    209       C  
ATOM   1816  O   ASP B1317      71.043  -6.987  62.443  1.00 26.04           O  
ANISOU 1816  O   ASP B1317     3630   2971   3293    -28     63    182       O  
ATOM   1817  CB  ASP B1317      69.699 -10.140  62.770  1.00 29.74           C  
ANISOU 1817  CB  ASP B1317     4235   3255   3807     21     15    292       C  
ATOM   1818  CG  ASP B1317      71.159 -10.424  62.783  1.00 33.86           C  
ANISOU 1818  CG  ASP B1317     4740   3839   4285    104     52    325       C  
ATOM   1819  OD1 ASP B1317      71.871  -9.711  63.516  1.00 34.94           O  
ANISOU 1819  OD1 ASP B1317     4781   4104   4388     93     73    329       O  
ATOM   1820  OD2 ASP B1317      71.624 -11.316  62.040  1.00 36.58           O  
ANISOU 1820  OD2 ASP B1317     5166   4110   4624    180     60    346       O  
ATOM   1821  N   SER B1318      69.879  -7.566  64.292  1.00 26.66           N  
ANISOU 1821  N   SER B1318     3656   3091   3381    -84     45    227       N  
ATOM   1822  CA  SER B1318      70.387  -6.436  65.078  1.00 26.29           C  
ANISOU 1822  CA  SER B1318     3528   3161   3299   -125     66    198       C  
ATOM   1823  C   SER B1318      71.903  -6.361  65.259  1.00 28.33           C  
ANISOU 1823  C   SER B1318     3738   3522   3504    -92     90    220       C  
ATOM   1824  O   SER B1318      72.425  -5.323  65.719  1.00 30.76           O  
ANISOU 1824  O   SER B1318     3987   3922   3778   -140    104    188       O  
ATOM   1825  CB  SER B1318      69.732  -6.385  66.453  1.00 27.60           C  
ANISOU 1825  CB  SER B1318     3638   3393   3454   -169     64    212       C  
ATOM   1826  OG  SER B1318      70.141  -7.487  67.265  1.00 27.53           O  
ANISOU 1826  OG  SER B1318     3601   3435   3424   -134     64    286       O  
ATOM   1827  N   SER B1319      72.598  -7.435  64.914  1.00 28.91           N  
ANISOU 1827  N   SER B1319     3835   3580   3566    -14     96    277       N  
ATOM   1828  CA  SER B1319      74.061  -7.525  65.080  1.00 30.35           C  
ANISOU 1828  CA  SER B1319     3963   3875   3693     31    121    321       C  
ATOM   1829  C   SER B1319      74.849  -6.787  64.007  1.00 29.34           C  
ANISOU 1829  C   SER B1319     3841   3753   3552     44    134    290       C  
ATOM   1830  O   SER B1319      76.008  -6.427  64.216  1.00 29.55           O  
ANISOU 1830  O   SER B1319     3799   3900   3528     50    151    316       O  
ATOM   1831  CB  SER B1319      74.463  -8.992  65.096  1.00 32.85           C  
ANISOU 1831  CB  SER B1319     4311   4167   4002    128    132    403       C  
ATOM   1832  OG  SER B1319      74.179  -9.611  63.844  1.00 34.76           O  
ANISOU 1832  OG  SER B1319     4662   4265   4278    184    128    392       O  
ATOM   1833  N   VAL B1320      74.199  -6.532  62.886  1.00 28.79           N  
ANISOU 1833  N   VAL B1320     3846   3565   3526     43    122    240       N  
ATOM   1834  CA  VAL B1320      74.830  -5.972  61.697  1.00 27.66           C  
ANISOU 1834  CA  VAL B1320     3722   3410   3377     67    133    217       C  
ATOM   1835  C   VAL B1320      75.027  -4.430  61.659  1.00 26.51           C  
ANISOU 1835  C   VAL B1320     3527   3319   3225    -14    137    163       C  
ATOM   1836  O   VAL B1320      74.096  -3.645  61.834  1.00 25.56           O  
ANISOU 1836  O   VAL B1320     3416   3157   3137    -83    127    108       O  
ATOM   1837  CB  VAL B1320      74.048  -6.435  60.450  1.00 27.42           C  
ANISOU 1837  CB  VAL B1320     3797   3230   3390    103    118    191       C  
ATOM   1838  CG1 VAL B1320      74.586  -5.818  59.173  1.00 28.22           C  
ANISOU 1838  CG1 VAL B1320     3918   3318   3485    128    129    166       C  
ATOM   1839  CG2 VAL B1320      74.071  -7.963  60.382  1.00 27.93           C  
ANISOU 1839  CG2 VAL B1320     3927   3232   3452    186    119    243       C  
ATOM   1840  N   GLY B1321      76.253  -4.016  61.317  1.00 27.78           N  
ANISOU 1840  N   GLY B1321     3642   3566   3345      1    155    185       N  
ATOM   1841  CA  GLY B1321      76.587  -2.585  61.097  1.00 27.69           C  
ANISOU 1841  CA  GLY B1321     3596   3597   3328    -76    160    140       C  
ATOM   1842  C   GLY B1321      77.189  -2.268  59.719  1.00 29.02           C  
ANISOU 1842  C   GLY B1321     3784   3744   3497    -34    170    144       C  
ATOM   1843  O   GLY B1321      77.922  -1.303  59.582  1.00 30.47           O  
ANISOU 1843  O   GLY B1321     3920   3998   3658    -84    178    139       O  
ATOM   1844  N   TYR B1322      76.816  -3.062  58.727  1.00 30.02           N  
ANISOU 1844  N   TYR B1322     3986   3772   3647     47    169    149       N  
ATOM   1845  CA  TYR B1322      77.481  -3.139  57.433  1.00 31.39           C  
ANISOU 1845  CA  TYR B1322     4183   3936   3807    119    183    169       C  
ATOM   1846  C   TYR B1322      76.599  -3.901  56.429  1.00 30.45           C  
ANISOU 1846  C   TYR B1322     4170   3675   3722    181    172    146       C  
ATOM   1847  O   TYR B1322      76.201  -5.048  56.673  1.00 31.19           O  
ANISOU 1847  O   TYR B1322     4316   3713   3821    228    164    163       O  
ATOM   1848  CB  TYR B1322      78.817  -3.876  57.574  1.00 35.16           C  
ANISOU 1848  CB  TYR B1322     4611   4523   4222    204    207    251       C  
ATOM   1849  CG  TYR B1322      78.731  -5.199  58.332  1.00 37.68           C  
ANISOU 1849  CG  TYR B1322     4949   4836   4529    267    210    296       C  
ATOM   1850  CD1 TYR B1322      78.855  -5.235  59.731  1.00 39.10           C  
ANISOU 1850  CD1 TYR B1322     5058   5108   4690    217    206    321       C  
ATOM   1851  CD2 TYR B1322      78.528  -6.415  57.667  1.00 40.16           C  
ANISOU 1851  CD2 TYR B1322     5357   5051   4848    374    218    314       C  
ATOM   1852  CE1 TYR B1322      78.765  -6.430  60.440  1.00 39.32           C  
ANISOU 1852  CE1 TYR B1322     5098   5131   4708    275    211    371       C  
ATOM   1853  CE2 TYR B1322      78.430  -7.610  58.378  1.00 39.75           C  
ANISOU 1853  CE2 TYR B1322     5330   4981   4790    428    224    359       C  
ATOM   1854  CZ  TYR B1322      78.557  -7.609  59.758  1.00 39.64           C  
ANISOU 1854  CZ  TYR B1322     5234   5063   4762    381    221    392       C  
ATOM   1855  OH  TYR B1322      78.476  -8.783  60.471  1.00 40.41           O  
ANISOU 1855  OH  TYR B1322     5351   5147   4854    437    229    446       O  
ATOM   1856  N   TYR B1323      76.309  -3.263  55.302  1.00 27.84           N  
ANISOU 1856  N   TYR B1323     3873   3290   3413    175    169    110       N  
ATOM   1857  CA  TYR B1323      75.462  -3.844  54.252  1.00 27.45           C  
ANISOU 1857  CA  TYR B1323     3923   3118   3389    217    153     83       C  
ATOM   1858  C   TYR B1323      75.997  -3.233  52.953  1.00 26.86           C  
ANISOU 1858  C   TYR B1323     3851   3053   3300    250    168     79       C  
ATOM   1859  O   TYR B1323      76.378  -2.056  52.955  1.00 27.97           O  
ANISOU 1859  O   TYR B1323     3927   3255   3444    195    178     75       O  
ATOM   1860  CB  TYR B1323      73.962  -3.499  54.475  1.00 26.77           C  
ANISOU 1860  CB  TYR B1323     3865   2947   3357    137    124     34       C  
ATOM   1861  CG  TYR B1323      73.061  -4.131  53.426  1.00 25.39           C  
ANISOU 1861  CG  TYR B1323     3786   2660   3200    165    101     11       C  
ATOM   1862  CD1 TYR B1323      72.643  -5.463  53.541  1.00 25.39           C  
ANISOU 1862  CD1 TYR B1323     3859   2590   3197    199     82     23       C  
ATOM   1863  CD2 TYR B1323      72.645  -3.429  52.296  1.00 24.04           C  
ANISOU 1863  CD2 TYR B1323     3636   2452   3044    153     96    -17       C  
ATOM   1864  CE1 TYR B1323      71.837  -6.048  52.565  1.00 25.17           C  
ANISOU 1864  CE1 TYR B1323     3925   2459   3176    209     55      0       C  
ATOM   1865  CE2 TYR B1323      71.829  -4.004  51.334  1.00 24.59           C  
ANISOU 1865  CE2 TYR B1323     3789   2432   3119    169     69    -37       C  
ATOM   1866  CZ  TYR B1323      71.427  -5.330  51.459  1.00 24.59           C  
ANISOU 1866  CZ  TYR B1323     3866   2363   3112    192     46    -31       C  
ATOM   1867  OH  TYR B1323      70.638  -5.946  50.474  1.00 24.04           O  
ANISOU 1867  OH  TYR B1323     3890   2203   3039    195     15    -54       O  
ATOM   1868  N   THR B1324      76.126  -4.040  51.894  1.00 26.94           N  
ANISOU 1868  N   THR B1324     3935   3010   3287    341    171     86       N  
ATOM   1869  CA  THR B1324      76.480  -3.501  50.551  1.00 25.98           C  
ANISOU 1869  CA  THR B1324     3824   2894   3151    377    183     81       C  
ATOM   1870  C   THR B1324      75.287  -3.652  49.648  1.00 25.99           C  
ANISOU 1870  C   THR B1324     3913   2781   3181    365    155     31       C  
ATOM   1871  O   THR B1324      74.806  -4.762  49.413  1.00 25.71           O  
ANISOU 1871  O   THR B1324     3967   2663   3136    406    139     19       O  
ATOM   1872  CB  THR B1324      77.755  -4.144  49.925  1.00 26.95           C  
ANISOU 1872  CB  THR B1324     3953   3076   3209    500    217    133       C  
ATOM   1873  OG1 THR B1324      78.756  -4.341  50.920  1.00 27.80           O  
ANISOU 1873  OG1 THR B1324     3985   3292   3285    518    239    191       O  
ATOM   1874  CG2 THR B1324      78.323  -3.292  48.811  1.00 26.98           C  
ANISOU 1874  CG2 THR B1324     3925   3130   3195    519    234    142       C  
ATOM   1875  N   VAL B1325      74.816  -2.516  49.117  1.00 25.20           N  
ANISOU 1875  N   VAL B1325     3786   2677   3111    307    150      7       N  
ATOM   1876  CA  VAL B1325      73.799  -2.477  48.094  1.00 25.29           C  
ANISOU 1876  CA  VAL B1325     3860   2608   3139    298    126    -27       C  
ATOM   1877  C   VAL B1325      74.453  -2.781  46.750  1.00 26.19           C  
ANISOU 1877  C   VAL B1325     4016   2728   3203    389    140    -18       C  
ATOM   1878  O   VAL B1325      75.486  -2.180  46.401  1.00 24.79           O  
ANISOU 1878  O   VAL B1325     3782   2633   3003    422    171     12       O  
ATOM   1879  CB  VAL B1325      73.123  -1.055  48.036  1.00 24.35           C  
ANISOU 1879  CB  VAL B1325     3688   2493   3069    213    125    -45       C  
ATOM   1880  CG1 VAL B1325      71.930  -1.095  47.104  1.00 24.16           C  
ANISOU 1880  CG1 VAL B1325     3720   2397   3061    199     98    -70       C  
ATOM   1881  CG2 VAL B1325      72.727  -0.572  49.411  1.00 24.94           C  
ANISOU 1881  CG2 VAL B1325     3713   2580   3181    135    125    -52       C  
ATOM   1882  N   THR B1326      73.820  -3.691  46.010  1.00 26.67           N  
ANISOU 1882  N   THR B1326     4178   2706   3246    422    117    -45       N  
ATOM   1883  CA  THR B1326      74.317  -4.332  44.811  1.00 28.49           C  
ANISOU 1883  CA  THR B1326     4484   2922   3418    519    128    -48       C  
ATOM   1884  C   THR B1326      73.358  -4.125  43.650  1.00 28.14           C  
ANISOU 1884  C   THR B1326     4491   2826   3373    492     98    -85       C  
ATOM   1885  O   THR B1326      72.151  -3.989  43.839  1.00 27.35           O  
ANISOU 1885  O   THR B1326     4401   2675   3313    407     60   -109       O  
ATOM   1886  CB  THR B1326      74.428  -5.860  45.087  1.00 29.42           C  
ANISOU 1886  CB  THR B1326     4704   2972   3502    584    125    -52       C  
ATOM   1887  OG1 THR B1326      75.451  -6.087  46.056  1.00 31.87           O  
ANISOU 1887  OG1 THR B1326     4958   3349   3801    628    159     -4       O  
ATOM   1888  CG2 THR B1326      74.758  -6.644  43.882  1.00 31.12           C  
ANISOU 1888  CG2 THR B1326     5025   3146   3652    684    135    -68       C  
ATOM   1889  N   GLY B1327      73.894  -4.141  42.449  1.00 28.40           N  
ANISOU 1889  N   GLY B1327     4555   2881   3355    568    114    -84       N  
ATOM   1890  CA  GLY B1327      73.080  -4.148  41.246  1.00 28.67           C  
ANISOU 1890  CA  GLY B1327     4651   2872   3369    556     85   -118       C  
ATOM   1891  C   GLY B1327      72.497  -2.777  40.990  1.00 28.06           C  
ANISOU 1891  C   GLY B1327     4485   2835   3339    481     79   -108       C  
ATOM   1892  O   GLY B1327      71.355  -2.666  40.564  1.00 28.88           O  
ANISOU 1892  O   GLY B1327     4614   2901   3458    421     43   -130       O  
ATOM   1893  N   LEU B1328      73.268  -1.742  41.282  1.00 28.12           N  
ANISOU 1893  N   LEU B1328     4391   2921   3370    480    116    -69       N  
ATOM   1894  CA  LEU B1328      72.870  -0.363  41.023  1.00 28.42           C  
ANISOU 1894  CA  LEU B1328     4351   2993   3454    420    122    -53       C  
ATOM   1895  C   LEU B1328      73.376   0.103  39.636  1.00 28.97           C  
ANISOU 1895  C   LEU B1328     4408   3114   3482    480    141    -32       C  
ATOM   1896  O   LEU B1328      74.213  -0.539  39.018  1.00 33.63           O  
ANISOU 1896  O   LEU B1328     5037   3732   4008    571    157    -25       O  
ATOM   1897  CB  LEU B1328      73.410   0.559  42.104  1.00 27.45           C  
ANISOU 1897  CB  LEU B1328     4135   2917   3378    373    149    -26       C  
ATOM   1898  CG  LEU B1328      72.941   0.261  43.542  1.00 27.24           C  
ANISOU 1898  CG  LEU B1328     4104   2854   3389    312    135    -43       C  
ATOM   1899  CD1 LEU B1328      73.827   1.065  44.453  1.00 26.68           C  
ANISOU 1899  CD1 LEU B1328     3949   2848   3337    281    165    -17       C  
ATOM   1900  CD2 LEU B1328      71.460   0.526  43.775  1.00 27.17           C  
ANISOU 1900  CD2 LEU B1328     4106   2786   3429    237    106    -67       C  
ATOM   1901  N   GLU B1329      72.869   1.225  39.162  1.00 28.79           N  
ANISOU 1901  N   GLU B1329     4333   3109   3495    435    144    -16       N  
ATOM   1902  CA  GLU B1329      73.229   1.803  37.866  1.00 28.81           C  
ANISOU 1902  CA  GLU B1329     4313   3166   3466    481    162     12       C  
ATOM   1903  C   GLU B1329      74.204   2.997  38.087  1.00 26.82           C  
ANISOU 1903  C   GLU B1329     3961   2985   3244    471    205     66       C  
ATOM   1904  O   GLU B1329      73.980   3.809  38.970  1.00 25.61           O  
ANISOU 1904  O   GLU B1329     3758   2817   3154    395    213     72       O  
ATOM   1905  CB  GLU B1329      71.954   2.231  37.124  1.00 30.51           C  
ANISOU 1905  CB  GLU B1329     4536   3356   3698    438    137      4       C  
ATOM   1906  CG  GLU B1329      72.128   3.156  35.913  1.00 33.87           C  
ANISOU 1906  CG  GLU B1329     4914   3842   4112    465    158     46       C  
ATOM   1907  CD  GLU B1329      72.585   2.432  34.652  1.00 35.67           C  
ANISOU 1907  CD  GLU B1329     5197   4106   4249    555    154     39       C  
ATOM   1908  OE1 GLU B1329      73.209   1.350  34.764  1.00 40.34           O  
ANISOU 1908  OE1 GLU B1329     5854   4686   4786    615    153     12       O  
ATOM   1909  OE2 GLU B1329      72.326   2.929  33.539  1.00 37.21           O  
ANISOU 1909  OE2 GLU B1329     5374   4341   4422    571    156     62       O  
ATOM   1910  N   PRO B1330      75.284   3.105  37.289  1.00 25.31           N  
ANISOU 1910  N   PRO B1330     3743   2871   3003    543    232    106       N  
ATOM   1911  CA  PRO B1330      76.195   4.253  37.434  1.00 23.59           C  
ANISOU 1911  CA  PRO B1330     3428   2724   2811    519    268    165       C  
ATOM   1912  C   PRO B1330      75.519   5.606  37.246  1.00 21.89           C  
ANISOU 1912  C   PRO B1330     3165   2487   2662    444    275    183       C  
ATOM   1913  O   PRO B1330      74.623   5.742  36.423  1.00 21.66           O  
ANISOU 1913  O   PRO B1330     3160   2433   2636    449    263    175       O  
ATOM   1914  CB  PRO B1330      77.245   4.050  36.308  1.00 25.35           C  
ANISOU 1914  CB  PRO B1330     3636   3037   2959    621    292    211       C  
ATOM   1915  CG  PRO B1330      76.942   2.741  35.659  1.00 26.60           C  
ANISOU 1915  CG  PRO B1330     3895   3162   3047    707    273    166       C  
ATOM   1916  CD  PRO B1330      75.771   2.104  36.301  1.00 26.59           C  
ANISOU 1916  CD  PRO B1330     3968   3058   3076    653    234    100       C  
ATOM   1917  N   GLY B1331      76.021   6.604  37.936  1.00 20.18           N  
ANISOU 1917  N   GLY B1331     2884   2289   2493    379    298    212       N  
ATOM   1918  CA  GLY B1331      75.534   7.961  37.806  1.00 19.63           C  
ANISOU 1918  CA  GLY B1331     2777   2192   2487    313    316    236       C  
ATOM   1919  C   GLY B1331      74.107   8.208  38.247  1.00 18.85           C  
ANISOU 1919  C   GLY B1331     2712   2004   2445    261    304    197       C  
ATOM   1920  O   GLY B1331      73.550   9.259  37.896  1.00 18.78           O  
ANISOU 1920  O   GLY B1331     2683   1969   2483    231    324    222       O  
ATOM   1921  N   ILE B1332      73.499   7.303  39.010  1.00 17.71           N  
ANISOU 1921  N   ILE B1332     2616   1814   2298    252    275    145       N  
ATOM   1922  CA  ILE B1332      72.139   7.553  39.582  1.00 16.46           C  
ANISOU 1922  CA  ILE B1332     2478   1582   2193    200    265    116       C  
ATOM   1923  C   ILE B1332      72.122   7.901  41.076  1.00 15.46           C  
ANISOU 1923  C   ILE B1332     2343   1420   2111    130    275     91       C  
ATOM   1924  O   ILE B1332      72.769   7.272  41.928  1.00 16.10           O  
ANISOU 1924  O   ILE B1332     2427   1518   2171    123    266     71       O  
ATOM   1925  CB  ILE B1332      71.196   6.386  39.278  1.00 16.08           C  
ANISOU 1925  CB  ILE B1332     2488   1508   2112    227    222     83       C  
ATOM   1926  CG1 ILE B1332      71.137   6.182  37.769  1.00 17.62           C  
ANISOU 1926  CG1 ILE B1332     2696   1739   2258    286    213    103       C  
ATOM   1927  CG2 ILE B1332      69.796   6.572  39.895  1.00 15.29           C  
ANISOU 1927  CG2 ILE B1332     2399   1351   2060    174    210     67       C  
ATOM   1928  CD1 ILE B1332      70.010   5.348  37.308  1.00 18.53           C  
ANISOU 1928  CD1 ILE B1332     2865   1828   2345    289    169     76       C  
ATOM   1929  N   ASP B1333      71.336   8.900  41.428  1.00 15.51           N  
ANISOU 1929  N   ASP B1333     2340   1376   2174     83    298     94       N  
ATOM   1930  CA  ASP B1333      71.188   9.193  42.848  1.00 14.84           C  
ANISOU 1930  CA  ASP B1333     2259   1254   2124     21    308     62       C  
ATOM   1931  C   ASP B1333      70.206   8.203  43.419  1.00 14.06           C  
ANISOU 1931  C   ASP B1333     2193   1127   2019     24    274     28       C  
ATOM   1932  O   ASP B1333      69.108   8.054  42.905  1.00 13.70           O  
ANISOU 1932  O   ASP B1333     2163   1061   1982     40    261     35       O  
ATOM   1933  CB  ASP B1333      70.593  10.579  43.087  1.00 15.32           C  
ANISOU 1933  CB  ASP B1333     2314   1261   2246    -20    350     73       C  
ATOM   1934  CG  ASP B1333      71.494  11.645  42.743  1.00 16.19           C  
ANISOU 1934  CG  ASP B1333     2399   1381   2371    -44    384    105       C  
ATOM   1935  OD1 ASP B1333      72.692  11.428  42.432  1.00 17.71           O  
ANISOU 1935  OD1 ASP B1333     2564   1637   2527    -39    377    124       O  
ATOM   1936  OD2 ASP B1333      70.953  12.790  42.705  1.00 17.08           O  
ANISOU 1936  OD2 ASP B1333     2518   1437   2533    -66    424    121       O  
ATOM   1937  N   TYR B1334      70.638   7.558  44.507  1.00 14.03           N  
ANISOU 1937  N   TYR B1334     2196   1132   2000      3    260     -1       N  
ATOM   1938  CA  TYR B1334      69.765   6.718  45.287  1.00 13.89           C  
ANISOU 1938  CA  TYR B1334     2205   1087   1984     -6    232    -29       C  
ATOM   1939  C   TYR B1334      69.513   7.275  46.658  1.00 13.65           C  
ANISOU 1939  C   TYR B1334     2165   1033   1986    -63    252    -51       C  
ATOM   1940  O   TYR B1334      70.462   7.647  47.344  1.00 14.41           O  
ANISOU 1940  O   TYR B1334     2242   1154   2077    -96    269    -61       O  
ATOM   1941  CB  TYR B1334      70.370   5.315  45.413  1.00 13.72           C  
ANISOU 1941  CB  TYR B1334     2207   1091   1912     27    199    -41       C  
ATOM   1942  CG  TYR B1334      70.501   4.579  44.085  1.00 13.91           C  
ANISOU 1942  CG  TYR B1334     2262   1127   1893     90    177    -29       C  
ATOM   1943  CD1 TYR B1334      69.430   4.025  43.462  1.00 14.21           C  
ANISOU 1943  CD1 TYR B1334     2339   1134   1924    100    146    -35       C  
ATOM   1944  CD2 TYR B1334      71.746   4.434  43.446  1.00 14.71           C  
ANISOU 1944  CD2 TYR B1334     2354   1281   1953    141    189    -10       C  
ATOM   1945  CE1 TYR B1334      69.546   3.452  42.209  1.00 14.44           C  
ANISOU 1945  CE1 TYR B1334     2404   1175   1907    152    128    -31       C  
ATOM   1946  CE2 TYR B1334      71.884   3.822  42.233  1.00 15.29           C  
ANISOU 1946  CE2 TYR B1334     2462   1367   1980    206    176     -3       C  
ATOM   1947  CZ  TYR B1334      70.801   3.293  41.606  1.00 15.02           C  
ANISOU 1947  CZ  TYR B1334     2477   1293   1937    211    144    -19       C  
ATOM   1948  OH  TYR B1334      70.943   2.658  40.394  1.00 15.47           O  
ANISOU 1948  OH  TYR B1334     2578   1361   1937    272    129    -21       O  
ATOM   1949  N   ASP B1335      68.260   7.310  47.071  1.00 13.68           N  
ANISOU 1949  N   ASP B1335     2179   1000   2015    -76    250    -57       N  
ATOM   1950  CA  ASP B1335      67.920   7.680  48.449  1.00 14.14           C  
ANISOU 1950  CA  ASP B1335     2235   1040   2095   -120    268    -82       C  
ATOM   1951  C   ASP B1335      67.926   6.361  49.234  1.00 13.84           C  
ANISOU 1951  C   ASP B1335     2206   1023   2029   -121    229    -99       C  
ATOM   1952  O   ASP B1335      67.066   5.435  48.982  1.00 13.76           O  
ANISOU 1952  O   ASP B1335     2213   1002   2011   -104    193    -89       O  
ATOM   1953  CB  ASP B1335      66.578   8.349  48.563  1.00 15.06           C  
ANISOU 1953  CB  ASP B1335     2354   1118   2249   -120    292    -71       C  
ATOM   1954  CG  ASP B1335      66.507   9.655  47.797  1.00 15.49           C  
ANISOU 1954  CG  ASP B1335     2405   1144   2336   -110    338    -46       C  
ATOM   1955  OD1 ASP B1335      67.610  10.229  47.573  1.00 16.55           O  
ANISOU 1955  OD1 ASP B1335     2535   1283   2468   -126    357    -50       O  
ATOM   1956  OD2 ASP B1335      65.409   9.974  47.287  1.00 15.86           O  
ANISOU 1956  OD2 ASP B1335     2447   1175   2403    -83    350    -14       O  
ATOM   1957  N   ILE B1336      68.847   6.272  50.177  1.00 14.08           N  
ANISOU 1957  N   ILE B1336     2224   1084   2041   -148    233   -118       N  
ATOM   1958  CA  ILE B1336      69.065   5.004  50.899  1.00 13.86           C  
ANISOU 1958  CA  ILE B1336     2199   1082   1983   -142    200   -123       C  
ATOM   1959  C   ILE B1336      68.662   5.247  52.338  1.00 14.32           C  
ANISOU 1959  C   ILE B1336     2246   1143   2051   -187    212   -145       C  
ATOM   1960  O   ILE B1336      69.169   6.167  53.007  1.00 14.94           O  
ANISOU 1960  O   ILE B1336     2310   1235   2130   -229    243   -165       O  
ATOM   1961  CB  ILE B1336      70.535   4.591  50.851  1.00 14.24           C  
ANISOU 1961  CB  ILE B1336     2232   1186   1991   -125    197   -115       C  
ATOM   1962  CG1 ILE B1336      70.938   4.277  49.433  1.00 14.82           C  
ANISOU 1962  CG1 ILE B1336     2320   1262   2046    -68    189    -93       C  
ATOM   1963  CG2 ILE B1336      70.728   3.368  51.754  1.00 14.23           C  
ANISOU 1963  CG2 ILE B1336     2233   1210   1961   -116    173   -115       C  
ATOM   1964  CD1 ILE B1336      72.407   4.322  49.185  1.00 15.46           C  
ANISOU 1964  CD1 ILE B1336     2373   1409   2092    -49    201    -72       C  
ATOM   1965  N   SER B1337      67.708   4.477  52.794  1.00 14.00           N  
ANISOU 1965  N   SER B1337     2215   1089   2014   -183    189   -140       N  
ATOM   1966  CA  SER B1337      67.164   4.567  54.138  1.00 14.31           C  
ANISOU 1966  CA  SER B1337     2241   1137   2057   -215    198   -154       C  
ATOM   1967  C   SER B1337      67.543   3.339  54.948  1.00 14.65           C  
ANISOU 1967  C   SER B1337     2278   1217   2071   -214    167   -148       C  
ATOM   1968  O   SER B1337      67.463   2.212  54.459  1.00 14.17           O  
ANISOU 1968  O   SER B1337     2237   1144   2000   -185    132   -127       O  
ATOM   1969  CB  SER B1337      65.619   4.728  54.125  1.00 14.90           C  
ANISOU 1969  CB  SER B1337     2319   1179   2161   -211    200   -138       C  
ATOM   1970  OG  SER B1337      65.211   5.882  53.404  1.00 16.75           O  
ANISOU 1970  OG  SER B1337     2558   1382   2423   -202    235   -134       O  
ATOM   1971  N   VAL B1338      67.890   3.552  56.233  1.00 15.00           N  
ANISOU 1971  N   VAL B1338     2297   1302   2099   -248    182   -165       N  
ATOM   1972  CA  VAL B1338      68.085   2.432  57.152  1.00 15.80           C  
ANISOU 1972  CA  VAL B1338     2385   1444   2174   -247    158   -150       C  
ATOM   1973  C   VAL B1338      67.172   2.742  58.329  1.00 16.40           C  
ANISOU 1973  C   VAL B1338     2445   1529   2256   -277    171   -161       C  
ATOM   1974  O   VAL B1338      67.122   3.879  58.817  1.00 15.79           O  
ANISOU 1974  O   VAL B1338     2363   1455   2180   -307    207   -193       O  
ATOM   1975  CB  VAL B1338      69.530   2.188  57.555  1.00 16.58           C  
ANISOU 1975  CB  VAL B1338     2457   1609   2232   -249    160   -147       C  
ATOM   1976  CG1 VAL B1338      69.589   0.880  58.349  1.00 17.39           C  
ANISOU 1976  CG1 VAL B1338     2550   1744   2312   -231    135   -118       C  
ATOM   1977  CG2 VAL B1338      70.371   2.093  56.332  1.00 16.60           C  
ANISOU 1977  CG2 VAL B1338     2471   1607   2226   -212    157   -133       C  
ATOM   1978  N   ILE B1339      66.340   1.767  58.697  1.00 16.46           N  
ANISOU 1978  N   ILE B1339     2452   1532   2268   -268    143   -131       N  
ATOM   1979  CA  ILE B1339      65.250   1.948  59.657  1.00 17.06           C  
ANISOU 1979  CA  ILE B1339     2509   1620   2350   -285    153   -126       C  
ATOM   1980  C   ILE B1339      65.515   0.982  60.785  1.00 17.71           C  
ANISOU 1980  C   ILE B1339     2566   1756   2405   -293    135   -107       C  
ATOM   1981  O   ILE B1339      65.770  -0.213  60.548  1.00 18.46           O  
ANISOU 1981  O   ILE B1339     2672   1844   2496   -275    100    -74       O  
ATOM   1982  CB  ILE B1339      63.881   1.634  59.020  1.00 16.86           C  
ANISOU 1982  CB  ILE B1339     2495   1555   2356   -273    133    -90       C  
ATOM   1983  CG1 ILE B1339      63.703   2.570  57.776  1.00 17.53           C  
ANISOU 1983  CG1 ILE B1339     2600   1594   2465   -258    152   -101       C  
ATOM   1984  CG2 ILE B1339      62.741   1.770  60.038  1.00 17.29           C  
ANISOU 1984  CG2 ILE B1339     2519   1637   2412   -284    145    -71       C  
ATOM   1985  CD1 ILE B1339      62.341   2.640  57.229  1.00 18.90           C  
ANISOU 1985  CD1 ILE B1339     2770   1747   2663   -250    144    -65       C  
ATOM   1986  N   THR B1340      65.436   1.473  62.018  1.00 18.29           N  
ANISOU 1986  N   THR B1340     2612   1880   2457   -317    159   -125       N  
ATOM   1987  CA  THR B1340      65.619   0.656  63.215  1.00 19.44           C  
ANISOU 1987  CA  THR B1340     2723   2091   2572   -326    146   -102       C  
ATOM   1988  C   THR B1340      64.316  -0.068  63.480  1.00 18.99           C  
ANISOU 1988  C   THR B1340     2657   2022   2533   -319    125    -54       C  
ATOM   1989  O   THR B1340      63.250   0.499  63.377  1.00 19.44           O  
ANISOU 1989  O   THR B1340     2714   2059   2610   -318    139    -52       O  
ATOM   1990  CB  THR B1340      65.964   1.580  64.395  1.00 20.53           C  
ANISOU 1990  CB  THR B1340     2837   2291   2670   -360    182   -145       C  
ATOM   1991  OG1 THR B1340      67.050   2.429  64.027  1.00 20.89           O  
ANISOU 1991  OG1 THR B1340     2894   2339   2701   -383    200   -189       O  
ATOM   1992  CG2 THR B1340      66.340   0.811  65.693  1.00 21.16           C  
ANISOU 1992  CG2 THR B1340     2872   2460   2707   -371    170   -121       C  
ATOM   1993  N   LEU B1341      64.413  -1.376  63.721  1.00 18.34           N  
ANISOU 1993  N   LEU B1341     2569   1950   2447   -312     89     -7       N  
ATOM   1994  CA  LEU B1341      63.234  -2.189  63.980  1.00 18.57           C  
ANISOU 1994  CA  LEU B1341     2589   1970   2494   -318     61     47       C  
ATOM   1995  C   LEU B1341      63.173  -2.652  65.408  1.00 19.52           C  
ANISOU 1995  C   LEU B1341     2662   2166   2586   -327     64     77       C  
ATOM   1996  O   LEU B1341      64.194  -3.049  65.938  1.00 20.61           O  
ANISOU 1996  O   LEU B1341     2786   2348   2696   -321     65     78       O  
ATOM   1997  CB  LEU B1341      63.237  -3.378  63.060  1.00 18.17           C  
ANISOU 1997  CB  LEU B1341     2584   1854   2464   -309     16     83       C  
ATOM   1998  CG  LEU B1341      63.379  -3.135  61.554  1.00 18.50           C  
ANISOU 1998  CG  LEU B1341     2678   1825   2526   -295      8     57       C  
ATOM   1999  CD1 LEU B1341      63.646  -4.442  60.819  1.00 19.06           C  
ANISOU 1999  CD1 LEU B1341     2807   1834   2600   -281    -32     83       C  
ATOM   2000  CD2 LEU B1341      62.160  -2.390  60.997  1.00 18.30           C  
ANISOU 2000  CD2 LEU B1341     2648   1780   2525   -311     10     59       C  
ATOM   2001  N   ILE B1342      61.968  -2.626  66.015  1.00 20.18           N  
ANISOU 2001  N   ILE B1342     2714   2277   2675   -338     65    111       N  
ATOM   2002  CA  ILE B1342      61.671  -3.334  67.269  1.00 21.99           C  
ANISOU 2002  CA  ILE B1342     2895   2575   2882   -346     57    162       C  
ATOM   2003  C   ILE B1342      60.451  -4.202  67.007  1.00 23.19           C  
ANISOU 2003  C   ILE B1342     3045   2697   3066   -362     17    236       C  
ATOM   2004  O   ILE B1342      59.843  -4.047  65.968  1.00 23.04           O  
ANISOU 2004  O   ILE B1342     3056   2620   3078   -369      2    237       O  
ATOM   2005  CB  ILE B1342      61.345  -2.363  68.407  1.00 22.03           C  
ANISOU 2005  CB  ILE B1342     2858   2661   2852   -346    102    136       C  
ATOM   2006  CG1 ILE B1342      60.101  -1.526  68.090  1.00 22.17           C  
ANISOU 2006  CG1 ILE B1342     2874   2660   2887   -337    124    136       C  
ATOM   2007  CG2 ILE B1342      62.568  -1.540  68.658  1.00 21.48           C  
ANISOU 2007  CG2 ILE B1342     2797   2619   2746   -350    133     63       C  
ATOM   2008  CD1 ILE B1342      59.408  -0.974  69.319  1.00 23.03           C  
ANISOU 2008  CD1 ILE B1342     2939   2851   2960   -326    164    142       C  
ATOM   2009  N   ASN B1343      60.112  -5.139  67.901  1.00 24.28           N  
ANISOU 2009  N   ASN B1343     3148   2878   3197   -375     -2    302       N  
ATOM   2010  CA  ASN B1343      58.909  -5.907  67.709  1.00 25.42           C  
ANISOU 2010  CA  ASN B1343     3286   3003   3369   -405    -42    377       C  
ATOM   2011  C   ASN B1343      57.699  -5.002  67.606  1.00 24.74           C  
ANISOU 2011  C   ASN B1343     3166   2947   3287   -407    -24    386       C  
ATOM   2012  O   ASN B1343      57.421  -4.224  68.513  1.00 23.84           O  
ANISOU 2012  O   ASN B1343     3004   2909   3144   -386     19    377       O  
ATOM   2013  CB  ASN B1343      58.758  -6.951  68.787  1.00 27.23           C  
ANISOU 2013  CB  ASN B1343     3475   3281   3587   -418    -61    452       C  
ATOM   2014  CG  ASN B1343      57.773  -8.027  68.414  1.00 29.32           C  
ANISOU 2014  CG  ASN B1343     3753   3499   3884   -465   -116    534       C  
ATOM   2015  OD1 ASN B1343      58.003  -8.800  67.476  1.00 30.58           O  
ANISOU 2015  OD1 ASN B1343     3986   3562   4071   -483   -155    536       O  
ATOM   2016  ND2 ASN B1343      56.670  -8.076  69.117  1.00 31.30           N  
ANISOU 2016  ND2 ASN B1343     3938   3820   4131   -487   -121    603       N  
ATOM   2017  N   GLY B1344      57.063  -5.027  66.429  1.00 25.15           N  
ANISOU 2017  N   GLY B1344     3248   2937   3369   -427    -52    399       N  
ATOM   2018  CA  GLY B1344      55.838  -4.272  66.175  1.00 25.02           C  
ANISOU 2018  CA  GLY B1344     3195   2953   3358   -426    -38    427       C  
ATOM   2019  C   GLY B1344      55.992  -2.766  65.991  1.00 23.54           C  
ANISOU 2019  C   GLY B1344     3010   2772   3161   -378     24    359       C  
ATOM   2020  O   GLY B1344      54.996  -2.041  65.957  1.00 24.20           O  
ANISOU 2020  O   GLY B1344     3059   2892   3243   -359     52    387       O  
ATOM   2021  N   GLY B1345      57.216  -2.314  65.769  1.00 22.04           N  
ANISOU 2021  N   GLY B1345     2865   2542   2966   -360     47    278       N  
ATOM   2022  CA  GLY B1345      57.499  -0.877  65.654  1.00 20.62           C  
ANISOU 2022  CA  GLY B1345     2698   2356   2777   -324    108    208       C  
ATOM   2023  C   GLY B1345      58.775  -0.653  64.855  1.00 20.05           C  
ANISOU 2023  C   GLY B1345     2683   2222   2713   -323    107    139       C  
ATOM   2024  O   GLY B1345      59.512  -1.600  64.584  1.00 20.80           O  
ANISOU 2024  O   GLY B1345     2801   2290   2812   -339     68    143       O  
ATOM   2025  N   GLU B1346      59.038   0.618  64.516  1.00 18.93           N  
ANISOU 2025  N   GLU B1346     2563   2057   2571   -301    155     81       N  
ATOM   2026  CA  GLU B1346      60.234   0.986  63.832  1.00 18.58           C  
ANISOU 2026  CA  GLU B1346     2562   1966   2530   -303    160     21       C  
ATOM   2027  C   GLU B1346      60.448   2.482  63.940  1.00 18.06           C  
ANISOU 2027  C   GLU B1346     2514   1889   2456   -288    223    -39       C  
ATOM   2028  O   GLU B1346      59.498   3.204  64.335  1.00 19.33           O  
ANISOU 2028  O   GLU B1346     2664   2065   2614   -264    264    -30       O  
ATOM   2029  CB  GLU B1346      60.107   0.585  62.368  1.00 18.13           C  
ANISOU 2029  CB  GLU B1346     2535   1846   2506   -303    123     41       C  
ATOM   2030  CG  GLU B1346      59.047   1.335  61.593  1.00 19.59           C  
ANISOU 2030  CG  GLU B1346     2718   2011   2715   -286    141     62       C  
ATOM   2031  CD  GLU B1346      58.893   0.788  60.197  1.00 20.06           C  
ANISOU 2031  CD  GLU B1346     2804   2022   2796   -295     95     85       C  
ATOM   2032  OE1 GLU B1346      58.934   1.569  59.205  1.00 20.76           O  
ANISOU 2032  OE1 GLU B1346     2911   2077   2900   -277    115     67       O  
ATOM   2033  OE2 GLU B1346      58.688  -0.468  60.057  1.00 21.59           O  
ANISOU 2033  OE2 GLU B1346     3004   2210   2990   -324     38    124       O  
ATOM   2034  N   SER B1347      61.684   2.882  63.670  1.00 18.09           N  
ANISOU 2034  N   SER B1347     2548   1873   2452   -301    231    -94       N  
ATOM   2035  CA  SER B1347      62.079   4.295  63.688  1.00 17.58           C  
ANISOU 2035  CA  SER B1347     2514   1782   2380   -303    286   -157       C  
ATOM   2036  C   SER B1347      61.530   5.015  62.498  1.00 17.81           C  
ANISOU 2036  C   SER B1347     2569   1746   2449   -276    306   -150       C  
ATOM   2037  O   SER B1347      61.273   4.431  61.461  1.00 17.17           O  
ANISOU 2037  O   SER B1347     2486   1640   2395   -266    270   -111       O  
ATOM   2038  CB  SER B1347      63.612   4.431  63.713  1.00 17.23           C  
ANISOU 2038  CB  SER B1347     2484   1748   2312   -338    281   -206       C  
ATOM   2039  OG  SER B1347      64.254   4.033  62.514  1.00 16.34           O  
ANISOU 2039  OG  SER B1347     2383   1600   2222   -334    250   -193       O  
ATOM   2040  N   ALA B1348      61.633   6.350  62.567  1.00 18.63           N  
ANISOU 2040  N   ALA B1348     2708   1816   2552   -270    364   -198       N  
ATOM   2041  CA  ALA B1348      61.684   7.129  61.363  1.00 19.13           C  
ANISOU 2041  CA  ALA B1348     2803   1813   2650   -254    384   -202       C  
ATOM   2042  C   ALA B1348      62.947   6.754  60.557  1.00 19.15           C  
ANISOU 2042  C   ALA B1348     2813   1804   2656   -283    346   -217       C  
ATOM   2043  O   ALA B1348      63.949   6.261  61.113  1.00 20.56           O  
ANISOU 2043  O   ALA B1348     2982   2025   2805   -317    323   -239       O  
ATOM   2044  CB  ALA B1348      61.700   8.643  61.673  1.00 19.75           C  
ANISOU 2044  CB  ALA B1348     2932   1846   2727   -248    458   -254       C  
ATOM   2045  N   PRO B1349      62.898   6.916  59.240  1.00 18.87           N  
ANISOU 2045  N   PRO B1349     2789   1727   2654   -263    340   -196       N  
ATOM   2046  CA  PRO B1349      64.084   6.427  58.481  1.00 18.72           C  
ANISOU 2046  CA  PRO B1349     2773   1709   2631   -279    304   -202       C  
ATOM   2047  C   PRO B1349      65.220   7.416  58.596  1.00 18.87           C  
ANISOU 2047  C   PRO B1349     2813   1717   2637   -314    335   -252       C  
ATOM   2048  O   PRO B1349      64.956   8.635  58.748  1.00 18.11           O  
ANISOU 2048  O   PRO B1349     2747   1580   2553   -319    387   -279       O  
ATOM   2049  CB  PRO B1349      63.579   6.441  57.049  1.00 18.53           C  
ANISOU 2049  CB  PRO B1349     2755   1645   2637   -246    293   -166       C  
ATOM   2050  CG  PRO B1349      62.611   7.628  57.069  1.00 18.99           C  
ANISOU 2050  CG  PRO B1349     2824   1670   2720   -223    350   -161       C  
ATOM   2051  CD  PRO B1349      61.845   7.387  58.327  1.00 18.64           C  
ANISOU 2051  CD  PRO B1349     2762   1660   2658   -222    359   -157       C  
ATOM   2052  N   THR B1350      66.421   6.891  58.657  1.00 18.50           N  
ANISOU 2052  N   THR B1350     2751   1712   2564   -340    307   -260       N  
ATOM   2053  CA  THR B1350      67.643   7.683  58.461  1.00 19.35           C  
ANISOU 2053  CA  THR B1350     2869   1824   2660   -381    323   -289       C  
ATOM   2054  C   THR B1350      67.843   7.528  56.961  1.00 19.88           C  
ANISOU 2054  C   THR B1350     2937   1862   2751   -345    308   -256       C  
ATOM   2055  O   THR B1350      68.082   6.390  56.467  1.00 19.57           O  
ANISOU 2055  O   THR B1350     2883   1849   2703   -314    267   -225       O  
ATOM   2056  CB  THR B1350      68.868   7.162  59.220  1.00 19.58           C  
ANISOU 2056  CB  THR B1350     2866   1933   2639   -421    299   -298       C  
ATOM   2057  OG1 THR B1350      68.647   7.184  60.646  1.00 21.30           O  
ANISOU 2057  OG1 THR B1350     3077   2190   2825   -454    308   -326       O  
ATOM   2058  CG2 THR B1350      70.083   7.986  58.871  1.00 20.71           C  
ANISOU 2058  CG2 THR B1350     3010   2089   2769   -470    311   -314       C  
ATOM   2059  N   THR B1351      67.685   8.616  56.244  1.00 20.74           N  
ANISOU 2059  N   THR B1351     3071   1917   2890   -343    342   -261       N  
ATOM   2060  CA  THR B1351      67.810   8.630  54.750  1.00 20.95           C  
ANISOU 2060  CA  THR B1351     3098   1920   2939   -307    334   -227       C  
ATOM   2061  C   THR B1351      68.860   9.596  54.262  1.00 21.98           C  
ANISOU 2061  C   THR B1351     3235   2044   3072   -340    357   -236       C  
ATOM   2062  O   THR B1351      68.886  10.784  54.631  1.00 22.22           O  
ANISOU 2062  O   THR B1351     3293   2033   3115   -380    399   -264       O  
ATOM   2063  CB  THR B1351      66.448   8.936  54.102  1.00 21.26           C  
ANISOU 2063  CB  THR B1351     3151   1909   3017   -262    351   -201       C  
ATOM   2064  OG1 THR B1351      65.428   8.127  54.706  1.00 22.02           O  
ANISOU 2064  OG1 THR B1351     3236   2020   3109   -245    331   -188       O  
ATOM   2065  CG2 THR B1351      66.484   8.751  52.573  1.00 21.98           C  
ANISOU 2065  CG2 THR B1351     3238   1991   3121   -224    334   -163       C  
ATOM   2066  N   LEU B1352      69.717   9.104  53.380  1.00 20.96           N  
ANISOU 2066  N   LEU B1352     3084   1950   2928   -323    331   -208       N  
ATOM   2067  CA  LEU B1352      70.737   9.934  52.795  1.00 21.22           C  
ANISOU 2067  CA  LEU B1352     3111   1989   2961   -353    348   -201       C  
ATOM   2068  C   LEU B1352      70.743   9.614  51.336  1.00 21.46           C  
ANISOU 2068  C   LEU B1352     3133   2018   3001   -292    336   -159       C  
ATOM   2069  O   LEU B1352      70.365   8.502  50.934  1.00 19.55           O  
ANISOU 2069  O   LEU B1352     2889   1790   2746   -239    303   -142       O  
ATOM   2070  CB  LEU B1352      72.095   9.668  53.429  1.00 22.32           C  
ANISOU 2070  CB  LEU B1352     3217   2211   3053   -402    331   -205       C  
ATOM   2071  CG  LEU B1352      72.196  10.166  54.872  1.00 23.29           C  
ANISOU 2071  CG  LEU B1352     3348   2341   3157   -478    344   -252       C  
ATOM   2072  CD1 LEU B1352      73.513   9.741  55.524  1.00 23.16           C  
ANISOU 2072  CD1 LEU B1352     3284   2430   3083   -526    319   -245       C  
ATOM   2073  CD2 LEU B1352      72.072  11.687  54.913  1.00 25.13           C  
ANISOU 2073  CD2 LEU B1352     3627   2502   3418   -535    389   -282       C  
ATOM   2074  N   THR B1353      71.162  10.572  50.544  1.00 19.64           N  
ANISOU 2074  N   THR B1353     2903   1770   2789   -304    361   -141       N  
ATOM   2075  CA  THR B1353      71.306  10.342  49.083  1.00 20.31           C  
ANISOU 2075  CA  THR B1353     2974   1866   2874   -246    351    -97       C  
ATOM   2076  C   THR B1353      72.765  10.240  48.672  1.00 21.02           C  
ANISOU 2076  C   THR B1353     3029   2029   2928   -255    341    -70       C  
ATOM   2077  O   THR B1353      73.566  11.089  49.024  1.00 21.68           O  
ANISOU 2077  O   THR B1353     3099   2127   3011   -320    359    -71       O  
ATOM   2078  CB  THR B1353      70.645  11.475  48.320  1.00 20.04           C  
ANISOU 2078  CB  THR B1353     2958   1769   2887   -237    390    -78       C  
ATOM   2079  OG1 THR B1353      69.318  11.691  48.811  1.00 21.03           O  
ANISOU 2079  OG1 THR B1353     3110   1837   3041   -227    408    -94       O  
ATOM   2080  CG2 THR B1353      70.634  11.155  46.837  1.00 20.16           C  
ANISOU 2080  CG2 THR B1353     2958   1805   2896   -174    376    -33       C  
ATOM   2081  N   GLN B1354      73.103   9.221  47.862  1.00 19.88           N  
ANISOU 2081  N   GLN B1354     2870   1931   2750   -187    314    -43       N  
ATOM   2082  CA  GLN B1354      74.413   8.958  47.315  1.00 20.80           C  
ANISOU 2082  CA  GLN B1354     2949   2128   2824   -167    308     -5       C  
ATOM   2083  C   GLN B1354      74.256   8.597  45.836  1.00 20.06           C  
ANISOU 2083  C   GLN B1354     2862   2038   2721    -86    302     26       C  
ATOM   2084  O   GLN B1354      73.395   7.760  45.475  1.00 18.97           O  
ANISOU 2084  O   GLN B1354     2760   1869   2579    -34    281     13       O  
ATOM   2085  CB  GLN B1354      75.011   7.813  48.075  1.00 19.63           C  
ANISOU 2085  CB  GLN B1354     2787   2042   2629   -151    283     -9       C  
ATOM   2086  CG  GLN B1354      76.342   7.332  47.557  1.00 20.95           C  
ANISOU 2086  CG  GLN B1354     2911   2304   2742   -107    280     39       C  
ATOM   2087  CD  GLN B1354      77.335   8.464  47.562  1.00 22.34           C  
ANISOU 2087  CD  GLN B1354     3037   2533   2916   -178    299     70       C  
ATOM   2088  OE1 GLN B1354      77.676   8.984  48.620  1.00 24.51           O  
ANISOU 2088  OE1 GLN B1354     3293   2827   3191   -265    302     54       O  
ATOM   2089  NE2 GLN B1354      77.795   8.830  46.422  1.00 23.72           N  
ANISOU 2089  NE2 GLN B1354     3191   2735   3085   -146    311    114       N  
ATOM   2090  N   GLN B1355      75.091   9.220  44.981  1.00 21.93           N  
ANISOU 2090  N   GLN B1355     3066   2318   2949    -81    319     71       N  
ATOM   2091  CA  GLN B1355      75.188   8.819  43.594  1.00 22.99           C  
ANISOU 2091  CA  GLN B1355     3199   2478   3056      0    315    105       C  
ATOM   2092  C   GLN B1355      76.189   7.723  43.378  1.00 24.61           C  
ANISOU 2092  C   GLN B1355     3390   2765   3195     67    300    126       C  
ATOM   2093  O   GLN B1355      77.244   7.713  44.018  1.00 25.80           O  
ANISOU 2093  O   GLN B1355     3498   2984   3319     41    305    146       O  
ATOM   2094  CB  GLN B1355      75.570  10.021  42.723  1.00 23.49           C  
ANISOU 2094  CB  GLN B1355     3229   2553   3141    -16    344    152       C  
ATOM   2095  CG  GLN B1355      75.265   9.820  41.243  1.00 24.15           C  
ANISOU 2095  CG  GLN B1355     3319   2648   3207     64    343    182       C  
ATOM   2096  CD  GLN B1355      75.480  11.097  40.398  1.00 25.18           C  
ANISOU 2096  CD  GLN B1355     3416   2783   3368     45    375    236       C  
ATOM   2097  OE1 GLN B1355      76.464  11.207  39.657  1.00 26.00           O  
ANISOU 2097  OE1 GLN B1355     3477   2963   3438     72    383    288       O  
ATOM   2098  NE2 GLN B1355      74.535  12.017  40.461  1.00 24.18           N  
ANISOU 2098  NE2 GLN B1355     3308   2577   3302      8    396    229       N  
ATOM   2099  N   THR B1356      75.853   6.771  42.517  1.00 24.30           N  
ANISOU 2099  N   THR B1356     3389   2721   3122    152    284    123       N  
ATOM   2100  CA  THR B1356      76.870   5.819  42.026  1.00 24.62           C  
ANISOU 2100  CA  THR B1356     3424   2836   3092    239    283    152       C  
ATOM   2101  C   THR B1356      77.880   6.488  41.066  1.00 25.10           C  
ANISOU 2101  C   THR B1356     3428   2980   3127    266    308    216       C  
ATOM   2102  O   THR B1356      77.658   7.557  40.528  1.00 24.68           O  
ANISOU 2102  O   THR B1356     3352   2914   3110    229    323    236       O  
ATOM   2103  CB  THR B1356      76.229   4.601  41.347  1.00 24.74           C  
ANISOU 2103  CB  THR B1356     3516   2811   3072    321    261    122       C  
ATOM   2104  OG1 THR B1356      75.098   5.013  40.564  1.00 24.61           O  
ANISOU 2104  OG1 THR B1356     3527   2737   3084    309    251    106       O  
ATOM   2105  CG2 THR B1356      75.796   3.585  42.439  1.00 24.28           C  
ANISOU 2105  CG2 THR B1356     3503   2706   3015    312    237     80       C  
ATOM   2106  N   ALA B1357      78.994   5.806  40.864  1.00 26.61           N  
ANISOU 2106  N   ALA B1357     3595   3260   3253    338    317    255       N  
ATOM   2107  CA  ALA B1357      80.082   6.308  40.077  1.00 27.85           C  
ANISOU 2107  CA  ALA B1357     3687   3519   3376    369    341    328       C  
ATOM   2108  C   ALA B1357      79.756   6.299  38.583  1.00 28.59           C  
ANISOU 2108  C   ALA B1357     3806   3608   3447    446    347    340       C  
ATOM   2109  O   ALA B1357      78.861   5.569  38.178  1.00 27.30           O  
ANISOU 2109  O   ALA B1357     3720   3378   3274    492    329    290       O  
ATOM   2110  CB  ALA B1357      81.314   5.481  40.373  1.00 28.42           C  
ANISOU 2110  CB  ALA B1357     3724   3696   3377    437    352    373       C  
TER    2111      ALA B1357                                                      
ATOM   2112  N   THR C   4      38.176  13.427  21.600  1.00 29.92           N  
ANISOU 2112  N   THR C   4     4285   3175   3908     11    263   -233       N  
ATOM   2113  CA  THR C   4      39.617  13.073  21.559  1.00 27.92           C  
ANISOU 2113  CA  THR C   4     4021   2928   3658    -20    258   -238       C  
ATOM   2114  C   THR C   4      39.822  11.649  21.022  1.00 25.58           C  
ANISOU 2114  C   THR C   4     3704   2649   3363    -14    233   -205       C  
ATOM   2115  O   THR C   4      39.441  10.674  21.644  1.00 25.41           O  
ANISOU 2115  O   THR C   4     3662   2661   3329    -11    214   -190       O  
ATOM   2116  CB  THR C   4      40.230  13.204  22.957  1.00 29.38           C  
ANISOU 2116  CB  THR C   4     4184   3151   3825    -48    257   -266       C  
ATOM   2117  OG1 THR C   4      39.909  14.514  23.450  1.00 30.86           O  
ANISOU 2117  OG1 THR C   4     4395   3319   4009    -53    283   -298       O  
ATOM   2118  CG2 THR C   4      41.716  13.011  22.909  1.00 29.83           C  
ANISOU 2118  CG2 THR C   4     4228   3225   3880    -78    255   -276       C  
ATOM   2119  N   SER C   5      40.470  11.544  19.877  1.00 24.04           N  
ANISOU 2119  N   SER C   5     3520   2430   3183    -15    234   -196       N  
ATOM   2120  CA  SER C   5      40.452  10.282  19.163  1.00 22.85           C  
ANISOU 2120  CA  SER C   5     3359   2284   3036     -3    214   -165       C  
ATOM   2121  C   SER C   5      41.405   9.272  19.785  1.00 21.14           C  
ANISOU 2121  C   SER C   5     3118   2104   2807    -15    195   -161       C  
ATOM   2122  O   SER C   5      42.575   9.569  20.019  1.00 21.83           O  
ANISOU 2122  O   SER C   5     3196   2205   2891    -33    199   -180       O  
ATOM   2123  CB  SER C   5      40.840  10.526  17.730  1.00 22.58           C  
ANISOU 2123  CB  SER C   5     3342   2215   3020      0    222   -157       C  
ATOM   2124  OG  SER C   5      40.820   9.332  17.032  1.00 23.99           O  
ANISOU 2124  OG  SER C   5     3513   2398   3202     11    205   -131       O  
ATOM   2125  N   ASP C   6      40.932   8.050  19.955  1.00 20.18           N  
ANISOU 2125  N   ASP C   6     2989   1998   2678     -3    177   -135       N  
ATOM   2126  CA  ASP C   6      41.776   6.976  20.388  1.00 19.74           C  
ANISOU 2126  CA  ASP C   6     2919   1969   2609     -3    159   -124       C  
ATOM   2127  C   ASP C   6      42.302   6.116  19.208  1.00 18.26           C  
ANISOU 2127  C   ASP C   6     2740   1765   2433      9    150   -104       C  
ATOM   2128  O   ASP C   6      42.931   5.063  19.422  1.00 17.42           O  
ANISOU 2128  O   ASP C   6     2628   1675   2313     19    135    -90       O  
ATOM   2129  CB  ASP C   6      41.124   6.118  21.466  1.00 19.65           C  
ANISOU 2129  CB  ASP C   6     2903   1985   2577      0    146   -109       C  
ATOM   2130  CG  ASP C   6      39.953   5.239  20.941  1.00 20.05           C  
ANISOU 2130  CG  ASP C   6     2969   2020   2629      7    140    -82       C  
ATOM   2131  OD1 ASP C   6      39.851   5.059  19.712  1.00 19.94           O  
ANISOU 2131  OD1 ASP C   6     2966   1978   2630     14    142    -72       O  
ATOM   2132  OD2 ASP C   6      39.040   4.870  21.740  1.00 21.08           O  
ANISOU 2132  OD2 ASP C   6     3098   2169   2742      1    137    -74       O  
ATOM   2133  N   LEU C   7      41.973   6.484  17.970  1.00 17.94           N  
ANISOU 2133  N   LEU C   7     2713   1690   2411     13    159   -101       N  
ATOM   2134  CA  LEU C   7      42.449   5.785  16.803  1.00 17.25           C  
ANISOU 2134  CA  LEU C   7     2632   1587   2334     23    153    -86       C  
ATOM   2135  C   LEU C   7      43.969   5.846  16.594  1.00 16.90           C  
ANISOU 2135  C   LEU C   7     2574   1557   2288     19    152    -99       C  
ATOM   2136  O   LEU C   7      44.681   6.772  17.029  1.00 17.10           O  
ANISOU 2136  O   LEU C   7     2588   1598   2309      1    162   -125       O  
ATOM   2137  CB  LEU C   7      41.822   6.347  15.522  1.00 17.31           C  
ANISOU 2137  CB  LEU C   7     2655   1562   2360     27    166    -82       C  
ATOM   2138  CG  LEU C   7      40.293   6.304  15.361  1.00 17.92           C  
ANISOU 2138  CG  LEU C   7     2740   1631   2437     35    168    -70       C  
ATOM   2139  CD1 LEU C   7      39.869   6.903  14.047  1.00 18.94           C  
ANISOU 2139  CD1 LEU C   7     2881   1735   2579     45    180    -66       C  
ATOM   2140  CD2 LEU C   7      39.812   4.902  15.401  1.00 18.14           C  
ANISOU 2140  CD2 LEU C   7     2769   1668   2455     38    154    -48       C  
ATOM   2141  N   ILE C   8      44.476   4.865  15.863  1.00 16.54           N  
ANISOU 2141  N   ILE C   8     2530   1509   2244     34    140    -84       N  
ATOM   2142  CA  ILE C   8      45.828   4.983  15.339  1.00 16.37           C  
ANISOU 2142  CA  ILE C   8     2494   1502   2221     33    140    -97       C  
ATOM   2143  C   ILE C   8      45.962   6.312  14.543  1.00 16.69           C  
ANISOU 2143  C   ILE C   8     2541   1522   2278     10    162   -117       C  
ATOM   2144  O   ILE C   8      45.167   6.517  13.602  1.00 15.61           O  
ANISOU 2144  O   ILE C   8     2422   1349   2157     14    169   -105       O  
ATOM   2145  CB  ILE C   8      46.155   3.773  14.412  1.00 16.91           C  
ANISOU 2145  CB  ILE C   8     2569   1562   2292     57    128    -78       C  
ATOM   2146  CG1 ILE C   8      46.093   2.474  15.192  1.00 17.21           C  
ANISOU 2146  CG1 ILE C   8     2613   1612   2312     80    110    -58       C  
ATOM   2147  CG2 ILE C   8      47.536   3.904  13.796  1.00 17.34           C  
ANISOU 2147  CG2 ILE C   8     2604   1638   2343     57    128    -93       C  
ATOM   2148  CD1 ILE C   8      45.855   1.255  14.304  1.00 17.01           C  
ANISOU 2148  CD1 ILE C   8     2611   1559   2292    101    103    -34       C  
ATOM   2149  N   PRO C   9      46.942   7.192  14.900  1.00 17.90           N  
ANISOU 2149  N   PRO C   9     2678   1698   2421    -14    172   -146       N  
ATOM   2150  CA  PRO C   9      47.048   8.466  14.186  1.00 17.99           C  
ANISOU 2150  CA  PRO C   9     2706   1683   2446    -40    197   -163       C  
ATOM   2151  C   PRO C   9      47.240   8.249  12.662  1.00 17.19           C  
ANISOU 2151  C   PRO C   9     2613   1558   2357    -33    198   -150       C  
ATOM   2152  O   PRO C   9      48.023   7.371  12.226  1.00 16.81           O  
ANISOU 2152  O   PRO C   9     2548   1534   2304    -21    185   -145       O  
ATOM   2153  CB  PRO C   9      48.267   9.148  14.845  1.00 19.20           C  
ANISOU 2153  CB  PRO C   9     2838   1876   2581    -73    206   -199       C  
ATOM   2154  CG  PRO C   9      48.223   8.662  16.267  1.00 19.01           C  
ANISOU 2154  CG  PRO C   9     2792   1891   2537    -65    192   -201       C  
ATOM   2155  CD  PRO C   9      47.729   7.210  16.138  1.00 18.35           C  
ANISOU 2155  CD  PRO C   9     2709   1805   2455    -23    167   -166       C  
ATOM   2156  N   ALA C  10      46.551   9.042  11.852  1.00 17.40           N  
ANISOU 2156  N   ALA C  10     2669   1542   2400    -36    216   -145       N  
ATOM   2157  CA  ALA C  10      46.854   9.023  10.442  1.00 16.92           C  
ANISOU 2157  CA  ALA C  10     2615   1464   2348    -35    221   -136       C  
ATOM   2158  C   ALA C  10      48.308   9.443  10.195  1.00 17.95           C  
ANISOU 2158  C   ALA C  10     2730   1619   2468    -67    230   -162       C  
ATOM   2159  O   ALA C  10      48.846  10.335  10.925  1.00 18.75           O  
ANISOU 2159  O   ALA C  10     2831   1733   2559   -100    245   -190       O  
ATOM   2160  CB  ALA C  10      45.902   9.893   9.683  1.00 16.83           C  
ANISOU 2160  CB  ALA C  10     2637   1406   2350    -31    239   -126       C  
ATOM   2161  N   PRO C  11      48.928   8.896   9.160  1.00 18.14           N  
ANISOU 2161  N   PRO C  11     2743   1653   2494    -61    224   -156       N  
ATOM   2162  CA  PRO C  11      50.347   9.037   8.990  1.00 18.78           C  
ANISOU 2162  CA  PRO C  11     2800   1775   2560    -87    227   -181       C  
ATOM   2163  C   PRO C  11      50.675  10.425   8.429  1.00 20.16           C  
ANISOU 2163  C   PRO C  11     2998   1926   2735   -132    259   -199       C  
ATOM   2164  O   PRO C  11      49.844  11.014   7.758  1.00 19.76           O  
ANISOU 2164  O   PRO C  11     2985   1823   2699   -129    273   -183       O  
ATOM   2165  CB  PRO C  11      50.710   7.913   8.013  1.00 19.28           C  
ANISOU 2165  CB  PRO C  11     2847   1852   2624    -59    210   -166       C  
ATOM   2166  CG  PRO C  11      49.493   7.651   7.250  1.00 18.74           C  
ANISOU 2166  CG  PRO C  11     2807   1736   2577    -36    208   -136       C  
ATOM   2167  CD  PRO C  11      48.365   7.904   8.216  1.00 18.13           C  
ANISOU 2167  CD  PRO C  11     2746   1636   2504    -28    209   -128       C  
ATOM   2168  N   PRO C  12      51.920  10.871   8.631  1.00 21.92           N  
ANISOU 2168  N   PRO C  12     3200   2191   2937   -173    269   -232       N  
ATOM   2169  CA  PRO C  12      52.261  12.077   7.919  1.00 23.45           C  
ANISOU 2169  CA  PRO C  12     3422   2357   3128   -220    301   -247       C  
ATOM   2170  C   PRO C  12      52.216  11.864   6.398  1.00 24.50           C  
ANISOU 2170  C   PRO C  12     3567   2468   3273   -208    302   -226       C  
ATOM   2171  O   PRO C  12      52.608  10.804   5.879  1.00 23.58           O  
ANISOU 2171  O   PRO C  12     3418   2384   3154   -182    280   -217       O  
ATOM   2172  CB  PRO C  12      53.679  12.347   8.389  1.00 23.58           C  
ANISOU 2172  CB  PRO C  12     3403   2440   3116   -267    309   -288       C  
ATOM   2173  CG  PRO C  12      54.271  11.019   8.571  1.00 23.79           C  
ANISOU 2173  CG  PRO C  12     3377   2531   3131   -230    276   -285       C  
ATOM   2174  CD  PRO C  12      53.122  10.081   8.960  1.00 23.28           C  
ANISOU 2174  CD  PRO C  12     3320   2438   3085   -171    251   -250       C  
ATOM   2175  N   LEU C  13      51.768  12.874   5.668  1.00 26.68           N  
ANISOU 2175  N   LEU C  13     3891   2688   3558   -226    329   -218       N  
ATOM   2176  CA  LEU C  13      51.628  12.744   4.209  1.00 27.96           C  
ANISOU 2176  CA  LEU C  13     4065   2828   3727   -214    331   -195       C  
ATOM   2177  C   LEU C  13      52.987  12.512   3.506  1.00 27.46           C  
ANISOU 2177  C   LEU C  13     3970   2815   3647   -245    332   -215       C  
ATOM   2178  O   LEU C  13      53.045  11.927   2.392  1.00 26.30           O  
ANISOU 2178  O   LEU C  13     3813   2672   3505   -226    323   -198       O  
ATOM   2179  CB  LEU C  13      50.876  13.958   3.648  1.00 30.00           C  
ANISOU 2179  CB  LEU C  13     4387   3017   3994   -222    361   -181       C  
ATOM   2180  CG  LEU C  13      49.600  14.446   4.369  1.00 30.39           C  
ANISOU 2180  CG  LEU C  13     4471   3019   4054   -194    366   -168       C  
ATOM   2181  CD1 LEU C  13      49.504  15.987   4.400  1.00 31.59           C  
ANISOU 2181  CD1 LEU C  13     4686   3116   4201   -226    406   -177       C  
ATOM   2182  CD2 LEU C  13      48.319  13.844   3.804  1.00 31.27           C  
ANISOU 2182  CD2 LEU C  13     4587   3111   4181   -134    349   -130       C  
ATOM   2183  N   SER C  14      54.074  12.896   4.183  1.00 28.07           N  
ANISOU 2183  N   SER C  14     4023   2938   3701   -292    342   -252       N  
ATOM   2184  CA  SER C  14      55.427  12.580   3.761  1.00 30.30           C  
ANISOU 2184  CA  SER C  14     4261   3289   3960   -320    340   -278       C  
ATOM   2185  C   SER C  14      55.712  11.083   3.646  1.00 29.58           C  
ANISOU 2185  C   SER C  14     4120   3250   3868   -266    303   -268       C  
ATOM   2186  O   SER C  14      56.625  10.684   2.936  1.00 32.64           O  
ANISOU 2186  O   SER C  14     4475   3686   4241   -272    298   -280       O  
ATOM   2187  CB  SER C  14      56.430  13.232   4.721  1.00 30.48           C  
ANISOU 2187  CB  SER C  14     4263   3363   3953   -379    355   -323       C  
ATOM   2188  OG  SER C  14      56.487  12.553   5.956  1.00 31.10           O  
ANISOU 2188  OG  SER C  14     4304   3487   4025   -351    331   -331       O  
ATOM   2189  N   LYS C  15      54.940  10.256   4.362  1.00 28.39           N  
ANISOU 2189  N   LYS C  15     3965   3090   3731   -214    278   -249       N  
ATOM   2190  CA  LYS C  15      55.056   8.792   4.279  1.00 26.90           C  
ANISOU 2190  CA  LYS C  15     3744   2934   3543   -159    246   -235       C  
ATOM   2191  C   LYS C  15      54.078   8.158   3.288  1.00 25.07           C  
ANISOU 2191  C   LYS C  15     3536   2653   3337   -119    237   -200       C  
ATOM   2192  O   LYS C  15      54.029   6.928   3.207  1.00 25.45           O  
ANISOU 2192  O   LYS C  15     3568   2715   3387    -74    213   -187       O  
ATOM   2193  CB  LYS C  15      54.842   8.147   5.653  1.00 27.52           C  
ANISOU 2193  CB  LYS C  15     3806   3032   3616   -127    226   -234       C  
ATOM   2194  CG  LYS C  15      55.967   8.418   6.611  1.00 28.95           C  
ANISOU 2194  CG  LYS C  15     3948   3285   3766   -155    227   -271       C  
ATOM   2195  CD  LYS C  15      55.817   7.684   7.909  1.00 30.31           C  
ANISOU 2195  CD  LYS C  15     4102   3483   3929   -118    205   -266       C  
ATOM   2196  CE  LYS C  15      56.219   6.231   7.713  1.00 30.65           C  
ANISOU 2196  CE  LYS C  15     4120   3563   3963    -57    177   -253       C  
ATOM   2197  NZ  LYS C  15      56.521   5.633   9.029  1.00 30.92           N  
ANISOU 2197  NZ  LYS C  15     4128   3645   3974    -28    158   -258       N  
ATOM   2198  N   VAL C  16      53.274   8.970   2.593  1.00 23.78           N  
ANISOU 2198  N   VAL C  16     3413   2432   3189   -133    256   -183       N  
ATOM   2199  CA  VAL C  16      52.357   8.506   1.548  1.00 23.59           C  
ANISOU 2199  CA  VAL C  16     3409   2370   3184   -102    250   -153       C  
ATOM   2200  C   VAL C  16      52.780   9.034   0.163  1.00 24.22           C  
ANISOU 2200  C   VAL C  16     3496   2445   3260   -127    267   -153       C  
ATOM   2201  O   VAL C  16      52.378  10.100  -0.263  1.00 24.72           O  
ANISOU 2201  O   VAL C  16     3596   2467   3326   -149    291   -145       O  
ATOM   2202  CB  VAL C  16      50.881   8.901   1.858  1.00 23.62           C  
ANISOU 2202  CB  VAL C  16     3450   2318   3205    -85    255   -129       C  
ATOM   2203  CG1 VAL C  16      49.940   8.376   0.762  1.00 24.08           C  
ANISOU 2203  CG1 VAL C  16     3520   2350   3276    -54    248   -100       C  
ATOM   2204  CG2 VAL C  16      50.486   8.446   3.254  1.00 23.57           C  
ANISOU 2204  CG2 VAL C  16     3436   2320   3200    -67    240   -130       C  
ATOM   2205  N   PRO C  17      53.640   8.287  -0.524  1.00 24.27           N  
ANISOU 2205  N   PRO C  17     3469   2494   3256   -120    256   -162       N  
ATOM   2206  CA  PRO C  17      54.068   8.609  -1.881  1.00 24.69           C  
ANISOU 2206  CA  PRO C  17     3524   2550   3304   -141    269   -162       C  
ATOM   2207  C   PRO C  17      52.947   8.708  -2.910  1.00 23.80           C  
ANISOU 2207  C   PRO C  17     3445   2388   3209   -122    274   -129       C  
ATOM   2208  O   PRO C  17      51.879   8.147  -2.738  1.00 23.82           O  
ANISOU 2208  O   PRO C  17     3458   2365   3227    -85    261   -108       O  
ATOM   2209  CB  PRO C  17      55.012   7.452  -2.203  1.00 24.86           C  
ANISOU 2209  CB  PRO C  17     3499   2631   3313   -119    249   -176       C  
ATOM   2210  CG  PRO C  17      55.568   7.041  -0.868  1.00 25.66           C  
ANISOU 2210  CG  PRO C  17     3573   2773   3402   -109    235   -196       C  
ATOM   2211  CD  PRO C  17      54.394   7.148   0.027  1.00 25.29           C  
ANISOU 2211  CD  PRO C  17     3557   2678   3374    -93    232   -176       C  
ATOM   2212  N   LEU C  18      53.213   9.448  -3.982  1.00 23.88           N  
ANISOU 2212  N   LEU C  18     3471   2389   3212   -151    295   -127       N  
ATOM   2213  CA  LEU C  18      52.351   9.529  -5.152  1.00 22.93           C  
ANISOU 2213  CA  LEU C  18     3375   2236   3100   -133    300    -98       C  
ATOM   2214  C   LEU C  18      53.035   8.890  -6.354  1.00 23.63           C  
ANISOU 2214  C   LEU C  18     3434   2361   3180   -133    293   -103       C  
ATOM   2215  O   LEU C  18      54.234   9.135  -6.619  1.00 24.33           O  
ANISOU 2215  O   LEU C  18     3503   2489   3252   -169    303   -127       O  
ATOM   2216  CB  LEU C  18      52.065  11.008  -5.458  1.00 24.01           C  
ANISOU 2216  CB  LEU C  18     3561   2327   3232   -163    332    -87       C  
ATOM   2217  CG  LEU C  18      50.956  11.430  -6.439  1.00 24.10           C  
ANISOU 2217  CG  LEU C  18     3611   2297   3249   -138    342    -52       C  
ATOM   2218  CD1 LEU C  18      49.580  11.034  -5.995  1.00 24.83           C  
ANISOU 2218  CD1 LEU C  18     3710   2366   3356    -89    327    -30       C  
ATOM   2219  CD2 LEU C  18      50.911  12.982  -6.436  1.00 24.74           C  
ANISOU 2219  CD2 LEU C  18     3749   2329   3320   -170    377    -46       C  
ATOM   2220  N   GLN C  19      52.283   8.078  -7.101  1.00 22.60           N  
ANISOU 2220  N   GLN C  19     3300   2225   3060    -95    279    -83       N  
ATOM   2221  CA  GLN C  19      52.833   7.467  -8.332  1.00 21.83           C  
ANISOU 2221  CA  GLN C  19     3177   2160   2954    -93    274    -88       C  
ATOM   2222  C   GLN C  19      53.407   8.550  -9.269  1.00 21.85           C  
ANISOU 2222  C   GLN C  19     3195   2165   2942   -136    301    -88       C  
ATOM   2223  O   GLN C  19      52.679   9.400  -9.730  1.00 21.26           O  
ANISOU 2223  O   GLN C  19     3159   2050   2868   -141    318    -64       O  
ATOM   2224  CB  GLN C  19      51.774   6.684  -9.104  1.00 21.01           C  
ANISOU 2224  CB  GLN C  19     3077   2044   2862    -55    262    -65       C  
ATOM   2225  CG  GLN C  19      52.300   6.077 -10.401  1.00 21.46           C  
ANISOU 2225  CG  GLN C  19     3109   2133   2910    -54    258    -72       C  
ATOM   2226  CD  GLN C  19      53.478   5.113 -10.216  1.00 21.54           C  
ANISOU 2226  CD  GLN C  19     3080   2192   2912    -47    243   -102       C  
ATOM   2227  OE1 GLN C  19      53.347   4.043  -9.639  1.00 21.34           O  
ANISOU 2227  OE1 GLN C  19     3045   2169   2894    -15    224   -107       O  
ATOM   2228  NE2 GLN C  19      54.628   5.490 -10.750  1.00 23.48           N  
ANISOU 2228  NE2 GLN C  19     3305   2476   3140    -77    253   -121       N  
ATOM   2229  N   GLN C  20      54.690   8.435  -9.578  1.00 21.68           N  
ANISOU 2229  N   GLN C  20     3142   2193   2902   -164    303   -115       N  
ATOM   2230  CA  GLN C  20      55.341   9.357 -10.520  1.00 23.53           C  
ANISOU 2230  CA  GLN C  20     3386   2436   3116   -212    328   -118       C  
ATOM   2231  C   GLN C  20      54.640   9.296 -11.894  1.00 22.54           C  
ANISOU 2231  C   GLN C  20     3276   2294   2994   -194    331    -90       C  
ATOM   2232  O   GLN C  20      54.200   8.275 -12.343  1.00 22.20           O  
ANISOU 2232  O   GLN C  20     3212   2262   2960   -155    311    -83       O  
ATOM   2233  CB  GLN C  20      56.841   8.983 -10.626  1.00 23.91           C  
ANISOU 2233  CB  GLN C  20     3384   2558   3141   -239    325   -156       C  
ATOM   2234  CG  GLN C  20      57.694   9.718 -11.650  1.00 24.90           C  
ANISOU 2234  CG  GLN C  20     3509   2710   3241   -294    349   -166       C  
ATOM   2235  CD  GLN C  20      59.192   9.389 -11.610  1.00 24.83           C  
ANISOU 2235  CD  GLN C  20     3443   2786   3203   -322    346   -209       C  
ATOM   2236  OE1 GLN C  20      59.633   8.281 -11.272  1.00 24.37           O  
ANISOU 2236  OE1 GLN C  20     3338   2776   3144   -283    320   -228       O  
ATOM   2237  NE2 GLN C  20      59.985  10.352 -11.992  1.00 26.15           N  
ANISOU 2237  NE2 GLN C  20     3616   2974   3344   -390    374   -225       N  
ATOM   2238  N   ASN C  21      54.523  10.442 -12.544  1.00 23.74           N  
ANISOU 2238  N   ASN C  21     3468   2416   3134   -226    359    -72       N  
ATOM   2239  CA  ASN C  21      53.966  10.525 -13.895  1.00 24.29           C  
ANISOU 2239  CA  ASN C  21     3552   2477   3200   -212    365    -45       C  
ATOM   2240  C   ASN C  21      52.594   9.869 -14.070  1.00 22.12           C  
ANISOU 2240  C   ASN C  21     3280   2182   2942   -154    346    -19       C  
ATOM   2241  O   ASN C  21      52.330   9.208 -15.075  1.00 20.73           O  
ANISOU 2241  O   ASN C  21     3083   2027   2763   -133    336    -11       O  
ATOM   2242  CB  ASN C  21      54.942  10.013 -14.937  1.00 26.12           C  
ANISOU 2242  CB  ASN C  21     3743   2766   3414   -231    362    -63       C  
ATOM   2243  CG  ASN C  21      54.535  10.393 -16.366  1.00 28.32           C  
ANISOU 2243  CG  ASN C  21     4042   3037   3680   -231    375    -35       C  
ATOM   2244  OD1 ASN C  21      53.866  11.416 -16.584  1.00 30.72           O  
ANISOU 2244  OD1 ASN C  21     4399   3293   3980   -235    397     -5       O  
ATOM   2245  ND2 ASN C  21      54.906   9.550 -17.340  1.00 28.78           N  
ANISOU 2245  ND2 ASN C  21     4059   3143   3730   -223    363    -45       N  
ATOM   2246  N   PHE C  22      51.733  10.054 -13.071  1.00 21.10           N  
ANISOU 2246  N   PHE C  22     3174   2015   2828   -131    343     -8       N  
ATOM   2247  CA  PHE C  22      50.417   9.429 -13.076  1.00 20.85           C  
ANISOU 2247  CA  PHE C  22     3140   1971   2809    -81    326     12       C  
ATOM   2248  C   PHE C  22      49.660   9.684 -14.350  1.00 19.92           C  
ANISOU 2248  C   PHE C  22     3037   1851   2680    -62    333     41       C  
ATOM   2249  O   PHE C  22      49.528  10.836 -14.771  1.00 20.73           O  
ANISOU 2249  O   PHE C  22     3181   1926   2770    -72    357     62       O  
ATOM   2250  CB  PHE C  22      49.600   9.904 -11.898  1.00 20.25           C  
ANISOU 2250  CB  PHE C  22     3093   1856   2744    -65    327     21       C  
ATOM   2251  CG  PHE C  22      48.240   9.260 -11.802  1.00 20.15           C  
ANISOU 2251  CG  PHE C  22     3074   1839   2740    -18    311     38       C  
ATOM   2252  CD1 PHE C  22      48.097   7.924 -11.423  1.00 19.70           C  
ANISOU 2252  CD1 PHE C  22     2983   1806   2695     -1    286     24       C  
ATOM   2253  CD2 PHE C  22      47.118   9.974 -12.082  1.00 19.18           C  
ANISOU 2253  CD2 PHE C  22     2982   1692   2610      7    321     67       C  
ATOM   2254  CE1 PHE C  22      46.815   7.319 -11.319  1.00 19.38           C  
ANISOU 2254  CE1 PHE C  22     2938   1766   2658     31    273     36       C  
ATOM   2255  CE2 PHE C  22      45.873   9.408 -11.977  1.00 19.73           C  
ANISOU 2255  CE2 PHE C  22     3042   1769   2683     45    306     79       C  
ATOM   2256  CZ  PHE C  22      45.705   8.080 -11.653  1.00 19.57           C  
ANISOU 2256  CZ  PHE C  22     2985   1775   2673     53    283     63       C  
ATOM   2257  N   GLN C  23      49.133   8.607 -14.936  1.00 18.91           N  
ANISOU 2257  N   GLN C  23     2877   1751   2555    -34    314     42       N  
ATOM   2258  CA  GLN C  23      48.412   8.605 -16.185  1.00 19.07           C  
ANISOU 2258  CA  GLN C  23     2898   1785   2562    -14    316     65       C  
ATOM   2259  C   GLN C  23      46.952   8.310 -15.931  1.00 19.25           C  
ANISOU 2259  C   GLN C  23     2923   1801   2588     26    306     82       C  
ATOM   2260  O   GLN C  23      46.512   7.140 -15.878  1.00 18.30           O  
ANISOU 2260  O   GLN C  23     2772   1704   2475     41    286     70       O  
ATOM   2261  CB  GLN C  23      48.991   7.596 -17.160  1.00 19.25           C  
ANISOU 2261  CB  GLN C  23     2880   1853   2580    -21    305     47       C  
ATOM   2262  CG  GLN C  23      50.468   7.828 -17.480  1.00 19.29           C  
ANISOU 2262  CG  GLN C  23     2874   1877   2575    -61    315     27       C  
ATOM   2263  CD  GLN C  23      50.693   9.090 -18.278  1.00 20.70           C  
ANISOU 2263  CD  GLN C  23     3086   2044   2733    -86    342     48       C  
ATOM   2264  OE1 GLN C  23      50.428   9.126 -19.471  1.00 20.16           O  
ANISOU 2264  OE1 GLN C  23     3015   1994   2650    -80    346     64       O  
ATOM   2265  NE2 GLN C  23      51.194  10.162 -17.607  1.00 21.59           N  
ANISOU 2265  NE2 GLN C  23     3234   2125   2844   -118    362     48       N  
ATOM   2266  N   ASP C  24      46.174   9.349 -15.768  1.00 18.57           N  
ANISOU 2266  N   ASP C  24     2874   1685   2494     44    320    109       N  
ATOM   2267  CA  ASP C  24      44.745   9.166 -15.480  1.00 18.60           C  
ANISOU 2267  CA  ASP C  24     2877   1693   2497     86    311    124       C  
ATOM   2268  C   ASP C  24      44.015   8.281 -16.515  1.00 18.42           C  
ANISOU 2268  C   ASP C  24     2818   1717   2461    105    298    127       C  
ATOM   2269  O   ASP C  24      43.142   7.511 -16.185  1.00 18.75           O  
ANISOU 2269  O   ASP C  24     2839   1779   2505    121    284    121       O  
ATOM   2270  CB  ASP C  24      44.048  10.518 -15.244  1.00 20.04           C  
ANISOU 2270  CB  ASP C  24     3107   1839   2667    111    330    153       C  
ATOM   2271  CG  ASP C  24      44.153  11.490 -16.414  1.00 21.32           C  
ANISOU 2271  CG  ASP C  24     3301   1993   2805    116    352    181       C  
ATOM   2272  OD1 ASP C  24      44.830  11.213 -17.439  1.00 20.45           O  
ANISOU 2272  OD1 ASP C  24     3174   1908   2687     94    353    178       O  
ATOM   2273  OD2 ASP C  24      43.549  12.623 -16.230  1.00 22.55           O  
ANISOU 2273  OD2 ASP C  24     3505   2113   2949    145    369    207       O  
ATOM   2274  N   ASN C  25      44.392   8.374 -17.774  1.00 18.23           N  
ANISOU 2274  N   ASN C  25     2788   1716   2421     98    305    134       N  
ATOM   2275  CA  ASN C  25      43.705   7.673 -18.825  1.00 18.32           C  
ANISOU 2275  CA  ASN C  25     2768   1776   2416    114    296    138       C  
ATOM   2276  C   ASN C  25      43.996   6.164 -18.733  1.00 17.66           C  
ANISOU 2276  C   ASN C  25     2645   1718   2347     96    277    103       C  
ATOM   2277  O   ASN C  25      43.125   5.365 -19.083  1.00 18.06           O  
ANISOU 2277  O   ASN C  25     2670   1802   2388    108    268     98       O  
ATOM   2278  CB  ASN C  25      44.114   8.195 -20.184  1.00 18.64           C  
ANISOU 2278  CB  ASN C  25     2812   1834   2434    109    310    154       C  
ATOM   2279  CG  ASN C  25      45.604   8.173 -20.390  1.00 19.54           C  
ANISOU 2279  CG  ASN C  25     2926   1941   2557     67    315    135       C  
ATOM   2280  OD1 ASN C  25      46.371   8.905 -19.708  1.00 20.05           O  
ANISOU 2280  OD1 ASN C  25     3019   1967   2630     44    327    133       O  
ATOM   2281  ND2 ASN C  25      46.054   7.310 -21.279  1.00 18.90           N  
ANISOU 2281  ND2 ASN C  25     2808   1901   2471     53    307    117       N  
ATOM   2282  N   GLN C  26      45.163   5.800 -18.201  1.00 17.38           N  
ANISOU 2282  N   GLN C  26     2607   1666   2330     70    274     79       N  
ATOM   2283  CA  GLN C  26      45.409   4.319 -17.964  1.00 16.76           C  
ANISOU 2283  CA  GLN C  26     2500   1602   2265     63    256     48       C  
ATOM   2284  C   GLN C  26      44.934   3.795 -16.606  1.00 17.28           C  
ANISOU 2284  C   GLN C  26     2572   1646   2348     69    245     39       C  
ATOM   2285  O   GLN C  26      44.748   2.565 -16.468  1.00 17.15           O  
ANISOU 2285  O   GLN C  26     2541   1639   2336     68    233     19       O  
ATOM   2286  CB  GLN C  26      46.887   3.993 -18.054  1.00 16.43           C  
ANISOU 2286  CB  GLN C  26     2447   1564   2231     40    255     24       C  
ATOM   2287  CG  GLN C  26      47.456   4.117 -19.464  1.00 16.87           C  
ANISOU 2287  CG  GLN C  26     2488   1652   2269     29    262     23       C  
ATOM   2288  CD  GLN C  26      48.937   3.831 -19.523  1.00 16.74           C  
ANISOU 2288  CD  GLN C  26     2456   1648   2256      7    261     -2       C  
ATOM   2289  OE1 GLN C  26      49.725   4.742 -19.605  1.00 18.18           O  
ANISOU 2289  OE1 GLN C  26     2647   1827   2431    -13    274      1       O  
ATOM   2290  NE2 GLN C  26      49.328   2.551 -19.428  1.00 16.52           N  
ANISOU 2290  NE2 GLN C  26     2405   1634   2235     14    247    -31       N  
ATOM   2291  N   PHE C  27      44.872   4.627 -15.574  1.00 17.18           N  
ANISOU 2291  N   PHE C  27     2582   1600   2342     73    250     49       N  
ATOM   2292  CA  PHE C  27      44.298   4.184 -14.305  1.00 16.67           C  
ANISOU 2292  CA  PHE C  27     2523   1520   2291     80    240     43       C  
ATOM   2293  C   PHE C  27      42.793   3.837 -14.416  1.00 17.03           C  
ANISOU 2293  C   PHE C  27     2560   1585   2324     97    236     53       C  
ATOM   2294  O   PHE C  27      42.201   3.164 -13.556  1.00 16.44           O  
ANISOU 2294  O   PHE C  27     2484   1507   2255     98    227     44       O  
ATOM   2295  CB  PHE C  27      44.466   5.247 -13.222  1.00 16.84           C  
ANISOU 2295  CB  PHE C  27     2570   1506   2319     80    248     52       C  
ATOM   2296  CG  PHE C  27      44.195   4.747 -11.866  1.00 16.89           C  
ANISOU 2296  CG  PHE C  27     2580   1498   2340     82    237     42       C  
ATOM   2297  CD1 PHE C  27      45.029   3.789 -11.265  1.00 16.75           C  
ANISOU 2297  CD1 PHE C  27     2552   1478   2334     72    225     20       C  
ATOM   2298  CD2 PHE C  27      43.079   5.177 -11.175  1.00 17.13           C  
ANISOU 2298  CD2 PHE C  27     2621   1519   2367     99    239     56       C  
ATOM   2299  CE1 PHE C  27      44.717   3.326  -9.977  1.00 17.05           C  
ANISOU 2299  CE1 PHE C  27     2595   1501   2381     76    216     14       C  
ATOM   2300  CE2 PHE C  27      42.825   4.750  -9.866  1.00 17.26           C  
ANISOU 2300  CE2 PHE C  27     2641   1523   2394     99    230     47       C  
ATOM   2301  CZ  PHE C  27      43.611   3.770  -9.314  1.00 17.04           C  
ANISOU 2301  CZ  PHE C  27     2604   1491   2378     86    218     27       C  
ATOM   2302  N   HIS C  28      42.134   4.440 -15.403  1.00 17.76           N  
ANISOU 2302  N   HIS C  28     2650   1702   2395    112    244     72       N  
ATOM   2303  CA  HIS C  28      40.755   4.205 -15.757  1.00 17.85           C  
ANISOU 2303  CA  HIS C  28     2645   1750   2386    130    242     80       C  
ATOM   2304  C   HIS C  28      40.381   2.744 -15.789  1.00 18.14           C  
ANISOU 2304  C   HIS C  28     2658   1811   2422    112    231     55       C  
ATOM   2305  O   HIS C  28      41.206   1.931 -16.182  1.00 19.08           O  
ANISOU 2305  O   HIS C  28     2770   1927   2549     93    227     36       O  
ATOM   2306  CB  HIS C  28      40.501   4.830 -17.168  1.00 20.02           C  
ANISOU 2306  CB  HIS C  28     2913   2058   2635    146    251    100       C  
ATOM   2307  CG  HIS C  28      39.161   4.538 -17.769  1.00 20.45           C  
ANISOU 2307  CG  HIS C  28     2940   2168   2659    164    249    105       C  
ATOM   2308  ND1 HIS C  28      38.106   5.415 -17.698  1.00 21.74           N  
ANISOU 2308  ND1 HIS C  28     3109   2350   2801    201    254    130       N  
ATOM   2309  CD2 HIS C  28      38.736   3.504 -18.529  1.00 21.18           C  
ANISOU 2309  CD2 HIS C  28     3001   2309   2738    149    243     87       C  
ATOM   2310  CE1 HIS C  28      37.060   4.903 -18.323  1.00 23.02           C  
ANISOU 2310  CE1 HIS C  28     3237   2576   2934    209    250    126       C  
ATOM   2311  NE2 HIS C  28      37.431   3.742 -18.852  1.00 22.89           N  
ANISOU 2311  NE2 HIS C  28     3197   2577   2922    174    244     99       N  
ATOM   2312  N   GLY C  29      39.196   2.444 -15.307  1.00 18.50           N  
ANISOU 2312  N   GLY C  29     2696   1877   2457    117    227     54       N  
ATOM   2313  CA  GLY C  29      38.592   1.134 -15.456  1.00 18.11           C  
ANISOU 2313  CA  GLY C  29     2627   1855   2397     95    221     31       C  
ATOM   2314  C   GLY C  29      38.341   0.341 -14.193  1.00 17.88           C  
ANISOU 2314  C   GLY C  29     2609   1802   2380     78    215     16       C  
ATOM   2315  O   GLY C  29      38.251   0.857 -13.117  1.00 17.70           O  
ANISOU 2315  O   GLY C  29     2602   1756   2368     88    214     25       O  
ATOM   2316  N   LYS C  30      38.205  -0.961 -14.405  1.00 18.97           N  
ANISOU 2316  N   LYS C  30     2742   1949   2514     50    213     -7       N  
ATOM   2317  CA  LYS C  30      37.934  -1.920 -13.350  1.00 19.12           C  
ANISOU 2317  CA  LYS C  30     2777   1946   2539     29    210    -22       C  
ATOM   2318  C   LYS C  30      39.177  -2.415 -12.631  1.00 17.35           C  
ANISOU 2318  C   LYS C  30     2581   1666   2343     28    204    -30       C  
ATOM   2319  O   LYS C  30      40.157  -2.948 -13.232  1.00 17.85           O  
ANISOU 2319  O   LYS C  30     2649   1716   2415     26    203    -42       O  
ATOM   2320  CB  LYS C  30      37.161  -3.133 -13.934  1.00 21.28           C  
ANISOU 2320  CB  LYS C  30     3041   2251   2790     -4    214    -46       C  
ATOM   2321  CG  LYS C  30      36.788  -4.175 -12.946  1.00 22.46           C  
ANISOU 2321  CG  LYS C  30     3214   2377   2940    -33    215    -62       C  
ATOM   2322  CD  LYS C  30      36.777  -5.594 -13.531  1.00 23.87           C  
ANISOU 2322  CD  LYS C  30     3405   2554   3110    -70    222    -91       C  
ATOM   2323  CE  LYS C  30      35.721  -5.882 -14.570  1.00 26.00           C  
ANISOU 2323  CE  LYS C  30     3643   2889   3344    -97    231   -107       C  
ATOM   2324  NZ  LYS C  30      34.417  -6.091 -13.908  1.00 27.26           N  
ANISOU 2324  NZ  LYS C  30     3796   3082   3479   -125    236   -113       N  
ATOM   2325  N   TRP C  31      39.109  -2.256 -11.309  1.00 16.02           N  
ANISOU 2325  N   TRP C  31     2429   1470   2185     31    200    -24       N  
ATOM   2326  CA  TRP C  31      40.087  -2.784 -10.353  1.00 16.27           C  
ANISOU 2326  CA  TRP C  31     2487   1456   2237     33    194    -30       C  
ATOM   2327  C   TRP C  31      39.509  -3.667  -9.229  1.00 17.36           C  
ANISOU 2327  C   TRP C  31     2647   1576   2373     16    192    -36       C  
ATOM   2328  O   TRP C  31      38.619  -3.237  -8.485  1.00 17.84           O  
ANISOU 2328  O   TRP C  31     2704   1648   2426     12    193    -28       O  
ATOM   2329  CB  TRP C  31      40.805  -1.599  -9.739  1.00 15.54           C  
ANISOU 2329  CB  TRP C  31     2395   1347   2160     54    191    -15       C  
ATOM   2330  CG  TRP C  31      41.724  -0.779 -10.598  1.00 15.11           C  
ANISOU 2330  CG  TRP C  31     2331   1298   2111     66    194    -10       C  
ATOM   2331  CD1 TRP C  31      41.463   0.482 -11.124  1.00 14.62           C  
ANISOU 2331  CD1 TRP C  31     2260   1251   2043     77    202      7       C  
ATOM   2332  CD2 TRP C  31      43.068  -1.081 -10.946  1.00 14.43           C  
ANISOU 2332  CD2 TRP C  31     2245   1202   2035     68    192    -22       C  
ATOM   2333  NE1 TRP C  31      42.605   0.969 -11.757  1.00 14.48           N  
ANISOU 2333  NE1 TRP C  31     2240   1229   2031     79    205      6       N  
ATOM   2334  CE2 TRP C  31      43.585   0.020 -11.681  1.00 14.97           C  
ANISOU 2334  CE2 TRP C  31     2303   1282   2103     73    198    -12       C  
ATOM   2335  CE3 TRP C  31      43.903  -2.174 -10.715  1.00 14.26           C  
ANISOU 2335  CE3 TRP C  31     2233   1164   2020     70    185    -39       C  
ATOM   2336  CZ2 TRP C  31      44.870   0.048 -12.157  1.00 14.74           C  
ANISOU 2336  CZ2 TRP C  31     2267   1254   2077     72    198    -22       C  
ATOM   2337  CZ3 TRP C  31      45.218  -2.107 -11.202  1.00 14.30           C  
ANISOU 2337  CZ3 TRP C  31     2229   1173   2029     78    183    -49       C  
ATOM   2338  CH2 TRP C  31      45.666  -0.988 -11.904  1.00 14.72           C  
ANISOU 2338  CH2 TRP C  31     2266   1244   2080     76    190    -41       C  
ATOM   2339  N   TYR C  32      40.029  -4.886  -9.068  1.00 17.41           N  
ANISOU 2339  N   TYR C  32     2680   1552   2383      7    191    -51       N  
ATOM   2340  CA  TYR C  32      39.549  -5.793  -8.038  1.00 17.63           C  
ANISOU 2340  CA  TYR C  32     2737   1555   2405    -10    192    -55       C  
ATOM   2341  C   TYR C  32      40.283  -5.555  -6.749  1.00 16.22           C  
ANISOU 2341  C   TYR C  32     2575   1345   2241     10    183    -45       C  
ATOM   2342  O   TYR C  32      41.487  -5.267  -6.770  1.00 16.12           O  
ANISOU 2342  O   TYR C  32     2561   1321   2244     36    177    -44       O  
ATOM   2343  CB  TYR C  32      39.757  -7.249  -8.489  1.00 19.15           C  
ANISOU 2343  CB  TYR C  32     2960   1724   2591    -27    198    -75       C  
ATOM   2344  CG  TYR C  32      38.904  -7.657  -9.666  1.00 20.71           C  
ANISOU 2344  CG  TYR C  32     3143   1956   2768    -59    209    -91       C  
ATOM   2345  CD1 TYR C  32      37.565  -8.077  -9.487  1.00 23.73           C  
ANISOU 2345  CD1 TYR C  32     3527   2361   3127   -100    219    -99       C  
ATOM   2346  CD2 TYR C  32      39.417  -7.630 -10.919  1.00 22.98           C  
ANISOU 2346  CD2 TYR C  32     3414   2260   3057    -50    210   -100       C  
ATOM   2347  CE1 TYR C  32      36.813  -8.462 -10.588  1.00 25.24           C  
ANISOU 2347  CE1 TYR C  32     3701   2593   3295   -132    230   -117       C  
ATOM   2348  CE2 TYR C  32      38.674  -8.015 -12.011  1.00 25.04           C  
ANISOU 2348  CE2 TYR C  32     3659   2557   3297    -80    220   -117       C  
ATOM   2349  CZ  TYR C  32      37.371  -8.432 -11.834  1.00 26.00           C  
ANISOU 2349  CZ  TYR C  32     3780   2703   3394   -121    230   -126       C  
ATOM   2350  OH  TYR C  32      36.686  -8.797 -12.986  1.00 28.35           O  
ANISOU 2350  OH  TYR C  32     4057   3047   3668   -151    241   -146       O  
ATOM   2351  N   VAL C  33      39.571  -5.595  -5.601  1.00 15.75           N  
ANISOU 2351  N   VAL C  33     2528   1280   2177     -1    183    -38       N  
ATOM   2352  CA  VAL C  33      40.166  -5.464  -4.281  1.00 15.71           C  
ANISOU 2352  CA  VAL C  33     2538   1248   2181     15    175    -29       C  
ATOM   2353  C   VAL C  33      40.864  -6.759  -3.901  1.00 15.98           C  
ANISOU 2353  C   VAL C  33     2613   1243   2215     21    173    -35       C  
ATOM   2354  O   VAL C  33      40.217  -7.813  -3.752  1.00 17.03           O  
ANISOU 2354  O   VAL C  33     2777   1358   2334     -3    181    -41       O  
ATOM   2355  CB  VAL C  33      39.075  -5.043  -3.283  1.00 15.77           C  
ANISOU 2355  CB  VAL C  33     2541   1270   2179      0    176    -20       C  
ATOM   2356  CG1 VAL C  33      39.550  -5.045  -1.863  1.00 15.68           C  
ANISOU 2356  CG1 VAL C  33     2548   1234   2174     12    169    -12       C  
ATOM   2357  CG2 VAL C  33      38.505  -3.699  -3.674  1.00 15.88           C  
ANISOU 2357  CG2 VAL C  33     2519   1320   2192      7    178    -13       C  
ATOM   2358  N   VAL C  34      42.168  -6.719  -3.733  1.00 15.54           N  
ANISOU 2358  N   VAL C  34     2559   1172   2171     55    165    -35       N  
ATOM   2359  CA  VAL C  34      42.956  -7.892  -3.337  1.00 15.44           C  
ANISOU 2359  CA  VAL C  34     2586   1124   2155     75    162    -39       C  
ATOM   2360  C   VAL C  34      43.297  -7.795  -1.852  1.00 16.22           C  
ANISOU 2360  C   VAL C  34     2697   1211   2253     93    154    -26       C  
ATOM   2361  O   VAL C  34      43.305  -8.795  -1.134  1.00 17.40           O  
ANISOU 2361  O   VAL C  34     2890   1329   2393     98    154    -22       O  
ATOM   2362  CB  VAL C  34      44.244  -8.063  -4.176  1.00 15.48           C  
ANISOU 2362  CB  VAL C  34     2583   1132   2166    107    158    -50       C  
ATOM   2363  CG1 VAL C  34      45.053  -9.292  -3.743  1.00 15.76           C  
ANISOU 2363  CG1 VAL C  34     2661   1131   2193    140    155    -53       C  
ATOM   2364  CG2 VAL C  34      43.892  -8.179  -5.614  1.00 15.72           C  
ANISOU 2364  CG2 VAL C  34     2601   1176   2196     89    166    -63       C  
ATOM   2365  N   GLY C  35      43.652  -6.587  -1.407  1.00 15.28           N  
ANISOU 2365  N   GLY C  35     2544   1117   2143    103    147    -21       N  
ATOM   2366  CA  GLY C  35      44.027  -6.376   0.003  1.00 15.67           C  
ANISOU 2366  CA  GLY C  35     2598   1163   2190    118    139    -11       C  
ATOM   2367  C   GLY C  35      43.495  -5.051   0.517  1.00 15.02           C  
ANISOU 2367  C   GLY C  35     2486   1105   2115    103    139     -6       C  
ATOM   2368  O   GLY C  35      43.239  -4.124  -0.246  1.00 16.00           O  
ANISOU 2368  O   GLY C  35     2584   1248   2247     93    144     -8       O  
ATOM   2369  N   ARG C  36      43.299  -4.983   1.818  1.00 15.18           N  
ANISOU 2369  N   ARG C  36     2515   1122   2129    103    135      2       N  
ATOM   2370  CA  ARG C  36      42.727  -3.796   2.491  1.00 15.20           C  
ANISOU 2370  CA  ARG C  36     2495   1143   2135     90    136      5       C  
ATOM   2371  C   ARG C  36      43.350  -3.669   3.864  1.00 15.20           C  
ANISOU 2371  C   ARG C  36     2497   1147   2132    105    128      9       C  
ATOM   2372  O   ARG C  36      43.591  -4.647   4.560  1.00 16.36           O  
ANISOU 2372  O   ARG C  36     2671   1278   2267    117    123     15       O  
ATOM   2373  CB  ARG C  36      41.202  -3.919   2.652  1.00 16.05           C  
ANISOU 2373  CB  ARG C  36     2609   1253   2233     61    144     11       C  
ATOM   2374  CG  ARG C  36      40.806  -5.277   3.286  1.00 18.02           C  
ANISOU 2374  CG  ARG C  36     2898   1480   2467     49    145     16       C  
ATOM   2375  CD  ARG C  36      39.322  -5.376   3.563  1.00 19.06           C  
ANISOU 2375  CD  ARG C  36     3032   1624   2584     13    153     18       C  
ATOM   2376  NE  ARG C  36      38.809  -4.128   4.162  1.00 20.41           N  
ANISOU 2376  NE  ARG C  36     3173   1823   2757     13    152     19       N  
ATOM   2377  CZ  ARG C  36      37.529  -3.861   4.431  1.00 22.83           C  
ANISOU 2377  CZ  ARG C  36     3467   2155   3049    -10    158     19       C  
ATOM   2378  NH1 ARG C  36      36.570  -4.743   4.200  1.00 25.19           N  
ANISOU 2378  NH1 ARG C  36     3781   2461   3330    -43    166     16       N  
ATOM   2379  NH2 ARG C  36      37.205  -2.682   4.920  1.00 24.35           N  
ANISOU 2379  NH2 ARG C  36     3635   2371   3245     -1    157     19       N  
ATOM   2380  N   ALA C  37      43.568  -2.432   4.300  1.00 14.75           N  
ANISOU 2380  N   ALA C  37     2415   1109   2081    104    129      5       N  
ATOM   2381  CA  ALA C  37      44.054  -2.163   5.601  1.00 14.63           C  
ANISOU 2381  CA  ALA C  37     2395   1103   2059    113    122      5       C  
ATOM   2382  C   ALA C  37      43.554  -0.743   5.950  1.00 14.99           C  
ANISOU 2382  C   ALA C  37     2421   1163   2112     97    130      1       C  
ATOM   2383  O   ALA C  37      43.271   0.059   5.070  1.00 16.99           O  
ANISOU 2383  O   ALA C  37     2664   1417   2375     89    138     -2       O  
ATOM   2384  CB  ALA C  37      45.552  -2.177   5.620  1.00 14.70           C  
ANISOU 2384  CB  ALA C  37     2390   1127   2065    137    115     -4       C  
ATOM   2385  N   GLY C  38      43.241  -0.574   7.199  1.00 15.26           N  
ANISOU 2385  N   GLY C  38     2457   1203   2138     93    127      3       N  
ATOM   2386  CA  GLY C  38      42.966   0.831   7.678  1.00 14.55           C  
ANISOU 2386  CA  GLY C  38     2350   1124   2052     82    135     -4       C  
ATOM   2387  C   GLY C  38      42.937   0.869   9.184  1.00 15.31           C  
ANISOU 2387  C   GLY C  38     2445   1233   2137     81    130     -5       C  
ATOM   2388  O   GLY C  38      43.035  -0.198   9.799  1.00 16.13           O  
ANISOU 2388  O   GLY C  38     2563   1336   2229     88    121      3       O  
ATOM   2389  N   ASN C  39      42.743   2.051   9.771  1.00 14.66           N  
ANISOU 2389  N   ASN C  39     2352   1160   2057     72    138    -15       N  
ATOM   2390  CA  ASN C  39      42.661   2.176  11.215  1.00 14.80           C  
ANISOU 2390  CA  ASN C  39     2366   1193   2062     68    134    -18       C  
ATOM   2391  C   ASN C  39      41.285   2.036  11.767  1.00 15.00           C  
ANISOU 2391  C   ASN C  39     2399   1220   2080     59    136     -9       C  
ATOM   2392  O   ASN C  39      41.122   1.972  12.993  1.00 15.65           O  
ANISOU 2392  O   ASN C  39     2479   1317   2150     55    132    -10       O  
ATOM   2393  CB  ASN C  39      43.299   3.445  11.721  1.00 14.03           C  
ANISOU 2393  CB  ASN C  39     2253   1108   1967     60    142    -38       C  
ATOM   2394  CG  ASN C  39      42.618   4.673  11.281  1.00 13.94           C  
ANISOU 2394  CG  ASN C  39     2246   1083   1966     52    158    -44       C  
ATOM   2395  OD1 ASN C  39      41.894   4.695  10.306  1.00 13.94           O  
ANISOU 2395  OD1 ASN C  39     2254   1068   1973     57    163    -35       O  
ATOM   2396  ND2 ASN C  39      42.942   5.795  11.950  1.00 14.18           N  
ANISOU 2396  ND2 ASN C  39     2273   1119   1997     41    169    -63       N  
ATOM   2397  N   MET C  40      40.241   1.981  10.951  1.00 15.82           N  
ANISOU 2397  N   MET C  40     2507   1316   2187     55    141     -3       N  
ATOM   2398  CA  MET C  40      38.906   1.801  11.550  1.00 17.35           C  
ANISOU 2398  CA  MET C  40     2702   1523   2366     44    143      1       C  
ATOM   2399  C   MET C  40      38.830   0.438  12.190  1.00 19.12           C  
ANISOU 2399  C   MET C  40     2943   1747   2575     35    134     13       C  
ATOM   2400  O   MET C  40      39.227  -0.564  11.531  1.00 21.21           O  
ANISOU 2400  O   MET C  40     3224   1993   2840     37    131     22       O  
ATOM   2401  CB  MET C  40      37.808   1.976  10.507  1.00 17.60           C  
ANISOU 2401  CB  MET C  40     2729   1558   2397     42    151      4       C  
ATOM   2402  CG  MET C  40      36.387   1.896  11.037  1.00 17.81           C  
ANISOU 2402  CG  MET C  40     2750   1611   2405     31    154      5       C  
ATOM   2403  SD  MET C  40      35.154   2.034   9.768  1.00 18.82           S  
ANISOU 2403  SD  MET C  40     2865   1759   2525     32    162      6       S  
ATOM   2404  CE  MET C  40      35.176   0.352   9.220  1.00 18.25           C  
ANISOU 2404  CE  MET C  40     2810   1676   2444      6    158     14       C  
ATOM   2405  N   ARG C  41      38.339   0.364  13.429  1.00 21.68           N  
ANISOU 2405  N   ARG C  41     3266   2087   2882     25    132     15       N  
ATOM   2406  CA  ARG C  41      38.276  -0.934  14.119  1.00 24.54           C  
ANISOU 2406  CA  ARG C  41     3651   2444   3225     15    126     29       C  
ATOM   2407  C   ARG C  41      37.128  -1.773  13.518  1.00 27.24           C  
ANISOU 2407  C   ARG C  41     4010   2783   3557     -8    132     36       C  
ATOM   2408  O   ARG C  41      35.999  -1.289  13.396  1.00 28.71           O  
ANISOU 2408  O   ARG C  41     4178   2993   3736    -23    139     30       O  
ATOM   2409  CB  ARG C  41      38.189  -0.745  15.616  1.00 25.12           C  
ANISOU 2409  CB  ARG C  41     3720   2540   3283     11    123     29       C  
ATOM   2410  CG  ARG C  41      39.462  -0.051  16.114  1.00 25.30           C  
ANISOU 2410  CG  ARG C  41     3728   2571   3314     31    117     18       C  
ATOM   2411  CD  ARG C  41      39.690  -0.126  17.594  1.00 25.76           C  
ANISOU 2411  CD  ARG C  41     3782   2652   3353     31    111     20       C  
ATOM   2412  NE  ARG C  41      40.930   0.592  17.987  1.00 26.80           N  
ANISOU 2412  NE  ARG C  41     3893   2800   3488     46    107      5       N  
ATOM   2413  CZ  ARG C  41      40.983   1.882  18.349  1.00 25.98           C  
ANISOU 2413  CZ  ARG C  41     3766   2714   3392     39    114    -17       C  
ATOM   2414  NH1 ARG C  41      39.882   2.600  18.444  1.00 25.20           N  
ANISOU 2414  NH1 ARG C  41     3661   2616   3295     26    124    -25       N  
ATOM   2415  NH2 ARG C  41      42.128   2.450  18.668  1.00 24.92           N  
ANISOU 2415  NH2 ARG C  41     3614   2597   3257     45    113    -33       N  
ATOM   2416  N   LEU C  42      37.457  -2.998  13.109  1.00 30.27           N  
ANISOU 2416  N   LEU C  42     4425   3140   3935    -11    131     48       N  
ATOM   2417  CA  LEU C  42      36.450  -3.983  12.638  1.00 33.65           C  
ANISOU 2417  CA  LEU C  42     4875   3561   4347    -44    140     53       C  
ATOM   2418  C   LEU C  42      36.207  -5.012  13.721  1.00 35.96           C  
ANISOU 2418  C   LEU C  42     5203   3845   4614    -64    141     66       C  
ATOM   2419  O   LEU C  42      37.152  -5.499  14.295  1.00 36.45           O  
ANISOU 2419  O   LEU C  42     5289   3886   4674    -41    133     78       O  
ATOM   2420  CB  LEU C  42      36.942  -4.705  11.382  1.00 35.32           C  
ANISOU 2420  CB  LEU C  42     5108   3742   4569    -38    142     54       C  
ATOM   2421  CG  LEU C  42      37.023  -3.933  10.066  1.00 35.06           C  
ANISOU 2421  CG  LEU C  42     5046   3716   4556    -26    144     43       C  
ATOM   2422  CD1 LEU C  42      37.828  -4.708   9.029  1.00 35.51           C  
ANISOU 2422  CD1 LEU C  42     5126   3742   4624    -14    143     44       C  
ATOM   2423  CD2 LEU C  42      35.642  -3.613   9.528  1.00 34.52           C  
ANISOU 2423  CD2 LEU C  42     4957   3680   4478    -52    153     34       C  
ATOM   2424  N   ARG C  43      34.949  -5.322  14.002  1.00 40.75           N  
ANISOU 2424  N   ARG C  43     5813   4471   5198   -105    150     65       N  
ATOM   2425  CA  ARG C  43      34.616  -6.227  15.107  1.00 43.78           C  
ANISOU 2425  CA  ARG C  43     6232   4849   5553   -131    153     78       C  
ATOM   2426  C   ARG C  43      34.349  -7.588  14.515  1.00 46.07           C  
ANISOU 2426  C   ARG C  43     6573   5103   5828   -162    165     86       C  
ATOM   2427  O   ARG C  43      33.744  -7.675  13.444  1.00 47.38           O  
ANISOU 2427  O   ARG C  43     6730   5275   5995   -184    174     73       O  
ATOM   2428  CB  ARG C  43      33.406  -5.744  15.915  1.00 46.84           C  
ANISOU 2428  CB  ARG C  43     6592   5286   5918   -163    158     70       C  
ATOM   2429  CG  ARG C  43      33.623  -5.809  17.434  1.00 48.65           C  
ANISOU 2429  CG  ARG C  43     6831   5523   6131   -161    153     82       C  
ATOM   2430  CD  ARG C  43      32.428  -6.371  18.184  1.00 50.96           C  
ANISOU 2430  CD  ARG C  43     7135   5840   6386   -214    164     84       C  
ATOM   2431  NE  ARG C  43      31.199  -5.621  17.930  1.00 52.15           N  
ANISOU 2431  NE  ARG C  43     7238   6047   6528   -238    170     62       N  
ATOM   2432  CZ  ARG C  43      29.967  -6.057  18.210  1.00 54.53           C  
ANISOU 2432  CZ  ARG C  43     7538   6384   6794   -291    182     56       C  
ATOM   2433  NH1 ARG C  43      29.760  -7.264  18.755  1.00 54.83           N  
ANISOU 2433  NH1 ARG C  43     7628   6402   6803   -334    192     71       N  
ATOM   2434  NH2 ARG C  43      28.923  -5.279  17.932  1.00 54.83           N  
ANISOU 2434  NH2 ARG C  43     7525   6483   6823   -301    186     34       N  
ATOM   2435  N   GLU C  44      34.786  -8.631  15.225  1.00 47.16           N  
ANISOU 2435  N   GLU C  44     6766   5203   5948   -162    167    105       N  
ATOM   2436  CA  GLU C  44      34.923  -9.979  14.651  1.00 47.28           C  
ANISOU 2436  CA  GLU C  44     6846   5165   5954   -177    179    115       C  
ATOM   2437  C   GLU C  44      33.643 -10.398  13.939  1.00 44.66           C  
ANISOU 2437  C   GLU C  44     6518   4844   5604   -241    197     99       C  
ATOM   2438  O   GLU C  44      32.546 -10.276  14.469  1.00 46.13           O  
ANISOU 2438  O   GLU C  44     6689   5070   5767   -288    205     93       O  
ATOM   2439  CB  GLU C  44      35.343 -11.025  15.692  1.00 50.38           C  
ANISOU 2439  CB  GLU C  44     7304   5516   6321   -171    181    141       C  
ATOM   2440  CG  GLU C  44      36.014 -12.234  15.056  1.00 51.66           C  
ANISOU 2440  CG  GLU C  44     7536   5612   6481   -154    189    152       C  
ATOM   2441  CD  GLU C  44      36.784 -13.086  16.052  1.00 53.98           C  
ANISOU 2441  CD  GLU C  44     7892   5864   6754   -119    186    182       C  
ATOM   2442  OE1 GLU C  44      36.140 -13.744  16.903  1.00 54.73           O  
ANISOU 2442  OE1 GLU C  44     8033   5946   6817   -158    199    197       O  
ATOM   2443  OE2 GLU C  44      38.035 -13.100  15.969  1.00 54.10           O  
ANISOU 2443  OE2 GLU C  44     7909   5862   6780    -52    172    190       O  
ATOM   2444  N   ASP C  45      33.811 -10.835  12.704  1.00 43.35           N  
ANISOU 2444  N   ASP C  45     6368   4653   5450   -243    204     90       N  
ATOM   2445  CA  ASP C  45      32.712 -10.980  11.771  1.00 43.51           C  
ANISOU 2445  CA  ASP C  45     6373   4699   5457   -297    219     69       C  
ATOM   2446  C   ASP C  45      33.308 -11.768  10.616  1.00 44.75           C  
ANISOU 2446  C   ASP C  45     6570   4807   5626   -288    226     66       C  
ATOM   2447  O   ASP C  45      33.579 -11.242   9.537  1.00 45.31           O  
ANISOU 2447  O   ASP C  45     6604   4890   5720   -266    220     53       O  
ATOM   2448  CB  ASP C  45      32.211  -9.595  11.327  1.00 43.48           C  
ANISOU 2448  CB  ASP C  45     6288   4762   5468   -285    210     52       C  
ATOM   2449  CG  ASP C  45      30.949  -9.656  10.475  1.00 43.32           C  
ANISOU 2449  CG  ASP C  45     6243   4789   5428   -338    225     29       C  
ATOM   2450  OD1 ASP C  45      30.297 -10.727  10.385  1.00 44.78           O  
ANISOU 2450  OD1 ASP C  45     6467   4963   5582   -398    243     23       O  
ATOM   2451  OD2 ASP C  45      30.603  -8.601   9.910  1.00 43.25           O  
ANISOU 2451  OD2 ASP C  45     6172   4829   5428   -319    218     17       O  
ATOM   2452  N   LYS C  46      33.512 -13.050  10.877  1.00 46.16           N  
ANISOU 2452  N   LYS C  46     6827   4925   5786   -306    239     78       N  
ATOM   2453  CA  LYS C  46      34.283 -13.928   9.998  1.00 46.01           C  
ANISOU 2453  CA  LYS C  46     6859   4845   5776   -286    245     78       C  
ATOM   2454  C   LYS C  46      33.503 -14.383   8.760  1.00 46.07           C  
ANISOU 2454  C   LYS C  46     6871   4859   5775   -341    265     52       C  
ATOM   2455  O   LYS C  46      33.895 -15.360   8.098  1.00 46.86           O  
ANISOU 2455  O   LYS C  46     7028   4902   5872   -344    277     49       O  
ATOM   2456  CB  LYS C  46      34.833 -15.120  10.794  1.00 46.30           C  
ANISOU 2456  CB  LYS C  46     6988   4811   5794   -274    254    103       C  
ATOM   2457  CG  LYS C  46      35.799 -14.730  11.918  1.00 46.70           C  
ANISOU 2457  CG  LYS C  46     7033   4859   5852   -208    233    128       C  
ATOM   2458  CD  LYS C  46      35.990 -15.861  12.925  1.00 46.59           C  
ANISOU 2458  CD  LYS C  46     7108   4787   5806   -208    244    155       C  
ATOM   2459  CE  LYS C  46      34.846 -15.923  13.931  1.00 46.25           C  
ANISOU 2459  CE  LYS C  46     7071   4768   5731   -274    256    160       C  
ATOM   2460  NZ  LYS C  46      34.590 -17.311  14.401  1.00 46.81           N  
ANISOU 2460  NZ  LYS C  46     7247   4772   5765   -310    281    178       N  
ATOM   2461  N   ASP C  47      32.384 -13.715   8.475  1.00 43.85           N  
ANISOU 2461  N   ASP C  47     6528   4647   5483   -385    268     33       N  
ATOM   2462  CA  ASP C  47      31.844 -13.629   7.116  1.00 42.46           C  
ANISOU 2462  CA  ASP C  47     6320   4504   5308   -414    276      6       C  
ATOM   2463  C   ASP C  47      31.223 -12.229   6.918  1.00 37.13           C  
ANISOU 2463  C   ASP C  47     5552   3914   4640   -403    263     -3       C  
ATOM   2464  O   ASP C  47      30.003 -12.048   6.933  1.00 38.01           O  
ANISOU 2464  O   ASP C  47     5630   4087   4723   -454    273    -19       O  
ATOM   2465  CB  ASP C  47      30.844 -14.761   6.821  1.00 44.99           C  
ANISOU 2465  CB  ASP C  47     6686   4817   5589   -501    306    -11       C  
ATOM   2466  CG  ASP C  47      31.521 -16.058   6.418  1.00 46.94           C  
ANISOU 2466  CG  ASP C  47     7023   4976   5835   -504    322     -9       C  
ATOM   2467  OD1 ASP C  47      32.640 -16.031   5.875  1.00 47.75           O  
ANISOU 2467  OD1 ASP C  47     7134   5040   5968   -441    310     -2       O  
ATOM   2468  OD2 ASP C  47      30.927 -17.130   6.654  1.00 50.87           O  
ANISOU 2468  OD2 ASP C  47     7587   5442   6299   -572    349    -14       O  
ATOM   2469  N   PRO C  48      32.075 -11.232   6.733  1.00 34.79           N  
ANISOU 2469  N   PRO C  48     5217   3623   4379   -335    242      4       N  
ATOM   2470  CA  PRO C  48      31.516  -9.900   6.636  1.00 31.68           C  
ANISOU 2470  CA  PRO C  48     4748   3299   3990   -320    232     -2       C  
ATOM   2471  C   PRO C  48      31.094  -9.508   5.212  1.00 30.17           C  
ANISOU 2471  C   PRO C  48     4512   3148   3799   -324    235    -21       C  
ATOM   2472  O   PRO C  48      31.283 -10.279   4.251  1.00 32.04           O  
ANISOU 2472  O   PRO C  48     4775   3360   4036   -341    245    -31       O  
ATOM   2473  CB  PRO C  48      32.664  -9.035   7.128  1.00 33.17           C  
ANISOU 2473  CB  PRO C  48     4922   3468   4212   -252    212     13       C  
ATOM   2474  CG  PRO C  48      33.904  -9.792   6.748  1.00 33.49           C  
ANISOU 2474  CG  PRO C  48     5010   3443   4270   -223    210     22       C  
ATOM   2475  CD  PRO C  48      33.530 -11.222   6.508  1.00 34.28           C  
ANISOU 2475  CD  PRO C  48     5171   3507   4346   -272    229     17       C  
ATOM   2476  N   ALA C  49      30.504  -8.318   5.104  1.00 28.38           N  
ANISOU 2476  N   ALA C  49     4223   2986   3572   -306    228    -26       N  
ATOM   2477  CA  ALA C  49      30.375  -7.670   3.802  1.00 25.99           C  
ANISOU 2477  CA  ALA C  49     3877   2719   3277   -286    226    -36       C  
ATOM   2478  C   ALA C  49      31.755  -7.449   3.216  1.00 25.47           C  
ANISOU 2478  C   ALA C  49     3823   2602   3249   -235    215    -26       C  
ATOM   2479  O   ALA C  49      32.765  -7.356   3.945  1.00 26.39           O  
ANISOU 2479  O   ALA C  49     3964   2673   3388   -202    205    -11       O  
ATOM   2480  CB  ALA C  49      29.642  -6.349   3.900  1.00 25.75           C  
ANISOU 2480  CB  ALA C  49     3786   2757   3240   -260    219    -38       C  
ATOM   2481  N   LYS C  50      31.789  -7.333   1.891  1.00 24.66           N  
ANISOU 2481  N   LYS C  50     3701   2515   3151   -229    217    -35       N  
ATOM   2482  CA  LYS C  50      33.040  -7.210   1.154  1.00 26.60           C  
ANISOU 2482  CA  LYS C  50     3957   2721   3428   -188    210    -29       C  
ATOM   2483  C   LYS C  50      33.030  -6.000   0.205  1.00 24.76           C  
ANISOU 2483  C   LYS C  50     3674   2526   3206   -153    204    -29       C  
ATOM   2484  O   LYS C  50      31.971  -5.593  -0.263  1.00 23.97           O  
ANISOU 2484  O   LYS C  50     3537   2486   3084   -165    209    -37       O  
ATOM   2485  CB  LYS C  50      33.282  -8.505   0.380  1.00 26.88           C  
ANISOU 2485  CB  LYS C  50     4032   2722   3458   -217    221    -41       C  
ATOM   2486  CG  LYS C  50      33.286  -9.768   1.231  1.00 31.36           C  
ANISOU 2486  CG  LYS C  50     4661   3242   4011   -252    230    -40       C  
ATOM   2487  CD  LYS C  50      33.563 -10.993   0.413  1.00 32.83           C  
ANISOU 2487  CD  LYS C  50     4893   3388   4192   -276    244    -53       C  
ATOM   2488  CE  LYS C  50      33.819 -12.239   1.239  1.00 34.60           C  
ANISOU 2488  CE  LYS C  50     5193   3546   4405   -296    254    -47       C  
ATOM   2489  NZ  LYS C  50      35.227 -12.309   1.731  1.00 35.19           N  
ANISOU 2489  NZ  LYS C  50     5298   3565   4505   -234    240    -28       N  
ATOM   2490  N   MET C  51      34.210  -5.397  -0.052  1.00 24.13           N  
ANISOU 2490  N   MET C  51     3594   2417   3156   -108    194    -19       N  
ATOM   2491  CA  MET C  51      34.402  -4.549  -1.228  1.00 25.61           C  
ANISOU 2491  CA  MET C  51     3750   2627   3352    -82    193    -19       C  
ATOM   2492  C   MET C  51      35.082  -5.437  -2.268  1.00 23.35           C  
ANISOU 2492  C   MET C  51     3482   2315   3072    -89    196    -28       C  
ATOM   2493  O   MET C  51      36.146  -6.040  -2.019  1.00 24.22           O  
ANISOU 2493  O   MET C  51     3625   2376   3199    -78    192    -26       O  
ATOM   2494  CB  MET C  51      35.212  -3.261  -0.950  1.00 27.35           C  
ANISOU 2494  CB  MET C  51     3958   2835   3597    -36    184     -6       C  
ATOM   2495  CG  MET C  51      35.388  -2.365  -2.169  1.00 27.95           C  
ANISOU 2495  CG  MET C  51     4009   2931   3680    -11    185     -3       C  
ATOM   2496  SD  MET C  51      35.701  -0.567  -2.002  1.00 31.95           S  
ANISOU 2496  SD  MET C  51     4500   3439   4200     31    184     10       S  
ATOM   2497  CE  MET C  51      37.456  -0.357  -2.233  1.00 32.75           C  
ANISOU 2497  CE  MET C  51     4617   3495   4331     48    180     12       C  
ATOM   2498  N   VAL C  52      34.410  -5.583  -3.394  1.00 22.12           N  
ANISOU 2498  N   VAL C  52     3306   2198   2900   -107    203    -39       N  
ATOM   2499  CA  VAL C  52      34.763  -6.554  -4.386  1.00 22.26           C  
ANISOU 2499  CA  VAL C  52     3340   2200   2916   -125    210    -53       C  
ATOM   2500  C   VAL C  52      35.696  -5.917  -5.413  1.00 20.90           C  
ANISOU 2500  C   VAL C  52     3150   2025   2763    -88    204    -49       C  
ATOM   2501  O   VAL C  52      36.688  -6.510  -5.795  1.00 18.81           O  
ANISOU 2501  O   VAL C  52     2909   1724   2513    -80    203    -54       O  
ATOM   2502  CB  VAL C  52      33.522  -7.080  -5.113  1.00 23.35           C  
ANISOU 2502  CB  VAL C  52     3461   2390   3020   -171    223    -72       C  
ATOM   2503  CG1 VAL C  52      33.902  -7.993  -6.268  1.00 24.66           C  
ANISOU 2503  CG1 VAL C  52     3643   2542   3184   -189    231    -90       C  
ATOM   2504  CG2 VAL C  52      32.547  -7.730  -4.141  1.00 23.78           C  
ANISOU 2504  CG2 VAL C  52     3532   2453   3049   -217    231    -80       C  
ATOM   2505  N   ALA C  53      35.319  -4.712  -5.870  1.00 19.68           N  
ANISOU 2505  N   ALA C  53     2957   1912   2606    -66    202    -40       N  
ATOM   2506  CA  ALA C  53      36.028  -3.999  -6.906  1.00 18.55           C  
ANISOU 2506  CA  ALA C  53     2797   1775   2476    -37    199    -34       C  
ATOM   2507  C   ALA C  53      35.644  -2.500  -6.897  1.00 17.65           C  
ANISOU 2507  C   ALA C  53     2656   1690   2360     -5    198    -16       C  
ATOM   2508  O   ALA C  53      34.668  -2.073  -6.268  1.00 17.50           O  
ANISOU 2508  O   ALA C  53     2623   1698   2325     -5    199    -12       O  
ATOM   2509  CB  ALA C  53      35.756  -4.599  -8.260  1.00 19.10           C  
ANISOU 2509  CB  ALA C  53     2853   1872   2529    -56    206    -49       C  
ATOM   2510  N   THR C  54      36.384  -1.740  -7.654  1.00 17.06           N  
ANISOU 2510  N   THR C  54     2573   1610   2297     20    197     -7       N  
ATOM   2511  CA  THR C  54      36.051  -0.315  -7.835  1.00 16.97           C  
ANISOU 2511  CA  THR C  54     2545   1620   2281     52    199      9       C  
ATOM   2512  C   THR C  54      36.283  -0.003  -9.304  1.00 17.79           C  
ANISOU 2512  C   THR C  54     2634   1746   2379     63    203     13       C  
ATOM   2513  O   THR C  54      37.314  -0.421  -9.892  1.00 17.97           O  
ANISOU 2513  O   THR C  54     2665   1746   2416     57    202      7       O  
ATOM   2514  CB  THR C  54      36.954   0.515  -6.988  1.00 16.40           C  
ANISOU 2514  CB  THR C  54     2492   1506   2233     72    197     20       C  
ATOM   2515  OG1 THR C  54      36.927   0.105  -5.637  1.00 17.33           O  
ANISOU 2515  OG1 THR C  54     2624   1601   2357     60    192     15       O  
ATOM   2516  CG2 THR C  54      36.506   2.029  -7.020  1.00 16.26           C  
ANISOU 2516  CG2 THR C  54     2469   1500   2209    105    203     38       C  
ATOM   2517  N   ILE C  55      35.333   0.719  -9.889  1.00 18.16           N  
ANISOU 2517  N   ILE C  55     2659   1840   2401     83    208     24       N  
ATOM   2518  CA  ILE C  55      35.389   1.193 -11.280  1.00 18.41           C  
ANISOU 2518  CA  ILE C  55     2674   1900   2419    100    213     33       C  
ATOM   2519  C   ILE C  55      35.676   2.696 -11.300  1.00 19.31           C  
ANISOU 2519  C   ILE C  55     2802   1997   2539    141    218     58       C  
ATOM   2520  O   ILE C  55      34.918   3.513 -10.756  1.00 18.55           O  
ANISOU 2520  O   ILE C  55     2706   1912   2430    168    220     71       O  
ATOM   2521  CB  ILE C  55      34.132   0.828 -12.093  1.00 19.01           C  
ANISOU 2521  CB  ILE C  55     2715   2050   2457     95    215     25       C  
ATOM   2522  CG1 ILE C  55      33.925  -0.689 -12.122  1.00 19.17           C  
ANISOU 2522  CG1 ILE C  55     2731   2079   2471     45    215     -2       C  
ATOM   2523  CG2 ILE C  55      34.211   1.411 -13.479  1.00 19.37           C  
ANISOU 2523  CG2 ILE C  55     2744   2126   2486    118    220     38       C  
ATOM   2524  CD1 ILE C  55      32.624  -1.183 -12.731  1.00 19.42           C  
ANISOU 2524  CD1 ILE C  55     2726   2189   2460     25    219    -17       C  
ATOM   2525  N   TYR C  56      36.781   3.062 -11.918  1.00 18.55           N  
ANISOU 2525  N   TYR C  56     2718   1871   2458    143    221     64       N  
ATOM   2526  CA  TYR C  56      37.190   4.484 -12.023  1.00 19.71           C  
ANISOU 2526  CA  TYR C  56     2887   1993   2608    173    230     88       C  
ATOM   2527  C   TYR C  56      36.995   4.957 -13.462  1.00 21.63           C  
ANISOU 2527  C   TYR C  56     3119   2269   2828    193    237    103       C  
ATOM   2528  O   TYR C  56      37.836   4.646 -14.301  1.00 21.25           O  
ANISOU 2528  O   TYR C  56     3069   2218   2786    176    238     98       O  
ATOM   2529  CB  TYR C  56      38.661   4.586 -11.656  1.00 19.39           C  
ANISOU 2529  CB  TYR C  56     2869   1899   2597    155    231     82       C  
ATOM   2530  CG  TYR C  56      38.917   4.382 -10.217  1.00 19.33           C  
ANISOU 2530  CG  TYR C  56     2874   1859   2608    143    225     71       C  
ATOM   2531  CD1 TYR C  56      39.126   3.128  -9.709  1.00 18.95           C  
ANISOU 2531  CD1 TYR C  56     2819   1809   2570    119    215     51       C  
ATOM   2532  CD2 TYR C  56      38.970   5.435  -9.342  1.00 19.57           C  
ANISOU 2532  CD2 TYR C  56     2927   1861   2646    157    232     81       C  
ATOM   2533  CE1 TYR C  56      39.382   2.931  -8.365  1.00 18.94           C  
ANISOU 2533  CE1 TYR C  56     2830   1780   2584    111    209     44       C  
ATOM   2534  CE2 TYR C  56      39.210   5.240  -8.017  1.00 20.01           C  
ANISOU 2534  CE2 TYR C  56     2992   1893   2717    146    227     70       C  
ATOM   2535  CZ  TYR C  56      39.442   3.972  -7.521  1.00 18.76           C  
ANISOU 2535  CZ  TYR C  56     2823   1736   2567    124    214     52       C  
ATOM   2536  OH  TYR C  56      39.674   3.828  -6.161  1.00 19.68           O  
ANISOU 2536  OH  TYR C  56     2950   1831   2696    116    209     45       O  
ATOM   2537  N   GLU C  57      35.918   5.705 -13.753  1.00 22.85           N  
ANISOU 2537  N   GLU C  57     3267   2460   2953    232    242    122       N  
ATOM   2538  CA  GLU C  57      35.589   6.173 -15.093  1.00 24.84           C  
ANISOU 2538  CA  GLU C  57     3508   2752   3176    258    249    141       C  
ATOM   2539  C   GLU C  57      36.093   7.600 -15.226  1.00 25.18           C  
ANISOU 2539  C   GLU C  57     3594   2751   3222    289    263    170       C  
ATOM   2540  O   GLU C  57      35.577   8.500 -14.576  1.00 24.64           O  
ANISOU 2540  O   GLU C  57     3548   2666   3146    324    270    185       O  
ATOM   2541  CB  GLU C  57      34.081   6.167 -15.357  1.00 28.16           C  
ANISOU 2541  CB  GLU C  57     3895   3246   3555    289    247    146       C  
ATOM   2542  CG  GLU C  57      33.322   4.847 -15.253  1.00 30.45           C  
ANISOU 2542  CG  GLU C  57     4144   3591   3833    255    237    116       C  
ATOM   2543  CD  GLU C  57      31.799   5.036 -15.088  1.00 32.48           C  
ANISOU 2543  CD  GLU C  57     4369   3922   4048    286    235    118       C  
ATOM   2544  OE1 GLU C  57      31.316   6.192 -15.042  1.00 35.59           O  
ANISOU 2544  OE1 GLU C  57     4774   4325   4423    343    241    144       O  
ATOM   2545  OE2 GLU C  57      31.046   4.038 -14.995  1.00 33.14           O  
ANISOU 2545  OE2 GLU C  57     4417   4059   4113    254    230     93       O  
ATOM   2546  N   LEU C  58      37.154   7.801 -15.993  1.00 25.40           N  
ANISOU 2546  N   LEU C  58     3636   2754   3258    273    270    175       N  
ATOM   2547  CA  LEU C  58      37.682   9.144 -16.209  1.00 25.62           C  
ANISOU 2547  CA  LEU C  58     3711   2738   3285    293    288    202       C  
ATOM   2548  C   LEU C  58      36.719   9.944 -17.091  1.00 26.61           C  
ANISOU 2548  C   LEU C  58     3841   2900   3370    349    297    234       C  
ATOM   2549  O   LEU C  58      36.231   9.462 -18.097  1.00 25.70           O  
ANISOU 2549  O   LEU C  58     3690   2845   3229    357    291    236       O  
ATOM   2550  CB  LEU C  58      39.056   9.100 -16.866  1.00 24.76           C  
ANISOU 2550  CB  LEU C  58     3613   2603   3191    256    294    197       C  
ATOM   2551  CG  LEU C  58      39.728  10.488 -17.109  1.00 24.92           C  
ANISOU 2551  CG  LEU C  58     3687   2573   3207    263    317    222       C  
ATOM   2552  CD1 LEU C  58      40.247  11.047 -15.792  1.00 24.26           C  
ANISOU 2552  CD1 LEU C  58     3640   2428   3148    247    324    214       C  
ATOM   2553  CD2 LEU C  58      40.864  10.390 -18.086  1.00 25.52           C  
ANISOU 2553  CD2 LEU C  58     3762   2648   3284    228    323    219       C  
ATOM   2554  N   LYS C  59      36.498  11.190 -16.712  1.00 27.39           N  
ANISOU 2554  N   LYS C  59     3987   2960   3461    388    312    259       N  
ATOM   2555  CA  LYS C  59      35.489  12.046 -17.333  1.00 28.38           C  
ANISOU 2555  CA  LYS C  59     4123   3114   3543    456    320    292       C  
ATOM   2556  C   LYS C  59      36.227  13.141 -18.069  1.00 28.64           C  
ANISOU 2556  C   LYS C  59     4214   3099   3569    466    343    323       C  
ATOM   2557  O   LYS C  59      37.388  13.434 -17.749  1.00 26.95           O  
ANISOU 2557  O   LYS C  59     4035   2819   3383    422    354    316       O  
ATOM   2558  CB  LYS C  59      34.557  12.621 -16.254  1.00 28.85           C  
ANISOU 2558  CB  LYS C  59     4199   3167   3596    502    322    297       C  
ATOM   2559  CG  LYS C  59      33.764  11.524 -15.553  1.00 29.25           C  
ANISOU 2559  CG  LYS C  59     4191   3273   3648    487    301    267       C  
ATOM   2560  CD  LYS C  59      32.667  10.955 -16.464  1.00 31.05           C  
ANISOU 2560  CD  LYS C  59     4362   3600   3833    513    291    269       C  
ATOM   2561  CE  LYS C  59      32.606   9.429 -16.389  1.00 30.84           C  
ANISOU 2561  CE  LYS C  59     4279   3619   3818    454    273    231       C  
ATOM   2562  NZ  LYS C  59      31.434   8.866 -17.116  1.00 32.23           N  
ANISOU 2562  NZ  LYS C  59     4398   3899   3949    472    265    226       N  
ATOM   2563  N   GLU C  60      35.556  13.751 -19.052  1.00 32.85           N  
ANISOU 2563  N   GLU C  60     4755   3665   4061    523    351    356       N  
ATOM   2564  CA  GLU C  60      36.124  14.865 -19.837  1.00 34.80           C  
ANISOU 2564  CA  GLU C  60     5064   3864   4291    539    376    392       C  
ATOM   2565  C   GLU C  60      36.644  16.001 -18.948  1.00 33.92           C  
ANISOU 2565  C   GLU C  60     5033   3657   4198    538    399    401       C  
ATOM   2566  O   GLU C  60      37.696  16.603 -19.230  1.00 34.21           O  
ANISOU 2566  O   GLU C  60     5120   3633   4243    502    419    410       O  
ATOM   2567  CB  GLU C  60      35.101  15.404 -20.858  1.00 36.89           C  
ANISOU 2567  CB  GLU C  60     5330   4183   4502    617    380    430       C  
ATOM   2568  CG  GLU C  60      35.630  16.426 -21.852  1.00 38.52           C  
ANISOU 2568  CG  GLU C  60     5599   4349   4685    634    405    470       C  
ATOM   2569  CD  GLU C  60      34.777  16.553 -23.130  1.00 40.54           C  
ANISOU 2569  CD  GLU C  60     5833   4683   4886    699    403    503       C  
ATOM   2570  OE1 GLU C  60      33.612  16.084 -23.147  1.00 42.30           O  
ANISOU 2570  OE1 GLU C  60     5998   4990   5082    744    385    498       O  
ATOM   2571  OE2 GLU C  60      35.258  17.144 -24.123  1.00 38.63           O  
ANISOU 2571  OE2 GLU C  60     5631   4423   4624    704    421    534       O  
ATOM   2572  N   ASP C  61      35.954  16.261 -17.845  1.00 32.83           N  
ANISOU 2572  N   ASP C  61     4904   3506   4064    570    396    395       N  
ATOM   2573  CA  ASP C  61      36.403  17.308 -16.936  1.00 32.47           C  
ANISOU 2573  CA  ASP C  61     4933   3369   4034    567    419    399       C  
ATOM   2574  C   ASP C  61      37.543  16.906 -15.990  1.00 31.57           C  
ANISOU 2574  C   ASP C  61     4818   3210   3967    486    417    362       C  
ATOM   2575  O   ASP C  61      37.882  17.660 -15.091  1.00 31.91           O  
ANISOU 2575  O   ASP C  61     4913   3186   4023    476    434    357       O  
ATOM   2576  CB  ASP C  61      35.212  17.906 -16.186  1.00 32.20           C  
ANISOU 2576  CB  ASP C  61     4917   3337   3981    642    421    410       C  
ATOM   2577  CG  ASP C  61      34.665  17.005 -15.107  1.00 31.62           C  
ANISOU 2577  CG  ASP C  61     4782   3304   3926    629    396    376       C  
ATOM   2578  OD1 ASP C  61      35.103  15.840 -14.974  1.00 29.75           O  
ANISOU 2578  OD1 ASP C  61     4490   3098   3715    569    377    345       O  
ATOM   2579  OD2 ASP C  61      33.769  17.454 -14.382  1.00 32.46           O  
ANISOU 2579  OD2 ASP C  61     4899   3414   4019    683    398    379       O  
ATOM   2580  N   LYS C  62      38.094  15.699 -16.189  1.00 31.39           N  
ANISOU 2580  N   LYS C  62     4734   3228   3964    431    397    334       N  
ATOM   2581  CA  LYS C  62      39.255  15.131 -15.491  1.00 29.67           C  
ANISOU 2581  CA  LYS C  62     4503   2985   3785    357    391    299       C  
ATOM   2582  C   LYS C  62      38.973  14.485 -14.115  1.00 27.50           C  
ANISOU 2582  C   LYS C  62     4198   2715   3535    346    374    269       C  
ATOM   2583  O   LYS C  62      39.907  13.931 -13.479  1.00 27.58           O  
ANISOU 2583  O   LYS C  62     4193   2711   3574    291    367    240       O  
ATOM   2584  CB  LYS C  62      40.444  16.101 -15.434  1.00 30.68           C  
ANISOU 2584  CB  LYS C  62     4694   3040   3920    316    420    302       C  
ATOM   2585  CG  LYS C  62      41.151  16.278 -16.776  1.00 31.68           C  
ANISOU 2585  CG  LYS C  62     4833   3172   4032    294    432    318       C  
ATOM   2586  CD  LYS C  62      41.418  14.883 -17.364  1.00 31.76           C  
ANISOU 2586  CD  LYS C  62     4766   3250   4051    266    405    296       C  
ATOM   2587  CE  LYS C  62      42.552  14.832 -18.350  1.00 32.28           C  
ANISOU 2587  CE  LYS C  62     4831   3320   4113    219    415    293       C  
ATOM   2588  NZ  LYS C  62      42.676  13.434 -18.852  1.00 31.85           N  
ANISOU 2588  NZ  LYS C  62     4704   3331   4066    201    388    270       N  
ATOM   2589  N   SER C  63      37.702  14.467 -13.723  1.00 26.18           N  
ANISOU 2589  N   SER C  63     4015   2577   3352    399    365    276       N  
ATOM   2590  CA  SER C  63      37.292  13.847 -12.458  1.00 25.14           C  
ANISOU 2590  CA  SER C  63     3855   2458   3239    390    348    250       C  
ATOM   2591  C   SER C  63      36.980  12.390 -12.796  1.00 23.46           C  
ANISOU 2591  C   SER C  63     3572   2313   3027    371    323    232       C  
ATOM   2592  O   SER C  63      36.892  12.033 -13.990  1.00 22.63           O  
ANISOU 2592  O   SER C  63     3444   2248   2904    375    320    241       O  
ATOM   2593  CB  SER C  63      36.057  14.556 -11.884  1.00 26.16           C  
ANISOU 2593  CB  SER C  63     4001   2592   3346    455    353    264       C  
ATOM   2594  OG  SER C  63      34.968  14.395 -12.756  1.00 26.86           O  
ANISOU 2594  OG  SER C  63     4059   2747   3399    507    346    283       O  
ATOM   2595  N   TYR C  64      36.868  11.540 -11.767  1.00 22.86           N  
ANISOU 2595  N   TYR C  64     3466   2247   2969    346    307    205       N  
ATOM   2596  CA  TYR C  64      36.450  10.160 -11.990  1.00 21.96           C  
ANISOU 2596  CA  TYR C  64     3297   2193   2854    327    286    187       C  
ATOM   2597  C   TYR C  64      35.070   9.967 -11.382  1.00 22.67           C  
ANISOU 2597  C   TYR C  64     3361   2327   2923    358    278    185       C  
ATOM   2598  O   TYR C  64      34.831  10.373 -10.261  1.00 23.56           O  
ANISOU 2598  O   TYR C  64     3491   2417   3044    368    280    181       O  
ATOM   2599  CB  TYR C  64      37.363   9.132 -11.298  1.00 21.10           C  
ANISOU 2599  CB  TYR C  64     3173   2066   2777    272    274    158       C  
ATOM   2600  CG  TYR C  64      38.711   8.869 -11.889  1.00 20.43           C  
ANISOU 2600  CG  TYR C  64     3092   1959   2709    234    277    150       C  
ATOM   2601  CD1 TYR C  64      38.854   8.122 -13.048  1.00 20.12           C  
ANISOU 2601  CD1 TYR C  64     3026   1956   2662    223    271    147       C  
ATOM   2602  CD2 TYR C  64      39.855   9.344 -11.283  1.00 20.45           C  
ANISOU 2602  CD2 TYR C  64     3124   1912   2734    208    285    143       C  
ATOM   2603  CE1 TYR C  64      40.098   7.874 -13.558  1.00 18.79           C  
ANISOU 2603  CE1 TYR C  64     2858   1773   2506    191    272    137       C  
ATOM   2604  CE2 TYR C  64      41.122   9.102 -11.805  1.00 19.65           C  
ANISOU 2604  CE2 TYR C  64     3020   1801   2643    173    287    132       C  
ATOM   2605  CZ  TYR C  64      41.215   8.391 -12.968  1.00 19.13           C  
ANISOU 2605  CZ  TYR C  64     2928   1771   2569    168    280    131       C  
ATOM   2606  OH  TYR C  64      42.492   8.168 -13.417  1.00 18.79           O  
ANISOU 2606  OH  TYR C  64     2880   1721   2535    135    282    118       O  
ATOM   2607  N   ASN C  65      34.202   9.298 -12.112  1.00 23.74           N  
ANISOU 2607  N   ASN C  65     3454   2533   3033    368    269    183       N  
ATOM   2608  CA  ASN C  65      32.982   8.699 -11.598  1.00 24.09           C  
ANISOU 2608  CA  ASN C  65     3458   2636   3056    376    258    170       C  
ATOM   2609  C   ASN C  65      33.455   7.374 -11.015  1.00 22.67           C  
ANISOU 2609  C   ASN C  65     3260   2449   2902    314    246    140       C  
ATOM   2610  O   ASN C  65      34.029   6.555 -11.713  1.00 23.84           O  
ANISOU 2610  O   ASN C  65     3396   2602   3059    280    241    130       O  
ATOM   2611  CB  ASN C  65      32.022   8.464 -12.759  1.00 26.07           C  
ANISOU 2611  CB  ASN C  65     3669   2970   3264    401    255    177       C  
ATOM   2612  CG  ASN C  65      30.575   8.338 -12.336  1.00 28.84           C  
ANISOU 2612  CG  ASN C  65     3983   3395   3579    429    249    170       C  
ATOM   2613  OD1 ASN C  65      30.205   7.392 -11.639  1.00 28.04           O  
ANISOU 2613  OD1 ASN C  65     3855   3317   3481    390    240    144       O  
ATOM   2614  ND2 ASN C  65      29.722   9.282 -12.790  1.00 31.67           N  
ANISOU 2614  ND2 ASN C  65     4339   3794   3898    498    256    193       N  
ATOM   2615  N   VAL C  66      33.315   7.222  -9.709  1.00 22.15           N  
ANISOU 2615  N   VAL C  66     3200   2364   2850    302    241    128       N  
ATOM   2616  CA  VAL C  66      33.812   6.068  -8.971  1.00 21.81           C  
ANISOU 2616  CA  VAL C  66     3150   2302   2831    250    231    104       C  
ATOM   2617  C   VAL C  66      32.646   5.159  -8.514  1.00 22.16           C  
ANISOU 2617  C   VAL C  66     3161   2405   2854    234    223     87       C  
ATOM   2618  O   VAL C  66      31.766   5.596  -7.721  1.00 22.95           O  
ANISOU 2618  O   VAL C  66     3254   2526   2938    256    224     88       O  
ATOM   2619  CB  VAL C  66      34.636   6.534  -7.748  1.00 21.85           C  
ANISOU 2619  CB  VAL C  66     3190   2244   2867    242    233    102       C  
ATOM   2620  CG1 VAL C  66      35.084   5.326  -6.886  1.00 21.84           C  
ANISOU 2620  CG1 VAL C  66     3183   2227   2886    197    222     80       C  
ATOM   2621  CG2 VAL C  66      35.840   7.324  -8.194  1.00 22.37           C  
ANISOU 2621  CG2 VAL C  66     3287   2258   2951    244    243    112       C  
ATOM   2622  N   THR C  67      32.633   3.941  -9.015  1.00 21.38           N  
ANISOU 2622  N   THR C  67     3042   2330   2751    195    218     70       N  
ATOM   2623  CA  THR C  67      31.637   2.941  -8.637  1.00 22.24           C  
ANISOU 2623  CA  THR C  67     3123   2489   2838    164    214     50       C  
ATOM   2624  C   THR C  67      32.288   1.946  -7.728  1.00 22.02           C  
ANISOU 2624  C   THR C  67     3116   2413   2836    119    209     34       C  
ATOM   2625  O   THR C  67      33.153   1.138  -8.171  1.00 21.61           O  
ANISOU 2625  O   THR C  67     3076   2332   2803     91    208     25       O  
ATOM   2626  CB  THR C  67      31.115   2.218  -9.855  1.00 22.50           C  
ANISOU 2626  CB  THR C  67     3124   2582   2842    146    215     39       C  
ATOM   2627  OG1 THR C  67      30.619   3.169 -10.793  1.00 24.15           O  
ANISOU 2627  OG1 THR C  67     3315   2837   3025    194    219     57       O  
ATOM   2628  CG2 THR C  67      30.023   1.180  -9.521  1.00 22.38           C  
ANISOU 2628  CG2 THR C  67     3081   2625   2797    104    215     14       C  
ATOM   2629  N   LYS C  68      31.868   1.952  -6.472  1.00 21.78           N  
ANISOU 2629  N   LYS C  68     3090   2378   2806    114    207     30       N  
ATOM   2630  CA  LYS C  68      32.294   0.909  -5.541  1.00 22.42           C  
ANISOU 2630  CA  LYS C  68     3190   2422   2904     72    203     16       C  
ATOM   2631  C   LYS C  68      31.316  -0.250  -5.619  1.00 22.65           C  
ANISOU 2631  C   LYS C  68     3201   2499   2904     28    205     -3       C  
ATOM   2632  O   LYS C  68      30.101  -0.064  -5.486  1.00 23.63           O  
ANISOU 2632  O   LYS C  68     3296   2687   2994     29    207     -7       O  
ATOM   2633  CB  LYS C  68      32.398   1.465  -4.112  1.00 23.39           C  
ANISOU 2633  CB  LYS C  68     3330   2516   3041     83    200     21       C  
ATOM   2634  CG  LYS C  68      33.215   2.756  -4.073  1.00 24.27           C  
ANISOU 2634  CG  LYS C  68     3459   2587   3174    123    202     38       C  
ATOM   2635  CD  LYS C  68      33.322   3.337  -2.695  1.00 25.64           C  
ANISOU 2635  CD  LYS C  68     3649   2734   3359    132    201     39       C  
ATOM   2636  CE  LYS C  68      32.215   4.346  -2.430  1.00 25.61           C  
ANISOU 2636  CE  LYS C  68     3630   2767   3331    169    206     46       C  
ATOM   2637  NZ  LYS C  68      32.071   4.596  -0.969  1.00 26.33           N  
ANISOU 2637  NZ  LYS C  68     3730   2845   3427    168    205     41       N  
ATOM   2638  N   VAL C  69      31.863  -1.439  -5.769  1.00 20.66           N  
ANISOU 2638  N   VAL C  69     2969   2217   2662    -11    205    -15       N  
ATOM   2639  CA  VAL C  69      31.132  -2.673  -5.928  1.00 21.92           C  
ANISOU 2639  CA  VAL C  69     3124   2408   2796    -63    212    -37       C  
ATOM   2640  C   VAL C  69      31.302  -3.469  -4.671  1.00 21.04           C  
ANISOU 2640  C   VAL C  69     3046   2253   2693    -94    211    -42       C  
ATOM   2641  O   VAL C  69      32.413  -3.920  -4.355  1.00 20.73           O  
ANISOU 2641  O   VAL C  69     3044   2148   2683    -94    208    -39       O  
ATOM   2642  CB  VAL C  69      31.611  -3.449  -7.171  1.00 21.84           C  
ANISOU 2642  CB  VAL C  69     3118   2391   2787    -82    216    -49       C  
ATOM   2643  CG1 VAL C  69      30.755  -4.709  -7.390  1.00 22.64           C  
ANISOU 2643  CG1 VAL C  69     3217   2526   2857   -143    227    -76       C  
ATOM   2644  CG2 VAL C  69      31.517  -2.535  -8.401  1.00 22.37           C  
ANISOU 2644  CG2 VAL C  69     3152   2500   2845    -45    215    -39       C  
ATOM   2645  N   MET C  70      30.188  -3.642  -3.946  1.00 21.85           N  
ANISOU 2645  N   MET C  70     3136   2398   2768   -120    215    -51       N  
ATOM   2646  CA  MET C  70      30.171  -4.222  -2.614  1.00 22.57           C  
ANISOU 2646  CA  MET C  70     3256   2458   2861   -148    216    -52       C  
ATOM   2647  C   MET C  70      29.453  -5.575  -2.682  1.00 22.23           C  
ANISOU 2647  C   MET C  70     3225   2433   2787   -216    229    -74       C  
ATOM   2648  O   MET C  70      28.670  -5.790  -3.597  1.00 22.92           O  
ANISOU 2648  O   MET C  70     3283   2580   2845   -240    236    -91       O  
ATOM   2649  CB  MET C  70      29.411  -3.301  -1.628  1.00 24.42           C  
ANISOU 2649  CB  MET C  70     3466   2730   3083   -127    212    -45       C  
ATOM   2650  CG  MET C  70      29.673  -1.804  -1.808  1.00 25.17           C  
ANISOU 2650  CG  MET C  70     3541   2828   3192    -62    205    -28       C  
ATOM   2651  SD  MET C  70      31.382  -1.385  -1.510  1.00 27.78           S  
ANISOU 2651  SD  MET C  70     3910   3070   3574    -30    197    -11       S  
ATOM   2652  CE  MET C  70      31.680  -1.833   0.198  1.00 25.91           C  
ANISOU 2652  CE  MET C  70     3703   2792   3347    -49    193    -10       C  
ATOM   2653  N   PHE C  71      29.679  -6.455  -1.695  1.00 21.42           N  
ANISOU 2653  N   PHE C  71     3167   2283   2689   -249    232    -75       N  
ATOM   2654  CA  PHE C  71      28.970  -7.723  -1.616  1.00 22.66           C  
ANISOU 2654  CA  PHE C  71     3347   2449   2814   -321    248    -96       C  
ATOM   2655  C   PHE C  71      28.423  -7.792  -0.182  1.00 22.64           C  
ANISOU 2655  C   PHE C  71     3354   2451   2796   -343    250    -92       C  
ATOM   2656  O   PHE C  71      29.200  -7.967   0.736  1.00 23.16           O  
ANISOU 2656  O   PHE C  71     3460   2452   2885   -328    244    -76       O  
ATOM   2657  CB  PHE C  71      29.858  -8.912  -1.935  1.00 23.48           C  
ANISOU 2657  CB  PHE C  71     3510   2478   2934   -342    256   -101       C  
ATOM   2658  CG  PHE C  71      29.093 -10.163  -2.375  1.00 24.55           C  
ANISOU 2658  CG  PHE C  71     3666   2627   3032   -419    278   -128       C  
ATOM   2659  CD1 PHE C  71      28.216 -10.110  -3.461  1.00 24.57           C  
ANISOU 2659  CD1 PHE C  71     3622   2707   3003   -447    286   -151       C  
ATOM   2660  CD2 PHE C  71      29.353 -11.400  -1.798  1.00 25.03           C  
ANISOU 2660  CD2 PHE C  71     3798   2622   3090   -460    291   -132       C  
ATOM   2661  CE1 PHE C  71      27.562 -11.247  -3.911  1.00 25.78           C  
ANISOU 2661  CE1 PHE C  71     3795   2876   3122   -524    308   -181       C  
ATOM   2662  CE2 PHE C  71      28.696 -12.559  -2.250  1.00 26.29           C  
ANISOU 2662  CE2 PHE C  71     3987   2786   3215   -537    315   -159       C  
ATOM   2663  CZ  PHE C  71      27.813 -12.477  -3.320  1.00 26.52           C  
ANISOU 2663  CZ  PHE C  71     3965   2897   3214   -572    324   -186       C  
ATOM   2664  N   GLN C  72      27.117  -7.589  -0.008  1.00 23.50           N  
ANISOU 2664  N   GLN C  72     3422   2642   2865   -373    256   -106       N  
ATOM   2665  CA  GLN C  72      26.468  -7.471   1.324  1.00 23.57           C  
ANISOU 2665  CA  GLN C  72     3426   2672   2854   -391    257   -104       C  
ATOM   2666  C   GLN C  72      25.358  -8.542   1.446  1.00 24.86           C  
ANISOU 2666  C   GLN C  72     3595   2880   2968   -479    277   -130       C  
ATOM   2667  O   GLN C  72      24.410  -8.497   0.673  1.00 24.51           O  
ANISOU 2667  O   GLN C  72     3505   2920   2888   -505    285   -153       O  
ATOM   2668  CB  GLN C  72      25.826  -6.099   1.470  1.00 22.98           C  
ANISOU 2668  CB  GLN C  72     3289   2669   2770   -342    246   -100       C  
ATOM   2669  CG  GLN C  72      26.790  -4.956   1.198  1.00 21.45           C  
ANISOU 2669  CG  GLN C  72     3090   2439   2619   -262    231    -78       C  
ATOM   2670  CD  GLN C  72      26.185  -3.577   1.503  1.00 21.79           C  
ANISOU 2670  CD  GLN C  72     3086   2539   2653   -210    223    -73       C  
ATOM   2671  OE1 GLN C  72      24.985  -3.348   1.331  1.00 22.43           O  
ANISOU 2671  OE1 GLN C  72     3121   2709   2692   -218    228    -87       O  
ATOM   2672  NE2 GLN C  72      26.988  -2.702   1.992  1.00 21.14           N  
ANISOU 2672  NE2 GLN C  72     3016   2410   2605   -158    213    -54       N  
ATOM   2673  N   ARG C  73      25.530  -9.482   2.374  1.00 27.29           N  
ANISOU 2673  N   ARG C  73     3961   3133   3272   -524    287   -127       N  
ATOM   2674  CA  ARG C  73      24.733 -10.724   2.456  1.00 30.74           C  
ANISOU 2674  CA  ARG C  73     4429   3585   3666   -619    312   -151       C  
ATOM   2675  C   ARG C  73      24.144 -11.038   1.084  1.00 30.92           C  
ANISOU 2675  C   ARG C  73     4420   3664   3661   -656    324   -180       C  
ATOM   2676  O   ARG C  73      22.920 -10.990   0.845  1.00 29.89           O  
ANISOU 2676  O   ARG C  73     4238   3636   3482   -701    334   -206       O  
ATOM   2677  CB  ARG C  73      23.694 -10.685   3.568  1.00 32.74           C  
ANISOU 2677  CB  ARG C  73     4663   3896   3879   -662    318   -158       C  
ATOM   2678  CG  ARG C  73      22.806  -9.466   3.582  1.00 32.46           C  
ANISOU 2678  CG  ARG C  73     4540   3968   3823   -628    307   -165       C  
ATOM   2679  CD  ARG C  73      22.209  -9.227   4.954  1.00 33.04           C  
ANISOU 2679  CD  ARG C  73     4604   4074   3875   -642    306   -162       C  
ATOM   2680  NE  ARG C  73      21.390  -8.024   4.876  1.00 33.60           N  
ANISOU 2680  NE  ARG C  73     4592   4247   3926   -598    295   -170       N  
ATOM   2681  CZ  ARG C  73      20.969  -7.295   5.901  1.00 35.47           C  
ANISOU 2681  CZ  ARG C  73     4799   4523   4153   -573    287   -165       C  
ATOM   2682  NH1 ARG C  73      20.223  -6.216   5.665  1.00 35.83           N  
ANISOU 2682  NH1 ARG C  73     4773   4662   4178   -525    278   -174       N  
ATOM   2683  NH2 ARG C  73      21.241  -7.635   7.147  1.00 35.96           N  
ANISOU 2683  NH2 ARG C  73     4903   4536   4221   -594    288   -153       N  
ATOM   2684  N   LYS C  74      25.075 -11.320   0.175  1.00 33.29           N  
ANISOU 2684  N   LYS C  74     4749   3904   3992   -631    322   -176       N  
ATOM   2685  CA  LYS C  74      24.822 -11.829  -1.200  1.00 35.18           C  
ANISOU 2685  CA  LYS C  74     4978   4175   4215   -666    335   -203       C  
ATOM   2686  C   LYS C  74      24.404 -10.807  -2.283  1.00 37.52           C  
ANISOU 2686  C   LYS C  74     5191   4562   4502   -624    324   -210       C  
ATOM   2687  O   LYS C  74      24.657 -11.040  -3.469  1.00 43.72           O  
ANISOU 2687  O   LYS C  74     5971   5350   5290   -625    328   -222       O  
ATOM   2688  CB  LYS C  74      23.874 -13.036  -1.175  1.00 36.31           C  
ANISOU 2688  CB  LYS C  74     5146   4343   4305   -775    366   -237       C  
ATOM   2689  CG  LYS C  74      24.194 -14.008  -0.054  1.00 36.55           C  
ANISOU 2689  CG  LYS C  74     5263   4284   4337   -816    379   -226       C  
ATOM   2690  CD  LYS C  74      25.638 -14.474  -0.053  1.00 37.57           C  
ANISOU 2690  CD  LYS C  74     5469   4289   4516   -770    374   -203       C  
ATOM   2691  CE  LYS C  74      26.078 -14.988   1.294  1.00 38.18           C  
ANISOU 2691  CE  LYS C  74     5618   4286   4602   -773    376   -179       C  
ATOM   2692  NZ  LYS C  74      27.538 -14.791   1.494  1.00 39.07           N  
ANISOU 2692  NZ  LYS C  74     5766   4310   4767   -687    356   -147       N  
ATOM   2693  N   LYS C  75      23.738  -9.722  -1.912  1.00 37.77           N  
ANISOU 2693  N   LYS C  75     5159   4670   4519   -587    312   -204       N  
ATOM   2694  CA  LYS C  75      23.381  -8.681  -2.865  1.00 35.75           C  
ANISOU 2694  CA  LYS C  75     4833   4496   4255   -534    301   -204       C  
ATOM   2695  C   LYS C  75      24.715  -8.112  -3.393  1.00 32.85           C  
ANISOU 2695  C   LYS C  75     4486   4052   3944   -459    285   -177       C  
ATOM   2696  O   LYS C  75      25.571  -7.713  -2.614  1.00 28.85           O  
ANISOU 2696  O   LYS C  75     4010   3473   3477   -415    273   -151       O  
ATOM   2697  CB  LYS C  75      22.572  -7.544  -2.191  1.00 37.35           C  
ANISOU 2697  CB  LYS C  75     4977   4777   4437   -492    290   -196       C  
ATOM   2698  CG  LYS C  75      21.055  -7.438  -2.439  1.00 38.54           C  
ANISOU 2698  CG  LYS C  75     5056   5067   4519   -526    298   -226       C  
ATOM   2699  CD  LYS C  75      20.610  -5.970  -2.211  1.00 38.42           C  
ANISOU 2699  CD  LYS C  75     4983   5118   4497   -441    281   -210       C  
ATOM   2700  CE  LYS C  75      19.133  -5.741  -1.873  1.00 39.93           C  
ANISOU 2700  CE  LYS C  75     5105   5443   4621   -461    287   -234       C  
ATOM   2701  NZ  LYS C  75      18.773  -6.291  -0.538  1.00 39.17           N  
ANISOU 2701  NZ  LYS C  75     5032   5338   4512   -520    295   -243       N  
ATOM   2702  N   CYS C  76      24.911  -8.135  -4.704  1.00 31.41           N  
ANISOU 2702  N   CYS C  76     4286   3886   3761   -450    286   -185       N  
ATOM   2703  CA  CYS C  76      25.869  -7.226  -5.313  1.00 30.53           C  
ANISOU 2703  CA  CYS C  76     4168   3740   3690   -372    270   -160       C  
ATOM   2704  C   CYS C  76      25.281  -5.846  -5.152  1.00 28.83           C  
ANISOU 2704  C   CYS C  76     3898   3592   3463   -311    258   -145       C  
ATOM   2705  O   CYS C  76      24.096  -5.657  -5.411  1.00 29.37           O  
ANISOU 2705  O   CYS C  76     3913   3762   3482   -324    263   -161       O  
ATOM   2706  CB  CYS C  76      26.021  -7.510  -6.808  1.00 31.47           C  
ANISOU 2706  CB  CYS C  76     4272   3881   3801   -378    275   -174       C  
ATOM   2707  SG  CYS C  76      26.889  -9.037  -7.115  1.00 32.57           S  
ANISOU 2707  SG  CYS C  76     4483   3930   3960   -434    289   -190       S  
ATOM   2708  N   LYS C  77      26.083  -4.879  -4.715  1.00 27.92           N  
ANISOU 2708  N   LYS C  77     3796   3424   3387   -245    244   -116       N  
ATOM   2709  CA  LYS C  77      25.624  -3.511  -4.656  1.00 27.77           C  
ANISOU 2709  CA  LYS C  77     3735   3456   3359   -180    235   -101       C  
ATOM   2710  C   LYS C  77      26.645  -2.480  -5.078  1.00 27.61           C  
ANISOU 2710  C   LYS C  77     3727   3384   3379   -110    225    -73       C  
ATOM   2711  O   LYS C  77      27.874  -2.714  -5.078  1.00 25.26           O  
ANISOU 2711  O   LYS C  77     3471   3001   3122   -107    222    -64       O  
ATOM   2712  CB  LYS C  77      25.085  -3.187  -3.281  1.00 29.03           C  
ANISOU 2712  CB  LYS C  77     3892   3627   3509   -178    233    -99       C  
ATOM   2713  CG  LYS C  77      23.921  -4.101  -3.001  1.00 31.27           C  
ANISOU 2713  CG  LYS C  77     4154   3981   3743   -250    245   -128       C  
ATOM   2714  CD  LYS C  77      23.074  -3.657  -1.897  1.00 31.75           C  
ANISOU 2714  CD  LYS C  77     4191   4092   3780   -246    244   -130       C  
ATOM   2715  CE  LYS C  77      23.701  -3.990  -0.557  1.00 31.47           C  
ANISOU 2715  CE  LYS C  77     4207   3974   3775   -264    242   -120       C  
ATOM   2716  NZ  LYS C  77      22.780  -4.643   0.384  1.00 31.62           N  
ANISOU 2716  NZ  LYS C  77     4219   4036   3755   -326    251   -139       N  
ATOM   2717  N   TYR C  78      26.104  -1.349  -5.492  1.00 25.91           N  
ANISOU 2717  N   TYR C  78     3473   3224   3144    -53    222    -62       N  
ATOM   2718  CA  TYR C  78      26.861  -0.369  -6.258  1.00 26.96           C  
ANISOU 2718  CA  TYR C  78     3613   3327   3301      6    217    -39       C  
ATOM   2719  C   TYR C  78      26.657   0.980  -5.582  1.00 27.06           C  
ANISOU 2719  C   TYR C  78     3624   3340   3316     70    213    -19       C  
ATOM   2720  O   TYR C  78      25.502   1.389  -5.261  1.00 30.53           O  
ANISOU 2720  O   TYR C  78     4027   3855   3717     89    214    -25       O  
ATOM   2721  CB  TYR C  78      26.414  -0.401  -7.722  1.00 26.70           C  
ANISOU 2721  CB  TYR C  78     3544   3362   3237     13    221    -44       C  
ATOM   2722  CG  TYR C  78      26.547  -1.787  -8.302  1.00 25.94           C  
ANISOU 2722  CG  TYR C  78     3453   3265   3135    -56    227    -69       C  
ATOM   2723  CD1 TYR C  78      27.756  -2.222  -8.864  1.00 25.53           C  
ANISOU 2723  CD1 TYR C  78     3436   3141   3121    -65    227    -66       C  
ATOM   2724  CD2 TYR C  78      25.481  -2.701  -8.247  1.00 26.01           C  
ANISOU 2724  CD2 TYR C  78     3435   3345   3101   -116    236    -99       C  
ATOM   2725  CE1 TYR C  78      27.871  -3.531  -9.365  1.00 25.82           C  
ANISOU 2725  CE1 TYR C  78     3484   3172   3152   -127    235    -91       C  
ATOM   2726  CE2 TYR C  78      25.605  -3.991  -8.738  1.00 26.47           C  
ANISOU 2726  CE2 TYR C  78     3507   3394   3154   -184    246   -125       C  
ATOM   2727  CZ  TYR C  78      26.808  -4.392  -9.288  1.00 27.41           C  
ANISOU 2727  CZ  TYR C  78     3666   3436   3312   -186    245   -120       C  
ATOM   2728  OH  TYR C  78      26.906  -5.664  -9.778  1.00 27.75           O  
ANISOU 2728  OH  TYR C  78     3727   3467   3348   -250    256   -146       O  
ATOM   2729  N   MET C  79      27.758   1.644  -5.267  1.00 27.23           N  
ANISOU 2729  N   MET C  79     3684   3280   3381    101    210      0       N  
ATOM   2730  CA  MET C  79      27.706   3.003  -4.749  1.00 27.03           C  
ANISOU 2730  CA  MET C  79     3666   3242   3360    162    210     18       C  
ATOM   2731  C   MET C  79      28.645   3.872  -5.531  1.00 25.79           C  
ANISOU 2731  C   MET C  79     3533   3035   3227    202    212     39       C  
ATOM   2732  O   MET C  79      29.775   3.487  -5.851  1.00 23.02           O  
ANISOU 2732  O   MET C  79     3209   2627   2909    180    211     41       O  
ATOM   2733  CB  MET C  79      28.082   3.086  -3.280  1.00 27.75           C  
ANISOU 2733  CB  MET C  79     3784   3281   3476    151    207     16       C  
ATOM   2734  CG  MET C  79      26.903   3.060  -2.336  1.00 29.76           C  
ANISOU 2734  CG  MET C  79     4012   3595   3699    147    207      4       C  
ATOM   2735  SD  MET C  79      27.348   2.854  -0.609  1.00 31.08           S  
ANISOU 2735  SD  MET C  79     4209   3706   3891    120    204      0       S  
ATOM   2736  CE  MET C  79      28.044   1.234  -0.733  1.00 27.99           C  
ANISOU 2736  CE  MET C  79     3839   3277   3517     48    202    -10       C  
ATOM   2737  N   ILE C  80      28.173   5.074  -5.781  1.00 26.71           N  
ANISOU 2737  N   ILE C  80     3646   3176   3327    265    216     56       N  
ATOM   2738  CA  ILE C  80      28.822   5.985  -6.685  1.00 27.24           C  
ANISOU 2738  CA  ILE C  80     3736   3209   3404    307    222     79       C  
ATOM   2739  C   ILE C  80      29.372   7.169  -5.889  1.00 28.04           C  
ANISOU 2739  C   ILE C  80     3881   3242   3529    342    228     94       C  
ATOM   2740  O   ILE C  80      28.633   7.766  -5.120  1.00 31.65           O  
ANISOU 2740  O   ILE C  80     4335   3719   3970    375    230     94       O  
ATOM   2741  CB  ILE C  80      27.797   6.466  -7.723  1.00 27.88           C  
ANISOU 2741  CB  ILE C  80     3784   3371   3437    356    225     89       C  
ATOM   2742  CG1 ILE C  80      27.366   5.301  -8.590  1.00 27.74           C  
ANISOU 2742  CG1 ILE C  80     3723   3419   3395    312    221     71       C  
ATOM   2743  CG2 ILE C  80      28.375   7.593  -8.595  1.00 28.60           C  
ANISOU 2743  CG2 ILE C  80     3907   3424   3535    408    233    118       C  
ATOM   2744  CD1 ILE C  80      25.874   5.129  -8.739  1.00 28.43           C  
ANISOU 2744  CD1 ILE C  80     3755   3620   3425    325    219     58       C  
ATOM   2745  N   ASN C  81      30.629   7.499  -6.117  1.00 28.23           N  
ANISOU 2745  N   ASN C  81     3942   3193   3588    335    232    103       N  
ATOM   2746  CA  ASN C  81      31.276   8.739  -5.644  1.00 28.94           C  
ANISOU 2746  CA  ASN C  81     4079   3217   3698    365    243    117       C  
ATOM   2747  C   ASN C  81      31.859   9.464  -6.852  1.00 27.32           C  
ANISOU 2747  C   ASN C  81     3899   2987   3493    389    254    139       C  
ATOM   2748  O   ASN C  81      31.854   8.920  -7.942  1.00 27.83           O  
ANISOU 2748  O   ASN C  81     3941   3084   3546    380    250    141       O  
ATOM   2749  CB  ASN C  81      32.440   8.416  -4.691  1.00 30.54           C  
ANISOU 2749  CB  ASN C  81     4306   3355   3940    319    240    104       C  
ATOM   2750  CG  ASN C  81      32.000   8.143  -3.273  1.00 32.10           C  
ANISOU 2750  CG  ASN C  81     4497   3559   4141    306    234     89       C  
ATOM   2751  OD1 ASN C  81      30.826   7.836  -3.000  1.00 35.14           O  
ANISOU 2751  OD1 ASN C  81     4850   4003   4497    315    230     83       O  
ATOM   2752  ND2 ASN C  81      32.950   8.213  -2.360  1.00 32.25           N  
ANISOU 2752  ND2 ASN C  81     4540   3523   4189    281    235     82       N  
ATOM   2753  N   THR C  82      32.369  10.681  -6.625  1.00 26.83           N  
ANISOU 2753  N   THR C  82     3885   2865   3442    416    268    153       N  
ATOM   2754  CA  THR C  82      33.198  11.440  -7.591  1.00 26.44           C  
ANISOU 2754  CA  THR C  82     3874   2773   3398    427    282    173       C  
ATOM   2755  C   THR C  82      34.536  11.825  -6.968  1.00 25.10           C  
ANISOU 2755  C   THR C  82     3745   2525   3264    389    291    165       C  
ATOM   2756  O   THR C  82      34.569  12.436  -5.874  1.00 26.04           O  
ANISOU 2756  O   THR C  82     3891   2610   3393    394    298    159       O  
ATOM   2757  CB  THR C  82      32.548  12.764  -8.053  1.00 27.98           C  
ANISOU 2757  CB  THR C  82     4101   2964   3563    498    299    200       C  
ATOM   2758  OG1 THR C  82      31.167  12.570  -8.337  1.00 29.51           O  
ANISOU 2758  OG1 THR C  82     4254   3240   3717    544    291    204       O  
ATOM   2759  CG2 THR C  82      33.236  13.245  -9.281  1.00 28.25           C  
ANISOU 2759  CG2 THR C  82     4164   2972   3595    503    311    222       C  
ATOM   2760  N   PHE C  83      35.638  11.445  -7.619  1.00 22.98           N  
ANISOU 2760  N   PHE C  83     3479   2236   3013    349    291    163       N  
ATOM   2761  CA  PHE C  83      36.966  11.886  -7.181  1.00 22.74           C  
ANISOU 2761  CA  PHE C  83     3485   2144   3010    313    302    155       C  
ATOM   2762  C   PHE C  83      37.328  13.113  -8.023  1.00 22.06           C  
ANISOU 2762  C   PHE C  83     3448   2020   2914    333    325    178       C  
ATOM   2763  O   PHE C  83      37.360  13.014  -9.259  1.00 21.58           O  
ANISOU 2763  O   PHE C  83     3380   1979   2839    341    327    193       O  
ATOM   2764  CB  PHE C  83      37.994  10.775  -7.312  1.00 22.92           C  
ANISOU 2764  CB  PHE C  83     3481   2172   3054    260    289    136       C  
ATOM   2765  CG  PHE C  83      37.861   9.696  -6.246  1.00 22.85           C  
ANISOU 2765  CG  PHE C  83     3442   2180   3058    236    270    114       C  
ATOM   2766  CD1 PHE C  83      36.804   9.662  -5.325  1.00 23.87           C  
ANISOU 2766  CD1 PHE C  83     3562   2329   3179    256    265    111       C  
ATOM   2767  CD2 PHE C  83      38.777   8.656  -6.215  1.00 24.65           C  
ANISOU 2767  CD2 PHE C  83     3651   2409   3303    197    259     97       C  
ATOM   2768  CE1 PHE C  83      36.707   8.688  -4.349  1.00 23.78           C  
ANISOU 2768  CE1 PHE C  83     3528   2330   3176    231    250     93       C  
ATOM   2769  CE2 PHE C  83      38.674   7.663  -5.248  1.00 23.07           C  
ANISOU 2769  CE2 PHE C  83     3432   2219   3112    179    244     80       C  
ATOM   2770  CZ  PHE C  83      37.602   7.641  -4.353  1.00 24.42           C  
ANISOU 2770  CZ  PHE C  83     3596   2406   3273    193    240     79       C  
ATOM   2771  N   VAL C  84      37.593  14.219  -7.348  1.00 21.79           N  
ANISOU 2771  N   VAL C  84     3465   1930   2883    339    345    179       N  
ATOM   2772  CA  VAL C  84      37.909  15.517  -7.990  1.00 23.27           C  
ANISOU 2772  CA  VAL C  84     3715   2067   3058    357    373    201       C  
ATOM   2773  C   VAL C  84      39.415  15.697  -7.861  1.00 22.55           C  
ANISOU 2773  C   VAL C  84     3647   1932   2989    291    385    185       C  
ATOM   2774  O   VAL C  84      39.919  15.575  -6.753  1.00 20.79           O  
ANISOU 2774  O   VAL C  84     3421   1693   2785    257    383    160       O  
ATOM   2775  CB  VAL C  84      37.234  16.700  -7.285  1.00 23.44           C  
ANISOU 2775  CB  VAL C  84     3788   2050   3068    403    392    211       C  
ATOM   2776  CG1 VAL C  84      37.643  18.031  -7.940  1.00 24.24           C  
ANISOU 2776  CG1 VAL C  84     3967   2087   3155    417    425    234       C  
ATOM   2777  CG2 VAL C  84      35.743  16.525  -7.307  1.00 23.50           C  
ANISOU 2777  CG2 VAL C  84     3766   2112   3050    470    379    223       C  
ATOM   2778  N   PRO C  85      40.120  15.980  -8.979  1.00 24.78           N  
ANISOU 2778  N   PRO C  85     3948   2201   3264    273    398    198       N  
ATOM   2779  CA  PRO C  85      41.574  16.063  -8.891  1.00 25.16           C  
ANISOU 2779  CA  PRO C  85     4008   2222   3328    206    409    178       C  
ATOM   2780  C   PRO C  85      42.077  17.059  -7.856  1.00 26.83           C  
ANISOU 2780  C   PRO C  85     4271   2375   3545    180    432    163       C  
ATOM   2781  O   PRO C  85      41.648  18.237  -7.863  1.00 26.84           O  
ANISOU 2781  O   PRO C  85     4338   2328   3533    210    458    182       O  
ATOM   2782  CB  PRO C  85      41.979  16.503 -10.313  1.00 27.00           C  
ANISOU 2782  CB  PRO C  85     4266   2447   3543    202    425    201       C  
ATOM   2783  CG  PRO C  85      40.882  15.981 -11.182  1.00 26.37           C  
ANISOU 2783  CG  PRO C  85     4153   2417   3446    257    409    224       C  
ATOM   2784  CD  PRO C  85      39.650  16.181 -10.359  1.00 26.09           C  
ANISOU 2784  CD  PRO C  85     4121   2387   3405    311    403    229       C  
ATOM   2785  N   GLY C  86      42.941  16.597  -6.957  1.00 26.71           N  
ANISOU 2785  N   GLY C  86     4232   2367   3550    129    424    131       N  
ATOM   2786  CA  GLY C  86      43.545  17.423  -5.905  1.00 28.19           C  
ANISOU 2786  CA  GLY C  86     4458   2509   3743     93    445    109       C  
ATOM   2787  C   GLY C  86      44.710  18.254  -6.411  1.00 28.30           C  
ANISOU 2787  C   GLY C  86     4517   2486   3748     37    476    103       C  
ATOM   2788  O   GLY C  86      44.692  18.703  -7.545  1.00 30.39           O  
ANISOU 2788  O   GLY C  86     4812   2735   3997     47    491    128       O  
ATOM   2789  N   SER C  87      45.762  18.383  -5.605  1.00 29.45           N  
ANISOU 2789  N   SER C  87     4660   2627   3900    -23    484     69       N  
ATOM   2790  CA  SER C  87      46.890  19.280  -5.913  1.00 31.11           C  
ANISOU 2790  CA  SER C  87     4916   2804   4098    -88    518     56       C  
ATOM   2791  C   SER C  87      47.895  18.852  -7.006  1.00 30.86           C  
ANISOU 2791  C   SER C  87     4856   2808   4059   -130    517     54       C  
ATOM   2792  O   SER C  87      48.525  19.685  -7.640  1.00 31.70           O  
ANISOU 2792  O   SER C  87     5011   2884   4149   -170    548     57       O  
ATOM   2793  CB  SER C  87      47.659  19.582  -4.613  1.00 32.09           C  
ANISOU 2793  CB  SER C  87     5042   2923   4227   -143    529     15       C  
ATOM   2794  OG  SER C  87      46.899  20.401  -3.729  1.00 35.21           O  
ANISOU 2794  OG  SER C  87     5487   3267   4622   -118    545     16       O  
ATOM   2795  N   GLN C  88      48.083  17.540  -7.168  1.00 28.65           N  
ANISOU 2795  N   GLN C  88     4501   2592   3790   -122    482     45       N  
ATOM   2796  CA  GLN C  88      49.061  16.957  -8.075  1.00 28.43           C  
ANISOU 2796  CA  GLN C  88     4435   2609   3757   -157    475     36       C  
ATOM   2797  C   GLN C  88      48.447  15.722  -8.753  1.00 25.83           C  
ANISOU 2797  C   GLN C  88     4052   2326   3437   -108    441     53       C  
ATOM   2798  O   GLN C  88      47.479  15.200  -8.276  1.00 24.82           O  
ANISOU 2798  O   GLN C  88     3905   2203   3319    -62    421     61       O  
ATOM   2799  CB  GLN C  88      50.298  16.561  -7.290  1.00 30.11           C  
ANISOU 2799  CB  GLN C  88     4606   2862   3972   -214    469     -6       C  
ATOM   2800  CG  GLN C  88      51.071  17.764  -6.771  1.00 32.28           C  
ANISOU 2800  CG  GLN C  88     4930   3102   4232   -278    507    -28       C  
ATOM   2801  CD  GLN C  88      52.405  17.388  -6.180  1.00 34.39           C  
ANISOU 2801  CD  GLN C  88     5147   3425   4491   -338    502    -73       C  
ATOM   2802  OE1 GLN C  88      52.474  16.552  -5.274  1.00 37.49           O  
ANISOU 2802  OE1 GLN C  88     5488   3858   4896   -323    474    -91       O  
ATOM   2803  NE2 GLN C  88      53.483  18.017  -6.670  1.00 35.17           N  
ANISOU 2803  NE2 GLN C  88     5262   3532   4568   -408    530    -91       N  
ATOM   2804  N   PRO C  89      48.932  15.323  -9.933  1.00 24.25           N  
ANISOU 2804  N   PRO C  89     3829   2156   3227   -120    438     58       N  
ATOM   2805  CA  PRO C  89      48.338  14.114 -10.643  1.00 23.01           C  
ANISOU 2805  CA  PRO C  89     3623   2043   3077    -76    408     70       C  
ATOM   2806  C   PRO C  89      48.400  12.818  -9.824  1.00 21.06           C  
ANISOU 2806  C   PRO C  89     3318   1836   2848    -67    375     47       C  
ATOM   2807  O   PRO C  89      49.448  12.452  -9.322  1.00 20.69           O  
ANISOU 2807  O   PRO C  89     3244   1813   2804   -101    370     17       O  
ATOM   2808  CB  PRO C  89      49.191  13.997 -11.919  1.00 23.29           C  
ANISOU 2808  CB  PRO C  89     3644   2105   3098   -106    414     70       C  
ATOM   2809  CG  PRO C  89      49.779  15.368 -12.072  1.00 24.48           C  
ANISOU 2809  CG  PRO C  89     3855   2213   3231   -150    452     73       C  
ATOM   2810  CD  PRO C  89      50.073  15.848 -10.697  1.00 24.72           C  
ANISOU 2810  CD  PRO C  89     3903   2219   3268   -176    462     49       C  
ATOM   2811  N   GLY C  90      47.249  12.206  -9.648  1.00 20.56           N  
ANISOU 2811  N   GLY C  90     3241   1777   2793    -20    357     61       N  
ATOM   2812  CA  GLY C  90      47.170  10.970  -8.866  1.00 19.57           C  
ANISOU 2812  CA  GLY C  90     3071   1681   2682     -9    328     43       C  
ATOM   2813  C   GLY C  90      46.560  11.247  -7.536  1.00 19.92           C  
ANISOU 2813  C   GLY C  90     3129   1703   2734      3    327     40       C  
ATOM   2814  O   GLY C  90      46.301  10.335  -6.807  1.00 17.79           O  
ANISOU 2814  O   GLY C  90     2832   1451   2475     15    306     31       O  
ATOM   2815  N   GLU C  91      46.294  12.535  -7.236  1.00 19.87           N  
ANISOU 2815  N   GLU C  91     3172   1654   2723      1    351     50       N  
ATOM   2816  CA  GLU C  91      45.761  12.944  -5.947  1.00 21.04           C  
ANISOU 2816  CA  GLU C  91     3337   1779   2877     12    353     45       C  
ATOM   2817  C   GLU C  91      44.351  13.420  -6.209  1.00 20.19           C  
ANISOU 2817  C   GLU C  91     3256   1653   2762     62    358     74       C  
ATOM   2818  O   GLU C  91      44.087  14.065  -7.215  1.00 20.35           O  
ANISOU 2818  O   GLU C  91     3305   1658   2769     78    374     96       O  
ATOM   2819  CB  GLU C  91      46.505  14.110  -5.340  1.00 22.77           C  
ANISOU 2819  CB  GLU C  91     3596   1962   3091    -27    380     30       C  
ATOM   2820  CG  GLU C  91      47.801  13.814  -4.662  1.00 24.27           C  
ANISOU 2820  CG  GLU C  91     3760   2177   3284    -76    377     -4       C  
ATOM   2821  CD  GLU C  91      48.085  14.876  -3.625  1.00 25.85           C  
ANISOU 2821  CD  GLU C  91     3996   2343   3480   -107    400    -21       C  
ATOM   2822  OE1 GLU C  91      48.921  15.772  -3.934  1.00 29.08           O  
ANISOU 2822  OE1 GLU C  91     4438   2734   3878   -154    428    -32       O  
ATOM   2823  OE2 GLU C  91      47.427  14.848  -2.538  1.00 25.69           O  
ANISOU 2823  OE2 GLU C  91     3977   2315   3468    -85    392    -25       O  
ATOM   2824  N   PHE C  92      43.462  13.157  -5.269  1.00 19.48           N  
ANISOU 2824  N   PHE C  92     3156   1567   2676     89    346     72       N  
ATOM   2825  CA  PHE C  92      42.059  13.426  -5.443  1.00 19.66           C  
ANISOU 2825  CA  PHE C  92     3190   1590   2688    142    346     96       C  
ATOM   2826  C   PHE C  92      41.424  13.756  -4.107  1.00 19.15           C  
ANISOU 2826  C   PHE C  92     3136   1512   2627    157    346     87       C  
ATOM   2827  O   PHE C  92      42.021  13.441  -3.059  1.00 17.80           O  
ANISOU 2827  O   PHE C  92     2951   1342   2468    126    339     64       O  
ATOM   2828  CB  PHE C  92      41.307  12.277  -6.103  1.00 20.04           C  
ANISOU 2828  CB  PHE C  92     3192   1687   2732    166    322    105       C  
ATOM   2829  CG  PHE C  92      41.905  11.838  -7.402  1.00 20.25           C  
ANISOU 2829  CG  PHE C  92     3204   1733   2756    151    320    110       C  
ATOM   2830  CD1 PHE C  92      42.963  10.927  -7.401  1.00 19.71           C  
ANISOU 2830  CD1 PHE C  92     3106   1682   2700    113    308     88       C  
ATOM   2831  CD2 PHE C  92      41.467  12.360  -8.602  1.00 20.15           C  
ANISOU 2831  CD2 PHE C  92     3208   1722   2724    177    332    135       C  
ATOM   2832  CE1 PHE C  92      43.519  10.537  -8.569  1.00 19.91           C  
ANISOU 2832  CE1 PHE C  92     3117   1726   2722    101    307     90       C  
ATOM   2833  CE2 PHE C  92      42.058  11.985  -9.808  1.00 20.61           C  
ANISOU 2833  CE2 PHE C  92     3251   1799   2778    161    331    138       C  
ATOM   2834  CZ  PHE C  92      43.087  11.054  -9.768  1.00 20.93           C  
ANISOU 2834  CZ  PHE C  92     3260   1858   2834    122    318    114       C  
ATOM   2835  N   THR C  93      40.258  14.414  -4.157  1.00 20.16           N  
ANISOU 2835  N   THR C  93     3287   1632   2740    207    354    107       N  
ATOM   2836  CA  THR C  93      39.374  14.540  -2.980  1.00 20.78           C  
ANISOU 2836  CA  THR C  93     3363   1713   2817    233    349    100       C  
ATOM   2837  C   THR C  93      37.995  14.106  -3.433  1.00 21.59           C  
ANISOU 2837  C   THR C  93     3439   1862   2902    284    336    117       C  
ATOM   2838  O   THR C  93      37.714  13.958  -4.630  1.00 21.02           O  
ANISOU 2838  O   THR C  93     3358   1810   2816    303    334    136       O  
ATOM   2839  CB  THR C  93      39.362  15.940  -2.361  1.00 21.62           C  
ANISOU 2839  CB  THR C  93     3530   1764   2919    243    377     98       C  
ATOM   2840  OG1 THR C  93      38.585  16.776  -3.181  1.00 22.26           O  
ANISOU 2840  OG1 THR C  93     3648   1830   2979    297    393    126       O  
ATOM   2841  CG2 THR C  93      40.745  16.508  -2.227  1.00 21.92           C  
ANISOU 2841  CG2 THR C  93     3601   1761   2968    187    396     82       C  
ATOM   2842  N   LEU C  94      37.155  13.774  -2.476  1.00 23.83           N  
ANISOU 2842  N   LEU C  94     3700   2171   3183    300    324    109       N  
ATOM   2843  CA  LEU C  94      35.792  13.410  -2.814  1.00 24.90           C  
ANISOU 2843  CA  LEU C  94     3806   2359   3295    345    312    121       C  
ATOM   2844  C   LEU C  94      35.136  14.736  -3.167  1.00 27.57           C  
ANISOU 2844  C   LEU C  94     4187   2675   3610    404    333    141       C  
ATOM   2845  O   LEU C  94      35.824  15.808  -3.148  1.00 29.35           O  
ANISOU 2845  O   LEU C  94     4471   2838   3843    401    357    145       O  
ATOM   2846  CB  LEU C  94      35.121  12.663  -1.658  1.00 25.04           C  
ANISOU 2846  CB  LEU C  94     3787   2413   3313    338    295    103       C  
ATOM   2847  CG  LEU C  94      35.531  11.189  -1.560  1.00 26.29           C  
ANISOU 2847  CG  LEU C  94     3904   2600   3485    291    274     90       C  
ATOM   2848  CD1 LEU C  94      37.043  10.952  -1.596  1.00 26.32           C  
ANISOU 2848  CD1 LEU C  94     3918   2567   3514    245    275     80       C  
ATOM   2849  CD2 LEU C  94      34.966  10.606  -0.280  1.00 26.71           C  
ANISOU 2849  CD2 LEU C  94     3933   2677   3537    281    262     74       C  
ATOM   2850  N   GLY C  95      33.872  14.713  -3.563  1.00 27.56           N  
ANISOU 2850  N   GLY C  95     4164   2724   3580    458    328    155       N  
ATOM   2851  CA  GLY C  95      33.194  16.024  -3.857  1.00 29.89           C  
ANISOU 2851  CA  GLY C  95     4506   2999   3849    529    348    176       C  
ATOM   2852  C   GLY C  95      33.141  17.016  -2.672  1.00 31.04           C  
ANISOU 2852  C   GLY C  95     4698   3095   3999    546    365    166       C  
ATOM   2853  O   GLY C  95      33.686  16.779  -1.588  1.00 33.23           O  
ANISOU 2853  O   GLY C  95     4971   3352   4300    499    362    142       O  
ATOM   2854  N   ALA C  96      32.482  18.155  -2.848  1.00 31.31           N  
ANISOU 2854  N   ALA C  96     4778   3109   4008    615    384    184       N  
ATOM   2855  CA  ALA C  96      32.045  18.912  -1.670  1.00 31.61           C  
ANISOU 2855  CA  ALA C  96     4845   3121   4042    644    396    171       C  
ATOM   2856  C   ALA C  96      31.031  17.984  -0.983  1.00 31.59           C  
ANISOU 2856  C   ALA C  96     4769   3204   4028    653    369    155       C  
ATOM   2857  O   ALA C  96      30.259  17.276  -1.646  1.00 32.88           O  
ANISOU 2857  O   ALA C  96     4879   3442   4169    673    352    163       O  
ATOM   2858  CB  ALA C  96      31.441  20.273  -2.047  1.00 31.30           C  
ANISOU 2858  CB  ALA C  96     4873   3046   3973    729    422    195       C  
ATOM   2859  N   ILE C  97      31.071  17.925   0.340  1.00 31.35           N  
ANISOU 2859  N   ILE C  97     4734   3166   4012    628    366    129       N  
ATOM   2860  CA  ILE C  97      30.128  17.078   1.096  1.00 33.10           C  
ANISOU 2860  CA  ILE C  97     4889   3465   4220    629    344    112       C  
ATOM   2861  C   ILE C  97      29.570  17.760   2.381  1.00 32.70           C  
ANISOU 2861  C   ILE C  97     4855   3408   4162    659    352     95       C  
ATOM   2862  O   ILE C  97      30.278  18.533   3.026  1.00 32.97           O  
ANISOU 2862  O   ILE C  97     4941   3370   4215    644    370     84       O  
ATOM   2863  CB  ILE C  97      30.794  15.765   1.488  1.00 32.89           C  
ANISOU 2863  CB  ILE C  97     4818   3456   4221    548    323     95       C  
ATOM   2864  CG1 ILE C  97      31.719  15.991   2.649  1.00 32.02           C  
ANISOU 2864  CG1 ILE C  97     4734   3290   4139    501    330     74       C  
ATOM   2865  CG2 ILE C  97      31.560  15.120   0.332  1.00 32.34           C  
ANISOU 2865  CG2 ILE C  97     4740   3381   4165    512    318    107       C  
ATOM   2866  CD1 ILE C  97      31.882  14.733   3.371  1.00 31.55           C  
ANISOU 2866  CD1 ILE C  97     4625   3268   4094    446    308     57       C  
ATOM   2867  N   LYS C  98      28.302  17.497   2.709  1.00 32.96           N  
ANISOU 2867  N   LYS C  98     4840   3518   4162    701    340     89       N  
ATOM   2868  CA  LYS C  98      27.640  18.030   3.914  1.00 33.39           C  
ANISOU 2868  CA  LYS C  98     4899   3583   4204    733    345     71       C  
ATOM   2869  C   LYS C  98      28.371  17.464   5.132  1.00 31.99           C  
ANISOU 2869  C   LYS C  98     4710   3385   4059    656    337     44       C  
ATOM   2870  O   LYS C  98      28.456  16.251   5.306  1.00 28.94           O  
ANISOU 2870  O   LYS C  98     4272   3043   3681    601    316     37       O  
ATOM   2871  CB  LYS C  98      26.174  17.602   3.881  1.00 35.44           C  
ANISOU 2871  CB  LYS C  98     5094   3950   4419    781    329     69       C  
ATOM   2872  CG  LYS C  98      25.250  18.106   4.983  1.00 37.12           C  
ANISOU 2872  CG  LYS C  98     5298   4197   4608    826    332     49       C  
ATOM   2873  CD  LYS C  98      23.821  17.555   4.831  1.00 39.45           C  
ANISOU 2873  CD  LYS C  98     5519   4616   4854    865    316     45       C  
ATOM   2874  CE  LYS C  98      23.295  17.612   3.388  1.00 41.17           C  
ANISOU 2874  CE  LYS C  98     5723   4880   5039    919    314     71       C  
ATOM   2875  NZ  LYS C  98      21.807  17.575   3.252  1.00 42.38           N  
ANISOU 2875  NZ  LYS C  98     5816   5152   5132    987    306     66       N  
ATOM   2876  N   SER C  99      28.974  18.353   5.916  1.00 31.12           N  
ANISOU 2876  N   SER C  99     4652   3204   3965    650    356     32       N  
ATOM   2877  CA  SER C  99      29.807  17.987   7.052  1.00 30.12           C  
ANISOU 2877  CA  SER C  99     4521   3054   3867    580    352      7       C  
ATOM   2878  C   SER C  99      29.568  18.934   8.240  1.00 30.69           C  
ANISOU 2878  C   SER C  99     4626   3101   3934    603    368    -14       C  
ATOM   2879  O   SER C  99      29.683  20.142   8.061  1.00 30.29           O  
ANISOU 2879  O   SER C  99     4640   2989   3880    643    395    -11       O  
ATOM   2880  CB  SER C  99      31.274  18.078   6.644  1.00 29.96           C  
ANISOU 2880  CB  SER C  99     4538   2963   3879    524    362     10       C  
ATOM   2881  OG  SER C  99      32.062  18.341   7.777  1.00 33.16           O  
ANISOU 2881  OG  SER C  99     4963   3332   4304    478    370    -15       O  
ATOM   2882  N   PRO C 100      29.212  18.429   9.436  1.00 29.98           N  
ANISOU 2882  N   PRO C 100     4494   3054   3841    581    355    -36       N  
ATOM   2883  CA  PRO C 100      28.805  17.048   9.692  1.00 28.82           C  
ANISOU 2883  CA  PRO C 100     4276   2985   3689    544    327    -39       C  
ATOM   2884  C   PRO C 100      27.518  16.793   8.935  1.00 28.55           C  
ANISOU 2884  C   PRO C 100     4203   3024   3618    599    318    -24       C  
ATOM   2885  O   PRO C 100      26.914  17.755   8.462  1.00 27.99           O  
ANISOU 2885  O   PRO C 100     4161   2949   3526    672    332    -15       O  
ATOM   2886  CB  PRO C 100      28.512  17.042  11.216  1.00 28.47           C  
ANISOU 2886  CB  PRO C 100     4214   2964   3639    529    324    -66       C  
ATOM   2887  CG  PRO C 100      29.083  18.305  11.736  1.00 29.88           C  
ANISOU 2887  CG  PRO C 100     4454   3067   3829    541    350    -80       C  
ATOM   2888  CD  PRO C 100      28.954  19.273  10.619  1.00 30.70           C  
ANISOU 2888  CD  PRO C 100     4610   3128   3925    601    370    -61       C  
ATOM   2889  N   PRO C 101      27.100  15.536   8.783  1.00 26.75           N  
ANISOU 2889  N   PRO C 101     3916   2865   3381    565    296    -23       N  
ATOM   2890  CA  PRO C 101      27.768  14.385   9.350  1.00 25.64           C  
ANISOU 2890  CA  PRO C 101     3750   2727   3262    486    280    -31       C  
ATOM   2891  C   PRO C 101      28.850  13.797   8.406  1.00 22.72           C  
ANISOU 2891  C   PRO C 101     3393   2318   2922    444    276    -16       C  
ATOM   2892  O   PRO C 101      29.613  12.929   8.810  1.00 22.25           O  
ANISOU 2892  O   PRO C 101     3323   2248   2883    385    265    -21       O  
ATOM   2893  CB  PRO C 101      26.614  13.402   9.545  1.00 26.95           C  
ANISOU 2893  CB  PRO C 101     3855   2988   3397    478    263    -36       C  
ATOM   2894  CG  PRO C 101      25.579  13.759   8.525  1.00 27.88           C  
ANISOU 2894  CG  PRO C 101     3955   3157   3479    541    266    -25       C  
ATOM   2895  CD  PRO C 101      25.926  15.135   7.989  1.00 27.56           C  
ANISOU 2895  CD  PRO C 101     3973   3051   3445    603    286    -13       C  
ATOM   2896  N   GLY C 102      28.965  14.265   7.155  1.00 21.50           N  
ANISOU 2896  N   GLY C 102     3260   2141   2765    477    284      2       N  
ATOM   2897  CA  GLY C 102      30.058  13.778   6.286  1.00 21.07           C  
ANISOU 2897  CA  GLY C 102     3217   2049   2737    436    282     14       C  
ATOM   2898  C   GLY C 102      31.424  14.239   6.754  1.00 20.88           C  
ANISOU 2898  C   GLY C 102     3235   1951   2746    400    293      6       C  
ATOM   2899  O   GLY C 102      31.522  15.041   7.673  1.00 20.81           O  
ANISOU 2899  O   GLY C 102     3253   1915   2740    408    305     -8       O  
ATOM   2900  N   PRO C 103      32.519  13.679   6.182  1.00 20.30           N  
ANISOU 2900  N   PRO C 103     3165   1851   2695    357    288     11       N  
ATOM   2901  CA  PRO C 103      33.819  14.145   6.581  1.00 20.35           C  
ANISOU 2901  CA  PRO C 103     3206   1800   2727    321    299      0       C  
ATOM   2902  C   PRO C 103      34.114  15.593   6.253  1.00 20.67           C  
ANISOU 2902  C   PRO C 103     3304   1780   2767    348    327      2       C  
ATOM   2903  O   PRO C 103      33.847  15.991   5.150  1.00 21.37           O  
ANISOU 2903  O   PRO C 103     3412   1860   2847    382    335     22       O  
ATOM   2904  CB  PRO C 103      34.791  13.301   5.745  1.00 20.24           C  
ANISOU 2904  CB  PRO C 103     3181   1780   2730    282    289      8       C  
ATOM   2905  CG  PRO C 103      34.008  12.876   4.596  1.00 20.67           C  
ANISOU 2905  CG  PRO C 103     3215   1868   2768    310    283     27       C  
ATOM   2906  CD  PRO C 103      32.644  12.612   5.172  1.00 21.08           C  
ANISOU 2906  CD  PRO C 103     3236   1976   2796    336    274     23       C  
ATOM   2907  N   THR C 104      34.780  16.269   7.179  1.00 21.18           N  
ANISOU 2907  N   THR C 104     3399   1805   2843    324    341    -17       N  
ATOM   2908  CA  THR C 104      35.264  17.648   6.990  1.00 22.17           C  
ANISOU 2908  CA  THR C 104     3590   1862   2969    333    373    -20       C  
ATOM   2909  C   THR C 104      36.246  17.736   5.826  1.00 21.76           C  
ANISOU 2909  C   THR C 104     3561   1776   2928    307    382     -7       C  
ATOM   2910  O   THR C 104      36.233  18.704   5.099  1.00 22.76           O  
ANISOU 2910  O   THR C 104     3740   1858   3047    334    405      5       O  
ATOM   2911  CB  THR C 104      35.989  18.147   8.256  1.00 23.60           C  
ANISOU 2911  CB  THR C 104     3791   2015   3160    292    385    -51       C  
ATOM   2912  OG1 THR C 104      35.532  17.376   9.363  1.00 24.90           O  
ANISOU 2912  OG1 THR C 104     3907   2231   3322    284    363    -64       O  
ATOM   2913  CG2 THR C 104      35.709  19.618   8.500  1.00 25.46           C  
ANISOU 2913  CG2 THR C 104     4093   2194   3385    325    418    -59       C  
ATOM   2914  N   SER C 105      37.097  16.712   5.662  1.00 21.15           N  
ANISOU 2914  N   SER C 105     3447   1722   2866    258    364    -11       N  
ATOM   2915  CA  SER C 105      38.027  16.681   4.529  1.00 20.80           C  
ANISOU 2915  CA  SER C 105     3416   1657   2830    233    370      0       C  
ATOM   2916  C   SER C 105      38.297  15.243   4.114  1.00 19.28           C  
ANISOU 2916  C   SER C 105     3167   1511   2645    211    341      4       C  
ATOM   2917  O   SER C 105      38.078  14.310   4.892  1.00 18.04           O  
ANISOU 2917  O   SER C 105     2970   1393   2491    200    320     -3       O  
ATOM   2918  CB  SER C 105      39.332  17.431   4.861  1.00 22.16           C  
ANISOU 2918  CB  SER C 105     3626   1782   3011    180    393    -22       C  
ATOM   2919  OG  SER C 105      40.217  16.631   5.647  1.00 24.12           O  
ANISOU 2919  OG  SER C 105     3833   2059   3271    130    376    -44       O  
ATOM   2920  N   THR C 106      38.748  15.108   2.863  1.00 19.57           N  
ANISOU 2920  N   THR C 106     3208   1542   2684    206    343     19       N  
ATOM   2921  CA  THR C 106      39.072  13.789   2.311  1.00 18.69           C  
ANISOU 2921  CA  THR C 106     3051   1469   2579    187    320     24       C  
ATOM   2922  C   THR C 106      40.342  13.934   1.481  1.00 18.13           C  
ANISOU 2922  C   THR C 106     2994   1377   2517    152    329     22       C  
ATOM   2923  O   THR C 106      40.722  15.075   1.088  1.00 19.49           O  
ANISOU 2923  O   THR C 106     3212   1505   2684    148    356     25       O  
ATOM   2924  CB  THR C 106      37.925  13.256   1.470  1.00 19.00           C  
ANISOU 2924  CB  THR C 106     3068   1544   2605    227    308     45       C  
ATOM   2925  OG1 THR C 106      37.650  14.107   0.347  1.00 19.27           O  
ANISOU 2925  OG1 THR C 106     3135   1559   2628    259    325     66       O  
ATOM   2926  CG2 THR C 106      36.655  13.105   2.316  1.00 18.79           C  
ANISOU 2926  CG2 THR C 106     3022   1549   2565    257    299     43       C  
ATOM   2927  N   LEU C 107      41.022  12.837   1.256  1.00 17.54           N  
ANISOU 2927  N   LEU C 107     2882   1330   2450    125    311     17       N  
ATOM   2928  CA  LEU C 107      42.231  12.805   0.425  1.00 16.86           C  
ANISOU 2928  CA  LEU C 107     2798   1237   2368     93    317     13       C  
ATOM   2929  C   LEU C 107      42.323  11.390  -0.155  1.00 16.36           C  
ANISOU 2929  C   LEU C 107     2692   1214   2309     93    292     17       C  
ATOM   2930  O   LEU C 107      42.103  10.440   0.573  1.00 17.12           O  
ANISOU 2930  O   LEU C 107     2760   1335   2409     93    273     11       O  
ATOM   2931  CB  LEU C 107      43.475  13.071   1.252  1.00 17.45           C  
ANISOU 2931  CB  LEU C 107     2874   1305   2448     47    324    -13       C  
ATOM   2932  CG  LEU C 107      44.809  13.224   0.550  1.00 18.11           C  
ANISOU 2932  CG  LEU C 107     2960   1388   2531      7    334    -24       C  
ATOM   2933  CD1 LEU C 107      44.898  14.689   0.117  1.00 18.77           C  
ANISOU 2933  CD1 LEU C 107     3101   1423   2607     -2    368    -20       C  
ATOM   2934  CD2 LEU C 107      45.973  12.957   1.499  1.00 18.80           C  
ANISOU 2934  CD2 LEU C 107     3024   1499   2619    -33    329    -54       C  
ATOM   2935  N   VAL C 108      42.644  11.303  -1.427  1.00 16.00           N  
ANISOU 2935  N   VAL C 108     2646   1170   2261     91    295     28       N  
ATOM   2936  CA  VAL C 108      42.867  10.003  -2.067  1.00 15.93           C  
ANISOU 2936  CA  VAL C 108     2601   1194   2255     88    275     28       C  
ATOM   2937  C   VAL C 108      44.201  10.200  -2.769  1.00 16.52           C  
ANISOU 2937  C   VAL C 108     2678   1266   2332     57    284     19       C  
ATOM   2938  O   VAL C 108      44.373  11.228  -3.439  1.00 17.87           O  
ANISOU 2938  O   VAL C 108     2879   1413   2496     52    305     28       O  
ATOM   2939  CB  VAL C 108      41.775   9.699  -3.091  1.00 15.84           C  
ANISOU 2939  CB  VAL C 108     2582   1199   2234    119    271     49       C  
ATOM   2940  CG1 VAL C 108      42.120   8.426  -3.893  1.00 16.00           C  
ANISOU 2940  CG1 VAL C 108     2572   1249   2258    110    255     46       C  
ATOM   2941  CG2 VAL C 108      40.464   9.594  -2.362  1.00 15.62           C  
ANISOU 2941  CG2 VAL C 108     2550   1184   2201    146    265     54       C  
ATOM   2942  N   ARG C 109      45.119   9.260  -2.642  1.00 16.30           N  
ANISOU 2942  N   ARG C 109     2621   1263   2309     39    269      3       N  
ATOM   2943  CA  ARG C 109      46.399   9.258  -3.381  1.00 16.11           C  
ANISOU 2943  CA  ARG C 109     2587   1250   2281     12    275     -7       C  
ATOM   2944  C   ARG C 109      46.659   7.898  -3.984  1.00 15.60           C  
ANISOU 2944  C   ARG C 109     2490   1216   2219     21    254    -10       C  
ATOM   2945  O   ARG C 109      46.630   6.864  -3.271  1.00 15.46           O  
ANISOU 2945  O   ARG C 109     2454   1214   2206     30    236    -17       O  
ATOM   2946  CB  ARG C 109      47.588   9.586  -2.492  1.00 17.48           C  
ANISOU 2946  CB  ARG C 109     2756   1431   2454    -21    280    -33       C  
ATOM   2947  CG  ARG C 109      47.623  11.009  -2.072  1.00 19.41           C  
ANISOU 2947  CG  ARG C 109     3038   1642   2693    -43    306    -37       C  
ATOM   2948  CD  ARG C 109      49.026  11.340  -1.566  1.00 21.54           C  
ANISOU 2948  CD  ARG C 109     3297   1931   2954    -89    315    -68       C  
ATOM   2949  NE  ARG C 109      49.118  12.772  -1.340  1.00 23.15           N  
ANISOU 2949  NE  ARG C 109     3545   2097   3151   -119    346    -74       N  
ATOM   2950  CZ  ARG C 109      49.959  13.333  -0.475  1.00 24.52           C  
ANISOU 2950  CZ  ARG C 109     3721   2279   3317   -161    359   -103       C  
ATOM   2951  NH1 ARG C 109      50.888  12.608   0.149  1.00 25.38           N  
ANISOU 2951  NH1 ARG C 109     3783   2440   3419   -177    342   -128       N  
ATOM   2952  NH2 ARG C 109      49.963  14.663  -0.315  1.00 26.26           N  
ANISOU 2952  NH2 ARG C 109     3991   2455   3529   -191    391   -109       N  
ATOM   2953  N   VAL C 110      46.956   7.914  -5.263  1.00 14.99           N  
ANISOU 2953  N   VAL C 110     2409   1147   2137     17    260     -5       N  
ATOM   2954  CA  VAL C 110      47.463   6.716  -5.905  1.00 14.43           C  
ANISOU 2954  CA  VAL C 110     2309   1105   2066     21    244    -13       C  
ATOM   2955  C   VAL C 110      48.943   6.634  -5.605  1.00 14.92           C  
ANISOU 2955  C   VAL C 110     2353   1190   2123     -2    243    -38       C  
ATOM   2956  O   VAL C 110      49.756   7.401  -6.100  1.00 16.09           O  
ANISOU 2956  O   VAL C 110     2504   1344   2264    -29    259    -45       O  
ATOM   2957  CB  VAL C 110      47.230   6.755  -7.402  1.00 14.08           C  
ANISOU 2957  CB  VAL C 110     2266   1068   2016     25    250      0       C  
ATOM   2958  CG1 VAL C 110      47.826   5.457  -7.984  1.00 13.73           C  
ANISOU 2958  CG1 VAL C 110     2191   1054   1972     29    234    -13       C  
ATOM   2959  CG2 VAL C 110      45.743   6.867  -7.681  1.00 13.69           C  
ANISOU 2959  CG2 VAL C 110     2228   1008   1965     51    251     22       C  
ATOM   2960  N   VAL C 111      49.302   5.640  -4.790  1.00 15.35           N  
ANISOU 2960  N   VAL C 111     2387   1262   2180      9    225    -51       N  
ATOM   2961  CA  VAL C 111      50.610   5.486  -4.290  1.00 15.72           C  
ANISOU 2961  CA  VAL C 111     2412   1340   2218     -3    221    -75       C  
ATOM   2962  C   VAL C 111      51.544   4.857  -5.318  1.00 16.37           C  
ANISOU 2962  C   VAL C 111     2469   1456   2292     -1    216    -87       C  
ATOM   2963  O   VAL C 111      52.680   5.330  -5.533  1.00 17.20           O  
ANISOU 2963  O   VAL C 111     2558   1592   2384    -27    224   -107       O  
ATOM   2964  CB  VAL C 111      50.620   4.677  -2.968  1.00 15.52           C  
ANISOU 2964  CB  VAL C 111     2379   1323   2195     16    203    -82       C  
ATOM   2965  CG1 VAL C 111      52.007   4.245  -2.556  1.00 15.75           C  
ANISOU 2965  CG1 VAL C 111     2377   1397   2209     17    194   -106       C  
ATOM   2966  CG2 VAL C 111      49.884   5.432  -1.897  1.00 15.84           C  
ANISOU 2966  CG2 VAL C 111     2439   1337   2240      9    210    -75       C  
ATOM   2967  N   SER C 112      51.074   3.741  -5.886  1.00 17.05           N  
ANISOU 2967  N   SER C 112     2552   1541   2383     26    203    -80       N  
ATOM   2968  CA  SER C 112      51.843   3.048  -6.946  1.00 17.31           C  
ANISOU 2968  CA  SER C 112     2563   1604   2408     33    198    -92       C  
ATOM   2969  C   SER C 112      50.894   2.288  -7.826  1.00 16.97           C  
ANISOU 2969  C   SER C 112     2529   1545   2373     52    193    -78       C  
ATOM   2970  O   SER C 112      49.868   1.758  -7.373  1.00 16.23           O  
ANISOU 2970  O   SER C 112     2451   1426   2286     67    186    -65       O  
ATOM   2971  CB  SER C 112      52.830   2.048  -6.338  1.00 18.16           C  
ANISOU 2971  CB  SER C 112     2648   1744   2507     57    181   -112       C  
ATOM   2972  OG  SER C 112      52.219   1.088  -5.481  1.00 18.39           O  
ANISOU 2972  OG  SER C 112     2692   1752   2543     87    167   -104       O  
ATOM   2973  N   THR C 113      51.251   2.222  -9.119  1.00 16.17           N  
ANISOU 2973  N   THR C 113     2415   1462   2264     46    198    -82       N  
ATOM   2974  CA  THR C 113      50.525   1.413 -10.082  1.00 16.38           C  
ANISOU 2974  CA  THR C 113     2445   1484   2294     60    194    -75       C  
ATOM   2975  C   THR C 113      51.349   1.214 -11.325  1.00 16.55           C  
ANISOU 2975  C   THR C 113     2445   1538   2305     56    196    -88       C  
ATOM   2976  O   THR C 113      52.073   2.127 -11.749  1.00 17.36           O  
ANISOU 2976  O   THR C 113     2537   1660   2398     32    208    -92       O  
ATOM   2977  CB  THR C 113      49.191   2.057 -10.486  1.00 16.22           C  
ANISOU 2977  CB  THR C 113     2443   1441   2277     54    203    -50       C  
ATOM   2978  OG1 THR C 113      48.436   1.231 -11.357  1.00 17.04           O  
ANISOU 2978  OG1 THR C 113     2545   1548   2379     64    200    -47       O  
ATOM   2979  CG2 THR C 113      49.358   3.505 -11.124  1.00 16.41           C  
ANISOU 2979  CG2 THR C 113     2473   1466   2294     30    222    -38       C  
ATOM   2980  N   ASN C 114      51.219   0.038 -11.951  1.00 16.49           N  
ANISOU 2980  N   ASN C 114     2433   1536   2296     76    188    -96       N  
ATOM   2981  CA  ASN C 114      51.727  -0.155 -13.299  1.00 16.13           C  
ANISOU 2981  CA  ASN C 114     2368   1520   2240     72    191   -107       C  
ATOM   2982  C   ASN C 114      50.582  -0.260 -14.324  1.00 15.19           C  
ANISOU 2982  C   ASN C 114     2256   1392   2121     67    197    -92       C  
ATOM   2983  O   ASN C 114      50.755  -0.759 -15.438  1.00 15.67           O  
ANISOU 2983  O   ASN C 114     2303   1475   2174     68    198   -102       O  
ATOM   2984  CB  ASN C 114      52.712  -1.335 -13.365  1.00 16.56           C  
ANISOU 2984  CB  ASN C 114     2407   1597   2288     98    180   -134       C  
ATOM   2985  CG  ASN C 114      52.050  -2.649 -13.034  1.00 16.49           C  
ANISOU 2985  CG  ASN C 114     2420   1558   2285    126    170   -135       C  
ATOM   2986  OD1 ASN C 114      50.838  -2.690 -12.722  1.00 16.97           O  
ANISOU 2986  OD1 ASN C 114     2504   1587   2356    119    172   -118       O  
ATOM   2987  ND2 ASN C 114      52.829  -3.717 -13.098  1.00 17.06           N  
ANISOU 2987  ND2 ASN C 114     2488   1642   2350    156    161   -157       N  
ATOM   2988  N   TYR C 115      49.392   0.152 -13.914  1.00 15.47           N  
ANISOU 2988  N   TYR C 115     2311   1402   2163     64    200    -71       N  
ATOM   2989  CA  TYR C 115      48.198   0.307 -14.763  1.00 15.25           C  
ANISOU 2989  CA  TYR C 115     2287   1376   2130     60    206    -54       C  
ATOM   2990  C   TYR C 115      47.526  -0.952 -15.285  1.00 14.63           C  
ANISOU 2990  C   TYR C 115     2206   1301   2048     67    201    -65       C  
ATOM   2991  O   TYR C 115      46.285  -1.005 -15.368  1.00 14.40           O  
ANISOU 2991  O   TYR C 115     2183   1271   2015     64    203    -53       O  
ATOM   2992  CB  TYR C 115      48.399   1.248 -15.971  1.00 15.86           C  
ANISOU 2992  CB  TYR C 115     2354   1476   2194     46    219    -43       C  
ATOM   2993  CG  TYR C 115      48.934   2.620 -15.546  1.00 16.03           C  
ANISOU 2993  CG  TYR C 115     2387   1486   2215     31    231    -32       C  
ATOM   2994  CD1 TYR C 115      48.145   3.505 -14.798  1.00 16.71           C  
ANISOU 2994  CD1 TYR C 115     2497   1544   2306     34    237    -10       C  
ATOM   2995  CD2 TYR C 115      50.228   2.953 -15.770  1.00 17.31           C  
ANISOU 2995  CD2 TYR C 115     2537   1667   2371     14    236    -46       C  
ATOM   2996  CE1 TYR C 115      48.656   4.736 -14.390  1.00 16.76           C  
ANISOU 2996  CE1 TYR C 115     2521   1535   2311     16    251     -3       C  
ATOM   2997  CE2 TYR C 115      50.762   4.170 -15.343  1.00 17.55           C  
ANISOU 2997  CE2 TYR C 115     2581   1687   2398     -8    250    -40       C  
ATOM   2998  CZ  TYR C 115      49.962   5.037 -14.633  1.00 17.27           C  
ANISOU 2998  CZ  TYR C 115     2576   1617   2369     -7    258    -19       C  
ATOM   2999  OH  TYR C 115      50.487   6.235 -14.201  1.00 18.17           O  
ANISOU 2999  OH  TYR C 115     2710   1715   2479    -33    275    -16       O  
ATOM   3000  N   ASN C 116      48.326  -1.924 -15.630  1.00 15.24           N  
ANISOU 3000  N   ASN C 116     2276   1388   2124     75    195    -88       N  
ATOM   3001  CA  ASN C 116      47.765  -3.129 -16.223  1.00 15.33           C  
ANISOU 3001  CA  ASN C 116     2292   1401   2131     76    194   -102       C  
ATOM   3002  C   ASN C 116      47.752  -4.312 -15.299  1.00 15.30           C  
ANISOU 3002  C   ASN C 116     2312   1366   2134     90    186   -115       C  
ATOM   3003  O   ASN C 116      47.243  -5.355 -15.726  1.00 15.93           O  
ANISOU 3003  O   ASN C 116     2403   1438   2208     86    188   -128       O  
ATOM   3004  CB  ASN C 116      48.563  -3.443 -17.469  1.00 15.74           C  
ANISOU 3004  CB  ASN C 116     2322   1484   2173     77    196   -120       C  
ATOM   3005  CG  ASN C 116      48.456  -2.345 -18.522  1.00 15.50           C  
ANISOU 3005  CG  ASN C 116     2271   1484   2131     61    205   -105       C  
ATOM   3006  OD1 ASN C 116      47.358  -1.895 -18.897  1.00 15.98           O  
ANISOU 3006  OD1 ASN C 116     2333   1553   2185     53    211    -86       O  
ATOM   3007  ND2 ASN C 116      49.607  -1.960 -19.054  1.00 15.94           N  
ANISOU 3007  ND2 ASN C 116     2309   1565   2181     59    208   -113       N  
ATOM   3008  N   GLN C 117      48.319  -4.163 -14.122  1.00 15.10           N  
ANISOU 3008  N   GLN C 117     2297   1323   2117    103    179   -112       N  
ATOM   3009  CA  GLN C 117      48.366  -5.243 -13.123  1.00 15.21           C  
ANISOU 3009  CA  GLN C 117     2339   1304   2135    121    172   -120       C  
ATOM   3010  C   GLN C 117      47.940  -4.882 -11.740  1.00 14.94           C  
ANISOU 3010  C   GLN C 117     2321   1247   2109    121    168   -104       C  
ATOM   3011  O   GLN C 117      47.034  -5.490 -11.218  1.00 15.22           O  
ANISOU 3011  O   GLN C 117     2381   1257   2144    115    169   -100       O  
ATOM   3012  CB  GLN C 117      49.739  -5.858 -13.086  1.00 15.57           C  
ANISOU 3012  CB  GLN C 117     2381   1358   2177    152    165   -140       C  
ATOM   3013  CG  GLN C 117      49.946  -6.927 -12.027  1.00 15.98           C  
ANISOU 3013  CG  GLN C 117     2467   1376   2229    181    158   -145       C  
ATOM   3014  CD  GLN C 117      51.367  -7.422 -11.918  1.00 16.83           C  
ANISOU 3014  CD  GLN C 117     2567   1500   2328    222    150   -163       C  
ATOM   3015  OE1 GLN C 117      52.329  -6.672 -11.963  1.00 17.98           O  
ANISOU 3015  OE1 GLN C 117     2676   1684   2468    227    146   -168       O  
ATOM   3016  NE2 GLN C 117      51.514  -8.722 -11.706  1.00 17.91           N  
ANISOU 3016  NE2 GLN C 117     2738   1607   2458    254    148   -174       N  
ATOM   3017  N   HIS C 118      48.560  -3.873 -11.136  1.00 14.22           N  
ANISOU 3017  N   HIS C 118     2214   1165   2020    123    166    -97       N  
ATOM   3018  CA  HIS C 118      48.280  -3.537  -9.751  1.00 13.65           C  
ANISOU 3018  CA  HIS C 118     2155   1074   1954    125    162    -85       C  
ATOM   3019  C   HIS C 118      48.119  -2.037  -9.571  1.00 13.70           C  
ANISOU 3019  C   HIS C 118     2149   1090   1965    107    169    -70       C  
ATOM   3020  O   HIS C 118      48.687  -1.294 -10.355  1.00 13.66           O  
ANISOU 3020  O   HIS C 118     2125   1107   1956     98    175    -72       O  
ATOM   3021  CB  HIS C 118      49.352  -3.987  -8.785  1.00 14.16           C  
ANISOU 3021  CB  HIS C 118     2224   1138   2018    151    152    -94       C  
ATOM   3022  CG  HIS C 118      50.674  -3.361  -9.025  1.00 14.43           C  
ANISOU 3022  CG  HIS C 118     2227   1208   2046    156    151   -107       C  
ATOM   3023  ND1 HIS C 118      51.057  -2.175  -8.408  1.00 14.71           N  
ANISOU 3023  ND1 HIS C 118     2248   1258   2082    141    154   -102       N  
ATOM   3024  CD2 HIS C 118      51.657  -3.700  -9.867  1.00 15.03           C  
ANISOU 3024  CD2 HIS C 118     2284   1313   2113    169    150   -125       C  
ATOM   3025  CE1 HIS C 118      52.290  -1.907  -8.816  1.00 15.03           C  
ANISOU 3025  CE1 HIS C 118     2260   1336   2111    142    154   -120       C  
ATOM   3026  NE2 HIS C 118      52.648  -2.795  -9.715  1.00 15.44           N  
ANISOU 3026  NE2 HIS C 118     2307   1400   2157    160    151   -133       N  
ATOM   3027  N   ALA C 119      47.472  -1.699  -8.481  1.00 13.04           N  
ANISOU 3027  N   ALA C 119     2078    988   1886    104    168    -58       N  
ATOM   3028  CA  ALA C 119      47.454  -0.279  -7.980  1.00 13.12           C  
ANISOU 3028  CA  ALA C 119     2084    999   1899     92    175    -47       C  
ATOM   3029  C   ALA C 119      47.333  -0.354  -6.494  1.00 13.51           C  
ANISOU 3029  C   ALA C 119     2146   1034   1953     97    168    -44       C  
ATOM   3030  O   ALA C 119      46.652  -1.256  -5.940  1.00 13.81           O  
ANISOU 3030  O   ALA C 119     2200   1055   1990    104    162    -42       O  
ATOM   3031  CB  ALA C 119      46.315   0.483  -8.557  1.00 13.21           C  
ANISOU 3031  CB  ALA C 119     2099   1010   1909     81    185    -30       C  
ATOM   3032  N   MET C 120      47.901   0.657  -5.820  1.00 13.65           N  
ANISOU 3032  N   MET C 120     2158   1055   1972     90    172    -46       N  
ATOM   3033  CA  MET C 120      47.843   0.775  -4.383  1.00 14.25           C  
ANISOU 3033  CA  MET C 120     2241   1121   2049     92    167    -45       C  
ATOM   3034  C   MET C 120      47.418   2.204  -4.045  1.00 14.51           C  
ANISOU 3034  C   MET C 120     2280   1146   2085     75    180    -36       C  
ATOM   3035  O   MET C 120      48.041   3.158  -4.520  1.00 14.89           O  
ANISOU 3035  O   MET C 120     2324   1202   2132     60    192    -40       O  
ATOM   3036  CB  MET C 120      49.150   0.362  -3.695  1.00 15.61           C  
ANISOU 3036  CB  MET C 120     2401   1313   2214    105    158    -61       C  
ATOM   3037  CG  MET C 120      49.007   0.165  -2.205  1.00 17.20           C  
ANISOU 3037  CG  MET C 120     2612   1508   2415    113    150    -59       C  
ATOM   3038  SD  MET C 120      50.438  -0.507  -1.325  1.00 19.37           S  
ANISOU 3038  SD  MET C 120     2870   1813   2674    139    136    -75       S  
ATOM   3039  CE  MET C 120      51.386   0.956  -1.377  1.00 20.64           C  
ANISOU 3039  CE  MET C 120     3004   2007   2830    108    148    -92       C  
ATOM   3040  N   VAL C 121      46.306   2.286  -3.341  1.00 13.64           N  
ANISOU 3040  N   VAL C 121     2184   1020   1978     78    180    -24       N  
ATOM   3041  CA  VAL C 121      45.604   3.579  -3.156  1.00 13.54           C  
ANISOU 3041  CA  VAL C 121     2182    995   1966     70    193    -14       C  
ATOM   3042  C   VAL C 121      45.389   3.820  -1.680  1.00 13.95           C  
ANISOU 3042  C   VAL C 121     2240   1039   2019     69    190    -16       C  
ATOM   3043  O   VAL C 121      44.881   2.972  -0.987  1.00 13.85           O  
ANISOU 3043  O   VAL C 121     2230   1026   2006     77    179    -13       O  
ATOM   3044  CB  VAL C 121      44.340   3.656  -3.968  1.00 13.32           C  
ANISOU 3044  CB  VAL C 121     2159    965   1935     78    198      1       C  
ATOM   3045  CG1 VAL C 121      43.743   5.078  -3.804  1.00 13.19           C  
ANISOU 3045  CG1 VAL C 121     2157    935   1916     80    213     13       C  
ATOM   3046  CG2 VAL C 121      44.652   3.365  -5.391  1.00 13.43           C  
ANISOU 3046  CG2 VAL C 121     2164    992   1946     77    200      1       C  
ATOM   3047  N   PHE C 122      45.735   5.057  -1.268  1.00 14.17           N  
ANISOU 3047  N   PHE C 122     2275   1059   2047     57    203    -20       N  
ATOM   3048  CA  PHE C 122      45.583   5.542   0.130  1.00 14.50           C  
ANISOU 3048  CA  PHE C 122     2324   1095   2090     53    204    -25       C  
ATOM   3049  C   PHE C 122      44.390   6.501   0.166  1.00 14.68           C  
ANISOU 3049  C   PHE C 122     2366   1098   2112     59    217    -12       C  
ATOM   3050  O   PHE C 122      44.356   7.448  -0.650  1.00 14.82           O  
ANISOU 3050  O   PHE C 122     2399   1102   2129     57    233     -6       O  
ATOM   3051  CB  PHE C 122      46.831   6.321   0.519  1.00 15.33           C  
ANISOU 3051  CB  PHE C 122     2425   1207   2191     30    213    -44       C  
ATOM   3052  CG  PHE C 122      46.737   7.014   1.822  1.00 16.02           C  
ANISOU 3052  CG  PHE C 122     2521   1288   2277     20    219    -53       C  
ATOM   3053  CD1 PHE C 122      47.098   6.435   2.983  1.00 16.27           C  
ANISOU 3053  CD1 PHE C 122     2538   1339   2304     22    206    -63       C  
ATOM   3054  CD2 PHE C 122      46.398   8.369   1.842  1.00 16.58           C  
ANISOU 3054  CD2 PHE C 122     2617   1334   2348      8    240    -52       C  
ATOM   3055  CE1 PHE C 122      47.052   7.103   4.199  1.00 16.05           C  
ANISOU 3055  CE1 PHE C 122     2514   1310   2272     10    211    -73       C  
ATOM   3056  CE2 PHE C 122      46.361   9.044   3.025  1.00 17.07           C  
ANISOU 3056  CE2 PHE C 122     2688   1389   2407     -3    248    -64       C  
ATOM   3057  CZ  PHE C 122      46.677   8.432   4.201  1.00 16.34           C  
ANISOU 3057  CZ  PHE C 122     2575   1320   2310     -3    233    -76       C  
ATOM   3058  N   PHE C 123      43.537   6.296   1.179  1.00 14.62           N  
ANISOU 3058  N   PHE C 123     2360   1090   2102     68    211     -9       N  
ATOM   3059  CA  PHE C 123      42.359   7.153   1.467  1.00 15.30           C  
ANISOU 3059  CA  PHE C 123     2462   1166   2186     81    221      0       C  
ATOM   3060  C   PHE C 123      42.426   7.704   2.876  1.00 15.50           C  
ANISOU 3060  C   PHE C 123     2493   1184   2210     74    224    -11       C  
ATOM   3061  O   PHE C 123      42.744   6.966   3.830  1.00 15.14           O  
ANISOU 3061  O   PHE C 123     2435   1153   2164     67    211    -19       O  
ATOM   3062  CB  PHE C 123      41.067   6.380   1.311  1.00 15.69           C  
ANISOU 3062  CB  PHE C 123     2502   1231   2227     97    211     11       C  
ATOM   3063  CG  PHE C 123      40.916   5.658   0.030  1.00 15.88           C  
ANISOU 3063  CG  PHE C 123     2516   1267   2249    101    207     19       C  
ATOM   3064  CD1 PHE C 123      41.360   4.295  -0.115  1.00 15.62           C  
ANISOU 3064  CD1 PHE C 123     2472   1243   2218     91    193     14       C  
ATOM   3065  CD2 PHE C 123      40.258   6.244  -1.036  1.00 16.49           C  
ANISOU 3065  CD2 PHE C 123     2597   1349   2319    117    217     31       C  
ATOM   3066  CE1 PHE C 123      41.202   3.639  -1.301  1.00 15.93           C  
ANISOU 3066  CE1 PHE C 123     2504   1293   2254     92    191     18       C  
ATOM   3067  CE2 PHE C 123      40.100   5.550  -2.221  1.00 16.63           C  
ANISOU 3067  CE2 PHE C 123     2602   1383   2332    117    213     36       C  
ATOM   3068  CZ  PHE C 123      40.596   4.267  -2.336  1.00 16.23           C  
ANISOU 3068  CZ  PHE C 123     2541   1339   2286    103    201     28       C  
ATOM   3069  N   LYS C 124      42.140   9.009   3.062  1.00 16.58           N  
ANISOU 3069  N   LYS C 124     2653   1300   2345     78    242    -12       N  
ATOM   3070  CA  LYS C 124      42.098   9.628   4.416  1.00 17.67           C  
ANISOU 3070  CA  LYS C 124     2800   1432   2482     71    248    -26       C  
ATOM   3071  C   LYS C 124      40.821  10.459   4.470  1.00 18.54           C  
ANISOU 3071  C   LYS C 124     2929   1530   2585     99    259    -16       C  
ATOM   3072  O   LYS C 124      40.613  11.295   3.581  1.00 19.25           O  
ANISOU 3072  O   LYS C 124     3043   1597   2672    113    275     -6       O  
ATOM   3073  CB  LYS C 124      43.263  10.542   4.672  1.00 18.33           C  
ANISOU 3073  CB  LYS C 124     2898   1500   2567     42    264    -45       C  
ATOM   3074  CG  LYS C 124      43.379  11.070   6.108  1.00 18.65           C  
ANISOU 3074  CG  LYS C 124     2941   1539   2603     28    269    -65       C  
ATOM   3075  CD  LYS C 124      44.306  12.261   6.049  1.00 19.49           C  
ANISOU 3075  CD  LYS C 124     3073   1622   2707     -3    295    -83       C  
ATOM   3076  CE  LYS C 124      44.786  12.731   7.384  1.00 19.99           C  
ANISOU 3076  CE  LYS C 124     3136   1693   2765    -29    301   -110       C  
ATOM   3077  NZ  LYS C 124      45.581  13.954   7.249  1.00 21.30           N  
ANISOU 3077  NZ  LYS C 124     3334   1833   2926    -67    331   -130       N  
ATOM   3078  N   HIS C 125      40.002  10.253   5.493  1.00 19.06           N  
ANISOU 3078  N   HIS C 125     2985   1610   2644    109    252    -19       N  
ATOM   3079  CA  HIS C 125      38.710  10.946   5.659  1.00 19.53           C  
ANISOU 3079  CA  HIS C 125     3057   1669   2693    142    260    -12       C  
ATOM   3080  C   HIS C 125      38.701  11.417   7.095  1.00 18.89           C  
ANISOU 3080  C   HIS C 125     2981   1586   2610    134    264    -30       C  
ATOM   3081  O   HIS C 125      38.898  10.659   8.018  1.00 18.96           O  
ANISOU 3081  O   HIS C 125     2968   1616   2619    116    250    -38       O  
ATOM   3082  CB  HIS C 125      37.517  10.029   5.424  1.00 19.94           C  
ANISOU 3082  CB  HIS C 125     3082   1759   2733    161    245      0       C  
ATOM   3083  CG  HIS C 125      37.341   9.539   4.003  1.00 20.71           C  
ANISOU 3083  CG  HIS C 125     3171   1867   2828    170    242     15       C  
ATOM   3084  ND1 HIS C 125      36.114   9.216   3.476  1.00 22.58           N  
ANISOU 3084  ND1 HIS C 125     3392   2138   3048    193    237     26       N  
ATOM   3085  CD2 HIS C 125      38.230   9.316   3.013  1.00 21.84           C  
ANISOU 3085  CD2 HIS C 125     3317   1997   2981    156    242     20       C  
ATOM   3086  CE1 HIS C 125      36.253   8.774   2.246  1.00 22.90           C  
ANISOU 3086  CE1 HIS C 125     3426   2186   3089    193    235     36       C  
ATOM   3087  NE2 HIS C 125      37.531   8.858   1.923  1.00 22.43           N  
ANISOU 3087  NE2 HIS C 125     3379   2095   3046    172    238     33       N  
ATOM   3088  N   VAL C 126      38.507  12.738   7.275  1.00 18.88           N  
ANISOU 3088  N   VAL C 126     3013   1554   2605    148    286    -36       N  
ATOM   3089  CA  VAL C 126      38.626  13.382   8.572  1.00 19.36           C  
ANISOU 3089  CA  VAL C 126     3084   1605   2664    137    295    -57       C  
ATOM   3090  C   VAL C 126      37.220  13.797   8.963  1.00 19.10           C  
ANISOU 3090  C   VAL C 126     3055   1583   2616    179    298    -53       C  
ATOM   3091  O   VAL C 126      36.516  14.406   8.145  1.00 19.02           O  
ANISOU 3091  O   VAL C 126     3066   1561   2598    218    309    -39       O  
ATOM   3092  CB  VAL C 126      39.481  14.673   8.497  1.00 19.66           C  
ANISOU 3092  CB  VAL C 126     3168   1595   2707    119    323    -72       C  
ATOM   3093  CG1 VAL C 126      39.533  15.388   9.826  1.00 20.36           C  
ANISOU 3093  CG1 VAL C 126     3270   1675   2791    106    335    -98       C  
ATOM   3094  CG2 VAL C 126      40.865  14.320   7.970  1.00 19.31           C  
ANISOU 3094  CG2 VAL C 126     3115   1549   2671     77    322    -78       C  
ATOM   3095  N   PHE C 127      36.843  13.479  10.192  1.00 19.78           N  
ANISOU 3095  N   PHE C 127     3121   1697   2697    173    289    -66       N  
ATOM   3096  CA  PHE C 127      35.566  13.871  10.778  1.00 20.36           C  
ANISOU 3096  CA  PHE C 127     3191   1790   2753    210    291    -68       C  
ATOM   3097  C   PHE C 127      35.960  14.645  12.011  1.00 22.95           C  
ANISOU 3097  C   PHE C 127     3537   2100   3082    194    304    -95       C  
ATOM   3098  O   PHE C 127      36.112  14.099  13.096  1.00 23.05           O  
ANISOU 3098  O   PHE C 127     3524   2140   3093    169    292   -107       O  
ATOM   3099  CB  PHE C 127      34.630  12.708  11.114  1.00 20.47           C  
ANISOU 3099  CB  PHE C 127     3161   1861   2754    213    268    -61       C  
ATOM   3100  CG  PHE C 127      34.238  11.876   9.926  1.00 19.91           C  
ANISOU 3100  CG  PHE C 127     3072   1812   2680    221    257    -40       C  
ATOM   3101  CD1 PHE C 127      35.055  10.854   9.494  1.00 20.72           C  
ANISOU 3101  CD1 PHE C 127     3162   1914   2795    188    244    -33       C  
ATOM   3102  CD2 PHE C 127      33.032  12.013   9.358  1.00 19.35           C  
ANISOU 3102  CD2 PHE C 127     2991   1770   2588    260    258    -30       C  
ATOM   3103  CE1 PHE C 127      34.639  10.016   8.489  1.00 20.56           C  
ANISOU 3103  CE1 PHE C 127     3125   1916   2770    191    235    -18       C  
ATOM   3104  CE2 PHE C 127      32.632  11.244   8.313  1.00 19.91           C  
ANISOU 3104  CE2 PHE C 127     3042   1869   2653    263    249    -14       C  
ATOM   3105  CZ  PHE C 127      33.426  10.221   7.873  1.00 20.38           C  
ANISOU 3105  CZ  PHE C 127     3092   1923   2727    226    237     -9       C  
ATOM   3106  N   GLN C 128      36.138  15.944  11.770  1.00 25.19           N  
ANISOU 3106  N   GLN C 128     3869   2334   3366    208    331   -102       N  
ATOM   3107  CA  GLN C 128      36.696  16.930  12.677  1.00 27.62           C  
ANISOU 3107  CA  GLN C 128     4208   2609   3676    187    352   -130       C  
ATOM   3108  C   GLN C 128      37.999  16.503  13.265  1.00 26.18           C  
ANISOU 3108  C   GLN C 128     4009   2435   3503    127    346   -148       C  
ATOM   3109  O   GLN C 128      39.030  16.747  12.668  1.00 27.37           O  
ANISOU 3109  O   GLN C 128     4177   2557   3662     97    357   -151       O  
ATOM   3110  CB  GLN C 128      35.692  17.323  13.756  1.00 31.60           C  
ANISOU 3110  CB  GLN C 128     4709   3132   4164    216    355   -144       C  
ATOM   3111  CG  GLN C 128      34.292  17.433  13.230  1.00 34.31           C  
ANISOU 3111  CG  GLN C 128     5050   3494   4491    280    352   -126       C  
ATOM   3112  CD  GLN C 128      33.903  18.850  12.891  1.00 36.92           C  
ANISOU 3112  CD  GLN C 128     5440   3772   4813    327    382   -128       C  
ATOM   3113  OE1 GLN C 128      32.748  19.195  13.045  1.00 40.58           O  
ANISOU 3113  OE1 GLN C 128     5903   4256   5257    383    384   -126       O  
ATOM   3114  NE2 GLN C 128      34.859  19.686  12.457  1.00 38.08           N  
ANISOU 3114  NE2 GLN C 128     5642   3853   4971    306    408   -133       N  
ATOM   3115  N   ASN C 129      37.936  15.866  14.424  1.00 25.60           N  
ANISOU 3115  N   ASN C 129     3898   2403   3424    111    329   -160       N  
ATOM   3116  CA  ASN C 129      39.107  15.484  15.145  1.00 25.96           C  
ANISOU 3116  CA  ASN C 129     3924   2466   3473     62    323   -179       C  
ATOM   3117  C   ASN C 129      39.426  13.993  14.975  1.00 23.71           C  
ANISOU 3117  C   ASN C 129     3596   2222   3191     52    293   -160       C  
ATOM   3118  O   ASN C 129      40.426  13.531  15.475  1.00 24.68           O  
ANISOU 3118  O   ASN C 129     3698   2366   3313     19    284   -171       O  
ATOM   3119  CB  ASN C 129      38.939  15.894  16.600  1.00 27.34           C  
ANISOU 3119  CB  ASN C 129     4093   2657   3636     51    328   -206       C  
ATOM   3120  CG  ASN C 129      39.024  17.396  16.798  1.00 30.76           C  
ANISOU 3120  CG  ASN C 129     4578   3042   4067     48    362   -232       C  
ATOM   3121  OD1 ASN C 129      39.639  18.090  16.019  1.00 31.95           O  
ANISOU 3121  OD1 ASN C 129     4766   3147   4224     35    383   -235       O  
ATOM   3122  ND2 ASN C 129      38.402  17.897  17.864  1.00 30.86           N  
ANISOU 3122  ND2 ASN C 129     4594   3061   4068     59    370   -252       N  
ATOM   3123  N   ARG C 130      38.623  13.299  14.209  1.00 19.93           N  
ANISOU 3123  N   ARG C 130     3105   1753   2712     80    280   -134       N  
ATOM   3124  CA  ARG C 130      38.826  11.854  13.984  1.00 19.85           C  
ANISOU 3124  CA  ARG C 130     3063   1773   2704     71    254   -116       C  
ATOM   3125  C   ARG C 130      39.235  11.607  12.541  1.00 19.03           C  
ANISOU 3125  C   ARG C 130     2967   1651   2612     75    254    -99       C  
ATOM   3126  O   ARG C 130      38.501  11.918  11.577  1.00 20.34           O  
ANISOU 3126  O   ARG C 130     3147   1802   2778    102    261    -85       O  
ATOM   3127  CB  ARG C 130      37.557  11.091  14.370  1.00 19.66           C  
ANISOU 3127  CB  ARG C 130     3018   1784   2667     90    239   -103       C  
ATOM   3128  CG  ARG C 130      37.502  10.845  15.853  1.00 20.77           C  
ANISOU 3128  CG  ARG C 130     3141   1953   2795     75    232   -116       C  
ATOM   3129  CD  ARG C 130      36.153  10.217  16.303  1.00 20.32           C  
ANISOU 3129  CD  ARG C 130     3065   1934   2721     89    221   -106       C  
ATOM   3130  NE  ARG C 130      36.039   8.792  15.994  1.00 20.26           N  
ANISOU 3130  NE  ARG C 130     3041   1945   2709     78    202    -86       N  
ATOM   3131  CZ  ARG C 130      36.554   7.812  16.741  1.00 19.43           C  
ANISOU 3131  CZ  ARG C 130     2926   1857   2599     56    188    -82       C  
ATOM   3132  NH1 ARG C 130      37.201   8.082  17.887  1.00 19.72           N  
ANISOU 3132  NH1 ARG C 130     2957   1903   2631     43    188    -97       N  
ATOM   3133  NH2 ARG C 130      36.399   6.523  16.364  1.00 19.75           N  
ANISOU 3133  NH2 ARG C 130     2962   1906   2635     49    175    -62       N  
ATOM   3134  N   GLU C 131      40.424  11.071  12.407  1.00 18.41           N  
ANISOU 3134  N   GLU C 131     2877   1577   2538     49    247   -103       N  
ATOM   3135  CA  GLU C 131      41.084  10.910  11.122  1.00 17.91           C  
ANISOU 3135  CA  GLU C 131     2819   1498   2484     46    248    -93       C  
ATOM   3136  C   GLU C 131      41.111   9.402  10.806  1.00 17.19           C  
ANISOU 3136  C   GLU C 131     2703   1432   2393     50    224    -76       C  
ATOM   3137  O   GLU C 131      41.831   8.660  11.478  1.00 17.58           O  
ANISOU 3137  O   GLU C 131     2735   1504   2439     37    211    -81       O  
ATOM   3138  CB  GLU C 131      42.466  11.485  11.164  1.00 19.45           C  
ANISOU 3138  CB  GLU C 131     3020   1686   2682     13    260   -114       C  
ATOM   3139  CG  GLU C 131      42.412  13.030  11.374  1.00 20.73           C  
ANISOU 3139  CG  GLU C 131     3219   1813   2843      4    290   -133       C  
ATOM   3140  CD  GLU C 131      43.704  13.771  11.176  1.00 22.34           C  
ANISOU 3140  CD  GLU C 131     3438   2004   3046    -35    309   -155       C  
ATOM   3141  OE1 GLU C 131      44.725  13.189  10.835  1.00 22.30           O  
ANISOU 3141  OE1 GLU C 131     3410   2022   3040    -56    300   -159       O  
ATOM   3142  OE2 GLU C 131      43.725  15.035  11.356  1.00 23.46           O  
ANISOU 3142  OE2 GLU C 131     3618   2110   3185    -50    337   -172       O  
ATOM   3143  N   TYR C 132      40.361   8.996   9.805  1.00 15.38           N  
ANISOU 3143  N   TYR C 132     2475   1200   2166     69    221    -57       N  
ATOM   3144  CA  TYR C 132      40.419   7.550   9.360  1.00 15.05           C  
ANISOU 3144  CA  TYR C 132     2417   1174   2124     69    202    -42       C  
ATOM   3145  C   TYR C 132      41.342   7.519   8.186  1.00 15.15           C  
ANISOU 3145  C   TYR C 132     2433   1174   2147     64    205    -41       C  
ATOM   3146  O   TYR C 132      41.470   8.477   7.461  1.00 15.89           O  
ANISOU 3146  O   TYR C 132     2542   1248   2246     66    220    -42       O  
ATOM   3147  CB  TYR C 132      39.070   7.067   8.990  1.00 14.74           C  
ANISOU 3147  CB  TYR C 132     2375   1147   2078     84    197    -27       C  
ATOM   3148  CG  TYR C 132      38.112   6.966  10.180  1.00 15.42           C  
ANISOU 3148  CG  TYR C 132     2453   1255   2149     85    194    -30       C  
ATOM   3149  CD1 TYR C 132      37.327   8.070  10.555  1.00 16.04           C  
ANISOU 3149  CD1 TYR C 132     2537   1333   2221    101    206    -37       C  
ATOM   3150  CD2 TYR C 132      37.950   5.846  10.871  1.00 16.25           C  
ANISOU 3150  CD2 TYR C 132     2548   1378   2245     73    180    -26       C  
ATOM   3151  CE1 TYR C 132      36.448   7.997  11.624  1.00 16.43           C  
ANISOU 3151  CE1 TYR C 132     2576   1408   2256    102    203    -42       C  
ATOM   3152  CE2 TYR C 132      37.118   5.745  11.945  1.00 16.24           C  
ANISOU 3152  CE2 TYR C 132     2540   1400   2229     69    177    -28       C  
ATOM   3153  CZ  TYR C 132      36.323   6.805  12.337  1.00 16.67           C  
ANISOU 3153  CZ  TYR C 132     2593   1463   2277     83    188    -37       C  
ATOM   3154  OH  TYR C 132      35.454   6.677  13.398  1.00 18.12           O  
ANISOU 3154  OH  TYR C 132     2766   1676   2443     80    185    -42       O  
ATOM   3155  N   PHE C 133      41.986   6.370   7.972  1.00 14.81           N  
ANISOU 3155  N   PHE C 133     2378   1143   2104     60    190    -37       N  
ATOM   3156  CA  PHE C 133      42.714   6.162   6.736  1.00 14.90           C  
ANISOU 3156  CA  PHE C 133     2389   1148   2122     59    191    -34       C  
ATOM   3157  C   PHE C 133      42.629   4.696   6.364  1.00 15.39           C  
ANISOU 3157  C   PHE C 133     2445   1219   2183     67    175    -23       C  
ATOM   3158  O   PHE C 133      42.371   3.840   7.208  1.00 16.06           O  
ANISOU 3158  O   PHE C 133     2528   1313   2260     68    163    -19       O  
ATOM   3159  CB  PHE C 133      44.169   6.637   6.775  1.00 15.14           C  
ANISOU 3159  CB  PHE C 133     2414   1182   2154     43    196    -52       C  
ATOM   3160  CG  PHE C 133      45.060   5.923   7.763  1.00 14.94           C  
ANISOU 3160  CG  PHE C 133     2371   1183   2120     39    182    -62       C  
ATOM   3161  CD1 PHE C 133      44.935   6.097   9.127  1.00 15.31           C  
ANISOU 3161  CD1 PHE C 133     2414   1243   2159     35    180    -70       C  
ATOM   3162  CD2 PHE C 133      46.008   4.965   7.317  1.00 14.78           C  
ANISOU 3162  CD2 PHE C 133     2338   1181   2097     47    170    -62       C  
ATOM   3163  CE1 PHE C 133      45.770   5.422  10.008  1.00 15.52           C  
ANISOU 3163  CE1 PHE C 133     2423   1299   2172     37    166    -77       C  
ATOM   3164  CE2 PHE C 133      46.841   4.323   8.171  1.00 14.96           C  
ANISOU 3164  CE2 PHE C 133     2345   1231   2107     53    157    -70       C  
ATOM   3165  CZ  PHE C 133      46.700   4.494   9.522  1.00 15.45           C  
ANISOU 3165  CZ  PHE C 133     2402   1306   2159     49    154    -75       C  
ATOM   3166  N   HIS C 134      42.856   4.482   5.062  1.00 14.87           N  
ANISOU 3166  N   HIS C 134     2379   1148   2122     70    176    -18       N  
ATOM   3167  CA  HIS C 134      42.765   3.098   4.520  1.00 15.47           C  
ANISOU 3167  CA  HIS C 134     2454   1227   2196     76    165    -10       C  
ATOM   3168  C   HIS C 134      43.734   2.990   3.384  1.00 15.67           C  
ANISOU 3168  C   HIS C 134     2474   1251   2227     77    166    -14       C  
ATOM   3169  O   HIS C 134      44.055   3.958   2.767  1.00 15.88           O  
ANISOU 3169  O   HIS C 134     2499   1274   2258     72    177    -18       O  
ATOM   3170  CB  HIS C 134      41.372   2.977   3.998  1.00 16.30           C  
ANISOU 3170  CB  HIS C 134     2562   1332   2296     77    168      0       C  
ATOM   3171  CG  HIS C 134      41.002   1.619   3.527  1.00 17.82           C  
ANISOU 3171  CG  HIS C 134     2758   1526   2483     75    161      6       C  
ATOM   3172  ND1 HIS C 134      40.130   0.810   4.204  1.00 19.69           N  
ANISOU 3172  ND1 HIS C 134     3002   1768   2708     66    156     10       N  
ATOM   3173  CD2 HIS C 134      41.298   0.982   2.378  1.00 18.92           C  
ANISOU 3173  CD2 HIS C 134     2899   1664   2626     76    160      6       C  
ATOM   3174  CE1 HIS C 134      39.964  -0.318   3.531  1.00 19.30           C  
ANISOU 3174  CE1 HIS C 134     2962   1715   2655     59    154     12       C  
ATOM   3175  NE2 HIS C 134      40.676  -0.243   2.419  1.00 19.92           N  
ANISOU 3175  NE2 HIS C 134     3036   1789   2742     67    155      9       N  
ATOM   3176  N   ILE C 135      44.193   1.768   3.107  1.00 14.61           N  
ANISOU 3176  N   ILE C 135     2340   1120   2090     85    155    -14       N  
ATOM   3177  CA  ILE C 135      44.997   1.445   1.944  1.00 14.74           C  
ANISOU 3177  CA  ILE C 135     2350   1140   2110     89    155    -19       C  
ATOM   3178  C   ILE C 135      44.357   0.305   1.222  1.00 14.76           C  
ANISOU 3178  C   ILE C 135     2362   1134   2110     94    151    -11       C  
ATOM   3179  O   ILE C 135      44.087  -0.746   1.823  1.00 14.14           O  
ANISOU 3179  O   ILE C 135     2299   1048   2025     98    143     -7       O  
ATOM   3180  CB  ILE C 135      46.455   1.130   2.318  1.00 15.36           C  
ANISOU 3180  CB  ILE C 135     2416   1234   2182     98    147    -32       C  
ATOM   3181  CG1 ILE C 135      47.042   2.132   3.354  1.00 15.18           C  
ANISOU 3181  CG1 ILE C 135     2383   1227   2157     87    150    -43       C  
ATOM   3182  CG2 ILE C 135      47.340   1.018   1.082  1.00 15.79           C  
ANISOU 3182  CG2 ILE C 135     2459   1300   2238    101    148    -40       C  
ATOM   3183  CD1 ILE C 135      46.878   1.748   4.787  1.00 15.23           C  
ANISOU 3183  CD1 ILE C 135     2393   1239   2155     94    141    -41       C  
ATOM   3184  N   THR C 136      44.136   0.463  -0.063  1.00 14.02           N  
ANISOU 3184  N   THR C 136     2265   1043   2020     90    157    -10       N  
ATOM   3185  CA  THR C 136      43.617  -0.665  -0.855  1.00 14.65           C  
ANISOU 3185  CA  THR C 136     2352   1118   2095     90    155     -8       C  
ATOM   3186  C   THR C 136      44.632  -1.091  -1.876  1.00 14.64           C  
ANISOU 3186  C   THR C 136     2345   1121   2096     98    153    -17       C  
ATOM   3187  O   THR C 136      45.214  -0.278  -2.610  1.00 14.39           O  
ANISOU 3187  O   THR C 136     2298   1101   2068     96    159    -20       O  
ATOM   3188  CB  THR C 136      42.302  -0.289  -1.521  1.00 14.55           C  
ANISOU 3188  CB  THR C 136     2335   1113   2078     79    163      0       C  
ATOM   3189  OG1 THR C 136      41.370   0.110  -0.513  1.00 15.74           O  
ANISOU 3189  OG1 THR C 136     2489   1266   2223     75    164      5       O  
ATOM   3190  CG2 THR C 136      41.801  -1.462  -2.314  1.00 15.52           C  
ANISOU 3190  CG2 THR C 136     2465   1236   2193     71    163     -3       C  
ATOM   3191  N   LEU C 137      44.810  -2.441  -1.970  1.00 14.29           N  
ANISOU 3191  N   LEU C 137     2316   1066   2046    107    147    -21       N  
ATOM   3192  CA  LEU C 137      45.649  -3.087  -3.002  1.00 14.72           C  
ANISOU 3192  CA  LEU C 137     2367   1123   2100    119    146    -32       C  
ATOM   3193  C   LEU C 137      44.710  -3.641  -4.050  1.00 14.39           C  
ANISOU 3193  C   LEU C 137     2333   1078   2055    104    152    -32       C  
ATOM   3194  O   LEU C 137      43.880  -4.525  -3.773  1.00 15.02           O  
ANISOU 3194  O   LEU C 137     2437   1142   2128     94    154    -30       O  
ATOM   3195  CB  LEU C 137      46.514  -4.188  -2.408  1.00 15.21           C  
ANISOU 3195  CB  LEU C 137     2446   1174   2155    145    136    -38       C  
ATOM   3196  CG  LEU C 137      47.403  -4.953  -3.370  1.00 15.82           C  
ANISOU 3196  CG  LEU C 137     2524   1256   2229    166    134    -51       C  
ATOM   3197  CD1 LEU C 137      48.511  -4.086  -3.904  1.00 15.48           C  
ANISOU 3197  CD1 LEU C 137     2445   1247   2187    171    133    -62       C  
ATOM   3198  CD2 LEU C 137      47.948  -6.318  -2.837  1.00 17.10           C  
ANISOU 3198  CD2 LEU C 137     2718   1397   2380    199    127    -54       C  
ATOM   3199  N   TYR C 138      44.841  -3.179  -5.258  1.00 13.60           N  
ANISOU 3199  N   TYR C 138     2214    995   1957    100    158    -35       N  
ATOM   3200  CA  TYR C 138      43.987  -3.481  -6.375  1.00 14.18           C  
ANISOU 3200  CA  TYR C 138     2285   1077   2024     84    165    -37       C  
ATOM   3201  C   TYR C 138      44.727  -4.267  -7.401  1.00 14.11           C  
ANISOU 3201  C   TYR C 138     2277   1071   2014     92    165    -51       C  
ATOM   3202  O   TYR C 138      45.931  -4.027  -7.614  1.00 13.73           O  
ANISOU 3202  O   TYR C 138     2215   1031   1969    109    161    -58       O  
ATOM   3203  CB  TYR C 138      43.593  -2.145  -7.047  1.00 14.30           C  
ANISOU 3203  CB  TYR C 138     2277   1115   2039     78    172    -27       C  
ATOM   3204  CG  TYR C 138      42.553  -1.276  -6.392  1.00 14.60           C  
ANISOU 3204  CG  TYR C 138     2314   1157   2075     73    176    -13       C  
ATOM   3205  CD1 TYR C 138      41.238  -1.696  -6.193  1.00 15.43           C  
ANISOU 3205  CD1 TYR C 138     2422   1270   2168     61    178    -10       C  
ATOM   3206  CD2 TYR C 138      42.867   0.073  -6.112  1.00 14.82           C  
ANISOU 3206  CD2 TYR C 138     2336   1185   2109     80    180     -4       C  
ATOM   3207  CE1 TYR C 138      40.272  -0.856  -5.687  1.00 15.51           C  
ANISOU 3207  CE1 TYR C 138     2426   1292   2172     61    181      0       C  
ATOM   3208  CE2 TYR C 138      41.919   0.945  -5.582  1.00 15.70           C  
ANISOU 3208  CE2 TYR C 138     2448   1299   2216     82    185      7       C  
ATOM   3209  CZ  TYR C 138      40.628   0.508  -5.395  1.00 15.74           C  
ANISOU 3209  CZ  TYR C 138     2452   1317   2209     76    185     10       C  
ATOM   3210  OH  TYR C 138      39.664   1.330  -4.876  1.00 17.30           O  
ANISOU 3210  OH  TYR C 138     2648   1524   2400     83    189     20       O  
ATOM   3211  N   GLY C 139      44.036  -5.234  -8.040  1.00 14.90           N  
ANISOU 3211  N   GLY C 139     2389   1165   2104     78    170    -59       N  
ATOM   3212  CA  GLY C 139      44.563  -5.917  -9.237  1.00 15.00           C  
ANISOU 3212  CA  GLY C 139     2400   1184   2114     82    172    -76       C  
ATOM   3213  C   GLY C 139      43.631  -5.721 -10.407  1.00 14.65           C  
ANISOU 3213  C   GLY C 139     2337   1167   2060     59    181    -78       C  
ATOM   3214  O   GLY C 139      42.405  -5.491 -10.230  1.00 14.72           O  
ANISOU 3214  O   GLY C 139     2343   1187   2060     38    186    -70       O  
ATOM   3215  N   ARG C 140      44.160  -5.883 -11.603  1.00 15.50           N  
ANISOU 3215  N   ARG C 140     2431   1292   2165     62    184    -90       N  
ATOM   3216  CA  ARG C 140      43.334  -5.895 -12.783  1.00 16.45           C  
ANISOU 3216  CA  ARG C 140     2535   1443   2272     40    192    -94       C  
ATOM   3217  C   ARG C 140      42.638  -7.282 -12.918  1.00 17.60           C  
ANISOU 3217  C   ARG C 140     2707   1574   2406     17    199   -113       C  
ATOM   3218  O   ARG C 140      41.633  -7.416 -13.598  1.00 18.89           O  
ANISOU 3218  O   ARG C 140     2859   1765   2553     -9    207   -119       O  
ATOM   3219  CB  ARG C 140      44.114  -5.594 -14.038  1.00 16.23           C  
ANISOU 3219  CB  ARG C 140     2482   1441   2243     48    193   -101       C  
ATOM   3220  CG  ARG C 140      44.525  -4.133 -14.194  1.00 16.11           C  
ANISOU 3220  CG  ARG C 140     2443   1446   2232     58    192    -83       C  
ATOM   3221  CD  ARG C 140      43.343  -3.255 -14.272  1.00 15.56           C  
ANISOU 3221  CD  ARG C 140     2362   1396   2153     48    197    -63       C  
ATOM   3222  NE  ARG C 140      43.766  -1.882 -14.647  1.00 15.64           N  
ANISOU 3222  NE  ARG C 140     2357   1420   2164     58    201    -45       N  
ATOM   3223  CZ  ARG C 140      42.964  -0.861 -14.924  1.00 15.78           C  
ANISOU 3223  CZ  ARG C 140     2366   1455   2171     60    207    -24       C  
ATOM   3224  NH1 ARG C 140      41.659  -0.949 -14.798  1.00 15.94           N  
ANISOU 3224  NH1 ARG C 140     2383   1492   2178     58    209    -18       N  
ATOM   3225  NH2 ARG C 140      43.495   0.307 -15.291  1.00 16.49           N  
ANISOU 3225  NH2 ARG C 140     2454   1549   2261     67    213     -8       N  
ATOM   3226  N   THR C 141      43.163  -8.281 -12.240  1.00 18.94           N  
ANISOU 3226  N   THR C 141     2915   1701   2580     27    198   -123       N  
ATOM   3227  CA  THR C 141      42.440  -9.535 -12.061  1.00 20.55           C  
ANISOU 3227  CA  THR C 141     3158   1878   2772      1    208   -137       C  
ATOM   3228  C   THR C 141      42.317  -9.694 -10.536  1.00 20.82           C  
ANISOU 3228  C   THR C 141     3224   1876   2811      6    203   -123       C  
ATOM   3229  O   THR C 141      42.773  -8.870  -9.789  1.00 20.97           O  
ANISOU 3229  O   THR C 141     3228   1896   2841     29    193   -106       O  
ATOM   3230  CB  THR C 141      43.206 -10.702 -12.633  1.00 21.83           C  
ANISOU 3230  CB  THR C 141     3350   2011   2931     13    212   -160       C  
ATOM   3231  OG1 THR C 141      44.441 -10.811 -11.949  1.00 24.35           O  
ANISOU 3231  OG1 THR C 141     3685   2303   3263     59    202   -156       O  
ATOM   3232  CG2 THR C 141      43.463 -10.485 -14.110  1.00 22.03           C  
ANISOU 3232  CG2 THR C 141     3341   2076   2953     11    215   -175       C  
ATOM   3233  N   LYS C 142      41.711 -10.797 -10.105  1.00 22.11           N  
ANISOU 3233  N   LYS C 142     3432   2006   2962    -18    213   -132       N  
ATOM   3234  CA  LYS C 142      41.347 -10.922  -8.702  1.00 22.97           C  
ANISOU 3234  CA  LYS C 142     3568   2087   3069    -22    212   -117       C  
ATOM   3235  C   LYS C 142      42.513 -11.374  -7.812  1.00 22.75           C  
ANISOU 3235  C   LYS C 142     3577   2015   3052     22    203   -110       C  
ATOM   3236  O   LYS C 142      42.362 -11.358  -6.604  1.00 24.10           O  
ANISOU 3236  O   LYS C 142     3766   2166   3221     25    199    -95       O  
ATOM   3237  CB  LYS C 142      40.103 -11.854  -8.522  1.00 24.54           C  
ANISOU 3237  CB  LYS C 142     3803   2273   3246    -76    229   -128       C  
ATOM   3238  CG  LYS C 142      39.077 -11.725  -9.647  1.00 26.98           C  
ANISOU 3238  CG  LYS C 142     4078   2633   3538   -120    240   -145       C  
ATOM   3239  CD  LYS C 142      37.659 -12.143  -9.261  1.00 29.80           C  
ANISOU 3239  CD  LYS C 142     4446   3005   3869   -179    254   -152       C  
ATOM   3240  CE  LYS C 142      36.809 -12.557 -10.451  1.00 31.63           C  
ANISOU 3240  CE  LYS C 142     4662   3279   4077   -228    270   -179       C  
ATOM   3241  NZ  LYS C 142      35.345 -12.506 -10.177  1.00 34.66           N  
ANISOU 3241  NZ  LYS C 142     5027   3710   4430   -282    280   -186       N  
ATOM   3242  N   GLU C 143      43.659 -11.767  -8.384  1.00 24.23           N  
ANISOU 3242  N   GLU C 143     3771   2192   3244     59    199   -121       N  
ATOM   3243  CA  GLU C 143      44.848 -12.120  -7.630  1.00 25.49           C  
ANISOU 3243  CA  GLU C 143     3954   2323   3408    112    189   -115       C  
ATOM   3244  C   GLU C 143      46.089 -11.312  -8.060  1.00 24.77           C  
ANISOU 3244  C   GLU C 143     3815   2269   3327    151    176   -117       C  
ATOM   3245  O   GLU C 143      46.118 -10.678  -9.125  1.00 24.45           O  
ANISOU 3245  O   GLU C 143     3732   2266   3290    139    177   -125       O  
ATOM   3246  CB  GLU C 143      45.130 -13.635  -7.775  1.00 28.99           C  
ANISOU 3246  CB  GLU C 143     4463   2713   3839    126    200   -130       C  
ATOM   3247  CG  GLU C 143      44.151 -14.508  -6.984  1.00 30.70           C  
ANISOU 3247  CG  GLU C 143     4740   2881   4041     91    214   -124       C  
ATOM   3248  CD  GLU C 143      43.013 -15.101  -7.795  1.00 33.60           C  
ANISOU 3248  CD  GLU C 143     5127   3243   4396     28    235   -144       C  
ATOM   3249  OE1 GLU C 143      42.951 -14.859  -9.023  1.00 36.94           O  
ANISOU 3249  OE1 GLU C 143     5514   3701   4821     14    238   -161       O  
ATOM   3250  OE2 GLU C 143      42.179 -15.821  -7.187  1.00 35.77           O  
ANISOU 3250  OE2 GLU C 143     5452   3482   4655     -9    250   -142       O  
ATOM   3251  N   LEU C 144      47.080 -11.314  -7.171  1.00 23.86           N  
ANISOU 3251  N   LEU C 144     3705   2149   3212    196    164   -110       N  
ATOM   3252  CA  LEU C 144      48.343 -10.650  -7.364  1.00 23.87           C  
ANISOU 3252  CA  LEU C 144     3664   2188   3217    232    152   -115       C  
ATOM   3253  C   LEU C 144      49.505 -11.522  -6.868  1.00 24.78           C  
ANISOU 3253  C   LEU C 144     3806   2289   3321    293    145   -120       C  
ATOM   3254  O   LEU C 144      49.291 -12.505  -6.122  1.00 25.73           O  
ANISOU 3254  O   LEU C 144     3981   2361   3431    309    148   -113       O  
ATOM   3255  CB  LEU C 144      48.345  -9.247  -6.687  1.00 23.01           C  
ANISOU 3255  CB  LEU C 144     3512   2112   3117    220    144   -100       C  
ATOM   3256  CG  LEU C 144      47.647  -8.091  -7.409  1.00 22.39           C  
ANISOU 3256  CG  LEU C 144     3395   2063   3047    180    150    -96       C  
ATOM   3257  CD1 LEU C 144      47.696  -6.880  -6.449  1.00 21.69           C  
ANISOU 3257  CD1 LEU C 144     3283   1992   2966    175    144    -81       C  
ATOM   3258  CD2 LEU C 144      48.249  -7.725  -8.759  1.00 22.31           C  
ANISOU 3258  CD2 LEU C 144     3351   2087   3038    180    152   -110       C  
ATOM   3259  N   THR C 145      50.730 -11.196  -7.273  1.00 25.95           N  
ANISOU 3259  N   THR C 145     3915   2478   3464    328    136   -132       N  
ATOM   3260  CA  THR C 145      51.925 -11.910  -6.792  1.00 26.74           C  
ANISOU 3260  CA  THR C 145     4029   2580   3548    395    126   -139       C  
ATOM   3261  C   THR C 145      52.106 -11.831  -5.266  1.00 27.29           C  
ANISOU 3261  C   THR C 145     4111   2645   3610    419    117   -120       C  
ATOM   3262  O   THR C 145      51.570 -10.931  -4.605  1.00 26.18           O  
ANISOU 3262  O   THR C 145     3951   2516   3480    383    115   -105       O  
ATOM   3263  CB  THR C 145      53.222 -11.412  -7.449  1.00 26.32           C  
ANISOU 3263  CB  THR C 145     3920   2590   3487    423    118   -158       C  
ATOM   3264  OG1 THR C 145      53.373  -9.981  -7.257  1.00 24.87           O  
ANISOU 3264  OG1 THR C 145     3680   2455   3312    391    113   -153       O  
ATOM   3265  CG2 THR C 145      53.235 -11.743  -8.929  1.00 26.88           C  
ANISOU 3265  CG2 THR C 145     3985   2666   3560    413    127   -179       C  
ATOM   3266  N   SER C 146      52.823 -12.800  -4.706  1.00 27.92           N  
ANISOU 3266  N   SER C 146     4227   2709   3671    481    111   -119       N  
ATOM   3267  CA  SER C 146      53.223 -12.735  -3.304  1.00 28.29           C  
ANISOU 3267  CA  SER C 146     4277   2765   3705    515    100   -103       C  
ATOM   3268  C   SER C 146      54.009 -11.471  -3.033  1.00 27.49           C  
ANISOU 3268  C   SER C 146     4101   2740   3603    511     88   -109       C  
ATOM   3269  O   SER C 146      53.823 -10.835  -2.017  1.00 26.13           O  
ANISOU 3269  O   SER C 146     3915   2579   3431    496     83    -96       O  
ATOM   3270  CB  SER C 146      54.062 -13.940  -2.895  1.00 29.41           C  
ANISOU 3270  CB  SER C 146     4464   2889   3820    596     95   -102       C  
ATOM   3271  OG  SER C 146      55.424 -13.719  -3.217  1.00 30.91           O  
ANISOU 3271  OG  SER C 146     4602   3147   3993    648     83   -121       O  
ATOM   3272  N   GLU C 147      54.890 -11.114  -3.959  1.00 28.76           N  
ANISOU 3272  N   GLU C 147     4215   2952   3760    522     85   -131       N  
ATOM   3273  CA  GLU C 147      55.770  -9.942  -3.810  1.00 27.04           C  
ANISOU 3273  CA  GLU C 147     3927   2811   3536    513     77   -143       C  
ATOM   3274  C   GLU C 147      55.026  -8.595  -3.606  1.00 26.14           C  
ANISOU 3274  C   GLU C 147     3787   2702   3444    442     83   -134       C  
ATOM   3275  O   GLU C 147      55.304  -7.868  -2.674  1.00 25.25           O  
ANISOU 3275  O   GLU C 147     3648   2620   3325    435     78   -131       O  
ATOM   3276  CB  GLU C 147      56.624  -9.836  -5.060  1.00 29.68           C  
ANISOU 3276  CB  GLU C 147     4221   3191   3863    522     78   -170       C  
ATOM   3277  CG  GLU C 147      57.985  -9.203  -4.914  1.00 31.81           C  
ANISOU 3277  CG  GLU C 147     4426   3549   4109    542     68   -190       C  
ATOM   3278  CD  GLU C 147      59.015  -9.884  -5.822  1.00 33.13           C  
ANISOU 3278  CD  GLU C 147     4576   3756   4255    593     65   -216       C  
ATOM   3279  OE1 GLU C 147      60.049  -9.255  -6.137  1.00 36.12           O  
ANISOU 3279  OE1 GLU C 147     4892   4214   4615    592     61   -238       O  
ATOM   3280  OE2 GLU C 147      58.842 -11.081  -6.207  1.00 35.02           O  
ANISOU 3280  OE2 GLU C 147     4863   3948   4492    636     67   -215       O  
ATOM   3281  N   LEU C 148      54.100  -8.338  -4.513  1.00 24.59           N  
ANISOU 3281  N   LEU C 148     3598   2477   3268    396     94   -131       N  
ATOM   3282  CA  LEU C 148      53.283  -7.124  -4.517  1.00 23.13           C  
ANISOU 3282  CA  LEU C 148     3395   2290   3101    336    102   -121       C  
ATOM   3283  C   LEU C 148      52.474  -7.095  -3.234  1.00 23.00           C  
ANISOU 3283  C   LEU C 148     3407   2243   3090    326    100   -101       C  
ATOM   3284  O   LEU C 148      52.285  -6.046  -2.671  1.00 21.52           O  
ANISOU 3284  O   LEU C 148     3198   2070   2908    298    102    -95       O  
ATOM   3285  CB  LEU C 148      52.354  -7.074  -5.721  1.00 22.75           C  
ANISOU 3285  CB  LEU C 148     3355   2218   3068    299    114   -120       C  
ATOM   3286  CG  LEU C 148      52.962  -6.921  -7.100  1.00 22.30           C  
ANISOU 3286  CG  LEU C 148     3269   2193   3009    296    118   -138       C  
ATOM   3287  CD1 LEU C 148      51.935  -7.234  -8.168  1.00 22.34           C  
ANISOU 3287  CD1 LEU C 148     3292   2169   3024    269    128   -136       C  
ATOM   3288  CD2 LEU C 148      53.496  -5.502  -7.278  1.00 23.12           C  
ANISOU 3288  CD2 LEU C 148     3326   2344   3113    266    121   -143       C  
ATOM   3289  N   LYS C 149      51.942  -8.241  -2.810  1.00 21.59           N  
ANISOU 3289  N   LYS C 149     3279   2017   2907    347    100    -90       N  
ATOM   3290  CA  LYS C 149      51.135  -8.323  -1.593  1.00 23.09           C  
ANISOU 3290  CA  LYS C 149     3498   2177   3098    336    100    -70       C  
ATOM   3291  C   LYS C 149      51.936  -8.056  -0.343  1.00 22.04           C  
ANISOU 3291  C   LYS C 149     3348   2075   2950    366     88    -67       C  
ATOM   3292  O   LYS C 149      51.534  -7.308   0.583  1.00 20.86           O  
ANISOU 3292  O   LYS C 149     3188   1933   2805    342     87    -57       O  
ATOM   3293  CB  LYS C 149      50.458  -9.682  -1.487  1.00 23.94           C  
ANISOU 3293  CB  LYS C 149     3669   2226   3200    347    105    -60       C  
ATOM   3294  CG  LYS C 149      49.307  -9.923  -2.473  1.00 24.83           C  
ANISOU 3294  CG  LYS C 149     3802   2307   3325    302    119    -62       C  
ATOM   3295  CD  LYS C 149      48.539 -11.212  -2.149  1.00 26.27           C  
ANISOU 3295  CD  LYS C 149     4053   2429   3497    299    128    -54       C  
ATOM   3296  CE  LYS C 149      49.002 -12.366  -2.978  1.00 27.33           C  
ANISOU 3296  CE  LYS C 149     4224   2537   3623    329    134    -67       C  
ATOM   3297  NZ  LYS C 149      47.847 -13.254  -3.255  1.00 27.88           N  
ANISOU 3297  NZ  LYS C 149     4348   2554   3690    290    152    -67       N  
ATOM   3298  N   GLU C 150      53.132  -8.637  -0.289  1.00 23.57           N  
ANISOU 3298  N   GLU C 150     3535   2296   3123    421     79    -77       N  
ATOM   3299  CA  GLU C 150      53.987  -8.443   0.865  1.00 26.11           C  
ANISOU 3299  CA  GLU C 150     3835   2660   3424    455     67    -77       C  
ATOM   3300  C   GLU C 150      54.406  -6.980   0.944  1.00 24.93           C  
ANISOU 3300  C   GLU C 150     3625   2568   3279    416     67    -91       C  
ATOM   3301  O   GLU C 150      54.470  -6.398   2.012  1.00 25.56           O  
ANISOU 3301  O   GLU C 150     3688   2670   3352    408     63    -87       O  
ATOM   3302  CB  GLU C 150      55.171  -9.412   0.838  1.00 28.08           C  
ANISOU 3302  CB  GLU C 150     4088   2934   3644    530     56    -86       C  
ATOM   3303  CG  GLU C 150      54.699 -10.866   0.600  1.00 30.95           C  
ANISOU 3303  CG  GLU C 150     4525   3228   4006    564     61    -73       C  
ATOM   3304  CD  GLU C 150      55.284 -11.950   1.484  1.00 33.27           C  
ANISOU 3304  CD  GLU C 150     4858   3512   4268    640     53    -61       C  
ATOM   3305  OE1 GLU C 150      55.956 -11.633   2.484  1.00 35.52           O  
ANISOU 3305  OE1 GLU C 150     5115   3849   4532    670     41    -58       O  
ATOM   3306  OE2 GLU C 150      55.062 -13.191   1.181  1.00 34.76           O  
ANISOU 3306  OE2 GLU C 150     5115   3641   4451    674     60    -54       O  
ATOM   3307  N   ASN C 151      54.676  -6.400  -0.223  1.00 25.16           N  
ANISOU 3307  N   ASN C 151     3623   2618   3316    391     73   -107       N  
ATOM   3308  CA  ASN C 151      54.938  -4.992  -0.416  1.00 23.50           C  
ANISOU 3308  CA  ASN C 151     3367   2448   3112    344     80   -120       C  
ATOM   3309  C   ASN C 151      53.838  -4.079   0.202  1.00 21.77           C  
ANISOU 3309  C   ASN C 151     3159   2199   2912    295     88   -105       C  
ATOM   3310  O   ASN C 151      54.129  -3.060   0.794  1.00 23.15           O  
ANISOU 3310  O   ASN C 151     3307   2404   3084    270     91   -112       O  
ATOM   3311  CB  ASN C 151      55.009  -4.757  -1.920  1.00 24.18           C  
ANISOU 3311  CB  ASN C 151     3439   2537   3208    323     89   -131       C  
ATOM   3312  CG  ASN C 151      55.736  -3.522  -2.318  1.00 25.79           C  
ANISOU 3312  CG  ASN C 151     3597   2794   3408    286     96   -150       C  
ATOM   3313  OD1 ASN C 151      55.346  -2.404  -1.983  1.00 29.02           O  
ANISOU 3313  OD1 ASN C 151     3999   3199   3826    241    105   -146       O  
ATOM   3314  ND2 ASN C 151      56.798  -3.718  -3.151  1.00 26.92           N  
ANISOU 3314  ND2 ASN C 151     3708   2984   3534    303     94   -172       N  
ATOM   3315  N   PHE C 152      52.601  -4.431  -0.056  1.00 19.64           N  
ANISOU 3315  N   PHE C 152     2927   1874   2661    280     94    -87       N  
ATOM   3316  CA  PHE C 152      51.408  -3.769   0.495  1.00 18.16           C  
ANISOU 3316  CA  PHE C 152     2753   1657   2488    243    101    -72       C  
ATOM   3317  C   PHE C 152      51.317  -3.970   1.998  1.00 18.16           C  
ANISOU 3317  C   PHE C 152     2764   1656   2477    257     93    -63       C  
ATOM   3318  O   PHE C 152      50.926  -3.095   2.705  1.00 18.14           O  
ANISOU 3318  O   PHE C 152     2754   1658   2480    231     97    -60       O  
ATOM   3319  CB  PHE C 152      50.150  -4.244  -0.244  1.00 17.15           C  
ANISOU 3319  CB  PHE C 152     2657   1483   2374    226    108    -60       C  
ATOM   3320  CG  PHE C 152      48.874  -4.074   0.531  1.00 16.51           C  
ANISOU 3320  CG  PHE C 152     2597   1374   2300    203    112    -43       C  
ATOM   3321  CD1 PHE C 152      48.300  -2.872   0.685  1.00 15.93           C  
ANISOU 3321  CD1 PHE C 152     2509   1305   2236    172    119    -40       C  
ATOM   3322  CD2 PHE C 152      48.222  -5.166   1.021  1.00 16.30           C  
ANISOU 3322  CD2 PHE C 152     2610   1315   2268    212    110    -31       C  
ATOM   3323  CE1 PHE C 152      47.126  -2.731   1.422  1.00 15.49           C  
ANISOU 3323  CE1 PHE C 152     2470   1231   2184    155    122    -27       C  
ATOM   3324  CE2 PHE C 152      47.032  -5.089   1.674  1.00 16.01           C  
ANISOU 3324  CE2 PHE C 152     2591   1258   2234    188    114    -18       C  
ATOM   3325  CZ  PHE C 152      46.465  -3.848   1.888  1.00 15.20           C  
ANISOU 3325  CZ  PHE C 152     2466   1169   2140    160    119    -17       C  
ATOM   3326  N   ILE C 153      51.602  -5.184   2.479  1.00 19.00           N  
ANISOU 3326  N   ILE C 153     2897   1753   2569    300     83    -56       N  
ATOM   3327  CA  ILE C 153      51.727  -5.367   3.913  1.00 19.74           C  
ANISOU 3327  CA  ILE C 153     2997   1855   2646    319     75    -47       C  
ATOM   3328  C   ILE C 153      52.783  -4.421   4.505  1.00 21.29           C  
ANISOU 3328  C   ILE C 153     3143   2115   2829    319     70    -64       C  
ATOM   3329  O   ILE C 153      52.498  -3.746   5.491  1.00 20.50           O  
ANISOU 3329  O   ILE C 153     3034   2024   2728    298     71    -62       O  
ATOM   3330  CB  ILE C 153      52.068  -6.824   4.261  1.00 19.67           C  
ANISOU 3330  CB  ILE C 153     3026   1828   2618    375     66    -36       C  
ATOM   3331  CG1 ILE C 153      50.918  -7.691   3.885  1.00 19.39           C  
ANISOU 3331  CG1 ILE C 153     3046   1727   2593    362     75    -20       C  
ATOM   3332  CG2 ILE C 153      52.410  -6.976   5.737  1.00 19.83           C  
ANISOU 3332  CG2 ILE C 153     3048   1869   2615    403     56    -26       C  
ATOM   3333  CD1 ILE C 153      51.307  -9.158   3.986  1.00 20.16           C  
ANISOU 3333  CD1 ILE C 153     3192   1796   2671    417     71    -11       C  
ATOM   3334  N   ARG C 154      53.978  -4.352   3.903  1.00 21.93           N  
ANISOU 3334  N   ARG C 154     3190   2243   2897    338     67    -85       N  
ATOM   3335  CA  ARG C 154      55.084  -3.535   4.419  1.00 24.01           C  
ANISOU 3335  CA  ARG C 154     3402   2579   3140    333     64   -107       C  
ATOM   3336  C   ARG C 154      54.675  -2.062   4.437  1.00 22.82           C  
ANISOU 3336  C   ARG C 154     3233   2428   3006    269     78   -116       C  
ATOM   3337  O   ARG C 154      54.882  -1.331   5.420  1.00 23.20           O  
ANISOU 3337  O   ARG C 154     3262   2506   3044    250     79   -125       O  
ATOM   3338  CB  ARG C 154      56.389  -3.745   3.599  1.00 26.71           C  
ANISOU 3338  CB  ARG C 154     3708   2977   3462    361     59   -131       C  
ATOM   3339  CG  ARG C 154      57.442  -2.619   3.682  1.00 30.61           C  
ANISOU 3339  CG  ARG C 154     4143   3548   3938    329     64   -162       C  
ATOM   3340  CD  ARG C 154      58.447  -2.606   2.526  1.00 34.78           C  
ANISOU 3340  CD  ARG C 154     4637   4124   4454    334     66   -186       C  
ATOM   3341  NE  ARG C 154      59.683  -3.378   2.754  1.00 38.04           N  
ANISOU 3341  NE  ARG C 154     5017   4608   4828    397     50   -201       N  
ATOM   3342  CZ  ARG C 154      60.020  -4.529   2.150  1.00 40.57           C  
ANISOU 3342  CZ  ARG C 154     5351   4925   5138    458     41   -199       C  
ATOM   3343  NH1 ARG C 154      59.207  -5.141   1.276  1.00 39.89           N  
ANISOU 3343  NH1 ARG C 154     5311   4766   5080    462     46   -182       N  
ATOM   3344  NH2 ARG C 154      61.197  -5.095   2.423  1.00 41.76           N  
ANISOU 3344  NH2 ARG C 154     5468   5150   5248    519     28   -215       N  
ATOM   3345  N   PHE C 155      54.064  -1.628   3.354  1.00 21.89           N  
ANISOU 3345  N   PHE C 155     3127   2277   2912    236     90   -113       N  
ATOM   3346  CA  PHE C 155      53.662  -0.232   3.258  1.00 21.38           C  
ANISOU 3346  CA  PHE C 155     3055   2206   2862    181    107   -119       C  
ATOM   3347  C   PHE C 155      52.577   0.057   4.331  1.00 21.45           C  
ANISOU 3347  C   PHE C 155     3087   2181   2881    168    108   -103       C  
ATOM   3348  O   PHE C 155      52.632   1.090   4.979  1.00 21.92           O  
ANISOU 3348  O   PHE C 155     3135   2255   2939    138    117   -113       O  
ATOM   3349  CB  PHE C 155      53.169   0.107   1.845  1.00 20.57           C  
ANISOU 3349  CB  PHE C 155     2962   2073   2779    158    119   -115       C  
ATOM   3350  CG  PHE C 155      52.611   1.497   1.724  1.00 19.99           C  
ANISOU 3350  CG  PHE C 155     2894   1982   2719    110    137   -115       C  
ATOM   3351  CD1 PHE C 155      53.439   2.618   1.795  1.00 20.52           C  
ANISOU 3351  CD1 PHE C 155     2938   2082   2776     75    149   -137       C  
ATOM   3352  CD2 PHE C 155      51.257   1.671   1.577  1.00 19.34           C  
ANISOU 3352  CD2 PHE C 155     2841   1851   2656    101    143    -94       C  
ATOM   3353  CE1 PHE C 155      52.901   3.897   1.640  1.00 19.80           C  
ANISOU 3353  CE1 PHE C 155     2862   1964   2696     34    169   -135       C  
ATOM   3354  CE2 PHE C 155      50.711   2.964   1.479  1.00 18.77           C  
ANISOU 3354  CE2 PHE C 155     2778   1759   2594     67    160    -93       C  
ATOM   3355  CZ  PHE C 155      51.514   4.037   1.493  1.00 19.19           C  
ANISOU 3355  CZ  PHE C 155     2817   1834   2639     36    174   -111       C  
ATOM   3356  N   SER C 156      51.593  -0.832   4.514  1.00 21.51           N  
ANISOU 3356  N   SER C 156     3129   2146   2897    187    102    -80       N  
ATOM   3357  CA  SER C 156      50.558  -0.638   5.534  1.00 20.32           C  
ANISOU 3357  CA  SER C 156     2997   1970   2751    174    104    -67       C  
ATOM   3358  C   SER C 156      51.176  -0.514   6.928  1.00 21.57           C  
ANISOU 3358  C   SER C 156     3138   2166   2889    184     96    -74       C  
ATOM   3359  O   SER C 156      50.836   0.414   7.701  1.00 21.13           O  
ANISOU 3359  O   SER C 156     3077   2115   2835    156    103    -79       O  
ATOM   3360  CB  SER C 156      49.544  -1.806   5.512  1.00 20.32           C  
ANISOU 3360  CB  SER C 156     3037   1928   2756    191     99    -44       C  
ATOM   3361  OG  SER C 156      48.855  -1.797   4.279  1.00 20.06           O  
ANISOU 3361  OG  SER C 156     3015   1867   2740    175    107    -40       O  
ATOM   3362  N   LYS C 157      52.089  -1.415   7.232  1.00 21.51           N  
ANISOU 3362  N   LYS C 157     3124   2189   2860    225     82    -76       N  
ATOM   3363  CA  LYS C 157      52.776  -1.428   8.535  1.00 22.79           C  
ANISOU 3363  CA  LYS C 157     3265   2397   2995    243     73    -82       C  
ATOM   3364  C   LYS C 157      53.573  -0.162   8.748  1.00 22.00           C  
ANISOU 3364  C   LYS C 157     3121   2349   2886    208     81   -112       C  
ATOM   3365  O   LYS C 157      53.656   0.316   9.921  1.00 22.54           O  
ANISOU 3365  O   LYS C 157     3176   2446   2942    196     80   -119       O  
ATOM   3366  CB  LYS C 157      53.695  -2.633   8.651  1.00 24.62           C  
ANISOU 3366  CB  LYS C 157     3496   2657   3201    303     57    -79       C  
ATOM   3367  CG  LYS C 157      52.916  -3.935   8.803  1.00 26.06           C  
ANISOU 3367  CG  LYS C 157     3732   2784   3385    336     51    -49       C  
ATOM   3368  CD  LYS C 157      53.478  -4.814   9.915  1.00 29.09           C  
ANISOU 3368  CD  LYS C 157     4124   3193   3735    391     36    -38       C  
ATOM   3369  CE  LYS C 157      54.609  -5.695   9.427  1.00 29.82           C  
ANISOU 3369  CE  LYS C 157     4211   3314   3804    453     26    -43       C  
ATOM   3370  NZ  LYS C 157      55.173  -6.442  10.579  1.00 31.40           N  
ANISOU 3370  NZ  LYS C 157     4418   3545   3967    512     12    -30       N  
ATOM   3371  N   SER C 158      54.112   0.398   7.671  1.00 22.68           N  
ANISOU 3371  N   SER C 158     3188   2448   2978    186     90   -130       N  
ATOM   3372  CA  SER C 158      54.905   1.620   7.750  1.00 22.73           C  
ANISOU 3372  CA  SER C 158     3159   2502   2974    143    103   -160       C  
ATOM   3373  C   SER C 158      54.015   2.809   8.136  1.00 22.73           C  
ANISOU 3373  C   SER C 158     3177   2466   2993     94    120   -161       C  
ATOM   3374  O   SER C 158      54.507   3.803   8.685  1.00 22.84           O  
ANISOU 3374  O   SER C 158     3170   2513   2995     57    132   -186       O  
ATOM   3375  CB  SER C 158      55.698   1.864   6.465  1.00 22.33           C  
ANISOU 3375  CB  SER C 158     3088   2474   2922    130    110   -178       C  
ATOM   3376  OG  SER C 158      54.895   2.387   5.463  1.00 22.01           O  
ANISOU 3376  OG  SER C 158     3075   2378   2910    101    125   -168       O  
ATOM   3377  N   LEU C 159      52.722   2.699   7.909  1.00 22.08           N  
ANISOU 3377  N   LEU C 159     3132   2320   2936     94    123   -136       N  
ATOM   3378  CA  LEU C 159      51.794   3.786   8.279  1.00 22.37           C  
ANISOU 3378  CA  LEU C 159     3187   2322   2988     58    139   -135       C  
ATOM   3379  C   LEU C 159      51.243   3.559   9.652  1.00 21.11           C  
ANISOU 3379  C   LEU C 159     3034   2164   2822     68    131   -128       C  
ATOM   3380  O   LEU C 159      50.314   4.261  10.070  1.00 22.83           O  
ANISOU 3380  O   LEU C 159     3269   2353   3051     48    141   -124       O  
ATOM   3381  CB  LEU C 159      50.697   3.954   7.227  1.00 22.27           C  
ANISOU 3381  CB  LEU C 159     3206   2253   3002     53    148   -116       C  
ATOM   3382  CG  LEU C 159      51.232   4.166   5.815  1.00 23.22           C  
ANISOU 3382  CG  LEU C 159     3320   2373   3127     43    157   -122       C  
ATOM   3383  CD1 LEU C 159      50.155   4.120   4.784  1.00 23.35           C  
ANISOU 3383  CD1 LEU C 159     3363   2343   3163     46    162   -101       C  
ATOM   3384  CD2 LEU C 159      52.021   5.484   5.648  1.00 23.01           C  
ANISOU 3384  CD2 LEU C 159     3281   2366   3093     -1    177   -148       C  
ATOM   3385  N   GLY C 160      51.771   2.564  10.357  1.00 21.68           N  
ANISOU 3385  N   GLY C 160     3093   2269   2873    103    113   -123       N  
ATOM   3386  CA  GLY C 160      51.381   2.237  11.746  1.00 21.14           C  
ANISOU 3386  CA  GLY C 160     3028   2210   2792    116    103   -114       C  
ATOM   3387  C   GLY C 160      50.347   1.127  11.979  1.00 19.43           C  
ANISOU 3387  C   GLY C 160     2847   1953   2581    144     93    -82       C  
ATOM   3388  O   GLY C 160      49.935   0.921  13.138  1.00 20.27           O  
ANISOU 3388  O   GLY C 160     2959   2065   2676    149     87    -73       O  
ATOM   3389  N   LEU C 161      49.941   0.398  10.930  1.00 18.77           N  
ANISOU 3389  N   LEU C 161     2787   1832   2512    158     92    -66       N  
ATOM   3390  CA  LEU C 161      48.857  -0.614  11.097  1.00 18.28           C  
ANISOU 3390  CA  LEU C 161     2762   1728   2453    172     86    -38       C  
ATOM   3391  C   LEU C 161      49.476  -1.939  11.475  1.00 19.70           C  
ANISOU 3391  C   LEU C 161     2955   1917   2610    218     72    -25       C  
ATOM   3392  O   LEU C 161      50.392  -2.408  10.792  1.00 19.89           O  
ANISOU 3392  O   LEU C 161     2971   1955   2628    245     66    -31       O  
ATOM   3393  CB  LEU C 161      47.984  -0.788   9.860  1.00 17.23           C  
ANISOU 3393  CB  LEU C 161     2652   1551   2343    160     94    -28       C  
ATOM   3394  CG  LEU C 161      47.297   0.562   9.495  1.00 16.69           C  
ANISOU 3394  CG  LEU C 161     2575   1472   2292    124    110    -38       C  
ATOM   3395  CD1 LEU C 161      46.710   0.454   8.098  1.00 15.96           C  
ANISOU 3395  CD1 LEU C 161     2495   1350   2216    118    117    -31       C  
ATOM   3396  CD2 LEU C 161      46.259   0.900  10.549  1.00 16.43           C  
ANISOU 3396  CD2 LEU C 161     2550   1432   2257    109    113    -31       C  
ATOM   3397  N   PRO C 162      48.992  -2.505  12.583  1.00 21.29           N  
ANISOU 3397  N   PRO C 162     3177   2113   2798    228     66     -8       N  
ATOM   3398  CA  PRO C 162      49.485  -3.828  12.912  1.00 22.58           C  
ANISOU 3398  CA  PRO C 162     3365   2275   2937    276     54      9       C  
ATOM   3399  C   PRO C 162      48.961  -4.881  11.938  1.00 23.83           C  
ANISOU 3399  C   PRO C 162     3569   2379   3106    286     57     25       C  
ATOM   3400  O   PRO C 162      47.987  -4.663  11.232  1.00 22.23           O  
ANISOU 3400  O   PRO C 162     3378   2142   2926    251     68     26       O  
ATOM   3401  CB  PRO C 162      48.973  -4.069  14.327  1.00 23.50           C  
ANISOU 3401  CB  PRO C 162     3497   2395   3036    276     49     25       C  
ATOM   3402  CG  PRO C 162      47.967  -3.020  14.616  1.00 22.13           C  
ANISOU 3402  CG  PRO C 162     3311   2215   2879    226     60     17       C  
ATOM   3403  CD  PRO C 162      47.837  -2.130  13.417  1.00 20.65           C  
ANISOU 3403  CD  PRO C 162     3106   2017   2720    198     71      0       C  
ATOM   3404  N   GLU C 163      49.627  -6.038  11.939  1.00 24.75           N  
ANISOU 3404  N   GLU C 163     3711   2490   3203    336     49     36       N  
ATOM   3405  CA  GLU C 163      49.266  -7.141  11.041  1.00 26.49           C  
ANISOU 3405  CA  GLU C 163     3980   2656   3428    348     54     49       C  
ATOM   3406  C   GLU C 163      47.743  -7.518  11.064  1.00 25.77           C  
ANISOU 3406  C   GLU C 163     3933   2510   3348    306     66     65       C  
ATOM   3407  O   GLU C 163      47.159  -7.819  10.017  1.00 26.47           O  
ANISOU 3407  O   GLU C 163     4041   2564   3452    285     75     63       O  
ATOM   3408  CB  GLU C 163      50.203  -8.343  11.281  1.00 28.76           C  
ANISOU 3408  CB  GLU C 163     4297   2943   3687    417     44     61       C  
ATOM   3409  CG  GLU C 163      50.884  -8.916  10.014  1.00 30.42           C  
ANISOU 3409  CG  GLU C 163     4515   3143   3901    449     44     51       C  
ATOM   3410  CD  GLU C 163      52.109  -9.744  10.339  1.00 32.00           C  
ANISOU 3410  CD  GLU C 163     4722   3367   4067    528     32     56       C  
ATOM   3411  OE1 GLU C 163      52.541  -9.735  11.502  1.00 33.50           O  
ANISOU 3411  OE1 GLU C 163     4902   3594   4230    557     22     64       O  
ATOM   3412  OE2 GLU C 163      52.670 -10.362   9.433  1.00 36.68           O  
ANISOU 3412  OE2 GLU C 163     5327   3950   4657    564     32     49       O  
ATOM   3413  N   ASN C 164      47.070  -7.394  12.199  1.00 26.86           N  
ANISOU 3413  N   ASN C 164     4079   2649   3475    286     66     77       N  
ATOM   3414  CA  ASN C 164      45.625  -7.680  12.285  1.00 27.13           C  
ANISOU 3414  CA  ASN C 164     4147   2646   3514    241     78     88       C  
ATOM   3415  C   ASN C 164      44.682  -6.621  11.692  1.00 27.49           C  
ANISOU 3415  C   ASN C 164     4160   2699   3584    191     87     73       C  
ATOM   3416  O   ASN C 164      43.448  -6.819  11.681  1.00 27.99           O  
ANISOU 3416  O   ASN C 164     4243   2742   3648    153     97     79       O  
ATOM   3417  CB  ASN C 164      45.175  -7.896  13.745  1.00 28.28           C  
ANISOU 3417  CB  ASN C 164     4310   2796   3637    235     76    106       C  
ATOM   3418  CG  ASN C 164      45.030  -6.590  14.506  1.00 28.32           C  
ANISOU 3418  CG  ASN C 164     4263   2847   3647    213     73     93       C  
ATOM   3419  OD1 ASN C 164      45.976  -5.832  14.603  1.00 29.49           O  
ANISOU 3419  OD1 ASN C 164     4370   3036   3799    232     65     77       O  
ATOM   3420  ND2 ASN C 164      43.831  -6.334  15.063  1.00 28.70           N  
ANISOU 3420  ND2 ASN C 164     4316   2893   3695    172     80     97       N  
ATOM   3421  N   HIS C 165      45.249  -5.508  11.226  1.00 24.24           N  
ANISOU 3421  N   HIS C 165     3701   2318   3189    191     85     54       N  
ATOM   3422  CA  HIS C 165      44.487  -4.514  10.501  1.00 23.76           C  
ANISOU 3422  CA  HIS C 165     3616   2261   3150    156     94     42       C  
ATOM   3423  C   HIS C 165      44.681  -4.685   8.996  1.00 23.02           C  
ANISOU 3423  C   HIS C 165     3523   2152   3071    158     99     35       C  
ATOM   3424  O   HIS C 165      44.097  -3.925   8.218  1.00 24.07           O  
ANISOU 3424  O   HIS C 165     3637   2287   3219    134    107     27       O  
ATOM   3425  CB  HIS C 165      44.898  -3.106  10.992  1.00 22.31           C  
ANISOU 3425  CB  HIS C 165     3389   2114   2973    149     93     26       C  
ATOM   3426  CG  HIS C 165      44.256  -2.705  12.285  1.00 23.65           C  
ANISOU 3426  CG  HIS C 165     3554   2297   3132    133     94     29       C  
ATOM   3427  ND1 HIS C 165      43.331  -1.709  12.355  1.00 23.78           N  
ANISOU 3427  ND1 HIS C 165     3556   2319   3159    105    102     22       N  
ATOM   3428  CD2 HIS C 165      44.357  -3.210  13.542  1.00 24.64           C  
ANISOU 3428  CD2 HIS C 165     3691   2433   3236    144     86     40       C  
ATOM   3429  CE1 HIS C 165      42.894  -1.581  13.604  1.00 24.40           C  
ANISOU 3429  CE1 HIS C 165     3634   2412   3224     97    101     25       C  
ATOM   3430  NE2 HIS C 165      43.515  -2.472  14.348  1.00 24.91           N  
ANISOU 3430  NE2 HIS C 165     3713   2481   3269    118     91     37       N  
ATOM   3431  N   ILE C 166      45.503  -5.656   8.582  1.00 22.08           N  
ANISOU 3431  N   ILE C 166     3424   2020   2945    190     94     37       N  
ATOM   3432  CA  ILE C 166      45.854  -5.833   7.172  1.00 21.76           C  
ANISOU 3432  CA  ILE C 166     3380   1970   2916    196     97     28       C  
ATOM   3433  C   ILE C 166      45.290  -7.161   6.712  1.00 23.63           C  
ANISOU 3433  C   ILE C 166     3667   2163   3146    194    103     37       C  
ATOM   3434  O   ILE C 166      45.610  -8.219   7.305  1.00 24.96           O  
ANISOU 3434  O   ILE C 166     3876   2310   3296    221    100     49       O  
ATOM   3435  CB  ILE C 166      47.389  -5.800   6.958  1.00 21.92           C  
ANISOU 3435  CB  ILE C 166     3378   2019   2932    236     88     17       C  
ATOM   3436  CG1 ILE C 166      47.971  -4.476   7.483  1.00 20.73           C  
ANISOU 3436  CG1 ILE C 166     3180   1913   2783    229     85      3       C  
ATOM   3437  CG2 ILE C 166      47.773  -5.974   5.481  1.00 21.71           C  
ANISOU 3437  CG2 ILE C 166     3346   1986   2915    242     91      5       C  
ATOM   3438  CD1 ILE C 166      49.474  -4.385   7.581  1.00 21.67           C  
ANISOU 3438  CD1 ILE C 166     3269   2075   2887    263     75    -10       C  
ATOM   3439  N   VAL C 167      44.442  -7.131   5.665  1.00 22.06           N  
ANISOU 3439  N   VAL C 167     3470   1953   2959    162    114     32       N  
ATOM   3440  CA  VAL C 167      43.552  -8.285   5.369  1.00 22.44           C  
ANISOU 3440  CA  VAL C 167     3566   1962   2997    140    125     38       C  
ATOM   3441  C   VAL C 167      43.574  -8.568   3.861  1.00 22.71           C  
ANISOU 3441  C   VAL C 167     3599   1987   3040    134    131     25       C  
ATOM   3442  O   VAL C 167      43.525  -7.646   3.068  1.00 24.42           O  
ANISOU 3442  O   VAL C 167     3776   2230   3271    124    132     15       O  
ATOM   3443  CB  VAL C 167      42.083  -8.043   5.804  1.00 21.80           C  
ANISOU 3443  CB  VAL C 167     3486   1885   2911     91    133     42       C  
ATOM   3444  CG1 VAL C 167      41.229  -9.278   5.620  1.00 22.64           C  
ANISOU 3444  CG1 VAL C 167     3644   1957   3001     60    147     45       C  
ATOM   3445  CG2 VAL C 167      42.021  -7.590   7.282  1.00 22.27           C  
ANISOU 3445  CG2 VAL C 167     3538   1961   2962     94    127     52       C  
ATOM   3446  N   PHE C 168      43.554  -9.863   3.472  1.00 21.78           N  
ANISOU 3446  N   PHE C 168     3533   1830   2912    137    139     25       N  
ATOM   3447  CA  PHE C 168      43.389 -10.211   2.041  1.00 21.73           C  
ANISOU 3447  CA  PHE C 168     3528   1815   2911    124    148     10       C  
ATOM   3448  C   PHE C 168      42.151 -11.048   1.812  1.00 22.08           C  
ANISOU 3448  C   PHE C 168     3612   1833   2942     74    165      8       C  
ATOM   3449  O   PHE C 168      42.244 -12.305   1.834  1.00 22.39           O  
ANISOU 3449  O   PHE C 168     3712   1825   2967     78    174      9       O  
ATOM   3450  CB  PHE C 168      44.584 -10.917   1.513  1.00 22.07           C  
ANISOU 3450  CB  PHE C 168     3590   1841   2953    170    144      4       C  
ATOM   3451  CG  PHE C 168      45.841 -10.151   1.615  1.00 22.23           C  
ANISOU 3451  CG  PHE C 168     3566   1898   2980    214    129      1       C  
ATOM   3452  CD1 PHE C 168      46.560 -10.147   2.790  1.00 22.28           C  
ANISOU 3452  CD1 PHE C 168     3575   1912   2976    250    118     11       C  
ATOM   3453  CD2 PHE C 168      46.310  -9.424   0.528  1.00 22.24           C  
ANISOU 3453  CD2 PHE C 168     3522   1931   2996    215    127    -13       C  
ATOM   3454  CE1 PHE C 168      47.714  -9.435   2.927  1.00 22.85           C  
ANISOU 3454  CE1 PHE C 168     3604   2028   3051    284    105      4       C  
ATOM   3455  CE2 PHE C 168      47.487  -8.748   0.628  1.00 22.38           C  
ANISOU 3455  CE2 PHE C 168     3501   1985   3015    247    116    -19       C  
ATOM   3456  CZ  PHE C 168      48.192  -8.722   1.837  1.00 22.75           C  
ANISOU 3456  CZ  PHE C 168     3547   2046   3051    279    105    -12       C  
ATOM   3457  N   PRO C 169      40.970 -10.418   1.650  1.00 20.92           N  
ANISOU 3457  N   PRO C 169     3437   1716   2796     28    171      4       N  
ATOM   3458  CA  PRO C 169      39.717 -11.185   1.604  1.00 22.55           C  
ANISOU 3458  CA  PRO C 169     3675   1909   2983    -26    188      0       C  
ATOM   3459  C   PRO C 169      39.639 -12.142   0.400  1.00 23.82           C  
ANISOU 3459  C   PRO C 169     3866   2046   3138    -44    202    -16       C  
ATOM   3460  O   PRO C 169      40.022 -11.755  -0.698  1.00 24.03           O  
ANISOU 3460  O   PRO C 169     3860   2093   3178    -30    199    -28       O  
ATOM   3461  CB  PRO C 169      38.650 -10.097   1.455  1.00 22.85           C  
ANISOU 3461  CB  PRO C 169     3658   2001   3021    -58    189     -3       C  
ATOM   3462  CG  PRO C 169      39.268  -8.908   2.122  1.00 21.30           C  
ANISOU 3462  CG  PRO C 169     3423   1827   2841    -21    173      6       C  
ATOM   3463  CD  PRO C 169      40.686  -8.950   1.608  1.00 21.61           C  
ANISOU 3463  CD  PRO C 169     3462   1852   2896     24    164      4       C  
ATOM   3464  N   VAL C 170      39.074 -13.344   0.602  1.00 27.26           N  
ANISOU 3464  N   VAL C 170     4363   2441   3551    -80    220    -19       N  
ATOM   3465  CA  VAL C 170      38.865 -14.253  -0.516  1.00 27.71           C  
ANISOU 3465  CA  VAL C 170     4452   2476   3600   -107    237    -40       C  
ATOM   3466  C   VAL C 170      37.950 -13.638  -1.597  1.00 28.62           C  
ANISOU 3466  C   VAL C 170     4511   2650   3714   -149    242    -59       C  
ATOM   3467  O   VAL C 170      36.825 -13.241  -1.308  1.00 31.03           O  
ANISOU 3467  O   VAL C 170     4790   2994   4006   -193    247    -60       O  
ATOM   3468  CB  VAL C 170      38.270 -15.617  -0.049  1.00 29.25           C  
ANISOU 3468  CB  VAL C 170     4730   2615   3768   -151    260    -41       C  
ATOM   3469  CG1 VAL C 170      37.959 -16.492  -1.240  1.00 29.23           C  
ANISOU 3469  CG1 VAL C 170     4757   2592   3753   -189    281    -68       C  
ATOM   3470  CG2 VAL C 170      39.242 -16.304   0.888  1.00 29.15           C  
ANISOU 3470  CG2 VAL C 170     4781   2542   3753    -99    255    -20       C  
ATOM   3471  N   PRO C 171      38.402 -13.593  -2.859  1.00 29.99           N  
ANISOU 3471  N   PRO C 171     4663   2832   3897   -135    242    -74       N  
ATOM   3472  CA  PRO C 171      37.545 -13.038  -3.943  1.00 31.43           C  
ANISOU 3472  CA  PRO C 171     4792   3075   4075   -171    247    -91       C  
ATOM   3473  C   PRO C 171      36.246 -13.775  -4.266  1.00 34.45           C  
ANISOU 3473  C   PRO C 171     5192   3471   4426   -246    269   -111       C  
ATOM   3474  O   PRO C 171      36.127 -14.998  -4.026  1.00 32.26           O  
ANISOU 3474  O   PRO C 171     4983   3141   4132   -277    287   -120       O  
ATOM   3475  CB  PRO C 171      38.451 -13.097  -5.177  1.00 31.55           C  
ANISOU 3475  CB  PRO C 171     4796   3087   4104   -140    244   -103       C  
ATOM   3476  CG  PRO C 171      39.824 -13.160  -4.664  1.00 31.02           C  
ANISOU 3476  CG  PRO C 171     4750   2980   4054    -77    230    -90       C  
ATOM   3477  CD  PRO C 171      39.789 -13.810  -3.314  1.00 30.93           C  
ANISOU 3477  CD  PRO C 171     4794   2923   4034    -77    233    -75       C  
ATOM   3478  N   ILE C 172      35.307 -13.042  -4.871  1.00 36.22           N  
ANISOU 3478  N   ILE C 172     5355   3766   4639   -274    270   -121       N  
ATOM   3479  CA  ILE C 172      33.966 -13.550  -5.241  1.00 37.78           C  
ANISOU 3479  CA  ILE C 172     5550   4003   4801   -348    290   -144       C  
ATOM   3480  C   ILE C 172      33.780 -13.407  -6.761  1.00 39.72           C  
ANISOU 3480  C   ILE C 172     5754   4296   5040   -358    295   -166       C  
ATOM   3481  O   ILE C 172      34.288 -12.460  -7.376  1.00 40.47           O  
ANISOU 3481  O   ILE C 172     5802   4420   5155   -311    279   -157       O  
ATOM   3482  CB  ILE C 172      32.816 -12.794  -4.521  1.00 38.65           C  
ANISOU 3482  CB  ILE C 172     5616   4177   4892   -373    288   -138       C  
ATOM   3483  CG1 ILE C 172      33.146 -12.577  -3.053  1.00 37.57           C  
ANISOU 3483  CG1 ILE C 172     5503   4004   4768   -347    278   -113       C  
ATOM   3484  CG2 ILE C 172      31.492 -13.506  -4.661  1.00 39.21           C  
ANISOU 3484  CG2 ILE C 172     5691   4286   4920   -456    311   -164       C  
ATOM   3485  CD1 ILE C 172      33.886 -11.283  -2.848  1.00 35.68           C  
ANISOU 3485  CD1 ILE C 172     5219   3776   4559   -279    254    -91       C  
ATOM   3486  N   ASP C 173      33.029 -14.330  -7.353  1.00 39.45           N  
ANISOU 3486  N   ASP C 173     5739   4273   4976   -424    317   -196       N  
ATOM   3487  CA  ASP C 173      32.787 -14.356  -8.810  1.00 40.40           C  
ANISOU 3487  CA  ASP C 173     5823   4442   5083   -442    324   -221       C  
ATOM   3488  C   ASP C 173      31.625 -13.490  -9.289  1.00 40.70           C  
ANISOU 3488  C   ASP C 173     5781   4586   5094   -463    322   -228       C  
ATOM   3489  O   ASP C 173      31.267 -13.521 -10.474  1.00 41.27           O  
ANISOU 3489  O   ASP C 173     5818   4711   5148   -484    329   -250       O  
ATOM   3490  CB  ASP C 173      32.638 -15.814  -9.285  1.00 41.26           C  
ANISOU 3490  CB  ASP C 173     5995   4511   5172   -503    352   -254       C  
ATOM   3491  CG  ASP C 173      33.960 -16.548  -9.292  1.00 42.65           C  
ANISOU 3491  CG  ASP C 173     6239   4592   5374   -460    352   -250       C  
ATOM   3492  OD1 ASP C 173      35.008 -15.865  -9.147  1.00 43.23           O  
ANISOU 3492  OD1 ASP C 173     6295   4648   5481   -386    329   -225       O  
ATOM   3493  OD2 ASP C 173      33.970 -17.798  -9.476  1.00 44.94           O  
ANISOU 3493  OD2 ASP C 173     6598   4826   5648   -500    376   -273       O  
ATOM   3494  N   GLN C 174      31.083 -12.673  -8.395  1.00 41.34           N  
ANISOU 3494  N   GLN C 174     5832   4702   5173   -451    312   -209       N  
ATOM   3495  CA  GLN C 174      29.812 -12.016  -8.617  1.00 41.37           C  
ANISOU 3495  CA  GLN C 174     5769   4808   5142   -475    313   -217       C  
ATOM   3496  C   GLN C 174      30.016 -10.559  -8.992  1.00 39.98           C  
ANISOU 3496  C   GLN C 174     5531   4676   4981   -405    292   -193       C  
ATOM   3497  O   GLN C 174      31.097 -10.023  -8.808  1.00 38.09           O  
ANISOU 3497  O   GLN C 174     5304   4386   4781   -346    277   -169       O  
ATOM   3498  CB  GLN C 174      28.979 -12.122  -7.329  1.00 43.67           C  
ANISOU 3498  CB  GLN C 174     6070   5110   5412   -510    318   -214       C  
ATOM   3499  CG  GLN C 174      27.498 -12.311  -7.547  1.00 44.64           C  
ANISOU 3499  CG  GLN C 174     6151   5328   5480   -578    334   -243       C  
ATOM   3500  CD  GLN C 174      27.147 -13.661  -8.142  1.00 48.27           C  
ANISOU 3500  CD  GLN C 174     6649   5780   5910   -662    361   -281       C  
ATOM   3501  OE1 GLN C 174      27.975 -14.572  -8.216  1.00 49.22           O  
ANISOU 3501  OE1 GLN C 174     6839   5810   6050   -670    371   -285       O  
ATOM   3502  NE2 GLN C 174      25.899 -13.797  -8.564  1.00 48.29           N  
ANISOU 3502  NE2 GLN C 174     6605   5881   5860   -724    376   -312       N  
ATOM   3503  N   CYS C 175      28.956  -9.937  -9.512  1.00 38.95           N  
ANISOU 3503  N   CYS C 175     5337   4644   4817   -412    292   -201       N  
ATOM   3504  CA  CYS C 175      28.817  -8.477  -9.645  1.00 38.24           C  
ANISOU 3504  CA  CYS C 175     5191   4604   4731   -347    275   -177       C  
ATOM   3505  C   CYS C 175      29.499  -7.883 -10.852  1.00 39.65           C  
ANISOU 3505  C   CYS C 175     5348   4790   4926   -301    267   -167       C  
ATOM   3506  O   CYS C 175      28.956  -7.002 -11.529  1.00 41.06           O  
ANISOU 3506  O   CYS C 175     5473   5042   5083   -271    263   -161       O  
ATOM   3507  CB  CYS C 175      29.332  -7.748  -8.395  1.00 35.50           C  
ANISOU 3507  CB  CYS C 175     4864   4208   4417   -301    261   -147       C  
ATOM   3508  SG  CYS C 175      28.830  -8.494  -6.837  1.00 33.91           S  
ANISOU 3508  SG  CYS C 175     4701   3978   4205   -350    269   -152       S  
ATOM   3509  N   ILE C 176      30.713  -8.342 -11.096  1.00 39.96           N  
ANISOU 3509  N   ILE C 176     5429   4753   5000   -290    266   -165       N  
ATOM   3510  CA  ILE C 176      31.645  -7.636 -11.936  1.00 42.01           C  
ANISOU 3510  CA  ILE C 176     5676   5001   5283   -238    256   -149       C  
ATOM   3511  C   ILE C 176      32.349  -8.804 -12.648  1.00 45.01           C  
ANISOU 3511  C   ILE C 176     6090   5338   5671   -266    265   -172       C  
ATOM   3512  O   ILE C 176      32.872  -9.721 -11.999  1.00 47.90           O  
ANISOU 3512  O   ILE C 176     6511   5635   6053   -285    270   -179       O  
ATOM   3513  CB  ILE C 176      32.510  -6.686 -11.025  1.00 40.15           C  
ANISOU 3513  CB  ILE C 176     5455   4712   5086   -182    241   -117       C  
ATOM   3514  CG1 ILE C 176      32.408  -5.225 -11.483  1.00 39.22           C  
ANISOU 3514  CG1 ILE C 176     5296   4637   4967   -130    232    -93       C  
ATOM   3515  CG2 ILE C 176      33.914  -7.223 -10.781  1.00 40.78           C  
ANISOU 3515  CG2 ILE C 176     5582   4707   5202   -169    237   -115       C  
ATOM   3516  CD1 ILE C 176      33.391  -4.275 -10.831  1.00 38.28           C  
ANISOU 3516  CD1 ILE C 176     5194   4465   4884    -81    222    -66       C  
ATOM   3517  N   ASP C 177      32.254  -8.820 -13.972  1.00 47.16           N  
ANISOU 3517  N   ASP C 177     6332   5657   5927   -271    269   -186       N  
ATOM   3518  CA  ASP C 177      32.544 -10.015 -14.774  1.00 47.89           C  
ANISOU 3518  CA  ASP C 177     6449   5730   6013   -311    283   -217       C  
ATOM   3519  C   ASP C 177      33.580 -10.942 -14.122  1.00 49.16           C  
ANISOU 3519  C   ASP C 177     6681   5791   6205   -312    285   -221       C  
ATOM   3520  O   ASP C 177      33.205 -11.913 -13.453  1.00 47.04           O  
ANISOU 3520  O   ASP C 177     6456   5490   5926   -357    298   -236       O  
ATOM   3521  CB  ASP C 177      32.968  -9.623 -16.204  1.00 48.31           C  
ANISOU 3521  CB  ASP C 177     6467   5821   6065   -287    280   -219       C  
ATOM   3522  CG  ASP C 177      31.783  -9.297 -17.114  1.00 47.81           C  
ANISOU 3522  CG  ASP C 177     6343   5864   5955   -308    285   -231       C  
ATOM   3523  OD1 ASP C 177      30.684  -8.957 -16.619  1.00 46.57           O  
ANISOU 3523  OD1 ASP C 177     6159   5764   5771   -320    286   -229       O  
ATOM   3524  OD2 ASP C 177      31.966  -9.397 -18.345  1.00 48.33           O  
ANISOU 3524  OD2 ASP C 177     6386   5964   6010   -310    289   -244       O  
TER    3525      ASP C 177                                                      
ATOM   3526  N   ALA D1265      35.849  -0.595  35.372  1.00 36.07           N  
ANISOU 3526  N   ALA D1265     5174   4357   4172   -121   -361     25       N  
ATOM   3527  CA  ALA D1265      34.718   0.308  35.066  1.00 35.40           C  
ANISOU 3527  CA  ALA D1265     5037   4299   4115   -202   -288     28       C  
ATOM   3528  C   ALA D1265      34.636   0.570  33.561  1.00 34.81           C  
ANISOU 3528  C   ALA D1265     4938   4177   4109   -197   -255      5       C  
ATOM   3529  O   ALA D1265      34.913   1.685  33.063  1.00 33.77           O  
ANISOU 3529  O   ALA D1265     4727   4075   4027   -188   -204    -51       O  
ATOM   3530  CB  ALA D1265      34.847   1.615  35.848  1.00 29.72           C  
ANISOU 3530  CB  ALA D1265     4221   3671   3398   -212   -241    -25       C  
ATOM   3531  N   GLU D1266      34.234  -0.464  32.825  1.00 34.02           N  
ANISOU 3531  N   GLU D1266     4913   4002   4008   -206   -284     50       N  
ATOM   3532  CA  GLU D1266      33.943  -0.280  31.416  1.00 35.04           C  
ANISOU 3532  CA  GLU D1266     5024   4095   4193   -210   -252     36       C  
ATOM   3533  C   GLU D1266      32.885   0.804  31.261  1.00 32.11           C  
ANISOU 3533  C   GLU D1266     4592   3771   3837   -269   -181     32       C  
ATOM   3534  O   GLU D1266      31.931   0.903  32.064  1.00 33.11           O  
ANISOU 3534  O   GLU D1266     4721   3936   3922   -330   -167     64       O  
ATOM   3535  CB  GLU D1266      33.482  -1.582  30.753  1.00 36.50           C  
ANISOU 3535  CB  GLU D1266     5300   4198   4368   -224   -292     85       C  
ATOM   3536  CG  GLU D1266      32.065  -2.039  31.114  1.00 38.76           C  
ANISOU 3536  CG  GLU D1266     5635   4480   4612   -319   -281    148       C  
ATOM   3537  CD  GLU D1266      31.799  -3.511  30.837  1.00 41.01           C  
ANISOU 3537  CD  GLU D1266     6033   4675   4873   -338   -333    198       C  
ATOM   3538  OE1 GLU D1266      30.639  -3.866  30.506  1.00 41.83           O  
ANISOU 3538  OE1 GLU D1266     6163   4767   4964   -419   -312    230       O  
ATOM   3539  OE2 GLU D1266      32.732  -4.332  30.951  1.00 43.54           O  
ANISOU 3539  OE2 GLU D1266     6419   4938   5185   -273   -395    200       O  
ATOM   3540  N   VAL D1267      33.040   1.619  30.224  1.00 29.48           N  
ANISOU 3540  N   VAL D1267     4206   3437   3558   -250   -137     -7       N  
ATOM   3541  CA  VAL D1267      32.005   2.564  29.900  1.00 26.79           C  
ANISOU 3541  CA  VAL D1267     3821   3127   3230   -290    -78     -8       C  
ATOM   3542  C   VAL D1267      30.822   1.736  29.395  1.00 25.37           C  
ANISOU 3542  C   VAL D1267     3687   2923   3029   -337    -86     40       C  
ATOM   3543  O   VAL D1267      30.942   0.937  28.460  1.00 26.01           O  
ANISOU 3543  O   VAL D1267     3808   2948   3125   -322   -111     51       O  
ATOM   3544  CB  VAL D1267      32.471   3.609  28.859  1.00 26.53           C  
ANISOU 3544  CB  VAL D1267     3737   3088   3254   -255    -30    -56       C  
ATOM   3545  CG1 VAL D1267      31.343   4.583  28.501  1.00 25.51           C  
ANISOU 3545  CG1 VAL D1267     3575   2984   3132   -282     25    -55       C  
ATOM   3546  CG2 VAL D1267      33.697   4.369  29.379  1.00 26.90           C  
ANISOU 3546  CG2 VAL D1267     3738   3161   3319   -223    -18   -113       C  
ATOM   3547  N   PRO D1268      29.659   1.920  29.979  1.00 24.39           N  
ANISOU 3547  N   PRO D1268     3553   2847   2867   -397    -66     62       N  
ATOM   3548  CA  PRO D1268      28.507   1.116  29.504  1.00 24.19           C  
ANISOU 3548  CA  PRO D1268     3563   2811   2815   -453    -71     99       C  
ATOM   3549  C   PRO D1268      28.079   1.439  28.079  1.00 24.00           C  
ANISOU 3549  C   PRO D1268     3513   2775   2829   -435    -42     82       C  
ATOM   3550  O   PRO D1268      28.031   2.599  27.663  1.00 22.88           O  
ANISOU 3550  O   PRO D1268     3314   2661   2716   -402      0     49       O  
ATOM   3551  CB  PRO D1268      27.373   1.509  30.459  1.00 24.73           C  
ANISOU 3551  CB  PRO D1268     3601   2961   2832   -519    -45    109       C  
ATOM   3552  CG  PRO D1268      27.840   2.766  31.070  1.00 24.93           C  
ANISOU 3552  CG  PRO D1268     3564   3034   2874   -482    -17     68       C  
ATOM   3553  CD  PRO D1268      29.299   2.669  31.185  1.00 24.80           C  
ANISOU 3553  CD  PRO D1268     3564   2972   2887   -424    -44     52       C  
ATOM   3554  N   GLN D1269      27.741   0.376  27.370  1.00 23.58           N  
ANISOU 3554  N   GLN D1269     3509   2679   2771   -457    -67    105       N  
ATOM   3555  CA  GLN D1269      27.073   0.429  26.070  1.00 24.27           C  
ANISOU 3555  CA  GLN D1269     3577   2767   2877   -454    -45     94       C  
ATOM   3556  C   GLN D1269      25.601   0.735  26.209  1.00 24.40           C  
ANISOU 3556  C   GLN D1269     3555   2860   2852   -512    -13     95       C  
ATOM   3557  O   GLN D1269      24.942   0.352  27.204  1.00 25.98           O  
ANISOU 3557  O   GLN D1269     3769   3099   3002   -583    -18    116       O  
ATOM   3558  CB  GLN D1269      27.154  -0.941  25.408  1.00 25.42           C  
ANISOU 3558  CB  GLN D1269     3790   2844   3024   -468    -87    113       C  
ATOM   3559  CG  GLN D1269      28.574  -1.433  25.209  1.00 25.56           C  
ANISOU 3559  CG  GLN D1269     3847   2788   3074   -403   -129    105       C  
ATOM   3560  CD  GLN D1269      28.595  -2.723  24.430  1.00 26.97           C  
ANISOU 3560  CD  GLN D1269     4092   2897   3257   -408   -171    115       C  
ATOM   3561  OE1 GLN D1269      28.881  -3.761  24.982  1.00 29.52           O  
ANISOU 3561  OE1 GLN D1269     4494   3162   3559   -422   -220    142       O  
ATOM   3562  NE2 GLN D1269      28.319  -2.649  23.135  1.00 27.21           N  
ANISOU 3562  NE2 GLN D1269     4094   2928   3313   -390   -153     93       N  
ATOM   3563  N   LEU D1270      25.067   1.370  25.170  1.00 24.44           N  
ANISOU 3563  N   LEU D1270     3515   2894   2875   -482     18     71       N  
ATOM   3564  CA  LEU D1270      23.616   1.376  24.983  1.00 24.58           C  
ANISOU 3564  CA  LEU D1270     3499   2988   2851   -531     39     64       C  
ATOM   3565  C   LEU D1270      23.149  -0.065  24.796  1.00 26.48           C  
ANISOU 3565  C   LEU D1270     3792   3203   3064   -606     10     86       C  
ATOM   3566  O   LEU D1270      23.854  -0.907  24.228  1.00 26.65           O  
ANISOU 3566  O   LEU D1270     3869   3142   3113   -591    -21     98       O  
ATOM   3567  CB  LEU D1270      23.229   2.221  23.783  1.00 24.43           C  
ANISOU 3567  CB  LEU D1270     3431   2997   2851   -468     71     34       C  
ATOM   3568  CG  LEU D1270      23.451   3.693  24.086  1.00 22.55           C  
ANISOU 3568  CG  LEU D1270     3151   2786   2631   -409    104     13       C  
ATOM   3569  CD1 LEU D1270      23.396   4.455  22.783  1.00 22.14           C  
ANISOU 3569  CD1 LEU D1270     3079   2728   2604   -334    130     -4       C  
ATOM   3570  CD2 LEU D1270      22.442   4.232  25.091  1.00 22.98           C  
ANISOU 3570  CD2 LEU D1270     3161   2933   2637   -442    122     -1       C  
ATOM   3571  N   THR D1271      21.975  -0.356  25.328  1.00 28.18           N  
ANISOU 3571  N   THR D1271     3993   3492   3221   -691     21     88       N  
ATOM   3572  CA  THR D1271      21.436  -1.732  25.212  1.00 30.39           C  
ANISOU 3572  CA  THR D1271     4329   3747   3469   -784      0    107       C  
ATOM   3573  C   THR D1271      20.210  -1.830  24.356  1.00 31.48           C  
ANISOU 3573  C   THR D1271     4418   3961   3582   -820     22     74       C  
ATOM   3574  O   THR D1271      19.838  -2.937  23.970  1.00 34.37           O  
ANISOU 3574  O   THR D1271     4828   4298   3932   -890      7     79       O  
ATOM   3575  CB  THR D1271      21.148  -2.386  26.564  1.00 32.64           C  
ANISOU 3575  CB  THR D1271     4662   4041   3697   -884    -11    143       C  
ATOM   3576  OG1 THR D1271      20.229  -1.595  27.334  1.00 33.35           O  
ANISOU 3576  OG1 THR D1271     4677   4256   3738   -921     24    123       O  
ATOM   3577  CG2 THR D1271      22.451  -2.609  27.330  1.00 32.78           C  
ANISOU 3577  CG2 THR D1271     4747   3971   3736   -845    -47    180       C  
ATOM   3578  N   ASP D1272      19.622  -0.699  23.994  1.00 28.99           N  
ANISOU 3578  N   ASP D1272     4016   3737   3262   -767     55     35       N  
ATOM   3579  CA  ASP D1272      18.361  -0.706  23.297  1.00 29.83           C  
ANISOU 3579  CA  ASP D1272     4061   3942   3330   -795     76     -5       C  
ATOM   3580  C   ASP D1272      18.339   0.174  22.051  1.00 28.40           C  
ANISOU 3580  C   ASP D1272     3828   3783   3179   -683     91    -37       C  
ATOM   3581  O   ASP D1272      17.301   0.750  21.714  1.00 28.54           O  
ANISOU 3581  O   ASP D1272     3772   3912   3159   -665    113    -79       O  
ATOM   3582  CB  ASP D1272      17.219  -0.378  24.291  1.00 30.53           C  
ANISOU 3582  CB  ASP D1272     4090   4161   3347   -866    100    -27       C  
ATOM   3583  CG  ASP D1272      17.233   1.073  24.792  1.00 31.53           C  
ANISOU 3583  CG  ASP D1272     4154   4348   3475   -783    122    -48       C  
ATOM   3584  OD1 ASP D1272      18.271   1.757  24.694  1.00 29.04           O  
ANISOU 3584  OD1 ASP D1272     3858   3956   3216   -693    118    -33       O  
ATOM   3585  OD2 ASP D1272      16.181   1.544  25.259  1.00 31.73           O  
ANISOU 3585  OD2 ASP D1272     4108   4502   3445   -809    143    -86       O  
ATOM   3586  N   LEU D1273      19.470   0.248  21.334  1.00 27.30           N  
ANISOU 3586  N   LEU D1273     3727   3544   3101   -606     77    -21       N  
ATOM   3587  CA  LEU D1273      19.518   0.958  20.062  1.00 26.55           C  
ANISOU 3587  CA  LEU D1273     3597   3459   3029   -508     91    -43       C  
ATOM   3588  C   LEU D1273      18.508   0.274  19.124  1.00 28.28           C  
ANISOU 3588  C   LEU D1273     3788   3741   3215   -542     89    -75       C  
ATOM   3589  O   LEU D1273      18.503  -0.948  19.003  1.00 29.85           O  
ANISOU 3589  O   LEU D1273     4028   3900   3412   -617     67    -69       O  
ATOM   3590  CB  LEU D1273      20.940   0.946  19.492  1.00 25.41           C  
ANISOU 3590  CB  LEU D1273     3502   3203   2949   -443     77    -22       C  
ATOM   3591  CG  LEU D1273      21.113   1.613  18.125  1.00 24.50           C  
ANISOU 3591  CG  LEU D1273     3363   3091   2855   -349     93    -37       C  
ATOM   3592  CD1 LEU D1273      20.943   3.101  18.256  1.00 23.63           C  
ANISOU 3592  CD1 LEU D1273     3216   3020   2740   -278    127    -45       C  
ATOM   3593  CD2 LEU D1273      22.464   1.247  17.501  1.00 24.50           C  
ANISOU 3593  CD2 LEU D1273     3408   2990   2908   -311     75    -23       C  
ATOM   3594  N   SER D1274      17.661   1.071  18.496  1.00 29.04           N  
ANISOU 3594  N   SER D1274     3816   3935   3282   -485    111   -112       N  
ATOM   3595  CA  SER D1274      16.629   0.593  17.594  1.00 30.42           C  
ANISOU 3595  CA  SER D1274     3944   4195   3416   -504    112   -154       C  
ATOM   3596  C   SER D1274      16.475   1.569  16.419  1.00 30.25           C  
ANISOU 3596  C   SER D1274     3881   4215   3394   -378    126   -175       C  
ATOM   3597  O   SER D1274      16.842   2.755  16.511  1.00 28.71           O  
ANISOU 3597  O   SER D1274     3686   4007   3216   -288    141   -163       O  
ATOM   3598  CB  SER D1274      15.299   0.439  18.361  1.00 31.32           C  
ANISOU 3598  CB  SER D1274     4001   4439   3459   -592    125   -191       C  
ATOM   3599  OG  SER D1274      14.676   1.683  18.551  1.00 32.59           O  
ANISOU 3599  OG  SER D1274     4095   4700   3587   -516    145   -220       O  
ATOM   3600  N   PHE D1275      15.909   1.072  15.328  1.00 32.52           N  
ANISOU 3600  N   PHE D1275     4139   4555   3660   -373    121   -209       N  
ATOM   3601  CA  PHE D1275      15.698   1.867  14.127  1.00 32.21           C  
ANISOU 3601  CA  PHE D1275     4065   4563   3609   -254    130   -228       C  
ATOM   3602  C   PHE D1275      14.223   2.218  13.941  1.00 34.27           C  
ANISOU 3602  C   PHE D1275     4237   4988   3793   -236    139   -289       C  
ATOM   3603  O   PHE D1275      13.327   1.395  14.212  1.00 34.78           O  
ANISOU 3603  O   PHE D1275     4260   5138   3814   -335    136   -330       O  
ATOM   3604  CB  PHE D1275      16.236   1.136  12.897  1.00 31.75           C  
ANISOU 3604  CB  PHE D1275     4032   4451   3579   -239    115   -227       C  
ATOM   3605  CG  PHE D1275      17.680   0.731  13.022  1.00 30.88           C  
ANISOU 3605  CG  PHE D1275     3999   4194   3538   -250    101   -180       C  
ATOM   3606  CD1 PHE D1275      18.682   1.687  13.050  1.00 31.15           C  
ANISOU 3606  CD1 PHE D1275     4066   4158   3612   -172    114   -143       C  
ATOM   3607  CD2 PHE D1275      18.045  -0.608  13.123  1.00 31.06           C  
ANISOU 3607  CD2 PHE D1275     4066   4151   3584   -337     75   -178       C  
ATOM   3608  CE1 PHE D1275      20.005   1.301  13.155  1.00 30.24           C  
ANISOU 3608  CE1 PHE D1275     4008   3926   3552   -181    101   -113       C  
ATOM   3609  CE2 PHE D1275      19.365  -0.986  13.219  1.00 30.33           C  
ANISOU 3609  CE2 PHE D1275     4039   3935   3549   -332     56   -144       C  
ATOM   3610  CZ  PHE D1275      20.344  -0.037  13.217  1.00 29.15           C  
ANISOU 3610  CZ  PHE D1275     3906   3734   3434   -253     69   -115       C  
ATOM   3611  N   VAL D1276      13.991   3.443  13.487  1.00 35.00           N  
ANISOU 3611  N   VAL D1276     4306   5126   3866   -109    150   -296       N  
ATOM   3612  CA  VAL D1276      12.650   3.972  13.219  1.00 37.02           C  
ANISOU 3612  CA  VAL D1276     4477   5544   4045    -53    154   -358       C  
ATOM   3613  C   VAL D1276      12.667   4.711  11.879  1.00 36.98           C  
ANISOU 3613  C   VAL D1276     4471   5552   4026     91    153   -359       C  
ATOM   3614  O   VAL D1276      13.747   5.079  11.395  1.00 35.26           O  
ANISOU 3614  O   VAL D1276     4322   5214   3861    147    159   -304       O  
ATOM   3615  CB  VAL D1276      12.209   4.968  14.332  1.00 38.41           C  
ANISOU 3615  CB  VAL D1276     4627   5771   4194    -24    164   -370       C  
ATOM   3616  CG1 VAL D1276      12.486   4.400  15.702  1.00 38.28           C  
ANISOU 3616  CG1 VAL D1276     4630   5714   4198   -154    167   -351       C  
ATOM   3617  CG2 VAL D1276      12.889   6.331  14.209  1.00 38.66           C  
ANISOU 3617  CG2 VAL D1276     4710   5720   4257    106    174   -330       C  
ATOM   3618  N   ASP D1277      11.482   4.941  11.305  1.00 37.79           N  
ANISOU 3618  N   ASP D1277     4496   5807   4053    151    148   -421       N  
ATOM   3619  CA  ASP D1277      11.303   5.800  10.112  1.00 39.66           C  
ANISOU 3619  CA  ASP D1277     4730   6080   4258    309    146   -424       C  
ATOM   3620  C   ASP D1277      12.408   5.598   9.077  1.00 39.66           C  
ANISOU 3620  C   ASP D1277     4798   5959   4308    338    147   -370       C  
ATOM   3621  O   ASP D1277      13.207   6.492   8.801  1.00 38.65           O  
ANISOU 3621  O   ASP D1277     4739   5733   4210    424    159   -315       O  
ATOM   3622  CB  ASP D1277      11.234   7.281  10.522  1.00 41.36           C  
ANISOU 3622  CB  ASP D1277     4969   6285   4459    431    153   -408       C  
ATOM   3623  CG  ASP D1277      10.186   7.543  11.581  1.00 42.43           C  
ANISOU 3623  CG  ASP D1277     5033   6546   4543    410    150   -468       C  
ATOM   3624  OD1 ASP D1277       9.293   6.677  11.751  1.00 45.62           O  
ANISOU 3624  OD1 ASP D1277     5353   7079   4901    321    143   -532       O  
ATOM   3625  OD2 ASP D1277      10.256   8.597  12.241  1.00 43.59           O  
ANISOU 3625  OD2 ASP D1277     5205   6663   4694    478    156   -456       O  
ATOM   3626  N   ILE D1278      12.425   4.398   8.523  1.00 38.68           N  
ANISOU 3626  N   ILE D1278     4654   5849   4191    259    137   -392       N  
ATOM   3627  CA  ILE D1278      13.452   3.950   7.585  1.00 39.24           C  
ANISOU 3627  CA  ILE D1278     4778   5821   4310    266    134   -354       C  
ATOM   3628  C   ILE D1278      12.976   4.243   6.160  1.00 40.09           C  
ANISOU 3628  C   ILE D1278     4851   6018   4361    380    129   -379       C  
ATOM   3629  O   ILE D1278      12.085   3.562   5.631  1.00 42.13           O  
ANISOU 3629  O   ILE D1278     5037   6400   4570    359    116   -445       O  
ATOM   3630  CB  ILE D1278      13.722   2.429   7.768  1.00 37.18           C  
ANISOU 3630  CB  ILE D1278     4519   5520   4085    122    121   -370       C  
ATOM   3631  CG1 ILE D1278      14.132   2.129   9.231  1.00 37.19           C  
ANISOU 3631  CG1 ILE D1278     4560   5440   4131     15    123   -342       C  
ATOM   3632  CG2 ILE D1278      14.782   1.911   6.780  1.00 36.33           C  
ANISOU 3632  CG2 ILE D1278     4459   5319   4025    135    113   -343       C  
ATOM   3633  CD1 ILE D1278      13.809   0.730   9.699  1.00 38.34           C  
ANISOU 3633  CD1 ILE D1278     4695   5592   4279   -133    110   -373       C  
ATOM   3634  N   THR D1279      13.530   5.297   5.574  1.00 40.49           N  
ANISOU 3634  N   THR D1279     4957   6014   4414    499    141   -329       N  
ATOM   3635  CA  THR D1279      13.262   5.627   4.184  1.00 40.15           C  
ANISOU 3635  CA  THR D1279     4900   6037   4316    615    137   -337       C  
ATOM   3636  C   THR D1279      14.426   5.094   3.393  1.00 41.51           C  
ANISOU 3636  C   THR D1279     5121   6111   4539    591    142   -299       C  
ATOM   3637  O   THR D1279      15.359   4.520   3.955  1.00 43.51           O  
ANISOU 3637  O   THR D1279     5413   6253   4864    496    145   -274       O  
ATOM   3638  CB  THR D1279      13.146   7.144   3.945  1.00 40.90           C  
ANISOU 3638  CB  THR D1279     5039   6127   4372    766    149   -300       C  
ATOM   3639  OG1 THR D1279      14.437   7.744   4.047  1.00 38.69           O  
ANISOU 3639  OG1 THR D1279     4859   5687   4154    772    174   -221       O  
ATOM   3640  CG2 THR D1279      12.181   7.790   4.910  1.00 41.93           C  
ANISOU 3640  CG2 THR D1279     5134   6333   4464    796    144   -335       C  
ATOM   3641  N   ASP D1280      14.367   5.296   2.085  1.00 40.52           N  
ANISOU 3641  N   ASP D1280     4990   6036   4370    685    140   -300       N  
ATOM   3642  CA  ASP D1280      15.455   4.899   1.181  1.00 40.76           C  
ANISOU 3642  CA  ASP D1280     5059   5990   4434    678    146   -268       C  
ATOM   3643  C   ASP D1280      16.701   5.802   1.200  1.00 41.11           C  
ANISOU 3643  C   ASP D1280     5200   5898   4522    712    176   -187       C  
ATOM   3644  O   ASP D1280      17.712   5.492   0.544  1.00 41.53           O  
ANISOU 3644  O   ASP D1280     5283   5890   4605    697    184   -163       O  
ATOM   3645  CB  ASP D1280      14.908   4.771  -0.236  1.00 41.91           C  
ANISOU 3645  CB  ASP D1280     5159   6254   4510    763    135   -302       C  
ATOM   3646  CG  ASP D1280      14.324   6.061  -0.775  1.00 42.63           C  
ANISOU 3646  CG  ASP D1280     5267   6407   4522    916    142   -279       C  
ATOM   3647  OD1 ASP D1280      14.238   7.071  -0.036  1.00 41.50           O  
ANISOU 3647  OD1 ASP D1280     5169   6219   4379    959    154   -244       O  
ATOM   3648  OD2 ASP D1280      13.925   6.044  -1.961  1.00 43.56           O  
ANISOU 3648  OD2 ASP D1280     5353   6621   4574    999    132   -300       O  
ATOM   3649  N   SER D1281      16.624   6.932   1.896  1.00 41.24           N  
ANISOU 3649  N   SER D1281     5260   5873   4534    758    193   -150       N  
ATOM   3650  CA  SER D1281      17.808   7.742   2.157  1.00 39.74           C  
ANISOU 3650  CA  SER D1281     5161   5546   4393    760    225    -82       C  
ATOM   3651  C   SER D1281      17.990   8.138   3.618  1.00 36.28           C  
ANISOU 3651  C   SER D1281     4747   5034   4002    705    234    -69       C  
ATOM   3652  O   SER D1281      18.859   8.945   3.915  1.00 34.41           O  
ANISOU 3652  O   SER D1281     4582   4692   3799    711    263    -20       O  
ATOM   3653  CB  SER D1281      17.813   8.982   1.250  1.00 41.14           C  
ANISOU 3653  CB  SER D1281     5400   5717   4515    888    248    -34       C  
ATOM   3654  OG  SER D1281      16.602   9.695   1.369  1.00 43.92           O  
ANISOU 3654  OG  SER D1281     5735   6152   4800    985    235    -53       O  
ATOM   3655  N   SER D1282      17.195   7.556   4.527  1.00 35.57           N  
ANISOU 3655  N   SER D1282     4598   5005   3912    646    211   -116       N  
ATOM   3656  CA  SER D1282      17.201   7.977   5.930  1.00 34.94           C  
ANISOU 3656  CA  SER D1282     4532   4879   3864    603    218   -110       C  
ATOM   3657  C   SER D1282      16.962   6.814   6.887  1.00 33.17           C  
ANISOU 3657  C   SER D1282     4257   4677   3666    479    197   -148       C  
ATOM   3658  O   SER D1282      16.192   5.936   6.604  1.00 33.00           O  
ANISOU 3658  O   SER D1282     4174   4748   3613    446    176   -196       O  
ATOM   3659  CB  SER D1282      16.144   9.082   6.173  1.00 37.22           C  
ANISOU 3659  CB  SER D1282     4812   5236   4092    704    219   -124       C  
ATOM   3660  OG  SER D1282      16.327   9.712   7.423  1.00 38.81           O  
ANISOU 3660  OG  SER D1282     5041   5378   4326    680    230   -112       O  
ATOM   3661  N   ILE D1283      17.652   6.808   8.029  1.00 32.48           N  
ANISOU 3661  N   ILE D1283     4202   4502   3635    407    204   -126       N  
ATOM   3662  CA  ILE D1283      17.348   5.890   9.109  1.00 32.44           C  
ANISOU 3662  CA  ILE D1283     4164   4516   3646    295    186   -154       C  
ATOM   3663  C   ILE D1283      17.310   6.657  10.435  1.00 32.27           C  
ANISOU 3663  C   ILE D1283     4156   4470   3636    284    198   -143       C  
ATOM   3664  O   ILE D1283      18.306   7.256  10.845  1.00 30.78           O  
ANISOU 3664  O   ILE D1283     4022   4179   3494    289    215   -104       O  
ATOM   3665  CB  ILE D1283      18.350   4.712   9.201  1.00 31.41           C  
ANISOU 3665  CB  ILE D1283     4059   4300   3573    201    172   -142       C  
ATOM   3666  CG1 ILE D1283      18.376   3.895   7.888  1.00 31.23           C  
ANISOU 3666  CG1 ILE D1283     4019   4305   3540    211    158   -162       C  
ATOM   3667  CG2 ILE D1283      18.007   3.797  10.385  1.00 31.35           C  
ANISOU 3667  CG2 ILE D1283     4034   4301   3574     86    154   -161       C  
ATOM   3668  CD1 ILE D1283      19.572   2.963   7.755  1.00 30.48           C  
ANISOU 3668  CD1 ILE D1283     3962   4114   3504    155    143   -149       C  
ATOM   3669  N   GLY D1284      16.136   6.697  11.079  1.00 32.46           N  
ANISOU 3669  N   GLY D1284     4122   4599   3612    272    190   -185       N  
ATOM   3670  CA  GLY D1284      16.035   7.261  12.428  1.00 30.47           C  
ANISOU 3670  CA  GLY D1284     3870   4338   3366    247    197   -185       C  
ATOM   3671  C   GLY D1284      16.650   6.283  13.436  1.00 30.19           C  
ANISOU 3671  C   GLY D1284     3850   4244   3377    117    189   -171       C  
ATOM   3672  O   GLY D1284      16.481   5.064  13.299  1.00 29.73           O  
ANISOU 3672  O   GLY D1284     3775   4205   3315     35    171   -186       O  
ATOM   3673  N   LEU D1285      17.381   6.780  14.440  1.00 29.51           N  
ANISOU 3673  N   LEU D1285     3801   4080   3329     99    199   -144       N  
ATOM   3674  CA  LEU D1285      17.870   5.917  15.522  1.00 29.29           C  
ANISOU 3674  CA  LEU D1285     3787   4008   3331    -13    188   -132       C  
ATOM   3675  C   LEU D1285      17.180   6.345  16.804  1.00 30.51           C  
ANISOU 3675  C   LEU D1285     3907   4228   3456    -41    192   -154       C  
ATOM   3676  O   LEU D1285      16.831   7.526  16.978  1.00 34.06           O  
ANISOU 3676  O   LEU D1285     4344   4707   3888     36    207   -167       O  
ATOM   3677  CB  LEU D1285      19.396   6.011  15.728  1.00 28.14           C  
ANISOU 3677  CB  LEU D1285     3706   3731   3254    -19    193    -90       C  
ATOM   3678  CG  LEU D1285      20.358   5.564  14.650  1.00 28.38           C  
ANISOU 3678  CG  LEU D1285     3772   3688   3321     -1    188    -70       C  
ATOM   3679  CD1 LEU D1285      21.659   6.325  14.790  1.00 25.59           C  
ANISOU 3679  CD1 LEU D1285     3465   3237   3017     29    208    -43       C  
ATOM   3680  CD2 LEU D1285      20.660   4.072  14.764  1.00 28.35           C  
ANISOU 3680  CD2 LEU D1285     3781   3656   3334    -87    157    -70       C  
ATOM   3681  N   ARG D1286      16.991   5.384  17.689  1.00 29.50           N  
ANISOU 3681  N   ARG D1286     3769   4119   3318   -152    179   -157       N  
ATOM   3682  CA  ARG D1286      16.459   5.648  19.004  1.00 30.29           C  
ANISOU 3682  CA  ARG D1286     3838   4281   3387   -198    183   -174       C  
ATOM   3683  C   ARG D1286      17.085   4.705  20.049  1.00 29.07           C  
ANISOU 3683  C   ARG D1286     3722   4068   3254   -310    170   -143       C  
ATOM   3684  O   ARG D1286      17.264   3.470  19.830  1.00 30.65           O  
ANISOU 3684  O   ARG D1286     3952   4232   3461   -386    152   -128       O  
ATOM   3685  CB  ARG D1286      14.936   5.528  18.941  1.00 33.29           C  
ANISOU 3685  CB  ARG D1286     4138   4818   3691   -213    183   -231       C  
ATOM   3686  CG  ARG D1286      14.219   5.696  20.269  1.00 37.17           C  
ANISOU 3686  CG  ARG D1286     4582   5404   4136   -272    189   -259       C  
ATOM   3687  CD  ARG D1286      12.716   5.819  20.062  1.00 40.32           C  
ANISOU 3687  CD  ARG D1286     4888   5976   4453   -262    191   -330       C  
ATOM   3688  NE  ARG D1286      12.149   4.689  19.311  1.00 43.57           N  
ANISOU 3688  NE  ARG D1286     5276   6441   4836   -332    184   -351       N  
ATOM   3689  CZ  ARG D1286      10.865   4.572  18.977  1.00 45.72           C  
ANISOU 3689  CZ  ARG D1286     5461   6873   5034   -339    186   -420       C  
ATOM   3690  NH1 ARG D1286       9.984   5.524  19.307  1.00 48.08           N  
ANISOU 3690  NH1 ARG D1286     5687   7303   5278   -268    191   -477       N  
ATOM   3691  NH2 ARG D1286      10.446   3.493  18.306  1.00 46.38           N  
ANISOU 3691  NH2 ARG D1286     5529   6995   5098   -415    181   -441       N  
ATOM   3692  N   TRP D1287      17.432   5.297  21.189  1.00 28.80           N  
ANISOU 3692  N   TRP D1287     3694   4020   3229   -315    178   -135       N  
ATOM   3693  CA  TRP D1287      17.955   4.580  22.337  1.00 27.59           C  
ANISOU 3693  CA  TRP D1287     3574   3826   3082   -408    165   -106       C  
ATOM   3694  C   TRP D1287      17.455   5.290  23.589  1.00 28.10           C  
ANISOU 3694  C   TRP D1287     3596   3967   3111   -422    178   -129       C  
ATOM   3695  O   TRP D1287      16.974   6.431  23.525  1.00 29.21           O  
ANISOU 3695  O   TRP D1287     3695   4165   3239   -343    194   -163       O  
ATOM   3696  CB  TRP D1287      19.501   4.523  22.333  1.00 26.89           C  
ANISOU 3696  CB  TRP D1287     3553   3602   3062   -385    155    -66       C  
ATOM   3697  CG  TRP D1287      20.189   5.858  22.386  1.00 25.12           C  
ANISOU 3697  CG  TRP D1287     3330   3337   2875   -298    177    -70       C  
ATOM   3698  CD1 TRP D1287      20.630   6.496  23.507  1.00 24.87           C  
ANISOU 3698  CD1 TRP D1287     3298   3296   2853   -299    185    -72       C  
ATOM   3699  CD2 TRP D1287      20.537   6.719  21.284  1.00 24.76           C  
ANISOU 3699  CD2 TRP D1287     3294   3252   2860   -203    195    -73       C  
ATOM   3700  NE1 TRP D1287      21.218   7.662  23.201  1.00 24.07           N  
ANISOU 3700  NE1 TRP D1287     3207   3149   2790   -220    208    -79       N  
ATOM   3701  CE2 TRP D1287      21.196   7.841  21.841  1.00 24.91           C  
ANISOU 3701  CE2 TRP D1287     3324   3230   2908   -161    216    -76       C  
ATOM   3702  CE3 TRP D1287      20.396   6.641  19.871  1.00 25.26           C  
ANISOU 3702  CE3 TRP D1287     3362   3308   2927   -152    197    -73       C  
ATOM   3703  CZ2 TRP D1287      21.657   8.914  21.055  1.00 24.67           C  
ANISOU 3703  CZ2 TRP D1287     3316   3148   2908    -77    242    -77       C  
ATOM   3704  CZ3 TRP D1287      20.836   7.706  19.101  1.00 24.75           C  
ANISOU 3704  CZ3 TRP D1287     3317   3200   2887    -63    221    -70       C  
ATOM   3705  CH2 TRP D1287      21.484   8.831  19.691  1.00 24.68           C  
ANISOU 3705  CH2 TRP D1287     3327   3141   2906    -30    245    -69       C  
ATOM   3706  N   THR D1288      17.631   4.637  24.722  1.00 27.94           N  
ANISOU 3706  N   THR D1288     3595   3944   3074   -514    167   -108       N  
ATOM   3707  CA  THR D1288      17.389   5.275  26.002  1.00 26.52           C  
ANISOU 3707  CA  THR D1288     3381   3829   2866   -529    178   -125       C  
ATOM   3708  C   THR D1288      18.666   5.929  26.523  1.00 25.66           C  
ANISOU 3708  C   THR D1288     3310   3626   2813   -480    178   -104       C  
ATOM   3709  O   THR D1288      19.679   5.243  26.695  1.00 25.93           O  
ANISOU 3709  O   THR D1288     3403   3568   2880   -510    160    -64       O  
ATOM   3710  CB  THR D1288      16.862   4.276  27.034  1.00 27.97           C  
ANISOU 3710  CB  THR D1288     3563   4072   2990   -659    170   -113       C  
ATOM   3711  OG1 THR D1288      15.616   3.734  26.569  1.00 28.26           O  
ANISOU 3711  OG1 THR D1288     3555   4212   2969   -716    176   -145       O  
ATOM   3712  CG2 THR D1288      16.630   4.945  28.365  1.00 28.04           C  
ANISOU 3712  CG2 THR D1288     3532   4158   2964   -674    181   -134       C  
ATOM   3713  N   PRO D1289      18.645   7.248  26.794  1.00 25.22           N  
ANISOU 3713  N   PRO D1289     3221   3592   2767   -405    198   -137       N  
ATOM   3714  CA  PRO D1289      19.873   7.789  27.344  1.00 23.00           C  
ANISOU 3714  CA  PRO D1289     2974   3228   2537   -377    201   -124       C  
ATOM   3715  C   PRO D1289      20.313   7.185  28.675  1.00 23.38           C  
ANISOU 3715  C   PRO D1289     3035   3280   2567   -456    185   -104       C  
ATOM   3716  O   PRO D1289      19.466   6.817  29.525  1.00 24.86           O  
ANISOU 3716  O   PRO D1289     3190   3563   2691   -525    183   -112       O  
ATOM   3717  CB  PRO D1289      19.574   9.296  27.497  1.00 24.17           C  
ANISOU 3717  CB  PRO D1289     3085   3407   2689   -294    225   -171       C  
ATOM   3718  CG  PRO D1289      18.429   9.526  26.611  1.00 24.96           C  
ANISOU 3718  CG  PRO D1289     3150   3576   2755   -248    231   -198       C  
ATOM   3719  CD  PRO D1289      17.608   8.285  26.736  1.00 25.41           C  
ANISOU 3719  CD  PRO D1289     3182   3714   2755   -343    215   -191       C  
ATOM   3720  N   LEU D1290      21.628   7.061  28.845  1.00 22.58           N  
ANISOU 3720  N   LEU D1290     2981   3084   2513   -446    175    -79       N  
ATOM   3721  CA  LEU D1290      22.248   6.523  30.054  1.00 22.39           C  
ANISOU 3721  CA  LEU D1290     2977   3053   2474   -500    155    -58       C  
ATOM   3722  C   LEU D1290      22.344   7.644  31.089  1.00 21.46           C  
ANISOU 3722  C   LEU D1290     2817   2984   2353   -476    173    -97       C  
ATOM   3723  O   LEU D1290      22.412   8.818  30.748  1.00 21.06           O  
ANISOU 3723  O   LEU D1290     2744   2922   2335   -407    199   -134       O  
ATOM   3724  CB  LEU D1290      23.617   5.913  29.711  1.00 22.86           C  
ANISOU 3724  CB  LEU D1290     3099   3004   2583   -485    131    -27       C  
ATOM   3725  CG  LEU D1290      23.629   4.650  28.877  1.00 23.84           C  
ANISOU 3725  CG  LEU D1290     3273   3075   2707   -514    105      9       C  
ATOM   3726  CD1 LEU D1290      25.044   4.279  28.454  1.00 24.07           C  
ANISOU 3726  CD1 LEU D1290     3351   3005   2789   -474     82     23       C  
ATOM   3727  CD2 LEU D1290      22.952   3.512  29.613  1.00 24.71           C  
ANISOU 3727  CD2 LEU D1290     3409   3223   2755   -609     83     41       C  
ATOM   3728  N   ASN D1291      22.353   7.311  32.375  1.00 22.22           N  
ANISOU 3728  N   ASN D1291     2905   3130   2405   -532    161    -90       N  
ATOM   3729  CA  ASN D1291      22.066   8.294  33.376  1.00 23.24           C  
ANISOU 3729  CA  ASN D1291     2978   3336   2513   -520    179   -136       C  
ATOM   3730  C   ASN D1291      23.268   8.763  34.180  1.00 23.65           C  
ANISOU 3730  C   ASN D1291     3036   3352   2595   -497    176   -149       C  
ATOM   3731  O   ASN D1291      23.170   9.768  34.861  1.00 23.95           O  
ANISOU 3731  O   ASN D1291     3029   3439   2631   -473    194   -198       O  
ATOM   3732  CB  ASN D1291      20.955   7.789  34.304  1.00 24.04           C  
ANISOU 3732  CB  ASN D1291     3045   3560   2528   -602    175   -135       C  
ATOM   3733  CG  ASN D1291      19.649   7.589  33.580  1.00 25.50           C  
ANISOU 3733  CG  ASN D1291     3199   3811   2677   -621    185   -147       C  
ATOM   3734  OD1 ASN D1291      19.052   8.553  33.086  1.00 25.73           O  
ANISOU 3734  OD1 ASN D1291     3181   3878   2715   -555    204   -196       O  
ATOM   3735  ND2 ASN D1291      19.189   6.337  33.478  1.00 26.03           N  
ANISOU 3735  ND2 ASN D1291     3296   3892   2701   -709    171   -106       N  
ATOM   3736  N   SER D1292      24.402   8.047  34.106  1.00 23.59           N  
ANISOU 3736  N   SER D1292     3081   3265   2614   -502    152   -114       N  
ATOM   3737  CA  SER D1292      25.584   8.438  34.898  1.00 23.71           C  
ANISOU 3737  CA  SER D1292     3094   3262   2652   -480    147   -135       C  
ATOM   3738  C   SER D1292      26.002   9.856  34.530  1.00 23.38           C  
ANISOU 3738  C   SER D1292     3022   3190   2669   -416    183   -193       C  
ATOM   3739  O   SER D1292      25.916  10.279  33.386  1.00 21.97           O  
ANISOU 3739  O   SER D1292     2856   2958   2532   -377    203   -198       O  
ATOM   3740  CB  SER D1292      26.770   7.462  34.771  1.00 24.88           C  
ANISOU 3740  CB  SER D1292     3298   3335   2817   -478    110    -98       C  
ATOM   3741  OG  SER D1292      27.922   8.047  35.368  1.00 24.66           O  
ANISOU 3741  OG  SER D1292     3253   3300   2816   -445    112   -136       O  
ATOM   3742  N   SER D1293      26.459  10.557  35.533  1.00 22.78           N  
ANISOU 3742  N   SER D1293     2913   3149   2593   -410    192   -236       N  
ATOM   3743  CA  SER D1293      26.870  11.932  35.397  1.00 23.42           C  
ANISOU 3743  CA  SER D1293     2971   3201   2726   -363    229   -297       C  
ATOM   3744  C   SER D1293      28.151  12.006  34.573  1.00 21.40           C  
ANISOU 3744  C   SER D1293     2749   2848   2533   -337    236   -299       C  
ATOM   3745  O   SER D1293      28.485  13.032  34.031  1.00 23.04           O  
ANISOU 3745  O   SER D1293     2959   3004   2790   -304    272   -336       O  
ATOM   3746  CB  SER D1293      27.075  12.523  36.783  1.00 24.82           C  
ANISOU 3746  CB  SER D1293     3100   3448   2881   -373    232   -348       C  
ATOM   3747  OG  SER D1293      27.991  11.774  37.556  1.00 25.88           O  
ANISOU 3747  OG  SER D1293     3240   3597   2995   -397    201   -333       O  
ATOM   3748  N   THR D1294      28.817  10.855  34.426  1.00 21.16           N  
ANISOU 3748  N   THR D1294     2750   2792   2497   -352    201   -257       N  
ATOM   3749  CA  THR D1294      30.090  10.764  33.686  1.00 19.94           C  
ANISOU 3749  CA  THR D1294     2619   2563   2392   -329    202   -264       C  
ATOM   3750  C   THR D1294      29.872  10.846  32.183  1.00 18.91           C  
ANISOU 3750  C   THR D1294     2520   2365   2299   -306    222   -244       C  
ATOM   3751  O   THR D1294      30.804  11.124  31.444  1.00 19.12           O  
ANISOU 3751  O   THR D1294     2559   2336   2370   -287    239   -261       O  
ATOM   3752  CB  THR D1294      30.895   9.483  33.983  1.00 20.82           C  
ANISOU 3752  CB  THR D1294     2756   2671   2482   -337    151   -233       C  
ATOM   3753  OG1 THR D1294      30.119   8.343  33.709  1.00 21.10           O  
ANISOU 3753  OG1 THR D1294     2831   2703   2481   -360    119   -170       O  
ATOM   3754  CG2 THR D1294      31.323   9.407  35.501  1.00 21.42           C  
ANISOU 3754  CG2 THR D1294     2803   2817   2517   -350    128   -255       C  
ATOM   3755  N   ILE D1295      28.654  10.593  31.740  1.00 18.48           N  
ANISOU 3755  N   ILE D1295     2474   2326   2219   -310    220   -211       N  
ATOM   3756  CA  ILE D1295      28.376  10.510  30.300  1.00 18.68           C  
ANISOU 3756  CA  ILE D1295     2529   2298   2269   -285    232   -187       C  
ATOM   3757  C   ILE D1295      28.301  11.901  29.738  1.00 19.30           C  
ANISOU 3757  C   ILE D1295     2606   2344   2383   -245    280   -221       C  
ATOM   3758  O   ILE D1295      27.561  12.745  30.227  1.00 19.71           O  
ANISOU 3758  O   ILE D1295     2636   2432   2422   -233    299   -248       O  
ATOM   3759  CB  ILE D1295      27.170   9.659  29.962  1.00 19.06           C  
ANISOU 3759  CB  ILE D1295     2586   2381   2276   -305    210   -145       C  
ATOM   3760  CG1 ILE D1295      27.383   8.286  30.545  1.00 20.04           C  
ANISOU 3760  CG1 ILE D1295     2731   2516   2366   -351    164   -109       C  
ATOM   3761  CG2 ILE D1295      26.973   9.474  28.466  1.00 17.96           C  
ANISOU 3761  CG2 ILE D1295     2472   2192   2157   -277    218   -124       C  
ATOM   3762  CD1 ILE D1295      26.272   7.356  30.420  1.00 20.61           C  
ANISOU 3762  CD1 ILE D1295     2814   2623   2391   -393    144    -71       C  
ATOM   3763  N   ILE D1296      29.037  12.102  28.656  1.00 18.33           N  
ANISOU 3763  N   ILE D1296     2512   2151   2302   -224    300   -219       N  
ATOM   3764  CA  ILE D1296      29.139  13.403  28.049  1.00 18.28           C  
ANISOU 3764  CA  ILE D1296     2523   2094   2329   -192    349   -244       C  
ATOM   3765  C   ILE D1296      28.419  13.441  26.728  1.00 18.11           C  
ANISOU 3765  C   ILE D1296     2532   2044   2304   -154    359   -211       C  
ATOM   3766  O   ILE D1296      28.140  14.537  26.193  1.00 18.30           O  
ANISOU 3766  O   ILE D1296     2581   2028   2341   -115    395   -222       O  
ATOM   3767  CB  ILE D1296      30.609  13.910  27.943  1.00 19.49           C  
ANISOU 3767  CB  ILE D1296     2683   2194   2526   -205    377   -279       C  
ATOM   3768  CG1 ILE D1296      31.494  13.015  27.044  1.00 20.31           C  
ANISOU 3768  CG1 ILE D1296     2802   2269   2645   -211    363   -257       C  
ATOM   3769  CG2 ILE D1296      31.201  14.088  29.334  1.00 20.07           C  
ANISOU 3769  CG2 ILE D1296     2718   2310   2598   -234    371   -325       C  
ATOM   3770  CD1 ILE D1296      32.505  13.810  26.284  1.00 20.94           C  
ANISOU 3770  CD1 ILE D1296     2901   2291   2764   -214    410   -284       C  
ATOM   3771  N   GLY D1297      28.006  12.271  26.248  1.00 16.22           N  
ANISOU 3771  N   GLY D1297     2293   1827   2042   -162    324   -172       N  
ATOM   3772  CA  GLY D1297      27.245  12.200  24.988  1.00 16.11           C  
ANISOU 3772  CA  GLY D1297     2299   1802   2017   -125    329   -145       C  
ATOM   3773  C   GLY D1297      27.480  10.918  24.253  1.00 15.63           C  
ANISOU 3773  C   GLY D1297     2249   1734   1955   -141    298   -112       C  
ATOM   3774  O   GLY D1297      27.908   9.935  24.857  1.00 15.93           O  
ANISOU 3774  O   GLY D1297     2280   1784   1986   -180    264   -105       O  
ATOM   3775  N   TYR D1298      27.196  10.928  22.968  1.00 15.57           N  
ANISOU 3775  N   TYR D1298     2261   1705   1948   -107    308    -94       N  
ATOM   3776  CA  TYR D1298      27.199   9.713  22.087  1.00 15.51           C  
ANISOU 3776  CA  TYR D1298     2261   1695   1934   -115    279    -67       C  
ATOM   3777  C   TYR D1298      27.843  10.066  20.781  1.00 16.10           C  
ANISOU 3777  C   TYR D1298     2363   1719   2034    -80    304    -61       C  
ATOM   3778  O   TYR D1298      27.559  11.100  20.236  1.00 16.77           O  
ANISOU 3778  O   TYR D1298     2464   1786   2118    -39    340    -61       O  
ATOM   3779  CB  TYR D1298      25.780   9.211  21.833  1.00 16.08           C  
ANISOU 3779  CB  TYR D1298     2316   1829   1962   -113    260    -55       C  
ATOM   3780  CG  TYR D1298      25.176   8.923  23.172  1.00 15.90           C  
ANISOU 3780  CG  TYR D1298     2267   1865   1909   -158    241    -63       C  
ATOM   3781  CD1 TYR D1298      25.491   7.723  23.852  1.00 16.69           C  
ANISOU 3781  CD1 TYR D1298     2373   1967   1999   -218    203    -48       C  
ATOM   3782  CD2 TYR D1298      24.286   9.814  23.775  1.00 16.67           C  
ANISOU 3782  CD2 TYR D1298     2337   2016   1980   -141    258    -85       C  
ATOM   3783  CE1 TYR D1298      24.990   7.478  25.090  1.00 16.84           C  
ANISOU 3783  CE1 TYR D1298     2374   2041   1984   -265    189    -50       C  
ATOM   3784  CE2 TYR D1298      23.778   9.575  25.034  1.00 17.07           C  
ANISOU 3784  CE2 TYR D1298     2357   2131   1997   -187    243    -96       C  
ATOM   3785  CZ  TYR D1298      24.089   8.430  25.688  1.00 17.03           C  
ANISOU 3785  CZ  TYR D1298     2358   2130   1980   -253    212    -76       C  
ATOM   3786  OH  TYR D1298      23.571   8.293  26.981  1.00 18.32           O  
ANISOU 3786  OH  TYR D1298     2495   2362   2103   -302    202    -84       O  
ATOM   3787  N   ARG D1299      28.657   9.164  20.242  1.00 15.89           N  
ANISOU 3787  N   ARG D1299     2342   1670   2022    -93    284    -56       N  
ATOM   3788  CA  ARG D1299      29.122   9.274  18.861  1.00 16.23           C  
ANISOU 3788  CA  ARG D1299     2404   1683   2078    -63    304    -49       C  
ATOM   3789  C   ARG D1299      28.334   8.314  17.997  1.00 17.03           C  
ANISOU 3789  C   ARG D1299     2503   1812   2156    -51    274    -30       C  
ATOM   3790  O   ARG D1299      28.185   7.147  18.353  1.00 16.95           O  
ANISOU 3790  O   ARG D1299     2485   1817   2137    -81    230    -27       O  
ATOM   3791  CB  ARG D1299      30.660   9.069  18.737  1.00 15.95           C  
ANISOU 3791  CB  ARG D1299     2369   1614   2074    -80    307    -70       C  
ATOM   3792  CG  ARG D1299      31.201   9.200  17.337  1.00 16.22           C  
ANISOU 3792  CG  ARG D1299     2418   1628   2117    -57    331    -67       C  
ATOM   3793  CD  ARG D1299      32.695   9.036  17.288  1.00 17.33           C  
ANISOU 3793  CD  ARG D1299     2547   1756   2282    -77    335   -100       C  
ATOM   3794  NE  ARG D1299      33.041   7.624  17.471  1.00 17.53           N  
ANISOU 3794  NE  ARG D1299     2555   1796   2307    -80    274   -110       N  
ATOM   3795  CZ  ARG D1299      33.717   7.156  18.533  1.00 17.54           C  
ANISOU 3795  CZ  ARG D1299     2542   1804   2316    -97    242   -135       C  
ATOM   3796  NH1 ARG D1299      34.153   7.947  19.478  1.00 18.25           N  
ANISOU 3796  NH1 ARG D1299     2620   1897   2416   -118    266   -157       N  
ATOM   3797  NH2 ARG D1299      33.962   5.859  18.603  1.00 18.12           N  
ANISOU 3797  NH2 ARG D1299     2618   1881   2386    -88    183   -138       N  
ATOM   3798  N   ILE D1300      27.961   8.743  16.803  1.00 18.03           N  
ANISOU 3798  N   ILE D1300     2640   1938   2269     -8    297    -18       N  
ATOM   3799  CA  ILE D1300      27.224   7.887  15.895  1.00 18.00           C  
ANISOU 3799  CA  ILE D1300     2628   1969   2241      6    272     -9       C  
ATOM   3800  C   ILE D1300      28.113   7.712  14.678  1.00 17.96           C  
ANISOU 3800  C   ILE D1300     2636   1937   2251     25    282     -8       C  
ATOM   3801  O   ILE D1300      28.467   8.710  14.024  1.00 17.98           O  
ANISOU 3801  O   ILE D1300     2659   1915   2255     56    325      0       O  
ATOM   3802  CB  ILE D1300      25.852   8.501  15.445  1.00 18.74           C  
ANISOU 3802  CB  ILE D1300     2714   2111   2293     52    286     -2       C  
ATOM   3803  CG1 ILE D1300      24.876   8.765  16.633  1.00 19.20           C  
ANISOU 3803  CG1 ILE D1300     2750   2215   2329     37    278    -12       C  
ATOM   3804  CG2 ILE D1300      25.265   7.655  14.298  1.00 19.46           C  
ANISOU 3804  CG2 ILE D1300     2792   2243   2360     70    264      0       C  
ATOM   3805  CD1 ILE D1300      24.392  10.205  16.718  1.00 19.86           C  
ANISOU 3805  CD1 ILE D1300     2845   2299   2398     94    313    -15       C  
ATOM   3806  N   THR D1301      28.491   6.476  14.367  1.00 17.07           N  
ANISOU 3806  N   THR D1301     2514   1825   2146      7    243    -17       N  
ATOM   3807  CA  THR D1301      29.314   6.223  13.189  1.00 17.81           C  
ANISOU 3807  CA  THR D1301     2611   1907   2249     28    248    -25       C  
ATOM   3808  C   THR D1301      28.506   5.339  12.254  1.00 17.74           C  
ANISOU 3808  C   THR D1301     2591   1933   2215     45    220    -24       C  
ATOM   3809  O   THR D1301      27.924   4.325  12.680  1.00 18.71           O  
ANISOU 3809  O   THR D1301     2706   2069   2331     15    179    -30       O  
ATOM   3810  CB  THR D1301      30.623   5.527  13.587  1.00 18.03           C  
ANISOU 3810  CB  THR D1301     2634   1907   2307      4    222    -51       C  
ATOM   3811  OG1 THR D1301      31.253   6.340  14.545  1.00 17.49           O  
ANISOU 3811  OG1 THR D1301     2568   1819   2257    -14    248    -59       O  
ATOM   3812  CG2 THR D1301      31.578   5.261  12.423  1.00 18.80           C  
ANISOU 3812  CG2 THR D1301     2725   2005   2412     25    227    -71       C  
ATOM   3813  N   VAL D1302      28.492   5.712  10.993  1.00 18.70           N  
ANISOU 3813  N   VAL D1302     2713   2071   2321     86    245    -19       N  
ATOM   3814  CA  VAL D1302      27.788   4.964   9.945  1.00 19.22           C  
ANISOU 3814  CA  VAL D1302     2761   2179   2359    108    223    -25       C  
ATOM   3815  C   VAL D1302      28.810   4.531   8.906  1.00 19.74           C  
ANISOU 3815  C   VAL D1302     2824   2240   2437    123    221    -42       C  
ATOM   3816  O   VAL D1302      29.549   5.366   8.340  1.00 20.10           O  
ANISOU 3816  O   VAL D1302     2880   2274   2481    142    263    -34       O  
ATOM   3817  CB  VAL D1302      26.661   5.798   9.280  1.00 20.77           C  
ANISOU 3817  CB  VAL D1302     2956   2423   2511    160    250     -6       C  
ATOM   3818  CG1 VAL D1302      26.054   4.977   8.125  1.00 21.77           C  
ANISOU 3818  CG1 VAL D1302     3056   2605   2607    183    227    -22       C  
ATOM   3819  CG2 VAL D1302      25.622   6.188  10.303  1.00 20.32           C  
ANISOU 3819  CG2 VAL D1302     2893   2389   2439    150    248     -1       C  
ATOM   3820  N   VAL D1303      28.800   3.237   8.603  1.00 19.83           N  
ANISOU 3820  N   VAL D1303     2821   2259   2452    112    174    -68       N  
ATOM   3821  CA  VAL D1303      29.678   2.621   7.633  1.00 20.40           C  
ANISOU 3821  CA  VAL D1303     2882   2335   2532    130    160    -97       C  
ATOM   3822  C   VAL D1303      28.770   1.878   6.644  1.00 20.01           C  
ANISOU 3822  C   VAL D1303     2813   2332   2455    148    137   -111       C  
ATOM   3823  O   VAL D1303      27.849   1.150   7.090  1.00 20.45           O  
ANISOU 3823  O   VAL D1303     2869   2395   2506    120    105   -117       O  
ATOM   3824  CB  VAL D1303      30.667   1.599   8.322  1.00 20.93           C  
ANISOU 3824  CB  VAL D1303     2956   2359   2637    104    113   -128       C  
ATOM   3825  CG1 VAL D1303      31.546   0.874   7.279  1.00 21.50           C  
ANISOU 3825  CG1 VAL D1303     3010   2444   2714    132     91   -170       C  
ATOM   3826  CG2 VAL D1303      31.539   2.312   9.389  1.00 20.52           C  
ANISOU 3826  CG2 VAL D1303     2913   2274   2608     85    133   -123       C  
ATOM   3827  N   ALA D1304      28.975   2.062   5.338  1.00 18.24           N  
ANISOU 3827  N   ALA D1304     2573   2147   2208    190    156   -118       N  
ATOM   3828  CA  ALA D1304      28.389   1.168   4.333  1.00 18.73           C  
ANISOU 3828  CA  ALA D1304     2610   2257   2249    207    127   -147       C  
ATOM   3829  C   ALA D1304      29.102  -0.139   4.417  1.00 18.70           C  
ANISOU 3829  C   ALA D1304     2606   2220   2279    187     75   -192       C  
ATOM   3830  O   ALA D1304      30.323  -0.262   4.189  1.00 20.17           O  
ANISOU 3830  O   ALA D1304     2788   2389   2483    200     72   -214       O  
ATOM   3831  CB  ALA D1304      28.513   1.736   2.942  1.00 19.06           C  
ANISOU 3831  CB  ALA D1304     2635   2353   2252    260    161   -143       C  
ATOM   3832  N   ALA D1305      28.353  -1.178   4.682  1.00 19.08           N  
ANISOU 3832  N   ALA D1305     2658   2261   2330    157     32   -212       N  
ATOM   3833  CA  ALA D1305      28.967  -2.391   5.093  1.00 19.98           C  
ANISOU 3833  CA  ALA D1305     2795   2316   2478    135    -21   -246       C  
ATOM   3834  C   ALA D1305      29.907  -2.949   4.017  1.00 20.80           C  
ANISOU 3834  C   ALA D1305     2880   2433   2589    177    -41   -294       C  
ATOM   3835  O   ALA D1305      29.560  -3.037   2.795  1.00 21.46           O  
ANISOU 3835  O   ALA D1305     2930   2578   2646    207    -33   -316       O  
ATOM   3836  CB  ALA D1305      27.894  -3.420   5.458  1.00 20.67           C  
ANISOU 3836  CB  ALA D1305     2900   2390   2561     84    -58   -258       C  
ATOM   3837  N   GLY D1306      31.108  -3.269   4.470  1.00 21.05           N  
ANISOU 3837  N   GLY D1306     2926   2418   2651    186    -66   -314       N  
ATOM   3838  CA  GLY D1306      32.207  -3.688   3.599  1.00 21.97           C  
ANISOU 3838  CA  GLY D1306     3018   2556   2774    231    -84   -367       C  
ATOM   3839  C   GLY D1306      33.183  -2.556   3.319  1.00 23.41           C  
ANISOU 3839  C   GLY D1306     3169   2777   2946    251    -31   -360       C  
ATOM   3840  O   GLY D1306      34.300  -2.810   2.892  1.00 23.69           O  
ANISOU 3840  O   GLY D1306     3181   2833   2988    281    -44   -407       O  
ATOM   3841  N   GLU D1307      32.771  -1.318   3.536  1.00 23.83           N  
ANISOU 3841  N   GLU D1307     3225   2844   2982    235     27   -305       N  
ATOM   3842  CA  GLU D1307      33.709  -0.170   3.426  1.00 24.87           C  
ANISOU 3842  CA  GLU D1307     3343   2998   3107    236     84   -294       C  
ATOM   3843  C   GLU D1307      34.662  -0.172   4.625  1.00 23.93           C  
ANISOU 3843  C   GLU D1307     3235   2835   3022    217     69   -308       C  
ATOM   3844  O   GLU D1307      34.414  -0.736   5.662  1.00 22.91           O  
ANISOU 3844  O   GLU D1307     3134   2655   2916    201     28   -303       O  
ATOM   3845  CB  GLU D1307      32.985   1.189   3.383  1.00 26.17           C  
ANISOU 3845  CB  GLU D1307     3524   3174   3245    227    150   -231       C  
ATOM   3846  CG  GLU D1307      32.746   1.723   2.014  1.00 29.29           C  
ANISOU 3846  CG  GLU D1307     3904   3629   3595    258    190   -218       C  
ATOM   3847  CD  GLU D1307      33.963   2.461   1.498  1.00 30.62           C  
ANISOU 3847  CD  GLU D1307     4061   3821   3750    253    239   -225       C  
ATOM   3848  OE1 GLU D1307      33.836   3.175   0.487  1.00 33.80           O  
ANISOU 3848  OE1 GLU D1307     4467   4266   4109    270    286   -199       O  
ATOM   3849  OE2 GLU D1307      35.067   2.333   2.100  1.00 33.86           O  
ANISOU 3849  OE2 GLU D1307     4460   4215   4190    230    232   -260       O  
ATOM   3850  N   GLY D1308      35.788   0.491   4.439  1.00 24.62           N  
ANISOU 3850  N   GLY D1308     3298   2950   3105    215    107   -327       N  
ATOM   3851  CA  GLY D1308      36.814   0.526   5.459  1.00 24.90           C  
ANISOU 3851  CA  GLY D1308     3329   2965   3166    202     95   -355       C  
ATOM   3852  C   GLY D1308      36.864   1.793   6.243  1.00 24.50           C  
ANISOU 3852  C   GLY D1308     3293   2896   3118    161    153   -316       C  
ATOM   3853  O   GLY D1308      37.638   1.883   7.190  1.00 26.21           O  
ANISOU 3853  O   GLY D1308     3503   3100   3353    146    145   -339       O  
ATOM   3854  N   ILE D1309      36.108   2.797   5.783  1.00 23.46           N  
ANISOU 3854  N   ILE D1309     3180   2768   2965    148    211   -262       N  
ATOM   3855  CA  ILE D1309      36.033   4.143   6.387  1.00 22.24           C  
ANISOU 3855  CA  ILE D1309     3051   2588   2810    113    273   -221       C  
ATOM   3856  C   ILE D1309      34.521   4.427   6.576  1.00 21.24           C  
ANISOU 3856  C   ILE D1309     2960   2436   2673    122    275   -163       C  
ATOM   3857  O   ILE D1309      33.730   3.998   5.747  1.00 21.15           O  
ANISOU 3857  O   ILE D1309     2947   2449   2639    152    260   -153       O  
ATOM   3858  CB  ILE D1309      36.680   5.192   5.476  1.00 22.58           C  
ANISOU 3858  CB  ILE D1309     3091   2662   2826     96    346   -217       C  
ATOM   3859  CG1 ILE D1309      38.206   5.206   5.631  1.00 23.00           C  
ANISOU 3859  CG1 ILE D1309     3103   2746   2888     67    358   -280       C  
ATOM   3860  CG2 ILE D1309      36.256   6.635   5.818  1.00 21.82           C  
ANISOU 3860  CG2 ILE D1309     3043   2524   2722     69    413   -162       C  
ATOM   3861  CD1 ILE D1309      38.873   6.235   4.804  1.00 23.64           C  
ANISOU 3861  CD1 ILE D1309     3184   2859   2939     31    437   -278       C  
ATOM   3862  N   PRO D1310      34.116   5.104   7.645  1.00 19.87           N  
ANISOU 3862  N   PRO D1310     2811   2224   2511    100    291   -134       N  
ATOM   3863  CA  PRO D1310      32.717   5.488   7.710  1.00 19.62           C  
ANISOU 3863  CA  PRO D1310     2804   2187   2461    115    298    -88       C  
ATOM   3864  C   PRO D1310      32.345   6.539   6.645  1.00 20.67           C  
ANISOU 3864  C   PRO D1310     2961   2335   2557    142    354    -52       C  
ATOM   3865  O   PRO D1310      33.220   7.246   6.176  1.00 21.97           O  
ANISOU 3865  O   PRO D1310     3135   2496   2714    129    402    -53       O  
ATOM   3866  CB  PRO D1310      32.581   6.090   9.132  1.00 19.37           C  
ANISOU 3866  CB  PRO D1310     2790   2117   2450     85    307    -75       C  
ATOM   3867  CG  PRO D1310      33.769   5.617   9.847  1.00 19.03           C  
ANISOU 3867  CG  PRO D1310     2729   2064   2438     58    285   -117       C  
ATOM   3868  CD  PRO D1310      34.848   5.613   8.833  1.00 19.17           C  
ANISOU 3868  CD  PRO D1310     2725   2108   2449     63    305   -148       C  
ATOM   3869  N   ILE D1311      31.054   6.613   6.352  1.00 22.24           N  
ANISOU 3869  N   ILE D1311     3170   2553   2727    177    347    -24       N  
ATOM   3870  CA  ILE D1311      30.460   7.596   5.410  1.00 22.53           C  
ANISOU 3870  CA  ILE D1311     3238   2604   2718    222    391     15       C  
ATOM   3871  C   ILE D1311      30.073   8.816   6.223  1.00 22.36           C  
ANISOU 3871  C   ILE D1311     3260   2536   2697    222    426     47       C  
ATOM   3872  O   ILE D1311      30.130   9.932   5.746  1.00 23.83           O  
ANISOU 3872  O   ILE D1311     3495   2700   2860    243    476     81       O  
ATOM   3873  CB  ILE D1311      29.185   7.059   4.639  1.00 24.42           C  
ANISOU 3873  CB  ILE D1311     3458   2903   2917    274    360     20       C  
ATOM   3874  CG1 ILE D1311      28.716   8.051   3.574  1.00 24.68           C  
ANISOU 3874  CG1 ILE D1311     3525   2956   2894    334    402     60       C  
ATOM   3875  CG2 ILE D1311      28.012   6.682   5.550  1.00 23.67           C  
ANISOU 3875  CG2 ILE D1311     3348   2821   2825    271    323     15       C  
ATOM   3876  CD1 ILE D1311      27.936   7.481   2.416  1.00 24.89           C  
ANISOU 3876  CD1 ILE D1311     3524   3059   2874    387    378     53       C  
ATOM   3877  N   PHE D1312      29.643   8.571   7.454  1.00 22.04           N  
ANISOU 3877  N   PHE D1312     3207   2483   2682    201    397     37       N  
ATOM   3878  CA  PHE D1312      29.068   9.619   8.276  1.00 22.21           C  
ANISOU 3878  CA  PHE D1312     3261   2475   2703    209    421     58       C  
ATOM   3879  C   PHE D1312      29.465   9.426   9.714  1.00 20.37           C  
ANISOU 3879  C   PHE D1312     3013   2214   2511    156    405     36       C  
ATOM   3880  O   PHE D1312      29.556   8.301  10.190  1.00 19.93           O  
ANISOU 3880  O   PHE D1312     2921   2176   2473    128    358     12       O  
ATOM   3881  CB  PHE D1312      27.546   9.666   8.148  1.00 25.68           C  
ANISOU 3881  CB  PHE D1312     3694   2960   3101    264    400     71       C  
ATOM   3882  CG  PHE D1312      27.045  10.344   6.882  1.00 27.85           C  
ANISOU 3882  CG  PHE D1312     4001   3254   3323    337    426    101       C  
ATOM   3883  CD1 PHE D1312      27.545  11.560   6.485  1.00 29.94           C  
ANISOU 3883  CD1 PHE D1312     4332   3464   3577    355    480    135       C  
ATOM   3884  CD2 PHE D1312      26.021   9.790   6.129  1.00 30.34           C  
ANISOU 3884  CD2 PHE D1312     4285   3644   3595    386    396     96       C  
ATOM   3885  CE1 PHE D1312      27.093  12.203   5.338  1.00 31.43           C  
ANISOU 3885  CE1 PHE D1312     4564   3666   3711    426    502    170       C  
ATOM   3886  CE2 PHE D1312      25.544  10.409   4.977  1.00 31.84           C  
ANISOU 3886  CE2 PHE D1312     4505   3862   3730    463    416    123       C  
ATOM   3887  CZ  PHE D1312      26.070  11.629   4.584  1.00 32.90           C  
ANISOU 3887  CZ  PHE D1312     4714   3935   3851    488    468    165       C  
ATOM   3888  N   GLU D1313      29.648  10.534  10.420  1.00 18.94           N  
ANISOU 3888  N   GLU D1313     2863   1988   2341    146    442     44       N  
ATOM   3889  CA  GLU D1313      29.955  10.446  11.855  1.00 18.64           C  
ANISOU 3889  CA  GLU D1313     2808   1933   2338     99    427     21       C  
ATOM   3890  C   GLU D1313      29.539  11.729  12.519  1.00 19.60           C  
ANISOU 3890  C   GLU D1313     2965   2021   2458    111    462     32       C  
ATOM   3891  O   GLU D1313      29.761  12.796  11.947  1.00 20.60           O  
ANISOU 3891  O   GLU D1313     3144   2107   2576    129    511     51       O  
ATOM   3892  CB  GLU D1313      31.432  10.179  12.091  1.00 18.45           C  
ANISOU 3892  CB  GLU D1313     2769   1891   2348     49    434     -9       C  
ATOM   3893  CG  GLU D1313      31.811   9.862  13.542  1.00 18.71           C  
ANISOU 3893  CG  GLU D1313     2778   1919   2410      8    408    -37       C  
ATOM   3894  CD  GLU D1313      33.212   9.197  13.589  1.00 18.85           C  
ANISOU 3894  CD  GLU D1313     2767   1943   2451    -22    394    -76       C  
ATOM   3895  OE1 GLU D1313      34.269   9.901  13.582  1.00 19.57           O  
ANISOU 3895  OE1 GLU D1313     2860   2020   2556    -51    437   -100       O  
ATOM   3896  OE2 GLU D1313      33.282   7.980  13.436  1.00 19.69           O  
ANISOU 3896  OE2 GLU D1313     2850   2071   2557    -15    343    -88       O  
ATOM   3897  N   ASP D1314      28.990  11.605  13.700  1.00 18.82           N  
ANISOU 3897  N   ASP D1314     2846   1938   2367     99    437     19       N  
ATOM   3898  CA  ASP D1314      28.452  12.787  14.413  1.00 20.02           C  
ANISOU 3898  CA  ASP D1314     3025   2066   2514    118    462     20       C  
ATOM   3899  C   ASP D1314      28.454  12.566  15.911  1.00 20.01           C  
ANISOU 3899  C   ASP D1314     2990   2080   2533     76    440     -6       C  
ATOM   3900  O   ASP D1314      28.621  11.447  16.411  1.00 19.20           O  
ANISOU 3900  O   ASP D1314     2847   2008   2437     39    399    -17       O  
ATOM   3901  CB  ASP D1314      27.028  13.032  13.972  1.00 20.99           C  
ANISOU 3901  CB  ASP D1314     3154   2228   2593    189    451     38       C  
ATOM   3902  CG  ASP D1314      26.670  14.515  13.887  1.00 23.30           C  
ANISOU 3902  CG  ASP D1314     3508   2474   2871    244    490     50       C  
ATOM   3903  OD1 ASP D1314      27.255  15.359  14.606  1.00 23.83           O  
ANISOU 3903  OD1 ASP D1314     3604   2482   2966    217    521     38       O  
ATOM   3904  OD2 ASP D1314      25.843  14.788  13.009  1.00 25.92           O  
ANISOU 3904  OD2 ASP D1314     3861   2826   3160    316    489     71       O  
ATOM   3905  N   PHE D1315      28.219  13.651  16.612  1.00 20.27           N  
ANISOU 3905  N   PHE D1315     3044   2087   2569     87    465    -15       N  
ATOM   3906  CA  PHE D1315      28.128  13.651  18.069  1.00 20.00           C  
ANISOU 3906  CA  PHE D1315     2978   2073   2547     54    449    -43       C  
ATOM   3907  C   PHE D1315      26.838  14.290  18.521  1.00 20.53           C  
ANISOU 3907  C   PHE D1315     3044   2170   2584    102    445    -47       C  
ATOM   3908  O   PHE D1315      26.385  15.307  17.935  1.00 20.16           O  
ANISOU 3908  O   PHE D1315     3044   2092   2522    163    472    -37       O  
ATOM   3909  CB  PHE D1315      29.310  14.415  18.651  1.00 21.23           C  
ANISOU 3909  CB  PHE D1315     3151   2174   2741     12    487    -69       C  
ATOM   3910  CG  PHE D1315      29.122  14.809  20.082  1.00 21.61           C  
ANISOU 3910  CG  PHE D1315     3176   2237   2796     -6    481   -101       C  
ATOM   3911  CD1 PHE D1315      29.427  13.918  21.125  1.00 22.02           C  
ANISOU 3911  CD1 PHE D1315     3178   2334   2853    -51    444   -119       C  
ATOM   3912  CD2 PHE D1315      28.658  16.065  20.411  1.00 22.32           C  
ANISOU 3912  CD2 PHE D1315     3299   2296   2885     24    511   -113       C  
ATOM   3913  CE1 PHE D1315      29.241  14.274  22.426  1.00 21.68           C  
ANISOU 3913  CE1 PHE D1315     3111   2315   2810    -68    439   -148       C  
ATOM   3914  CE2 PHE D1315      28.492  16.428  21.740  1.00 22.73           C  
ANISOU 3914  CE2 PHE D1315     3324   2369   2942      8    506   -150       C  
ATOM   3915  CZ  PHE D1315      28.796  15.557  22.745  1.00 23.10           C  
ANISOU 3915  CZ  PHE D1315     3314   2471   2991    -40    472   -167       C  
ATOM   3916  N   VAL D1316      26.276  13.746  19.587  1.00 20.07           N  
ANISOU 3916  N   VAL D1316     2938   2173   2513     76    411    -65       N  
ATOM   3917  CA  VAL D1316      25.149  14.329  20.315  1.00 20.34           C  
ANISOU 3917  CA  VAL D1316     2954   2255   2518    110    405    -85       C  
ATOM   3918  C   VAL D1316      25.382  14.296  21.802  1.00 20.86           C  
ANISOU 3918  C   VAL D1316     2985   2344   2595     59    396   -115       C  
ATOM   3919  O   VAL D1316      25.975  13.345  22.313  1.00 21.53           O  
ANISOU 3919  O   VAL D1316     3045   2442   2690     -1    373   -113       O  
ATOM   3920  CB  VAL D1316      23.805  13.680  20.004  1.00 20.17           C  
ANISOU 3920  CB  VAL D1316     2894   2323   2446    137    373    -82       C  
ATOM   3921  CG1 VAL D1316      23.537  13.838  18.531  1.00 20.07           C  
ANISOU 3921  CG1 VAL D1316     2914   2294   2416    200    382    -57       C  
ATOM   3922  CG2 VAL D1316      23.752  12.205  20.375  1.00 19.62           C  
ANISOU 3922  CG2 VAL D1316     2781   2305   2367     67    334    -76       C  
ATOM   3923  N   ASP D1317      24.899  15.329  22.511  1.00 22.35           N  
ANISOU 3923  N   ASP D1317     3175   2539   2776     89    410   -145       N  
ATOM   3924  CA  ASP D1317      25.053  15.403  23.968  1.00 23.24           C  
ANISOU 3924  CA  ASP D1317     3250   2685   2894     46    403   -180       C  
ATOM   3925  C   ASP D1317      24.300  14.259  24.692  1.00 21.62           C  
ANISOU 3925  C   ASP D1317     2984   2581   2647      3    360   -178       C  
ATOM   3926  O   ASP D1317      23.518  13.559  24.105  1.00 21.10           O  
ANISOU 3926  O   ASP D1317     2904   2562   2549     10    340   -159       O  
ATOM   3927  CB  ASP D1317      24.558  16.734  24.483  1.00 26.78           C  
ANISOU 3927  CB  ASP D1317     3710   3125   3338     96    424   -218       C  
ATOM   3928  CG  ASP D1317      23.048  16.894  24.367  1.00 28.75           C  
ANISOU 3928  CG  ASP D1317     3935   3455   3534    161    404   -230       C  
ATOM   3929  OD1 ASP D1317      22.325  15.914  24.602  1.00 30.17           O  
ANISOU 3929  OD1 ASP D1317     4059   3729   3675    133    372   -226       O  
ATOM   3930  OD2 ASP D1317      22.564  18.019  24.071  1.00 30.70           O  
ANISOU 3930  OD2 ASP D1317     4219   3672   3774    241    420   -247       O  
ATOM   3931  N   SER D1318      24.603  14.108  25.975  1.00 21.39           N  
ANISOU 3931  N   SER D1318     2924   2583   2619    -45    351   -199       N  
ATOM   3932  CA  SER D1318      24.068  13.048  26.816  1.00 20.98           C  
ANISOU 3932  CA  SER D1318     2827   2617   2525   -101    315   -194       C  
ATOM   3933  C   SER D1318      22.550  13.095  27.095  1.00 21.84           C  
ANISOU 3933  C   SER D1318     2891   2830   2575    -86    304   -213       C  
ATOM   3934  O   SER D1318      21.960  12.093  27.476  1.00 22.72           O  
ANISOU 3934  O   SER D1318     2972   3015   2645   -141    279   -201       O  
ATOM   3935  CB  SER D1318      24.786  13.080  28.155  1.00 21.59           C  
ANISOU 3935  CB  SER D1318     2886   2705   2612   -147    311   -215       C  
ATOM   3936  OG  SER D1318      24.449  14.256  28.868  1.00 23.99           O  
ANISOU 3936  OG  SER D1318     3170   3031   2912   -117    332   -262       O  
ATOM   3937  N   SER D1319      21.945  14.268  26.912  1.00 22.15           N  
ANISOU 3937  N   SER D1319     2930   2877   2609    -13    323   -246       N  
ATOM   3938  CA  SER D1319      20.472  14.414  26.979  1.00 23.52           C  
ANISOU 3938  CA  SER D1319     3055   3159   2721     21    312   -276       C  
ATOM   3939  C   SER D1319      19.725  13.943  25.731  1.00 24.82           C  
ANISOU 3939  C   SER D1319     3221   3350   2859     55    302   -256       C  
ATOM   3940  O   SER D1319      18.467  14.020  25.697  1.00 26.16           O  
ANISOU 3940  O   SER D1319     3341   3625   2971     87    292   -289       O  
ATOM   3941  CB  SER D1319      20.143  15.885  27.204  1.00 24.48           C  
ANISOU 3941  CB  SER D1319     3183   3272   2845    106    330   -324       C  
ATOM   3942  OG  SER D1319      20.019  16.511  25.977  1.00 23.86           O  
ANISOU 3942  OG  SER D1319     3156   3131   2778    192    343   -312       O  
ATOM   3943  N   VAL D1320      20.437  13.430  24.732  1.00 25.35           N  
ANISOU 3943  N   VAL D1320     3333   3339   2959     47    305   -212       N  
ATOM   3944  CA  VAL D1320      19.842  12.985  23.463  1.00 26.34           C  
ANISOU 3944  CA  VAL D1320     3461   3485   3062     80    296   -195       C  
ATOM   3945  C   VAL D1320      19.687  11.452  23.311  1.00 26.81           C  
ANISOU 3945  C   VAL D1320     3498   3585   3103     -2    271   -171       C  
ATOM   3946  O   VAL D1320      20.622  10.697  23.601  1.00 27.10           O  
ANISOU 3946  O   VAL D1320     3558   3565   3170    -68    263   -143       O  
ATOM   3947  CB  VAL D1320      20.655  13.525  22.274  1.00 25.97           C  
ANISOU 3947  CB  VAL D1320     3482   3327   3058    138    318   -166       C  
ATOM   3948  CG1 VAL D1320      20.048  13.127  20.950  1.00 26.11           C  
ANISOU 3948  CG1 VAL D1320     3499   3371   3047    181    310   -151       C  
ATOM   3949  CG2 VAL D1320      20.743  15.047  22.308  1.00 27.02           C  
ANISOU 3949  CG2 VAL D1320     3655   3405   3206    219    346   -186       C  
ATOM   3950  N   GLY D1321      18.510  11.027  22.828  1.00 26.13           N  
ANISOU 3950  N   GLY D1321     3370   3595   2963      4    258   -188       N  
ATOM   3951  CA  GLY D1321      18.170   9.620  22.559  1.00 26.75           C  
ANISOU 3951  CA  GLY D1321     3430   3715   3017    -74    237   -174       C  
ATOM   3952  C   GLY D1321      17.576   9.397  21.165  1.00 26.96           C  
ANISOU 3952  C   GLY D1321     3448   3770   3022    -25    233   -177       C  
ATOM   3953  O   GLY D1321      17.077   8.300  20.870  1.00 26.93           O  
ANISOU 3953  O   GLY D1321     3422   3818   2992    -88    218   -179       O  
ATOM   3954  N   TYR D1322      17.623  10.416  20.294  1.00 28.57           N  
ANISOU 3954  N   TYR D1322     3677   3941   3236     83    248   -179       N  
ATOM   3955  CA  TYR D1322      17.170  10.323  18.893  1.00 30.49           C  
ANISOU 3955  CA  TYR D1322     3919   4208   3458    146    245   -179       C  
ATOM   3956  C   TYR D1322      18.314  10.776  18.008  1.00 30.33           C  
ANISOU 3956  C   TYR D1322     3971   4061   3490    196    262   -137       C  
ATOM   3957  O   TYR D1322      19.163  11.526  18.489  1.00 30.30           O  
ANISOU 3957  O   TYR D1322     4010   3973   3528    205    281   -123       O  
ATOM   3958  CB  TYR D1322      16.031  11.303  18.572  1.00 34.80           C  
ANISOU 3958  CB  TYR D1322     4432   4843   3948    255    245   -221       C  
ATOM   3959  CG  TYR D1322      15.023  11.629  19.627  1.00 38.54           C  
ANISOU 3959  CG  TYR D1322     4839   5432   4371    252    239   -276       C  
ATOM   3960  CD1 TYR D1322      13.872  10.843  19.787  1.00 40.32           C  
ANISOU 3960  CD1 TYR D1322     4982   5805   4532    199    223   -321       C  
ATOM   3961  CD2 TYR D1322      15.156  12.787  20.419  1.00 40.32           C  
ANISOU 3961  CD2 TYR D1322     5081   5630   4608    305    250   -292       C  
ATOM   3962  CE1 TYR D1322      12.912  11.166  20.730  1.00 40.74           C  
ANISOU 3962  CE1 TYR D1322     4964   5983   4529    195    219   -379       C  
ATOM   3963  CE2 TYR D1322      14.192  13.115  21.373  1.00 42.10           C  
ANISOU 3963  CE2 TYR D1322     5238   5976   4782    309    242   -351       C  
ATOM   3964  CZ  TYR D1322      13.087  12.300  21.516  1.00 41.59           C  
ANISOU 3964  CZ  TYR D1322     5086   6064   4650    255    226   -394       C  
ATOM   3965  OH  TYR D1322      12.159  12.614  22.444  1.00 43.92           O  
ANISOU 3965  OH  TYR D1322     5308   6490   4889    255    221   -457       O  
ATOM   3966  N   TYR D1323      18.335  10.288  16.762  1.00 28.99           N  
ANISOU 3966  N   TYR D1323     3811   3887   3315    218    257   -122       N  
ATOM   3967  CA  TYR D1323      19.215  10.824  15.701  1.00 27.93           C  
ANISOU 3967  CA  TYR D1323     3740   3659   3213    278    277    -87       C  
ATOM   3968  C   TYR D1323      18.749  10.359  14.344  1.00 28.07           C  
ANISOU 3968  C   TYR D1323     3745   3723   3197    320    267    -86       C  
ATOM   3969  O   TYR D1323      18.561   9.169  14.156  1.00 29.34           O  
ANISOU 3969  O   TYR D1323     3870   3923   3351    256    245    -96       O  
ATOM   3970  CB  TYR D1323      20.658  10.381  15.869  1.00 27.05           C  
ANISOU 3970  CB  TYR D1323     3668   3443   3164    212    284    -56       C  
ATOM   3971  CG  TYR D1323      21.606  11.027  14.888  1.00 27.49           C  
ANISOU 3971  CG  TYR D1323     3784   3411   3248    261    312    -25       C  
ATOM   3972  CD1 TYR D1323      22.208  12.250  15.170  1.00 27.50           C  
ANISOU 3972  CD1 TYR D1323     3837   3337   3274    292    345    -15       C  
ATOM   3973  CD2 TYR D1323      21.907  10.429  13.664  1.00 28.71           C  
ANISOU 3973  CD2 TYR D1323     3947   3559   3402    270    308     -9       C  
ATOM   3974  CE1 TYR D1323      23.095  12.840  14.260  1.00 29.05           C  
ANISOU 3974  CE1 TYR D1323     4093   3453   3490    321    378     13       C  
ATOM   3975  CE2 TYR D1323      22.778  11.020  12.757  1.00 28.78           C  
ANISOU 3975  CE2 TYR D1323     4009   3497   3428    307    338     18       C  
ATOM   3976  CZ  TYR D1323      23.376  12.232  13.059  1.00 29.56           C  
ANISOU 3976  CZ  TYR D1323     4162   3520   3548    328    375     32       C  
ATOM   3977  OH  TYR D1323      24.269  12.829  12.178  1.00 29.37           O  
ANISOU 3977  OH  TYR D1323     4195   3424   3536    348    411     60       O  
ATOM   3978  N   THR D1324      18.605  11.280  13.403  1.00 28.50           N  
ANISOU 3978  N   THR D1324     3833   3765   3230    425    282    -74       N  
ATOM   3979  CA  THR D1324      18.207  10.932  12.044  1.00 27.64           C  
ANISOU 3979  CA  THR D1324     3714   3704   3084    476    273    -73       C  
ATOM   3980  C   THR D1324      19.428  10.796  11.133  1.00 27.44           C  
ANISOU 3980  C   THR D1324     3744   3583   3098    469    290    -30       C  
ATOM   3981  O   THR D1324      20.141  11.767  10.950  1.00 28.30           O  
ANISOU 3981  O   THR D1324     3920   3605   3227    508    321      1       O  
ATOM   3982  CB  THR D1324      17.302  11.971  11.412  1.00 29.02           C  
ANISOU 3982  CB  THR D1324     3897   3931   3198    608    275    -83       C  
ATOM   3983  OG1 THR D1324      16.206  12.249  12.277  1.00 29.59           O  
ANISOU 3983  OG1 THR D1324     3915   4098   3230    628    259   -132       O  
ATOM   3984  CG2 THR D1324      16.760  11.399  10.056  1.00 28.77           C  
ANISOU 3984  CG2 THR D1324     3834   3978   3117    654    259    -92       C  
ATOM   3985  N   VAL D1325      19.682   9.598  10.602  1.00 27.76           N  
ANISOU 3985  N   VAL D1325     3758   3639   3148    414    273    -34       N  
ATOM   3986  CA  VAL D1325      20.737   9.406   9.626  1.00 27.14           C  
ANISOU 3986  CA  VAL D1325     3719   3496   3097    415    286     -4       C  
ATOM   3987  C   VAL D1325      20.091   9.637   8.265  1.00 29.41           C  
ANISOU 3987  C   VAL D1325     4002   3845   3327    506    286     -3       C  
ATOM   3988  O   VAL D1325      19.257   8.842   7.834  1.00 30.98           O  
ANISOU 3988  O   VAL D1325     4143   4139   3490    506    259    -37       O  
ATOM   3989  CB  VAL D1325      21.338   7.967   9.670  1.00 25.53           C  
ANISOU 3989  CB  VAL D1325     3490   3280   2930    322    262    -16       C  
ATOM   3990  CG1 VAL D1325      22.541   7.866   8.717  1.00 24.86           C  
ANISOU 3990  CG1 VAL D1325     3440   3131   2872    328    276      6       C  
ATOM   3991  CG2 VAL D1325      21.721   7.590  11.086  1.00 25.04           C  
ANISOU 3991  CG2 VAL D1325     3426   3179   2909    238    252    -21       C  
ATOM   3992  N   THR D1326      20.484  10.705   7.598  1.00 30.22           N  
ANISOU 3992  N   THR D1326     4167   3895   3417    581    316     33       N  
ATOM   3993  CA  THR D1326      19.985  11.048   6.267  1.00 31.30           C  
ANISOU 3993  CA  THR D1326     4316   4081   3492    679    319     44       C  
ATOM   3994  C   THR D1326      21.053  10.998   5.195  1.00 32.48           C  
ANISOU 3994  C   THR D1326     4509   4176   3654    677    342     80       C  
ATOM   3995  O   THR D1326      22.252  10.887   5.488  1.00 34.12           O  
ANISOU 3995  O   THR D1326     4744   4301   3918    605    362     96       O  
ATOM   3996  CB  THR D1326      19.440  12.478   6.302  1.00 32.56           C  
ANISOU 3996  CB  THR D1326     4532   4227   3612    786    335     64       C  
ATOM   3997  OG1 THR D1326      20.437  13.327   6.865  1.00 33.25           O  
ANISOU 3997  OG1 THR D1326     4695   4188   3747    757    372    100       O  
ATOM   3998  CG2 THR D1326      18.200  12.557   7.180  1.00 32.57           C  
ANISOU 3998  CG2 THR D1326     4475   4314   3582    811    307     16       C  
ATOM   3999  N   GLY D1327      20.615  11.093   3.942  1.00 32.83           N  
ANISOU 3999  N   GLY D1327     4555   4278   3639    757    340     88       N  
ATOM   4000  CA  GLY D1327      21.542  11.177   2.810  1.00 33.03           C  
ANISOU 4000  CA  GLY D1327     4624   4266   3660    766    366    125       C  
ATOM   4001  C   GLY D1327      22.181   9.839   2.498  1.00 32.06           C  
ANISOU 4001  C   GLY D1327     4446   4163   3572    685    349     96       C  
ATOM   4002  O   GLY D1327      23.257   9.772   1.850  1.00 31.53           O  
ANISOU 4002  O   GLY D1327     4405   4053   3520    661    372    116       O  
ATOM   4003  N   LEU D1328      21.499   8.775   2.886  1.00 29.98           N  
ANISOU 4003  N   LEU D1328     4108   3967   3315    647    308     45       N  
ATOM   4004  CA  LEU D1328      21.957   7.395   2.622  1.00 31.64           C  
ANISOU 4004  CA  LEU D1328     4270   4194   3557    576    282     10       C  
ATOM   4005  C   LEU D1328      21.483   6.967   1.246  1.00 33.88           C  
ANISOU 4005  C   LEU D1328     4519   4569   3785    632    269     -8       C  
ATOM   4006  O   LEU D1328      20.594   7.584   0.668  1.00 36.23           O  
ANISOU 4006  O   LEU D1328     4814   4934   4016    721    271     -3       O  
ATOM   4007  CB  LEU D1328      21.369   6.428   3.621  1.00 30.88           C  
ANISOU 4007  CB  LEU D1328     4122   4125   3486    503    246    -33       C  
ATOM   4008  CG  LEU D1328      21.771   6.627   5.094  1.00 29.97           C  
ANISOU 4008  CG  LEU D1328     4030   3934   3423    439    251    -22       C  
ATOM   4009  CD1 LEU D1328      20.856   5.781   5.964  1.00 30.06           C  
ANISOU 4009  CD1 LEU D1328     3990   3996   3432    379    218    -62       C  
ATOM   4010  CD2 LEU D1328      23.234   6.288   5.346  1.00 29.17           C  
ANISOU 4010  CD2 LEU D1328     3958   3741   3384    379    258    -10       C  
ATOM   4011  N   GLU D1329      22.104   5.903   0.757  1.00 34.42           N  
ANISOU 4011  N   GLU D1329     4559   4639   3880    584    252    -35       N  
ATOM   4012  CA  GLU D1329      21.813   5.323  -0.547  1.00 36.11           C  
ANISOU 4012  CA  GLU D1329     4731   4938   4048    623    238    -64       C  
ATOM   4013  C   GLU D1329      20.796   4.172  -0.403  1.00 34.34           C  
ANISOU 4013  C   GLU D1329     4434   4794   3817    587    195   -130       C  
ATOM   4014  O   GLU D1329      20.905   3.387   0.524  1.00 33.20           O  
ANISOU 4014  O   GLU D1329     4281   4609   3724    500    174   -154       O  
ATOM   4015  CB  GLU D1329      23.122   4.806  -1.143  1.00 37.00           C  
ANISOU 4015  CB  GLU D1329     4853   5007   4195    589    243    -65       C  
ATOM   4016  CG  GLU D1329      23.071   4.369  -2.589  1.00 40.01           C  
ANISOU 4016  CG  GLU D1329     5200   5470   4530    635    236    -89       C  
ATOM   4017  CD  GLU D1329      22.795   5.520  -3.525  1.00 39.58           C  
ANISOU 4017  CD  GLU D1329     5179   5457   4400    733    269    -41       C  
ATOM   4018  OE1 GLU D1329      21.974   6.425  -3.176  1.00 39.41           O  
ANISOU 4018  OE1 GLU D1329     5184   5445   4343    788    279    -13       O  
ATOM   4019  OE2 GLU D1329      23.369   5.499  -4.623  1.00 40.56           O  
ANISOU 4019  OE2 GLU D1329     5305   5609   4495    759    283    -35       O  
ATOM   4020  N   PRO D1330      19.810   4.073  -1.323  1.00 34.07           N  
ANISOU 4020  N   PRO D1330     4352   4877   3714    649    182   -162       N  
ATOM   4021  CA  PRO D1330      18.791   3.027  -1.156  1.00 32.48           C  
ANISOU 4021  CA  PRO D1330     4079   4759   3501    602    147   -233       C  
ATOM   4022  C   PRO D1330      19.318   1.623  -1.363  1.00 30.53           C  
ANISOU 4022  C   PRO D1330     3811   4488   3301    520    121   -279       C  
ATOM   4023  O   PRO D1330      20.148   1.406  -2.252  1.00 30.56           O  
ANISOU 4023  O   PRO D1330     3822   4474   3311    541    123   -276       O  
ATOM   4024  CB  PRO D1330      17.753   3.353  -2.235  1.00 35.26           C  
ANISOU 4024  CB  PRO D1330     4383   5250   3763    701    143   -260       C  
ATOM   4025  CG  PRO D1330      17.957   4.800  -2.555  1.00 35.83           C  
ANISOU 4025  CG  PRO D1330     4517   5300   3796    808    174   -191       C  
ATOM   4026  CD  PRO D1330      19.409   5.087  -2.313  1.00 35.57           C  
ANISOU 4026  CD  PRO D1330     4557   5130   3827    768    202   -133       C  
ATOM   4027  N   GLY D1331      18.860   0.697  -0.540  1.00 28.80           N  
ANISOU 4027  N   GLY D1331     3569   4262   3110    427     97   -320       N  
ATOM   4028  CA  GLY D1331      19.113  -0.720  -0.736  1.00 27.77           C  
ANISOU 4028  CA  GLY D1331     3423   4112   3015    351     65   -373       C  
ATOM   4029  C   GLY D1331      20.474  -1.148  -0.246  1.00 26.32           C  
ANISOU 4029  C   GLY D1331     3297   3795   2907    303     58   -348       C  
ATOM   4030  O   GLY D1331      20.887  -2.264  -0.519  1.00 26.52           O  
ANISOU 4030  O   GLY D1331     3323   3789   2964    260     29   -388       O  
ATOM   4031  N   ILE D1332      21.115  -0.312   0.583  1.00 26.07           N  
ANISOU 4031  N   ILE D1332     3314   3686   2904    307     80   -289       N  
ATOM   4032  CA  ILE D1332      22.457  -0.591   1.043  1.00 23.91           C  
ANISOU 4032  CA  ILE D1332     3088   3301   2694    274     73   -269       C  
ATOM   4033  C   ILE D1332      22.358  -0.907   2.506  1.00 22.92           C  
ANISOU 4033  C   ILE D1332     2992   3110   2606    196     60   -258       C  
ATOM   4034  O   ILE D1332      21.618  -0.217   3.226  1.00 22.64           O  
ANISOU 4034  O   ILE D1332     2952   3099   2549    192     78   -237       O  
ATOM   4035  CB  ILE D1332      23.359   0.660   0.839  1.00 24.03           C  
ANISOU 4035  CB  ILE D1332     3136   3283   2709    334    114   -213       C  
ATOM   4036  CG1 ILE D1332      23.520   0.973  -0.660  1.00 24.33           C  
ANISOU 4036  CG1 ILE D1332     3154   3387   2701    409    130   -216       C  
ATOM   4037  CG2 ILE D1332      24.758   0.461   1.452  1.00 22.90           C  
ANISOU 4037  CG2 ILE D1332     3033   3038   2628    297    110   -200       C  
ATOM   4038  CD1 ILE D1332      24.128  -0.151  -1.448  1.00 24.69           C  
ANISOU 4038  CD1 ILE D1332     3177   3438   2765    396    100   -267       C  
ATOM   4039  N   ASP D1333      23.088  -1.929   2.914  1.00 22.62           N  
ANISOU 4039  N   ASP D1333     2983   2993   2618    140     28   -275       N  
ATOM   4040  CA  ASP D1333      23.263  -2.222   4.364  1.00 21.85           C  
ANISOU 4040  CA  ASP D1333     2927   2815   2556     70     14   -255       C  
ATOM   4041  C   ASP D1333      24.242  -1.271   4.996  1.00 21.98           C  
ANISOU 4041  C   ASP D1333     2976   2775   2600     95     38   -208       C  
ATOM   4042  O   ASP D1333      25.402  -1.153   4.541  1.00 22.14           O  
ANISOU 4042  O   ASP D1333     3008   2760   2644    130     41   -206       O  
ATOM   4043  CB  ASP D1333      23.802  -3.622   4.603  1.00 22.58           C  
ANISOU 4043  CB  ASP D1333     3056   2831   2689     15    -32   -286       C  
ATOM   4044  CG  ASP D1333      22.865  -4.719   4.142  1.00 23.92           C  
ANISOU 4044  CG  ASP D1333     3208   3038   2840    -32    -58   -338       C  
ATOM   4045  OD1 ASP D1333      21.706  -4.455   3.843  1.00 25.02           O  
ANISOU 4045  OD1 ASP D1333     3300   3272   2933    -38    -40   -354       O  
ATOM   4046  OD2 ASP D1333      23.335  -5.889   4.023  1.00 26.44           O  
ANISOU 4046  OD2 ASP D1333     3561   3293   3190    -62    -98   -371       O  
ATOM   4047  N   TYR D1334      23.789  -0.632   6.080  1.00 22.22           N  
ANISOU 4047  N   TYR D1334     3016   2800   2626     71     55   -178       N  
ATOM   4048  CA  TYR D1334      24.634   0.249   6.854  1.00 21.79           C  
ANISOU 4048  CA  TYR D1334     2990   2690   2598     82     78   -140       C  
ATOM   4049  C   TYR D1334      24.918  -0.364   8.239  1.00 20.46           C  
ANISOU 4049  C   TYR D1334     2856   2455   2462     13     51   -133       C  
ATOM   4050  O   TYR D1334      23.998  -0.819   8.908  1.00 21.07           O  
ANISOU 4050  O   TYR D1334     2932   2551   2522    -42     38   -138       O  
ATOM   4051  CB  TYR D1334      24.007   1.621   6.949  1.00 22.22           C  
ANISOU 4051  CB  TYR D1334     3033   2788   2619    124    120   -111       C  
ATOM   4052  CG  TYR D1334      24.017   2.330   5.612  1.00 22.31           C  
ANISOU 4052  CG  TYR D1334     3031   2846   2598    202    147   -105       C  
ATOM   4053  CD1 TYR D1334      25.183   2.937   5.162  1.00 22.56           C  
ANISOU 4053  CD1 TYR D1334     3088   2835   2648    234    174    -85       C  
ATOM   4054  CD2 TYR D1334      22.899   2.382   4.803  1.00 23.58           C  
ANISOU 4054  CD2 TYR D1334     3155   3096   2706    242    148   -123       C  
ATOM   4055  CE1 TYR D1334      25.222   3.553   3.919  1.00 23.99           C  
ANISOU 4055  CE1 TYR D1334     3266   3055   2792    299    201    -74       C  
ATOM   4056  CE2 TYR D1334      22.937   2.998   3.565  1.00 24.67           C  
ANISOU 4056  CE2 TYR D1334     3288   3276   2807    319    170   -113       C  
ATOM   4057  CZ  TYR D1334      24.109   3.613   3.157  1.00 24.61           C  
ANISOU 4057  CZ  TYR D1334     3316   3217   2818    345    198    -83       C  
ATOM   4058  OH  TYR D1334      24.159   4.211   1.942  1.00 26.06           O  
ANISOU 4058  OH  TYR D1334     3502   3439   2958    415    223    -68       O  
ATOM   4059  N   ASP D1335      26.200  -0.364   8.618  1.00 20.50           N  
ANISOU 4059  N   ASP D1335     2889   2392   2505     18     44   -125       N  
ATOM   4060  CA  ASP D1335      26.654  -0.867   9.920  1.00 20.86           C  
ANISOU 4060  CA  ASP D1335     2972   2374   2578    -30     16   -116       C  
ATOM   4061  C   ASP D1335      26.664   0.396  10.754  1.00 19.66           C  
ANISOU 4061  C   ASP D1335     2817   2228   2424    -25     56    -86       C  
ATOM   4062  O   ASP D1335      27.484   1.291  10.501  1.00 19.60           O  
ANISOU 4062  O   ASP D1335     2805   2210   2429     14     86    -78       O  
ATOM   4063  CB  ASP D1335      28.076  -1.446   9.828  1.00 21.26           C  
ANISOU 4063  CB  ASP D1335     3046   2364   2665    -10    -12   -135       C  
ATOM   4064  CG  ASP D1335      28.127  -2.837   9.177  1.00 22.90           C  
ANISOU 4064  CG  ASP D1335     3270   2550   2880    -15    -62   -171       C  
ATOM   4065  OD1 ASP D1335      27.087  -3.514   9.028  1.00 24.59           O  
ANISOU 4065  OD1 ASP D1335     3487   2780   3075    -55    -77   -180       O  
ATOM   4066  OD2 ASP D1335      29.244  -3.222   8.781  1.00 24.77           O  
ANISOU 4066  OD2 ASP D1335     3512   2758   3139     21    -85   -198       O  
ATOM   4067  N   ILE D1336      25.696   0.503  11.676  1.00 19.39           N  
ANISOU 4067  N   ILE D1336     2781   2217   2369    -68     58    -72       N  
ATOM   4068  CA  ILE D1336      25.470   1.718  12.457  1.00 18.76           C  
ANISOU 4068  CA  ILE D1336     2691   2153   2281    -59     94    -51       C  
ATOM   4069  C   ILE D1336      25.870   1.487  13.934  1.00 18.78           C  
ANISOU 4069  C   ILE D1336     2720   2114   2300   -110     77    -39       C  
ATOM   4070  O   ILE D1336      25.308   0.626  14.630  1.00 18.87           O  
ANISOU 4070  O   ILE D1336     2746   2126   2298   -170     48    -37       O  
ATOM   4071  CB  ILE D1336      23.983   2.163  12.323  1.00 19.40           C  
ANISOU 4071  CB  ILE D1336     2738   2316   2315    -56    112    -54       C  
ATOM   4072  CG1 ILE D1336      23.662   2.495  10.834  1.00 20.61           C  
ANISOU 4072  CG1 ILE D1336     2868   2516   2445      9    129    -65       C  
ATOM   4073  CG2 ILE D1336      23.785   3.385  13.220  1.00 19.33           C  
ANISOU 4073  CG2 ILE D1336     2724   2318   2299    -42    143    -38       C  
ATOM   4074  CD1 ILE D1336      22.278   3.004  10.545  1.00 21.83           C  
ANISOU 4074  CD1 ILE D1336     2983   2763   2547     36    143    -76       C  
ATOM   4075  N   SER D1337      26.779   2.340  14.414  1.00 17.51           N  
ANISOU 4075  N   SER D1337     2566   1923   2163    -88     98    -31       N  
ATOM   4076  CA  SER D1337      27.411   2.243  15.754  1.00 18.03           C  
ANISOU 4076  CA  SER D1337     2652   1953   2246   -120     83    -24       C  
ATOM   4077  C   SER D1337      27.008   3.488  16.547  1.00 18.13           C  
ANISOU 4077  C   SER D1337     2646   1993   2248   -119    121    -15       C  
ATOM   4078  O   SER D1337      27.149   4.615  16.086  1.00 18.02           O  
ANISOU 4078  O   SER D1337     2623   1984   2240    -77    162    -16       O  
ATOM   4079  CB  SER D1337      28.957   2.151  15.600  1.00 18.66           C  
ANISOU 4079  CB  SER D1337     2743   1985   2361    -93     73    -40       C  
ATOM   4080  OG  SER D1337      29.361   0.879  15.073  1.00 19.55           O  
ANISOU 4080  OG  SER D1337     2876   2069   2482    -91     27    -55       O  
ATOM   4081  N   VAL D1338      26.512   3.287  17.764  1.00 17.35           N  
ANISOU 4081  N   VAL D1338     2549   1909   2132   -166    108     -7       N  
ATOM   4082  CA  VAL D1338      26.360   4.361  18.746  1.00 17.13           C  
ANISOU 4082  CA  VAL D1338     2505   1902   2099   -167    136     -6       C  
ATOM   4083  C   VAL D1338      27.305   3.964  19.906  1.00 17.08           C  
ANISOU 4083  C   VAL D1338     2520   1860   2109   -197    111     -5       C  
ATOM   4084  O   VAL D1338      27.293   2.824  20.397  1.00 17.66           O  
ANISOU 4084  O   VAL D1338     2619   1919   2171   -238     70      5       O  
ATOM   4085  CB  VAL D1338      24.892   4.659  19.156  1.00 17.63           C  
ANISOU 4085  CB  VAL D1338     2540   2038   2118   -187    147     -7       C  
ATOM   4086  CG1 VAL D1338      24.847   5.915  20.011  1.00 17.26           C  
ANISOU 4086  CG1 VAL D1338     2477   2008   2071   -169    178    -15       C  
ATOM   4087  CG2 VAL D1338      24.029   4.893  17.932  1.00 17.68           C  
ANISOU 4087  CG2 VAL D1338     2525   2086   2102   -146    162    -15       C  
ATOM   4088  N   ILE D1339      28.235   4.868  20.198  1.00 15.40           N  
ANISOU 4088  N   ILE D1339     2300   1626   1922   -172    136    -18       N  
ATOM   4089  CA  ILE D1339      29.234   4.752  21.196  1.00 15.12           C  
ANISOU 4089  CA  ILE D1339     2272   1571   1902   -185    119    -28       C  
ATOM   4090  C   ILE D1339      28.987   5.731  22.334  1.00 14.64           C  
ANISOU 4090  C   ILE D1339     2190   1539   1831   -199    145    -35       C  
ATOM   4091  O   ILE D1339      28.958   6.979  22.089  1.00 14.37           O  
ANISOU 4091  O   ILE D1339     2140   1508   1811   -173    191    -50       O  
ATOM   4092  CB  ILE D1339      30.651   5.012  20.607  1.00 14.59           C  
ANISOU 4092  CB  ILE D1339     2203   1469   1871   -151    130    -54       C  
ATOM   4093  CG1 ILE D1339      30.997   4.033  19.458  1.00 15.09           C  
ANISOU 4093  CG1 ILE D1339     2281   1509   1941   -130    101    -55       C  
ATOM   4094  CG2 ILE D1339      31.695   4.951  21.699  1.00 14.81           C  
ANISOU 4094  CG2 ILE D1339     2227   1492   1907   -158    112    -74       C  
ATOM   4095  CD1 ILE D1339      30.625   4.426  18.082  1.00 15.32           C  
ANISOU 4095  CD1 ILE D1339     2303   1545   1973   -103    132    -52       C  
ATOM   4096  N   THR D1340      28.975   5.224  23.571  1.00 14.62           N  
ANISOU 4096  N   THR D1340     2192   1552   1808   -235    116    -29       N  
ATOM   4097  CA  THR D1340      28.830   6.024  24.794  1.00 14.99           C  
ANISOU 4097  CA  THR D1340     2216   1635   1844   -250    134    -41       C  
ATOM   4098  C   THR D1340      30.148   6.694  25.089  1.00 14.87           C  
ANISOU 4098  C   THR D1340     2189   1597   1861   -229    149    -75       C  
ATOM   4099  O   THR D1340      31.193   6.101  25.080  1.00 14.90           O  
ANISOU 4099  O   THR D1340     2204   1578   1879   -219    122    -84       O  
ATOM   4100  CB  THR D1340      28.405   5.113  25.953  1.00 15.30           C  
ANISOU 4100  CB  THR D1340     2269   1703   1841   -301     95    -19       C  
ATOM   4101  OG1 THR D1340      27.262   4.345  25.568  1.00 15.57           O  
ANISOU 4101  OG1 THR D1340     2316   1756   1843   -335     82      6       O  
ATOM   4102  CG2 THR D1340      28.099   5.867  27.190  1.00 15.48           C  
ANISOU 4102  CG2 THR D1340     2261   1778   1843   -319    112    -33       C  
ATOM   4103  N   LEU D1341      30.124   8.026  25.296  1.00 14.80           N  
ANISOU 4103  N   LEU D1341     2157   1598   1867   -218    196   -101       N  
ATOM   4104  CA  LEU D1341      31.331   8.784  25.534  1.00 15.04           C  
ANISOU 4104  CA  LEU D1341     2174   1611   1930   -209    221   -141       C  
ATOM   4105  C   LEU D1341      31.425   9.306  26.976  1.00 15.55           C  
ANISOU 4105  C   LEU D1341     2211   1713   1983   -229    224   -168       C  
ATOM   4106  O   LEU D1341      30.449   9.825  27.520  1.00 16.38           O  
ANISOU 4106  O   LEU D1341     2304   1850   2067   -237    237   -166       O  
ATOM   4107  CB  LEU D1341      31.348  10.000  24.597  1.00 14.80           C  
ANISOU 4107  CB  LEU D1341     2148   1547   1926   -187    278   -155       C  
ATOM   4108  CG  LEU D1341      31.310   9.793  23.081  1.00 14.93           C  
ANISOU 4108  CG  LEU D1341     2188   1531   1952   -162    288   -134       C  
ATOM   4109  CD1 LEU D1341      31.453  11.124  22.436  1.00 15.14           C  
ANISOU 4109  CD1 LEU D1341     2230   1521   1999   -146    347   -146       C  
ATOM   4110  CD2 LEU D1341      32.348   8.837  22.528  1.00 14.66           C  
ANISOU 4110  CD2 LEU D1341     2156   1483   1931   -160    260   -139       C  
ATOM   4111  N   ILE D1342      32.586   9.188  27.588  1.00 16.56           N  
ANISOU 4111  N   ILE D1342     2324   1847   2119   -233    211   -200       N  
ATOM   4112  CA  ILE D1342      32.923   9.896  28.816  1.00 17.29           C  
ANISOU 4112  CA  ILE D1342     2384   1976   2209   -248    224   -241       C  
ATOM   4113  C   ILE D1342      34.075  10.852  28.536  1.00 18.68           C  
ANISOU 4113  C   ILE D1342     2541   2130   2425   -246    267   -298       C  
ATOM   4114  O   ILE D1342      34.582  10.917  27.385  1.00 17.75           O  
ANISOU 4114  O   ILE D1342     2437   1972   2333   -237    288   -300       O  
ATOM   4115  CB  ILE D1342      33.314   8.936  29.968  1.00 17.95           C  
ANISOU 4115  CB  ILE D1342     2462   2102   2257   -256    169   -237       C  
ATOM   4116  CG1 ILE D1342      34.653   8.237  29.703  1.00 17.95           C  
ANISOU 4116  CG1 ILE D1342     2463   2088   2266   -232    137   -258       C  
ATOM   4117  CG2 ILE D1342      32.170   7.973  30.263  1.00 17.69           C  
ANISOU 4117  CG2 ILE D1342     2456   2085   2177   -275    131   -178       C  
ATOM   4118  CD1 ILE D1342      35.142   7.426  30.883  1.00 18.98           C  
ANISOU 4118  CD1 ILE D1342     2593   2260   2358   -225     82   -259       C  
ATOM   4119  N   ASN D1343      34.526  11.561  29.557  1.00 19.63           N  
ANISOU 4119  N   ASN D1343     2628   2283   2548   -262    284   -348       N  
ATOM   4120  CA  ASN D1343      35.694  12.397  29.336  1.00 21.47           C  
ANISOU 4120  CA  ASN D1343     2840   2501   2815   -275    327   -411       C  
ATOM   4121  C   ASN D1343      36.953  11.593  29.116  1.00 20.88           C  
ANISOU 4121  C   ASN D1343     2747   2445   2741   -266    297   -436       C  
ATOM   4122  O   ASN D1343      37.357  10.914  30.042  1.00 22.81           O  
ANISOU 4122  O   ASN D1343     2968   2739   2957   -255    250   -449       O  
ATOM   4123  CB  ASN D1343      35.897  13.332  30.481  1.00 23.36           C  
ANISOU 4123  CB  ASN D1343     3044   2773   3056   -297    351   -468       C  
ATOM   4124  CG  ASN D1343      36.751  14.480  30.090  1.00 24.78           C  
ANISOU 4124  CG  ASN D1343     3217   2920   3276   -325    415   -529       C  
ATOM   4125  OD1 ASN D1343      37.815  14.319  29.473  1.00 25.70           O  
ANISOU 4125  OD1 ASN D1343     3323   3033   3408   -336    425   -557       O  
ATOM   4126  ND2 ASN D1343      36.315  15.673  30.493  1.00 25.55           N  
ANISOU 4126  ND2 ASN D1343     3320   2997   3389   -340    458   -558       N  
ATOM   4127  N   GLY D1344      37.488  11.580  27.889  1.00 20.24           N  
ANISOU 4127  N   GLY D1344     2678   2328   2683   -263    318   -439       N  
ATOM   4128  CA  GLY D1344      38.700  10.785  27.594  1.00 20.77           C  
ANISOU 4128  CA  GLY D1344     2720   2423   2746   -246    287   -472       C  
ATOM   4129  C   GLY D1344      38.504   9.259  27.505  1.00 19.91           C  
ANISOU 4129  C   GLY D1344     2635   2319   2610   -203    210   -426       C  
ATOM   4130  O   GLY D1344      39.500   8.494  27.455  1.00 21.19           O  
ANISOU 4130  O   GLY D1344     2778   2510   2762   -173    170   -458       O  
ATOM   4131  N   GLY D1345      37.268   8.822  27.359  1.00 18.56           N  
ANISOU 4131  N   GLY D1345     2506   2117   2426   -199    192   -356       N  
ATOM   4132  CA  GLY D1345      36.937   7.365  27.303  1.00 18.00           C  
ANISOU 4132  CA  GLY D1345     2473   2037   2328   -171    123   -307       C  
ATOM   4133  C   GLY D1345      35.653   7.090  26.521  1.00 17.30           C  
ANISOU 4133  C   GLY D1345     2425   1909   2238   -178    127   -244       C  
ATOM   4134  O   GLY D1345      34.849   7.979  26.204  1.00 17.28           O  
ANISOU 4134  O   GLY D1345     2424   1895   2246   -195    175   -231       O  
ATOM   4135  N   GLU D1346      35.449   5.810  26.157  1.00 16.56           N  
ANISOU 4135  N   GLU D1346     2369   1794   2128   -160     73   -207       N  
ATOM   4136  CA  GLU D1346      34.268   5.445  25.425  1.00 15.96           C  
ANISOU 4136  CA  GLU D1346     2326   1692   2046   -171     74   -157       C  
ATOM   4137  C   GLU D1346      33.990   3.973  25.581  1.00 16.04           C  
ANISOU 4137  C   GLU D1346     2383   1682   2028   -168      8   -119       C  
ATOM   4138  O   GLU D1346      34.894   3.177  25.797  1.00 17.86           O  
ANISOU 4138  O   GLU D1346     2629   1903   2253   -138    -39   -133       O  
ATOM   4139  CB  GLU D1346      34.404   5.797  23.939  1.00 16.02           C  
ANISOU 4139  CB  GLU D1346     2330   1674   2083   -154    109   -164       C  
ATOM   4140  CG  GLU D1346      35.492   5.014  23.201  1.00 16.61           C  
ANISOU 4140  CG  GLU D1346     2405   1736   2169   -120     77   -190       C  
ATOM   4141  CD  GLU D1346      35.715   5.565  21.821  1.00 16.23           C  
ANISOU 4141  CD  GLU D1346     2345   1676   2144   -111    122   -204       C  
ATOM   4142  OE1 GLU D1346      35.405   4.861  20.843  1.00 16.10           O  
ANISOU 4142  OE1 GLU D1346     2348   1641   2126    -94    103   -184       O  
ATOM   4143  OE2 GLU D1346      36.056   6.825  21.709  1.00 15.88           O  
ANISOU 4143  OE2 GLU D1346     2277   1639   2117   -128    184   -229       O  
ATOM   4144  N   SER D1347      32.745   3.627  25.441  1.00 15.82           N  
ANISOU 4144  N   SER D1347     2380   1648   1981   -198      6    -75       N  
ATOM   4145  CA  SER D1347      32.316   2.196  25.402  1.00 16.09           C  
ANISOU 4145  CA  SER D1347     2473   1651   1990   -211    -48    -36       C  
ATOM   4146  C   SER D1347      32.716   1.508  24.121  1.00 16.67           C  
ANISOU 4146  C   SER D1347     2565   1682   2086   -177    -68    -44       C  
ATOM   4147  O   SER D1347      32.970   2.109  23.063  1.00 15.77           O  
ANISOU 4147  O   SER D1347     2420   1570   2002   -154    -33    -68       O  
ATOM   4148  CB  SER D1347      30.796   2.153  25.542  1.00 15.39           C  
ANISOU 4148  CB  SER D1347     2391   1583   1871   -266    -32      1       C  
ATOM   4149  OG  SER D1347      30.160   2.501  24.333  1.00 14.64           O  
ANISOU 4149  OG  SER D1347     2279   1489   1793   -260      0      0       O  
ATOM   4150  N   ALA D1348      32.608   0.164  24.171  1.00 16.97           N  
ANISOU 4150  N   ALA D1348     2664   1678   2104   -181   -125    -18       N  
ATOM   4151  CA  ALA D1348      32.604  -0.605  22.972  1.00 17.75           C  
ANISOU 4151  CA  ALA D1348     2787   1737   2218   -162   -146    -21       C  
ATOM   4152  C   ALA D1348      31.383  -0.233  22.110  1.00 16.88           C  
ANISOU 4152  C   ALA D1348     2657   1647   2110   -196   -103     -7       C  
ATOM   4153  O   ALA D1348      30.321   0.159  22.617  1.00 17.49           O  
ANISOU 4153  O   ALA D1348     2724   1758   2163   -245    -77     16       O  
ATOM   4154  CB  ALA D1348      32.542  -2.081  23.319  1.00 18.24           C  
ANISOU 4154  CB  ALA D1348     2933   1742   2256   -170   -213      5       C  
ATOM   4155  N   PRO D1349      31.522  -0.232  20.801  1.00 17.70           N  
ANISOU 4155  N   PRO D1349     2745   1743   2237   -166    -92    -26       N  
ATOM   4156  CA  PRO D1349      30.427   0.265  20.020  1.00 17.77           C  
ANISOU 4156  CA  PRO D1349     2727   1783   2241   -185    -50    -17       C  
ATOM   4157  C   PRO D1349      29.197  -0.662  20.059  1.00 19.54           C  
ANISOU 4157  C   PRO D1349     2984   2003   2434   -241    -71      9       C  
ATOM   4158  O   PRO D1349      29.386  -1.881  20.065  1.00 20.57           O  
ANISOU 4158  O   PRO D1349     3169   2083   2560   -251   -121     16       O  
ATOM   4159  CB  PRO D1349      31.016   0.313  18.574  1.00 17.46           C  
ANISOU 4159  CB  PRO D1349     2669   1735   2228   -135    -41    -45       C  
ATOM   4160  CG  PRO D1349      32.146  -0.637  18.624  1.00 18.42           C  
ANISOU 4160  CG  PRO D1349     2820   1816   2362   -102    -95    -67       C  
ATOM   4161  CD  PRO D1349      32.695  -0.648  19.970  1.00 17.86           C  
ANISOU 4161  CD  PRO D1349     2764   1737   2282   -107   -117    -63       C  
ATOM   4162  N   THR D1350      27.998  -0.107  20.149  1.00 19.58           N  
ANISOU 4162  N   THR D1350     2961   2062   2415   -277    -36     21       N  
ATOM   4163  CA  THR D1350      26.766  -0.863  19.947  1.00 21.34           C  
ANISOU 4163  CA  THR D1350     3198   2304   2606   -335    -44     32       C  
ATOM   4164  C   THR D1350      26.396  -0.699  18.497  1.00 22.17           C  
ANISOU 4164  C   THR D1350     3271   2431   2720   -301    -25     12       C  
ATOM   4165  O   THR D1350      25.986   0.367  18.047  1.00 20.43           O  
ANISOU 4165  O   THR D1350     3003   2262   2497   -270     16      3       O  
ATOM   4166  CB  THR D1350      25.604  -0.484  20.893  1.00 21.83           C  
ANISOU 4166  CB  THR D1350     3237   2430   2624   -396    -21     46       C  
ATOM   4167  OG1 THR D1350      26.021  -0.607  22.230  1.00 23.99           O  
ANISOU 4167  OG1 THR D1350     3540   2689   2887   -423    -38     66       O  
ATOM   4168  CG2 THR D1350      24.441  -1.428  20.684  1.00 22.91           C  
ANISOU 4168  CG2 THR D1350     3389   2589   2724   -470    -32     50       C  
ATOM   4169  N   THR D1351      26.528  -1.787  17.787  1.00 23.20           N  
ANISOU 4169  N   THR D1351     3434   2520   2858   -305    -59      3       N  
ATOM   4170  CA  THR D1351      26.423  -1.805  16.321  1.00 23.53           C  
ANISOU 4170  CA  THR D1351     3449   2578   2910   -265    -50    -21       C  
ATOM   4171  C   THR D1351      25.193  -2.598  15.955  1.00 26.01           C  
ANISOU 4171  C   THR D1351     3766   2921   3194   -324    -58    -28       C  
ATOM   4172  O   THR D1351      24.877  -3.607  16.561  1.00 26.32           O  
ANISOU 4172  O   THR D1351     3854   2926   3217   -392    -88    -17       O  
ATOM   4173  CB  THR D1351      27.714  -2.406  15.679  1.00 24.53           C  
ANISOU 4173  CB  THR D1351     3602   2643   3073   -213    -84    -41       C  
ATOM   4174  OG1 THR D1351      28.838  -1.581  16.014  1.00 25.57           O  
ANISOU 4174  OG1 THR D1351     3719   2766   3228   -166    -70    -44       O  
ATOM   4175  CG2 THR D1351      27.579  -2.530  14.176  1.00 24.87           C  
ANISOU 4175  CG2 THR D1351     3618   2708   3121   -177    -77    -68       C  
ATOM   4176  N   LEU D1352      24.455  -2.074  15.006  1.00 25.81           N  
ANISOU 4176  N   LEU D1352     3688   2964   3153   -300    -28    -46       N  
ATOM   4177  CA  LEU D1352      23.372  -2.817  14.376  1.00 26.74           C  
ANISOU 4177  CA  LEU D1352     3794   3123   3242   -346    -34    -69       C  
ATOM   4178  C   LEU D1352      23.462  -2.576  12.869  1.00 25.55           C  
ANISOU 4178  C   LEU D1352     3605   3002   3098   -276    -23    -97       C  
ATOM   4179  O   LEU D1352      23.922  -1.515  12.421  1.00 26.21           O  
ANISOU 4179  O   LEU D1352     3661   3104   3192   -203      4    -91       O  
ATOM   4180  CB  LEU D1352      22.031  -2.351  14.893  1.00 27.79           C  
ANISOU 4180  CB  LEU D1352     3883   3348   3326   -394     -5    -71       C  
ATOM   4181  CG  LEU D1352      21.624  -2.689  16.324  1.00 29.12           C  
ANISOU 4181  CG  LEU D1352     4080   3514   3471   -483    -11    -50       C  
ATOM   4182  CD1 LEU D1352      20.353  -1.967  16.666  1.00 30.27           C  
ANISOU 4182  CD1 LEU D1352     4159   3776   3565   -508     22    -65       C  
ATOM   4183  CD2 LEU D1352      21.468  -4.195  16.519  1.00 30.55           C  
ANISOU 4183  CD2 LEU D1352     4326   3637   3644   -574    -47    -48       C  
ATOM   4184  N   THR D1353      23.024  -3.569  12.096  1.00 26.45           N  
ANISOU 4184  N   THR D1353     3723   3122   3205   -303    -45   -127       N  
ATOM   4185  CA  THR D1353      22.999  -3.450  10.618  1.00 25.77           C  
ANISOU 4185  CA  THR D1353     3595   3077   3116   -241    -37   -158       C  
ATOM   4186  C   THR D1353      21.565  -3.209  10.141  1.00 28.12           C  
ANISOU 4186  C   THR D1353     3832   3487   3362   -256    -14   -184       C  
ATOM   4187  O   THR D1353      20.611  -3.999  10.439  1.00 27.22           O  
ANISOU 4187  O   THR D1353     3717   3403   3221   -342    -23   -206       O  
ATOM   4188  CB  THR D1353      23.631  -4.678   9.920  1.00 26.15           C  
ANISOU 4188  CB  THR D1353     3682   3062   3192   -242    -80   -187       C  
ATOM   4189  OG1 THR D1353      25.011  -4.795  10.275  1.00 26.12           O  
ANISOU 4189  OG1 THR D1353     3721   2971   3229   -206   -103   -172       O  
ATOM   4190  CG2 THR D1353      23.543  -4.550   8.391  1.00 25.79           C  
ANISOU 4190  CG2 THR D1353     3586   3075   3137   -180    -70   -222       C  
ATOM   4191  N   GLN D1354      21.398  -2.094   9.425  1.00 26.15           N  
ANISOU 4191  N   GLN D1354     3535   3305   3095   -174     17   -183       N  
ATOM   4192  CA  GLN D1354      20.116  -1.752   8.823  1.00 28.28           C  
ANISOU 4192  CA  GLN D1354     3742   3694   3310   -159     36   -214       C  
ATOM   4193  C   GLN D1354      20.290  -1.396   7.354  1.00 28.13           C  
ANISOU 4193  C   GLN D1354     3693   3715   3280    -69     44   -229       C  
ATOM   4194  O   GLN D1354      21.230  -0.681   6.973  1.00 26.27           O  
ANISOU 4194  O   GLN D1354     3475   3439   3066      0     59   -201       O  
ATOM   4195  CB  GLN D1354      19.452  -0.596   9.544  1.00 29.29           C  
ANISOU 4195  CB  GLN D1354     3841   3882   3406   -139     65   -197       C  
ATOM   4196  CG  GLN D1354      18.037  -0.306   9.053  1.00 30.94           C  
ANISOU 4196  CG  GLN D1354     3977   4227   3548   -120     78   -238       C  
ATOM   4197  CD  GLN D1354      17.126  -1.529   9.138  1.00 32.81           C  
ANISOU 4197  CD  GLN D1354     4190   4516   3759   -225     60   -287       C  
ATOM   4198  OE1 GLN D1354      16.471  -1.907   8.162  1.00 36.12           O  
ANISOU 4198  OE1 GLN D1354     4563   5015   4145   -215     56   -334       O  
ATOM   4199  NE2 GLN D1354      17.081  -2.142  10.303  1.00 32.60           N  
ANISOU 4199  NE2 GLN D1354     4197   4446   3742   -328     52   -275       N  
ATOM   4200  N   GLN D1355      19.411  -1.945   6.525  1.00 29.76           N  
ANISOU 4200  N   GLN D1355     3854   4003   3450    -77     36   -277       N  
ATOM   4201  CA  GLN D1355      19.420  -1.645   5.112  1.00 30.36           C  
ANISOU 4201  CA  GLN D1355     3895   4137   3502      8     43   -296       C  
ATOM   4202  C   GLN D1355      18.405  -0.561   4.884  1.00 33.49           C  
ANISOU 4202  C   GLN D1355     4241   4645   3837     74     69   -298       C  
ATOM   4203  O   GLN D1355      17.309  -0.612   5.452  1.00 34.53           O  
ANISOU 4203  O   GLN D1355     4335   4852   3932     31     71   -325       O  
ATOM   4204  CB  GLN D1355      19.080  -2.877   4.281  1.00 31.10           C  
ANISOU 4204  CB  GLN D1355     3966   4261   3588    -30     17   -355       C  
ATOM   4205  CG  GLN D1355      19.346  -2.637   2.809  1.00 32.16           C  
ANISOU 4205  CG  GLN D1355     4070   4444   3703     61     21   -371       C  
ATOM   4206  CD  GLN D1355      19.015  -3.807   1.928  1.00 34.16           C  
ANISOU 4206  CD  GLN D1355     4294   4735   3948     29     -5   -438       C  
ATOM   4207  OE1 GLN D1355      19.757  -4.797   1.878  1.00 35.39           O  
ANISOU 4207  OE1 GLN D1355     4489   4805   4150    -10    -33   -455       O  
ATOM   4208  NE2 GLN D1355      17.890  -3.707   1.205  1.00 35.95           N  
ANISOU 4208  NE2 GLN D1355     4451   5095   4113     53      1   -485       N  
ATOM   4209  N   THR D1356      18.771   0.432   4.080  1.00 34.43           N  
ANISOU 4209  N   THR D1356     4362   4777   3940    178     90   -271       N  
ATOM   4210  CA  THR D1356      17.802   1.428   3.587  1.00 35.11           C  
ANISOU 4210  CA  THR D1356     4407   4974   3959    268    108   -277       C  
ATOM   4211  C   THR D1356      16.776   0.761   2.622  1.00 37.18           C  
ANISOU 4211  C   THR D1356     4598   5363   4165    275     92   -345       C  
ATOM   4212  O   THR D1356      17.087  -0.243   1.967  1.00 36.25           O  
ANISOU 4212  O   THR D1356     4473   5234   4065    239     73   -376       O  
ATOM   4213  CB  THR D1356      18.516   2.575   2.842  1.00 36.34           C  
ANISOU 4213  CB  THR D1356     4600   5099   4107    375    134   -227       C  
ATOM   4214  OG1 THR D1356      19.433   2.023   1.880  1.00 38.02           O  
ANISOU 4214  OG1 THR D1356     4826   5276   4343    381    128   -228       O  
ATOM   4215  CG2 THR D1356      19.250   3.503   3.827  1.00 36.33           C  
ANISOU 4215  CG2 THR D1356     4659   4998   4145    375    158   -170       C  
ATOM   4216  N   ALA D1357      15.570   1.329   2.548  1.00 38.79           N  
ANISOU 4216  N   ALA D1357     4746   5691   4300    325     97   -374       N  
ATOM   4217  CA  ALA D1357      14.435   0.701   1.846  1.00 40.60           C  
ANISOU 4217  CA  ALA D1357     4893   6064   4469    319     82   -452       C  
ATOM   4218  C   ALA D1357      14.740   0.276   0.401  1.00 41.33           C  
ANISOU 4218  C   ALA D1357     4969   6185   4547    369     72   -474       C  
ATOM   4219  O   ALA D1357      15.509   0.922  -0.283  1.00 41.74           O  
ANISOU 4219  O   ALA D1357     5061   6195   4603    455     83   -426       O  
ATOM   4220  CB  ALA D1357      13.214   1.625   1.890  1.00 39.84           C  
ANISOU 4220  CB  ALA D1357     4739   6106   4291    401     88   -479       C  
TER    4221      ALA D1357                                                      
HETATM 4222  O   HOH A 201      42.273  -5.287  28.811  1.00 25.51           O  
HETATM 4223  O   HOH A 202      57.154   1.246  57.033  1.00 21.28           O  
HETATM 4224  O   HOH A 203      54.672  16.380  32.905  1.00 25.47           O  
HETATM 4225  O   HOH A 204      54.886 -11.386  33.291  1.00 28.57           O  
HETATM 4226  O   HOH A 205      50.541  -5.393  18.600  1.00 32.03           O  
HETATM 4227  O   HOH A 206      50.707   5.334  19.839  1.00 26.91           O  
HETATM 4228  O   HOH A 207      66.715   0.378  35.713  1.00 39.97           O  
HETATM 4229  O   HOH A 208      57.555  15.003  37.275  1.00 26.86           O  
HETATM 4230  O   HOH A 209      53.489   6.651  20.257  1.00 31.52           O  
HETATM 4231  O   HOH A 210      51.873  -7.042  24.594  1.00 23.21           O  
HETATM 4232  O   HOH A 211      40.400  16.230  26.772  1.00 30.80           O  
HETATM 4233  O   HOH A 212      44.493   0.298  50.536  1.00 27.00           O  
HETATM 4234  O   HOH A 213      64.230  24.818  32.661  1.00 32.29           O  
HETATM 4235  O   HOH A 214      51.795   9.910  55.086  1.00 29.44           O  
HETATM 4236  O   HOH A 215      60.913  -1.996  19.587  1.00 36.94           O  
HETATM 4237  O   HOH A 216      42.028   9.758  34.485  1.00 24.25           O  
HETATM 4238  O   HOH A 217      50.976  -2.355  51.613  1.00 19.51           O  
HETATM 4239  O   HOH A 218      45.470  -0.654  17.443  1.00 24.33           O  
HETATM 4240  O   HOH A 219      36.613  19.346  35.979  1.00 27.42           O  
HETATM 4241  O   HOH A 220      36.813   1.173  43.849  1.00 32.09           O  
HETATM 4242  O   HOH A 221      57.211   3.782  55.855  1.00 28.24           O  
HETATM 4243  O   HOH A 222      59.167  -8.861  38.738  1.00 28.27           O  
HETATM 4244  O   HOH A 223      52.670   9.632  46.896  1.00 24.34           O  
HETATM 4245  O   HOH A 224      57.082 -11.437  25.840  1.00 38.84           O  
HETATM 4246  O   HOH A 225      41.396   0.375  24.329  1.00 22.74           O  
HETATM 4247  O   HOH A 226      61.587  27.469  52.961  1.00 26.73           O  
HETATM 4248  O   HOH A 227      51.733   3.751  53.444  1.00 21.07           O  
HETATM 4249  O   HOH A 228      64.934  14.179  45.686  1.00 28.66           O  
HETATM 4250  O   HOH A 229      54.962  -9.385  17.561  1.00 38.80           O  
HETATM 4251  O   HOH A 230      39.103   1.271  42.299  1.00 22.40           O  
HETATM 4252  O   HOH A 231      54.393  11.992  23.858  1.00 20.75           O  
HETATM 4253  O   HOH A 232      62.132  -9.177  48.317  1.00 20.43           O  
HETATM 4254  O   HOH A 233      57.731  -0.325  38.477  1.00 28.54           O  
HETATM 4255  O   HOH A 234      41.114   2.984  24.810  1.00 33.41           O  
HETATM 4256  O   HOH A 235      59.003  17.622  31.643  1.00 31.15           O  
HETATM 4257  O   HOH A 236      76.159  11.750  36.927  1.00 36.03           O  
HETATM 4258  O   HOH A 237      46.153  16.247  45.103  1.00 41.41           O  
HETATM 4259  O   HOH A 238      46.670  -4.356  18.330  1.00 35.46           O  
HETATM 4260  O   HOH A 239      47.561   5.864  19.140  1.00 18.53           O  
HETATM 4261  O   HOH A 240      40.465  -6.264  38.259  1.00 33.25           O  
HETATM 4262  O   HOH A 241      49.657  -7.258  28.621  1.00 23.37           O  
HETATM 4263  O   HOH A 242      52.705  -9.898  50.656  1.00 31.27           O  
HETATM 4264  O   HOH A 243      52.774  18.207  33.688  1.00 33.24           O  
HETATM 4265  O   HOH A 244      43.474   7.578  32.451  1.00 21.75           O  
HETATM 4266  O   HOH A 245      38.430   7.133  39.524  1.00 39.89           O  
HETATM 4267  O   HOH A 246      61.943 -11.767  41.975  1.00 27.69           O  
HETATM 4268  O   HOH A 247      51.861  17.798  36.350  1.00 20.42           O  
HETATM 4269  O   HOH A 248      54.872  15.876  36.871  1.00 25.50           O  
HETATM 4270  O   HOH A 249      52.453  -4.022  53.068  1.00 20.19           O  
HETATM 4271  O   HOH A 250      67.391  -1.201  26.658  1.00 32.70           O  
HETATM 4272  O   HOH A 251      49.978   9.479  19.905  1.00 42.01           O  
HETATM 4273  O   HOH A 252      49.696  -8.052  21.019  1.00 32.72           O  
HETATM 4274  O   HOH A 253      59.518  -4.544  62.993  1.00 23.21           O  
HETATM 4275  O   HOH A 254      37.304   7.764  45.489  1.00 25.04           O  
HETATM 4276  O   HOH A 255      45.334 -11.374  35.724  1.00 25.79           O  
HETATM 4277  O   HOH A 256      57.138  15.943  32.943  1.00 24.96           O  
HETATM 4278  O   HOH A 257      54.513  15.453  23.114  1.00 27.60           O  
HETATM 4279  O   HOH A 258      47.394  -5.498  22.674  1.00 21.90           O  
HETATM 4280  O   HOH A 259      39.265  -6.501  26.888  1.00 37.07           O  
HETATM 4281  O   HOH A 260      62.938  -4.993  34.327  1.00 31.04           O  
HETATM 4282  O   HOH A 261      56.700 -14.442  43.637  1.00 19.06           O  
HETATM 4283  O   HOH A 262      62.260   2.618  25.873  1.00 25.92           O  
HETATM 4284  O   HOH A 263      55.109 -13.227  29.326  1.00 26.71           O  
HETATM 4285  O   HOH A 264      58.811  14.828  42.232  1.00 26.46           O  
HETATM 4286  O   HOH A 265      56.435 -10.731  39.427  1.00 24.42           O  
HETATM 4287  O   HOH A 266      49.456  -8.603  61.067  1.00 38.82           O  
HETATM 4288  O   HOH A 267      69.028   1.164  34.028  1.00 29.67           O  
HETATM 4289  O   HOH A 268      54.108   7.650  47.531  1.00 35.88           O  
HETATM 4290  O   HOH A 269      44.389   5.090  54.433  1.00 27.70           O  
HETATM 4291  O   HOH A 270      57.422  -5.054  57.526  1.00 28.36           O  
HETATM 4292  O   HOH A 271      55.154   9.121  44.881  1.00 36.48           O  
HETATM 4293  O   HOH A 272      58.040  13.690  39.893  1.00 18.60           O  
HETATM 4294  O   HOH A 273      59.867  10.868  44.994  1.00 30.61           O  
HETATM 4295  O   HOH A 274      67.309 -15.657  44.923  1.00 23.05           O  
HETATM 4296  O   HOH A 275      53.687  19.605  26.765  1.00 29.22           O  
HETATM 4297  O   HOH A 276      43.626  -4.375  51.275  1.00 28.39           O  
HETATM 4298  O   HOH A 277      50.011  18.355  43.963  1.00 30.47           O  
HETATM 4299  O   HOH A 278      45.839  13.682  53.368  1.00 28.40           O  
HETATM 4300  O   HOH A 279      57.845   4.020  53.118  1.00 22.22           O  
HETATM 4301  O   HOH A 280      47.575 -16.979  33.536  1.00 41.43           O  
HETATM 4302  O   HOH A 281      50.128  13.028  57.203  1.00 36.35           O  
HETATM 4303  O   HOH A 282      55.153   8.850  21.333  1.00 30.00           O  
HETATM 4304  O   HOH A 283      51.192   6.473  54.483  1.00 32.46           O  
HETATM 4305  O   HOH A 284      37.982  -0.234  30.129  1.00 24.46           O  
HETATM 4306  O   HOH A 285      42.217  12.103  52.317  1.00 35.29           O  
HETATM 4307  O   HOH A 286      61.912  12.971  45.053  1.00 30.15           O  
HETATM 4308  O   HOH A 287      55.677  -0.270  62.600  1.00 26.47           O  
HETATM 4309  O   HOH A 288      63.425  22.216  34.448  1.00 28.55           O  
HETATM 4310  O   HOH A 289      58.589  16.575  34.994  1.00 25.63           O  
HETATM 4311  O   HOH A 290      36.654   0.184  24.704  1.00 34.64           O  
HETATM 4312  O   HOH A 291      53.834  11.285  45.141  1.00 41.68           O  
HETATM 4313  O   HOH A 292      61.757  14.174  47.655  1.00 38.61           O  
HETATM 4314  O   HOH A 293      50.351  -5.935  26.366  1.00 20.84           O  
HETATM 4315  O   HOH A 294      52.670  15.383  21.354  1.00 36.54           O  
HETATM 4316  O   HOH A 295      48.161  -6.960  25.097  1.00 23.71           O  
HETATM 4317  O   HOH A 296      67.701  10.081  25.411  1.00 37.35           O  
HETATM 4318  O   HOH A 297      42.444  -1.492  49.817  1.00 26.66           O  
HETATM 4319  O   HOH A 298      34.176  -4.034  20.615  1.00 36.76           O  
HETATM 4320  O   HOH A 299      52.807  -4.791  17.586  1.00 35.94           O  
HETATM 4321  O   HOH A 300      51.027  -9.618  24.989  1.00 25.90           O  
HETATM 4322  O   HOH A 301      43.420   1.006  53.250  1.00 37.25           O  
HETATM 4323  O   HOH A 302      53.685   4.877  16.352  1.00 35.63           O  
HETATM 4324  O   HOH B1401      60.006  -4.147  58.182  1.00 29.66           O  
HETATM 4325  O   HOH B1402      62.311   7.462  65.308  1.00 23.55           O  
HETATM 4326  O   HOH B1403      68.653  13.522  43.678  1.00 23.59           O  
HETATM 4327  O   HOH B1404      58.007   4.696  40.633  1.00 25.84           O  
HETATM 4328  O   HOH B1405      65.060   5.405  50.843  1.00 19.81           O  
HETATM 4329  O   HOH B1406      59.974   4.215  59.181  1.00 26.06           O  
HETATM 4330  O   HOH B1407      80.941   2.145  64.200  1.00 31.67           O  
HETATM 4331  O   HOH B1408      71.126  -3.315  66.832  1.00 22.84           O  
HETATM 4332  O   HOH B1409      70.013  -4.287  48.486  1.00 34.02           O  
HETATM 4333  O   HOH B1410      61.286  -5.345  70.412  1.00 23.92           O  
HETATM 4334  O   HOH B1411      60.833  -6.214  52.437  1.00 30.07           O  
HETATM 4335  O   HOH B1412      63.121  10.626  58.985  1.00 36.05           O  
HETATM 4336  O   HOH B1413      54.961   3.314  46.768  1.00 23.19           O  
HETATM 4337  O   HOH B1414      69.176  -6.354  70.118  1.00 33.96           O  
HETATM 4338  O   HOH B1415      61.786   9.121  45.145  1.00 19.20           O  
HETATM 4339  O   HOH B1416      69.856  10.340  62.395  1.00 32.99           O  
HETATM 4340  O   HOH B1417      63.481   1.280  71.315  1.00 51.32           O  
HETATM 4341  O   HOH B1418      67.045   8.792  66.871  1.00 35.52           O  
HETATM 4342  O   HOH B1419      78.795   8.997  53.865  1.00 35.69           O  
HETATM 4343  O   HOH B1420      82.317   7.590  50.530  1.00 45.93           O  
HETATM 4344  O   HOH B1421      67.687   3.963  61.796  1.00 19.96           O  
HETATM 4345  O   HOH B1422      63.029   8.592  47.697  1.00 30.06           O  
HETATM 4346  O   HOH B1423      80.358  -1.309  47.388  1.00 29.19           O  
HETATM 4347  O   HOH B1424      67.418  12.568  46.069  1.00 23.78           O  
HETATM 4348  O   HOH B1425      63.443   3.073  43.129  1.00 20.03           O  
HETATM 4349  O   HOH B1426      78.443   9.716  38.370  1.00 22.59           O  
HETATM 4350  O   HOH B1427      54.929  -0.063  67.929  1.00 25.07           O  
HETATM 4351  O   HOH B1428      76.241  11.743  45.655  1.00 30.28           O  
HETATM 4352  O   HOH B1429      75.010   2.538  69.039  1.00 39.23           O  
HETATM 4353  O   HOH B1430      76.671  -4.705  41.819  1.00 35.78           O  
HETATM 4354  O   HOH B1431      66.439  10.988  57.386  1.00 25.79           O  
HETATM 4355  O   HOH B1432      71.325  -9.581  53.015  1.00 37.72           O  
HETATM 4356  O   HOH B1433      80.325   9.301  49.973  1.00 35.15           O  
HETATM 4357  O   HOH B1434      57.174   4.875  62.930  1.00 36.06           O  
HETATM 4358  O   HOH B1435      56.358   2.383  64.503  1.00 32.21           O  
HETATM 4359  O   HOH B1436      79.699  -4.197  54.155  1.00 40.71           O  
HETATM 4360  O   HOH B1437      70.013   2.018  71.431  1.00 33.77           O  
HETATM 4361  O   HOH B1438      63.046   7.360  50.167  1.00 29.16           O  
HETATM 4362  O   HOH B1439      57.741   2.237  39.083  1.00 29.31           O  
HETATM 4363  O   HOH B1440      60.536   1.563  71.766  1.00 29.33           O  
HETATM 4364  O   HOH C 201      46.522  14.297   9.806  1.00 32.80           O  
HETATM 4365  O   HOH C 202      36.096 -10.886  -7.119  1.00 33.37           O  
HETATM 4366  O   HOH C 203      42.283  13.561 -14.008  1.00 24.59           O  
HETATM 4367  O   HOH C 204      37.921   2.598  21.775  1.00 30.89           O  
HETATM 4368  O   HOH C 205      45.635  -9.996   9.134  1.00 28.17           O  
HETATM 4369  O   HOH C 206      50.310   6.246  12.093  1.00 25.93           O  
HETATM 4370  O   HOH C 207      35.845  15.925   0.465  1.00 25.29           O  
HETATM 4371  O   HOH C 208      50.920  12.993 -14.923  1.00 28.60           O  
HETATM 4372  O   HOH C 209      47.163   0.641 -19.323  1.00 22.18           O  
HETATM 4373  O   HOH C 210      51.329  -1.314  -5.788  1.00 24.52           O  
HETATM 4374  O   HOH C 211      32.365   4.212 -12.414  1.00 28.40           O  
HETATM 4375  O   HOH C 212      22.295  -6.923   1.545  1.00 23.71           O  
HETATM 4376  O   HOH C 213      51.804  11.940 -10.318  1.00 25.67           O  
HETATM 4377  O   HOH C 214      50.275   1.174  15.715  1.00 25.86           O  
HETATM 4378  O   HOH C 215      36.193  -7.329   4.418  1.00 41.84           O  
HETATM 4379  O   HOH C 216      29.836  -7.154   7.357  1.00 33.10           O  
HETATM 4380  O   HOH C 217      24.440 -12.410  -5.697  1.00 35.86           O  
HETATM 4381  O   HOH C 218      37.282  -9.066  -5.426  1.00 28.63           O  
HETATM 4382  O   HOH C 219      55.515   2.587  -9.177  1.00 26.23           O  
HETATM 4383  O   HOH C 220      48.329  12.445  12.453  1.00 33.20           O  
HETATM 4384  O   HOH C 221      42.528 -11.228  -1.870  1.00 26.79           O  
HETATM 4385  O   HOH C 222      34.096 -10.364  -9.219  1.00 37.12           O  
HETATM 4386  O   HOH C 223      55.281  -3.200 -14.004  1.00 28.68           O  
HETATM 4387  O   HOH C 224      41.842  10.335  14.770  1.00 23.93           O  
HETATM 4388  O   HOH C 225      35.981   3.314 -21.066  1.00 33.97           O  
HETATM 4389  O   HOH C 226      43.960 -12.022   5.014  1.00 29.89           O  
HETATM 4390  O   HOH C 227      42.783   2.664  15.000  1.00 18.27           O  
HETATM 4391  O   HOH C 228      44.942  -3.098 -18.739  1.00 31.05           O  
HETATM 4392  O   HOH C 229      37.375  17.954 -12.437  1.00 33.92           O  
HETATM 4393  O   HOH C 230      40.115  -5.396 -14.602  1.00 26.19           O  
HETATM 4394  O   HOH C 231      34.176  12.714  14.441  1.00 31.84           O  
HETATM 4395  O   HOH C 232      37.686  -7.767  -0.547  1.00 28.56           O  
HETATM 4396  O   HOH C 233      47.321 -10.254   6.533  1.00 33.67           O  
HETATM 4397  O   HOH C 234      53.258   6.410 -14.180  1.00 29.50           O  
HETATM 4398  O   HOH C 235      39.127  -2.112 -16.760  1.00 25.97           O  
HETATM 4399  O   HOH C 236      37.241   5.179  18.742  1.00 23.86           O  
HETATM 4400  O   HOH C 237      23.619  -9.825  -6.511  1.00 29.99           O  
HETATM 4401  O   HOH C 238      55.123   4.705  -6.733  1.00 38.41           O  
HETATM 4402  O   HOH C 239      41.500  14.504   4.362  1.00 30.24           O  
HETATM 4403  O   HOH C 240      33.618   0.185  13.356  1.00 41.03           O  
HETATM 4404  O   HOH C 241      39.975  -9.770  -5.744  1.00 26.82           O  
HETATM 4405  O   HOH C 242      38.959   9.364  24.081  1.00 27.02           O  
HETATM 4406  O   HOH C 243      41.303  -3.663   8.102  1.00 45.38           O  
HETATM 4407  O   HOH C 244      44.956  13.859  -9.880  1.00 26.79           O  
HETATM 4408  O   HOH C 245      39.595   5.481  24.440  1.00 29.11           O  
HETATM 4409  O   HOH C 246      48.346 -15.567  -4.801  1.00 41.24           O  
HETATM 4410  O   HOH C 247      22.392  -3.914  -6.849  1.00 28.47           O  
HETATM 4411  O   HOH C 248      45.583  11.641  13.052  1.00 26.85           O  
HETATM 4412  O   HOH C 249      34.879  16.988   2.700  1.00 30.69           O  
HETATM 4413  O   HOH C 250      55.802  12.736 -11.425  1.00 25.85           O  
HETATM 4414  O   HOH C 251      43.229   0.071  16.375  1.00 22.44           O  
HETATM 4415  O   HOH C 252      46.049  -8.531 -11.299  1.00 26.10           O  
HETATM 4416  O   HOH C 253      48.970   7.150 -20.966  1.00 23.15           O  
HETATM 4417  O   HOH C 254      27.326  -8.838   4.529  1.00 28.27           O  
HETATM 4418  O   HOH C 255      51.896  14.412  -3.428  1.00 34.92           O  
HETATM 4419  O   HOH C 256      31.353  -4.003  20.329  1.00 26.31           O  
HETATM 4420  O   HOH C 257      28.807 -13.136   9.339  1.00 46.59           O  
HETATM 4421  O   HOH C 258      40.287  18.389  -4.894  1.00 23.39           O  
HETATM 4422  O   HOH C 259      38.541 -14.058   3.393  1.00 36.92           O  
HETATM 4423  O   HOH C 260      40.311  19.998  -9.788  1.00 41.32           O  
HETATM 4424  O   HOH C 261      37.614  20.009   2.863  1.00 34.02           O  
HETATM 4425  O   HOH C 262      34.604   3.952  14.091  1.00 31.87           O  
HETATM 4426  O   HOH C 263      41.034  -2.722  10.669  1.00 29.65           O  
HETATM 4427  O   HOH C 264      49.299  19.548 -10.482  1.00 33.98           O  
HETATM 4428  O   HOH C 265      49.482 -10.736 -10.989  1.00 24.20           O  
HETATM 4429  O   HOH C 266      57.371  -1.895   6.903  1.00 41.72           O  
HETATM 4430  O   HOH C 267      55.720  11.455  -7.684  1.00 29.54           O  
HETATM 4431  O   HOH C 268      54.248  15.401   5.751  1.00 33.84           O  
HETATM 4432  O   HOH C 269      51.094  15.365   7.198  1.00 29.90           O  
HETATM 4433  O   HOH C 270      38.406  17.636   1.263  1.00 29.72           O  
HETATM 4434  O   HOH C 271      54.741   0.592  -3.902  1.00 28.19           O  
HETATM 4435  O   HOH C 272      37.216   2.672  17.028  1.00 24.18           O  
HETATM 4436  O   HOH C 273      51.608  -6.286  14.218  1.00 37.72           O  
HETATM 4437  O   HOH C 274      55.659  11.241  -3.997  1.00 39.84           O  
HETATM 4438  O   HOH C 275      47.046  -8.231 -14.780  1.00 30.69           O  
HETATM 4439  O   HOH C 276      44.509   1.341 -19.241  1.00 31.15           O  
HETATM 4440  O   HOH C 277      35.733  14.578  16.107  1.00 30.84           O  
HETATM 4441  O   HOH C 278      59.669  -3.844  -4.222  1.00 38.14           O  
HETATM 4442  O   HOH C 279      36.820   6.820  -0.294  1.00 37.62           O  
HETATM 4443  O   HOH C 280      56.585   7.254  -5.815  1.00 28.90           O  
HETATM 4444  O   HOH C 281      34.192  -5.749   6.259  1.00 37.34           O  
HETATM 4445  O   HOH C 282      27.027  10.458  -5.556  1.00 40.09           O  
HETATM 4446  O   HOH C 283      53.246  -1.710  12.361  1.00 36.95           O  
HETATM 4447  O   HOH C 284      28.595 -12.557  12.409  1.00 39.06           O  
HETATM 4448  O   HOH C 285      54.387   6.432 -16.691  1.00 27.66           O  
HETATM 4449  O   HOH C 286      33.637  -2.113  15.439  1.00 31.10           O  
HETATM 4450  O   HOH C 287      46.455  12.022 -20.577  1.00 45.84           O  
HETATM 4451  O   HOH C 288      52.793  13.320 -12.220  1.00 24.38           O  
HETATM 4452  O   HOH C 289      40.946  -3.466  16.372  1.00 34.46           O  
HETATM 4453  O   HOH C 290      41.049  -4.930  13.605  1.00 37.76           O  
HETATM 4454  O   HOH C 291      42.542  -2.446 -17.824  1.00 37.61           O  
HETATM 4455  O   HOH C 292      55.292  -1.797  -5.649  1.00 35.29           O  
HETATM 4456  O   HOH C 293      36.436  -9.703  -2.708  1.00 29.39           O  
HETATM 4457  O   HOH C 294      39.954   7.153 -20.541  1.00 40.12           O  
HETATM 4458  O   HOH C 295      42.739  11.002 -21.803  1.00 36.56           O  
HETATM 4459  O   HOH C 296      37.840   4.271 -22.640  1.00 34.97           O  
HETATM 4460  O   HOH C 297      57.965   7.487 -14.677  1.00 29.91           O  
HETATM 4461  O   HOH C 298      26.843  10.267  -2.765  1.00 42.39           O  
HETATM 4462  O   HOH C 299      44.205  12.038  15.245  1.00 31.89           O  
HETATM 4463  O   HOH C 300      40.428  -4.340 -17.291  1.00 35.27           O  
HETATM 4464  O   HOH C 301      51.395   5.475  14.408  1.00 27.41           O  
HETATM 4465  O   HOH C 302      37.399   6.991 -22.224  1.00 34.44           O  
HETATM 4466  O   HOH C 303      49.726  18.805 -13.081  1.00 38.74           O  
HETATM 4467  O   HOH D1401      15.118   2.338  20.816  1.00 38.58           O  
HETATM 4468  O   HOH D1402      22.886  20.417  24.105  1.00 30.33           O  
HETATM 4469  O   HOH D1403      23.258  10.003  28.672  1.00 22.31           O  
HETATM 4470  O   HOH D1404      27.976  16.951  26.651  1.00 30.65           O  
HETATM 4471  O   HOH D1405      34.935   2.398  20.692  1.00 19.97           O  
HETATM 4472  O   HOH D1406      30.692  -4.729   7.311  1.00 30.36           O  
HETATM 4473  O   HOH D1407      37.380   1.325   1.493  1.00 43.58           O  
HETATM 4474  O   HOH D1408      22.333  12.791   9.954  1.00 34.54           O  
HETATM 4475  O   HOH D1409      30.060   5.857  32.771  1.00 36.86           O  
HETATM 4476  O   HOH D1410      33.127   5.016  16.209  1.00 23.85           O  
HETATM 4477  O   HOH D1411      32.830  -2.545   6.849  1.00 28.49           O  
HETATM 4478  O   HOH D1412      37.995   8.213  20.478  1.00 20.65           O  
HETATM 4479  O   HOH D1413      31.301   3.559   4.693  1.00 20.64           O  
HETATM 4480  O   HOH D1414      19.047   4.570  30.983  1.00 29.89           O  
HETATM 4481  O   HOH D1415      26.905  -5.942   7.828  1.00 24.89           O  
HETATM 4482  O   HOH D1416      39.660   3.314   8.329  1.00 23.55           O  
HETATM 4483  O   HOH D1417      22.090   4.890  33.617  1.00 26.62           O  
HETATM 4484  O   HOH D1418      30.590  12.706  37.343  1.00 30.82           O  
HETATM 4485  O   HOH D1419      17.339  14.246  28.224  1.00 30.00           O  
HETATM 4486  O   HOH D1420      31.665  -1.892   9.106  1.00 43.27           O  
HETATM 4487  O   HOH D1421      26.758   2.705  23.360  1.00 20.28           O  
HETATM 4488  O   HOH D1422      22.767  12.432  34.072  1.00 28.17           O  
HETATM 4489  O   HOH D1423      33.418   9.380   4.360  1.00 29.88           O  
HETATM 4490  O   HOH D1424      29.461  -0.367  32.508  1.00 36.95           O  
HETATM 4491  O   HOH D1425      29.767   1.234  12.311  1.00 22.78           O  
HETATM 4492  O   HOH D1426      35.750  10.533  24.853  1.00 33.62           O  
HETATM 4493  O   HOH D1427      35.083   1.110  28.355  1.00 32.80           O  
HETATM 4494  O   HOH D1428      33.565  11.831  32.196  1.00 23.50           O  
HETATM 4495  O   HOH D1429      24.358   7.978  -5.553  1.00 35.76           O  
HETATM 4496  O   HOH D1430      31.880  -1.060  26.618  1.00 27.59           O  
HETATM 4497  O   HOH D1431      29.882  16.424  14.539  1.00 36.28           O  
HETATM 4498  O   HOH D1432      25.139   5.559  32.941  1.00 24.41           O  
HETATM 4499  O   HOH D1433      16.067  12.359  23.625  1.00 39.72           O  
HETATM 4500  O   HOH D1434      20.206   1.816  26.873  1.00 34.22           O  
HETATM 4501  O   HOH D1435      30.667  14.844  33.285  1.00 32.36           O  
HETATM 4502  O   HOH D1436      39.757   0.022   7.999  1.00 34.73           O  
HETATM 4503  O   HOH D1437      17.884  16.664  23.952  1.00 33.74           O  
HETATM 4504  O   HOH D1438      37.656  10.252  32.914  1.00 39.84           O  
HETATM 4505  O   HOH D1439      37.718   4.004  26.820  1.00 25.47           O  
HETATM 4506  O   HOH D1440      20.786  -5.768  23.930  1.00 52.60           O  
HETATM 4507  O   HOH D1441      10.902   2.014   9.685  1.00 31.28           O  
HETATM 4508  O   HOH D1442      26.131  -6.586   5.062  1.00 28.03           O  
HETATM 4509  O   HOH D1443      24.351  16.757  16.061  1.00 41.35           O  
HETATM 4510  O   HOH D1444      18.042  -3.850  26.371  1.00 34.96           O  
HETATM 4511  O   HOH D1445      37.517   4.078   1.207  1.00 29.94           O  
HETATM 4512  O   HOH D1446      23.260  17.283  20.665  1.00 23.52           O  
HETATM 4513  O   HOH D1447      14.841  -1.606  21.993  1.00 39.18           O  
HETATM 4514  O   HOH D1448       8.117   9.108   9.567  1.00 30.21           O  
HETATM 4515  O   HOH D1449      14.129   3.463  23.003  1.00 40.37           O  
HETATM 4516  O   HOH D1450      22.379  15.716   9.219  1.00 44.84           O  
HETATM 4517  O   HOH D1451      31.243  -0.890  11.481  1.00 28.41           O  
CONECT  602 1403                                                                
CONECT 1403  602                                                                
CONECT 2707 3508                                                                
CONECT 3508 2707                                                                
MASTER      460    0    0    8   42    0    0    6 4513    4    4   48          
END                                                                             



If you find results from this site helpful for your research, please cite one of our papers:

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