CNRS Nantes University UFIP UFIP
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***  D3 CRISTAL   ***

elNémo ID: 2001292303262582

Job options:

ID        	=	 2001292303262582
JOBID     	=	 D3 CRISTAL 
USERID    	=	 unknown
PRIVAT    	=	 0

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

DOPROJMODS	=	 0
DORMSD    	=	 0

NRBL      	=	 0
CUTOFF    	=	 0
CAONLY    	=	 0


Input data for this run:

HEADER D3 CRISTAL 

HEADER    HYDROLASE/HYDROLASE INHIBITOR           20-OCT-10   3PBL              
TITLE     STRUCTURE OF THE HUMAN DOPAMINE D3 RECEPTOR IN COMPLEX WITH           
TITLE    2 ETICLOPRIDE                                                          
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: D(3) DOPAMINE RECEPTOR, LYSOZYME CHIMERA;                  
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 SYNONYM: DOPAMINE D3 RECEPTOR, ENDOLYSIN, LYSIS PROTEIN, MURAMIDASE; 
COMPND   5 EC: 3.2.1.17;                                                        
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS, ENTEROBACTERIA PHAGE T4;          
SOURCE   3 ORGANISM_COMMON: HUMAN, BACTERIOPHAGE T4;                            
SOURCE   4 ORGANISM_TAXID: 9606, 10665;                                         
SOURCE   5 GENE: DRD3, E;                                                       
SOURCE   6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 7108;                                       
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: SF9;                                       
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS;                          
SOURCE  10 EXPRESSION_SYSTEM_VECTOR: PFASTBAC                                   
KEYWDS    STRUCTURAL GENOMICS, PSI-2, PSI-BIOLOGY, PROTEIN STRUCTURE            
KEYWDS   2 INITIATIVE, ACCELERATED TECHNOLOGIES CENTER FOR GENE TO 3D           
KEYWDS   3 STRUCTURE, ATCG3D, 7TM, G PROTEIN-COUPLED RECEPTOR, GPCR, GPCR       
KEYWDS   4 NETWORK, SIGNAL TRANSDUCTION, HYDROLASE, ETICLOPRIDE, DOPAMINE,      
KEYWDS   5 NEUROTRANSMITTER, CHIMERA, T4L FUSION, MEMBRANE PROTEIN,             
KEYWDS   6 TRANSMEMBRANE, HYDROLASE-HYDROLASE INHIBITOR COMPLEX                 
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    E.Y.T.CHIEN,W.LIU,G.W.HAN,V.KATRITCH,Q.ZHAO,V.CHEREZOV,R.C.STEVENS,   
AUTHOR   2 ACCELERATED TECHNOLOGIES CENTER FOR GENE TO 3D STRUCTURE (ATCG3D),   
AUTHOR   3 GPCR NETWORK (GPCR)                                                  
REVDAT   4   16-AUG-17 3PBL    1       SOURCE REMARK                            
REVDAT   3   09-MAY-12 3PBL    1       KEYWDS REMARK VERSN                      
REVDAT   2   08-DEC-10 3PBL    1       JRNL                                     
REVDAT   1   03-NOV-10 3PBL    0                                                
JRNL        AUTH   E.Y.CHIEN,W.LIU,Q.ZHAO,V.KATRITCH,G.W.HAN,M.A.HANSON,L.SHI,  
JRNL        AUTH 2 A.H.NEWMAN,J.A.JAVITCH,V.CHEREZOV,R.C.STEVENS                
JRNL        TITL   STRUCTURE OF THE HUMAN DOPAMINE D3 RECEPTOR IN COMPLEX WITH  
JRNL        TITL 2 A D2/D3 SELECTIVE ANTAGONIST.                                
JRNL        REF    SCIENCE                       V. 330  1091 2010              
JRNL        REFN                   ISSN 0036-8075                               
JRNL        PMID   21097933                                                     
JRNL        DOI    10.1126/SCIENCE.1197410                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.89 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : BUSTER 2.8.0                                         
REMARK   3   AUTHORS     : BRICOGNE,BLANC,BRANDL,FLENSBURG,KELLER,              
REMARK   3               : PACIOREK,ROVERSI,SHARFF,SMART,VONRHEIN,              
REMARK   3               : WOMACK,MATTHEWS,TEN EYCK,TRONRUD                     
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.89                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 36.45                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : NULL                           
REMARK   3   NUMBER OF REFLECTIONS             : 25845                          
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)  : 0.245                          
REMARK   3   R VALUE            (WORKING SET)  : 0.243                          
REMARK   3   FREE R VALUE                      : 0.272                          
REMARK   3   FREE R VALUE TEST SET SIZE   (%)  : 5.100                          
REMARK   3   FREE R VALUE TEST SET COUNT       : 1318                           
REMARK   3   ESTIMATED ERROR OF FREE R VALUE   : NULL                           
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED               : 13                       
REMARK   3   BIN RESOLUTION RANGE HIGH   (ANGSTROMS) : 2.89                     
REMARK   3   BIN RESOLUTION RANGE LOW    (ANGSTROMS) : 3.01                     
REMARK   3   BIN COMPLETENESS (WORKING+TEST)     (%) : NULL                     
REMARK   3   REFLECTIONS IN BIN (WORKING + TEST SET) : 1136                     
REMARK   3   BIN R VALUE        (WORKING + TEST SET) : 0.2685                   
REMARK   3   REFLECTIONS IN BIN        (WORKING SET) : 1088                     
REMARK   3   BIN R VALUE               (WORKING SET) : 0.2678                   
REMARK   3   BIN FREE R VALUE                        : 0.2864                   
REMARK   3   BIN FREE R VALUE TEST SET SIZE      (%) : 4.23                     
REMARK   3   BIN FREE R VALUE TEST SET COUNT         : 48                       
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE     : NULL                     
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 6695                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 92                                      
REMARK   3   SOLVENT ATOMS            : 0                                       
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 48.31                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 76.45                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -3.49130                                             
REMARK   3    B22 (A**2) : 0.74120                                              
REMARK   3    B33 (A**2) : 2.75010                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT                    (A) : 0.586               
REMARK   3   DPI (BLOW EQ-10) BASED ON R VALUE        (A) : NULL                
REMARK   3   DPI (BLOW EQ-9) BASED ON FREE R VALUE    (A) : NULL                
REMARK   3   DPI (CRUICKSHANK) BASED ON R VALUE       (A) : NULL                
REMARK   3   DPI (CRUICKSHANK) BASED ON FREE R VALUE  (A) : NULL                
REMARK   3                                                                      
REMARK   3   REFERENCES: BLOW, D. (2002) ACTA CRYST D58, 792-797                
REMARK   3               CRUICKSHANK, D.W.J. (1999) ACTA CRYST D55, 583-601     
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.888                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.855                         
REMARK   3                                                                      
REMARK   3   NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15                    
REMARK   3   TERM                          COUNT    WEIGHT   FUNCTION.          
REMARK   3    BOND LENGTHS              : 6941   ; 2.000  ; NULL                
REMARK   3    BOND ANGLES               : 9462   ; 2.000  ; NULL                
REMARK   3    TORSION ANGLES            : 2295   ; 2.000  ; NULL                
REMARK   3    TRIGONAL CARBON PLANES    : 119    ; 2.000  ; NULL                
REMARK   3    GENERAL PLANES            : 1011   ; 5.000  ; NULL                
REMARK   3    ISOTROPIC THERMAL FACTORS : 6845   ; 20.000 ; NULL                
REMARK   3    BAD NON-BONDED CONTACTS   : 0      ; 5.000  ; NULL                
REMARK   3    IMPROPER TORSIONS         : NULL   ; NULL   ; NULL                
REMARK   3    PSEUDOROTATION ANGLES     : NULL   ; NULL   ; NULL                
REMARK   3    CHIRAL IMPROPER TORSION   : 927    ; 5.000  ; NULL                
REMARK   3    SUM OF OCCUPANCIES        : NULL   ; NULL   ; NULL                
REMARK   3    UTILITY DISTANCES         : NULL   ; NULL   ; NULL                
REMARK   3    UTILITY ANGLES            : NULL   ; NULL   ; NULL                
REMARK   3    UTILITY TORSION           : NULL   ; NULL   ; NULL                
REMARK   3    IDEAL-DIST CONTACT TERM   : 8330   ; 4.000  ; NULL                
REMARK   3                                                                      
REMARK   3   RMS DEVIATIONS FROM IDEAL VALUES.                                  
REMARK   3    BOND LENGTHS                       (A) : 0.009                    
REMARK   3    BOND ANGLES                  (DEGREES) : 1.08                     
REMARK   3    PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 4.97                     
REMARK   3    OTHER TORSION ANGLES         (DEGREES) : 16.55                    
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 6                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: { A|32 - A|221 }                                       
REMARK   3    ORIGIN FOR THE GROUP (A):    4.7976  -14.0348   -1.9304           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.0993 T22:   -0.0353                                    
REMARK   3     T33:   -0.2078 T12:    0.0363                                    
REMARK   3     T13:   -0.0560 T23:    0.0918                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    2.0941 L22:    2.7240                                    
REMARK   3     L33:    7.3932 L12:    0.4607                                    
REMARK   3     L13:    1.6858 L23:   -0.0696                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:    0.0612 S12:   -0.0288 S13:   -0.0925                     
REMARK   3     S21:    0.0731 S22:   -0.0412 S23:   -0.1758                     
REMARK   3     S31:    0.5442 S32:    0.0957 S33:   -0.0200                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: { A|1002 - A|1161 }                                    
REMARK   3    ORIGIN FOR THE GROUP (A):    5.5073    4.2583  -43.7494           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.1337 T22:   -0.2610                                    
REMARK   3     T33:   -0.2938 T12:    0.0088                                    
REMARK   3     T13:   -0.0413 T23:    0.0498                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    2.0889 L22:    8.3154                                    
REMARK   3     L33:    6.4425 L12:    2.7453                                    
REMARK   3     L13:   -0.5626 L23:    2.4152                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:   -0.1829 S12:    0.1327 S13:   -0.1822                     
REMARK   3     S21:   -0.2488 S22:    0.2827 S23:   -0.1628                     
REMARK   3     S31:   -0.0561 S32:   -0.3260 S33:   -0.0998                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: { A|319 - A|400 }                                      
REMARK   3    ORIGIN FOR THE GROUP (A):   -3.4354  -20.3907   -4.2989           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:    0.2148 T22:    0.1178                                    
REMARK   3     T33:   -0.1288 T12:   -0.1520                                    
REMARK   3     T13:   -0.1520 T23:    0.1243                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    1.7410 L22:    6.4693                                    
REMARK   3     L33:    3.4020 L12:    0.5841                                    
REMARK   3     L13:    2.5263 L23:   -0.4586                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:    0.0521 S12:   -0.2087 S13:   -0.2072                     
REMARK   3     S21:   -0.0863 S22:   -0.0391 S23:    0.1340                     
REMARK   3     S31:    0.1772 S32:   -0.0594 S33:   -0.0129                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: { B|32 - B|221 }                                       
REMARK   3    ORIGIN FOR THE GROUP (A):    6.3324   12.5149    2.5559           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.2539 T22:   -0.0016                                    
REMARK   3     T33:   -0.1927 T12:   -0.0591                                    
REMARK   3     T13:   -0.0035 T23:    0.0093                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    2.6235 L22:    3.6053                                    
REMARK   3     L33:    6.7173 L12:   -1.1982                                    
REMARK   3     L13:   -1.6767 L23:    1.4972                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:   -0.0085 S12:   -0.0929 S13:    0.3128                     
REMARK   3     S21:    0.0184 S22:    0.0959 S23:   -0.2410                     
REMARK   3     S31:   -0.4641 S32:    0.1454 S33:   -0.0874                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION: { B|1002 - B|1161 }                                    
REMARK   3    ORIGIN FOR THE GROUP (A):  -13.6628   19.8011   48.5178           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:    0.0489 T22:   -0.0127                                    
REMARK   3     T33:   -0.0989 T12:    0.1063                                    
REMARK   3     T13:   -0.0897 T23:   -0.1274                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    8.3154 L22:    5.8979                                    
REMARK   3     L33:    6.8090 L12:   -0.6974                                    
REMARK   3     L13:    1.4248 L23:    0.5641                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:    0.0102 S12:   -0.3413 S13:   -0.4534                     
REMARK   3     S21:    0.1362 S22:    0.0312 S23:   -0.0426                     
REMARK   3     S31:    0.5442 S32:    0.2359 S33:   -0.0413                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    SELECTION: { B|319 - B|400 }                                      
REMARK   3    ORIGIN FOR THE GROUP (A):    4.4916   22.9023    3.4233           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:    0.2635 T22:   -0.0272                                    
REMARK   3     T33:   -0.1211 T12:    0.0393                                    
REMARK   3     T13:    0.0641 T23:    0.0032                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    4.0113 L22:    6.8493                                    
REMARK   3     L33:    1.7839 L12:   -0.0541                                    
REMARK   3     L13:   -2.9104 L23:    0.2789                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:    0.0376 S12:   -0.1348 S13:    0.3897                     
REMARK   3     S21:   -0.0097 S22:   -0.0395 S23:   -0.1295                     
REMARK   3     S31:   -0.1938 S32:    0.0934 S33:    0.0019                     
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 3PBL COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 21-OCT-10.                  
REMARK 100 THE DEPOSITION ID IS D_1000062191.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 15-APR-10                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 45                                 
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 23-ID-B                            
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0330                             
REMARK 200  MONOCHROMATOR                  : DOUBLE CRYSTAL                     
REMARK 200  OPTICS                         : MIRRORS                            
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARMOSAIC 300 MM CCD               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 26229                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.900                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 78.5                               
REMARK 200  DATA REDUNDANCY                : 7.700                              
REMARK 200  R MERGE                    (I) : 0.11400                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 9.2000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.90                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.00                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 32.1                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.30                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.66500                            
REMARK 200  R SYM FOR SHELL            (I) : 0.99000                            
REMARK 200   FOR SHELL         : 0.800                              
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: PDB ENTRY 2RH1                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 63.51                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.37                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: LIPIDIC CUBIC PHASE MADE OF MONOOLEIN    
REMARK 280  AND 10% CHOLESTEROL, 30% PEG400, 300MM AMMONIUM ACETATE, 2%         
REMARK 280  GLUCOSE, 100MM BIS TRIS PROPANE PH 7.5, 1MM ETICLOPRIDE, LIPIDIC    
REMARK 280  CUBIC PHASE, TEMPERATURE 293K                                       
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000       44.41400            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       88.05800            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       46.24600            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       88.05800            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       44.41400            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       46.24600            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 300 REMARK: THE AUTHOR STATES THAT THE BIOLOGICAL UNIT OF THIS PROTEIN   
REMARK 300 IS UNKNOWN.                                                          
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: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     ASP A    -8                                                      
REMARK 465     TYR A    -7                                                      
REMARK 465     LYS A    -6                                                      
REMARK 465     ASP A    -5                                                      
REMARK 465     ASP A    -4                                                      
REMARK 465     ASP A    -3                                                      
REMARK 465     ASP A    -2                                                      
REMARK 465     GLY A    -1                                                      
REMARK 465     ALA A     0                                                      
REMARK 465     PRO A     1                                                      
REMARK 465     ALA A     2                                                      
REMARK 465     SER A     3                                                      
REMARK 465     LEU A     4                                                      
REMARK 465     SER A     5                                                      
REMARK 465     GLN A     6                                                      
REMARK 465     LEU A     7                                                      
REMARK 465     SER A     8                                                      
REMARK 465     SER A     9                                                      
REMARK 465     HIS A    10                                                      
REMARK 465     LEU A    11                                                      
REMARK 465     ASN A    12                                                      
REMARK 465     TYR A    13                                                      
REMARK 465     THR A    14                                                      
REMARK 465     CYS A    15                                                      
REMARK 465     GLY A    16                                                      
REMARK 465     ALA A    17                                                      
REMARK 465     GLU A    18                                                      
REMARK 465     ASN A    19                                                      
REMARK 465     SER A    20                                                      
REMARK 465     THR A    21                                                      
REMARK 465     GLY A    22                                                      
REMARK 465     ALA A    23                                                      
REMARK 465     SER A    24                                                      
REMARK 465     GLN A    25                                                      
REMARK 465     ALA A    26                                                      
REMARK 465     ARG A    27                                                      
REMARK 465     PRO A    28                                                      
REMARK 465     HIS A    29                                                      
REMARK 465     ALA A    30                                                      
REMARK 465     TYR A    31                                                      
REMARK 465     GLY A   401                                                      
REMARK 465     ARG A   402                                                      
REMARK 465     PRO A   403                                                      
REMARK 465     LEU A   404                                                      
REMARK 465     GLU A   405                                                      
REMARK 465     VAL A   406                                                      
REMARK 465     LEU A   407                                                      
REMARK 465     PHE A   408                                                      
REMARK 465     GLN A   409                                                      
REMARK 465     ASP B    -8                                                      
REMARK 465     TYR B    -7                                                      
REMARK 465     LYS B    -6                                                      
REMARK 465     ASP B    -5                                                      
REMARK 465     ASP B    -4                                                      
REMARK 465     ASP B    -3                                                      
REMARK 465     ASP B    -2                                                      
REMARK 465     GLY B    -1                                                      
REMARK 465     ALA B     0                                                      
REMARK 465     PRO B     1                                                      
REMARK 465     ALA B     2                                                      
REMARK 465     SER B     3                                                      
REMARK 465     LEU B     4                                                      
REMARK 465     SER B     5                                                      
REMARK 465     GLN B     6                                                      
REMARK 465     LEU B     7                                                      
REMARK 465     SER B     8                                                      
REMARK 465     SER B     9                                                      
REMARK 465     HIS B    10                                                      
REMARK 465     LEU B    11                                                      
REMARK 465     ASN B    12                                                      
REMARK 465     TYR B    13                                                      
REMARK 465     THR B    14                                                      
REMARK 465     CYS B    15                                                      
REMARK 465     GLY B    16                                                      
REMARK 465     ALA B    17                                                      
REMARK 465     GLU B    18                                                      
REMARK 465     ASN B    19                                                      
REMARK 465     SER B    20                                                      
REMARK 465     THR B    21                                                      
REMARK 465     GLY B    22                                                      
REMARK 465     ALA B    23                                                      
REMARK 465     SER B    24                                                      
REMARK 465     GLN B    25                                                      
REMARK 465     ALA B    26                                                      
REMARK 465     ARG B    27                                                      
REMARK 465     PRO B    28                                                      
REMARK 465     HIS B    29                                                      
REMARK 465     ALA B    30                                                      
REMARK 465     TYR B    31                                                      
REMARK 465     VAL B   136                                                      
REMARK 465     HIS B   137                                                      
REMARK 465     TYR B   138                                                      
REMARK 465     GLN B   139                                                      
REMARK 465     HIS B   140                                                      
REMARK 465     GLY B   141                                                      
REMARK 465     THR B   142                                                      
REMARK 465     GLY B   143                                                      
REMARK 465     GLN B   144                                                      
REMARK 465     GLY B   401                                                      
REMARK 465     ARG B   402                                                      
REMARK 465     PRO B   403                                                      
REMARK 465     LEU B   404                                                      
REMARK 465     GLU B   405                                                      
REMARK 465     VAL B   406                                                      
REMARK 465     LEU B   407                                                      
REMARK 465     PHE B   408                                                      
REMARK 465     GLN B   409                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     GLN A 144    CG   CD   OE1  NE2                                  
REMARK 470     SER A 145    OG                                                  
REMARK 470     GLU A1108    CG   CD   OE1  OE2                                  
REMARK 470     THR A 357    OG1  CG2                                            
REMARK 470     SER B 145    OG                                                  
REMARK 470     ARG B 149    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ASN B1040    CG   OD1  ND2                                       
REMARK 470     ASN B1053    CG   OD1  ND2                                       
REMARK 470     ASN B1055    CG   OD1  ND2                                       
REMARK 470     ARG B1080    CG   CD   NE   CZ   NH1  NH2                        
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    SER A 196   CB  -  CA  -  C   ANGL. DEV. =  15.3 DEGREES          
REMARK 500    PHE A 197   N   -  CA  -  CB  ANGL. DEV. = -17.0 DEGREES          
REMARK 500    THR A 357   N   -  CA  -  CB  ANGL. DEV. = -11.8 DEGREES          
REMARK 500    CYS A 358   N   -  CA  -  CB  ANGL. DEV. = -25.1 DEGREES          
REMARK 500    SER B 196   CB  -  CA  -  C   ANGL. DEV. =  17.9 DEGREES          
REMARK 500    PHE B 197   N   -  CA  -  CB  ANGL. DEV. = -21.3 DEGREES          
REMARK 500    PHE B 197   N   -  CA  -  C   ANGL. DEV. =  19.0 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    GLN A 144     -164.98   -179.59                                   
REMARK 500    PHE A 170       40.61   -107.43                                   
REMARK 500    PHE A 197      -61.89   -104.58                                   
REMARK 500    ALA A1093      -36.27    -37.69                                   
REMARK 500    ARG A1125       92.75    -67.51                                   
REMARK 500    GLN A 356      112.03   -178.63                                   
REMARK 500    CYS A 358       89.10    -64.38                                   
REMARK 500    HIS A 359       65.10   -100.67                                   
REMARK 500    MET B 134       73.51   -117.34                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ETQ A 1200                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ETQ B 1200                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAL A 1500                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAL B 1501                
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: ATCG3D_74   RELATED DB: TARGETTRACK                      
REMARK 900 RELATED ID: GPCR-38   RELATED DB: TARGETTRACK                        
DBREF  3PBL A    2   221  UNP    P35462   DRD3_HUMAN       2    221             
DBREF  3PBL A 1002  1161  UNP    P00720   LYS_BPT4         2    161             
DBREF  3PBL A  319   400  UNP    P35462   DRD3_HUMAN     319    400             
DBREF  3PBL B    2   221  UNP    P35462   DRD3_HUMAN       2    221             
DBREF  3PBL B 1002  1161  UNP    P00720   LYS_BPT4         2    161             
DBREF  3PBL B  319   400  UNP    P35462   DRD3_HUMAN     319    400             
SEQADV 3PBL ASP A   -8  UNP  P35462              EXPRESSION TAG                 
SEQADV 3PBL TYR A   -7  UNP  P35462              EXPRESSION TAG                 
SEQADV 3PBL LYS A   -6  UNP  P35462              EXPRESSION TAG                 
SEQADV 3PBL ASP A   -5  UNP  P35462              EXPRESSION TAG                 
SEQADV 3PBL ASP A   -4  UNP  P35462              EXPRESSION TAG                 
SEQADV 3PBL ASP A   -3  UNP  P35462              EXPRESSION TAG                 
SEQADV 3PBL ASP A   -2  UNP  P35462              EXPRESSION TAG                 
SEQADV 3PBL GLY A   -1  UNP  P35462              EXPRESSION TAG                 
SEQADV 3PBL ALA A    0  UNP  P35462              EXPRESSION TAG                 
SEQADV 3PBL PRO A    1  UNP  P35462              EXPRESSION TAG                 
SEQADV 3PBL TRP A  119  UNP  P35462    LEU   119 ENGINEERED MUTATION            
SEQADV 3PBL THR A 1054  UNP  P00720    CYS    54 ENGINEERED MUTATION            
SEQADV 3PBL ALA A 1097  UNP  P00720    CYS    97 ENGINEERED MUTATION            
SEQADV 3PBL GLY A  401  UNP  P35462              EXPRESSION TAG                 
SEQADV 3PBL ARG A  402  UNP  P35462              EXPRESSION TAG                 
SEQADV 3PBL PRO A  403  UNP  P35462              EXPRESSION TAG                 
SEQADV 3PBL LEU A  404  UNP  P35462              EXPRESSION TAG                 
SEQADV 3PBL GLU A  405  UNP  P35462              EXPRESSION TAG                 
SEQADV 3PBL VAL A  406  UNP  P35462              EXPRESSION TAG                 
SEQADV 3PBL LEU A  407  UNP  P35462              EXPRESSION TAG                 
SEQADV 3PBL PHE A  408  UNP  P35462              EXPRESSION TAG                 
SEQADV 3PBL GLN A  409  UNP  P35462              EXPRESSION TAG                 
SEQADV 3PBL ASP B   -8  UNP  P35462              EXPRESSION TAG                 
SEQADV 3PBL TYR B   -7  UNP  P35462              EXPRESSION TAG                 
SEQADV 3PBL LYS B   -6  UNP  P35462              EXPRESSION TAG                 
SEQADV 3PBL ASP B   -5  UNP  P35462              EXPRESSION TAG                 
SEQADV 3PBL ASP B   -4  UNP  P35462              EXPRESSION TAG                 
SEQADV 3PBL ASP B   -3  UNP  P35462              EXPRESSION TAG                 
SEQADV 3PBL ASP B   -2  UNP  P35462              EXPRESSION TAG                 
SEQADV 3PBL GLY B   -1  UNP  P35462              EXPRESSION TAG                 
SEQADV 3PBL ALA B    0  UNP  P35462              EXPRESSION TAG                 
SEQADV 3PBL PRO B    1  UNP  P35462              EXPRESSION TAG                 
SEQADV 3PBL TRP B  119  UNP  P35462    LEU   119 ENGINEERED MUTATION            
SEQADV 3PBL THR B 1054  UNP  P00720    CYS    54 ENGINEERED MUTATION            
SEQADV 3PBL ALA B 1097  UNP  P00720    CYS    97 ENGINEERED MUTATION            
SEQADV 3PBL GLY B  401  UNP  P35462              EXPRESSION TAG                 
SEQADV 3PBL ARG B  402  UNP  P35462              EXPRESSION TAG                 
SEQADV 3PBL PRO B  403  UNP  P35462              EXPRESSION TAG                 
SEQADV 3PBL LEU B  404  UNP  P35462              EXPRESSION TAG                 
SEQADV 3PBL GLU B  405  UNP  P35462              EXPRESSION TAG                 
SEQADV 3PBL VAL B  406  UNP  P35462              EXPRESSION TAG                 
SEQADV 3PBL LEU B  407  UNP  P35462              EXPRESSION TAG                 
SEQADV 3PBL PHE B  408  UNP  P35462              EXPRESSION TAG                 
SEQADV 3PBL GLN B  409  UNP  P35462              EXPRESSION TAG                 
SEQRES   1 A  481  ASP TYR LYS ASP ASP ASP ASP GLY ALA PRO ALA SER LEU          
SEQRES   2 A  481  SER GLN LEU SER SER HIS LEU ASN TYR THR CYS GLY ALA          
SEQRES   3 A  481  GLU ASN SER THR GLY ALA SER GLN ALA ARG PRO HIS ALA          
SEQRES   4 A  481  TYR TYR ALA LEU SER TYR CYS ALA LEU ILE LEU ALA ILE          
SEQRES   5 A  481  VAL PHE GLY ASN GLY LEU VAL CYS MET ALA VAL LEU LYS          
SEQRES   6 A  481  GLU ARG ALA LEU GLN THR THR THR ASN TYR LEU VAL VAL          
SEQRES   7 A  481  SER LEU ALA VAL ALA ASP LEU LEU VAL ALA THR LEU VAL          
SEQRES   8 A  481  MET PRO TRP VAL VAL TYR LEU GLU VAL THR GLY GLY VAL          
SEQRES   9 A  481  TRP ASN PHE SER ARG ILE CYS CYS ASP VAL PHE VAL THR          
SEQRES  10 A  481  LEU ASP VAL MET MET CYS THR ALA SER ILE TRP ASN LEU          
SEQRES  11 A  481  CYS ALA ILE SER ILE ASP ARG TYR THR ALA VAL VAL MET          
SEQRES  12 A  481  PRO VAL HIS TYR GLN HIS GLY THR GLY GLN SER SER CYS          
SEQRES  13 A  481  ARG ARG VAL ALA LEU MET ILE THR ALA VAL TRP VAL LEU          
SEQRES  14 A  481  ALA PHE ALA VAL SER CYS PRO LEU LEU PHE GLY PHE ASN          
SEQRES  15 A  481  THR THR GLY ASP PRO THR VAL CYS SER ILE SER ASN PRO          
SEQRES  16 A  481  ASP PHE VAL ILE TYR SER SER VAL VAL SER PHE TYR LEU          
SEQRES  17 A  481  PRO PHE GLY VAL THR VAL LEU VAL TYR ALA ARG ILE TYR          
SEQRES  18 A  481  VAL VAL LEU LYS GLN ARG ARG ARG LYS ASN ILE PHE GLU          
SEQRES  19 A  481  MET LEU ARG ILE ASP GLU GLY LEU ARG LEU LYS ILE TYR          
SEQRES  20 A  481  LYS ASP THR GLU GLY TYR TYR THR ILE GLY ILE GLY HIS          
SEQRES  21 A  481  LEU LEU THR LYS SER PRO SER LEU ASN ALA ALA LYS SER          
SEQRES  22 A  481  GLU LEU ASP LYS ALA ILE GLY ARG ASN THR ASN GLY VAL          
SEQRES  23 A  481  ILE THR LYS ASP GLU ALA GLU LYS LEU PHE ASN GLN ASP          
SEQRES  24 A  481  VAL ASP ALA ALA VAL ARG GLY ILE LEU ARG ASN ALA LYS          
SEQRES  25 A  481  LEU LYS PRO VAL TYR ASP SER LEU ASP ALA VAL ARG ARG          
SEQRES  26 A  481  ALA ALA LEU ILE ASN MET VAL PHE GLN MET GLY GLU THR          
SEQRES  27 A  481  GLY VAL ALA GLY PHE THR ASN SER LEU ARG MET LEU GLN          
SEQRES  28 A  481  GLN LYS ARG TRP ASP GLU ALA ALA VAL ASN LEU ALA LYS          
SEQRES  29 A  481  SER ARG TRP TYR ASN GLN THR PRO ASN ARG ALA LYS ARG          
SEQRES  30 A  481  VAL ILE THR THR PHE ARG THR GLY THR TRP ASP ALA TYR          
SEQRES  31 A  481  GLY VAL PRO LEU ARG GLU LYS LYS ALA THR GLN MET VAL          
SEQRES  32 A  481  ALA ILE VAL LEU GLY ALA PHE ILE VAL CYS TRP LEU PRO          
SEQRES  33 A  481  PHE PHE LEU THR HIS VAL LEU ASN THR HIS CYS GLN THR          
SEQRES  34 A  481  CYS HIS VAL SER PRO GLU LEU TYR SER ALA THR THR TRP          
SEQRES  35 A  481  LEU GLY TYR VAL ASN SER ALA LEU ASN PRO VAL ILE TYR          
SEQRES  36 A  481  THR THR PHE ASN ILE GLU PHE ARG LYS ALA PHE LEU LYS          
SEQRES  37 A  481  ILE LEU SER CYS GLY ARG PRO LEU GLU VAL LEU PHE GLN          
SEQRES   1 B  481  ASP TYR LYS ASP ASP ASP ASP GLY ALA PRO ALA SER LEU          
SEQRES   2 B  481  SER GLN LEU SER SER HIS LEU ASN TYR THR CYS GLY ALA          
SEQRES   3 B  481  GLU ASN SER THR GLY ALA SER GLN ALA ARG PRO HIS ALA          
SEQRES   4 B  481  TYR TYR ALA LEU SER TYR CYS ALA LEU ILE LEU ALA ILE          
SEQRES   5 B  481  VAL PHE GLY ASN GLY LEU VAL CYS MET ALA VAL LEU LYS          
SEQRES   6 B  481  GLU ARG ALA LEU GLN THR THR THR ASN TYR LEU VAL VAL          
SEQRES   7 B  481  SER LEU ALA VAL ALA ASP LEU LEU VAL ALA THR LEU VAL          
SEQRES   8 B  481  MET PRO TRP VAL VAL TYR LEU GLU VAL THR GLY GLY VAL          
SEQRES   9 B  481  TRP ASN PHE SER ARG ILE CYS CYS ASP VAL PHE VAL THR          
SEQRES  10 B  481  LEU ASP VAL MET MET CYS THR ALA SER ILE TRP ASN LEU          
SEQRES  11 B  481  CYS ALA ILE SER ILE ASP ARG TYR THR ALA VAL VAL MET          
SEQRES  12 B  481  PRO VAL HIS TYR GLN HIS GLY THR GLY GLN SER SER CYS          
SEQRES  13 B  481  ARG ARG VAL ALA LEU MET ILE THR ALA VAL TRP VAL LEU          
SEQRES  14 B  481  ALA PHE ALA VAL SER CYS PRO LEU LEU PHE GLY PHE ASN          
SEQRES  15 B  481  THR THR GLY ASP PRO THR VAL CYS SER ILE SER ASN PRO          
SEQRES  16 B  481  ASP PHE VAL ILE TYR SER SER VAL VAL SER PHE TYR LEU          
SEQRES  17 B  481  PRO PHE GLY VAL THR VAL LEU VAL TYR ALA ARG ILE TYR          
SEQRES  18 B  481  VAL VAL LEU LYS GLN ARG ARG ARG LYS ASN ILE PHE GLU          
SEQRES  19 B  481  MET LEU ARG ILE ASP GLU GLY LEU ARG LEU LYS ILE TYR          
SEQRES  20 B  481  LYS ASP THR GLU GLY TYR TYR THR ILE GLY ILE GLY HIS          
SEQRES  21 B  481  LEU LEU THR LYS SER PRO SER LEU ASN ALA ALA LYS SER          
SEQRES  22 B  481  GLU LEU ASP LYS ALA ILE GLY ARG ASN THR ASN GLY VAL          
SEQRES  23 B  481  ILE THR LYS ASP GLU ALA GLU LYS LEU PHE ASN GLN ASP          
SEQRES  24 B  481  VAL ASP ALA ALA VAL ARG GLY ILE LEU ARG ASN ALA LYS          
SEQRES  25 B  481  LEU LYS PRO VAL TYR ASP SER LEU ASP ALA VAL ARG ARG          
SEQRES  26 B  481  ALA ALA LEU ILE ASN MET VAL PHE GLN MET GLY GLU THR          
SEQRES  27 B  481  GLY VAL ALA GLY PHE THR ASN SER LEU ARG MET LEU GLN          
SEQRES  28 B  481  GLN LYS ARG TRP ASP GLU ALA ALA VAL ASN LEU ALA LYS          
SEQRES  29 B  481  SER ARG TRP TYR ASN GLN THR PRO ASN ARG ALA LYS ARG          
SEQRES  30 B  481  VAL ILE THR THR PHE ARG THR GLY THR TRP ASP ALA TYR          
SEQRES  31 B  481  GLY VAL PRO LEU ARG GLU LYS LYS ALA THR GLN MET VAL          
SEQRES  32 B  481  ALA ILE VAL LEU GLY ALA PHE ILE VAL CYS TRP LEU PRO          
SEQRES  33 B  481  PHE PHE LEU THR HIS VAL LEU ASN THR HIS CYS GLN THR          
SEQRES  34 B  481  CYS HIS VAL SER PRO GLU LEU TYR SER ALA THR THR TRP          
SEQRES  35 B  481  LEU GLY TYR VAL ASN SER ALA LEU ASN PRO VAL ILE TYR          
SEQRES  36 B  481  THR THR PHE ASN ILE GLU PHE ARG LYS ALA PHE LEU LYS          
SEQRES  37 B  481  ILE LEU SER CYS GLY ARG PRO LEU GLU VAL LEU PHE GLN          
HET    ETQ  A1200      23                                                       
HET    MAL  A1500      23                                                       
HET    ETQ  B1200      23                                                       
HET    MAL  B1501      23                                                       
HETNAM     ETQ 3-CHLORO-5-ETHYL-N-{[(2S)-1-ETHYLPYRROLIDIN-2-                   
HETNAM   2 ETQ  YL]METHYL}-6-HYDROXY-2-METHOXYBENZAMIDE                         
HETNAM     MAL MALTOSE                                                          
FORMUL   3  ETQ    2(C17 H25 CL N2 O3)                                          
FORMUL   4  MAL    2(C12 H22 O11)                                               
HELIX    1   1 LEU A   34  GLU A   57  1                                  24    
HELIX    2   2 THR A   62  VAL A   82  1                                  21    
HELIX    3   3 VAL A   82  THR A   92  1                                  11    
HELIX    4   4 SER A   99  MET A  134  1                                  36    
HELIX    5   5 MET A  134  GLY A  141  1                                   8    
HELIX    6   6 SER A  146  PHE A  170  1                                  25    
HELIX    7   7 ASN A  185  PHE A  197  1                                  13    
HELIX    8   8 PHE A  197  GLN A  217  1                                  21    
HELIX    9   9 ASN A 1002  GLY A 1012  1                                  11    
HELIX   10  10 SER A 1038  GLY A 1051  1                                  14    
HELIX   11  11 THR A 1059  ASN A 1081  1                                  23    
HELIX   12  12 LEU A 1084  SER A 1090  1                                   7    
HELIX   13  13 ASP A 1092  ALA A 1112  1                                  21    
HELIX   14  14 PHE A 1114  GLN A 1123  1                                  10    
HELIX   15  15 ARG A 1125  LYS A 1135  1                                  11    
HELIX   16  16 SER A 1136  THR A 1142  1                                   7    
HELIX   17  17 THR A 1142  GLY A 1156  1                                  15    
HELIX   18  18 PRO A  321  HIS A  354  1                                  34    
HELIX   19  19 SER A  361  ASN A  387  1                                  27    
HELIX   20  20 ASN A  387  SER A  399  1                                  13    
HELIX   21  21 LEU B   34  LEU B   55  1                                  22    
HELIX   22  22 GLU B   57  GLN B   61  5                                   5    
HELIX   23  23 THR B   64  VAL B   82  1                                  19    
HELIX   24  24 VAL B   82  THR B   92  1                                  11    
HELIX   25  25 SER B   99  MET B  134  1                                  36    
HELIX   26  26 SER B  145  CYS B  166  1                                  22    
HELIX   27  27 PRO B  167  GLY B  171  5                                   5    
HELIX   28  28 ASN B  185  SER B  196  1                                  12    
HELIX   29  29 PHE B  197  ARG B  219  1                                  23    
HELIX   30  30 ASN B 1002  GLY B 1012  1                                  11    
HELIX   31  31 SER B 1038  GLY B 1051  1                                  14    
HELIX   32  32 THR B 1059  ASN B 1081  1                                  23    
HELIX   33  33 LEU B 1084  LEU B 1091  1                                   8    
HELIX   34  34 ASP B 1092  GLY B 1107  1                                  16    
HELIX   35  35 GLY B 1107  ALA B 1112  1                                   6    
HELIX   36  36 PHE B 1114  GLN B 1123  1                                  10    
HELIX   37  37 ARG B 1125  LEU B 1133  1                                   9    
HELIX   38  38 SER B 1136  THR B 1142  1                                   7    
HELIX   39  39 THR B 1142  GLY B 1156  1                                  15    
HELIX   40  40 PRO B  321  CYS B  355  1                                  35    
HELIX   41  41 SER B  361  ASN B  387  1                                  27    
HELIX   42  42 ASN B  387  LEU B  398  1                                  12    
SHEET    1   A 3 TYR A1018  LYS A1019  0                                        
SHEET    2   A 3 TYR A1025  ILE A1027 -1  O  THR A1026   N  TYR A1018           
SHEET    3   A 3 HIS A1031  THR A1034 -1  O  LEU A1033   N  TYR A1025           
SHEET    1   B 3 ARG B1014  LYS B1019  0                                        
SHEET    2   B 3 TYR B1025  GLY B1028 -1  O  THR B1026   N  TYR B1018           
SHEET    3   B 3 HIS B1031  THR B1034 -1  O  HIS B1031   N  ILE B1027           
SSBOND   1 CYS A  103    CYS A  181                          1555   1555  2.03  
SSBOND   2 CYS A  355    CYS A  358                          1555   1555  2.03  
SSBOND   3 CYS B  103    CYS B  181                          1555   1555  2.06  
SSBOND   4 CYS B  355    CYS B  358                          1555   1555  2.04  
SITE     1 AC1 10 PHE A 106  ASP A 110  VAL A 111  CYS A 114                    
SITE     2 AC1 10 ILE A 183  SER A 192  PHE A 345  HIS A 349                    
SITE     3 AC1 10 THR A 369  TYR A 373                                          
SITE     1 AC2  8 ASP B 110  VAL B 111  CYS B 114  ILE B 183                    
SITE     2 AC2  8 SER B 192  PHE B 345  HIS B 349  TYR B 373                    
SITE     1 AC3 14 GLU A1011  ASP A1020  GLU A1022  THR A1026                    
SITE     2 AC3 14 GLY A1030  HIS A1031  LEU A1032  ASP A1070                    
SITE     3 AC3 14 VAL A1103  PHE A1104  GLN A1105  MET A1106                    
SITE     4 AC3 14 GLY A1107  ARG A1145                                          
SITE     1 AC4 11 GLU B1011  ASP B1020  THR B1026  GLY B1030                    
SITE     2 AC4 11 HIS B1031  LEU B1032  ASP B1070  VAL B1103                    
SITE     3 AC4 11 PHE B1104  GLN B1105  GLY B1107                               
CRYST1   88.828   92.492  176.116  90.00  90.00  90.00 P 21 21 21    8          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.011258  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.010812  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.005678        0.00000                         
ATOM      1  N   TYR A  32      -4.995 -32.674  12.084  1.00125.43           N  
ANISOU    1  N   TYR A  32    22483  14517  10657  -6205  -2180   3633       N  
ATOM      2  CA  TYR A  32      -4.015 -32.114  11.167  1.00120.88           C  
ANISOU    2  CA  TYR A  32    21697  13750  10484  -5427  -2193   3371       C  
ATOM      3  C   TYR A  32      -2.628 -32.600  11.532  1.00124.28           C  
ANISOU    3  C   TYR A  32    22667  13588  10964  -4894  -2462   3375       C  
ATOM      4  O   TYR A  32      -1.723 -31.807  11.712  1.00120.25           O  
ANISOU    4  O   TYR A  32    21834  13172  10685  -4301  -2396   3229       O  
ATOM      5  CB  TYR A  32      -4.047 -30.588  11.213  1.00117.82           C  
ANISOU    5  CB  TYR A  32    20441  13983  10342  -5068  -1864   3174       C  
ATOM      6  CG  TYR A  32      -5.399 -29.916  10.976  1.00119.78           C  
ANISOU    6  CG  TYR A  32    20051  14913  10548  -5476  -1577   3145       C  
ATOM      7  CD1 TYR A  32      -5.917 -29.770   9.704  1.00120.66           C  
ANISOU    7  CD1 TYR A  32    19903  15123  10820  -5501  -1533   3028       C  
ATOM      8  CD2 TYR A  32      -6.119 -29.380  12.025  1.00121.74           C  
ANISOU    8  CD2 TYR A  32    19929  15736  10591  -5781  -1348   3218       C  
ATOM      9  CE1 TYR A  32      -7.112 -29.150   9.496  1.00121.75           C  
ANISOU    9  CE1 TYR A  32    19438  15901  10921  -5816  -1298   3000       C  
ATOM     10  CE2 TYR A  32      -7.311 -28.755  11.819  1.00122.90           C  
ANISOU   10  CE2 TYR A  32    19460  16541  10696  -6071  -1090   3173       C  
ATOM     11  CZ  TYR A  32      -7.802 -28.643  10.556  1.00130.14           C  
ANISOU   11  CZ  TYR A  32    20124  17538  11784  -6080  -1075   3068       C  
ATOM     12  OH  TYR A  32      -9.000 -28.017  10.357  1.00132.47           O  
ANISOU   12  OH  TYR A  32    19780  18521  12032  -6337   -839   3025       O  
ATOM     13  N   ALA A  33      -2.465 -33.911  11.644  1.00124.63           N  
ANISOU   13  N   ALA A  33    23549  13025  10779  -5112  -2786   3545       N  
ATOM     14  CA  ALA A  33      -1.226 -34.474  12.152  1.00125.34           C  
ANISOU   14  CA  ALA A  33    24204  12563  10855  -4631  -3077   3583       C  
ATOM     15  C   ALA A  33      -0.202 -34.883  11.113  1.00127.42           C  
ANISOU   15  C   ALA A  33    24760  12303  11350  -3966  -3287   3399       C  
ATOM     16  O   ALA A  33       0.934 -34.414  11.119  1.00124.56           O  
ANISOU   16  O   ALA A  33    24192  11916  11222  -3264  -3305   3250       O  
ATOM     17  CB  ALA A  33      -1.526 -35.678  12.998  1.00131.96           C  
ANISOU   17  CB  ALA A  33    25872  12988  11279  -5177  -3349   3884       C  
ATOM     18  N   LEU A  34      -0.600 -35.783  10.234  1.00125.79           N  
ANISOU   18  N   LEU A  34    25047  11693  11053  -4200  -3453   3408       N  
ATOM     19  CA  LEU A  34       0.274 -36.199   9.169  1.00124.96           C  
ANISOU   19  CA  LEU A  34    25231  11118  11130  -3579  -3630   3210       C  
ATOM     20  C   LEU A  34      -0.133 -35.381   7.990  1.00123.43           C  
ANISOU   20  C   LEU A  34    24376  11331  11193  -3512  -3358   2995       C  
ATOM     21  O   LEU A  34       0.601 -35.227   7.035  1.00120.96           O  
ANISOU   21  O   LEU A  34    23960  10890  11108  -2926  -3362   2773       O  
ATOM     22  CB  LEU A  34       0.087 -37.666   8.868  1.00130.72           C  
ANISOU   22  CB  LEU A  34    26963  11119  11585  -3853  -3994   3326       C  
ATOM     23  CG  LEU A  34       0.602 -38.469  10.041  1.00139.59           C  
ANISOU   23  CG  LEU A  34    28799  11787  12454  -3843  -4302   3544       C  
ATOM     24  CD1 LEU A  34       2.043 -38.877   9.789  1.00140.42           C  
ANISOU   24  CD1 LEU A  34    29274  11384  12696  -2915  -4561   3387       C  
ATOM     25  CD2 LEU A  34       0.498 -37.582  11.255  1.00139.61           C  
ANISOU   25  CD2 LEU A  34    28236  12364  12446  -3994  -4078   3658       C  
ATOM     26  N   SER A  35      -1.326 -34.833   8.060  1.00118.06           N  
ANISOU   26  N   SER A  35    23222  11179  10458  -4112  -3116   3063       N  
ATOM     27  CA  SER A  35      -1.767 -34.024   6.917  1.00113.78           C  
ANISOU   27  CA  SER A  35    22051  11031  10151  -4046  -2877   2867       C  
ATOM     28  C   SER A  35      -0.727 -32.986   6.525  1.00111.60           C  
ANISOU   28  C   SER A  35    21221  10954  10229  -3268  -2722   2630       C  
ATOM     29  O   SER A  35      -0.363 -32.881   5.354  1.00109.34           O  
ANISOU   29  O   SER A  35    20852  10569  10125  -2905  -2710   2439       O  
ATOM     30  CB  SER A  35      -3.088 -33.311   7.232  1.00116.49           C  
ANISOU   30  CB  SER A  35    21791  12051  10418  -4661  -2603   2953       C  
ATOM     31  OG  SER A  35      -4.137 -34.243   7.438  1.00129.89           O  
ANISOU   31  OG  SER A  35    23922  13652  11779  -5460  -2727   3172       O  
ATOM     32  N   TYR A  36      -0.256 -32.226   7.513  1.00105.54           N  
ANISOU   32  N   TYR A  36    20092  10475   9532  -3050  -2607   2650       N  
ATOM     33  CA  TYR A  36       0.739 -31.172   7.281  1.00100.79           C  
ANISOU   33  CA  TYR A  36    18951  10102   9243  -2389  -2468   2453       C  
ATOM     34  C   TYR A  36       2.026 -31.708   6.642  1.00104.27           C  
ANISOU   34  C   TYR A  36    19726  10089   9804  -1738  -2668   2321       C  
ATOM     35  O   TYR A  36       2.578 -31.086   5.735  1.00101.09           O  
ANISOU   35  O   TYR A  36    18939   9827   9643  -1303  -2552   2124       O  
ATOM     36  CB  TYR A  36       1.056 -30.403   8.580  1.00100.68           C  
ANISOU   36  CB  TYR A  36    18618  10407   9230  -2316  -2371   2516       C  
ATOM     37  CG  TYR A  36       0.145 -29.203   8.824  1.00 99.79           C  
ANISOU   37  CG  TYR A  36    17824  10928   9165  -2597  -2056   2488       C  
ATOM     38  CD1 TYR A  36      -0.994 -29.317   9.625  1.00103.94           C  
ANISOU   38  CD1 TYR A  36    18349  11715   9431  -3212  -1968   2654       C  
ATOM     39  CD2 TYR A  36       0.422 -27.954   8.247  1.00 96.22           C  
ANISOU   39  CD2 TYR A  36    16742  10821   8996  -2237  -1851   2294       C  
ATOM     40  CE1 TYR A  36      -1.839 -28.218   9.848  1.00102.70           C  
ANISOU   40  CE1 TYR A  36    17555  12166   9300  -3397  -1677   2604       C  
ATOM     41  CE2 TYR A  36      -0.418 -26.851   8.464  1.00 95.01           C  
ANISOU   41  CE2 TYR A  36    16018  11207   8874  -2434  -1589   2254       C  
ATOM     42  CZ  TYR A  36      -1.545 -26.994   9.267  1.00104.01           C  
ANISOU   42  CZ  TYR A  36    17148  12615   9758  -2981  -1501   2397       C  
ATOM     43  OH  TYR A  36      -2.381 -25.925   9.492  1.00102.57           O  
ANISOU   43  OH  TYR A  36    16397  12987   9586  -3110  -1242   2336       O  
ATOM     44  N   CYS A  37       2.488 -32.864   7.101  1.00104.01           N  
ANISOU   44  N   CYS A  37    20413   9525   9582  -1666  -2970   2430       N  
ATOM     45  CA  CYS A  37       3.686 -33.481   6.538  1.00104.94           C  
ANISOU   45  CA  CYS A  37    20890   9207   9774  -1001  -3181   2297       C  
ATOM     46  C   CYS A  37       3.493 -33.839   5.065  1.00107.92           C  
ANISOU   46  C   CYS A  37    21406   9396  10203   -915  -3177   2130       C  
ATOM     47  O   CYS A  37       4.416 -33.694   4.265  1.00106.56           O  
ANISOU   47  O   CYS A  37    21094   9192  10203   -304  -3162   1928       O  
ATOM     48  CB  CYS A  37       4.051 -34.713   7.351  1.00110.28           C  
ANISOU   48  CB  CYS A  37    22397   9310  10194   -981  -3540   2463       C  
ATOM     49  SG  CYS A  37       3.862 -34.388   9.107  1.00114.51           S  
ANISOU   49  SG  CYS A  37    22854  10083  10571  -1335  -3536   2711       S  
ATOM     50  N   ALA A  38       2.292 -34.299   4.716  1.00105.15           N  
ANISOU   50  N   ALA A  38    21314   8954   9682  -1549  -3190   2216       N  
ATOM     51  CA  ALA A  38       1.932 -34.555   3.321  1.00104.67           C  
ANISOU   51  CA  ALA A  38    21355   8768   9647  -1574  -3177   2065       C  
ATOM     52  C   ALA A  38       2.061 -33.272   2.506  1.00102.54           C  
ANISOU   52  C   ALA A  38    20254   9037   9668  -1304  -2865   1875       C  
ATOM     53  O   ALA A  38       2.678 -33.251   1.439  1.00101.38           O  
ANISOU   53  O   ALA A  38    20075   8805   9639   -842  -2845   1674       O  
ATOM     54  CB  ALA A  38       0.511 -35.095   3.230  1.00107.79           C  
ANISOU   54  CB  ALA A  38    22043   9106   9807  -2409  -3228   2221       C  
ATOM     55  N   LEU A  39       1.480 -32.199   3.028  1.00 95.29           N  
ANISOU   55  N   LEU A  39    18692   8671   8843  -1588  -2625   1940       N  
ATOM     56  CA  LEU A  39       1.535 -30.902   2.374  1.00 90.25           C  
ANISOU   56  CA  LEU A  39    17298   8530   8462  -1378  -2348   1788       C  
ATOM     57  C   LEU A  39       2.982 -30.444   2.250  1.00 91.63           C  
ANISOU   57  C   LEU A  39    17248   8729   8839   -657  -2320   1642       C  
ATOM     58  O   LEU A  39       3.394 -29.979   1.194  1.00 89.53           O  
ANISOU   58  O   LEU A  39    16704   8586   8729   -333  -2208   1470       O  
ATOM     59  CB  LEU A  39       0.717 -29.874   3.156  1.00 87.92           C  
ANISOU   59  CB  LEU A  39    16434   8773   8198  -1752  -2132   1885       C  
ATOM     60  CG  LEU A  39       0.328 -28.617   2.385  1.00 88.93           C  
ANISOU   60  CG  LEU A  39    15877   9381   8531  -1708  -1876   1758       C  
ATOM     61  CD1 LEU A  39      -0.758 -28.943   1.369  1.00 90.17           C  
ANISOU   61  CD1 LEU A  39    16102   9551   8608  -2104  -1878   1746       C  
ATOM     62  CD2 LEU A  39      -0.136 -27.532   3.343  1.00 89.61           C  
ANISOU   62  CD2 LEU A  39    15436   9954   8659  -1873  -1684   1817       C  
ATOM     63  N   ILE A  40       3.746 -30.591   3.329  1.00 88.69           N  
ANISOU   63  N   ILE A  40    16993   8264   8442   -432  -2431   1720       N  
ATOM     64  CA  ILE A  40       5.170 -30.248   3.335  1.00 87.54           C  
ANISOU   64  CA  ILE A  40    16632   8169   8460    233  -2441   1602       C  
ATOM     65  C   ILE A  40       5.896 -30.798   2.116  1.00 92.59           C  
ANISOU   65  C   ILE A  40    17482   8562   9137    717  -2507   1416       C  
ATOM     66  O   ILE A  40       6.587 -30.056   1.419  1.00 90.04           O  
ANISOU   66  O   ILE A  40    16689   8524   8996   1093  -2350   1263       O  
ATOM     67  CB  ILE A  40       5.885 -30.762   4.614  1.00 93.15           C  
ANISOU   67  CB  ILE A  40    17655   8668   9068    414  -2658   1727       C  
ATOM     68  CG1 ILE A  40       5.728 -29.750   5.755  1.00 91.04           C  
ANISOU   68  CG1 ILE A  40    16927   8815   8848    201  -2525   1830       C  
ATOM     69  CG2 ILE A  40       7.370 -31.041   4.345  1.00 95.38           C  
ANISOU   69  CG2 ILE A  40    17981   8818   9440   1157  -2786   1594       C  
ATOM     70  CD1 ILE A  40       6.240 -30.244   7.102  1.00 99.98           C  
ANISOU   70  CD1 ILE A  40    18391   9762   9836    267  -2743   1983       C  
ATOM     71  N   LEU A  41       5.739 -32.093   1.856  1.00 93.03           N  
ANISOU   71  N   LEU A  41    18265   8088   8995    697  -2741   1427       N  
ATOM     72  CA  LEU A  41       6.405 -32.712   0.707  1.00 94.81           C  
ANISOU   72  CA  LEU A  41    18772   8042   9211   1193  -2816   1227       C  
ATOM     73  C   LEU A  41       5.788 -32.223  -0.608  1.00 95.91           C  
ANISOU   73  C   LEU A  41    18630   8392   9418   1016  -2611   1097       C  
ATOM     74  O   LEU A  41       6.515 -31.887  -1.544  1.00 94.78           O  
ANISOU   74  O   LEU A  41    18221   8406   9385   1472  -2492    908       O  
ATOM     75  CB  LEU A  41       6.386 -34.244   0.804  1.00100.31           C  
ANISOU   75  CB  LEU A  41    20415   8049   9650   1230  -3155   1264       C  
ATOM     76  CG  LEU A  41       6.953 -34.830   2.106  1.00107.95           C  
ANISOU   76  CG  LEU A  41    21763   8742  10512   1396  -3408   1414       C  
ATOM     77  CD1 LEU A  41       7.231 -36.328   1.956  1.00114.13           C  
ANISOU   77  CD1 LEU A  41    23516   8793  11056   1650  -3767   1390       C  
ATOM     78  CD2 LEU A  41       8.215 -34.093   2.564  1.00108.83           C  
ANISOU   78  CD2 LEU A  41    21306   9224  10819   1991  -3332   1351       C  
ATOM     79  N   ALA A  42       4.459 -32.150  -0.664  1.00 91.06           N  
ANISOU   79  N   ALA A  42    18039   7830   8728    352  -2567   1205       N  
ATOM     80  CA  ALA A  42       3.760 -31.648  -1.854  1.00 88.58           C  
ANISOU   80  CA  ALA A  42    17446   7743   8468    138  -2397   1106       C  
ATOM     81  C   ALA A  42       4.311 -30.299  -2.334  1.00 87.35           C  
ANISOU   81  C   ALA A  42    16523   8106   8560    451  -2125    991       C  
ATOM     82  O   ALA A  42       4.439 -30.061  -3.536  1.00 86.23           O  
ANISOU   82  O   ALA A  42    16248   8053   8462    624  -2022    837       O  
ATOM     83  CB  ALA A  42       2.268 -31.536  -1.574  1.00 88.88           C  
ANISOU   83  CB  ALA A  42    17437   7920   8414   -621  -2371   1270       C  
ATOM     84  N   ILE A  43       4.644 -29.429  -1.385  1.00 80.65           N  
ANISOU   84  N   ILE A  43    15213   7582   7847    499  -2022   1069       N  
ATOM     85  CA  ILE A  43       5.165 -28.096  -1.688  1.00 76.47           C  
ANISOU   85  CA  ILE A  43    13996   7523   7535    727  -1791    989       C  
ATOM     86  C   ILE A  43       6.616 -28.117  -2.181  1.00 79.81           C  
ANISOU   86  C   ILE A  43    14325   7966   8034   1370  -1780    837       C  
ATOM     87  O   ILE A  43       6.942 -27.485  -3.187  1.00 77.51           O  
ANISOU   87  O   ILE A  43    13697   7919   7834   1548  -1617    714       O  
ATOM     88  CB  ILE A  43       5.050 -27.173  -0.455  1.00 77.38           C  
ANISOU   88  CB  ILE A  43    13707   7951   7742    552  -1711   1116       C  
ATOM     89  CG1 ILE A  43       3.573 -26.859  -0.184  1.00 76.67           C  
ANISOU   89  CG1 ILE A  43    13523   8014   7594    -43  -1642   1227       C  
ATOM     90  CG2 ILE A  43       5.843 -25.880  -0.667  1.00 75.55           C  
ANISOU   90  CG2 ILE A  43    12865   8124   7716    837  -1530   1036       C  
ATOM     91  CD1 ILE A  43       3.330 -26.070   1.086  1.00 81.40           C  
ANISOU   91  CD1 ILE A  43    13807   8895   8228   -226  -1566   1338       C  
ATOM     92  N   VAL A  44       7.483 -28.840  -1.476  1.00 78.54           N  
ANISOU   92  N   VAL A  44    14450   7575   7818   1717  -1955    852       N  
ATOM     93  CA  VAL A  44       8.884 -28.968  -1.896  1.00 79.67           C  
ANISOU   93  CA  VAL A  44    14486   7777   8007   2371  -1959    702       C  
ATOM     94  C   VAL A  44       8.984 -29.747  -3.213  1.00 85.98           C  
ANISOU   94  C   VAL A  44    15641   8334   8691   2629  -1978    522       C  
ATOM     95  O   VAL A  44       9.943 -29.574  -3.968  1.00 86.32           O  
ANISOU   95  O   VAL A  44    15444   8579   8775   3107  -1875    361       O  
ATOM     96  CB  VAL A  44       9.766 -29.656  -0.823  1.00 86.11           C  
ANISOU   96  CB  VAL A  44    15560   8389   8769   2732  -2186    757       C  
ATOM     97  CG1 VAL A  44      11.230 -29.669  -1.258  1.00 87.71           C  
ANISOU   97  CG1 VAL A  44    15519   8779   9027   3432  -2169    597       C  
ATOM     98  CG2 VAL A  44       9.629 -28.952   0.517  1.00 83.72           C  
ANISOU   98  CG2 VAL A  44    14972   8298   8539   2452  -2185    935       C  
ATOM     99  N   PHE A  45       7.992 -30.595  -3.483  1.00 83.90           N  
ANISOU   99  N   PHE A  45    15950   7664   8265   2291  -2108    547       N  
ATOM    100  CA  PHE A  45       7.926 -31.358  -4.728  1.00 86.17           C  
ANISOU  100  CA  PHE A  45    16659   7672   8409   2459  -2149    374       C  
ATOM    101  C   PHE A  45       7.578 -30.457  -5.918  1.00 86.41           C  
ANISOU  101  C   PHE A  45    16241   8071   8518   2317  -1897    280       C  
ATOM    102  O   PHE A  45       8.401 -30.268  -6.815  1.00 86.56           O  
ANISOU  102  O   PHE A  45    16064   8275   8551   2758  -1770    106       O  
ATOM    103  CB  PHE A  45       6.904 -32.497  -4.586  1.00 90.89           C  
ANISOU  103  CB  PHE A  45    18027   7717   8792   2037  -2394    456       C  
ATOM    104  CG  PHE A  45       6.869 -33.448  -5.756  1.00 96.02           C  
ANISOU  104  CG  PHE A  45    19261   7972   9251   2220  -2501    271       C  
ATOM    105  CD1 PHE A  45       7.963 -34.255  -6.049  1.00103.16           C  
ANISOU  105  CD1 PHE A  45    20544   8596  10057   2923  -2622     89       C  
ATOM    106  CD2 PHE A  45       5.730 -33.557  -6.546  1.00 97.84           C  
ANISOU  106  CD2 PHE A  45    19679   8114   9382   1703  -2498    271       C  
ATOM    107  CE1 PHE A  45       7.929 -35.137  -7.120  1.00107.74           C  
ANISOU  107  CE1 PHE A  45    21713   8789  10434   3121  -2724   -107       C  
ATOM    108  CE2 PHE A  45       5.690 -34.440  -7.616  1.00104.22           C  
ANISOU  108  CE2 PHE A  45    21074   8536   9990   1851  -2616     92       C  
ATOM    109  CZ  PHE A  45       6.792 -35.230  -7.903  1.00106.29           C  
ANISOU  109  CZ  PHE A  45    21747   8492  10145   2567  -2724   -105       C  
ATOM    110  N   GLY A  46       6.374 -29.889  -5.912  1.00 79.30           N  
ANISOU  110  N   GLY A  46    15166   7310   7654   1714  -1828    400       N  
ATOM    111  CA  GLY A  46       5.879 -29.118  -7.051  1.00 76.47           C  
ANISOU  111  CA  GLY A  46    14474   7241   7341   1537  -1641    331       C  
ATOM    112  C   GLY A  46       6.717 -27.899  -7.397  1.00 77.19           C  
ANISOU  112  C   GLY A  46    13898   7825   7607   1823  -1402    272       C  
ATOM    113  O   GLY A  46       7.131 -27.721  -8.546  1.00 76.91           O  
ANISOU  113  O   GLY A  46    13761   7922   7540   2057  -1281    127       O  
ATOM    114  N   ASN A  47       6.966 -27.060  -6.394  1.00 71.44           N  
ANISOU  114  N   ASN A  47    12739   7368   7037   1775  -1339    391       N  
ATOM    115  CA  ASN A  47       7.722 -25.813  -6.579  1.00 68.72           C  
ANISOU  115  CA  ASN A  47    11772   7487   6853   1950  -1137    370       C  
ATOM    116  C   ASN A  47       9.226 -26.081  -6.746  1.00 74.06           C  
ANISOU  116  C   ASN A  47    12360   8257   7523   2542  -1115    247       C  
ATOM    117  O   ASN A  47       9.963 -25.239  -7.256  1.00 72.45           O  
ANISOU  117  O   ASN A  47    11695   8438   7393   2711   -942    197       O  
ATOM    118  CB  ASN A  47       7.478 -24.837  -5.412  1.00 66.47           C  
ANISOU  118  CB  ASN A  47    11109   7431   6715   1690  -1104    526       C  
ATOM    119  CG  ASN A  47       6.005 -24.410  -5.282  1.00 86.38           C  
ANISOU  119  CG  ASN A  47    13602   9977   9243   1156  -1088    629       C  
ATOM    120  OD1 ASN A  47       5.651 -23.251  -5.535  1.00 77.65           O  
ANISOU  120  OD1 ASN A  47    12097   9166   8238    992   -954    653       O  
ATOM    121  ND2 ASN A  47       5.150 -25.343  -4.872  1.00 79.90           N  
ANISOU  121  ND2 ASN A  47    13205   8857   8296    886  -1235    695       N  
ATOM    122  N   GLY A  48       9.669 -27.255  -6.299  1.00 73.35           N  
ANISOU  122  N   GLY A  48    12714   7828   7328   2849  -1302    208       N  
ATOM    123  CA  GLY A  48      11.013 -27.742  -6.590  1.00 76.05           C  
ANISOU  123  CA  GLY A  48    13046   8229   7620   3488  -1308     57       C  
ATOM    124  C   GLY A  48      11.145 -28.074  -8.063  1.00 81.13           C  
ANISOU  124  C   GLY A  48    13829   8868   8130   3714  -1201   -140       C  
ATOM    125  O   GLY A  48      12.214 -27.896  -8.647  1.00 82.55           O  
ANISOU  125  O   GLY A  48    13708   9363   8293   4159  -1066   -273       O  
ATOM    126  N   LEU A  49      10.055 -28.561  -8.663  1.00 76.94           N  
ANISOU  126  N   LEU A  49    13744   8009   7482   3391  -1263   -158       N  
ATOM    127  CA  LEU A  49      10.003 -28.804 -10.105  1.00 77.65           C  
ANISOU  127  CA  LEU A  49    13995   8084   7423   3516  -1166   -339       C  
ATOM    128  C   LEU A  49       9.909 -27.494 -10.864  1.00 77.49           C  
ANISOU  128  C   LEU A  49    13391   8556   7497   3297   -910   -318       C  
ATOM    129  O   LEU A  49      10.715 -27.231 -11.752  1.00 78.11           O  
ANISOU  129  O   LEU A  49    13226   8933   7518   3622   -735   -454       O  
ATOM    130  CB  LEU A  49       8.813 -29.691 -10.482  1.00 78.80           C  
ANISOU  130  CB  LEU A  49    14803   7733   7404   3166  -1344   -348       C  
ATOM    131  CG  LEU A  49       9.015 -31.200 -10.363  1.00 88.11           C  
ANISOU  131  CG  LEU A  49    16757   8339   8382   3482  -1598   -458       C  
ATOM    132  CD1 LEU A  49       7.695 -31.915 -10.590  1.00 89.02           C  
ANISOU  132  CD1 LEU A  49    17484   7995   8345   2953  -1790   -408       C  
ATOM    133  CD2 LEU A  49      10.070 -31.683 -11.349  1.00 94.50           C  
ANISOU  133  CD2 LEU A  49    17688   9177   9041   4162  -1523   -728       C  
ATOM    134  N   VAL A  50       8.923 -26.675 -10.512  1.00 70.09           N  
ANISOU  134  N   VAL A  50    12238   7708   6683   2755   -892   -148       N  
ATOM    135  CA  VAL A  50       8.729 -25.374 -11.163  1.00 66.78           C  
ANISOU  135  CA  VAL A  50    11322   7699   6353   2520   -691   -104       C  
ATOM    136  C   VAL A  50      10.059 -24.646 -11.363  1.00 70.51           C  
ANISOU  136  C   VAL A  50    11290   8619   6883   2865   -502   -150       C  
ATOM    137  O   VAL A  50      10.308 -24.090 -12.427  1.00 69.82           O  
ANISOU  137  O   VAL A  50    10986   8807   6738   2889   -330   -213       O  
ATOM    138  CB  VAL A  50       7.755 -24.476 -10.363  1.00 66.86           C  
ANISOU  138  CB  VAL A  50    11085   7795   6523   2022   -710     92       C  
ATOM    139  CG1 VAL A  50       7.905 -23.017 -10.756  1.00 63.84           C  
ANISOU  139  CG1 VAL A  50    10164   7837   6255   1898   -526    147       C  
ATOM    140  CG2 VAL A  50       6.320 -24.944 -10.557  1.00 66.55           C  
ANISOU  140  CG2 VAL A  50    11405   7480   6400   1599   -836    136       C  
ATOM    141  N   CYS A  51      10.912 -24.669 -10.345  1.00 67.79           N  
ANISOU  141  N   CYS A  51    10761   8365   6631   3107   -545   -111       N  
ATOM    142  CA  CYS A  51      12.238 -24.073 -10.448  1.00 68.70           C  
ANISOU  142  CA  CYS A  51    10375   8941   6786   3422   -392   -148       C  
ATOM    143  C   CYS A  51      13.131 -24.857 -11.398  1.00 76.47           C  
ANISOU  143  C   CYS A  51    11470  10000   7584   3952   -313   -362       C  
ATOM    144  O   CYS A  51      13.808 -24.271 -12.235  1.00 76.55           O  
ANISOU  144  O   CYS A  51    11108  10437   7540   4063   -104   -423       O  
ATOM    145  CB  CYS A  51      12.890 -23.987  -9.072  1.00 69.14           C  
ANISOU  145  CB  CYS A  51    10229   9069   6971   3545   -498    -52       C  
ATOM    146  SG  CYS A  51      11.967 -22.945  -7.916  1.00 68.63           S  
ANISOU  146  SG  CYS A  51     9990   8988   7097   2971   -558    175       S  
ATOM    147  N   MET A  52      13.129 -26.179 -11.265  1.00 76.37           N  
ANISOU  147  N   MET A  52    11993   9574   7451   4279   -484   -478       N  
ATOM    148  CA  MET A  52      13.912 -27.044 -12.152  1.00 81.02           C  
ANISOU  148  CA  MET A  52    12781  10172   7832   4855   -432   -718       C  
ATOM    149  C   MET A  52      13.571 -26.815 -13.634  1.00 84.62           C  
ANISOU  149  C   MET A  52    13276  10745   8130   4741   -247   -832       C  
ATOM    150  O   MET A  52      14.464 -26.795 -14.484  1.00 87.05           O  
ANISOU  150  O   MET A  52    13365  11411   8299   5123    -57   -990       O  
ATOM    151  CB  MET A  52      13.693 -28.525 -11.800  1.00 86.86           C  
ANISOU  151  CB  MET A  52    14256  10301   8444   5145   -698   -816       C  
ATOM    152  CG  MET A  52      14.391 -29.008 -10.525  1.00 92.56           C  
ANISOU  152  CG  MET A  52    15002  10924   9244   5487   -887   -765       C  
ATOM    153  SD  MET A  52      15.977 -29.848 -10.795  1.00103.45           S  
ANISOU  153  SD  MET A  52    16350  12487  10469   6459   -883  -1019       S  
ATOM    154  CE  MET A  52      15.524 -31.197 -11.891  1.00104.41           C  
ANISOU  154  CE  MET A  52    17348  12032  10291   6753   -982  -1278       C  
ATOM    155  N   ALA A  53      12.285 -26.641 -13.933  1.00 78.00           N  
ANISOU  155  N   ALA A  53    12697   9644   7295   4218   -304   -749       N  
ATOM    156  CA  ALA A  53      11.829 -26.490 -15.311  1.00 77.92           C  
ANISOU  156  CA  ALA A  53    12800   9687   7120   4074   -179   -844       C  
ATOM    157  C   ALA A  53      12.411 -25.237 -15.957  1.00 81.03           C  
ANISOU  157  C   ALA A  53    12568  10683   7537   3998     95   -802       C  
ATOM    158  O   ALA A  53      13.022 -25.310 -17.016  1.00 83.20           O  
ANISOU  158  O   ALA A  53    12781  11213   7617   4271    273   -959       O  
ATOM    159  CB  ALA A  53      10.312 -26.454 -15.361  1.00 75.88           C  
ANISOU  159  CB  ALA A  53    12859   9087   6885   3495   -323   -729       C  
ATOM    160  N   VAL A  54      12.225 -24.099 -15.295  1.00 74.46           N  
ANISOU  160  N   VAL A  54    11303  10066   6921   3620    121   -589       N  
ATOM    161  CA  VAL A  54      12.674 -22.792 -15.795  1.00 73.04           C  
ANISOU  161  CA  VAL A  54    10577  10402   6773   3435    338   -501       C  
ATOM    162  C   VAL A  54      14.182 -22.705 -15.970  1.00 80.31           C  
ANISOU  162  C   VAL A  54    11078  11815   7619   3859    523   -591       C  
ATOM    163  O   VAL A  54      14.674 -22.278 -17.013  1.00 81.42           O  
ANISOU  163  O   VAL A  54    10995  12339   7602   3892    739   -647       O  
ATOM    164  CB  VAL A  54      12.253 -21.653 -14.834  1.00 72.76           C  
ANISOU  164  CB  VAL A  54    10223  10436   6985   2999    283   -266       C  
ATOM    165  CG1 VAL A  54      13.083 -20.396 -15.085  1.00 72.27           C  
ANISOU  165  CG1 VAL A  54     9604  10902   6953   2888    473   -175       C  
ATOM    166  CG2 VAL A  54      10.762 -21.371 -14.965  1.00 69.54           C  
ANISOU  166  CG2 VAL A  54    10066   9734   6622   2539    172   -170       C  
ATOM    167  N   LEU A  55      14.908 -23.099 -14.934  1.00 78.60           N  
ANISOU  167  N   LEU A  55    10739  11623   7503   4166    435   -594       N  
ATOM    168  CA  LEU A  55      16.366 -23.030 -14.947  1.00 82.17           C  
ANISOU  168  CA  LEU A  55    10720  12602   7900   4583    584   -668       C  
ATOM    169  C   LEU A  55      16.957 -23.852 -16.100  1.00 91.67           C  
ANISOU  169  C   LEU A  55    12063  13948   8819   5092    736   -927       C  
ATOM    170  O   LEU A  55      17.934 -23.428 -16.720  1.00 94.10           O  
ANISOU  170  O   LEU A  55    11906  14845   9004   5258    973   -981       O  
ATOM    171  CB  LEU A  55      16.938 -23.463 -13.585  1.00 83.00           C  
ANISOU  171  CB  LEU A  55    10743  12641   8150   4863    405   -634       C  
ATOM    172  CG  LEU A  55      16.597 -22.484 -12.441  1.00 83.56           C  
ANISOU  172  CG  LEU A  55    10567  12711   8471   4385    300   -389       C  
ATOM    173  CD1 LEU A  55      16.509 -23.175 -11.079  1.00 83.47           C  
ANISOU  173  CD1 LEU A  55    10794  12342   8580   4537     42   -345       C  
ATOM    174  CD2 LEU A  55      17.583 -21.312 -12.398  1.00 86.42           C  
ANISOU  174  CD2 LEU A  55    10242  13710   8883   4247    460   -284       C  
ATOM    175  N   LYS A  56      16.341 -24.994 -16.413  1.00 90.05           N  
ANISOU  175  N   LYS A  56    12508  13219   8487   5306    602  -1086       N  
ATOM    176  CA  LYS A  56      16.831 -25.878 -17.482  1.00 94.97           C  
ANISOU  176  CA  LYS A  56    13378  13892   8813   5837    717  -1368       C  
ATOM    177  C   LYS A  56      16.242 -25.559 -18.863  1.00 98.65           C  
ANISOU  177  C   LYS A  56    13996  14407   9080   5556    878  -1421       C  
ATOM    178  O   LYS A  56      16.984 -25.412 -19.834  1.00101.49           O  
ANISOU  178  O   LYS A  56    14106  15237   9217   5795   1133  -1555       O  
ATOM    179  CB  LYS A  56      16.576 -27.353 -17.129  1.00100.32           C  
ANISOU  179  CB  LYS A  56    14762  13940   9413   6261    459  -1535       C  
ATOM    180  CG  LYS A  56      17.668 -27.994 -16.273  1.00118.07           C  
ANISOU  180  CG  LYS A  56    16883  16281  11695   6899    368  -1619       C  
ATOM    181  CD  LYS A  56      18.894 -28.346 -17.113  1.00134.14           C  
ANISOU  181  CD  LYS A  56    18666  18819  13481   7593    595  -1883       C  
ATOM    182  CE  LYS A  56      20.030 -28.907 -16.269  1.00149.49           C  
ANISOU  182  CE  LYS A  56    20395  20943  15460   8269    498  -1963       C  
ATOM    183  NZ  LYS A  56      21.124 -29.441 -17.132  1.00165.61           N  
ANISOU  183  NZ  LYS A  56    22274  23431  17219   9038    702  -2267       N  
ATOM    184  N   GLU A  57      14.918 -25.455 -18.946  1.00 91.88           N  
ANISOU  184  N   GLU A  57    13528  13100   8282   5050    727  -1315       N  
ATOM    185  CA  GLU A  57      14.225 -25.270 -20.227  1.00 91.68           C  
ANISOU  185  CA  GLU A  57    13737  13041   8058   4780    816  -1364       C  
ATOM    186  C   GLU A  57      14.432 -23.869 -20.833  1.00 94.08           C  
ANISOU  186  C   GLU A  57    13490  13895   8360   4405   1053  -1210       C  
ATOM    187  O   GLU A  57      13.966 -22.868 -20.272  1.00 89.57           O  
ANISOU  187  O   GLU A  57    12658  13359   8016   3928   1000   -967       O  
ATOM    188  CB  GLU A  57      12.728 -25.531 -20.044  1.00 90.03           C  
ANISOU  188  CB  GLU A  57    14041  12240   7926   4324    556  -1272       C  
ATOM    189  CG  GLU A  57      11.970 -25.754 -21.337  1.00100.87           C  
ANISOU  189  CG  GLU A  57    15823  13452   9050   4148    564  -1377       C  
ATOM    190  CD  GLU A  57      12.187 -27.134 -21.903  1.00123.86           C  
ANISOU  190  CD  GLU A  57    19335  16046  11681   4635    504  -1673       C  
ATOM    191  OE1 GLU A  57      12.111 -28.115 -21.130  1.00119.76           O  
ANISOU  191  OE1 GLU A  57    19215  15081  11207   4855    284  -1733       O  
ATOM    192  OE2 GLU A  57      12.429 -27.237 -23.122  1.00120.33           O  
ANISOU  192  OE2 GLU A  57    18997  15778  10947   4796    666  -1846       O  
ATOM    193  N   ARG A  58      15.113 -23.814 -21.983  1.00 94.18           N  
ANISOU  193  N   ARG A  58    13372  14321   8092   4622   1307  -1355       N  
ATOM    194  CA  ARG A  58      15.381 -22.551 -22.698  1.00 93.41           C  
ANISOU  194  CA  ARG A  58    12814  14755   7923   4261   1540  -1211       C  
ATOM    195  C   ARG A  58      14.107 -21.742 -22.937  1.00 92.61           C  
ANISOU  195  C   ARG A  58    12877  14395   7915   3620   1416  -1005       C  
ATOM    196  O   ARG A  58      14.057 -20.542 -22.654  1.00 89.42           O  
ANISOU  196  O   ARG A  58    12104  14204   7666   3209   1442   -770       O  
ATOM    197  CB  ARG A  58      16.055 -22.830 -24.050  1.00 99.39           C  
ANISOU  197  CB  ARG A  58    13569  15904   8291   4569   1813  -1425       C  
ATOM    198  CG  ARG A  58      16.436 -21.574 -24.855  1.00112.09           C  
ANISOU  198  CG  ARG A  58    14721  18101   9765   4186   2071  -1270       C  
ATOM    199  CD  ARG A  58      17.033 -21.931 -26.223  1.00129.41           C  
ANISOU  199  CD  ARG A  58    16956  20687  11526   4486   2353  -1494       C  
ATOM    200  NE  ARG A  58      16.021 -21.964 -27.288  1.00140.16           N  
ANISOU  200  NE  ARG A  58    18823  21749  12683   4209   2302  -1522       N  
ATOM    201  CZ  ARG A  58      16.139 -21.397 -28.497  1.00158.76           C  
ANISOU  201  CZ  ARG A  58    21114  24479  14730   3996   2520  -1504       C  
ATOM    202  NH1 ARG A  58      17.245 -20.742 -28.866  1.00149.48           N  
ANISOU  202  NH1 ARG A  58    19380  24029  13385   3999   2835  -1456       N  
ATOM    203  NH2 ARG A  58      15.137 -21.503 -29.368  1.00145.87           N  
ANISOU  203  NH2 ARG A  58    19986  22510  12927   3755   2415  -1528       N  
ATOM    204  N   ALA A  59      13.088 -22.413 -23.466  1.00 88.56           N  
ANISOU  204  N   ALA A  59    12932  13424   7291   3553   1265  -1100       N  
ATOM    205  CA  ALA A  59      11.818 -21.778 -23.802  1.00 84.78           C  
ANISOU  205  CA  ALA A  59    12630  12719   6865   3005   1127   -935       C  
ATOM    206  C   ALA A  59      11.180 -21.068 -22.607  1.00 83.65           C  
ANISOU  206  C   ALA A  59    12296  12410   7078   2641    948   -691       C  
ATOM    207  O   ALA A  59      10.673 -19.956 -22.742  1.00 80.73           O  
ANISOU  207  O   ALA A  59    11744  12138   6789   2226    934   -495       O  
ATOM    208  CB  ALA A  59      10.861 -22.811 -24.369  1.00 86.63           C  
ANISOU  208  CB  ALA A  59    13509  12473   6935   3018    948  -1090       C  
ATOM    209  N   LEU A  60      11.231 -21.703 -21.439  1.00 79.35           N  
ANISOU  209  N   LEU A  60    11812  11615   6722   2822    808   -709       N  
ATOM    210  CA  LEU A  60      10.559 -21.183 -20.248  1.00 74.98           C  
ANISOU  210  CA  LEU A  60    11139  10878   6474   2508    633   -508       C  
ATOM    211  C   LEU A  60      11.272 -20.012 -19.570  1.00 76.70           C  
ANISOU  211  C   LEU A  60    10801  11465   6874   2393    734   -335       C  
ATOM    212  O   LEU A  60      10.770 -19.483 -18.583  1.00 72.88           O  
ANISOU  212  O   LEU A  60    10209  10857   6625   2149    604   -179       O  
ATOM    213  CB  LEU A  60      10.356 -22.305 -19.227  1.00 75.27           C  
ANISOU  213  CB  LEU A  60    11479  10509   6611   2708    439   -576       C  
ATOM    214  CG  LEU A  60       9.319 -23.358 -19.603  1.00 80.98           C  
ANISOU  214  CG  LEU A  60    12808  10755   7204   2638    249   -679       C  
ATOM    215  CD1 LEU A  60       9.333 -24.474 -18.580  1.00 82.01           C  
ANISOU  215  CD1 LEU A  60    13258  10503   7401   2851     66   -735       C  
ATOM    216  CD2 LEU A  60       7.926 -22.749 -19.715  1.00 80.62           C  
ANISOU  216  CD2 LEU A  60    12811  10584   7239   2101    117   -518       C  
ATOM    217  N   GLN A  61      12.423 -19.595 -20.094  1.00 75.87           N  
ANISOU  217  N   GLN A  61    10352  11831   6644   2544    962   -363       N  
ATOM    218  CA  GLN A  61      13.208 -18.513 -19.480  1.00 75.01           C  
ANISOU  218  CA  GLN A  61     9725  12099   6678   2401   1048   -198       C  
ATOM    219  C   GLN A  61      12.727 -17.094 -19.862  1.00 76.71           C  
ANISOU  219  C   GLN A  61     9799  12425   6923   1894   1059     13       C  
ATOM    220  O   GLN A  61      13.486 -16.309 -20.442  1.00 78.18           O  
ANISOU  220  O   GLN A  61     9687  13031   6986   1771   1236     83       O  
ATOM    221  CB  GLN A  61      14.691 -18.688 -19.835  1.00 80.53           C  
ANISOU  221  CB  GLN A  61    10069  13318   7211   2752   1282   -307       C  
ATOM    222  CG  GLN A  61      15.339 -19.876 -19.152  1.00 96.05           C  
ANISOU  222  CG  GLN A  61    12079  15215   9200   3295   1236   -481       C  
ATOM    223  CD  GLN A  61      16.710 -20.207 -19.714  1.00120.20           C  
ANISOU  223  CD  GLN A  61    14815  18815  12040   3736   1478   -639       C  
ATOM    224  OE1 GLN A  61      17.393 -19.347 -20.278  1.00117.15           O  
ANISOU  224  OE1 GLN A  61    14006  18965  11539   3560   1690   -561       O  
ATOM    225  NE2 GLN A  61      17.124 -21.463 -19.558  1.00115.15           N  
ANISOU  225  NE2 GLN A  61    14378  18050  11322   4317   1441   -862       N  
ATOM    226  N   THR A  62      11.479 -16.766 -19.521  1.00 69.63           N  
ANISOU  226  N   THR A  62     9118  11164   6174   1606    864    117       N  
ATOM    227  CA  THR A  62      10.910 -15.442 -19.810  1.00 67.39           C  
ANISOU  227  CA  THR A  62     8765  10913   5928   1184    824    309       C  
ATOM    228  C   THR A  62      10.702 -14.657 -18.516  1.00 68.55           C  
ANISOU  228  C   THR A  62     8737  10963   6347   1001    690    461       C  
ATOM    229  O   THR A  62      10.681 -15.238 -17.428  1.00 67.12           O  
ANISOU  229  O   THR A  62     8559  10621   6323   1156    600    420       O  
ATOM    230  CB  THR A  62       9.569 -15.551 -20.568  1.00 72.97           C  
ANISOU  230  CB  THR A  62     9836  11332   6559   1014    697    305       C  
ATOM    231  OG1 THR A  62       8.593 -16.195 -19.740  1.00 69.30           O  
ANISOU  231  OG1 THR A  62     9577  10497   6258   1029    500    276       O  
ATOM    232  CG2 THR A  62       9.743 -16.342 -21.861  1.00 74.97           C  
ANISOU  232  CG2 THR A  62    10317  11654   6514   1184    813    141       C  
ATOM    233  N   THR A  63      10.546 -13.339 -18.638  1.00 64.17           N  
ANISOU  233  N   THR A  63     8075  10486   5823    674    666    633       N  
ATOM    234  CA  THR A  63      10.391 -12.458 -17.470  1.00 61.78           C  
ANISOU  234  CA  THR A  63     7638  10093   5743    500    540    766       C  
ATOM    235  C   THR A  63       9.237 -12.880 -16.555  1.00 63.02           C  
ANISOU  235  C   THR A  63     7976   9887   6079    538    355    740       C  
ATOM    236  O   THR A  63       9.371 -12.857 -15.329  1.00 61.56           O  
ANISOU  236  O   THR A  63     7686   9641   6063    575    287    760       O  
ATOM    237  CB  THR A  63      10.169 -10.980 -17.884  1.00 69.31           C  
ANISOU  237  CB  THR A  63     8584  11082   6669    148    495    946       C  
ATOM    238  OG1 THR A  63      11.387 -10.434 -18.402  1.00 71.33           O  
ANISOU  238  OG1 THR A  63     8611  11715   6777     26    658   1016       O  
ATOM    239  CG2 THR A  63       9.706 -10.136 -16.690  1.00 65.33           C  
ANISOU  239  CG2 THR A  63     8058  10382   6384     11    324   1047       C  
ATOM    240  N   THR A  64       8.107 -13.252 -17.144  1.00 58.67           N  
ANISOU  240  N   THR A  64     7686   9131   5474    502    273    702       N  
ATOM    241  CA  THR A  64       6.985 -13.728 -16.356  1.00 56.65           C  
ANISOU  241  CA  THR A  64     7573   8600   5351    500    114    680       C  
ATOM    242  C   THR A  64       7.440 -14.897 -15.505  1.00 61.39           C  
ANISOU  242  C   THR A  64     8198   9123   6004    731    121    578       C  
ATOM    243  O   THR A  64       7.322 -14.875 -14.281  1.00 59.62           O  
ANISOU  243  O   THR A  64     7905   8812   5935    731     45    613       O  
ATOM    244  CB  THR A  64       5.834 -14.194 -17.245  1.00 64.79           C  
ANISOU  244  CB  THR A  64     8864   9481   6271    428     29    637       C  
ATOM    245  OG1 THR A  64       5.346 -13.081 -17.997  1.00 66.19           O  
ANISOU  245  OG1 THR A  64     9037   9713   6397    235    -14    744       O  
ATOM    246  CG2 THR A  64       4.700 -14.787 -16.408  1.00 60.83           C  
ANISOU  246  CG2 THR A  64     8475   8758   5882    384   -125    621       C  
ATOM    247  N   ASN A  65       7.986 -15.911 -16.163  1.00 60.40           N  
ANISOU  247  N   ASN A  65     8198   9024   5729    948    206    447       N  
ATOM    248  CA  ASN A  65       8.381 -17.123 -15.472  1.00 61.21           C  
ANISOU  248  CA  ASN A  65     8411   8997   5849   1213    180    339       C  
ATOM    249  C   ASN A  65       9.392 -16.845 -14.360  1.00 65.35           C  
ANISOU  249  C   ASN A  65     8650   9674   6508   1333    208    384       C  
ATOM    250  O   ASN A  65       9.223 -17.313 -13.236  1.00 64.12           O  
ANISOU  250  O   ASN A  65     8553   9345   6465   1388     99    391       O  
ATOM    251  CB  ASN A  65       8.897 -18.162 -16.473  1.00 64.30           C  
ANISOU  251  CB  ASN A  65     9006   9399   6025   1486    270    169       C  
ATOM    252  CG  ASN A  65       7.774 -18.791 -17.304  1.00 85.28           C  
ANISOU  252  CG  ASN A  65    12052  11801   8548   1372    175    103       C  
ATOM    253  OD1 ASN A  65       6.611 -18.838 -16.881  1.00 76.78           O  
ANISOU  253  OD1 ASN A  65    11112  10505   7557   1139     16    167       O  
ATOM    254  ND2 ASN A  65       8.124 -19.287 -18.487  1.00 80.48           N  
ANISOU  254  ND2 ASN A  65    11614  11253   7711   1529    272    -30       N  
ATOM    255  N   TYR A  66      10.414 -16.047 -14.652  1.00 63.39           N  
ANISOU  255  N   TYR A  66     8090   9764   6232   1331    340    429       N  
ATOM    256  CA  TYR A  66      11.401 -15.669 -13.630  1.00 63.75           C  
ANISOU  256  CA  TYR A  66     7827  10003   6394   1392    348    485       C  
ATOM    257  C   TYR A  66      10.761 -15.118 -12.337  1.00 64.69           C  
ANISOU  257  C   TYR A  66     7939   9933   6706   1198    194    593       C  
ATOM    258  O   TYR A  66      11.278 -15.357 -11.243  1.00 64.58           O  
ANISOU  258  O   TYR A  66     7824   9928   6785   1314    135    600       O  
ATOM    259  CB  TYR A  66      12.404 -14.657 -14.190  1.00 66.94           C  
ANISOU  259  CB  TYR A  66     7891  10817   6725   1269    494    560       C  
ATOM    260  CG  TYR A  66      13.429 -15.240 -15.150  1.00 72.92           C  
ANISOU  260  CG  TYR A  66     8523  11901   7282   1534    682    443       C  
ATOM    261  CD1 TYR A  66      14.274 -16.278 -14.754  1.00 77.48           C  
ANISOU  261  CD1 TYR A  66     9021  12579   7838   1951    708    313       C  
ATOM    262  CD2 TYR A  66      13.582 -14.729 -16.440  1.00 75.14           C  
ANISOU  262  CD2 TYR A  66     8761  12414   7374   1388    834    462       C  
ATOM    263  CE1 TYR A  66      15.231 -16.806 -15.622  1.00 82.27           C  
ANISOU  263  CE1 TYR A  66     9486  13529   8243   2258    893    182       C  
ATOM    264  CE2 TYR A  66      14.536 -15.248 -17.316  1.00 79.73           C  
ANISOU  264  CE2 TYR A  66     9201  13353   7739   1644   1035    342       C  
ATOM    265  CZ  TYR A  66      15.356 -16.286 -16.899  1.00 90.27           C  
ANISOU  265  CZ  TYR A  66    10433  14805   9060   2098   1070    192       C  
ATOM    266  OH  TYR A  66      16.301 -16.811 -17.753  1.00 96.13           O  
ANISOU  266  OH  TYR A  66    11018  15936   9572   2416   1278     48       O  
ATOM    267  N   LEU A  67       9.650 -14.387 -12.462  1.00 58.67           N  
ANISOU  267  N   LEU A  67     7285   9021   5987    930    125    669       N  
ATOM    268  CA  LEU A  67       8.887 -13.943 -11.284  1.00 55.86           C  
ANISOU  268  CA  LEU A  67     6951   8491   5782    789     -8    739       C  
ATOM    269  C   LEU A  67       8.131 -15.115 -10.685  1.00 58.06           C  
ANISOU  269  C   LEU A  67     7463   8517   6079    882    -99    677       C  
ATOM    270  O   LEU A  67       7.923 -15.161  -9.480  1.00 56.79           O  
ANISOU  270  O   LEU A  67     7298   8266   6014    861   -183    710       O  
ATOM    271  CB  LEU A  67       7.904 -12.800 -11.613  1.00 54.53           C  
ANISOU  271  CB  LEU A  67     6818   8263   5638    537    -61    823       C  
ATOM    272  CG  LEU A  67       8.472 -11.383 -11.832  1.00 59.53           C  
ANISOU  272  CG  LEU A  67     7292   9054   6272    360    -39    928       C  
ATOM    273  CD1 LEU A  67       7.357 -10.392 -12.161  1.00 58.71           C  
ANISOU  273  CD1 LEU A  67     7309   8818   6179    185   -133    994       C  
ATOM    274  CD2 LEU A  67       9.272 -10.894 -10.624  1.00 61.82           C  
ANISOU  274  CD2 LEU A  67     7405   9420   6664    336    -75    975       C  
ATOM    275  N   VAL A  68       7.716 -16.054 -11.525  1.00 54.82           N  
ANISOU  275  N   VAL A  68     7285   7990   5555    954    -92    593       N  
ATOM    276  CA  VAL A  68       7.080 -17.278 -11.041  1.00 54.67           C  
ANISOU  276  CA  VAL A  68     7546   7709   5516   1003   -194    541       C  
ATOM    277  C   VAL A  68       8.062 -18.100 -10.197  1.00 59.54           C  
ANISOU  277  C   VAL A  68     8185   8289   6148   1270   -217    499       C  
ATOM    278  O   VAL A  68       7.664 -18.704  -9.194  1.00 58.77           O  
ANISOU  278  O   VAL A  68     8244   7998   6086   1249   -329    522       O  
ATOM    279  CB  VAL A  68       6.512 -18.128 -12.208  1.00 59.60           C  
ANISOU  279  CB  VAL A  68     8467   8195   5984   1007   -204    451       C  
ATOM    280  CG1 VAL A  68       6.067 -19.494 -11.725  1.00 60.43           C  
ANISOU  280  CG1 VAL A  68     8921   8003   6036   1048   -327    398       C  
ATOM    281  CG2 VAL A  68       5.362 -17.389 -12.882  1.00 58.12           C  
ANISOU  281  CG2 VAL A  68     8268   8030   5784    732   -233    508       C  
ATOM    282  N   VAL A  69       9.336 -18.108 -10.594  1.00 57.28           N  
ANISOU  282  N   VAL A  69     7729   8216   5819   1517   -116    445       N  
ATOM    283  CA  VAL A  69      10.379 -18.756  -9.798  1.00 58.31           C  
ANISOU  283  CA  VAL A  69     7811   8378   5968   1819   -149    408       C  
ATOM    284  C   VAL A  69      10.416 -18.176  -8.393  1.00 60.41           C  
ANISOU  284  C   VAL A  69     7914   8661   6378   1691   -237    521       C  
ATOM    285  O   VAL A  69      10.286 -18.911  -7.414  1.00 60.57           O  
ANISOU  285  O   VAL A  69     8116   8480   6419   1768   -360    530       O  
ATOM    286  CB  VAL A  69      11.784 -18.624 -10.427  1.00 64.20           C  
ANISOU  286  CB  VAL A  69     8268   9480   6645   2088     -8    343       C  
ATOM    287  CG1 VAL A  69      12.876 -18.801  -9.369  1.00 65.21           C  
ANISOU  287  CG1 VAL A  69     8182   9755   6840   2327    -63    357       C  
ATOM    288  CG2 VAL A  69      11.955 -19.633 -11.547  1.00 66.54           C  
ANISOU  288  CG2 VAL A  69     8801   9720   6760   2371     58    182       C  
ATOM    289  N   SER A  70      10.575 -16.859  -8.287  1.00 54.77           N  
ANISOU  289  N   SER A  70     6904   8163   5742   1483   -187    608       N  
ATOM    290  CA  SER A  70      10.674 -16.236  -6.965  1.00 52.95           C  
ANISOU  290  CA  SER A  70     6539   7954   5626   1366   -273    698       C  
ATOM    291  C   SER A  70       9.421 -16.526  -6.137  1.00 54.63           C  
ANISOU  291  C   SER A  70     6999   7888   5871   1211   -379    731       C  
ATOM    292  O   SER A  70       9.522 -16.745  -4.938  1.00 54.19           O  
ANISOU  292  O   SER A  70     6973   7765   5852   1231   -472    768       O  
ATOM    293  CB  SER A  70      10.932 -14.725  -7.054  1.00 55.29           C  
ANISOU  293  CB  SER A  70     6565   8465   5976   1132   -227    781       C  
ATOM    294  OG  SER A  70       9.767 -13.976  -6.757  1.00 61.08           O  
ANISOU  294  OG  SER A  70     7398   9048   6762    884   -276    833       O  
ATOM    295  N   LEU A  71       8.255 -16.547  -6.778  1.00 50.01           N  
ANISOU  295  N   LEU A  71     6575   7176   5251   1048   -366    722       N  
ATOM    296  CA  LEU A  71       7.012 -16.911  -6.091  1.00 48.97           C  
ANISOU  296  CA  LEU A  71     6638   6850   5118    878   -450    753       C  
ATOM    297  C   LEU A  71       7.058 -18.366  -5.652  1.00 54.57           C  
ANISOU  297  C   LEU A  71     7642   7338   5753   1002   -538    724       C  
ATOM    298  O   LEU A  71       6.538 -18.715  -4.590  1.00 53.84           O  
ANISOU  298  O   LEU A  71     7673   7127   5656    892   -622    778       O  
ATOM    299  CB  LEU A  71       5.786 -16.685  -6.987  1.00 48.27           C  
ANISOU  299  CB  LEU A  71     6620   6728   4991    684   -431    748       C  
ATOM    300  CG  LEU A  71       4.418 -17.119  -6.428  1.00 52.62           C  
ANISOU  300  CG  LEU A  71     7322   7159   5513    475   -505    780       C  
ATOM    301  CD1 LEU A  71       4.115 -16.390  -5.132  1.00 51.81           C  
ANISOU  301  CD1 LEU A  71     7074   7133   5479    382   -523    839       C  
ATOM    302  CD2 LEU A  71       3.309 -16.886  -7.435  1.00 54.70           C  
ANISOU  302  CD2 LEU A  71     7600   7451   5732    308   -501    772       C  
ATOM    303  N   ALA A  72       7.661 -19.212  -6.484  1.00 53.09           N  
ANISOU  303  N   ALA A  72     7599   7087   5485   1231   -524    638       N  
ATOM    304  CA  ALA A  72       7.896 -20.606  -6.125  1.00 55.06           C  
ANISOU  304  CA  ALA A  72     8190   7082   5648   1420   -635    598       C  
ATOM    305  C   ALA A  72       8.891 -20.728  -4.963  1.00 59.62           C  
ANISOU  305  C   ALA A  72     8678   7700   6274   1628   -707    634       C  
ATOM    306  O   ALA A  72       8.772 -21.629  -4.138  1.00 60.08           O  
ANISOU  306  O   ALA A  72     9026   7521   6282   1667   -844    664       O  
ATOM    307  CB  ALA A  72       8.391 -21.383  -7.333  1.00 58.04           C  
ANISOU  307  CB  ALA A  72     8746   7395   5911   1685   -599    468       C  
ATOM    308  N   VAL A  73       9.865 -19.820  -4.903  1.00 56.02           N  
ANISOU  308  N   VAL A  73     7836   7547   5900   1733   -632    642       N  
ATOM    309  CA  VAL A  73      10.830 -19.786  -3.794  1.00 56.71           C  
ANISOU  309  CA  VAL A  73     7777   7734   6035   1899   -716    685       C  
ATOM    310  C   VAL A  73      10.162 -19.376  -2.475  1.00 58.83           C  
ANISOU  310  C   VAL A  73     8079   7925   6350   1632   -800    792       C  
ATOM    311  O   VAL A  73      10.530 -19.875  -1.418  1.00 59.37           O  
ANISOU  311  O   VAL A  73     8251   7907   6399   1733   -929    835       O  
ATOM    312  CB  VAL A  73      12.031 -18.840  -4.093  1.00 60.96           C  
ANISOU  312  CB  VAL A  73     7861   8669   6633   2002   -621    678       C  
ATOM    313  CG1 VAL A  73      13.010 -18.812  -2.920  1.00 61.98           C  
ANISOU  313  CG1 VAL A  73     7820   8927   6803   2148   -737    728       C  
ATOM    314  CG2 VAL A  73      12.747 -19.258  -5.381  1.00 62.87           C  
ANISOU  314  CG2 VAL A  73     8033   9059   6794   2283   -508    565       C  
ATOM    315  N   ALA A  74       9.175 -18.484  -2.538  1.00 53.51           N  
ANISOU  315  N   ALA A  74     7328   7289   5716   1316   -732    830       N  
ATOM    316  CA  ALA A  74       8.403 -18.087  -1.347  1.00 52.35           C  
ANISOU  316  CA  ALA A  74     7214   7098   5579   1078   -784    907       C  
ATOM    317  C   ALA A  74       7.702 -19.282  -0.709  1.00 58.00           C  
ANISOU  317  C   ALA A  74     8296   7550   6190   1012   -886    944       C  
ATOM    318  O   ALA A  74       7.468 -19.315   0.498  1.00 57.61           O  
ANISOU  318  O   ALA A  74     8316   7465   6106    903   -956   1014       O  
ATOM    319  CB  ALA A  74       7.371 -17.016  -1.701  1.00 51.10           C  
ANISOU  319  CB  ALA A  74     6928   7027   5458    822   -692    913       C  
ATOM    320  N   ASP A  75       7.366 -20.258  -1.536  1.00 56.31           N  
ANISOU  320  N   ASP A  75     8345   7149   5901   1050   -901    902       N  
ATOM    321  CA  ASP A  75       6.647 -21.430  -1.092  1.00 57.73           C  
ANISOU  321  CA  ASP A  75     8933   7047   5955    922  -1014    948       C  
ATOM    322  C   ASP A  75       7.634 -22.519  -0.652  1.00 63.65           C  
ANISOU  322  C   ASP A  75     9959   7586   6641   1234  -1166    944       C  
ATOM    323  O   ASP A  75       7.361 -23.269   0.283  1.00 64.50           O  
ANISOU  323  O   ASP A  75    10376   7482   6649   1141  -1300   1028       O  
ATOM    324  CB  ASP A  75       5.722 -21.905  -2.222  1.00 60.09           C  
ANISOU  324  CB  ASP A  75     9420   7226   6185    763   -986    904       C  
ATOM    325  CG  ASP A  75       4.803 -20.784  -2.742  1.00 69.27           C  
ANISOU  325  CG  ASP A  75    10283   8624   7412    518   -857    904       C  
ATOM    326  OD1 ASP A  75       4.370 -19.947  -1.910  1.00 68.52           O  
ANISOU  326  OD1 ASP A  75     9977   8696   7363    363   -819    960       O  
ATOM    327  OD2 ASP A  75       4.529 -20.739  -3.971  1.00 74.65           O  
ANISOU  327  OD2 ASP A  75    10961   9319   8084    509   -806    841       O  
ATOM    328  N   LEU A  76       8.787 -22.599  -1.308  1.00 60.99           N  
ANISOU  328  N   LEU A  76     9505   7324   6342   1615  -1149    851       N  
ATOM    329  CA  LEU A  76       9.822 -23.544  -0.893  1.00 63.59           C  
ANISOU  329  CA  LEU A  76    10040   7506   6617   2003  -1302    831       C  
ATOM    330  C   LEU A  76      10.342 -23.192   0.500  1.00 67.05           C  
ANISOU  330  C   LEU A  76    10336   8048   7090   2017  -1398    930       C  
ATOM    331  O   LEU A  76      10.484 -24.070   1.344  1.00 69.01           O  
ANISOU  331  O   LEU A  76    10919   8054   7245   2109  -1581    992       O  
ATOM    332  CB  LEU A  76      10.980 -23.594  -1.899  1.00 65.24           C  
ANISOU  332  CB  LEU A  76    10054   7885   6849   2438  -1234    696       C  
ATOM    333  CG  LEU A  76      10.760 -24.451  -3.153  1.00 71.64           C  
ANISOU  333  CG  LEU A  76    11183   8485   7553   2588  -1212    570       C  
ATOM    334  CD1 LEU A  76      11.708 -24.048  -4.278  1.00 72.48           C  
ANISOU  334  CD1 LEU A  76    10945   8913   7682   2903  -1051    438       C  
ATOM    335  CD2 LEU A  76      10.910 -25.930  -2.824  1.00 77.62           C  
ANISOU  335  CD2 LEU A  76    12511   8814   8167   2850  -1430    545       C  
ATOM    336  N   LEU A  77      10.612 -21.916   0.755  1.00 60.81           N  
ANISOU  336  N   LEU A  77     9098   7591   6415   1909  -1297    951       N  
ATOM    337  CA  LEU A  77      11.055 -21.512   2.094  1.00 60.32           C  
ANISOU  337  CA  LEU A  77     8920   7631   6369   1881  -1398   1039       C  
ATOM    338  C   LEU A  77       9.977 -21.804   3.142  1.00 63.95           C  
ANISOU  338  C   LEU A  77     9685   7886   6728   1556  -1467   1145       C  
ATOM    339  O   LEU A  77      10.273 -22.433   4.158  1.00 65.52           O  
ANISOU  339  O   LEU A  77    10113   7941   6838   1628  -1637   1222       O  
ATOM    340  CB  LEU A  77      11.472 -20.034   2.143  1.00 58.23           C  
ANISOU  340  CB  LEU A  77     8175   7727   6224   1771  -1292   1036       C  
ATOM    341  CG  LEU A  77      12.799 -19.670   1.461  1.00 63.70           C  
ANISOU  341  CG  LEU A  77     8498   8716   6987   2052  -1252    973       C  
ATOM    342  CD1 LEU A  77      13.040 -18.176   1.558  1.00 62.23           C  
ANISOU  342  CD1 LEU A  77     7924   8830   6891   1824  -1171    997       C  
ATOM    343  CD2 LEU A  77      13.975 -20.430   2.043  1.00 68.73           C  
ANISOU  343  CD2 LEU A  77     9137   9389   7589   2432  -1426    978       C  
ATOM    344  N   VAL A  78       8.738 -21.376   2.889  1.00 58.59           N  
ANISOU  344  N   VAL A  78     9003   7217   6042   1207  -1340   1154       N  
ATOM    345  CA  VAL A  78       7.616 -21.672   3.799  1.00 58.50           C  
ANISOU  345  CA  VAL A  78     9236   7086   5905    866  -1371   1252       C  
ATOM    346  C   VAL A  78       7.575 -23.139   4.222  1.00 65.62           C  
ANISOU  346  C   VAL A  78    10648   7638   6648    894  -1554   1326       C  
ATOM    347  O   VAL A  78       7.371 -23.436   5.399  1.00 66.87           O  
ANISOU  347  O   VAL A  78    11002   7720   6686    745  -1653   1436       O  
ATOM    348  CB  VAL A  78       6.244 -21.306   3.187  1.00 60.78           C  
ANISOU  348  CB  VAL A  78     9468   7441   6186    538  -1222   1237       C  
ATOM    349  CG1 VAL A  78       5.155 -22.269   3.658  1.00 62.09           C  
ANISOU  349  CG1 VAL A  78    10001   7417   6172    220  -1282   1332       C  
ATOM    350  CG2 VAL A  78       5.879 -19.879   3.535  1.00 58.39           C  
ANISOU  350  CG2 VAL A  78     8796   7430   5958    401  -1093   1219       C  
ATOM    351  N   ALA A  79       7.783 -24.049   3.273  1.00 63.39           N  
ANISOU  351  N   ALA A  79    10618   7127   6341   1085  -1611   1266       N  
ATOM    352  CA  ALA A  79       7.719 -25.488   3.557  1.00 66.42           C  
ANISOU  352  CA  ALA A  79    11581   7100   6554   1119  -1816   1328       C  
ATOM    353  C   ALA A  79       8.916 -26.017   4.352  1.00 72.54           C  
ANISOU  353  C   ALA A  79    12511   7754   7295   1506  -2023   1361       C  
ATOM    354  O   ALA A  79       8.801 -27.055   5.000  1.00 74.59           O  
ANISOU  354  O   ALA A  79    13277   7674   7390   1474  -2225   1460       O  
ATOM    355  CB  ALA A  79       7.564 -26.275   2.262  1.00 68.44           C  
ANISOU  355  CB  ALA A  79    12110   7119   6774   1227  -1828   1229       C  
ATOM    356  N   THR A  80      10.048 -25.309   4.300  1.00 68.61           N  
ANISOU  356  N   THR A  80    11588   7543   6940   1849  -1988   1290       N  
ATOM    357  CA  THR A  80      11.301 -25.770   4.926  1.00 71.10           C  
ANISOU  357  CA  THR A  80    11960   7819   7235   2284  -2194   1305       C  
ATOM    358  C   THR A  80      11.771 -24.950   6.144  1.00 74.61           C  
ANISOU  358  C   THR A  80    12107   8527   7713   2221  -2238   1390       C  
ATOM    359  O   THR A  80      12.626 -25.416   6.901  1.00 76.89           O  
ANISOU  359  O   THR A  80    12509   8757   7947   2505  -2453   1440       O  
ATOM    360  CB  THR A  80      12.470 -25.813   3.901  1.00 77.63           C  
ANISOU  360  CB  THR A  80    12530   8805   8160   2809  -2165   1149       C  
ATOM    361  OG1 THR A  80      12.908 -24.482   3.601  1.00 73.62           O  
ANISOU  361  OG1 THR A  80    11396   8765   7813   2768  -1977   1100       O  
ATOM    362  CG2 THR A  80      12.053 -26.523   2.614  1.00 76.03           C  
ANISOU  362  CG2 THR A  80    12610   8368   7911   2892  -2104   1035       C  
ATOM    363  N   LEU A  81      11.244 -23.739   6.329  1.00 68.03           N  
ANISOU  363  N   LEU A  81    10918   7973   6956   1880  -2058   1397       N  
ATOM    364  CA  LEU A  81      11.651 -22.892   7.464  1.00 67.27           C  
ANISOU  364  CA  LEU A  81    10576   8113   6872   1796  -2103   1459       C  
ATOM    365  C   LEU A  81      10.506 -22.443   8.385  1.00 69.36           C  
ANISOU  365  C   LEU A  81    10939   8382   7034   1335  -2032   1544       C  
ATOM    366  O   LEU A  81      10.764 -21.953   9.488  1.00 68.91           O  
ANISOU  366  O   LEU A  81    10811   8447   6925   1260  -2103   1601       O  
ATOM    367  CB  LEU A  81      12.412 -21.656   6.968  1.00 65.73           C  
ANISOU  367  CB  LEU A  81     9818   8305   6850   1887  -1982   1370       C  
ATOM    368  CG  LEU A  81      13.573 -21.864   5.984  1.00 72.09           C  
ANISOU  368  CG  LEU A  81    10385   9254   7751   2312  -1990   1274       C  
ATOM    369  CD1 LEU A  81      14.399 -20.578   5.895  1.00 71.32           C  
ANISOU  369  CD1 LEU A  81     9740   9581   7777   2294  -1918   1242       C  
ATOM    370  CD2 LEU A  81      14.463 -23.053   6.355  1.00 78.52           C  
ANISOU  370  CD2 LEU A  81    11440   9911   8484   2749  -2234   1294       C  
ATOM    371  N   VAL A  82       9.258 -22.606   7.948  1.00 64.68           N  
ANISOU  371  N   VAL A  82    10494   7691   6392   1033  -1895   1547       N  
ATOM    372  CA  VAL A  82       8.106 -22.178   8.741  1.00 63.38           C  
ANISOU  372  CA  VAL A  82    10362   7609   6112    616  -1795   1611       C  
ATOM    373  C   VAL A  82       7.195 -23.341   9.136  1.00 69.72           C  
ANISOU  373  C   VAL A  82    11648   8144   6700    344  -1867   1733       C  
ATOM    374  O   VAL A  82       6.792 -23.459  10.292  1.00 70.48           O  
ANISOU  374  O   VAL A  82    11916   8245   6617    108  -1910   1843       O  
ATOM    375  CB  VAL A  82       7.284 -21.111   7.990  1.00 64.10           C  
ANISOU  375  CB  VAL A  82    10109   7933   6313    432  -1553   1516       C  
ATOM    376  CG1 VAL A  82       5.893 -20.963   8.604  1.00 63.67           C  
ANISOU  376  CG1 VAL A  82    10120   7963   6108     32  -1439   1570       C  
ATOM    377  CG2 VAL A  82       8.024 -19.774   7.992  1.00 62.11           C  
ANISOU  377  CG2 VAL A  82     9443   7946   6212    567  -1498   1434       C  
ATOM    378  N   MET A  83       6.875 -24.207   8.188  1.00 67.33           N  
ANISOU  378  N   MET A  83    11588   7607   6388    348  -1887   1719       N  
ATOM    379  CA  MET A  83       5.903 -25.262   8.442  1.00 69.51           C  
ANISOU  379  CA  MET A  83    12333   7630   6448     -2  -1955   1841       C  
ATOM    380  C   MET A  83       6.375 -26.375   9.382  1.00 78.05           C  
ANISOU  380  C   MET A  83    13945   8375   7337     55  -2224   1985       C  
ATOM    381  O   MET A  83       5.541 -27.043   9.999  1.00 79.93           O  
ANISOU  381  O   MET A  83    14556   8468   7347   -343  -2278   2131       O  
ATOM    382  CB  MET A  83       5.421 -25.847   7.125  1.00 71.94           C  
ANISOU  382  CB  MET A  83    12788   7761   6785    -42  -1925   1778       C  
ATOM    383  CG  MET A  83       4.610 -24.851   6.330  1.00 72.53           C  
ANISOU  383  CG  MET A  83    12418   8158   6983   -222  -1678   1683       C  
ATOM    384  SD  MET A  83       4.009 -25.546   4.800  1.00 77.25           S  
ANISOU  384  SD  MET A  83    13207   8559   7584   -305  -1667   1615       S  
ATOM    385  CE  MET A  83       2.847 -26.763   5.445  1.00 77.39           C  
ANISOU  385  CE  MET A  83    13769   8332   7305   -856  -1792   1801       C  
ATOM    386  N   PRO A  84       7.701 -26.590   9.500  1.00 76.22           N  
ANISOU  386  N   PRO A  84    13749   8033   7176    538  -2405   1953       N  
ATOM    387  CA  PRO A  84       8.145 -27.547  10.519  1.00 79.77           C  
ANISOU  387  CA  PRO A  84    14701   8179   7431    612  -2686   2101       C  
ATOM    388  C   PRO A  84       7.726 -27.114  11.924  1.00 83.76           C  
ANISOU  388  C   PRO A  84    15191   8862   7772    266  -2669   2236       C  
ATOM    389  O   PRO A  84       7.331 -27.944  12.751  1.00 86.45           O  
ANISOU  389  O   PRO A  84    16028   8961   7858      8  -2821   2409       O  
ATOM    390  CB  PRO A  84       9.673 -27.524  10.386  1.00 82.37           C  
ANISOU  390  CB  PRO A  84    14872   8522   7902   1233  -2843   2014       C  
ATOM    391  CG  PRO A  84       9.926 -27.078   8.995  1.00 84.54           C  
ANISOU  391  CG  PRO A  84    14771   8952   8396   1468  -2670   1829       C  
ATOM    392  CD  PRO A  84       8.828 -26.110   8.677  1.00 76.52           C  
ANISOU  392  CD  PRO A  84    13417   8215   7443   1029  -2381   1795       C  
ATOM    393  N   TRP A  85       7.808 -25.814  12.175  1.00 77.09           N  
ANISOU  393  N   TRP A  85    13812   8428   7049    251  -2489   2155       N  
ATOM    394  CA  TRP A  85       7.414 -25.257  13.452  1.00 76.80           C  
ANISOU  394  CA  TRP A  85    13723   8604   6853    -42  -2441   2241       C  
ATOM    395  C   TRP A  85       5.885 -25.299  13.592  1.00 79.24           C  
ANISOU  395  C   TRP A  85    14107   9011   6988   -587  -2245   2306       C  
ATOM    396  O   TRP A  85       5.366 -25.588  14.667  1.00 80.85           O  
ANISOU  396  O   TRP A  85    14563   9227   6930   -912  -2272   2449       O  
ATOM    397  CB  TRP A  85       7.959 -23.833  13.593  1.00 73.13           C  
ANISOU  397  CB  TRP A  85    12709   8514   6562    117  -2323   2112       C  
ATOM    398  CG  TRP A  85       9.486 -23.707  13.437  1.00 74.81           C  
ANISOU  398  CG  TRP A  85    12752   8731   6940    606  -2506   2053       C  
ATOM    399  CD1 TRP A  85      10.166 -22.835  12.616  1.00 75.61           C  
ANISOU  399  CD1 TRP A  85    12383   9056   7289    853  -2415   1906       C  
ATOM    400  CD2 TRP A  85      10.494 -24.473  14.118  1.00 78.02           C  
ANISOU  400  CD2 TRP A  85    13436   8950   7257    890  -2814   2149       C  
ATOM    401  NE1 TRP A  85      11.524 -23.015  12.748  1.00 76.93           N  
ANISOU  401  NE1 TRP A  85    12473   9236   7522   1250  -2629   1904       N  
ATOM    402  CE2 TRP A  85      11.753 -24.010  13.663  1.00 81.72           C  
ANISOU  402  CE2 TRP A  85    13523   9593   7933   1311  -2883   2044       C  
ATOM    403  CE3 TRP A  85      10.457 -25.501  15.070  1.00 82.85           C  
ANISOU  403  CE3 TRP A  85    14587   9275   7618    823  -3050   2323       C  
ATOM    404  CZ2 TRP A  85      12.959 -24.542  14.128  1.00 84.18           C  
ANISOU  404  CZ2 TRP A  85    13927   9839   8219   1702  -3179   2094       C  
ATOM    405  CZ3 TRP A  85      11.660 -26.030  15.528  1.00 87.35           C  
ANISOU  405  CZ3 TRP A  85    15305   9719   8163   1228  -3363   2377       C  
ATOM    406  CH2 TRP A  85      12.893 -25.549  15.056  1.00 87.61           C  
ANISOU  406  CH2 TRP A  85    14901   9968   8418   1681  -3425   2256       C  
ATOM    407  N   VAL A  86       5.166 -25.048  12.501  1.00 73.07           N  
ANISOU  407  N   VAL A  86    13105   8326   6332   -694  -2053   2208       N  
ATOM    408  CA  VAL A  86       3.706 -25.197  12.492  1.00 72.95           C  
ANISOU  408  CA  VAL A  86    13126   8438   6153  -1202  -1885   2270       C  
ATOM    409  C   VAL A  86       3.300 -26.633  12.826  1.00 80.05           C  
ANISOU  409  C   VAL A  86    14649   8981   6785  -1513  -2069   2466       C  
ATOM    410  O   VAL A  86       2.269 -26.859  13.453  1.00 81.01           O  
ANISOU  410  O   VAL A  86    14886   9236   6658  -2005  -1987   2593       O  
ATOM    411  CB  VAL A  86       3.090 -24.799  11.124  1.00 74.26           C  
ANISOU  411  CB  VAL A  86    12977   8731   6505  -1223  -1703   2137       C  
ATOM    412  CG1 VAL A  86       1.588 -25.087  11.092  1.00 75.28           C  
ANISOU  412  CG1 VAL A  86    13138   9015   6449  -1757  -1566   2216       C  
ATOM    413  CG2 VAL A  86       3.356 -23.336  10.827  1.00 70.48           C  
ANISOU  413  CG2 VAL A  86    11936   8589   6253   -983  -1526   1966       C  
ATOM    414  N   VAL A  87       4.115 -27.596  12.409  1.00 78.56           N  
ANISOU  414  N   VAL A  87    14872   8348   6627  -1225  -2322   2489       N  
ATOM    415  CA  VAL A  87       3.856 -29.000  12.723  1.00 82.85           C  
ANISOU  415  CA  VAL A  87    16117   8455   6905  -1480  -2556   2678       C  
ATOM    416  C   VAL A  87       4.219 -29.334  14.181  1.00 89.95           C  
ANISOU  416  C   VAL A  87    17356   9259   7563  -1552  -2737   2858       C  
ATOM    417  O   VAL A  87       3.647 -30.262  14.768  1.00 93.46           O  
ANISOU  417  O   VAL A  87    18335   9472   7704  -1973  -2865   3062       O  
ATOM    418  CB  VAL A  87       4.605 -29.960  11.764  1.00 88.26           C  
ANISOU  418  CB  VAL A  87    17204   8649   7681  -1086  -2791   2622       C  
ATOM    419  CG1 VAL A  87       4.175 -31.407  12.003  1.00 92.74           C  
ANISOU  419  CG1 VAL A  87    18575   8710   7950  -1412  -3046   2815       C  
ATOM    420  CG2 VAL A  87       4.352 -29.578  10.313  1.00 85.36           C  
ANISOU  420  CG2 VAL A  87    16497   8393   7541   -981  -2615   2434       C  
ATOM    421  N   TYR A  88       5.161 -28.590  14.763  1.00 84.97           N  
ANISOU  421  N   TYR A  88    16439   8805   7042  -1179  -2762   2793       N  
ATOM    422  CA  TYR A  88       5.506 -28.769  16.179  1.00 87.08           C  
ANISOU  422  CA  TYR A  88    16977   9036   7072  -1245  -2927   2954       C  
ATOM    423  C   TYR A  88       4.406 -28.218  17.093  1.00 90.27           C  
ANISOU  423  C   TYR A  88    17223   9831   7243  -1794  -2691   3034       C  
ATOM    424  O   TYR A  88       3.985 -28.896  18.025  1.00 93.36           O  
ANISOU  424  O   TYR A  88    18061  10111   7301  -2173  -2791   3243       O  
ATOM    425  CB  TYR A  88       6.860 -28.126  16.505  1.00 87.22           C  
ANISOU  425  CB  TYR A  88    16717   9155   7268   -700  -3046   2856       C  
ATOM    426  CG  TYR A  88       7.082 -27.864  17.982  1.00 90.82           C  
ANISOU  426  CG  TYR A  88    17263   9743   7501   -814  -3136   2977       C  
ATOM    427  CD1 TYR A  88       7.425 -28.892  18.850  1.00 97.08           C  
ANISOU  427  CD1 TYR A  88    18674  10183   8029   -835  -3454   3185       C  
ATOM    428  CD2 TYR A  88       6.948 -26.577  18.509  1.00 89.15           C  
ANISOU  428  CD2 TYR A  88    16560   9989   7324   -893  -2919   2878       C  
ATOM    429  CE1 TYR A  88       7.626 -28.647  20.205  1.00 99.51           C  
ANISOU  429  CE1 TYR A  88    19081  10622   8108   -951  -3544   3300       C  
ATOM    430  CE2 TYR A  88       7.149 -26.323  19.862  1.00 91.59           C  
ANISOU  430  CE2 TYR A  88    16976  10422   7404  -1000  -3004   2973       C  
ATOM    431  CZ  TYR A  88       7.486 -27.359  20.702  1.00102.70           C  
ANISOU  431  CZ  TYR A  88    18971  11504   8545  -1037  -3310   3187       C  
ATOM    432  OH  TYR A  88       7.682 -27.106  22.039  1.00105.77           O  
ANISOU  432  OH  TYR A  88    19481  12023   8683  -1154  -3401   3285       O  
ATOM    433  N   LEU A  89       3.938 -26.999  16.817  1.00 83.09           N  
ANISOU  433  N   LEU A  89    15699   9383   6488  -1826  -2381   2868       N  
ATOM    434  CA  LEU A  89       2.848 -26.392  17.597  1.00 83.08           C  
ANISOU  434  CA  LEU A  89    15482   9815   6268  -2274  -2122   2898       C  
ATOM    435  C   LEU A  89       1.526 -27.137  17.436  1.00 88.97           C  
ANISOU  435  C   LEU A  89    16434  10589   6781  -2856  -2020   3036       C  
ATOM    436  O   LEU A  89       0.616 -26.961  18.239  1.00 90.36           O  
ANISOU  436  O   LEU A  89    16546  11105   6683  -3288  -1845   3119       O  
ATOM    437  CB  LEU A  89       2.636 -24.916  17.220  1.00 79.27           C  
ANISOU  437  CB  LEU A  89    14327   9780   6012  -2109  -1837   2667       C  
ATOM    438  CG  LEU A  89       3.563 -23.858  17.831  1.00 82.33           C  
ANISOU  438  CG  LEU A  89    14453  10325   6503  -1756  -1858   2548       C  
ATOM    439  CD1 LEU A  89       3.099 -22.459  17.448  1.00 79.28           C  
ANISOU  439  CD1 LEU A  89    13502  10339   6282  -1685  -1576   2336       C  
ATOM    440  CD2 LEU A  89       3.633 -23.983  19.342  1.00 87.96           C  
ANISOU  440  CD2 LEU A  89    15437  11097   6886  -1939  -1941   2682       C  
ATOM    441  N   GLU A  90       1.415 -27.945  16.388  1.00 85.49           N  
ANISOU  441  N   GLU A  90    16223   9825   6433  -2879  -2123   3054       N  
ATOM    442  CA  GLU A  90       0.254 -28.808  16.200  1.00 88.10           C  
ANISOU  442  CA  GLU A  90    16835  10115   6525  -3477  -2095   3210       C  
ATOM    443  C   GLU A  90       0.309 -30.057  17.086  1.00 96.47           C  
ANISOU  443  C   GLU A  90    18647  10783   7225  -3809  -2367   3486       C  
ATOM    444  O   GLU A  90      -0.723 -30.485  17.607  1.00 99.07           O  
ANISOU  444  O   GLU A  90    19143  11274   7225  -4444  -2288   3667       O  
ATOM    445  CB  GLU A  90       0.116 -29.207  14.727  1.00 88.48           C  
ANISOU  445  CB  GLU A  90    16903   9931   6785  -3396  -2132   3118       C  
ATOM    446  CG  GLU A  90      -0.672 -28.203  13.887  1.00 96.12           C  
ANISOU  446  CG  GLU A  90    17198  11375   7949  -3432  -1821   2937       C  
ATOM    447  CD  GLU A  90      -2.190 -28.358  14.019  1.00121.94           C  
ANISOU  447  CD  GLU A  90    20347  15018  10966  -4107  -1634   3047       C  
ATOM    448  OE1 GLU A  90      -2.663 -29.302  14.701  1.00117.55           O  
ANISOU  448  OE1 GLU A  90    20252  14340  10070  -4619  -1740   3278       O  
ATOM    449  OE2 GLU A  90      -2.916 -27.528  13.422  1.00116.27           O  
ANISOU  449  OE2 GLU A  90    19062  14735  10379  -4132  -1389   2907       O  
ATOM    450  N   VAL A  91       1.498 -30.642  17.255  1.00 94.01           N  
ANISOU  450  N   VAL A  91    18786   9977   6956  -3389  -2692   3526       N  
ATOM    451  CA  VAL A  91       1.665 -31.845  18.098  1.00 98.93           C  
ANISOU  451  CA  VAL A  91    20204  10149   7235  -3633  -3008   3795       C  
ATOM    452  C   VAL A  91       1.347 -31.541  19.570  1.00104.14           C  
ANISOU  452  C   VAL A  91    20867  11134   7567  -3983  -2923   3950       C  
ATOM    453  O   VAL A  91       0.629 -32.300  20.228  1.00107.99           O  
ANISOU  453  O   VAL A  91    21810  11554   7666  -4587  -2977   4199       O  
ATOM    454  CB  VAL A  91       3.095 -32.434  17.989  1.00103.91           C  
ANISOU  454  CB  VAL A  91    21260  10223   7996  -2985  -3389   3777       C  
ATOM    455  CG1 VAL A  91       3.279 -33.592  18.966  1.00109.27           C  
ANISOU  455  CG1 VAL A  91    22784  10434   8300  -3202  -3740   4063       C  
ATOM    456  CG2 VAL A  91       3.377 -32.885  16.563  1.00102.83           C  
ANISOU  456  CG2 VAL A  91    21214   9743   8113  -2655  -3478   3631       C  
ATOM    457  N   THR A  92       1.897 -30.434  20.069  1.00 97.42           N  
ANISOU  457  N   THR A  92    19531  10631   6854  -3621  -2799   3803       N  
ATOM    458  CA  THR A  92       1.478 -29.852  21.345  1.00 98.15           C  
ANISOU  458  CA  THR A  92    19472  11160   6662  -3921  -2628   3873       C  
ATOM    459  C   THR A  92       0.139 -29.139  21.118  1.00101.38           C  
ANISOU  459  C   THR A  92    19327  12167   7026  -4334  -2206   3785       C  
ATOM    460  O   THR A  92      -0.233 -28.864  19.980  1.00 98.41           O  
ANISOU  460  O   THR A  92    18598  11880   6913  -4258  -2065   3634       O  
ATOM    461  CB  THR A  92       2.522 -28.838  21.887  1.00100.76           C  
ANISOU  461  CB  THR A  92    19472  11654   7159  -3385  -2649   3715       C  
ATOM    462  OG1 THR A  92       2.546 -27.674  21.056  1.00 94.59           O  
ANISOU  462  OG1 THR A  92    18001  11195   6743  -3066  -2403   3435       O  
ATOM    463  CG2 THR A  92       3.915 -29.448  21.925  1.00 99.75           C  
ANISOU  463  CG2 THR A  92    19751  11011   7140  -2878  -3064   3763       C  
ATOM    464  N   GLY A  93      -0.583 -28.825  22.189  1.00100.47           N  
ANISOU  464  N   GLY A  93    19118  12489   6565  -4745  -2005   3870       N  
ATOM    465  CA  GLY A  93      -1.873 -28.138  22.060  1.00 99.93           C  
ANISOU  465  CA  GLY A  93    18488  13060   6420  -5094  -1600   3778       C  
ATOM    466  C   GLY A  93      -1.771 -26.633  21.835  1.00 99.57           C  
ANISOU  466  C   GLY A  93    17736  13439   6659  -4636  -1342   3466       C  
ATOM    467  O   GLY A  93      -2.702 -25.895  22.161  1.00 99.76           O  
ANISOU  467  O   GLY A  93    17320  14045   6541  -4828  -1015   3377       O  
ATOM    468  N   GLY A  94      -0.659 -26.178  21.258  1.00 92.09           N  
ANISOU  468  N   GLY A  94    16684  12212   6096  -4033  -1491   3298       N  
ATOM    469  CA  GLY A  94      -0.382 -24.750  21.097  1.00 87.89           C  
ANISOU  469  CA  GLY A  94    15584  11990   5822  -3597  -1311   3022       C  
ATOM    470  C   GLY A  94       0.601 -24.224  22.129  1.00 91.43           C  
ANISOU  470  C   GLY A  94    16124  12405   6212  -3308  -1438   2987       C  
ATOM    471  O   GLY A  94       0.532 -23.057  22.520  1.00 89.52           O  
ANISOU  471  O   GLY A  94    15515  12515   5984  -3145  -1254   2805       O  
ATOM    472  N   VAL A  95       1.524 -25.083  22.558  1.00 89.69           N  
ANISOU  472  N   VAL A  95    16414  11746   5917  -3230  -1776   3158       N  
ATOM    473  CA  VAL A  95       2.516 -24.737  23.572  1.00 89.89           C  
ANISOU  473  CA  VAL A  95    16577  11716   5859  -2983  -1959   3161       C  
ATOM    474  C   VAL A  95       3.915 -24.695  22.952  1.00 91.02           C  
ANISOU  474  C   VAL A  95    16703  11512   6369  -2426  -2239   3080       C  
ATOM    475  O   VAL A  95       4.315 -25.612  22.236  1.00 91.17           O  
ANISOU  475  O   VAL A  95    16982  11137   6521  -2301  -2445   3162       O  
ATOM    476  CB  VAL A  95       2.492 -25.750  24.724  1.00 98.65           C  
ANISOU  476  CB  VAL A  95    18297  12651   6533  -3332  -2154   3444       C  
ATOM    477  CG1 VAL A  95       3.510 -25.374  25.790  1.00 99.34           C  
ANISOU  477  CG1 VAL A  95    18522  12703   6518  -3079  -2364   3448       C  
ATOM    478  CG2 VAL A  95       1.095 -25.827  25.320  1.00101.18           C  
ANISOU  478  CG2 VAL A  95    18604  13383   6458  -3933  -1854   3539       C  
ATOM    479  N   TRP A  96       4.653 -23.629  23.249  1.00 85.20           N  
ANISOU  479  N   TRP A  96    15665  10938   5768  -2101  -2249   2915       N  
ATOM    480  CA  TRP A  96       5.941 -23.353  22.623  1.00 82.73           C  
ANISOU  480  CA  TRP A  96    15185  10439   5809  -1599  -2458   2810       C  
ATOM    481  C   TRP A  96       7.054 -23.394  23.665  1.00 88.16           C  
ANISOU  481  C   TRP A  96    16094  11029   6372  -1410  -2768   2888       C  
ATOM    482  O   TRP A  96       7.167 -22.495  24.499  1.00 87.57           O  
ANISOU  482  O   TRP A  96    15881  11210   6180  -1433  -2718   2808       O  
ATOM    483  CB  TRP A  96       5.894 -21.981  21.959  1.00 77.62           C  
ANISOU  483  CB  TRP A  96    13965  10084   5445  -1412  -2226   2551       C  
ATOM    484  CG  TRP A  96       7.185 -21.536  21.376  1.00 76.61           C  
ANISOU  484  CG  TRP A  96    13604   9859   5644   -970  -2405   2443       C  
ATOM    485  CD1 TRP A  96       8.126 -20.764  21.982  1.00 79.48           C  
ANISOU  485  CD1 TRP A  96    13839  10326   6035   -777  -2546   2376       C  
ATOM    486  CD2 TRP A  96       7.679 -21.817  20.058  1.00 74.75           C  
ANISOU  486  CD2 TRP A  96    13216   9451   5735   -692  -2454   2390       C  
ATOM    487  NE1 TRP A  96       9.180 -20.550  21.131  1.00 77.38           N  
ANISOU  487  NE1 TRP A  96    13318   9991   6091   -420  -2678   2297       N  
ATOM    488  CE2 TRP A  96       8.930 -21.182  19.940  1.00 77.73           C  
ANISOU  488  CE2 TRP A  96    13339   9875   6320   -344  -2611   2298       C  
ATOM    489  CE3 TRP A  96       7.184 -22.542  18.966  1.00 75.43           C  
ANISOU  489  CE3 TRP A  96    13361   9365   5936   -721  -2383   2408       C  
ATOM    490  CZ2 TRP A  96       9.701 -21.249  18.771  1.00 75.56           C  
ANISOU  490  CZ2 TRP A  96    12838   9519   6354    -14  -2672   2225       C  
ATOM    491  CZ3 TRP A  96       7.953 -22.613  17.806  1.00 75.30           C  
ANISOU  491  CZ3 TRP A  96    13162   9224   6225   -366  -2454   2322       C  
ATOM    492  CH2 TRP A  96       9.196 -21.970  17.721  1.00 75.10           C  
ANISOU  492  CH2 TRP A  96    12856   9286   6392    -13  -2584   2232       C  
ATOM    493  N   ASN A  97       7.878 -24.437  23.598  1.00 86.64           N  
ANISOU  493  N   ASN A  97    16259  10462   6199  -1200  -3104   3035       N  
ATOM    494  CA  ASN A  97       8.943 -24.660  24.576  1.00 89.11           C  
ANISOU  494  CA  ASN A  97    16823  10660   6375  -1003  -3455   3143       C  
ATOM    495  C   ASN A  97      10.305 -24.096  24.166  1.00 90.95           C  
ANISOU  495  C   ASN A  97    16693  10934   6928   -499  -3643   3009       C  
ATOM    496  O   ASN A  97      11.248 -24.139  24.955  1.00 92.93           O  
ANISOU  496  O   ASN A  97    17058  11163   7088   -314  -3942   3077       O  
ATOM    497  CB  ASN A  97       9.081 -26.159  24.854  1.00 94.60           C  
ANISOU  497  CB  ASN A  97    18167  10917   6860  -1035  -3760   3397       C  
ATOM    498  CG  ASN A  97       7.787 -26.780  25.342  1.00118.51           C  
ANISOU  498  CG  ASN A  97    21592  13915   9520  -1616  -3606   3571       C  
ATOM    499  OD1 ASN A  97       7.216 -26.342  26.342  1.00111.39           O  
ANISOU  499  OD1 ASN A  97    20714  13291   8318  -1960  -3460   3609       O  
ATOM    500  ND2 ASN A  97       7.315 -27.804  24.636  1.00112.58           N  
ANISOU  500  ND2 ASN A  97    21161  12845   8770  -1745  -3637   3676       N  
ATOM    501  N   PHE A  98      10.408 -23.567  22.948  1.00 83.47           N  
ANISOU  501  N   PHE A  98    15304  10077   6335   -301  -3477   2829       N  
ATOM    502  CA  PHE A  98      11.677 -23.030  22.439  1.00 81.82           C  
ANISOU  502  CA  PHE A  98    14702   9961   6425    130  -3625   2708       C  
ATOM    503  C   PHE A  98      11.858 -21.544  22.757  1.00 83.26           C  
ANISOU  503  C   PHE A  98    14463  10502   6671     68  -3499   2546       C  
ATOM    504  O   PHE A  98      10.911 -20.849  23.133  1.00 81.60           O  
ANISOU  504  O   PHE A  98    14213  10464   6327   -243  -3245   2478       O  
ATOM    505  CB  PHE A  98      11.792 -23.252  20.927  1.00 81.38           C  
ANISOU  505  CB  PHE A  98    14414   9816   6692    376  -3526   2607       C  
ATOM    506  CG  PHE A  98      11.920 -24.702  20.527  1.00 85.13           C  
ANISOU  506  CG  PHE A  98    15320   9895   7132    556  -3723   2734       C  
ATOM    507  CD1 PHE A  98      13.171 -25.291  20.386  1.00 90.22           C  
ANISOU  507  CD1 PHE A  98    16009  10402   7869   1042  -4045   2761       C  
ATOM    508  CD2 PHE A  98      10.788 -25.473  20.278  1.00 87.35           C  
ANISOU  508  CD2 PHE A  98    15967   9947   7273    244  -3598   2819       C  
ATOM    509  CE1 PHE A  98      13.290 -26.620  20.013  1.00 93.73           C  
ANISOU  509  CE1 PHE A  98    16909  10438   8264   1261  -4245   2856       C  
ATOM    510  CE2 PHE A  98      10.904 -26.807  19.905  1.00 92.67           C  
ANISOU  510  CE2 PHE A  98    17118  10198   7894    393  -3808   2931       C  
ATOM    511  CZ  PHE A  98      12.155 -27.378  19.773  1.00 93.06           C  
ANISOU  511  CZ  PHE A  98    17261  10064   8035    926  -4134   2941       C  
ATOM    512  N   SER A  99      13.090 -21.072  22.591  1.00 79.73           N  
ANISOU  512  N   SER A  99    13707  10172   6415    371  -3690   2481       N  
ATOM    513  CA  SER A  99      13.463 -19.691  22.896  1.00 78.49           C  
ANISOU  513  CA  SER A  99    13201  10310   6312    309  -3649   2341       C  
ATOM    514  C   SER A  99      12.530 -18.687  22.246  1.00 79.62           C  
ANISOU  514  C   SER A  99    13087  10593   6572    116  -3279   2168       C  
ATOM    515  O   SER A  99      12.089 -18.896  21.118  1.00 77.19           O  
ANISOU  515  O   SER A  99    12650  10221   6457    167  -3095   2121       O  
ATOM    516  CB  SER A  99      14.892 -19.411  22.412  1.00 82.53           C  
ANISOU  516  CB  SER A  99    13335  10953   7071    643  -3872   2298       C  
ATOM    517  OG  SER A  99      15.184 -18.019  22.432  1.00 90.49           O  
ANISOU  517  OG  SER A  99    13993  12222   8168    528  -3806   2154       O  
ATOM    518  N   ARG A 100      12.257 -17.586  22.945  1.00 76.26           N  
ANISOU  518  N   ARG A 100    12605  10349   6019    -78  -3192   2065       N  
ATOM    519  CA  ARG A 100      11.449 -16.503  22.376  1.00 73.36           C  
ANISOU  519  CA  ARG A 100    12005  10112   5757   -200  -2880   1882       C  
ATOM    520  C   ARG A 100      12.084 -15.937  21.102  1.00 75.16           C  
ANISOU  520  C   ARG A 100    11829  10385   6341    -18  -2857   1781       C  
ATOM    521  O   ARG A 100      11.378 -15.504  20.190  1.00 72.33           O  
ANISOU  521  O   ARG A 100    11302  10047   6131    -49  -2606   1678       O  
ATOM    522  CB  ARG A 100      11.226 -15.386  23.402  1.00 74.15           C  
ANISOU  522  CB  ARG A 100    12163  10369   5641   -372  -2846   1768       C  
ATOM    523  CG  ARG A 100      10.278 -15.747  24.546  1.00 84.55           C  
ANISOU  523  CG  ARG A 100    13836  11718   6573   -597  -2748   1825       C  
ATOM    524  CD  ARG A 100       8.887 -16.186  24.070  1.00 92.78           C  
ANISOU  524  CD  ARG A 100    14904  12777   7571   -738  -2424   1828       C  
ATOM    525  NE  ARG A 100       8.258 -15.221  23.166  1.00 97.79           N  
ANISOU  525  NE  ARG A 100    15230  13522   8405   -700  -2160   1635       N  
ATOM    526  CZ  ARG A 100       7.081 -15.401  22.561  1.00110.25           C  
ANISOU  526  CZ  ARG A 100    16725  15167   9999   -790  -1880   1606       C  
ATOM    527  NH1 ARG A 100       6.378 -16.516  22.754  1.00 95.72           N  
ANISOU  527  NH1 ARG A 100    15088  13301   7982   -976  -1814   1761       N  
ATOM    528  NH2 ARG A 100       6.597 -14.459  21.752  1.00 96.91           N  
ANISOU  528  NH2 ARG A 100    14759  13571   8490   -713  -1685   1430       N  
ATOM    529  N   ILE A 101      13.413 -15.964  21.043  1.00 73.24           N  
ANISOU  529  N   ILE A 101    11421  10188   6217    167  -3123   1821       N  
ATOM    530  CA  ILE A 101      14.155 -15.551  19.851  1.00 71.82           C  
ANISOU  530  CA  ILE A 101    10843  10101   6345    329  -3116   1754       C  
ATOM    531  C   ILE A 101      13.834 -16.491  18.683  1.00 74.97           C  
ANISOU  531  C   ILE A 101    11213  10365   6908    498  -2986   1784       C  
ATOM    532  O   ILE A 101      13.719 -16.048  17.538  1.00 72.18           O  
ANISOU  532  O   ILE A 101    10600  10061   6766    531  -2813   1694       O  
ATOM    533  CB  ILE A 101      15.696 -15.525  20.110  1.00 77.32           C  
ANISOU  533  CB  ILE A 101    11331  10950   7096    494  -3444   1810       C  
ATOM    534  CG1 ILE A 101      16.061 -14.479  21.180  1.00 79.23           C  
ANISOU  534  CG1 ILE A 101    11596  11329   7179    283  -3594   1767       C  
ATOM    535  CG2 ILE A 101      16.460 -15.235  18.827  1.00 76.89           C  
ANISOU  535  CG2 ILE A 101    10838  11047   7331    651  -3411   1758       C  
ATOM    536  CD1 ILE A 101      16.019 -14.994  22.631  1.00 89.07           C  
ANISOU  536  CD1 ILE A 101    13221  12510   8112    222  -3793   1869       C  
ATOM    537  N   CYS A 102      13.682 -17.782  18.981  1.00 73.89           N  
ANISOU  537  N   CYS A 102    11387  10036   6650    590  -3085   1913       N  
ATOM    538  CA  CYS A 102      13.325 -18.778  17.963  1.00 73.47           C  
ANISOU  538  CA  CYS A 102    11412   9797   6705    732  -2994   1942       C  
ATOM    539  C   CYS A 102      11.857 -18.680  17.532  1.00 73.58           C  
ANISOU  539  C   CYS A 102    11519   9748   6691    477  -2684   1893       C  
ATOM    540  O   CYS A 102      11.500 -19.126  16.448  1.00 71.86           O  
ANISOU  540  O   CYS A 102    11265   9432   6607    544  -2561   1869       O  
ATOM    541  CB  CYS A 102      13.638 -20.195  18.461  1.00 77.49           C  
ANISOU  541  CB  CYS A 102    12309  10068   7067    901  -3242   2102       C  
ATOM    542  SG  CYS A 102      13.440 -21.483  17.188  1.00 82.00           S  
ANISOU  542  SG  CYS A 102    13042  10355   7758   1137  -3205   2121       S  
ATOM    543  N   CYS A 103      11.012 -18.110  18.386  1.00 68.92           N  
ANISOU  543  N   CYS A 103    11039   9240   5908    197  -2565   1873       N  
ATOM    544  CA  CYS A 103       9.625 -17.828  18.024  1.00 66.55           C  
ANISOU  544  CA  CYS A 103    10730   8981   5575    -27  -2264   1806       C  
ATOM    545  C   CYS A 103       9.529 -16.620  17.091  1.00 66.23           C  
ANISOU  545  C   CYS A 103    10317   9086   5761     12  -2089   1637       C  
ATOM    546  O   CYS A 103       8.759 -16.631  16.130  1.00 63.82           O  
ANISOU  546  O   CYS A 103     9912   8772   5563    -22  -1894   1587       O  
ATOM    547  CB  CYS A 103       8.785 -17.576  19.275  1.00 68.23           C  
ANISOU  547  CB  CYS A 103    11149   9297   5479   -295  -2181   1821       C  
ATOM    548  SG  CYS A 103       7.131 -16.928  18.941  1.00 70.57           S  
ANISOU  548  SG  CYS A 103    11311   9780   5721   -520  -1802   1698       S  
ATOM    549  N   ASP A 104      10.311 -15.582  17.384  1.00 61.72           N  
ANISOU  549  N   ASP A 104     9571   8637   5243     60  -2181   1561       N  
ATOM    550  CA  ASP A 104      10.328 -14.362  16.573  1.00 59.06           C  
ANISOU  550  CA  ASP A 104     8944   8402   5094     70  -2061   1418       C  
ATOM    551  C   ASP A 104      10.716 -14.678  15.134  1.00 60.66           C  
ANISOU  551  C   ASP A 104     8927   8567   5552    230  -2023   1418       C  
ATOM    552  O   ASP A 104       9.975 -14.342  14.212  1.00 58.42           O  
ANISOU  552  O   ASP A 104     8536   8286   5374    198  -1827   1346       O  
ATOM    553  CB  ASP A 104      11.303 -13.331  17.152  1.00 61.83           C  
ANISOU  553  CB  ASP A 104     9197   8855   5439     57  -2234   1367       C  
ATOM    554  CG  ASP A 104      10.946 -12.908  18.577  1.00 74.86           C  
ANISOU  554  CG  ASP A 104    11090  10543   6812    -93  -2274   1339       C  
ATOM    555  OD1 ASP A 104       9.742 -12.856  18.914  1.00 75.65           O  
ANISOU  555  OD1 ASP A 104    11333  10656   6754   -196  -2075   1290       O  
ATOM    556  OD2 ASP A 104      11.874 -12.625  19.368  1.00 82.99           O  
ANISOU  556  OD2 ASP A 104    12153  11620   7761   -108  -2505   1363       O  
ATOM    557  N   VAL A 105      11.873 -15.326  14.961  1.00 57.84           N  
ANISOU  557  N   VAL A 105     8505   8198   5275    423  -2216   1494       N  
ATOM    558  CA  VAL A 105      12.334 -15.822  13.652  1.00 56.69           C  
ANISOU  558  CA  VAL A 105     8176   8034   5329    625  -2187   1492       C  
ATOM    559  C   VAL A 105      11.216 -16.560  12.933  1.00 59.18           C  
ANISOU  559  C   VAL A 105     8649   8190   5648    591  -2008   1493       C  
ATOM    560  O   VAL A 105      10.875 -16.227  11.796  1.00 56.61           O  
ANISOU  560  O   VAL A 105     8157   7889   5465    595  -1846   1421       O  
ATOM    561  CB  VAL A 105      13.544 -16.798  13.788  1.00 62.84           C  
ANISOU  561  CB  VAL A 105     8955   8802   6118    904  -2429   1580       C  
ATOM    562  CG1 VAL A 105      13.653 -17.729  12.579  1.00 62.51           C  
ANISOU  562  CG1 VAL A 105     8893   8661   6198   1145  -2375   1574       C  
ATOM    563  CG2 VAL A 105      14.838 -16.032  13.979  1.00 63.83           C  
ANISOU  563  CG2 VAL A 105     8760   9178   6313    965  -2591   1567       C  
ATOM    564  N   PHE A 106      10.645 -17.552  13.615  1.00 57.10           N  
ANISOU  564  N   PHE A 106     8722   7766   5205    523  -2052   1586       N  
ATOM    565  CA  PHE A 106       9.543 -18.348  13.067  1.00 56.23           C  
ANISOU  565  CA  PHE A 106     8806   7506   5054    416  -1915   1611       C  
ATOM    566  C   PHE A 106       8.366 -17.496  12.607  1.00 56.20           C  
ANISOU  566  C   PHE A 106     8648   7624   5080    212  -1661   1516       C  
ATOM    567  O   PHE A 106       7.868 -17.684  11.505  1.00 54.17           O  
ANISOU  567  O   PHE A 106     8325   7330   4929    214  -1541   1480       O  
ATOM    568  CB  PHE A 106       9.059 -19.384  14.083  1.00 60.57           C  
ANISOU  568  CB  PHE A 106     9767   7893   5353    270  -2010   1748       C  
ATOM    569  CG  PHE A 106       7.619 -19.781  13.905  1.00 62.08           C  
ANISOU  569  CG  PHE A 106    10114   8046   5429    -20  -1828   1774       C  
ATOM    570  CD1 PHE A 106       7.257 -20.701  12.943  1.00 65.37           C  
ANISOU  570  CD1 PHE A 106    10672   8275   5893    -16  -1810   1802       C  
ATOM    571  CD2 PHE A 106       6.623 -19.227  14.703  1.00 64.42           C  
ANISOU  571  CD2 PHE A 106    10405   8524   5549   -299  -1677   1765       C  
ATOM    572  CE1 PHE A 106       5.923 -21.074  12.775  1.00 66.51           C  
ANISOU  572  CE1 PHE A 106    10935   8419   5916   -336  -1661   1838       C  
ATOM    573  CE2 PHE A 106       5.286 -19.594  14.542  1.00 67.43           C  
ANISOU  573  CE2 PHE A 106    10861   8952   5808   -584  -1504   1795       C  
ATOM    574  CZ  PHE A 106       4.938 -20.518  13.575  1.00 65.64           C  
ANISOU  574  CZ  PHE A 106    10758   8544   5636   -626  -1505   1841       C  
ATOM    575  N   VAL A 107       7.916 -16.567  13.441  1.00 51.92           N  
ANISOU  575  N   VAL A 107     8062   7232   4432     63  -1591   1467       N  
ATOM    576  CA  VAL A 107       6.774 -15.741  13.057  1.00 49.77           C  
ANISOU  576  CA  VAL A 107     7645   7093   4172    -66  -1366   1364       C  
ATOM    577  C   VAL A 107       7.141 -14.734  11.956  1.00 51.32           C  
ANISOU  577  C   VAL A 107     7558   7341   4599     58  -1312   1255       C  
ATOM    578  O   VAL A 107       6.345 -14.540  11.043  1.00 49.92           O  
ANISOU  578  O   VAL A 107     7275   7192   4499     30  -1162   1202       O  
ATOM    579  CB  VAL A 107       6.095 -15.027  14.261  1.00 54.16           C  
ANISOU  579  CB  VAL A 107     8257   7805   4515   -213  -1289   1315       C  
ATOM    580  CG1 VAL A 107       4.891 -14.247  13.803  1.00 52.81           C  
ANISOU  580  CG1 VAL A 107     7920   7790   4353   -270  -1064   1197       C  
ATOM    581  CG2 VAL A 107       5.650 -16.028  15.287  1.00 56.13           C  
ANISOU  581  CG2 VAL A 107     8788   8033   4504   -388  -1318   1440       C  
ATOM    582  N   THR A 108       8.321 -14.114  11.999  1.00 47.47           N  
ANISOU  582  N   THR A 108     6950   6880   4208    168  -1443   1233       N  
ATOM    583  CA  THR A 108       8.642 -13.127  10.957  1.00 45.85           C  
ANISOU  583  CA  THR A 108     6506   6729   4188    220  -1392   1152       C  
ATOM    584  C   THR A 108       8.713 -13.812   9.592  1.00 48.54           C  
ANISOU  584  C   THR A 108     6755   7014   4673    323  -1332   1172       C  
ATOM    585  O   THR A 108       8.089 -13.367   8.630  1.00 46.47           O  
ANISOU  585  O   THR A 108     6395   6768   4496    298  -1198   1115       O  
ATOM    586  CB  THR A 108       9.953 -12.330  11.188  1.00 56.06           C  
ANISOU  586  CB  THR A 108     7664   8095   5541    251  -1551   1143       C  
ATOM    587  OG1 THR A 108      11.075 -13.083  10.720  1.00 57.71           O  
ANISOU  587  OG1 THR A 108     7755   8329   5845    403  -1663   1214       O  
ATOM    588  CG2 THR A 108      10.145 -11.963  12.649  1.00 56.25           C  
ANISOU  588  CG2 THR A 108     7833   8146   5392    166  -1676   1142       C  
ATOM    589  N   LEU A 109       9.465 -14.904   9.512  1.00 46.02           N  
ANISOU  589  N   LEU A 109     6494   6626   4365    461  -1443   1246       N  
ATOM    590  CA  LEU A 109       9.539 -15.673   8.269  1.00 45.32           C  
ANISOU  590  CA  LEU A 109     6379   6465   4376    591  -1394   1248       C  
ATOM    591  C   LEU A 109       8.137 -15.953   7.715  1.00 48.83           C  
ANISOU  591  C   LEU A 109     6930   6834   4788    452  -1237   1228       C  
ATOM    592  O   LEU A 109       7.857 -15.653   6.555  1.00 47.67           O  
ANISOU  592  O   LEU A 109     6656   6712   4745    463  -1130   1175       O  
ATOM    593  CB  LEU A 109      10.333 -16.972   8.461  1.00 47.20           C  
ANISOU  593  CB  LEU A 109     6771   6588   4575    798  -1552   1319       C  
ATOM    594  CG  LEU A 109      11.823 -16.902   8.105  1.00 52.81           C  
ANISOU  594  CG  LEU A 109     7241   7436   5389   1048  -1662   1310       C  
ATOM    595  CD1 LEU A 109      12.513 -15.663   8.682  1.00 52.87           C  
ANISOU  595  CD1 LEU A 109     7004   7659   5424    952  -1722   1299       C  
ATOM    596  CD2 LEU A 109      12.527 -18.185   8.553  1.00 58.05           C  
ANISOU  596  CD2 LEU A 109     8098   7979   5980   1307  -1855   1376       C  
ATOM    597  N   ASP A 110       7.249 -16.485   8.548  1.00 46.29           N  
ANISOU  597  N   ASP A 110     6825   6456   4307    293  -1227   1279       N  
ATOM    598  CA  ASP A 110       5.864 -16.718   8.135  1.00 45.82           C  
ANISOU  598  CA  ASP A 110     6818   6399   4191    110  -1084   1271       C  
ATOM    599  C   ASP A 110       5.202 -15.460   7.530  1.00 48.66           C  
ANISOU  599  C   ASP A 110     6931   6920   4638     73   -937   1168       C  
ATOM    600  O   ASP A 110       4.500 -15.545   6.516  1.00 47.75           O  
ANISOU  600  O   ASP A 110     6756   6813   4575     34   -846   1141       O  
ATOM    601  CB  ASP A 110       5.036 -17.241   9.309  1.00 49.16           C  
ANISOU  601  CB  ASP A 110     7452   6832   4394   -108  -1079   1346       C  
ATOM    602  CG  ASP A 110       3.701 -17.820   8.870  1.00 61.99           C  
ANISOU  602  CG  ASP A 110     9142   8479   5934   -336   -965   1373       C  
ATOM    603  OD1 ASP A 110       3.641 -18.542   7.846  1.00 63.06           O  
ANISOU  603  OD1 ASP A 110     9354   8472   6132   -322   -983   1386       O  
ATOM    604  OD2 ASP A 110       2.700 -17.556   9.562  1.00 68.74           O  
ANISOU  604  OD2 ASP A 110     9963   9517   6638   -537   -858   1377       O  
ATOM    605  N   VAL A 111       5.437 -14.298   8.132  1.00 45.04           N  
ANISOU  605  N   VAL A 111     6363   6566   4183     95   -938   1109       N  
ATOM    606  CA  VAL A 111       4.934 -13.041   7.571  1.00 44.01           C  
ANISOU  606  CA  VAL A 111     6060   6534   4128    108   -842   1009       C  
ATOM    607  C   VAL A 111       5.661 -12.676   6.262  1.00 48.58           C  
ANISOU  607  C   VAL A 111     6501   7070   4886    211   -856    992       C  
ATOM    608  O   VAL A 111       5.045 -12.229   5.287  1.00 46.59           O  
ANISOU  608  O   VAL A 111     6159   6843   4699    210   -773    948       O  
ATOM    609  CB  VAL A 111       5.085 -11.870   8.567  1.00 47.76           C  
ANISOU  609  CB  VAL A 111     6533   7076   4539    114   -873    940       C  
ATOM    610  CG1 VAL A 111       4.539 -10.581   7.969  1.00 46.75           C  
ANISOU  610  CG1 VAL A 111     6299   6990   4473    162   -804    833       C  
ATOM    611  CG2 VAL A 111       4.382 -12.179   9.864  1.00 48.90           C  
ANISOU  611  CG2 VAL A 111     6805   7302   4471     17   -837    947       C  
ATOM    612  N   MET A 112       6.973 -12.882   6.247  1.00 47.50           N  
ANISOU  612  N   MET A 112     6336   6902   4810    298   -964   1031       N  
ATOM    613  CA  MET A 112       7.801 -12.453   5.132  1.00 47.68           C  
ANISOU  613  CA  MET A 112     6195   6955   4967    371   -967   1020       C  
ATOM    614  C   MET A 112       7.479 -13.209   3.865  1.00 52.66           C  
ANISOU  614  C   MET A 112     6822   7539   5646    424   -887   1022       C  
ATOM    615  O   MET A 112       7.340 -12.600   2.809  1.00 51.83           O  
ANISOU  615  O   MET A 112     6614   7468   5612    414   -820    990       O  
ATOM    616  CB  MET A 112       9.275 -12.635   5.469  1.00 51.45           C  
ANISOU  616  CB  MET A 112     6590   7488   5470    461  -1096   1064       C  
ATOM    617  CG  MET A 112      10.223 -11.936   4.506  1.00 55.69           C  
ANISOU  617  CG  MET A 112     6904   8144   6111    475  -1093   1059       C  
ATOM    618  SD  MET A 112      11.903 -12.592   4.588  1.00 62.42           S  
ANISOU  618  SD  MET A 112     7575   9154   6987    645  -1215   1111       S  
ATOM    619  CE  MET A 112      12.101 -12.786   6.361  1.00 60.29           C  
ANISOU  619  CE  MET A 112     7447   8848   6613    626  -1388   1150       C  
ATOM    620  N   MET A 113       7.369 -14.529   3.959  1.00 50.60           N  
ANISOU  620  N   MET A 113     6716   7179   5329    472   -912   1060       N  
ATOM    621  CA  MET A 113       7.045 -15.320   2.783  1.00 50.58           C  
ANISOU  621  CA  MET A 113     6774   7099   5345    514   -856   1049       C  
ATOM    622  C   MET A 113       5.668 -14.904   2.282  1.00 53.59           C  
ANISOU  622  C   MET A 113     7139   7507   5714    357   -752   1018       C  
ATOM    623  O   MET A 113       5.518 -14.559   1.117  1.00 53.09           O  
ANISOU  623  O   MET A 113     6988   7471   5712    372   -692    984       O  
ATOM    624  CB  MET A 113       7.096 -16.819   3.066  1.00 54.63           C  
ANISOU  624  CB  MET A 113     7546   7441   5771    573   -936   1094       C  
ATOM    625  CG  MET A 113       8.465 -17.341   3.572  1.00 60.31           C  
ANISOU  625  CG  MET A 113     8288   8136   6492    801  -1069   1122       C  
ATOM    626  SD  MET A 113       9.969 -16.865   2.642  1.00 65.37           S  
ANISOU  626  SD  MET A 113     8618   8966   7253   1048  -1059   1071       S  
ATOM    627  CE  MET A 113      10.466 -15.349   3.459  1.00 61.52           C  
ANISOU  627  CE  MET A 113     7873   8688   6814    911  -1087   1089       C  
ATOM    628  N   CYS A 114       4.668 -14.873   3.154  1.00 50.13           N  
ANISOU  628  N   CYS A 114     6762   7103   5183    213   -731   1031       N  
ATOM    629  CA  CYS A 114       3.329 -14.503   2.709  1.00 49.24           C  
ANISOU  629  CA  CYS A 114     6579   7082   5046     93   -638    998       C  
ATOM    630  C   CYS A 114       3.291 -13.102   2.109  1.00 51.46           C  
ANISOU  630  C   CYS A 114     6682   7448   5421    161   -600    934       C  
ATOM    631  O   CYS A 114       2.571 -12.867   1.143  1.00 51.00           O  
ANISOU  631  O   CYS A 114     6559   7430   5390    142   -554    909       O  
ATOM    632  CB  CYS A 114       2.321 -14.604   3.840  1.00 50.53           C  
ANISOU  632  CB  CYS A 114     6777   7352   5070    -58   -602   1014       C  
ATOM    633  SG  CYS A 114       0.636 -14.479   3.236  1.00 54.76           S  
ANISOU  633  SG  CYS A 114     7180   8072   5553   -204   -498    986       S  
ATOM    634  N   THR A 115       4.065 -12.178   2.676  1.00 47.28           N  
ANISOU  634  N   THR A 115     6108   6930   4927    225   -643    914       N  
ATOM    635  CA  THR A 115       4.231 -10.839   2.084  1.00 46.30           C  
ANISOU  635  CA  THR A 115     5893   6823   4878    268   -646    870       C  
ATOM    636  C   THR A 115       4.899 -10.912   0.709  1.00 49.42           C  
ANISOU  636  C   THR A 115     6231   7188   5358    298   -639    895       C  
ATOM    637  O   THR A 115       4.461 -10.256  -0.241  1.00 48.42           O  
ANISOU  637  O   THR A 115     6068   7067   5263    295   -614    877       O  
ATOM    638  CB  THR A 115       5.081  -9.910   2.982  1.00 53.85           C  
ANISOU  638  CB  THR A 115     6861   7767   5832    277   -727    856       C  
ATOM    639  OG1 THR A 115       4.302  -9.475   4.103  1.00 53.45           O  
ANISOU  639  OG1 THR A 115     6872   7755   5681    273   -717    799       O  
ATOM    640  CG2 THR A 115       5.560  -8.688   2.199  1.00 51.86           C  
ANISOU  640  CG2 THR A 115     6570   7482   5652    269   -764    845       C  
ATOM    641  N   ALA A 116       5.959 -11.711   0.611  1.00 46.00           N  
ANISOU  641  N   ALA A 116     5795   6739   4944    349   -665    932       N  
ATOM    642  CA  ALA A 116       6.646 -11.915  -0.664  1.00 45.56           C  
ANISOU  642  CA  ALA A 116     5672   6704   4933    403   -632    942       C  
ATOM    643  C   ALA A 116       5.690 -12.470  -1.725  1.00 48.83           C  
ANISOU  643  C   ALA A 116     6151   7075   5325    388   -570    922       C  
ATOM    644  O   ALA A 116       5.749 -12.051  -2.885  1.00 48.62           O  
ANISOU  644  O   ALA A 116     6076   7079   5319    384   -531    917       O  
ATOM    645  CB  ALA A 116       7.865 -12.838  -0.495  1.00 47.22           C  
ANISOU  645  CB  ALA A 116     5861   6938   5144    531   -669    963       C  
ATOM    646  N   SER A 117       4.803 -13.385  -1.325  1.00 44.65           N  
ANISOU  646  N   SER A 117     5742   6486   4735    343   -571    922       N  
ATOM    647  CA  SER A 117       3.900 -14.045  -2.268  1.00 44.26           C  
ANISOU  647  CA  SER A 117     5771   6399   4644    283   -541    910       C  
ATOM    648  C   SER A 117       2.967 -13.037  -2.902  1.00 47.00           C  
ANISOU  648  C   SER A 117     6016   6832   5010    224   -514    891       C  
ATOM    649  O   SER A 117       3.008 -12.812  -4.105  1.00 46.13           O  
ANISOU  649  O   SER A 117     5889   6726   4914    239   -497    882       O  
ATOM    650  CB  SER A 117       3.078 -15.151  -1.586  1.00 48.50           C  
ANISOU  650  CB  SER A 117     6465   6875   5088    167   -567    935       C  
ATOM    651  OG  SER A 117       3.823 -16.354  -1.417  1.00 58.78           O  
ANISOU  651  OG  SER A 117     7961   8025   6350    242   -622    953       O  
ATOM    652  N   ILE A 118       2.131 -12.422  -2.081  1.00 43.45           N  
ANISOU  652  N   ILE A 118     5504   6461   4543    181   -515    879       N  
ATOM    653  CA  ILE A 118       1.123 -11.507  -2.585  1.00 43.06           C  
ANISOU  653  CA  ILE A 118     5360   6503   4498    183   -511    850       C  
ATOM    654  C   ILE A 118       1.749 -10.414  -3.442  1.00 45.35           C  
ANISOU  654  C   ILE A 118     5633   6747   4850    256   -535    851       C  
ATOM    655  O   ILE A 118       1.162 -10.016  -4.446  1.00 45.02           O  
ANISOU  655  O   ILE A 118     5574   6727   4806    261   -550    849       O  
ATOM    656  CB  ILE A 118       0.335 -10.858  -1.433  1.00 46.99           C  
ANISOU  656  CB  ILE A 118     5785   7115   4954    204   -502    812       C  
ATOM    657  CG1 ILE A 118      -0.858 -10.039  -1.963  1.00 48.17           C  
ANISOU  657  CG1 ILE A 118     5821   7391   5091    268   -509    768       C  
ATOM    658  CG2 ILE A 118       1.271  -9.976  -0.568  1.00 47.80           C  
ANISOU  658  CG2 ILE A 118     5925   7149   5089    285   -534    794       C  
ATOM    659  CD1 ILE A 118      -1.948 -10.855  -2.635  1.00 55.97           C  
ANISOU  659  CD1 ILE A 118     6732   8510   6025    151   -498    786       C  
ATOM    660  N   TRP A 119       2.932  -9.936  -3.048  1.00 40.95           N  
ANISOU  660  N   TRP A 119     5088   6139   4334    283   -553    866       N  
ATOM    661  CA  TRP A 119       3.592  -8.838  -3.768  1.00 40.39           C  
ANISOU  661  CA  TRP A 119     5018   6032   4295    281   -584    890       C  
ATOM    662  C   TRP A 119       4.179  -9.280  -5.106  1.00 43.57           C  
ANISOU  662  C   TRP A 119     5414   6452   4691    255   -541    925       C  
ATOM    663  O   TRP A 119       3.968  -8.593  -6.101  1.00 43.79           O  
ANISOU  663  O   TRP A 119     5468   6467   4702    227   -556    947       O  
ATOM    664  CB  TRP A 119       4.631  -8.115  -2.890  1.00 39.48           C  
ANISOU  664  CB  TRP A 119     4908   5892   4203    257   -634    904       C  
ATOM    665  CG  TRP A 119       3.973  -7.090  -1.997  1.00 40.80           C  
ANISOU  665  CG  TRP A 119     5146   6007   4351    296   -697    853       C  
ATOM    666  CD1 TRP A 119       3.729  -7.195  -0.664  1.00 43.77           C  
ANISOU  666  CD1 TRP A 119     5538   6401   4692    331   -704    806       C  
ATOM    667  CD2 TRP A 119       3.425  -5.830  -2.404  1.00 41.33           C  
ANISOU  667  CD2 TRP A 119     5309   5989   4406    337   -766    832       C  
ATOM    668  NE1 TRP A 119       3.084  -6.075  -0.208  1.00 43.94           N  
ANISOU  668  NE1 TRP A 119     5646   6372   4677    410   -757    739       N  
ATOM    669  CE2 TRP A 119       2.878  -5.223  -1.258  1.00 45.75           C  
ANISOU  669  CE2 TRP A 119     5938   6521   4926    432   -808    752       C  
ATOM    670  CE3 TRP A 119       3.348  -5.154  -3.627  1.00 42.96           C  
ANISOU  670  CE3 TRP A 119     5579   6131   4612    315   -808    875       C  
ATOM    671  CZ2 TRP A 119       2.261  -3.972  -1.295  1.00 46.27           C  
ANISOU  671  CZ2 TRP A 119     6144   6479   4959    550   -897    696       C  
ATOM    672  CZ3 TRP A 119       2.741  -3.910  -3.663  1.00 45.50           C  
ANISOU  672  CZ3 TRP A 119     6054   6327   4905    403   -914    843       C  
ATOM    673  CH2 TRP A 119       2.204  -3.333  -2.502  1.00 46.93           C  
ANISOU  673  CH2 TRP A 119     6312   6466   5055    541   -961    746       C  
ATOM    674  N   ASN A 120       4.896 -10.410  -5.140  1.00 39.36           N  
ANISOU  674  N   ASN A 120     4867   5941   4148    287   -493    924       N  
ATOM    675  CA  ASN A 120       5.256 -11.058  -6.416  1.00 38.99           C  
ANISOU  675  CA  ASN A 120     4837   5920   4058    309   -434    922       C  
ATOM    676  C   ASN A 120       4.038 -11.147  -7.300  1.00 41.52           C  
ANISOU  676  C   ASN A 120     5230   6211   4335    267   -443    908       C  
ATOM    677  O   ASN A 120       4.056 -10.708  -8.448  1.00 41.74           O  
ANISOU  677  O   ASN A 120     5274   6263   4324    237   -431    926       O  
ATOM    678  CB  ASN A 120       5.734 -12.498  -6.217  1.00 40.04           C  
ANISOU  678  CB  ASN A 120     5023   6027   4163    411   -407    889       C  
ATOM    679  CG  ASN A 120       7.198 -12.601  -5.945  1.00 62.16           C  
ANISOU  679  CG  ASN A 120     7715   8923   6980    511   -387    897       C  
ATOM    680  OD1 ASN A 120       8.008 -11.913  -6.562  1.00 56.74           O  
ANISOU  680  OD1 ASN A 120     6902   8370   6287    484   -344    924       O  
ATOM    681  ND2 ASN A 120       7.562 -13.495  -5.031  1.00 53.57           N  
ANISOU  681  ND2 ASN A 120     6670   7788   5894    618   -426    883       N  
ATOM    682  N   LEU A 121       2.977 -11.721  -6.743  1.00 37.09           N  
ANISOU  682  N   LEU A 121     4706   5623   3762    240   -472    884       N  
ATOM    683  CA  LEU A 121       1.733 -11.905  -7.467  1.00 37.01           C  
ANISOU  683  CA  LEU A 121     4725   5634   3703    175   -500    874       C  
ATOM    684  C   LEU A 121       1.279 -10.607  -8.104  1.00 40.86           C  
ANISOU  684  C   LEU A 121     5164   6160   4201    186   -545    894       C  
ATOM    685  O   LEU A 121       0.814 -10.610  -9.231  1.00 41.71           O  
ANISOU  685  O   LEU A 121     5309   6283   4256    155   -571    902       O  
ATOM    686  CB  LEU A 121       0.646 -12.430  -6.539  1.00 37.25           C  
ANISOU  686  CB  LEU A 121     4734   5707   3712    102   -524    864       C  
ATOM    687  CG  LEU A 121      -0.029 -13.705  -7.020  1.00 42.77           C  
ANISOU  687  CG  LEU A 121     5542   6383   4324    -25   -544    858       C  
ATOM    688  CD1 LEU A 121       0.954 -14.593  -7.756  1.00 43.31           C  
ANISOU  688  CD1 LEU A 121     5788   6313   4356     27   -524    838       C  
ATOM    689  CD2 LEU A 121      -0.625 -14.442  -5.831  1.00 45.64           C  
ANISOU  689  CD2 LEU A 121     5921   6774   4647   -143   -552    874       C  
ATOM    690  N   CYS A 122       1.434  -9.506  -7.379  1.00 36.27           N  
ANISOU  690  N   CYS A 122     4539   5570   3671    236   -575    902       N  
ATOM    691  CA  CYS A 122       1.157  -8.176  -7.909  1.00 36.13           C  
ANISOU  691  CA  CYS A 122     4551   5523   3654    271   -649    926       C  
ATOM    692  C   CYS A 122       2.176  -7.749  -8.966  1.00 40.54           C  
ANISOU  692  C   CYS A 122     5183   6037   4181    205   -636    988       C  
ATOM    693  O   CYS A 122       1.804  -7.117  -9.957  1.00 41.25           O  
ANISOU  693  O   CYS A 122     5347   6103   4224    192   -696   1026       O  
ATOM    694  CB  CYS A 122       1.122  -7.154  -6.767  1.00 36.37           C  
ANISOU  694  CB  CYS A 122     4586   5510   3723    347   -699    902       C  
ATOM    695  SG  CYS A 122       1.306  -5.423  -7.260  1.00 41.14           S  
ANISOU  695  SG  CYS A 122     5348   5968   4315    380   -823    943       S  
ATOM    696  N   ALA A 123       3.453  -8.072  -8.757  1.00 36.87           N  
ANISOU  696  N   ALA A 123     4686   5593   3728    161   -563   1005       N  
ATOM    697  CA  ALA A 123       4.498  -7.761  -9.744  1.00 37.54           C  
ANISOU  697  CA  ALA A 123     4786   5723   3756     73   -518   1066       C  
ATOM    698  C   ALA A 123       4.169  -8.384 -11.084  1.00 41.51           C  
ANISOU  698  C   ALA A 123     5340   6266   4166     68   -475   1060       C  
ATOM    699  O   ALA A 123       4.279  -7.738 -12.115  1.00 42.13           O  
ANISOU  699  O   ALA A 123     5490   6353   4164    -12   -489   1120       O  
ATOM    700  CB  ALA A 123       5.851  -8.247  -9.270  1.00 38.65           C  
ANISOU  700  CB  ALA A 123     4810   5962   3912     68   -435   1066       C  
ATOM    701  N   ILE A 124       3.770  -9.649 -11.046  1.00 37.69           N  
ANISOU  701  N   ILE A 124     4858   5789   3672    132   -437    990       N  
ATOM    702  CA  ILE A 124       3.271 -10.358 -12.221  1.00 37.97           C  
ANISOU  702  CA  ILE A 124     4988   5834   3606    120   -425    963       C  
ATOM    703  C   ILE A 124       2.056  -9.683 -12.847  1.00 41.11           C  
ANISOU  703  C   ILE A 124     5438   6209   3972     76   -538    995       C  
ATOM    704  O   ILE A 124       1.988  -9.563 -14.059  1.00 41.65           O  
ANISOU  704  O   ILE A 124     5595   6296   3933     28   -548   1020       O  
ATOM    705  CB  ILE A 124       2.886 -11.808 -11.859  1.00 41.15           C  
ANISOU  705  CB  ILE A 124     5443   6192   3999    161   -413    886       C  
ATOM    706  CG1 ILE A 124       4.146 -12.679 -11.798  1.00 42.38           C  
ANISOU  706  CG1 ILE A 124     5612   6362   4127    268   -311    840       C  
ATOM    707  CG2 ILE A 124       1.866 -12.375 -12.852  1.00 42.33           C  
ANISOU  707  CG2 ILE A 124     5714   6322   4048     94   -468    860       C  
ATOM    708  CD1 ILE A 124       3.968 -13.920 -10.955  1.00 50.41           C  
ANISOU  708  CD1 ILE A 124     6719   7275   5162    324   -335    786       C  
ATOM    709  N   SER A 125       1.094  -9.261 -12.029  1.00 36.60           N  
ANISOU  709  N   SER A 125     4808   5624   3476    111   -627    990       N  
ATOM    710  CA  SER A 125      -0.110  -8.592 -12.531  1.00 36.80           C  
ANISOU  710  CA  SER A 125     4843   5667   3474    131   -754   1011       C  
ATOM    711  C   SER A 125       0.241  -7.431 -13.417  1.00 41.10           C  
ANISOU  711  C   SER A 125     5503   6150   3964    117   -814   1090       C  
ATOM    712  O   SER A 125      -0.311  -7.296 -14.501  1.00 41.89           O  
ANISOU  712  O   SER A 125     5681   6263   3971     94   -892   1122       O  
ATOM    713  CB  SER A 125      -0.946  -8.042 -11.397  1.00 40.40           C  
ANISOU  713  CB  SER A 125     5190   6150   4010    233   -820    982       C  
ATOM    714  OG  SER A 125      -1.211  -9.051 -10.460  1.00 50.25           O  
ANISOU  714  OG  SER A 125     6340   7464   5287    204   -757    930       O  
ATOM    715  N   ILE A 126       1.149  -6.586 -12.940  1.00 37.08           N  
ANISOU  715  N   ILE A 126     5026   5569   3493    101   -798   1132       N  
ATOM    716  CA  ILE A 126       1.615  -5.435 -13.707  1.00 37.76           C  
ANISOU  716  CA  ILE A 126     5269   5573   3505     21   -864   1233       C  
ATOM    717  C   ILE A 126       2.338  -5.904 -14.962  1.00 41.63           C  
ANISOU  717  C   ILE A 126     5808   6149   3862   -113   -764   1277       C  
ATOM    718  O   ILE A 126       2.168  -5.337 -16.045  1.00 42.75           O  
ANISOU  718  O   ILE A 126     6099   6262   3884   -183   -834   1356       O  
ATOM    719  CB  ILE A 126       2.551  -4.547 -12.864  1.00 41.06           C  
ANISOU  719  CB  ILE A 126     5721   5906   3974    -40   -869   1274       C  
ATOM    720  CG1 ILE A 126       1.773  -3.923 -11.702  1.00 41.34           C  
ANISOU  720  CG1 ILE A 126     5768   5838   4103    122   -981   1215       C  
ATOM    721  CG2 ILE A 126       3.173  -3.459 -13.713  1.00 43.57           C  
ANISOU  721  CG2 ILE A 126     6233   6140   4182   -210   -933   1403       C  
ATOM    722  CD1 ILE A 126       2.629  -3.112 -10.778  1.00 48.68           C  
ANISOU  722  CD1 ILE A 126     6768   6660   5069     56  -1009   1235       C  
ATOM    723  N   ASP A 127       3.137  -6.955 -14.814  1.00 36.81           N  
ANISOU  723  N   ASP A 127     5086   5649   3253   -124   -604   1221       N  
ATOM    724  CA  ASP A 127       3.859  -7.535 -15.947  1.00 37.06           C  
ANISOU  724  CA  ASP A 127     5145   5800   3136   -194   -479   1224       C  
ATOM    725  C   ASP A 127       2.908  -7.912 -17.076  1.00 40.19           C  
ANISOU  725  C   ASP A 127     5671   6186   3415   -192   -542   1209       C  
ATOM    726  O   ASP A 127       3.192  -7.634 -18.232  1.00 41.51           O  
ANISOU  726  O   ASP A 127     5948   6404   3418   -288   -521   1267       O  
ATOM    727  CB  ASP A 127       4.682  -8.744 -15.494  1.00 38.30           C  
ANISOU  727  CB  ASP A 127     5176   6058   3318   -108   -325   1129       C  
ATOM    728  CG  ASP A 127       5.317  -9.490 -16.646  1.00 46.73           C  
ANISOU  728  CG  ASP A 127     6280   7261   4213   -100   -188   1088       C  
ATOM    729  OD1 ASP A 127       6.384  -9.042 -17.129  1.00 48.72           O  
ANISOU  729  OD1 ASP A 127     6468   7676   4367   -186    -79   1145       O  
ATOM    730  OD2 ASP A 127       4.758 -10.538 -17.040  1.00 50.09           O  
ANISOU  730  OD2 ASP A 127     6804   7644   4585    -18   -188    994       O  
ATOM    731  N   ARG A 128       1.775  -8.517 -16.746  1.00 35.10           N  
ANISOU  731  N   ARG A 128     5009   5498   2831   -114   -628   1141       N  
ATOM    732  CA  ARG A 128       0.778  -8.847 -17.766  1.00 35.65           C  
ANISOU  732  CA  ARG A 128     5183   5577   2786   -141   -727   1131       C  
ATOM    733  C   ARG A 128       0.124  -7.582 -18.311  1.00 40.29           C  
ANISOU  733  C   ARG A 128     5857   6118   3333   -153   -898   1236       C  
ATOM    734  O   ARG A 128       0.021  -7.410 -19.517  1.00 41.40           O  
ANISOU  734  O   ARG A 128     6145   6274   3313   -225   -945   1287       O  
ATOM    735  CB  ARG A 128      -0.290  -9.809 -17.235  1.00 35.42           C  
ANISOU  735  CB  ARG A 128     5087   5555   2817   -111   -790   1048       C  
ATOM    736  CG  ARG A 128       0.234 -11.089 -16.561  1.00 45.64           C  
ANISOU  736  CG  ARG A 128     6362   6831   4148    -92   -668    954       C  
ATOM    737  CD  ARG A 128       1.564 -11.581 -17.127  1.00 55.90           C  
ANISOU  737  CD  ARG A 128     7746   8147   5348    -61   -507    917       C  
ATOM    738  NE  ARG A 128       1.503 -11.811 -18.571  1.00 65.37           N  
ANISOU  738  NE  ARG A 128     9112   9376   6349   -115   -507    904       N  
ATOM    739  CZ  ARG A 128       2.562 -11.864 -19.385  1.00 81.16           C  
ANISOU  739  CZ  ARG A 128    11173  11458   8206    -95   -366    890       C  
ATOM    740  NH1 ARG A 128       3.794 -11.691 -18.923  1.00 70.43           N  
ANISOU  740  NH1 ARG A 128     9685  10186   6889    -29   -218    895       N  
ATOM    741  NH2 ARG A 128       2.392 -12.079 -20.684  1.00 68.79           N  
ANISOU  741  NH2 ARG A 128     9781   9923   6432   -149   -371    871       N  
ATOM    742  N   TYR A 129      -0.299  -6.690 -17.426  1.00 35.67           N  
ANISOU  742  N   TYR A 129     5213   5464   2875    -62  -1000   1262       N  
ATOM    743  CA  TYR A 129      -0.847  -5.395 -17.833  1.00 36.26           C  
ANISOU  743  CA  TYR A 129     5420   5446   2913    -15  -1188   1356       C  
ATOM    744  C   TYR A 129      -0.018  -4.742 -18.927  1.00 42.10           C  
ANISOU  744  C   TYR A 129     6376   6132   3488   -172  -1180   1477       C  
ATOM    745  O   TYR A 129      -0.577  -4.198 -19.869  1.00 43.22           O  
ANISOU  745  O   TYR A 129     6683   6229   3509   -179  -1335   1555       O  
ATOM    746  CB  TYR A 129      -0.955  -4.470 -16.620  1.00 36.38           C  
ANISOU  746  CB  TYR A 129     5400   5355   3067    116  -1257   1351       C  
ATOM    747  CG  TYR A 129      -1.299  -3.027 -16.907  1.00 39.11           C  
ANISOU  747  CG  TYR A 129     5961   5530   3369    198  -1464   1442       C  
ATOM    748  CD1 TYR A 129      -2.610  -2.634 -17.148  1.00 42.23           C  
ANISOU  748  CD1 TYR A 129     6359   5933   3752    403  -1666   1431       C  
ATOM    749  CD2 TYR A 129      -0.318  -2.044 -16.889  1.00 40.67           C  
ANISOU  749  CD2 TYR A 129     6367   5557   3529     74  -1478   1540       C  
ATOM    750  CE1 TYR A 129      -2.931  -1.297 -17.394  1.00 44.75           C  
ANISOU  750  CE1 TYR A 129     6926   6055   4022    537  -1887   1507       C  
ATOM    751  CE2 TYR A 129      -0.632  -0.706 -17.131  1.00 43.69           C  
ANISOU  751  CE2 TYR A 129     7033   5716   3853    143  -1702   1629       C  
ATOM    752  CZ  TYR A 129      -1.939  -0.345 -17.381  1.00 51.19           C  
ANISOU  752  CZ  TYR A 129     8019   6637   4793    404  -1910   1607       C  
ATOM    753  OH  TYR A 129      -2.243   0.967 -17.621  1.00 53.27           O  
ANISOU  753  OH  TYR A 129     8607   6645   4988    525  -2157   1688       O  
ATOM    754  N   THR A 130       1.307  -4.806 -18.826  1.00 39.30           N  
ANISOU  754  N   THR A 130     6008   5815   3109   -310  -1005   1501       N  
ATOM    755  CA  THR A 130       2.147  -4.220 -19.877  1.00 41.42           C  
ANISOU  755  CA  THR A 130     6450   6100   3187   -513   -968   1628       C  
ATOM    756  C   THR A 130       2.179  -5.085 -21.135  1.00 45.78           C  
ANISOU  756  C   THR A 130     7050   6798   3548   -576   -876   1602       C  
ATOM    757  O   THR A 130       2.136  -4.563 -22.245  1.00 46.90           O  
ANISOU  757  O   THR A 130     7393   6931   3495   -696   -943   1708       O  
ATOM    758  CB  THR A 130       3.589  -3.920 -19.417  1.00 53.45           C  
ANISOU  758  CB  THR A 130     7900   7692   4715   -675   -811   1676       C  
ATOM    759  OG1 THR A 130       4.313  -5.141 -19.244  1.00 54.54           O  
ANISOU  759  OG1 THR A 130     7823   8032   4868   -639   -588   1564       O  
ATOM    760  CG2 THR A 130       3.585  -3.127 -18.117  1.00 51.98           C  
ANISOU  760  CG2 THR A 130     7700   7346   4703   -626   -912   1684       C  
ATOM    761  N   ALA A 131       2.238  -6.400 -20.972  1.00 41.22           N  
ANISOU  761  N   ALA A 131     6330   6330   3000   -493   -739   1460       N  
ATOM    762  CA  ALA A 131       2.172  -7.298 -22.125  1.00 41.88           C  
ANISOU  762  CA  ALA A 131     6508   6516   2888   -522   -672   1402       C  
ATOM    763  C   ALA A 131       0.834  -7.209 -22.872  1.00 45.71           C  
ANISOU  763  C   ALA A 131     7136   6936   3295   -512   -893   1424       C  
ATOM    764  O   ALA A 131       0.759  -7.593 -24.028  1.00 46.43           O  
ANISOU  764  O   ALA A 131     7379   7089   3173   -583   -887   1417       O  
ATOM    765  CB  ALA A 131       2.448  -8.730 -21.701  1.00 41.65           C  
ANISOU  765  CB  ALA A 131     6367   6550   2907   -412   -523   1235       C  
ATOM    766  N   VAL A 132      -0.209  -6.704 -22.214  1.00 41.66           N  
ANISOU  766  N   VAL A 132     6563   6327   2938   -409  -1090   1443       N  
ATOM    767  CA  VAL A 132      -1.536  -6.563 -22.823  1.00 42.26           C  
ANISOU  767  CA  VAL A 132     6708   6395   2955   -367  -1326   1467       C  
ATOM    768  C   VAL A 132      -1.776  -5.181 -23.417  1.00 48.57           C  
ANISOU  768  C   VAL A 132     7702   7088   3664   -370  -1521   1625       C  
ATOM    769  O   VAL A 132      -2.252  -5.066 -24.546  1.00 50.40           O  
ANISOU  769  O   VAL A 132     8103   7336   3710   -422  -1656   1686       O  
ATOM    770  CB  VAL A 132      -2.638  -6.824 -21.803  1.00 44.46           C  
ANISOU  770  CB  VAL A 132     6770   6698   3426   -223  -1436   1392       C  
ATOM    771  CG1 VAL A 132      -3.959  -6.221 -22.281  1.00 45.70           C  
ANISOU  771  CG1 VAL A 132     6940   6881   3543   -131  -1714   1447       C  
ATOM    772  CG2 VAL A 132      -2.764  -8.317 -21.545  1.00 43.20           C  
ANISOU  772  CG2 VAL A 132     6507   6622   3284   -274  -1328   1259       C  
ATOM    773  N   VAL A 133      -1.463  -4.141 -22.647  1.00 45.32           N  
ANISOU  773  N   VAL A 133     7305   6545   3369   -315  -1558   1691       N  
ATOM    774  CA  VAL A 133      -1.619  -2.759 -23.108  1.00 47.57           C  
ANISOU  774  CA  VAL A 133     7853   6658   3565   -312  -1769   1847       C  
ATOM    775  C   VAL A 133      -0.604  -2.401 -24.197  1.00 54.78           C  
ANISOU  775  C   VAL A 133     9018   7564   4234   -583  -1686   1985       C  
ATOM    776  O   VAL A 133      -0.962  -1.774 -25.190  1.00 56.38           O  
ANISOU  776  O   VAL A 133     9484   7689   4251   -635  -1868   2111       O  
ATOM    777  CB  VAL A 133      -1.493  -1.747 -21.945  1.00 50.98           C  
ANISOU  777  CB  VAL A 133     8299   6906   4165   -194  -1841   1867       C  
ATOM    778  CG1 VAL A 133      -1.597  -0.311 -22.454  1.00 53.55           C  
ANISOU  778  CG1 VAL A 133     8991   6985   4372   -196  -2087   2033       C  
ATOM    779  CG2 VAL A 133      -2.563  -2.003 -20.907  1.00 49.65           C  
ANISOU  779  CG2 VAL A 133     7882   6787   4197     89  -1918   1733       C  
ATOM    780  N   MET A 134       0.652  -2.802 -24.009  1.00 52.12           N  
ANISOU  780  N   MET A 134     8586   7338   3879   -753  -1416   1965       N  
ATOM    781  CA  MET A 134       1.738  -2.452 -24.926  1.00 54.52           C  
ANISOU  781  CA  MET A 134     9059   7718   3937  -1037  -1290   2095       C  
ATOM    782  C   MET A 134       2.430  -3.708 -25.448  1.00 58.36           C  
ANISOU  782  C   MET A 134     9396   8477   4302  -1099  -1007   1981       C  
ATOM    783  O   MET A 134       3.599  -3.938 -25.149  1.00 57.96           O  
ANISOU  783  O   MET A 134     9192   8585   4245  -1199   -770   1961       O  
ATOM    784  CB  MET A 134       2.743  -1.549 -24.209  1.00 57.65           C  
ANISOU  784  CB  MET A 134     9474   8041   4390  -1200  -1239   2196       C  
ATOM    785  CG  MET A 134       2.304  -0.092 -24.138  1.00 64.00           C  
ANISOU  785  CG  MET A 134    10604   8531   5182  -1221  -1534   2356       C  
ATOM    786  SD  MET A 134       3.627   1.037 -23.610  1.00 70.77           S  
ANISOU  786  SD  MET A 134    11598   9288   6004  -1559  -1498   2518       S  
ATOM    787  CE  MET A 134       3.447   2.354 -24.846  1.00 71.85           C  
ANISOU  787  CE  MET A 134    12288   9177   5834  -1804  -1766   2787       C  
ATOM    788  N   PRO A 135       1.716  -4.508 -26.265  1.00 55.26           N  
ANISOU  788  N   PRO A 135     9060   8145   3790  -1031  -1047   1902       N  
ATOM    789  CA  PRO A 135       2.158  -5.862 -26.597  1.00 54.82           C  
ANISOU  789  CA  PRO A 135     8897   8285   3646  -1001   -815   1737       C  
ATOM    790  C   PRO A 135       3.325  -5.940 -27.572  1.00 61.99           C  
ANISOU  790  C   PRO A 135     9878   9415   4260  -1183   -578   1775       C  
ATOM    791  O   PRO A 135       4.144  -6.855 -27.453  1.00 61.42           O  
ANISOU  791  O   PRO A 135     9646   9528   4162  -1116   -326   1636       O  
ATOM    792  CB  PRO A 135       0.917  -6.500 -27.230  1.00 56.66           C  
ANISOU  792  CB  PRO A 135     9239   8477   3810   -919   -995   1664       C  
ATOM    793  CG  PRO A 135      -0.060  -5.388 -27.463  1.00 61.92           C  
ANISOU  793  CG  PRO A 135    10057   8989   4480   -916  -1306   1816       C  
ATOM    794  CD  PRO A 135       0.572  -4.099 -27.093  1.00 58.09           C  
ANISOU  794  CD  PRO A 135     9643   8396   4032  -1005  -1325   1979       C  
ATOM    795  N   VAL A 136       3.384  -5.006 -28.526  1.00 61.37           N  
ANISOU  795  N   VAL A 136    10044   9331   3944  -1394   -663   1958       N  
ATOM    796  CA  VAL A 136       4.438  -4.984 -29.544  1.00 64.08           C  
ANISOU  796  CA  VAL A 136    10461   9935   3953  -1612   -433   2017       C  
ATOM    797  C   VAL A 136       5.762  -4.539 -28.942  1.00 69.90           C  
ANISOU  797  C   VAL A 136    10985  10846   4728  -1764   -218   2085       C  
ATOM    798  O   VAL A 136       6.825  -4.974 -29.378  1.00 71.54           O  
ANISOU  798  O   VAL A 136    11058  11387   4738  -1842     72   2041       O  
ATOM    799  CB  VAL A 136       4.099  -4.030 -30.693  1.00 70.53           C  
ANISOU  799  CB  VAL A 136    11634  10681   4483  -1843   -610   2229       C  
ATOM    800  CG1 VAL A 136       5.204  -4.051 -31.727  1.00 73.57           C  
ANISOU  800  CG1 VAL A 136    12074  11391   4489  -2096   -339   2290       C  
ATOM    801  CG2 VAL A 136       2.770  -4.400 -31.335  1.00 70.31           C  
ANISOU  801  CG2 VAL A 136    11803  10511   4400  -1707   -860   2179       C  
ATOM    802  N   HIS A 137       5.681  -3.662 -27.944  1.00 66.24           N  
ANISOU  802  N   HIS A 137    10489  10178   4502  -1799   -369   2186       N  
ATOM    803  CA  HIS A 137       6.848  -3.196 -27.194  1.00 67.17           C  
ANISOU  803  CA  HIS A 137    10400  10431   4692  -1964   -220   2253       C  
ATOM    804  C   HIS A 137       7.299  -4.200 -26.113  1.00 69.78           C  
ANISOU  804  C   HIS A 137    10359  10888   5266  -1715    -44   2048       C  
ATOM    805  O   HIS A 137       8.493  -4.322 -25.846  1.00 70.49           O  
ANISOU  805  O   HIS A 137    10195  11265   5321  -1806    179   2042       O  
ATOM    806  CB  HIS A 137       6.546  -1.822 -26.576  1.00 68.22           C  
ANISOU  806  CB  HIS A 137    10728  10243   4951  -2105   -488   2435       C  
ATOM    807  CG  HIS A 137       7.511  -1.406 -25.508  1.00 71.46           C  
ANISOU  807  CG  HIS A 137    10929  10714   5508  -2237   -406   2471       C  
ATOM    808  ND1 HIS A 137       8.664  -0.699 -25.779  1.00 76.29           N  
ANISOU  808  ND1 HIS A 137    11535  11529   5923  -2640   -294   2648       N  
ATOM    809  CD2 HIS A 137       7.489  -1.594 -24.167  1.00 70.69           C  
ANISOU  809  CD2 HIS A 137    10623  10521   5715  -2048   -429   2361       C  
ATOM    810  CE1 HIS A 137       9.311  -0.471 -24.650  1.00 74.95           C  
ANISOU  810  CE1 HIS A 137    11155  11383   5941  -2693   -268   2641       C  
ATOM    811  NE2 HIS A 137       8.621  -1.006 -23.657  1.00 71.81           N  
ANISOU  811  NE2 HIS A 137    10643  10796   5846  -2324   -348   2464       N  
ATOM    812  N   TYR A 138       6.348  -4.901 -25.494  1.00 64.17           N  
ANISOU  812  N   TYR A 138     9614   9982   4784  -1417   -158   1893       N  
ATOM    813  CA  TYR A 138       6.657  -5.927 -24.494  1.00 62.18           C  
ANISOU  813  CA  TYR A 138     9082   9802   4744  -1178    -26   1706       C  
ATOM    814  C   TYR A 138       7.538  -7.032 -25.062  1.00 70.27           C  
ANISOU  814  C   TYR A 138     9966  11144   5590  -1082    257   1564       C  
ATOM    815  O   TYR A 138       8.500  -7.435 -24.419  1.00 69.69           O  
ANISOU  815  O   TYR A 138     9624  11265   5590   -999    430   1494       O  
ATOM    816  CB  TYR A 138       5.372  -6.552 -23.933  1.00 60.48           C  
ANISOU  816  CB  TYR A 138     8904   9342   4735   -934   -201   1582       C  
ATOM    817  CG  TYR A 138       5.604  -7.612 -22.858  1.00 60.06           C  
ANISOU  817  CG  TYR A 138     8625   9311   4884   -712    -99   1412       C  
ATOM    818  CD1 TYR A 138       5.780  -7.256 -21.520  1.00 60.19           C  
ANISOU  818  CD1 TYR A 138     8479   9247   5143   -674   -140   1426       C  
ATOM    819  CD2 TYR A 138       5.642  -8.967 -23.179  1.00 60.91           C  
ANISOU  819  CD2 TYR A 138     8732   9493   4919   -541     18   1237       C  
ATOM    820  CE1 TYR A 138       6.000  -8.215 -20.538  1.00 58.77           C  
ANISOU  820  CE1 TYR A 138     8125   9080   5125   -483    -64   1289       C  
ATOM    821  CE2 TYR A 138       5.860  -9.934 -22.197  1.00 60.42           C  
ANISOU  821  CE2 TYR A 138     8526   9408   5023   -340     81   1097       C  
ATOM    822  CZ  TYR A 138       6.038  -9.548 -20.880  1.00 64.48           C  
ANISOU  822  CZ  TYR A 138     8864   9861   5775   -317     40   1133       C  
ATOM    823  OH  TYR A 138       6.254 -10.497 -19.908  1.00 62.12           O  
ANISOU  823  OH  TYR A 138     8452   9532   5619   -128     86   1011       O  
ATOM    824  N   GLN A 139       7.197  -7.532 -26.251  1.00 70.95           N  
ANISOU  824  N   GLN A 139    10243  11284   5432  -1065    289   1510       N  
ATOM    825  CA  GLN A 139       7.981  -8.585 -26.915  1.00 73.86           C  
ANISOU  825  CA  GLN A 139    10539  11943   5580   -929    556   1347       C  
ATOM    826  C   GLN A 139       9.417  -8.153 -27.206  1.00 83.86           C  
ANISOU  826  C   GLN A 139    11583  13623   6658  -1092    817   1426       C  
ATOM    827  O   GLN A 139      10.344  -8.969 -27.133  1.00 84.82           O  
ANISOU  827  O   GLN A 139    11473  14036   6716   -895   1057   1275       O  
ATOM    828  CB  GLN A 139       7.332  -8.998 -28.232  1.00 76.68           C  
ANISOU  828  CB  GLN A 139    11200  12275   5660   -935    520   1296       C  
ATOM    829  CG  GLN A 139       6.084  -9.825 -28.079  1.00 89.25           C  
ANISOU  829  CG  GLN A 139    12965  13570   7375   -758    318   1163       C  
ATOM    830  CD  GLN A 139       5.420 -10.114 -29.413  1.00111.92           C  
ANISOU  830  CD  GLN A 139    16153  16418   9952   -817    242   1133       C  
ATOM    831  OE1 GLN A 139       4.198 -10.109 -29.519  1.00106.13           O  
ANISOU  831  OE1 GLN A 139    15588  15457   9280   -842    -18   1153       O  
ATOM    832  NE2 GLN A 139       6.225 -10.357 -30.443  1.00108.85           N  
ANISOU  832  NE2 GLN A 139    15831  16302   9224   -843    469   1084       N  
ATOM    833  N   HIS A 140       9.586  -6.877 -27.551  1.00 84.37           N  
ANISOU  833  N   HIS A 140    11724  13721   6614  -1453    757   1665       N  
ATOM    834  CA  HIS A 140      10.896  -6.305 -27.851  1.00 88.80           C  
ANISOU  834  CA  HIS A 140    12075  14699   6967  -1724    981   1790       C  
ATOM    835  C   HIS A 140      11.738  -6.105 -26.587  1.00 94.71           C  
ANISOU  835  C   HIS A 140    12464  15566   7954  -1730   1031   1806       C  
ATOM    836  O   HIS A 140      12.935  -6.408 -26.574  1.00 96.47           O  
ANISOU  836  O   HIS A 140    12345  16242   8068  -1724   1289   1762       O  
ATOM    837  CB  HIS A 140      10.718  -4.969 -28.562  1.00 91.83           C  
ANISOU  837  CB  HIS A 140    12734  15005   7153  -2161    846   2067       C  
ATOM    838  CG  HIS A 140      11.983  -4.420 -29.135  1.00 99.62           C  
ANISOU  838  CG  HIS A 140    13555  16462   7834  -2526   1085   2217       C  
ATOM    839  ND1 HIS A 140      12.931  -3.778 -28.366  1.00102.42           N  
ANISOU  839  ND1 HIS A 140    13635  17007   8274  -2770   1138   2340       N  
ATOM    840  CD2 HIS A 140      12.457  -4.414 -30.406  1.00105.46           C  
ANISOU  840  CD2 HIS A 140    14356  17557   8159  -2720   1287   2271       C  
ATOM    841  CE1 HIS A 140      13.936  -3.401 -29.138  1.00106.24           C  
ANISOU  841  CE1 HIS A 140    13989  17965   8412  -3121   1365   2473       C  
ATOM    842  NE2 HIS A 140      13.673  -3.774 -30.381  1.00108.53           N  
ANISOU  842  NE2 HIS A 140    14478  18371   8388  -3090   1471   2432       N  
ATOM    843  N   GLY A 141      11.105  -5.589 -25.535  1.00 90.82           N  
ANISOU  843  N   GLY A 141    12042  14696   7768  -1731    781   1863       N  
ATOM    844  CA  GLY A 141      11.776  -5.316 -24.257  1.00 90.83           C  
ANISOU  844  CA  GLY A 141    11762  14748   8003  -1758    776   1886       C  
ATOM    845  C   GLY A 141      11.895  -6.497 -23.296  1.00 95.17           C  
ANISOU  845  C   GLY A 141    12067  15311   8783  -1348    841   1662       C  
ATOM    846  O   GLY A 141      12.344  -6.324 -22.152  1.00 94.15           O  
ANISOU  846  O   GLY A 141    11726  15187   8858  -1341    803   1672       O  
ATOM    847  N   THR A 142      11.451  -7.682 -23.731  1.00 92.57           N  
ANISOU  847  N   THR A 142    11816  14947   8410  -1021    907   1465       N  
ATOM    848  CA  THR A 142      11.757  -8.945 -23.035  1.00 92.04           C  
ANISOU  848  CA  THR A 142    11560  14933   8478   -628    998   1249       C  
ATOM    849  C   THR A 142      12.865  -9.701 -23.788  1.00100.60           C  
ANISOU  849  C   THR A 142    12437  16485   9303   -460   1295   1124       C  
ATOM    850  O   THR A 142      13.562 -10.535 -23.195  1.00100.98           O  
ANISOU  850  O   THR A 142    12243  16702   9424   -151   1403    977       O  
ATOM    851  CB  THR A 142      10.498  -9.854 -22.838  1.00 96.83           C  
ANISOU  851  CB  THR A 142    12431  15140   9220   -366    839   1100       C  
ATOM    852  OG1 THR A 142       9.912 -10.180 -24.108  1.00 96.71           O  
ANISOU  852  OG1 THR A 142    12689  15087   8969   -369    850   1053       O  
ATOM    853  CG2 THR A 142       9.464  -9.163 -21.935  1.00 92.05           C  
ANISOU  853  CG2 THR A 142    11941  14159   8875   -472    574   1200       C  
ATOM    854  N   GLY A 143      13.023  -9.391 -25.081  1.00100.17           N  
ANISOU  854  N   GLY A 143    12482  16648   8929   -644   1421   1181       N  
ATOM    855  CA  GLY A 143      14.113  -9.923 -25.907  1.00104.16           C  
ANISOU  855  CA  GLY A 143    12769  17679   9128   -521   1735   1075       C  
ATOM    856  C   GLY A 143      15.260  -8.922 -25.951  1.00111.24           C  
ANISOU  856  C   GLY A 143    13318  19053   9895   -892   1883   1272       C  
ATOM    857  O   GLY A 143      15.479  -8.262 -26.971  1.00113.51           O  
ANISOU  857  O   GLY A 143    13670  19575   9885  -1226   1986   1412       O  
ATOM    858  N   GLN A 144      15.975  -8.810 -24.829  1.00107.68           N  
ANISOU  858  N   GLN A 144    12514  18746   9655   -865   1877   1294       N  
ATOM    859  CA  GLN A 144      17.217  -8.019 -24.721  1.00110.85           C  
ANISOU  859  CA  GLN A 144    12499  19677   9941  -1207   2021   1460       C  
ATOM    860  C   GLN A 144      17.747  -8.149 -23.272  1.00112.90           C  
ANISOU  860  C   GLN A 144    12429  19964  10504  -1066   1936   1432       C  
ATOM    861  O   GLN A 144      17.299  -9.039 -22.533  1.00109.29           O  
ANISOU  861  O   GLN A 144    12044  19201  10280   -641   1835   1256       O  
ATOM    862  CB  GLN A 144      17.036  -6.544 -25.110  1.00112.99           C  
ANISOU  862  CB  GLN A 144    12967  19863  10101  -1836   1904   1764       C  
ATOM    863  N   SER A 145      18.682  -7.280 -22.864  1.00111.69           N  
ANISOU  863  N   SER A 145    11939  20168  10330  -1449   1960   1614       N  
ATOM    864  CA  SER A 145      19.253  -7.314 -21.497  1.00110.49           C  
ANISOU  864  CA  SER A 145    11464  20081  10437  -1368   1861   1607       C  
ATOM    865  C   SER A 145      18.129  -6.806 -20.573  1.00108.62           C  
ANISOU  865  C   SER A 145    11624  19139  10507  -1456   1529   1674       C  
ATOM    866  O   SER A 145      18.160  -5.667 -20.081  1.00107.98           O  
ANISOU  866  O   SER A 145    11606  18930  10492  -1893   1361   1873       O  
ATOM    867  CB  SER A 145      20.489  -6.408 -21.406  1.00118.04           C  
ANISOU  867  CB  SER A 145    11988  21611  11250  -1852   1949   1809       C  
ATOM    868  N   SER A 146      17.168  -7.695 -20.312  1.00100.77           N  
ANISOU  868  N   SER A 146    10893  17712   9683  -1030   1436   1495       N  
ATOM    869  CA  SER A 146      15.933  -7.378 -19.590  1.00 95.68           C  
ANISOU  869  CA  SER A 146    10624  16440   9291  -1044   1157   1522       C  
ATOM    870  C   SER A 146      15.994  -8.121 -18.264  1.00 96.18           C  
ANISOU  870  C   SER A 146    10548  16381   9617   -704   1070   1392       C  
ATOM    871  O   SER A 146      14.946  -8.462 -17.698  1.00 92.62           O  
ANISOU  871  O   SER A 146    10367  15472   9355   -525    906   1321       O  
ATOM    872  CB  SER A 146      14.655  -7.795 -20.328  1.00 96.94           C  
ANISOU  872  CB  SER A 146    11201  16213   9420   -888   1098   1441       C  
ATOM    873  OG  SER A 146      13.505  -7.629 -19.516  1.00102.07           O  
ANISOU  873  OG  SER A 146    12118  16348  10318   -839    849   1441       O  
ATOM    874  N   CYS A 147      17.210  -8.387 -17.777  1.00 93.62           N  
ANISOU  874  N   CYS A 147     9792  16492   9285   -619   1176   1367       N  
ATOM    875  CA  CYS A 147      17.387  -9.050 -16.486  1.00 91.22           C  
ANISOU  875  CA  CYS A 147     9352  16100   9208   -309   1074   1266       C  
ATOM    876  C   CYS A 147      17.612  -8.004 -15.388  1.00 92.11           C  
ANISOU  876  C   CYS A 147     9384  16143   9470   -655    889   1425       C  
ATOM    877  O   CYS A 147      17.086  -8.145 -14.276  1.00 88.86           O  
ANISOU  877  O   CYS A 147     9105  15381   9275   -533    709   1389       O  
ATOM    878  CB  CYS A 147      18.521 -10.088 -16.534  1.00 94.79           C  
ANISOU  878  CB  CYS A 147     9404  17042   9570     89   1259   1118       C  
ATOM    879  SG  CYS A 147      18.174 -11.575 -15.509  1.00 96.63           S  
ANISOU  879  SG  CYS A 147     9761  16944  10011    702   1143    901       S  
ATOM    880  N   ARG A 148      18.355  -6.939 -15.708  1.00 89.50           N  
ANISOU  880  N   ARG A 148     8875  16130   9002  -1117    924   1605       N  
ATOM    881  CA  ARG A 148      18.561  -5.840 -14.749  1.00 88.22           C  
ANISOU  881  CA  ARG A 148     8712  15862   8944  -1511    721   1763       C  
ATOM    882  C   ARG A 148      17.268  -5.093 -14.362  1.00 86.11           C  
ANISOU  882  C   ARG A 148     8956  14948   8816  -1646    485   1816       C  
ATOM    883  O   ARG A 148      17.294  -4.231 -13.483  1.00 85.61           O  
ANISOU  883  O   ARG A 148     8980  14705   8844  -1905    293   1911       O  
ATOM    884  CB  ARG A 148      19.643  -4.859 -15.237  1.00 93.12           C  
ANISOU  884  CB  ARG A 148     9068  16961   9351  -2044    795   1960       C  
ATOM    885  CG  ARG A 148      21.054  -5.259 -14.803  1.00107.07           C  
ANISOU  885  CG  ARG A 148    10230  19375  11077  -1991    904   1942       C  
ATOM    886  CD  ARG A 148      21.965  -4.059 -14.511  1.00122.11           C  
ANISOU  886  CD  ARG A 148    11922  21589  12884  -2626    817   2168       C  
ATOM    887  NE  ARG A 148      22.893  -3.784 -15.611  1.00136.60           N  
ANISOU  887  NE  ARG A 148    13416  24070  14415  -2953   1052   2282       N  
ATOM    888  CZ  ARG A 148      24.066  -3.156 -15.488  1.00155.30           C  
ANISOU  888  CZ  ARG A 148    15360  27009  16639  -3427   1073   2445       C  
ATOM    889  NH1 ARG A 148      24.494  -2.710 -14.309  1.00142.71           N  
ANISOU  889  NH1 ARG A 148    13642  25401  15179  -3641    849   2514       N  
ATOM    890  NH2 ARG A 148      24.831  -2.973 -16.561  1.00145.99           N  
ANISOU  890  NH2 ARG A 148    13864  26452  15153  -3718   1320   2545       N  
ATOM    891  N   ARG A 149      16.154  -5.424 -15.011  1.00 78.41           N  
ANISOU  891  N   ARG A 149     8308  13645   7839  -1458    491   1745       N  
ATOM    892  CA  ARG A 149      14.834  -5.002 -14.553  1.00 73.90           C  
ANISOU  892  CA  ARG A 149     8150  12511   7418  -1433    280   1743       C  
ATOM    893  C   ARG A 149      14.275  -6.059 -13.620  1.00 71.81           C  
ANISOU  893  C   ARG A 149     7887  12045   7352  -1011    236   1571       C  
ATOM    894  O   ARG A 149      13.984  -5.774 -12.462  1.00 69.76           O  
ANISOU  894  O   ARG A 149     7697  11558   7250  -1006     77   1567       O  
ATOM    895  CB  ARG A 149      13.891  -4.787 -15.739  1.00 74.45           C  
ANISOU  895  CB  ARG A 149     8544  12372   7370  -1472    284   1770       C  
ATOM    896  CG  ARG A 149      12.629  -3.973 -15.430  1.00 84.09           C  
ANISOU  896  CG  ARG A 149    10170  13086   8696  -1526     47   1814       C  
ATOM    897  CD  ARG A 149      12.320  -3.025 -16.596  1.00 98.64           C  
ANISOU  897  CD  ARG A 149    12294  14837  10346  -1818     -1   1966       C  
ATOM    898  NE  ARG A 149      11.130  -2.199 -16.390  1.00108.40           N  
ANISOU  898  NE  ARG A 149    13922  15605  11660  -1816   -245   2005       N  
ATOM    899  CZ  ARG A 149      11.058  -1.137 -15.585  1.00124.85           C  
ANISOU  899  CZ  ARG A 149    16191  17433  13814  -1981   -448   2083       C  
ATOM    900  NH1 ARG A 149      12.109  -0.743 -14.859  1.00113.00           N  
ANISOU  900  NH1 ARG A 149    14527  16085  12322  -2220   -453   2144       N  
ATOM    901  NH2 ARG A 149       9.910  -0.469 -15.492  1.00112.28           N  
ANISOU  901  NH2 ARG A 149    14955  15434  12273  -1886   -660   2088       N  
ATOM    902  N   VAL A 150      14.148  -7.281 -14.129  1.00 66.09           N  
ANISOU  902  N   VAL A 150     7116  11402   6593   -674    374   1430       N  
ATOM    903  CA  VAL A 150      13.670  -8.428 -13.344  1.00 63.02           C  
ANISOU  903  CA  VAL A 150     6766  10826   6354   -295    335   1277       C  
ATOM    904  C   VAL A 150      14.378  -8.511 -11.984  1.00 65.62           C  
ANISOU  904  C   VAL A 150     6877  11241   6814   -238    258   1274       C  
ATOM    905  O   VAL A 150      13.732  -8.685 -10.943  1.00 62.91           O  
ANISOU  905  O   VAL A 150     6671  10610   6621   -138    121   1236       O  
ATOM    906  CB  VAL A 150      13.876  -9.757 -14.120  1.00 67.77           C  
ANISOU  906  CB  VAL A 150     7320  11582   6847     44    501   1128       C  
ATOM    907  CG1 VAL A 150      13.664 -10.967 -13.220  1.00 66.24           C  
ANISOU  907  CG1 VAL A 150     7169  11219   6781    407    444    990       C  
ATOM    908  CG2 VAL A 150      12.946  -9.818 -15.312  1.00 67.11           C  
ANISOU  908  CG2 VAL A 150     7519  11334   6647     13    533   1109       C  
ATOM    909  N   ALA A 151      15.705  -8.383 -12.008  1.00 63.79           N  
ANISOU  909  N   ALA A 151     6290  11442   6504   -316    345   1318       N  
ATOM    910  CA  ALA A 151      16.500  -8.293 -10.790  1.00 63.62           C  
ANISOU  910  CA  ALA A 151     6028  11564   6579   -326    249   1343       C  
ATOM    911  C   ALA A 151      15.849  -7.298  -9.847  1.00 63.93           C  
ANISOU  911  C   ALA A 151     6306  11246   6738   -579     39   1423       C  
ATOM    912  O   ALA A 151      15.498  -7.634  -8.713  1.00 61.91           O  
ANISOU  912  O   ALA A 151     6128  10778   6616   -421    -82   1367       O  
ATOM    913  CB  ALA A 151      17.919  -7.845 -11.116  1.00 68.29           C  
ANISOU  913  CB  ALA A 151     6199  12710   7037   -544    348   1434       C  
ATOM    914  N   LEU A 152      15.654  -6.083 -10.354  1.00 59.88           N  
ANISOU  914  N   LEU A 152     5947  10652   6152   -957     -6   1550       N  
ATOM    915  CA  LEU A 152      15.170  -4.969  -9.547  1.00 58.25           C  
ANISOU  915  CA  LEU A 152     5993  10121   6019  -1204   -214   1623       C  
ATOM    916  C   LEU A 152      13.746  -5.171  -9.034  1.00 57.82           C  
ANISOU  916  C   LEU A 152     6265   9615   6091   -975   -312   1529       C  
ATOM    917  O   LEU A 152      13.407  -4.684  -7.960  1.00 56.56           O  
ANISOU  917  O   LEU A 152     6245   9229   6017  -1011   -467   1522       O  
ATOM    918  CB  LEU A 152      15.272  -3.651 -10.328  1.00 60.15           C  
ANISOU  918  CB  LEU A 152     6396  10336   6122  -1643   -258   1784       C  
ATOM    919  CG  LEU A 152      15.417  -2.388  -9.469  1.00 65.73           C  
ANISOU  919  CG  LEU A 152     7285  10844   6846  -1988   -481   1884       C  
ATOM    920  CD1 LEU A 152      16.692  -2.450  -8.611  1.00 68.09           C  
ANISOU  920  CD1 LEU A 152     7225  11493   7151  -2128   -511   1916       C  
ATOM    921  CD2 LEU A 152      15.408  -1.136 -10.345  1.00 69.74           C  
ANISOU  921  CD2 LEU A 152     8056  11247   7195  -2415   -550   2050       C  
ATOM    922  N   MET A 153      12.925  -5.892  -9.791  1.00 52.06           N  
ANISOU  922  N   MET A 153     5645   8784   5351   -753   -222   1453       N  
ATOM    923  CA  MET A 153      11.569  -6.222  -9.352  1.00 48.83           C  
ANISOU  923  CA  MET A 153     5476   8034   5043   -548   -297   1365       C  
ATOM    924  C   MET A 153      11.578  -7.278  -8.260  1.00 50.30           C  
ANISOU  924  C   MET A 153     5571   8208   5331   -292   -305   1265       C  
ATOM    925  O   MET A 153      10.883  -7.143  -7.254  1.00 48.36           O  
ANISOU  925  O   MET A 153     5455   7748   5170   -245   -412   1232       O  
ATOM    926  CB  MET A 153      10.741  -6.760 -10.509  1.00 50.61           C  
ANISOU  926  CB  MET A 153     5828   8193   5207   -428   -215   1321       C  
ATOM    927  CG  MET A 153      10.514  -5.790 -11.634  1.00 55.54           C  
ANISOU  927  CG  MET A 153     6607   8782   5715   -651   -230   1423       C  
ATOM    928  SD  MET A 153       9.699  -6.612 -13.008  1.00 59.64           S  
ANISOU  928  SD  MET A 153     7242   9284   6135   -500   -133   1360       S  
ATOM    929  CE  MET A 153       8.047  -6.875 -12.333  1.00 53.89           C  
ANISOU  929  CE  MET A 153     6704   8228   5542   -314   -273   1276       C  
ATOM    930  N   ILE A 154      12.344  -8.345  -8.470  1.00 46.99           N  
ANISOU  930  N   ILE A 154     4950   8018   4883   -106   -193   1213       N  
ATOM    931  CA  ILE A 154      12.419  -9.417  -7.482  1.00 45.82           C  
ANISOU  931  CA  ILE A 154     4764   7836   4811    150   -224   1131       C  
ATOM    932  C   ILE A 154      12.990  -8.816  -6.198  1.00 49.33           C  
ANISOU  932  C   ILE A 154     5111   8314   5317     35   -350   1180       C  
ATOM    933  O   ILE A 154      12.391  -8.950  -5.124  1.00 47.49           O  
ANISOU  933  O   ILE A 154     5015   7876   5154     94   -450   1149       O  
ATOM    934  CB  ILE A 154      13.295 -10.606  -7.951  1.00 50.63           C  
ANISOU  934  CB  ILE A 154     5192   8686   5359    418   -106   1060       C  
ATOM    935  CG1 ILE A 154      12.775 -11.201  -9.262  1.00 51.08           C  
ANISOU  935  CG1 ILE A 154     5385   8702   5322    525     13    995       C  
ATOM    936  CG2 ILE A 154      13.315 -11.713  -6.898  1.00 51.00           C  
ANISOU  936  CG2 ILE A 154     5280   8627   5471    691   -181    989       C  
ATOM    937  CD1 ILE A 154      13.847 -11.936 -10.050  1.00 61.57           C  
ANISOU  937  CD1 ILE A 154     6508  10355   6532    740    162    930       C  
ATOM    938  N   THR A 155      14.131  -8.137  -6.324  1.00 47.06           N  
ANISOU  938  N   THR A 155     4592   8306   4980   -162   -347   1261       N  
ATOM    939  CA  THR A 155      14.748  -7.442  -5.200  1.00 47.17           C  
ANISOU  939  CA  THR A 155     4523   8372   5028   -340   -491   1319       C  
ATOM    940  C   THR A 155      13.740  -6.640  -4.416  1.00 48.34           C  
ANISOU  940  C   THR A 155     4982   8157   5227   -455   -630   1316       C  
ATOM    941  O   THR A 155      13.603  -6.834  -3.208  1.00 47.15           O  
ANISOU  941  O   THR A 155     4886   7902   5128   -373   -731   1279       O  
ATOM    942  CB  THR A 155      15.798  -6.452  -5.663  1.00 56.45           C  
ANISOU  942  CB  THR A 155     5495   9838   6115   -687   -491   1437       C  
ATOM    943  OG1 THR A 155      16.992  -7.161  -5.978  1.00 58.42           O  
ANISOU  943  OG1 THR A 155     5349  10537   6312   -565   -384   1433       O  
ATOM    944  CG2 THR A 155      16.087  -5.421  -4.572  1.00 54.57           C  
ANISOU  944  CG2 THR A 155     5322   9518   5894   -972   -687   1504       C  
ATOM    945  N   ALA A 156      13.045  -5.735  -5.111  1.00 43.92           N  
ANISOU  945  N   ALA A 156     4635   7418   4634   -622   -638   1353       N  
ATOM    946  CA  ALA A 156      12.056  -4.856  -4.486  1.00 42.34           C  
ANISOU  946  CA  ALA A 156     4741   6884   4461   -682   -770   1334       C  
ATOM    947  C   ALA A 156      11.146  -5.688  -3.642  1.00 43.81           C  
ANISOU  947  C   ALA A 156     5008   6923   4716   -412   -769   1229       C  
ATOM    948  O   ALA A 156      11.056  -5.485  -2.435  1.00 42.95           O  
ANISOU  948  O   ALA A 156     4971   6722   4627   -404   -870   1196       O  
ATOM    949  CB  ALA A 156      11.245  -4.119  -5.530  1.00 42.93           C  
ANISOU  949  CB  ALA A 156     5039   6784   4491   -763   -768   1366       C  
ATOM    950  N   VAL A 157      10.512  -6.657  -4.292  1.00 39.55           N  
ANISOU  950  N   VAL A 157     4463   6376   4188   -220   -657   1180       N  
ATOM    951  CA  VAL A 157       9.491  -7.475  -3.660  1.00 37.97           C  
ANISOU  951  CA  VAL A 157     4362   6041   4026    -24   -650   1098       C  
ATOM    952  C   VAL A 157       9.992  -8.129  -2.385  1.00 43.28           C  
ANISOU  952  C   VAL A 157     4968   6757   4719     61   -699   1077       C  
ATOM    953  O   VAL A 157       9.275  -8.146  -1.387  1.00 42.40           O  
ANISOU  953  O   VAL A 157     4977   6521   4611    102   -750   1036       O  
ATOM    954  CB  VAL A 157       8.957  -8.562  -4.605  1.00 40.89           C  
ANISOU  954  CB  VAL A 157     4737   6418   4382    119   -541   1061       C  
ATOM    955  CG1 VAL A 157       8.113  -9.568  -3.829  1.00 39.57           C  
ANISOU  955  CG1 VAL A 157     4658   6146   4231    256   -546   1001       C  
ATOM    956  CG2 VAL A 157       8.146  -7.932  -5.731  1.00 40.33           C  
ANISOU  956  CG2 VAL A 157     4774   6271   4279     50   -522   1076       C  
ATOM    957  N   TRP A 158      11.214  -8.659  -2.407  1.00 42.14           N  
ANISOU  957  N   TRP A 158     4624   6815   4570    101   -685   1105       N  
ATOM    958  CA  TRP A 158      11.766  -9.301  -1.214  1.00 43.07           C  
ANISOU  958  CA  TRP A 158     4685   6981   4700    205   -763   1097       C  
ATOM    959  C   TRP A 158      12.133  -8.295  -0.132  1.00 45.41           C  
ANISOU  959  C   TRP A 158     4997   7268   4987     29   -901   1126       C  
ATOM    960  O   TRP A 158      11.871  -8.536   1.041  1.00 44.87           O  
ANISOU  960  O   TRP A 158     5030   7110   4908     81   -979   1100       O  
ATOM    961  CB  TRP A 158      12.977 -10.159  -1.555  1.00 44.52           C  
ANISOU  961  CB  TRP A 158     4632   7411   4873    361   -729   1107       C  
ATOM    962  CG  TRP A 158      12.621 -11.454  -2.203  1.00 46.03           C  
ANISOU  962  CG  TRP A 158     4896   7542   5049    610   -637   1048       C  
ATOM    963  CD1 TRP A 158      12.805 -11.795  -3.510  1.00 49.68           C  
ANISOU  963  CD1 TRP A 158     5293   8108   5474    691   -512   1021       C  
ATOM    964  CD2 TRP A 158      12.023 -12.587  -1.573  1.00 45.63           C  
ANISOU  964  CD2 TRP A 158     5046   7298   4992    785   -677   1008       C  
ATOM    965  NE1 TRP A 158      12.362 -13.075  -3.734  1.00 49.16           N  
ANISOU  965  NE1 TRP A 158     5394   7900   5385    923   -483    953       N  
ATOM    966  CE2 TRP A 158      11.874 -13.584  -2.560  1.00 49.98           C  
ANISOU  966  CE2 TRP A 158     5671   7811   5508    966   -590    954       C  
ATOM    967  CE3 TRP A 158      11.593 -12.856  -0.268  1.00 46.82           C  
ANISOU  967  CE3 TRP A 158     5350   7301   5140    782   -781   1018       C  
ATOM    968  CZ2 TRP A 158      11.315 -14.831  -2.285  1.00 49.44           C  
ANISOU  968  CZ2 TRP A 158     5851   7528   5405   1120   -626    918       C  
ATOM    969  CZ3 TRP A 158      11.038 -14.099   0.009  1.00 48.55           C  
ANISOU  969  CZ3 TRP A 158     5788   7339   5320    922   -801    997       C  
ATOM    970  CH2 TRP A 158      10.904 -15.070  -0.998  1.00 49.72           C  
ANISOU  970  CH2 TRP A 158     6032   7421   5438   1078   -734    950       C  
ATOM    971  N   VAL A 159      12.718  -7.164  -0.518  1.00 41.21           N  
ANISOU  971  N   VAL A 159     4403   6818   4437   -206   -941   1182       N  
ATOM    972  CA  VAL A 159      13.119  -6.157   0.464  1.00 41.20           C  
ANISOU  972  CA  VAL A 159     4466   6781   4406   -413  -1100   1207       C  
ATOM    973  C   VAL A 159      11.885  -5.561   1.125  1.00 43.07           C  
ANISOU  973  C   VAL A 159     5018   6720   4628   -398  -1149   1135       C  
ATOM    974  O   VAL A 159      11.875  -5.335   2.333  1.00 42.49           O  
ANISOU  974  O   VAL A 159     5051   6577   4518   -415  -1258   1102       O  
ATOM    975  CB  VAL A 159      13.953  -5.036  -0.150  1.00 46.57           C  
ANISOU  975  CB  VAL A 159     5069   7581   5044   -731  -1150   1297       C  
ATOM    976  CG1 VAL A 159      14.582  -4.207   0.943  1.00 48.13           C  
ANISOU  976  CG1 VAL A 159     5319   7773   5197   -962  -1344   1325       C  
ATOM    977  CG2 VAL A 159      15.029  -5.602  -1.033  1.00 47.79           C  
ANISOU  977  CG2 VAL A 159     4871   8098   5190   -730  -1048   1358       C  
ATOM    978  N   LEU A 160      10.842  -5.323   0.332  1.00 38.56           N  
ANISOU  978  N   LEU A 160     4584   6001   4066   -344  -1070   1105       N  
ATOM    979  CA  LEU A 160       9.523  -4.954   0.874  1.00 37.15           C  
ANISOU  979  CA  LEU A 160     4643   5606   3866   -240  -1085   1016       C  
ATOM    980  C   LEU A 160       8.989  -6.048   1.764  1.00 39.37           C  
ANISOU  980  C   LEU A 160     4908   5909   4142    -63  -1036    962       C  
ATOM    981  O   LEU A 160       8.355  -5.760   2.775  1.00 39.35           O  
ANISOU  981  O   LEU A 160     5049   5819   4084    -19  -1075    895       O  
ATOM    982  CB  LEU A 160       8.507  -4.710  -0.240  1.00 36.36           C  
ANISOU  982  CB  LEU A 160     4625   5409   3779   -174  -1011   1001       C  
ATOM    983  CG  LEU A 160       7.109  -4.230   0.175  1.00 40.53           C  
ANISOU  983  CG  LEU A 160     5344   5779   4277    -31  -1025    904       C  
ATOM    984  CD1 LEU A 160       7.147  -2.829   0.763  1.00 42.30           C  
ANISOU  984  CD1 LEU A 160     5811   5821   4441    -99  -1175    867       C  
ATOM    985  CD2 LEU A 160       6.141  -4.279  -1.014  1.00 41.51           C  
ANISOU  985  CD2 LEU A 160     5475   5878   4419     60   -957    901       C  
ATOM    986  N   ALA A 161       9.233  -7.298   1.365  1.00 34.75           N  
ANISOU  986  N   ALA A 161     4178   5436   3591     35   -952    990       N  
ATOM    987  CA  ALA A 161       8.846  -8.464   2.153  1.00 33.78           C  
ANISOU  987  CA  ALA A 161     4081   5310   3443    163   -928    968       C  
ATOM    988  C   ALA A 161       9.496  -8.418   3.513  1.00 38.70           C  
ANISOU  988  C   ALA A 161     4726   5960   4018    134  -1045    976       C  
ATOM    989  O   ALA A 161       8.845  -8.589   4.534  1.00 38.20           O  
ANISOU  989  O   ALA A 161     4792   5839   3883    161  -1058    939       O  
ATOM    990  CB  ALA A 161       9.225  -9.760   1.435  1.00 34.32           C  
ANISOU  990  CB  ALA A 161     4052   5448   3542    280   -861    998       C  
ATOM    991  N   PHE A 162      10.791  -8.175   3.529  1.00 36.73           N  
ANISOU  991  N   PHE A 162     4336   5833   3788     61  -1132   1029       N  
ATOM    992  CA  PHE A 162      11.516  -8.258   4.768  1.00 37.90           C  
ANISOU  992  CA  PHE A 162     4478   6037   3884     37  -1268   1047       C  
ATOM    993  C   PHE A 162      11.103  -7.115   5.685  1.00 42.60           C  
ANISOU  993  C   PHE A 162     5273   6510   4403    -94  -1356    993       C  
ATOM    994  O   PHE A 162      10.665  -7.350   6.812  1.00 42.68           O  
ANISOU  994  O   PHE A 162     5425   6466   4327    -49  -1390    955       O  
ATOM    995  CB  PHE A 162      13.024  -8.256   4.518  1.00 41.47           C  
ANISOU  995  CB  PHE A 162     4673   6717   4368    -16  -1351   1119       C  
ATOM    996  CG  PHE A 162      13.822  -8.227   5.769  1.00 44.69           C  
ANISOU  996  CG  PHE A 162     5055   7209   4717    -63  -1528   1145       C  
ATOM    997  CD1 PHE A 162      13.954  -9.375   6.538  1.00 48.29           C  
ANISOU  997  CD1 PHE A 162     5529   7678   5139    128  -1580   1159       C  
ATOM    998  CD2 PHE A 162      14.394  -7.048   6.214  1.00 48.27           C  
ANISOU  998  CD2 PHE A 162     5516   7698   5128   -315  -1667   1160       C  
ATOM    999  CE1 PHE A 162      14.672  -9.362   7.721  1.00 50.82           C  
ANISOU  999  CE1 PHE A 162     5842   8078   5389     92  -1766   1190       C  
ATOM   1000  CE2 PHE A 162      15.117  -7.022   7.394  1.00 52.88           C  
ANISOU 1000  CE2 PHE A 162     6085   8366   5640   -377  -1853   1184       C  
ATOM   1001  CZ  PHE A 162      15.258  -8.185   8.151  1.00 51.33           C  
ANISOU 1001  CZ  PHE A 162     5876   8211   5414   -162  -1901   1199       C  
ATOM   1002  N   ALA A 163      11.225  -5.884   5.198  1.00 39.59           N  
ANISOU 1002  N   ALA A 163     4939   6073   4030   -253  -1397    987       N  
ATOM   1003  CA  ALA A 163      10.949  -4.720   6.020  1.00 40.39           C  
ANISOU 1003  CA  ALA A 163     5285   6020   4041   -360  -1510    921       C  
ATOM   1004  C   ALA A 163       9.602  -4.848   6.748  1.00 44.27           C  
ANISOU 1004  C   ALA A 163     5970   6394   4454   -189  -1435    811       C  
ATOM   1005  O   ALA A 163       9.488  -4.511   7.924  1.00 44.50           O  
ANISOU 1005  O   ALA A 163     6168   6373   4369   -197  -1515    747       O  
ATOM   1006  CB  ALA A 163      10.988  -3.475   5.179  1.00 41.72           C  
ANISOU 1006  CB  ALA A 163     5559   6073   4222   -520  -1554    929       C  
ATOM   1007  N   VAL A 164       8.594  -5.363   6.056  1.00 40.08           N  
ANISOU 1007  N   VAL A 164     5401   5860   3968    -46  -1279    790       N  
ATOM   1008  CA  VAL A 164       7.269  -5.557   6.656  1.00 40.02           C  
ANISOU 1008  CA  VAL A 164     5501   5830   3875     96  -1183    697       C  
ATOM   1009  C   VAL A 164       7.273  -6.528   7.843  1.00 45.96           C  
ANISOU 1009  C   VAL A 164     6264   6667   4531    117  -1177    710       C  
ATOM   1010  O   VAL A 164       6.506  -6.351   8.797  1.00 46.25           O  
ANISOU 1010  O   VAL A 164     6429   6712   4432    167  -1145    627       O  
ATOM   1011  CB  VAL A 164       6.254  -6.070   5.612  1.00 42.42           C  
ANISOU 1011  CB  VAL A 164     5710   6166   4242    198  -1033    697       C  
ATOM   1012  CG1 VAL A 164       4.998  -6.595   6.290  1.00 42.21           C  
ANISOU 1012  CG1 VAL A 164     5706   6220   4113    296   -922    634       C  
ATOM   1013  CG2 VAL A 164       5.909  -4.965   4.614  1.00 42.33           C  
ANISOU 1013  CG2 VAL A 164     5757   6049   4277    216  -1048    666       C  
ATOM   1014  N   SER A 165       8.142  -7.541   7.775  1.00 43.35           N  
ANISOU 1014  N   SER A 165     5811   6407   4251     94  -1211    812       N  
ATOM   1015  CA  SER A 165       8.218  -8.619   8.776  1.00 43.65           C  
ANISOU 1015  CA  SER A 165     5894   6494   4196    118  -1233    855       C  
ATOM   1016  C   SER A 165       9.190  -8.364   9.906  1.00 49.29           C  
ANISOU 1016  C   SER A 165     6670   7230   4827     50  -1407    874       C  
ATOM   1017  O   SER A 165       9.045  -8.925  10.990  1.00 49.57           O  
ANISOU 1017  O   SER A 165     6823   7282   4729     54  -1440    888       O  
ATOM   1018  CB  SER A 165       8.643  -9.912   8.099  1.00 46.34           C  
ANISOU 1018  CB  SER A 165     6124   6864   4621    186  -1211    948       C  
ATOM   1019  OG  SER A 165       7.735 -10.230   7.066  1.00 56.17           O  
ANISOU 1019  OG  SER A 165     7336   8085   5923    222  -1068    933       O  
ATOM   1020  N   CYS A 166      10.176  -7.511   9.664  1.00 47.08           N  
ANISOU 1020  N   CYS A 166     6320   6962   4605    -46  -1530    884       N  
ATOM   1021  CA  CYS A 166      11.286  -7.380  10.601  1.00 48.90           C  
ANISOU 1021  CA  CYS A 166     6552   7258   4771   -138  -1728    924       C  
ATOM   1022  C   CYS A 166      10.915  -6.805  11.978  1.00 54.31           C  
ANISOU 1022  C   CYS A 166     7495   7875   5266   -195  -1805    842       C  
ATOM   1023  O   CYS A 166      11.631  -7.071  12.942  1.00 55.96           O  
ANISOU 1023  O   CYS A 166     7737   8145   5382   -242  -1962    885       O  
ATOM   1024  CB  CYS A 166      12.470  -6.613   9.981  1.00 50.29           C  
ANISOU 1024  CB  CYS A 166     6557   7515   5034   -292  -1848    971       C  
ATOM   1025  SG  CYS A 166      12.477  -4.828  10.243  1.00 55.62           S  
ANISOU 1025  SG  CYS A 166     7459   8043   5633   -524  -1970    888       S  
ATOM   1026  N   PRO A 167       9.812  -6.032  12.090  1.00 50.17           N  
ANISOU 1026  N   PRO A 167     7154   7242   4665   -163  -1704    717       N  
ATOM   1027  CA  PRO A 167       9.477  -5.525  13.431  1.00 51.52           C  
ANISOU 1027  CA  PRO A 167     7581   7372   4621   -181  -1764    617       C  
ATOM   1028  C   PRO A 167       9.295  -6.624  14.485  1.00 55.51           C  
ANISOU 1028  C   PRO A 167     8139   7974   4980   -147  -1747    665       C  
ATOM   1029  O   PRO A 167       9.696  -6.447  15.639  1.00 57.00           O  
ANISOU 1029  O   PRO A 167     8487   8171   4999   -216  -1885    648       O  
ATOM   1030  CB  PRO A 167       8.160  -4.778  13.205  1.00 52.98           C  
ANISOU 1030  CB  PRO A 167     7898   7477   4756    -57  -1609    468       C  
ATOM   1031  CG  PRO A 167       8.220  -4.346  11.797  1.00 56.04           C  
ANISOU 1031  CG  PRO A 167     8162   7794   5334    -57  -1580    494       C  
ATOM   1032  CD  PRO A 167       8.955  -5.429  11.055  1.00 50.36           C  
ANISOU 1032  CD  PRO A 167     7176   7185   4773    -98  -1569    650       C  
ATOM   1033  N   LEU A 168       8.718  -7.754  14.075  1.00 50.41           N  
ANISOU 1033  N   LEU A 168     7389   7385   4381    -67  -1600    736       N  
ATOM   1034  CA  LEU A 168       8.504  -8.895  14.974  1.00 50.71           C  
ANISOU 1034  CA  LEU A 168     7519   7483   4267    -70  -1591    813       C  
ATOM   1035  C   LEU A 168       9.831  -9.356  15.557  1.00 56.41           C  
ANISOU 1035  C   LEU A 168     8241   8219   4975   -108  -1828    923       C  
ATOM   1036  O   LEU A 168       9.906  -9.785  16.710  1.00 57.74           O  
ANISOU 1036  O   LEU A 168     8579   8411   4950   -146  -1914    962       O  
ATOM   1037  CB  LEU A 168       7.856 -10.056  14.226  1.00 49.20           C  
ANISOU 1037  CB  LEU A 168     7238   7304   4151    -23  -1442    894       C  
ATOM   1038  CG  LEU A 168       6.567  -9.741  13.472  1.00 52.43           C  
ANISOU 1038  CG  LEU A 168     7578   7746   4596     14  -1224    808       C  
ATOM   1039  CD1 LEU A 168       6.199 -10.904  12.553  1.00 51.58           C  
ANISOU 1039  CD1 LEU A 168     7379   7630   4590     20  -1134    903       C  
ATOM   1040  CD2 LEU A 168       5.437  -9.395  14.442  1.00 55.15           C  
ANISOU 1040  CD2 LEU A 168     8045   8205   4705     -2  -1097    707       C  
ATOM   1041  N   LEU A 169      10.870  -9.251  14.735  1.00 52.95           N  
ANISOU 1041  N   LEU A 169     7594   7797   4728    -94  -1933    976       N  
ATOM   1042  CA  LEU A 169      12.229  -9.637  15.090  1.00 54.43           C  
ANISOU 1042  CA  LEU A 169     7683   8065   4932    -94  -2166   1078       C  
ATOM   1043  C   LEU A 169      12.837  -8.733  16.166  1.00 60.92           C  
ANISOU 1043  C   LEU A 169     8621   8916   5609   -243  -2369   1038       C  
ATOM   1044  O   LEU A 169      13.635  -9.188  16.990  1.00 62.29           O  
ANISOU 1044  O   LEU A 169     8813   9163   5691   -248  -2574   1118       O  
ATOM   1045  CB  LEU A 169      13.105  -9.607  13.829  1.00 53.93           C  
ANISOU 1045  CB  LEU A 169     7310   8087   5094    -50  -2184   1123       C  
ATOM   1046  CG  LEU A 169      14.076 -10.765  13.627  1.00 59.77           C  
ANISOU 1046  CG  LEU A 169     7873   8933   5903    119  -2298   1239       C  
ATOM   1047  CD1 LEU A 169      13.349 -12.099  13.733  1.00 59.65           C  
ANISOU 1047  CD1 LEU A 169     8038   8792   5835    273  -2214   1288       C  
ATOM   1048  CD2 LEU A 169      14.753 -10.630  12.279  1.00 61.46           C  
ANISOU 1048  CD2 LEU A 169     7766   9275   6311    169  -2248   1252       C  
ATOM   1049  N   PHE A 170      12.457  -7.457  16.153  1.00 58.02           N  
ANISOU 1049  N   PHE A 170     8363   8475   5208   -355  -2335    912       N  
ATOM   1050  CA  PHE A 170      12.981  -6.476  17.110  1.00 60.40           C  
ANISOU 1050  CA  PHE A 170     8838   8757   5352   -522  -2539    850       C  
ATOM   1051  C   PHE A 170      11.946  -6.074  18.163  1.00 65.35           C  
ANISOU 1051  C   PHE A 170     9807   9293   5728   -507  -2460    713       C  
ATOM   1052  O   PHE A 170      11.825  -4.906  18.521  1.00 65.94           O  
ANISOU 1052  O   PHE A 170    10095   9265   5695   -591  -2520    579       O  
ATOM   1053  CB  PHE A 170      13.558  -5.266  16.357  1.00 62.77           C  
ANISOU 1053  CB  PHE A 170     9062   9019   5768   -688  -2625    814       C  
ATOM   1054  CG  PHE A 170      14.535  -5.659  15.275  1.00 64.29           C  
ANISOU 1054  CG  PHE A 170     8876   9372   6179   -707  -2659    944       C  
ATOM   1055  CD1 PHE A 170      15.813  -6.122  15.605  1.00 69.72           C  
ANISOU 1055  CD1 PHE A 170     9343  10272   6876   -759  -2875   1061       C  
ATOM   1056  CD2 PHE A 170      14.162  -5.630  13.933  1.00 64.55           C  
ANISOU 1056  CD2 PHE A 170     8757   9380   6390   -644  -2473    947       C  
ATOM   1057  CE1 PHE A 170      16.713  -6.524  14.612  1.00 70.79           C  
ANISOU 1057  CE1 PHE A 170     9088  10621   7190   -730  -2883   1165       C  
ATOM   1058  CE2 PHE A 170      15.056  -6.025  12.928  1.00 67.44           C  
ANISOU 1058  CE2 PHE A 170     8770   9930   6924   -644  -2478   1054       C  
ATOM   1059  CZ  PHE A 170      16.334  -6.472  13.270  1.00 67.75           C  
ANISOU 1059  CZ  PHE A 170     8567  10210   6966   -675  -2673   1157       C  
ATOM   1060  N   GLY A 171      11.193  -7.067  18.637  1.00 62.21           N  
ANISOU 1060  N   GLY A 171     9477   8941   5219   -403  -2324    746       N  
ATOM   1061  CA  GLY A 171      10.412  -6.947  19.869  1.00 63.78           C  
ANISOU 1061  CA  GLY A 171     9967   9148   5119   -407  -2266    652       C  
ATOM   1062  C   GLY A 171       8.899  -6.894  19.742  1.00 67.04           C  
ANISOU 1062  C   GLY A 171    10437   9586   5449   -297  -1965    539       C  
ATOM   1063  O   GLY A 171       8.198  -7.093  20.733  1.00 68.22           O  
ANISOU 1063  O   GLY A 171    10768   9821   5332   -296  -1872    490       O  
ATOM   1064  N   PHE A 172       8.381  -6.633  18.545  1.00 61.51           N  
ANISOU 1064  N   PHE A 172     9568   8850   4953   -209  -1813    500       N  
ATOM   1065  CA  PHE A 172       6.928  -6.420  18.376  1.00 60.89           C  
ANISOU 1065  CA  PHE A 172     9500   8839   4798    -84  -1546    374       C  
ATOM   1066  C   PHE A 172       6.096  -7.698  18.382  1.00 63.66           C  
ANISOU 1066  C   PHE A 172     9753   9342   5093    -92  -1357    477       C  
ATOM   1067  O   PHE A 172       4.866  -7.644  18.238  1.00 63.22           O  
ANISOU 1067  O   PHE A 172     9640   9416   4963    -17  -1130    394       O  
ATOM   1068  CB  PHE A 172       6.636  -5.585  17.121  1.00 61.22           C  
ANISOU 1068  CB  PHE A 172     9426   8782   5053     16  -1483    293       C  
ATOM   1069  CG  PHE A 172       7.017  -4.151  17.278  1.00 64.11           C  
ANISOU 1069  CG  PHE A 172     9999   8978   5380     19  -1632    149       C  
ATOM   1070  CD1 PHE A 172       6.086  -3.225  17.720  1.00 68.63           C  
ANISOU 1070  CD1 PHE A 172    10779   9526   5771    183  -1542    -62       C  
ATOM   1071  CD2 PHE A 172       8.326  -3.737  17.044  1.00 66.47           C  
ANISOU 1071  CD2 PHE A 172    10304   9155   5795   -147  -1875    222       C  
ATOM   1072  CE1 PHE A 172       6.443  -1.907  17.895  1.00 71.34           C  
ANISOU 1072  CE1 PHE A 172    11402   9651   6054    189  -1711   -202       C  
ATOM   1073  CE2 PHE A 172       8.695  -2.420  17.213  1.00 70.95           C  
ANISOU 1073  CE2 PHE A 172    11118   9538   6302   -211  -2042    105       C  
ATOM   1074  CZ  PHE A 172       7.757  -1.499  17.637  1.00 70.61           C  
ANISOU 1074  CZ  PHE A 172    11354   9396   6080    -41  -1972   -109       C  
ATOM   1075  N   ASN A 173       6.766  -8.838  18.542  1.00 59.75           N  
ANISOU 1075  N   ASN A 173     9244   8836   4622   -184  -1466    661       N  
ATOM   1076  CA  ASN A 173       6.080 -10.080  18.794  1.00 59.88           C  
ANISOU 1076  CA  ASN A 173     9282   8949   4519   -253  -1344    778       C  
ATOM   1077  C   ASN A 173       5.899 -10.205  20.297  1.00 67.73           C  
ANISOU 1077  C   ASN A 173    10522  10044   5167   -350  -1362    775       C  
ATOM   1078  O   ASN A 173       6.658 -10.899  20.976  1.00 68.92           O  
ANISOU 1078  O   ASN A 173    10817  10142   5226   -430  -1547    911       O  
ATOM   1079  CB  ASN A 173       6.861 -11.260  18.228  1.00 58.08           C  
ANISOU 1079  CB  ASN A 173     8996   8612   4461   -268  -1473    969       C  
ATOM   1080  CG  ASN A 173       6.085 -12.560  18.312  1.00 80.54           C  
ANISOU 1080  CG  ASN A 173    11920  11492   7191   -371  -1363   1098       C  
ATOM   1081  OD1 ASN A 173       4.874 -12.565  18.570  1.00 75.23           O  
ANISOU 1081  OD1 ASN A 173    11256  10977   6350   -459  -1151   1052       O  
ATOM   1082  ND2 ASN A 173       6.779 -13.673  18.097  1.00 74.32           N  
ANISOU 1082  ND2 ASN A 173    11196  10566   6476   -363  -1515   1261       N  
ATOM   1083  N   THR A 174       4.895  -9.504  20.812  1.00 65.57           N  
ANISOU 1083  N   THR A 174    10298   9929   4686   -317  -1175    611       N  
ATOM   1084  CA  THR A 174       4.571  -9.528  22.230  1.00 68.20           C  
ANISOU 1084  CA  THR A 174    10861  10409   4642   -401  -1141    577       C  
ATOM   1085  C   THR A 174       3.386 -10.467  22.468  1.00 73.74           C  
ANISOU 1085  C   THR A 174    11524  11350   5142   -534   -897    660       C  
ATOM   1086  O   THR A 174       2.399 -10.426  21.722  1.00 72.41           O  
ANISOU 1086  O   THR A 174    11135  11324   5053   -488   -679    605       O  
ATOM   1087  CB  THR A 174       4.228  -8.118  22.725  1.00 77.34           C  
ANISOU 1087  CB  THR A 174    12121  11619   5646   -256  -1084    317       C  
ATOM   1088  OG1 THR A 174       3.040  -7.648  22.068  1.00 76.67           O  
ANISOU 1088  OG1 THR A 174    11846  11683   5603    -99   -826    173       O  
ATOM   1089  CG2 THR A 174       5.382  -7.165  22.435  1.00 74.84           C  
ANISOU 1089  CG2 THR A 174    11872  11048   5517   -199  -1345    252       C  
ATOM   1090  N   THR A 175       3.496 -11.323  23.488  1.00 72.91           N  
ANISOU 1090  N   THR A 175    11638  11299   4767   -726   -951    806       N  
ATOM   1091  CA  THR A 175       2.377 -12.171  23.924  1.00 74.66           C  
ANISOU 1091  CA  THR A 175    11874  11780   4713   -936   -726    900       C  
ATOM   1092  C   THR A 175       2.247 -12.089  25.429  1.00 82.15           C  
ANISOU 1092  C   THR A 175    13084  12905   5225  -1051   -705    879       C  
ATOM   1093  O   THR A 175       3.143 -11.581  26.097  1.00 82.69           O  
ANISOU 1093  O   THR A 175    13353  12837   5229   -984   -913    828       O  
ATOM   1094  CB  THR A 175       2.561 -13.648  23.523  1.00 80.84           C  
ANISOU 1094  CB  THR A 175    12724  12416   5575  -1138   -822   1173       C  
ATOM   1095  OG1 THR A 175       3.695 -14.194  24.209  1.00 78.32           O  
ANISOU 1095  OG1 THR A 175    12693  11875   5190  -1184  -1118   1324       O  
ATOM   1096  CG2 THR A 175       2.736 -13.790  21.988  1.00 76.47           C  
ANISOU 1096  CG2 THR A 175    11935  11683   5438  -1015   -847   1187       C  
ATOM   1097  N   GLY A 176       1.129 -12.586  25.952  1.00 81.17           N  
ANISOU 1097  N   GLY A 176    12950  13109   4782  -1250   -453    922       N  
ATOM   1098  CA  GLY A 176       0.861 -12.568  27.396  1.00 84.67           C  
ANISOU 1098  CA  GLY A 176    13636  13787   4748  -1391   -381    907       C  
ATOM   1099  C   GLY A 176       1.368 -13.791  28.149  1.00 90.00           C  
ANISOU 1099  C   GLY A 176    14647  14337   5211  -1696   -570   1196       C  
ATOM   1100  O   GLY A 176       1.152 -13.919  29.353  1.00 93.11           O  
ANISOU 1100  O   GLY A 176    15277  14924   5177  -1865   -521   1226       O  
ATOM   1101  N   ASP A 177       2.037 -14.695  27.439  1.00 84.23           N  
ANISOU 1101  N   ASP A 177    13964  13280   4759  -1747   -793   1406       N  
ATOM   1102  CA  ASP A 177       2.577 -15.913  28.034  1.00 85.68           C  
ANISOU 1102  CA  ASP A 177    14509  13271   4774  -1981  -1024   1691       C  
ATOM   1103  C   ASP A 177       3.625 -16.489  27.081  1.00 85.75           C  
ANISOU 1103  C   ASP A 177    14523  12868   5191  -1830  -1320   1816       C  
ATOM   1104  O   ASP A 177       3.369 -16.594  25.882  1.00 82.60           O  
ANISOU 1104  O   ASP A 177    13876  12404   5103  -1752  -1237   1792       O  
ATOM   1105  CB  ASP A 177       1.447 -16.919  28.291  1.00 90.34           C  
ANISOU 1105  CB  ASP A 177    15183  14086   5057  -2373   -813   1874       C  
ATOM   1106  CG  ASP A 177       1.944 -18.229  28.889  1.00103.91           C  
ANISOU 1106  CG  ASP A 177    17357  15550   6572  -2636  -1074   2190       C  
ATOM   1107  OD1 ASP A 177       2.487 -19.055  28.126  1.00103.49           O  
ANISOU 1107  OD1 ASP A 177    17398  15138   6786  -2599  -1292   2346       O  
ATOM   1108  OD2 ASP A 177       1.774 -18.441  30.113  1.00112.53           O  
ANISOU 1108  OD2 ASP A 177    18738  16797   7220  -2869  -1064   2281       O  
ATOM   1109  N   PRO A 178       4.808 -16.853  27.605  1.00 82.49           N  
ANISOU 1109  N   PRO A 178    14376  12203   4763  -1768  -1667   1940       N  
ATOM   1110  CA  PRO A 178       5.918 -17.308  26.764  1.00 80.06           C  
ANISOU 1110  CA  PRO A 178    14033  11561   4824  -1551  -1954   2027       C  
ATOM   1111  C   PRO A 178       5.702 -18.643  26.044  1.00 83.56           C  
ANISOU 1111  C   PRO A 178    14596  11791   5363  -1646  -1995   2233       C  
ATOM   1112  O   PRO A 178       6.393 -18.915  25.060  1.00 81.02           O  
ANISOU 1112  O   PRO A 178    14158  11244   5383  -1419  -2141   2245       O  
ATOM   1113  CB  PRO A 178       7.078 -17.432  27.755  1.00 83.88           C  
ANISOU 1113  CB  PRO A 178    14792  11917   5163  -1489  -2309   2122       C  
ATOM   1114  CG  PRO A 178       6.438 -17.653  29.057  1.00 91.71           C  
ANISOU 1114  CG  PRO A 178    16102  13079   5664  -1775  -2229   2199       C  
ATOM   1115  CD  PRO A 178       5.186 -16.839  29.029  1.00 86.96           C  
ANISOU 1115  CD  PRO A 178    15277  12819   4945  -1875  -1817   1998       C  
ATOM   1116  N   THR A 179       4.775 -19.468  26.528  1.00 82.75           N  
ANISOU 1116  N   THR A 179    14741  11761   4940  -1990  -1874   2391       N  
ATOM   1117  CA  THR A 179       4.469 -20.740  25.869  1.00 83.23           C  
ANISOU 1117  CA  THR A 179    14985  11590   5049  -2142  -1921   2587       C  
ATOM   1118  C   THR A 179       3.530 -20.553  24.668  1.00 85.37           C  
ANISOU 1118  C   THR A 179    14903  11993   5542  -2186  -1636   2477       C  
ATOM   1119  O   THR A 179       3.382 -21.459  23.850  1.00 84.77           O  
ANISOU 1119  O   THR A 179    14926  11694   5590  -2253  -1690   2590       O  
ATOM   1120  CB  THR A 179       3.864 -21.776  26.844  1.00 94.73           C  
ANISOU 1120  CB  THR A 179    16900  13045   6047  -2573  -1940   2838       C  
ATOM   1121  OG1 THR A 179       2.536 -21.385  27.215  1.00 95.45           O  
ANISOU 1121  OG1 THR A 179    16824  13577   5864  -2902  -1565   2777       O  
ATOM   1122  CG2 THR A 179       4.734 -21.926  28.093  1.00 95.84           C  
ANISOU 1122  CG2 THR A 179    17412  13075   5928  -2540  -2229   2953       C  
ATOM   1123  N   VAL A 180       2.898 -19.383  24.570  1.00 80.94           N  
ANISOU 1123  N   VAL A 180    13962  11779   5014  -2133  -1355   2252       N  
ATOM   1124  CA  VAL A 180       2.073 -19.023  23.411  1.00 78.47           C  
ANISOU 1124  CA  VAL A 180    13269  11615   4931  -2107  -1109   2123       C  
ATOM   1125  C   VAL A 180       2.908 -18.198  22.440  1.00 78.60           C  
ANISOU 1125  C   VAL A 180    13009  11484   5373  -1704  -1194   1949       C  
ATOM   1126  O   VAL A 180       3.284 -17.070  22.754  1.00 77.10           O  
ANISOU 1126  O   VAL A 180    12675  11397   5223  -1507  -1185   1776       O  
ATOM   1127  CB  VAL A 180       0.808 -18.226  23.837  1.00 83.57           C  
ANISOU 1127  CB  VAL A 180    13653  12755   5343  -2248   -752   1974       C  
ATOM   1128  CG1 VAL A 180       0.237 -17.435  22.677  1.00 80.62           C  
ANISOU 1128  CG1 VAL A 180    12837  12533   5262  -2058   -554   1776       C  
ATOM   1129  CG2 VAL A 180      -0.248 -19.174  24.419  1.00 87.09           C  
ANISOU 1129  CG2 VAL A 180    14268  13424   5399  -2727   -605   2166       C  
ATOM   1130  N   CYS A 181       3.198 -18.786  21.277  1.00 73.79           N  
ANISOU 1130  N   CYS A 181    12360  10629   5049  -1610  -1284   2001       N  
ATOM   1131  CA  CYS A 181       3.964 -18.145  20.199  1.00 70.59           C  
ANISOU 1131  CA  CYS A 181    11686  10098   5036  -1271  -1349   1865       C  
ATOM   1132  C   CYS A 181       3.029 -17.813  19.032  1.00 72.33           C  
ANISOU 1132  C   CYS A 181    11594  10453   5435  -1283  -1113   1757       C  
ATOM   1133  O   CYS A 181       2.679 -18.681  18.233  1.00 71.84           O  
ANISOU 1133  O   CYS A 181    11581  10268   5446  -1385  -1108   1848       O  
ATOM   1134  CB  CYS A 181       5.102 -19.077  19.737  1.00 70.84           C  
ANISOU 1134  CB  CYS A 181    11907   9772   5239  -1098  -1639   1992       C  
ATOM   1135  SG  CYS A 181       6.087 -18.540  18.273  1.00 71.36           S  
ANISOU 1135  SG  CYS A 181    11636   9719   5759   -715  -1708   1859       S  
ATOM   1136  N   SER A 182       2.622 -16.551  18.947  1.00 67.43           N  
ANISOU 1136  N   SER A 182    10686  10069   4866  -1170   -939   1560       N  
ATOM   1137  CA  SER A 182       1.686 -16.110  17.912  1.00 65.59           C  
ANISOU 1137  CA  SER A 182    10145   9997   4779  -1149   -728   1448       C  
ATOM   1138  C   SER A 182       1.679 -14.586  17.796  1.00 67.90           C  
ANISOU 1138  C   SER A 182    10197  10424   5177   -904   -640   1222       C  
ATOM   1139  O   SER A 182       2.095 -13.884  18.731  1.00 69.37           O  
ANISOU 1139  O   SER A 182    10472  10648   5236   -828   -690   1142       O  
ATOM   1140  CB  SER A 182       0.273 -16.583  18.245  1.00 71.31           C  
ANISOU 1140  CB  SER A 182    10837  11023   5235  -1460   -508   1503       C  
ATOM   1141  OG  SER A 182      -0.175 -15.987  19.454  1.00 82.27           O  
ANISOU 1141  OG  SER A 182    12229  12705   6325  -1511   -379   1427       O  
ATOM   1142  N   ILE A 183       1.200 -14.085  16.655  1.00 61.16           N  
ANISOU 1142  N   ILE A 183     9082   9620   4535   -790   -532   1121       N  
ATOM   1143  CA  ILE A 183       1.049 -12.646  16.457  1.00 59.63           C  
ANISOU 1143  CA  ILE A 183     8707   9522   4426   -556   -458    911       C  
ATOM   1144  C   ILE A 183      -0.198 -12.216  17.189  1.00 65.67           C  
ANISOU 1144  C   ILE A 183     9380  10655   4919   -593   -231    802       C  
ATOM   1145  O   ILE A 183      -1.311 -12.470  16.724  1.00 65.86           O  
ANISOU 1145  O   ILE A 183     9199  10919   4907   -676    -57    801       O  
ATOM   1146  CB  ILE A 183       0.931 -12.246  14.972  1.00 60.05           C  
ANISOU 1146  CB  ILE A 183     8538   9502   4775   -412   -435    851       C  
ATOM   1147  CG1 ILE A 183       2.257 -12.469  14.257  1.00 58.34           C  
ANISOU 1147  CG1 ILE A 183     8377   8978   4811   -333   -637    924       C  
ATOM   1148  CG2 ILE A 183       0.573 -10.782  14.843  1.00 60.33           C  
ANISOU 1148  CG2 ILE A 183     8445   9631   4845   -183   -362    643       C  
ATOM   1149  CD1 ILE A 183       2.201 -12.193  12.785  1.00 63.08           C  
ANISOU 1149  CD1 ILE A 183     8791   9507   5668   -226   -614    887       C  
ATOM   1150  N   SER A 184       0.004 -11.586  18.344  1.00 63.77           N  
ANISOU 1150  N   SER A 184     9280  10483   4465   -533   -239    707       N  
ATOM   1151  CA  SER A 184      -1.086 -11.107  19.181  1.00 66.50           C  
ANISOU 1151  CA  SER A 184     9554  11208   4504   -516    -15    573       C  
ATOM   1152  C   SER A 184      -1.132  -9.574  19.290  1.00 71.35           C  
ANISOU 1152  C   SER A 184    10146  11838   5127   -177      8    307       C  
ATOM   1153  O   SER A 184      -2.031  -9.035  19.935  1.00 73.88           O  
ANISOU 1153  O   SER A 184    10399  12479   5191    -69    198    148       O  
ATOM   1154  CB  SER A 184      -0.998 -11.751  20.574  1.00 72.48           C  
ANISOU 1154  CB  SER A 184    10556  12073   4909   -749    -14    677       C  
ATOM   1155  OG  SER A 184       0.341 -11.853  21.029  1.00 79.74           O  
ANISOU 1155  OG  SER A 184    11756  12664   5876   -749   -280    752       O  
ATOM   1156  N   ASN A 185      -0.198  -8.871  18.648  1.00 65.94           N  
ANISOU 1156  N   ASN A 185     9523  10818   4711    -11   -184    256       N  
ATOM   1157  CA  ASN A 185      -0.118  -7.412  18.783  1.00 66.68           C  
ANISOU 1157  CA  ASN A 185     9702  10836   4797    272   -220     21       C  
ATOM   1158  C   ASN A 185      -1.202  -6.684  17.976  1.00 71.66           C  
ANISOU 1158  C   ASN A 185    10102  11627   5500    528    -62   -140       C  
ATOM   1159  O   ASN A 185      -1.235  -6.803  16.748  1.00 68.73           O  
ANISOU 1159  O   ASN A 185     9560  11156   5397    546    -89    -75       O  
ATOM   1160  CB  ASN A 185       1.262  -6.896  18.370  1.00 64.54           C  
ANISOU 1160  CB  ASN A 185     9587  10170   4765    295   -495     45       C  
ATOM   1161  CG  ASN A 185       1.438  -5.421  18.670  1.00 84.36           C  
ANISOU 1161  CG  ASN A 185    12294  12544   7216    514   -579   -180       C  
ATOM   1162  OD1 ASN A 185       1.574  -4.598  17.766  1.00 75.37           O  
ANISOU 1162  OD1 ASN A 185    11140  11218   6280    656   -653   -252       O  
ATOM   1163  ND2 ASN A 185       1.410  -5.080  19.946  1.00 80.04           N  
ANISOU 1163  ND2 ASN A 185    11972  12074   6365    534   -577   -293       N  
ATOM   1164  N   PRO A 186      -2.075  -5.909  18.659  1.00 71.85           N  
ANISOU 1164  N   PRO A 186    10125  11906   5269    758     92   -358       N  
ATOM   1165  CA  PRO A 186      -3.214  -5.228  18.015  1.00 72.94           C  
ANISOU 1165  CA  PRO A 186    10023  12262   5430   1065    244   -527       C  
ATOM   1166  C   PRO A 186      -2.843  -4.232  16.921  1.00 75.28           C  
ANISOU 1166  C   PRO A 186    10384  12209   6011   1304     74   -608       C  
ATOM   1167  O   PRO A 186      -3.557  -4.124  15.925  1.00 74.51           O  
ANISOU 1167  O   PRO A 186    10041  12214   6057   1442    138   -623       O  
ATOM   1168  CB  PRO A 186      -3.889  -4.477  19.172  1.00 78.73           C  
ANISOU 1168  CB  PRO A 186    10845  13268   5800   1321    391   -776       C  
ATOM   1169  CG  PRO A 186      -3.414  -5.139  20.403  1.00 84.23           C  
ANISOU 1169  CG  PRO A 186    11736  14024   6244   1040    395   -682       C  
ATOM   1170  CD  PRO A 186      -2.035  -5.632  20.106  1.00 76.46           C  
ANISOU 1170  CD  PRO A 186    10943  12607   5502    774    128   -471       C  
ATOM   1171  N   ASP A 187      -1.751  -3.498  17.115  1.00 70.99           N  
ANISOU 1171  N   ASP A 187    10175  11269   5527   1326   -151   -652       N  
ATOM   1172  CA  ASP A 187      -1.298  -2.529  16.114  1.00 69.23           C  
ANISOU 1172  CA  ASP A 187    10072  10687   5545   1481   -334   -702       C  
ATOM   1173  C   ASP A 187      -0.666  -3.240  14.907  1.00 67.71           C  
ANISOU 1173  C   ASP A 187     9717  10336   5672   1246   -422   -470       C  
ATOM   1174  O   ASP A 187      -1.141  -3.071  13.786  1.00 66.01           O  
ANISOU 1174  O   ASP A 187     9337  10117   5628   1359   -399   -462       O  
ATOM   1175  CB  ASP A 187      -0.343  -1.490  16.737  1.00 72.48           C  
ANISOU 1175  CB  ASP A 187    10912  10743   5883   1518   -559   -817       C  
ATOM   1176  CG  ASP A 187      -1.065  -0.493  17.671  1.00 87.64           C  
ANISOU 1176  CG  ASP A 187    13058  12746   7496   1866   -494  -1110       C  
ATOM   1177  OD1 ASP A 187      -2.247  -0.150  17.412  1.00 90.24           O  
ANISOU 1177  OD1 ASP A 187    13222  13309   7757   2202   -329  -1262       O  
ATOM   1178  OD2 ASP A 187      -0.443  -0.043  18.663  1.00 96.02           O  
ANISOU 1178  OD2 ASP A 187    14463  13649   8370   1822   -617  -1199       O  
ATOM   1179  N   PHE A 188       0.364  -4.056  15.130  1.00 61.75           N  
ANISOU 1179  N   PHE A 188     9006   9476   4980    948   -521   -288       N  
ATOM   1180  CA  PHE A 188       1.029  -4.767  14.026  1.00 58.50           C  
ANISOU 1180  CA  PHE A 188     8451   8931   4844    766   -598    -89       C  
ATOM   1181  C   PHE A 188       0.061  -5.507  13.098  1.00 60.09           C  
ANISOU 1181  C   PHE A 188     8356   9336   5139    768   -435    -20       C  
ATOM   1182  O   PHE A 188       0.201  -5.446  11.877  1.00 57.23           O  
ANISOU 1182  O   PHE A 188     7897   8852   4996    780   -481     37       O  
ATOM   1183  CB  PHE A 188       2.044  -5.769  14.569  1.00 59.72           C  
ANISOU 1183  CB  PHE A 188     8657   9039   4993    509   -692     84       C  
ATOM   1184  CG  PHE A 188       2.951  -6.354  13.510  1.00 59.14           C  
ANISOU 1184  CG  PHE A 188     8477   8809   5184    383   -799    253       C  
ATOM   1185  CD1 PHE A 188       4.111  -5.685  13.119  1.00 61.93           C  
ANISOU 1185  CD1 PHE A 188     8911   8941   5679    348   -990    271       C  
ATOM   1186  CD2 PHE A 188       2.658  -7.576  12.916  1.00 60.33           C  
ANISOU 1186  CD2 PHE A 188     8458   9050   5416    287   -710    391       C  
ATOM   1187  CE1 PHE A 188       4.957  -6.222  12.144  1.00 61.28           C  
ANISOU 1187  CE1 PHE A 188     8692   8780   5811    254  -1062    415       C  
ATOM   1188  CE2 PHE A 188       3.500  -8.123  11.939  1.00 61.46           C  
ANISOU 1188  CE2 PHE A 188     8520   9057   5775    221   -799    520       C  
ATOM   1189  CZ  PHE A 188       4.647  -7.442  11.552  1.00 59.08           C  
ANISOU 1189  CZ  PHE A 188     8252   8587   5609    222   -960    527       C  
ATOM   1190  N   VAL A 189      -0.902  -6.214  13.692  1.00 57.83           N  
ANISOU 1190  N   VAL A 189     7933   9375   4664    719   -251    -16       N  
ATOM   1191  CA  VAL A 189      -1.885  -7.012  12.942  1.00 56.91           C  
ANISOU 1191  CA  VAL A 189     7532   9500   4592    649   -104     61       C  
ATOM   1192  C   VAL A 189      -2.657  -6.165  11.925  1.00 60.77           C  
ANISOU 1192  C   VAL A 189     7861  10036   5194    909    -74    -55       C  
ATOM   1193  O   VAL A 189      -2.860  -6.583  10.779  1.00 58.75           O  
ANISOU 1193  O   VAL A 189     7445   9767   5111    849    -80     36       O  
ATOM   1194  CB  VAL A 189      -2.882  -7.739  13.896  1.00 62.96           C  
ANISOU 1194  CB  VAL A 189     8176  10672   5074    520     96     72       C  
ATOM   1195  CG1 VAL A 189      -4.200  -8.051  13.192  1.00 63.59           C  
ANISOU 1195  CG1 VAL A 189     7917  11096   5147    523    259     71       C  
ATOM   1196  CG2 VAL A 189      -2.267  -9.017  14.439  1.00 62.20           C  
ANISOU 1196  CG2 VAL A 189     8209  10509   4914    184     52    273       C  
ATOM   1197  N   ILE A 190      -3.078  -4.975  12.344  1.00 59.42           N  
ANISOU 1197  N   ILE A 190     7768   9902   4908   1217    -62   -262       N  
ATOM   1198  CA  ILE A 190      -3.750  -4.050  11.442  1.00 59.81           C  
ANISOU 1198  CA  ILE A 190     7729   9947   5049   1526    -78   -383       C  
ATOM   1199  C   ILE A 190      -2.796  -3.653  10.321  1.00 61.25           C  
ANISOU 1199  C   ILE A 190     8061   9715   5496   1487   -279   -299       C  
ATOM   1200  O   ILE A 190      -3.142  -3.726   9.146  1.00 60.07           O  
ANISOU 1200  O   ILE A 190     7758   9565   5500   1515   -291   -243       O  
ATOM   1201  CB  ILE A 190      -4.184  -2.771  12.153  1.00 66.01           C  
ANISOU 1201  CB  ILE A 190     8679  10751   5652   1911    -76   -636       C  
ATOM   1202  CG1 ILE A 190      -5.167  -3.073  13.283  1.00 69.58           C  
ANISOU 1202  CG1 ILE A 190     8956  11682   5800   1985    153   -745       C  
ATOM   1203  CG2 ILE A 190      -4.820  -1.818  11.162  1.00 67.93           C  
ANISOU 1203  CG2 ILE A 190     8880  10935   5995   2265   -139   -748       C  
ATOM   1204  CD1 ILE A 190      -5.109  -2.041  14.413  1.00 83.39           C  
ANISOU 1204  CD1 ILE A 190    11002  13374   7310   2271    139   -982       C  
ATOM   1205  N   TYR A 191      -1.592  -3.238  10.702  1.00 56.96           N  
ANISOU 1205  N   TYR A 191     7810   8851   4982   1397   -436   -285       N  
ATOM   1206  CA  TYR A 191      -0.564  -2.801   9.755  1.00 54.75           C  
ANISOU 1206  CA  TYR A 191     7672   8217   4913   1309   -623   -198       C  
ATOM   1207  C   TYR A 191      -0.332  -3.868   8.708  1.00 55.79           C  
ANISOU 1207  C   TYR A 191     7586   8383   5229   1098   -592     -9       C  
ATOM   1208  O   TYR A 191      -0.542  -3.626   7.516  1.00 54.46           O  
ANISOU 1208  O   TYR A 191     7347   8147   5197   1155   -623     21       O  
ATOM   1209  CB  TYR A 191       0.713  -2.431  10.532  1.00 55.93           C  
ANISOU 1209  CB  TYR A 191     8102   8123   5026   1161   -782   -188       C  
ATOM   1210  CG  TYR A 191       2.085  -2.551   9.865  1.00 55.58           C  
ANISOU 1210  CG  TYR A 191     8101   7849   5168    911   -940    -27       C  
ATOM   1211  CD1 TYR A 191       2.530  -1.620   8.937  1.00 57.60           C  
ANISOU 1211  CD1 TYR A 191     8488   7856   5541    912  -1081    -16       C  
ATOM   1212  CD2 TYR A 191       2.980  -3.546  10.266  1.00 55.04           C  
ANISOU 1212  CD2 TYR A 191     7961   7829   5124    679   -960    111       C  
ATOM   1213  CE1 TYR A 191       3.813  -1.717   8.382  1.00 57.39           C  
ANISOU 1213  CE1 TYR A 191     8458   7697   5649    658  -1204    132       C  
ATOM   1214  CE2 TYR A 191       4.256  -3.651   9.726  1.00 54.67           C  
ANISOU 1214  CE2 TYR A 191     7902   7648   5224    488  -1094    242       C  
ATOM   1215  CZ  TYR A 191       4.681  -2.741   8.786  1.00 61.53           C  
ANISOU 1215  CZ  TYR A 191     8845   8330   6202    462  -1202    253       C  
ATOM   1216  OH  TYR A 191       5.965  -2.865   8.255  1.00 60.69           O  
ANISOU 1216  OH  TYR A 191     8675   8170   6216    248  -1312    389       O  
ATOM   1217  N   SER A 192       0.046  -5.062   9.153  1.00 51.54           N  
ANISOU 1217  N   SER A 192     6970   7942   4672    873   -541    112       N  
ATOM   1218  CA  SER A 192       0.394  -6.122   8.216  1.00 49.54           C  
ANISOU 1218  CA  SER A 192     6579   7672   4573    693   -534    276       C  
ATOM   1219  C   SER A 192      -0.767  -6.417   7.293  1.00 54.35           C  
ANISOU 1219  C   SER A 192     6974   8457   5217    749   -429    277       C  
ATOM   1220  O   SER A 192      -0.575  -6.478   6.083  1.00 52.95           O  
ANISOU 1220  O   SER A 192     6748   8178   5194    727   -473    341       O  
ATOM   1221  CB  SER A 192       0.826  -7.401   8.919  1.00 52.42           C  
ANISOU 1221  CB  SER A 192     6947   8096   4875    488   -510    394       C  
ATOM   1222  OG  SER A 192       1.166  -8.374   7.945  1.00 59.46           O  
ANISOU 1222  OG  SER A 192     7757   8931   5907    368   -521    526       O  
ATOM   1223  N   SER A 193      -1.964  -6.577   7.859  1.00 52.66           N  
ANISOU 1223  N   SER A 193     6621   8542   4845    811   -292    206       N  
ATOM   1224  CA  SER A 193      -3.169  -6.853   7.071  1.00 52.83           C  
ANISOU 1224  CA  SER A 193     6390   8810   4874    847   -200    205       C  
ATOM   1225  C   SER A 193      -3.339  -5.894   5.884  1.00 56.30           C  
ANISOU 1225  C   SER A 193     6820   9121   5452   1060   -290    152       C  
ATOM   1226  O   SER A 193      -3.629  -6.327   4.763  1.00 54.94           O  
ANISOU 1226  O   SER A 193     6521   8973   5383    991   -300    230       O  
ATOM   1227  CB  SER A 193      -4.393  -6.761   7.959  1.00 58.94           C  
ANISOU 1227  CB  SER A 193     6989   9977   5427    949    -46     95       C  
ATOM   1228  OG  SER A 193      -4.538  -5.443   8.434  1.00 69.30           O  
ANISOU 1228  OG  SER A 193     8406  11256   6667   1281    -72    -90       O  
ATOM   1229  N   VAL A 194      -3.154  -4.597   6.129  1.00 53.80           N  
ANISOU 1229  N   VAL A 194     6682   8644   5118   1309   -376     24       N  
ATOM   1230  CA  VAL A 194      -3.133  -3.613   5.043  1.00 53.49           C  
ANISOU 1230  CA  VAL A 194     6734   8396   5195   1489   -505     -3       C  
ATOM   1231  C   VAL A 194      -1.973  -3.868   4.081  1.00 55.53           C  
ANISOU 1231  C   VAL A 194     7097   8376   5626   1264   -607    148       C  
ATOM   1232  O   VAL A 194      -2.208  -4.136   2.905  1.00 54.05           O  
ANISOU 1232  O   VAL A 194     6805   8197   5534   1227   -619    222       O  
ATOM   1233  CB  VAL A 194      -3.019  -2.166   5.552  1.00 59.05           C  
ANISOU 1233  CB  VAL A 194     7717   8894   5825   1768   -616   -162       C  
ATOM   1234  CG1 VAL A 194      -2.641  -1.232   4.412  1.00 58.54           C  
ANISOU 1234  CG1 VAL A 194     7853   8506   5882   1844   -795   -133       C  
ATOM   1235  CG2 VAL A 194      -4.318  -1.725   6.189  1.00 61.91           C  
ANISOU 1235  CG2 VAL A 194     7955   9554   6014   2110   -519   -346       C  
ATOM   1236  N   VAL A 195      -0.733  -3.785   4.576  1.00 51.88           N  
ANISOU 1236  N   VAL A 195     6821   7705   5185   1117   -680    191       N  
ATOM   1237  CA  VAL A 195       0.442  -3.890   3.704  1.00 49.98           C  
ANISOU 1237  CA  VAL A 195     6648   7259   5085    928   -769    320       C  
ATOM   1238  C   VAL A 195       0.638  -5.291   3.126  1.00 52.44           C  
ANISOU 1238  C   VAL A 195     6778   7678   5469    746   -687    446       C  
ATOM   1239  O   VAL A 195       1.082  -5.416   1.989  1.00 51.06           O  
ANISOU 1239  O   VAL A 195     6585   7422   5395    672   -718    527       O  
ATOM   1240  CB  VAL A 195       1.736  -3.433   4.407  1.00 53.84           C  
ANISOU 1240  CB  VAL A 195     7334   7561   5564    805   -881    335       C  
ATOM   1241  CG1 VAL A 195       2.963  -3.860   3.614  1.00 52.22           C  
ANISOU 1241  CG1 VAL A 195     7085   7276   5481    589   -927    480       C  
ATOM   1242  CG2 VAL A 195       1.727  -1.930   4.582  1.00 55.53           C  
ANISOU 1242  CG2 VAL A 195     7819   7558   5721    939  -1018    231       C  
ATOM   1243  N   SER A 196       0.306  -6.336   3.882  1.00 49.38           N  
ANISOU 1243  N   SER A 196     6294   7461   5008    670   -590    461       N  
ATOM   1244  CA  SER A 196       0.508  -7.715   3.407  1.00 48.36           C  
ANISOU 1244  CA  SER A 196     6078   7374   4924    503   -542    574       C  
ATOM   1245  C   SER A 196      -0.594  -7.931   2.376  1.00 53.05           C  
ANISOU 1245  C   SER A 196     6531   8091   5535    527   -492    574       C  
ATOM   1246  O   SER A 196      -0.306  -8.234   1.215  1.00 52.73           O  
ANISOU 1246  O   SER A 196     6481   7970   5584    475   -517    635       O  
ATOM   1247  CB  SER A 196       0.851  -8.674   4.558  1.00 52.73           C  
ANISOU 1247  CB  SER A 196     6674   7971   5388    384   -515    618       C  
ATOM   1248  OG  SER A 196       2.131  -8.398   5.098  1.00 63.51           O  
ANISOU 1248  OG  SER A 196     8156   9195   6779    366   -611    639       O  
ATOM   1249  N   PHE A 197      -1.851  -7.783   2.767  1.00 50.36           N  
ANISOU 1249  N   PHE A 197     6064   7978   5094    605   -423    503       N  
ATOM   1250  CA  PHE A 197      -2.907  -8.028   1.806  1.00 50.36           C  
ANISOU 1250  CA  PHE A 197     5892   8142   5101    608   -397    511       C  
ATOM   1251  C   PHE A 197      -3.732  -6.965   1.106  1.00 54.44           C  
ANISOU 1251  C   PHE A 197     6324   8727   5633    841   -443    433       C  
ATOM   1252  O   PHE A 197      -3.675  -6.822  -0.117  1.00 53.18           O  
ANISOU 1252  O   PHE A 197     6178   8468   5559    847   -514    476       O  
ATOM   1253  CB  PHE A 197      -3.755  -8.830   2.798  1.00 53.69           C  
ANISOU 1253  CB  PHE A 197     6180   8849   5369    485   -282    510       C  
ATOM   1254  CG  PHE A 197      -4.691  -9.807   2.149  1.00 56.21           C  
ANISOU 1254  CG  PHE A 197     6330   9376   5651    295   -242    576       C  
ATOM   1255  CD1 PHE A 197      -4.196 -10.928   1.479  1.00 58.41           C  
ANISOU 1255  CD1 PHE A 197     6721   9491   5981     69   -281    687       C  
ATOM   1256  CD2 PHE A 197      -6.071  -9.625   2.228  1.00 60.80           C  
ANISOU 1256  CD2 PHE A 197     6640  10335   6127    341   -176    521       C  
ATOM   1257  CE1 PHE A 197      -5.065 -11.843   0.878  1.00 60.24           C  
ANISOU 1257  CE1 PHE A 197     6850   9883   6156   -148   -271    747       C  
ATOM   1258  CE2 PHE A 197      -6.950 -10.537   1.640  1.00 64.64           C  
ANISOU 1258  CE2 PHE A 197     6954  11045   6561    105   -159    595       C  
ATOM   1259  CZ  PHE A 197      -6.445 -11.648   0.963  1.00 61.46           C  
ANISOU 1259  CZ  PHE A 197     6719  10426   6207   -162   -216    711       C  
ATOM   1260  N   TYR A 198      -4.468  -6.186   1.878  1.00 52.61           N  
ANISOU 1260  N   TYR A 198     6028   8659   5304   1062   -414    310       N  
ATOM   1261  CA  TYR A 198      -5.478  -5.319   1.292  1.00 54.25           C  
ANISOU 1261  CA  TYR A 198     6118   8996   5498   1337   -462    225       C  
ATOM   1262  C   TYR A 198      -4.925  -4.267   0.331  1.00 56.62           C  
ANISOU 1262  C   TYR A 198     6643   8966   5903   1485   -624    230       C  
ATOM   1263  O   TYR A 198      -5.669  -3.747  -0.489  1.00 57.42           O  
ANISOU 1263  O   TYR A 198     6677   9127   6015   1672   -700    206       O  
ATOM   1264  CB  TYR A 198      -6.331  -4.689   2.393  1.00 58.59           C  
ANISOU 1264  CB  TYR A 198     6563   9802   5896   1606   -389     67       C  
ATOM   1265  CG  TYR A 198      -7.080  -5.735   3.196  1.00 61.98           C  
ANISOU 1265  CG  TYR A 198     6721  10644   6184   1419   -216     82       C  
ATOM   1266  CD1 TYR A 198      -8.037  -6.554   2.589  1.00 64.68           C  
ANISOU 1266  CD1 TYR A 198     6760  11314   6501   1257   -168    151       C  
ATOM   1267  CD2 TYR A 198      -6.830  -5.916   4.549  1.00 63.63           C  
ANISOU 1267  CD2 TYR A 198     6995  10919   6263   1360   -115     42       C  
ATOM   1268  CE1 TYR A 198      -8.720  -7.520   3.308  1.00 66.73           C  
ANISOU 1268  CE1 TYR A 198     6791  11955   6606   1011    -20    189       C  
ATOM   1269  CE2 TYR A 198      -7.514  -6.878   5.279  1.00 66.11           C  
ANISOU 1269  CE2 TYR A 198     7088  11615   6417   1140     41     79       C  
ATOM   1270  CZ  TYR A 198      -8.455  -7.677   4.652  1.00 75.04           C  
ANISOU 1270  CZ  TYR A 198     7923  13066   7523    950     90    159       C  
ATOM   1271  OH  TYR A 198      -9.132  -8.628   5.382  1.00 78.59           O  
ANISOU 1271  OH  TYR A 198     8173  13900   7789    664    236    217       O  
ATOM   1272  N   LEU A 199      -3.633  -3.960   0.414  1.00 51.09           N  
ANISOU 1272  N   LEU A 199     6206   7940   5267   1382   -688    275       N  
ATOM   1273  CA  LEU A 199      -3.018  -3.048  -0.542  1.00 50.47           C  
ANISOU 1273  CA  LEU A 199     6355   7558   5265   1424   -838    316       C  
ATOM   1274  C   LEU A 199      -2.581  -3.758  -1.823  1.00 52.80           C  
ANISOU 1274  C   LEU A 199     6607   7807   5647   1202   -842    455       C  
ATOM   1275  O   LEU A 199      -3.069  -3.425  -2.893  1.00 52.78           O  
ANISOU 1275  O   LEU A 199     6602   7793   5660   1280   -918    481       O  
ATOM   1276  CB  LEU A 199      -1.853  -2.273   0.079  1.00 50.34           C  
ANISOU 1276  CB  LEU A 199     6628   7249   5249   1379   -920    305       C  
ATOM   1277  CG  LEU A 199      -1.073  -1.392  -0.905  1.00 55.11           C  
ANISOU 1277  CG  LEU A 199     7485   7546   5908   1313  -1075    384       C  
ATOM   1278  CD1 LEU A 199      -2.003  -0.432  -1.676  1.00 57.24           C  
ANISOU 1278  CD1 LEU A 199     7858   7741   6149   1586  -1200    339       C  
ATOM   1279  CD2 LEU A 199       0.014  -0.617  -0.177  1.00 58.22           C  
ANISOU 1279  CD2 LEU A 199     8155   7688   6277   1217  -1171    375       C  
ATOM   1280  N   PRO A 200      -1.658  -4.728  -1.734  1.00 47.68           N  
ANISOU 1280  N   PRO A 200     5943   7132   5040    953   -771    538       N  
ATOM   1281  CA  PRO A 200      -1.283  -5.365  -2.991  1.00 46.32           C  
ANISOU 1281  CA  PRO A 200     5750   6926   4923    796   -769    640       C  
ATOM   1282  C   PRO A 200      -2.449  -6.071  -3.691  1.00 51.18           C  
ANISOU 1282  C   PRO A 200     6186   7747   5512    793   -740    645       C  
ATOM   1283  O   PRO A 200      -2.446  -6.177  -4.917  1.00 50.77           O  
ANISOU 1283  O   PRO A 200     6157   7656   5478    741   -782    703       O  
ATOM   1284  CB  PRO A 200      -0.186  -6.357  -2.578  1.00 46.60           C  
ANISOU 1284  CB  PRO A 200     5789   6931   4986    608   -696    696       C  
ATOM   1285  CG  PRO A 200      -0.328  -6.530  -1.112  1.00 51.10           C  
ANISOU 1285  CG  PRO A 200     6333   7577   5505    634   -651    638       C  
ATOM   1286  CD  PRO A 200      -0.860  -5.236  -0.604  1.00 48.25           C  
ANISOU 1286  CD  PRO A 200     6042   7190   5100    835   -713    541       C  
ATOM   1287  N   PHE A 201      -3.428  -6.540  -2.920  1.00 48.96           N  
ANISOU 1287  N   PHE A 201     5727   7708   5167    821   -672    591       N  
ATOM   1288  CA  PHE A 201      -4.660  -7.145  -3.473  1.00 49.79           C  
ANISOU 1288  CA  PHE A 201     5621   8073   5225    783   -661    596       C  
ATOM   1289  C   PHE A 201      -5.480  -6.100  -4.225  1.00 53.15           C  
ANISOU 1289  C   PHE A 201     5997   8552   5644   1026   -774    556       C  
ATOM   1290  O   PHE A 201      -5.918  -6.335  -5.341  1.00 52.91           O  
ANISOU 1290  O   PHE A 201     5914   8576   5615    976   -837    604       O  
ATOM   1291  CB  PHE A 201      -5.451  -7.814  -2.331  1.00 53.18           C  
ANISOU 1291  CB  PHE A 201     5855   8793   5558    714   -552    559       C  
ATOM   1292  CG  PHE A 201      -6.918  -8.049  -2.608  1.00 57.35           C  
ANISOU 1292  CG  PHE A 201     6092   9692   6005    718   -546    540       C  
ATOM   1293  CD1 PHE A 201      -7.339  -8.908  -3.625  1.00 60.57           C  
ANISOU 1293  CD1 PHE A 201     6431  10178   6406    503   -586    616       C  
ATOM   1294  CD2 PHE A 201      -7.889  -7.463  -1.780  1.00 62.36           C  
ANISOU 1294  CD2 PHE A 201     6506  10640   6547    928   -497    438       C  
ATOM   1295  CE1 PHE A 201      -8.723  -9.148  -3.842  1.00 64.02           C  
ANISOU 1295  CE1 PHE A 201     6557  11014   6753    460   -596    608       C  
ATOM   1296  CE2 PHE A 201      -9.257  -7.696  -1.985  1.00 67.81           C  
ANISOU 1296  CE2 PHE A 201     6853  11764   7147    927   -484    421       C  
ATOM   1297  CZ  PHE A 201      -9.672  -8.542  -3.019  1.00 65.88           C  
ANISOU 1297  CZ  PHE A 201     6518  11609   6906    670   -542    516       C  
ATOM   1298  N   GLY A 202      -5.642  -4.936  -3.610  1.00 49.55           N  
ANISOU 1298  N   GLY A 202     5600   8057   5170   1302   -819    464       N  
ATOM   1299  CA  GLY A 202      -6.294  -3.805  -4.243  1.00 50.68           C  
ANISOU 1299  CA  GLY A 202     5778   8177   5300   1600   -962    419       C  
ATOM   1300  C   GLY A 202      -5.595  -3.321  -5.499  1.00 52.81           C  
ANISOU 1300  C   GLY A 202     6300   8141   5624   1546  -1094    515       C  
ATOM   1301  O   GLY A 202      -6.247  -2.911  -6.458  1.00 53.85           O  
ANISOU 1301  O   GLY A 202     6419   8303   5737   1677  -1218    535       O  
ATOM   1302  N   VAL A 203      -4.270  -3.352  -5.509  1.00 46.75           N  
ANISOU 1302  N   VAL A 203     5748   7109   4904   1347  -1072    583       N  
ATOM   1303  CA  VAL A 203      -3.550  -2.988  -6.715  1.00 45.88           C  
ANISOU 1303  CA  VAL A 203     5848   6771   4815   1235  -1163    689       C  
ATOM   1304  C   VAL A 203      -3.914  -3.982  -7.816  1.00 49.35           C  
ANISOU 1304  C   VAL A 203     6147   7361   5244   1081  -1135    756       C  
ATOM   1305  O   VAL A 203      -4.498  -3.600  -8.844  1.00 50.26           O  
ANISOU 1305  O   VAL A 203     6291   7482   5323   1162  -1255    790       O  
ATOM   1306  CB  VAL A 203      -2.026  -2.972  -6.504  1.00 48.25           C  
ANISOU 1306  CB  VAL A 203     6322   6859   5150   1016  -1119    752       C  
ATOM   1307  CG1 VAL A 203      -1.299  -3.063  -7.836  1.00 47.61           C  
ANISOU 1307  CG1 VAL A 203     6349   6678   5062    823  -1140    873       C  
ATOM   1308  CG2 VAL A 203      -1.597  -1.708  -5.749  1.00 49.24           C  
ANISOU 1308  CG2 VAL A 203     6691   6758   5262   1125  -1219    709       C  
ATOM   1309  N   THR A 204      -3.607  -5.257  -7.581  1.00 43.91           N  
ANISOU 1309  N   THR A 204     5336   6778   4570    871   -999    771       N  
ATOM   1310  CA  THR A 204      -3.811  -6.298  -8.595  1.00 42.95           C  
ANISOU 1310  CA  THR A 204     5154   6747   4420    695   -978    823       C  
ATOM   1311  C   THR A 204      -5.243  -6.375  -9.094  1.00 48.52           C  
ANISOU 1311  C   THR A 204     5679   7685   5072    772  -1063    804       C  
ATOM   1312  O   THR A 204      -5.469  -6.650 -10.270  1.00 48.30           O  
ANISOU 1312  O   THR A 204     5682   7670   5001    689  -1130    855       O  
ATOM   1313  CB  THR A 204      -3.505  -7.696  -8.073  1.00 47.26           C  
ANISOU 1313  CB  THR A 204     5631   7360   4967    499   -849    821       C  
ATOM   1314  OG1 THR A 204      -4.608  -8.143  -7.263  1.00 46.47           O  
ANISOU 1314  OG1 THR A 204     5321   7503   4831    502   -820    773       O  
ATOM   1315  CG2 THR A 204      -2.170  -7.730  -7.294  1.00 44.71           C  
ANISOU 1315  CG2 THR A 204     5416   6877   4695    459   -770    827       C  
ATOM   1316  N   VAL A 205      -6.206  -6.177  -8.197  1.00 46.50           N  
ANISOU 1316  N   VAL A 205     5216   7652   4801    923  -1056    729       N  
ATOM   1317  CA  VAL A 205      -7.611  -6.235  -8.594  1.00 48.44           C  
ANISOU 1317  CA  VAL A 205     5212   8207   4987   1006  -1138    709       C  
ATOM   1318  C   VAL A 205      -7.927  -5.111  -9.550  1.00 54.38           C  
ANISOU 1318  C   VAL A 205     6067   8869   5726   1247  -1323    724       C  
ATOM   1319  O   VAL A 205      -8.672  -5.306 -10.502  1.00 55.58           O  
ANISOU 1319  O   VAL A 205     6117   9173   5828   1227  -1431    760       O  
ATOM   1320  CB  VAL A 205      -8.586  -6.152  -7.411  1.00 53.91           C  
ANISOU 1320  CB  VAL A 205     5614   9231   5639   1154  -1076    615       C  
ATOM   1321  CG1 VAL A 205      -9.828  -5.367  -7.809  1.00 56.77           C  
ANISOU 1321  CG1 VAL A 205     5765   9852   5952   1460  -1214    566       C  
ATOM   1322  CG2 VAL A 205      -8.962  -7.553  -6.933  1.00 53.56           C  
ANISOU 1322  CG2 VAL A 205     5371   9437   5541    829   -953    640       C  
ATOM   1323  N   LEU A 206      -7.363  -3.935  -9.307  1.00 51.16           N  
ANISOU 1323  N   LEU A 206     5893   8198   5348   1459  -1382    705       N  
ATOM   1324  CA  LEU A 206      -7.626  -2.798 -10.188  1.00 52.90           C  
ANISOU 1324  CA  LEU A 206     6294   8268   5537   1692  -1589    734       C  
ATOM   1325  C   LEU A 206      -6.770  -2.866 -11.471  1.00 55.58           C  
ANISOU 1325  C   LEU A 206     6898   8362   5857   1459  -1640    865       C  
ATOM   1326  O   LEU A 206      -7.194  -2.391 -12.534  1.00 56.93           O  
ANISOU 1326  O   LEU A 206     7166   8498   5968   1544  -1812    924       O  
ATOM   1327  CB  LEU A 206      -7.468  -1.469  -9.429  1.00 54.40           C  
ANISOU 1327  CB  LEU A 206     6692   8244   5733   2010  -1669    659       C  
ATOM   1328  CG  LEU A 206      -8.468  -1.260  -8.265  1.00 61.12           C  
ANISOU 1328  CG  LEU A 206     7279   9383   6560   2329  -1629    504       C  
ATOM   1329  CD1 LEU A 206      -8.133   0.016  -7.476  1.00 62.68           C  
ANISOU 1329  CD1 LEU A 206     7776   9296   6743   2632  -1706    410       C  
ATOM   1330  CD2 LEU A 206      -9.933  -1.233  -8.728  1.00 66.44           C  
ANISOU 1330  CD2 LEU A 206     7634  10435   7175   2585  -1737    463       C  
ATOM   1331  N   VAL A 207      -5.592  -3.478 -11.386  1.00 49.28           N  
ANISOU 1331  N   VAL A 207     6203   7430   5092   1180  -1492    908       N  
ATOM   1332  CA  VAL A 207      -4.838  -3.820 -12.591  1.00 48.01           C  
ANISOU 1332  CA  VAL A 207     6211   7148   4883    943  -1486   1012       C  
ATOM   1333  C   VAL A 207      -5.639  -4.780 -13.468  1.00 52.04           C  
ANISOU 1333  C   VAL A 207     6568   7873   5330    837  -1510   1024       C  
ATOM   1334  O   VAL A 207      -5.855  -4.525 -14.652  1.00 53.41           O  
ANISOU 1334  O   VAL A 207     6859   8015   5420    824  -1636   1091       O  
ATOM   1335  CB  VAL A 207      -3.509  -4.496 -12.260  1.00 49.59           C  
ANISOU 1335  CB  VAL A 207     6463   7258   5119    709  -1303   1030       C  
ATOM   1336  CG1 VAL A 207      -2.995  -5.285 -13.466  1.00 48.62           C  
ANISOU 1336  CG1 VAL A 207     6412   7139   4921    494  -1249   1092       C  
ATOM   1337  CG2 VAL A 207      -2.502  -3.464 -11.792  1.00 49.45           C  
ANISOU 1337  CG2 VAL A 207     6651   7010   5129    720  -1316   1060       C  
ATOM   1338  N   TYR A 208      -6.077  -5.889 -12.882  1.00 46.99           N  
ANISOU 1338  N   TYR A 208     5698   7445   4711    733  -1405    967       N  
ATOM   1339  CA  TYR A 208      -6.849  -6.878 -13.626  1.00 47.05           C  
ANISOU 1339  CA  TYR A 208     5583   7650   4644    572  -1445    976       C  
ATOM   1340  C   TYR A 208      -8.212  -6.365 -14.083  1.00 52.01           C  
ANISOU 1340  C   TYR A 208     6036   8506   5221    744  -1636    975       C  
ATOM   1341  O   TYR A 208      -8.747  -6.838 -15.076  1.00 52.67           O  
ANISOU 1341  O   TYR A 208     6097   8700   5217    620  -1738   1012       O  
ATOM   1342  CB  TYR A 208      -7.003  -8.167 -12.823  1.00 47.66           C  
ANISOU 1342  CB  TYR A 208     5503   7872   4734    376  -1311    931       C  
ATOM   1343  CG  TYR A 208      -6.000  -9.200 -13.232  1.00 47.99           C  
ANISOU 1343  CG  TYR A 208     5745   7741   4748    148  -1205    948       C  
ATOM   1344  CD1 TYR A 208      -6.066  -9.776 -14.494  1.00 50.57           C  
ANISOU 1344  CD1 TYR A 208     6199   8047   4969      1  -1267    974       C  
ATOM   1345  CD2 TYR A 208      -4.983  -9.592 -12.380  1.00 47.12           C  
ANISOU 1345  CD2 TYR A 208     5708   7497   4700    111  -1057    928       C  
ATOM   1346  CE1 TYR A 208      -5.159 -10.719 -14.901  1.00 50.67           C  
ANISOU 1346  CE1 TYR A 208     6414   7906   4932   -148  -1170    962       C  
ATOM   1347  CE2 TYR A 208      -4.060 -10.546 -12.778  1.00 47.31           C  
ANISOU 1347  CE2 TYR A 208     5909   7379   4688    -27   -971    927       C  
ATOM   1348  CZ  TYR A 208      -4.163 -11.105 -14.048  1.00 56.27           C  
ANISOU 1348  CZ  TYR A 208     7176   8493   5710   -141  -1022    936       C  
ATOM   1349  OH  TYR A 208      -3.268 -12.053 -14.476  1.00 58.37           O  
ANISOU 1349  OH  TYR A 208     7638   8625   5916   -223   -936    908       O  
ATOM   1350  N   ALA A 209      -8.776  -5.408 -13.361  1.00 49.04           N  
ANISOU 1350  N   ALA A 209     5538   8211   4886   1048  -1697    925       N  
ATOM   1351  CA  ALA A 209      -9.948  -4.708 -13.845  1.00 51.61           C  
ANISOU 1351  CA  ALA A 209     5719   8731   5159   1309  -1906    920       C  
ATOM   1352  C   ALA A 209      -9.633  -4.170 -15.233  1.00 55.52           C  
ANISOU 1352  C   ALA A 209     6516   8996   5584   1308  -2075   1020       C  
ATOM   1353  O   ALA A 209     -10.365  -4.415 -16.185  1.00 56.49           O  
ANISOU 1353  O   ALA A 209     6559   9283   5620   1266  -2223   1062       O  
ATOM   1354  CB  ALA A 209     -10.303  -3.575 -12.916  1.00 53.87           C  
ANISOU 1354  CB  ALA A 209     5952   9030   5487   1712  -1948    836       C  
ATOM   1355  N   ARG A 210      -8.516  -3.460 -15.343  1.00 50.49           N  
ANISOU 1355  N   ARG A 210     6227   7993   4963   1313  -2054   1069       N  
ATOM   1356  CA  ARG A 210      -8.124  -2.838 -16.606  1.00 50.67           C  
ANISOU 1356  CA  ARG A 210     6577   7785   4890   1282  -2204   1184       C  
ATOM   1357  C   ARG A 210      -7.722  -3.863 -17.671  1.00 52.61           C  
ANISOU 1357  C   ARG A 210     6891   8057   5043    941  -2138   1244       C  
ATOM   1358  O   ARG A 210      -7.930  -3.630 -18.861  1.00 53.59           O  
ANISOU 1358  O   ARG A 210     7172   8146   5043    912  -2294   1326       O  
ATOM   1359  CB  ARG A 210      -6.995  -1.824 -16.368  1.00 49.71           C  
ANISOU 1359  CB  ARG A 210     6805   7295   4787   1305  -2189   1234       C  
ATOM   1360  CG  ARG A 210      -6.599  -0.967 -17.584  1.00 60.17           C  
ANISOU 1360  CG  ARG A 210     8515   8362   5983   1263  -2362   1376       C  
ATOM   1361  CD  ARG A 210      -7.746  -0.109 -18.153  1.00 71.96           C  
ANISOU 1361  CD  ARG A 210    10072   9866   7405   1590  -2669   1403       C  
ATOM   1362  NE  ARG A 210      -8.264   0.872 -17.198  1.00 81.83           N  
ANISOU 1362  NE  ARG A 210    11330  11040   8721   1993  -2788   1317       N  
ATOM   1363  CZ  ARG A 210      -9.187   1.792 -17.482  1.00102.04           C  
ANISOU 1363  CZ  ARG A 210    13978  13568  11226   2383  -3070   1316       C  
ATOM   1364  NH1 ARG A 210      -9.711   1.880 -18.702  1.00 93.19           N  
ANISOU 1364  NH1 ARG A 210    12937  12486   9985   2401  -3280   1417       N  
ATOM   1365  NH2 ARG A 210      -9.592   2.636 -16.538  1.00 91.86           N  
ANISOU 1365  NH2 ARG A 210    12713  12205   9985   2786  -3154   1206       N  
ATOM   1366  N   ILE A 211      -7.157  -4.993 -17.263  1.00 46.36           N  
ANISOU 1366  N   ILE A 211     6014   7312   4290    704  -1922   1198       N  
ATOM   1367  CA  ILE A 211      -6.820  -6.024 -18.235  1.00 45.56           C  
ANISOU 1367  CA  ILE A 211     6005   7225   4082    429  -1863   1222       C  
ATOM   1368  C   ILE A 211      -8.084  -6.485 -18.934  1.00 52.23           C  
ANISOU 1368  C   ILE A 211     6700   8311   4835    395  -2037   1220       C  
ATOM   1369  O   ILE A 211      -8.107  -6.630 -20.154  1.00 52.90           O  
ANISOU 1369  O   ILE A 211     6953   8370   4775    282  -2134   1275       O  
ATOM   1370  CB  ILE A 211      -6.093  -7.215 -17.596  1.00 46.26           C  
ANISOU 1370  CB  ILE A 211     6048   7308   4221    238  -1633   1156       C  
ATOM   1371  CG1 ILE A 211      -4.691  -6.778 -17.147  1.00 45.15           C  
ANISOU 1371  CG1 ILE A 211     6058   6956   4140    240  -1478   1174       C  
ATOM   1372  CG2 ILE A 211      -5.997  -8.380 -18.577  1.00 46.49           C  
ANISOU 1372  CG2 ILE A 211     6185   7363   4117      5  -1606   1145       C  
ATOM   1373  CD1 ILE A 211      -3.788  -7.917 -16.701  1.00 50.13           C  
ANISOU 1373  CD1 ILE A 211     6686   7564   4798     95  -1271   1118       C  
ATOM   1374  N   TYR A 212      -9.142  -6.688 -18.155  1.00 50.18           N  
ANISOU 1374  N   TYR A 212     6112   8316   4639    483  -2080   1161       N  
ATOM   1375  CA  TYR A 212     -10.429  -7.113 -18.692  1.00 52.53           C  
ANISOU 1375  CA  TYR A 212     6186   8923   4850    430  -2258   1163       C  
ATOM   1376  C   TYR A 212     -10.949  -6.046 -19.642  1.00 59.09           C  
ANISOU 1376  C   TYR A 212     7103   9749   5601    657  -2517   1235       C  
ATOM   1377  O   TYR A 212     -11.280  -6.344 -20.786  1.00 59.86           O  
ANISOU 1377  O   TYR A 212     7287   9898   5558    521  -2664   1286       O  
ATOM   1378  CB  TYR A 212     -11.420  -7.381 -17.549  1.00 54.62           C  
ANISOU 1378  CB  TYR A 212     6030   9534   5188    491  -2232   1093       C  
ATOM   1379  CG  TYR A 212     -12.790  -7.861 -17.980  1.00 59.61           C  
ANISOU 1379  CG  TYR A 212     6347  10577   5727    391  -2410   1099       C  
ATOM   1380  CD1 TYR A 212     -12.957  -9.110 -18.584  1.00 62.18           C  
ANISOU 1380  CD1 TYR A 212     6713  10971   5943    -13  -2428   1115       C  
ATOM   1381  CD2 TYR A 212     -13.929  -7.074 -17.767  1.00 63.18           C  
ANISOU 1381  CD2 TYR A 212     6457  11365   6184    705  -2574   1083       C  
ATOM   1382  CE1 TYR A 212     -14.224  -9.559 -18.982  1.00 66.37           C  
ANISOU 1382  CE1 TYR A 212     6944  11903   6370   -166  -2614   1132       C  
ATOM   1383  CE2 TYR A 212     -15.195  -7.514 -18.157  1.00 67.26           C  
ANISOU 1383  CE2 TYR A 212     6618  12332   6605    599  -2746   1095       C  
ATOM   1384  CZ  TYR A 212     -15.335  -8.757 -18.762  1.00 75.47           C  
ANISOU 1384  CZ  TYR A 212     7697  13442   7537    130  -2769   1128       C  
ATOM   1385  OH  TYR A 212     -16.578  -9.194 -19.152  1.00 80.19           O  
ANISOU 1385  OH  TYR A 212     7942  14502   8026    -33  -2961   1151       O  
ATOM   1386  N   VAL A 213     -10.980  -4.798 -19.182  1.00 56.83           N  
ANISOU 1386  N   VAL A 213     6844   9365   5383   1006  -2588   1238       N  
ATOM   1387  CA  VAL A 213     -11.530  -3.697 -19.984  1.00 59.51           C  
ANISOU 1387  CA  VAL A 213     7304   9665   5643   1285  -2872   1309       C  
ATOM   1388  C   VAL A 213     -10.906  -3.651 -21.375  1.00 63.55           C  
ANISOU 1388  C   VAL A 213     8203   9942   6000   1085  -2952   1426       C  
ATOM   1389  O   VAL A 213     -11.611  -3.423 -22.354  1.00 65.35           O  
ANISOU 1389  O   VAL A 213     8463  10264   6102   1144  -3200   1490       O  
ATOM   1390  CB  VAL A 213     -11.340  -2.315 -19.304  1.00 63.95           C  
ANISOU 1390  CB  VAL A 213     8010  10005   6283   1675  -2933   1296       C  
ATOM   1391  CG1 VAL A 213     -11.784  -1.204 -20.230  1.00 66.86           C  
ANISOU 1391  CG1 VAL A 213     8615  10246   6544   1952  -3253   1387       C  
ATOM   1392  CG2 VAL A 213     -12.112  -2.241 -17.995  1.00 64.50           C  
ANISOU 1392  CG2 VAL A 213     7689  10355   6462   1945  -2876   1164       C  
ATOM   1393  N   VAL A 214      -9.596  -3.890 -21.450  1.00 58.09           N  
ANISOU 1393  N   VAL A 214     7782   8986   5302    852  -2741   1451       N  
ATOM   1394  CA  VAL A 214      -8.853  -3.814 -22.710  1.00 58.29           C  
ANISOU 1394  CA  VAL A 214     8177   8816   5155    652  -2762   1557       C  
ATOM   1395  C   VAL A 214      -9.127  -5.012 -23.624  1.00 63.33           C  
ANISOU 1395  C   VAL A 214     8789   9624   5651    377  -2762   1540       C  
ATOM   1396  O   VAL A 214      -9.455  -4.835 -24.799  1.00 65.18           O  
ANISOU 1396  O   VAL A 214     9194   9866   5706    333  -2953   1619       O  
ATOM   1397  CB  VAL A 214      -7.334  -3.708 -22.463  1.00 59.68           C  
ANISOU 1397  CB  VAL A 214     8587   8737   5353    493  -2515   1580       C  
ATOM   1398  CG1 VAL A 214      -6.578  -3.697 -23.781  1.00 60.13           C  
ANISOU 1398  CG1 VAL A 214     8978   8674   5195    265  -2502   1685       C  
ATOM   1399  CG2 VAL A 214      -7.016  -2.466 -21.650  1.00 59.64           C  
ANISOU 1399  CG2 VAL A 214     8686   8521   5455    711  -2552   1608       C  
ATOM   1400  N   LEU A 215      -8.992  -6.220 -23.086  1.00 58.77           N  
ANISOU 1400  N   LEU A 215     8042   9155   5134    188  -2568   1437       N  
ATOM   1401  CA  LEU A 215      -9.248  -7.448 -23.850  1.00 59.65           C  
ANISOU 1401  CA  LEU A 215     8180   9384   5102    -87  -2576   1399       C  
ATOM   1402  C   LEU A 215     -10.717  -7.604 -24.247  1.00 68.73           C  
ANISOU 1402  C   LEU A 215     9100  10828   6185    -82  -2852   1408       C  
ATOM   1403  O   LEU A 215     -11.023  -8.210 -25.266  1.00 69.73           O  
ANISOU 1403  O   LEU A 215     9346  11019   6131   -286  -2969   1419       O  
ATOM   1404  CB  LEU A 215      -8.797  -8.675 -23.060  1.00 57.45           C  
ANISOU 1404  CB  LEU A 215     7819   9106   4902   -269  -2337   1291       C  
ATOM   1405  CG  LEU A 215      -7.296  -8.965 -23.103  1.00 59.74           C  
ANISOU 1405  CG  LEU A 215     8364   9161   5174   -346  -2079   1267       C  
ATOM   1406  CD1 LEU A 215      -6.748  -9.161 -21.711  1.00 57.37           C  
ANISOU 1406  CD1 LEU A 215     7916   8813   5070   -287  -1877   1207       C  
ATOM   1407  CD2 LEU A 215      -7.008 -10.178 -23.983  1.00 62.69           C  
ANISOU 1407  CD2 LEU A 215     8953   9505   5359   -578  -2025   1203       C  
ATOM   1408  N   LYS A 216     -11.623  -7.067 -23.440  1.00 68.46           N  
ANISOU 1408  N   LYS A 216     8727  11002   6282    154  -2958   1397       N  
ATOM   1409  CA  LYS A 216     -13.032  -7.031 -23.802  1.00 72.45           C  
ANISOU 1409  CA  LYS A 216     8948  11858   6724    214  -3239   1415       C  
ATOM   1410  C   LYS A 216     -13.272  -6.025 -24.935  1.00 81.41           C  
ANISOU 1410  C   LYS A 216    10297  12913   7720    406  -3517   1525       C  
ATOM   1411  O   LYS A 216     -14.185  -6.209 -25.755  1.00 84.07           O  
ANISOU 1411  O   LYS A 216    10540  13482   7919    350  -3773   1562       O  
ATOM   1412  CB  LYS A 216     -13.891  -6.686 -22.577  1.00 75.65           C  
ANISOU 1412  CB  LYS A 216     8896  12560   7289    467  -3247   1357       C  
ATOM   1413  CG  LYS A 216     -15.408  -6.647 -22.853  1.00 93.53           C  
ANISOU 1413  CG  LYS A 216    10754  15295   9487    558  -3529   1368       C  
ATOM   1414  CD  LYS A 216     -16.231  -6.852 -21.574  1.00103.94           C  
ANISOU 1414  CD  LYS A 216    11545  17024  10922    644  -3446   1285       C  
ATOM   1415  CE  LYS A 216     -17.621  -6.221 -21.676  1.00118.42           C  
ANISOU 1415  CE  LYS A 216    12939  19335  12721    967  -3724   1290       C  
ATOM   1416  NZ  LYS A 216     -17.599  -4.749 -21.416  1.00126.70           N  
ANISOU 1416  NZ  LYS A 216    14060  20238  13842   1557  -3819   1279       N  
ATOM   1417  N   GLN A 217     -12.453  -4.971 -24.973  1.00 78.95           N  
ANISOU 1417  N   GLN A 217    10292  12273   7431    604  -3485   1587       N  
ATOM   1418  CA  GLN A 217     -12.557  -3.930 -26.004  1.00 82.12           C  
ANISOU 1418  CA  GLN A 217    10990  12526   7685    774  -3752   1716       C  
ATOM   1419  C   GLN A 217     -11.676  -4.258 -27.206  1.00 88.13           C  
ANISOU 1419  C   GLN A 217    12177  13076   8232    459  -3694   1791       C  
ATOM   1420  O   GLN A 217     -10.620  -3.655 -27.419  1.00 87.27           O  
ANISOU 1420  O   GLN A 217    12417  12664   8077    431  -3586   1865       O  
ATOM   1421  CB  GLN A 217     -12.236  -2.550 -25.418  1.00 83.59           C  
ANISOU 1421  CB  GLN A 217    11329  12456   7974   1134  -3794   1758       C  
ATOM   1422  CG  GLN A 217     -13.377  -2.025 -24.548  1.00101.74           C  
ANISOU 1422  CG  GLN A 217    13241  15007  10407   1555  -3951   1684       C  
ATOM   1423  CD  GLN A 217     -13.073  -0.715 -23.842  1.00121.61           C  
ANISOU 1423  CD  GLN A 217    15948  17238  13020   1939  -3991   1688       C  
ATOM   1424  OE1 GLN A 217     -11.916  -0.398 -23.544  1.00114.92           O  
ANISOU 1424  OE1 GLN A 217    15414  16042  12210   1821  -3808   1715       O  
ATOM   1425  NE2 GLN A 217     -14.125   0.053 -23.556  1.00116.81           N  
ANISOU 1425  NE2 GLN A 217    15149  16791  12441   2412  -4241   1653       N  
ATOM   1426  N   ARG A 218     -12.143  -5.227 -27.988  1.00 87.16           N  
ANISOU 1426  N   ARG A 218    12016  13144   7957    207  -3771   1769       N  
ATOM   1427  CA  ARG A 218     -11.438  -5.702 -29.175  1.00 87.92           C  
ANISOU 1427  CA  ARG A 218    12497  13100   7808    -87  -3716   1807       C  
ATOM   1428  C   ARG A 218     -11.741  -4.796 -30.367  1.00 96.45           C  
ANISOU 1428  C   ARG A 218    13864  14114   8669      3  -4023   1961       C  
ATOM   1429  O   ARG A 218     -12.511  -5.152 -31.271  1.00 99.20           O  
ANISOU 1429  O   ARG A 218    14221  14637   8834    -97  -4266   1985       O  
ATOM   1430  CB  ARG A 218     -11.802  -7.174 -29.479  1.00 89.43           C  
ANISOU 1430  CB  ARG A 218    12594  13482   7904   -404  -3683   1699       C  
ATOM   1431  CG  ARG A 218     -10.981  -8.188 -28.668  1.00 97.71           C  
ANISOU 1431  CG  ARG A 218    13611  14447   9069   -574  -3332   1567       C  
ATOM   1432  CD  ARG A 218     -11.747  -9.471 -28.306  1.00109.84           C  
ANISOU 1432  CD  ARG A 218    14908  16200  10626   -800  -3356   1459       C  
ATOM   1433  NE  ARG A 218     -11.128 -10.125 -27.144  1.00117.44           N  
ANISOU 1433  NE  ARG A 218    15773  17080  11770   -846  -3064   1359       N  
ATOM   1434  CZ  ARG A 218     -11.664 -11.124 -26.432  1.00133.04           C  
ANISOU 1434  CZ  ARG A 218    17532  19201  13816  -1027  -3037   1280       C  
ATOM   1435  NH1 ARG A 218     -12.859 -11.634 -26.747  1.00123.20           N  
ANISOU 1435  NH1 ARG A 218    16105  18230  12476  -1220  -3280   1284       N  
ATOM   1436  NH2 ARG A 218     -10.990 -11.620 -25.389  1.00117.52           N  
ANISOU 1436  NH2 ARG A 218    15536  17116  12000  -1041  -2779   1207       N  
ATOM   1437  N   ARG A 219     -11.139  -3.612 -30.350  1.00 93.60           N  
ANISOU 1437  N   ARG A 219    13763  13487   8312    173  -4034   2074       N  
ATOM   1438  CA  ARG A 219     -11.217  -2.705 -31.496  1.00 96.87           C  
ANISOU 1438  CA  ARG A 219    14559  13761   8486    219  -4308   2249       C  
ATOM   1439  C   ARG A 219     -10.225  -3.176 -32.546  1.00 99.74           C  
ANISOU 1439  C   ARG A 219    15300  14020   8577   -145  -4129   2290       C  
ATOM   1440  O   ARG A 219      -9.052  -3.421 -32.236  1.00 97.33           O  
ANISOU 1440  O   ARG A 219    15086  13595   8300   -308  -3785   2251       O  
ATOM   1441  CB  ARG A 219     -10.944  -1.245 -31.104  1.00 99.64           C  
ANISOU 1441  CB  ARG A 219    15124  13824   8911    501  -4415   2368       C  
ATOM   1442  CG  ARG A 219      -9.702  -1.016 -30.239  1.00109.54           C  
ANISOU 1442  CG  ARG A 219    16463  14850  10308    421  -4076   2345       C  
ATOM   1443  CD  ARG A 219      -9.772   0.330 -29.526  1.00124.44           C  
ANISOU 1443  CD  ARG A 219    18468  16488  12325    756  -4232   2410       C  
ATOM   1444  NE  ARG A 219      -9.388   0.224 -28.117  1.00133.15           N  
ANISOU 1444  NE  ARG A 219    19315  17575  13700    842  -3981   2279       N  
ATOM   1445  CZ  ARG A 219      -9.199   1.266 -27.303  1.00150.88           C  
ANISOU 1445  CZ  ARG A 219    21682  19575  16069   1082  -4035   2297       C  
ATOM   1446  NH1 ARG A 219      -9.357   2.520 -27.742  1.00143.28           N  
ANISOU 1446  NH1 ARG A 219    21124  18326  14989   1273  -4342   2444       N  
ATOM   1447  NH2 ARG A 219      -8.848   1.054 -26.039  1.00135.79           N  
ANISOU 1447  NH2 ARG A 219    19531  17681  14382   1129  -3798   2167       N  
ATOM   1448  N   ARG A 220     -10.712  -3.329 -33.776  1.00 97.72           N  
ANISOU 1448  N   ARG A 220    15238  13849   8044   -260  -4364   2359       N  
ATOM   1449  CA  ARG A 220      -9.871  -3.677 -34.920  1.00 97.48           C  
ANISOU 1449  CA  ARG A 220    15603  13747   7687   -577  -4228   2404       C  
ATOM   1450  C   ARG A 220      -8.803  -2.593 -35.100  1.00 99.40           C  
ANISOU 1450  C   ARG A 220    16213  13720   7834   -612  -4122   2569       C  
ATOM   1451  O   ARG A 220      -8.888  -1.505 -34.506  1.00 99.28           O  
ANISOU 1451  O   ARG A 220    16222  13529   7973   -383  -4250   2667       O  
ATOM   1452  CB  ARG A 220     -10.735  -3.801 -36.186  1.00101.62           C  
ANISOU 1452  CB  ARG A 220    16297  14399   7916   -652  -4577   2474       C  
ATOM   1453  CG  ARG A 220     -10.088  -4.526 -37.368  1.00112.34           C  
ANISOU 1453  CG  ARG A 220    18004  15771   8908   -994  -4432   2453       C  
ATOM   1454  CD  ARG A 220     -10.970  -4.449 -38.617  1.00124.93           C  
ANISOU 1454  CD  ARG A 220    19810  17467  10190  -1053  -4831   2551       C  
ATOM   1455  NE  ARG A 220     -10.987  -3.099 -39.204  1.00135.02           N  
ANISOU 1455  NE  ARG A 220    21421  18571  11309   -934  -5092   2796       N  
ATOM   1456  CZ  ARG A 220     -10.372  -2.724 -40.334  1.00149.50           C  
ANISOU 1456  CZ  ARG A 220    23745  20294  12765  -1141  -5092   2942       C  
ATOM   1457  NH1 ARG A 220      -9.664  -3.585 -41.067  1.00135.59           N  
ANISOU 1457  NH1 ARG A 220    22188  18608  10723  -1453  -4826   2852       N  
ATOM   1458  NH2 ARG A 220     -10.472  -1.462 -40.745  1.00137.54           N  
ANISOU 1458  NH2 ARG A 220    22547  18586  11126  -1027  -5370   3181       N  
ATOM   1459  N   LYS A 221      -7.784  -2.902 -35.891  1.00 94.14           N  
ANISOU 1459  N   LYS A 221    15838  13031   6900   -908  -3883   2593       N  
ATOM   1460  CA  LYS A 221      -6.762  -1.927 -36.214  1.00 93.98           C  
ANISOU 1460  CA  LYS A 221    16172  12815   6720  -1038  -3783   2775       C  
ATOM   1461  C   LYS A 221      -6.871  -1.498 -37.666  1.00100.29           C  
ANISOU 1461  C   LYS A 221    17417  13586   7102  -1203  -4002   2956       C  
ATOM   1462  O   LYS A 221      -7.526  -2.147 -38.476  1.00101.21           O  
ANISOU 1462  O   LYS A 221    17571  13856   7029  -1255  -4154   2906       O  
ATOM   1463  CB  LYS A 221      -5.378  -2.490 -35.910  1.00 93.75           C  
ANISOU 1463  CB  LYS A 221    16090  12839   6691  -1252  -3303   2681       C  
ATOM   1464  CG  LYS A 221      -5.305  -3.138 -34.549  1.00104.23           C  
ANISOU 1464  CG  LYS A 221    16990  14216   8397  -1105  -3096   2486       C  
ATOM   1465  CD  LYS A 221      -3.917  -3.103 -33.969  1.00112.24           C  
ANISOU 1465  CD  LYS A 221    17957  15209   9479  -1228  -2713   2467       C  
ATOM   1466  CE  LYS A 221      -3.902  -3.802 -32.622  1.00121.44           C  
ANISOU 1466  CE  LYS A 221    18720  16418  11003  -1073  -2538   2276       C  
ATOM   1467  NZ  LYS A 221      -2.664  -3.511 -31.839  1.00131.44           N  
ANISOU 1467  NZ  LYS A 221    19906  17643  12391  -1138  -2244   2285       N  
ATOM   1468  N   ASN A1002      -6.223  -0.379 -37.963  1.00 55.76           N  
ANISOU 1468  N   ASN A1002     6705   8108   6374  -1392    912   -144       N  
ATOM   1469  CA  ASN A1002      -6.231   0.244 -39.283  1.00 54.12           C  
ANISOU 1469  CA  ASN A1002     6167   8055   6340  -1109    561    -88       C  
ATOM   1470  C   ASN A1002      -4.834   0.802 -39.591  1.00 52.93           C  
ANISOU 1470  C   ASN A1002     6344   7661   6107   -807    322    125       C  
ATOM   1471  O   ASN A1002      -3.888   0.564 -38.838  1.00 50.76           O  
ANISOU 1471  O   ASN A1002     6481   7130   5676   -822    389    217       O  
ATOM   1472  CB  ASN A1002      -7.305   1.344 -39.336  1.00 57.14           C  
ANISOU 1472  CB  ASN A1002     5984   8707   7019   -883    561   -236       C  
ATOM   1473  CG  ASN A1002      -7.177   2.370 -38.200  1.00 76.10           C  
ANISOU 1473  CG  ASN A1002     8454  10994   9465   -672    783   -269       C  
ATOM   1474  OD1 ASN A1002      -6.200   2.390 -37.441  1.00 63.87           O  
ANISOU 1474  OD1 ASN A1002     7387   9178   7702   -676    865   -151       O  
ATOM   1475  ND2 ASN A1002      -8.179   3.231 -38.088  1.00 72.45           N  
ANISOU 1475  ND2 ASN A1002     7501  10730   9297   -480    866   -445       N  
ATOM   1476  N   ILE A1003      -4.701   1.535 -40.693  1.00 47.75           N  
ANISOU 1476  N   ILE A1003     5519   7077   5547   -557     34    192       N  
ATOM   1477  CA  ILE A1003      -3.408   2.084 -41.101  1.00 43.87           C  
ANISOU 1477  CA  ILE A1003     5313   6373   4981   -336   -143    349       C  
ATOM   1478  C   ILE A1003      -2.843   3.061 -40.073  1.00 46.74           C  
ANISOU 1478  C   ILE A1003     5826   6589   5343   -127    -46    386       C  
ATOM   1479  O   ILE A1003      -1.623   3.203 -39.934  1.00 43.87           O  
ANISOU 1479  O   ILE A1003     5758   6019   4891    -55   -103    482       O  
ATOM   1480  CB  ILE A1003      -3.507   2.789 -42.478  1.00 46.56           C  
ANISOU 1480  CB  ILE A1003     5515   6802   5374   -158   -444    402       C  
ATOM   1481  CG1 ILE A1003      -2.122   3.214 -42.978  1.00 43.71           C  
ANISOU 1481  CG1 ILE A1003     5489   6213   4908    -37   -548    522       C  
ATOM   1482  CG2 ILE A1003      -4.445   3.992 -42.391  1.00 49.31           C  
ANISOU 1482  CG2 ILE A1003     5525   7300   5910    115   -521    356       C  
ATOM   1483  CD1 ILE A1003      -1.032   2.180 -42.776  1.00 44.82           C  
ANISOU 1483  CD1 ILE A1003     5922   6158   4952   -205   -443    540       C  
ATOM   1484  N   PHE A1004      -3.736   3.720 -39.349  1.00 45.64           N  
ANISOU 1484  N   PHE A1004     5464   6561   5317    -49    116    281       N  
ATOM   1485  CA  PHE A1004      -3.331   4.789 -38.453  1.00 44.91           C  
ANISOU 1485  CA  PHE A1004     5518   6331   5215    143    220    293       C  
ATOM   1486  C   PHE A1004      -2.720   4.207 -37.189  1.00 47.24           C  
ANISOU 1486  C   PHE A1004     6193   6445   5311    -66    411    307       C  
ATOM   1487  O   PHE A1004      -1.598   4.553 -36.823  1.00 44.74           O  
ANISOU 1487  O   PHE A1004     6183   5934   4883     12    326    407       O  
ATOM   1488  CB  PHE A1004      -4.520   5.721 -38.161  1.00 50.00           C  
ANISOU 1488  CB  PHE A1004     5794   7126   6079    324    355    144       C  
ATOM   1489  CG  PHE A1004      -5.164   6.280 -39.416  1.00 53.30           C  
ANISOU 1489  CG  PHE A1004     5854   7700   6699    571     64    152       C  
ATOM   1490  CD1 PHE A1004      -4.501   7.236 -40.189  1.00 55.19           C  
ANISOU 1490  CD1 PHE A1004     6263   7800   6908    843   -205    297       C  
ATOM   1491  CD2 PHE A1004      -6.411   5.831 -39.841  1.00 58.85           C  
ANISOU 1491  CD2 PHE A1004     6086   8676   7598    499     33     13       C  
ATOM   1492  CE1 PHE A1004      -5.076   7.748 -41.355  1.00 58.09           C  
ANISOU 1492  CE1 PHE A1004     6413   8259   7399   1061   -530    336       C  
ATOM   1493  CE2 PHE A1004      -6.990   6.336 -41.005  1.00 63.81           C  
ANISOU 1493  CE2 PHE A1004     6414   9437   8394    736   -331     40       C  
ATOM   1494  CZ  PHE A1004      -6.315   7.299 -41.763  1.00 60.64           C  
ANISOU 1494  CZ  PHE A1004     6266   8853   7920   1028   -630    220       C  
ATOM   1495  N   GLU A1005      -3.445   3.297 -36.549  1.00 45.46           N  
ANISOU 1495  N   GLU A1005     5971   6276   5026   -359    647    203       N  
ATOM   1496  CA  GLU A1005      -2.932   2.610 -35.370  1.00 45.14           C  
ANISOU 1496  CA  GLU A1005     6396   6022   4734   -599    789    239       C  
ATOM   1497  C   GLU A1005      -1.720   1.739 -35.692  1.00 45.67           C  
ANISOU 1497  C   GLU A1005     6789   5885   4678   -624    531    405       C  
ATOM   1498  O   GLU A1005      -0.845   1.557 -34.852  1.00 44.68           O  
ANISOU 1498  O   GLU A1005     7067   5529   4382   -654    467    497       O  
ATOM   1499  CB  GLU A1005      -4.024   1.760 -34.730  1.00 49.99           C  
ANISOU 1499  CB  GLU A1005     7000   6717   5276   -969   1128     79       C  
ATOM   1500  CG  GLU A1005      -5.098   2.572 -34.013  1.00 66.23           C  
ANISOU 1500  CG  GLU A1005     8798   8917   7450   -988   1489   -140       C  
ATOM   1501  CD  GLU A1005      -4.709   2.959 -32.578  1.00 92.21           C  
ANISOU 1501  CD  GLU A1005    12568  11979  10490  -1097   1715   -147       C  
ATOM   1502  OE1 GLU A1005      -5.594   2.906 -31.686  1.00 86.74           O  
ANISOU 1502  OE1 GLU A1005    11893  11322   9742  -1369   2151   -357       O  
ATOM   1503  OE2 GLU A1005      -3.526   3.312 -32.345  1.00 85.38           O  
ANISOU 1503  OE2 GLU A1005    12062  10903   9476   -945   1468     34       O  
ATOM   1504  N   MET A1006      -1.667   1.207 -36.907  1.00 40.87           N  
ANISOU 1504  N   MET A1006     6008   5352   4168   -606    371    430       N  
ATOM   1505  CA  MET A1006      -0.503   0.445 -37.350  1.00 38.35           C  
ANISOU 1505  CA  MET A1006     5933   4833   3805   -583    163    543       C  
ATOM   1506  C   MET A1006       0.751   1.301 -37.267  1.00 39.55           C  
ANISOU 1506  C   MET A1006     6180   4856   3993   -328    -22    627       C  
ATOM   1507  O   MET A1006       1.686   0.971 -36.553  1.00 39.08           O  
ANISOU 1507  O   MET A1006     6415   4582   3852   -318   -126    698       O  
ATOM   1508  CB  MET A1006      -0.684  -0.049 -38.791  1.00 39.83           C  
ANISOU 1508  CB  MET A1006     5912   5131   4090   -612     67    521       C  
ATOM   1509  CG  MET A1006       0.379  -1.037 -39.248  1.00 42.15           C  
ANISOU 1509  CG  MET A1006     6451   5199   4366   -629    -54    580       C  
ATOM   1510  SD  MET A1006       0.436  -1.242 -41.035  1.00 45.28           S  
ANISOU 1510  SD  MET A1006     6665   5691   4847   -639   -150    539       S  
ATOM   1511  CE  MET A1006       1.261  -2.826 -41.158  1.00 42.49           C  
ANISOU 1511  CE  MET A1006     6646   5033   4466   -759   -136    541       C  
ATOM   1512  N   LEU A1007       0.764   2.409 -37.993  1.00 34.34           N  
ANISOU 1512  N   LEU A1007     5283   4315   3448   -135    -83    614       N  
ATOM   1513  CA  LEU A1007       1.969   3.230 -38.069  1.00 32.33           C  
ANISOU 1513  CA  LEU A1007     5110   3948   3226     47   -224    662       C  
ATOM   1514  C   LEU A1007       2.326   3.880 -36.724  1.00 37.55           C  
ANISOU 1514  C   LEU A1007     5980   4504   3785     72   -192    679       C  
ATOM   1515  O   LEU A1007       3.509   4.040 -36.416  1.00 37.01           O  
ANISOU 1515  O   LEU A1007     6059   4298   3707    128   -344    717       O  
ATOM   1516  CB  LEU A1007       1.868   4.259 -39.206  1.00 31.35           C  
ANISOU 1516  CB  LEU A1007     4792   3929   3192    199   -281    650       C  
ATOM   1517  CG  LEU A1007       2.239   3.687 -40.586  1.00 34.52           C  
ANISOU 1517  CG  LEU A1007     5145   4334   3636    151   -376    647       C  
ATOM   1518  CD1 LEU A1007       1.755   4.588 -41.708  1.00 34.75           C  
ANISOU 1518  CD1 LEU A1007     5060   4468   3676    241   -448    652       C  
ATOM   1519  CD2 LEU A1007       3.765   3.413 -40.703  1.00 34.52           C  
ANISOU 1519  CD2 LEU A1007     5278   4156   3683    164   -438    639       C  
ATOM   1520  N   ARG A1008       1.321   4.214 -35.912  1.00 35.65           N  
ANISOU 1520  N   ARG A1008     5746   4328   3471      5     13    625       N  
ATOM   1521  CA  ARG A1008       1.583   4.684 -34.546  1.00 36.42           C  
ANISOU 1521  CA  ARG A1008     6135   4299   3403    -49     84    625       C  
ATOM   1522  C   ARG A1008       2.530   3.698 -33.866  1.00 39.68           C  
ANISOU 1522  C   ARG A1008     6898   4508   3670   -168   -103    720       C  
ATOM   1523  O   ARG A1008       3.568   4.090 -33.337  1.00 39.64           O  
ANISOU 1523  O   ARG A1008     7081   4376   3606   -115   -292    769       O  
ATOM   1524  CB  ARG A1008       0.282   4.843 -33.731  1.00 39.87           C  
ANISOU 1524  CB  ARG A1008     6566   4814   3771   -188    420    509       C  
ATOM   1525  CG  ARG A1008       0.458   4.998 -32.186  1.00 53.97           C  
ANISOU 1525  CG  ARG A1008     8792   6427   5287   -370    552    496       C  
ATOM   1526  CD  ARG A1008       1.461   6.120 -31.776  1.00 65.10           C  
ANISOU 1526  CD  ARG A1008    10386   7718   6631   -239    408    538       C  
ATOM   1527  NE  ARG A1008       1.323   6.561 -30.365  1.00 78.77           N  
ANISOU 1527  NE  ARG A1008    12514   9317   8096   -426    606    480       N  
ATOM   1528  CZ  ARG A1008       2.172   6.307 -29.352  1.00 92.72           C  
ANISOU 1528  CZ  ARG A1008    14764  10887   9577   -596    423    567       C  
ATOM   1529  NH1 ARG A1008       3.289   5.589 -29.508  1.00 78.90           N  
ANISOU 1529  NH1 ARG A1008    13124   9040   7816   -560      7    714       N  
ATOM   1530  NH2 ARG A1008       1.898   6.791 -28.145  1.00 79.29           N  
ANISOU 1530  NH2 ARG A1008    13451   9072   7602   -803    651    492       N  
ATOM   1531  N   ILE A1009       2.180   2.420 -33.904  1.00 35.89           N  
ANISOU 1531  N   ILE A1009     6510   3985   3140   -324    -82    740       N  
ATOM   1532  CA  ILE A1009       2.992   1.395 -33.259  1.00 36.64           C  
ANISOU 1532  CA  ILE A1009     6993   3830   3100   -402   -295    845       C  
ATOM   1533  C   ILE A1009       4.409   1.395 -33.805  1.00 39.94           C  
ANISOU 1533  C   ILE A1009     7317   4158   3701   -176   -626    897       C  
ATOM   1534  O   ILE A1009       5.379   1.502 -33.043  1.00 40.87           O  
ANISOU 1534  O   ILE A1009     7652   4119   3759   -122   -879    959       O  
ATOM   1535  CB  ILE A1009       2.389  -0.007 -33.464  1.00 40.62           C  
ANISOU 1535  CB  ILE A1009     7618   4271   3545   -595   -204    851       C  
ATOM   1536  CG1 ILE A1009       1.156  -0.175 -32.581  1.00 43.20           C  
ANISOU 1536  CG1 ILE A1009     8143   4630   3642   -908    137    778       C  
ATOM   1537  CG2 ILE A1009       3.409  -1.062 -33.146  1.00 42.14           C  
ANISOU 1537  CG2 ILE A1009     8169   4160   3683   -559   -506    974       C  
ATOM   1538  CD1 ILE A1009       0.370  -1.396 -32.881  1.00 50.69           C  
ANISOU 1538  CD1 ILE A1009     9153   5570   4537  -1163    306    736       C  
ATOM   1539  N   ASP A1010       4.498   1.288 -35.133  1.00 34.98           N  
ANISOU 1539  N   ASP A1010     6357   3638   3295    -71   -615    848       N  
ATOM   1540  CA  ASP A1010       5.763   1.113 -35.851  1.00 33.84           C  
ANISOU 1540  CA  ASP A1010     6071   3415   3370    100   -829    836       C  
ATOM   1541  C   ASP A1010       6.645   2.359 -35.780  1.00 37.49           C  
ANISOU 1541  C   ASP A1010     6408   3924   3912    220   -929    798       C  
ATOM   1542  O   ASP A1010       7.855   2.255 -35.563  1.00 37.69           O  
ANISOU 1542  O   ASP A1010     6423   3837   4060    318  -1166    788       O  
ATOM   1543  CB  ASP A1010       5.496   0.770 -37.329  1.00 33.94           C  
ANISOU 1543  CB  ASP A1010     5826   3532   3537    104   -710    764       C  
ATOM   1544  CG  ASP A1010       5.056  -0.672 -37.547  1.00 40.08           C  
ANISOU 1544  CG  ASP A1010     6741   4204   4284    -17   -664    777       C  
ATOM   1545  OD1 ASP A1010       5.359  -1.543 -36.722  1.00 42.67           O  
ANISOU 1545  OD1 ASP A1010     7365   4307   4538    -37   -786    846       O  
ATOM   1546  OD2 ASP A1010       4.426  -0.940 -38.578  1.00 42.82           O  
ANISOU 1546  OD2 ASP A1010     6938   4670   4662   -106   -527    721       O  
ATOM   1547  N   GLU A1011       6.036   3.526 -35.979  1.00 33.74           N  
ANISOU 1547  N   GLU A1011     5828   3604   3386    215   -754    762       N  
ATOM   1548  CA  GLU A1011       6.769   4.795 -36.000  1.00 33.62           C  
ANISOU 1548  CA  GLU A1011     5747   3615   3411    285   -794    715       C  
ATOM   1549  C   GLU A1011       6.916   5.389 -34.605  1.00 40.05           C  
ANISOU 1549  C   GLU A1011     6819   4358   4039    228   -854    746       C  
ATOM   1550  O   GLU A1011       8.008   5.796 -34.204  1.00 41.27           O  
ANISOU 1550  O   GLU A1011     7008   4453   4221    240  -1048    724       O  
ATOM   1551  CB  GLU A1011       6.046   5.817 -36.882  1.00 34.00           C  
ANISOU 1551  CB  GLU A1011     5650   3797   3470    328   -601    676       C  
ATOM   1552  CG  GLU A1011       5.881   5.403 -38.340  1.00 42.88           C  
ANISOU 1552  CG  GLU A1011     6589   4990   4713    340   -561    648       C  
ATOM   1553  CD  GLU A1011       7.050   5.830 -39.219  1.00 61.32           C  
ANISOU 1553  CD  GLU A1011     8845   7287   7167    351   -593    567       C  
ATOM   1554  OE1 GLU A1011       7.116   7.032 -39.597  1.00 58.97           O  
ANISOU 1554  OE1 GLU A1011     8581   7003   6823    365   -528    543       O  
ATOM   1555  OE2 GLU A1011       7.889   4.954 -39.540  1.00 50.79           O  
ANISOU 1555  OE2 GLU A1011     7432   5888   5978    335   -656    510       O  
ATOM   1556  N   GLY A1012       5.805   5.464 -33.880  1.00 36.92           N  
ANISOU 1556  N   GLY A1012     6597   3977   3455    135   -668    768       N  
ATOM   1557  CA  GLY A1012       5.794   6.096 -32.567  1.00 37.88           C  
ANISOU 1557  CA  GLY A1012     7029   4018   3347     31   -645    772       C  
ATOM   1558  C   GLY A1012       5.605   7.596 -32.675  1.00 40.54           C  
ANISOU 1558  C   GLY A1012     7309   4411   3682     90   -469    695       C  
ATOM   1559  O   GLY A1012       5.919   8.203 -33.701  1.00 39.03           O  
ANISOU 1559  O   GLY A1012     6892   4282   3655    211   -473    660       O  
ATOM   1560  N   LEU A1013       5.117   8.187 -31.591  1.00 37.57           N  
ANISOU 1560  N   LEU A1013     7206   3976   3095    -19   -298    660       N  
ATOM   1561  CA  LEU A1013       4.700   9.574 -31.579  1.00 37.44           C  
ANISOU 1561  CA  LEU A1013     7190   3965   3072     50    -64    571       C  
ATOM   1562  C   LEU A1013       5.584  10.377 -30.634  1.00 42.45           C  
ANISOU 1562  C   LEU A1013     8153   4470   3506    -77   -158    549       C  
ATOM   1563  O   LEU A1013       5.754   9.995 -29.484  1.00 44.26           O  
ANISOU 1563  O   LEU A1013     8725   4601   3491   -273   -229    574       O  
ATOM   1564  CB  LEU A1013       3.250   9.628 -31.106  1.00 39.03           C  
ANISOU 1564  CB  LEU A1013     7404   4199   3226     18    303    488       C  
ATOM   1565  CG  LEU A1013       2.434  10.923 -31.123  1.00 44.60           C  
ANISOU 1565  CG  LEU A1013     8044   4897   4004    162    610    365       C  
ATOM   1566  CD1 LEU A1013       1.045  10.617 -30.555  1.00 47.16           C  
ANISOU 1566  CD1 LEU A1013     8306   5278   4336     90    979    239       C  
ATOM   1567  CD2 LEU A1013       3.097  12.068 -30.357  1.00 47.52           C  
ANISOU 1567  CD2 LEU A1013     8765   5099   4190     97    647    320       C  
ATOM   1568  N   ARG A1014       6.139  11.488 -31.116  1.00 37.74           N  
ANISOU 1568  N   ARG A1014     7506   3857   2978     -2   -165    500       N  
ATOM   1569  CA  ARG A1014       6.884  12.423 -30.257  1.00 38.45           C  
ANISOU 1569  CA  ARG A1014     7911   3829   2867   -159   -207    446       C  
ATOM   1570  C   ARG A1014       6.442  13.862 -30.496  1.00 41.86           C  
ANISOU 1570  C   ARG A1014     8423   4183   3300    -70     86    352       C  
ATOM   1571  O   ARG A1014       6.085  14.220 -31.610  1.00 39.92           O  
ANISOU 1571  O   ARG A1014     7947   3973   3248    135    169    353       O  
ATOM   1572  CB  ARG A1014       8.389  12.309 -30.503  1.00 37.25           C  
ANISOU 1572  CB  ARG A1014     7660   3701   2791   -230   -575    453       C  
ATOM   1573  CG  ARG A1014       8.978  10.947 -30.151  1.00 41.80           C  
ANISOU 1573  CG  ARG A1014     8194   4297   3393   -271   -933    541       C  
ATOM   1574  CD  ARG A1014      10.453  11.069 -29.804  1.00 44.31           C  
ANISOU 1574  CD  ARG A1014     8496   4607   3734   -382  -1319    504       C  
ATOM   1575  NE  ARG A1014      11.149   9.782 -29.830  1.00 46.19           N  
ANISOU 1575  NE  ARG A1014     8561   4854   4135   -308  -1708    572       N  
ATOM   1576  CZ  ARG A1014      12.420   9.613 -29.463  1.00 61.09           C  
ANISOU 1576  CZ  ARG A1014    10358   6741   6113   -352  -2137    539       C  
ATOM   1577  NH1 ARG A1014      13.144  10.649 -29.035  1.00 49.45           N  
ANISOU 1577  NH1 ARG A1014     8952   5286   4550   -530  -2223    433       N  
ATOM   1578  NH2 ARG A1014      12.973   8.404 -29.518  1.00 48.14           N  
ANISOU 1578  NH2 ARG A1014     8551   5071   4670   -213  -2494    598       N  
ATOM   1579  N   LEU A1015       6.493  14.680 -29.448  1.00 40.42           N  
ANISOU 1579  N   LEU A1015     8621   3861   2876   -230    223    273       N  
ATOM   1580  CA  LEU A1015       6.050  16.073 -29.519  1.00 41.26           C  
ANISOU 1580  CA  LEU A1015     8888   3824   2965   -139    531    170       C  
ATOM   1581  C   LEU A1015       7.175  17.102 -29.711  1.00 46.43           C  
ANISOU 1581  C   LEU A1015     9714   4381   3544   -262    429    122       C  
ATOM   1582  O   LEU A1015       6.946  18.123 -30.345  1.00 47.47           O  
ANISOU 1582  O   LEU A1015     9899   4395   3743   -119    609     79       O  
ATOM   1583  CB  LEU A1015       5.245  16.431 -28.281  1.00 43.82           C  
ANISOU 1583  CB  LEU A1015     9560   4017   3075   -251    867     63       C  
ATOM   1584  CG  LEU A1015       4.092  15.491 -27.940  1.00 48.73           C  
ANISOU 1584  CG  LEU A1015    10055   4723   3738   -221   1064     51       C  
ATOM   1585  CD1 LEU A1015       3.351  16.034 -26.723  1.00 52.62           C  
ANISOU 1585  CD1 LEU A1015    10926   5053   4012   -377   1496   -117       C  
ATOM   1586  CD2 LEU A1015       3.146  15.305 -29.106  1.00 49.75           C  
ANISOU 1586  CD2 LEU A1015     9699   4981   4225    117   1154     63       C  
ATOM   1587  N   LYS A1016       8.366  16.864 -29.163  1.00 42.65           N  
ANISOU 1587  N   LYS A1016     9337   3938   2930   -532    133    120       N  
ATOM   1588  CA  LYS A1016       9.516  17.754 -29.405  1.00 42.85           C  
ANISOU 1588  CA  LYS A1016     9446   3917   2919   -709     30     37       C  
ATOM   1589  C   LYS A1016      10.178  17.324 -30.701  1.00 43.83           C  
ANISOU 1589  C   LYS A1016     9148   4182   3323   -619   -147     64       C  
ATOM   1590  O   LYS A1016       9.929  16.216 -31.158  1.00 41.88           O  
ANISOU 1590  O   LYS A1016     8591   4068   3255   -464   -269    154       O  
ATOM   1591  CB  LYS A1016      10.520  17.693 -28.251  1.00 47.75           C  
ANISOU 1591  CB  LYS A1016    10296   4543   3305  -1053   -253     -8       C  
ATOM   1592  CG  LYS A1016      10.017  18.321 -26.940  1.00 65.81           C  
ANISOU 1592  CG  LYS A1016    13130   6647   5229  -1245    -37    -71       C  
ATOM   1593  CD  LYS A1016      10.759  17.802 -25.686  1.00 79.30           C  
ANISOU 1593  CD  LYS A1016    15102   8376   6653  -1571   -414    -52       C  
ATOM   1594  CE  LYS A1016      10.358  16.346 -25.317  1.00 90.58           C  
ANISOU 1594  CE  LYS A1016    16458   9879   8079  -1490   -621     97       C  
ATOM   1595  NZ  LYS A1016      10.726  15.945 -23.912  1.00101.95           N  
ANISOU 1595  NZ  LYS A1016    18374  11239   9123  -1809   -921    137       N  
ATOM   1596  N   ILE A1017      11.003  18.185 -31.301  1.00 40.06           N  
ANISOU 1596  N   ILE A1017     8694   3659   2866   -753   -118    -35       N  
ATOM   1597  CA  ILE A1017      11.753  17.794 -32.500  1.00 38.42           C  
ANISOU 1597  CA  ILE A1017     8118   3576   2903   -750   -228    -61       C  
ATOM   1598  C   ILE A1017      12.818  16.773 -32.113  1.00 42.65           C  
ANISOU 1598  C   ILE A1017     8333   4296   3577   -877   -603    -95       C  
ATOM   1599  O   ILE A1017      13.406  16.883 -31.039  1.00 44.80           O  
ANISOU 1599  O   ILE A1017     8740   4573   3710  -1082   -809   -144       O  
ATOM   1600  CB  ILE A1017      12.466  18.984 -33.195  1.00 42.65           C  
ANISOU 1600  CB  ILE A1017     8807   4002   3395   -953    -60   -196       C  
ATOM   1601  CG1 ILE A1017      11.460  19.993 -33.740  1.00 42.97           C  
ANISOU 1601  CG1 ILE A1017     9198   3803   3324   -769    254   -142       C  
ATOM   1602  CG2 ILE A1017      13.324  18.491 -34.357  1.00 42.47           C  
ANISOU 1602  CG2 ILE A1017     8407   4116   3616  -1025   -123   -272       C  
ATOM   1603  CD1 ILE A1017      12.085  21.063 -34.618  1.00 48.47           C  
ANISOU 1603  CD1 ILE A1017    10131   4340   3947   -966    428   -243       C  
ATOM   1604  N   TYR A1018      13.063  15.787 -32.977  1.00 36.67           N  
ANISOU 1604  N   TYR A1018     7172   3668   3092   -748   -713    -75       N  
ATOM   1605  CA  TYR A1018      14.136  14.817 -32.746  1.00 37.19           C  
ANISOU 1605  CA  TYR A1018     6880   3876   3374   -803  -1076   -133       C  
ATOM   1606  C   TYR A1018      14.858  14.395 -34.022  1.00 41.08           C  
ANISOU 1606  C   TYR A1018     6943   4469   4196   -787  -1036   -254       C  
ATOM   1607  O   TYR A1018      14.294  14.443 -35.104  1.00 39.79           O  
ANISOU 1607  O   TYR A1018     6779   4274   4066   -689   -777   -224       O  
ATOM   1608  CB  TYR A1018      13.591  13.585 -32.027  1.00 37.49           C  
ANISOU 1608  CB  TYR A1018     6924   3926   3393   -627  -1313     34       C  
ATOM   1609  CG  TYR A1018      12.631  12.739 -32.825  1.00 35.87           C  
ANISOU 1609  CG  TYR A1018     6592   3735   3301   -381  -1166    151       C  
ATOM   1610  CD1 TYR A1018      13.079  11.633 -33.542  1.00 37.16           C  
ANISOU 1610  CD1 TYR A1018     6388   3977   3756   -264  -1305    138       C  
ATOM   1611  CD2 TYR A1018      11.274  13.022 -32.837  1.00 35.35           C  
ANISOU 1611  CD2 TYR A1018     6755   3606   3070   -271   -891    250       C  
ATOM   1612  CE1 TYR A1018      12.203  10.834 -34.269  1.00 35.98           C  
ANISOU 1612  CE1 TYR A1018     6155   3837   3678    -88  -1176    234       C  
ATOM   1613  CE2 TYR A1018      10.383  12.232 -33.563  1.00 34.70           C  
ANISOU 1613  CE2 TYR A1018     6522   3567   3095    -83   -790    338       C  
ATOM   1614  CZ  TYR A1018      10.854  11.135 -34.278  1.00 41.45           C  
ANISOU 1614  CZ  TYR A1018     7065   4496   4187    -14   -936    338       C  
ATOM   1615  OH  TYR A1018       9.971  10.353 -34.995  1.00 41.55           O  
ANISOU 1615  OH  TYR A1018     6966   4547   4273    124   -836    414       O  
ATOM   1616  N   LYS A1019      16.112  13.985 -33.893  1.00 39.00           N  
ANISOU 1616  N   LYS A1019     6315   4320   4182   -893  -1299   -411       N  
ATOM   1617  CA  LYS A1019      16.840  13.434 -35.019  1.00 38.35           C  
ANISOU 1617  CA  LYS A1019     5779   4331   4463   -879  -1229   -574       C  
ATOM   1618  C   LYS A1019      16.415  11.980 -35.172  1.00 40.98           C  
ANISOU 1618  C   LYS A1019     5925   4672   4973   -576  -1389   -437       C  
ATOM   1619  O   LYS A1019      16.314  11.260 -34.185  1.00 41.63           O  
ANISOU 1619  O   LYS A1019     6054   4736   5027   -446  -1735   -307       O  
ATOM   1620  CB  LYS A1019      18.349  13.539 -34.792  1.00 43.78           C  
ANISOU 1620  CB  LYS A1019     6060   5148   5427  -1088  -1439   -844       C  
ATOM   1621  CG  LYS A1019      18.882  14.969 -34.764  1.00 53.49           C  
ANISOU 1621  CG  LYS A1019     7458   6373   6492  -1470  -1232  -1030       C  
ATOM   1622  CD  LYS A1019      20.414  15.008 -34.841  1.00 66.42           C  
ANISOU 1622  CD  LYS A1019     8554   8188   8495  -1718  -1361  -1373       C  
ATOM   1623  CE  LYS A1019      20.922  16.390 -35.266  1.00 78.66           C  
ANISOU 1623  CE  LYS A1019    10268   9719   9901  -2169   -984  -1610       C  
ATOM   1624  NZ  LYS A1019      22.409  16.476 -35.377  1.00 90.47           N  
ANISOU 1624  NZ  LYS A1019    11177  11418  11779  -2475  -1048  -2004       N  
ATOM   1625  N   ASP A1020      16.162  11.548 -36.402  1.00 35.89           N  
ANISOU 1625  N   ASP A1020     5141   4028   4470   -496  -1137   -465       N  
ATOM   1626  CA  ASP A1020      15.731  10.174 -36.658  1.00 34.66           C  
ANISOU 1626  CA  ASP A1020     4846   3857   4465   -245  -1237   -355       C  
ATOM   1627  C   ASP A1020      16.919   9.199 -36.824  1.00 41.13           C  
ANISOU 1627  C   ASP A1020     5171   4725   5730   -164  -1445   -540       C  
ATOM   1628  O   ASP A1020      18.056   9.536 -36.489  1.00 43.45           O  
ANISOU 1628  O   ASP A1020     5186   5095   6230   -280  -1603   -740       O  
ATOM   1629  CB  ASP A1020      14.770  10.134 -37.860  1.00 34.05           C  
ANISOU 1629  CB  ASP A1020     4904   3745   4288   -206   -896   -285       C  
ATOM   1630  CG  ASP A1020      15.463  10.337 -39.200  1.00 45.41           C  
ANISOU 1630  CG  ASP A1020     6153   5202   5898   -369   -606   -511       C  
ATOM   1631  OD1 ASP A1020      16.653  10.738 -39.247  1.00 48.31           O  
ANISOU 1631  OD1 ASP A1020     6276   5621   6459   -554   -575   -756       O  
ATOM   1632  OD2 ASP A1020      14.791  10.095 -40.221  1.00 50.06           O  
ANISOU 1632  OD2 ASP A1020     6853   5754   6413   -346   -395   -458       O  
ATOM   1633  N   THR A1021      16.651   7.992 -37.329  1.00 37.40           N  
ANISOU 1633  N   THR A1021     4578   4203   5431     37  -1448   -494       N  
ATOM   1634  CA  THR A1021      17.687   6.961 -37.473  1.00 40.27           C  
ANISOU 1634  CA  THR A1021     4484   4558   6257    191  -1642   -669       C  
ATOM   1635  C   THR A1021      18.780   7.365 -38.462  1.00 46.32           C  
ANISOU 1635  C   THR A1021     4826   5415   7358     10  -1352  -1032       C  
ATOM   1636  O   THR A1021      19.920   6.945 -38.308  1.00 49.69           O  
ANISOU 1636  O   THR A1021     4772   5884   8223     87  -1548  -1260       O  
ATOM   1637  CB  THR A1021      17.095   5.587 -37.914  1.00 47.69           C  
ANISOU 1637  CB  THR A1021     5459   5378   7284    422  -1627   -557       C  
ATOM   1638  OG1 THR A1021      16.673   5.647 -39.285  1.00 46.19           O  
ANISOU 1638  OG1 THR A1021     5294   5196   7059    306  -1169   -639       O  
ATOM   1639  CG2 THR A1021      15.916   5.170 -37.017  1.00 43.13           C  
ANISOU 1639  CG2 THR A1021     5331   4709   6348    525  -1818   -228       C  
ATOM   1640  N   GLU A1022      18.421   8.164 -39.472  1.00 41.08           N  
ANISOU 1640  N   GLU A1022     4351   4767   6492   -234   -893  -1095       N  
ATOM   1641  CA  GLU A1022      19.376   8.671 -40.466  1.00 43.21           C  
ANISOU 1641  CA  GLU A1022     4344   5096   6980   -511   -517  -1452       C  
ATOM   1642  C   GLU A1022      20.102   9.912 -39.979  1.00 48.98           C  
ANISOU 1642  C   GLU A1022     5028   5922   7659   -797   -522  -1609       C  
ATOM   1643  O   GLU A1022      21.153  10.273 -40.513  1.00 52.10           O  
ANISOU 1643  O   GLU A1022     5081   6396   8318  -1055   -278  -1967       O  
ATOM   1644  CB  GLU A1022      18.684   9.006 -41.787  1.00 42.55           C  
ANISOU 1644  CB  GLU A1022     4607   4938   6623   -697    -44  -1437       C  
ATOM   1645  CG  GLU A1022      17.922   7.842 -42.417  1.00 53.69           C  
ANISOU 1645  CG  GLU A1022     6100   6263   8037   -496      6  -1307       C  
ATOM   1646  CD  GLU A1022      16.403   7.927 -42.194  1.00 74.87           C  
ANISOU 1646  CD  GLU A1022     9258   8898  10290   -373   -102   -931       C  
ATOM   1647  OE1 GLU A1022      15.844   7.022 -41.519  1.00 66.86           O  
ANISOU 1647  OE1 GLU A1022     8251   7860   9293   -118   -377   -738       O  
ATOM   1648  OE2 GLU A1022      15.776   8.901 -42.697  1.00 69.46           O  
ANISOU 1648  OE2 GLU A1022     8942   8187   9262   -536     90   -844       O  
ATOM   1649  N   GLY A1023      19.537  10.566 -38.970  1.00 43.64           N  
ANISOU 1649  N   GLY A1023     4709   5232   6639   -788   -758  -1371       N  
ATOM   1650  CA  GLY A1023      20.132  11.776 -38.396  1.00 45.23           C  
ANISOU 1650  CA  GLY A1023     4961   5499   6727  -1083   -780  -1497       C  
ATOM   1651  C   GLY A1023      19.389  13.040 -38.781  1.00 46.64           C  
ANISOU 1651  C   GLY A1023     5713   5568   6439  -1311   -432  -1395       C  
ATOM   1652  O   GLY A1023      19.880  14.151 -38.536  1.00 47.89           O  
ANISOU 1652  O   GLY A1023     5994   5736   6467  -1621   -333  -1531       O  
ATOM   1653  N   TYR A1024      18.198  12.863 -39.364  1.00 39.53           N  
ANISOU 1653  N   TYR A1024     5171   4552   5296  -1149   -275  -1157       N  
ATOM   1654  CA  TYR A1024      17.401  13.959 -39.904  1.00 37.43           C  
ANISOU 1654  CA  TYR A1024     5449   4142   4631  -1279     17  -1042       C  
ATOM   1655  C   TYR A1024      16.349  14.404 -38.906  1.00 39.29           C  
ANISOU 1655  C   TYR A1024     6066   4302   4560  -1100   -161   -763       C  
ATOM   1656  O   TYR A1024      15.752  13.577 -38.219  1.00 37.26           O  
ANISOU 1656  O   TYR A1024     5749   4079   4329   -833   -413   -584       O  
ATOM   1657  CB  TYR A1024      16.712  13.527 -41.207  1.00 36.42           C  
ANISOU 1657  CB  TYR A1024     5465   3938   4437  -1211    254   -968       C  
ATOM   1658  CG  TYR A1024      17.645  13.309 -42.385  1.00 39.74           C  
ANISOU 1658  CG  TYR A1024     5664   4374   5061  -1476    576  -1271       C  
ATOM   1659  CD1 TYR A1024      18.680  14.203 -42.651  1.00 44.73           C  
ANISOU 1659  CD1 TYR A1024     6275   5005   5714  -1879    842  -1566       C  
ATOM   1660  CD2 TYR A1024      17.476  12.230 -43.252  1.00 39.74           C  
ANISOU 1660  CD2 TYR A1024     5511   4378   5212  -1373    670  -1293       C  
ATOM   1661  CE1 TYR A1024      19.529  14.022 -43.722  1.00 48.01           C  
ANISOU 1661  CE1 TYR A1024     6498   5431   6314  -2176   1217  -1890       C  
ATOM   1662  CE2 TYR A1024      18.325  12.050 -44.335  1.00 42.97           C  
ANISOU 1662  CE2 TYR A1024     5754   4779   5793  -1652   1038  -1609       C  
ATOM   1663  CZ  TYR A1024      19.349  12.960 -44.554  1.00 52.42           C  
ANISOU 1663  CZ  TYR A1024     6914   5983   7021  -2057   1324  -1914       C  
ATOM   1664  OH  TYR A1024      20.212  12.823 -45.602  1.00 56.09           O  
ANISOU 1664  OH  TYR A1024     7217   6440   7656  -2393   1764  -2277       O  
ATOM   1665  N   TYR A1025      16.113  15.715 -38.847  1.00 36.80           N  
ANISOU 1665  N   TYR A1025     6180   3854   3949  -1265     14   -747       N  
ATOM   1666  CA  TYR A1025      15.135  16.280 -37.909  1.00 35.91           C  
ANISOU 1666  CA  TYR A1025     6443   3638   3562  -1111    -73   -537       C  
ATOM   1667  C   TYR A1025      13.694  15.834 -38.204  1.00 36.95           C  
ANISOU 1667  C   TYR A1025     6719   3715   3604   -776    -69   -288       C  
ATOM   1668  O   TYR A1025      13.216  15.912 -39.329  1.00 35.85           O  
ANISOU 1668  O   TYR A1025     6700   3505   3416   -729     88   -240       O  
ATOM   1669  CB  TYR A1025      15.219  17.815 -37.889  1.00 39.03           C  
ANISOU 1669  CB  TYR A1025     7299   3849   3680  -1348    152   -599       C  
ATOM   1670  CG  TYR A1025      16.497  18.360 -37.284  1.00 43.81           C  
ANISOU 1670  CG  TYR A1025     7800   4522   4325  -1716    120   -843       C  
ATOM   1671  CD1 TYR A1025      17.448  19.000 -38.072  1.00 48.49           C  
ANISOU 1671  CD1 TYR A1025     8394   5090   4940  -2097    381  -1093       C  
ATOM   1672  CD2 TYR A1025      16.758  18.224 -35.925  1.00 45.36           C  
ANISOU 1672  CD2 TYR A1025     7912   4807   4517  -1727   -175   -840       C  
ATOM   1673  CE1 TYR A1025      18.619  19.494 -37.519  1.00 52.86           C  
ANISOU 1673  CE1 TYR A1025     8790   5737   5556  -2474    350  -1354       C  
ATOM   1674  CE2 TYR A1025      17.922  18.716 -35.366  1.00 49.57           C  
ANISOU 1674  CE2 TYR A1025     8324   5424   5087  -2082   -266  -1072       C  
ATOM   1675  CZ  TYR A1025      18.846  19.348 -36.165  1.00 60.60           C  
ANISOU 1675  CZ  TYR A1025     9644   6828   6553  -2451     -3  -1338       C  
ATOM   1676  OH  TYR A1025      20.004  19.836 -35.608  1.00 66.85           O  
ANISOU 1676  OH  TYR A1025    10258   7735   7407  -2841    -92  -1603       O  
ATOM   1677  N   THR A1026      13.002  15.402 -37.162  1.00 32.46           N  
ANISOU 1677  N   THR A1026     6163   3177   2994   -580   -246   -145       N  
ATOM   1678  CA  THR A1026      11.702  14.791 -37.293  1.00 30.48           C  
ANISOU 1678  CA  THR A1026     5930   2931   2721   -300   -255     42       C  
ATOM   1679  C   THR A1026      10.837  15.154 -36.090  1.00 35.57           C  
ANISOU 1679  C   THR A1026     6813   3513   3190   -195   -263    140       C  
ATOM   1680  O   THR A1026      11.349  15.564 -35.059  1.00 36.53           O  
ANISOU 1680  O   THR A1026     7065   3606   3208   -342   -330     82       O  
ATOM   1681  CB  THR A1026      11.886  13.278 -37.405  1.00 38.30           C  
ANISOU 1681  CB  THR A1026     6559   4059   3933   -212   -431     59       C  
ATOM   1682  OG1 THR A1026      12.629  12.986 -38.597  1.00 38.91           O  
ANISOU 1682  OG1 THR A1026     6432   4171   4182   -315   -342    -70       O  
ATOM   1683  CG2 THR A1026      10.548  12.548 -37.450  1.00 37.07           C  
ANISOU 1683  CG2 THR A1026     6408   3929   3748     15   -436    229       C  
ATOM   1684  N   ILE A1027       9.523  15.032 -36.232  1.00 32.43           N  
ANISOU 1684  N   ILE A1027     6469   3094   2759     34   -179    263       N  
ATOM   1685  CA  ILE A1027       8.591  15.299 -35.133  1.00 33.32           C  
ANISOU 1685  CA  ILE A1027     6765   3151   2743    130   -102    311       C  
ATOM   1686  C   ILE A1027       7.242  14.629 -35.395  1.00 37.69           C  
ANISOU 1686  C   ILE A1027     7163   3777   3379    361    -51    405       C  
ATOM   1687  O   ILE A1027       6.859  14.413 -36.539  1.00 36.67           O  
ANISOU 1687  O   ILE A1027     6888   3691   3355    481    -63    451       O  
ATOM   1688  CB  ILE A1027       8.398  16.822 -34.925  1.00 37.92           C  
ANISOU 1688  CB  ILE A1027     7712   3530   3167    125     98    261       C  
ATOM   1689  CG1 ILE A1027       7.526  17.101 -33.696  1.00 39.35           C  
ANISOU 1689  CG1 ILE A1027     8087   3636   3228    190    242    254       C  
ATOM   1690  CG2 ILE A1027       7.791  17.457 -36.156  1.00 38.56           C  
ANISOU 1690  CG2 ILE A1027     7863   3503   3285    316    198    310       C  
ATOM   1691  CD1 ILE A1027       7.675  18.480 -33.155  1.00 47.19           C  
ANISOU 1691  CD1 ILE A1027     9485   4406   4040    104    425    166       C  
ATOM   1692  N   GLY A1028       6.519  14.296 -34.338  1.00 35.79           N  
ANISOU 1692  N   GLY A1028     6970   3552   3076    382     14    416       N  
ATOM   1693  CA  GLY A1028       5.271  13.575 -34.501  1.00 36.16           C  
ANISOU 1693  CA  GLY A1028     6818   3700   3221    536     87    461       C  
ATOM   1694  C   GLY A1028       5.538  12.139 -34.912  1.00 40.82           C  
ANISOU 1694  C   GLY A1028     7175   4428   3907    479    -93    519       C  
ATOM   1695  O   GLY A1028       6.550  11.544 -34.523  1.00 40.33           O  
ANISOU 1695  O   GLY A1028     7138   4364   3821    337   -270    523       O  
ATOM   1696  N   ILE A1029       4.631  11.584 -35.710  1.00 38.22           N  
ANISOU 1696  N   ILE A1029     6617   4204   3700    600    -70    554       N  
ATOM   1697  CA  ILE A1029       4.681  10.162 -36.047  1.00 37.29           C  
ANISOU 1697  CA  ILE A1029     6322   4190   3655    533   -188    596       C  
ATOM   1698  C   ILE A1029       5.481   9.994 -37.327  1.00 40.27           C  
ANISOU 1698  C   ILE A1029     6590   4581   4131    530   -312    602       C  
ATOM   1699  O   ILE A1029       4.946   9.987 -38.442  1.00 40.17           O  
ANISOU 1699  O   ILE A1029     6464   4622   4176    604   -309    622       O  
ATOM   1700  CB  ILE A1029       3.274   9.534 -36.140  1.00 41.08           C  
ANISOU 1700  CB  ILE A1029     6621   4793   4194    582    -76    598       C  
ATOM   1701  CG1 ILE A1029       2.531   9.693 -34.802  1.00 43.24           C  
ANISOU 1701  CG1 ILE A1029     7021   5042   4366    522    137    538       C  
ATOM   1702  CG2 ILE A1029       3.378   8.063 -36.504  1.00 41.08           C  
ANISOU 1702  CG2 ILE A1029     6511   4861   4236    473   -180    635       C  
ATOM   1703  CD1 ILE A1029       1.035   9.835 -34.950  1.00 50.98           C  
ANISOU 1703  CD1 ILE A1029     7756   6140   5474    633    339    460       C  
ATOM   1704  N   GLY A1030       6.792   9.914 -37.132  1.00 36.43           N  
ANISOU 1704  N   GLY A1030     6145   4037   3659    425   -421    562       N  
ATOM   1705  CA  GLY A1030       7.751   9.803 -38.216  1.00 35.57           C  
ANISOU 1705  CA  GLY A1030     5929   3925   3663    370   -467    503       C  
ATOM   1706  C   GLY A1030       7.760  10.887 -39.279  1.00 38.73           C  
ANISOU 1706  C   GLY A1030     6426   4276   4015    370   -361    476       C  
ATOM   1707  O   GLY A1030       8.219  10.623 -40.380  1.00 38.25           O  
ANISOU 1707  O   GLY A1030     6306   4217   4011    294   -339    428       O  
ATOM   1708  N   HIS A1031       7.284  12.095 -38.975  1.00 35.77           N  
ANISOU 1708  N   HIS A1031     6251   3820   3520    439   -280    499       N  
ATOM   1709  CA  HIS A1031       7.283  13.178 -39.977  1.00 36.44           C  
ANISOU 1709  CA  HIS A1031     6538   3789   3518    447   -208    498       C  
ATOM   1710  C   HIS A1031       8.653  13.839 -40.116  1.00 39.53           C  
ANISOU 1710  C   HIS A1031     7065   4087   3869    220   -138    375       C  
ATOM   1711  O   HIS A1031       9.056  14.590 -39.243  1.00 39.50           O  
ANISOU 1711  O   HIS A1031     7202   4012   3795    156   -100    326       O  
ATOM   1712  CB  HIS A1031       6.236  14.261 -39.661  1.00 38.71           C  
ANISOU 1712  CB  HIS A1031     7015   3971   3722    651   -151    560       C  
ATOM   1713  CG  HIS A1031       6.238  15.402 -40.638  1.00 43.76           C  
ANISOU 1713  CG  HIS A1031     7963   4422   4242    684   -126    587       C  
ATOM   1714  ND1 HIS A1031       5.595  15.344 -41.859  1.00 46.21           N  
ANISOU 1714  ND1 HIS A1031     8311   4717   4529    788   -235    676       N  
ATOM   1715  CD2 HIS A1031       6.824  16.624 -40.582  1.00 46.99           C  
ANISOU 1715  CD2 HIS A1031     8724   4621   4511    596    -22    542       C  
ATOM   1716  CE1 HIS A1031       5.775  16.483 -42.507  1.00 47.50           C  
ANISOU 1716  CE1 HIS A1031     8874   4645   4529    781   -215    703       C  
ATOM   1717  NE2 HIS A1031       6.519  17.276 -41.756  1.00 48.14           N  
ANISOU 1717  NE2 HIS A1031     9153   4598   4539    660    -61    617       N  
ATOM   1718  N   LEU A1032       9.346  13.584 -41.222  1.00 35.41           N  
ANISOU 1718  N   LEU A1032     6512   3563   3379     62    -90    300       N  
ATOM   1719  CA  LEU A1032      10.617  14.248 -41.483  1.00 36.12           C  
ANISOU 1719  CA  LEU A1032     6704   3574   3446   -208     42    134       C  
ATOM   1720  C   LEU A1032      10.360  15.699 -41.813  1.00 41.26           C  
ANISOU 1720  C   LEU A1032     7804   4014   3859   -241    157    170       C  
ATOM   1721  O   LEU A1032       9.617  16.003 -42.751  1.00 41.37           O  
ANISOU 1721  O   LEU A1032     8059   3921   3740   -148    152    280       O  
ATOM   1722  CB  LEU A1032      11.382  13.600 -42.641  1.00 36.36           C  
ANISOU 1722  CB  LEU A1032     6602   3639   3575   -405    150     -2       C  
ATOM   1723  CG  LEU A1032      12.782  14.179 -42.895  1.00 42.58           C  
ANISOU 1723  CG  LEU A1032     7401   4380   4397   -740    348   -245       C  
ATOM   1724  CD1 LEU A1032      13.754  13.108 -43.375  1.00 43.32           C  
ANISOU 1724  CD1 LEU A1032     7101   4585   4773   -875    427   -456       C  
ATOM   1725  CD2 LEU A1032      12.715  15.315 -43.881  1.00 46.53           C  
ANISOU 1725  CD2 LEU A1032     8394   4674   4612   -933    551   -248       C  
ATOM   1726  N   LEU A1033      10.991  16.585 -41.043  1.00 38.29           N  
ANISOU 1726  N   LEU A1033     7575   3557   3417   -380    230     78       N  
ATOM   1727  CA  LEU A1033      10.852  18.020 -41.224  1.00 39.60           C  
ANISOU 1727  CA  LEU A1033     8235   3467   3344   -433    362     96       C  
ATOM   1728  C   LEU A1033      11.839  18.572 -42.244  1.00 45.18           C  
ANISOU 1728  C   LEU A1033     9189   4048   3930   -802    568    -53       C  
ATOM   1729  O   LEU A1033      11.452  19.341 -43.118  1.00 46.68           O  
ANISOU 1729  O   LEU A1033     9845   4000   3891   -812    642     28       O  
ATOM   1730  CB  LEU A1033      11.027  18.734 -39.887  1.00 40.20           C  
ANISOU 1730  CB  LEU A1033     8419   3489   3364   -460    381     49       C  
ATOM   1731  CG  LEU A1033       9.782  18.734 -39.010  1.00 43.67           C  
ANISOU 1731  CG  LEU A1033     8868   3916   3807   -116    303    191       C  
ATOM   1732  CD1 LEU A1033      10.121  19.320 -37.683  1.00 44.61           C  
ANISOU 1732  CD1 LEU A1033     9125   3986   3841   -229    352    109       C  
ATOM   1733  CD2 LEU A1033       8.669  19.524 -39.663  1.00 47.11           C  
ANISOU 1733  CD2 LEU A1033     9628   4130   4142    159    336    326       C  
ATOM   1734  N   THR A1034      13.107  18.190 -42.135  1.00 41.61           N  
ANISOU 1734  N   THR A1034     8437   3739   3632  -1110    658   -282       N  
ATOM   1735  CA  THR A1034      14.122  18.681 -43.062  1.00 43.44           C  
ANISOU 1735  CA  THR A1034     8852   3875   3778  -1535    936   -493       C  
ATOM   1736  C   THR A1034      15.404  17.851 -43.042  1.00 47.48           C  
ANISOU 1736  C   THR A1034     8808   4623   4610  -1787   1009   -779       C  
ATOM   1737  O   THR A1034      15.835  17.359 -41.987  1.00 47.08           O  
ANISOU 1737  O   THR A1034     8327   4761   4800  -1711    817   -843       O  
ATOM   1738  CB  THR A1034      14.490  20.142 -42.756  1.00 52.08           C  
ANISOU 1738  CB  THR A1034    10429   4739   4622  -1785   1106   -566       C  
ATOM   1739  OG1 THR A1034      15.642  20.516 -43.513  1.00 52.20           O  
ANISOU 1739  OG1 THR A1034    10545   4702   4584  -2290   1421   -837       O  
ATOM   1740  CG2 THR A1034      14.806  20.315 -41.287  1.00 51.50           C  
ANISOU 1740  CG2 THR A1034    10141   4778   4649  -1769    979   -624       C  
ATOM   1741  N   LYS A1035      16.011  17.725 -44.220  1.00 44.30           N  
ANISOU 1741  N   LYS A1035     8444   4184   4204  -2090   1285   -961       N  
ATOM   1742  CA  LYS A1035      17.307  17.082 -44.364  1.00 45.20           C  
ANISOU 1742  CA  LYS A1035     8024   4489   4663  -2360   1444  -1306       C  
ATOM   1743  C   LYS A1035      18.496  18.038 -44.082  1.00 51.98           C  
ANISOU 1743  C   LYS A1035     8877   5342   5530  -2819   1674  -1615       C  
ATOM   1744  O   LYS A1035      19.656  17.625 -44.133  1.00 53.87           O  
ANISOU 1744  O   LYS A1035     8596   5760   6113  -3065   1811  -1959       O  
ATOM   1745  CB  LYS A1035      17.432  16.467 -45.765  1.00 47.93           C  
ANISOU 1745  CB  LYS A1035     8402   4795   5013  -2524   1715  -1419       C  
ATOM   1746  CG  LYS A1035      16.633  15.188 -45.974  1.00 51.16           C  
ANISOU 1746  CG  LYS A1035     8590   5295   5553  -2148   1498  -1233       C  
ATOM   1747  CD  LYS A1035      17.165  14.374 -47.165  1.00 61.49           C  
ANISOU 1747  CD  LYS A1035     9758   6614   6990  -2374   1806  -1469       C  
ATOM   1748  CE  LYS A1035      16.400  13.044 -47.365  1.00 67.71           C  
ANISOU 1748  CE  LYS A1035    10346   7478   7902  -2035   1604  -1305       C  
ATOM   1749  NZ  LYS A1035      17.061  12.079 -48.320  1.00 76.15           N  
ANISOU 1749  NZ  LYS A1035    11178   8567   9190  -2227   1913  -1588       N  
ATOM   1750  N   SER A1036      18.207  19.302 -43.776  1.00 49.05           N  
ANISOU 1750  N   SER A1036     9062   4764   4812  -2934   1720  -1516       N  
ATOM   1751  CA  SER A1036      19.245  20.266 -43.416  1.00 52.19           C  
ANISOU 1751  CA  SER A1036     9515   5145   5172  -3401   1928  -1799       C  
ATOM   1752  C   SER A1036      19.743  19.987 -41.991  1.00 56.59           C  
ANISOU 1752  C   SER A1036     9529   5956   6018  -3297   1596  -1873       C  
ATOM   1753  O   SER A1036      18.985  19.433 -41.179  1.00 53.15           O  
ANISOU 1753  O   SER A1036     8974   5587   5633  -2852   1227  -1614       O  
ATOM   1754  CB  SER A1036      18.686  21.688 -43.510  1.00 56.11           C  
ANISOU 1754  CB  SER A1036    10867   5280   5174  -3522   2065  -1642       C  
ATOM   1755  OG  SER A1036      19.718  22.656 -43.479  1.00 68.36           O  
ANISOU 1755  OG  SER A1036    12594   6760   6619  -4094   2377  -1949       O  
ATOM   1756  N   PRO A1037      21.013  20.365 -41.673  1.00 56.76           N  
ANISOU 1756  N   PRO A1037     9237   6116   6214  -3736   1714  -2238       N  
ATOM   1757  CA  PRO A1037      21.509  20.293 -40.291  1.00 57.25           C  
ANISOU 1757  CA  PRO A1037     8896   6386   6469  -3699   1341  -2302       C  
ATOM   1758  C   PRO A1037      21.175  21.536 -39.456  1.00 61.86           C  
ANISOU 1758  C   PRO A1037    10071   6782   6652  -3832   1314  -2190       C  
ATOM   1759  O   PRO A1037      21.845  21.809 -38.463  1.00 64.03           O  
ANISOU 1759  O   PRO A1037    10134   7197   6999  -4028   1117  -2341       O  
ATOM   1760  CB  PRO A1037      23.036  20.150 -40.459  1.00 63.43           C  
ANISOU 1760  CB  PRO A1037     9027   7417   7657  -4134   1483  -2788       C  
ATOM   1761  CG  PRO A1037      23.311  20.241 -41.910  1.00 69.27           C  
ANISOU 1761  CG  PRO A1037     9899   8050   8370  -4449   2024  -2995       C  
ATOM   1762  CD  PRO A1037      22.091  20.769 -42.587  1.00 62.17           C  
ANISOU 1762  CD  PRO A1037     9866   6800   6955  -4316   2188  -2643       C  
ATOM   1763  N   SER A1038      20.141  22.267 -39.858  1.00 56.43           N  
ANISOU 1763  N   SER A1038    10121   5764   5555  -3714   1489  -1935       N  
ATOM   1764  CA  SER A1038      19.671  23.429 -39.130  1.00 56.68           C  
ANISOU 1764  CA  SER A1038    10774   5548   5214  -3762   1504  -1814       C  
ATOM   1765  C   SER A1038      18.438  23.079 -38.327  1.00 57.50           C  
ANISOU 1765  C   SER A1038    10988   5609   5252  -3208   1196  -1467       C  
ATOM   1766  O   SER A1038      17.449  22.603 -38.878  1.00 54.57           O  
ANISOU 1766  O   SER A1038    10698   5162   4872  -2812   1163  -1226       O  
ATOM   1767  CB  SER A1038      19.311  24.547 -40.102  1.00 61.34           C  
ANISOU 1767  CB  SER A1038    12161   5738   5409  -3960   1898  -1769       C  
ATOM   1768  OG  SER A1038      18.581  25.572 -39.450  1.00 69.55           O  
ANISOU 1768  OG  SER A1038    13844   6470   6112  -3844   1895  -1592       O  
ATOM   1769  N   LEU A1039      18.491  23.340 -37.026  1.00 54.83           N  
ANISOU 1769  N   LEU A1039    10673   5314   4848  -3225    991  -1464       N  
ATOM   1770  CA  LEU A1039      17.312  23.225 -36.174  1.00 52.25           C  
ANISOU 1770  CA  LEU A1039    10567   4893   4392  -2795    809  -1185       C  
ATOM   1771  C   LEU A1039      16.361  24.424 -36.387  1.00 56.97           C  
ANISOU 1771  C   LEU A1039    11924   5080   4644  -2688   1081  -1043       C  
ATOM   1772  O   LEU A1039      15.197  24.366 -35.986  1.00 54.78           O  
ANISOU 1772  O   LEU A1039    11824   4688   4303  -2274   1022   -825       O  
ATOM   1773  CB  LEU A1039      17.731  23.080 -34.700  1.00 53.48           C  
ANISOU 1773  CB  LEU A1039    10563   5209   4548  -2903    510  -1246       C  
ATOM   1774  CG  LEU A1039      16.676  22.776 -33.621  1.00 56.20           C  
ANISOU 1774  CG  LEU A1039    11081   5505   4768  -2550    328  -1016       C  
ATOM   1775  CD1 LEU A1039      15.484  22.032 -34.189  1.00 52.93           C  
ANISOU 1775  CD1 LEU A1039    10588   5067   4458  -2055    342   -772       C  
ATOM   1776  CD2 LEU A1039      17.285  21.989 -32.450  1.00 59.10           C  
ANISOU 1776  CD2 LEU A1039    11094   6126   5235  -2630   -100  -1058       C  
ATOM   1777  N   ASN A1040      16.843  25.500 -37.018  1.00 56.78           N  
ANISOU 1777  N   ASN A1040    12349   4815   4410  -3055   1388  -1182       N  
ATOM   1778  CA  ASN A1040      15.949  26.570 -37.476  1.00 57.70           C  
ANISOU 1778  CA  ASN A1040    13218   4481   4225  -2894   1617  -1027       C  
ATOM   1779  C   ASN A1040      15.051  26.090 -38.613  1.00 59.74           C  
ANISOU 1779  C   ASN A1040    13490   4663   4545  -2487   1585   -801       C  
ATOM   1780  O   ASN A1040      13.828  26.144 -38.501  1.00 58.22           O  
ANISOU 1780  O   ASN A1040    13475   4315   4330  -2001   1497   -571       O  
ATOM   1781  CB  ASN A1040      16.723  27.803 -37.961  1.00 62.73           C  
ANISOU 1781  CB  ASN A1040    14424   4830   4579  -3430   1956  -1224       C  
ATOM   1782  CG  ASN A1040      17.409  28.545 -36.844  1.00 86.55           C  
ANISOU 1782  CG  ASN A1040    17605   7831   7451  -3840   2014  -1432       C  
ATOM   1783  OD1 ASN A1040      17.060  28.396 -35.674  1.00 79.31           O  
ANISOU 1783  OD1 ASN A1040    16592   6995   6548  -3661   1826  -1377       O  
ATOM   1784  ND2 ASN A1040      18.393  29.367 -37.203  1.00 82.50           N  
ANISOU 1784  ND2 ASN A1040    17384   7199   6762  -4446   2295  -1689       N  
ATOM   1785  N   ALA A1041      15.662  25.632 -39.708  1.00 56.33           N  
ANISOU 1785  N   ALA A1041    12866   4343   4196  -2709   1666   -893       N  
ATOM   1786  CA  ALA A1041      14.902  25.199 -40.889  1.00 54.94           C  
ANISOU 1786  CA  ALA A1041    12775   4083   4018  -2414   1629   -696       C  
ATOM   1787  C   ALA A1041      13.848  24.177 -40.497  1.00 55.05           C  
ANISOU 1787  C   ALA A1041    12355   4299   4261  -1856   1325   -476       C  
ATOM   1788  O   ALA A1041      12.723  24.214 -41.002  1.00 53.79           O  
ANISOU 1788  O   ALA A1041    12414   3978   4047  -1461   1231   -247       O  
ATOM   1789  CB  ALA A1041      15.821  24.625 -41.959  1.00 56.43           C  
ANISOU 1789  CB  ALA A1041    12715   4428   4298  -2784   1782   -882       C  
ATOM   1790  N   ALA A1042      14.223  23.282 -39.585  1.00 49.85           N  
ANISOU 1790  N   ALA A1042    11102   3983   3854  -1844   1154   -554       N  
ATOM   1791  CA  ALA A1042      13.303  22.306 -39.030  1.00 46.52           C  
ANISOU 1791  CA  ALA A1042    10312   3747   3618  -1401    903   -377       C  
ATOM   1792  C   ALA A1042      12.094  23.003 -38.406  1.00 51.05           C  
ANISOU 1792  C   ALA A1042    11253   4089   4056  -1050    906   -211       C  
ATOM   1793  O   ALA A1042      10.964  22.721 -38.782  1.00 50.13           O  
ANISOU 1793  O   ALA A1042    11118   3933   3996   -652    821    -29       O  
ATOM   1794  CB  ALA A1042      14.012  21.452 -38.015  1.00 46.28           C  
ANISOU 1794  CB  ALA A1042     9761   4028   3795  -1506    716   -491       C  
ATOM   1795  N   LYS A1043      12.329  23.929 -37.480  1.00 49.27           N  
ANISOU 1795  N   LYS A1043    11349   3704   3667  -1209   1018   -302       N  
ATOM   1796  CA  LYS A1043      11.234  24.705 -36.868  1.00 50.25           C  
ANISOU 1796  CA  LYS A1043    11857   3557   3678   -891   1100   -199       C  
ATOM   1797  C   LYS A1043      10.474  25.545 -37.892  1.00 56.90           C  
ANISOU 1797  C   LYS A1043    13176   4034   4409   -635   1188    -67       C  
ATOM   1798  O   LYS A1043       9.288  25.809 -37.731  1.00 57.21           O  
ANISOU 1798  O   LYS A1043    13327   3911   4502   -190   1171     57       O  
ATOM   1799  CB  LYS A1043      11.757  25.636 -35.768  1.00 54.77           C  
ANISOU 1799  CB  LYS A1043    12787   3978   4047  -1188   1251   -355       C  
ATOM   1800  CG  LYS A1043      12.176  24.927 -34.502  1.00 61.87           C  
ANISOU 1800  CG  LYS A1043    13338   5167   5003  -1344   1096   -438       C  
ATOM   1801  CD  LYS A1043      12.845  25.873 -33.512  1.00 73.27           C  
ANISOU 1801  CD  LYS A1043    15172   6469   6196  -1738   1216   -613       C  
ATOM   1802  CE  LYS A1043      13.321  25.117 -32.277  1.00 81.61           C  
ANISOU 1802  CE  LYS A1043    15926   7812   7269  -1919    973   -677       C  
ATOM   1803  NZ  LYS A1043      13.978  26.006 -31.292  1.00 91.68           N  
ANISOU 1803  NZ  LYS A1043    17597   8970   8270  -2346   1044   -853       N  
ATOM   1804  N   SER A1044      11.169  25.978 -38.935  1.00 55.51           N  
ANISOU 1804  N   SER A1044    13298   3713   4081   -926   1278   -108       N  
ATOM   1805  CA  SER A1044      10.563  26.821 -39.949  1.00 57.87           C  
ANISOU 1805  CA  SER A1044    14178   3607   4202   -734   1313     36       C  
ATOM   1806  C   SER A1044       9.585  25.999 -40.776  1.00 59.47           C  
ANISOU 1806  C   SER A1044    14094   3927   4573   -309   1060    240       C  
ATOM   1807  O   SER A1044       8.491  26.459 -41.097  1.00 60.72           O  
ANISOU 1807  O   SER A1044    14509   3831   4731    136    943    410       O  
ATOM   1808  CB  SER A1044      11.637  27.450 -40.837  1.00 64.32           C  
ANISOU 1808  CB  SER A1044    15460   4229   4751  -1261   1514    -82       C  
ATOM   1809  OG  SER A1044      11.161  28.644 -41.433  1.00 77.72           O  
ANISOU 1809  OG  SER A1044    17965   5396   6171  -1143   1587     38       O  
ATOM   1810  N   GLU A1045       9.982  24.777 -41.106  1.00 52.80           N  
ANISOU 1810  N   GLU A1045    12706   3465   3891   -440    960    208       N  
ATOM   1811  CA  GLU A1045       9.103  23.845 -41.807  1.00 50.84           C  
ANISOU 1811  CA  GLU A1045    12133   3383   3802   -102    721    374       C  
ATOM   1812  C   GLU A1045       8.009  23.299 -40.895  1.00 52.23           C  
ANISOU 1812  C   GLU A1045    11877   3739   4229    335    584    449       C  
ATOM   1813  O   GLU A1045       6.943  22.911 -41.362  1.00 51.47           O  
ANISOU 1813  O   GLU A1045    11618   3684   4256    705    390    595       O  
ATOM   1814  CB  GLU A1045       9.917  22.684 -42.375  1.00 50.11           C  
ANISOU 1814  CB  GLU A1045    11616   3613   3809   -404    710    282       C  
ATOM   1815  CG  GLU A1045      10.673  23.037 -43.644  1.00 64.00           C  
ANISOU 1815  CG  GLU A1045    13788   5197   5334   -789    857    221       C  
ATOM   1816  CD  GLU A1045       9.797  22.971 -44.878  1.00 86.59           C  
ANISOU 1816  CD  GLU A1045    16937   7901   8062   -566    671    430       C  
ATOM   1817  OE1 GLU A1045       8.933  22.064 -44.924  1.00 78.67           O  
ANISOU 1817  OE1 GLU A1045    15517   7118   7257   -230    430    553       O  
ATOM   1818  OE2 GLU A1045       9.973  23.815 -45.792  1.00 84.20           O  
ANISOU 1818  OE2 GLU A1045    17309   7249   7436   -756    750    470       O  
ATOM   1819  N   LEU A1046       8.289  23.260 -39.598  1.00 48.08           N  
ANISOU 1819  N   LEU A1046    11180   3325   3765    248    689    332       N  
ATOM   1820  CA  LEU A1046       7.348  22.723 -38.614  1.00 47.09           C  
ANISOU 1820  CA  LEU A1046    10696   3363   3833    557    641    359       C  
ATOM   1821  C   LEU A1046       6.189  23.698 -38.416  1.00 54.67           C  
ANISOU 1821  C   LEU A1046    11943   4019   4811    972    703    417       C  
ATOM   1822  O   LEU A1046       5.018  23.297 -38.360  1.00 54.50           O  
ANISOU 1822  O   LEU A1046    11618   4087   5003   1359    614    482       O  
ATOM   1823  CB  LEU A1046       8.066  22.452 -37.277  1.00 46.09           C  
ANISOU 1823  CB  LEU A1046    10426   3395   3689    280    725    216       C  
ATOM   1824  CG  LEU A1046       7.267  21.913 -36.080  1.00 49.64           C  
ANISOU 1824  CG  LEU A1046    10626   3985   4251    464    743    209       C  
ATOM   1825  CD1 LEU A1046       6.365  20.754 -36.477  1.00 47.91           C  
ANISOU 1825  CD1 LEU A1046     9946   4004   4252    730    594    313       C  
ATOM   1826  CD2 LEU A1046       8.195  21.502 -34.936  1.00 50.17           C  
ANISOU 1826  CD2 LEU A1046    10619   4210   4235    114    725     97       C  
ATOM   1827  N   ASP A1047       6.534  24.979 -38.305  1.00 54.14           N  
ANISOU 1827  N   ASP A1047    12447   3583   4540    882    870    367       N  
ATOM   1828  CA  ASP A1047       5.545  26.042 -38.237  1.00 57.35           C  
ANISOU 1828  CA  ASP A1047    13212   3610   4970   1301    934    412       C  
ATOM   1829  C   ASP A1047       4.695  26.002 -39.499  1.00 61.51           C  
ANISOU 1829  C   ASP A1047    13736   4041   5594   1690    656    600       C  
ATOM   1830  O   ASP A1047       3.470  25.948 -39.422  1.00 62.57           O  
ANISOU 1830  O   ASP A1047    13617   4171   5984   2179    550    648       O  
ATOM   1831  CB  ASP A1047       6.228  27.404 -38.086  1.00 62.46           C  
ANISOU 1831  CB  ASP A1047    14576   3828   5328   1068   1155    334       C  
ATOM   1832  CG  ASP A1047       6.925  27.574 -36.729  1.00 76.21           C  
ANISOU 1832  CG  ASP A1047    16362   5634   6961    703   1402    137       C  
ATOM   1833  OD1 ASP A1047       6.864  26.665 -35.868  1.00 74.40           O  
ANISOU 1833  OD1 ASP A1047    15657   5751   6859    650   1387     77       O  
ATOM   1834  OD2 ASP A1047       7.543  28.640 -36.520  1.00 87.49           O  
ANISOU 1834  OD2 ASP A1047    18363   6741   8138    438   1601     43       O  
ATOM   1835  N   LYS A1048       5.357  25.978 -40.652  1.00 56.92           N  
ANISOU 1835  N   LYS A1048    13412   3404   4810   1442    536    683       N  
ATOM   1836  CA  LYS A1048       4.681  25.943 -41.950  1.00 57.93           C  
ANISOU 1836  CA  LYS A1048    13658   3419   4935   1723    223    878       C  
ATOM   1837  C   LYS A1048       3.649  24.824 -42.051  1.00 60.17           C  
ANISOU 1837  C   LYS A1048    13251   4071   5540   2057    -25    944       C  
ATOM   1838  O   LYS A1048       2.601  25.001 -42.658  1.00 62.24           O  
ANISOU 1838  O   LYS A1048    13504   4220   5926   2496   -308   1078       O  
ATOM   1839  CB  LYS A1048       5.710  25.799 -43.079  1.00 59.30           C  
ANISOU 1839  CB  LYS A1048    14156   3564   4809   1253    209    906       C  
ATOM   1840  CG  LYS A1048       5.152  26.029 -44.490  1.00 74.61           C  
ANISOU 1840  CG  LYS A1048    16495   5260   6595   1447   -109   1120       C  
ATOM   1841  CD  LYS A1048       6.215  25.873 -45.593  1.00 83.34           C  
ANISOU 1841  CD  LYS A1048    17988   6322   7358    891    -30   1106       C  
ATOM   1842  CE  LYS A1048       7.333  26.910 -45.486  1.00 92.40           C  
ANISOU 1842  CE  LYS A1048    19785   7139   8186    425    322    974       C  
ATOM   1843  NZ  LYS A1048       7.945  27.189 -46.821  1.00102.94           N  
ANISOU 1843  NZ  LYS A1048    21783   8216   9114      9    361   1015       N  
ATOM   1844  N   ALA A1049       3.949  23.677 -41.451  1.00 53.02           N  
ANISOU 1844  N   ALA A1049    11784   3593   4769   1842     60    845       N  
ATOM   1845  CA  ALA A1049       3.085  22.501 -41.548  1.00 51.15           C  
ANISOU 1845  CA  ALA A1049    10920   3719   4798   2047   -129    885       C  
ATOM   1846  C   ALA A1049       1.910  22.527 -40.573  1.00 56.26           C  
ANISOU 1846  C   ALA A1049    11197   4431   5747   2443    -61    815       C  
ATOM   1847  O   ALA A1049       1.004  21.695 -40.681  1.00 56.03           O  
ANISOU 1847  O   ALA A1049    10657   4671   5960   2643   -208    830       O  
ATOM   1848  CB  ALA A1049       3.905  21.240 -41.322  1.00 47.64           C  
ANISOU 1848  CB  ALA A1049    10099   3646   4358   1653    -61    809       C  
ATOM   1849  N   ILE A1050       1.936  23.457 -39.618  1.00 53.71           N  
ANISOU 1849  N   ILE A1050    11133   3867   5407   2509    200    708       N  
ATOM   1850  CA  ILE A1050       0.936  23.514 -38.545  1.00 54.79           C  
ANISOU 1850  CA  ILE A1050    10954   4048   5817   2806    390    575       C  
ATOM   1851  C   ILE A1050       0.146  24.827 -38.539  1.00 63.96           C  
ANISOU 1851  C   ILE A1050    12414   4786   7101   3282    425    560       C  
ATOM   1852  O   ILE A1050      -1.072  24.825 -38.384  1.00 66.59           O  
ANISOU 1852  O   ILE A1050    12360   5155   7785   3725    397    500       O  
ATOM   1853  CB  ILE A1050       1.606  23.284 -37.165  1.00 55.58           C  
ANISOU 1853  CB  ILE A1050    11063   4256   5801   2434    727    412       C  
ATOM   1854  CG1 ILE A1050       1.912  21.799 -36.953  1.00 51.72           C  
ANISOU 1854  CG1 ILE A1050    10120   4198   5332   2141    662    411       C  
ATOM   1855  CG2 ILE A1050       0.724  23.769 -36.041  1.00 59.40           C  
ANISOU 1855  CG2 ILE A1050    11486   4625   6460   2677   1035    241       C  
ATOM   1856  CD1 ILE A1050       0.680  20.884 -37.005  1.00 57.61           C  
ANISOU 1856  CD1 ILE A1050    10288   5220   6380   2392    590    400       C  
ATOM   1857  N   GLY A1051       0.840  25.943 -38.706  1.00 62.24           N  
ANISOU 1857  N   GLY A1051    12875   4158   6616   3190    498    593       N  
ATOM   1858  CA  GLY A1051       0.188  27.248 -38.788  1.00 67.55           C  
ANISOU 1858  CA  GLY A1051    13952   4338   7375   3656    510    598       C  
ATOM   1859  C   GLY A1051       0.189  27.974 -37.459  1.00 73.58           C  
ANISOU 1859  C   GLY A1051    14919   4889   8149   3643    964    382       C  
ATOM   1860  O   GLY A1051      -0.821  28.544 -37.049  1.00 77.53           O  
ANISOU 1860  O   GLY A1051    15329   5180   8950   4126   1084    275       O  
ATOM   1861  N   ARG A1052       1.332  27.927 -36.784  1.00 67.46           N  
ANISOU 1861  N   ARG A1052    14399   4173   7059   3079   1213    295       N  
ATOM   1862  CA  ARG A1052       1.574  28.682 -35.563  1.00 69.10           C  
ANISOU 1862  CA  ARG A1052    14960   4146   7147   2927   1632     96       C  
ATOM   1863  C   ARG A1052       3.042  28.505 -35.229  1.00 70.37           C  
ANISOU 1863  C   ARG A1052    15382   4432   6922   2242   1714     63       C  
ATOM   1864  O   ARG A1052       3.642  27.502 -35.619  1.00 65.85           O  
ANISOU 1864  O   ARG A1052    14482   4236   6303   1952   1509    139       O  
ATOM   1865  CB  ARG A1052       0.708  28.178 -34.402  1.00 69.28           C  
ANISOU 1865  CB  ARG A1052    14498   4384   7439   3065   1908   -101       C  
ATOM   1866  CG  ARG A1052       0.991  26.740 -33.978  1.00 73.54           C  
ANISOU 1866  CG  ARG A1052    14515   5463   7962   2698   1861   -112       C  
ATOM   1867  CD  ARG A1052       0.108  26.301 -32.815  1.00 82.61           C  
ANISOU 1867  CD  ARG A1052    15304   6770   9316   2772   2190   -321       C  
ATOM   1868  NE  ARG A1052       0.616  25.071 -32.209  1.00 84.00           N  
ANISOU 1868  NE  ARG A1052    15224   7351   9341   2315   2177   -328       N  
ATOM   1869  CZ  ARG A1052       1.544  25.011 -31.250  1.00 94.90           C  
ANISOU 1869  CZ  ARG A1052    16928   8746  10383   1822   2316   -399       C  
ATOM   1870  NH1 ARG A1052       2.099  26.117 -30.748  1.00 83.15           N  
ANISOU 1870  NH1 ARG A1052    16029   6917   8649   1657   2522   -491       N  
ATOM   1871  NH2 ARG A1052       1.927  23.821 -30.790  1.00 77.29           N  
ANISOU 1871  NH2 ARG A1052    14457   6860   8048   1484   2215   -373       N  
ATOM   1872  N   ASN A1053       3.625  29.461 -34.516  1.00 69.81           N  
ANISOU 1872  N   ASN A1053    15876   4049   6598   1982   2003    -70       N  
ATOM   1873  CA  ASN A1053       5.010  29.309 -34.084  1.00 67.71           C  
ANISOU 1873  CA  ASN A1053    15787   3936   6003   1317   2058   -142       C  
ATOM   1874  C   ASN A1053       5.123  28.275 -32.949  1.00 69.46           C  
ANISOU 1874  C   ASN A1053    15564   4576   6253   1067   2110   -247       C  
ATOM   1875  O   ASN A1053       4.953  28.606 -31.767  1.00 70.74           O  
ANISOU 1875  O   ASN A1053    15917   4635   6328    968   2394   -411       O  
ATOM   1876  CB  ASN A1053       5.618  30.650 -33.674  1.00 73.00           C  
ANISOU 1876  CB  ASN A1053    17222   4150   6363   1054   2333   -265       C  
ATOM   1877  CG  ASN A1053       7.077  30.524 -33.260  1.00 99.48           C  
ANISOU 1877  CG  ASN A1053    20701   7693   9406    339   2349   -369       C  
ATOM   1878  OD1 ASN A1053       7.802  29.637 -33.731  1.00 90.49           O  
ANISOU 1878  OD1 ASN A1053    19174   6928   8279     75   2110   -313       O  
ATOM   1879  ND2 ASN A1053       7.514  31.409 -32.367  1.00 96.14           N  
ANISOU 1879  ND2 ASN A1053    20799   7008   8722     24   2627   -543       N  
ATOM   1880  N   THR A1054       5.405  27.028 -33.337  1.00 62.29           N  
ANISOU 1880  N   THR A1054    14130   4099   5440    956   1837   -150       N  
ATOM   1881  CA  THR A1054       5.509  25.894 -32.412  1.00 59.66           C  
ANISOU 1881  CA  THR A1054    13398   4145   5127    744   1804   -201       C  
ATOM   1882  C   THR A1054       6.690  26.027 -31.459  1.00 63.60           C  
ANISOU 1882  C   THR A1054    14165   4679   5319    194   1844   -321       C  
ATOM   1883  O   THR A1054       6.569  25.744 -30.265  1.00 63.52           O  
ANISOU 1883  O   THR A1054    14184   4741   5209     36   1957   -417       O  
ATOM   1884  CB  THR A1054       5.704  24.561 -33.185  1.00 63.94           C  
ANISOU 1884  CB  THR A1054    13388   5081   5824    736   1478    -63       C  
ATOM   1885  OG1 THR A1054       6.756  24.711 -34.149  1.00 64.15           O  
ANISOU 1885  OG1 THR A1054    13525   5102   5747    499   1315    -11       O  
ATOM   1886  CG2 THR A1054       4.421  24.138 -33.897  1.00 61.63           C  
ANISOU 1886  CG2 THR A1054    12724   4856   5837   1228   1399     37       C  
ATOM   1887  N   ASN A1055       7.832  26.437 -32.012  1.00 60.27           N  
ANISOU 1887  N   ASN A1055    13944   4212   4742   -128   1741   -326       N  
ATOM   1888  CA  ASN A1055       9.090  26.553 -31.272  1.00 60.58           C  
ANISOU 1888  CA  ASN A1055    14153   4332   4532   -682   1698   -455       C  
ATOM   1889  C   ASN A1055       9.650  25.187 -30.853  1.00 61.61           C  
ANISOU 1889  C   ASN A1055    13784   4893   4732   -876   1389   -429       C  
ATOM   1890  O   ASN A1055      10.375  25.079 -29.867  1.00 62.47           O  
ANISOU 1890  O   ASN A1055    13981   5096   4658  -1246   1296   -525       O  
ATOM   1891  CB  ASN A1055       8.926  27.484 -30.058  1.00 64.82           C  
ANISOU 1891  CB  ASN A1055    15223   4588   4819   -838   1992   -611       C  
ATOM   1892  CG  ASN A1055      10.212  28.212 -29.696  1.00 92.23           C  
ANISOU 1892  CG  ASN A1055    19077   7977   7989  -1407   1997   -759       C  
ATOM   1893  OD1 ASN A1055      11.040  28.507 -30.561  1.00 87.26           O  
ANISOU 1893  OD1 ASN A1055    18468   7343   7343  -1613   1922   -770       O  
ATOM   1894  ND2 ASN A1055      10.378  28.518 -28.412  1.00 88.05           N  
ANISOU 1894  ND2 ASN A1055    18875   7379   7201  -1707   2108   -897       N  
ATOM   1895  N   GLY A1056       9.323  24.152 -31.622  1.00 54.71           N  
ANISOU 1895  N   GLY A1056    12422   4254   4111   -625   1202   -296       N  
ATOM   1896  CA  GLY A1056       9.852  22.819 -31.383  1.00 52.02           C  
ANISOU 1896  CA  GLY A1056    11628   4269   3869   -753    897   -257       C  
ATOM   1897  C   GLY A1056       8.835  21.830 -30.845  1.00 54.25           C  
ANISOU 1897  C   GLY A1056    11676   4686   4250   -509    878   -172       C  
ATOM   1898  O   GLY A1056       9.041  20.622 -30.951  1.00 51.89           O  
ANISOU 1898  O   GLY A1056    10997   4640   4078   -506    629    -97       O  
ATOM   1899  N   VAL A1057       7.731  22.321 -30.286  1.00 51.91           N  
ANISOU 1899  N   VAL A1057    11605   4207   3910   -313   1169   -206       N  
ATOM   1900  CA  VAL A1057       6.761  21.440 -29.626  1.00 50.90           C  
ANISOU 1900  CA  VAL A1057    11295   4200   3845   -175   1236   -183       C  
ATOM   1901  C   VAL A1057       5.368  21.493 -30.244  1.00 54.67           C  
ANISOU 1901  C   VAL A1057    11552   4634   4588    277   1433   -157       C  
ATOM   1902  O   VAL A1057       4.923  22.541 -30.712  1.00 56.36           O  
ANISOU 1902  O   VAL A1057    11938   4606   4872    517   1606   -189       O  
ATOM   1903  CB  VAL A1057       6.646  21.759 -28.132  1.00 56.92           C  
ANISOU 1903  CB  VAL A1057    12474   4833   4320   -427   1445   -310       C  
ATOM   1904  CG1 VAL A1057       7.723  21.027 -27.368  1.00 56.34           C  
ANISOU 1904  CG1 VAL A1057    12457   4922   4028   -825   1107   -285       C  
ATOM   1905  CG2 VAL A1057       6.726  23.266 -27.895  1.00 59.60           C  
ANISOU 1905  CG2 VAL A1057    13308   4838   4498   -485   1734   -445       C  
ATOM   1906  N   ILE A1058       4.682  20.354 -30.232  1.00 48.99           N  
ANISOU 1906  N   ILE A1058    10456   4136   4020    388   1382   -104       N  
ATOM   1907  CA  ILE A1058       3.321  20.265 -30.748  1.00 49.12           C  
ANISOU 1907  CA  ILE A1058    10163   4176   4324    784   1532   -109       C  
ATOM   1908  C   ILE A1058       2.435  19.518 -29.774  1.00 54.49           C  
ANISOU 1908  C   ILE A1058    10721   4967   5016    727   1760   -204       C  
ATOM   1909  O   ILE A1058       2.889  19.096 -28.721  1.00 54.90           O  
ANISOU 1909  O   ILE A1058    11018   5038   4803    381   1784   -237       O  
ATOM   1910  CB  ILE A1058       3.280  19.594 -32.135  1.00 49.39           C  
ANISOU 1910  CB  ILE A1058     9791   4397   4578    973   1234     44       C  
ATOM   1911  CG1 ILE A1058       3.573  18.098 -32.050  1.00 46.77           C  
ANISOU 1911  CG1 ILE A1058     9175   4348   4247    782   1028    119       C  
ATOM   1912  CG2 ILE A1058       4.271  20.267 -33.055  1.00 49.30           C  
ANISOU 1912  CG2 ILE A1058     9974   4266   4493    921   1057    114       C  
ATOM   1913  CD1 ILE A1058       3.720  17.455 -33.395  1.00 46.31           C  
ANISOU 1913  CD1 ILE A1058     8796   4446   4356    894    760    245       C  
ATOM   1914  N   THR A1059       1.160  19.393 -30.121  1.00 52.16           N  
ANISOU 1914  N   THR A1059    10070   4732   5018   1048   1925   -262       N  
ATOM   1915  CA  THR A1059       0.204  18.679 -29.301  1.00 53.55           C  
ANISOU 1915  CA  THR A1059    10078   5026   5243    969   2214   -397       C  
ATOM   1916  C   THR A1059       0.046  17.313 -29.905  1.00 55.06           C  
ANISOU 1916  C   THR A1059     9854   5514   5552    940   1961   -274       C  
ATOM   1917  O   THR A1059       0.545  17.057 -30.991  1.00 51.57           O  
ANISOU 1917  O   THR A1059     9239   5163   5192   1041   1606   -109       O  
ATOM   1918  CB  THR A1059      -1.182  19.343 -29.307  1.00 64.41           C  
ANISOU 1918  CB  THR A1059    11207   6315   6951   1337   2584   -597       C  
ATOM   1919  OG1 THR A1059      -1.840  19.055 -30.548  1.00 63.70           O  
ANISOU 1919  OG1 THR A1059    10586   6393   7225   1702   2344   -514       O  
ATOM   1920  CG2 THR A1059      -1.078  20.854 -29.107  1.00 64.74           C  
ANISOU 1920  CG2 THR A1059    11632   6001   6967   1513   2787   -696       C  
ATOM   1921  N   LYS A1060      -0.664  16.443 -29.201  1.00 53.87           N  
ANISOU 1921  N   LYS A1060     9590   5490   5389    765   2187   -375       N  
ATOM   1922  CA  LYS A1060      -1.014  15.129 -29.729  1.00 52.18           C  
ANISOU 1922  CA  LYS A1060     8995   5535   5296    723   2019   -295       C  
ATOM   1923  C   LYS A1060      -1.839  15.294 -31.006  1.00 56.09           C  
ANISOU 1923  C   LYS A1060     8960   6160   6194   1127   1905   -286       C  
ATOM   1924  O   LYS A1060      -1.507  14.723 -32.043  1.00 53.32           O  
ANISOU 1924  O   LYS A1060     8409   5942   5909   1184   1550   -121       O  
ATOM   1925  CB  LYS A1060      -1.806  14.325 -28.685  1.00 57.35           C  
ANISOU 1925  CB  LYS A1060     9675   6258   5855    433   2386   -455       C  
ATOM   1926  CG  LYS A1060      -1.981  12.839 -29.010  1.00 69.81           C  
ANISOU 1926  CG  LYS A1060    11028   8053   7444    263   2225   -365       C  
ATOM   1927  CD  LYS A1060      -3.031  12.177 -28.103  1.00 84.27           C  
ANISOU 1927  CD  LYS A1060    12846   9946   9228    -22   2687   -577       C  
ATOM   1928  CE  LYS A1060      -3.100  10.648 -28.292  1.00 95.03           C  
ANISOU 1928  CE  LYS A1060    14134  11460  10511   -275   2543   -479       C  
ATOM   1929  NZ  LYS A1060      -1.914   9.910 -27.743  1.00101.14           N  
ANISOU 1929  NZ  LYS A1060    15463  12091  10875   -565   2239   -269       N  
ATOM   1930  N   ASP A1061      -2.895  16.104 -30.924  1.00 56.17           N  
ANISOU 1930  N   ASP A1061     8760   6109   6472   1411   2194   -475       N  
ATOM   1931  CA  ASP A1061      -3.885  16.210 -31.999  1.00 57.64           C  
ANISOU 1931  CA  ASP A1061     8396   6431   7074   1811   2061   -497       C  
ATOM   1932  C   ASP A1061      -3.320  16.861 -33.254  1.00 58.71           C  
ANISOU 1932  C   ASP A1061     8600   6461   7245   2098   1629   -286       C  
ATOM   1933  O   ASP A1061      -3.686  16.481 -34.373  1.00 57.05           O  
ANISOU 1933  O   ASP A1061     8047   6411   7220   2275   1315   -186       O  
ATOM   1934  CB  ASP A1061      -5.133  16.960 -31.510  1.00 65.28           C  
ANISOU 1934  CB  ASP A1061     9093   7333   8375   2085   2474   -788       C  
ATOM   1935  CG  ASP A1061      -6.001  16.115 -30.572  1.00 81.39           C  
ANISOU 1935  CG  ASP A1061    10895   9559  10471   1788   2926  -1043       C  
ATOM   1936  OD1 ASP A1061      -6.524  16.671 -29.577  1.00 86.25           O  
ANISOU 1936  OD1 ASP A1061    11599  10038  11135   1759   3437  -1315       O  
ATOM   1937  OD2 ASP A1061      -6.164  14.897 -30.828  1.00 86.45           O  
ANISOU 1937  OD2 ASP A1061    11298  10459  11091   1553   2809   -990       O  
ATOM   1938  N   GLU A1062      -2.439  17.841 -33.061  1.00 54.61           N  
ANISOU 1938  N   GLU A1062     8569   5664   6516   2096   1629   -230       N  
ATOM   1939  CA  GLU A1062      -1.658  18.401 -34.161  1.00 52.62           C  
ANISOU 1939  CA  GLU A1062     8528   5280   6186   2224   1270    -32       C  
ATOM   1940  C   GLU A1062      -0.850  17.290 -34.809  1.00 53.20           C  
ANISOU 1940  C   GLU A1062     8539   5560   6116   1958    963    137       C  
ATOM   1941  O   GLU A1062      -0.951  17.055 -36.017  1.00 52.41           O  
ANISOU 1941  O   GLU A1062     8261   5541   6109   2093    666    259       O  
ATOM   1942  CB  GLU A1062      -0.728  19.515 -33.669  1.00 54.05           C  
ANISOU 1942  CB  GLU A1062     9282   5143   6111   2128   1386    -39       C  
ATOM   1943  CG  GLU A1062      -1.471  20.801 -33.360  1.00 68.81           C  
ANISOU 1943  CG  GLU A1062    11283   6719   8142   2477   1642   -183       C  
ATOM   1944  CD  GLU A1062      -0.632  21.852 -32.653  1.00 87.30           C  
ANISOU 1944  CD  GLU A1062    14236   8736  10197   2305   1844   -236       C  
ATOM   1945  OE1 GLU A1062       0.568  21.615 -32.406  1.00 75.24           O  
ANISOU 1945  OE1 GLU A1062    12998   7238   8352   1903   1750   -163       O  
ATOM   1946  OE2 GLU A1062      -1.185  22.934 -32.347  1.00 83.78           O  
ANISOU 1946  OE2 GLU A1062    13971   7995   9866   2582   2093   -368       O  
ATOM   1947  N   ALA A1063      -0.072  16.595 -33.984  1.00 47.93           N  
ANISOU 1947  N   ALA A1063     8037   4954   5219   1584   1030    134       N  
ATOM   1948  CA  ALA A1063       0.748  15.481 -34.430  1.00 44.61           C  
ANISOU 1948  CA  ALA A1063     7556   4695   4697   1347    774    261       C  
ATOM   1949  C   ALA A1063      -0.064  14.513 -35.261  1.00 49.06           C  
ANISOU 1949  C   ALA A1063     7690   5491   5459   1437    641    298       C  
ATOM   1950  O   ALA A1063       0.440  13.986 -36.255  1.00 46.56           O  
ANISOU 1950  O   ALA A1063     7309   5250   5132   1394    384    414       O  
ATOM   1951  CB  ALA A1063       1.345  14.763 -33.238  1.00 44.51           C  
ANISOU 1951  CB  ALA A1063     7734   4708   4469   1004    854    233       C  
ATOM   1952  N   GLU A1064      -1.314  14.283 -34.848  1.00 48.69           N  
ANISOU 1952  N   GLU A1064     7348   5558   5594   1528    846    168       N  
ATOM   1953  CA  GLU A1064      -2.212  13.343 -35.532  1.00 49.36           C  
ANISOU 1953  CA  GLU A1064     6984   5894   5878   1565    743    162       C  
ATOM   1954  C   GLU A1064      -2.641  13.859 -36.902  1.00 54.76           C  
ANISOU 1954  C   GLU A1064     7467   6591   6747   1891    445    243       C  
ATOM   1955  O   GLU A1064      -2.600  13.117 -37.892  1.00 52.67           O  
ANISOU 1955  O   GLU A1064     7056   6469   6486   1832    183    343       O  
ATOM   1956  CB  GLU A1064      -3.469  13.059 -34.697  1.00 54.17           C  
ANISOU 1956  CB  GLU A1064     7288   6631   6662   1543   1088    -55       C  
ATOM   1957  CG  GLU A1064      -3.268  12.232 -33.418  1.00 66.16           C  
ANISOU 1957  CG  GLU A1064     9030   8158   7951   1140   1376   -132       C  
ATOM   1958  CD  GLU A1064      -4.491  12.302 -32.479  1.00 97.64           C  
ANISOU 1958  CD  GLU A1064    12809  12203  12085   1091   1847   -406       C  
ATOM   1959  OE1 GLU A1064      -5.641  12.237 -32.980  1.00100.70           O  
ANISOU 1959  OE1 GLU A1064    12662  12781  12818   1272   1895   -543       O  
ATOM   1960  OE2 GLU A1064      -4.311  12.428 -31.242  1.00 94.98           O  
ANISOU 1960  OE2 GLU A1064    12837  11726  11524    853   2176   -508       O  
ATOM   1961  N   LYS A1065      -3.067  15.121 -36.962  1.00 54.75           N  
ANISOU 1961  N   LYS A1065     7509   6413   6880   2230    472    201       N  
ATOM   1962  CA  LYS A1065      -3.511  15.685 -38.234  1.00 56.42           C  
ANISOU 1962  CA  LYS A1065     7616   6582   7240   2569    125    302       C  
ATOM   1963  C   LYS A1065      -2.329  15.712 -39.211  1.00 57.43           C  
ANISOU 1963  C   LYS A1065     8135   6596   7090   2424   -148    505       C  
ATOM   1964  O   LYS A1065      -2.469  15.297 -40.356  1.00 57.03           O  
ANISOU 1964  O   LYS A1065     7989   6642   7039   2438   -456    612       O  
ATOM   1965  CB  LYS A1065      -4.193  17.060 -38.067  1.00 63.31           C  
ANISOU 1965  CB  LYS A1065     8510   7219   8326   3010    190    220       C  
ATOM   1966  CG  LYS A1065      -3.267  18.279 -38.050  1.00 79.43           C  
ANISOU 1966  CG  LYS A1065    11158   8881  10141   3073    207    308       C  
ATOM   1967  CD  LYS A1065      -4.000  19.565 -38.408  1.00 95.36           C  
ANISOU 1967  CD  LYS A1065    13233  10621  12379   3590    101    297       C  
ATOM   1968  CE  LYS A1065      -3.019  20.716 -38.627  1.00105.35           C  
ANISOU 1968  CE  LYS A1065    15193  11480  13356   3593     75    416       C  
ATOM   1969  NZ  LYS A1065      -3.612  21.788 -39.479  1.00119.37           N  
ANISOU 1969  NZ  LYS A1065    17134  12951  15272   4092   -222    509       N  
ATOM   1970  N   LEU A1066      -1.164  16.157 -38.744  1.00 52.04           N  
ANISOU 1970  N   LEU A1066     7884   5721   6168   2238    -15    529       N  
ATOM   1971  CA  LEU A1066       0.058  16.104 -39.551  1.00 49.54           C  
ANISOU 1971  CA  LEU A1066     7888   5321   5613   2022   -180    654       C  
ATOM   1972  C   LEU A1066       0.307  14.702 -40.089  1.00 51.71           C  
ANISOU 1972  C   LEU A1066     7943   5838   5865   1779   -305    695       C  
ATOM   1973  O   LEU A1066       0.720  14.539 -41.232  1.00 50.54           O  
ANISOU 1973  O   LEU A1066     7908   5674   5620   1704   -501    786       O  
ATOM   1974  CB  LEU A1066       1.278  16.543 -38.733  1.00 48.06           C  
ANISOU 1974  CB  LEU A1066     8060   4977   5223   1784     12    613       C  
ATOM   1975  CG  LEU A1066       2.641  16.636 -39.444  1.00 50.88           C  
ANISOU 1975  CG  LEU A1066     8713   5242   5377   1529    -80    671       C  
ATOM   1976  CD1 LEU A1066       2.661  17.689 -40.557  1.00 52.84           C  
ANISOU 1976  CD1 LEU A1066     9304   5246   5526   1664   -206    758       C  
ATOM   1977  CD2 LEU A1066       3.726  16.932 -38.423  1.00 52.80           C  
ANISOU 1977  CD2 LEU A1066     9174   5404   5483   1280     88    587       C  
ATOM   1978  N   PHE A1067       0.061  13.696 -39.261  1.00 47.88           N  
ANISOU 1978  N   PHE A1067     7207   5542   5444   1631   -166    619       N  
ATOM   1979  CA  PHE A1067       0.214  12.307 -39.678  1.00 45.90           C  
ANISOU 1979  CA  PHE A1067     6775   5483   5182   1411   -258    646       C  
ATOM   1980  C   PHE A1067      -0.819  11.895 -40.728  1.00 51.91           C  
ANISOU 1980  C   PHE A1067     7246   6407   6069   1522   -463    675       C  
ATOM   1981  O   PHE A1067      -0.463  11.283 -41.742  1.00 50.55           O  
ANISOU 1981  O   PHE A1067     7110   6281   5815   1386   -634    743       O  
ATOM   1982  CB  PHE A1067       0.137  11.385 -38.462  1.00 46.93           C  
ANISOU 1982  CB  PHE A1067     6806   5715   5310   1220    -60    566       C  
ATOM   1983  CG  PHE A1067      -0.004   9.926 -38.802  1.00 47.15           C  
ANISOU 1983  CG  PHE A1067     6650   5914   5352   1026   -125    578       C  
ATOM   1984  CD1 PHE A1067       0.904   9.300 -39.623  1.00 48.08           C  
ANISOU 1984  CD1 PHE A1067     6858   6012   5397    893   -275    646       C  
ATOM   1985  CD2 PHE A1067      -1.036   9.176 -38.269  1.00 50.45           C  
ANISOU 1985  CD2 PHE A1067     6823   6490   5855    948     14    492       C  
ATOM   1986  CE1 PHE A1067       0.773   7.958 -39.919  1.00 48.37           C  
ANISOU 1986  CE1 PHE A1067     6773   6160   5444    720   -309    645       C  
ATOM   1987  CE2 PHE A1067      -1.168   7.831 -38.562  1.00 52.53           C  
ANISOU 1987  CE2 PHE A1067     6981   6875   6104    735    -24    497       C  
ATOM   1988  CZ  PHE A1067      -0.268   7.224 -39.386  1.00 48.54           C  
ANISOU 1988  CZ  PHE A1067     6597   6324   5523    637   -195    582       C  
ATOM   1989  N   ASN A1068      -2.086  12.230 -40.496  1.00 51.71           N  
ANISOU 1989  N   ASN A1068     6924   6471   6254   1754   -445    601       N  
ATOM   1990  CA  ASN A1068      -3.138  11.883 -41.451  1.00 54.12           C  
ANISOU 1990  CA  ASN A1068     6890   6960   6712   1867   -700    611       C  
ATOM   1991  C   ASN A1068      -2.917  12.466 -42.852  1.00 59.15           C  
ANISOU 1991  C   ASN A1068     7770   7469   7235   1992  -1064    766       C  
ATOM   1992  O   ASN A1068      -3.376  11.892 -43.841  1.00 60.13           O  
ANISOU 1992  O   ASN A1068     7754   7736   7355   1940  -1333    812       O  
ATOM   1993  CB  ASN A1068      -4.521  12.276 -40.921  1.00 60.75           C  
ANISOU 1993  CB  ASN A1068     7293   7915   7872   2136   -619    460       C  
ATOM   1994  CG  ASN A1068      -5.129  11.203 -40.008  1.00 92.20           C  
ANISOU 1994  CG  ASN A1068    10931  12137  11962   1887   -318    284       C  
ATOM   1995  OD1 ASN A1068      -6.291  10.803 -40.186  1.00 92.22           O  
ANISOU 1995  OD1 ASN A1068    10447  12382  12212   1925   -356    159       O  
ATOM   1996  ND2 ASN A1068      -4.341  10.726 -39.029  1.00 82.59           N  
ANISOU 1996  ND2 ASN A1068     9985  10846  10548   1605    -33    268       N  
ATOM   1997  N   GLN A1069      -2.218  13.597 -42.933  1.00 55.32           N  
ANISOU 1997  N   GLN A1069     7705   6698   6616   2112  -1065    840       N  
ATOM   1998  CA  GLN A1069      -1.796  14.153 -44.220  1.00 55.83           C  
ANISOU 1998  CA  GLN A1069     8166   6575   6473   2134  -1350    990       C  
ATOM   1999  C   GLN A1069      -0.752  13.244 -44.852  1.00 56.51           C  
ANISOU 1999  C   GLN A1069     8443   6700   6329   1732  -1317   1018       C  
ATOM   2000  O   GLN A1069      -0.915  12.787 -45.979  1.00 56.88           O  
ANISOU 2000  O   GLN A1069     8544   6801   6265   1626  -1552   1085       O  
ATOM   2001  CB  GLN A1069      -1.208  15.556 -44.044  1.00 57.95           C  
ANISOU 2001  CB  GLN A1069     8902   6496   6621   2281  -1278   1035       C  
ATOM   2002  CG  GLN A1069      -2.214  16.603 -43.577  1.00 74.60           C  
ANISOU 2002  CG  GLN A1069    10902   8477   8964   2737  -1321   1005       C  
ATOM   2003  CD  GLN A1069      -1.556  17.810 -42.925  1.00 90.36           C  
ANISOU 2003  CD  GLN A1069    13336  10141  10854   2806  -1088    987       C  
ATOM   2004  OE1 GLN A1069      -0.393  18.118 -43.185  1.00 83.51           O  
ANISOU 2004  OE1 GLN A1069    12933   9093   9702   2545  -1009   1038       O  
ATOM   2005  NE2 GLN A1069      -2.304  18.501 -42.072  1.00 83.48           N  
ANISOU 2005  NE2 GLN A1069    12311   9185  10223   3134   -946    883       N  
ATOM   2006  N   ASP A1070       0.313  12.968 -44.108  1.00 50.21           N  
ANISOU 2006  N   ASP A1070     7737   5869   5470   1511  -1031    950       N  
ATOM   2007  CA  ASP A1070       1.418  12.165 -44.623  1.00 47.80           C  
ANISOU 2007  CA  ASP A1070     7572   5571   5019   1173   -960    933       C  
ATOM   2008  C   ASP A1070       0.924  10.843 -45.172  1.00 50.73           C  
ANISOU 2008  C   ASP A1070     7689   6158   5429   1031  -1058    923       C  
ATOM   2009  O   ASP A1070       1.480  10.330 -46.145  1.00 49.52           O  
ANISOU 2009  O   ASP A1070     7704   5978   5133    806  -1091    927       O  
ATOM   2010  CB  ASP A1070       2.476  11.915 -43.540  1.00 47.29           C  
ANISOU 2010  CB  ASP A1070     7504   5484   4978   1018   -703    841       C  
ATOM   2011  CG  ASP A1070       3.232  13.182 -43.149  1.00 58.89           C  
ANISOU 2011  CG  ASP A1070     9291   6732   6355   1043   -592    827       C  
ATOM   2012  OD1 ASP A1070       3.157  14.179 -43.906  1.00 61.73           O  
ANISOU 2012  OD1 ASP A1070     9960   6908   6588   1126   -680    892       O  
ATOM   2013  OD2 ASP A1070       3.898  13.177 -42.085  1.00 62.79           O  
ANISOU 2013  OD2 ASP A1070     9766   7215   6876    960   -437    754       O  
ATOM   2014  N   VAL A1071      -0.121  10.303 -44.554  1.00 47.43           N  
ANISOU 2014  N   VAL A1071     6888   5940   5193   1126  -1065    883       N  
ATOM   2015  CA  VAL A1071      -0.718   9.060 -45.025  1.00 47.37           C  
ANISOU 2015  CA  VAL A1071     6639   6142   5218    961  -1150    856       C  
ATOM   2016  C   VAL A1071      -1.421   9.271 -46.367  1.00 54.06           C  
ANISOU 2016  C   VAL A1071     7527   7026   5985   1009  -1494    935       C  
ATOM   2017  O   VAL A1071      -1.309   8.450 -47.275  1.00 53.65           O  
ANISOU 2017  O   VAL A1071     7556   7029   5802    766  -1582    941       O  
ATOM   2018  CB  VAL A1071      -1.695   8.478 -43.991  1.00 51.74           C  
ANISOU 2018  CB  VAL A1071     6787   6899   5974    990  -1026    761       C  
ATOM   2019  CG1 VAL A1071      -2.227   7.118 -44.455  1.00 51.90           C  
ANISOU 2019  CG1 VAL A1071     6604   7119   5999    743  -1074    715       C  
ATOM   2020  CG2 VAL A1071      -1.008   8.355 -42.629  1.00 49.30           C  
ANISOU 2020  CG2 VAL A1071     6552   6508   5672    928   -732    707       C  
ATOM   2021  N   ASP A1072      -2.132  10.380 -46.497  1.00 53.62           N  
ANISOU 2021  N   ASP A1072     7459   6914   6001   1326  -1708    996       N  
ATOM   2022  CA  ASP A1072      -2.728  10.753 -47.774  1.00 56.76           C  
ANISOU 2022  CA  ASP A1072     7989   7288   6289   1414  -2130   1107       C  
ATOM   2023  C   ASP A1072      -1.666  10.904 -48.862  1.00 59.15           C  
ANISOU 2023  C   ASP A1072     8883   7361   6230   1166  -2164   1195       C  
ATOM   2024  O   ASP A1072      -1.773  10.303 -49.929  1.00 59.80           O  
ANISOU 2024  O   ASP A1072     9103   7492   6126    940  -2354   1227       O  
ATOM   2025  CB  ASP A1072      -3.523  12.056 -47.624  1.00 62.60           C  
ANISOU 2025  CB  ASP A1072     8676   7918   7189   1871  -2361   1164       C  
ATOM   2026  CG  ASP A1072      -4.906  11.833 -47.035  1.00 78.67           C  
ANISOU 2026  CG  ASP A1072    10052  10230   9609   2106  -2439   1046       C  
ATOM   2027  OD1 ASP A1072      -5.041  10.946 -46.166  1.00 77.85           O  
ANISOU 2027  OD1 ASP A1072     9595  10338   9648   1926  -2123    899       O  
ATOM   2028  OD2 ASP A1072      -5.853  12.547 -47.433  1.00 90.15           O  
ANISOU 2028  OD2 ASP A1072    11347  11676  11231   2466  -2812   1088       O  
ATOM   2029  N   ALA A1073      -0.639  11.702 -48.583  1.00 54.16           N  
ANISOU 2029  N   ALA A1073     8612   6479   5488   1162  -1946   1205       N  
ATOM   2030  CA  ALA A1073       0.458  11.897 -49.529  1.00 53.79           C  
ANISOU 2030  CA  ALA A1073     9118   6207   5114    870  -1871   1232       C  
ATOM   2031  C   ALA A1073       1.051  10.555 -49.907  1.00 55.89           C  
ANISOU 2031  C   ALA A1073     9318   6595   5321    492  -1681   1124       C  
ATOM   2032  O   ALA A1073       1.412  10.333 -51.056  1.00 56.18           O  
ANISOU 2032  O   ALA A1073     9717   6537   5090    218  -1720   1132       O  
ATOM   2033  CB  ALA A1073       1.527  12.788 -48.940  1.00 53.13           C  
ANISOU 2033  CB  ALA A1073     9303   5897   4986    859  -1581   1193       C  
ATOM   2034  N   ALA A1074       1.139   9.656 -48.933  1.00 50.72           N  
ANISOU 2034  N   ALA A1074     8252   6119   4903    469  -1465   1018       N  
ATOM   2035  CA  ALA A1074       1.618   8.303 -49.194  1.00 48.93           C  
ANISOU 2035  CA  ALA A1074     7945   5976   4668    168  -1294    911       C  
ATOM   2036  C   ALA A1074       0.691   7.584 -50.164  1.00 54.52           C  
ANISOU 2036  C   ALA A1074     8624   6823   5268     37  -1548    944       C  
ATOM   2037  O   ALA A1074       1.175   6.978 -51.115  1.00 55.07           O  
ANISOU 2037  O   ALA A1074     8952   6828   5144   -267  -1481    893       O  
ATOM   2038  CB  ALA A1074       1.769   7.514 -47.902  1.00 47.28           C  
ANISOU 2038  CB  ALA A1074     7371   5885   4708    205  -1082    825       C  
ATOM   2039  N   VAL A1075      -0.626   7.658 -49.954  1.00 52.21           N  
ANISOU 2039  N   VAL A1075     8013   6720   5104    241  -1826   1001       N  
ATOM   2040  CA  VAL A1075      -1.564   7.018 -50.891  1.00 54.54           C  
ANISOU 2040  CA  VAL A1075     8243   7178   5300     96  -2132   1021       C  
ATOM   2041  C   VAL A1075      -1.374   7.593 -52.284  1.00 60.78           C  
ANISOU 2041  C   VAL A1075     9574   7785   5736    -26  -2393   1127       C  
ATOM   2042  O   VAL A1075      -1.100   6.857 -53.228  1.00 60.32           O  
ANISOU 2042  O   VAL A1075     9784   7700   5434   -381  -2376   1087       O  
ATOM   2043  CB  VAL A1075      -3.040   7.193 -50.493  1.00 60.93           C  
ANISOU 2043  CB  VAL A1075     8559   8236   6355    361  -2431   1036       C  
ATOM   2044  CG1 VAL A1075      -3.954   6.815 -51.653  1.00 64.58           C  
ANISOU 2044  CG1 VAL A1075     9011   8846   6679    221  -2866   1075       C  
ATOM   2045  CG2 VAL A1075      -3.365   6.361 -49.274  1.00 58.97           C  
ANISOU 2045  CG2 VAL A1075     7838   8185   6382    337  -2140    900       C  
ATOM   2046  N   ARG A1076      -1.508   8.913 -52.392  1.00 60.01           N  
ANISOU 2046  N   ARG A1076     9698   7521   5582    250  -2615   1257       N  
ATOM   2047  CA  ARG A1076      -1.364   9.609 -53.667  1.00 63.61           C  
ANISOU 2047  CA  ARG A1076    10785   7738   5646    145  -2899   1389       C  
ATOM   2048  C   ARG A1076      -0.045   9.245 -54.359  1.00 66.68           C  
ANISOU 2048  C   ARG A1076    11689   7925   5720   -310  -2521   1297       C  
ATOM   2049  O   ARG A1076      -0.034   8.896 -55.546  1.00 68.77           O  
ANISOU 2049  O   ARG A1076    12371   8119   5637   -637  -2651   1313       O  
ATOM   2050  CB  ARG A1076      -1.437  11.126 -53.454  1.00 66.59           C  
ANISOU 2050  CB  ARG A1076    11403   7876   6021    517  -3073   1527       C  
ATOM   2051  CG  ARG A1076      -2.829  11.676 -53.097  1.00 83.29           C  
ANISOU 2051  CG  ARG A1076    13099  10123   8426   1007  -3531   1617       C  
ATOM   2052  CD  ARG A1076      -2.719  13.129 -52.570  1.00 97.61           C  
ANISOU 2052  CD  ARG A1076    15118  11655  10315   1406  -3543   1704       C  
ATOM   2053  NE  ARG A1076      -4.010  13.826 -52.473  1.00113.60           N  
ANISOU 2053  NE  ARG A1076    16850  13712  12602   1921  -4031   1793       N  
ATOM   2054  CZ  ARG A1076      -4.905  13.661 -51.494  1.00128.50           C  
ANISOU 2054  CZ  ARG A1076    17992  15865  14965   2233  -4002   1673       C  
ATOM   2055  NH1 ARG A1076      -4.689  12.801 -50.506  1.00111.95           N  
ANISOU 2055  NH1 ARG A1076    15440  14015  13079   2058  -3531   1490       N  
ATOM   2056  NH2 ARG A1076      -6.038  14.354 -51.507  1.00119.78           N  
ANISOU 2056  NH2 ARG A1076    16609  14766  14136   2722  -4447   1723       N  
ATOM   2057  N   GLY A1077       1.051   9.312 -53.600  1.00 60.22           N  
ANISOU 2057  N   GLY A1077    10819   7021   5040   -342  -2050   1176       N  
ATOM   2058  CA  GLY A1077       2.393   9.025 -54.112  1.00 59.43           C  
ANISOU 2058  CA  GLY A1077    11084   6743   4755   -737  -1624   1025       C  
ATOM   2059  C   GLY A1077       2.465   7.707 -54.853  1.00 64.79           C  
ANISOU 2059  C   GLY A1077    11787   7503   5327  -1099  -1512    904       C  
ATOM   2060  O   GLY A1077       3.120   7.607 -55.893  1.00 66.55           O  
ANISOU 2060  O   GLY A1077    12509   7544   5234  -1478  -1334    822       O  
ATOM   2061  N   ILE A1078       1.766   6.705 -54.322  1.00 60.24           N  
ANISOU 2061  N   ILE A1078    10714   7181   4994  -1015  -1586    877       N  
ATOM   2062  CA  ILE A1078       1.712   5.373 -54.918  1.00 60.49           C  
ANISOU 2062  CA  ILE A1078    10750   7288   4946  -1346  -1484    757       C  
ATOM   2063  C   ILE A1078       0.905   5.354 -56.216  1.00 69.00           C  
ANISOU 2063  C   ILE A1078    12207   8370   5638  -1573  -1877    854       C  
ATOM   2064  O   ILE A1078       1.318   4.723 -57.192  1.00 70.31           O  
ANISOU 2064  O   ILE A1078    12764   8427   5524  -1985  -1712    746       O  
ATOM   2065  CB  ILE A1078       1.095   4.349 -53.949  1.00 61.56           C  
ANISOU 2065  CB  ILE A1078    10307   7669   5412  -1222  -1467    710       C  
ATOM   2066  CG1 ILE A1078       1.984   4.158 -52.720  1.00 58.23           C  
ANISOU 2066  CG1 ILE A1078     9603   7208   5315  -1061  -1100    613       C  
ATOM   2067  CG2 ILE A1078       0.918   3.011 -54.634  1.00 63.70           C  
ANISOU 2067  CG2 ILE A1078    10651   7990   5564  -1581  -1392    596       C  
ATOM   2068  CD1 ILE A1078       1.329   3.356 -51.634  1.00 63.08           C  
ANISOU 2068  CD1 ILE A1078     9751   8016   6202   -927  -1103    601       C  
ATOM   2069  N   LEU A1079      -0.237   6.039 -56.230  1.00 68.21           N  
ANISOU 2069  N   LEU A1079    11999   8388   5532  -1305  -2405   1042       N  
ATOM   2070  CA  LEU A1079      -1.111   6.050 -57.413  1.00 73.01           C  
ANISOU 2070  CA  LEU A1079    12927   9023   5791  -1477  -2915   1157       C  
ATOM   2071  C   LEU A1079      -0.492   6.825 -58.582  1.00 80.89           C  
ANISOU 2071  C   LEU A1079    14774   9681   6280  -1730  -2964   1235       C  
ATOM   2072  O   LEU A1079      -0.832   6.596 -59.749  1.00 84.22           O  
ANISOU 2072  O   LEU A1079    15670  10047   6284  -2057  -3249   1283       O  
ATOM   2073  CB  LEU A1079      -2.489   6.629 -57.071  1.00 75.48           C  
ANISOU 2073  CB  LEU A1079    12819   9548   6312  -1056  -3508   1317       C  
ATOM   2074  CG  LEU A1079      -3.276   5.972 -55.933  1.00 78.26           C  
ANISOU 2074  CG  LEU A1079    12346  10245   7145   -841  -3464   1223       C  
ATOM   2075  CD1 LEU A1079      -4.710   6.482 -55.934  1.00 82.59           C  
ANISOU 2075  CD1 LEU A1079    12497  11012   7872   -509  -4082   1329       C  
ATOM   2076  CD2 LEU A1079      -3.243   4.450 -56.030  1.00 79.83           C  
ANISOU 2076  CD2 LEU A1079    12402  10598   7333  -1247  -3201   1050       C  
ATOM   2077  N   ARG A1080       0.411   7.747 -58.259  1.00 76.59           N  
ANISOU 2077  N   ARG A1080    14464   8900   5739  -1623  -2679   1238       N  
ATOM   2078  CA  ARG A1080       1.192   8.436 -59.281  1.00 79.19           C  
ANISOU 2078  CA  ARG A1080    15642   8871   5576  -1953  -2563   1257       C  
ATOM   2079  C   ARG A1080       2.383   7.597 -59.735  1.00 81.44           C  
ANISOU 2079  C   ARG A1080    16164   9044   5735  -2464  -1912    979       C  
ATOM   2080  O   ARG A1080       2.937   7.852 -60.808  1.00 84.53           O  
ANISOU 2080  O   ARG A1080    17302   9164   5652  -2893  -1761    935       O  
ATOM   2081  CB  ARG A1080       1.682   9.798 -58.781  1.00 79.43           C  
ANISOU 2081  CB  ARG A1080    15860   8675   5645  -1689  -2489   1343       C  
ATOM   2082  CG  ARG A1080       0.566  10.788 -58.504  1.00 92.52           C  
ANISOU 2082  CG  ARG A1080    17431  10339   7385  -1177  -3120   1609       C  
ATOM   2083  CD  ARG A1080       1.069  12.209 -58.632  1.00106.37           C  
ANISOU 2083  CD  ARG A1080    19807  11710   8899  -1097  -3112   1726       C  
ATOM   2084  NE  ARG A1080       0.253  13.162 -57.884  1.00117.23           N  
ANISOU 2084  NE  ARG A1080    20905  13082  10555   -493  -3511   1905       N  
ATOM   2085  CZ  ARG A1080       0.266  13.294 -56.557  1.00129.41           C  
ANISOU 2085  CZ  ARG A1080    21802  14782  12587   -137  -3284   1827       C  
ATOM   2086  NH1 ARG A1080       1.041  12.516 -55.797  1.00113.15           N  
ANISOU 2086  NH1 ARG A1080    19299  12904  10788   -301  -2734   1604       N  
ATOM   2087  NH2 ARG A1080      -0.513  14.207 -55.978  1.00118.35           N  
ANISOU 2087  NH2 ARG A1080    20218  13334  11414    394  -3625   1968       N  
ATOM   2088  N   ASN A1081       2.796   6.620 -58.926  1.00 73.03           N  
ANISOU 2088  N   ASN A1081    14502   8155   5090  -2421  -1513    781       N  
ATOM   2089  CA  ASN A1081       3.866   5.715 -59.340  1.00 71.92           C  
ANISOU 2089  CA  ASN A1081    14500   7907   4919  -2838   -914    489       C  
ATOM   2090  C   ASN A1081       3.339   4.665 -60.317  1.00 78.52           C  
ANISOU 2090  C   ASN A1081    15584   8784   5467  -3216  -1015    436       C  
ATOM   2091  O   ASN A1081       2.294   4.050 -60.087  1.00 77.70           O  
ANISOU 2091  O   ASN A1081    15122   8925   5476  -3085  -1382    529       O  
ATOM   2092  CB  ASN A1081       4.560   5.055 -58.145  1.00 65.64           C  
ANISOU 2092  CB  ASN A1081    13039   7226   4676  -2625   -503    304       C  
ATOM   2093  CG  ASN A1081       5.956   4.541 -58.491  1.00 79.17           C  
ANISOU 2093  CG  ASN A1081    14885   8754   6441  -2959    155    -24       C  
ATOM   2094  OD1 ASN A1081       6.108   3.609 -59.278  1.00 72.56           O  
ANISOU 2094  OD1 ASN A1081    14266   7849   5455  -3311    382   -195       O  
ATOM   2095  ND2 ASN A1081       6.980   5.152 -57.903  1.00 68.44           N  
ANISOU 2095  ND2 ASN A1081    13376   7313   5317  -2858    473   -141       N  
ATOM   2096  N   ALA A1082       4.083   4.482 -61.407  1.00 78.12           N  
ANISOU 2096  N   ALA A1082    16164   8486   5030  -3729   -649    258       N  
ATOM   2097  CA  ALA A1082       3.713   3.576 -62.486  1.00 81.31           C  
ANISOU 2097  CA  ALA A1082    16978   8861   5055  -4190   -684    181       C  
ATOM   2098  C   ALA A1082       4.016   2.109 -62.155  1.00 83.45           C  
ANISOU 2098  C   ALA A1082    16825   9221   5662  -4277   -257    -81       C  
ATOM   2099  O   ALA A1082       3.587   1.214 -62.889  1.00 85.84           O  
ANISOU 2099  O   ALA A1082    17376   9530   5708  -4629   -293   -153       O  
ATOM   2100  CB  ALA A1082       4.426   3.988 -63.769  1.00 86.45           C  
ANISOU 2100  CB  ALA A1082    18552   9169   5125  -4751   -388     65       C  
ATOM   2101  N   LYS A1083       4.752   1.870 -61.064  1.00 75.65           N  
ANISOU 2101  N   LYS A1083    15249   8272   5223  -3965    118   -218       N  
ATOM   2102  CA  LYS A1083       5.075   0.511 -60.593  1.00 73.52           C  
ANISOU 2102  CA  LYS A1083    14570   8037   5327  -3949    481   -440       C  
ATOM   2103  C   LYS A1083       4.189   0.064 -59.439  1.00 74.06           C  
ANISOU 2103  C   LYS A1083    13999   8381   5761  -3540    134   -278       C  
ATOM   2104  O   LYS A1083       3.778  -1.092 -59.376  1.00 74.34           O  
ANISOU 2104  O   LYS A1083    13896   8478   5870  -3637    165   -351       O  
ATOM   2105  CB  LYS A1083       6.533   0.430 -60.118  1.00 74.48           C  
ANISOU 2105  CB  LYS A1083    14458   7995   5845  -3864   1098   -719       C  
ATOM   2106  CG  LYS A1083       7.589   0.343 -61.236  1.00 92.27           C  
ANISOU 2106  CG  LYS A1083    17235   9959   7864  -4358   1692  -1045       C  
ATOM   2107  CD  LYS A1083       8.692  -0.681 -60.900  1.00102.44           C  
ANISOU 2107  CD  LYS A1083    18154  11120   9647  -4316   2302  -1417       C  
ATOM   2108  CE  LYS A1083       8.124  -2.126 -60.839  1.00113.94           C  
ANISOU 2108  CE  LYS A1083    19490  12598  11204  -4320   2271  -1458       C  
ATOM   2109  NZ  LYS A1083       9.145  -3.180 -60.542  1.00123.15           N  
ANISOU 2109  NZ  LYS A1083    20349  13580  12864  -4226   2818  -1807       N  
ATOM   2110  N   LEU A1084       3.922   0.980 -58.514  1.00 67.15           N  
ANISOU 2110  N   LEU A1084    12774   7643   5098  -3118   -146    -81       N  
ATOM   2111  CA  LEU A1084       3.232   0.650 -57.268  1.00 63.57           C  
ANISOU 2111  CA  LEU A1084    11712   7423   5018  -2740   -364     32       C  
ATOM   2112  C   LEU A1084       1.704   0.675 -57.377  1.00 68.23           C  
ANISOU 2112  C   LEU A1084    12188   8270   5467  -2709   -921    229       C  
ATOM   2113  O   LEU A1084       1.027   0.112 -56.524  1.00 66.60           O  
ANISOU 2113  O   LEU A1084    11524   8260   5519  -2541  -1025    257       O  
ATOM   2114  CB  LEU A1084       3.687   1.605 -56.158  1.00 60.52           C  
ANISOU 2114  CB  LEU A1084    11004   7054   4936  -2326   -350    111       C  
ATOM   2115  CG  LEU A1084       5.199   1.653 -55.904  1.00 63.71           C  
ANISOU 2115  CG  LEU A1084    11392   7257   5558  -2323    144   -100       C  
ATOM   2116  CD1 LEU A1084       5.550   2.836 -55.034  1.00 61.86           C  
ANISOU 2116  CD1 LEU A1084    10970   7041   5494  -2005     80     -2       C  
ATOM   2117  CD2 LEU A1084       5.700   0.358 -55.272  1.00 64.26           C  
ANISOU 2117  CD2 LEU A1084    11141   7292   5984  -2261    432   -275       C  
ATOM   2118  N   LYS A1085       1.165   1.320 -58.412  1.00 67.44           N  
ANISOU 2118  N   LYS A1085    12501   8160   4962  -2882  -1286    352       N  
ATOM   2119  CA  LYS A1085      -0.289   1.433 -58.570  1.00 69.25           C  
ANISOU 2119  CA  LYS A1085    12561   8648   5102  -2818  -1894    525       C  
ATOM   2120  C   LYS A1085      -0.971   0.081 -58.843  1.00 74.05           C  
ANISOU 2120  C   LYS A1085    13058   9415   5662  -3138  -1925    416       C  
ATOM   2121  O   LYS A1085      -1.942  -0.264 -58.158  1.00 73.14           O  
ANISOU 2121  O   LYS A1085    12421   9576   5792  -2986  -2153    450       O  
ATOM   2122  CB  LYS A1085      -0.642   2.453 -59.661  1.00 75.41           C  
ANISOU 2122  CB  LYS A1085    13881   9332   5438  -2912  -2353    699       C  
ATOM   2123  CG  LYS A1085      -2.120   2.838 -59.712  1.00 90.12           C  
ANISOU 2123  CG  LYS A1085    15469  11464   7311  -2702  -3081    894       C  
ATOM   2124  CD  LYS A1085      -2.422   3.753 -60.897  1.00102.87           C  
ANISOU 2124  CD  LYS A1085    17732  12920   8434  -2809  -3605   1083       C  
ATOM   2125  CE  LYS A1085      -3.818   4.359 -60.810  1.00114.35           C  
ANISOU 2125  CE  LYS A1085    18816  14615  10015  -2444  -4386   1284       C  
ATOM   2126  NZ  LYS A1085      -4.890   3.322 -60.877  1.00124.63           N  
ANISOU 2126  NZ  LYS A1085    19656  16276  11423  -2617  -4668   1201       N  
ATOM   2127  N   PRO A1086      -0.463  -0.693 -59.830  1.00 71.93           N  
ANISOU 2127  N   PRO A1086    13295   8960   5074  -3615  -1650    254       N  
ATOM   2128  CA  PRO A1086      -1.078  -1.994 -60.139  1.00 73.09           C  
ANISOU 2128  CA  PRO A1086    13418   9218   5134  -3971  -1650    133       C  
ATOM   2129  C   PRO A1086      -1.014  -2.975 -58.968  1.00 72.84           C  
ANISOU 2129  C   PRO A1086    12884   9252   5540  -3817  -1316     18       C  
ATOM   2130  O   PRO A1086      -1.880  -3.845 -58.833  1.00 74.01           O  
ANISOU 2130  O   PRO A1086    12824   9585   5713  -3993  -1435    -26       O  
ATOM   2131  CB  PRO A1086      -0.239  -2.519 -61.314  1.00 77.05           C  
ANISOU 2131  CB  PRO A1086    14619   9413   5243  -4474  -1261    -57       C  
ATOM   2132  CG  PRO A1086       0.507  -1.348 -61.832  1.00 82.08           C  
ANISOU 2132  CG  PRO A1086    15691   9837   5658  -4444  -1218      6       C  
ATOM   2133  CD  PRO A1086       0.730  -0.456 -60.662  1.00 74.03           C  
ANISOU 2133  CD  PRO A1086    14176   8889   5061  -3884  -1248    132       C  
ATOM   2134  N   VAL A1087       0.012  -2.831 -58.134  1.00 64.24           N  
ANISOU 2134  N   VAL A1087    11638   7998   4771  -3518   -917    -33       N  
ATOM   2135  CA  VAL A1087       0.145  -3.645 -56.934  1.00 60.51           C  
ANISOU 2135  CA  VAL A1087    10763   7536   4690  -3324   -657   -102       C  
ATOM   2136  C   VAL A1087      -0.967  -3.233 -55.982  1.00 61.74           C  
ANISOU 2136  C   VAL A1087    10395   8012   5051  -3046  -1025     56       C  
ATOM   2137  O   VAL A1087      -1.753  -4.058 -55.545  1.00 61.92           O  
ANISOU 2137  O   VAL A1087    10177   8190   5158  -3159  -1059     16       O  
ATOM   2138  CB  VAL A1087       1.520  -3.438 -56.234  1.00 61.23           C  
ANISOU 2138  CB  VAL A1087    10788   7391   5086  -3029   -250   -175       C  
ATOM   2139  CG1 VAL A1087       1.840  -4.614 -55.342  1.00 59.59           C  
ANISOU 2139  CG1 VAL A1087    10393   7070   5177  -2949     43   -285       C  
ATOM   2140  CG2 VAL A1087       2.642  -3.236 -57.255  1.00 62.34           C  
ANISOU 2140  CG2 VAL A1087    11384   7257   5044  -3243     75   -331       C  
ATOM   2141  N   TYR A1088      -1.039  -1.936 -55.709  1.00 56.21           N  
ANISOU 2141  N   TYR A1088     9549   7390   4418  -2715  -1267    210       N  
ATOM   2142  CA  TYR A1088      -1.951  -1.380 -54.717  1.00 54.82           C  
ANISOU 2142  CA  TYR A1088     8858   7475   4497  -2386  -1535    326       C  
ATOM   2143  C   TYR A1088      -3.414  -1.572 -55.093  1.00 61.36           C  
ANISOU 2143  C   TYR A1088     9448   8618   5249  -2544  -1963    349       C  
ATOM   2144  O   TYR A1088      -4.265  -1.741 -54.220  1.00 60.42           O  
ANISOU 2144  O   TYR A1088     8841   8735   5382  -2431  -2026    332       O  
ATOM   2145  CB  TYR A1088      -1.648   0.109 -54.528  1.00 55.08           C  
ANISOU 2145  CB  TYR A1088     8890   7460   4578  -2017  -1689    470       C  
ATOM   2146  CG  TYR A1088      -2.525   0.803 -53.516  1.00 56.93           C  
ANISOU 2146  CG  TYR A1088     8619   7919   5093  -1647  -1915    563       C  
ATOM   2147  CD1 TYR A1088      -2.118   0.953 -52.197  1.00 55.50           C  
ANISOU 2147  CD1 TYR A1088     8183   7704   5200  -1377  -1650    552       C  
ATOM   2148  CD2 TYR A1088      -3.763   1.318 -53.883  1.00 61.61           C  
ANISOU 2148  CD2 TYR A1088     8991   8749   5671  -1566  -2400    644       C  
ATOM   2149  CE1 TYR A1088      -2.925   1.587 -51.265  1.00 56.20           C  
ANISOU 2149  CE1 TYR A1088     7847   7977   5530  -1075  -1786    601       C  
ATOM   2150  CE2 TYR A1088      -4.578   1.954 -52.962  1.00 63.12           C  
ANISOU 2150  CE2 TYR A1088     8675   9134   6173  -1212  -2552    679       C  
ATOM   2151  CZ  TYR A1088      -4.155   2.086 -51.656  1.00 66.94           C  
ANISOU 2151  CZ  TYR A1088     8951   9567   6915   -985  -2206    648       C  
ATOM   2152  OH  TYR A1088      -4.978   2.719 -50.754  1.00 69.51           O  
ANISOU 2152  OH  TYR A1088     8810  10067   7533   -671  -2295    649       O  
ATOM   2153  N   ASP A1089      -3.715  -1.534 -56.383  1.00 61.61           N  
ANISOU 2153  N   ASP A1089     9821   8658   4931  -2829  -2259    370       N  
ATOM   2154  CA  ASP A1089      -5.082  -1.784 -56.822  1.00 65.86           C  
ANISOU 2154  CA  ASP A1089    10113   9512   5397  -3016  -2726    370       C  
ATOM   2155  C   ASP A1089      -5.502  -3.218 -56.501  1.00 70.40           C  
ANISOU 2155  C   ASP A1089    10511  10201   6035  -3371  -2478    189       C  
ATOM   2156  O   ASP A1089      -6.600  -3.438 -55.988  1.00 72.37           O  
ANISOU 2156  O   ASP A1089    10241  10766   6490  -3378  -2658    141       O  
ATOM   2157  CB  ASP A1089      -5.244  -1.482 -58.309  1.00 72.03           C  
ANISOU 2157  CB  ASP A1089    11403  10242   5722  -3292  -3139    441       C  
ATOM   2158  CG  ASP A1089      -5.117  -0.001 -58.616  1.00 83.98           C  
ANISOU 2158  CG  ASP A1089    13100  11656   7153  -2941  -3498    646       C  
ATOM   2159  OD1 ASP A1089      -5.572   0.825 -57.800  1.00 83.77           O  
ANISOU 2159  OD1 ASP A1089    12602  11763   7463  -2475  -3685    738       O  
ATOM   2160  OD2 ASP A1089      -4.563   0.342 -59.679  1.00 91.89           O  
ANISOU 2160  OD2 ASP A1089    14768  12415   7733  -3153  -3566    704       O  
ATOM   2161  N   SER A1090      -4.615  -4.181 -56.758  1.00 64.80           N  
ANISOU 2161  N   SER A1090    10229   9215   5176  -3661  -2027     67       N  
ATOM   2162  CA  SER A1090      -4.914  -5.603 -56.524  1.00 64.77           C  
ANISOU 2162  CA  SER A1090    10202   9227   5182  -4027  -1756   -104       C  
ATOM   2163  C   SER A1090      -4.687  -6.049 -55.077  1.00 64.26           C  
ANISOU 2163  C   SER A1090     9842   9105   5468  -3805  -1378   -142       C  
ATOM   2164  O   SER A1090      -4.708  -7.255 -54.792  1.00 64.33           O  
ANISOU 2164  O   SER A1090     9956   9014   5474  -4080  -1078   -272       O  
ATOM   2165  CB  SER A1090      -4.072  -6.486 -57.446  1.00 68.77           C  
ANISOU 2165  CB  SER A1090    11341   9404   5385  -4418  -1422   -237       C  
ATOM   2166  OG  SER A1090      -2.773  -6.687 -56.911  1.00 72.92           O  
ANISOU 2166  OG  SER A1090    12031   9583   6091  -4195   -924   -286       O  
ATOM   2167  N   LEU A1091      -4.450  -5.092 -54.179  1.00 56.78           N  
ANISOU 2167  N   LEU A1091     8606   8183   4785  -3334  -1394    -26       N  
ATOM   2168  CA  LEU A1091      -4.329  -5.375 -52.752  1.00 53.32           C  
ANISOU 2168  CA  LEU A1091     7917   7706   4635  -3130  -1106    -40       C  
ATOM   2169  C   LEU A1091      -5.604  -4.987 -52.025  1.00 59.12           C  
ANISOU 2169  C   LEU A1091     8085   8808   5569  -3045  -1314    -39       C  
ATOM   2170  O   LEU A1091      -6.459  -4.297 -52.574  1.00 61.95           O  
ANISOU 2170  O   LEU A1091     8175   9443   5922  -3011  -1723     -8       O  
ATOM   2171  CB  LEU A1091      -3.148  -4.623 -52.148  1.00 49.17           C  
ANISOU 2171  CB  LEU A1091     7472   6947   4265  -2706   -938     54       C  
ATOM   2172  CG  LEU A1091      -1.752  -5.191 -52.375  1.00 51.71           C  
ANISOU 2172  CG  LEU A1091     8211   6884   4553  -2727   -593    -10       C  
ATOM   2173  CD1 LEU A1091      -0.791  -4.519 -51.400  1.00 48.67           C  
ANISOU 2173  CD1 LEU A1091     7736   6351   4407  -2306   -462     61       C  
ATOM   2174  CD2 LEU A1091      -1.720  -6.705 -52.214  1.00 54.41           C  
ANISOU 2174  CD2 LEU A1091     8750   7053   4869  -3016   -312   -141       C  
ATOM   2175  N   ASP A1092      -5.717  -5.489 -50.802  1.00 54.49           N  
ANISOU 2175  N   ASP A1092     7345   8201   5158  -3028  -1021    -92       N  
ATOM   2176  CA  ASP A1092      -6.890  -5.276 -49.986  1.00 56.42           C  
ANISOU 2176  CA  ASP A1092     7062   8768   5608  -3018  -1072   -158       C  
ATOM   2177  C   ASP A1092      -6.599  -4.260 -48.899  1.00 58.61           C  
ANISOU 2177  C   ASP A1092     7143   9013   6114  -2559   -998    -67       C  
ATOM   2178  O   ASP A1092      -5.447  -3.942 -48.603  1.00 55.57           O  
ANISOU 2178  O   ASP A1092     7051   8344   5722  -2303   -870     40       O  
ATOM   2179  CB  ASP A1092      -7.356  -6.594 -49.363  1.00 59.80           C  
ANISOU 2179  CB  ASP A1092     7529   9186   6005  -3436   -746   -313       C  
ATOM   2180  CG  ASP A1092      -6.202  -7.444 -48.869  1.00 67.11           C  
ANISOU 2180  CG  ASP A1092     8993   9667   6838  -3449   -381   -277       C  
ATOM   2181  OD1 ASP A1092      -6.040  -7.571 -47.637  1.00 66.88           O  
ANISOU 2181  OD1 ASP A1092     8987   9516   6907  -3343   -140   -261       O  
ATOM   2182  OD2 ASP A1092      -5.457  -7.985 -49.712  1.00 72.57           O  
ANISOU 2182  OD2 ASP A1092    10099  10112   7361  -3562   -343   -275       O  
ATOM   2183  N   ALA A1093      -7.673  -3.761 -48.312  1.00 56.86           N  
ANISOU 2183  N   ALA A1093     6399   9094   6111  -2479  -1069   -142       N  
ATOM   2184  CA  ALA A1093      -7.624  -2.777 -47.266  1.00 54.95           C  
ANISOU 2184  CA  ALA A1093     5937   8853   6086  -2088   -980    -98       C  
ATOM   2185  C   ALA A1093      -6.474  -2.991 -46.309  1.00 54.65           C  
ANISOU 2185  C   ALA A1093     6302   8469   5994  -1981   -648    -18       C  
ATOM   2186  O   ALA A1093      -5.913  -2.043 -45.823  1.00 52.57           O  
ANISOU 2186  O   ALA A1093     6063   8100   5813  -1623   -652     81       O  
ATOM   2187  CB  ALA A1093      -8.903  -2.949 -46.541  1.00 59.19           C  
ANISOU 2187  CB  ALA A1093     5961   9697   6831  -2250   -853   -293       C  
ATOM   2188  N   VAL A1094      -6.127  -4.222 -46.006  1.00 49.72           N  
ANISOU 2188  N   VAL A1094     6008   7652   5232  -2282   -387    -60       N  
ATOM   2189  CA  VAL A1094      -5.195  -4.455 -44.955  1.00 46.58           C  
ANISOU 2189  CA  VAL A1094     5947   6942   4810  -2166   -140     11       C  
ATOM   2190  C   VAL A1094      -3.876  -4.480 -45.626  1.00 47.08           C  
ANISOU 2190  C   VAL A1094     6369   6722   4797  -2007   -215    117       C  
ATOM   2191  O   VAL A1094      -3.015  -3.693 -45.303  1.00 44.29           O  
ANISOU 2191  O   VAL A1094     6082   6236   4511  -1681   -249    215       O  
ATOM   2192  CB  VAL A1094      -5.433  -5.758 -44.301  1.00 51.90           C  
ANISOU 2192  CB  VAL A1094     6865   7486   5370  -2538    144    -74       C  
ATOM   2193  CG1 VAL A1094      -4.541  -5.933 -43.174  1.00 49.68           C  
ANISOU 2193  CG1 VAL A1094     6952   6875   5050  -2392    311     22       C  
ATOM   2194  CG2 VAL A1094      -6.801  -5.806 -43.845  1.00 55.13           C  
ANISOU 2194  CG2 VAL A1094     6887   8210   5851  -2796    264   -239       C  
ATOM   2195  N   ARG A1095      -3.724  -5.374 -46.583  1.00 43.62           N  
ANISOU 2195  N   ARG A1095     6154   6195   4223  -2266   -215     67       N  
ATOM   2196  CA  ARG A1095      -2.454  -5.469 -47.315  1.00 41.13           C  
ANISOU 2196  CA  ARG A1095     6169   5601   3859  -2154   -214    109       C  
ATOM   2197  C   ARG A1095      -2.040  -4.146 -47.959  1.00 42.92           C  
ANISOU 2197  C   ARG A1095     6295   5899   4115  -1878   -421    187       C  
ATOM   2198  O   ARG A1095      -0.848  -3.875 -48.105  1.00 40.57           O  
ANISOU 2198  O   ARG A1095     6191   5374   3849  -1696   -359    216       O  
ATOM   2199  CB  ARG A1095      -2.516  -6.566 -48.384  1.00 41.99           C  
ANISOU 2199  CB  ARG A1095     6536   5622   3795  -2522   -156      5       C  
ATOM   2200  CG  ARG A1095      -2.479  -7.990 -47.843  1.00 47.76           C  
ANISOU 2200  CG  ARG A1095     7562   6110   4473  -2768    102    -65       C  
ATOM   2201  CD  ARG A1095      -2.352  -8.993 -48.974  1.00 48.70           C  
ANISOU 2201  CD  ARG A1095     8002   6078   4424  -3102    192   -180       C  
ATOM   2202  NE  ARG A1095      -2.199 -10.375 -48.511  1.00 49.22           N  
ANISOU 2202  NE  ARG A1095     8442   5823   4436  -3308    450   -244       N  
ATOM   2203  CZ  ARG A1095      -3.184 -11.164 -48.077  1.00 57.81           C  
ANISOU 2203  CZ  ARG A1095     9572   6985   5409  -3681    555   -312       C  
ATOM   2204  NH1 ARG A1095      -4.437 -10.731 -48.008  1.00 45.23           N  
ANISOU 2204  NH1 ARG A1095     7571   5822   3794  -3888    436   -355       N  
ATOM   2205  NH2 ARG A1095      -2.909 -12.404 -47.696  1.00 40.01           N  
ANISOU 2205  NH2 ARG A1095     7773   4351   3077  -3849    791   -353       N  
ATOM   2206  N   ARG A1096      -3.023  -3.342 -48.358  1.00 40.47           N  
ANISOU 2206  N   ARG A1096     5687   5887   3803  -1856   -669    205       N  
ATOM   2207  CA  ARG A1096      -2.776  -1.982 -48.804  1.00 39.57           C  
ANISOU 2207  CA  ARG A1096     5521   5812   3703  -1571   -888    302       C  
ATOM   2208  C   ARG A1096      -2.071  -1.215 -47.707  1.00 42.28           C  
ANISOU 2208  C   ARG A1096     5833   6032   4198  -1232   -772    371       C  
ATOM   2209  O   ARG A1096      -1.096  -0.505 -47.944  1.00 40.29           O  
ANISOU 2209  O   ARG A1096     5753   5619   3934  -1054   -776    425       O  
ATOM   2210  CB  ARG A1096      -4.094  -1.285 -49.119  1.00 41.53           C  
ANISOU 2210  CB  ARG A1096     5401   6385   3994  -1527  -1210    313       C  
ATOM   2211  CG  ARG A1096      -4.658  -1.659 -50.469  1.00 51.30           C  
ANISOU 2211  CG  ARG A1096     6714   7744   5032  -1819  -1473    281       C  
ATOM   2212  CD  ARG A1096      -5.972  -0.947 -50.797  1.00 57.95           C  
ANISOU 2212  CD  ARG A1096     7138   8916   5966  -1724  -1892    291       C  
ATOM   2213  NE  ARG A1096      -6.087  -0.723 -52.236  1.00 63.38           N  
ANISOU 2213  NE  ARG A1096     8070   9614   6395  -1856  -2275    353       N  
ATOM   2214  CZ  ARG A1096      -7.226  -0.672 -52.917  1.00 81.01           C  
ANISOU 2214  CZ  ARG A1096    10048  12124   8608  -1966  -2709    331       C  
ATOM   2215  NH1 ARG A1096      -8.401  -0.840 -52.319  1.00 73.42           N  
ANISOU 2215  NH1 ARG A1096     8484  11490   7924  -1966  -2787    210       N  
ATOM   2216  NH2 ARG A1096      -7.183  -0.467 -54.224  1.00 68.38           N  
ANISOU 2216  NH2 ARG A1096     8809  10472   6699  -2109  -3072    412       N  
ATOM   2217  N   ALA A1097      -2.578  -1.374 -46.493  1.00 39.68           N  
ANISOU 2217  N   ALA A1097     5310   5776   3990  -1196   -648    349       N  
ATOM   2218  CA  ALA A1097      -2.010  -0.712 -45.334  1.00 37.81           C  
ANISOU 2218  CA  ALA A1097     5079   5428   3858   -930   -541    404       C  
ATOM   2219  C   ALA A1097      -0.519  -1.010 -45.128  1.00 40.09           C  
ANISOU 2219  C   ALA A1097     5684   5411   4138   -855   -428    437       C  
ATOM   2220  O   ALA A1097       0.206  -0.136 -44.663  1.00 38.55           O  
ANISOU 2220  O   ALA A1097     5515   5127   4003   -620   -438    490       O  
ATOM   2221  CB  ALA A1097      -2.807  -1.074 -44.087  1.00 39.71           C  
ANISOU 2221  CB  ALA A1097     5165   5761   4162  -1015   -368    347       C  
ATOM   2222  N   ALA A1098      -0.067  -2.224 -45.467  1.00 36.93           N  
ANISOU 2222  N   ALA A1098     5500   4844   3687  -1048   -324    384       N  
ATOM   2223  CA  ALA A1098       1.356  -2.597 -45.341  1.00 35.38           C  
ANISOU 2223  CA  ALA A1098     5532   4352   3561   -940   -235    376       C  
ATOM   2224  C   ALA A1098       2.226  -1.976 -46.441  1.00 39.64           C  
ANISOU 2224  C   ALA A1098     6128   4829   4104   -879   -255    340       C  
ATOM   2225  O   ALA A1098       3.399  -1.686 -46.217  1.00 39.01           O  
ANISOU 2225  O   ALA A1098     6090   4585   4146   -714   -205    319       O  
ATOM   2226  CB  ALA A1098       1.521  -4.090 -45.340  1.00 37.12           C  
ANISOU 2226  CB  ALA A1098     5977   4369   3759  -1127   -105    315       C  
ATOM   2227  N   LEU A1099       1.661  -1.777 -47.630  1.00 36.66           N  
ANISOU 2227  N   LEU A1099     5769   4579   3581  -1045   -331    319       N  
ATOM   2228  CA  LEU A1099       2.369  -1.054 -48.682  1.00 36.32           C  
ANISOU 2228  CA  LEU A1099     5866   4470   3465  -1046   -334    290       C  
ATOM   2229  C   LEU A1099       2.528   0.405 -48.265  1.00 40.53           C  
ANISOU 2229  C   LEU A1099     6303   5059   4037   -796   -444    381       C  
ATOM   2230  O   LEU A1099       3.626   0.957 -48.340  1.00 39.15           O  
ANISOU 2230  O   LEU A1099     6217   4744   3915   -715   -344    341       O  
ATOM   2231  CB  LEU A1099       1.635  -1.144 -50.025  1.00 38.08           C  
ANISOU 2231  CB  LEU A1099     6223   4798   3450  -1311   -453    274       C  
ATOM   2232  CG  LEU A1099       2.442  -0.678 -51.242  1.00 42.36           C  
ANISOU 2232  CG  LEU A1099     7064   5196   3833  -1432   -381    212       C  
ATOM   2233  CD1 LEU A1099       3.559  -1.648 -51.544  1.00 42.27           C  
ANISOU 2233  CD1 LEU A1099     7221   4936   3904  -1563    -46     30       C  
ATOM   2234  CD2 LEU A1099       1.558  -0.517 -52.446  1.00 46.69           C  
ANISOU 2234  CD2 LEU A1099     7793   5863   4082  -1673   -613    251       C  
ATOM   2235  N   ILE A1100       1.446   1.030 -47.805  1.00 38.49           N  
ANISOU 2235  N   ILE A1100     5854   4998   3775   -681   -621    476       N  
ATOM   2236  CA  ILE A1100       1.555   2.391 -47.295  1.00 37.87           C  
ANISOU 2236  CA  ILE A1100     5716   4930   3743   -426   -696    554       C  
ATOM   2237  C   ILE A1100       2.672   2.446 -46.272  1.00 40.68           C  
ANISOU 2237  C   ILE A1100     6087   5134   4237   -301   -538    528       C  
ATOM   2238  O   ILE A1100       3.501   3.354 -46.309  1.00 40.40           O  
ANISOU 2238  O   ILE A1100     6142   5001   4208   -208   -510    525       O  
ATOM   2239  CB  ILE A1100       0.270   2.903 -46.639  1.00 41.89           C  
ANISOU 2239  CB  ILE A1100     5956   5641   4317   -277   -834    612       C  
ATOM   2240  CG1 ILE A1100      -0.813   3.119 -47.690  1.00 45.24           C  
ANISOU 2240  CG1 ILE A1100     6308   6232   4648   -331  -1097    642       C  
ATOM   2241  CG2 ILE A1100       0.535   4.227 -45.943  1.00 41.36           C  
ANISOU 2241  CG2 ILE A1100     5882   5519   4314     -6   -841    668       C  
ATOM   2242  CD1 ILE A1100      -2.022   3.878 -47.165  1.00 56.05           C  
ANISOU 2242  CD1 ILE A1100     7344   7792   6160   -104  -1257    668       C  
ATOM   2243  N   ASN A1101       2.689   1.450 -45.390  1.00 36.52           N  
ANISOU 2243  N   ASN A1101     5505   4574   3799   -329   -455    507       N  
ATOM   2244  CA  ASN A1101       3.678   1.349 -44.320  1.00 35.18           C  
ANISOU 2244  CA  ASN A1101     5364   4253   3751   -208   -393    499       C  
ATOM   2245  C   ASN A1101       5.127   1.266 -44.817  1.00 39.13           C  
ANISOU 2245  C   ASN A1101     5937   4576   4355   -199   -316    401       C  
ATOM   2246  O   ASN A1101       6.021   1.871 -44.240  1.00 38.22           O  
ANISOU 2246  O   ASN A1101     5791   4391   4338    -74   -325    384       O  
ATOM   2247  CB  ASN A1101       3.346   0.143 -43.438  1.00 35.73           C  
ANISOU 2247  CB  ASN A1101     5468   4270   3837   -278   -355    510       C  
ATOM   2248  CG  ASN A1101       4.238   0.039 -42.214  1.00 51.82           C  
ANISOU 2248  CG  ASN A1101     7589   6140   5960   -143   -386    538       C  
ATOM   2249  OD1 ASN A1101       5.471  -0.069 -42.334  1.00 48.64           O  
ANISOU 2249  OD1 ASN A1101     7206   5583   5694    -52   -409    484       O  
ATOM   2250  ND2 ASN A1101       3.622   0.037 -41.027  1.00 37.00           N  
ANISOU 2250  ND2 ASN A1101     5762   4289   4006   -149   -388    603       N  
ATOM   2251  N   MET A1102       5.366   0.519 -45.884  1.00 36.93           N  
ANISOU 2251  N   MET A1102     5740   4227   4065   -357   -217    304       N  
ATOM   2252  CA  MET A1102       6.715   0.435 -46.431  1.00 37.20           C  
ANISOU 2252  CA  MET A1102     5797   4097   4239   -370    -70    149       C  
ATOM   2253  C   MET A1102       7.079   1.773 -47.047  1.00 41.98           C  
ANISOU 2253  C   MET A1102     6455   4741   4755   -403    -33    124       C  
ATOM   2254  O   MET A1102       8.196   2.256 -46.852  1.00 42.29           O  
ANISOU 2254  O   MET A1102     6424   4702   4941   -351     51     21       O  
ATOM   2255  CB  MET A1102       6.846  -0.683 -47.472  1.00 40.66           C  
ANISOU 2255  CB  MET A1102     6356   4423   4671   -563     96     16       C  
ATOM   2256  CG  MET A1102       6.864  -2.088 -46.881  1.00 44.55           C  
ANISOU 2256  CG  MET A1102     6862   4769   5295   -519    106      0       C  
ATOM   2257  SD  MET A1102       6.971  -3.360 -48.153  1.00 50.40           S  
ANISOU 2257  SD  MET A1102     7801   5339   6008   -766    347   -180       S  
ATOM   2258  CE  MET A1102       8.596  -2.982 -48.818  1.00 48.12           C  
ANISOU 2258  CE  MET A1102     7423   4892   5970   -720    599   -433       C  
ATOM   2259  N   VAL A1103       6.140   2.372 -47.778  1.00 38.87           N  
ANISOU 2259  N   VAL A1103     6194   4455   4119   -497   -118    214       N  
ATOM   2260  CA  VAL A1103       6.394   3.652 -48.449  1.00 39.38           C  
ANISOU 2260  CA  VAL A1103     6434   4498   4032   -547   -106    218       C  
ATOM   2261  C   VAL A1103       6.555   4.754 -47.416  1.00 42.45           C  
ANISOU 2261  C   VAL A1103     6736   4907   4484   -340   -184    294       C  
ATOM   2262  O   VAL A1103       7.295   5.717 -47.624  1.00 42.35           O  
ANISOU 2262  O   VAL A1103     6845   4812   4434   -379    -96    240       O  
ATOM   2263  CB  VAL A1103       5.280   4.020 -49.452  1.00 44.79           C  
ANISOU 2263  CB  VAL A1103     7326   5259   4432   -652   -278    328       C  
ATOM   2264  CG1 VAL A1103       5.374   5.481 -49.848  1.00 45.47           C  
ANISOU 2264  CG1 VAL A1103     7652   5281   4344   -626   -345    396       C  
ATOM   2265  CG2 VAL A1103       5.360   3.134 -50.683  1.00 46.21           C  
ANISOU 2265  CG2 VAL A1103     7711   5377   4471   -949   -163    220       C  
ATOM   2266  N   PHE A1104       5.880   4.604 -46.288  1.00 38.22           N  
ANISOU 2266  N   PHE A1104     6030   4467   4025   -164   -312    397       N  
ATOM   2267  CA  PHE A1104       6.073   5.536 -45.201  1.00 37.02           C  
ANISOU 2267  CA  PHE A1104     5831   4313   3923      3   -352    445       C  
ATOM   2268  C   PHE A1104       7.506   5.403 -44.737  1.00 40.68           C  
ANISOU 2268  C   PHE A1104     6225   4672   4561    -12   -255    317       C  
ATOM   2269  O   PHE A1104       8.234   6.381 -44.669  1.00 40.78           O  
ANISOU 2269  O   PHE A1104     6291   4633   4571    -28   -202    263       O  
ATOM   2270  CB  PHE A1104       5.122   5.240 -44.058  1.00 38.26           C  
ANISOU 2270  CB  PHE A1104     5854   4571   4113    131   -442    539       C  
ATOM   2271  CG  PHE A1104       4.605   6.463 -43.363  1.00 39.74           C  
ANISOU 2271  CG  PHE A1104     6058   4788   4254    288   -486    611       C  
ATOM   2272  CD1 PHE A1104       3.465   7.107 -43.829  1.00 43.65           C  
ANISOU 2272  CD1 PHE A1104     6544   5364   4675    379   -576    680       C  
ATOM   2273  CD2 PHE A1104       5.232   6.944 -42.220  1.00 41.17           C  
ANISOU 2273  CD2 PHE A1104     6263   4904   4475    353   -456    599       C  
ATOM   2274  CE1 PHE A1104       2.967   8.209 -43.172  1.00 45.17           C  
ANISOU 2274  CE1 PHE A1104     6744   5548   4870    564   -588    721       C  
ATOM   2275  CE2 PHE A1104       4.745   8.047 -41.555  1.00 44.17           C  
ANISOU 2275  CE2 PHE A1104     6699   5282   4803    479   -448    641       C  
ATOM   2276  CZ  PHE A1104       3.611   8.684 -42.030  1.00 43.46           C  
ANISOU 2276  CZ  PHE A1104     6592   5248   4674    601   -490    694       C  
ATOM   2277  N   GLN A1105       7.918   4.178 -44.452  1.00 37.06           N  
ANISOU 2277  N   GLN A1105     5645   4170   4266    -10   -245    256       N  
ATOM   2278  CA  GLN A1105       9.283   3.928 -44.008  1.00 37.62           C  
ANISOU 2278  CA  GLN A1105     5576   4143   4575     28   -221    119       C  
ATOM   2279  C   GLN A1105      10.332   4.340 -45.040  1.00 43.96           C  
ANISOU 2279  C   GLN A1105     6361   4886   5454   -127     -8    -86       C  
ATOM   2280  O   GLN A1105      11.356   4.915 -44.668  1.00 44.64           O  
ANISOU 2280  O   GLN A1105     6322   4953   5686   -127     18   -205       O  
ATOM   2281  CB  GLN A1105       9.477   2.449 -43.652  1.00 39.36           C  
ANISOU 2281  CB  GLN A1105     5714   4271   4970     98   -276     95       C  
ATOM   2282  CG  GLN A1105      10.854   2.104 -43.029  1.00 46.49           C  
ANISOU 2282  CG  GLN A1105     6421   5061   6185    224   -357    -34       C  
ATOM   2283  CD  GLN A1105      10.933   0.673 -42.493  1.00 56.70           C  
ANISOU 2283  CD  GLN A1105     7717   6200   7626    360   -493     -5       C  
ATOM   2284  OE1 GLN A1105      10.012  -0.129 -42.673  1.00 50.85           O  
ANISOU 2284  OE1 GLN A1105     7142   5431   6746    304   -459     85       O  
ATOM   2285  NE2 GLN A1105      12.038   0.352 -41.834  1.00 45.34           N  
ANISOU 2285  NE2 GLN A1105     6108   4646   6471    532   -668    -85       N  
ATOM   2286  N   MET A1106      10.073   4.061 -46.319  1.00 41.56           N  
ANISOU 2286  N   MET A1106     6200   4557   5034   -301    156   -146       N  
ATOM   2287  CA  MET A1106      11.124   4.079 -47.344  1.00 43.46           C  
ANISOU 2287  CA  MET A1106     6445   4704   5364   -507    445   -398       C  
ATOM   2288  C   MET A1106      10.900   4.994 -48.558  1.00 48.39           C  
ANISOU 2288  C   MET A1106     7417   5301   5669   -769    604   -413       C  
ATOM   2289  O   MET A1106      11.783   5.094 -49.411  1.00 50.14           O  
ANISOU 2289  O   MET A1106     7704   5430   5918  -1010    908   -647       O  
ATOM   2290  CB  MET A1106      11.354   2.650 -47.838  1.00 47.05           C  
ANISOU 2290  CB  MET A1106     6820   5065   5992   -535    576   -536       C  
ATOM   2291  CG  MET A1106      11.862   1.707 -46.760  1.00 51.23           C  
ANISOU 2291  CG  MET A1106     7064   5535   6866   -275    426   -559       C  
ATOM   2292  SD  MET A1106      12.092   0.016 -47.359  1.00 57.80           S  
ANISOU 2292  SD  MET A1106     7872   6181   7907   -273    592   -722       S  
ATOM   2293  CE  MET A1106      10.369  -0.515 -47.487  1.00 52.75           C  
ANISOU 2293  CE  MET A1106     7545   5612   6886   -360    451   -455       C  
ATOM   2294  N   GLY A1107       9.747   5.651 -48.649  1.00 43.94           N  
ANISOU 2294  N   GLY A1107     7090   4796   4811   -730    406   -181       N  
ATOM   2295  CA  GLY A1107       9.444   6.519 -49.796  1.00 45.18           C  
ANISOU 2295  CA  GLY A1107     7664   4881   4622   -945    460   -146       C  
ATOM   2296  C   GLY A1107       9.041   5.775 -51.065  1.00 50.56           C  
ANISOU 2296  C   GLY A1107     8588   5519   5104  -1179    532   -182       C  
ATOM   2297  O   GLY A1107       9.500   4.653 -51.305  1.00 50.97           O  
ANISOU 2297  O   GLY A1107     8503   5540   5325  -1268    720   -353       O  
ATOM   2298  N   GLU A1108       8.208   6.415 -51.894  1.00 47.87           N  
ANISOU 2298  N   GLU A1108     8643   5149   4395  -1278    365    -27       N  
ATOM   2299  CA  GLU A1108       7.577   5.754 -53.055  1.00 49.09           C  
ANISOU 2299  CA  GLU A1108     9076   5288   4289  -1506    318    -10       C  
ATOM   2300  C   GLU A1108       8.555   5.043 -54.003  1.00 54.37           C  
ANISOU 2300  C   GLU A1108     9913   5812   4935  -1873    742   -296       C  
ATOM   2301  O   GLU A1108       8.204   4.022 -54.594  1.00 54.66           O  
ANISOU 2301  O   GLU A1108    10018   5851   4901  -2024    773   -345       O  
ATOM   2302  CB  GLU A1108       6.709   6.744 -53.847  1.00 52.37           C  
ANISOU 2302  CB  GLU A1108     9956   5649   4292  -1560     20    197       C  
ATOM   2303  N   THR A1109       9.773   5.565 -54.136  1.00 52.06           N  
ANISOU 2303  N   THR A1109     9672   5392   4715  -2038   1101   -514       N  
ATOM   2304  CA  THR A1109      10.742   5.034 -55.109  1.00 54.81           C  
ANISOU 2304  CA  THR A1109    10187   5587   5052  -2423   1589   -844       C  
ATOM   2305  C   THR A1109      11.637   3.917 -54.540  1.00 58.52           C  
ANISOU 2305  C   THR A1109    10119   6071   6047  -2294   1856  -1111       C  
ATOM   2306  O   THR A1109      12.102   3.039 -55.285  1.00 60.20           O  
ANISOU 2306  O   THR A1109    10389   6168   6315  -2522   2207  -1369       O  
ATOM   2307  CB  THR A1109      11.603   6.176 -55.714  1.00 64.92           C  
ANISOU 2307  CB  THR A1109    11840   6705   6120  -2759   1912  -1002       C  
ATOM   2308  OG1 THR A1109      11.700   7.250 -54.773  1.00 64.02           O  
ANISOU 2308  OG1 THR A1109    11577   6646   6101  -2524   1731   -871       O  
ATOM   2309  CG2 THR A1109      10.971   6.703 -57.001  1.00 65.52           C  
ANISOU 2309  CG2 THR A1109    12692   6625   5576  -3111   1837   -873       C  
ATOM   2310  N   GLY A1110      11.873   3.953 -53.229  1.00 52.95           N  
ANISOU 2310  N   GLY A1110     8928   5476   5715  -1924   1676  -1053       N  
ATOM   2311  CA  GLY A1110      12.628   2.899 -52.550  1.00 52.88           C  
ANISOU 2311  CA  GLY A1110     8422   5459   6211  -1713   1785  -1245       C  
ATOM   2312  C   GLY A1110      11.854   1.594 -52.568  1.00 56.62           C  
ANISOU 2312  C   GLY A1110     8895   5924   6696  -1613   1654  -1152       C  
ATOM   2313  O   GLY A1110      12.382   0.549 -52.959  1.00 58.16           O  
ANISOU 2313  O   GLY A1110     9009   5987   7103  -1672   1926  -1390       O  
ATOM   2314  N   VAL A1111      10.592   1.673 -52.149  1.00 51.06           N  
ANISOU 2314  N   VAL A1111     8279   5348   5771  -1475   1262   -831       N  
ATOM   2315  CA  VAL A1111       9.644   0.560 -52.227  1.00 50.39           C  
ANISOU 2315  CA  VAL A1111     8254   5284   5608  -1464   1122   -725       C  
ATOM   2316  C   VAL A1111       9.471   0.028 -53.663  1.00 57.28           C  
ANISOU 2316  C   VAL A1111     9517   6048   6200  -1851   1355   -862       C  
ATOM   2317  O   VAL A1111       9.252  -1.173 -53.867  1.00 57.98           O  
ANISOU 2317  O   VAL A1111     9632   6062   6337  -1910   1436   -934       O  
ATOM   2318  CB  VAL A1111       8.265   0.996 -51.681  1.00 51.87           C  
ANISOU 2318  CB  VAL A1111     8458   5666   5585  -1324    702   -402       C  
ATOM   2319  CG1 VAL A1111       7.213  -0.100 -51.885  1.00 51.82           C  
ANISOU 2319  CG1 VAL A1111     8519   5710   5462  -1408    581   -325       C  
ATOM   2320  CG2 VAL A1111       8.380   1.379 -50.205  1.00 49.53           C  
ANISOU 2320  CG2 VAL A1111     7837   5450   5533   -983    515   -285       C  
ATOM   2321  N   ALA A1112       9.570   0.922 -54.648  1.00 55.07           N  
ANISOU 2321  N   ALA A1112     9606   5729   5590  -2142   1466   -897       N  
ATOM   2322  CA  ALA A1112       9.458   0.549 -56.056  1.00 57.68           C  
ANISOU 2322  CA  ALA A1112    10413   5932   5569  -2577   1691  -1029       C  
ATOM   2323  C   ALA A1112      10.604  -0.354 -56.540  1.00 63.70           C  
ANISOU 2323  C   ALA A1112    11132   6484   6586  -2751   2247  -1427       C  
ATOM   2324  O   ALA A1112      10.523  -0.931 -57.626  1.00 66.02           O  
ANISOU 2324  O   ALA A1112    11816   6644   6624  -3119   2494  -1579       O  
ATOM   2325  CB  ALA A1112       9.380   1.800 -56.920  1.00 60.12           C  
ANISOU 2325  CB  ALA A1112    11212   6199   5433  -2854   1668   -963       C  
ATOM   2326  N   GLY A1113      11.663  -0.475 -55.742  1.00 59.55           N  
ANISOU 2326  N   GLY A1113    10131   5921   6574  -2487   2432  -1611       N  
ATOM   2327  CA  GLY A1113      12.832  -1.273 -56.115  1.00 62.30           C  
ANISOU 2327  CA  GLY A1113    10320   6068   7285  -2570   2957  -2030       C  
ATOM   2328  C   GLY A1113      12.785  -2.741 -55.724  1.00 66.16           C  
ANISOU 2328  C   GLY A1113    10598   6441   8098  -2339   2962  -2095       C  
ATOM   2329  O   GLY A1113      13.722  -3.478 -56.016  1.00 69.11           O  
ANISOU 2329  O   GLY A1113    10819   6611   8826  -2344   3385  -2453       O  
ATOM   2330  N   PHE A1114      11.708  -3.177 -55.072  1.00 59.70           N  
ANISOU 2330  N   PHE A1114     9783   5727   7173  -2144   2524  -1775       N  
ATOM   2331  CA  PHE A1114      11.529  -4.596 -54.719  1.00 59.84           C  
ANISOU 2331  CA  PHE A1114     9733   5596   7409  -1978   2516  -1803       C  
ATOM   2332  C   PHE A1114      10.741  -5.223 -55.884  1.00 65.42           C  
ANISOU 2332  C   PHE A1114    10950   6231   7676  -2411   2656  -1836       C  
ATOM   2333  O   PHE A1114       9.600  -5.651 -55.702  1.00 63.39           O  
ANISOU 2333  O   PHE A1114    10836   6073   7178  -2449   2348  -1601       O  
ATOM   2334  CB  PHE A1114      10.621  -4.742 -53.483  1.00 58.07           C  
ANISOU 2334  CB  PHE A1114     9351   5522   7191  -1670   2010  -1448       C  
ATOM   2335  CG  PHE A1114      11.211  -4.212 -52.198  1.00 57.39           C  
ANISOU 2335  CG  PHE A1114     8841   5506   7460  -1262   1784  -1362       C  
ATOM   2336  CD1 PHE A1114      11.668  -5.086 -51.219  1.00 60.60           C  
ANISOU 2336  CD1 PHE A1114     9006   5754   8264   -906   1678  -1376       C  
ATOM   2337  CD2 PHE A1114      11.261  -2.850 -51.945  1.00 57.42           C  
ANISOU 2337  CD2 PHE A1114     8748   5706   7362  -1244   1640  -1249       C  
ATOM   2338  CE1 PHE A1114      12.188  -4.614 -50.025  1.00 60.29           C  
ANISOU 2338  CE1 PHE A1114     8630   5776   8502   -562   1410  -1284       C  
ATOM   2339  CE2 PHE A1114      11.778  -2.372 -50.751  1.00 58.89           C  
ANISOU 2339  CE2 PHE A1114     8585   5956   7834   -916   1424  -1177       C  
ATOM   2340  CZ  PHE A1114      12.245  -3.259 -49.790  1.00 57.61           C  
ANISOU 2340  CZ  PHE A1114     8178   5658   8052   -585   1295  -1194       C  
ATOM   2341  N   THR A1115      11.349  -5.287 -57.067  1.00 65.58           N  
ANISOU 2341  N   THR A1115    11250   6080   7585  -2773   3137  -2151       N  
ATOM   2342  CA  THR A1115      10.615  -5.573 -58.299  1.00 67.45           C  
ANISOU 2342  CA  THR A1115    12075   6273   7280  -3280   3240  -2171       C  
ATOM   2343  C   THR A1115      10.041  -6.956 -58.151  1.00 71.73           C  
ANISOU 2343  C   THR A1115    12697   6697   7861  -3258   3202  -2160       C  
ATOM   2344  O   THR A1115       8.850  -7.159 -58.375  1.00 70.98           O  
ANISOU 2344  O   THR A1115    12867   6736   7366  -3468   2891  -1942       O  
ATOM   2345  CB  THR A1115      11.514  -5.617 -59.525  1.00 80.32           C  
ANISOU 2345  CB  THR A1115    14029   7667   8822  -3696   3873  -2581       C  
ATOM   2346  OG1 THR A1115      12.089  -4.321 -59.744  1.00 80.99           O  
ANISOU 2346  OG1 THR A1115    14121   7829   8823  -3805   3977  -2624       O  
ATOM   2347  CG2 THR A1115      10.704  -6.046 -60.747  1.00 81.76           C  
ANISOU 2347  CG2 THR A1115    14891   7779   8396  -4246   3935  -2588       C  
ATOM   2348  N   ASN A1116      10.908  -7.900 -57.784  1.00 69.36           N  
ANISOU 2348  N   ASN A1116    12163   6130   8059  -3006   3514  -2412       N  
ATOM   2349  CA  ASN A1116      10.540  -9.318 -57.629  1.00 69.96           C  
ANISOU 2349  CA  ASN A1116    12375   5991   8216  -2968   3555  -2446       C  
ATOM   2350  C   ASN A1116       9.335  -9.532 -56.708  1.00 69.08           C  
ANISOU 2350  C   ASN A1116    12212   6078   7958  -2827   3010  -2058       C  
ATOM   2351  O   ASN A1116       8.458 -10.353 -56.991  1.00 69.56           O  
ANISOU 2351  O   ASN A1116    12591   6099   7739  -3087   2960  -2006       O  
ATOM   2352  CB  ASN A1116      11.740 -10.117 -57.085  1.00 73.76           C  
ANISOU 2352  CB  ASN A1116    12517   6144   9366  -2543   3849  -2722       C  
ATOM   2353  CG  ASN A1116      12.687 -10.598 -58.184  1.00105.69           C  
ANISOU 2353  CG  ASN A1116    16728   9872  13558  -2780   4536  -3212       C  
ATOM   2354  OD1 ASN A1116      12.348 -11.496 -58.954  1.00104.80           O  
ANISOU 2354  OD1 ASN A1116    17069   9539  13211  -3105   4815  -3360       O  
ATOM   2355  ND2 ASN A1116      13.888 -10.018 -58.240  1.00 99.77           N  
ANISOU 2355  ND2 ASN A1116    15605   9093  13211  -2640   4845  -3496       N  
ATOM   2356  N   SER A1117       9.313  -8.780 -55.609  1.00 60.99           N  
ANISOU 2356  N   SER A1117    10793   5262   7118  -2454   2641  -1818       N  
ATOM   2357  CA  SER A1117       8.302  -8.920 -54.563  1.00 57.22           C  
ANISOU 2357  CA  SER A1117    10210   4959   6571  -2289   2191  -1491       C  
ATOM   2358  C   SER A1117       6.991  -8.219 -54.928  1.00 58.54           C  
ANISOU 2358  C   SER A1117    10515   5476   6253  -2587   1867  -1256       C  
ATOM   2359  O   SER A1117       5.917  -8.633 -54.513  1.00 57.29           O  
ANISOU 2359  O   SER A1117    10381   5448   5937  -2659   1616  -1082       O  
ATOM   2360  CB  SER A1117       8.848  -8.347 -53.252  1.00 57.34           C  
ANISOU 2360  CB  SER A1117     9790   5040   6957  -1802   1953  -1356       C  
ATOM   2361  OG  SER A1117      10.251  -8.561 -53.134  1.00 65.79           O  
ANISOU 2361  OG  SER A1117    10637   5858   8504  -1527   2213  -1613       O  
ATOM   2362  N   LEU A1118       7.093  -7.154 -55.712  1.00 54.75           N  
ANISOU 2362  N   LEU A1118    10124   5132   5547  -2764   1873  -1267       N  
ATOM   2363  CA  LEU A1118       5.935  -6.351 -56.093  1.00 53.56           C  
ANISOU 2363  CA  LEU A1118    10088   5286   4977  -2971   1498  -1039       C  
ATOM   2364  C   LEU A1118       5.071  -7.110 -57.087  1.00 60.03           C  
ANISOU 2364  C   LEU A1118    11304   6106   5398  -3440   1490  -1086       C  
ATOM   2365  O   LEU A1118       3.847  -7.010 -57.070  1.00 59.25           O  
ANISOU 2365  O   LEU A1118    11187   6264   5059  -3565   1107   -898       O  
ATOM   2366  CB  LEU A1118       6.402  -5.016 -56.700  1.00 53.53           C  
ANISOU 2366  CB  LEU A1118    10183   5339   4817  -3032   1513  -1041       C  
ATOM   2367  CG  LEU A1118       7.231  -4.112 -55.783  1.00 55.59           C  
ANISOU 2367  CG  LEU A1118    10073   5627   5423  -2636   1507  -1005       C  
ATOM   2368  CD1 LEU A1118       7.937  -3.041 -56.581  1.00 57.12           C  
ANISOU 2368  CD1 LEU A1118    10478   5770   5455  -2812   1697  -1111       C  
ATOM   2369  CD2 LEU A1118       6.357  -3.489 -54.715  1.00 54.60           C  
ANISOU 2369  CD2 LEU A1118     9653   5763   5328  -2343   1049   -699       C  
ATOM   2370  N   ARG A1119       5.731  -7.851 -57.968  1.00 59.80           N  
ANISOU 2370  N   ARG A1119    11616   5789   5315  -3714   1928  -1367       N  
ATOM   2371  CA  ARG A1119       5.049  -8.751 -58.871  1.00 62.90           C  
ANISOU 2371  CA  ARG A1119    12436   6120   5342  -4192   1989  -1459       C  
ATOM   2372  C   ARG A1119       4.403  -9.889 -58.076  1.00 66.97           C  
ANISOU 2372  C   ARG A1119    12831   6618   5998  -4124   1903  -1404       C  
ATOM   2373  O   ARG A1119       3.236 -10.221 -58.286  1.00 67.58           O  
ANISOU 2373  O   ARG A1119    13017   6885   5774  -4425   1636  -1305       O  
ATOM   2374  CB  ARG A1119       6.034  -9.314 -59.897  1.00 67.09           C  
ANISOU 2374  CB  ARG A1119    13372   6290   5831  -4480   2577  -1820       C  
ATOM   2375  CG  ARG A1119       5.402 -10.275 -60.909  1.00 83.94           C  
ANISOU 2375  CG  ARG A1119    16041   8314   7537  -5039   2694  -1951       C  
ATOM   2376  CD  ARG A1119       6.359 -10.651 -62.042  1.00101.19           C  
ANISOU 2376  CD  ARG A1119    18695  10139   9614  -5386   3323  -2335       C  
ATOM   2377  NE  ARG A1119       7.560 -11.330 -61.544  1.00111.90           N  
ANISOU 2377  NE  ARG A1119    19810  11151  11557  -5029   3834  -2612       N  
ATOM   2378  CZ  ARG A1119       8.724 -10.740 -61.241  1.00126.94           C  
ANISOU 2378  CZ  ARG A1119    21376  12974  13882  -4693   4091  -2753       C  
ATOM   2379  NH1 ARG A1119       8.900  -9.424 -61.377  1.00114.73           N  
ANISOU 2379  NH1 ARG A1119    19745  11640  12207  -4697   3945  -2645       N  
ATOM   2380  NH2 ARG A1119       9.734 -11.481 -60.792  1.00115.38           N  
ANISOU 2380  NH2 ARG A1119    19653  11196  12991  -4347   4486  -3017       N  
ATOM   2381  N   MET A1120       5.167 -10.464 -57.151  1.00 62.82           N  
ANISOU 2381  N   MET A1120    12087   5858   5925  -3740   2109  -1473       N  
ATOM   2382  CA  MET A1120       4.696 -11.588 -56.347  1.00 62.80           C  
ANISOU 2382  CA  MET A1120    12077   5742   6042  -3676   2075  -1427       C  
ATOM   2383  C   MET A1120       3.447 -11.244 -55.542  1.00 63.61           C  
ANISOU 2383  C   MET A1120    11927   6216   6028  -3656   1618  -1144       C  
ATOM   2384  O   MET A1120       2.603 -12.112 -55.293  1.00 64.43           O  
ANISOU 2384  O   MET A1120    12144   6328   6007  -3878   1566  -1119       O  
ATOM   2385  CB  MET A1120       5.812 -12.093 -55.423  1.00 65.06           C  
ANISOU 2385  CB  MET A1120    12186   5691   6845  -3189   2277  -1508       C  
ATOM   2386  CG  MET A1120       6.710 -13.129 -56.099  1.00 72.81           C  
ANISOU 2386  CG  MET A1120    13470   6211   7985  -3259   2778  -1843       C  
ATOM   2387  SD  MET A1120       8.149 -13.669 -55.140  1.00 78.36           S  
ANISOU 2387  SD  MET A1120    13904   6489   9380  -2610   2958  -1977       S  
ATOM   2388  CE  MET A1120       8.537 -15.220 -55.977  1.00 80.72           C  
ANISOU 2388  CE  MET A1120    14697   6240   9732  -2816   3495  -2335       C  
ATOM   2389  N   LEU A1121       3.332  -9.981 -55.141  1.00 56.54           N  
ANISOU 2389  N   LEU A1121    10695   5610   5178  -3415   1327   -961       N  
ATOM   2390  CA  LEU A1121       2.138  -9.513 -54.439  1.00 54.30           C  
ANISOU 2390  CA  LEU A1121    10124   5693   4816  -3385    929   -734       C  
ATOM   2391  C   LEU A1121       0.973  -9.320 -55.402  1.00 59.79           C  
ANISOU 2391  C   LEU A1121    10923   6678   5117  -3813    672   -706       C  
ATOM   2392  O   LEU A1121      -0.187  -9.464 -55.009  1.00 60.02           O  
ANISOU 2392  O   LEU A1121    10757   6973   5075  -3939    424   -617       O  
ATOM   2393  CB  LEU A1121       2.406  -8.208 -53.689  1.00 51.04           C  
ANISOU 2393  CB  LEU A1121     9342   5456   4595  -2969    722   -567       C  
ATOM   2394  CG  LEU A1121       3.258  -8.321 -52.427  1.00 53.41           C  
ANISOU 2394  CG  LEU A1121     9453   5568   5272  -2539    816   -536       C  
ATOM   2395  CD1 LEU A1121       3.821  -6.957 -52.052  1.00 50.99           C  
ANISOU 2395  CD1 LEU A1121     8882   5381   5109  -2212    691   -442       C  
ATOM   2396  CD2 LEU A1121       2.462  -8.911 -51.289  1.00 54.93           C  
ANISOU 2396  CD2 LEU A1121     9552   5817   5503  -2508    701   -420       C  
ATOM   2397  N   GLN A1122       1.271  -8.980 -56.653  1.00 57.46           N  
ANISOU 2397  N   GLN A1122    10935   6335   4562  -4056    718   -794       N  
ATOM   2398  CA  GLN A1122       0.221  -8.825 -57.649  1.00 59.69           C  
ANISOU 2398  CA  GLN A1122    11388   6861   4430  -4478    404   -760       C  
ATOM   2399  C   GLN A1122      -0.330 -10.198 -58.036  1.00 65.96           C  
ANISOU 2399  C   GLN A1122    12456   7571   5034  -4942    543   -913       C  
ATOM   2400  O   GLN A1122      -1.545 -10.394 -58.113  1.00 67.83           O  
ANISOU 2400  O   GLN A1122    12574   8101   5099  -5212    224   -862       O  
ATOM   2401  CB  GLN A1122       0.737  -8.067 -58.871  1.00 62.44           C  
ANISOU 2401  CB  GLN A1122    12114   7129   4483  -4650    413   -800       C  
ATOM   2402  CG  GLN A1122      -0.380  -7.563 -59.779  1.00 77.17           C  
ANISOU 2402  CG  GLN A1122    14124   9278   5920  -4974    -96   -683       C  
ATOM   2403  CD  GLN A1122       0.060  -6.441 -60.698  1.00 95.12           C  
ANISOU 2403  CD  GLN A1122    16748  11489   7906  -5022   -210   -625       C  
ATOM   2404  OE1 GLN A1122       1.192  -5.969 -60.628  1.00 89.86           O  
ANISOU 2404  OE1 GLN A1122    16168  10600   7376  -4832    130   -689       O  
ATOM   2405  NE2 GLN A1122      -0.844  -6.002 -61.564  1.00 88.95           N  
ANISOU 2405  NE2 GLN A1122    16185  10896   6716  -5295   -711   -507       N  
ATOM   2406  N   GLN A1123       0.571 -11.157 -58.222  1.00 61.93           N  
ANISOU 2406  N   GLN A1123    12281   6654   4595  -5018   1031  -1121       N  
ATOM   2407  CA  GLN A1123       0.194 -12.523 -58.572  1.00 64.02           C  
ANISOU 2407  CA  GLN A1123    12895   6744   4685  -5453   1245  -1291       C  
ATOM   2408  C   GLN A1123      -0.424 -13.257 -57.378  1.00 65.91           C  
ANISOU 2408  C   GLN A1123    12896   7024   5123  -5364   1209  -1224       C  
ATOM   2409  O   GLN A1123      -0.637 -14.471 -57.433  1.00 67.95           O  
ANISOU 2409  O   GLN A1123    13463   7065   5290  -5674   1442  -1363       O  
ATOM   2410  CB  GLN A1123       1.421 -13.286 -59.085  1.00 66.77           C  
ANISOU 2410  CB  GLN A1123    13673   6586   5110  -5490   1817  -1556       C  
ATOM   2411  CG  GLN A1123       2.081 -12.656 -60.323  1.00 78.14           C  
ANISOU 2411  CG  GLN A1123    15439   7940   6312  -5685   1977  -1686       C  
ATOM   2412  CD  GLN A1123       3.419 -13.279 -60.679  1.00 92.58           C  
ANISOU 2412  CD  GLN A1123    17551   9276   8348  -5629   2616  -1995       C  
ATOM   2413  OE1 GLN A1123       3.977 -14.074 -59.920  1.00 84.19           O  
ANISOU 2413  OE1 GLN A1123    16381   7923   7685  -5317   2880  -2083       O  
ATOM   2414  NE2 GLN A1123       3.941 -12.916 -61.842  1.00 88.38           N  
ANISOU 2414  NE2 GLN A1123    17402   8630   7550  -5933   2866  -2174       N  
ATOM   2415  N   LYS A1124      -0.679 -12.512 -56.297  1.00 57.90           N  
ANISOU 2415  N   LYS A1124    11392   6249   4357  -4967    957  -1025       N  
ATOM   2416  CA  LYS A1124      -1.331 -13.009 -55.079  1.00 56.26           C  
ANISOU 2416  CA  LYS A1124    10957   6116   4302  -4904    916   -949       C  
ATOM   2417  C   LYS A1124      -0.518 -14.055 -54.317  1.00 60.03           C  
ANISOU 2417  C   LYS A1124    11694   6115   5001  -4716   1283  -1015       C  
ATOM   2418  O   LYS A1124      -0.956 -14.532 -53.281  1.00 59.78           O  
ANISOU 2418  O   LYS A1124    11604   6062   5050  -4689   1285   -948       O  
ATOM   2419  CB  LYS A1124      -2.746 -13.512 -55.374  1.00 61.00           C  
ANISOU 2419  CB  LYS A1124    11531   7018   4630  -5443    734   -996       C  
ATOM   2420  CG  LYS A1124      -3.667 -12.447 -55.966  1.00 69.57           C  
ANISOU 2420  CG  LYS A1124    12268   8601   5564  -5546    251   -908       C  
ATOM   2421  CD  LYS A1124      -4.422 -11.687 -54.894  1.00 75.64           C  
ANISOU 2421  CD  LYS A1124    12434   9734   6573  -5264    -13   -764       C  
ATOM   2422  CE  LYS A1124      -5.008 -10.386 -55.423  1.00 86.35           C  
ANISOU 2422  CE  LYS A1124    13437  11486   7887  -5142   -505   -649       C  
ATOM   2423  NZ  LYS A1124      -5.724 -10.552 -56.717  1.00 99.91           N  
ANISOU 2423  NZ  LYS A1124    15317  13392   9254  -5627   -801   -724       N  
ATOM   2424  N   ARG A1125       0.680 -14.363 -54.804  1.00 57.21           N  
ANISOU 2424  N   ARG A1125    11621   5359   4756  -4569   1587  -1151       N  
ATOM   2425  CA  ARG A1125       1.594 -15.262 -54.115  1.00 57.94           C  
ANISOU 2425  CA  ARG A1125    11922   4956   5135  -4272   1874  -1214       C  
ATOM   2426  C   ARG A1125       2.056 -14.582 -52.831  1.00 59.29           C  
ANISOU 2426  C   ARG A1125    11721   5169   5637  -3716   1692  -1022       C  
ATOM   2427  O   ARG A1125       3.021 -13.825 -52.839  1.00 57.34           O  
ANISOU 2427  O   ARG A1125    11264   4891   5630  -3344   1693  -1023       O  
ATOM   2428  CB  ARG A1125       2.809 -15.577 -54.998  1.00 60.77           C  
ANISOU 2428  CB  ARG A1125    12549   4924   5617  -4196   2242  -1450       C  
ATOM   2429  CG  ARG A1125       2.478 -16.038 -56.419  1.00 74.64           C  
ANISOU 2429  CG  ARG A1125    14722   6644   6996  -4774   2446  -1660       C  
ATOM   2430  CD  ARG A1125       3.744 -16.387 -57.210  1.00 87.51           C  
ANISOU 2430  CD  ARG A1125    16623   7839   8787  -4694   2913  -1945       C  
ATOM   2431  NE  ARG A1125       3.427 -16.871 -58.550  1.00102.03           N  
ANISOU 2431  NE  ARG A1125    18952   9604  10211  -5300   3147  -2162       N  
ATOM   2432  CZ  ARG A1125       2.880 -18.060 -58.824  1.00120.94           C  
ANISOU 2432  CZ  ARG A1125    21795  11782  12374  -5717   3320  -2283       C  
ATOM   2433  NH1 ARG A1125       2.574 -18.923 -57.852  1.00106.25           N  
ANISOU 2433  NH1 ARG A1125    19988   9733  10650  -5602   3304  -2205       N  
ATOM   2434  NH2 ARG A1125       2.632 -18.396 -60.091  1.00112.99           N  
ANISOU 2434  NH2 ARG A1125    21255  10723  10952  -6301   3519  -2489       N  
ATOM   2435  N   TRP A1126       1.358 -14.841 -51.734  1.00 55.72           N  
ANISOU 2435  N   TRP A1126    11211   4787   5172  -3713   1555   -877       N  
ATOM   2436  CA  TRP A1126       1.638 -14.159 -50.479  1.00 52.99           C  
ANISOU 2436  CA  TRP A1126    10566   4511   5058  -3267   1360   -687       C  
ATOM   2437  C   TRP A1126       2.856 -14.746 -49.788  1.00 58.04           C  
ANISOU 2437  C   TRP A1126    11393   4650   6008  -2831   1463   -691       C  
ATOM   2438  O   TRP A1126       3.814 -14.036 -49.521  1.00 55.61           O  
ANISOU 2438  O   TRP A1126    10831   4318   5981  -2401   1380   -660       O  
ATOM   2439  CB  TRP A1126       0.443 -14.241 -49.535  1.00 51.81           C  
ANISOU 2439  CB  TRP A1126    10336   4594   4755  -3471   1228   -561       C  
ATOM   2440  CG  TRP A1126      -0.863 -13.787 -50.118  1.00 53.23           C  
ANISOU 2440  CG  TRP A1126    10259   5272   4694  -3887   1090   -584       C  
ATOM   2441  CD1 TRP A1126      -2.035 -14.489 -50.143  1.00 58.74           C  
ANISOU 2441  CD1 TRP A1126    11045   6110   5163  -4392   1136   -656       C  
ATOM   2442  CD2 TRP A1126      -1.134 -12.533 -50.746  1.00 51.44           C  
ANISOU 2442  CD2 TRP A1126     9638   5457   4450  -3828    850   -544       C  
ATOM   2443  NE1 TRP A1126      -3.018 -13.749 -50.747  1.00 58.40           N  
ANISOU 2443  NE1 TRP A1126    10614   6571   5005  -4621    904   -673       N  
ATOM   2444  CE2 TRP A1126      -2.495 -12.545 -51.129  1.00 57.29           C  
ANISOU 2444  CE2 TRP A1126    10205   6581   4980  -4262    707   -588       C  
ATOM   2445  CE3 TRP A1126      -0.361 -11.398 -51.022  1.00 50.11           C  
ANISOU 2445  CE3 TRP A1126     9264   5354   4421  -3463    733   -482       C  
ATOM   2446  CZ2 TRP A1126      -3.101 -11.470 -51.766  1.00 56.39           C  
ANISOU 2446  CZ2 TRP A1126     9728   6889   4809  -4277    395   -548       C  
ATOM   2447  CZ3 TRP A1126      -0.961 -10.331 -51.665  1.00 51.25           C  
ANISOU 2447  CZ3 TRP A1126     9129   5886   4457  -3519    470   -436       C  
ATOM   2448  CH2 TRP A1126      -2.319 -10.374 -52.032  1.00 54.05           C  
ANISOU 2448  CH2 TRP A1126     9324   6596   4618  -3893    276   -457       C  
ATOM   2449  N   ASP A1127       2.808 -16.041 -49.500  1.00 58.57           N  
ANISOU 2449  N   ASP A1127    11913   4310   6031  -2945   1620   -735       N  
ATOM   2450  CA  ASP A1127       3.900 -16.751 -48.821  1.00 60.73           C  
ANISOU 2450  CA  ASP A1127    12428   4040   6606  -2504   1655   -729       C  
ATOM   2451  C   ASP A1127       5.252 -16.572 -49.499  1.00 65.46           C  
ANISOU 2451  C   ASP A1127    12872   4428   7573  -2137   1788   -909       C  
ATOM   2452  O   ASP A1127       6.275 -16.471 -48.824  1.00 65.04           O  
ANISOU 2452  O   ASP A1127    12681   4145   7885  -1623   1663   -873       O  
ATOM   2453  CB  ASP A1127       3.603 -18.260 -48.737  1.00 67.07           C  
ANISOU 2453  CB  ASP A1127    13855   4370   7258  -2752   1856   -790       C  
ATOM   2454  CG  ASP A1127       3.118 -18.697 -47.357  1.00 81.83           C  
ANISOU 2454  CG  ASP A1127    16010   6084   8998  -2751   1699   -579       C  
ATOM   2455  OD1 ASP A1127       2.251 -18.030 -46.747  1.00 81.00           O  
ANISOU 2455  OD1 ASP A1127    15677   6394   8707  -2934   1551   -442       O  
ATOM   2456  OD2 ASP A1127       3.608 -19.737 -46.879  1.00 92.38           O  
ANISOU 2456  OD2 ASP A1127    17846   6842  10411  -2574   1741   -563       O  
ATOM   2457  N   GLU A1128       5.255 -16.568 -50.829  1.00 63.21           N  
ANISOU 2457  N   GLU A1128    12621   4211   7184  -2431   2049  -1125       N  
ATOM   2458  CA  GLU A1128       6.492 -16.408 -51.584  1.00 64.26           C  
ANISOU 2458  CA  GLU A1128    12621   4152   7643  -2182   2284  -1362       C  
ATOM   2459  C   GLU A1128       7.076 -15.013 -51.390  1.00 65.18           C  
ANISOU 2459  C   GLU A1128    12204   4598   7962  -1880   2101  -1299       C  
ATOM   2460  O   GLU A1128       8.268 -14.864 -51.116  1.00 65.65           O  
ANISOU 2460  O   GLU A1128    12026   4461   8457  -1434   2125  -1395       O  
ATOM   2461  CB  GLU A1128       6.252 -16.660 -53.070  1.00 67.46           C  
ANISOU 2461  CB  GLU A1128    13275   4569   7787  -2673   2629  -1608       C  
ATOM   2462  CG  GLU A1128       5.882 -18.094 -53.401  1.00 81.45           C  
ANISOU 2462  CG  GLU A1128    15617   5940   9391  -2983   2892  -1741       C  
ATOM   2463  CD  GLU A1128       5.958 -18.387 -54.889  1.00102.66           C  
ANISOU 2463  CD  GLU A1128    18591   8539  11876  -3417   3292  -2041       C  
ATOM   2464  OE1 GLU A1128       6.733 -17.704 -55.606  1.00 96.06           O  
ANISOU 2464  OE1 GLU A1128    17551   7766  11179  -3337   3470  -2212       O  
ATOM   2465  OE2 GLU A1128       5.245 -19.308 -55.341  1.00 99.34           O  
ANISOU 2465  OE2 GLU A1128    18642   7973  11129  -3883   3451  -2122       O  
ATOM   2466  N   ALA A1129       6.218 -14.007 -51.537  1.00 58.91           N  
ANISOU 2466  N   ALA A1129    11222   4296   6867  -2128   1910  -1153       N  
ATOM   2467  CA  ALA A1129       6.598 -12.615 -51.374  1.00 55.95           C  
ANISOU 2467  CA  ALA A1129    10417   4238   6602  -1909   1735  -1073       C  
ATOM   2468  C   ALA A1129       7.214 -12.375 -50.010  1.00 59.78           C  
ANISOU 2468  C   ALA A1129    10659   4643   7414  -1411   1487   -925       C  
ATOM   2469  O   ALA A1129       8.222 -11.687 -49.900  1.00 58.89           O  
ANISOU 2469  O   ALA A1129    10234   4538   7604  -1103   1471   -991       O  
ATOM   2470  CB  ALA A1129       5.400 -11.724 -51.560  1.00 54.23           C  
ANISOU 2470  CB  ALA A1129    10094   4499   6014  -2206   1509   -903       C  
ATOM   2471  N   ALA A1130       6.612 -12.950 -48.973  1.00 57.12           N  
ANISOU 2471  N   ALA A1130    10496   4220   6989  -1378   1298   -737       N  
ATOM   2472  CA  ALA A1130       7.136 -12.810 -47.608  1.00 56.61           C  
ANISOU 2472  CA  ALA A1130    10318   4037   7155   -951   1019   -572       C  
ATOM   2473  C   ALA A1130       8.557 -13.373 -47.483  1.00 63.85           C  
ANISOU 2473  C   ALA A1130    11199   4520   8542   -506   1057   -723       C  
ATOM   2474  O   ALA A1130       9.463 -12.674 -47.014  1.00 63.19           O  
ANISOU 2474  O   ALA A1130    10760   4483   8767   -144    885   -722       O  
ATOM   2475  CB  ALA A1130       6.210 -13.477 -46.594  1.00 57.86           C  
ANISOU 2475  CB  ALA A1130    10811   4108   7065  -1083    875   -370       C  
ATOM   2476  N   VAL A1131       8.756 -14.619 -47.918  1.00 63.58           N  
ANISOU 2476  N   VAL A1131    11510   4063   8586   -533   1281   -875       N  
ATOM   2477  CA  VAL A1131      10.089 -15.231 -47.881  1.00 66.89           C  
ANISOU 2477  CA  VAL A1131    11861   4034   9523    -69   1333  -1062       C  
ATOM   2478  C   VAL A1131      11.058 -14.445 -48.760  1.00 69.99           C  
ANISOU 2478  C   VAL A1131    11777   4582  10233     25   1565  -1342       C  
ATOM   2479  O   VAL A1131      12.254 -14.398 -48.483  1.00 71.68           O  
ANISOU 2479  O   VAL A1131    11660   4620  10957    472   1503  -1483       O  
ATOM   2480  CB  VAL A1131      10.072 -16.704 -48.331  1.00 75.33           C  
ANISOU 2480  CB  VAL A1131    13425   4585  10611   -138   1601  -1213       C  
ATOM   2481  CG1 VAL A1131      11.492 -17.295 -48.321  1.00 79.79           C  
ANISOU 2481  CG1 VAL A1131    13843   4671  11803    418   1653  -1444       C  
ATOM   2482  CG2 VAL A1131       9.143 -17.521 -47.438  1.00 75.99           C  
ANISOU 2482  CG2 VAL A1131    14050   4468  10353   -282   1407   -951       C  
ATOM   2483  N   ASN A1132      10.522 -13.822 -49.807  1.00 64.09           N  
ANISOU 2483  N   ASN A1132    11011   4165   9173   -421   1818  -1428       N  
ATOM   2484  CA  ASN A1132      11.299 -12.971 -50.703  1.00 63.70           C  
ANISOU 2484  CA  ASN A1132    10620   4284   9298   -462   2082  -1683       C  
ATOM   2485  C   ASN A1132      11.767 -11.687 -50.020  1.00 64.40           C  
ANISOU 2485  C   ASN A1132    10241   4683   9543   -220   1800  -1570       C  
ATOM   2486  O   ASN A1132      12.945 -11.335 -50.087  1.00 65.90           O  
ANISOU 2486  O   ASN A1132    10049   4822  10170     37   1900  -1792       O  
ATOM   2487  CB  ASN A1132      10.467 -12.614 -51.945  1.00 63.87           C  
ANISOU 2487  CB  ASN A1132    10879   4557   8833  -1042   2338  -1741       C  
ATOM   2488  CG  ASN A1132      11.307 -12.482 -53.196  1.00 89.86           C  
ANISOU 2488  CG  ASN A1132    14133   7751  12259  -1204   2826  -2122       C  
ATOM   2489  OD1 ASN A1132      11.892 -13.459 -53.674  1.00 86.74           O  
ANISOU 2489  OD1 ASN A1132    13882   6968  12109  -1160   3184  -2409       O  
ATOM   2490  ND2 ASN A1132      11.353 -11.276 -53.749  1.00 81.37           N  
ANISOU 2490  ND2 ASN A1132    12914   6998  11006  -1416   2875  -2143       N  
ATOM   2491  N   LEU A1133      10.841 -10.993 -49.366  1.00 56.65           N  
ANISOU 2491  N   LEU A1133     9280   4023   8220   -323   1475  -1255       N  
ATOM   2492  CA  LEU A1133      11.149  -9.704 -48.741  1.00 53.58           C  
ANISOU 2492  CA  LEU A1133     8523   3933   7903   -156   1227  -1138       C  
ATOM   2493  C   LEU A1133      12.125  -9.844 -47.570  1.00 60.24           C  
ANISOU 2493  C   LEU A1133     9111   4592   9184    342    933  -1108       C  
ATOM   2494  O   LEU A1133      12.811  -8.878 -47.232  1.00 59.33           O  
ANISOU 2494  O   LEU A1133     8626   4654   9264    502    810  -1136       O  
ATOM   2495  CB  LEU A1133       9.873  -8.997 -48.247  1.00 49.46           C  
ANISOU 2495  CB  LEU A1133     8096   3755   6941   -354    968   -828       C  
ATOM   2496  CG  LEU A1133       8.826  -8.521 -49.253  1.00 51.40           C  
ANISOU 2496  CG  LEU A1133     8493   4278   6756   -795   1091   -803       C  
ATOM   2497  CD1 LEU A1133       7.651  -7.911 -48.538  1.00 48.26           C  
ANISOU 2497  CD1 LEU A1133     8086   4184   6069   -870    802   -525       C  
ATOM   2498  CD2 LEU A1133       9.423  -7.527 -50.182  1.00 53.28           C  
ANISOU 2498  CD2 LEU A1133     8582   4652   7010   -899   1281   -967       C  
ATOM   2499  N   ALA A1134      12.172 -11.022 -46.940  1.00 59.77           N  
ANISOU 2499  N   ALA A1134     9289   4168   9252    568    786  -1042       N  
ATOM   2500  CA  ALA A1134      13.093 -11.259 -45.818  1.00 62.34           C  
ANISOU 2500  CA  ALA A1134     9441   4266   9980   1067    413   -990       C  
ATOM   2501  C   ALA A1134      14.537 -11.145 -46.284  1.00 70.80           C  
ANISOU 2501  C   ALA A1134    10018   5234  11648   1358    564  -1343       C  
ATOM   2502  O   ALA A1134      15.389 -10.600 -45.578  1.00 71.20           O  
ANISOU 2502  O   ALA A1134     9674   5351  12029   1671    267  -1354       O  
ATOM   2503  CB  ALA A1134      12.848 -12.622 -45.193  1.00 66.03           C  
ANISOU 2503  CB  ALA A1134    10372   4284  10432   1233    240   -856       C  
ATOM   2504  N   LYS A1135      14.791 -11.627 -47.500  1.00 70.48           N  
ANISOU 2504  N   LYS A1135     9991   5050  11737   1207   1055  -1660       N  
ATOM   2505  CA  LYS A1135      16.133 -11.628 -48.083  1.00 74.63           C  
ANISOU 2505  CA  LYS A1135    10040   5454  12861   1427   1335  -2081       C  
ATOM   2506  C   LYS A1135      16.708 -10.231 -48.299  1.00 78.20           C  
ANISOU 2506  C   LYS A1135    10006   6302  13405   1308   1421  -2220       C  
ATOM   2507  O   LYS A1135      17.852 -10.111 -48.736  1.00 81.47           O  
ANISOU 2507  O   LYS A1135     9956   6667  14332   1442   1680  -2605       O  
ATOM   2508  CB  LYS A1135      16.175 -12.539 -49.322  1.00 79.87           C  
ANISOU 2508  CB  LYS A1135    10934   5830  13581   1234   1906  -2403       C  
ATOM   2509  CG  LYS A1135      15.905 -14.009 -49.049  1.00 95.19           C  
ANISOU 2509  CG  LYS A1135    13318   7280  15570   1438   1834  -2334       C  
ATOM   2510  CD  LYS A1135      15.920 -14.818 -50.343  1.00107.58           C  
ANISOU 2510  CD  LYS A1135    15152   8577  17149   1179   2456  -2680       C  
ATOM   2511  CE  LYS A1135      15.517 -16.271 -50.098  1.00122.47           C  
ANISOU 2511  CE  LYS A1135    17587   9950  18994   1311   2410  -2593       C  
ATOM   2512  NZ  LYS A1135      15.592 -17.110 -51.328  1.00136.42           N  
ANISOU 2512  NZ  LYS A1135    19644  11401  20789   1067   3037  -2959       N  
ATOM   2513  N   SER A1136      15.933  -9.187 -47.986  1.00 70.92           N  
ANISOU 2513  N   SER A1136     9186   5749  12012   1055   1229  -1935       N  
ATOM   2514  CA  SER A1136      16.339  -7.811 -48.263  1.00 69.59           C  
ANISOU 2514  CA  SER A1136     8687   5926  11826    871   1342  -2042       C  
ATOM   2515  C   SER A1136      17.238  -7.096 -47.276  1.00 75.90           C  
ANISOU 2515  C   SER A1136     9002   6855  12984   1178    985  -2045       C  
ATOM   2516  O   SER A1136      17.423  -7.521 -46.136  1.00 76.30           O  
ANISOU 2516  O   SER A1136     8998   6774  13220   1557    504  -1867       O  
ATOM   2517  CB  SER A1136      15.053  -6.997 -48.397  1.00 67.92           C  
ANISOU 2517  CB  SER A1136     8834   6016  10955    488   1285  -1737       C  
ATOM   2518  OG  SER A1136      14.624  -6.495 -47.138  1.00 73.54           O  
ANISOU 2518  OG  SER A1136     9544   6880  11518    650    799  -1401       O  
ATOM   2519  N   ARG A1137      17.770  -5.978 -47.742  1.00 73.90           N  
ANISOU 2519  N   ARG A1137     8455   6850  12772    961   1219  -2245       N  
ATOM   2520  CA  ARG A1137      18.536  -5.067 -46.908  1.00 74.85           C  
ANISOU 2520  CA  ARG A1137     8137   7164  13138   1121    922  -2260       C  
ATOM   2521  C   ARG A1137      17.607  -4.327 -45.937  1.00 74.39           C  
ANISOU 2521  C   ARG A1137     8360   7310  12594   1075    489  -1818       C  
ATOM   2522  O   ARG A1137      18.034  -3.910 -44.857  1.00 74.89           O  
ANISOU 2522  O   ARG A1137     8202   7451  12800   1291     69  -1715       O  
ATOM   2523  CB  ARG A1137      19.316  -4.087 -47.804  1.00 78.02           C  
ANISOU 2523  CB  ARG A1137     8227   7750  13668    803   1396  -2635       C  
ATOM   2524  CG  ARG A1137      20.050  -2.959 -47.084  1.00 92.39           C  
ANISOU 2524  CG  ARG A1137     9630   9813  15660    833   1165  -2680       C  
ATOM   2525  CD  ARG A1137      21.233  -3.461 -46.264  1.00110.62           C  
ANISOU 2525  CD  ARG A1137    11328  12028  18674   1296    826  -2876       C  
ATOM   2526  NE  ARG A1137      21.483  -2.585 -45.114  1.00119.10           N  
ANISOU 2526  NE  ARG A1137    12209  13313  19729   1385    325  -2702       N  
ATOM   2527  CZ  ARG A1137      22.588  -2.607 -44.370  1.00138.81           C  
ANISOU 2527  CZ  ARG A1137    14122  15833  22788   1693    -32  -2882       C  
ATOM   2528  NH1 ARG A1137      23.587  -3.454 -44.649  1.00133.57           N  
ANISOU 2528  NH1 ARG A1137    12931  14993  22825   1997     56  -3262       N  
ATOM   2529  NH2 ARG A1137      22.703  -1.765 -43.346  1.00123.79           N  
ANISOU 2529  NH2 ARG A1137    12146  14126  20760   1696   -486  -2701       N  
ATOM   2530  N   TRP A1138      16.343  -4.170 -46.325  1.00 66.67           N  
ANISOU 2530  N   TRP A1138     7855   6417  11058    788    591  -1581       N  
ATOM   2531  CA  TRP A1138      15.321  -3.570 -45.449  1.00 62.42           C  
ANISOU 2531  CA  TRP A1138     7586   6051  10081    747    248  -1193       C  
ATOM   2532  C   TRP A1138      15.147  -4.373 -44.151  1.00 66.41           C  
ANISOU 2532  C   TRP A1138     8206   6385  10640   1067   -215   -953       C  
ATOM   2533  O   TRP A1138      15.010  -3.804 -43.068  1.00 64.60           O  
ANISOU 2533  O   TRP A1138     8001   6261  10284   1149   -565   -745       O  
ATOM   2534  CB  TRP A1138      14.000  -3.439 -46.228  1.00 58.13           C  
ANISOU 2534  CB  TRP A1138     7455   5610   9022    410    451  -1042       C  
ATOM   2535  CG  TRP A1138      12.775  -3.158 -45.423  1.00 55.88           C  
ANISOU 2535  CG  TRP A1138     7435   5457   8341    383    167   -689       C  
ATOM   2536  CD1 TRP A1138      12.590  -2.148 -44.539  1.00 56.84           C  
ANISOU 2536  CD1 TRP A1138     7517   5754   8327    426    -70   -518       C  
ATOM   2537  CD2 TRP A1138      11.541  -3.887 -45.464  1.00 54.62           C  
ANISOU 2537  CD2 TRP A1138     7610   5266   7876    266    147   -507       C  
ATOM   2538  NE1 TRP A1138      11.325  -2.212 -44.006  1.00 54.14           N  
ANISOU 2538  NE1 TRP A1138     7443   5484   7643    367   -213   -256       N  
ATOM   2539  CE2 TRP A1138      10.661  -3.271 -44.562  1.00 56.00           C  
ANISOU 2539  CE2 TRP A1138     7887   5613   7778    258    -88   -249       C  
ATOM   2540  CE3 TRP A1138      11.104  -5.014 -46.167  1.00 57.05           C  
ANISOU 2540  CE3 TRP A1138     8141   5414   8122    141    329   -564       C  
ATOM   2541  CZ2 TRP A1138       9.364  -3.732 -44.346  1.00 54.25           C  
ANISOU 2541  CZ2 TRP A1138     7920   5435   7258    124   -132    -69       C  
ATOM   2542  CZ3 TRP A1138       9.812  -5.474 -45.951  1.00 57.17           C  
ANISOU 2542  CZ3 TRP A1138     8440   5474   7809    -11    251   -365       C  
ATOM   2543  CH2 TRP A1138       8.959  -4.829 -45.050  1.00 55.59           C  
ANISOU 2543  CH2 TRP A1138     8274   5473   7375    -20     29   -130       C  
ATOM   2544  N   TYR A1139      15.193  -5.694 -44.280  1.00 65.25           N  
ANISOU 2544  N   TYR A1139     8189   5939  10666   1227   -198   -997       N  
ATOM   2545  CA  TYR A1139      15.019  -6.608 -43.156  1.00 66.48           C  
ANISOU 2545  CA  TYR A1139     8586   5843  10831   1503   -614   -770       C  
ATOM   2546  C   TYR A1139      16.195  -6.548 -42.191  1.00 73.65           C  
ANISOU 2546  C   TYR A1139     9159   6657  12167   1893  -1049   -812       C  
ATOM   2547  O   TYR A1139      15.993  -6.408 -40.996  1.00 73.17           O  
ANISOU 2547  O   TYR A1139     9285   6587  11929   1997  -1486   -550       O  
ATOM   2548  CB  TYR A1139      14.843  -8.028 -43.686  1.00 70.12           C  
ANISOU 2548  CB  TYR A1139     9308   5954  11378   1560   -438   -842       C  
ATOM   2549  CG  TYR A1139      14.445  -9.078 -42.671  1.00 73.43           C  
ANISOU 2549  CG  TYR A1139    10160   6051  11688   1755   -799   -584       C  
ATOM   2550  CD1 TYR A1139      13.109  -9.292 -42.344  1.00 72.80           C  
ANISOU 2550  CD1 TYR A1139    10575   6009  11077   1473   -799   -316       C  
ATOM   2551  CD2 TYR A1139      15.402  -9.895 -42.077  1.00 79.03           C  
ANISOU 2551  CD2 TYR A1139    10802   6393  12833   2209  -1130   -628       C  
ATOM   2552  CE1 TYR A1139      12.743 -10.278 -41.430  1.00 75.49           C  
ANISOU 2552  CE1 TYR A1139    11396   6018  11268   1579  -1073    -98       C  
ATOM   2553  CE2 TYR A1139      15.047 -10.882 -41.164  1.00 82.05           C  
ANISOU 2553  CE2 TYR A1139    11700   6412  13061   2371  -1475   -374       C  
ATOM   2554  CZ  TYR A1139      13.719 -11.068 -40.846  1.00 86.50           C  
ANISOU 2554  CZ  TYR A1139    12818   7008  13040   2023  -1416   -110       C  
ATOM   2555  OH  TYR A1139      13.373 -12.043 -39.942  1.00 90.19           O  
ANISOU 2555  OH  TYR A1139    13870   7088  13310   2115  -1709    127       O  
ATOM   2556  N   ASN A1140      17.420  -6.643 -42.702  1.00 73.77           N  
ANISOU 2556  N   ASN A1140     8676   6609  12745   2087   -931  -1161       N  
ATOM   2557  CA  ASN A1140      18.619  -6.564 -41.844  1.00 77.69           C  
ANISOU 2557  CA  ASN A1140     8739   7051  13728   2472  -1389  -1248       C  
ATOM   2558  C   ASN A1140      18.705  -5.259 -41.054  1.00 79.26           C  
ANISOU 2558  C   ASN A1140     8807   7575  13732   2346  -1663  -1123       C  
ATOM   2559  O   ASN A1140      19.102  -5.250 -39.890  1.00 80.84           O  
ANISOU 2559  O   ASN A1140     8986   7718  14011   2589  -2226   -973       O  
ATOM   2560  CB  ASN A1140      19.896  -6.742 -42.671  1.00 82.93           C  
ANISOU 2560  CB  ASN A1140     8770   7663  15078   2640  -1109  -1729       C  
ATOM   2561  CG  ASN A1140      20.168  -8.190 -43.014  1.00111.26           C  
ANISOU 2561  CG  ASN A1140    12416  10817  19041   2968  -1044  -1865       C  
ATOM   2562  OD1 ASN A1140      21.320  -8.590 -43.166  1.00112.87           O  
ANISOU 2562  OD1 ASN A1140    12087  10872  19928   3315  -1065  -2203       O  
ATOM   2563  ND2 ASN A1140      19.111  -8.990 -43.126  1.00100.85           N  
ANISOU 2563  ND2 ASN A1140    11732   9283  17304   2862   -957  -1626       N  
ATOM   2564  N   GLN A1141      18.327  -4.165 -41.707  1.00 71.72           N  
ANISOU 2564  N   GLN A1141     7823   6929  12498   1956  -1272  -1183       N  
ATOM   2565  CA  GLN A1141      18.304  -2.835 -41.096  1.00 69.00           C  
ANISOU 2565  CA  GLN A1141     7426   6875  11916   1780  -1429  -1081       C  
ATOM   2566  C   GLN A1141      17.306  -2.700 -39.929  1.00 68.90           C  
ANISOU 2566  C   GLN A1141     7919   6863  11396   1754  -1794   -666       C  
ATOM   2567  O   GLN A1141      17.674  -2.255 -38.841  1.00 69.85           O  
ANISOU 2567  O   GLN A1141     8010   7029  11501   1845  -2220   -559       O  
ATOM   2568  CB  GLN A1141      17.982  -1.785 -42.171  1.00 67.44           C  
ANISOU 2568  CB  GLN A1141     7218   6925  11481   1370   -899  -1215       C  
ATOM   2569  CG  GLN A1141      19.196  -1.225 -42.878  1.00 91.84           C  
ANISOU 2569  CG  GLN A1141     9773  10128  14995   1276   -607  -1635       C  
ATOM   2570  CD  GLN A1141      19.796  -0.047 -42.115  1.00117.35           C  
ANISOU 2570  CD  GLN A1141    12758  13578  18253   1205   -848  -1660       C  
ATOM   2571  OE1 GLN A1141      20.934  -0.116 -41.632  1.00118.45           O  
ANISOU 2571  OE1 GLN A1141    12400  13728  18877   1403  -1108  -1869       O  
ATOM   2572  NE2 GLN A1141      19.026   1.038 -41.989  1.00106.85           N  
ANISOU 2572  NE2 GLN A1141    11768  12414  16415    929   -782  -1458       N  
ATOM   2573  N   THR A1142      16.046  -3.063 -40.164  1.00 61.09           N  
ANISOU 2573  N   THR A1142     7390   5833   9989   1589  -1604   -463       N  
ATOM   2574  CA  THR A1142      14.988  -2.915 -39.159  1.00 57.93           C  
ANISOU 2574  CA  THR A1142     7457   5450   9104   1495  -1818   -126       C  
ATOM   2575  C   THR A1142      14.180  -4.211 -39.133  1.00 61.16           C  
ANISOU 2575  C   THR A1142     8285   5604   9350   1521  -1803     26       C  
ATOM   2576  O   THR A1142      13.086  -4.279 -39.681  1.00 58.09           O  
ANISOU 2576  O   THR A1142     8121   5295   8654   1277  -1498     91       O  
ATOM   2577  CB  THR A1142      14.101  -1.680 -39.451  1.00 58.61           C  
ANISOU 2577  CB  THR A1142     7635   5832   8803   1178  -1540    -61       C  
ATOM   2578  OG1 THR A1142      13.940  -1.520 -40.864  1.00 55.77           O  
ANISOU 2578  OG1 THR A1142     7149   5566   8475   1006  -1102   -237       O  
ATOM   2579  CG2 THR A1142      14.745  -0.420 -38.899  1.00 56.67           C  
ANISOU 2579  CG2 THR A1142     7183   5766   8582   1146  -1687   -107       C  
ATOM   2580  N   PRO A1143      14.735  -5.253 -38.501  1.00 60.48           N  
ANISOU 2580  N   PRO A1143     8312   5192   9475   1817  -2159     76       N  
ATOM   2581  CA  PRO A1143      14.207  -6.616 -38.623  1.00 61.11           C  
ANISOU 2581  CA  PRO A1143     8792   4948   9480   1861  -2113    162       C  
ATOM   2582  C   PRO A1143      12.873  -6.899 -37.945  1.00 61.50           C  
ANISOU 2582  C   PRO A1143     9436   4954   8977   1610  -2112    444       C  
ATOM   2583  O   PRO A1143      12.197  -7.852 -38.335  1.00 61.61           O  
ANISOU 2583  O   PRO A1143     9764   4789   8857   1497  -1911    473       O  
ATOM   2584  CB  PRO A1143      15.305  -7.489 -37.985  1.00 68.53           C  
ANISOU 2584  CB  PRO A1143     9699   5517  10821   2305  -2588    150       C  
ATOM   2585  CG  PRO A1143      16.489  -6.598 -37.805  1.00 74.84           C  
ANISOU 2585  CG  PRO A1143     9921   6510  12005   2481  -2816    -24       C  
ATOM   2586  CD  PRO A1143      15.946  -5.215 -37.666  1.00 66.09           C  
ANISOU 2586  CD  PRO A1143     8783   5798  10530   2139  -2660     41       C  
ATOM   2587  N   ASN A1144      12.505  -6.114 -36.937  1.00 55.21           N  
ANISOU 2587  N   ASN A1144     8804   4307   7868   1491  -2300    620       N  
ATOM   2588  CA  ASN A1144      11.247  -6.343 -36.231  1.00 53.27           C  
ANISOU 2588  CA  ASN A1144     9098   4028   7115   1215  -2239    839       C  
ATOM   2589  C   ASN A1144      10.084  -5.744 -37.012  1.00 51.41           C  
ANISOU 2589  C   ASN A1144     8752   4127   6656    883  -1771    787       C  
ATOM   2590  O   ASN A1144       9.075  -6.413 -37.266  1.00 50.16           O  
ANISOU 2590  O   ASN A1144     8857   3928   6275    657  -1537    825       O  
ATOM   2591  CB  ASN A1144      11.319  -5.775 -34.813  1.00 54.22           C  
ANISOU 2591  CB  ASN A1144     9485   4140   6978   1199  -2591   1019       C  
ATOM   2592  CG  ASN A1144      12.329  -6.513 -33.938  1.00 79.03           C  
ANISOU 2592  CG  ASN A1144    12858   6902  10269   1516  -3160   1121       C  
ATOM   2593  OD1 ASN A1144      13.126  -5.889 -33.239  1.00 73.17           O  
ANISOU 2593  OD1 ASN A1144    11989   6202   9609   1656  -3546   1143       O  
ATOM   2594  ND2 ASN A1144      12.304  -7.846 -33.979  1.00 73.73           N  
ANISOU 2594  ND2 ASN A1144    12545   5839   9630   1634  -3245   1184       N  
ATOM   2595  N   ARG A1145      10.250  -4.487 -37.413  1.00 44.63           N  
ANISOU 2595  N   ARG A1145     7505   3586   5868    853  -1659    690       N  
ATOM   2596  CA  ARG A1145       9.264  -3.810 -38.241  1.00 40.68           C  
ANISOU 2596  CA  ARG A1145     6865   3386   5206    609  -1297    640       C  
ATOM   2597  C   ARG A1145       9.039  -4.553 -39.546  1.00 45.19           C  
ANISOU 2597  C   ARG A1145     7366   3925   5878    529  -1033    514       C  
ATOM   2598  O   ARG A1145       7.928  -4.574 -40.067  1.00 43.72           O  
ANISOU 2598  O   ARG A1145     7240   3892   5480    289   -806    524       O  
ATOM   2599  CB  ARG A1145       9.688  -2.379 -38.553  1.00 37.01           C  
ANISOU 2599  CB  ARG A1145     6055   3180   4826    630  -1250    551       C  
ATOM   2600  CG  ARG A1145       8.547  -1.571 -39.153  1.00 41.18           C  
ANISOU 2600  CG  ARG A1145     6530   3978   5136    420   -977    556       C  
ATOM   2601  CD  ARG A1145       8.913  -0.122 -39.434  1.00 41.15           C  
ANISOU 2601  CD  ARG A1145     6298   4168   5169    434   -932    490       C  
ATOM   2602  NE  ARG A1145       7.813   0.580 -40.095  1.00 38.22           N  
ANISOU 2602  NE  ARG A1145     5902   4002   4616    293   -729    507       N  
ATOM   2603  CZ  ARG A1145       7.804   1.882 -40.366  1.00 46.91           C  
ANISOU 2603  CZ  ARG A1145     6909   5242   5672    288   -670    484       C  
ATOM   2604  NH1 ARG A1145       8.842   2.649 -40.048  1.00 33.45           N  
ANISOU 2604  NH1 ARG A1145     5124   3515   4071    356   -748    425       N  
ATOM   2605  NH2 ARG A1145       6.744   2.430 -40.954  1.00 30.23           N  
ANISOU 2605  NH2 ARG A1145     4791   3279   3415    212   -554    516       N  
ATOM   2606  N   ALA A1146      10.092  -5.147 -40.086  1.00 43.69           N  
ANISOU 2606  N   ALA A1146     7032   3542   6025    722  -1061    370       N  
ATOM   2607  CA  ALA A1146       9.954  -5.939 -41.301  1.00 43.92           C  
ANISOU 2607  CA  ALA A1146     7064   3487   6137    626   -782    225       C  
ATOM   2608  C   ALA A1146       9.074  -7.150 -41.028  1.00 47.50           C  
ANISOU 2608  C   ALA A1146     7948   3734   6367    487   -752    338       C  
ATOM   2609  O   ALA A1146       8.150  -7.428 -41.786  1.00 46.35           O  
ANISOU 2609  O   ALA A1146     7892   3690   6030    208   -501    305       O  
ATOM   2610  CB  ALA A1146      11.326  -6.374 -41.830  1.00 47.46           C  
ANISOU 2610  CB  ALA A1146     7262   3726   7042    883   -776      5       C  
ATOM   2611  N   LYS A1147       9.357  -7.849 -39.933  1.00 44.76           N  
ANISOU 2611  N   LYS A1147     7900   3088   6018    652  -1029    470       N  
ATOM   2612  CA  LYS A1147       8.605  -9.043 -39.554  1.00 45.82           C  
ANISOU 2612  CA  LYS A1147     8545   2955   5910    495  -1001    581       C  
ATOM   2613  C   LYS A1147       7.105  -8.783 -39.407  1.00 46.89           C  
ANISOU 2613  C   LYS A1147     8832   3353   5630     83   -789    663       C  
ATOM   2614  O   LYS A1147       6.293  -9.670 -39.685  1.00 47.50           O  
ANISOU 2614  O   LYS A1147     9192   3336   5521   -185   -595    654       O  
ATOM   2615  CB  LYS A1147       9.143  -9.620 -38.244  1.00 51.44           C  
ANISOU 2615  CB  LYS A1147     9639   3296   6610    725  -1398    752       C  
ATOM   2616  CG  LYS A1147      10.278 -10.620 -38.405  1.00 67.84           C  
ANISOU 2616  CG  LYS A1147    11766   4936   9073   1107  -1596    679       C  
ATOM   2617  CD  LYS A1147      10.901 -10.936 -37.040  1.00 81.27           C  
ANISOU 2617  CD  LYS A1147    13810   6303  10768   1389  -2126    878       C  
ATOM   2618  CE  LYS A1147      11.255 -12.408 -36.865  1.00 97.21           C  
ANISOU 2618  CE  LYS A1147    16312   7735  12889   1614  -2308    930       C  
ATOM   2619  NZ  LYS A1147      11.492 -12.710 -35.420  1.00110.40           N  
ANISOU 2619  NZ  LYS A1147    18527   9070  14351   1763  -2842   1198       N  
ATOM   2620  N   ARG A1148       6.746  -7.577 -38.962  1.00 40.12           N  
ANISOU 2620  N   ARG A1148     7773   2817   4655     28   -816    718       N  
ATOM   2621  CA  ARG A1148       5.342  -7.213 -38.753  1.00 37.87           C  
ANISOU 2621  CA  ARG A1148     7530   2801   4056   -311   -615    757       C  
ATOM   2622  C   ARG A1148       4.658  -6.763 -40.019  1.00 39.11           C  
ANISOU 2622  C   ARG A1148     7345   3286   4230   -480   -383    632       C  
ATOM   2623  O   ARG A1148       3.460  -6.929 -40.162  1.00 38.90           O  
ANISOU 2623  O   ARG A1148     7339   3429   4011   -779   -208    614       O  
ATOM   2624  CB  ARG A1148       5.219  -6.100 -37.732  1.00 35.04           C  
ANISOU 2624  CB  ARG A1148     7120   2612   3582   -277   -718    846       C  
ATOM   2625  CG  ARG A1148       5.446  -6.539 -36.300  1.00 41.24           C  
ANISOU 2625  CG  ARG A1148     8385   3106   4179   -263   -927    996       C  
ATOM   2626  CD  ARG A1148       5.001  -5.445 -35.334  1.00 40.06           C  
ANISOU 2626  CD  ARG A1148     8240   3153   3829   -355   -911   1049       C  
ATOM   2627  NE  ARG A1148       5.767  -4.228 -35.557  1.00 35.56           N  
ANISOU 2627  NE  ARG A1148     7275   2769   3466   -115  -1040   1009       N  
ATOM   2628  CZ  ARG A1148       6.932  -3.958 -34.991  1.00 47.38           C  
ANISOU 2628  CZ  ARG A1148     8802   4126   5076    122  -1369   1059       C  
ATOM   2629  NH1 ARG A1148       7.479  -4.801 -34.134  1.00 37.29           N  
ANISOU 2629  NH1 ARG A1148     7939   2504   3724    201  -1669   1178       N  
ATOM   2630  NH2 ARG A1148       7.552  -2.828 -35.274  1.00 35.01           N  
ANISOU 2630  NH2 ARG A1148     6866   2752   3685    268  -1424    988       N  
ATOM   2631  N   VAL A1149       5.409  -6.163 -40.925  1.00 34.10           N  
ANISOU 2631  N   VAL A1149     6401   2741   3814   -313   -392    537       N  
ATOM   2632  CA  VAL A1149       4.857  -5.784 -42.216  1.00 32.40           C  
ANISOU 2632  CA  VAL A1149     5963   2777   3572   -481   -222    433       C  
ATOM   2633  C   VAL A1149       4.744  -7.013 -43.109  1.00 37.83           C  
ANISOU 2633  C   VAL A1149     6831   3294   4250   -657    -68    332       C  
ATOM   2634  O   VAL A1149       3.725  -7.230 -43.751  1.00 37.40           O  
ANISOU 2634  O   VAL A1149     6781   3408   4022   -950     53    293       O  
ATOM   2635  CB  VAL A1149       5.724  -4.741 -42.900  1.00 34.52           C  
ANISOU 2635  CB  VAL A1149     5951   3150   4014   -310   -242    356       C  
ATOM   2636  CG1 VAL A1149       5.227  -4.493 -44.308  1.00 33.83           C  
ANISOU 2636  CG1 VAL A1149     5770   3242   3842   -510    -96    262       C  
ATOM   2637  CG2 VAL A1149       5.727  -3.468 -42.078  1.00 32.70           C  
ANISOU 2637  CG2 VAL A1149     5580   3088   3757   -183   -367    446       C  
ATOM   2638  N   ILE A1150       5.803  -7.812 -43.146  1.00 36.27           N  
ANISOU 2638  N   ILE A1150     6771   2753   4256   -472    -84    272       N  
ATOM   2639  CA  ILE A1150       5.803  -9.057 -43.907  1.00 38.13           C  
ANISOU 2639  CA  ILE A1150     7244   2743   4501   -612     91    158       C  
ATOM   2640  C   ILE A1150       4.686  -9.997 -43.428  1.00 44.40           C  
ANISOU 2640  C   ILE A1150     8393   3460   5016   -913    152    235       C  
ATOM   2641  O   ILE A1150       4.021 -10.632 -44.243  1.00 45.59           O  
ANISOU 2641  O   ILE A1150     8666   3631   5024  -1228    338    142       O  
ATOM   2642  CB  ILE A1150       7.178  -9.767 -43.827  1.00 43.25           C  
ANISOU 2642  CB  ILE A1150     7964   2981   5487   -275     42     71       C  
ATOM   2643  CG1 ILE A1150       8.227  -8.983 -44.605  1.00 42.70           C  
ANISOU 2643  CG1 ILE A1150     7513   3004   5706    -97    111   -101       C  
ATOM   2644  CG2 ILE A1150       7.103 -11.171 -44.384  1.00 46.89           C  
ANISOU 2644  CG2 ILE A1150     8770   3103   5941   -401    232    -33       C  
ATOM   2645  CD1 ILE A1150       9.631  -9.473 -44.375  1.00 51.82           C  
ANISOU 2645  CD1 ILE A1150     8577   3821   7292    290     27   -219       C  
ATOM   2646  N   THR A1151       4.462 -10.085 -42.120  1.00 41.28           N  
ANISOU 2646  N   THR A1151     8199   2975   4510   -874     14    389       N  
ATOM   2647  CA  THR A1151       3.366 -10.922 -41.613  1.00 42.77           C  
ANISOU 2647  CA  THR A1151     8753   3095   4402  -1235    132    436       C  
ATOM   2648  C   THR A1151       2.010 -10.406 -42.092  1.00 44.60           C  
ANISOU 2648  C   THR A1151     8713   3782   4450  -1608    290    373       C  
ATOM   2649  O   THR A1151       1.119 -11.188 -42.417  1.00 44.89           O  
ANISOU 2649  O   THR A1151     8914   3835   4306  -1992    466    300       O  
ATOM   2650  CB  THR A1151       3.362 -11.019 -40.074  1.00 52.02           C  
ANISOU 2650  CB  THR A1151    10258   4077   5429  -1179    -18    606       C  
ATOM   2651  OG1 THR A1151       4.372 -11.948 -39.658  1.00 54.31           O  
ANISOU 2651  OG1 THR A1151    10952   3852   5832   -912   -195    671       O  
ATOM   2652  CG2 THR A1151       2.006 -11.501 -39.556  1.00 51.90           C  
ANISOU 2652  CG2 THR A1151    10518   4132   5070  -1658    195    614       C  
ATOM   2653  N   THR A1152       1.865  -9.084 -42.129  1.00 39.09           N  
ANISOU 2653  N   THR A1152     7595   3442   3816  -1486    207    391       N  
ATOM   2654  CA  THR A1152       0.631  -8.457 -42.589  1.00 38.25           C  
ANISOU 2654  CA  THR A1152     7158   3767   3608  -1738    280    332       C  
ATOM   2655  C   THR A1152       0.365  -8.809 -44.051  1.00 42.57           C  
ANISOU 2655  C   THR A1152     7629   4413   4133  -1944    342    208       C  
ATOM   2656  O   THR A1152      -0.768  -9.086 -44.427  1.00 43.74           O  
ANISOU 2656  O   THR A1152     7693   4784   4143  -2296    416    132       O  
ATOM   2657  CB  THR A1152       0.684  -6.928 -42.424  1.00 43.11           C  
ANISOU 2657  CB  THR A1152     7390   4665   4325  -1489    151    381       C  
ATOM   2658  OG1 THR A1152       0.890  -6.610 -41.046  1.00 45.14           O  
ANISOU 2658  OG1 THR A1152     7766   4826   4558  -1353    109    481       O  
ATOM   2659  CG2 THR A1152      -0.606  -6.298 -42.897  1.00 41.44           C  
ANISOU 2659  CG2 THR A1152     6819   4865   4062  -1679    173    317       C  
ATOM   2660  N   PHE A1153       1.411  -8.792 -44.870  1.00 37.88           N  
ANISOU 2660  N   PHE A1153     7062   3659   3672  -1756    321    164       N  
ATOM   2661  CA  PHE A1153       1.275  -9.163 -46.268  1.00 38.45           C  
ANISOU 2661  CA  PHE A1153     7168   3767   3676  -1986    409     35       C  
ATOM   2662  C   PHE A1153       0.920 -10.625 -46.361  1.00 44.44           C  
ANISOU 2662  C   PHE A1153     8300   4283   4302  -2301    581    -42       C  
ATOM   2663  O   PHE A1153      -0.001 -10.991 -47.085  1.00 45.88           O  
ANISOU 2663  O   PHE A1153     8490   4639   4302  -2690    640   -130       O  
ATOM   2664  CB  PHE A1153       2.578  -8.950 -47.037  1.00 39.68           C  
ANISOU 2664  CB  PHE A1153     7338   3735   4005  -1755    447    -42       C  
ATOM   2665  CG  PHE A1153       2.845  -7.524 -47.427  1.00 38.95           C  
ANISOU 2665  CG  PHE A1153     6947   3887   3964  -1586    330    -13       C  
ATOM   2666  CD1 PHE A1153       1.890  -6.776 -48.111  1.00 41.57           C  
ANISOU 2666  CD1 PHE A1153     7114   4560   4122  -1767    219      7       C  
ATOM   2667  CD2 PHE A1153       4.071  -6.947 -47.158  1.00 39.62           C  
ANISOU 2667  CD2 PHE A1153     6936   3842   4275  -1255    313    -18       C  
ATOM   2668  CE1 PHE A1153       2.149  -5.472 -48.486  1.00 40.88           C  
ANISOU 2668  CE1 PHE A1153     6852   4629   4052  -1608    102     47       C  
ATOM   2669  CE2 PHE A1153       4.329  -5.655 -47.534  1.00 40.83           C  
ANISOU 2669  CE2 PHE A1153     6888   4184   4442  -1152    242     -5       C  
ATOM   2670  CZ  PHE A1153       3.370  -4.912 -48.196  1.00 38.62           C  
ANISOU 2670  CZ  PHE A1153     6527   4193   3953  -1324    142     40       C  
ATOM   2671  N   ARG A1154       1.661 -11.456 -45.629  1.00 40.94           N  
ANISOU 2671  N   ARG A1154     8188   3420   3946  -2134    633     -8       N  
ATOM   2672  CA  ARG A1154       1.486 -12.904 -45.696  1.00 43.29           C  
ANISOU 2672  CA  ARG A1154     8950   3374   4123  -2393    810    -77       C  
ATOM   2673  C   ARG A1154       0.054 -13.275 -45.343  1.00 48.10           C  
ANISOU 2673  C   ARG A1154     9625   4193   4458  -2867    893    -82       C  
ATOM   2674  O   ARG A1154      -0.610 -13.954 -46.102  1.00 49.59           O  
ANISOU 2674  O   ARG A1154     9940   4423   4478  -3280   1034   -208       O  
ATOM   2675  CB  ARG A1154       2.466 -13.639 -44.766  1.00 44.31           C  
ANISOU 2675  CB  ARG A1154     9452   2988   4396  -2068    766      3       C  
ATOM   2676  CG  ARG A1154       2.894 -15.019 -45.286  1.00 57.29           C  
ANISOU 2676  CG  ARG A1154    11561   4146   6060  -2138    950   -114       C  
ATOM   2677  CD  ARG A1154       3.031 -16.074 -44.192  1.00 69.41           C  
ANISOU 2677  CD  ARG A1154    13659   5187   7528  -2077    913     -1       C  
ATOM   2678  NE  ARG A1154       3.634 -15.531 -42.978  1.00 78.70           N  
ANISOU 2678  NE  ARG A1154    14786   6287   8828  -1674    623    185       N  
ATOM   2679  CZ  ARG A1154       3.509 -16.063 -41.761  1.00 98.59           C  
ANISOU 2679  CZ  ARG A1154    17779   8502  11178  -1677    507    349       C  
ATOM   2680  NH1 ARG A1154       2.809 -17.182 -41.567  1.00 90.63           N  
ANISOU 2680  NH1 ARG A1154    17346   7211   9877  -2066    690    347       N  
ATOM   2681  NH2 ARG A1154       4.093 -15.467 -40.721  1.00 85.98           N  
ANISOU 2681  NH2 ARG A1154    16134   6866   9669  -1327    206    514       N  
ATOM   2682  N   THR A1155      -0.428 -12.787 -44.209  1.00 43.98           N  
ANISOU 2682  N   THR A1155     8995   3822   3892  -2841    828     26       N  
ATOM   2683  CA  THR A1155      -1.691 -13.239 -43.654  1.00 45.82           C  
ANISOU 2683  CA  THR A1155     9321   4194   3895  -3303    980    -15       C  
ATOM   2684  C   THR A1155      -2.878 -12.364 -44.018  1.00 49.91           C  
ANISOU 2684  C   THR A1155     9269   5294   4401  -3524    951   -101       C  
ATOM   2685  O   THR A1155      -4.016 -12.818 -43.959  1.00 52.32           O  
ANISOU 2685  O   THR A1155     9535   5787   4557  -3990   1102   -220       O  
ATOM   2686  CB  THR A1155      -1.607 -13.301 -42.129  1.00 50.64           C  
ANISOU 2686  CB  THR A1155    10216   4596   4431  -3219    988    116       C  
ATOM   2687  OG1 THR A1155      -1.302 -12.000 -41.609  1.00 43.18           O  
ANISOU 2687  OG1 THR A1155     8896   3876   3635  -2855    812    213       O  
ATOM   2688  CG2 THR A1155      -0.539 -14.310 -41.695  1.00 51.09           C  
ANISOU 2688  CG2 THR A1155    10899   4028   4485  -3007    948    215       C  
ATOM   2689  N   GLY A1156      -2.633 -11.111 -44.374  1.00 44.24           N  
ANISOU 2689  N   GLY A1156     8107   4851   3852  -3195    751    -54       N  
ATOM   2690  CA  GLY A1156      -3.725 -10.167 -44.620  1.00 44.50           C  
ANISOU 2690  CA  GLY A1156     7587   5398   3923  -3295    658   -115       C  
ATOM   2691  C   GLY A1156      -4.544  -9.846 -43.376  1.00 50.74           C  
ANISOU 2691  C   GLY A1156     8210   6357   4712  -3387    779   -129       C  
ATOM   2692  O   GLY A1156      -5.717  -9.483 -43.491  1.00 52.56           O  
ANISOU 2692  O   GLY A1156     8002   6988   4982  -3605    793   -255       O  
ATOM   2693  N   THR A1157      -3.920  -9.984 -42.198  1.00 47.24           N  
ANISOU 2693  N   THR A1157     8117   5601   4229  -3229    861    -18       N  
ATOM   2694  CA  THR A1157      -4.539  -9.680 -40.897  1.00 48.41           C  
ANISOU 2694  CA  THR A1157     8241   5829   4323  -3334   1028    -32       C  
ATOM   2695  C   THR A1157      -3.620  -8.806 -40.031  1.00 50.17           C  
ANISOU 2695  C   THR A1157     8540   5904   4617  -2886    897    132       C  
ATOM   2696  O   THR A1157      -2.447  -8.566 -40.371  1.00 47.37           O  
ANISOU 2696  O   THR A1157     8271   5359   4367  -2510    682    251       O  
ATOM   2697  CB  THR A1157      -4.809 -10.952 -40.105  1.00 59.58           C  
ANISOU 2697  CB  THR A1157    10231   6929   5477  -3752   1296    -63       C  
ATOM   2698  OG1 THR A1157      -3.577 -11.658 -39.936  1.00 58.10           O  
ANISOU 2698  OG1 THR A1157    10633   6220   5222  -3529   1183     99       O  
ATOM   2699  CG2 THR A1157      -5.804 -11.836 -40.827  1.00 62.50           C  
ANISOU 2699  CG2 THR A1157    10547   7454   5748  -4286   1473   -257       C  
ATOM   2700  N   TRP A1158      -4.149  -8.346 -38.898  1.00 48.12           N  
ANISOU 2700  N   TRP A1158     8255   5729   4298  -2965   1055    108       N  
ATOM   2701  CA  TRP A1158      -3.377  -7.505 -37.982  1.00 46.39           C  
ANISOU 2701  CA  TRP A1158     8149   5379   4098  -2615    944    246       C  
ATOM   2702  C   TRP A1158      -2.916  -8.299 -36.749  1.00 52.18           C  
ANISOU 2702  C   TRP A1158     9587   5675   4562  -2744   1011    356       C  
ATOM   2703  O   TRP A1158      -2.682  -7.731 -35.679  1.00 51.83           O  
ANISOU 2703  O   TRP A1158     9718   5548   4427  -2650   1009    425       O  
ATOM   2704  CB  TRP A1158      -4.210  -6.305 -37.526  1.00 45.54           C  
ANISOU 2704  CB  TRP A1158     7581   5627   4094  -2583   1070    142       C  
ATOM   2705  CG  TRP A1158      -4.941  -5.533 -38.603  1.00 46.25           C  
ANISOU 2705  CG  TRP A1158     6996   6144   4433  -2487    986     25       C  
ATOM   2706  CD1 TRP A1158      -6.236  -5.713 -39.008  1.00 52.04           C  
ANISOU 2706  CD1 TRP A1158     7319   7212   5243  -2794   1134   -178       C  
ATOM   2707  CD2 TRP A1158      -4.438  -4.424 -39.359  1.00 43.32           C  
ANISOU 2707  CD2 TRP A1158     6307   5898   4256  -2063    708    103       C  
ATOM   2708  NE1 TRP A1158      -6.561  -4.793 -39.978  1.00 50.80           N  
ANISOU 2708  NE1 TRP A1158     6614   7367   5321  -2541    898   -208       N  
ATOM   2709  CE2 TRP A1158      -5.474  -3.993 -40.212  1.00 48.78           C  
ANISOU 2709  CE2 TRP A1158     6455   6966   5113  -2105    652    -29       C  
ATOM   2710  CE3 TRP A1158      -3.209  -3.758 -39.402  1.00 41.68           C  
ANISOU 2710  CE3 TRP A1158     6231   5512   4092  -1678    494    259       C  
ATOM   2711  CZ2 TRP A1158      -5.313  -2.928 -41.104  1.00 46.66           C  
ANISOU 2711  CZ2 TRP A1158     5872   6851   5006  -1762    373     25       C  
ATOM   2712  CZ3 TRP A1158      -3.049  -2.703 -40.286  1.00 41.55           C  
ANISOU 2712  CZ3 TRP A1158     5886   5665   4236  -1389    288    283       C  
ATOM   2713  CH2 TRP A1158      -4.094  -2.296 -41.123  1.00 43.70           C  
ANISOU 2713  CH2 TRP A1158     5715   6264   4626  -1426    222    184       C  
ATOM   2714  N   ASP A1159      -2.782  -9.614 -36.896  1.00 50.71           N  
ANISOU 2714  N   ASP A1159     9869   5175   4222  -2968   1053    376       N  
ATOM   2715  CA  ASP A1159      -2.316 -10.467 -35.798  1.00 52.89           C  
ANISOU 2715  CA  ASP A1159    10922   4960   4215  -3073   1050    510       C  
ATOM   2716  C   ASP A1159      -0.858 -10.169 -35.463  1.00 53.78           C  
ANISOU 2716  C   ASP A1159    11237   4774   4425  -2557    653    717       C  
ATOM   2717  O   ASP A1159      -0.380 -10.544 -34.394  1.00 56.17           O  
ANISOU 2717  O   ASP A1159    12139   4698   4507  -2546    534    862       O  
ATOM   2718  CB  ASP A1159      -2.476 -11.955 -36.144  1.00 57.93           C  
ANISOU 2718  CB  ASP A1159    12047   5280   4685  -3397   1169    484       C  
ATOM   2719  CG  ASP A1159      -3.907 -12.322 -36.523  1.00 73.00           C  
ANISOU 2719  CG  ASP A1159    13730   7503   6504  -3971   1554    247       C  
ATOM   2720  OD1 ASP A1159      -4.086 -13.246 -37.349  1.00 75.61           O  
ANISOU 2720  OD1 ASP A1159    14171   7748   6810  -4192   1621    172       O  
ATOM   2721  OD2 ASP A1159      -4.848 -11.677 -36.011  1.00 79.99           O  
ANISOU 2721  OD2 ASP A1159    14300   8727   7366  -4206   1796    110       O  
ATOM   2722  N   ALA A1160      -0.167  -9.505 -36.392  1.00 45.42           N  
ANISOU 2722  N   ALA A1160     9689   3884   3686  -2160    441    717       N  
ATOM   2723  CA  ALA A1160       1.194  -9.009 -36.191  1.00 42.86           C  
ANISOU 2723  CA  ALA A1160     9363   3387   3534  -1679     87    850       C  
ATOM   2724  C   ALA A1160       1.286  -7.950 -35.097  1.00 44.22           C  
ANISOU 2724  C   ALA A1160     9531   3653   3619  -1587     11    920       C  
ATOM   2725  O   ALA A1160       2.309  -7.843 -34.422  1.00 44.61           O  
ANISOU 2725  O   ALA A1160     9830   3449   3669  -1324   -294   1055       O  
ATOM   2726  CB  ALA A1160       1.721  -8.449 -37.493  1.00 40.83           C  
ANISOU 2726  CB  ALA A1160     8565   3344   3605  -1399     -5    776       C  
ATOM   2727  N   TYR A1161       0.209  -7.182 -34.932  1.00 38.82           N  
ANISOU 2727  N   TYR A1161     8551   3325   2874  -1805    282    808       N  
ATOM   2728  CA  TYR A1161       0.129  -6.087 -33.953  1.00 38.92           C  
ANISOU 2728  CA  TYR A1161     8536   3450   2802  -1760    305    826       C  
ATOM   2729  C   TYR A1161      -0.849  -6.373 -32.805  1.00 49.79           C  
ANISOU 2729  C   TYR A1161    10315   4769   3835  -2205    634    770       C  
ATOM   2730  O   TYR A1161      -1.120  -5.498 -31.988  1.00 30.32           O  
ANISOU 2730  O   TYR A1161     7842   2405   1273  -2249    760    733       O  
ATOM   2731  CB  TYR A1161      -0.306  -4.806 -34.667  1.00 36.83           C  
ANISOU 2731  CB  TYR A1161     7590   3618   2786  -1604    385    709       C  
ATOM   2732  CG  TYR A1161       0.636  -4.380 -35.765  1.00 35.02           C  
ANISOU 2732  CG  TYR A1161     7025   3442   2837  -1234    120    744       C  
ATOM   2733  CD1 TYR A1161       1.589  -3.401 -35.546  1.00 34.81           C  
ANISOU 2733  CD1 TYR A1161     6909   3403   2915   -923    -95    810       C  
ATOM   2734  CD2 TYR A1161       0.578  -4.958 -37.013  1.00 35.24           C  
ANISOU 2734  CD2 TYR A1161     6864   3526   3000  -1249    117    689       C  
ATOM   2735  CE1 TYR A1161       2.449  -3.007 -36.528  1.00 32.97           C  
ANISOU 2735  CE1 TYR A1161     6393   3213   2922   -653   -271    806       C  
ATOM   2736  CE2 TYR A1161       1.444  -4.573 -38.011  1.00 33.98           C  
ANISOU 2736  CE2 TYR A1161     6456   3394   3061   -973    -60    692       C  
ATOM   2737  CZ  TYR A1161       2.381  -3.596 -37.757  1.00 40.96           C  
ANISOU 2737  CZ  TYR A1161     7243   4266   4055   -681   -238    745       C  
ATOM   2738  OH  TYR A1161       3.257  -3.218 -38.747  1.00 43.62           O  
ANISOU 2738  OH  TYR A1161     7351   4622   4600   -467   -353    712       O  
ATOM   2739  N   GLY A 319      -1.386  -7.587 -32.745  1.00 90.42           N  
ANISOU 2739  N   GLY A 319    23063   8519   2772  -5304  -2807   1793       N  
ATOM   2740  CA  GLY A 319      -2.331  -7.943 -31.695  1.00 84.68           C  
ANISOU 2740  CA  GLY A 319    21765   7736   2675  -4981  -3225   1666       C  
ATOM   2741  C   GLY A 319      -1.632  -8.436 -30.446  1.00 82.91           C  
ANISOU 2741  C   GLY A 319    20642   7987   2874  -4704  -2726   1614       C  
ATOM   2742  O   GLY A 319      -0.406  -8.411 -30.353  1.00 83.47           O  
ANISOU 2742  O   GLY A 319    20479   8422   2812  -4763  -2103   1685       O  
ATOM   2743  N   VAL A 320      -2.419  -8.887 -29.481  1.00 74.10           N  
ANISOU 2743  N   VAL A 320    19020   6857   2279  -4412  -3009   1500       N  
ATOM   2744  CA  VAL A 320      -1.876  -9.528 -28.300  1.00 70.21           C  
ANISOU 2744  CA  VAL A 320    17748   6757   2170  -4132  -2593   1436       C  
ATOM   2745  C   VAL A 320      -1.724 -11.012 -28.617  1.00 74.69           C  
ANISOU 2745  C   VAL A 320    18412   7362   2604  -3898  -2242   1293       C  
ATOM   2746  O   VAL A 320      -2.714 -11.670 -28.909  1.00 73.95           O  
ANISOU 2746  O   VAL A 320    18582   6969   2547  -3785  -2612   1194       O  
ATOM   2747  CB  VAL A 320      -2.803  -9.363 -27.088  1.00 69.60           C  
ANISOU 2747  CB  VAL A 320    17112   6653   2680  -3934  -3027   1381       C  
ATOM   2748  CG1 VAL A 320      -2.098  -9.822 -25.819  1.00 66.13           C  
ANISOU 2748  CG1 VAL A 320    15915   6624   2586  -3707  -2600   1352       C  
ATOM   2749  CG2 VAL A 320      -3.253  -7.918 -26.953  1.00 69.33           C  
ANISOU 2749  CG2 VAL A 320    17134   6449   2758  -4130  -3527   1479       C  
ATOM   2750  N   PRO A 321      -0.490 -11.547 -28.567  1.00 72.61           N  
ANISOU 2750  N   PRO A 321    17932   7446   2210  -3821  -1554   1280       N  
ATOM   2751  CA  PRO A 321      -0.264 -12.938 -28.972  1.00 74.13           C  
ANISOU 2751  CA  PRO A 321    18286   7649   2230  -3586  -1210   1125       C  
ATOM   2752  C   PRO A 321      -1.062 -13.956 -28.168  1.00 76.78           C  
ANISOU 2752  C   PRO A 321    18271   7917   2987  -3275  -1466    995       C  
ATOM   2753  O   PRO A 321      -1.427 -13.695 -27.021  1.00 72.49           O  
ANISOU 2753  O   PRO A 321    17146   7478   2917  -3192  -1680   1021       O  
ATOM   2754  CB  PRO A 321       1.231 -13.149 -28.709  1.00 76.85           C  
ANISOU 2754  CB  PRO A 321    18218   8433   2547  -3524   -459   1143       C  
ATOM   2755  CG  PRO A 321       1.810 -11.818 -28.621  1.00 81.86           C  
ANISOU 2755  CG  PRO A 321    18725   9222   3157  -3827   -398   1338       C  
ATOM   2756  CD  PRO A 321       0.754 -10.911 -28.106  1.00 74.50           C  
ANISOU 2756  CD  PRO A 321    17737   8069   2500  -3931  -1089   1405       C  
ATOM   2757  N   LEU A 322      -1.315 -15.116 -28.767  1.00 76.40           N  
ANISOU 2757  N   LEU A 322    18600   7687   2743  -3112  -1437    860       N  
ATOM   2758  CA  LEU A 322      -2.000 -16.194 -28.066  1.00 73.93           C  
ANISOU 2758  CA  LEU A 322    17986   7305   2800  -2841  -1656    754       C  
ATOM   2759  C   LEU A 322      -1.227 -16.573 -26.807  1.00 75.87           C  
ANISOU 2759  C   LEU A 322    17442   7953   3433  -2634  -1267    739       C  
ATOM   2760  O   LEU A 322      -1.797 -16.633 -25.719  1.00 72.08           O  
ANISOU 2760  O   LEU A 322    16460   7521   3405  -2540  -1523    754       O  
ATOM   2761  CB  LEU A 322      -2.158 -17.416 -28.969  1.00 76.92           C  
ANISOU 2761  CB  LEU A 322    18938   7435   2853  -2700  -1627    613       C  
ATOM   2762  CG  LEU A 322      -3.013 -18.534 -28.376  1.00 79.24           C  
ANISOU 2762  CG  LEU A 322    19023   7578   3506  -2474  -1962    531       C  
ATOM   2763  CD1 LEU A 322      -4.429 -18.040 -28.118  1.00 77.29           C  
ANISOU 2763  CD1 LEU A 322    18735   7052   3579  -2596  -2671    614       C  
ATOM   2764  CD2 LEU A 322      -3.007 -19.745 -29.294  1.00 85.26           C  
ANISOU 2764  CD2 LEU A 322    20393   8089   3911  -2326  -1912    386       C  
ATOM   2765  N   ARG A 323       0.075 -16.802 -26.962  1.00 75.07           N  
ANISOU 2765  N   ARG A 323    17237   8131   3155  -2573   -650    712       N  
ATOM   2766  CA  ARG A 323       0.948 -17.180 -25.846  1.00 73.13           C  
ANISOU 2766  CA  ARG A 323    16272   8244   3269  -2380   -282    700       C  
ATOM   2767  C   ARG A 323       0.701 -16.325 -24.611  1.00 74.18           C  
ANISOU 2767  C   ARG A 323    15827   8519   3837  -2453   -529    821       C  
ATOM   2768  O   ARG A 323       0.691 -16.844 -23.492  1.00 71.15           O  
ANISOU 2768  O   ARG A 323    14930   8267   3836  -2270   -544    795       O  
ATOM   2769  CB  ARG A 323       2.422 -17.068 -26.251  1.00 76.29           C  
ANISOU 2769  CB  ARG A 323    16599   8936   3451  -2396    384    710       C  
ATOM   2770  CG  ARG A 323       3.393 -17.766 -25.301  1.00 83.67           C  
ANISOU 2770  CG  ARG A 323    16872  10180   4738  -2142    771    659       C  
ATOM   2771  CD  ARG A 323       4.840 -17.667 -25.785  1.00 97.29           C  
ANISOU 2771  CD  ARG A 323    18489  12188   6288  -2151   1444    667       C  
ATOM   2772  NE  ARG A 323       4.988 -18.031 -27.199  1.00114.39           N  
ANISOU 2772  NE  ARG A 323    21334  14222   7906  -2156   1733    562       N  
ATOM   2773  CZ  ARG A 323       5.111 -19.275 -27.674  1.00131.73           C  
ANISOU 2773  CZ  ARG A 323    23788  16325   9940  -1865   1942    354       C  
ATOM   2774  NH1 ARG A 323       5.113 -20.329 -26.861  1.00117.63           N  
ANISOU 2774  NH1 ARG A 323    21622  14554   8517  -1548   1879    234       N  
ATOM   2775  NH2 ARG A 323       5.233 -19.468 -28.984  1.00121.94           N  
ANISOU 2775  NH2 ARG A 323    23236  14952   8144  -1893   2202    262       N  
ATOM   2776  N   GLU A 324       0.487 -15.026 -24.817  1.00 71.20           N  
ANISOU 2776  N   GLU A 324    15580   8092   3380  -2718   -741    947       N  
ATOM   2777  CA  GLU A 324       0.362 -14.082 -23.707  1.00 68.13           C  
ANISOU 2777  CA  GLU A 324    14701   7832   3353  -2786   -950   1051       C  
ATOM   2778  C   GLU A 324      -1.053 -14.042 -23.120  1.00 70.37           C  
ANISOU 2778  C   GLU A 324    14904   7903   3931  -2725  -1513   1020       C  
ATOM   2779  O   GLU A 324      -1.210 -13.930 -21.904  1.00 66.76           O  
ANISOU 2779  O   GLU A 324    13938   7584   3845  -2625  -1597   1032       O  
ATOM   2780  CB  GLU A 324       0.807 -12.677 -24.126  1.00 71.06           C  
ANISOU 2780  CB  GLU A 324    15229   8237   3535  -3091   -950   1202       C  
ATOM   2781  CG  GLU A 324       2.172 -12.602 -24.843  1.00 84.50           C  
ANISOU 2781  CG  GLU A 324    17033  10152   4922  -3213   -370   1265       C  
ATOM   2782  CD  GLU A 324       3.381 -12.764 -23.925  1.00 99.75           C  
ANISOU 2782  CD  GLU A 324    18305  12453   7143  -3107     60   1307       C  
ATOM   2783  OE1 GLU A 324       3.227 -13.231 -22.778  1.00 88.02           O  
ANISOU 2783  OE1 GLU A 324    16343  11050   6049  -2894    -41   1256       O  
ATOM   2784  OE2 GLU A 324       4.502 -12.423 -24.363  1.00 94.51           O  
ANISOU 2784  OE2 GLU A 324    17603  11990   6317  -3252    498   1402       O  
ATOM   2785  N   LYS A 325      -2.080 -14.131 -23.961  1.00 69.31           N  
ANISOU 2785  N   LYS A 325    15265   7428   3640  -2786  -1896    983       N  
ATOM   2786  CA  LYS A 325      -3.442 -14.275 -23.451  1.00 67.46           C  
ANISOU 2786  CA  LYS A 325    14902   6994   3736  -2706  -2397    948       C  
ATOM   2787  C   LYS A 325      -3.479 -15.430 -22.465  1.00 71.34           C  
ANISOU 2787  C   LYS A 325    14938   7637   4530  -2460  -2254    882       C  
ATOM   2788  O   LYS A 325      -3.950 -15.280 -21.337  1.00 68.53           O  
ANISOU 2788  O   LYS A 325    14117   7379   4544  -2383  -2393    895       O  
ATOM   2789  CB  LYS A 325      -4.435 -14.552 -24.575  1.00 71.90           C  
ANISOU 2789  CB  LYS A 325    16068   7146   4103  -2778  -2807    913       C  
ATOM   2790  CG  LYS A 325      -4.867 -13.328 -25.353  1.00 88.78           C  
ANISOU 2790  CG  LYS A 325    18636   9036   6062  -3026  -3182    985       C  
ATOM   2791  CD  LYS A 325      -5.835 -13.710 -26.476  1.00101.36           C  
ANISOU 2791  CD  LYS A 325    20864  10182   7468  -3095  -3632    951       C  
ATOM   2792  CE  LYS A 325      -6.255 -12.500 -27.317  1.00112.97           C  
ANISOU 2792  CE  LYS A 325    22832  11353   8739  -3360  -4062   1029       C  
ATOM   2793  NZ  LYS A 325      -6.948 -12.894 -28.586  1.00123.96           N  
ANISOU 2793  NZ  LYS A 325    24978  12289   9833  -3461  -4457   1007       N  
ATOM   2794  N   LYS A 326      -2.952 -16.576 -22.897  1.00 70.39           N  
ANISOU 2794  N   LYS A 326    14983   7531   4231  -2337  -1968    808       N  
ATOM   2795  CA  LYS A 326      -2.969 -17.809 -22.099  1.00 68.74           C  
ANISOU 2795  CA  LYS A 326    14439   7412   4268  -2114  -1871    745       C  
ATOM   2796  C   LYS A 326      -2.179 -17.701 -20.797  1.00 71.45           C  
ANISOU 2796  C   LYS A 326    14163   8099   4885  -2022  -1587    780       C  
ATOM   2797  O   LYS A 326      -2.498 -18.389 -19.827  1.00 69.30           O  
ANISOU 2797  O   LYS A 326    13544   7886   4901  -1890  -1648    767       O  
ATOM   2798  CB  LYS A 326      -2.437 -18.988 -22.918  1.00 73.03           C  
ANISOU 2798  CB  LYS A 326    15342   7877   4530  -1984  -1622    640       C  
ATOM   2799  CG  LYS A 326      -3.272 -19.337 -24.146  1.00 86.25           C  
ANISOU 2799  CG  LYS A 326    17687   9159   5924  -2047  -1952    594       C  
ATOM   2800  CD  LYS A 326      -4.719 -19.666 -23.790  1.00 93.44           C  
ANISOU 2800  CD  LYS A 326    18533   9822   7148  -2052  -2508    620       C  
ATOM   2801  CE  LYS A 326      -5.317 -20.686 -24.762  1.00109.49           C  
ANISOU 2801  CE  LYS A 326    21142  11481   8979  -2014  -2780    550       C  
ATOM   2802  NZ  LYS A 326      -5.255 -20.250 -26.189  1.00122.66           N  
ANISOU 2802  NZ  LYS A 326    23544  12895  10164  -2156  -2848    527       N  
ATOM   2803  N   ALA A 327      -1.149 -16.855 -20.782  1.00 68.99           N  
ANISOU 2803  N   ALA A 327    13737   7995   4480  -2113  -1299    840       N  
ATOM   2804  CA  ALA A 327      -0.415 -16.549 -19.552  1.00 67.08           C  
ANISOU 2804  CA  ALA A 327    12941   8039   4506  -2065  -1114    896       C  
ATOM   2805  C   ALA A 327      -1.256 -15.658 -18.665  1.00 69.22           C  
ANISOU 2805  C   ALA A 327    12979   8294   5026  -2128  -1460    952       C  
ATOM   2806  O   ALA A 327      -1.425 -15.937 -17.487  1.00 66.48           O  
ANISOU 2806  O   ALA A 327    12247   8056   4957  -2019  -1495    951       O  
ATOM   2807  CB  ALA A 327       0.900 -15.868 -19.859  1.00 69.60           C  
ANISOU 2807  CB  ALA A 327    13210   8558   4678  -2173   -748    965       C  
ATOM   2808  N   THR A 328      -1.784 -14.583 -19.239  1.00 67.37           N  
ANISOU 2808  N   THR A 328    13009   7912   4678  -2301  -1720    992       N  
ATOM   2809  CA  THR A 328      -2.634 -13.656 -18.501  1.00 65.76           C  
ANISOU 2809  CA  THR A 328    12620   7662   4705  -2334  -2066   1017       C  
ATOM   2810  C   THR A 328      -3.837 -14.359 -17.895  1.00 69.00           C  
ANISOU 2810  C   THR A 328    12858   7977   5382  -2196  -2306    956       C  
ATOM   2811  O   THR A 328      -4.276 -14.012 -16.803  1.00 67.06           O  
ANISOU 2811  O   THR A 328    12268   7817   5396  -2132  -2407    956       O  
ATOM   2812  CB  THR A 328      -3.127 -12.532 -19.401  1.00 74.57           C  
ANISOU 2812  CB  THR A 328    14123   8557   5654  -2526  -2377   1052       C  
ATOM   2813  OG1 THR A 328      -2.001 -11.779 -19.850  1.00 75.32           O  
ANISOU 2813  OG1 THR A 328    14344   8763   5512  -2697  -2151   1142       O  
ATOM   2814  CG2 THR A 328      -4.079 -11.615 -18.655  1.00 72.16           C  
ANISOU 2814  CG2 THR A 328    13621   8176   5619  -2511  -2757   1043       C  
ATOM   2815  N   GLN A 329      -4.366 -15.346 -18.608  1.00 66.91           N  
ANISOU 2815  N   GLN A 329    12849   7530   5045  -2158  -2392    909       N  
ATOM   2816  CA  GLN A 329      -5.448 -16.173 -18.085  1.00 66.03           C  
ANISOU 2816  CA  GLN A 329    12561   7330   5197  -2055  -2600    879       C  
ATOM   2817  C   GLN A 329      -4.975 -17.026 -16.901  1.00 68.29           C  
ANISOU 2817  C   GLN A 329    12438   7851   5656  -1914  -2337    880       C  
ATOM   2818  O   GLN A 329      -5.640 -17.093 -15.868  1.00 66.77           O  
ANISOU 2818  O   GLN A 329    11912   7725   5732  -1862  -2430    893       O  
ATOM   2819  CB  GLN A 329      -6.005 -17.068 -19.197  1.00 69.44           C  
ANISOU 2819  CB  GLN A 329    13417   7478   5487  -2069  -2785    845       C  
ATOM   2820  CG  GLN A 329      -7.188 -17.939 -18.780  1.00 84.60           C  
ANISOU 2820  CG  GLN A 329    15176   9270   7700  -2007  -3055    846       C  
ATOM   2821  CD  GLN A 329      -7.791 -18.704 -19.944  1.00107.48           C  
ANISOU 2821  CD  GLN A 329    18547  11828  10462  -2046  -3334    827       C  
ATOM   2822  OE1 GLN A 329      -8.013 -18.145 -21.028  1.00104.51           O  
ANISOU 2822  OE1 GLN A 329    18615  11216   9879  -2159  -3555    821       O  
ATOM   2823  NE2 GLN A 329      -8.063 -19.993 -19.726  1.00 99.27           N  
ANISOU 2823  NE2 GLN A 329    17460  10732   9526  -1965  -3362    824       N  
ATOM   2824  N   MET A 330      -3.824 -17.669 -17.056  1.00 64.86           N  
ANISOU 2824  N   MET A 330    12041   7535   5069  -1853  -2008    865       N  
ATOM   2825  CA  MET A 330      -3.273 -18.538 -16.018  1.00 63.25           C  
ANISOU 2825  CA  MET A 330    11500   7511   5020  -1721  -1798    866       C  
ATOM   2826  C   MET A 330      -3.075 -17.794 -14.703  1.00 64.89           C  
ANISOU 2826  C   MET A 330    11308   7926   5422  -1721  -1756    917       C  
ATOM   2827  O   MET A 330      -3.586 -18.205 -13.665  1.00 62.99           O  
ANISOU 2827  O   MET A 330    10811   7738   5383  -1665  -1817    932       O  
ATOM   2828  CB  MET A 330      -1.937 -19.106 -16.489  1.00 66.96           C  
ANISOU 2828  CB  MET A 330    12057   8071   5314  -1646  -1451    830       C  
ATOM   2829  CG  MET A 330      -1.275 -20.058 -15.527  1.00 69.84           C  
ANISOU 2829  CG  MET A 330    12111   8576   5847  -1497  -1277    823       C  
ATOM   2830  SD  MET A 330       0.246 -20.681 -16.246  1.00 76.50           S  
ANISOU 2830  SD  MET A 330    13042   9499   6525  -1374   -873    752       S  
ATOM   2831  CE  MET A 330       1.314 -19.246 -16.083  1.00 73.34           C  
ANISOU 2831  CE  MET A 330    12421   9329   6116  -1503   -650    842       C  
ATOM   2832  N   VAL A 331      -2.340 -16.690 -14.766  1.00 61.37           N  
ANISOU 2832  N   VAL A 331    10845   7581   4893  -1800  -1660    952       N  
ATOM   2833  CA  VAL A 331      -2.000 -15.907 -13.573  1.00 59.53           C  
ANISOU 2833  CA  VAL A 331    10298   7516   4806  -1803  -1640   1000       C  
ATOM   2834  C   VAL A 331      -3.185 -15.145 -12.959  1.00 62.01           C  
ANISOU 2834  C   VAL A 331    10522   7775   5265  -1814  -1911    987       C  
ATOM   2835  O   VAL A 331      -3.060 -14.586 -11.872  1.00 60.60           O  
ANISOU 2835  O   VAL A 331    10119   7713   5193  -1786  -1910   1004       O  
ATOM   2836  CB  VAL A 331      -0.848 -14.922 -13.858  1.00 64.14           C  
ANISOU 2836  CB  VAL A 331    10898   8199   5272  -1908  -1498   1061       C  
ATOM   2837  CG1 VAL A 331       0.412 -15.685 -14.219  1.00 65.20           C  
ANISOU 2837  CG1 VAL A 331    10995   8440   5338  -1863  -1167   1070       C  
ATOM   2838  CG2 VAL A 331      -1.220 -13.965 -14.968  1.00 65.24           C  
ANISOU 2838  CG2 VAL A 331    11370   8192   5227  -2060  -1657   1071       C  
ATOM   2839  N   ALA A 332      -4.322 -15.114 -13.653  1.00 58.82           N  
ANISOU 2839  N   ALA A 332    10298   7180   4872  -1842  -2151    950       N  
ATOM   2840  CA  ALA A 332      -5.576 -14.662 -13.051  1.00 57.97           C  
ANISOU 2840  CA  ALA A 332    10035   7018   4973  -1809  -2386    919       C  
ATOM   2841  C   ALA A 332      -6.078 -15.713 -12.067  1.00 61.08           C  
ANISOU 2841  C   ALA A 332    10162   7498   5549  -1717  -2309    923       C  
ATOM   2842  O   ALA A 332      -6.638 -15.393 -11.023  1.00 60.12           O  
ANISOU 2842  O   ALA A 332     9792   7464   5586  -1663  -2323    910       O  
ATOM   2843  CB  ALA A 332      -6.616 -14.415 -14.119  1.00 59.97           C  
ANISOU 2843  CB  ALA A 332    10532   7016   5236  -1870  -2698    890       C  
ATOM   2844  N   ILE A 333      -5.865 -16.975 -12.412  1.00 57.89           N  
ANISOU 2844  N   ILE A 333     9836   7058   5100  -1702  -2223    940       N  
ATOM   2845  CA  ILE A 333      -6.323 -18.079 -11.588  1.00 57.18           C  
ANISOU 2845  CA  ILE A 333     9546   7018   5163  -1654  -2184    969       C  
ATOM   2846  C   ILE A 333      -5.363 -18.341 -10.425  1.00 59.77           C  
ANISOU 2846  C   ILE A 333     9675   7549   5485  -1600  -1951   1000       C  
ATOM   2847  O   ILE A 333      -5.803 -18.744  -9.348  1.00 59.11           O  
ANISOU 2847  O   ILE A 333     9386   7549   5523  -1581  -1921   1032       O  
ATOM   2848  CB  ILE A 333      -6.526 -19.362 -12.440  1.00 61.26           C  
ANISOU 2848  CB  ILE A 333    10274   7363   5638  -1660  -2260    975       C  
ATOM   2849  CG1 ILE A 333      -7.515 -19.100 -13.590  1.00 63.04           C  
ANISOU 2849  CG1 ILE A 333    10740   7340   5872  -1729  -2558    955       C  
ATOM   2850  CG2 ILE A 333      -7.006 -20.519 -11.577  1.00 61.78           C  
ANISOU 2850  CG2 ILE A 333    10148   7461   5864  -1644  -2257   1030       C  
ATOM   2851  CD1 ILE A 333      -8.790 -18.341 -13.191  1.00 70.79           C  
ANISOU 2851  CD1 ILE A 333    11504   8289   7105  -1756  -2773    959       C  
ATOM   2852  N   VAL A 334      -4.066 -18.114 -10.629  1.00 55.81           N  
ANISOU 2852  N   VAL A 334     9234   7119   4851  -1588  -1794   1001       N  
ATOM   2853  CA  VAL A 334      -3.090 -18.245  -9.539  1.00 54.67           C  
ANISOU 2853  CA  VAL A 334     8901   7134   4735  -1544  -1634   1039       C  
ATOM   2854  C   VAL A 334      -3.404 -17.198  -8.480  1.00 57.43           C  
ANISOU 2854  C   VAL A 334     9100   7578   5144  -1554  -1681   1047       C  
ATOM   2855  O   VAL A 334      -3.323 -17.464  -7.284  1.00 56.60           O  
ANISOU 2855  O   VAL A 334     8850   7564   5092  -1525  -1630   1077       O  
ATOM   2856  CB  VAL A 334      -1.625 -18.078 -10.033  1.00 59.16           C  
ANISOU 2856  CB  VAL A 334     9512   7759   5206  -1538  -1467   1048       C  
ATOM   2857  CG1 VAL A 334      -0.665 -17.937  -8.868  1.00 58.49           C  
ANISOU 2857  CG1 VAL A 334     9214   7810   5201  -1512  -1383   1101       C  
ATOM   2858  CG2 VAL A 334      -1.213 -19.255 -10.895  1.00 60.18           C  
ANISOU 2858  CG2 VAL A 334     9779   7812   5274  -1475  -1366   1013       C  
ATOM   2859  N   LEU A 335      -3.779 -16.012  -8.942  1.00 54.05           N  
ANISOU 2859  N   LEU A 335     8748   7102   4685  -1593  -1797   1013       N  
ATOM   2860  CA  LEU A 335      -4.220 -14.944  -8.069  1.00 53.62           C  
ANISOU 2860  CA  LEU A 335     8596   7097   4681  -1571  -1875    986       C  
ATOM   2861  C   LEU A 335      -5.531 -15.312  -7.393  1.00 57.69           C  
ANISOU 2861  C   LEU A 335     8967   7620   5331  -1520  -1906    955       C  
ATOM   2862  O   LEU A 335      -5.684 -15.116  -6.195  1.00 57.03           O  
ANISOU 2862  O   LEU A 335     8758   7640   5273  -1471  -1838    948       O  
ATOM   2863  CB  LEU A 335      -4.397 -13.660  -8.874  1.00 54.25           C  
ANISOU 2863  CB  LEU A 335     8824   7076   4710  -1620  -2046    950       C  
ATOM   2864  CG  LEU A 335      -4.887 -12.422  -8.124  1.00 59.25           C  
ANISOU 2864  CG  LEU A 335     9403   7715   5395  -1570  -2177    893       C  
ATOM   2865  CD1 LEU A 335      -4.040 -12.146  -6.882  1.00 58.70           C  
ANISOU 2865  CD1 LEU A 335     9248   7773   5285  -1538  -2081    924       C  
ATOM   2866  CD2 LEU A 335      -4.884 -11.231  -9.068  1.00 62.79           C  
ANISOU 2866  CD2 LEU A 335    10051   8027   5781  -1643  -2390    875       C  
ATOM   2867  N   GLY A 336      -6.479 -15.837  -8.165  1.00 55.30           N  
ANISOU 2867  N   GLY A 336     8693   7203   5116  -1540  -2008    944       N  
ATOM   2868  CA  GLY A 336      -7.755 -16.301  -7.616  1.00 56.03           C  
ANISOU 2868  CA  GLY A 336     8597   7307   5387  -1519  -2027    941       C  
ATOM   2869  C   GLY A 336      -7.550 -17.304  -6.495  1.00 60.30           C  
ANISOU 2869  C   GLY A 336     9010   7977   5923  -1522  -1844   1010       C  
ATOM   2870  O   GLY A 336      -8.122 -17.164  -5.413  1.00 60.23           O  
ANISOU 2870  O   GLY A 336     8836   8079   5971  -1494  -1748   1006       O  
ATOM   2871  N   ALA A 337      -6.714 -18.308  -6.759  1.00 56.79           N  
ANISOU 2871  N   ALA A 337     8668   7511   5399  -1551  -1795   1067       N  
ATOM   2872  CA  ALA A 337      -6.344 -19.317  -5.767  1.00 56.60           C  
ANISOU 2872  CA  ALA A 337     8580   7568   5358  -1565  -1677   1141       C  
ATOM   2873  C   ALA A 337      -5.891 -18.674  -4.461  1.00 60.88           C  
ANISOU 2873  C   ALA A 337     9053   8250   5828  -1534  -1566   1141       C  
ATOM   2874  O   ALA A 337      -6.308 -19.080  -3.368  1.00 61.20           O  
ANISOU 2874  O   ALA A 337     9012   8371   5871  -1559  -1480   1187       O  
ATOM   2875  CB  ALA A 337      -5.238 -20.210  -6.310  1.00 56.96           C  
ANISOU 2875  CB  ALA A 337     8760   7552   5332  -1553  -1664   1165       C  
ATOM   2876  N   PHE A 338      -5.035 -17.667  -4.580  1.00 57.10           N  
ANISOU 2876  N   PHE A 338     8639   7786   5270  -1498  -1581   1101       N  
ATOM   2877  CA  PHE A 338      -4.500 -16.987  -3.412  1.00 56.96           C  
ANISOU 2877  CA  PHE A 338     8614   7855   5172  -1471  -1537   1102       C  
ATOM   2878  C   PHE A 338      -5.631 -16.408  -2.572  1.00 61.89           C  
ANISOU 2878  C   PHE A 338     9163   8545   5808  -1430  -1490   1046       C  
ATOM   2879  O   PHE A 338      -5.835 -16.817  -1.431  1.00 62.06           O  
ANISOU 2879  O   PHE A 338     9161   8643   5775  -1440  -1381   1081       O  
ATOM   2880  CB  PHE A 338      -3.527 -15.888  -3.837  1.00 58.26           C  
ANISOU 2880  CB  PHE A 338     8857   7997   5281  -1463  -1610   1081       C  
ATOM   2881  CG  PHE A 338      -2.653 -15.394  -2.730  1.00 59.96           C  
ANISOU 2881  CG  PHE A 338     9102   8257   5425  -1455  -1622   1112       C  
ATOM   2882  CD1 PHE A 338      -1.388 -15.934  -2.536  1.00 63.21           C  
ANISOU 2882  CD1 PHE A 338     9505   8665   5846  -1483  -1620   1194       C  
ATOM   2883  CD2 PHE A 338      -3.087 -14.383  -1.885  1.00 62.74           C  
ANISOU 2883  CD2 PHE A 338     9497   8630   5712  -1407  -1661   1053       C  
ATOM   2884  CE1 PHE A 338      -0.570 -15.477  -1.513  1.00 64.65           C  
ANISOU 2884  CE1 PHE A 338     9727   8850   5987  -1490  -1694   1239       C  
ATOM   2885  CE2 PHE A 338      -2.279 -13.919  -0.861  1.00 66.09           C  
ANISOU 2885  CE2 PHE A 338    10009   9055   6047  -1405  -1720   1085       C  
ATOM   2886  CZ  PHE A 338      -1.015 -14.468  -0.674  1.00 64.14           C  
ANISOU 2886  CZ  PHE A 338     9757   8789   5823  -1460  -1756   1189       C  
ATOM   2887  N   ILE A 339      -6.389 -15.489  -3.159  1.00 59.24           N  
ANISOU 2887  N   ILE A 339     8797   8168   5543  -1383  -1570    957       N  
ATOM   2888  CA  ILE A 339      -7.392 -14.740  -2.412  1.00 60.69           C  
ANISOU 2888  CA  ILE A 339     8889   8410   5762  -1296  -1520    867       C  
ATOM   2889  C   ILE A 339      -8.404 -15.669  -1.774  1.00 66.71           C  
ANISOU 2889  C   ILE A 339     9482   9260   6604  -1324  -1352    908       C  
ATOM   2890  O   ILE A 339      -8.912 -15.370  -0.705  1.00 67.60           O  
ANISOU 2890  O   ILE A 339     9537   9477   6669  -1266  -1197    864       O  
ATOM   2891  CB  ILE A 339      -8.139 -13.716  -3.292  1.00 64.34           C  
ANISOU 2891  CB  ILE A 339     9323   8774   6351  -1230  -1685    760       C  
ATOM   2892  CG1 ILE A 339      -7.189 -12.616  -3.769  1.00 63.86           C  
ANISOU 2892  CG1 ILE A 339     9451   8629   6184  -1227  -1854    731       C  
ATOM   2893  CG2 ILE A 339      -9.286 -13.071  -2.516  1.00 67.17           C  
ANISOU 2893  CG2 ILE A 339     9528   9193   6800  -1100  -1607    644       C  
ATOM   2894  CD1 ILE A 339      -7.626 -11.976  -5.061  1.00 71.51           C  
ANISOU 2894  CD1 ILE A 339    10478   9446   7247  -1240  -2075    682       C  
ATOM   2895  N   VAL A 340      -8.697 -16.793  -2.425  1.00 63.94           N  
ANISOU 2895  N   VAL A 340     9073   8862   6361  -1420  -1381    995       N  
ATOM   2896  CA  VAL A 340      -9.603 -17.791  -1.852  1.00 65.35           C  
ANISOU 2896  CA  VAL A 340     9090   9113   6626  -1497  -1247   1077       C  
ATOM   2897  C   VAL A 340      -8.939 -18.475  -0.658  1.00 69.42           C  
ANISOU 2897  C   VAL A 340     9706   9717   6952  -1561  -1102   1168       C  
ATOM   2898  O   VAL A 340      -9.596 -18.734   0.347  1.00 70.44           O  
ANISOU 2898  O   VAL A 340     9751   9962   7049  -1601   -914   1205       O  
ATOM   2899  CB  VAL A 340     -10.041 -18.837  -2.903  1.00 69.20           C  
ANISOU 2899  CB  VAL A 340     9538   9479   7276  -1598  -1388   1160       C  
ATOM   2900  CG1 VAL A 340     -10.874 -19.926  -2.263  1.00 70.78           C  
ANISOU 2900  CG1 VAL A 340     9581   9746   7567  -1721  -1276   1284       C  
ATOM   2901  CG2 VAL A 340     -10.825 -18.165  -4.018  1.00 69.28           C  
ANISOU 2901  CG2 VAL A 340     9476   9369   7477  -1552  -1572   1081       C  
ATOM   2902  N   CYS A 341      -7.636 -18.734  -0.764  1.00 65.06           N  
ANISOU 2902  N   CYS A 341     9335   9105   6280  -1573  -1190   1204       N  
ATOM   2903  CA  CYS A 341      -6.871 -19.367   0.324  1.00 65.29           C  
ANISOU 2903  CA  CYS A 341     9492   9167   6150  -1632  -1134   1293       C  
ATOM   2904  C   CYS A 341      -6.591 -18.467   1.525  1.00 68.47           C  
ANISOU 2904  C   CYS A 341    10003   9645   6369  -1576  -1047   1244       C  
ATOM   2905  O   CYS A 341      -6.672 -18.918   2.674  1.00 69.88           O  
ANISOU 2905  O   CYS A 341    10268   9878   6403  -1642   -936   1310       O  
ATOM   2906  CB  CYS A 341      -5.531 -19.895  -0.191  1.00 64.63           C  
ANISOU 2906  CB  CYS A 341     9523   8977   6055  -1636  -1277   1335       C  
ATOM   2907  SG  CYS A 341      -5.635 -21.499  -0.986  1.00 68.76           S  
ANISOU 2907  SG  CYS A 341    10042   9391   6694  -1715  -1364   1425       S  
ATOM   2908  N   TRP A 342      -6.245 -17.209   1.260  1.00 62.84           N  
ANISOU 2908  N   TRP A 342     9330   8910   5637  -1467  -1122   1135       N  
ATOM   2909  CA  TRP A 342      -5.777 -16.307   2.314  1.00 62.91           C  
ANISOU 2909  CA  TRP A 342     9508   8937   5459  -1404  -1116   1085       C  
ATOM   2910  C   TRP A 342      -6.825 -15.320   2.851  1.00 66.85           C  
ANISOU 2910  C   TRP A 342     9976   9514   5909  -1286   -978    949       C  
ATOM   2911  O   TRP A 342      -6.674 -14.834   3.966  1.00 68.11           O  
ANISOU 2911  O   TRP A 342    10318   9698   5864  -1238   -915    909       O  
ATOM   2912  CB  TRP A 342      -4.515 -15.558   1.856  1.00 60.54           C  
ANISOU 2912  CB  TRP A 342     9310   8539   5153  -1376  -1326   1076       C  
ATOM   2913  CG  TRP A 342      -3.250 -16.401   1.911  1.00 61.01           C  
ANISOU 2913  CG  TRP A 342     9430   8535   5218  -1459  -1429   1199       C  
ATOM   2914  CD1 TRP A 342      -2.568 -16.934   0.850  1.00 62.79           C  
ANISOU 2914  CD1 TRP A 342     9569   8708   5582  -1487  -1500   1244       C  
ATOM   2915  CD2 TRP A 342      -2.530 -16.800   3.086  1.00 61.79           C  
ANISOU 2915  CD2 TRP A 342     9691   8597   5188  -1508  -1481   1280       C  
ATOM   2916  NE1 TRP A 342      -1.471 -17.640   1.293  1.00 62.43           N  
ANISOU 2916  NE1 TRP A 342     9572   8606   5543  -1528  -1583   1338       N  
ATOM   2917  CE2 TRP A 342      -1.426 -17.575   2.661  1.00 65.01           C  
ANISOU 2917  CE2 TRP A 342    10057   8928   5717  -1553  -1604   1371       C  
ATOM   2918  CE3 TRP A 342      -2.713 -16.583   4.456  1.00 64.78           C  
ANISOU 2918  CE3 TRP A 342    10274   8987   5351  -1515  -1442   1280       C  
ATOM   2919  CZ2 TRP A 342      -0.508 -18.126   3.557  1.00 65.10           C  
ANISOU 2919  CZ2 TRP A 342    10194   8855   5687  -1605  -1737   1467       C  
ATOM   2920  CZ3 TRP A 342      -1.799 -17.138   5.349  1.00 67.02           C  
ANISOU 2920  CZ3 TRP A 342    10742   9179   5544  -1590  -1577   1387       C  
ATOM   2921  CH2 TRP A 342      -0.712 -17.900   4.893  1.00 66.87           C  
ANISOU 2921  CH2 TRP A 342    10646   9066   5695  -1636  -1745   1482       C  
ATOM   2922  N   LEU A 343      -7.880 -15.024   2.095  1.00 62.21           N  
ANISOU 2922  N   LEU A 343     9177   8948   5512  -1225   -944    869       N  
ATOM   2923  CA  LEU A 343      -8.926 -14.106   2.583  1.00 63.49           C  
ANISOU 2923  CA  LEU A 343     9259   9182   5684  -1075   -804    717       C  
ATOM   2924  C   LEU A 343      -9.623 -14.621   3.847  1.00 69.19           C  
ANISOU 2924  C   LEU A 343     9960  10054   6273  -1097   -486    738       C  
ATOM   2925  O   LEU A 343      -9.898 -13.840   4.757  1.00 70.87           O  
ANISOU 2925  O   LEU A 343    10279  10323   6325   -965   -343    616       O  
ATOM   2926  CB  LEU A 343      -9.961 -13.798   1.488  1.00 63.60           C  
ANISOU 2926  CB  LEU A 343     9011   9163   5991  -1013   -870    641       C  
ATOM   2927  CG  LEU A 343     -11.216 -12.985   1.832  1.00 70.57           C  
ANISOU 2927  CG  LEU A 343     9707  10112   6995   -835   -730    474       C  
ATOM   2928  CD1 LEU A 343     -10.881 -11.715   2.584  1.00 71.50           C  
ANISOU 2928  CD1 LEU A 343    10045  10208   6915   -654   -745    314       C  
ATOM   2929  CD2 LEU A 343     -11.975 -12.660   0.563  1.00 72.64           C  
ANISOU 2929  CD2 LEU A 343     9752  10267   7579   -792   -930    418       C  
ATOM   2930  N   PRO A 344      -9.913 -15.932   3.910  1.00 65.42           N  
ANISOU 2930  N   PRO A 344     9377   9636   5843  -1269   -374    895       N  
ATOM   2931  CA  PRO A 344     -10.483 -16.498   5.132  1.00 67.94           C  
ANISOU 2931  CA  PRO A 344     9716  10100   5997  -1346    -64    955       C  
ATOM   2932  C   PRO A 344      -9.677 -16.164   6.386  1.00 72.62           C  
ANISOU 2932  C   PRO A 344    10690  10685   6218  -1328    -22    940       C  
ATOM   2933  O   PRO A 344     -10.242 -15.697   7.374  1.00 75.15           O  
ANISOU 2933  O   PRO A 344    11090  11112   6351  -1246    242    849       O  
ATOM   2934  CB  PRO A 344     -10.444 -17.998   4.860  1.00 69.07           C  
ANISOU 2934  CB  PRO A 344     9794  10229   6221  -1575   -101   1164       C  
ATOM   2935  CG  PRO A 344     -10.590 -18.092   3.392  1.00 71.53           C  
ANISOU 2935  CG  PRO A 344     9904  10437   6836  -1562   -323   1157       C  
ATOM   2936  CD  PRO A 344      -9.847 -16.932   2.831  1.00 65.08           C  
ANISOU 2936  CD  PRO A 344     9204   9519   6004  -1403   -527   1020       C  
ATOM   2937  N   PHE A 345      -8.365 -16.387   6.323  1.00 66.83           N  
ANISOU 2937  N   PHE A 345    10191   9812   5390  -1396   -288   1022       N  
ATOM   2938  CA  PHE A 345      -7.468 -16.114   7.445  1.00 67.21           C  
ANISOU 2938  CA  PHE A 345    10625   9793   5118  -1401   -351   1032       C  
ATOM   2939  C   PHE A 345      -7.474 -14.644   7.857  1.00 71.97           C  
ANISOU 2939  C   PHE A 345    11392  10372   5581  -1195   -361    841       C  
ATOM   2940  O   PHE A 345      -7.710 -14.317   9.017  1.00 74.09           O  
ANISOU 2940  O   PHE A 345    11912  10680   5559  -1146   -186    779       O  
ATOM   2941  CB  PHE A 345      -6.039 -16.544   7.102  1.00 66.52           C  
ANISOU 2941  CB  PHE A 345    10666   9541   5066  -1490   -686   1150       C  
ATOM   2942  CG  PHE A 345      -5.039 -16.231   8.178  1.00 68.91           C  
ANISOU 2942  CG  PHE A 345    11355   9728   5100  -1505   -842   1176       C  
ATOM   2943  CD1 PHE A 345      -4.871 -17.086   9.258  1.00 73.90           C  
ANISOU 2943  CD1 PHE A 345    12241  10336   5501  -1652   -801   1300       C  
ATOM   2944  CD2 PHE A 345      -4.267 -15.076   8.115  1.00 70.21           C  
ANISOU 2944  CD2 PHE A 345    11656   9779   5242  -1394  -1072   1093       C  
ATOM   2945  CE1 PHE A 345      -3.950 -16.793  10.262  1.00 75.94           C  
ANISOU 2945  CE1 PHE A 345    12899  10445   5510  -1675  -1002   1331       C  
ATOM   2946  CE2 PHE A 345      -3.342 -14.777   9.108  1.00 74.17           C  
ANISOU 2946  CE2 PHE A 345    12527  10137   5518  -1420  -1275   1130       C  
ATOM   2947  CZ  PHE A 345      -3.184 -15.635  10.182  1.00 74.19           C  
ANISOU 2947  CZ  PHE A 345    12795  10102   5291  -1554  -1248   1245       C  
ATOM   2948  N   PHE A 346      -7.215 -13.758   6.905  1.00 66.87           N  
ANISOU 2948  N   PHE A 346    10644   9645   5120  -1079   -576    746       N  
ATOM   2949  CA  PHE A 346      -7.074 -12.339   7.221  1.00 67.62           C  
ANISOU 2949  CA  PHE A 346    10934   9664   5094   -892   -681    576       C  
ATOM   2950  C   PHE A 346      -8.347 -11.731   7.818  1.00 74.92           C  
ANISOU 2950  C   PHE A 346    11814  10710   5943   -705   -370    387       C  
ATOM   2951  O   PHE A 346      -8.285 -10.731   8.531  1.00 75.93           O  
ANISOU 2951  O   PHE A 346    12213  10779   5857   -541   -389    237       O  
ATOM   2952  CB  PHE A 346      -6.588 -11.555   5.995  1.00 66.84           C  
ANISOU 2952  CB  PHE A 346    10731   9446   5218   -844   -987    538       C  
ATOM   2953  CG  PHE A 346      -5.092 -11.616   5.799  1.00 66.22           C  
ANISOU 2953  CG  PHE A 346    10810   9228   5123   -966  -1294    673       C  
ATOM   2954  CD1 PHE A 346      -4.274 -10.598   6.269  1.00 69.58           C  
ANISOU 2954  CD1 PHE A 346    11519   9512   5405   -917  -1542    637       C  
ATOM   2955  CD2 PHE A 346      -4.501 -12.702   5.169  1.00 66.16           C  
ANISOU 2955  CD2 PHE A 346    10658   9221   5259  -1124  -1342    834       C  
ATOM   2956  CE1 PHE A 346      -2.895 -10.658   6.099  1.00 69.03           C  
ANISOU 2956  CE1 PHE A 346    11532   9319   5377  -1044  -1825    781       C  
ATOM   2957  CE2 PHE A 346      -3.124 -12.768   4.995  1.00 67.54           C  
ANISOU 2957  CE2 PHE A 346    10916   9281   5465  -1216  -1593    950       C  
ATOM   2958  CZ  PHE A 346      -2.323 -11.748   5.463  1.00 66.19           C  
ANISOU 2958  CZ  PHE A 346    10976   8986   5190  -1186  -1829    933       C  
ATOM   2959  N   LEU A 347      -9.494 -12.347   7.541  1.00 72.92           N  
ANISOU 2959  N   LEU A 347    11215  10616   5876   -724    -90    394       N  
ATOM   2960  CA  LEU A 347     -10.749 -11.937   8.169  1.00 76.51           C  
ANISOU 2960  CA  LEU A 347    11550  11222   6298   -554    279    230       C  
ATOM   2961  C   LEU A 347     -10.873 -12.524   9.574  1.00 83.11           C  
ANISOU 2961  C   LEU A 347    12634  12176   6769   -641    615    288       C  
ATOM   2962  O   LEU A 347     -11.343 -11.847  10.486  1.00 86.03           O  
ANISOU 2962  O   LEU A 347    13173  12607   6906   -465    865    119       O  
ATOM   2963  CB  LEU A 347     -11.961 -12.334   7.309  1.00 77.09           C  
ANISOU 2963  CB  LEU A 347    11110  11412   6770   -555    428    231       C  
ATOM   2964  CG  LEU A 347     -12.239 -11.508   6.041  1.00 80.46           C  
ANISOU 2964  CG  LEU A 347    11306  11722   7543   -411    150    110       C  
ATOM   2965  CD1 LEU A 347     -13.324 -12.172   5.207  1.00 81.19           C  
ANISOU 2965  CD1 LEU A 347    10928  11890   8030   -478    232    171       C  
ATOM   2966  CD2 LEU A 347     -12.619 -10.056   6.354  1.00 85.24           C  
ANISOU 2966  CD2 LEU A 347    11993  12280   8115   -101    143   -161       C  
ATOM   2967  N   THR A 348     -10.451 -13.776   9.749  1.00 78.80           N  
ANISOU 2967  N   THR A 348    12143  11645   6154   -909    614    521       N  
ATOM   2968  CA  THR A 348     -10.554 -14.438  11.056  1.00 81.85           C  
ANISOU 2968  CA  THR A 348    12806  12121   6171  -1047    903    614       C  
ATOM   2969  C   THR A 348      -9.536 -13.903  12.063  1.00 86.92           C  
ANISOU 2969  C   THR A 348    14029  12604   6392  -1012    732    577       C  
ATOM   2970  O   THR A 348      -9.900 -13.587  13.194  1.00 90.08           O  
ANISOU 2970  O   THR A 348    14728  13067   6433   -943   1015    485       O  
ATOM   2971  CB  THR A 348     -10.421 -15.990  10.957  1.00 88.69           C  
ANISOU 2971  CB  THR A 348    13591  13014   7094  -1363    895    888       C  
ATOM   2972  OG1 THR A 348      -9.724 -16.350   9.760  1.00 84.40           O  
ANISOU 2972  OG1 THR A 348    12880  12334   6853  -1424    513    976       O  
ATOM   2973  CG2 THR A 348     -11.789 -16.654  10.938  1.00 89.78           C  
ANISOU 2973  CG2 THR A 348    13340  13377   7396  -1456   1299    948       C  
ATOM   2974  N   HIS A 349      -8.273 -13.791  11.653  1.00 80.91           N  
ANISOU 2974  N   HIS A 349    13431  11631   5678  -1059    273    648       N  
ATOM   2975  CA  HIS A 349      -7.208 -13.337  12.558  1.00 81.78           C  
ANISOU 2975  CA  HIS A 349    14080  11546   5446  -1058     17    649       C  
ATOM   2976  C   HIS A 349      -7.398 -11.883  13.007  1.00 88.77           C  
ANISOU 2976  C   HIS A 349    15212  12375   6143   -784     25    400       C  
ATOM   2977  O   HIS A 349      -7.060 -11.535  14.137  1.00 91.22           O  
ANISOU 2977  O   HIS A 349    16030  12581   6048   -756      6    357       O  
ATOM   2978  CB  HIS A 349      -5.819 -13.520  11.927  1.00 78.94           C  
ANISOU 2978  CB  HIS A 349    13744  10981   5268  -1167   -478    790       C  
ATOM   2979  CG  HIS A 349      -4.697 -13.485  12.922  1.00 83.48           C  
ANISOU 2979  CG  HIS A 349    14832  11341   5546  -1253   -773    874       C  
ATOM   2980  ND1 HIS A 349      -4.097 -14.627  13.409  1.00 85.48           N  
ANISOU 2980  ND1 HIS A 349    15253  11516   5711  -1479   -888   1079       N  
ATOM   2981  CD2 HIS A 349      -4.078 -12.447  13.535  1.00 86.56           C  
ANISOU 2981  CD2 HIS A 349    15625  11546   5717  -1148  -1023    785       C  
ATOM   2982  CE1 HIS A 349      -3.153 -14.295  14.274  1.00 86.30           C  
ANISOU 2982  CE1 HIS A 349    15829  11392   5568  -1511  -1202   1116       C  
ATOM   2983  NE2 HIS A 349      -3.121 -12.977  14.368  1.00 87.29           N  
ANISOU 2983  NE2 HIS A 349    16111  11450   5607  -1318  -1290    944       N  
ATOM   2984  N   VAL A 350      -7.934 -11.042  12.128  1.00 85.20           N  
ANISOU 2984  N   VAL A 350    14441  11960   5972   -583     19    234       N  
ATOM   2985  CA  VAL A 350      -8.275  -9.666  12.491  1.00 87.85           C  
ANISOU 2985  CA  VAL A 350    14976  12236   6166   -290     31    -29       C  
ATOM   2986  C   VAL A 350      -9.404  -9.645  13.517  1.00 98.32           C  
ANISOU 2986  C   VAL A 350    16393  13748   7216   -155    566   -180       C  
ATOM   2987  O   VAL A 350      -9.334  -8.935  14.518  1.00101.08           O  
ANISOU 2987  O   VAL A 350    17211  14016   7180      1    617   -333       O  
ATOM   2988  CB  VAL A 350      -8.699  -8.842  11.257  1.00 89.83           C  
ANISOU 2988  CB  VAL A 350    14841  12474   6816   -114   -112   -167       C  
ATOM   2989  CG1 VAL A 350      -9.499  -7.617  11.678  1.00 93.17           C  
ANISOU 2989  CG1 VAL A 350    15368  12894   7138    225     32   -472       C  
ATOM   2990  CG2 VAL A 350      -7.471  -8.439  10.437  1.00 85.92           C  
ANISOU 2990  CG2 VAL A 350    14407  11762   6477   -204   -647    -67       C  
ATOM   2991  N   LEU A 351     -10.435 -10.442  13.268  1.00 97.32           N  
ANISOU 2991  N   LEU A 351    15826  13867   7285   -224    968   -130       N  
ATOM   2992  CA  LEU A 351     -11.631 -10.438  14.108  1.00102.94           C  
ANISOU 2992  CA  LEU A 351    16494  14804   7815   -100   1551   -266       C  
ATOM   2993  C   LEU A 351     -11.483 -11.235  15.415  1.00111.49           C  
ANISOU 2993  C   LEU A 351    18013  15948   8402   -305   1830   -131       C  
ATOM   2994  O   LEU A 351     -12.299 -11.074  16.326  1.00115.93           O  
ANISOU 2994  O   LEU A 351    18695  16673   8681   -193   2327   -262       O  
ATOM   2995  CB  LEU A 351     -12.836 -10.936  13.301  1.00103.24           C  
ANISOU 2995  CB  LEU A 351    15841  15073   8313   -111   1850   -246       C  
ATOM   2996  CG  LEU A 351     -13.242 -10.014  12.143  1.00106.37           C  
ANISOU 2996  CG  LEU A 351    15846  15406   9164    134   1629   -426       C  
ATOM   2997  CD1 LEU A 351     -14.083 -10.756  11.119  1.00105.47           C  
ANISOU 2997  CD1 LEU A 351    15095  15429   9550     18   1718   -311       C  
ATOM   2998  CD2 LEU A 351     -13.980  -8.783  12.661  1.00113.04           C  
ANISOU 2998  CD2 LEU A 351    16749  16277   9922    526   1858   -764       C  
ATOM   2999  N   ASN A 352     -10.462 -12.088  15.510  1.00106.94           N  
ANISOU 2999  N   ASN A 352    17678  15235   7720   -600   1519    124       N  
ATOM   3000  CA  ASN A 352     -10.175 -12.811  16.760  1.00110.38           C  
ANISOU 3000  CA  ASN A 352    18624  15657   7659   -818   1668    268       C  
ATOM   3001  C   ASN A 352      -9.491 -11.895  17.779  1.00118.41           C  
ANISOU 3001  C   ASN A 352    20352  16451   8186   -675   1487    126       C  
ATOM   3002  O   ASN A 352      -9.769 -11.971  18.982  1.00122.60           O  
ANISOU 3002  O   ASN A 352    21347  17022   8213   -696   1808     92       O  
ATOM   3003  CB  ASN A 352      -9.305 -14.051  16.494  1.00108.05           C  
ANISOU 3003  CB  ASN A 352    18342  15250   7460  -1165   1333    582       C  
ATOM   3004  CG  ASN A 352      -9.073 -14.903  17.749  1.00135.35           C  
ANISOU 3004  CG  ASN A 352    22326  18673  10427  -1428   1450    758       C  
ATOM   3005  OD1 ASN A 352      -9.885 -14.915  18.678  1.00135.31           O  
ANISOU 3005  OD1 ASN A 352    22519  18833  10058  -1426   1946    700       O  
ATOM   3006  ND2 ASN A 352      -7.960 -15.627  17.768  1.00124.85           N  
ANISOU 3006  ND2 ASN A 352    21225  17121   9090  -1656    992    974       N  
ATOM   3007  N   THR A 353      -8.606 -11.030  17.285  1.00113.60           N  
ANISOU 3007  N   THR A 353    19848  15598   7716   -543    966     53       N  
ATOM   3008  CA  THR A 353      -7.827 -10.134  18.140  1.00116.10           C  
ANISOU 3008  CA  THR A 353    20846  15643   7626   -427    660    -55       C  
ATOM   3009  C   THR A 353      -8.507  -8.772  18.373  1.00125.15           C  
ANISOU 3009  C   THR A 353    22112  16798   8642    -33    844   -403       C  
ATOM   3010  O   THR A 353      -8.242  -8.115  19.383  1.00128.32           O  
ANISOU 3010  O   THR A 353    23160  17026   8572     91    784   -536       O  
ATOM   3011  CB  THR A 353      -6.398  -9.947  17.581  1.00119.51           C  
ANISOU 3011  CB  THR A 353    21360  15775   8271   -534    -46     87       C  
ATOM   3012  OG1 THR A 353      -6.462  -9.492  16.225  1.00115.65           O  
ANISOU 3012  OG1 THR A 353    20318  15326   8299   -427   -207     36       O  
ATOM   3013  CG2 THR A 353      -5.629 -11.268  17.632  1.00115.76           C  
ANISOU 3013  CG2 THR A 353    20901  15240   7840   -884   -245    399       C  
ATOM   3014  N   HIS A 354      -9.375  -8.355  17.448  1.00122.39           N  
ANISOU 3014  N   HIS A 354    21174  16620   8710    169   1032   -555       N  
ATOM   3015  CA  HIS A 354     -10.241  -7.187  17.656  1.00126.87           C  
ANISOU 3015  CA  HIS A 354    21763  17232   9210    570   1285   -906       C  
ATOM   3016  C   HIS A 354     -11.635  -7.816  17.781  1.00137.49           C  
ANISOU 3016  C   HIS A 354    22650  18948  10640    596   2005   -949       C  
ATOM   3017  O   HIS A 354     -12.300  -8.085  16.780  1.00135.09           O  
ANISOU 3017  O   HIS A 354    21671  18813  10845    595   2110   -922       O  
ATOM   3018  CB  HIS A 354     -10.135  -6.221  16.475  1.00124.25           C  
ANISOU 3018  CB  HIS A 354    21101  16773   9335    765    880  -1030       C  
ATOM   3019  CG  HIS A 354      -8.760  -5.659  16.276  1.00124.50           C  
ANISOU 3019  CG  HIS A 354    21506  16463   9335    686    186   -941       C  
ATOM   3020  ND1 HIS A 354      -8.442  -4.348  16.557  1.00127.88           N  
ANISOU 3020  ND1 HIS A 354    22363  16636   9592    939   -141  -1154       N  
ATOM   3021  CD2 HIS A 354      -7.619  -6.233  15.825  1.00121.89           C  
ANISOU 3021  CD2 HIS A 354    21165  16000   9147    380   -245   -657       C  
ATOM   3022  CE1 HIS A 354      -7.166  -4.137  16.289  1.00124.19           C  
ANISOU 3022  CE1 HIS A 354    22117  15898   9171    762   -749   -981       C  
ATOM   3023  NE2 HIS A 354      -6.644  -5.265  15.843  1.00121.04           N  
ANISOU 3023  NE2 HIS A 354    21438  15580   8972    433   -802   -685       N  
ATOM   3024  N   CYS A 355     -12.056  -8.051  19.022  1.00142.41           N  
ANISOU 3024  N   CYS A 355    23665  19687  10756    600   2487  -1002       N  
ATOM   3025  CA  CYS A 355     -13.180  -8.940  19.305  1.00146.98           C  
ANISOU 3025  CA  CYS A 355    23870  20625  11351    488   3176   -934       C  
ATOM   3026  C   CYS A 355     -14.368  -8.294  20.029  1.00158.86           C  
ANISOU 3026  C   CYS A 355    25367  22345  12648    834   3846  -1253       C  
ATOM   3027  O   CYS A 355     -14.219  -7.518  20.972  1.00162.59           O  
ANISOU 3027  O   CYS A 355    26468  22694  12616   1064   3923  -1478       O  
ATOM   3028  CB  CYS A 355     -12.793 -10.235  20.028  1.00148.51           C  
ANISOU 3028  CB  CYS A 355    24375  20859  11192     60   3288   -615       C  
ATOM   3029  SG  CYS A 355     -14.162 -11.053  20.881  1.00159.38           S  
ANISOU 3029  SG  CYS A 355    25574  22653  12331    -59   4224   -574       S  
ATOM   3030  N   GLN A 356     -15.528  -8.676  19.489  1.00157.23           N  
ANISOU 3030  N   GLN A 356    24402  22448  12888    856   4294  -1255       N  
ATOM   3031  CA  GLN A 356     -16.881  -8.274  19.849  1.00163.49           C  
ANISOU 3031  CA  GLN A 356    24852  23529  13736   1161   4997  -1518       C  
ATOM   3032  C   GLN A 356     -17.740  -9.094  18.877  1.00165.88           C  
ANISOU 3032  C   GLN A 356    24242  24086  14700    983   5178  -1332       C  
ATOM   3033  O   GLN A 356     -17.701  -8.870  17.667  1.00161.05           O  
ANISOU 3033  O   GLN A 356    23170  23370  14651   1038   4744  -1328       O  
ATOM   3034  CB  GLN A 356     -17.086  -6.779  19.623  1.00166.21           C  
ANISOU 3034  CB  GLN A 356    25220  23723  14210   1687   4837  -1928       C  
ATOM   3035  CG  GLN A 356     -18.465  -6.276  20.017  1.00188.22           C  
ANISOU 3035  CG  GLN A 356    27644  26788  17083   2073   5559  -2248       C  
ATOM   3036  CD  GLN A 356     -19.580  -7.007  19.297  1.00207.82           C  
ANISOU 3036  CD  GLN A 356    29166  29594  20201   1955   5933  -2117       C  
ATOM   3037  OE1 GLN A 356     -20.020  -6.592  18.225  1.00200.94           O  
ANISOU 3037  OE1 GLN A 356    27691  28688  19970   2134   5683  -2211       O  
ATOM   3038  NE2 GLN A 356     -20.044  -8.104  19.885  1.00202.95           N  
ANISOU 3038  NE2 GLN A 356    28427  29274  19411   1631   6503  -1882       N  
ATOM   3039  N   THR A 357     -18.493 -10.056  19.407  1.00166.22           N  
ANISOU 3039  N   THR A 357    24060  24440  14657    741   5791  -1161       N  
ATOM   3040  CA  THR A 357     -18.997 -11.197  18.655  1.00163.97           C  
ANISOU 3040  CA  THR A 357    23098  24336  14867    397   5851   -851       C  
ATOM   3041  C   THR A 357     -18.079 -12.299  18.123  1.00161.31           C  
ANISOU 3041  C   THR A 357    22852  23844  14594    -58   5331   -467       C  
ATOM   3042  O   THR A 357     -18.235 -12.766  16.995  1.00157.05           O  
ANISOU 3042  O   THR A 357    21762  23296  14614   -185   5051   -317       O  
ATOM   3043  CB  THR A 357     -19.614 -10.433  17.471  1.00170.66           C  
ANISOU 3043  CB  THR A 357    23263  25160  16420    723   5647  -1057       C  
ATOM   3044  N   CYS A 358     -17.119 -12.702  18.952  1.00156.97           N  
ANISOU 3044  N   CYS A 358    23028  23149  13464   -285   5185   -322       N  
ATOM   3045  CA  CYS A 358     -16.117 -13.695  18.587  1.00151.32           C  
ANISOU 3045  CA  CYS A 358    22488  22248  12759   -674   4666     10       C  
ATOM   3046  C   CYS A 358     -16.844 -15.014  18.345  1.00155.96           C  
ANISOU 3046  C   CYS A 358    22583  23066  13609  -1043   4947    315       C  
ATOM   3047  O   CYS A 358     -16.993 -15.816  19.268  1.00159.24           O  
ANISOU 3047  O   CYS A 358    23276  23601  13627  -1336   5293    505       O  
ATOM   3048  CB  CYS A 358     -15.685 -13.623  20.054  1.00155.69           C  
ANISOU 3048  CB  CYS A 358    23868  22747  12540   -727   4878    -13       C  
ATOM   3049  SG  CYS A 358     -14.086 -13.002  20.317  1.00155.87           S  
ANISOU 3049  SG  CYS A 358    24685  22336  12201   -661   4159    -63       S  
ATOM   3050  N   HIS A 359     -17.287 -15.254  17.114  1.00149.28           N  
ANISOU 3050  N   HIS A 359    21051  22259  13411  -1054   4768    376       N  
ATOM   3051  CA  HIS A 359     -17.873 -16.547  16.797  1.00149.38           C  
ANISOU 3051  CA  HIS A 359    20631  22428  13699  -1430   4910    691       C  
ATOM   3052  C   HIS A 359     -16.642 -17.144  16.107  1.00146.03           C  
ANISOU 3052  C   HIS A 359    20436  21705  13344  -1630   4203    885       C  
ATOM   3053  O   HIS A 359     -16.651 -17.413  14.898  1.00141.43           O  
ANISOU 3053  O   HIS A 359    19424  21043  13268  -1657   3852    954       O  
ATOM   3054  CB  HIS A 359     -19.082 -16.426  15.851  1.00151.08           C  
ANISOU 3054  CB  HIS A 359    19990  22820  14593  -1308   5082    635       C  
ATOM   3055  CG  HIS A 359     -20.001 -17.613  15.861  1.00157.53           C  
ANISOU 3055  CG  HIS A 359    20352  23866  15636  -1673   5420    933       C  
ATOM   3056  ND1 HIS A 359     -20.468 -18.201  14.704  1.00156.97           N  
ANISOU 3056  ND1 HIS A 359    19680  23776  16184  -1810   5161   1094       N  
ATOM   3057  CD2 HIS A 359     -20.558 -18.307  16.885  1.00164.86           C  
ANISOU 3057  CD2 HIS A 359    21353  25037  16250  -1947   5985   1110       C  
ATOM   3058  CE1 HIS A 359     -21.265 -19.210  15.013  1.00160.34           C  
ANISOU 3058  CE1 HIS A 359    19810  24414  16696  -2155   5522   1365       C  
ATOM   3059  NE2 HIS A 359     -21.336 -19.296  16.330  1.00165.45           N  
ANISOU 3059  NE2 HIS A 359    20844  25235  16784  -2255   6041   1387       N  
ATOM   3060  N   VAL A 360     -15.580 -17.327  16.901  1.00141.35           N  
ANISOU 3060  N   VAL A 360    20541  20934  12233  -1756   3997    959       N  
ATOM   3061  CA  VAL A 360     -14.240 -17.667  16.404  1.00134.99           C  
ANISOU 3061  CA  VAL A 360    20021  19819  11449  -1867   3325   1082       C  
ATOM   3062  C   VAL A 360     -13.600 -18.779  17.250  1.00138.32           C  
ANISOU 3062  C   VAL A 360    20954  20143  11459  -2244   3231   1361       C  
ATOM   3063  O   VAL A 360     -12.750 -18.526  18.110  1.00138.41           O  
ANISOU 3063  O   VAL A 360    21607  19979  11003  -2246   3071   1337       O  
ATOM   3064  CB  VAL A 360     -13.327 -16.408  16.366  1.00136.32           C  
ANISOU 3064  CB  VAL A 360    20540  19764  11490  -1546   2967    833       C  
ATOM   3065  CG1 VAL A 360     -13.187 -15.791  17.763  1.00140.48           C  
ANISOU 3065  CG1 VAL A 360    21705  20277  11393  -1445   3222    695       C  
ATOM   3066  CG2 VAL A 360     -11.964 -16.739  15.757  1.00130.70           C  
ANISOU 3066  CG2 VAL A 360    20013  18760  10887  -1655   2304    965       C  
ATOM   3067  N   SER A 361     -14.028 -20.012  16.988  1.00134.11           N  
ANISOU 3067  N   SER A 361    20146  19694  11116  -2570   3285   1632       N  
ATOM   3068  CA  SER A 361     -13.515 -21.187  17.686  1.00134.51           C  
ANISOU 3068  CA  SER A 361    20637  19634  10837  -2958   3153   1923       C  
ATOM   3069  C   SER A 361     -12.171 -21.609  17.087  1.00131.92           C  
ANISOU 3069  C   SER A 361    20501  18975  10649  -3007   2444   2015       C  
ATOM   3070  O   SER A 361     -12.019 -21.595  15.865  1.00127.15           O  
ANISOU 3070  O   SER A 361    19476  18310  10525  -2894   2151   1980       O  
ATOM   3071  CB  SER A 361     -14.517 -22.342  17.581  1.00140.45           C  
ANISOU 3071  CB  SER A 361    21004  20585  11775  -3297   3446   2187       C  
ATOM   3072  OG  SER A 361     -14.830 -22.628  16.227  1.00144.84           O  
ANISOU 3072  OG  SER A 361    20944  21138  12951  -3263   3217   2219       O  
ATOM   3073  N   PRO A 362     -11.196 -22.005  17.939  1.00128.29           N  
ANISOU 3073  N   PRO A 362    20678  18289   9776  -3175   2165   2134       N  
ATOM   3074  CA  PRO A 362      -9.880 -22.456  17.451  1.00123.34           C  
ANISOU 3074  CA  PRO A 362    20213  17343   9307  -3216   1499   2224       C  
ATOM   3075  C   PRO A 362      -9.928 -23.571  16.396  1.00122.91           C  
ANISOU 3075  C   PRO A 362    19738  17252   9712  -3378   1255   2405       C  
ATOM   3076  O   PRO A 362      -8.968 -23.733  15.641  1.00118.32           O  
ANISOU 3076  O   PRO A 362    19105  16455   9395  -3301    769   2402       O  
ATOM   3077  CB  PRO A 362      -9.186 -22.968  18.721  1.00128.10           C  
ANISOU 3077  CB  PRO A 362    21543  17747   9384  -3459   1334   2382       C  
ATOM   3078  CG  PRO A 362      -9.844 -22.251  19.837  1.00137.76           C  
ANISOU 3078  CG  PRO A 362    23100  19138  10105  -3411   1852   2266       C  
ATOM   3079  CD  PRO A 362     -11.267 -22.035  19.414  1.00135.07           C  
ANISOU 3079  CD  PRO A 362    22158  19166   9997  -3331   2450   2185       C  
ATOM   3080  N   GLU A 363     -11.025 -24.328  16.354  1.00120.93           N  
ANISOU 3080  N   GLU A 363    19198  17200   9552  -3600   1588   2561       N  
ATOM   3081  CA  GLU A 363     -11.226 -25.357  15.328  1.00117.98           C  
ANISOU 3081  CA  GLU A 363    18428  16784   9615  -3748   1362   2725       C  
ATOM   3082  C   GLU A 363     -11.262 -24.685  13.958  1.00116.67           C  
ANISOU 3082  C   GLU A 363    17764  16631   9933  -3442   1228   2529       C  
ATOM   3083  O   GLU A 363     -10.603 -25.136  13.018  1.00112.63           O  
ANISOU 3083  O   GLU A 363    17146  15934   9714  -3411    803   2557       O  
ATOM   3084  CB  GLU A 363     -12.529 -26.153  15.549  1.00123.30           C  
ANISOU 3084  CB  GLU A 363    18843  17684  10321  -4049   1767   2933       C  
ATOM   3085  CG  GLU A 363     -12.904 -26.485  17.009  1.00138.48           C  
ANISOU 3085  CG  GLU A 363    21199  19715  11700  -4338   2145   3091       C  
ATOM   3086  CD  GLU A 363     -11.739 -27.006  17.842  1.00156.69           C  
ANISOU 3086  CD  GLU A 363    24215  21726  13594  -4509   1747   3215       C  
ATOM   3087  OE1 GLU A 363     -10.853 -27.691  17.287  1.00145.21           O  
ANISOU 3087  OE1 GLU A 363    22830  19995  12347  -4548   1180   3299       O  
ATOM   3088  OE2 GLU A 363     -11.713 -26.733  19.062  1.00152.80           O  
ANISOU 3088  OE2 GLU A 363    24226  21263  12566  -4599   1994   3222       O  
ATOM   3089  N   LEU A 364     -12.033 -23.600  13.866  1.00113.35           N  
ANISOU 3089  N   LEU A 364    17067  16420   9581  -3212   1595   2324       N  
ATOM   3090  CA  LEU A 364     -12.109 -22.788  12.651  1.00109.19           C  
ANISOU 3090  CA  LEU A 364    16129  15894   9466  -2917   1471   2122       C  
ATOM   3091  C   LEU A 364     -10.733 -22.227  12.295  1.00107.81           C  
ANISOU 3091  C   LEU A 364    16206  15482   9274  -2723   1025   2000       C  
ATOM   3092  O   LEU A 364     -10.266 -22.392  11.167  1.00103.55           O  
ANISOU 3092  O   LEU A 364    15467  14817   9061  -2656    693   1990       O  
ATOM   3093  CB  LEU A 364     -13.102 -21.631  12.837  1.00111.64           C  
ANISOU 3093  CB  LEU A 364    16187  16437   9796  -2683   1919   1904       C  
ATOM   3094  CG  LEU A 364     -13.499 -20.839  11.585  1.00113.56           C  
ANISOU 3094  CG  LEU A 364    15954  16694  10498  -2416   1825   1717       C  
ATOM   3095  CD1 LEU A 364     -14.636 -21.536  10.847  1.00114.75           C  
ANISOU 3095  CD1 LEU A 364    15567  16960  11071  -2557   1937   1845       C  
ATOM   3096  CD2 LEU A 364     -13.896 -19.415  11.945  1.00117.31           C  
ANISOU 3096  CD2 LEU A 364    16408  17282  10884  -2096   2097   1434       C  
ATOM   3097  N   TYR A 365     -10.090 -21.584  13.270  1.00104.72           N  
ANISOU 3097  N   TYR A 365    16266  15025   8496  -2647   1022   1917       N  
ATOM   3098  CA  TYR A 365      -8.791 -20.934  13.067  1.00101.16           C  
ANISOU 3098  CA  TYR A 365    16051  14355   8031  -2477    609   1813       C  
ATOM   3099  C   TYR A 365      -7.753 -21.867  12.437  1.00101.62           C  
ANISOU 3099  C   TYR A 365    16124  14193   8293  -2589    144   1959       C  
ATOM   3100  O   TYR A 365      -7.027 -21.461  11.528  1.00 97.88           O  
ANISOU 3100  O   TYR A 365    15507  13611   8072  -2430   -140   1874       O  
ATOM   3101  CB  TYR A 365      -8.260 -20.372  14.391  1.00104.81           C  
ANISOU 3101  CB  TYR A 365    17081  14733   8008  -2458    623   1765       C  
ATOM   3102  CG  TYR A 365      -6.950 -19.614  14.266  1.00103.86           C  
ANISOU 3102  CG  TYR A 365    17194  14378   7891  -2299    181   1673       C  
ATOM   3103  CD1 TYR A 365      -6.913 -18.326  13.730  1.00104.25           C  
ANISOU 3103  CD1 TYR A 365    17095  14441   8075  -2023    152   1456       C  
ATOM   3104  CD2 TYR A 365      -5.747 -20.184  14.688  1.00104.08           C  
ANISOU 3104  CD2 TYR A 365    17580  14153   7813  -2436   -236   1816       C  
ATOM   3105  CE1 TYR A 365      -5.711 -17.625  13.613  1.00103.12           C  
ANISOU 3105  CE1 TYR A 365    17147  14081   7952  -1914   -262   1403       C  
ATOM   3106  CE2 TYR A 365      -4.541 -19.492  14.576  1.00103.09           C  
ANISOU 3106  CE2 TYR A 365    17614  13813   7744  -2309   -648   1754       C  
ATOM   3107  CZ  TYR A 365      -4.529 -18.213  14.039  1.00108.68           C  
ANISOU 3107  CZ  TYR A 365    18162  14555   8576  -2061   -649   1557       C  
ATOM   3108  OH  TYR A 365      -3.337 -17.530  13.933  1.00107.80           O  
ANISOU 3108  OH  TYR A 365    18194  14230   8534  -1973  -1065   1527       O  
ATOM   3109  N   SER A 366      -7.690 -23.108  12.915  1.00 99.36           N  
ANISOU 3109  N   SER A 366    16016  13839   7895  -2858     75   2176       N  
ATOM   3110  CA  SER A 366      -6.772 -24.104  12.358  1.00 96.76           C  
ANISOU 3110  CA  SER A 366    15701  13290   7773  -2947   -361   2305       C  
ATOM   3111  C   SER A 366      -7.032 -24.346  10.875  1.00 97.52           C  
ANISOU 3111  C   SER A 366    15328  13413   8314  -2856   -435   2268       C  
ATOM   3112  O   SER A 366      -6.093 -24.548  10.103  1.00 94.46           O  
ANISOU 3112  O   SER A 366    14886  12859   8143  -2765   -771   2247       O  
ATOM   3113  CB  SER A 366      -6.882 -25.420  13.117  1.00102.88           C  
ANISOU 3113  CB  SER A 366    16744  13988   8358  -3265   -413   2547       C  
ATOM   3114  OG  SER A 366      -6.476 -25.242  14.458  1.00114.08           O  
ANISOU 3114  OG  SER A 366    18684  15325   9337  -3362   -422   2591       O  
ATOM   3115  N   ALA A 367      -8.303 -24.323  10.481  1.00 94.79           N  
ANISOU 3115  N   ALA A 367    14647  13265   8103  -2880   -123   2259       N  
ATOM   3116  CA  ALA A 367      -8.671 -24.473   9.077  1.00 92.18           C  
ANISOU 3116  CA  ALA A 367    13912  12940   8173  -2799   -207   2219       C  
ATOM   3117  C   ALA A 367      -8.161 -23.284   8.258  1.00 93.16           C  
ANISOU 3117  C   ALA A 367    13910  13040   8447  -2515   -309   2004       C  
ATOM   3118  O   ALA A 367      -7.390 -23.468   7.313  1.00 89.99           O  
ANISOU 3118  O   ALA A 367    13451  12497   8242  -2436   -591   1980       O  
ATOM   3119  CB  ALA A 367     -10.177 -24.614   8.930  1.00 95.10           C  
ANISOU 3119  CB  ALA A 367    13946  13510   8679  -2894    121   2264       C  
ATOM   3120  N   THR A 368      -8.571 -22.072   8.641  1.00 90.51           N  
ANISOU 3120  N   THR A 368    13554  12834   8001  -2364    -76   1849       N  
ATOM   3121  CA  THR A 368      -8.200 -20.849   7.907  1.00 87.82           C  
ANISOU 3121  CA  THR A 368    13111  12466   7789  -2116   -180   1653       C  
ATOM   3122  C   THR A 368      -6.698 -20.743   7.687  1.00 89.82           C  
ANISOU 3122  C   THR A 368    13565  12528   8032  -2061   -532   1650       C  
ATOM   3123  O   THR A 368      -6.260 -20.251   6.650  1.00 87.16           O  
ANISOU 3123  O   THR A 368    13084  12135   7900  -1934   -692   1565       O  
ATOM   3124  CB  THR A 368      -8.677 -19.560   8.617  1.00 95.92           C  
ANISOU 3124  CB  THR A 368    14205  13611   8630  -1953     67   1483       C  
ATOM   3125  OG1 THR A 368      -8.204 -19.544   9.970  1.00 97.61           O  
ANISOU 3125  OG1 THR A 368    14836  13796   8457  -2018    114   1521       O  
ATOM   3126  CG2 THR A 368     -10.190 -19.465   8.613  1.00 96.44           C  
ANISOU 3126  CG2 THR A 368    13952  13880   8809  -1943    433   1442       C  
ATOM   3127  N   THR A 369      -5.920 -21.197   8.669  1.00 87.92           N  
ANISOU 3127  N   THR A 369    13658  12185   7564  -2167   -654   1752       N  
ATOM   3128  CA  THR A 369      -4.468 -21.280   8.540  1.00 86.41           C  
ANISOU 3128  CA  THR A 369    13614  11797   7420  -2137  -1012   1780       C  
ATOM   3129  C   THR A 369      -4.088 -22.443   7.627  1.00 89.56           C  
ANISOU 3129  C   THR A 369    13854  12098   8077  -2196  -1198   1872       C  
ATOM   3130  O   THR A 369      -3.256 -22.280   6.736  1.00 87.02           O  
ANISOU 3130  O   THR A 369    13410  11692   7960  -2086  -1383   1823       O  
ATOM   3131  CB  THR A 369      -3.784 -21.468   9.906  1.00 96.93           C  
ANISOU 3131  CB  THR A 369    15371  13006   8452  -2242  -1144   1869       C  
ATOM   3132  OG1 THR A 369      -4.534 -22.406  10.677  1.00 99.55           O  
ANISOU 3132  OG1 THR A 369    15843  13391   8590  -2444   -973   2002       O  
ATOM   3133  CG2 THR A 369      -3.709 -20.154  10.671  1.00 96.79           C  
ANISOU 3133  CG2 THR A 369    15586  13003   8186  -2129  -1084   1747       C  
ATOM   3134  N   TRP A 370      -4.697 -23.609   7.842  1.00 88.19           N  
ANISOU 3134  N   TRP A 370    13693  11931   7884  -2369  -1144   2006       N  
ATOM   3135  CA  TRP A 370      -4.434 -24.777   6.992  1.00 87.44           C  
ANISOU 3135  CA  TRP A 370    13489  11717   8018  -2413  -1341   2084       C  
ATOM   3136  C   TRP A 370      -4.657 -24.423   5.523  1.00 88.11           C  
ANISOU 3136  C   TRP A 370    13270  11840   8368  -2266  -1320   1968       C  
ATOM   3137  O   TRP A 370      -3.790 -24.639   4.673  1.00 86.25           O  
ANISOU 3137  O   TRP A 370    12981  11489   8302  -2165  -1510   1928       O  
ATOM   3138  CB  TRP A 370      -5.323 -25.970   7.390  1.00 88.88           C  
ANISOU 3138  CB  TRP A 370    13716  11911   8143  -2645  -1274   2252       C  
ATOM   3139  CG  TRP A 370      -5.119 -27.203   6.520  1.00 89.64           C  
ANISOU 3139  CG  TRP A 370    13745  11851   8464  -2684  -1515   2325       C  
ATOM   3140  CD1 TRP A 370      -4.114 -28.131   6.633  1.00 92.89           C  
ANISOU 3140  CD1 TRP A 370    14339  12042   8913  -2703  -1835   2393       C  
ATOM   3141  CD2 TRP A 370      -5.935 -27.632   5.410  1.00 89.02           C  
ANISOU 3141  CD2 TRP A 370    13426  11793   8607  -2689  -1488   2324       C  
ATOM   3142  NE1 TRP A 370      -4.252 -29.102   5.664  1.00 92.08           N  
ANISOU 3142  NE1 TRP A 370    14137  11829   9020  -2701  -1986   2418       N  
ATOM   3143  CE2 TRP A 370      -5.359 -28.821   4.902  1.00 92.97           C  
ANISOU 3143  CE2 TRP A 370    14011  12078   9234  -2704  -1788   2383       C  
ATOM   3144  CE3 TRP A 370      -7.095 -27.129   4.801  1.00 90.20           C  
ANISOU 3144  CE3 TRP A 370    13307  12092   8872  -2676  -1275   2275       C  
ATOM   3145  CZ2 TRP A 370      -5.906 -29.517   3.810  1.00 92.04           C  
ANISOU 3145  CZ2 TRP A 370    13767  11887   9316  -2712  -1880   2396       C  
ATOM   3146  CZ3 TRP A 370      -7.636 -27.820   3.713  1.00 91.44           C  
ANISOU 3146  CZ3 TRP A 370    13318  12171   9256  -2703  -1391   2304       C  
ATOM   3147  CH2 TRP A 370      -7.039 -29.001   3.232  1.00 91.99           C  
ANISOU 3147  CH2 TRP A 370    13524  12019   9407  -2724  -1690   2364       C  
ATOM   3148  N   LEU A 371      -5.826 -23.864   5.241  1.00 83.99           N  
ANISOU 3148  N   LEU A 371    12560  11474   7880  -2253  -1086   1910       N  
ATOM   3149  CA  LEU A 371      -6.192 -23.459   3.892  1.00 81.62           C  
ANISOU 3149  CA  LEU A 371    12016  11189   7808  -2136  -1089   1807       C  
ATOM   3150  C   LEU A 371      -5.125 -22.566   3.272  1.00 83.00           C  
ANISOU 3150  C   LEU A 371    12200  11308   8029  -1964  -1212   1685       C  
ATOM   3151  O   LEU A 371      -4.812 -22.694   2.089  1.00 80.88           O  
ANISOU 3151  O   LEU A 371    11841  10968   7921  -1894  -1315   1641       O  
ATOM   3152  CB  LEU A 371      -7.518 -22.708   3.932  1.00 82.62           C  
ANISOU 3152  CB  LEU A 371    11949  11479   7962  -2120   -841   1743       C  
ATOM   3153  CG  LEU A 371      -8.175 -22.416   2.591  1.00 86.22           C  
ANISOU 3153  CG  LEU A 371    12164  11924   8670  -2043   -879   1665       C  
ATOM   3154  CD1 LEU A 371      -8.763 -23.690   2.004  1.00 87.03           C  
ANISOU 3154  CD1 LEU A 371    12182  11951   8936  -2185   -974   1792       C  
ATOM   3155  CD2 LEU A 371      -9.242 -21.364   2.774  1.00 89.74           C  
ANISOU 3155  CD2 LEU A 371    12425  12514   9157  -1965   -671   1561       C  
ATOM   3156  N   GLY A 372      -4.580 -21.663   4.087  1.00 79.78           N  
ANISOU 3156  N   GLY A 372    11924  10924   7464  -1911  -1200   1639       N  
ATOM   3157  CA  GLY A 372      -3.565 -20.707   3.650  1.00 78.00           C  
ANISOU 3157  CA  GLY A 372    11706  10650   7280  -1784  -1324   1553       C  
ATOM   3158  C   GLY A 372      -2.268 -21.351   3.208  1.00 80.77           C  
ANISOU 3158  C   GLY A 372    12070  10868   7752  -1770  -1529   1601       C  
ATOM   3159  O   GLY A 372      -1.624 -20.873   2.275  1.00 78.77           O  
ANISOU 3159  O   GLY A 372    11716  10590   7622  -1682  -1585   1542       O  
ATOM   3160  N   TYR A 373      -1.883 -22.434   3.875  1.00 78.61           N  
ANISOU 3160  N   TYR A 373    11919  10503   7446  -1855  -1636   1710       N  
ATOM   3161  CA  TYR A 373      -0.672 -23.173   3.511  1.00 78.30           C  
ANISOU 3161  CA  TYR A 373    11867  10320   7563  -1814  -1840   1744       C  
ATOM   3162  C   TYR A 373      -0.888 -24.096   2.304  1.00 82.51           C  
ANISOU 3162  C   TYR A 373    12278  10812   8261  -1776  -1836   1724       C  
ATOM   3163  O   TYR A 373       0.053 -24.350   1.540  1.00 81.93           O  
ANISOU 3163  O   TYR A 373    12125  10662   8345  -1670  -1919   1683       O  
ATOM   3164  CB  TYR A 373      -0.135 -23.958   4.714  1.00 80.88           C  
ANISOU 3164  CB  TYR A 373    12407  10519   7806  -1910  -2025   1861       C  
ATOM   3165  CG  TYR A 373       0.457 -23.065   5.783  1.00 82.95           C  
ANISOU 3165  CG  TYR A 373    12840  10753   7925  -1923  -2117   1876       C  
ATOM   3166  CD1 TYR A 373       1.594 -22.311   5.520  1.00 84.29           C  
ANISOU 3166  CD1 TYR A 373    12923  10868   8234  -1826  -2258   1839       C  
ATOM   3167  CD2 TYR A 373      -0.119 -22.964   7.050  1.00 85.27           C  
ANISOU 3167  CD2 TYR A 373    13401  11064   7935  -2043  -2066   1933       C  
ATOM   3168  CE1 TYR A 373       2.145 -21.487   6.478  1.00 86.07           C  
ANISOU 3168  CE1 TYR A 373    13329  11030   8342  -1848  -2403   1864       C  
ATOM   3169  CE2 TYR A 373       0.428 -22.135   8.018  1.00 87.14           C  
ANISOU 3169  CE2 TYR A 373    13863  11239   8009  -2046  -2183   1937       C  
ATOM   3170  CZ  TYR A 373       1.564 -21.401   7.720  1.00 93.74           C  
ANISOU 3170  CZ  TYR A 373    14614  11992   9009  -1949  -2381   1904       C  
ATOM   3171  OH  TYR A 373       2.138 -20.571   8.647  1.00 95.88           O  
ANISOU 3171  OH  TYR A 373    15125  12165   9139  -1962  -2560   1919       O  
ATOM   3172  N   VAL A 374      -2.119 -24.583   2.125  1.00 79.57           N  
ANISOU 3172  N   VAL A 374    11892  10483   7859  -1860  -1739   1751       N  
ATOM   3173  CA  VAL A 374      -2.472 -25.398   0.950  1.00 79.19           C  
ANISOU 3173  CA  VAL A 374    11777  10367   7946  -1834  -1772   1732       C  
ATOM   3174  C   VAL A 374      -2.163 -24.673  -0.363  1.00 82.02           C  
ANISOU 3174  C   VAL A 374    12026  10744   8394  -1695  -1719   1605       C  
ATOM   3175  O   VAL A 374      -1.765 -25.301  -1.352  1.00 81.58           O  
ANISOU 3175  O   VAL A 374    11976  10589   8433  -1615  -1778   1562       O  
ATOM   3176  CB  VAL A 374      -3.963 -25.770   0.946  1.00 83.76           C  
ANISOU 3176  CB  VAL A 374    12321  10997   8509  -1967  -1688   1793       C  
ATOM   3177  CG1 VAL A 374      -4.344 -26.435  -0.376  1.00 83.34           C  
ANISOU 3177  CG1 VAL A 374    12232  10840   8595  -1935  -1771   1763       C  
ATOM   3178  CG2 VAL A 374      -4.284 -26.671   2.127  1.00 85.43           C  
ANISOU 3178  CG2 VAL A 374    12660  11181   8617  -2145  -1729   1946       C  
ATOM   3179  N   ASN A 375      -2.358 -23.353  -0.353  1.00 77.85           N  
ANISOU 3179  N   ASN A 375    11435  10330   7814  -1671  -1613   1545       N  
ATOM   3180  CA  ASN A 375      -2.123 -22.493  -1.512  1.00 76.49           C  
ANISOU 3180  CA  ASN A 375    11196  10176   7689  -1581  -1571   1445       C  
ATOM   3181  C   ASN A 375      -0.794 -22.743  -2.203  1.00 80.77           C  
ANISOU 3181  C   ASN A 375    11725  10651   8312  -1485  -1609   1414       C  
ATOM   3182  O   ASN A 375      -0.733 -22.787  -3.430  1.00 80.33           O  
ANISOU 3182  O   ASN A 375    11671  10561   8288  -1428  -1571   1349       O  
ATOM   3183  CB  ASN A 375      -2.169 -21.033  -1.088  1.00 75.51           C  
ANISOU 3183  CB  ASN A 375    11049  10150   7492  -1570  -1519   1402       C  
ATOM   3184  CG  ASN A 375      -1.993 -20.096  -2.247  1.00 93.19           C  
ANISOU 3184  CG  ASN A 375    13252  12394   9761  -1516  -1505   1321       C  
ATOM   3185  OD1 ASN A 375      -2.856 -20.000  -3.117  1.00 86.46           O  
ANISOU 3185  OD1 ASN A 375    12390  11524   8935  -1519  -1493   1275       O  
ATOM   3186  ND2 ASN A 375      -0.864 -19.400  -2.275  1.00 84.59           N  
ANISOU 3186  ND2 ASN A 375    12152  11312   8676  -1488  -1533   1319       N  
ATOM   3187  N   SER A 376       0.264 -22.897  -1.412  1.00 77.94           N  
ANISOU 3187  N   SER A 376    11358  10266   7989  -1467  -1684   1460       N  
ATOM   3188  CA  SER A 376       1.613 -23.090  -1.949  1.00 78.33           C  
ANISOU 3188  CA  SER A 376    11322  10267   8171  -1363  -1702   1434       C  
ATOM   3189  C   SER A 376       1.712 -24.270  -2.911  1.00 82.45           C  
ANISOU 3189  C   SER A 376    11869  10691   8768  -1271  -1692   1382       C  
ATOM   3190  O   SER A 376       2.244 -24.125  -4.016  1.00 82.52           O  
ANISOU 3190  O   SER A 376    11829  10706   8817  -1178  -1581   1305       O  
ATOM   3191  CB  SER A 376       2.623 -23.264  -0.814  1.00 83.18           C  
ANISOU 3191  CB  SER A 376    11916  10824   8864  -1365  -1853   1509       C  
ATOM   3192  OG  SER A 376       3.077 -22.000  -0.354  1.00 92.90           O  
ANISOU 3192  OG  SER A 376    13107  12119  10072  -1402  -1871   1532       O  
ATOM   3193  N   ALA A 377       1.190 -25.423  -2.499  1.00 78.71           N  
ANISOU 3193  N   ALA A 377    11499  10117   8291  -1303  -1808   1426       N  
ATOM   3194  CA  ALA A 377       1.258 -26.634  -3.321  1.00 79.11           C  
ANISOU 3194  CA  ALA A 377    11625  10029   8403  -1206  -1857   1373       C  
ATOM   3195  C   ALA A 377       0.335 -26.605  -4.546  1.00 81.48           C  
ANISOU 3195  C   ALA A 377    12017  10315   8625  -1208  -1783   1307       C  
ATOM   3196  O   ALA A 377       0.488 -27.435  -5.443  1.00 82.24           O  
ANISOU 3196  O   ALA A 377    12220  10288   8742  -1101  -1808   1234       O  
ATOM   3197  CB  ALA A 377       0.962 -27.862  -2.474  1.00 80.93           C  
ANISOU 3197  CB  ALA A 377    11972  10125   8651  -1272  -2062   1461       C  
ATOM   3198  N   LEU A 378      -0.611 -25.662  -4.588  1.00 75.67           N  
ANISOU 3198  N   LEU A 378    11264   9681   7805  -1315  -1718   1324       N  
ATOM   3199  CA  LEU A 378      -1.541 -25.535  -5.724  1.00 74.54           C  
ANISOU 3199  CA  LEU A 378    11214   9495   7612  -1334  -1707   1273       C  
ATOM   3200  C   LEU A 378      -0.903 -24.935  -6.983  1.00 78.52           C  
ANISOU 3200  C   LEU A 378    11765  10005   8064  -1236  -1583   1166       C  
ATOM   3201  O   LEU A 378      -1.165 -25.403  -8.091  1.00 78.73           O  
ANISOU 3201  O   LEU A 378    11964   9912   8038  -1191  -1605   1102       O  
ATOM   3202  CB  LEU A 378      -2.771 -24.697  -5.343  1.00 73.36           C  
ANISOU 3202  CB  LEU A 378    11000   9437   7437  -1464  -1700   1318       C  
ATOM   3203  CG  LEU A 378      -3.699 -25.234  -4.254  1.00 77.96           C  
ANISOU 3203  CG  LEU A 378    11538  10037   8045  -1594  -1760   1430       C  
ATOM   3204  CD1 LEU A 378      -4.956 -24.385  -4.187  1.00 77.62           C  
ANISOU 3204  CD1 LEU A 378    11393  10081   8018  -1676  -1714   1437       C  
ATOM   3205  CD2 LEU A 378      -4.050 -26.690  -4.490  1.00 81.44           C  
ANISOU 3205  CD2 LEU A 378    12094  10314   8535  -1632  -1916   1486       C  
ATOM   3206  N   ASN A 379      -0.081 -23.897  -6.821  1.00 74.87           N  
ANISOU 3206  N   ASN A 379    11180   9667   7599  -1222  -1464   1158       N  
ATOM   3207  CA  ASN A 379       0.479 -23.176  -7.979  1.00 74.94           C  
ANISOU 3207  CA  ASN A 379    11231   9705   7536  -1181  -1321   1086       C  
ATOM   3208  C   ASN A 379       1.001 -24.132  -9.059  1.00 80.37           C  
ANISOU 3208  C   ASN A 379    12060  10284   8192  -1047  -1243    995       C  
ATOM   3209  O   ASN A 379       0.549 -24.058 -10.199  1.00 80.30           O  
ANISOU 3209  O   ASN A 379    12261  10199   8049  -1052  -1221    934       O  
ATOM   3210  CB  ASN A 379       1.562 -22.156  -7.570  1.00 74.69           C  
ANISOU 3210  CB  ASN A 379    11019   9808   7550  -1192  -1220   1119       C  
ATOM   3211  CG  ASN A 379       1.022 -21.037  -6.683  1.00 89.95           C  
ANISOU 3211  CG  ASN A 379    12891  11822   9465  -1304  -1303   1179       C  
ATOM   3212  OD1 ASN A 379       0.071 -20.338  -7.042  1.00 78.68           O  
ANISOU 3212  OD1 ASN A 379    11546  10391   7956  -1370  -1342   1160       O  
ATOM   3213  ND2 ASN A 379       1.638 -20.864  -5.515  1.00 82.93           N  
ANISOU 3213  ND2 ASN A 379    11874  10981   8653  -1313  -1353   1242       N  
ATOM   3214  N   PRO A 380       1.918 -25.057  -8.704  1.00 78.10           N  
ANISOU 3214  N   PRO A 380    11688   9963   8022   -917  -1227    974       N  
ATOM   3215  CA  PRO A 380       2.404 -25.998  -9.726  1.00 79.86           C  
ANISOU 3215  CA  PRO A 380    12061  10070   8211   -746  -1140    855       C  
ATOM   3216  C   PRO A 380       1.324 -26.907 -10.344  1.00 83.52           C  
ANISOU 3216  C   PRO A 380    12829  10336   8568   -744  -1310    816       C  
ATOM   3217  O   PRO A 380       1.491 -27.367 -11.477  1.00 84.68           O  
ANISOU 3217  O   PRO A 380    13206  10373   8595   -626  -1233    700       O  
ATOM   3218  CB  PRO A 380       3.459 -26.826  -8.974  1.00 82.92           C  
ANISOU 3218  CB  PRO A 380    12267  10435   8805   -601  -1166    847       C  
ATOM   3219  CG  PRO A 380       3.834 -26.002  -7.803  1.00 86.17           C  
ANISOU 3219  CG  PRO A 380    12427  10980   9334   -710  -1204    964       C  
ATOM   3220  CD  PRO A 380       2.578 -25.299  -7.409  1.00 79.60           C  
ANISOU 3220  CD  PRO A 380    11676  10188   8379   -903  -1306   1045       C  
ATOM   3221  N   VAL A 381       0.239 -27.165  -9.616  1.00 78.56           N  
ANISOU 3221  N   VAL A 381    12213   9657   7980   -880  -1535    915       N  
ATOM   3222  CA  VAL A 381      -0.897 -27.900 -10.173  1.00 78.75           C  
ANISOU 3222  CA  VAL A 381    12490   9489   7943   -929  -1739    917       C  
ATOM   3223  C   VAL A 381      -1.672 -27.038 -11.165  1.00 82.49           C  
ANISOU 3223  C   VAL A 381    13115   9944   8282  -1019  -1733    895       C  
ATOM   3224  O   VAL A 381      -2.264 -27.563 -12.104  1.00 83.30           O  
ANISOU 3224  O   VAL A 381    13504   9851   8293  -1011  -1870    851       O  
ATOM   3225  CB  VAL A 381      -1.843 -28.421  -9.071  1.00 81.86           C  
ANISOU 3225  CB  VAL A 381    12804   9853   8447  -1080  -1959   1058       C  
ATOM   3226  CG1 VAL A 381      -3.212 -28.744  -9.637  1.00 82.06           C  
ANISOU 3226  CG1 VAL A 381    13004   9724   8453  -1201  -2168   1102       C  
ATOM   3227  CG2 VAL A 381      -1.240 -29.648  -8.409  1.00 82.84           C  
ANISOU 3227  CG2 VAL A 381    12936   9875   8664   -996  -2073   1074       C  
ATOM   3228  N   ILE A 382      -1.661 -25.721 -10.971  1.00 77.70           N  
ANISOU 3228  N   ILE A 382    12351   9507   7662  -1105  -1618    925       N  
ATOM   3229  CA  ILE A 382      -2.264 -24.804 -11.948  1.00 77.33           C  
ANISOU 3229  CA  ILE A 382    12466   9425   7491  -1186  -1637    899       C  
ATOM   3230  C   ILE A 382      -1.350 -24.634 -13.162  1.00 81.85           C  
ANISOU 3230  C   ILE A 382    13255   9973   7872  -1091  -1439    792       C  
ATOM   3231  O   ILE A 382      -1.824 -24.601 -14.296  1.00 82.34           O  
ANISOU 3231  O   ILE A 382    13638   9879   7768  -1116  -1512    741       O  
ATOM   3232  CB  ILE A 382      -2.563 -23.420 -11.339  1.00 78.96           C  
ANISOU 3232  CB  ILE A 382    12461   9794   7745  -1300  -1614    959       C  
ATOM   3233  CG1 ILE A 382      -3.472 -23.560 -10.114  1.00 78.61           C  
ANISOU 3233  CG1 ILE A 382    12208   9798   7862  -1381  -1741   1051       C  
ATOM   3234  CG2 ILE A 382      -3.222 -22.515 -12.364  1.00 79.70           C  
ANISOU 3234  CG2 ILE A 382    12747   9806   7730  -1384  -1699    932       C  
ATOM   3235  CD1 ILE A 382      -3.822 -22.239  -9.473  1.00 86.37           C  
ANISOU 3235  CD1 ILE A 382    13010  10924   8884  -1453  -1717   1080       C  
ATOM   3236  N   TYR A 383      -0.043 -24.540 -12.919  1.00 78.55           N  
ANISOU 3236  N   TYR A 383    12665   9701   7479   -991  -1190    763       N  
ATOM   3237  CA  TYR A 383       0.940 -24.402 -14.000  1.00 80.36           C  
ANISOU 3237  CA  TYR A 383    13039   9952   7543   -898   -920    668       C  
ATOM   3238  C   TYR A 383       0.945 -25.603 -14.943  1.00 86.32           C  
ANISOU 3238  C   TYR A 383    14134  10503   8161   -742   -922    541       C  
ATOM   3239  O   TYR A 383       1.211 -25.455 -16.129  1.00 87.80           O  
ANISOU 3239  O   TYR A 383    14613  10636   8110   -708   -759    454       O  
ATOM   3240  CB  TYR A 383       2.357 -24.207 -13.449  1.00 82.17           C  
ANISOU 3240  CB  TYR A 383    12935  10376   7911   -812   -665    674       C  
ATOM   3241  CG  TYR A 383       2.586 -22.949 -12.624  1.00 82.30           C  
ANISOU 3241  CG  TYR A 383    12663  10574   8032   -957   -656    792       C  
ATOM   3242  CD1 TYR A 383       3.422 -22.976 -11.516  1.00 84.07           C  
ANISOU 3242  CD1 TYR A 383    12550  10912   8480   -916   -633    849       C  
ATOM   3243  CD2 TYR A 383       1.989 -21.733 -12.957  1.00 82.02           C  
ANISOU 3243  CD2 TYR A 383    12724  10564   7874  -1131   -713    843       C  
ATOM   3244  CE1 TYR A 383       3.655 -21.842 -10.760  1.00 83.85           C  
ANISOU 3244  CE1 TYR A 383    12311  11016   8532  -1044   -663    954       C  
ATOM   3245  CE2 TYR A 383       2.217 -20.586 -12.199  1.00 81.59           C  
ANISOU 3245  CE2 TYR A 383    12445  10647   7908  -1247   -738    938       C  
ATOM   3246  CZ  TYR A 383       3.053 -20.652 -11.103  1.00 89.33           C  
ANISOU 3246  CZ  TYR A 383    13114  11737   9091  -1203   -709    993       C  
ATOM   3247  OH  TYR A 383       3.298 -19.536 -10.333  1.00 90.06           O  
ANISOU 3247  OH  TYR A 383    13031  11931   9255  -1314   -772   1087       O  
ATOM   3248  N   THR A 384       0.669 -26.791 -14.423  1.00 82.95           N  
ANISOU 3248  N   THR A 384    13709   9948   7860   -652  -1112    532       N  
ATOM   3249  CA  THR A 384       0.547 -27.963 -15.279  1.00 85.10           C  
ANISOU 3249  CA  THR A 384    14355   9978   8002   -501  -1192    411       C  
ATOM   3250  C   THR A 384      -0.818 -28.010 -15.956  1.00 89.04           C  
ANISOU 3250  C   THR A 384    15213  10251   8369   -641  -1499    441       C  
ATOM   3251  O   THR A 384      -0.931 -28.493 -17.077  1.00 90.90           O  
ANISOU 3251  O   THR A 384    15878  10276   8382   -562  -1535    334       O  
ATOM   3252  CB  THR A 384       0.749 -29.258 -14.501  1.00 92.64           C  
ANISOU 3252  CB  THR A 384    15218  10834   9147   -365  -1347    399       C  
ATOM   3253  OG1 THR A 384      -0.222 -29.336 -13.456  1.00 90.00           O  
ANISOU 3253  OG1 THR A 384    14728  10490   8979   -547  -1637    558       O  
ATOM   3254  CG2 THR A 384       2.142 -29.303 -13.911  1.00 91.34           C  
ANISOU 3254  CG2 THR A 384    14714  10842   9148   -202  -1095    356       C  
ATOM   3255  N   THR A 385      -1.851 -27.516 -15.278  1.00 83.54           N  
ANISOU 3255  N   THR A 385    14344   9582   7816   -841  -1727    583       N  
ATOM   3256  CA  THR A 385      -3.212 -27.546 -15.818  1.00 83.61           C  
ANISOU 3256  CA  THR A 385    14606   9371   7790   -985  -2061    634       C  
ATOM   3257  C   THR A 385      -3.360 -26.777 -17.126  1.00 88.91           C  
ANISOU 3257  C   THR A 385    15637   9944   8202  -1036  -2040    572       C  
ATOM   3258  O   THR A 385      -3.889 -27.301 -18.110  1.00 90.90           O  
ANISOU 3258  O   THR A 385    16328   9914   8295  -1032  -2254    522       O  
ATOM   3259  CB  THR A 385      -4.229 -26.959 -14.821  1.00 90.00           C  
ANISOU 3259  CB  THR A 385    15081  10281   8834  -1176  -2233    787       C  
ATOM   3260  OG1 THR A 385      -4.377 -27.855 -13.715  1.00 90.20           O  
ANISOU 3260  OG1 THR A 385    14887  10327   9056  -1179  -2327    868       O  
ATOM   3261  CG2 THR A 385      -5.587 -26.747 -15.486  1.00 88.40           C  
ANISOU 3261  CG2 THR A 385    15078   9865   8645  -1325  -2564    837       C  
ATOM   3262  N   PHE A 386      -2.892 -25.536 -17.133  1.00 84.07           N  
ANISOU 3262  N   PHE A 386    14876   9534   7533  -1098  -1815    585       N  
ATOM   3263  CA  PHE A 386      -3.185 -24.624 -18.235  1.00 84.56           C  
ANISOU 3263  CA  PHE A 386    15265   9500   7364  -1210  -1853    567       C  
ATOM   3264  C   PHE A 386      -2.004 -24.396 -19.190  1.00 89.50           C  
ANISOU 3264  C   PHE A 386    16143  10185   7677  -1126  -1481    461       C  
ATOM   3265  O   PHE A 386      -2.203 -24.288 -20.406  1.00 91.60           O  
ANISOU 3265  O   PHE A 386    16901  10258   7645  -1167  -1530    405       O  
ATOM   3266  CB  PHE A 386      -3.723 -23.320 -17.658  1.00 84.30           C  
ANISOU 3266  CB  PHE A 386    14948   9600   7482  -1377  -1943    671       C  
ATOM   3267  CG  PHE A 386      -4.910 -23.522 -16.753  1.00 84.56           C  
ANISOU 3267  CG  PHE A 386    14716   9596   7818  -1449  -2243    764       C  
ATOM   3268  CD1 PHE A 386      -6.163 -23.790 -17.284  1.00 88.81           C  
ANISOU 3268  CD1 PHE A 386    15467   9866   8412  -1539  -2625    795       C  
ATOM   3269  CD2 PHE A 386      -4.770 -23.478 -15.376  1.00 85.14           C  
ANISOU 3269  CD2 PHE A 386    14337   9892   8121  -1435  -2144    827       C  
ATOM   3270  CE1 PHE A 386      -7.264 -23.988 -16.456  1.00 89.00           C  
ANISOU 3270  CE1 PHE A 386    15192   9877   8746  -1616  -2861    894       C  
ATOM   3271  CE2 PHE A 386      -5.867 -23.673 -14.541  1.00 87.18           C  
ANISOU 3271  CE2 PHE A 386    14354  10139   8630  -1511  -2358    916       C  
ATOM   3272  CZ  PHE A 386      -7.115 -23.929 -15.084  1.00 86.31           C  
ANISOU 3272  CZ  PHE A 386    14398   9793   8605  -1602  -2696    952       C  
ATOM   3273  N   ASN A 387      -0.789 -24.336 -18.642  1.00 84.61           N  
ANISOU 3273  N   ASN A 387    15196   9824   7129  -1020  -1117    441       N  
ATOM   3274  CA  ASN A 387       0.429 -24.199 -19.446  1.00 86.62           C  
ANISOU 3274  CA  ASN A 387    15587  10181   7144   -929   -694    349       C  
ATOM   3275  C   ASN A 387       0.874 -25.552 -19.996  1.00 92.60           C  
ANISOU 3275  C   ASN A 387    16608  10796   7780   -680   -577    187       C  
ATOM   3276  O   ASN A 387       1.120 -26.484 -19.232  1.00 91.53           O  
ANISOU 3276  O   ASN A 387    16236  10669   7872   -518   -614    157       O  
ATOM   3277  CB  ASN A 387       1.563 -23.594 -18.611  1.00 85.84           C  
ANISOU 3277  CB  ASN A 387    14974  10404   7239   -916   -381    406       C  
ATOM   3278  CG  ASN A 387       2.644 -22.948 -19.463  1.00109.67           C  
ANISOU 3278  CG  ASN A 387    18071  13569  10031   -938     45    377       C  
ATOM   3279  OD1 ASN A 387       3.612 -23.601 -19.865  1.00107.25           O  
ANISOU 3279  OD1 ASN A 387    17770  13320   9662   -746    389    264       O  
ATOM   3280  ND2 ASN A 387       2.483 -21.655 -19.740  1.00 99.46           N  
ANISOU 3280  ND2 ASN A 387    16832  12335   8623  -1173     28    482       N  
ATOM   3281  N   ILE A 388       0.985 -25.650 -21.319  1.00 92.10           N  
ANISOU 3281  N   ILE A 388    17071  10583   7339   -647   -450     79       N  
ATOM   3282  CA  ILE A 388       1.431 -26.886 -21.954  1.00 95.09           C  
ANISOU 3282  CA  ILE A 388    17775  10805   7550   -380   -317   -108       C  
ATOM   3283  C   ILE A 388       2.936 -27.079 -21.745  1.00 99.35           C  
ANISOU 3283  C   ILE A 388    17964  11610   8176   -161    206   -203       C  
ATOM   3284  O   ILE A 388       3.376 -28.178 -21.417  1.00100.04           O  
ANISOU 3284  O   ILE A 388    17951  11649   8411    100    236   -320       O  
ATOM   3285  CB  ILE A 388       1.114 -26.935 -23.483  1.00102.07           C  
ANISOU 3285  CB  ILE A 388    19410  11428   7945   -400   -319   -213       C  
ATOM   3286  CG1 ILE A 388      -0.354 -26.575 -23.778  1.00101.38           C  
ANISOU 3286  CG1 ILE A 388    19657  11059   7802   -645   -870   -102       C  
ATOM   3287  CG2 ILE A 388       1.442 -28.323 -24.051  1.00106.44           C  
ANISOU 3287  CG2 ILE A 388    20344  11768   8329    -90   -251   -427       C  
ATOM   3288  CD1 ILE A 388      -0.562 -25.154 -24.306  1.00109.35           C  
ANISOU 3288  CD1 ILE A 388    20803  12123   8622   -919   -852      4       C  
ATOM   3289  N   GLU A 389       3.719 -26.012 -21.911  1.00 95.47           N  
ANISOU 3289  N   GLU A 389    17265  11383   7625   -274    584   -144       N  
ATOM   3290  CA  GLU A 389       5.183 -26.133 -21.910  1.00 97.72           C  
ANISOU 3290  CA  GLU A 389    17221  11918   7990    -81   1119   -229       C  
ATOM   3291  C   GLU A 389       5.785 -26.472 -20.543  1.00 99.27           C  
ANISOU 3291  C   GLU A 389    16761  12278   8680     42   1091   -184       C  
ATOM   3292  O   GLU A 389       6.835 -27.116 -20.479  1.00101.50           O  
ANISOU 3292  O   GLU A 389    16808  12651   9107    305   1397   -308       O  
ATOM   3293  CB  GLU A 389       5.846 -24.875 -22.475  1.00100.58           C  
ANISOU 3293  CB  GLU A 389    17532  12516   8167   -284   1517   -141       C  
ATOM   3294  CG  GLU A 389       7.284 -25.118 -22.929  1.00115.05           C  
ANISOU 3294  CG  GLU A 389    19178  14563   9974    -76   2143   -262       C  
ATOM   3295  CD  GLU A 389       7.805 -24.035 -23.852  1.00136.43           C  
ANISOU 3295  CD  GLU A 389    22036  17443  12359   -299   2564   -188       C  
ATOM   3296  OE1 GLU A 389       7.817 -22.854 -23.437  1.00126.54           O  
ANISOU 3296  OE1 GLU A 389    20516  16347  11217   -594   2494     22       O  
ATOM   3297  OE2 GLU A 389       8.209 -24.367 -24.988  1.00134.56           O  
ANISOU 3297  OE2 GLU A 389    22211  17177  11740   -184   2963   -339       O  
ATOM   3298  N   PHE A 390       5.142 -26.028 -19.462  1.00 91.18           N  
ANISOU 3298  N   PHE A 390    15454  11280   7910   -140    729    -15       N  
ATOM   3299  CA  PHE A 390       5.485 -26.513 -18.122  1.00 88.87           C  
ANISOU 3299  CA  PHE A 390    14671  11059   8036    -38    590     29       C  
ATOM   3300  C   PHE A 390       5.186 -28.004 -18.062  1.00 92.97           C  
ANISOU 3300  C   PHE A 390    15393  11332   8598    202    372   -107       C  
ATOM   3301  O   PHE A 390       6.061 -28.808 -17.753  1.00 94.23           O  
ANISOU 3301  O   PHE A 390    15337  11507   8959    457    499   -211       O  
ATOM   3302  CB  PHE A 390       4.681 -25.800 -17.026  1.00 86.34           C  
ANISOU 3302  CB  PHE A 390    14122  10783   7901   -281    238    222       C  
ATOM   3303  CG  PHE A 390       5.315 -24.526 -16.521  1.00 86.73           C  
ANISOU 3303  CG  PHE A 390    13784  11088   8080   -450    396    361       C  
ATOM   3304  CD1 PHE A 390       6.617 -24.522 -16.037  1.00 90.98           C  
ANISOU 3304  CD1 PHE A 390    13887  11811   8872   -342    648    369       C  
ATOM   3305  CD2 PHE A 390       4.595 -23.338 -16.495  1.00 86.46           C  
ANISOU 3305  CD2 PHE A 390    13817  11085   7948   -714    243    489       C  
ATOM   3306  CE1 PHE A 390       7.200 -23.350 -15.562  1.00 90.93           C  
ANISOU 3306  CE1 PHE A 390    13539  12011   9001   -518    740    518       C  
ATOM   3307  CE2 PHE A 390       5.170 -22.165 -16.022  1.00 88.28           C  
ANISOU 3307  CE2 PHE A 390    13733  11518   8291   -871    338    619       C  
ATOM   3308  CZ  PHE A 390       6.474 -22.172 -15.555  1.00 87.68           C  
ANISOU 3308  CZ  PHE A 390    13243  11619   8452   -785    580    642       C  
ATOM   3309  N   ARG A 391       3.943 -28.357 -18.382  1.00 88.33           N  
ANISOU 3309  N   ARG A 391    15225  10495   7842    115     13    -99       N  
ATOM   3310  CA  ARG A 391       3.501 -29.753 -18.435  1.00 89.28           C  
ANISOU 3310  CA  ARG A 391    15627  10330   7966    296   -268   -205       C  
ATOM   3311  C   ARG A 391       4.459 -30.628 -19.259  1.00 97.69           C  
ANISOU 3311  C   ARG A 391    16901  11320   8899    639     39   -447       C  
ATOM   3312  O   ARG A 391       4.680 -31.796 -18.929  1.00 98.36           O  
ANISOU 3312  O   ARG A 391    16987  11250   9135    874   -104   -551       O  
ATOM   3313  CB  ARG A 391       2.079 -29.840 -19.015  1.00 88.87           C  
ANISOU 3313  CB  ARG A 391    16061  10008   7699    125   -656   -161       C  
ATOM   3314  CG  ARG A 391       1.280 -31.071 -18.583  1.00 99.44           C  
ANISOU 3314  CG  ARG A 391    17548  11069   9166    170  -1113   -149       C  
ATOM   3315  CD  ARG A 391       0.088 -31.348 -19.515  1.00112.08           C  
ANISOU 3315  CD  ARG A 391    19721  12342  10522     64  -1464   -152       C  
ATOM   3316  NE  ARG A 391      -0.811 -30.199 -19.677  1.00120.87           N  
ANISOU 3316  NE  ARG A 391    20844  13498  11584   -232  -1592     -5       N  
ATOM   3317  CZ  ARG A 391      -1.881 -30.178 -20.475  1.00138.18           C  
ANISOU 3317  CZ  ARG A 391    23481  15416  13605   -370  -1925     23       C  
ATOM   3318  NH1 ARG A 391      -2.215 -31.244 -21.196  1.00129.17           N  
ANISOU 3318  NH1 ARG A 391    22848  13929  12301   -256  -2175    -77       N  
ATOM   3319  NH2 ARG A 391      -2.629 -29.082 -20.553  1.00124.76           N  
ANISOU 3319  NH2 ARG A 391    21731  13758  11913   -618  -2048    149       N  
ATOM   3320  N   LYS A 392       5.018 -30.060 -20.328  1.00 97.13           N  
ANISOU 3320  N   LYS A 392    17019  11349   8536    668    464   -539       N  
ATOM   3321  CA  LYS A 392       6.025 -30.753 -21.138  1.00101.83           C  
ANISOU 3321  CA  LYS A 392    17773  11927   8989   1010    872   -784       C  
ATOM   3322  C   LYS A 392       7.316 -30.973 -20.346  1.00106.84           C  
ANISOU 3322  C   LYS A 392    17776  12786  10032   1227   1146   -825       C  
ATOM   3323  O   LYS A 392       7.832 -32.091 -20.296  1.00109.10           O  
ANISOU 3323  O   LYS A 392    18059  12947  10448   1565   1159  -1009       O  
ATOM   3324  CB  LYS A 392       6.343 -29.972 -22.426  1.00107.03           C  
ANISOU 3324  CB  LYS A 392    18765  12683   9218    942   1321   -843       C  
ATOM   3325  CG  LYS A 392       5.303 -30.092 -23.541  1.00120.42           C  
ANISOU 3325  CG  LYS A 392    21249  14066  10438    847   1091   -895       C  
ATOM   3326  CD  LYS A 392       5.737 -29.315 -24.791  1.00132.77           C  
ANISOU 3326  CD  LYS A 392    23172  15730  11543    769   1569   -948       C  
ATOM   3327  CE  LYS A 392       4.623 -29.227 -25.827  1.00143.65           C  
ANISOU 3327  CE  LYS A 392    25350  16777  12454    600   1253   -952       C  
ATOM   3328  NZ  LYS A 392       5.078 -28.577 -27.086  1.00156.09           N  
ANISOU 3328  NZ  LYS A 392    27372  18416  13521    526   1719  -1014       N  
ATOM   3329  N   ALA A 393       7.825 -29.905 -19.732  1.00101.41           N  
ANISOU 3329  N   ALA A 393    16571  12400   9560   1035   1320   -653       N  
ATOM   3330  CA  ALA A 393       9.114 -29.942 -19.029  1.00102.49           C  
ANISOU 3330  CA  ALA A 393    16078  12754  10111   1201   1575   -662       C  
ATOM   3331  C   ALA A 393       9.070 -30.770 -17.743  1.00104.45           C  
ANISOU 3331  C   ALA A 393    16037  12881  10767   1306   1150   -628       C  
ATOM   3332  O   ALA A 393      10.079 -31.354 -17.343  1.00106.43           O  
ANISOU 3332  O   ALA A 393    15927  13166  11347   1572   1265   -725       O  
ATOM   3333  CB  ALA A 393       9.588 -28.526 -18.724  1.00101.76           C  
ANISOU 3333  CB  ALA A 393    15564  12974  10126    921   1796   -458       C  
ATOM   3334  N   PHE A 394       7.900 -30.818 -17.109  1.00 97.08           N  
ANISOU 3334  N   PHE A 394    15266  11800   9818   1090    661   -486       N  
ATOM   3335  CA  PHE A 394       7.710 -31.531 -15.838  1.00 94.94           C  
ANISOU 3335  CA  PHE A 394    14785  11411   9876   1112    233   -411       C  
ATOM   3336  C   PHE A 394       7.862 -33.043 -16.014  1.00101.70           C  
ANISOU 3336  C   PHE A 394    15871  11988  10781   1448     72   -612       C  
ATOM   3337  O   PHE A 394       8.551 -33.707 -15.231  1.00102.26           O  
ANISOU 3337  O   PHE A 394    15643  12015  11196   1632    -46   -646       O  
ATOM   3338  CB  PHE A 394       6.323 -31.212 -15.257  1.00 92.36           C  
ANISOU 3338  CB  PHE A 394    14617  11006   9470    787   -187   -214       C  
ATOM   3339  CG  PHE A 394       6.240 -29.884 -14.532  1.00 90.65           C  
ANISOU 3339  CG  PHE A 394    14064  11033   9347    495   -162     -5       C  
ATOM   3340  CD1 PHE A 394       7.040 -28.798 -14.894  1.00 94.51           C  
ANISOU 3340  CD1 PHE A 394    14320  11769   9820    439    219     19       C  
ATOM   3341  CD2 PHE A 394       5.331 -29.715 -13.492  1.00 89.24           C  
ANISOU 3341  CD2 PHE A 394    13823  10827   9257    270   -523    170       C  
ATOM   3342  CE1 PHE A 394       6.945 -27.587 -14.218  1.00 92.51           C  
ANISOU 3342  CE1 PHE A 394    13803  11700   9647    177    185    207       C  
ATOM   3343  CE2 PHE A 394       5.231 -28.501 -12.815  1.00 89.26           C  
ANISOU 3343  CE2 PHE A 394    13562  11028   9323     34   -511    336       C  
ATOM   3344  CZ  PHE A 394       6.039 -27.441 -13.179  1.00 87.91           C  
ANISOU 3344  CZ  PHE A 394    13189  11071   9142     -7   -185    351       C  
ATOM   3345  N   LEU A 395       7.206 -33.573 -17.044  1.00 99.74           N  
ANISOU 3345  N   LEU A 395    16188  11521  10189   1523     23   -743       N  
ATOM   3346  CA  LEU A 395       7.326 -34.986 -17.414  1.00102.90           C  
ANISOU 3346  CA  LEU A 395    16911  11617  10568   1862   -128   -964       C  
ATOM   3347  C   LEU A 395       8.697 -35.304 -18.028  1.00112.34           C  
ANISOU 3347  C   LEU A 395    17958  12898  11829   2267    361  -1224       C  
ATOM   3348  O   LEU A 395       9.087 -36.467 -18.098  1.00115.22           O  
ANISOU 3348  O   LEU A 395    18441  13040  12298   2617    256  -1428       O  
ATOM   3349  CB  LEU A 395       6.206 -35.381 -18.390  1.00103.25           C  
ANISOU 3349  CB  LEU A 395    17651  11379  10202   1807   -349  -1021       C  
ATOM   3350  CG  LEU A 395       4.814 -35.589 -17.776  1.00104.08           C  
ANISOU 3350  CG  LEU A 395    17927  11292  10325   1500   -930   -808       C  
ATOM   3351  CD1 LEU A 395       3.699 -35.250 -18.771  1.00103.73           C  
ANISOU 3351  CD1 LEU A 395    18415  11098   9899   1302  -1053   -776       C  
ATOM   3352  CD2 LEU A 395       4.669 -37.021 -17.254  1.00107.73           C  
ANISOU 3352  CD2 LEU A 395    18529  11440  10963   1667  -1377   -858       C  
ATOM   3353  N   LYS A 396       9.414 -34.270 -18.472  1.00110.42           N  
ANISOU 3353  N   LYS A 396    17449  12970  11536   2218    890  -1215       N  
ATOM   3354  CA  LYS A 396      10.761 -34.419 -19.039  1.00115.79           C  
ANISOU 3354  CA  LYS A 396    17884  13797  12312   2569   1445  -1435       C  
ATOM   3355  C   LYS A 396      11.805 -34.656 -17.939  1.00121.02           C  
ANISOU 3355  C   LYS A 396    17860  14562  13561   2731   1409  -1412       C  
ATOM   3356  O   LYS A 396      12.748 -35.433 -18.131  1.00125.21           O  
ANISOU 3356  O   LYS A 396    18227  15044  14305   3141   1610  -1645       O  
ATOM   3357  CB  LYS A 396      11.124 -33.177 -19.874  1.00119.45           C  
ANISOU 3357  CB  LYS A 396    18295  14571  12518   2393   2015  -1385       C  
ATOM   3358  CG  LYS A 396      12.007 -33.446 -21.101  1.00140.19           C  
ANISOU 3358  CG  LYS A 396    21075  17266  14925   2727   2645  -1662       C  
ATOM   3359  CD  LYS A 396      13.407 -32.853 -20.971  1.00153.27           C  
ANISOU 3359  CD  LYS A 396    22025  19287  16922   2809   3204  -1650       C  
ATOM   3360  CE  LYS A 396      14.131 -32.853 -22.314  1.00170.57           C  
ANISOU 3360  CE  LYS A 396    24410  21607  18791   3042   3928  -1882       C  
ATOM   3361  NZ  LYS A 396      15.401 -32.080 -22.274  1.00182.24           N  
ANISOU 3361  NZ  LYS A 396    25184  23481  20578   3025   4513  -1811       N  
ATOM   3362  N   ILE A 397      11.626 -33.987 -16.795  1.00113.81           N  
ANISOU 3362  N   ILE A 397    16569  13768  12906   2419   1135  -1140       N  
ATOM   3363  CA  ILE A 397      12.503 -34.152 -15.620  1.00114.12           C  
ANISOU 3363  CA  ILE A 397    16008  13857  13496   2507    981  -1073       C  
ATOM   3364  C   ILE A 397      12.131 -35.410 -14.805  1.00118.35           C  
ANISOU 3364  C   ILE A 397    16695  14052  14221   2642    393  -1108       C  
ATOM   3365  O   ILE A 397      12.994 -36.034 -14.176  1.00120.27           O  
ANISOU 3365  O   ILE A 397    16589  14216  14892   2889    268  -1179       O  
ATOM   3366  CB  ILE A 397      12.458 -32.901 -14.685  1.00113.00           C  
ANISOU 3366  CB  ILE A 397    15471  13948  13514   2106    892   -765       C  
ATOM   3367  CG1 ILE A 397      12.835 -31.615 -15.440  1.00113.97           C  
ANISOU 3367  CG1 ILE A 397    15447  14389  13466   1932   1418   -699       C  
ATOM   3368  CG2 ILE A 397      13.391 -33.085 -13.495  1.00114.42           C  
ANISOU 3368  CG2 ILE A 397    15087  14137  14251   2193    690   -693       C  
ATOM   3369  CD1 ILE A 397      14.331 -31.351 -15.541  1.00125.07           C  
ANISOU 3369  CD1 ILE A 397    16260  16022  15239   2115   1863   -750       C  
ATOM   3370  N   LEU A 398      10.844 -35.764 -14.823  1.00112.82           N  
ANISOU 3370  N   LEU A 398    16509  13138  13218   2463     12  -1043       N  
ATOM   3371  CA  LEU A 398      10.329 -36.943 -14.120  1.00112.54           C  
ANISOU 3371  CA  LEU A 398    16697  12768  13297   2520   -567  -1038       C  
ATOM   3372  C   LEU A 398      10.555 -38.259 -14.895  1.00122.11           C  
ANISOU 3372  C   LEU A 398    18276  13675  14443   2951   -609  -1344       C  
ATOM   3373  O   LEU A 398      10.534 -39.337 -14.300  1.00122.72           O  
ANISOU 3373  O   LEU A 398    18443  13464  14721   3093  -1061  -1383       O  
ATOM   3374  CB  LEU A 398       8.835 -36.739 -13.811  1.00108.03           C  
ANISOU 3374  CB  LEU A 398    16475  12109  12460   2119   -943   -816       C  
ATOM   3375  CG  LEU A 398       8.010 -37.867 -13.173  1.00112.07           C  
ANISOU 3375  CG  LEU A 398    17297  12283  13004   2062  -1547   -749       C  
ATOM   3376  CD1 LEU A 398       8.697 -38.510 -11.956  1.00113.19           C  
ANISOU 3376  CD1 LEU A 398    17127  12317  13561   2161  -1864   -706       C  
ATOM   3377  CD2 LEU A 398       6.630 -37.329 -12.799  1.00109.95           C  
ANISOU 3377  CD2 LEU A 398    17195  12044  12535   1617  -1787   -488       C  
ATOM   3378  N   SER A 399      10.785 -38.165 -16.207  1.00122.66           N  
ANISOU 3378  N   SER A 399    18591  13795  14217   3158   -150  -1562       N  
ATOM   3379  CA  SER A 399      10.947 -39.347 -17.072  1.00127.77           C  
ANISOU 3379  CA  SER A 399    19680  14145  14721   3587   -150  -1883       C  
ATOM   3380  C   SER A 399      12.366 -39.954 -17.081  1.00138.18           C  
ANISOU 3380  C   SER A 399    20612  15466  16422   4089    109  -2151       C  
ATOM   3381  O   SER A 399      12.580 -41.044 -17.635  1.00142.49           O  
ANISOU 3381  O   SER A 399    21491  15732  16919   4503     54  -2442       O  
ATOM   3382  CB  SER A 399      10.535 -39.001 -18.513  1.00132.93           C  
ANISOU 3382  CB  SER A 399    20855  14821  14830   3594    229  -2014       C  
ATOM   3383  OG  SER A 399      10.855 -40.045 -19.420  1.00147.83           O  
ANISOU 3383  OG  SER A 399    23171  16448  16550   4052    325  -2360       O  
ATOM   3384  N   CYS A 400      13.325 -39.259 -16.469  1.00135.16           N  
ANISOU 3384  N   CYS A 400    19532  15381  16442   4063    364  -2056       N  
ATOM   3385  CA  CYS A 400      14.740 -39.652 -16.538  1.00140.80           C  
ANISOU 3385  CA  CYS A 400    19765  16153  17579   4524    686  -2294       C  
ATOM   3386  C   CYS A 400      15.010 -41.020 -15.891  1.00146.82           C  
ANISOU 3386  C   CYS A 400    20548  16530  18706   4865    149  -2443       C  
ATOM   3387  O   CYS A 400      14.844 -41.193 -14.675  1.00143.41           O  
ANISOU 3387  O   CYS A 400    19937  15977  18574   4670   -400  -2233       O  
ATOM   3388  CB  CYS A 400      15.609 -38.567 -15.877  1.00140.38           C  
ANISOU 3388  CB  CYS A 400    18939  16468  17931   4341    951  -2093       C  
ATOM   3389  SG  CYS A 400      15.151 -36.867 -16.346  1.00140.38           S  
ANISOU 3389  SG  CYS A 400    18923  16877  17537   3832   1396  -1833       S  
TER    3390      CYS A 400                                                      
ATOM   3391  N   TYR B  32      14.647  28.678 -13.262  1.00126.48           N  
ANISOU 3391  N   TYR B  32    20845  12405  14807  -3093   5151   1951       N  
ATOM   3392  CA  TYR B  32      14.747  27.499 -12.410  1.00120.74           C  
ANISOU 3392  CA  TYR B  32    19290  12276  14308  -3117   4697   1683       C  
ATOM   3393  C   TYR B  32      16.148  26.900 -12.461  1.00123.77           C  
ANISOU 3393  C   TYR B  32    19101  12988  14937  -3659   4872   1470       C  
ATOM   3394  O   TYR B  32      16.391  25.818 -11.926  1.00119.17           O  
ANISOU 3394  O   TYR B  32    17844  12922  14513  -3660   4542   1273       O  
ATOM   3395  CB  TYR B  32      13.711  26.451 -12.822  1.00117.73           C  
ANISOU 3395  CB  TYR B  32    18734  12293  13705  -2486   4270   1824       C  
ATOM   3396  CG  TYR B  32      12.286  26.955 -12.795  1.00119.94           C  
ANISOU 3396  CG  TYR B  32    19477  12362  13733  -1903   4061   2011       C  
ATOM   3397  CD1 TYR B  32      11.664  27.276 -11.595  1.00120.56           C  
ANISOU 3397  CD1 TYR B  32    19497  12379  13934  -1812   3809   1869       C  
ATOM   3398  CD2 TYR B  32      11.561  27.110 -13.969  1.00122.62           C  
ANISOU 3398  CD2 TYR B  32    20302  12597  13691  -1413   4110   2320       C  
ATOM   3399  CE1 TYR B  32      10.362  27.737 -11.566  1.00121.86           C  
ANISOU 3399  CE1 TYR B  32    20044  12390  13867  -1249   3629   2027       C  
ATOM   3400  CE2 TYR B  32      10.258  27.571 -13.950  1.00123.97           C  
ANISOU 3400  CE2 TYR B  32    20849  12636  13617   -833   3900   2475       C  
ATOM   3401  CZ  TYR B  32       9.664  27.882 -12.746  1.00130.16           C  
ANISOU 3401  CZ  TYR B  32    21537  13370  14550   -754   3668   2326       C  
ATOM   3402  OH  TYR B  32       8.367  28.341 -12.722  1.00131.96           O  
ANISOU 3402  OH  TYR B  32    22101  13504  14535   -149   3469   2468       O  
ATOM   3403  N   ALA B  33      17.067  27.609 -13.108  1.00124.72           N  
ANISOU 3403  N   ALA B  33    19503  12806  15078  -4108   5410   1511       N  
ATOM   3404  CA  ALA B  33      18.444  27.148 -13.232  1.00125.51           C  
ANISOU 3404  CA  ALA B  33    19056  13226  15405  -4639   5637   1301       C  
ATOM   3405  C   ALA B  33      19.185  26.938 -11.915  1.00127.27           C  
ANISOU 3405  C   ALA B  33    18602  13757  15996  -5072   5444    885       C  
ATOM   3406  O   ALA B  33      19.635  25.833 -11.615  1.00123.58           O  
ANISOU 3406  O   ALA B  33    17441  13857  15658  -5052   5175    710       O  
ATOM   3407  CB  ALA B  33      19.265  28.141 -14.040  1.00132.92           C  
ANISOU 3407  CB  ALA B  33    20462  13722  16320  -5121   6309   1393       C  
ATOM   3408  N   LEU B  34      19.307  28.007 -11.133  1.00125.93           N  
ANISOU 3408  N   LEU B  34    18667  13207  15972  -5440   5580    723       N  
ATOM   3409  CA  LEU B  34      19.994  27.941  -9.849  1.00125.08           C  
ANISOU 3409  CA  LEU B  34    17968  13375  16180  -5861   5392    304       C  
ATOM   3410  C   LEU B  34      18.943  28.044  -8.749  1.00124.61           C  
ANISOU 3410  C   LEU B  34    18008  13241  16098  -5506   4945    253       C  
ATOM   3411  O   LEU B  34      19.221  27.760  -7.584  1.00122.59           O  
ANISOU 3411  O   LEU B  34    17256  13290  16034  -5658   4643    -61       O  
ATOM   3412  CB  LEU B  34      21.042  29.043  -9.679  1.00131.67           C  
ANISOU 3412  CB  LEU B  34    18913  13893  17224  -6641   5879     67       C  
ATOM   3413  CG  LEU B  34      22.393  28.804 -10.358  1.00140.06           C  
ANISOU 3413  CG  LEU B  34    19557  15233  18427  -7156   6275    -54       C  
ATOM   3414  CD1 LEU B  34      23.217  30.082 -10.381  1.00147.73           C  
ANISOU 3414  CD1 LEU B  34    20831  15742  19556  -7934   6855   -227       C  
ATOM   3415  CD2 LEU B  34      23.152  27.684  -9.664  1.00140.03           C  
ANISOU 3415  CD2 LEU B  34    18562  16006  18636  -7227   5907   -385       C  
ATOM   3416  N   SER B  35      17.736  28.452  -9.126  1.00119.65           N  
ANISOU 3416  N   SER B  35    18018  12231  15214  -5009   4908    561       N  
ATOM   3417  CA  SER B  35      16.634  28.595  -8.164  1.00116.19           C  
ANISOU 3417  CA  SER B  35    17711  11710  14726  -4622   4523    539       C  
ATOM   3418  C   SER B  35      16.163  27.251  -7.613  1.00112.89           C  
ANISOU 3418  C   SER B  35    16683  11890  14318  -4224   3979    477       C  
ATOM   3419  O   SER B  35      15.498  27.209  -6.576  1.00110.05           O  
ANISOU 3419  O   SER B  35    16244  11586  13983  -4020   3648    367       O  
ATOM   3420  CB  SER B  35      15.455  29.367  -8.773  1.00120.94           C  
ANISOU 3420  CB  SER B  35    19125  11796  15031  -4137   4628    885       C  
ATOM   3421  OG  SER B  35      15.745  30.756  -8.863  1.00135.41           O  
ANISOU 3421  OG  SER B  35    21609  12974  16868  -4488   5090    896       O  
ATOM   3422  N   TYR B  36      16.494  26.163  -8.306  1.00106.59           N  
ANISOU 3422  N   TYR B  36    15499  11512  13490  -4111   3915    548       N  
ATOM   3423  CA  TYR B  36      16.367  24.821  -7.726  1.00101.26           C  
ANISOU 3423  CA  TYR B  36    14196  11405  12872  -3868   3467    432       C  
ATOM   3424  C   TYR B  36      17.633  24.465  -6.938  1.00105.12           C  
ANISOU 3424  C   TYR B  36    14054  12258  13629  -4326   3430     83       C  
ATOM   3425  O   TYR B  36      17.550  23.911  -5.846  1.00102.11           O  
ANISOU 3425  O   TYR B  36    13282  12179  13337  -4241   3070   -109       O  
ATOM   3426  CB  TYR B  36      16.082  23.762  -8.799  1.00100.07           C  
ANISOU 3426  CB  TYR B  36    13949  11525  12547  -3498   3395    650       C  
ATOM   3427  CG  TYR B  36      14.605  23.534  -9.087  1.00 99.12           C  
ANISOU 3427  CG  TYR B  36    14135  11346  12180  -2907   3142    885       C  
ATOM   3428  CD1 TYR B  36      13.876  24.437  -9.861  1.00103.60           C  
ANISOU 3428  CD1 TYR B  36    15354  11493  12516  -2679   3333   1143       C  
ATOM   3429  CD2 TYR B  36      13.943  22.406  -8.606  1.00 95.22           C  
ANISOU 3429  CD2 TYR B  36    13279  11231  11671  -2571   2725    843       C  
ATOM   3430  CE1 TYR B  36      12.522  24.229 -10.142  1.00102.27           C  
ANISOU 3430  CE1 TYR B  36    15403  11346  12110  -2114   3078   1329       C  
ATOM   3431  CE2 TYR B  36      12.590  22.188  -8.881  1.00 93.99           C  
ANISOU 3431  CE2 TYR B  36    13340  11071  11300  -2074   2503   1018       C  
ATOM   3432  CZ  TYR B  36      11.886  23.104  -9.650  1.00104.14           C  
ANISOU 3432  CZ  TYR B  36    15208  11999  12361  -1840   2664   1250       C  
ATOM   3433  OH  TYR B  36      10.550  22.905  -9.928  1.00103.71           O  
ANISOU 3433  OH  TYR B  36    15312  12009  12085  -1329   2423   1395       O  
ATOM   3434  N   CYS B  37      18.800  24.794  -7.484  1.00104.91           N  
ANISOU 3434  N   CYS B  37    13925  12220  13715  -4801   3810     -5       N  
ATOM   3435  CA  CYS B  37      20.074  24.578  -6.786  1.00106.22           C  
ANISOU 3435  CA  CYS B  37    13458  12767  14132  -5263   3801   -370       C  
ATOM   3436  C   CYS B  37      20.114  25.248  -5.408  1.00109.90           C  
ANISOU 3436  C   CYS B  37    13866  13152  14740  -5517   3635   -671       C  
ATOM   3437  O   CYS B  37      20.689  24.701  -4.466  1.00108.69           O  
ANISOU 3437  O   CYS B  37    13131  13447  14720  -5613   3358   -962       O  
ATOM   3438  CB  CYS B  37      21.239  25.101  -7.629  1.00111.95           C  
ANISOU 3438  CB  CYS B  37    14164  13414  14957  -5801   4319   -425       C  
ATOM   3439  SG  CYS B  37      21.236  24.529  -9.344  1.00115.59           S  
ANISOU 3439  SG  CYS B  37    14816  13892  15211  -5545   4607    -66       S  
ATOM   3440  N   ALA B  38      19.515  26.436  -5.308  1.00107.75           N  
ANISOU 3440  N   ALA B  38    14223  12303  14414  -5598   3810   -601       N  
ATOM   3441  CA  ALA B  38      19.401  27.166  -4.041  1.00108.43           C  
ANISOU 3441  CA  ALA B  38    14377  12228  14594  -5800   3672   -872       C  
ATOM   3442  C   ALA B  38      18.487  26.426  -3.071  1.00105.98           C  
ANISOU 3442  C   ALA B  38    13885  12180  14203  -5287   3151   -876       C  
ATOM   3443  O   ALA B  38      18.863  26.154  -1.930  1.00105.04           O  
ANISOU 3443  O   ALA B  38    13338  12385  14186  -5401   2872  -1179       O  
ATOM   3444  CB  ALA B  38      18.869  28.572  -4.285  1.00112.72           C  
ANISOU 3444  CB  ALA B  38    15733  12035  15060  -5917   4012   -749       C  
ATOM   3445  N   LEU B  39      17.289  26.093  -3.542  1.00 98.18           N  
ANISOU 3445  N   LEU B  39    13217  11072  13015  -4724   3030   -546       N  
ATOM   3446  CA  LEU B  39      16.286  25.430  -2.712  1.00 92.97           C  
ANISOU 3446  CA  LEU B  39    12443  10617  12266  -4241   2595   -520       C  
ATOM   3447  C   LEU B  39      16.742  24.048  -2.186  1.00 92.39           C  
ANISOU 3447  C   LEU B  39    11682  11167  12254  -4133   2259   -658       C  
ATOM   3448  O   LEU B  39      16.200  23.559  -1.192  1.00 89.40           O  
ANISOU 3448  O   LEU B  39    11145  10981  11840  -3874   1920   -732       O  
ATOM   3449  CB  LEU B  39      14.956  25.320  -3.482  1.00 90.50           C  
ANISOU 3449  CB  LEU B  39    12554  10104  11727  -3693   2563   -156       C  
ATOM   3450  CG  LEU B  39      13.688  24.892  -2.729  1.00 91.30           C  
ANISOU 3450  CG  LEU B  39    12662  10310  11718  -3201   2198   -101       C  
ATOM   3451  CD1 LEU B  39      13.479  25.711  -1.459  1.00 92.92           C  
ANISOU 3451  CD1 LEU B  39    13015  10316  11975  -3309   2121   -316       C  
ATOM   3452  CD2 LEU B  39      12.471  25.007  -3.641  1.00 92.41           C  
ANISOU 3452  CD2 LEU B  39    13229  10246  11637  -2725   2225    227       C  
ATOM   3453  N   ILE B  40      17.732  23.429  -2.835  1.00 88.32           N  
ANISOU 3453  N   ILE B  40    10791  10954  11814  -4309   2371   -688       N  
ATOM   3454  CA  ILE B  40      18.313  22.179  -2.330  1.00 85.46           C  
ANISOU 3454  CA  ILE B  40     9801  11165  11506  -4203   2086   -835       C  
ATOM   3455  C   ILE B  40      19.097  22.428  -1.053  1.00 90.69           C  
ANISOU 3455  C   ILE B  40    10098  12056  12302  -4511   1928  -1214       C  
ATOM   3456  O   ILE B  40      18.917  21.736  -0.055  1.00 88.02           O  
ANISOU 3456  O   ILE B  40     9496  12021  11928  -4268   1574  -1319       O  
ATOM   3457  CB  ILE B  40      19.257  21.519  -3.350  1.00 89.46           C  
ANISOU 3457  CB  ILE B  40     9990  11946  12057  -4304   2273   -796       C  
ATOM   3458  CG1 ILE B  40      18.452  20.875  -4.476  1.00 86.92           C  
ANISOU 3458  CG1 ILE B  40     9922  11544  11560  -3894   2307   -453       C  
ATOM   3459  CG2 ILE B  40      20.125  20.457  -2.677  1.00 89.51           C  
ANISOU 3459  CG2 ILE B  40     9332  12536  12141  -4263   2016  -1022       C  
ATOM   3460  CD1 ILE B  40      19.315  20.294  -5.577  1.00 95.80           C  
ANISOU 3460  CD1 ILE B  40    10819  12886  12695  -3971   2533   -398       C  
ATOM   3461  N   LEU B  41      19.978  23.416  -1.090  1.00 91.72           N  
ANISOU 3461  N   LEU B  41    10226  12049  12575  -5058   2202  -1431       N  
ATOM   3462  CA  LEU B  41      20.793  23.726   0.073  1.00 94.47           C  
ANISOU 3462  CA  LEU B  41    10202  12645  13046  -5408   2055  -1844       C  
ATOM   3463  C   LEU B  41      19.891  24.253   1.185  1.00 97.39           C  
ANISOU 3463  C   LEU B  41    10898  12771  13334  -5264   1833  -1911       C  
ATOM   3464  O   LEU B  41      20.025  23.851   2.338  1.00 96.29           O  
ANISOU 3464  O   LEU B  41    10441  12970  13175  -5168   1492  -2134       O  
ATOM   3465  CB  LEU B  41      21.900  24.722  -0.286  1.00100.56           C  
ANISOU 3465  CB  LEU B  41    10916  13294  13997  -6097   2443  -2085       C  
ATOM   3466  CG  LEU B  41      22.817  24.298  -1.443  1.00106.78           C  
ANISOU 3466  CG  LEU B  41    11396  14311  14864  -6274   2734  -2021       C  
ATOM   3467  CD1 LEU B  41      24.012  25.234  -1.535  1.00113.63           C  
ANISOU 3467  CD1 LEU B  41    12083  15158  15935  -7024   3092  -2349       C  
ATOM   3468  CD2 LEU B  41      23.276  22.840  -1.308  1.00106.28           C  
ANISOU 3468  CD2 LEU B  41    10690  14914  14779  -5916   2422  -2050       C  
ATOM   3469  N   ALA B  42      18.948  25.121   0.823  1.00 93.87           N  
ANISOU 3469  N   ALA B  42    11101  11750  12815  -5195   2028  -1704       N  
ATOM   3470  CA  ALA B  42      17.928  25.597   1.757  1.00 92.33           C  
ANISOU 3470  CA  ALA B  42    11268  11297  12518  -4967   1847  -1717       C  
ATOM   3471  C   ALA B  42      17.264  24.429   2.490  1.00 91.33           C  
ANISOU 3471  C   ALA B  42    10881  11553  12270  -4444   1427  -1647       C  
ATOM   3472  O   ALA B  42      16.974  24.519   3.684  1.00 90.73           O  
ANISOU 3472  O   ALA B  42    10787  11545  12142  -4360   1186  -1824       O  
ATOM   3473  CB  ALA B  42      16.879  26.423   1.016  1.00 92.98           C  
ANISOU 3473  CB  ALA B  42    12060  10774  12494  -4783   2101  -1412       C  
ATOM   3474  N   ILE B  43      17.031  23.336   1.766  1.00 84.38           N  
ANISOU 3474  N   ILE B  43     9829  10901  11332  -4108   1363  -1395       N  
ATOM   3475  CA  ILE B  43      16.441  22.128   2.339  1.00 79.84           C  
ANISOU 3475  CA  ILE B  43     9030  10661  10646  -3645   1021  -1312       C  
ATOM   3476  C   ILE B  43      17.409  21.412   3.270  1.00 84.04           C  
ANISOU 3476  C   ILE B  43     9013  11703  11215  -3712    766  -1587       C  
ATOM   3477  O   ILE B  43      17.073  21.153   4.428  1.00 82.42           O  
ANISOU 3477  O   ILE B  43     8751  11644  10921  -3522    495  -1695       O  
ATOM   3478  CB  ILE B  43      15.988  21.148   1.235  1.00 79.68           C  
ANISOU 3478  CB  ILE B  43     8998  10721  10555  -3315   1051   -997       C  
ATOM   3479  CG1 ILE B  43      14.661  21.614   0.644  1.00 78.65           C  
ANISOU 3479  CG1 ILE B  43     9381  10195  10309  -3052   1151   -723       C  
ATOM   3480  CG2 ILE B  43      15.857  19.736   1.780  1.00 77.06           C  
ANISOU 3480  CG2 ILE B  43     8325  10801  10152  -2970    748   -979       C  
ATOM   3481  CD1 ILE B  43      14.441  21.144  -0.769  1.00 85.66           C  
ANISOU 3481  CD1 ILE B  43    10354  11056  11136  -2895   1298   -454       C  
ATOM   3482  N   VAL B  44      18.603  21.098   2.764  1.00 82.48           N  
ANISOU 3482  N   VAL B  44     8417  11793  11127  -3951    857  -1698       N  
ATOM   3483  CA  VAL B  44      19.572  20.301   3.524  1.00 83.07           C  
ANISOU 3483  CA  VAL B  44     7924  12426  11213  -3929    601  -1942       C  
ATOM   3484  C   VAL B  44      20.068  21.070   4.742  1.00 90.00           C  
ANISOU 3484  C   VAL B  44     8680  13397  12117  -4226    459  -2324       C  
ATOM   3485  O   VAL B  44      20.327  20.475   5.787  1.00 89.64           O  
ANISOU 3485  O   VAL B  44     8337  13741  11980  -4034    135  -2493       O  
ATOM   3486  CB  VAL B  44      20.777  19.843   2.666  1.00 88.99           C  
ANISOU 3486  CB  VAL B  44     8235  13500  12076  -4107    752  -1998       C  
ATOM   3487  CG1 VAL B  44      21.725  18.987   3.494  1.00 90.16           C  
ANISOU 3487  CG1 VAL B  44     7791  14262  12203  -3985    453  -2246       C  
ATOM   3488  CG2 VAL B  44      20.307  19.056   1.445  1.00 85.53           C  
ANISOU 3488  CG2 VAL B  44     7938  12973  11586  -3809    889  -1642       C  
ATOM   3489  N   PHE B  45      20.185  22.390   4.602  1.00 89.63           N  
ANISOU 3489  N   PHE B  45     8904  12975  12175  -4684    707  -2460       N  
ATOM   3490  CA  PHE B  45      20.544  23.264   5.716  1.00 93.08           C  
ANISOU 3490  CA  PHE B  45     9320  13412  12633  -5015    604  -2845       C  
ATOM   3491  C   PHE B  45      19.457  23.204   6.776  1.00 93.43           C  
ANISOU 3491  C   PHE B  45     9663  13340  12495  -4632    343  -2795       C  
ATOM   3492  O   PHE B  45      19.713  22.801   7.908  1.00 93.53           O  
ANISOU 3492  O   PHE B  45     9406  13727  12405  -4504     19  -3015       O  
ATOM   3493  CB  PHE B  45      20.729  24.707   5.227  1.00 99.11           C  
ANISOU 3493  CB  PHE B  45    10452  13668  13537  -5574    993  -2953       C  
ATOM   3494  CG  PHE B  45      21.039  25.696   6.324  1.00105.02           C  
ANISOU 3494  CG  PHE B  45    11258  14336  14308  -5963    922  -3372       C  
ATOM   3495  CD1 PHE B  45      22.355  25.981   6.671  1.00113.39           C  
ANISOU 3495  CD1 PHE B  45    11826  15758  15501  -6491    910  -3819       C  
ATOM   3496  CD2 PHE B  45      20.012  26.354   6.995  1.00106.20           C  
ANISOU 3496  CD2 PHE B  45    11944  14066  14340  -5808    875  -3344       C  
ATOM   3497  CE1 PHE B  45      22.642  26.895   7.672  1.00118.58           C  
ANISOU 3497  CE1 PHE B  45    12539  16349  16169  -6882    836  -4244       C  
ATOM   3498  CE2 PHE B  45      20.292  27.265   7.996  1.00113.16           C  
ANISOU 3498  CE2 PHE B  45    12916  14853  15225  -6165    818  -3748       C  
ATOM   3499  CZ  PHE B  45      21.610  27.537   8.334  1.00116.54           C  
ANISOU 3499  CZ  PHE B  45    12865  15632  15782  -6719    793  -4207       C  
ATOM   3500  N   GLY B  46      18.245  23.594   6.389  1.00 86.85           N  
ANISOU 3500  N   GLY B  46     9382  12015  11603  -4423    491  -2504       N  
ATOM   3501  CA  GLY B  46      17.107  23.647   7.303  1.00 84.22           C  
ANISOU 3501  CA  GLY B  46     9365  11531  11105  -4068    309  -2442       C  
ATOM   3502  C   GLY B  46      16.813  22.315   7.964  1.00 84.46           C  
ANISOU 3502  C   GLY B  46     9121  11986  10983  -3597    -18  -2352       C  
ATOM   3503  O   GLY B  46      16.958  22.176   9.176  1.00 84.88           O  
ANISOU 3503  O   GLY B  46     9044  12284  10924  -3522   -276  -2572       O  
ATOM   3504  N   ASN B  47      16.417  21.327   7.169  1.00 77.62           N  
ANISOU 3504  N   ASN B  47     8198  11199  10097  -3283      3  -2036       N  
ATOM   3505  CA  ASN B  47      16.011  20.032   7.721  1.00 74.28           C  
ANISOU 3505  CA  ASN B  47     7612  11087   9524  -2833   -250  -1912       C  
ATOM   3506  C   ASN B  47      17.163  19.298   8.409  1.00 79.63           C  
ANISOU 3506  C   ASN B  47     7800  12291  10164  -2825   -494  -2142       C  
ATOM   3507  O   ASN B  47      16.938  18.444   9.271  1.00 77.93           O  
ANISOU 3507  O   ASN B  47     7509  12322   9781  -2479   -731  -2121       O  
ATOM   3508  CB  ASN B  47      15.358  19.151   6.651  1.00 71.72           C  
ANISOU 3508  CB  ASN B  47     7352  10705   9193  -2550   -152  -1556       C  
ATOM   3509  CG  ASN B  47      13.968  19.639   6.266  1.00 94.59           C  
ANISOU 3509  CG  ASN B  47    10698  13195  12047  -2391    -18  -1327       C  
ATOM   3510  OD1 ASN B  47      12.956  19.094   6.714  1.00 87.61           O  
ANISOU 3510  OD1 ASN B  47     9926  12319  11041  -2061   -123  -1194       O  
ATOM   3511  ND2 ASN B  47      13.915  20.682   5.447  1.00 88.73           N  
ANISOU 3511  ND2 ASN B  47    10217  12102  11392  -2617    228  -1287       N  
ATOM   3512  N   GLY B  48      18.393  19.637   8.041  1.00 79.24           N  
ANISOU 3512  N   GLY B  48     7424  12428  10257  -3194   -425  -2363       N  
ATOM   3513  CA  GLY B  48      19.548  19.113   8.747  1.00 81.77           C  
ANISOU 3513  CA  GLY B  48     7236  13298  10535  -3196   -675  -2641       C  
ATOM   3514  C   GLY B  48      19.517  19.534  10.206  1.00 87.56           C  
ANISOU 3514  C   GLY B  48     8000  14148  11119  -3192   -932  -2923       C  
ATOM   3515  O   GLY B  48      19.782  18.725  11.102  1.00 87.97           O  
ANISOU 3515  O   GLY B  48     7831  14604  10989  -2871  -1230  -3000       O  
ATOM   3516  N   LEU B  49      19.180  20.802  10.441  1.00 84.84           N  
ANISOU 3516  N   LEU B  49     7976  13430  10828  -3521   -809  -3071       N  
ATOM   3517  CA  LEU B  49      19.147  21.358  11.793  1.00 86.53           C  
ANISOU 3517  CA  LEU B  49     8271  13710  10898  -3570  -1025  -3377       C  
ATOM   3518  C   LEU B  49      17.997  20.792  12.631  1.00 85.94           C  
ANISOU 3518  C   LEU B  49     8498  13574  10581  -3057  -1187  -3173       C  
ATOM   3519  O   LEU B  49      18.100  20.718  13.852  1.00 87.32           O  
ANISOU 3519  O   LEU B  49     8630  13992  10556  -2923  -1449  -3383       O  
ATOM   3520  CB  LEU B  49      19.086  22.893  11.755  1.00 89.62           C  
ANISOU 3520  CB  LEU B  49     8985  13653  11414  -4072   -803  -3594       C  
ATOM   3521  CG  LEU B  49      20.429  23.610  11.588  1.00 99.75           C  
ANISOU 3521  CG  LEU B  49     9915  15109  12877  -4683   -729  -4001       C  
ATOM   3522  CD1 LEU B  49      21.272  22.983  10.478  1.00 99.93           C  
ANISOU 3522  CD1 LEU B  49     9506  15399  13065  -4777   -602  -3898       C  
ATOM   3523  CD2 LEU B  49      20.207  25.096  11.332  1.00104.67           C  
ANISOU 3523  CD2 LEU B  49    11000  15137  13634  -5173   -411  -4130       C  
ATOM   3524  N   VAL B  50      16.910  20.389  11.981  1.00 77.12           N  
ANISOU 3524  N   VAL B  50     7677  12156   9468  -2780  -1026  -2780       N  
ATOM   3525  CA  VAL B  50      15.810  19.721  12.678  1.00 73.38           C  
ANISOU 3525  CA  VAL B  50     7442  11656   8784  -2315  -1135  -2571       C  
ATOM   3526  C   VAL B  50      16.300  18.400  13.261  1.00 76.13           C  
ANISOU 3526  C   VAL B  50     7484  12483   8958  -1970  -1394  -2551       C  
ATOM   3527  O   VAL B  50      15.952  18.051  14.381  1.00 75.58           O  
ANISOU 3527  O   VAL B  50     7517  12546   8654  -1690  -1576  -2582       O  
ATOM   3528  CB  VAL B  50      14.597  19.474  11.743  1.00 72.97           C  
ANISOU 3528  CB  VAL B  50     7685  11252   8788  -2118   -910  -2179       C  
ATOM   3529  CG1 VAL B  50      13.534  18.630  12.436  1.00 69.94           C  
ANISOU 3529  CG1 VAL B  50     7468  10904   8203  -1678  -1000  -1980       C  
ATOM   3530  CG2 VAL B  50      14.009  20.805  11.269  1.00 73.43           C  
ANISOU 3530  CG2 VAL B  50     8115  10826   8959  -2353   -669  -2178       C  
ATOM   3531  N   CYS B  51      17.112  17.676  12.498  1.00 72.63           N  
ANISOU 3531  N   CYS B  51     6696  12288   8611  -1965  -1391  -2493       N  
ATOM   3532  CA  CYS B  51      17.713  16.435  12.984  1.00 72.97           C  
ANISOU 3532  CA  CYS B  51     6454  12786   8485  -1606  -1627  -2482       C  
ATOM   3533  C   CYS B  51      18.756  16.736  14.049  1.00 82.01           C  
ANISOU 3533  C   CYS B  51     7295  14362   9503  -1682  -1915  -2881       C  
ATOM   3534  O   CYS B  51      18.800  16.093  15.096  1.00 82.44           O  
ANISOU 3534  O   CYS B  51     7340  14696   9287  -1318  -2165  -2914       O  
ATOM   3535  CB  CYS B  51      18.356  15.645  11.841  1.00 72.32           C  
ANISOU 3535  CB  CYS B  51     6083  12855   8540  -1570  -1532  -2340       C  
ATOM   3536  SG  CYS B  51      17.178  14.844  10.741  1.00 70.88           S  
ANISOU 3536  SG  CYS B  51     6217  12302   8413  -1344  -1284  -1880       S  
ATOM   3537  N   MET B  52      19.600  17.719  13.767  1.00 82.56           N  
ANISOU 3537  N   MET B  52     7123  14490   9756  -2167  -1871  -3192       N  
ATOM   3538  CA  MET B  52      20.617  18.149  14.717  1.00 88.00           C  
ANISOU 3538  CA  MET B  52     7476  15610  10348  -2334  -2144  -3642       C  
ATOM   3539  C   MET B  52      20.005  18.642  16.037  1.00 92.40           C  
ANISOU 3539  C   MET B  52     8359  16083  10665  -2240  -2314  -3793       C  
ATOM   3540  O   MET B  52      20.622  18.515  17.094  1.00 95.18           O  
ANISOU 3540  O   MET B  52     8495  16876  10793  -2117  -2635  -4079       O  
ATOM   3541  CB  MET B  52      21.481  19.257  14.101  1.00 94.28           C  
ANISOU 3541  CB  MET B  52     8020  16382  11421  -2982  -1983  -3960       C  
ATOM   3542  CG  MET B  52      22.466  18.777  13.041  1.00 99.23           C  
ANISOU 3542  CG  MET B  52     8170  17292  12240  -3095  -1878  -3942       C  
ATOM   3543  SD  MET B  52      24.044  18.264  13.766  1.00109.73           S  
ANISOU 3543  SD  MET B  52     8739  19503  13450  -3016  -2267  -4369       S  
ATOM   3544  CE  MET B  52      24.762  19.831  14.289  1.00112.76           C  
ANISOU 3544  CE  MET B  52     8937  19950  13957  -3764  -2287  -4969       C  
ATOM   3545  N   ALA B  53      18.799  19.201  15.969  1.00 86.10           N  
ANISOU 3545  N   ALA B  53     8073  14747   9895  -2270  -2102  -3608       N  
ATOM   3546  CA  ALA B  53      18.134  19.738  17.149  1.00 86.78           C  
ANISOU 3546  CA  ALA B  53     8507  14704   9761  -2184  -2208  -3740       C  
ATOM   3547  C   ALA B  53      17.560  18.622  18.013  1.00 88.86           C  
ANISOU 3547  C   ALA B  53     8911  15151   9702  -1595  -2384  -3522       C  
ATOM   3548  O   ALA B  53      17.950  18.464  19.170  1.00 91.59           O  
ANISOU 3548  O   ALA B  53     9184  15850   9768  -1411  -2674  -3745       O  
ATOM   3549  CB  ALA B  53      17.034  20.707  16.743  1.00 85.47           C  
ANISOU 3549  CB  ALA B  53     8830  13916   9729  -2367  -1902  -3610       C  
ATOM   3550  N   VAL B  54      16.636  17.851  17.449  1.00 80.87           N  
ANISOU 3550  N   VAL B  54     8113  13900   8715  -1311  -2200  -3096       N  
ATOM   3551  CA  VAL B  54      15.939  16.817  18.210  1.00 79.02           C  
ANISOU 3551  CA  VAL B  54     8092  13739   8192   -802  -2279  -2858       C  
ATOM   3552  C   VAL B  54      16.920  15.824  18.826  1.00 85.95           C  
ANISOU 3552  C   VAL B  54     8675  15150   8832   -476  -2581  -2937       C  
ATOM   3553  O   VAL B  54      16.761  15.421  19.975  1.00 87.42           O  
ANISOU 3553  O   VAL B  54     9019  15515   8682   -135  -2760  -2957       O  
ATOM   3554  CB  VAL B  54      14.888  16.056  17.343  1.00 77.84           C  
ANISOU 3554  CB  VAL B  54     8152  13277   8147   -617  -2014  -2414       C  
ATOM   3555  CG1 VAL B  54      14.364  14.818  18.068  1.00 76.50           C  
ANISOU 3555  CG1 VAL B  54     8163  13213   7690   -132  -2069  -2177       C  
ATOM   3556  CG2 VAL B  54      13.730  16.968  16.985  1.00 75.53           C  
ANISOU 3556  CG2 VAL B  54     8193  12512   7993   -796  -1760  -2324       C  
ATOM   3557  N   LEU B  55      17.947  15.452  18.074  1.00 83.46           N  
ANISOU 3557  N   LEU B  55     7940  15100   8669   -553  -2631  -2985       N  
ATOM   3558  CA  LEU B  55      18.836  14.379  18.502  1.00 85.83           C  
ANISOU 3558  CA  LEU B  55     7960  15905   8745   -152  -2894  -3005       C  
ATOM   3559  C   LEU B  55      19.948  14.842  19.445  1.00 96.04           C  
ANISOU 3559  C   LEU B  55     8909  17722   9861   -204  -3254  -3463       C  
ATOM   3560  O   LEU B  55      20.685  14.013  19.967  1.00 98.25           O  
ANISOU 3560  O   LEU B  55     8963  18477   9892    199  -3523  -3511       O  
ATOM   3561  CB  LEU B  55      19.407  13.645  17.278  1.00 84.59           C  
ANISOU 3561  CB  LEU B  55     7505  15833   8804   -129  -2782  -2838       C  
ATOM   3562  CG  LEU B  55      18.333  12.980  16.395  1.00 84.05           C  
ANISOU 3562  CG  LEU B  55     7771  15311   8854    -13  -2470  -2397       C  
ATOM   3563  CD1 LEU B  55      18.930  12.375  15.122  1.00 83.14           C  
ANISOU 3563  CD1 LEU B  55     7375  15262   8953    -35  -2346  -2272       C  
ATOM   3564  CD2 LEU B  55      17.545  11.926  17.187  1.00 85.14           C  
ANISOU 3564  CD2 LEU B  55     8290  15380   8681    491  -2493  -2124       C  
ATOM   3565  N   LYS B  56      20.060  16.149  19.677  1.00 95.41           N  
ANISOU 3565  N   LYS B  56     8806  17559   9888   -680  -3263  -3809       N  
ATOM   3566  CA  LYS B  56      21.037  16.680  20.640  1.00101.28           C  
ANISOU 3566  CA  LYS B  56     9236  18795  10450   -790  -3613  -4304       C  
ATOM   3567  C   LYS B  56      20.397  17.130  21.955  1.00106.67           C  
ANISOU 3567  C   LYS B  56    10318  19401  10810   -661  -3751  -4436       C  
ATOM   3568  O   LYS B  56      20.970  16.910  23.027  1.00110.48           O  
ANISOU 3568  O   LYS B  56    10664  20367  10944   -395  -4110  -4683       O  
ATOM   3569  CB  LYS B  56      21.848  17.834  20.030  1.00106.87           C  
ANISOU 3569  CB  LYS B  56     9580  19534  11493  -1477  -3543  -4695       C  
ATOM   3570  CG  LYS B  56      22.892  17.386  18.999  1.00123.91           C  
ANISOU 3570  CG  LYS B  56    11180  22010  13888  -1587  -3506  -4710       C  
ATOM   3571  CD  LYS B  56      23.868  18.507  18.630  1.00138.97           C  
ANISOU 3571  CD  LYS B  56    12665  24067  16070  -2284  -3469  -5180       C  
ATOM   3572  CE  LYS B  56      24.828  18.073  17.515  1.00151.61           C  
ANISOU 3572  CE  LYS B  56    13724  25956  17925  -2407  -3363  -5165       C  
ATOM   3573  NZ  LYS B  56      25.868  19.103  17.193  1.00167.07           N  
ANISOU 3573  NZ  LYS B  56    15214  28122  20144  -3114  -3306  -5650       N  
ATOM   3574  N   GLU B  57      19.222  17.755  21.874  1.00100.11           N  
ANISOU 3574  N   GLU B  57     9974  17993  10070   -817  -3473  -4279       N  
ATOM   3575  CA  GLU B  57      18.543  18.295  23.057  1.00101.30           C  
ANISOU 3575  CA  GLU B  57    10534  18021   9937   -727  -3546  -4412       C  
ATOM   3576  C   GLU B  57      17.517  17.312  23.634  1.00102.41           C  
ANISOU 3576  C   GLU B  57    11091  18042   9777   -152  -3487  -4006       C  
ATOM   3577  O   GLU B  57      16.600  16.883  22.931  1.00 97.33           O  
ANISOU 3577  O   GLU B  57    10676  17015   9290    -65  -3185  -3603       O  
ATOM   3578  CB  GLU B  57      17.857  19.624  22.716  1.00101.71           C  
ANISOU 3578  CB  GLU B  57    10890  17518  10237  -1203  -3265  -4509       C  
ATOM   3579  CG  GLU B  57      18.801  20.732  22.224  1.00116.11           C  
ANISOU 3579  CG  GLU B  57    12406  19363  12346  -1842  -3260  -4932       C  
ATOM   3580  CD  GLU B  57      19.810  21.210  23.275  1.00145.47           C  
ANISOU 3580  CD  GLU B  57    15854  23573  15844  -2003  -3634  -5496       C  
ATOM   3581  OE1 GLU B  57      19.627  20.927  24.482  1.00143.89           O  
ANISOU 3581  OE1 GLU B  57    15818  23614  15242  -1628  -3887  -5581       O  
ATOM   3582  OE2 GLU B  57      20.792  21.886  22.889  1.00144.08           O  
ANISOU 3582  OE2 GLU B  57    15299  23552  15890  -2525  -3666  -5873       O  
ATOM   3583  N   ARG B  58      17.673  16.978  24.918  1.00102.20           N  
ANISOU 3583  N   ARG B  58    11169  18354   9308    221  -3768  -4131       N  
ATOM   3584  CA  ARG B  58      16.789  16.027  25.607  1.00100.41           C  
ANISOU 3584  CA  ARG B  58    11365  18045   8741    767  -3702  -3770       C  
ATOM   3585  C   ARG B  58      15.388  16.594  25.760  1.00101.27           C  
ANISOU 3585  C   ARG B  58    11965  17626   8887    679  -3384  -3616       C  
ATOM   3586  O   ARG B  58      14.403  15.876  25.587  1.00 97.44           O  
ANISOU 3586  O   ARG B  58    11766  16872   8385    923  -3126  -3210       O  
ATOM   3587  CB  ARG B  58      17.327  15.668  26.998  1.00106.52           C  
ANISOU 3587  CB  ARG B  58    12175  19312   8987   1187  -4079  -3969       C  
ATOM   3588  CG  ARG B  58      18.698  14.993  27.010  1.00123.09           C  
ANISOU 3588  CG  ARG B  58    13783  22024  10960   1415  -4440  -4120       C  
ATOM   3589  CD  ARG B  58      18.647  13.525  26.573  1.00133.75           C  
ANISOU 3589  CD  ARG B  58    15180  23387  12250   1899  -4346  -3657       C  
ATOM   3590  NE  ARG B  58      19.999  12.983  26.385  1.00148.08           N  
ANISOU 3590  NE  ARG B  58    16471  25778  14016   2094  -4662  -3815       N  
ATOM   3591  CZ  ARG B  58      20.559  12.654  25.215  1.00161.78           C  
ANISOU 3591  CZ  ARG B  58    17816  27554  16099   1954  -4575  -3736       C  
ATOM   3592  NH1 ARG B  58      19.897  12.770  24.062  1.00143.16           N  
ANISOU 3592  NH1 ARG B  58    15546  24686  14164   1616  -4187  -3485       N  
ATOM   3593  NH2 ARG B  58      21.807  12.186  25.204  1.00153.63           N  
ANISOU 3593  NH2 ARG B  58    16290  27115  14966   2189  -4886  -3919       N  
ATOM   3594  N   ALA B  59      15.307  17.885  26.080  1.00 99.55           N  
ANISOU 3594  N   ALA B  59    11836  17268   8720    326  -3392  -3959       N  
ATOM   3595  CA  ALA B  59      14.025  18.577  26.266  1.00 97.26           C  
ANISOU 3595  CA  ALA B  59    12000  16499   8456    260  -3101  -3868       C  
ATOM   3596  C   ALA B  59      13.151  18.653  24.997  1.00 95.49           C  
ANISOU 3596  C   ALA B  59    11847  15799   8637     86  -2716  -3535       C  
ATOM   3597  O   ALA B  59      11.970  18.989  25.089  1.00 93.22           O  
ANISOU 3597  O   ALA B  59    11908  15156   8355    139  -2459  -3383       O  
ATOM   3598  CB  ALA B  59      14.266  19.983  26.836  1.00101.85           C  
ANISOU 3598  CB  ALA B  59    12670  17021   9007    -89  -3201  -4349       C  
ATOM   3599  N   LEU B  60      13.729  18.353  23.830  1.00 89.81           N  
ANISOU 3599  N   LEU B  60    10789  15103   8232    -99  -2684  -3437       N  
ATOM   3600  CA  LEU B  60      12.984  18.305  22.563  1.00 84.95           C  
ANISOU 3600  CA  LEU B  60    10216  14097   7963   -224  -2356  -3116       C  
ATOM   3601  C   LEU B  60      12.738  16.875  22.050  1.00 85.05           C  
ANISOU 3601  C   LEU B  60    10163  14176   7977     86  -2273  -2712       C  
ATOM   3602  O   LEU B  60      12.192  16.700  20.956  1.00 81.20           O  
ANISOU 3602  O   LEU B  60     9670  13426   7758     -4  -2034  -2457       O  
ATOM   3603  CB  LEU B  60      13.713  19.112  21.471  1.00 85.28           C  
ANISOU 3603  CB  LEU B  60     9994  14032   8377   -702  -2308  -3286       C  
ATOM   3604  CG  LEU B  60      13.483  20.624  21.388  1.00 91.41           C  
ANISOU 3604  CG  LEU B  60    10978  14448   9305  -1091  -2174  -3536       C  
ATOM   3605  CD1 LEU B  60      14.213  21.183  20.175  1.00 91.66           C  
ANISOU 3605  CD1 LEU B  60    10768  14360   9699  -1540  -2069  -3621       C  
ATOM   3606  CD2 LEU B  60      11.999  20.981  21.333  1.00 91.20           C  
ANISOU 3606  CD2 LEU B  60    11381  13981   9289   -944  -1890  -3301       C  
ATOM   3607  N   GLN B  61      13.114  15.858  22.829  1.00 82.46           N  
ANISOU 3607  N   GLN B  61     9820  14178   7332    461  -2460  -2654       N  
ATOM   3608  CA  GLN B  61      12.973  14.458  22.387  1.00 79.54           C  
ANISOU 3608  CA  GLN B  61     9437  13843   6942    758  -2373  -2289       C  
ATOM   3609  C   GLN B  61      11.547  13.897  22.620  1.00 79.73           C  
ANISOU 3609  C   GLN B  61     9855  13575   6863    975  -2084  -1956       C  
ATOM   3610  O   GLN B  61      11.358  12.864  23.266  1.00 79.66           O  
ANISOU 3610  O   GLN B  61    10039  13660   6567   1338  -2078  -1766       O  
ATOM   3611  CB  GLN B  61      14.067  13.585  23.029  1.00 84.12           C  
ANISOU 3611  CB  GLN B  61     9850  14889   7225   1099  -2682  -2358       C  
ATOM   3612  CG  GLN B  61      15.463  13.870  22.446  1.00100.28           C  
ANISOU 3612  CG  GLN B  61    11389  17259   9454    879  -2909  -2629       C  
ATOM   3613  CD  GLN B  61      16.592  13.037  23.056  1.00124.81           C  
ANISOU 3613  CD  GLN B  61    14268  20897  12258   1267  -3246  -2723       C  
ATOM   3614  OE1 GLN B  61      17.674  12.911  22.468  1.00121.93           O  
ANISOU 3614  OE1 GLN B  61    13459  20832  12037   1188  -3391  -2860       O  
ATOM   3615  NE2 GLN B  61      16.351  12.472  24.236  1.00119.64           N  
ANISOU 3615  NE2 GLN B  61    13917  20377  11164   1713  -3364  -2651       N  
ATOM   3616  N   THR B  62      10.560  14.584  22.045  1.00 73.24           N  
ANISOU 3616  N   THR B  62     9144  12404   6281    746  -1830  -1889       N  
ATOM   3617  CA  THR B  62       9.142  14.252  22.193  1.00 70.76           C  
ANISOU 3617  CA  THR B  62     9126  11841   5917    880  -1539  -1632       C  
ATOM   3618  C   THR B  62       8.700  13.118  21.263  1.00 70.68           C  
ANISOU 3618  C   THR B  62     9074  11721   6060    935  -1341  -1298       C  
ATOM   3619  O   THR B  62       9.291  12.888  20.203  1.00 68.52           O  
ANISOU 3619  O   THR B  62     8551  11460   6021    800  -1373  -1260       O  
ATOM   3620  CB  THR B  62       8.257  15.491  21.868  1.00 77.94           C  
ANISOU 3620  CB  THR B  62    10132  12456   7026    650  -1359  -1712       C  
ATOM   3621  OG1 THR B  62       8.773  16.633  22.559  1.00 82.19           O  
ANISOU 3621  OG1 THR B  62    10715  13042   7471    528  -1532  -2059       O  
ATOM   3622  CG2 THR B  62       6.786  15.269  22.255  1.00 74.65           C  
ANISOU 3622  CG2 THR B  62     9983  11869   6511    816  -1079  -1515       C  
ATOM   3623  N   THR B  63       7.643  12.426  21.678  1.00 65.72           N  
ANISOU 3623  N   THR B  63     8699  10982   5290   1114  -1114  -1076       N  
ATOM   3624  CA  THR B  63       6.931  11.464  20.839  1.00 62.20           C  
ANISOU 3624  CA  THR B  63     8258  10378   4997   1101   -868   -792       C  
ATOM   3625  C   THR B  63       6.555  12.042  19.465  1.00 61.89           C  
ANISOU 3625  C   THR B  63     8010  10167   5341    815   -765   -779       C  
ATOM   3626  O   THR B  63       6.622  11.348  18.455  1.00 60.03           O  
ANISOU 3626  O   THR B  63     7648   9883   5280    750   -698   -632       O  
ATOM   3627  CB  THR B  63       5.657  10.962  21.556  1.00 70.05           C  
ANISOU 3627  CB  THR B  63     9546  11260   5810   1238   -588   -622       C  
ATOM   3628  OG1 THR B  63       4.993  10.006  20.732  1.00 67.12           O  
ANISOU 3628  OG1 THR B  63     9159  10748   5595   1171   -349   -388       O  
ATOM   3629  CG2 THR B  63       4.695  12.114  21.868  1.00 69.35           C  
ANISOU 3629  CG2 THR B  63     9521  11071   5758   1147   -468   -741       C  
ATOM   3630  N   THR B  64       6.175  13.314  19.429  1.00 57.22           N  
ANISOU 3630  N   THR B  64     7416   9472   4852    670   -751   -933       N  
ATOM   3631  CA  THR B  64       5.861  13.990  18.170  1.00 54.53           C  
ANISOU 3631  CA  THR B  64     6930   8961   4827    447   -665   -923       C  
ATOM   3632  C   THR B  64       7.114  14.426  17.389  1.00 57.83           C  
ANISOU 3632  C   THR B  64     7128   9423   5424    248   -841  -1052       C  
ATOM   3633  O   THR B  64       7.144  14.379  16.159  1.00 55.22           O  
ANISOU 3633  O   THR B  64     6654   9003   5323    109   -773   -959       O  
ATOM   3634  CB  THR B  64       4.969  15.209  18.429  1.00 61.74           C  
ANISOU 3634  CB  THR B  64     7982   9716   5761    418   -559  -1026       C  
ATOM   3635  OG1 THR B  64       3.733  14.767  18.998  1.00 61.25           O  
ANISOU 3635  OG1 THR B  64     8062   9642   5567    585   -354   -899       O  
ATOM   3636  CG2 THR B  64       4.685  15.957  17.139  1.00 58.86           C  
ANISOU 3636  CG2 THR B  64     7518   9168   5679    247   -481  -1003       C  
ATOM   3637  N   ASN B  65       8.147  14.842  18.107  1.00 56.58           N  
ANISOU 3637  N   ASN B  65     6929   9423   5145    227  -1058  -1280       N  
ATOM   3638  CA  ASN B  65       9.361  15.327  17.467  1.00 56.95           C  
ANISOU 3638  CA  ASN B  65     6732   9545   5360     -7  -1203  -1449       C  
ATOM   3639  C   ASN B  65      10.182  14.207  16.808  1.00 59.88           C  
ANISOU 3639  C   ASN B  65     6867  10099   5786     49  -1270  -1329       C  
ATOM   3640  O   ASN B  65      10.848  14.444  15.800  1.00 59.06           O  
ANISOU 3640  O   ASN B  65     6548   9992   5901   -160  -1271  -1366       O  
ATOM   3641  CB  ASN B  65      10.183  16.151  18.458  1.00 60.68           C  
ANISOU 3641  CB  ASN B  65     7197  10169   5690    -85  -1418  -1782       C  
ATOM   3642  CG  ASN B  65       9.419  17.371  18.963  1.00 84.20           C  
ANISOU 3642  CG  ASN B  65    10440  12911   8641   -165  -1326  -1922       C  
ATOM   3643  OD1 ASN B  65       8.241  17.546  18.648  1.00 77.38           O  
ANISOU 3643  OD1 ASN B  65     9750  11808   7843   -105  -1109  -1753       O  
ATOM   3644  ND2 ASN B  65      10.082  18.213  19.748  1.00 78.96           N  
ANISOU 3644  ND2 ASN B  65     9801  12329   7870   -291  -1494  -2249       N  
ATOM   3645  N   TYR B  66      10.102  12.986  17.339  1.00 56.32           N  
ANISOU 3645  N   TYR B  66     6491   9779   5130    341  -1291  -1175       N  
ATOM   3646  CA  TYR B  66      10.649  11.816  16.633  1.00 55.07           C  
ANISOU 3646  CA  TYR B  66     6187   9717   5019    446  -1293  -1015       C  
ATOM   3647  C   TYR B  66       9.932  11.580  15.305  1.00 55.00           C  
ANISOU 3647  C   TYR B  66     6164   9474   5260    306  -1067   -817       C  
ATOM   3648  O   TYR B  66      10.509  11.010  14.372  1.00 53.87           O  
ANISOU 3648  O   TYR B  66     5854   9374   5242    278  -1060   -747       O  
ATOM   3649  CB  TYR B  66      10.574  10.546  17.491  1.00 57.55           C  
ANISOU 3649  CB  TYR B  66     6692  10137   5039    812  -1311   -862       C  
ATOM   3650  CG  TYR B  66      11.608  10.482  18.607  1.00 63.46           C  
ANISOU 3650  CG  TYR B  66     7395  11214   5504   1039  -1594  -1039       C  
ATOM   3651  CD1 TYR B  66      12.955  10.775  18.360  1.00 67.43           C  
ANISOU 3651  CD1 TYR B  66     7546  12004   6071    970  -1831  -1257       C  
ATOM   3652  CD2 TYR B  66      11.246  10.101  19.904  1.00 66.28           C  
ANISOU 3652  CD2 TYR B  66     8048  11626   5508   1332  -1621   -998       C  
ATOM   3653  CE1 TYR B  66      13.902  10.716  19.370  1.00 72.23           C  
ANISOU 3653  CE1 TYR B  66     8060  12980   6404   1193  -2124  -1452       C  
ATOM   3654  CE2 TYR B  66      12.186  10.036  20.924  1.00 71.01           C  
ANISOU 3654  CE2 TYR B  66     8615  12563   5805   1584  -1910  -1167       C  
ATOM   3655  CZ  TYR B  66      13.517  10.347  20.650  1.00 80.99           C  
ANISOU 3655  CZ  TYR B  66     9485  14145   7141   1519  -2181  -1406       C  
ATOM   3656  OH  TYR B  66      14.477  10.287  21.645  1.00 87.57           O  
ANISOU 3656  OH  TYR B  66    10226  15385   7662   1781  -2505  -1611       O  
ATOM   3657  N   LEU B  67       8.673  12.009  15.230  1.00 49.17           N  
ANISOU 3657  N   LEU B  67     5593   8517   4573    242   -889   -741       N  
ATOM   3658  CA  LEU B  67       7.922  11.978  13.984  1.00 45.88           C  
ANISOU 3658  CA  LEU B  67     5144   7916   4373    111   -708   -597       C  
ATOM   3659  C   LEU B  67       8.295  13.157  13.100  1.00 48.42           C  
ANISOU 3659  C   LEU B  67     5344   8147   4906   -134   -720   -709       C  
ATOM   3660  O   LEU B  67       8.320  13.048  11.877  1.00 46.31           O  
ANISOU 3660  O   LEU B  67     4978   7808   4808   -241   -641   -619       O  
ATOM   3661  CB  LEU B  67       6.423  11.954  14.266  1.00 44.94           C  
ANISOU 3661  CB  LEU B  67     5205   7662   4209    169   -522   -491       C  
ATOM   3662  CG  LEU B  67       5.889  10.550  14.519  1.00 48.89           C  
ANISOU 3662  CG  LEU B  67     5814   8172   4590    313   -396   -312       C  
ATOM   3663  CD1 LEU B  67       4.523  10.582  15.184  1.00 49.10           C  
ANISOU 3663  CD1 LEU B  67     6001   8131   4523    366   -212   -261       C  
ATOM   3664  CD2 LEU B  67       5.831   9.813  13.195  1.00 48.89           C  
ANISOU 3664  CD2 LEU B  67     5701   8113   4762    220   -311   -187       C  
ATOM   3665  N   VAL B  68       8.601  14.287  13.716  1.00 46.18           N  
ANISOU 3665  N   VAL B  68     5101   7849   4598   -229   -803   -912       N  
ATOM   3666  CA  VAL B  68       9.097  15.423  12.955  1.00 46.15           C  
ANISOU 3666  CA  VAL B  68     5031   7722   4780   -492   -788  -1033       C  
ATOM   3667  C   VAL B  68      10.440  15.053  12.304  1.00 50.93           C  
ANISOU 3667  C   VAL B  68     5363   8500   5487   -621   -873  -1086       C  
ATOM   3668  O   VAL B  68      10.732  15.497  11.186  1.00 49.78           O  
ANISOU 3668  O   VAL B  68     5144   8245   5527   -821   -777  -1067       O  
ATOM   3669  CB  VAL B  68       9.219  16.686  13.816  1.00 51.81           C  
ANISOU 3669  CB  VAL B  68     5881   8363   5442   -601   -845  -1275       C  
ATOM   3670  CG1 VAL B  68       9.513  17.865  12.948  1.00 52.23           C  
ANISOU 3670  CG1 VAL B  68     5962   8192   5692   -882   -751  -1361       C  
ATOM   3671  CG2 VAL B  68       7.934  16.928  14.576  1.00 51.33           C  
ANISOU 3671  CG2 VAL B  68     6076   8180   5246   -414   -758  -1228       C  
ATOM   3672  N   VAL B  69      11.236  14.221  12.982  1.00 49.03           N  
ANISOU 3672  N   VAL B  69     4982   8540   5107   -473  -1039  -1142       N  
ATOM   3673  CA  VAL B  69      12.455  13.673  12.371  1.00 49.53           C  
ANISOU 3673  CA  VAL B  69     4752   8822   5247   -515  -1114  -1175       C  
ATOM   3674  C   VAL B  69      12.114  12.796  11.172  1.00 51.58           C  
ANISOU 3674  C   VAL B  69     4999   8985   5612   -457   -960   -929       C  
ATOM   3675  O   VAL B  69      12.699  12.954  10.099  1.00 51.30           O  
ANISOU 3675  O   VAL B  69     4800   8947   5744   -628   -892   -930       O  
ATOM   3676  CB  VAL B  69      13.315  12.855  13.357  1.00 55.29           C  
ANISOU 3676  CB  VAL B  69     5347   9900   5763   -266  -1337  -1265       C  
ATOM   3677  CG1 VAL B  69      13.913  11.636  12.665  1.00 54.49           C  
ANISOU 3677  CG1 VAL B  69     5078   9947   5679    -94  -1332  -1124       C  
ATOM   3678  CG2 VAL B  69      14.410  13.726  13.956  1.00 58.60           C  
ANISOU 3678  CG2 VAL B  69     5543  10558   6165   -445  -1533  -1601       C  
ATOM   3679  N   SER B  70      11.165  11.880  11.347  1.00 46.37           N  
ANISOU 3679  N   SER B  70     4525   8246   4850   -239   -887   -732       N  
ATOM   3680  CA  SER B  70      10.721  11.032  10.240  1.00 43.85           C  
ANISOU 3680  CA  SER B  70     4223   7821   4617   -208   -740   -529       C  
ATOM   3681  C   SER B  70      10.206  11.868   9.078  1.00 47.40           C  
ANISOU 3681  C   SER B  70     4686   8071   5252   -426   -602   -490       C  
ATOM   3682  O   SER B  70      10.410  11.522   7.923  1.00 45.81           O  
ANISOU 3682  O   SER B  70     4406   7845   5155   -483   -522   -407       O  
ATOM   3683  CB  SER B  70       9.638  10.065  10.697  1.00 45.36           C  
ANISOU 3683  CB  SER B  70     4633   7927   4676    -16   -651   -365       C  
ATOM   3684  OG  SER B  70       9.293   9.173   9.655  1.00 50.83           O  
ANISOU 3684  OG  SER B  70     5336   8534   5443    -13   -521   -211       O  
ATOM   3685  N   LEU B  71       9.546  12.979   9.390  1.00 45.15           N  
ANISOU 3685  N   LEU B  71     4532   7641   4984   -514   -571   -550       N  
ATOM   3686  CA  LEU B  71       9.110  13.920   8.361  1.00 44.56           C  
ANISOU 3686  CA  LEU B  71     4520   7363   5047   -671   -448   -514       C  
ATOM   3687  C   LEU B  71      10.305  14.588   7.687  1.00 50.04           C  
ANISOU 3687  C   LEU B  71     5080   8063   5871   -905   -438   -621       C  
ATOM   3688  O   LEU B  71      10.417  14.551   6.466  1.00 48.98           O  
ANISOU 3688  O   LEU B  71     4914   7863   5834   -984   -330   -524       O  
ATOM   3689  CB  LEU B  71       8.181  14.981   8.955  1.00 45.07           C  
ANISOU 3689  CB  LEU B  71     4789   7260   5074   -657   -412   -563       C  
ATOM   3690  CG  LEU B  71       7.663  16.056   7.999  1.00 49.74           C  
ANISOU 3690  CG  LEU B  71     5516   7615   5766   -743   -284   -516       C  
ATOM   3691  CD1 LEU B  71       7.272  15.450   6.654  1.00 48.35           C  
ANISOU 3691  CD1 LEU B  71     5290   7432   5647   -706   -200   -336       C  
ATOM   3692  CD2 LEU B  71       6.484  16.799   8.618  1.00 52.39           C  
ANISOU 3692  CD2 LEU B  71     6061   7816   6030   -609   -240   -526       C  
ATOM   3693  N   ALA B  72      11.189  15.190   8.487  1.00 49.13           N  
ANISOU 3693  N   ALA B  72     4881   8041   5745  -1031   -542   -835       N  
ATOM   3694  CA  ALA B  72      12.368  15.887   7.962  1.00 51.37           C  
ANISOU 3694  CA  ALA B  72     5004   8352   6163  -1321   -509   -985       C  
ATOM   3695  C   ALA B  72      13.210  15.013   7.020  1.00 55.33           C  
ANISOU 3695  C   ALA B  72     5254   9033   6734  -1326   -478   -916       C  
ATOM   3696  O   ALA B  72      13.589  15.464   5.937  1.00 55.60           O  
ANISOU 3696  O   ALA B  72     5261   8969   6897  -1527   -324   -890       O  
ATOM   3697  CB  ALA B  72      13.233  16.410   9.101  1.00 55.19           C  
ANISOU 3697  CB  ALA B  72     5364   9005   6601  -1447   -668  -1271       C  
ATOM   3698  N   VAL B  73      13.493  13.772   7.429  1.00 51.24           N  
ANISOU 3698  N   VAL B  73     4593   8761   6114  -1084   -602   -878       N  
ATOM   3699  CA  VAL B  73      14.237  12.818   6.590  1.00 50.70           C  
ANISOU 3699  CA  VAL B  73     4317   8861   6087  -1016   -569   -808       C  
ATOM   3700  C   VAL B  73      13.622  12.749   5.190  1.00 53.33           C  
ANISOU 3700  C   VAL B  73     4784   8974   6504  -1064   -371   -614       C  
ATOM   3701  O   VAL B  73      14.325  12.913   4.184  1.00 53.35           O  
ANISOU 3701  O   VAL B  73     4659   9000   6612  -1218   -254   -618       O  
ATOM   3702  CB  VAL B  73      14.229  11.394   7.183  1.00 53.66           C  
ANISOU 3702  CB  VAL B  73     4675   9412   6303   -665   -687   -725       C  
ATOM   3703  CG1 VAL B  73      14.984  10.439   6.277  1.00 53.52           C  
ANISOU 3703  CG1 VAL B  73     4480   9535   6320   -567   -633   -658       C  
ATOM   3704  CG2 VAL B  73      14.821  11.379   8.568  1.00 55.79           C  
ANISOU 3704  CG2 VAL B  73     4837   9930   6430   -543   -904   -899       C  
ATOM   3705  N   ALA B  74      12.303  12.512   5.147  1.00 48.50           N  
ANISOU 3705  N   ALA B  74     4417   8178   5832   -932   -333   -458       N  
ATOM   3706  CA  ALA B  74      11.510  12.542   3.908  1.00 46.71           C  
ANISOU 3706  CA  ALA B  74     4335   7766   5648   -951   -184   -295       C  
ATOM   3707  C   ALA B  74      11.962  13.652   2.989  1.00 52.96           C  
ANISOU 3707  C   ALA B  74     5144   8430   6548  -1189    -48   -319       C  
ATOM   3708  O   ALA B  74      12.138  13.428   1.794  1.00 52.90           O  
ANISOU 3708  O   ALA B  74     5129   8398   6572  -1221     71   -225       O  
ATOM   3709  CB  ALA B  74      10.031  12.719   4.216  1.00 45.88           C  
ANISOU 3709  CB  ALA B  74     4449   7506   5479   -844   -179   -210       C  
ATOM   3710  N   ASP B  75      12.157  14.843   3.555  1.00 51.31           N  
ANISOU 3710  N   ASP B  75     4994   8122   6381  -1363    -47   -449       N  
ATOM   3711  CA  ASP B  75      12.576  16.025   2.791  1.00 52.69           C  
ANISOU 3711  CA  ASP B  75     5261   8106   6653  -1627    127   -478       C  
ATOM   3712  C   ASP B  75      14.060  15.976   2.444  1.00 57.05           C  
ANISOU 3712  C   ASP B  75     5527   8843   7305  -1856    187   -607       C  
ATOM   3713  O   ASP B  75      14.433  16.313   1.329  1.00 57.44           O  
ANISOU 3713  O   ASP B  75     5611   8796   7418  -2011    383   -543       O  
ATOM   3714  CB  ASP B  75      12.227  17.316   3.554  1.00 56.11           C  
ANISOU 3714  CB  ASP B  75     5909   8319   7091  -1745    135   -590       C  
ATOM   3715  CG  ASP B  75      10.726  17.411   3.907  1.00 64.39           C  
ANISOU 3715  CG  ASP B  75     7211   9218   8035  -1487     93   -473       C  
ATOM   3716  OD1 ASP B  75       9.889  16.783   3.196  1.00 62.99           O  
ANISOU 3716  OD1 ASP B  75     7083   9044   7807  -1288    113   -290       O  
ATOM   3717  OD2 ASP B  75      10.397  18.115   4.900  1.00 70.69           O  
ANISOU 3717  OD2 ASP B  75     8140   9920   8800  -1489     42   -587       O  
ATOM   3718  N   LEU B  76      14.893  15.533   3.383  1.00 53.60           N  
ANISOU 3718  N   LEU B  76     4803   8699   6866  -1852     22   -787       N  
ATOM   3719  CA  LEU B  76      16.348  15.444   3.155  1.00 55.49           C  
ANISOU 3719  CA  LEU B  76     4681   9206   7198  -2046     53   -951       C  
ATOM   3720  C   LEU B  76      16.705  14.522   1.997  1.00 57.05           C  
ANISOU 3720  C   LEU B  76     4755   9513   7407  -1938    166   -807       C  
ATOM   3721  O   LEU B  76      17.702  14.741   1.309  1.00 58.61           O  
ANISOU 3721  O   LEU B  76     4745   9821   7704  -2154    318   -883       O  
ATOM   3722  CB  LEU B  76      17.092  14.964   4.413  1.00 57.03           C  
ANISOU 3722  CB  LEU B  76     4567   9768   7335  -1949   -199  -1164       C  
ATOM   3723  CG  LEU B  76      17.210  15.945   5.584  1.00 63.73           C  
ANISOU 3723  CG  LEU B  76     5429  10611   8175  -2137   -319  -1409       C  
ATOM   3724  CD1 LEU B  76      17.951  15.299   6.749  1.00 65.34           C  
ANISOU 3724  CD1 LEU B  76     5317  11243   8268  -1961   -601  -1604       C  
ATOM   3725  CD2 LEU B  76      17.907  17.220   5.150  1.00 69.62           C  
ANISOU 3725  CD2 LEU B  76     6133  11234   9084  -2616   -129  -1591       C  
ATOM   3726  N   LEU B  77      15.892  13.491   1.795  1.00 50.01           N  
ANISOU 3726  N   LEU B  77     3996   8593   6412  -1622    110   -619       N  
ATOM   3727  CA  LEU B  77      16.130  12.519   0.731  1.00 48.75           C  
ANISOU 3727  CA  LEU B  77     3771   8514   6237  -1488    207   -493       C  
ATOM   3728  C   LEU B  77      15.575  13.003  -0.616  1.00 51.63           C  
ANISOU 3728  C   LEU B  77     4386   8616   6614  -1591    425   -330       C  
ATOM   3729  O   LEU B  77      16.104  12.627  -1.666  1.00 51.73           O  
ANISOU 3729  O   LEU B  77     4326   8691   6637  -1605    573   -277       O  
ATOM   3730  CB  LEU B  77      15.531  11.166   1.112  1.00 46.51           C  
ANISOU 3730  CB  LEU B  77     3552   8292   5829  -1137     69   -390       C  
ATOM   3731  CG  LEU B  77      16.110  10.528   2.381  1.00 52.07           C  
ANISOU 3731  CG  LEU B  77     4061   9259   6464   -948   -137   -511       C  
ATOM   3732  CD1 LEU B  77      15.113   9.576   3.037  1.00 50.07           C  
ANISOU 3732  CD1 LEU B  77     4033   8920   6071   -663   -239   -390       C  
ATOM   3733  CD2 LEU B  77      17.425   9.821   2.070  1.00 56.51           C  
ANISOU 3733  CD2 LEU B  77     4298  10132   7040   -849   -132   -591       C  
ATOM   3734  N   VAL B  78      14.528  13.833  -0.590  1.00 46.83           N  
ANISOU 3734  N   VAL B  78     4081   7732   5981  -1627    446   -253       N  
ATOM   3735  CA  VAL B  78      14.062  14.510  -1.806  1.00 46.75           C  
ANISOU 3735  CA  VAL B  78     4336   7475   5952  -1702    644   -107       C  
ATOM   3736  C   VAL B  78      15.122  15.470  -2.351  1.00 53.62           C  
ANISOU 3736  C   VAL B  78     5165   8285   6924  -2033    874   -180       C  
ATOM   3737  O   VAL B  78      15.418  15.468  -3.544  1.00 54.11           O  
ANISOU 3737  O   VAL B  78     5288   8304   6968  -2087   1074    -79       O  
ATOM   3738  CB  VAL B  78      12.793  15.343  -1.565  1.00 49.92           C  
ANISOU 3738  CB  VAL B  78     5063   7610   6295  -1635    616    -28       C  
ATOM   3739  CG1 VAL B  78      12.384  16.067  -2.836  1.00 50.55           C  
ANISOU 3739  CG1 VAL B  78     5441   7451   6317  -1654    812    132       C  
ATOM   3740  CG2 VAL B  78      11.666  14.474  -1.110  1.00 47.27           C  
ANISOU 3740  CG2 VAL B  78     4758   7337   5867  -1357    437     37       C  
ATOM   3741  N   ALA B  79      15.681  16.294  -1.470  1.00 51.78           N  
ANISOU 3741  N   ALA B  79     4840   8045   6788  -2275    859   -367       N  
ATOM   3742  CA  ALA B  79      16.682  17.278  -1.867  1.00 54.82           C  
ANISOU 3742  CA  ALA B  79     5184   8354   7290  -2669   1104   -478       C  
ATOM   3743  C   ALA B  79      17.927  16.617  -2.447  1.00 59.92           C  
ANISOU 3743  C   ALA B  79     5448   9316   8003  -2767   1210   -551       C  
ATOM   3744  O   ALA B  79      18.560  17.167  -3.347  1.00 62.35           O  
ANISOU 3744  O   ALA B  79     5781   9541   8368  -3033   1501   -541       O  
ATOM   3745  CB  ALA B  79      17.059  18.164  -0.681  1.00 57.69           C  
ANISOU 3745  CB  ALA B  79     5481   8697   7744  -2929   1032   -726       C  
ATOM   3746  N   THR B  80      18.268  15.434  -1.944  1.00 54.75           N  
ANISOU 3746  N   THR B  80     4464   9014   7325  -2530    996   -617       N  
ATOM   3747  CA  THR B  80      19.507  14.774  -2.332  1.00 56.38           C  
ANISOU 3747  CA  THR B  80     4259   9574   7588  -2563   1069   -718       C  
ATOM   3748  C   THR B  80      19.332  13.723  -3.429  1.00 58.31           C  
ANISOU 3748  C   THR B  80     4564   9855   7737  -2292   1152   -525       C  
ATOM   3749  O   THR B  80      20.172  13.621  -4.316  1.00 60.20           O  
ANISOU 3749  O   THR B  80     4640  10219   8014  -2401   1373   -536       O  
ATOM   3750  CB  THR B  80      20.215  14.154  -1.104  1.00 65.06           C  
ANISOU 3750  CB  THR B  80     4938  11080   8703  -2441    794   -939       C  
ATOM   3751  OG1 THR B  80      19.258  13.480  -0.282  1.00 61.01           O  
ANISOU 3751  OG1 THR B  80     4597  10521   8064  -2093    531   -851       O  
ATOM   3752  CG2 THR B  80      20.901  15.243  -0.278  1.00 67.34           C  
ANISOU 3752  CG2 THR B  80     5028  11449   9110  -2824    776  -1221       C  
ATOM   3753  N   LEU B  81      18.260  12.939  -3.385  1.00 50.97           N  
ANISOU 3753  N   LEU B  81     3864   8823   6681  -1961    994   -367       N  
ATOM   3754  CA  LEU B  81      18.125  11.823  -4.331  1.00 49.21           C  
ANISOU 3754  CA  LEU B  81     3689   8651   6358  -1709   1047   -231       C  
ATOM   3755  C   LEU B  81      17.272  12.151  -5.551  1.00 52.71           C  
ANISOU 3755  C   LEU B  81     4512   8809   6705  -1714   1212    -33       C  
ATOM   3756  O   LEU B  81      17.421  11.505  -6.587  1.00 52.75           O  
ANISOU 3756  O   LEU B  81     4553   8858   6632  -1605   1334     47       O  
ATOM   3757  CB  LEU B  81      17.583  10.564  -3.640  1.00 46.64           C  
ANISOU 3757  CB  LEU B  81     3368   8412   5940  -1356    803   -204       C  
ATOM   3758  CG  LEU B  81      18.327   9.994  -2.422  1.00 51.99           C  
ANISOU 3758  CG  LEU B  81     3730   9384   6638  -1216    606   -362       C  
ATOM   3759  CD1 LEU B  81      18.091   8.497  -2.303  1.00 50.52           C  
ANISOU 3759  CD1 LEU B  81     3598   9265   6334   -837    500   -289       C  
ATOM   3760  CD2 LEU B  81      19.825  10.268  -2.489  1.00 58.35           C  
ANISOU 3760  CD2 LEU B  81     4113  10507   7550  -1374    697   -544       C  
ATOM   3761  N   VAL B  82      16.395  13.148  -5.434  1.00 48.84           N  
ANISOU 3761  N   VAL B  82     4316   8044   6199  -1806   1210     37       N  
ATOM   3762  CA  VAL B  82      15.411  13.456  -6.481  1.00 47.72           C  
ANISOU 3762  CA  VAL B  82     4554   7658   5920  -1722   1305    229       C  
ATOM   3763  C   VAL B  82      15.697  14.791  -7.175  1.00 55.13           C  
ANISOU 3763  C   VAL B  82     5714   8363   6868  -1977   1581    289       C  
ATOM   3764  O   VAL B  82      15.848  14.846  -8.394  1.00 55.87           O  
ANISOU 3764  O   VAL B  82     5967   8396   6865  -1981   1794    407       O  
ATOM   3765  CB  VAL B  82      13.968  13.451  -5.895  1.00 48.47           C  
ANISOU 3765  CB  VAL B  82     4854   7623   5938  -1526   1084    292       C  
ATOM   3766  CG1 VAL B  82      12.978  14.061  -6.874  1.00 48.35           C  
ANISOU 3766  CG1 VAL B  82     5207   7387   5778  -1437   1162    462       C  
ATOM   3767  CG2 VAL B  82      13.553  12.024  -5.505  1.00 45.67           C  
ANISOU 3767  CG2 VAL B  82     4373   7442   5537  -1286    884    272       C  
ATOM   3768  N   MET B  83      15.796  15.860  -6.391  1.00 53.71           N  
ANISOU 3768  N   MET B  83     5580   8034   6792  -2194   1598    203       N  
ATOM   3769  CA  MET B  83      15.897  17.214  -6.943  1.00 56.67           C  
ANISOU 3769  CA  MET B  83     6276   8091   7165  -2434   1877    271       C  
ATOM   3770  C   MET B  83      17.128  17.498  -7.814  1.00 65.03           C  
ANISOU 3770  C   MET B  83     7247   9180   8281  -2735   2226    249       C  
ATOM   3771  O   MET B  83      17.087  18.415  -8.640  1.00 67.24           O  
ANISOU 3771  O   MET B  83     7894   9163   8492  -2868   2513    381       O  
ATOM   3772  CB  MET B  83      15.794  18.250  -5.826  1.00 59.94           C  
ANISOU 3772  CB  MET B  83     6766   8322   7684  -2625   1828    144       C  
ATOM   3773  CG  MET B  83      14.368  18.459  -5.380  1.00 61.21           C  
ANISOU 3773  CG  MET B  83     7216   8306   7737  -2334   1626    244       C  
ATOM   3774  SD  MET B  83      14.182  19.550  -3.970  1.00 66.46           S  
ANISOU 3774  SD  MET B  83     7980   8771   8499  -2498   1546     75       S  
ATOM   3775  CE  MET B  83      15.051  21.023  -4.541  1.00 68.11           C  
ANISOU 3775  CE  MET B  83     8475   8617   8786  -2950   1961     47       C  
ATOM   3776  N   PRO B  84      18.225  16.739  -7.632  1.00 62.69           N  
ANISOU 3776  N   PRO B  84     6478   9243   8098  -2829   2222     85       N  
ATOM   3777  CA  PRO B  84      19.303  16.853  -8.615  1.00 66.02           C  
ANISOU 3777  CA  PRO B  84     6792   9742   8549  -3064   2574     79       C  
ATOM   3778  C   PRO B  84      18.865  16.479 -10.032  1.00 70.61           C  
ANISOU 3778  C   PRO B  84     7684  10225   8918  -2839   2731    320       C  
ATOM   3779  O   PRO B  84      19.199  17.176 -10.986  1.00 73.33           O  
ANISOU 3779  O   PRO B  84     8274  10381   9205  -3028   3086    425       O  
ATOM   3780  CB  PRO B  84      20.349  15.868  -8.096  1.00 68.00           C  
ANISOU 3780  CB  PRO B  84     6451  10464   8922  -3051   2456   -134       C  
ATOM   3781  CG  PRO B  84      20.144  15.879  -6.642  1.00 71.14           C  
ANISOU 3781  CG  PRO B  84     6671  10949   9408  -3026   2132   -297       C  
ATOM   3782  CD  PRO B  84      18.659  15.979  -6.448  1.00 63.15           C  
ANISOU 3782  CD  PRO B  84     6086   9642   8266  -2766   1941   -122       C  
ATOM   3783  N   TRP B  85      18.108  15.399 -10.167  1.00 64.67           N  
ANISOU 3783  N   TRP B  85     6948   9588   8035  -2450   2479    399       N  
ATOM   3784  CA  TRP B  85      17.636  14.980 -11.478  1.00 64.64           C  
ANISOU 3784  CA  TRP B  85     7229   9526   7804  -2223   2580    588       C  
ATOM   3785  C   TRP B  85      16.564  15.940 -12.001  1.00 68.51           C  
ANISOU 3785  C   TRP B  85     8256   9656   8118  -2140   2629    791       C  
ATOM   3786  O   TRP B  85      16.497  16.190 -13.200  1.00 69.60           O  
ANISOU 3786  O   TRP B  85     8707   9672   8066  -2087   2855    954       O  
ATOM   3787  CB  TRP B  85      17.121  13.539 -11.437  1.00 60.62           C  
ANISOU 3787  CB  TRP B  85     6590   9232   7210  -1872   2299    574       C  
ATOM   3788  CG  TRP B  85      18.156  12.552 -10.940  1.00 62.05           C  
ANISOU 3788  CG  TRP B  85     6301   9748   7526  -1865   2252    398       C  
ATOM   3789  CD1 TRP B  85      18.381  12.195  -9.641  1.00 63.95           C  
ANISOU 3789  CD1 TRP B  85     6228  10154   7915  -1849   2018    242       C  
ATOM   3790  CD2 TRP B  85      19.105  11.808 -11.729  1.00 63.74           C  
ANISOU 3790  CD2 TRP B  85     6324  10184   7710  -1822   2444    363       C  
ATOM   3791  NE1 TRP B  85      19.404  11.279  -9.569  1.00 64.65           N  
ANISOU 3791  NE1 TRP B  85     5944  10558   8061  -1771   2036    119       N  
ATOM   3792  CE2 TRP B  85      19.866  11.022 -10.835  1.00 67.84           C  
ANISOU 3792  CE2 TRP B  85     6404  11004   8369  -1754   2301    185       C  
ATOM   3793  CE3 TRP B  85      19.382  11.725 -13.099  1.00 66.83           C  
ANISOU 3793  CE3 TRP B  85     6887  10558   7948  -1802   2726    466       C  
ATOM   3794  CZ2 TRP B  85      20.886  10.162 -11.270  1.00 68.97           C  
ANISOU 3794  CZ2 TRP B  85     6259  11433   8513  -1647   2431    104       C  
ATOM   3795  CZ3 TRP B  85      20.395  10.867 -13.526  1.00 69.95           C  
ANISOU 3795  CZ3 TRP B  85     6997  11231   8352  -1730   2869    378       C  
ATOM   3796  CH2 TRP B  85      21.131  10.098 -12.614  1.00 70.54           C  
ANISOU 3796  CH2 TRP B  85     6618  11604   8579  -1644   2721    198       C  
ATOM   3797  N   VAL B  86      15.744  16.492 -11.107  1.00 63.83           N  
ANISOU 3797  N   VAL B  86     7782   8904   7567  -2096   2426    782       N  
ATOM   3798  CA  VAL B  86      14.751  17.504 -11.500  1.00 64.31           C  
ANISOU 3798  CA  VAL B  86     8348   8626   7460  -1975   2472    965       C  
ATOM   3799  C   VAL B  86      15.439  18.759 -12.050  1.00 72.50           C  
ANISOU 3799  C   VAL B  86     9692   9356   8499  -2279   2888   1044       C  
ATOM   3800  O   VAL B  86      14.906  19.426 -12.942  1.00 73.48           O  
ANISOU 3800  O   VAL B  86    10304   9213   8401  -2138   3049   1256       O  
ATOM   3801  CB  VAL B  86      13.826  17.895 -10.327  1.00 66.05           C  
ANISOU 3801  CB  VAL B  86     8608   8746   7744  -1874   2202    914       C  
ATOM   3802  CG1 VAL B  86      12.856  18.984 -10.754  1.00 67.28           C  
ANISOU 3802  CG1 VAL B  86     9288   8560   7715  -1699   2267   1102       C  
ATOM   3803  CG2 VAL B  86      13.065  16.681  -9.819  1.00 62.02           C  
ANISOU 3803  CG2 VAL B  86     7844   8504   7216  -1599   1841    852       C  
ATOM   3804  N   VAL B  87      16.618  19.071 -11.505  1.00 71.50           N  
ANISOU 3804  N   VAL B  87     9282   9275   8610  -2693   3066    863       N  
ATOM   3805  CA  VAL B  87      17.497  20.114 -12.050  1.00 76.08           C  
ANISOU 3805  CA  VAL B  87    10073   9604   9229  -3088   3526    891       C  
ATOM   3806  C   VAL B  87      17.973  19.745 -13.457  1.00 82.58           C  
ANISOU 3806  C   VAL B  87    10995  10497   9886  -3054   3821   1036       C  
ATOM   3807  O   VAL B  87      17.944  20.581 -14.362  1.00 85.86           O  
ANISOU 3807  O   VAL B  87    11900  10585  10136  -3115   4166   1229       O  
ATOM   3808  CB  VAL B  87      18.721  20.373 -11.122  1.00 81.83           C  
ANISOU 3808  CB  VAL B  87    10348  10476  10266  -3576   3622    597       C  
ATOM   3809  CG1 VAL B  87      19.969  20.738 -11.920  1.00 86.20           C  
ANISOU 3809  CG1 VAL B  87    10835  11033  10883  -3990   4103    565       C  
ATOM   3810  CG2 VAL B  87      18.389  21.446 -10.100  1.00 82.51           C  
ANISOU 3810  CG2 VAL B  87    10628  10261  10462  -3762   3569    501       C  
ATOM   3811  N   TYR B  88      18.402  18.497 -13.640  1.00 77.47           N  
ANISOU 3811  N   TYR B  88     9925  10253   9257  -2932   3703    949       N  
ATOM   3812  CA  TYR B  88      18.807  18.002 -14.962  1.00 78.94           C  
ANISOU 3812  CA  TYR B  88    10190  10543   9261  -2846   3954   1068       C  
ATOM   3813  C   TYR B  88      17.650  18.135 -15.950  1.00 81.98           C  
ANISOU 3813  C   TYR B  88    11143  10711   9296  -2463   3916   1337       C  
ATOM   3814  O   TYR B  88      17.790  18.780 -16.989  1.00 84.82           O  
ANISOU 3814  O   TYR B  88    11926  10843   9460  -2504   4271   1523       O  
ATOM   3815  CB  TYR B  88      19.308  16.546 -14.875  1.00 78.36           C  
ANISOU 3815  CB  TYR B  88     9597  10925   9251  -2696   3774    917       C  
ATOM   3816  CG  TYR B  88      19.281  15.763 -16.179  1.00 80.91           C  
ANISOU 3816  CG  TYR B  88    10062  11361   9319  -2438   3888   1042       C  
ATOM   3817  CD1 TYR B  88      20.199  16.027 -17.198  1.00 87.05           C  
ANISOU 3817  CD1 TYR B  88    10910  12138  10025  -2630   4347   1100       C  
ATOM   3818  CD2 TYR B  88      18.345  14.745 -16.384  1.00 78.36           C  
ANISOU 3818  CD2 TYR B  88     9802  11150   8822  -2026   3554   1080       C  
ATOM   3819  CE1 TYR B  88      20.176  15.307 -18.400  1.00 88.53           C  
ANISOU 3819  CE1 TYR B  88    11254  12433   9951  -2377   4456   1204       C  
ATOM   3820  CE2 TYR B  88      18.313  14.019 -17.576  1.00 79.91           C  
ANISOU 3820  CE2 TYR B  88    10145  11447   8767  -1801   3647   1161       C  
ATOM   3821  CZ  TYR B  88      19.229  14.302 -18.582  1.00 91.48           C  
ANISOU 3821  CZ  TYR B  88    11702  12913  10144  -1957   4091   1227       C  
ATOM   3822  OH  TYR B  88      19.196  13.583 -19.765  1.00 93.41           O  
ANISOU 3822  OH  TYR B  88    12117  13261  10113  -1717   4186   1297       O  
ATOM   3823  N   LEU B  89      16.500  17.560 -15.604  1.00 74.69           N  
ANISOU 3823  N   LEU B  89    10230   9866   8283  -2093   3492   1350       N  
ATOM   3824  CA  LEU B  89      15.310  17.632 -16.466  1.00 74.26           C  
ANISOU 3824  CA  LEU B  89    10637   9690   7888  -1695   3381   1561       C  
ATOM   3825  C   LEU B  89      14.874  19.064 -16.790  1.00 81.65           C  
ANISOU 3825  C   LEU B  89    12154  10199   8672  -1686   3593   1767       C  
ATOM   3826  O   LEU B  89      14.175  19.277 -17.775  1.00 82.64           O  
ANISOU 3826  O   LEU B  89    12719  10219   8463  -1369   3617   1972       O  
ATOM   3827  CB  LEU B  89      14.134  16.842 -15.866  1.00 70.11           C  
ANISOU 3827  CB  LEU B  89     9954   9345   7340  -1368   2894   1491       C  
ATOM   3828  CG  LEU B  89      14.010  15.384 -16.336  1.00 72.80           C  
ANISOU 3828  CG  LEU B  89    10064  10015   7583  -1162   2708   1414       C  
ATOM   3829  CD1 LEU B  89      13.649  14.478 -15.183  1.00 69.44           C  
ANISOU 3829  CD1 LEU B  89     9242   9789   7351  -1116   2353   1231       C  
ATOM   3830  CD2 LEU B  89      12.993  15.237 -17.468  1.00 75.79           C  
ANISOU 3830  CD2 LEU B  89    10805  10402   7589   -801   2608   1557       C  
ATOM   3831  N   GLU B  90      15.277  20.032 -15.967  1.00 80.01           N  
ANISOU 3831  N   GLU B  90    11973   9742   8686  -2011   3742   1706       N  
ATOM   3832  CA  GLU B  90      15.060  21.453 -16.271  1.00 83.77           C  
ANISOU 3832  CA  GLU B  90    13057   9736   9035  -2060   4035   1896       C  
ATOM   3833  C   GLU B  90      16.199  22.028 -17.118  1.00 92.44           C  
ANISOU 3833  C   GLU B  90    14375  10638  10109  -2427   4597   1979       C  
ATOM   3834  O   GLU B  90      15.958  22.875 -17.977  1.00 95.17           O  
ANISOU 3834  O   GLU B  90    15347  10625  10190  -2324   4891   2228       O  
ATOM   3835  CB  GLU B  90      14.880  22.267 -14.980  1.00 84.90           C  
ANISOU 3835  CB  GLU B  90    13195   9654   9411  -2243   3946   1774       C  
ATOM   3836  CG  GLU B  90      13.503  22.087 -14.304  1.00 92.24           C  
ANISOU 3836  CG  GLU B  90    14127  10644  10274  -1816   3481   1775       C  
ATOM   3837  CD  GLU B  90      12.440  23.103 -14.756  1.00116.34           C  
ANISOU 3837  CD  GLU B  90    17840  13328  13038  -1445   3517   2022       C  
ATOM   3838  OE1 GLU B  90      12.655  23.830 -15.753  1.00114.89           O  
ANISOU 3838  OE1 GLU B  90    18180  12837  12637  -1434   3879   2238       O  
ATOM   3839  OE2 GLU B  90      11.376  23.172 -14.098  1.00108.65           O  
ANISOU 3839  OE2 GLU B  90    16868  12377  12039  -1137   3192   2003       O  
ATOM   3840  N   VAL B  91      17.425  21.565 -16.869  1.00 90.03           N  
ANISOU 3840  N   VAL B  91    13559  10583  10067  -2835   4756   1770       N  
ATOM   3841  CA  VAL B  91      18.597  21.978 -17.656  1.00 95.10           C  
ANISOU 3841  CA  VAL B  91    14292  11125  10717  -3230   5314   1806       C  
ATOM   3842  C   VAL B  91      18.384  21.684 -19.142  1.00100.74           C  
ANISOU 3842  C   VAL B  91    15395  11837  11044  -2914   5497   2061       C  
ATOM   3843  O   VAL B  91      18.395  22.604 -19.961  1.00104.89           O  
ANISOU 3843  O   VAL B  91    16531  11977  11346  -2952   5900   2295       O  
ATOM   3844  CB  VAL B  91      19.902  21.289 -17.163  1.00 99.25           C  
ANISOU 3844  CB  VAL B  91    14071  12067  11571  -3625   5378   1505       C  
ATOM   3845  CG1 VAL B  91      21.013  21.389 -18.215  1.00103.72           C  
ANISOU 3845  CG1 VAL B  91    14659  12661  12087  -3924   5932   1552       C  
ATOM   3846  CG2 VAL B  91      20.353  21.892 -15.838  1.00 99.66           C  
ANISOU 3846  CG2 VAL B  91    13826  12066  11974  -4050   5334   1249       C  
ATOM   3847  N   THR B  92      18.189  20.408 -19.483  1.00 93.90           N  
ANISOU 3847  N   THR B  92    14217  11382  10080  -2598   5213   2014       N  
ATOM   3848  CA  THR B  92      17.725  20.032 -20.824  1.00 94.44           C  
ANISOU 3848  CA  THR B  92    14668  11484   9731  -2205   5262   2231       C  
ATOM   3849  C   THR B  92      16.226  20.351 -20.892  1.00 96.62           C  
ANISOU 3849  C   THR B  92    15390  11591   9732  -1717   4913   2403       C  
ATOM   3850  O   THR B  92      15.570  20.494 -19.856  1.00 93.21           O  
ANISOU 3850  O   THR B  92    14819  11130   9465  -1655   4576   2311       O  
ATOM   3851  CB  THR B  92      17.984  18.532 -21.149  1.00 98.60           C  
ANISOU 3851  CB  THR B  92    14733  12490  10239  -2034   5066   2088       C  
ATOM   3852  OG1 THR B  92      17.069  17.701 -20.426  1.00 93.24           O  
ANISOU 3852  OG1 THR B  92    13779  12030   9618  -1739   4505   1964       O  
ATOM   3853  CG2 THR B  92      19.409  18.133 -20.794  1.00 97.59           C  
ANISOU 3853  CG2 THR B  92    14034  12609  10435  -2454   5311   1867       C  
ATOM   3854  N   GLY B  93      15.681  20.481 -22.097  1.00 95.42           N  
ANISOU 3854  N   GLY B  93    15760  11352   9142  -1353   4994   2643       N  
ATOM   3855  CA  GLY B  93      14.265  20.818 -22.254  1.00 94.67           C  
ANISOU 3855  CA  GLY B  93    16071  11153   8745   -842   4664   2801       C  
ATOM   3856  C   GLY B  93      13.339  19.649 -21.953  1.00 93.49           C  
ANISOU 3856  C   GLY B  93    15520  11423   8580   -506   4084   2637       C  
ATOM   3857  O   GLY B  93      12.518  19.276 -22.789  1.00 93.66           O  
ANISOU 3857  O   GLY B  93    15755  11599   8231    -76   3876   2723       O  
ATOM   3858  N   GLY B  94      13.470  19.065 -20.764  1.00 85.34           N  
ANISOU 3858  N   GLY B  94    13916  10578   7933   -711   3831   2389       N  
ATOM   3859  CA  GLY B  94      12.669  17.904 -20.376  1.00 80.64           C  
ANISOU 3859  CA  GLY B  94    12929  10347   7362   -469   3335   2216       C  
ATOM   3860  C   GLY B  94      13.116  16.568 -20.947  1.00 82.80           C  
ANISOU 3860  C   GLY B  94    12907  10962   7592   -458   3296   2087       C  
ATOM   3861  O   GLY B  94      12.478  15.543 -20.692  1.00 79.23           O  
ANISOU 3861  O   GLY B  94    12173  10780   7150   -289   2923   1934       O  
ATOM   3862  N   VAL B  95      14.206  16.572 -21.710  1.00 81.99           N  
ANISOU 3862  N   VAL B  95    12879  10834   7439   -646   3704   2139       N  
ATOM   3863  CA  VAL B  95      14.713  15.357 -22.339  1.00 81.25           C  
ANISOU 3863  CA  VAL B  95    12557  11039   7276   -611   3724   2023       C  
ATOM   3864  C   VAL B  95      15.489  14.545 -21.307  1.00 81.86           C  
ANISOU 3864  C   VAL B  95    12024  11316   7762   -870   3650   1778       C  
ATOM   3865  O   VAL B  95      16.218  15.105 -20.487  1.00 81.60           O  
ANISOU 3865  O   VAL B  95    11780  11189   8036  -1197   3809   1725       O  
ATOM   3866  CB  VAL B  95      15.623  15.666 -23.566  1.00 89.70           C  
ANISOU 3866  CB  VAL B  95    13932  12029   8120   -694   4228   2172       C  
ATOM   3867  CG1 VAL B  95      16.316  14.400 -24.062  1.00 89.23           C  
ANISOU 3867  CG1 VAL B  95    13574  12281   8046   -687   4284   2017       C  
ATOM   3868  CG2 VAL B  95      14.816  16.301 -24.702  1.00 92.52           C  
ANISOU 3868  CG2 VAL B  95    14941  12226   7987   -343   4273   2425       C  
ATOM   3869  N   TRP B  96      15.316  13.226 -21.365  1.00 75.95           N  
ANISOU 3869  N   TRP B  96    11022  10843   6994   -708   3406   1620       N  
ATOM   3870  CA  TRP B  96      15.930  12.284 -20.433  1.00 73.10           C  
ANISOU 3870  CA  TRP B  96    10136  10683   6955   -840   3292   1399       C  
ATOM   3871  C   TRP B  96      16.767  11.272 -21.205  1.00 77.55           C  
ANISOU 3871  C   TRP B  96    10575  11456   7434   -793   3478   1316       C  
ATOM   3872  O   TRP B  96      16.209  10.415 -21.892  1.00 76.78           O  
ANISOU 3872  O   TRP B  96    10615  11464   7095   -540   3325   1278       O  
ATOM   3873  CB  TRP B  96      14.837  11.546 -19.666  1.00 68.07           C  
ANISOU 3873  CB  TRP B  96     9354  10137   6371   -661   2823   1280       C  
ATOM   3874  CG  TRP B  96      15.358  10.545 -18.693  1.00 66.85           C  
ANISOU 3874  CG  TRP B  96     8747  10154   6498   -736   2695   1082       C  
ATOM   3875  CD1 TRP B  96      15.699   9.247 -18.950  1.00 69.32           C  
ANISOU 3875  CD1 TRP B  96     8904  10649   6783   -622   2665    951       C  
ATOM   3876  CD2 TRP B  96      15.589  10.752 -17.296  1.00 64.91           C  
ANISOU 3876  CD2 TRP B  96     8187   9902   6573   -902   2578    993       C  
ATOM   3877  NE1 TRP B  96      16.133   8.635 -17.797  1.00 66.87           N  
ANISOU 3877  NE1 TRP B  96     8218  10438   6750   -680   2542    807       N  
ATOM   3878  CE2 TRP B  96      16.077   9.538 -16.768  1.00 67.40           C  
ANISOU 3878  CE2 TRP B  96     8169  10412   7027   -853   2477    828       C  
ATOM   3879  CE3 TRP B  96      15.434  11.847 -16.441  1.00 65.99           C  
ANISOU 3879  CE3 TRP B  96     8324   9879   6871  -1069   2553   1033       C  
ATOM   3880  CZ2 TRP B  96      16.411   9.389 -15.425  1.00 65.16           C  
ANISOU 3880  CZ2 TRP B  96     7549  10195   7015   -944   2337    713       C  
ATOM   3881  CZ3 TRP B  96      15.764  11.698 -15.107  1.00 65.81           C  
ANISOU 3881  CZ3 TRP B  96     7949   9927   7129  -1193   2412    896       C  
ATOM   3882  CH2 TRP B  96      16.248  10.476 -14.610  1.00 65.17           C  
ANISOU 3882  CH2 TRP B  96     7533  10069   7160  -1121   2298    743       C  
ATOM   3883  N   ASN B  97      18.093  11.353 -21.083  1.00 75.43           N  
ANISOU 3883  N   ASN B  97    10032  11267   7362  -1034   3803   1261       N  
ATOM   3884  CA  ASN B  97      18.989  10.476 -21.842  1.00 77.03           C  
ANISOU 3884  CA  ASN B  97    10106  11679   7483   -970   4036   1184       C  
ATOM   3885  C   ASN B  97      19.669   9.368 -21.023  1.00 78.67           C  
ANISOU 3885  C   ASN B  97     9803  12138   7949   -946   3913    963       C  
ATOM   3886  O   ASN B  97      20.639   8.763 -21.473  1.00 80.18           O  
ANISOU 3886  O   ASN B  97     9806  12522   8136   -915   4152    883       O  
ATOM   3887  CB  ASN B  97      20.024  11.327 -22.586  1.00 82.69           C  
ANISOU 3887  CB  ASN B  97    10917  12345   8157  -1210   4567   1293       C  
ATOM   3888  CG  ASN B  97      19.404  12.156 -23.704  1.00101.29           C  
ANISOU 3888  CG  ASN B  97    13886  14459  10139  -1120   4738   1537       C  
ATOM   3889  OD1 ASN B  97      19.567  13.375 -23.755  1.00 97.10           O  
ANISOU 3889  OD1 ASN B  97    13583  13689   9621  -1343   5004   1687       O  
ATOM   3890  ND2 ASN B  97      18.688  11.492 -24.606  1.00 90.58           N  
ANISOU 3890  ND2 ASN B  97    12828  13158   8430   -781   4586   1569       N  
ATOM   3891  N   PHE B  98      19.142   9.092 -19.834  1.00 72.12           N  
ANISOU 3891  N   PHE B  98     8775  11308   7319   -922   3549    871       N  
ATOM   3892  CA  PHE B  98      19.591   7.957 -19.016  1.00 70.52           C  
ANISOU 3892  CA  PHE B  98     8181  11309   7304   -814   3380    686       C  
ATOM   3893  C   PHE B  98      18.675   6.747 -19.179  1.00 72.52           C  
ANISOU 3893  C   PHE B  98     8607  11552   7396   -523   3094    625       C  
ATOM   3894  O   PHE B  98      17.604   6.831 -19.790  1.00 71.44           O  
ANISOU 3894  O   PHE B  98     8825  11290   7028   -431   2966    697       O  
ATOM   3895  CB  PHE B  98      19.644   8.344 -17.539  1.00 70.37           C  
ANISOU 3895  CB  PHE B  98     7853  11298   7587   -967   3178    614       C  
ATOM   3896  CG  PHE B  98      20.638   9.410 -17.239  1.00 74.39           C  
ANISOU 3896  CG  PHE B  98     8125  11849   8292  -1298   3441    603       C  
ATOM   3897  CD1 PHE B  98      21.973   9.085 -17.037  1.00 80.02           C  
ANISOU 3897  CD1 PHE B  98     8387  12849   9168  -1370   3627    458       C  
ATOM   3898  CD2 PHE B  98      20.248  10.740 -17.169  1.00 76.87           C  
ANISOU 3898  CD2 PHE B  98     8666  11919   8623  -1537   3516    719       C  
ATOM   3899  CE1 PHE B  98      22.905  10.069 -16.764  1.00 83.91           C  
ANISOU 3899  CE1 PHE B  98     8615  13414   9852  -1733   3880    403       C  
ATOM   3900  CE2 PHE B  98      21.172  11.731 -16.898  1.00 82.63           C  
ANISOU 3900  CE2 PHE B  98     9204  12653   9540  -1902   3790    680       C  
ATOM   3901  CZ  PHE B  98      22.505  11.396 -16.693  1.00 83.32           C  
ANISOU 3901  CZ  PHE B  98     8797  13056   9804  -2030   3972    509       C  
ATOM   3902  N   SER B  99      19.100   5.625 -18.609  1.00 68.65           N  
ANISOU 3902  N   SER B  99     7867  11197   7019   -378   2996    479       N  
ATOM   3903  CA  SER B  99      18.353   4.381 -18.709  1.00 67.24           C  
ANISOU 3903  CA  SER B  99     7861  10976   6710   -144   2777    393       C  
ATOM   3904  C   SER B  99      16.905   4.542 -18.269  1.00 68.27           C  
ANISOU 3904  C   SER B  99     8183  10947   6810   -169   2450    419       C  
ATOM   3905  O   SER B  99      16.589   5.374 -17.424  1.00 66.64           O  
ANISOU 3905  O   SER B  99     7878  10682   6761   -312   2331    474       O  
ATOM   3906  CB  SER B  99      19.018   3.298 -17.858  1.00 71.34           C  
ANISOU 3906  CB  SER B  99     8102  11610   7393     15   2714    256       C  
ATOM   3907  OG  SER B  99      18.310   2.070 -17.957  1.00 81.10           O  
ANISOU 3907  OG  SER B  99     9565  12744   8503    211   2549    169       O  
ATOM   3908  N   ARG B 100      16.034   3.725 -18.849  1.00 64.01           N  
ANISOU 3908  N   ARG B 100     7902  10354   6064    -34   2313    355       N  
ATOM   3909  CA  ARG B 100      14.624   3.692 -18.470  1.00 61.40           C  
ANISOU 3909  CA  ARG B 100     7701   9930   5698    -54   2003    333       C  
ATOM   3910  C   ARG B 100      14.446   3.238 -17.031  1.00 62.84           C  
ANISOU 3910  C   ARG B 100     7674  10075   6129    -82   1814    266       C  
ATOM   3911  O   ARG B 100      13.534   3.690 -16.335  1.00 60.39           O  
ANISOU 3911  O   ARG B 100     7349   9707   5890   -163   1609    290       O  
ATOM   3912  CB  ARG B 100      13.852   2.767 -19.409  1.00 62.18           C  
ANISOU 3912  CB  ARG B 100     8075  10023   5530     61   1914    218       C  
ATOM   3913  CG  ARG B 100      13.666   3.340 -20.821  1.00 74.87           C  
ANISOU 3913  CG  ARG B 100     9952  11674   6820    116   2022    294       C  
ATOM   3914  CD  ARG B 100      12.868   4.656 -20.810  1.00 81.35           C  
ANISOU 3914  CD  ARG B 100    10856  12468   7585     63   1907    445       C  
ATOM   3915  NE  ARG B 100      11.648   4.547 -20.001  1.00 82.91           N  
ANISOU 3915  NE  ARG B 100    10983  12651   7868     29   1579    373       N  
ATOM   3916  CZ  ARG B 100      10.892   5.571 -19.606  1.00 91.92           C  
ANISOU 3916  CZ  ARG B 100    12124  13768   9034      6   1437    476       C  
ATOM   3917  NH1 ARG B 100      11.201   6.824 -19.938  1.00 75.32           N  
ANISOU 3917  NH1 ARG B 100    10141  11606   6872     10   1592    668       N  
ATOM   3918  NH2 ARG B 100       9.810   5.334 -18.869  1.00 77.29           N  
ANISOU 3918  NH2 ARG B 100    10169  11936   7260    -20   1162    383       N  
ATOM   3919  N   ILE B 101      15.338   2.351 -16.595  1.00 60.02           N  
ANISOU 3919  N   ILE B 101     7167   9758   5878     20   1896    187       N  
ATOM   3920  CA  ILE B 101      15.359   1.854 -15.222  1.00 58.26           C  
ANISOU 3920  CA  ILE B 101     6774   9506   5855     47   1749    139       C  
ATOM   3921  C   ILE B 101      15.617   3.013 -14.274  1.00 61.70           C  
ANISOU 3921  C   ILE B 101     6963   9990   6490    -99   1704    219       C  
ATOM   3922  O   ILE B 101      14.911   3.163 -13.286  1.00 59.17           O  
ANISOU 3922  O   ILE B 101     6611   9601   6268   -156   1508    222       O  
ATOM   3923  CB  ILE B 101      16.447   0.777 -15.021  1.00 62.82           C  
ANISOU 3923  CB  ILE B 101     7249  10146   6473    260   1872     60       C  
ATOM   3924  CG1 ILE B 101      16.047  -0.542 -15.703  1.00 64.35           C  
ANISOU 3924  CG1 ILE B 101     7751  10216   6485    407   1892    -49       C  
ATOM   3925  CG2 ILE B 101      16.685   0.535 -13.548  1.00 62.46           C  
ANISOU 3925  CG2 ILE B 101     7004  10112   6616    320   1738     47       C  
ATOM   3926  CD1 ILE B 101      16.109  -0.536 -17.252  1.00 75.61           C  
ANISOU 3926  CD1 ILE B 101     9379  11674   7673    427   2058    -70       C  
ATOM   3927  N   CYS B 102      16.617   3.835 -14.593  1.00 60.59           N  
ANISOU 3927  N   CYS B 102     6657   9962   6401   -181   1905    269       N  
ATOM   3928  CA  CYS B 102      16.933   5.018 -13.788  1.00 60.31           C  
ANISOU 3928  CA  CYS B 102     6408   9957   6550   -372   1895    315       C  
ATOM   3929  C   CYS B 102      15.749   5.981 -13.691  1.00 61.56           C  
ANISOU 3929  C   CYS B 102     6760   9954   6675   -501   1758    405       C  
ATOM   3930  O   CYS B 102      15.515   6.578 -12.643  1.00 59.55           O  
ANISOU 3930  O   CYS B 102     6397   9663   6567   -600   1628    408       O  
ATOM   3931  CB  CYS B 102      18.161   5.752 -14.336  1.00 63.81           C  
ANISOU 3931  CB  CYS B 102     6676  10530   7039   -501   2191    334       C  
ATOM   3932  SG  CYS B 102      18.794   7.077 -13.232  1.00 68.63           S  
ANISOU 3932  SG  CYS B 102     6972  11198   7908   -789   2204    315       S  
ATOM   3933  N   CYS B 103      14.996   6.126 -14.776  1.00 58.26           N  
ANISOU 3933  N   CYS B 103     6633   9458   6044   -468   1779    470       N  
ATOM   3934  CA  CYS B 103      13.794   6.949 -14.743  1.00 56.92           C  
ANISOU 3934  CA  CYS B 103     6649   9172   5807   -507   1627    549       C  
ATOM   3935  C   CYS B 103      12.799   6.401 -13.721  1.00 57.60           C  
ANISOU 3935  C   CYS B 103     6684   9233   5970   -468   1348    474       C  
ATOM   3936  O   CYS B 103      12.248   7.154 -12.922  1.00 55.86           O  
ANISOU 3936  O   CYS B 103     6430   8952   5842   -534   1228    510       O  
ATOM   3937  CB  CYS B 103      13.154   7.053 -16.127  1.00 58.62           C  
ANISOU 3937  CB  CYS B 103     7174   9368   5732   -411   1664    611       C  
ATOM   3938  SG  CYS B 103      11.463   7.730 -16.127  1.00 61.73           S  
ANISOU 3938  SG  CYS B 103     7766   9701   5989   -343   1400    668       S  
ATOM   3939  N   ASP B 104      12.590   5.091 -13.720  1.00 53.14           N  
ANISOU 3939  N   ASP B 104     6132   8695   5363   -370   1275    367       N  
ATOM   3940  CA  ASP B 104      11.660   4.484 -12.765  1.00 50.71           C  
ANISOU 3940  CA  ASP B 104     5800   8343   5122   -366   1063    293       C  
ATOM   3941  C   ASP B 104      12.102   4.727 -11.328  1.00 51.97           C  
ANISOU 3941  C   ASP B 104     5750   8498   5498   -408   1013    299       C  
ATOM   3942  O   ASP B 104      11.311   5.123 -10.480  1.00 50.01           O  
ANISOU 3942  O   ASP B 104     5477   8208   5317   -459    868    307       O  
ATOM   3943  CB  ASP B 104      11.529   2.985 -13.011  1.00 53.14           C  
ANISOU 3943  CB  ASP B 104     6208   8629   5354   -282   1057    171       C  
ATOM   3944  CG  ASP B 104      11.149   2.660 -14.443  1.00 67.04           C  
ANISOU 3944  CG  ASP B 104     8179  10416   6878   -244   1096    124       C  
ATOM   3945  OD1 ASP B 104      10.034   3.043 -14.876  1.00 68.17           O  
ANISOU 3945  OD1 ASP B 104     8416  10591   6896   -279    960    113       O  
ATOM   3946  OD2 ASP B 104      11.976   2.018 -15.134  1.00 74.59           O  
ANISOU 3946  OD2 ASP B 104     9201  11385   7755   -153   1258     87       O  
ATOM   3947  N   VAL B 105      13.377   4.487 -11.061  1.00 48.50           N  
ANISOU 3947  N   VAL B 105     5145   8131   5150   -368   1130    281       N  
ATOM   3948  CA  VAL B 105      13.931   4.718  -9.733  1.00 47.08           C  
ANISOU 3948  CA  VAL B 105     4743   8000   5143   -384   1066    262       C  
ATOM   3949  C   VAL B 105      13.780   6.187  -9.364  1.00 50.72           C  
ANISOU 3949  C   VAL B 105     5148   8435   5690   -558   1045    317       C  
ATOM   3950  O   VAL B 105      13.404   6.517  -8.245  1.00 49.63           O  
ANISOU 3950  O   VAL B 105     4947   8268   5641   -594    907    304       O  
ATOM   3951  CB  VAL B 105      15.413   4.313  -9.652  1.00 52.11           C  
ANISOU 3951  CB  VAL B 105     5158   8798   5844   -290   1192    211       C  
ATOM   3952  CG1 VAL B 105      16.050   4.871  -8.395  1.00 51.87           C  
ANISOU 3952  CG1 VAL B 105     4856   8880   5972   -339   1112    172       C  
ATOM   3953  CG2 VAL B 105      15.545   2.798  -9.708  1.00 52.28           C  
ANISOU 3953  CG2 VAL B 105     5272   8805   5787    -57   1197    156       C  
ATOM   3954  N   PHE B 106      14.054   7.073 -10.307  1.00 48.42           N  
ANISOU 3954  N   PHE B 106     4920   8125   5352   -659   1201    383       N  
ATOM   3955  CA  PHE B 106      13.856   8.487 -10.045  1.00 48.41           C  
ANISOU 3955  CA  PHE B 106     4954   8030   5410   -820   1216    443       C  
ATOM   3956  C   PHE B 106      12.400   8.744  -9.676  1.00 48.99           C  
ANISOU 3956  C   PHE B 106     5192   7993   5430   -769   1023    479       C  
ATOM   3957  O   PHE B 106      12.112   9.317  -8.631  1.00 47.45           O  
ANISOU 3957  O   PHE B 106     4941   7750   5336   -824    920    463       O  
ATOM   3958  CB  PHE B 106      14.274   9.324 -11.254  1.00 52.83           C  
ANISOU 3958  CB  PHE B 106     5656   8533   5882   -915   1457    535       C  
ATOM   3959  CG  PHE B 106      13.754  10.727 -11.229  1.00 55.35           C  
ANISOU 3959  CG  PHE B 106     6167   8671   6193  -1025   1486    631       C  
ATOM   3960  CD1 PHE B 106      14.228  11.641 -10.303  1.00 59.21           C  
ANISOU 3960  CD1 PHE B 106     6539   9101   6855  -1218   1515    589       C  
ATOM   3961  CD2 PHE B 106      12.785  11.134 -12.139  1.00 58.23           C  
ANISOU 3961  CD2 PHE B 106     6849   8924   6353   -912   1480    751       C  
ATOM   3962  CE1 PHE B 106      13.739  12.945 -10.281  1.00 61.06           C  
ANISOU 3962  CE1 PHE B 106     7015   9114   7073  -1305   1567    675       C  
ATOM   3963  CE2 PHE B 106      12.293  12.431 -12.126  1.00 61.98           C  
ANISOU 3963  CE2 PHE B 106     7550   9207   6793   -947   1517    856       C  
ATOM   3964  CZ  PHE B 106      12.772  13.341 -11.197  1.00 60.55           C  
ANISOU 3964  CZ  PHE B 106     7295   8913   6798  -1148   1576    823       C  
ATOM   3965  N   VAL B 107      11.482   8.282 -10.517  1.00 44.65           N  
ANISOU 3965  N   VAL B 107     4821   7433   4710   -659    970    505       N  
ATOM   3966  CA  VAL B 107      10.072   8.602 -10.341  1.00 43.16           C  
ANISOU 3966  CA  VAL B 107     4746   7200   4451   -601    799    525       C  
ATOM   3967  C   VAL B 107       9.421   7.894  -9.158  1.00 45.84           C  
ANISOU 3967  C   VAL B 107     4970   7565   4882   -586    628    438       C  
ATOM   3968  O   VAL B 107       8.495   8.454  -8.565  1.00 45.04           O  
ANISOU 3968  O   VAL B 107     4881   7436   4796   -575    513    448       O  
ATOM   3969  CB  VAL B 107       9.280   8.328 -11.610  1.00 47.49           C  
ANISOU 3969  CB  VAL B 107     5477   7793   4773   -490    769    542       C  
ATOM   3970  CG1 VAL B 107       7.786   8.355 -11.333  1.00 46.58           C  
ANISOU 3970  CG1 VAL B 107     5380   7722   4595   -415    559    506       C  
ATOM   3971  CG2 VAL B 107       9.649   9.350 -12.643  1.00 49.19           C  
ANISOU 3971  CG2 VAL B 107     5884   7946   4861   -474    932    671       C  
ATOM   3972  N   THR B 108       9.886   6.694  -8.802  1.00 41.81           N  
ANISOU 3972  N   THR B 108     4374   7095   4417   -565    632    361       N  
ATOM   3973  CA  THR B 108       9.306   5.989  -7.646  1.00 40.08           C  
ANISOU 3973  CA  THR B 108     4102   6863   4263   -553    514    298       C  
ATOM   3974  C   THR B 108       9.819   6.585  -6.337  1.00 42.42           C  
ANISOU 3974  C   THR B 108     4266   7153   4698   -584    480    305       C  
ATOM   3975  O   THR B 108       9.165   6.465  -5.307  1.00 41.25           O  
ANISOU 3975  O   THR B 108     4104   6983   4585   -578    383    282       O  
ATOM   3976  CB  THR B 108       9.534   4.445  -7.660  1.00 48.65           C  
ANISOU 3976  CB  THR B 108     5228   7938   5319   -492    546    225       C  
ATOM   3977  OG1 THR B 108      10.848   4.133  -7.194  1.00 49.64           O  
ANISOU 3977  OG1 THR B 108     5248   8096   5518   -418    617    225       O  
ATOM   3978  CG2 THR B 108       9.350   3.872  -9.052  1.00 47.99           C  
ANISOU 3978  CG2 THR B 108     5279   7865   5089   -474    606    188       C  
ATOM   3979  N   LEU B 109      10.978   7.236  -6.379  1.00 39.39           N  
ANISOU 3979  N   LEU B 109     3781   6801   4384   -633    567    319       N  
ATOM   3980  CA  LEU B 109      11.495   7.928  -5.199  1.00 39.21           C  
ANISOU 3980  CA  LEU B 109     3621   6798   4481   -694    521    287       C  
ATOM   3981  C   LEU B 109      10.707   9.212  -4.955  1.00 42.36           C  
ANISOU 3981  C   LEU B 109     4114   7089   4892   -773    482    325       C  
ATOM   3982  O   LEU B 109      10.383   9.537  -3.821  1.00 41.07           O  
ANISOU 3982  O   LEU B 109     3919   6906   4778   -779    384    289       O  
ATOM   3983  CB  LEU B 109      13.001   8.229  -5.325  1.00 40.93           C  
ANISOU 3983  CB  LEU B 109     3652   7122   4778   -766    633    245       C  
ATOM   3984  CG  LEU B 109      13.990   7.232  -4.692  1.00 46.08           C  
ANISOU 3984  CG  LEU B 109     4107   7939   5461   -638    600    165       C  
ATOM   3985  CD1 LEU B 109      13.667   5.785  -5.021  1.00 45.55           C  
ANISOU 3985  CD1 LEU B 109     4162   7850   5295   -447    598    184       C  
ATOM   3986  CD2 LEU B 109      15.401   7.545  -5.122  1.00 50.69           C  
ANISOU 3986  CD2 LEU B 109     4461   8687   6114   -714    736    107       C  
ATOM   3987  N   ASP B 110      10.384   9.928  -6.022  1.00 39.54           N  
ANISOU 3987  N   ASP B 110     3905   6656   4464   -798    564    402       N  
ATOM   3988  CA  ASP B 110       9.637  11.174  -5.905  1.00 39.60           C  
ANISOU 3988  CA  ASP B 110     4057   6536   4455   -812    547    456       C  
ATOM   3989  C   ASP B 110       8.244  10.939  -5.315  1.00 42.31           C  
ANISOU 3989  C   ASP B 110     4427   6896   4754   -693    387    442       C  
ATOM   3990  O   ASP B 110       7.765  11.708  -4.466  1.00 41.35           O  
ANISOU 3990  O   ASP B 110     4333   6707   4669   -685    333    432       O  
ATOM   3991  CB  ASP B 110       9.523  11.829  -7.279  1.00 42.80           C  
ANISOU 3991  CB  ASP B 110     4668   6858   4736   -791    672    565       C  
ATOM   3992  CG  ASP B 110       9.055  13.265  -7.207  1.00 53.98           C  
ANISOU 3992  CG  ASP B 110     6289   8091   6128   -786    708    638       C  
ATOM   3993  OD1 ASP B 110       9.606  14.047  -6.405  1.00 54.87           O  
ANISOU 3993  OD1 ASP B 110     6384   8098   6366   -931    760    595       O  
ATOM   3994  OD2 ASP B 110       8.140  13.619  -7.977  1.00 61.24           O  
ANISOU 3994  OD2 ASP B 110     7405   8976   6889   -620    684    730       O  
ATOM   3995  N   VAL B 111       7.602   9.867  -5.771  1.00 38.75           N  
ANISOU 3995  N   VAL B 111     3964   6539   4222   -617    331    422       N  
ATOM   3996  CA  VAL B 111       6.289   9.492  -5.266  1.00 37.95           C  
ANISOU 3996  CA  VAL B 111     3838   6494   4087   -552    210    380       C  
ATOM   3997  C   VAL B 111       6.417   8.984  -3.841  1.00 42.22           C  
ANISOU 3997  C   VAL B 111     4280   7036   4725   -587    171    320       C  
ATOM   3998  O   VAL B 111       5.574   9.285  -2.982  1.00 41.77           O  
ANISOU 3998  O   VAL B 111     4207   6983   4681   -559    109    299       O  
ATOM   3999  CB  VAL B 111       5.619   8.420  -6.133  1.00 41.60           C  
ANISOU 3999  CB  VAL B 111     4305   7059   4442   -525    177    333       C  
ATOM   4000  CG1 VAL B 111       4.316   7.963  -5.502  1.00 41.07           C  
ANISOU 4000  CG1 VAL B 111     4160   7074   4369   -523     83    254       C  
ATOM   4001  CG2 VAL B 111       5.375   8.955  -7.521  1.00 42.60           C  
ANISOU 4001  CG2 VAL B 111     4548   7218   4420   -445    186    388       C  
ATOM   4002  N   MET B 112       7.478   8.224  -3.585  1.00 39.02           N  
ANISOU 4002  N   MET B 112     3819   6641   4368   -615    213    296       N  
ATOM   4003  CA  MET B 112       7.738   7.744  -2.238  1.00 38.44           C  
ANISOU 4003  CA  MET B 112     3687   6575   4345   -597    173    254       C  
ATOM   4004  C   MET B 112       7.883   8.922  -1.259  1.00 42.94           C  
ANISOU 4004  C   MET B 112     4226   7117   4973   -625    127    240       C  
ATOM   4005  O   MET B 112       7.183   8.967  -0.258  1.00 43.01           O  
ANISOU 4005  O   MET B 112     4251   7119   4973   -592     72    218       O  
ATOM   4006  CB  MET B 112       8.963   6.831  -2.215  1.00 41.21           C  
ANISOU 4006  CB  MET B 112     3982   6967   4707   -553    215    236       C  
ATOM   4007  CG  MET B 112       9.294   6.248  -0.857  1.00 45.07           C  
ANISOU 4007  CG  MET B 112     4446   7478   5198   -467    162    207       C  
ATOM   4008  SD  MET B 112      10.479   4.884  -0.994  1.00 50.59           S  
ANISOU 4008  SD  MET B 112     5133   8230   5860   -310    212    199       S  
ATOM   4009  CE  MET B 112      10.794   4.507   0.743  1.00 47.85           C  
ANISOU 4009  CE  MET B 112     4790   7925   5467   -150    117    185       C  
ATOM   4010  N   MET B 113       8.739   9.896  -1.547  1.00 40.00           N  
ANISOU 4010  N   MET B 113     3829   6716   4653   -704    169    239       N  
ATOM   4011  CA  MET B 113       8.949  10.976  -0.580  1.00 40.40           C  
ANISOU 4011  CA  MET B 113     3873   6719   4759   -765    134    186       C  
ATOM   4012  C   MET B 113       7.720  11.835  -0.385  1.00 44.54           C  
ANISOU 4012  C   MET B 113     4533   7141   5249   -717    111    215       C  
ATOM   4013  O   MET B 113       7.510  12.325   0.714  1.00 43.99           O  
ANISOU 4013  O   MET B 113     4479   7043   5191   -710     58    159       O  
ATOM   4014  CB  MET B 113      10.126  11.879  -0.955  1.00 44.32           C  
ANISOU 4014  CB  MET B 113     4323   7184   5331   -924    221    151       C  
ATOM   4015  CG  MET B 113      11.440  11.160  -1.200  1.00 48.81           C  
ANISOU 4015  CG  MET B 113     4699   7907   5940   -959    258    103       C  
ATOM   4016  SD  MET B 113      11.581   9.610  -0.297  1.00 52.37           S  
ANISOU 4016  SD  MET B 113     5042   8517   6339   -763    136     69       S  
ATOM   4017  CE  MET B 113      12.428  10.204   1.157  1.00 50.59           C  
ANISOU 4017  CE  MET B 113     4654   8412   6157   -811     17    -80       C  
ATOM   4018  N   CYS B 114       6.917  12.044  -1.429  1.00 41.77           N  
ANISOU 4018  N   CYS B 114     4281   6755   4835   -655    143    293       N  
ATOM   4019  CA  CYS B 114       5.684  12.816  -1.246  1.00 41.65           C  
ANISOU 4019  CA  CYS B 114     4369   6689   4768   -541    108    316       C  
ATOM   4020  C   CYS B 114       4.687  12.017  -0.435  1.00 43.81           C  
ANISOU 4020  C   CYS B 114     4550   7080   5017   -469     35    271       C  
ATOM   4021  O   CYS B 114       4.051  12.554   0.459  1.00 43.84           O  
ANISOU 4021  O   CYS B 114     4577   7064   5015   -405      8    240       O  
ATOM   4022  CB  CYS B 114       5.033  13.245  -2.559  1.00 42.81           C  
ANISOU 4022  CB  CYS B 114     4633   6818   4814   -433    133    405       C  
ATOM   4023  SG  CYS B 114       3.358  14.024  -2.274  1.00 47.54           S  
ANISOU 4023  SG  CYS B 114     5296   7443   5322   -196     59    416       S  
ATOM   4024  N   THR B 115       4.548  10.738  -0.750  1.00 38.83           N  
ANISOU 4024  N   THR B 115     3836   6552   4365   -489     30    260       N  
ATOM   4025  CA  THR B 115       3.680   9.867   0.031  1.00 37.94           C  
ANISOU 4025  CA  THR B 115     3659   6521   4235   -479     13    213       C  
ATOM   4026  C   THR B 115       4.123   9.869   1.492  1.00 41.10           C  
ANISOU 4026  C   THR B 115     4069   6883   4663   -483      7    182       C  
ATOM   4027  O   THR B 115       3.330  10.129   2.397  1.00 40.39           O  
ANISOU 4027  O   THR B 115     3982   6811   4552   -436      4    154       O  
ATOM   4028  CB  THR B 115       3.697   8.421  -0.504  1.00 43.71           C  
ANISOU 4028  CB  THR B 115     4362   7302   4945   -543     46    195       C  
ATOM   4029  OG1 THR B 115       3.370   8.415  -1.897  1.00 44.68           O  
ANISOU 4029  OG1 THR B 115     4483   7481   5014   -537     35    202       O  
ATOM   4030  CG2 THR B 115       2.700   7.567   0.231  1.00 40.83           C  
ANISOU 4030  CG2 THR B 115     3964   6988   4563   -582     79    142       C  
ATOM   4031  N   ALA B 116       5.402   9.589   1.704  1.00 37.70           N  
ANISOU 4031  N   ALA B 116     3632   6430   4262   -519      2    176       N  
ATOM   4032  CA  ALA B 116       5.983   9.537   3.041  1.00 37.72           C  
ANISOU 4032  CA  ALA B 116     3636   6442   4255   -492    -38    133       C  
ATOM   4033  C   ALA B 116       5.627  10.779   3.852  1.00 42.39           C  
ANISOU 4033  C   ALA B 116     4273   6988   4847   -478    -72     86       C  
ATOM   4034  O   ALA B 116       5.143  10.665   4.973  1.00 41.67           O  
ANISOU 4034  O   ALA B 116     4219   6916   4697   -417    -83     58       O  
ATOM   4035  CB  ALA B 116       7.518   9.366   2.960  1.00 38.89           C  
ANISOU 4035  CB  ALA B 116     3710   6632   4436   -514    -66    105       C  
ATOM   4036  N   SER B 117       5.860  11.957   3.275  1.00 39.96           N  
ANISOU 4036  N   SER B 117     3999   6596   4587   -528    -63     80       N  
ATOM   4037  CA  SER B 117       5.551  13.213   3.947  1.00 40.86           C  
ANISOU 4037  CA  SER B 117     4213   6613   4697   -512    -73     27       C  
ATOM   4038  C   SER B 117       4.102  13.242   4.440  1.00 45.22           C  
ANISOU 4038  C   SER B 117     4803   7193   5186   -374    -61     40       C  
ATOM   4039  O   SER B 117       3.855  13.467   5.625  1.00 45.91           O  
ANISOU 4039  O   SER B 117     4933   7283   5228   -325    -76    -22       O  
ATOM   4040  CB  SER B 117       5.809  14.405   3.025  1.00 45.61           C  
ANISOU 4040  CB  SER B 117     4923   7062   5345   -572    -14     51       C  
ATOM   4041  OG  SER B 117       7.189  14.726   2.955  1.00 56.79           O  
ANISOU 4041  OG  SER B 117     6301   8445   6833   -750      3    -13       O  
ATOM   4042  N   ILE B 118       3.146  12.992   3.549  1.00 41.31           N  
ANISOU 4042  N   ILE B 118     4271   6753   4674   -309    -33    102       N  
ATOM   4043  CA  ILE B 118       1.739  13.115   3.923  1.00 41.51           C  
ANISOU 4043  CA  ILE B 118     4267   6857   4646   -179    -14     90       C  
ATOM   4044  C   ILE B 118       1.339  12.130   5.015  1.00 44.18           C  
ANISOU 4044  C   ILE B 118     4543   7293   4950   -200     20     54       C  
ATOM   4045  O   ILE B 118       0.681  12.512   5.979  1.00 44.99           O  
ANISOU 4045  O   ILE B 118     4670   7416   5007   -116     52     12       O  
ATOM   4046  CB  ILE B 118       0.778  12.975   2.706  1.00 45.20           C  
ANISOU 4046  CB  ILE B 118     4650   7439   5087   -102    -19    130       C  
ATOM   4047  CG1 ILE B 118      -0.668  13.327   3.104  1.00 46.90           C  
ANISOU 4047  CG1 ILE B 118     4784   7787   5249     63     -6     90       C  
ATOM   4048  CG2 ILE B 118       0.841  11.567   2.100  1.00 45.41           C  
ANISOU 4048  CG2 ILE B 118     4559   7573   5122   -227    -12    133       C  
ATOM   4049  CD1 ILE B 118      -0.842  14.757   3.575  1.00 56.02           C  
ANISOU 4049  CD1 ILE B 118     6098   8813   6376    240      0     87       C  
ATOM   4050  N   TRP B 119       1.729  10.872   4.883  1.00 39.06           N  
ANISOU 4050  N   TRP B 119     3851   6684   4307   -298     39     74       N  
ATOM   4051  CA  TRP B 119       1.345   9.895   5.896  1.00 39.02           C  
ANISOU 4051  CA  TRP B 119     3857   6723   4246   -317    114     63       C  
ATOM   4052  C   TRP B 119       2.039  10.169   7.240  1.00 43.35           C  
ANISOU 4052  C   TRP B 119     4520   7220   4730   -260     84     39       C  
ATOM   4053  O   TRP B 119       1.507   9.822   8.290  1.00 43.63           O  
ANISOU 4053  O   TRP B 119     4613   7282   4682   -220    159     30       O  
ATOM   4054  CB  TRP B 119       1.605   8.470   5.412  1.00 37.52           C  
ANISOU 4054  CB  TRP B 119     3665   6532   4060   -417    166     96       C  
ATOM   4055  CG  TRP B 119       0.565   7.970   4.450  1.00 38.97           C  
ANISOU 4055  CG  TRP B 119     3733   6806   4269   -503    218     71       C  
ATOM   4056  CD1 TRP B 119       0.673   7.901   3.097  1.00 41.65           C  
ANISOU 4056  CD1 TRP B 119     4012   7174   4638   -540    167     71       C  
ATOM   4057  CD2 TRP B 119      -0.746   7.464   4.776  1.00 40.11           C  
ANISOU 4057  CD2 TRP B 119     3790   7055   4395   -577    332     16       C  
ATOM   4058  NE1 TRP B 119      -0.484   7.385   2.552  1.00 42.14           N  
ANISOU 4058  NE1 TRP B 119     3949   7369   4695   -624    210      4       N  
ATOM   4059  CE2 TRP B 119      -1.369   7.106   3.562  1.00 44.62           C  
ANISOU 4059  CE2 TRP B 119     4221   7739   4994   -668    317    -39       C  
ATOM   4060  CE3 TRP B 119      -1.452   7.281   5.976  1.00 42.31           C  
ANISOU 4060  CE3 TRP B 119     4088   7361   4629   -586    457     -4       C  
ATOM   4061  CZ2 TRP B 119      -2.670   6.581   3.512  1.00 45.43           C  
ANISOU 4061  CZ2 TRP B 119     4158   8006   5099   -794    411   -140       C  
ATOM   4062  CZ3 TRP B 119      -2.749   6.758   5.924  1.00 45.20           C  
ANISOU 4062  CZ3 TRP B 119     4301   7869   5004   -717    588    -83       C  
ATOM   4063  CH2 TRP B 119      -3.340   6.416   4.702  1.00 46.40           C  
ANISOU 4063  CH2 TRP B 119     4272   8156   5202   -832    557   -163       C  
ATOM   4064  N   ASN B 120       3.210  10.805   7.201  1.00 39.78           N  
ANISOU 4064  N   ASN B 120     4096   6712   4305   -266    -16     12       N  
ATOM   4065  CA  ASN B 120       3.884  11.256   8.415  1.00 40.07           C  
ANISOU 4065  CA  ASN B 120     4212   6741   4271   -219    -84    -60       C  
ATOM   4066  C   ASN B 120       3.058  12.287   9.125  1.00 45.07           C  
ANISOU 4066  C   ASN B 120     4921   7341   4862   -148    -59   -119       C  
ATOM   4067  O   ASN B 120       2.919  12.245  10.345  1.00 45.67           O  
ANISOU 4067  O   ASN B 120     5085   7446   4823    -74    -51   -162       O  
ATOM   4068  CB  ASN B 120       5.257  11.866   8.110  1.00 39.48           C  
ANISOU 4068  CB  ASN B 120     4097   6644   4258   -297   -190   -123       C  
ATOM   4069  CG  ASN B 120       6.392  10.990   8.571  1.00 59.43           C  
ANISOU 4069  CG  ASN B 120     6579   9272   6727   -265   -268   -140       C  
ATOM   4070  OD1 ASN B 120       6.357  10.470   9.678  1.00 54.45           O  
ANISOU 4070  OD1 ASN B 120     6028   8700   5962   -150   -290   -147       O  
ATOM   4071  ND2 ASN B 120       7.412  10.824   7.731  1.00 51.77           N  
ANISOU 4071  ND2 ASN B 120     5491   8340   5840   -336   -303   -143       N  
ATOM   4072  N   LEU B 121       2.518  13.223   8.351  1.00 41.74           N  
ANISOU 4072  N   LEU B 121     4492   6856   4511   -138    -39   -117       N  
ATOM   4073  CA  LEU B 121       1.613  14.236   8.896  1.00 42.76           C  
ANISOU 4073  CA  LEU B 121     4707   6945   4597    -16      4   -168       C  
ATOM   4074  C   LEU B 121       0.367  13.554   9.445  1.00 46.72           C  
ANISOU 4074  C   LEU B 121     5141   7581   5028     68    111   -147       C  
ATOM   4075  O   LEU B 121      -0.223  14.034  10.409  1.00 47.56           O  
ANISOU 4075  O   LEU B 121     5320   7699   5052    178    165   -203       O  
ATOM   4076  CB  LEU B 121       1.248  15.300   7.846  1.00 43.26           C  
ANISOU 4076  CB  LEU B 121     4808   6906   4722     41     14   -143       C  
ATOM   4077  CG  LEU B 121       2.437  16.066   7.227  1.00 48.23           C  
ANISOU 4077  CG  LEU B 121     5538   7361   5424    -85    -29   -159       C  
ATOM   4078  CD1 LEU B 121       2.013  16.878   5.995  1.00 48.94           C  
ANISOU 4078  CD1 LEU B 121     5711   7339   5544     -5     14    -82       C  
ATOM   4079  CD2 LEU B 121       3.135  16.954   8.261  1.00 52.07           C  
ANISOU 4079  CD2 LEU B 121     6177   7720   5886   -144    -60   -298       C  
ATOM   4080  N   CYS B 122      -0.004  12.420   8.851  1.00 42.38           N  
ANISOU 4080  N   CYS B 122     4461   7131   4509     -7    162    -82       N  
ATOM   4081  CA  CYS B 122      -1.086  11.600   9.396  1.00 43.12           C  
ANISOU 4081  CA  CYS B 122     4485   7351   4550    -10    304    -78       C  
ATOM   4082  C   CYS B 122      -0.707  10.882  10.682  1.00 47.06           C  
ANISOU 4082  C   CYS B 122     5126   7824   4929    -18    366    -69       C  
ATOM   4083  O   CYS B 122      -1.525  10.789  11.596  1.00 48.06           O  
ANISOU 4083  O   CYS B 122     5283   8012   4967     31    500    -88       O  
ATOM   4084  CB  CYS B 122      -1.604  10.573   8.390  1.00 43.22           C  
ANISOU 4084  CB  CYS B 122     4337   7457   4627   -137    358    -46       C  
ATOM   4085  SG  CYS B 122      -3.271  10.002   8.849  1.00 49.04           S  
ANISOU 4085  SG  CYS B 122     4907   8391   5334   -179    560    -99       S  
ATOM   4086  N   ALA B 123       0.510  10.353  10.750  1.00 42.20           N  
ANISOU 4086  N   ALA B 123     4602   7140   4292    -55    279    -36       N  
ATOM   4087  CA  ALA B 123       1.008   9.796  12.003  1.00 42.68           C  
ANISOU 4087  CA  ALA B 123     4836   7188   4193     13    297    -23       C  
ATOM   4088  C   ALA B 123       0.901  10.858  13.088  1.00 48.23           C  
ANISOU 4088  C   ALA B 123     5637   7899   4790    132    264   -113       C  
ATOM   4089  O   ALA B 123       0.323  10.619  14.151  1.00 48.78           O  
ANISOU 4089  O   ALA B 123     5822   7999   4712    207    386   -110       O  
ATOM   4090  CB  ALA B 123       2.440   9.351  11.857  1.00 42.88           C  
ANISOU 4090  CB  ALA B 123     4900   7187   4204     23    155     -3       C  
ATOM   4091  N   ILE B 124       1.445  12.038  12.783  1.00 45.37           N  
ANISOU 4091  N   ILE B 124     5254   7488   4497    134    122   -200       N  
ATOM   4092  CA  ILE B 124       1.509  13.166  13.722  1.00 46.62           C  
ANISOU 4092  CA  ILE B 124     5538   7611   4562    223     73   -324       C  
ATOM   4093  C   ILE B 124       0.134  13.583  14.221  1.00 51.15           C  
ANISOU 4093  C   ILE B 124     6143   8212   5081    335    233   -340       C  
ATOM   4094  O   ILE B 124      -0.043  13.812  15.409  1.00 52.48           O  
ANISOU 4094  O   ILE B 124     6457   8398   5084    440    273   -403       O  
ATOM   4095  CB  ILE B 124       2.238  14.381  13.097  1.00 49.85           C  
ANISOU 4095  CB  ILE B 124     5943   7908   5088    150    -54   -419       C  
ATOM   4096  CG1 ILE B 124       3.750  14.123  13.075  1.00 50.39           C  
ANISOU 4096  CG1 ILE B 124     5973   8007   5165     48   -216   -470       C  
ATOM   4097  CG2 ILE B 124       1.944  15.650  13.874  1.00 52.18           C  
ANISOU 4097  CG2 ILE B 124     6401   8114   5311    233    -50   -555       C  
ATOM   4098  CD1 ILE B 124       4.550  15.108  12.230  1.00 57.72           C  
ANISOU 4098  CD1 ILE B 124     6862   8826   6244   -107   -289   -548       C  
ATOM   4099  N   SER B 125      -0.840  13.669  13.325  1.00 46.84           N  
ANISOU 4099  N   SER B 125     5446   7701   4652    334    323   -294       N  
ATOM   4100  CA  SER B 125      -2.209  13.944  13.745  1.00 47.88           C  
ANISOU 4100  CA  SER B 125     5532   7927   4735    458    487   -317       C  
ATOM   4101  C   SER B 125      -2.656  12.922  14.789  1.00 52.31           C  
ANISOU 4101  C   SER B 125     6138   8581   5154    444    658   -282       C  
ATOM   4102  O   SER B 125      -2.965  13.287  15.920  1.00 53.40           O  
ANISOU 4102  O   SER B 125     6414   8735   5139    566    740   -338       O  
ATOM   4103  CB  SER B 125      -3.158  13.933  12.548  1.00 50.96           C  
ANISOU 4103  CB  SER B 125     5684   8419   5257    459    533   -281       C  
ATOM   4104  OG  SER B 125      -3.332  12.627  12.028  1.00 58.10           O  
ANISOU 4104  OG  SER B 125     6441   9419   6215    288    596   -211       O  
ATOM   4105  N   ILE B 126      -2.653  11.644  14.409  1.00 48.08           N  
ANISOU 4105  N   ILE B 126     5532   8082   4655    295    730   -189       N  
ATOM   4106  CA  ILE B 126      -3.034  10.539  15.301  1.00 49.10           C  
ANISOU 4106  CA  ILE B 126     5765   8244   4647    249    939   -129       C  
ATOM   4107  C   ILE B 126      -2.408  10.651  16.678  1.00 54.85           C  
ANISOU 4107  C   ILE B 126     6776   8919   5145    388    917   -139       C  
ATOM   4108  O   ILE B 126      -3.052  10.359  17.692  1.00 56.46           O  
ANISOU 4108  O   ILE B 126     7102   9165   5185    441   1124   -124       O  
ATOM   4109  CB  ILE B 126      -2.602   9.174  14.725  1.00 51.17           C  
ANISOU 4109  CB  ILE B 126     6040   8447   4957     81    971    -26       C  
ATOM   4110  CG1 ILE B 126      -3.609   8.691  13.677  1.00 51.38           C  
ANISOU 4110  CG1 ILE B 126     5806   8569   5147    -99   1094    -35       C  
ATOM   4111  CG2 ILE B 126      -2.470   8.146  15.835  1.00 53.25           C  
ANISOU 4111  CG2 ILE B 126     6571   8645   5016     95   1143     61       C  
ATOM   4112  CD1 ILE B 126      -3.286   7.320  13.091  1.00 58.27           C  
ANISOU 4112  CD1 ILE B 126     6727   9352   6062   -288   1159     40       C  
ATOM   4113  N   ASP B 127      -1.139  11.055  16.702  1.00 50.98           N  
ANISOU 4113  N   ASP B 127     6380   8360   4629    440    671   -176       N  
ATOM   4114  CA  ASP B 127      -0.392  11.180  17.951  1.00 52.11           C  
ANISOU 4114  CA  ASP B 127     6767   8500   4534    582    583   -221       C  
ATOM   4115  C   ASP B 127      -0.900  12.307  18.840  1.00 56.97           C  
ANISOU 4115  C   ASP B 127     7480   9135   5031    714    613   -350       C  
ATOM   4116  O   ASP B 127      -1.183  12.091  20.015  1.00 58.48           O  
ANISOU 4116  O   ASP B 127     7869   9365   4985    833    732   -349       O  
ATOM   4117  CB  ASP B 127       1.087  11.403  17.683  1.00 53.27           C  
ANISOU 4117  CB  ASP B 127     6909   8628   4704    578    296   -278       C  
ATOM   4118  CG  ASP B 127       1.900  11.286  18.934  1.00 68.03           C  
ANISOU 4118  CG  ASP B 127     8992  10558   6298    737    177   -331       C  
ATOM   4119  OD1 ASP B 127       2.042  10.141  19.418  1.00 70.05           O  
ANISOU 4119  OD1 ASP B 127     9398  10833   6385    828    253   -204       O  
ATOM   4120  OD2 ASP B 127       2.360  12.329  19.447  1.00 76.14           O  
ANISOU 4120  OD2 ASP B 127    10063  11608   7258    780     16   -505       O  
ATOM   4121  N   ARG B 128      -0.998  13.508  18.279  1.00 52.66           N  
ANISOU 4121  N   ARG B 128     6837   8541   4631    710    521   -459       N  
ATOM   4122  CA  ARG B 128      -1.543  14.647  19.013  1.00 54.11           C  
ANISOU 4122  CA  ARG B 128     7137   8705   4716    855    569   -592       C  
ATOM   4123  C   ARG B 128      -2.915  14.304  19.575  1.00 59.39           C  
ANISOU 4123  C   ARG B 128     7789   9483   5294    945    862   -544       C  
ATOM   4124  O   ARG B 128      -3.256  14.684  20.699  1.00 60.81           O  
ANISOU 4124  O   ARG B 128     8149   9688   5267   1094    958   -618       O  
ATOM   4125  CB  ARG B 128      -1.635  15.889  18.122  1.00 53.17           C  
ANISOU 4125  CB  ARG B 128     6944   8474   4784    853    488   -676       C  
ATOM   4126  CG  ARG B 128      -0.302  16.377  17.551  1.00 61.60           C  
ANISOU 4126  CG  ARG B 128     8033   9418   5956    717    249   -745       C  
ATOM   4127  CD  ARG B 128       0.865  16.214  18.525  1.00 73.72           C  
ANISOU 4127  CD  ARG B 128     9710  10987   7313    694     83   -850       C  
ATOM   4128  NE  ARG B 128       0.610  16.893  19.795  1.00 83.91           N  
ANISOU 4128  NE  ARG B 128    11230  12271   8381    838    110  -1000       N  
ATOM   4129  CZ  ARG B 128       1.261  16.664  20.937  1.00 96.51           C  
ANISOU 4129  CZ  ARG B 128    12982  13960   9729    899      2  -1094       C  
ATOM   4130  NH1 ARG B 128       2.239  15.757  21.020  1.00 78.16           N  
ANISOU 4130  NH1 ARG B 128    10603  11755   7339    860   -149  -1048       N  
ATOM   4131  NH2 ARG B 128       0.918  17.355  22.020  1.00 86.99           N  
ANISOU 4131  NH2 ARG B 128    12000  12740   8313   1037     44  -1243       N  
ATOM   4132  N   TYR B 129      -3.693  13.571  18.787  1.00 55.32           N  
ANISOU 4132  N   TYR B 129     7043   9048   4927    839   1011   -437       N  
ATOM   4133  CA  TYR B 129      -4.941  13.026  19.268  1.00 57.08           C  
ANISOU 4133  CA  TYR B 129     7195   9410   5085    848   1318   -398       C  
ATOM   4134  C   TYR B 129      -4.676  12.197  20.511  1.00 63.61           C  
ANISOU 4134  C   TYR B 129     8299  10223   5648    869   1449   -333       C  
ATOM   4135  O   TYR B 129      -5.265  12.447  21.554  1.00 65.58           O  
ANISOU 4135  O   TYR B 129     8681  10530   5706    999   1630   -375       O  
ATOM   4136  CB  TYR B 129      -5.612  12.178  18.196  1.00 57.38           C  
ANISOU 4136  CB  TYR B 129     6937   9544   5321    656   1431   -320       C  
ATOM   4137  CG  TYR B 129      -6.871  11.527  18.680  1.00 61.56           C  
ANISOU 4137  CG  TYR B 129     7354  10236   5801    590   1776   -306       C  
ATOM   4138  CD1 TYR B 129      -8.029  12.272  18.842  1.00 65.50           C  
ANISOU 4138  CD1 TYR B 129     7660  10917   6312    725   1922   -406       C  
ATOM   4139  CD2 TYR B 129      -6.905  10.170  18.991  1.00 63.11           C  
ANISOU 4139  CD2 TYR B 129     7650  10399   5931    396   1983   -198       C  
ATOM   4140  CE1 TYR B 129      -9.193  11.689  19.298  1.00 68.87           C  
ANISOU 4140  CE1 TYR B 129     7932  11534   6701    639   2266   -416       C  
ATOM   4141  CE2 TYR B 129      -8.065   9.574  19.445  1.00 66.71           C  
ANISOU 4141  CE2 TYR B 129     8009  10991   6348    277   2349   -198       C  
ATOM   4142  CZ  TYR B 129      -9.209  10.342  19.598  1.00 76.19           C  
ANISOU 4142  CZ  TYR B 129     8954  12417   7576    384   2490   -316       C  
ATOM   4143  OH  TYR B 129     -10.376   9.776  20.049  1.00 80.51           O  
ANISOU 4143  OH  TYR B 129     9350  13144   8097    243   2877   -340       O  
ATOM   4144  N   THR B 130      -3.770  11.232  20.409  1.00 60.15           N  
ANISOU 4144  N   THR B 130     7974   9706   5174    778   1361   -228       N  
ATOM   4145  CA  THR B 130      -3.457  10.373  21.554  1.00 62.38           C  
ANISOU 4145  CA  THR B 130     8575   9958   5167    850   1478   -136       C  
ATOM   4146  C   THR B 130      -2.991  11.171  22.779  1.00 69.68           C  
ANISOU 4146  C   THR B 130     9762  10900   5815   1082   1362   -246       C  
ATOM   4147  O   THR B 130      -3.377  10.851  23.898  1.00 72.14           O  
ANISOU 4147  O   THR B 130    10315  11239   5854   1195   1569   -207       O  
ATOM   4148  CB  THR B 130      -2.410   9.294  21.204  1.00 67.95           C  
ANISOU 4148  CB  THR B 130     9386  10570   5862    795   1355    -10       C  
ATOM   4149  OG1 THR B 130      -2.835   8.585  20.037  1.00 66.02           O  
ANISOU 4149  OG1 THR B 130     8921  10295   5867    568   1459     62       O  
ATOM   4150  CG2 THR B 130      -2.247   8.310  22.341  1.00 68.00           C  
ANISOU 4150  CG2 THR B 130     9765  10529   5544    913   1525    120       C  
ATOM   4151  N   ALA B 131      -2.190  12.214  22.577  1.00 66.32           N  
ANISOU 4151  N   ALA B 131     9304  10451   5444   1135   1054   -396       N  
ATOM   4152  CA  ALA B 131      -1.677  13.000  23.705  1.00 68.66           C  
ANISOU 4152  CA  ALA B 131     9845  10766   5476   1318    914   -550       C  
ATOM   4153  C   ALA B 131      -2.766  13.858  24.353  1.00 75.91           C  
ANISOU 4153  C   ALA B 131    10825  11712   6307   1439   1120   -653       C  
ATOM   4154  O   ALA B 131      -2.868  13.908  25.577  1.00 78.31           O  
ANISOU 4154  O   ALA B 131    11397  12061   6297   1605   1206   -696       O  
ATOM   4155  CB  ALA B 131      -0.514  13.870  23.267  1.00 68.39           C  
ANISOU 4155  CB  ALA B 131     9748  10688   5549   1272    556   -714       C  
ATOM   4156  N   VAL B 132      -3.583  14.511  23.528  1.00 72.48           N  
ANISOU 4156  N   VAL B 132    10150  11264   6125   1392   1203   -690       N  
ATOM   4157  CA  VAL B 132      -4.611  15.452  24.005  1.00 74.55           C  
ANISOU 4157  CA  VAL B 132    10436  11561   6330   1556   1384   -804       C  
ATOM   4158  C   VAL B 132      -5.916  14.790  24.490  1.00 82.08           C  
ANISOU 4158  C   VAL B 132    11326  12664   7197   1589   1781   -710       C  
ATOM   4159  O   VAL B 132      -6.637  15.365  25.308  1.00 83.96           O  
ANISOU 4159  O   VAL B 132    11665  12964   7271   1771   1966   -800       O  
ATOM   4160  CB  VAL B 132      -4.950  16.479  22.900  1.00 76.72           C  
ANISOU 4160  CB  VAL B 132    10496  11769   6884   1560   1303   -880       C  
ATOM   4161  CG1 VAL B 132      -6.238  17.218  23.216  1.00 78.72           C  
ANISOU 4161  CG1 VAL B 132    10705  12102   7105   1771   1542   -956       C  
ATOM   4162  CG2 VAL B 132      -3.790  17.445  22.712  1.00 75.77           C  
ANISOU 4162  CG2 VAL B 132    10526  11466   6799   1537    992  -1025       C  
ATOM   4163  N   VAL B 133      -6.211  13.593  23.983  1.00 79.46           N  
ANISOU 4163  N   VAL B 133    10830  12386   6975   1397   1930   -545       N  
ATOM   4164  CA  VAL B 133      -7.444  12.866  24.317  1.00 82.10           C  
ANISOU 4164  CA  VAL B 133    11059  12864   7270   1334   2342   -468       C  
ATOM   4165  C   VAL B 133      -7.207  11.641  25.216  1.00 89.45           C  
ANISOU 4165  C   VAL B 133    12297  13748   7941   1275   2543   -315       C  
ATOM   4166  O   VAL B 133      -8.030  11.352  26.090  1.00 92.17           O  
ANISOU 4166  O   VAL B 133    12746  14175   8098   1309   2900   -287       O  
ATOM   4167  CB  VAL B 133      -8.168  12.421  23.026  1.00 84.56           C  
ANISOU 4167  CB  VAL B 133    10943  13277   7908   1117   2422   -426       C  
ATOM   4168  CG1 VAL B 133      -9.436  11.638  23.351  1.00 87.11           C  
ANISOU 4168  CG1 VAL B 133    11108  13776   8213    981   2863   -386       C  
ATOM   4169  CG2 VAL B 133      -8.483  13.640  22.161  1.00 83.34           C  
ANISOU 4169  CG2 VAL B 133    10527  13176   7961   1244   2243   -554       C  
ATOM   4170  N   MET B 134      -6.084  10.942  25.013  1.00 85.74           N  
ANISOU 4170  N   MET B 134    11990  13146   7440   1214   2331   -213       N  
ATOM   4171  CA  MET B 134      -5.764   9.699  25.748  1.00 87.82           C  
ANISOU 4171  CA  MET B 134    12597  13326   7444   1203   2505    -36       C  
ATOM   4172  C   MET B 134      -4.479   9.912  26.580  1.00 93.08           C  
ANISOU 4172  C   MET B 134    13621  13944   7802   1454   2197    -60       C  
ATOM   4173  O   MET B 134      -3.424   9.362  26.230  1.00 91.27           O  
ANISOU 4173  O   MET B 134    13461  13642   7576   1455   1957     12       O  
ATOM   4174  CB  MET B 134      -5.505   8.549  24.750  1.00 88.51           C  
ANISOU 4174  CB  MET B 134    12582  13309   7738    962   2516    108       C  
ATOM   4175  CG  MET B 134      -6.531   8.384  23.634  1.00 91.43           C  
ANISOU 4175  CG  MET B 134    12526  13757   8457    682   2688     80       C  
ATOM   4176  SD  MET B 134      -8.249   8.267  24.191  1.00 99.65           S  
ANISOU 4176  SD  MET B 134    13418  14972   9472    564   3218     47       S  
ATOM   4177  CE  MET B 134      -8.179   7.087  25.559  1.00100.10           C  
ANISOU 4177  CE  MET B 134    14032  14870   9131    576   3601    243       C  
ATOM   4178  N   PRO B 135      -4.556  10.678  27.694  1.00 92.65           N  
ANISOU 4178  N   PRO B 135    13785  13956   7461   1680   2200   -176       N  
ATOM   4179  CA  PRO B 135      -3.313  10.941  28.434  1.00 93.46           C  
ANISOU 4179  CA  PRO B 135    14176  14066   7269   1905   1857   -251       C  
ATOM   4180  C   PRO B 135      -3.302  10.012  29.661  1.00101.07           C  
ANISOU 4180  C   PRO B 135    15594  15025   7783   2090   2079    -89       C  
ATOM   4181  O   PRO B 135      -3.916  10.316  30.692  1.00103.98           O  
ANISOU 4181  O   PRO B 135    16187  15450   7871   2237   2304   -127       O  
ATOM   4182  CB  PRO B 135      -3.344  12.422  28.843  1.00 95.97           C  
ANISOU 4182  CB  PRO B 135    14482  14441   7540   2030   1695   -515       C  
ATOM   4183  CG  PRO B 135      -4.813  12.831  28.770  1.00101.17           C  
ANISOU 4183  CG  PRO B 135    14974  15137   8329   1987   2065   -535       C  
ATOM   4184  CD  PRO B 135      -5.564  11.764  27.997  1.00 95.63           C  
ANISOU 4184  CD  PRO B 135    14045  14429   7862   1752   2360   -337       C  
ATOM   4185  N   SER B 145       8.050   1.398  25.997  1.00101.14           N  
ANISOU 4185  N   SER B 145    16118  15060   7251   3890   -127    958       N  
ATOM   4186  CA  SER B 145       6.830   2.080  26.414  1.00 99.96           C  
ANISOU 4186  CA  SER B 145    16020  14803   7156   3578    127    915       C  
ATOM   4187  C   SER B 145       6.077   2.591  25.180  1.00 99.25           C  
ANISOU 4187  C   SER B 145    15522  14576   7613   3031    275    829       C  
ATOM   4188  O   SER B 145       5.859   1.832  24.233  1.00 97.13           O  
ANISOU 4188  O   SER B 145    15241  14081   7582   2861    471    959       O  
ATOM   4189  CB  SER B 145       7.164   3.218  27.385  1.00105.03           C  
ANISOU 4189  CB  SER B 145    16557  15781   7568   3712   -188    667       C  
ATOM   4190  N   SER B 146       5.686   3.866  25.193  1.00 94.20           N  
ANISOU 4190  N   SER B 146    14578  14067   7146   2783    178    606       N  
ATOM   4191  CA  SER B 146       5.001   4.495  24.051  1.00 90.11           C  
ANISOU 4191  CA  SER B 146    13673  13460   7107   2330    275    512       C  
ATOM   4192  C   SER B 146       5.985   4.946  22.933  1.00 91.56           C  
ANISOU 4192  C   SER B 146    13410  13780   7600   2218    -50    359       C  
ATOM   4193  O   SER B 146       5.564   5.279  21.814  1.00 87.96           O  
ANISOU 4193  O   SER B 146    12666  13232   7522   1890     22    320       O  
ATOM   4194  CB  SER B 146       4.153   5.679  24.546  1.00 93.25           C  
ANISOU 4194  CB  SER B 146    13987  13913   7532   2169    334    352       C  
ATOM   4195  OG  SER B 146       3.144   6.023  23.613  1.00 99.17           O  
ANISOU 4195  OG  SER B 146    14487  14534   8659   1803    546    336       O  
ATOM   4196  N   CYS B 147       7.287   4.945  23.240  1.00 89.83           N  
ANISOU 4196  N   CYS B 147    13128  13803   7203   2500   -398    268       N  
ATOM   4197  CA  CYS B 147       8.347   5.228  22.253  1.00 88.00           C  
ANISOU 4197  CA  CYS B 147    12480  13730   7225   2420   -678    130       C  
ATOM   4198  C   CYS B 147       8.471   4.084  21.237  1.00 88.86           C  
ANISOU 4198  C   CYS B 147    12611  13661   7491   2420   -527    326       C  
ATOM   4199  O   CYS B 147       9.098   4.234  20.186  1.00 86.66           O  
ANISOU 4199  O   CYS B 147    11996  13449   7481   2288   -656    247       O  
ATOM   4200  CB  CYS B 147       9.694   5.455  22.962  1.00 91.72           C  
ANISOU 4200  CB  CYS B 147    12850  14570   7429   2742  -1083    -43       C  
ATOM   4201  SG  CYS B 147       9.575   6.430  24.514  1.00 98.75           S  
ANISOU 4201  SG  CYS B 147    13897  15665   7958   2872  -1248   -250       S  
ATOM   4202  N   ARG B 148       7.880   2.939  21.573  1.00 85.45           N  
ANISOU 4202  N   ARG B 148    12607  12985   6874   2561   -230    573       N  
ATOM   4203  CA  ARG B 148       7.751   1.825  20.650  1.00 83.71           C  
ANISOU 4203  CA  ARG B 148    12493  12512   6799   2505     -9    754       C  
ATOM   4204  C   ARG B 148       6.470   1.950  19.820  1.00 82.43           C  
ANISOU 4204  C   ARG B 148    12238  12114   6969   2041    296    774       C  
ATOM   4205  O   ARG B 148       6.455   1.544  18.662  1.00 80.32           O  
ANISOU 4205  O   ARG B 148    11832  11727   6959   1857    368    799       O  
ATOM   4206  CB  ARG B 148       7.775   0.503  21.415  1.00 87.86           C  
ANISOU 4206  CB  ARG B 148    13581  12851   6952   2874    187   1002       C  
ATOM   4207  CG  ARG B 148       9.011   0.337  22.322  1.00102.42           C  
ANISOU 4207  CG  ARG B 148    15541  14975   8399   3426   -137    990       C  
ATOM   4208  CD  ARG B 148       9.120  -1.081  22.901  1.00114.71           C  
ANISOU 4208  CD  ARG B 148    17709  16299   9577   3857     71   1275       C  
ATOM   4209  NE  ARG B 148       9.457  -2.063  21.863  1.00118.77           N  
ANISOU 4209  NE  ARG B 148    18271  16601  10255   3883    184   1393       N  
ATOM   4210  CZ  ARG B 148      10.616  -2.715  21.748  1.00134.15           C  
ANISOU 4210  CZ  ARG B 148    20262  18670  12037   4345    -15   1440       C  
ATOM   4211  NH1 ARG B 148      11.611  -2.546  22.623  1.00124.64           N  
ANISOU 4211  NH1 ARG B 148    19038  17840  10479   4853   -368   1380       N  
ATOM   4212  NH2 ARG B 148      10.773  -3.567  20.740  1.00120.33           N  
ANISOU 4212  NH2 ARG B 148    18576  16681  10465   4319    140   1536       N  
ATOM   4213  N   ARG B 149       5.406   2.518  20.397  1.00 76.65           N  
ANISOU 4213  N   ARG B 149    11561  11345   6216   1871    465    745       N  
ATOM   4214  CA  ARG B 149       4.162   2.790  19.643  1.00 73.07           C  
ANISOU 4214  CA  ARG B 149    10933  10759   6070   1456    712    721       C  
ATOM   4215  C   ARG B 149       4.378   3.819  18.516  1.00 71.81           C  
ANISOU 4215  C   ARG B 149    10297  10728   6260   1227    493    544       C  
ATOM   4216  O   ARG B 149       3.612   3.855  17.542  1.00 69.79           O  
ANISOU 4216  O   ARG B 149     9861  10383   6273    937    636    534       O  
ATOM   4217  CB  ARG B 149       3.027   3.245  20.571  1.00 73.73           C  
ANISOU 4217  CB  ARG B 149    11144  10832   6037   1379    932    711       C  
ATOM   4218  N   VAL B 150       5.420   4.644  18.647  1.00 66.17           N  
ANISOU 4218  N   VAL B 150     9388  10228   5526   1354    155    397       N  
ATOM   4219  CA  VAL B 150       5.826   5.559  17.580  1.00 62.53           C  
ANISOU 4219  CA  VAL B 150     8535   9858   5368   1151    -33    246       C  
ATOM   4220  C   VAL B 150       6.726   4.849  16.586  1.00 64.41           C  
ANISOU 4220  C   VAL B 150     8657  10094   5721   1182   -114    293       C  
ATOM   4221  O   VAL B 150       6.474   4.887  15.384  1.00 61.97           O  
ANISOU 4221  O   VAL B 150     8164   9706   5675    956    -51    293       O  
ATOM   4222  CB  VAL B 150       6.577   6.767  18.137  1.00 66.85           C  
ANISOU 4222  CB  VAL B 150     8926  10618   5857   1209   -323     37       C  
ATOM   4223  CG1 VAL B 150       7.123   7.617  17.013  1.00 64.70           C  
ANISOU 4223  CG1 VAL B 150     8301  10400   5883    989   -475   -101       C  
ATOM   4224  CG2 VAL B 150       5.656   7.580  19.007  1.00 67.29           C  
ANISOU 4224  CG2 VAL B 150     9094  10656   5816   1172   -235    -33       C  
ATOM   4225  N   ALA B 151       7.774   4.203  17.093  1.00 61.63           N  
ANISOU 4225  N   ALA B 151     8420   9849   5149   1497   -257    329       N  
ATOM   4226  CA  ALA B 151       8.739   3.494  16.249  1.00 60.71           C  
ANISOU 4226  CA  ALA B 151     8198   9763   5105   1602   -337    366       C  
ATOM   4227  C   ALA B 151       8.066   2.594  15.213  1.00 61.44           C  
ANISOU 4227  C   ALA B 151     8392   9586   5367   1429    -68    505       C  
ATOM   4228  O   ALA B 151       8.497   2.537  14.065  1.00 59.64           O  
ANISOU 4228  O   ALA B 151     7948   9366   5345   1322   -108    473       O  
ATOM   4229  CB  ALA B 151       9.691   2.683  17.105  1.00 64.81           C  
ANISOU 4229  CB  ALA B 151     8927  10405   5295   2053   -465    433       C  
ATOM   4230  N   LEU B 152       7.012   1.893  15.606  1.00 57.59           N  
ANISOU 4230  N   LEU B 152     8230   8865   4787   1379    219    641       N  
ATOM   4231  CA  LEU B 152       6.238   1.131  14.642  1.00 55.93           C  
ANISOU 4231  CA  LEU B 152     8090   8411   4750   1135    482    719       C  
ATOM   4232  C   LEU B 152       5.598   2.081  13.621  1.00 56.84           C  
ANISOU 4232  C   LEU B 152     7838   8583   5175    778    460    592       C  
ATOM   4233  O   LEU B 152       5.817   1.939  12.413  1.00 55.15           O  
ANISOU 4233  O   LEU B 152     7458   8347   5151    651    439    566       O  
ATOM   4234  CB  LEU B 152       5.172   0.298  15.344  1.00 57.66           C  
ANISOU 4234  CB  LEU B 152     8705   8388   4818   1083    823    854       C  
ATOM   4235  CG  LEU B 152       4.377  -0.657  14.453  1.00 61.74           C  
ANISOU 4235  CG  LEU B 152     9336   8640   5485    802   1120    908       C  
ATOM   4236  CD1 LEU B 152       5.279  -1.688  13.811  1.00 62.40           C  
ANISOU 4236  CD1 LEU B 152     9584   8584   5541    979   1111    982       C  
ATOM   4237  CD2 LEU B 152       3.292  -1.329  15.266  1.00 66.53           C  
ANISOU 4237  CD2 LEU B 152    10302   9028   5947    689   1487   1011       C  
ATOM   4238  N   MET B 153       4.827   3.057  14.106  1.00 52.38           N  
ANISOU 4238  N   MET B 153     7173   8094   4635    656    465    517       N  
ATOM   4239  CA  MET B 153       4.170   4.034  13.222  1.00 49.79           C  
ANISOU 4239  CA  MET B 153     6536   7823   4559    391    441    410       C  
ATOM   4240  C   MET B 153       5.107   4.576  12.143  1.00 49.90           C  
ANISOU 4240  C   MET B 153     6282   7930   4747    356    229    332       C  
ATOM   4241  O   MET B 153       4.781   4.570  10.957  1.00 47.97           O  
ANISOU 4241  O   MET B 153     5893   7647   4685    176    272    320       O  
ATOM   4242  CB  MET B 153       3.608   5.203  14.028  1.00 52.59           C  
ANISOU 4242  CB  MET B 153     6830   8277   4875    383    404    321       C  
ATOM   4243  CG  MET B 153       2.206   4.979  14.563  1.00 57.78           C  
ANISOU 4243  CG  MET B 153     7600   8870   5483    279    676    359       C  
ATOM   4244  SD  MET B 153       1.512   6.511  15.239  1.00 62.56           S  
ANISOU 4244  SD  MET B 153     8085   9603   6082    288    630    230       S  
ATOM   4245  CE  MET B 153       1.695   6.259  17.016  1.00 62.08           C  
ANISOU 4245  CE  MET B 153     8369   9550   5667    533    684    275       C  
ATOM   4246  N   ILE B 154       6.276   5.035  12.563  1.00 45.57           N  
ANISOU 4246  N   ILE B 154     5665   7524   4125    522      8    268       N  
ATOM   4247  CA  ILE B 154       7.275   5.560  11.630  1.00 43.67           C  
ANISOU 4247  CA  ILE B 154     5163   7390   4042    471   -162    183       C  
ATOM   4248  C   ILE B 154       7.624   4.526  10.567  1.00 46.39           C  
ANISOU 4248  C   ILE B 154     5509   7658   4458    473    -87    263       C  
ATOM   4249  O   ILE B 154       7.517   4.815   9.373  1.00 45.21           O  
ANISOU 4249  O   ILE B 154     5198   7486   4493    294    -68    238       O  
ATOM   4250  CB  ILE B 154       8.544   6.051  12.373  1.00 48.01           C  
ANISOU 4250  CB  ILE B 154     5612   8149   4479    640   -403     70       C  
ATOM   4251  CG1 ILE B 154       8.254   7.427  12.996  1.00 48.11           C  
ANISOU 4251  CG1 ILE B 154     5561   8217   4501    533   -489    -71       C  
ATOM   4252  CG2 ILE B 154       9.739   6.098  11.427  1.00 48.33           C  
ANISOU 4252  CG2 ILE B 154     5399   8314   4650    621   -521      7       C  
ATOM   4253  CD1 ILE B 154       9.073   7.773  14.215  1.00 53.72           C  
ANISOU 4253  CD1 ILE B 154     6280   9122   5008    710   -693   -197       C  
ATOM   4254  N   THR B 155       8.007   3.325  10.993  1.00 42.99           N  
ANISOU 4254  N   THR B 155     5302   7171   3862    696    -33    362       N  
ATOM   4255  CA  THR B 155       8.266   2.239  10.053  1.00 42.30           C  
ANISOU 4255  CA  THR B 155     5290   6963   3818    721     73    436       C  
ATOM   4256  C   THR B 155       7.128   2.121   9.044  1.00 43.91           C  
ANISOU 4256  C   THR B 155     5482   7011   4190    417    250    441       C  
ATOM   4257  O   THR B 155       7.352   2.160   7.828  1.00 42.03           O  
ANISOU 4257  O   THR B 155     5092   6782   4096    306    237    406       O  
ATOM   4258  CB  THR B 155       8.392   0.907  10.770  1.00 50.15           C  
ANISOU 4258  CB  THR B 155     6659   7811   4585    986    194    570       C  
ATOM   4259  OG1 THR B 155       9.245   1.071  11.900  1.00 51.53           O  
ANISOU 4259  OG1 THR B 155     6864   8167   4548   1305     13    562       O  
ATOM   4260  CG2 THR B 155       8.949  -0.150   9.841  1.00 47.75           C  
ANISOU 4260  CG2 THR B 155     6444   7393   4307   1081    271    623       C  
ATOM   4261  N   ALA B 156       5.906   2.008   9.561  1.00 40.59           N  
ANISOU 4261  N   ALA B 156     5202   6484   3736    288    413    470       N  
ATOM   4262  CA  ALA B 156       4.738   1.828   8.721  1.00 39.51           C  
ANISOU 4262  CA  ALA B 156     5023   6256   3735      4    573    445       C  
ATOM   4263  C   ALA B 156       4.610   2.960   7.713  1.00 41.70           C  
ANISOU 4263  C   ALA B 156     4981   6671   4192   -143    441    350       C  
ATOM   4264  O   ALA B 156       4.334   2.703   6.546  1.00 40.73           O  
ANISOU 4264  O   ALA B 156     4782   6522   4173   -287    480    322       O  
ATOM   4265  CB  ALA B 156       3.502   1.728   9.562  1.00 41.20           C  
ANISOU 4265  CB  ALA B 156     5357   6410   3887   -110    758    460       C  
ATOM   4266  N   VAL B 157       4.833   4.200   8.155  1.00 37.79           N  
ANISOU 4266  N   VAL B 157     4339   6305   3712    -98    292    299       N  
ATOM   4267  CA  VAL B 157       4.830   5.366   7.247  1.00 36.13           C  
ANISOU 4267  CA  VAL B 157     3897   6181   3649   -203    184    230       C  
ATOM   4268  C   VAL B 157       5.809   5.194   6.080  1.00 39.39           C  
ANISOU 4268  C   VAL B 157     4218   6609   4141   -208    123    228       C  
ATOM   4269  O   VAL B 157       5.531   5.610   4.952  1.00 37.92           O  
ANISOU 4269  O   VAL B 157     3921   6434   4054   -324    122    208       O  
ATOM   4270  CB  VAL B 157       5.189   6.702   7.975  1.00 39.78           C  
ANISOU 4270  CB  VAL B 157     4284   6728   4103   -148     47    163       C  
ATOM   4271  CG1 VAL B 157       5.480   7.812   6.965  1.00 38.66           C  
ANISOU 4271  CG1 VAL B 157     3979   6611   4097   -244    -34    112       C  
ATOM   4272  CG2 VAL B 157       4.080   7.126   8.910  1.00 39.92           C  
ANISOU 4272  CG2 VAL B 157     4367   6744   4059   -147    117    146       C  
ATOM   4273  N   TRP B 158       6.954   4.581   6.356  1.00 36.90           N  
ANISOU 4273  N   TRP B 158     3949   6313   3757    -52     77    250       N  
ATOM   4274  CA  TRP B 158       7.958   4.380   5.325  1.00 36.53           C  
ANISOU 4274  CA  TRP B 158     3797   6309   3775    -31     42    241       C  
ATOM   4275  C   TRP B 158       7.717   3.132   4.507  1.00 40.08           C  
ANISOU 4275  C   TRP B 158     4382   6633   4213    -44    177    289       C  
ATOM   4276  O   TRP B 158       7.738   3.199   3.280  1.00 38.99           O  
ANISOU 4276  O   TRP B 158     4162   6496   4156   -146    199    268       O  
ATOM   4277  CB  TRP B 158       9.337   4.355   5.946  1.00 36.68           C  
ANISOU 4277  CB  TRP B 158     3743   6467   3728    166    -82    212       C  
ATOM   4278  CG  TRP B 158       9.784   5.716   6.325  1.00 37.77           C  
ANISOU 4278  CG  TRP B 158     3689   6741   3919     93   -219    110       C  
ATOM   4279  CD1 TRP B 158       9.759   6.266   7.558  1.00 41.45           C  
ANISOU 4279  CD1 TRP B 158     4176   7272   4300    149   -315     55       C  
ATOM   4280  CD2 TRP B 158      10.309   6.712   5.449  1.00 37.32           C  
ANISOU 4280  CD2 TRP B 158     3430   6744   4005    -72   -248     40       C  
ATOM   4281  NE1 TRP B 158      10.256   7.541   7.517  1.00 41.03           N  
ANISOU 4281  NE1 TRP B 158     3943   7309   4339     12   -411    -67       N  
ATOM   4282  CE2 TRP B 158      10.600   7.840   6.229  1.00 41.72           C  
ANISOU 4282  CE2 TRP B 158     3900   7381   4571   -134   -356    -69       C  
ATOM   4283  CE3 TRP B 158      10.564   6.756   4.080  1.00 38.12           C  
ANISOU 4283  CE3 TRP B 158     3448   6825   4210   -178   -173     57       C  
ATOM   4284  CZ2 TRP B 158      11.131   9.005   5.690  1.00 41.36           C  
ANISOU 4284  CZ2 TRP B 158     3702   7361   4651   -328   -369   -160       C  
ATOM   4285  CZ3 TRP B 158      11.092   7.911   3.545  1.00 39.89           C  
ANISOU 4285  CZ3 TRP B 158     3522   7091   4543   -345   -182    -11       C  
ATOM   4286  CH2 TRP B 158      11.368   9.022   4.349  1.00 41.29           C  
ANISOU 4286  CH2 TRP B 158     3629   7315   4743   -433   -269   -118       C  
ATOM   4287  N   VAL B 159       7.480   2.003   5.176  1.00 37.69           N  
ANISOU 4287  N   VAL B 159     4325   6201   3793     57    283    349       N  
ATOM   4288  CA  VAL B 159       7.148   0.766   4.465  1.00 38.08           C  
ANISOU 4288  CA  VAL B 159     4567   6074   3827      7    446    373       C  
ATOM   4289  C   VAL B 159       5.986   0.998   3.507  1.00 41.15           C  
ANISOU 4289  C   VAL B 159     4869   6447   4320   -277    507    307       C  
ATOM   4290  O   VAL B 159       6.055   0.577   2.352  1.00 41.04           O  
ANISOU 4290  O   VAL B 159     4853   6398   4343   -349    544    270       O  
ATOM   4291  CB  VAL B 159       6.751  -0.397   5.390  1.00 43.49           C  
ANISOU 4291  CB  VAL B 159     5599   6555   4371     87    614    449       C  
ATOM   4292  CG1 VAL B 159       6.367  -1.610   4.549  1.00 44.24           C  
ANISOU 4292  CG1 VAL B 159     5913   6427   4468    -30    805    439       C  
ATOM   4293  CG2 VAL B 159       7.876  -0.764   6.326  1.00 44.83           C  
ANISOU 4293  CG2 VAL B 159     5900   6751   4383    443    544    526       C  
ATOM   4294  N   LEU B 160       4.931   1.666   3.981  1.00 36.77           N  
ANISOU 4294  N   LEU B 160     4233   5944   3792   -410    509    280       N  
ATOM   4295  CA  LEU B 160       3.800   2.026   3.120  1.00 36.16           C  
ANISOU 4295  CA  LEU B 160     4012   5930   3796   -628    525    201       C  
ATOM   4296  C   LEU B 160       4.204   2.942   1.964  1.00 38.34           C  
ANISOU 4296  C   LEU B 160     4096   6328   4142   -625    391    174       C  
ATOM   4297  O   LEU B 160       3.804   2.722   0.818  1.00 38.00           O  
ANISOU 4297  O   LEU B 160     4013   6308   4117   -732    404    120       O  
ATOM   4298  CB  LEU B 160       2.702   2.717   3.924  1.00 36.34           C  
ANISOU 4298  CB  LEU B 160     3947   6035   3826   -698    540    177       C  
ATOM   4299  CG  LEU B 160       1.422   3.024   3.135  1.00 41.20           C  
ANISOU 4299  CG  LEU B 160     4378   6774   4502   -879    550     79       C  
ATOM   4300  CD1 LEU B 160       0.626   1.739   2.950  1.00 43.20           C  
ANISOU 4300  CD1 LEU B 160     4726   6944   4743  -1094    732      9       C  
ATOM   4301  CD2 LEU B 160       0.584   4.112   3.811  1.00 42.83           C  
ANISOU 4301  CD2 LEU B 160     4435   7117   4720   -851    514     58       C  
ATOM   4302  N   ALA B 161       4.980   3.977   2.267  1.00 33.88           N  
ANISOU 4302  N   ALA B 161     3435   5837   3602   -517    276    202       N  
ATOM   4303  CA  ALA B 161       5.442   4.904   1.237  1.00 32.95           C  
ANISOU 4303  CA  ALA B 161     3187   5792   3542   -528    196    194       C  
ATOM   4304  C   ALA B 161       6.076   4.135   0.090  1.00 36.30           C  
ANISOU 4304  C   ALA B 161     3646   6190   3957   -527    240    193       C  
ATOM   4305  O   ALA B 161       5.898   4.482  -1.073  1.00 36.02           O  
ANISOU 4305  O   ALA B 161     3562   6196   3929   -583    230    178       O  
ATOM   4306  CB  ALA B 161       6.433   5.903   1.813  1.00 33.67           C  
ANISOU 4306  CB  ALA B 161     3201   5929   3664   -455    108    202       C  
ATOM   4307  N   PHE B 162       6.806   3.078   0.417  1.00 32.73           N  
ANISOU 4307  N   PHE B 162     3306   5668   3463   -428    295    212       N  
ATOM   4308  CA  PHE B 162       7.426   2.260  -0.609  1.00 32.91           C  
ANISOU 4308  CA  PHE B 162     3391   5652   3462   -392    359    202       C  
ATOM   4309  C   PHE B 162       6.437   1.304  -1.268  1.00 37.30           C  
ANISOU 4309  C   PHE B 162     4088   6104   3980   -528    456    145       C  
ATOM   4310  O   PHE B 162       6.481   1.118  -2.479  1.00 37.24           O  
ANISOU 4310  O   PHE B 162     4084   6112   3955   -575    474    101       O  
ATOM   4311  CB  PHE B 162       8.597   1.491  -0.020  1.00 35.72           C  
ANISOU 4311  CB  PHE B 162     3824   5978   3769   -178    382    239       C  
ATOM   4312  CG  PHE B 162       9.399   0.751  -1.035  1.00 38.04           C  
ANISOU 4312  CG  PHE B 162     4165   6251   4037    -87    453    226       C  
ATOM   4313  CD1 PHE B 162      10.040   1.427  -2.051  1.00 40.85           C  
ANISOU 4313  CD1 PHE B 162     4350   6731   4440   -114    436    207       C  
ATOM   4314  CD2 PHE B 162       9.518  -0.630  -0.970  1.00 41.79           C  
ANISOU 4314  CD2 PHE B 162     4893   6558   4427     35    568    235       C  
ATOM   4315  CE1 PHE B 162      10.784   0.741  -2.994  1.00 42.97           C  
ANISOU 4315  CE1 PHE B 162     4662   6994   4670    -15    524    190       C  
ATOM   4316  CE2 PHE B 162      10.269  -1.327  -1.910  1.00 45.89           C  
ANISOU 4316  CE2 PHE B 162     5479   7049   4909    152    647    213       C  
ATOM   4317  CZ  PHE B 162      10.899  -0.639  -2.927  1.00 43.54           C  
ANISOU 4317  CZ  PHE B 162     4972   6913   4658    129    621    186       C  
ATOM   4318  N   ALA B 163       5.552   0.700  -0.474  1.00 34.29           N  
ANISOU 4318  N   ALA B 163     3827   5625   3575   -610    531    131       N  
ATOM   4319  CA  ALA B 163       4.530  -0.228  -0.996  1.00 35.04           C  
ANISOU 4319  CA  ALA B 163     4039   5627   3648   -812    643     34       C  
ATOM   4320  C   ALA B 163       3.658   0.444  -2.045  1.00 38.93           C  
ANISOU 4320  C   ALA B 163     4337   6294   4162   -963    554    -61       C  
ATOM   4321  O   ALA B 163       3.355  -0.153  -3.080  1.00 39.05           O  
ANISOU 4321  O   ALA B 163     4398   6300   4138  -1075    584   -163       O  
ATOM   4322  CB  ALA B 163       3.666  -0.770   0.126  1.00 36.61           C  
ANISOU 4322  CB  ALA B 163     4362   5716   3832   -921    767     32       C  
ATOM   4323  N   VAL B 164       3.276   1.693  -1.779  1.00 35.01           N  
ANISOU 4323  N   VAL B 164     3644   5954   3703   -935    440    -32       N  
ATOM   4324  CA  VAL B 164       2.440   2.461  -2.708  1.00 35.14           C  
ANISOU 4324  CA  VAL B 164     3489   6157   3708   -993    337    -99       C  
ATOM   4325  C   VAL B 164       3.157   2.796  -4.017  1.00 40.03           C  
ANISOU 4325  C   VAL B 164     4112   6818   4279   -912    279    -79       C  
ATOM   4326  O   VAL B 164       2.525   2.890  -5.076  1.00 40.39           O  
ANISOU 4326  O   VAL B 164     4104   6988   4254   -957    219   -159       O  
ATOM   4327  CB  VAL B 164       1.926   3.777  -2.065  1.00 38.02           C  
ANISOU 4327  CB  VAL B 164     3698   6640   4106   -920    248    -54       C  
ATOM   4328  CG1 VAL B 164       1.452   4.763  -3.127  1.00 38.02           C  
ANISOU 4328  CG1 VAL B 164     3578   6807   4060   -857    127    -70       C  
ATOM   4329  CG2 VAL B 164       0.803   3.469  -1.093  1.00 38.55           C  
ANISOU 4329  CG2 VAL B 164     3711   6742   4194  -1031    316   -116       C  
ATOM   4330  N   SER B 165       4.473   2.970  -3.936  1.00 36.35           N  
ANISOU 4330  N   SER B 165     3700   6275   3835   -787    300     16       N  
ATOM   4331  CA  SER B 165       5.251   3.464  -5.057  1.00 35.93           C  
ANISOU 4331  CA  SER B 165     3642   6266   3745   -715    285     54       C  
ATOM   4332  C   SER B 165       5.743   2.332  -5.951  1.00 42.03           C  
ANISOU 4332  C   SER B 165     4545   6977   4449   -718    370     -1       C  
ATOM   4333  O   SER B 165       5.743   2.456  -7.169  1.00 42.39           O  
ANISOU 4333  O   SER B 165     4613   7087   4408   -715    361    -28       O  
ATOM   4334  CB  SER B 165       6.425   4.279  -4.532  1.00 37.21           C  
ANISOU 4334  CB  SER B 165     3748   6413   3978   -621    287    151       C  
ATOM   4335  OG  SER B 165       5.975   5.283  -3.645  1.00 41.79           O  
ANISOU 4335  OG  SER B 165     4252   7016   4610   -623    218    180       O  
ATOM   4336  N   CYS B 166       6.109   1.208  -5.356  1.00 39.95           N  
ANISOU 4336  N   CYS B 166     4406   6575   4200   -702    461    -19       N  
ATOM   4337  CA  CYS B 166       6.788   0.144  -6.097  1.00 41.46           C  
ANISOU 4337  CA  CYS B 166     4759   6669   4325   -648    566    -62       C  
ATOM   4338  C   CYS B 166       6.135  -0.298  -7.413  1.00 45.87           C  
ANISOU 4338  C   CYS B 166     5396   7255   4777   -764    571   -189       C  
ATOM   4339  O   CYS B 166       6.826  -0.822  -8.272  1.00 46.87           O  
ANISOU 4339  O   CYS B 166     5636   7341   4830   -689    645   -217       O  
ATOM   4340  CB  CYS B 166       7.040  -1.085  -5.205  1.00 43.07           C  
ANISOU 4340  CB  CYS B 166     5161   6674   4531   -592    678    -62       C  
ATOM   4341  SG  CYS B 166       5.533  -1.957  -4.628  1.00 48.41           S  
ANISOU 4341  SG  CYS B 166     5986   7206   5202   -843    750   -168       S  
ATOM   4342  N   PRO B 167       4.815  -0.114  -7.589  1.00 41.88           N  
ANISOU 4342  N   PRO B 167     4817   6847   4248   -933    488   -288       N  
ATOM   4343  CA  PRO B 167       4.339  -0.461  -8.934  1.00 42.90           C  
ANISOU 4343  CA  PRO B 167     4998   7058   4244  -1014    458   -431       C  
ATOM   4344  C   PRO B 167       5.102   0.216 -10.071  1.00 45.11           C  
ANISOU 4344  C   PRO B 167     5278   7437   4423   -859    435   -361       C  
ATOM   4345  O   PRO B 167       5.284  -0.389 -11.124  1.00 45.69           O  
ANISOU 4345  O   PRO B 167     5487   7503   4369   -858    476   -454       O  
ATOM   4346  CB  PRO B 167       2.875  -0.015  -8.906  1.00 45.17           C  
ANISOU 4346  CB  PRO B 167     5106   7539   4519  -1161    326   -535       C  
ATOM   4347  CG  PRO B 167       2.461  -0.265  -7.497  1.00 49.03           C  
ANISOU 4347  CG  PRO B 167     5562   7929   5138  -1258    388   -517       C  
ATOM   4348  CD  PRO B 167       3.686   0.070  -6.654  1.00 43.03           C  
ANISOU 4348  CD  PRO B 167     4854   7034   4460  -1067    445   -323       C  
ATOM   4349  N   LEU B 168       5.565   1.442  -9.845  1.00 39.88           N  
ANISOU 4349  N   LEU B 168     4496   6844   3811   -744    396   -204       N  
ATOM   4350  CA  LEU B 168       6.357   2.169 -10.846  1.00 39.81           C  
ANISOU 4350  CA  LEU B 168     4513   6899   3715   -623    429   -114       C  
ATOM   4351  C   LEU B 168       7.662   1.443 -11.200  1.00 43.68           C  
ANISOU 4351  C   LEU B 168     5106   7296   4197   -538    591   -102       C  
ATOM   4352  O   LEU B 168       8.206   1.620 -12.296  1.00 44.74           O  
ANISOU 4352  O   LEU B 168     5309   7480   4211   -467    662    -82       O  
ATOM   4353  CB  LEU B 168       6.659   3.591 -10.365  1.00 38.73           C  
ANISOU 4353  CB  LEU B 168     4262   6793   3661   -565    404     41       C  
ATOM   4354  CG  LEU B 168       5.442   4.488 -10.133  1.00 43.06           C  
ANISOU 4354  CG  LEU B 168     4731   7439   4191   -573    257     49       C  
ATOM   4355  CD1 LEU B 168       5.843   5.768  -9.428  1.00 42.34           C  
ANISOU 4355  CD1 LEU B 168     4582   7302   4205   -528    266    187       C  
ATOM   4356  CD2 LEU B 168       4.738   4.792 -11.436  1.00 46.78           C  
ANISOU 4356  CD2 LEU B 168     5267   8055   4452   -508    174     14       C  
ATOM   4357  N   LEU B 169       8.145   0.627 -10.267  1.00 39.29           N  
ANISOU 4357  N   LEU B 169     4570   6614   3745   -513    657   -110       N  
ATOM   4358  CA  LEU B 169       9.283  -0.258 -10.504  1.00 40.19           C  
ANISOU 4358  CA  LEU B 169     4786   6646   3839   -378    805   -121       C  
ATOM   4359  C   LEU B 169       8.922  -1.545 -11.243  1.00 46.87           C  
ANISOU 4359  C   LEU B 169     5875   7376   4557   -409    871   -273       C  
ATOM   4360  O   LEU B 169       9.809  -2.224 -11.755  1.00 47.57           O  
ANISOU 4360  O   LEU B 169     6086   7406   4584   -267   1005   -295       O  
ATOM   4361  CB  LEU B 169       9.985  -0.603  -9.183  1.00 39.68           C  
ANISOU 4361  CB  LEU B 169     4671   6505   3900   -266    836    -60       C  
ATOM   4362  CG  LEU B 169      11.032   0.418  -8.739  1.00 43.49           C  
ANISOU 4362  CG  LEU B 169     4916   7124   4483   -181    831     47       C  
ATOM   4363  CD1 LEU B 169      11.371   0.241  -7.275  1.00 43.14           C  
ANISOU 4363  CD1 LEU B 169     4800   7054   4535    -91    784     84       C  
ATOM   4364  CD2 LEU B 169      12.273   0.285  -9.614  1.00 47.11           C  
ANISOU 4364  CD2 LEU B 169     5338   7664   4896    -46    973     51       C  
ATOM   4365  N   PHE B 170       7.640  -1.887 -11.310  1.00 45.02           N  
ANISOU 4365  N   PHE B 170     5705   7119   4281   -599    790   -399       N  
ATOM   4366  CA  PHE B 170       7.215  -3.102 -12.018  1.00 47.48           C  
ANISOU 4366  CA  PHE B 170     6257   7311   4471   -695    854   -591       C  
ATOM   4367  C   PHE B 170       6.671  -2.824 -13.421  1.00 54.36           C  
ANISOU 4367  C   PHE B 170     7142   8356   5156   -758    768   -709       C  
ATOM   4368  O   PHE B 170       6.092  -3.722 -14.049  1.00 56.59           O  
ANISOU 4368  O   PHE B 170     7594   8585   5322   -894    777   -919       O  
ATOM   4369  CB  PHE B 170       6.161  -3.868 -11.211  1.00 49.73           C  
ANISOU 4369  CB  PHE B 170     6620   7454   4821   -919    854   -710       C  
ATOM   4370  CG  PHE B 170       6.478  -3.996  -9.744  1.00 49.92           C  
ANISOU 4370  CG  PHE B 170     6643   7332   4991   -852    914   -576       C  
ATOM   4371  CD1 PHE B 170       7.785  -4.127  -9.301  1.00 52.47           C  
ANISOU 4371  CD1 PHE B 170     7011   7575   5349   -581   1003   -436       C  
ATOM   4372  CD2 PHE B 170       5.455  -4.009  -8.810  1.00 51.71           C  
ANISOU 4372  CD2 PHE B 170     6814   7532   5302  -1046    884   -605       C  
ATOM   4373  CE1 PHE B 170       8.067  -4.241  -7.962  1.00 52.83           C  
ANISOU 4373  CE1 PHE B 170     7064   7522   5486   -483   1030   -323       C  
ATOM   4374  CE2 PHE B 170       5.726  -4.131  -7.464  1.00 53.84           C  
ANISOU 4374  CE2 PHE B 170     7121   7670   5666   -966    945   -479       C  
ATOM   4375  CZ  PHE B 170       7.036  -4.246  -7.036  1.00 51.68           C  
ANISOU 4375  CZ  PHE B 170     6913   7322   5403   -672   1004   -336       C  
ATOM   4376  N   GLY B 171       6.851  -1.594 -13.906  1.00 50.67           N  
ANISOU 4376  N   GLY B 171     6525   8085   4641   -661    691   -585       N  
ATOM   4377  CA  GLY B 171       6.494  -1.238 -15.280  1.00 52.35           C  
ANISOU 4377  CA  GLY B 171     6790   8473   4626   -639    618   -654       C  
ATOM   4378  C   GLY B 171       5.185  -0.486 -15.448  1.00 57.13           C  
ANISOU 4378  C   GLY B 171     7251   9299   5159   -719    397   -704       C  
ATOM   4379  O   GLY B 171       4.647  -0.410 -16.557  1.00 59.16           O  
ANISOU 4379  O   GLY B 171     7564   9728   5188   -702    294   -816       O  
ATOM   4380  N   PHE B 172       4.674   0.089 -14.366  1.00 51.71           N  
ANISOU 4380  N   PHE B 172     6375   8632   4641   -772    318   -629       N  
ATOM   4381  CA  PHE B 172       3.493   0.925 -14.461  1.00 51.68           C  
ANISOU 4381  CA  PHE B 172     6204   8861   4571   -780    116   -656       C  
ATOM   4382  C   PHE B 172       3.864   2.312 -14.978  1.00 55.18           C  
ANISOU 4382  C   PHE B 172     6652   9396   4916   -561     88   -449       C  
ATOM   4383  O   PHE B 172       2.979   3.083 -15.330  1.00 55.75           O  
ANISOU 4383  O   PHE B 172     6650   9670   4863   -473    -78   -450       O  
ATOM   4384  CB  PHE B 172       2.797   1.044 -13.111  1.00 52.18           C  
ANISOU 4384  CB  PHE B 172     6081   8909   4837   -898     70   -655       C  
ATOM   4385  CG  PHE B 172       1.329   0.768 -13.170  1.00 55.52           C  
ANISOU 4385  CG  PHE B 172     6343   9544   5207  -1059    -85   -875       C  
ATOM   4386  CD1 PHE B 172       0.464   1.648 -13.800  1.00 59.67           C  
ANISOU 4386  CD1 PHE B 172     6724  10374   5575   -936   -287   -903       C  
ATOM   4387  CD2 PHE B 172       0.806  -0.384 -12.602  1.00 58.53           C  
ANISOU 4387  CD2 PHE B 172     6721   9832   5688  -1329    -16  -1065       C  
ATOM   4388  CE1 PHE B 172      -0.902   1.391 -13.855  1.00 62.51           C  
ANISOU 4388  CE1 PHE B 172     6862  11004   5884  -1076   -446  -1141       C  
ATOM   4389  CE2 PHE B 172      -0.552  -0.649 -12.657  1.00 63.23           C  
ANISOU 4389  CE2 PHE B 172     7118  10656   6249  -1531   -137  -1304       C  
ATOM   4390  CZ  PHE B 172      -1.407   0.241 -13.286  1.00 62.40           C  
ANISOU 4390  CZ  PHE B 172     6795  10920   5995  -1403   -366  -1355       C  
ATOM   4391  N   ASN B 173       5.158   2.642 -15.019  1.00 51.04           N  
ANISOU 4391  N   ASN B 173     6220   8730   4442   -467    263   -277       N  
ATOM   4392  CA  ASN B 173       5.601   3.915 -15.595  1.00 51.60           C  
ANISOU 4392  CA  ASN B 173     6357   8835   4413   -307    303    -83       C  
ATOM   4393  C   ASN B 173       5.676   3.812 -17.126  1.00 59.63           C  
ANISOU 4393  C   ASN B 173     7574   9957   5127   -194    321   -117       C  
ATOM   4394  O   ASN B 173       6.759   3.799 -17.736  1.00 60.23           O  
ANISOU 4394  O   ASN B 173     7786   9957   5143   -138    518    -35       O  
ATOM   4395  CB  ASN B 173       6.940   4.369 -14.988  1.00 50.30           C  
ANISOU 4395  CB  ASN B 173     6166   8507   4436   -307    501     84       C  
ATOM   4396  CG  ASN B 173       7.389   5.758 -15.486  1.00 70.78           C  
ANISOU 4396  CG  ASN B 173     8853  11087   6954   -209    593    281       C  
ATOM   4397  OD1 ASN B 173       6.569   6.595 -15.888  1.00 64.94           O  
ANISOU 4397  OD1 ASN B 173     8189  10421   6065   -103    481    339       O  
ATOM   4398  ND2 ASN B 173       8.703   5.997 -15.458  1.00 61.37           N  
ANISOU 4398  ND2 ASN B 173     7660   9801   5858   -239    812    378       N  
ATOM   4399  N   THR B 174       4.502   3.741 -17.741  1.00 58.20           N  
ANISOU 4399  N   THR B 174     7393   9982   4739   -155    112   -254       N  
ATOM   4400  CA  THR B 174       4.393   3.640 -19.182  1.00 60.79           C  
ANISOU 4400  CA  THR B 174     7915  10455   4727    -25     77   -315       C  
ATOM   4401  C   THR B 174       4.348   4.952 -19.963  1.00 68.04           C  
ANISOU 4401  C   THR B 174     8992  11457   5404    229     63   -110       C  
ATOM   4402  O   THR B 174       3.490   5.796 -19.706  1.00 68.26           O  
ANISOU 4402  O   THR B 174     8940  11599   5398    347   -105    -52       O  
ATOM   4403  CB  THR B 174       3.053   3.022 -19.568  1.00 67.46           C  
ANISOU 4403  CB  THR B 174     8668  11556   5409    -80   -186   -591       C  
ATOM   4404  OG1 THR B 174       1.989   3.799 -19.002  1.00 65.86           O  
ANISOU 4404  OG1 THR B 174     8256  11522   5247    -21   -388   -572       O  
ATOM   4405  CG2 THR B 174       2.971   1.584 -19.053  1.00 64.44           C  
ANISOU 4405  CG2 THR B 174     8221  11068   5194   -357   -148   -834       C  
ATOM   4406  N   THR B 175       5.244   5.120 -20.931  1.00 66.92           N  
ANISOU 4406  N   THR B 175     9098  11254   5076    335    256      3       N  
ATOM   4407  CA  THR B 175       5.383   6.413 -21.600  1.00 68.58           C  
ANISOU 4407  CA  THR B 175     9533  11458   5066    564    327    246       C  
ATOM   4408  C   THR B 175       4.858   6.598 -23.029  1.00 76.33           C  
ANISOU 4408  C   THR B 175    10772  12650   5579    822    216    231       C  
ATOM   4409  O   THR B 175       4.037   7.480 -23.285  1.00 77.78           O  
ANISOU 4409  O   THR B 175    11029  12964   5559   1059     46    320       O  
ATOM   4410  CB  THR B 175       6.859   6.870 -21.616  1.00 76.23           C  
ANISOU 4410  CB  THR B 175    10629  12185   6150    508    693    458       C  
ATOM   4411  OG1 THR B 175       7.031   7.905 -22.592  1.00 79.76           O  
ANISOU 4411  OG1 THR B 175    11396  12609   6300    713    821    671       O  
ATOM   4412  CG2 THR B 175       7.774   5.704 -21.953  1.00 74.05           C  
ANISOU 4412  CG2 THR B 175    10356  11877   5904    398    869    331       C  
ATOM   4413  N   GLY B 176       5.352   5.784 -23.956  1.00 74.03           N  
ANISOU 4413  N   GLY B 176    10638  12396   5095    814    316    122       N  
ATOM   4414  CA  GLY B 176       5.250   6.071 -25.398  1.00 77.36           C  
ANISOU 4414  CA  GLY B 176    11390  12965   5038   1079    310    168       C  
ATOM   4415  C   GLY B 176       6.292   6.991 -26.046  1.00 82.04           C  
ANISOU 4415  C   GLY B 176    12319  13372   5480   1211    660    478       C  
ATOM   4416  O   GLY B 176       6.315   7.156 -27.276  1.00 85.13           O  
ANISOU 4416  O   GLY B 176    13035  13864   5447   1435    704    530       O  
ATOM   4417  N   ASP B 177       7.138   7.595 -25.213  1.00 75.73           N  
ANISOU 4417  N   ASP B 177    11444  12312   5016   1059    915    671       N  
ATOM   4418  CA  ASP B 177       8.240   8.434 -25.653  1.00 76.76           C  
ANISOU 4418  CA  ASP B 177    11836  12237   5091   1075   1310    938       C  
ATOM   4419  C   ASP B 177       9.393   8.213 -24.668  1.00 77.89           C  
ANISOU 4419  C   ASP B 177    11713  12194   5689    771   1563    944       C  
ATOM   4420  O   ASP B 177       9.345   8.694 -23.532  1.00 75.16           O  
ANISOU 4420  O   ASP B 177    11160  11735   5663    639   1522    991       O  
ATOM   4421  CB  ASP B 177       7.807   9.903 -25.673  1.00 79.92           C  
ANISOU 4421  CB  ASP B 177    12474  12530   5361   1263   1317   1202       C  
ATOM   4422  CG  ASP B 177       8.927  10.845 -26.101  1.00 90.43           C  
ANISOU 4422  CG  ASP B 177    14117  13598   6644   1222   1776   1482       C  
ATOM   4423  OD1 ASP B 177      10.109  10.429 -26.092  1.00 89.59           O  
ANISOU 4423  OD1 ASP B 177    13915  13411   6715    992   2086   1463       O  
ATOM   4424  OD2 ASP B 177       8.621  12.012 -26.443  1.00 99.39           O  
ANISOU 4424  OD2 ASP B 177    15598  14607   7559   1424   1842   1719       O  
ATOM   4425  N   PRO B 178      10.426   7.464 -25.085  1.00 74.30           N  
ANISOU 4425  N   PRO B 178    11249  11733   5247    685   1814    880       N  
ATOM   4426  CA  PRO B 178      11.484   7.117 -24.128  1.00 71.48           C  
ANISOU 4426  CA  PRO B 178    10582  11274   5303    448   2003    845       C  
ATOM   4427  C   PRO B 178      12.334   8.274 -23.584  1.00 74.42           C  
ANISOU 4427  C   PRO B 178    10902  11471   5903    288   2281   1050       C  
ATOM   4428  O   PRO B 178      12.990   8.101 -22.559  1.00 71.92           O  
ANISOU 4428  O   PRO B 178    10267  11114   5946     99   2337    996       O  
ATOM   4429  CB  PRO B 178      12.358   6.116 -24.901  1.00 74.75           C  
ANISOU 4429  CB  PRO B 178    11041  11756   5604    472   2222    735       C  
ATOM   4430  CG  PRO B 178      11.917   6.184 -26.313  1.00 82.41           C  
ANISOU 4430  CG  PRO B 178    12394  12821   6095    688   2221    760       C  
ATOM   4431  CD  PRO B 178      10.523   6.683 -26.329  1.00 78.07           C  
ANISOU 4431  CD  PRO B 178    11948  12345   5369    825   1863    771       C  
ATOM   4432  N   THR B 179      12.324   9.431 -24.244  1.00 73.35           N  
ANISOU 4432  N   THR B 179    11092  11227   5549    359   2457   1271       N  
ATOM   4433  CA  THR B 179      13.132  10.578 -23.798  1.00 73.66           C  
ANISOU 4433  CA  THR B 179    11135  11059   5794    154   2766   1449       C  
ATOM   4434  C   THR B 179      12.416  11.483 -22.770  1.00 75.73           C  
ANISOU 4434  C   THR B 179    11357  11178   6239    115   2570   1515       C  
ATOM   4435  O   THR B 179      13.023  12.400 -22.217  1.00 75.63           O  
ANISOU 4435  O   THR B 179    11325  10975   6437    -96   2791   1616       O  
ATOM   4436  CB  THR B 179      13.616  11.428 -25.002  1.00 81.93           C  
ANISOU 4436  CB  THR B 179    12622  11986   6524    210   3151   1674       C  
ATOM   4437  OG1 THR B 179      12.490  11.982 -25.692  1.00 81.43           O  
ANISOU 4437  OG1 THR B 179    12968  11899   6071    519   2968   1806       O  
ATOM   4438  CG2 THR B 179      14.435  10.578 -25.970  1.00 81.05           C  
ANISOU 4438  CG2 THR B 179    12536  12018   6242    237   3397   1606       C  
ATOM   4439  N   VAL B 180      11.137  11.217 -22.516  1.00 70.55           N  
ANISOU 4439  N   VAL B 180    10677  10626   5503    303   2171   1436       N  
ATOM   4440  CA  VAL B 180      10.348  11.970 -21.541  1.00 68.78           C  
ANISOU 4440  CA  VAL B 180    10398  10305   5431    315   1965   1475       C  
ATOM   4441  C   VAL B 180      10.174  11.100 -20.305  1.00 69.34           C  
ANISOU 4441  C   VAL B 180    10030  10478   5839    171   1727   1264       C  
ATOM   4442  O   VAL B 180       9.722   9.962 -20.423  1.00 68.16           O  
ANISOU 4442  O   VAL B 180     9742  10515   5639    230   1521   1088       O  
ATOM   4443  CB  VAL B 180       8.947  12.312 -22.110  1.00 73.93           C  
ANISOU 4443  CB  VAL B 180    11301  11054   5736    665   1679   1527       C  
ATOM   4444  CG1 VAL B 180       8.067  12.947 -21.050  1.00 72.17           C  
ANISOU 4444  CG1 VAL B 180    10968  10775   5678    712   1450   1533       C  
ATOM   4445  CG2 VAL B 180       9.067  13.222 -23.323  1.00 77.87           C  
ANISOU 4445  CG2 VAL B 180    12308  11432   5846    874   1910   1768       C  
ATOM   4446  N   CYS B 181      10.529  11.623 -19.130  1.00 64.42           N  
ANISOU 4446  N   CYS B 181     9220   9720   5539    -24   1767   1274       N  
ATOM   4447  CA  CYS B 181      10.387  10.869 -17.881  1.00 61.26           C  
ANISOU 4447  CA  CYS B 181     8444   9400   5433   -138   1560   1099       C  
ATOM   4448  C   CYS B 181       9.442  11.567 -16.915  1.00 62.24           C  
ANISOU 4448  C   CYS B 181     8532   9455   5659   -100   1350   1117       C  
ATOM   4449  O   CYS B 181       9.811  12.534 -16.246  1.00 61.60           O  
ANISOU 4449  O   CYS B 181     8469   9195   5741   -223   1465   1194       O  
ATOM   4450  CB  CYS B 181      11.743  10.629 -17.212  1.00 61.55           C  
ANISOU 4450  CB  CYS B 181     8215   9409   5760   -384   1764   1041       C  
ATOM   4451  SG  CYS B 181      11.646   9.717 -15.617  1.00 62.41           S  
ANISOU 4451  SG  CYS B 181     7923   9603   6187   -472   1521    854       S  
ATOM   4452  N   SER B 182       8.217  11.049 -16.861  1.00 57.02           N  
ANISOU 4452  N   SER B 182     7815   8953   4898     60   1052   1021       N  
ATOM   4453  CA  SER B 182       7.173  11.531 -15.963  1.00 55.25           C  
ANISOU 4453  CA  SER B 182     7509   8729   4752    133    833   1006       C  
ATOM   4454  C   SER B 182       6.151  10.414 -15.799  1.00 57.16           C  
ANISOU 4454  C   SER B 182     7542   9207   4968    183    556    813       C  
ATOM   4455  O   SER B 182       6.150   9.464 -16.590  1.00 57.48           O  
ANISOU 4455  O   SER B 182     7591   9383   4867    197    528    711       O  
ATOM   4456  CB  SER B 182       6.492  12.757 -16.557  1.00 61.02           C  
ANISOU 4456  CB  SER B 182     8559   9387   5240    384    823   1176       C  
ATOM   4457  OG  SER B 182       5.954  12.445 -17.834  1.00 71.53           O  
ANISOU 4457  OG  SER B 182    10060  10896   6224    615    733   1180       O  
ATOM   4458  N   ILE B 183       5.288  10.528 -14.785  1.00 51.56           N  
ANISOU 4458  N   ILE B 183     6660   8542   4390    190    376    749       N  
ATOM   4459  CA  ILE B 183       4.174   9.582 -14.610  1.00 50.45           C  
ANISOU 4459  CA  ILE B 183     6315   8632   4223    204    136    556       C  
ATOM   4460  C   ILE B 183       3.055   9.961 -15.572  1.00 56.30           C  
ANISOU 4460  C   ILE B 183     7153   9585   4652    472    -47    551       C  
ATOM   4461  O   ILE B 183       2.282  10.885 -15.302  1.00 56.67           O  
ANISOU 4461  O   ILE B 183     7218   9667   4648    664   -150    619       O  
ATOM   4462  CB  ILE B 183       3.584   9.583 -13.192  1.00 51.56           C  
ANISOU 4462  CB  ILE B 183     6224   8773   4593    121     33    486       C  
ATOM   4463  CG1 ILE B 183       4.648   9.339 -12.129  1.00 49.56           C  
ANISOU 4463  CG1 ILE B 183     5881   8335   4614    -89    179    497       C  
ATOM   4464  CG2 ILE B 183       2.545   8.488 -13.066  1.00 52.53           C  
ANISOU 4464  CG2 ILE B 183     6136   9123   4702     61   -148    271       C  
ATOM   4465  CD1 ILE B 183       4.117   9.535 -10.733  1.00 52.61           C  
ANISOU 4465  CD1 ILE B 183     6103   8703   5184   -136     98    458       C  
ATOM   4466  N   SER B 184       2.981   9.251 -16.696  1.00 53.48           N  
ANISOU 4466  N   SER B 184     6869   9385   4068    515    -93    460       N  
ATOM   4467  CA  SER B 184       1.986   9.536 -17.724  1.00 55.63           C  
ANISOU 4467  CA  SER B 184     7232   9916   3991    797   -293    431       C  
ATOM   4468  C   SER B 184       0.776   8.597 -17.667  1.00 59.06           C  
ANISOU 4468  C   SER B 184     7369  10684   4388    745   -566    143       C  
ATOM   4469  O   SER B 184      -0.243   8.877 -18.298  1.00 61.25           O  
ANISOU 4469  O   SER B 184     7615  11257   4400    990   -793     75       O  
ATOM   4470  CB  SER B 184       2.630   9.504 -19.123  1.00 61.30           C  
ANISOU 4470  CB  SER B 184     8259  10623   4410    911   -175    510       C  
ATOM   4471  OG  SER B 184       3.451   8.367 -19.325  1.00 68.26           O  
ANISOU 4471  OG  SER B 184     9112  11450   5375    676    -44    393       O  
ATOM   4472  N   ASN B 185       0.871   7.498 -16.912  1.00 52.99           N  
ANISOU 4472  N   ASN B 185     6386   9877   3870    433   -538    -32       N  
ATOM   4473  CA  ASN B 185      -0.208   6.505 -16.900  1.00 53.32           C  
ANISOU 4473  CA  ASN B 185     6171  10200   3890    298   -739   -332       C  
ATOM   4474  C   ASN B 185      -1.487   7.050 -16.270  1.00 57.15           C  
ANISOU 4474  C   ASN B 185     6384  10928   4404    403   -938   -397       C  
ATOM   4475  O   ASN B 185      -1.463   7.526 -15.136  1.00 54.66           O  
ANISOU 4475  O   ASN B 185     5980  10468   4322    370   -867   -295       O  
ATOM   4476  CB  ASN B 185       0.206   5.214 -16.193  1.00 49.95           C  
ANISOU 4476  CB  ASN B 185     5653   9608   3717    -58   -612   -481       C  
ATOM   4477  CG  ASN B 185      -0.855   4.122 -16.312  1.00 61.84           C  
ANISOU 4477  CG  ASN B 185     6951  11358   5186   -265   -766   -815       C  
ATOM   4478  OD1 ASN B 185      -1.914   4.205 -15.698  1.00 55.94           O  
ANISOU 4478  OD1 ASN B 185     5931  10810   4515   -319   -897   -933       O  
ATOM   4479  ND2 ASN B 185      -0.567   3.096 -17.103  1.00 50.75           N  
ANISOU 4479  ND2 ASN B 185     5676   9941   3666   -397   -731   -984       N  
ATOM   4480  N   PRO B 186      -2.607   6.976 -17.003  1.00 56.20           N  
ANISOU 4480  N   PRO B 186     6112  11208   4033    545  -1193   -584       N  
ATOM   4481  CA  PRO B 186      -3.894   7.459 -16.521  1.00 57.39           C  
ANISOU 4481  CA  PRO B 186     5949  11677   4180    686  -1397   -680       C  
ATOM   4482  C   PRO B 186      -4.444   6.713 -15.308  1.00 60.33           C  
ANISOU 4482  C   PRO B 186     5982  12078   4861    338  -1364   -872       C  
ATOM   4483  O   PRO B 186      -5.097   7.323 -14.467  1.00 60.39           O  
ANISOU 4483  O   PRO B 186     5788  12178   4977    436  -1405   -843       O  
ATOM   4484  CB  PRO B 186      -4.824   7.232 -17.712  1.00 63.41           C  
ANISOU 4484  CB  PRO B 186     6593  12912   4589    856  -1682   -907       C  
ATOM   4485  CG  PRO B 186      -3.948   7.164 -18.875  1.00 68.94           C  
ANISOU 4485  CG  PRO B 186     7670  13480   5044    957  -1615   -805       C  
ATOM   4486  CD  PRO B 186      -2.694   6.535 -18.402  1.00 61.00           C  
ANISOU 4486  CD  PRO B 186     6842  12028   4307    632  -1313   -716       C  
ATOM   4487  N   ASP B 187      -4.205   5.410 -15.221  1.00 55.70           N  
ANISOU 4487  N   ASP B 187     5365  11402   4398    -50  -1270  -1066       N  
ATOM   4488  CA  ASP B 187      -4.706   4.633 -14.087  1.00 54.25           C  
ANISOU 4488  CA  ASP B 187     4927  11201   4486   -401  -1190  -1236       C  
ATOM   4489  C   ASP B 187      -3.857   4.880 -12.840  1.00 53.24           C  
ANISOU 4489  C   ASP B 187     4927  10667   4634   -464   -959   -999       C  
ATOM   4490  O   ASP B 187      -4.398   5.167 -11.779  1.00 51.96           O  
ANISOU 4490  O   ASP B 187     4573  10537   4632   -496   -937   -993       O  
ATOM   4491  CB  ASP B 187      -4.786   3.142 -14.441  1.00 57.39           C  
ANISOU 4491  CB  ASP B 187     5312  11598   4895   -792  -1146  -1530       C  
ATOM   4492  CG  ASP B 187      -5.759   2.869 -15.583  1.00 72.11           C  
ANISOU 4492  CG  ASP B 187     6986  13926   6485   -776  -1406  -1834       C  
ATOM   4493  OD1 ASP B 187      -6.789   3.571 -15.639  1.00 75.03           O  
ANISOU 4493  OD1 ASP B 187     7053  14705   6749   -568  -1623  -1905       O  
ATOM   4494  OD2 ASP B 187      -5.499   1.972 -16.422  1.00 79.26           O  
ANISOU 4494  OD2 ASP B 187     8041  14809   7267   -946  -1403  -2015       O  
ATOM   4495  N   PHE B 188      -2.537   4.813 -12.970  1.00 47.23           N  
ANISOU 4495  N   PHE B 188     4472   9561   3910   -460   -794   -816       N  
ATOM   4496  CA  PHE B 188      -1.661   5.051 -11.827  1.00 43.80           C  
ANISOU 4496  CA  PHE B 188     4138   8792   3713   -506   -605   -618       C  
ATOM   4497  C   PHE B 188      -1.825   6.433 -11.208  1.00 46.57           C  
ANISOU 4497  C   PHE B 188     4454   9139   4104   -266   -637   -431       C  
ATOM   4498  O   PHE B 188      -1.740   6.573  -9.995  1.00 44.28           O  
ANISOU 4498  O   PHE B 188     4106   8710   4008   -340   -549   -375       O  
ATOM   4499  CB  PHE B 188      -0.204   4.887 -12.212  1.00 44.21           C  
ANISOU 4499  CB  PHE B 188     4470   8558   3770   -496   -444   -470       C  
ATOM   4500  CG  PHE B 188       0.724   4.964 -11.050  1.00 43.34           C  
ANISOU 4500  CG  PHE B 188     4416   8163   3889   -560   -277   -321       C  
ATOM   4501  CD1 PHE B 188       1.054   3.814 -10.337  1.00 45.98           C  
ANISOU 4501  CD1 PHE B 188     4764   8336   4369   -773   -156   -399       C  
ATOM   4502  CD2 PHE B 188       1.254   6.183 -10.645  1.00 44.40           C  
ANISOU 4502  CD2 PHE B 188     4607   8188   4077   -402   -240   -115       C  
ATOM   4503  CE1 PHE B 188       1.910   3.882  -9.237  1.00 45.01           C  
ANISOU 4503  CE1 PHE B 188     4685   7996   4422   -784    -33   -270       C  
ATOM   4504  CE2 PHE B 188       2.107   6.260  -9.543  1.00 45.32           C  
ANISOU 4504  CE2 PHE B 188     4741   8088   4389   -470   -116    -17       C  
ATOM   4505  CZ  PHE B 188       2.436   5.114  -8.841  1.00 42.64           C  
ANISOU 4505  CZ  PHE B 188     4389   7641   4174   -639    -29    -92       C  
ATOM   4506  N   VAL B 189      -2.024   7.456 -12.033  1.00 44.60           N  
ANISOU 4506  N   VAL B 189     4286   9012   3648     40   -749   -330       N  
ATOM   4507  CA  VAL B 189      -2.229   8.812 -11.516  1.00 43.69           C  
ANISOU 4507  CA  VAL B 189     4201   8856   3544    298   -765   -157       C  
ATOM   4508  C   VAL B 189      -3.439   8.874 -10.559  1.00 47.43           C  
ANISOU 4508  C   VAL B 189     4359   9547   4115    295   -854   -286       C  
ATOM   4509  O   VAL B 189      -3.332   9.440  -9.471  1.00 45.54           O  
ANISOU 4509  O   VAL B 189     4122   9149   4034    312   -768   -189       O  
ATOM   4510  CB  VAL B 189      -2.378   9.853 -12.657  1.00 49.68           C  
ANISOU 4510  CB  VAL B 189     5154   9709   4013    673   -865    -26       C  
ATOM   4511  CG1 VAL B 189      -2.883  11.175 -12.112  1.00 50.23           C  
ANISOU 4511  CG1 VAL B 189     5253   9761   4071    971   -898    110       C  
ATOM   4512  CG2 VAL B 189      -1.059  10.059 -13.373  1.00 48.68           C  
ANISOU 4512  CG2 VAL B 189     5374   9301   3823    672   -697    155       C  
ATOM   4513  N   ILE B 190      -4.567   8.272 -10.943  1.00 46.19           N  
ANISOU 4513  N   ILE B 190     3919   9768   3864    251  -1013   -525       N  
ATOM   4514  CA  ILE B 190      -5.756   8.241 -10.073  1.00 47.10           C  
ANISOU 4514  CA  ILE B 190     3679  10143   4075    212  -1068   -680       C  
ATOM   4515  C   ILE B 190      -5.430   7.483  -8.794  1.00 49.19           C  
ANISOU 4515  C   ILE B 190     3910  10168   4612   -141   -864   -706       C  
ATOM   4516  O   ILE B 190      -5.781   7.909  -7.690  1.00 48.97           O  
ANISOU 4516  O   ILE B 190     3778  10118   4711   -113   -801   -669       O  
ATOM   4517  CB  ILE B 190      -6.972   7.515 -10.692  1.00 53.49           C  
ANISOU 4517  CB  ILE B 190     4128  11431   4764    117  -1250   -996       C  
ATOM   4518  CG1 ILE B 190      -7.384   8.112 -12.037  1.00 56.93           C  
ANISOU 4518  CG1 ILE B 190     4575  12183   4872    492  -1496  -1010       C  
ATOM   4519  CG2 ILE B 190      -8.148   7.572  -9.735  1.00 55.35           C  
ANISOU 4519  CG2 ILE B 190     3967  11947   5116     72  -1265  -1149       C  
ATOM   4520  CD1 ILE B 190      -8.206   7.137 -12.882  1.00 67.89           C  
ANISOU 4520  CD1 ILE B 190     5676  14001   6119    312  -1677  -1358       C  
ATOM   4521  N   TYR B 191      -4.772   6.342  -8.952  1.00 43.70           N  
ANISOU 4521  N   TYR B 191     3331   9292   3981   -444   -756   -770       N  
ATOM   4522  CA  TYR B 191      -4.389   5.536  -7.805  1.00 40.86           C  
ANISOU 4522  CA  TYR B 191     3009   8678   3836   -736   -555   -775       C  
ATOM   4523  C   TYR B 191      -3.420   6.284  -6.910  1.00 41.61           C  
ANISOU 4523  C   TYR B 191     3305   8461   4044   -612   -445   -529       C  
ATOM   4524  O   TYR B 191      -3.517   6.212  -5.696  1.00 40.66           O  
ANISOU 4524  O   TYR B 191     3142   8245   4061   -700   -339   -511       O  
ATOM   4525  CB  TYR B 191      -3.787   4.206  -8.245  1.00 41.26           C  
ANISOU 4525  CB  TYR B 191     3217   8561   3900  -1012   -454   -871       C  
ATOM   4526  CG  TYR B 191      -2.808   3.644  -7.259  1.00 39.79           C  
ANISOU 4526  CG  TYR B 191     3239   8001   3877  -1147   -246   -753       C  
ATOM   4527  CD1 TYR B 191      -3.240   3.042  -6.090  1.00 41.47           C  
ANISOU 4527  CD1 TYR B 191     3388   8143   4226  -1356   -107   -813       C  
ATOM   4528  CD2 TYR B 191      -1.442   3.727  -7.494  1.00 38.55           C  
ANISOU 4528  CD2 TYR B 191     3338   7587   3720  -1045   -183   -582       C  
ATOM   4529  CE1 TYR B 191      -2.342   2.539  -5.186  1.00 39.77           C  
ANISOU 4529  CE1 TYR B 191     3392   7604   4114  -1416     65   -692       C  
ATOM   4530  CE2 TYR B 191      -0.539   3.224  -6.603  1.00 37.72           C  
ANISOU 4530  CE2 TYR B 191     3392   7201   3738  -1113    -25   -487       C  
ATOM   4531  CZ  TYR B 191      -0.989   2.633  -5.447  1.00 43.80           C  
ANISOU 4531  CZ  TYR B 191     4129   7900   4615  -1276     86   -535       C  
ATOM   4532  OH  TYR B 191      -0.072   2.134  -4.557  1.00 42.41           O  
ANISOU 4532  OH  TYR B 191     4141   7457   4518  -1283    226   -428       O  
ATOM   4533  N   SER B 192      -2.486   7.012  -7.487  1.00 37.09           N  
ANISOU 4533  N   SER B 192     2952   7736   3404   -423   -458   -354       N  
ATOM   4534  CA  SER B 192      -1.559   7.720  -6.640  1.00 35.40           C  
ANISOU 4534  CA  SER B 192     2896   7250   3303   -357   -357   -169       C  
ATOM   4535  C   SER B 192      -2.233   8.923  -6.000  1.00 41.98           C  
ANISOU 4535  C   SER B 192     3658   8153   4139   -147   -408   -112       C  
ATOM   4536  O   SER B 192      -2.030   9.171  -4.818  1.00 40.53           O  
ANISOU 4536  O   SER B 192     3488   7831   4081   -181   -327    -66       O  
ATOM   4537  CB  SER B 192      -0.287   8.129  -7.378  1.00 38.13           C  
ANISOU 4537  CB  SER B 192     3485   7401   3602   -281   -307    -18       C  
ATOM   4538  OG  SER B 192       0.714   8.485  -6.430  1.00 46.64           O  
ANISOU 4538  OG  SER B 192     4661   8236   4824   -320   -195     96       O  
ATOM   4539  N   SER B 193      -3.054   9.658  -6.744  1.00 41.93           N  
ANISOU 4539  N   SER B 193     3589   8368   3976    102   -545   -122       N  
ATOM   4540  CA  SER B 193      -3.675  10.871  -6.170  1.00 43.17           C  
ANISOU 4540  CA  SER B 193     3722   8565   4115    369   -581    -58       C  
ATOM   4541  C   SER B 193      -4.567  10.568  -4.957  1.00 47.72           C  
ANISOU 4541  C   SER B 193     4038   9282   4810    275   -547   -182       C  
ATOM   4542  O   SER B 193      -4.596  11.327  -3.984  1.00 46.81           O  
ANISOU 4542  O   SER B 193     3973   9051   4760    382   -488   -115       O  
ATOM   4543  CB  SER B 193      -4.446  11.672  -7.223  1.00 49.56           C  
ANISOU 4543  CB  SER B 193     4525   9611   4695    727   -743    -41       C  
ATOM   4544  OG  SER B 193      -5.280  10.839  -7.996  1.00 60.71           O  
ANISOU 4544  OG  SER B 193     5679  11392   5997    677   -884   -235       O  
ATOM   4545  N   VAL B 194      -5.277   9.449  -5.009  1.00 45.73           N  
ANISOU 4545  N   VAL B 194     3529   9266   4581     52   -561   -375       N  
ATOM   4546  CA  VAL B 194      -6.013   8.970  -3.839  1.00 46.03           C  
ANISOU 4546  CA  VAL B 194     3346   9403   4742   -119   -461   -493       C  
ATOM   4547  C   VAL B 194      -5.058   8.556  -2.708  1.00 47.72           C  
ANISOU 4547  C   VAL B 194     3763   9266   5104   -318   -280   -398       C  
ATOM   4548  O   VAL B 194      -5.028   9.187  -1.646  1.00 46.58           O  
ANISOU 4548  O   VAL B 194     3665   9018   5013   -226   -214   -328       O  
ATOM   4549  CB  VAL B 194      -6.951   7.795  -4.206  1.00 51.88           C  
ANISOU 4549  CB  VAL B 194     3784  10449   5478   -388   -476   -744       C  
ATOM   4550  CG1 VAL B 194      -7.144   6.848  -3.022  1.00 51.21           C  
ANISOU 4550  CG1 VAL B 194     3637  10272   5549   -725   -264   -825       C  
ATOM   4551  CG2 VAL B 194      -8.284   8.341  -4.693  1.00 55.10           C  
ANISOU 4551  CG2 VAL B 194     3843  11328   5765   -161   -647   -890       C  
ATOM   4552  N   VAL B 195      -4.261   7.521  -2.960  1.00 42.89           N  
ANISOU 4552  N   VAL B 195     3286   8480   4530   -552   -211   -401       N  
ATOM   4553  CA  VAL B 195      -3.516   6.849  -1.905  1.00 40.54           C  
ANISOU 4553  CA  VAL B 195     3145   7917   4340   -728    -50   -346       C  
ATOM   4554  C   VAL B 195      -2.280   7.632  -1.423  1.00 41.68           C  
ANISOU 4554  C   VAL B 195     3518   7801   4516   -587    -41   -168       C  
ATOM   4555  O   VAL B 195      -1.797   7.389  -0.320  1.00 39.67           O  
ANISOU 4555  O   VAL B 195     3360   7389   4323   -646     55   -124       O  
ATOM   4556  CB  VAL B 195      -3.103   5.435  -2.364  1.00 44.04           C  
ANISOU 4556  CB  VAL B 195     3680   8259   4796   -981     28   -417       C  
ATOM   4557  CG1 VAL B 195      -1.635   5.422  -2.774  1.00 41.86           C  
ANISOU 4557  CG1 VAL B 195     3649   7741   4514   -915     27   -281       C  
ATOM   4558  CG2 VAL B 195      -3.384   4.409  -1.268  1.00 44.31           C  
ANISOU 4558  CG2 VAL B 195     3742   8191   4903  -1215    219   -472       C  
ATOM   4559  N   SER B 196      -1.775   8.559  -2.241  1.00 38.57           N  
ANISOU 4559  N   SER B 196     3217   7371   4068   -413   -132    -79       N  
ATOM   4560  CA  SER B 196      -0.638   9.416  -1.850  1.00 37.40           C  
ANISOU 4560  CA  SER B 196     3259   6993   3959   -329   -109     54       C  
ATOM   4561  C   SER B 196      -1.311  10.555  -1.078  1.00 43.52           C  
ANISOU 4561  C   SER B 196     4011   7795   4730   -156   -128     67       C  
ATOM   4562  O   SER B 196      -1.098  10.677   0.129  1.00 44.33           O  
ANISOU 4562  O   SER B 196     4152   7800   4891   -185    -69     70       O  
ATOM   4563  CB  SER B 196       0.408   9.522  -2.974  1.00 40.44           C  
ANISOU 4563  CB  SER B 196     3782   7275   4308   -322   -118    131       C  
ATOM   4564  OG  SER B 196       1.081   8.305  -3.180  1.00 49.19           O  
ANISOU 4564  OG  SER B 196     4912   8333   5444   -481    -62    101       O  
ATOM   4565  N   PHE B 197      -2.110  11.387  -1.730  1.00 41.01           N  
ANISOU 4565  N   PHE B 197     3653   7610   4320     56   -208     71       N  
ATOM   4566  CA  PHE B 197      -2.688  12.524  -1.021  1.00 41.89           C  
ANISOU 4566  CA  PHE B 197     3788   7714   4415    270   -210     89       C  
ATOM   4567  C   PHE B 197      -4.089  12.706  -0.425  1.00 47.68           C  
ANISOU 4567  C   PHE B 197     4302   8695   5121    412   -221     -8       C  
ATOM   4568  O   PHE B 197      -4.226  12.963   0.776  1.00 46.91           O  
ANISOU 4568  O   PHE B 197     4216   8536   5073    419   -144    -26       O  
ATOM   4569  CB  PHE B 197      -2.536  13.369  -2.290  1.00 44.89           C  
ANISOU 4569  CB  PHE B 197     4322   8056   4677    475   -279    184       C  
ATOM   4570  CG  PHE B 197      -2.652  14.837  -2.061  1.00 47.87           C  
ANISOU 4570  CG  PHE B 197     4905   8279   5003    743   -264    268       C  
ATOM   4571  CD1 PHE B 197      -1.565  15.564  -1.601  1.00 50.20           C  
ANISOU 4571  CD1 PHE B 197     5467   8241   5368    666   -169    343       C  
ATOM   4572  CD2 PHE B 197      -3.840  15.498  -2.326  1.00 52.59           C  
ANISOU 4572  CD2 PHE B 197     5436   9070   5475   1077   -341    255       C  
ATOM   4573  CE1 PHE B 197      -1.659  16.931  -1.397  1.00 52.67           C  
ANISOU 4573  CE1 PHE B 197     6029   8353   5631    885   -127    406       C  
ATOM   4574  CE2 PHE B 197      -3.946  16.861  -2.127  1.00 57.03           C  
ANISOU 4574  CE2 PHE B 197     6253   9444   5973   1364   -307    341       C  
ATOM   4575  CZ  PHE B 197      -2.850  17.583  -1.658  1.00 54.20           C  
ANISOU 4575  CZ  PHE B 197     6215   8689   5690   1250   -186    418       C  
ATOM   4576  N   TYR B 198      -5.124  12.543  -1.241  1.00 46.06           N  
ANISOU 4576  N   TYR B 198     3875   8799   4825    525   -317    -88       N  
ATOM   4577  CA  TYR B 198      -6.454  12.912  -0.811  1.00 48.20           C  
ANISOU 4577  CA  TYR B 198     3900   9358   5057    722   -337   -186       C  
ATOM   4578  C   TYR B 198      -6.977  12.092   0.368  1.00 51.92           C  
ANISOU 4578  C   TYR B 198     4162   9933   5630    489   -203   -305       C  
ATOM   4579  O   TYR B 198      -7.614  12.639   1.265  1.00 52.73           O  
ANISOU 4579  O   TYR B 198     4191  10109   5734    637   -139   -335       O  
ATOM   4580  CB  TYR B 198      -7.454  12.755  -1.949  1.00 51.97           C  
ANISOU 4580  CB  TYR B 198     4110  10229   5408    868   -491   -292       C  
ATOM   4581  CG  TYR B 198      -7.227  13.758  -3.060  1.00 55.09           C  
ANISOU 4581  CG  TYR B 198     4728  10566   5637   1217   -618   -161       C  
ATOM   4582  CD1 TYR B 198      -7.252  15.125  -2.806  1.00 57.94           C  
ANISOU 4582  CD1 TYR B 198     5324  10762   5929   1580   -606    -36       C  
ATOM   4583  CD2 TYR B 198      -6.993  13.342  -4.365  1.00 56.58           C  
ANISOU 4583  CD2 TYR B 198     4941  10840   5716   1192   -728   -160       C  
ATOM   4584  CE1 TYR B 198      -7.043  16.048  -3.813  1.00 60.05           C  
ANISOU 4584  CE1 TYR B 198     5869  10924   6024   1905   -681    106       C  
ATOM   4585  CE2 TYR B 198      -6.787  14.263  -5.384  1.00 58.87           C  
ANISOU 4585  CE2 TYR B 198     5486  11062   5819   1528   -817    -19       C  
ATOM   4586  CZ  TYR B 198      -6.812  15.613  -5.097  1.00 66.75           C  
ANISOU 4586  CZ  TYR B 198     6740  11870   6752   1883   -783    124       C  
ATOM   4587  OH  TYR B 198      -6.603  16.521  -6.105  1.00 70.00           O  
ANISOU 4587  OH  TYR B 198     7473  12164   6959   2220   -832    285       O  
ATOM   4588  N   LEU B 199      -6.687  10.796   0.381  1.00 46.97           N  
ANISOU 4588  N   LEU B 199     3484   9285   5076    137   -133   -364       N  
ATOM   4589  CA  LEU B 199      -7.124   9.921   1.469  1.00 46.78           C  
ANISOU 4589  CA  LEU B 199     3335   9306   5131   -112     41   -455       C  
ATOM   4590  C   LEU B 199      -6.374  10.298   2.775  1.00 50.12           C  
ANISOU 4590  C   LEU B 199     4019   9432   5590    -88    152   -342       C  
ATOM   4591  O   LEU B 199      -7.010  10.677   3.762  1.00 50.93           O  
ANISOU 4591  O   LEU B 199     4052   9611   5686      0    246   -377       O  
ATOM   4592  CB  LEU B 199      -6.941   8.442   1.076  1.00 46.27           C  
ANISOU 4592  CB  LEU B 199     3241   9226   5114   -479    107   -535       C  
ATOM   4593  CG  LEU B 199      -6.933   7.351   2.148  1.00 50.56           C  
ANISOU 4593  CG  LEU B 199     3839   9644   5727   -780    335   -565       C  
ATOM   4594  CD1 LEU B 199      -8.080   7.534   3.110  1.00 53.15           C  
ANISOU 4594  CD1 LEU B 199     3940  10188   6066   -777    471   -658       C  
ATOM   4595  CD2 LEU B 199      -6.987   5.971   1.529  1.00 52.73           C  
ANISOU 4595  CD2 LEU B 199     4086   9918   6030  -1116    402   -676       C  
ATOM   4596  N   PRO B 200      -5.028  10.228   2.787  1.00 44.99           N  
ANISOU 4596  N   PRO B 200     3652   8477   4964   -149    136   -226       N  
ATOM   4597  CA  PRO B 200      -4.325  10.570   4.024  1.00 43.83           C  
ANISOU 4597  CA  PRO B 200     3718   8108   4829   -124    207   -158       C  
ATOM   4598  C   PRO B 200      -4.428  12.033   4.438  1.00 49.16           C  
ANISOU 4598  C   PRO B 200     4486   8728   5465    146    164   -131       C  
ATOM   4599  O   PRO B 200      -4.307  12.330   5.627  1.00 49.39           O  
ANISOU 4599  O   PRO B 200     4624   8665   5479    180    237   -134       O  
ATOM   4600  CB  PRO B 200      -2.870  10.217   3.716  1.00 43.52           C  
ANISOU 4600  CB  PRO B 200     3886   7831   4817   -229    164    -72       C  
ATOM   4601  CG  PRO B 200      -2.770  10.240   2.254  1.00 47.81           C  
ANISOU 4601  CG  PRO B 200     4384   8429   5354   -216     64    -61       C  
ATOM   4602  CD  PRO B 200      -4.090   9.746   1.758  1.00 45.28           C  
ANISOU 4602  CD  PRO B 200     3802   8392   5009   -252     65   -176       C  
ATOM   4603  N   PHE B 201      -4.624  12.944   3.489  1.00 46.42           N  
ANISOU 4603  N   PHE B 201     4143   8413   5080    353     57   -103       N  
ATOM   4604  CA  PHE B 201      -4.929  14.338   3.851  1.00 47.28           C  
ANISOU 4604  CA  PHE B 201     4372   8456   5136    646     47    -86       C  
ATOM   4605  C   PHE B 201      -6.368  14.432   4.391  1.00 51.61           C  
ANISOU 4605  C   PHE B 201     4670   9295   5644    809    106   -186       C  
ATOM   4606  O   PHE B 201      -6.657  15.227   5.284  1.00 52.59           O  
ANISOU 4606  O   PHE B 201     4884   9364   5732    991    168   -203       O  
ATOM   4607  CB  PHE B 201      -4.662  15.304   2.674  1.00 50.06           C  
ANISOU 4607  CB  PHE B 201     4884   8704   5432    851    -53      1       C  
ATOM   4608  CG  PHE B 201      -5.772  16.283   2.409  1.00 54.70           C  
ANISOU 4608  CG  PHE B 201     5427   9442   5916   1236    -91    -10       C  
ATOM   4609  CD1 PHE B 201      -5.931  17.408   3.201  1.00 59.26           C  
ANISOU 4609  CD1 PHE B 201     6200   9859   6457   1467    -31     -5       C  
ATOM   4610  CD2 PHE B 201      -6.651  16.082   1.355  1.00 58.83           C  
ANISOU 4610  CD2 PHE B 201     5718  10278   6356   1394   -195    -39       C  
ATOM   4611  CE1 PHE B 201      -6.965  18.310   2.959  1.00 63.21           C  
ANISOU 4611  CE1 PHE B 201     6679  10495   6843   1888    -59     -9       C  
ATOM   4612  CE2 PHE B 201      -7.688  16.983   1.101  1.00 64.81           C  
ANISOU 4612  CE2 PHE B 201     6414  11220   6990   1821   -251    -50       C  
ATOM   4613  CZ  PHE B 201      -7.844  18.096   1.905  1.00 64.14           C  
ANISOU 4613  CZ  PHE B 201     6541  10958   6873   2085   -175    -25       C  
ATOM   4614  N   GLY B 202      -7.262  13.604   3.868  1.00 47.62           N  
ANISOU 4614  N   GLY B 202     3839   9113   5142    727     98   -275       N  
ATOM   4615  CA  GLY B 202      -8.606  13.536   4.395  1.00 49.40           C  
ANISOU 4615  CA  GLY B 202     3752   9671   5348    816    180   -400       C  
ATOM   4616  C   GLY B 202      -8.590  13.118   5.850  1.00 51.67           C  
ANISOU 4616  C   GLY B 202     4089   9875   5667    652    376   -425       C  
ATOM   4617  O   GLY B 202      -9.114  13.824   6.714  1.00 52.80           O  
ANISOU 4617  O   GLY B 202     4237  10061   5765    859    460   -455       O  
ATOM   4618  N   VAL B 203      -7.969  11.974   6.120  1.00 45.72           N  
ANISOU 4618  N   VAL B 203     3412   8992   4968    312    457   -406       N  
ATOM   4619  CA  VAL B 203      -7.952  11.409   7.468  1.00 45.28           C  
ANISOU 4619  CA  VAL B 203     3441   8858   4905    156    658   -412       C  
ATOM   4620  C   VAL B 203      -7.385  12.411   8.467  1.00 48.95           C  
ANISOU 4620  C   VAL B 203     4192   9101   5305    362    658   -354       C  
ATOM   4621  O   VAL B 203      -7.905  12.574   9.573  1.00 50.36           O  
ANISOU 4621  O   VAL B 203     4377   9334   5426    428    808   -394       O  
ATOM   4622  CB  VAL B 203      -7.127  10.116   7.534  1.00 47.16           C  
ANISOU 4622  CB  VAL B 203     3830   8910   5177   -164    722   -360       C  
ATOM   4623  CG1 VAL B 203      -7.046   9.609   8.956  1.00 47.26           C  
ANISOU 4623  CG1 VAL B 203     4010   8814   5133   -258    927   -335       C  
ATOM   4624  CG2 VAL B 203      -7.739   9.070   6.641  1.00 47.89           C  
ANISOU 4624  CG2 VAL B 203     3676   9192   5328   -410    755   -452       C  
ATOM   4625  N   THR B 204      -6.322  13.092   8.067  1.00 43.53           N  
ANISOU 4625  N   THR B 204     3745   8171   4623    446    504   -276       N  
ATOM   4626  CA  THR B 204      -5.670  14.049   8.941  1.00 43.06           C  
ANISOU 4626  CA  THR B 204     3969   7884   4509    585    490   -258       C  
ATOM   4627  C   THR B 204      -6.612  15.209   9.287  1.00 48.96           C  
ANISOU 4627  C   THR B 204     4692   8717   5193    901    529   -317       C  
ATOM   4628  O   THR B 204      -6.700  15.603  10.443  1.00 49.04           O  
ANISOU 4628  O   THR B 204     4835   8668   5128    988    623   -359       O  
ATOM   4629  CB  THR B 204      -4.342  14.530   8.322  1.00 48.94           C  
ANISOU 4629  CB  THR B 204     4936   8367   5291    549    341   -191       C  
ATOM   4630  OG1 THR B 204      -3.538  13.387   8.020  1.00 45.64           O  
ANISOU 4630  OG1 THR B 204     4508   7912   4921    301    318   -145       O  
ATOM   4631  CG2 THR B 204      -3.580  15.416   9.275  1.00 48.11           C  
ANISOU 4631  CG2 THR B 204     5109   8035   5137    611    326   -217       C  
ATOM   4632  N   VAL B 205      -7.343  15.730   8.309  1.00 46.73           N  
ANISOU 4632  N   VAL B 205     4251   8590   4915   1107    460   -325       N  
ATOM   4633  CA  VAL B 205      -8.304  16.795   8.598  1.00 49.11           C  
ANISOU 4633  CA  VAL B 205     4522   8998   5140   1476    501   -379       C  
ATOM   4634  C   VAL B 205      -9.420  16.315   9.546  1.00 55.38           C  
ANISOU 4634  C   VAL B 205     5048  10091   5903   1481    687   -482       C  
ATOM   4635  O   VAL B 205      -9.801  17.045  10.456  1.00 56.38           O  
ANISOU 4635  O   VAL B 205     5276  10196   5951   1704    787   -530       O  
ATOM   4636  CB  VAL B 205      -8.893  17.413   7.315  1.00 54.32           C  
ANISOU 4636  CB  VAL B 205     5065   9802   5772   1764    374   -357       C  
ATOM   4637  CG1 VAL B 205     -10.081  18.297   7.647  1.00 57.58           C  
ANISOU 4637  CG1 VAL B 205     5367  10418   6093   2190    431   -428       C  
ATOM   4638  CG2 VAL B 205      -7.835  18.220   6.594  1.00 52.92           C  
ANISOU 4638  CG2 VAL B 205     5257   9260   5589   1820    261   -244       C  
ATOM   4639  N   LEU B 206      -9.920  15.092   9.355  1.00 52.86           N  
ANISOU 4639  N   LEU B 206     4412  10031   5641   1216    759   -527       N  
ATOM   4640  CA  LEU B 206     -10.901  14.506  10.293  1.00 55.12           C  
ANISOU 4640  CA  LEU B 206     4456  10578   5908   1129    994   -626       C  
ATOM   4641  C   LEU B 206     -10.360  14.493  11.712  1.00 58.34           C  
ANISOU 4641  C   LEU B 206     5180  10748   6239   1070   1142   -594       C  
ATOM   4642  O   LEU B 206     -11.058  14.860  12.654  1.00 60.20           O  
ANISOU 4642  O   LEU B 206     5382  11098   6393   1227   1313   -659       O  
ATOM   4643  CB  LEU B 206     -11.250  13.064   9.922  1.00 55.38           C  
ANISOU 4643  CB  LEU B 206     4206  10810   6024    738   1084   -676       C  
ATOM   4644  CG  LEU B 206     -12.000  12.832   8.616  1.00 61.64           C  
ANISOU 4644  CG  LEU B 206     4600  11946   6875    733    960   -769       C  
ATOM   4645  CD1 LEU B 206     -12.010  11.339   8.291  1.00 61.65           C  
ANISOU 4645  CD1 LEU B 206     4454  12008   6961    263   1052   -821       C  
ATOM   4646  CD2 LEU B 206     -13.418  13.401   8.710  1.00 68.25           C  
ANISOU 4646  CD2 LEU B 206     5030  13227   7674   1013   1021   -915       C  
ATOM   4647  N   VAL B 207      -9.115  14.042  11.843  1.00 52.06           N  
ANISOU 4647  N   VAL B 207     4677   9651   5451    862   1073   -502       N  
ATOM   4648  CA  VAL B 207      -8.426  13.964  13.123  1.00 51.31           C  
ANISOU 4648  CA  VAL B 207     4902   9342   5251    816   1158   -472       C  
ATOM   4649  C   VAL B 207      -8.323  15.338  13.774  1.00 56.65           C  
ANISOU 4649  C   VAL B 207     5808   9887   5830   1123   1121   -517       C  
ATOM   4650  O   VAL B 207      -8.740  15.517  14.912  1.00 58.12           O  
ANISOU 4650  O   VAL B 207     6076  10112   5896   1223   1285   -570       O  
ATOM   4651  CB  VAL B 207      -7.010  13.356  12.946  1.00 52.23           C  
ANISOU 4651  CB  VAL B 207     5254   9202   5390    605   1025   -379       C  
ATOM   4652  CG1 VAL B 207      -6.139  13.609  14.167  1.00 51.70           C  
ANISOU 4652  CG1 VAL B 207     5527   8933   5186    649   1019   -372       C  
ATOM   4653  CG2 VAL B 207      -7.114  11.868  12.650  1.00 51.64           C  
ANISOU 4653  CG2 VAL B 207     5052   9200   5368    307   1131   -339       C  
ATOM   4654  N   TYR B 208      -7.782  16.308  13.047  1.00 53.00           N  
ANISOU 4654  N   TYR B 208     5480   9248   5409   1266    931   -502       N  
ATOM   4655  CA  TYR B 208      -7.645  17.670  13.572  1.00 54.52           C  
ANISOU 4655  CA  TYR B 208     5950   9250   5516   1536    908   -559       C  
ATOM   4656  C   TYR B 208      -9.004  18.330  13.818  1.00 61.81           C  
ANISOU 4656  C   TYR B 208     6719  10389   6376   1875   1044   -635       C  
ATOM   4657  O   TYR B 208      -9.105  19.262  14.616  1.00 63.03           O  
ANISOU 4657  O   TYR B 208     7109  10419   6422   2106   1105   -706       O  
ATOM   4658  CB  TYR B 208      -6.789  18.538  12.639  1.00 55.11           C  
ANISOU 4658  CB  TYR B 208     6231   9053   5655   1578    722   -519       C  
ATOM   4659  CG  TYR B 208      -5.302  18.353  12.839  1.00 55.37           C  
ANISOU 4659  CG  TYR B 208     6497   8833   5708   1314    609   -504       C  
ATOM   4660  CD1 TYR B 208      -4.629  19.021  13.857  1.00 58.28           C  
ANISOU 4660  CD1 TYR B 208     7169   8991   5982   1323    597   -598       C  
ATOM   4661  CD2 TYR B 208      -4.566  17.511  12.016  1.00 53.98           C  
ANISOU 4661  CD2 TYR B 208     6220   8656   5634   1067    510   -421       C  
ATOM   4662  CE1 TYR B 208      -3.250  18.853  14.051  1.00 58.05           C  
ANISOU 4662  CE1 TYR B 208     7291   8801   5966   1085    471   -619       C  
ATOM   4663  CE2 TYR B 208      -3.189  17.334  12.201  1.00 53.56           C  
ANISOU 4663  CE2 TYR B 208     6329   8426   5597    856    404   -422       C  
ATOM   4664  CZ  TYR B 208      -2.537  18.005  13.220  1.00 62.20           C  
ANISOU 4664  CZ  TYR B 208     7676   9357   6601    864    377   -527       C  
ATOM   4665  OH  TYR B 208      -1.179  17.828  13.405  1.00 62.27           O  
ANISOU 4665  OH  TYR B 208     7780   9261   6620    661    253   -562       O  
ATOM   4666  N   ALA B 209     -10.036  17.845  13.126  1.00 59.58           N  
ANISOU 4666  N   ALA B 209     6033  10449   6156   1909   1088   -642       N  
ATOM   4667  CA  ALA B 209     -11.415  18.271  13.371  1.00 62.71           C  
ANISOU 4667  CA  ALA B 209     6168  11163   6497   2222   1230   -734       C  
ATOM   4668  C   ALA B 209     -11.890  17.765  14.722  1.00 68.02           C  
ANISOU 4668  C   ALA B 209     6797  11966   7082   2134   1490   -800       C  
ATOM   4669  O   ALA B 209     -12.450  18.524  15.505  1.00 70.23           O  
ANISOU 4669  O   ALA B 209     7149  12285   7249   2429   1620   -877       O  
ATOM   4670  CB  ALA B 209     -12.338  17.764  12.273  1.00 64.48           C  
ANISOU 4670  CB  ALA B 209     5908  11784   6807   2227   1188   -760       C  
ATOM   4671  N   ARG B 210     -11.667  16.483  14.995  1.00 63.30           N  
ANISOU 4671  N   ARG B 210     6118  11415   6517   1746   1588   -764       N  
ATOM   4672  CA  ARG B 210     -12.041  15.915  16.288  1.00 64.75           C  
ANISOU 4672  CA  ARG B 210     6329  11681   6590   1639   1868   -797       C  
ATOM   4673  C   ARG B 210     -11.232  16.548  17.430  1.00 67.72           C  
ANISOU 4673  C   ARG B 210     7186  11747   6797   1760   1861   -793       C  
ATOM   4674  O   ARG B 210     -11.786  16.842  18.490  1.00 70.02           O  
ANISOU 4674  O   ARG B 210     7546  12117   6942   1919   2069   -861       O  
ATOM   4675  CB  ARG B 210     -11.898  14.385  16.292  1.00 65.17           C  
ANISOU 4675  CB  ARG B 210     6286  11779   6697   1202   1990   -737       C  
ATOM   4676  CG  ARG B 210     -12.651  13.717  17.449  1.00 81.14           C  
ANISOU 4676  CG  ARG B 210     8256  13964   8612   1083   2359   -770       C  
ATOM   4677  CD  ARG B 210     -12.673  12.177  17.379  1.00 97.32           C  
ANISOU 4677  CD  ARG B 210    10227  16033  10716    639   2540   -715       C  
ATOM   4678  NE  ARG B 210     -13.498  11.632  16.282  1.00113.08           N  
ANISOU 4678  NE  ARG B 210    11739  18331  12898    438   2556   -800       N  
ATOM   4679  CZ  ARG B 210     -14.416  10.656  16.400  1.00133.05           C  
ANISOU 4679  CZ  ARG B 210    13975  21102  15477    121   2866   -875       C  
ATOM   4680  NH1 ARG B 210     -14.696  10.087  17.582  1.00123.13           N  
ANISOU 4680  NH1 ARG B 210    12879  19810  14096    -28   3233   -848       N  
ATOM   4681  NH2 ARG B 210     -15.088  10.254  15.318  1.00121.76           N  
ANISOU 4681  NH2 ARG B 210    12088  19963  14212    -62   2820   -993       N  
ATOM   4682  N   ILE B 211      -9.939  16.781  17.203  1.00 60.97           N  
ANISOU 4682  N   ILE B 211     6643  10569   5955   1683   1626   -738       N  
ATOM   4683  CA  ILE B 211      -9.077  17.408  18.210  1.00 60.58           C  
ANISOU 4683  CA  ILE B 211     7023  10248   5745   1764   1571   -777       C  
ATOM   4684  C   ILE B 211      -9.552  18.797  18.597  1.00 66.77           C  
ANISOU 4684  C   ILE B 211     7956  10974   6440   2133   1605   -893       C  
ATOM   4685  O   ILE B 211      -9.684  19.091  19.775  1.00 68.44           O  
ANISOU 4685  O   ILE B 211     8375  11161   6468   2255   1739   -971       O  
ATOM   4686  CB  ILE B 211      -7.621  17.534  17.733  1.00 60.93           C  
ANISOU 4686  CB  ILE B 211     7297  10004   5850   1607   1297   -736       C  
ATOM   4687  CG1 ILE B 211      -6.934  16.164  17.741  1.00 59.43           C  
ANISOU 4687  CG1 ILE B 211     7083   9823   5675   1298   1276   -634       C  
ATOM   4688  CG2 ILE B 211      -6.856  18.501  18.622  1.00 62.31           C  
ANISOU 4688  CG2 ILE B 211     7865   9933   5878   1718   1213   -844       C  
ATOM   4689  CD1 ILE B 211      -5.496  16.179  17.237  1.00 62.58           C  
ANISOU 4689  CD1 ILE B 211     7634  10005   6139   1149   1018   -602       C  
ATOM   4690  N   TYR B 212      -9.793  19.654  17.612  1.00 63.60           N  
ANISOU 4690  N   TYR B 212     7491  10530   6143   2335   1491   -899       N  
ATOM   4691  CA  TYR B 212     -10.264  21.011  17.890  1.00 66.22           C  
ANISOU 4691  CA  TYR B 212     8015  10762   6385   2735   1535   -999       C  
ATOM   4692  C   TYR B 212     -11.571  20.983  18.670  1.00 73.56           C  
ANISOU 4692  C   TYR B 212     8736  12010   7203   2975   1806  -1076       C  
ATOM   4693  O   TYR B 212     -11.763  21.788  19.587  1.00 75.33           O  
ANISOU 4693  O   TYR B 212     9222  12133   7266   3230   1916  -1182       O  
ATOM   4694  CB  TYR B 212     -10.448  21.804  16.595  1.00 67.71           C  
ANISOU 4694  CB  TYR B 212     8161  10882   6684   2957   1397   -957       C  
ATOM   4695  CG  TYR B 212     -11.089  23.167  16.776  1.00 72.87           C  
ANISOU 4695  CG  TYR B 212     9017  11435   7234   3441   1470  -1041       C  
ATOM   4696  CD1 TYR B 212     -10.318  24.291  17.060  1.00 75.54           C  
ANISOU 4696  CD1 TYR B 212     9876  11321   7504   3529   1413  -1103       C  
ATOM   4697  CD2 TYR B 212     -12.468  23.332  16.653  1.00 76.70           C  
ANISOU 4697  CD2 TYR B 212     9172  12282   7687   3813   1605  -1075       C  
ATOM   4698  CE1 TYR B 212     -10.899  25.542  17.222  1.00 79.87           C  
ANISOU 4698  CE1 TYR B 212    10680  11720   7946   3991   1504  -1180       C  
ATOM   4699  CE2 TYR B 212     -13.063  24.578  16.816  1.00 81.19           C  
ANISOU 4699  CE2 TYR B 212     9948  12758   8144   4324   1679  -1146       C  
ATOM   4700  CZ  TYR B 212     -12.273  25.680  17.099  1.00 89.09           C  
ANISOU 4700  CZ  TYR B 212    11535  13246   9069   4419   1635  -1189       C  
ATOM   4701  OH  TYR B 212     -12.862  26.918  17.259  1.00 94.03           O  
ANISOU 4701  OH  TYR B 212    12431  13725   9572   4944   1732  -1260       O  
ATOM   4702  N   VAL B 213     -12.462  20.058  18.308  1.00 70.93           N  
ANISOU 4702  N   VAL B 213     7930  12067   6955   2877   1928  -1044       N  
ATOM   4703  CA  VAL B 213     -13.771  19.951  18.962  1.00 74.40           C  
ANISOU 4703  CA  VAL B 213     8076  12878   7313   3062   2219  -1131       C  
ATOM   4704  C   VAL B 213     -13.623  19.497  20.419  1.00 79.54           C  
ANISOU 4704  C   VAL B 213     8951  13488   7783   2927   2447  -1157       C  
ATOM   4705  O   VAL B 213     -14.256  20.065  21.313  1.00 82.37           O  
ANISOU 4705  O   VAL B 213     9385  13929   7983   3207   2652  -1256       O  
ATOM   4706  CB  VAL B 213     -14.732  18.997  18.210  1.00 78.86           C  
ANISOU 4706  CB  VAL B 213     8042  13896   8025   2902   2306  -1126       C  
ATOM   4707  CG1 VAL B 213     -16.091  18.979  18.884  1.00 82.90           C  
ANISOU 4707  CG1 VAL B 213     8207  14828   8464   3089   2627  -1246       C  
ATOM   4708  CG2 VAL B 213     -14.890  19.425  16.765  1.00 78.27           C  
ANISOU 4708  CG2 VAL B 213     7755  13901   8084   3073   2059  -1105       C  
ATOM   4709  N   VAL B 214     -12.778  18.491  20.649  1.00 73.56           N  
ANISOU 4709  N   VAL B 214     8327  12599   7022   2538   2412  -1065       N  
ATOM   4710  CA  VAL B 214     -12.522  17.975  21.999  1.00 74.19           C  
ANISOU 4710  CA  VAL B 214     8679  12623   6889   2424   2604  -1060       C  
ATOM   4711  C   VAL B 214     -11.841  19.007  22.898  1.00 78.92           C  
ANISOU 4711  C   VAL B 214     9771  12935   7281   2651   2512  -1151       C  
ATOM   4712  O   VAL B 214     -12.203  19.140  24.062  1.00 81.13           O  
ANISOU 4712  O   VAL B 214    10223  13267   7337   2789   2733  -1219       O  
ATOM   4713  CB  VAL B 214     -11.674  16.683  21.964  1.00 75.38           C  
ANISOU 4713  CB  VAL B 214     8911  12670   7061   2019   2553   -924       C  
ATOM   4714  CG1 VAL B 214     -11.218  16.287  23.364  1.00 76.19           C  
ANISOU 4714  CG1 VAL B 214     9400  12664   6885   1983   2693   -904       C  
ATOM   4715  CG2 VAL B 214     -12.464  15.555  21.323  1.00 75.46           C  
ANISOU 4715  CG2 VAL B 214     8485  12953   7234   1751   2730   -867       C  
ATOM   4716  N   LEU B 215     -10.867  19.735  22.360  1.00 73.70           N  
ANISOU 4716  N   LEU B 215     9341  11975   6687   2669   2205  -1169       N  
ATOM   4717  CA  LEU B 215     -10.189  20.801  23.108  1.00 74.79           C  
ANISOU 4717  CA  LEU B 215     9943  11821   6652   2836   2101  -1302       C  
ATOM   4718  C   LEU B 215     -11.110  21.971  23.456  1.00 82.63           C  
ANISOU 4718  C   LEU B 215    11013  12830   7552   3260   2259  -1437       C  
ATOM   4719  O   LEU B 215     -11.076  22.490  24.576  1.00 84.42           O  
ANISOU 4719  O   LEU B 215    11567  12965   7544   3420   2356  -1565       O  
ATOM   4720  CB  LEU B 215      -8.999  21.338  22.316  1.00 72.45           C  
ANISOU 4720  CB  LEU B 215     9833  11207   6488   2708   1776  -1307       C  
ATOM   4721  CG  LEU B 215      -7.690  20.586  22.503  1.00 74.68           C  
ANISOU 4721  CG  LEU B 215    10248  11382   6745   2374   1583  -1263       C  
ATOM   4722  CD1 LEU B 215      -6.678  21.043  21.465  1.00 72.71           C  
ANISOU 4722  CD1 LEU B 215    10052  10889   6684   2221   1307  -1257       C  
ATOM   4723  CD2 LEU B 215      -7.167  20.814  23.912  1.00 79.24           C  
ANISOU 4723  CD2 LEU B 215    11200  11875   7033   2418   1584  -1399       C  
ATOM   4724  N   LYS B 216     -11.914  22.390  22.485  1.00 80.24           N  
ANISOU 4724  N   LYS B 216    10425  12650   7411   3473   2273  -1415       N  
ATOM   4725  CA  LYS B 216     -12.878  23.462  22.697  1.00 84.01           C  
ANISOU 4725  CA  LYS B 216    10937  13179   7804   3947   2428  -1528       C  
ATOM   4726  C   LYS B 216     -13.951  23.043  23.718  1.00 91.28           C  
ANISOU 4726  C   LYS B 216    11661  14457   8566   4079   2778  -1583       C  
ATOM   4727  O   LYS B 216     -14.513  23.896  24.415  1.00 94.80           O  
ANISOU 4727  O   LYS B 216    12281  14897   8844   4457   2945  -1713       O  
ATOM   4728  CB  LYS B 216     -13.514  23.876  21.360  1.00 87.07           C  
ANISOU 4728  CB  LYS B 216    11022  13683   8379   4182   2344  -1473       C  
ATOM   4729  CG  LYS B 216     -14.339  25.173  21.402  1.00106.39           C  
ANISOU 4729  CG  LYS B 216    13590  16102  10733   4761   2446  -1577       C  
ATOM   4730  CD  LYS B 216     -14.728  25.651  19.990  1.00116.56           C  
ANISOU 4730  CD  LYS B 216    14684  17437  12169   5025   2296  -1498       C  
ATOM   4731  CE  LYS B 216     -16.019  26.492  19.968  1.00132.48           C  
ANISOU 4731  CE  LYS B 216    16552  19692  14094   5663   2456  -1576       C  
ATOM   4732  NZ  LYS B 216     -15.862  27.873  20.512  1.00144.78           N  
ANISOU 4732  NZ  LYS B 216    18710  20818  15483   6070   2513  -1681       N  
ATOM   4733  N   GLN B 217     -14.212  21.737  23.821  1.00 86.64           N  
ANISOU 4733  N   GLN B 217    10745  14154   8020   3760   2916  -1490       N  
ATOM   4734  CA  GLN B 217     -15.250  21.212  24.723  1.00 89.66           C  
ANISOU 4734  CA  GLN B 217    10910  14890   8268   3808   3302  -1528       C  
ATOM   4735  C   GLN B 217     -14.761  20.887  26.140  1.00 93.40           C  
ANISOU 4735  C   GLN B 217    11798  15233   8458   3701   3451  -1545       C  
ATOM   4736  O   GLN B 217     -15.555  20.902  27.080  1.00 96.63           O  
ANISOU 4736  O   GLN B 217    12194  15842   8679   3869   3785  -1613       O  
ATOM   4737  CB  GLN B 217     -15.932  19.988  24.097  1.00 90.81           C  
ANISOU 4737  CB  GLN B 217    10490  15414   8601   3504   3439  -1439       C  
ATOM   4738  CG  GLN B 217     -16.932  20.360  23.001  1.00110.16           C  
ANISOU 4738  CG  GLN B 217    12419  18191  11245   3739   3408  -1488       C  
ATOM   4739  CD  GLN B 217     -17.502  19.158  22.267  1.00128.97           C  
ANISOU 4739  CD  GLN B 217    14237  20941  13826   3377   3489  -1442       C  
ATOM   4740  OE1 GLN B 217     -16.763  18.317  21.756  1.00120.20           O  
ANISOU 4740  OE1 GLN B 217    13161  19680  12828   2979   3335  -1330       O  
ATOM   4741  NE2 GLN B 217     -18.828  19.082  22.201  1.00125.76           N  
ANISOU 4741  NE2 GLN B 217    13292  21029  13461   3515   3734  -1551       N  
ATOM   4742  N   ARG B 218     -13.471  20.591  26.298  1.00 86.18           N  
ANISOU 4742  N   ARG B 218    11238  14015   7490   3447   3208  -1488       N  
ATOM   4743  CA  ARG B 218     -12.887  20.396  27.633  1.00 86.64           C  
ANISOU 4743  CA  ARG B 218    11740  13948   7230   3410   3278  -1520       C  
ATOM   4744  C   ARG B 218     -12.504  21.716  28.295  1.00 91.30           C  
ANISOU 4744  C   ARG B 218    12785  14284   7621   3714   3172  -1715       C  
ATOM   4745  O   ARG B 218     -12.271  21.758  29.502  1.00 92.99           O  
ANISOU 4745  O   ARG B 218    13358  14453   7521   3783   3267  -1794       O  
ATOM   4746  CB  ARG B 218     -11.658  19.483  27.576  1.00 83.86           C  
ANISOU 4746  CB  ARG B 218    11555  13435   6874   3052   3049  -1396       C  
ATOM   4747  CG  ARG B 218     -11.996  18.024  27.369  1.00 93.35           C  
ANISOU 4747  CG  ARG B 218    12477  14835   8155   2747   3246  -1213       C  
ATOM   4748  CD  ARG B 218     -10.794  17.130  27.593  1.00101.95           C  
ANISOU 4748  CD  ARG B 218    13833  15755   9148   2495   3066  -1093       C  
ATOM   4749  NE  ARG B 218     -11.003  15.813  26.993  1.00110.65           N  
ANISOU 4749  NE  ARG B 218    14668  16960  10415   2181   3191   -916       N  
ATOM   4750  CZ  ARG B 218     -10.126  14.810  27.032  1.00124.74           C  
ANISOU 4750  CZ  ARG B 218    16629  18622  12145   1965   3093   -775       C  
ATOM   4751  NH1 ARG B 218      -8.957  14.953  27.658  1.00112.91           N  
ANISOU 4751  NH1 ARG B 218    15528  16948  10423   2043   2844   -792       N  
ATOM   4752  NH2 ARG B 218     -10.422  13.652  26.443  1.00110.43           N  
ANISOU 4752  NH2 ARG B 218    14594  16873  10491   1681   3245   -633       N  
ATOM   4753  N   ARG B 219     -12.431  22.789  27.509  1.00 86.38           N  
ANISOU 4753  N   ARG B 219    12185  13478   7159   3895   2983  -1796       N  
ATOM   4754  CA  ARG B 219     -12.069  24.097  28.046  1.00 87.74           C  
ANISOU 4754  CA  ARG B 219    12828  13346   7164   4156   2898  -2001       C  
ATOM   4755  C   ARG B 219     -13.126  24.599  29.034  1.00 94.17           C  
ANISOU 4755  C   ARG B 219    13729  14314   7736   4547   3244  -2128       C  
ATOM   4756  O   ARG B 219     -12.789  25.247  30.023  1.00 95.74           O  
ANISOU 4756  O   ARG B 219    14388  14325   7664   4689   3255  -2303       O  
ATOM   4757  CB  ARG B 219     -11.847  25.118  26.919  1.00 87.69           C  
ANISOU 4757  CB  ARG B 219    12865  13070   7384   4272   2682  -2034       C  
ATOM   4758  CG  ARG B 219     -10.913  26.246  27.328  1.00101.44           C  
ANISOU 4758  CG  ARG B 219    15172  14370   8999   4308   2501  -2236       C  
ATOM   4759  CD  ARG B 219     -10.898  27.419  26.350  1.00116.16           C  
ANISOU 4759  CD  ARG B 219    17182  15918  11037   4500   2396  -2276       C  
ATOM   4760  NE  ARG B 219     -10.303  28.606  26.980  1.00132.47           N  
ANISOU 4760  NE  ARG B 219    19838  17559  12934   4588   2342  -2522       N  
ATOM   4761  CZ  ARG B 219      -8.992  28.818  27.145  1.00148.64           C  
ANISOU 4761  CZ  ARG B 219    22203  19312  14964   4238   2097  -2647       C  
ATOM   4762  NH1 ARG B 219      -8.089  27.932  26.714  1.00133.29           N  
ANISOU 4762  NH1 ARG B 219    20041  17447  13155   3815   1874  -2532       N  
ATOM   4763  NH2 ARG B 219      -8.575  29.933  27.746  1.00139.66           N  
ANISOU 4763  NH2 ARG B 219    21595  17802  13666   4309   2081  -2911       N  
ATOM   4764  N   ARG B 220     -14.396  24.298  28.759  1.00 91.20           N  
ANISOU 4764  N   ARG B 220    12896  14304   7453   4716   3525  -2062       N  
ATOM   4765  CA  ARG B 220     -15.486  24.570  29.699  1.00 95.04           C  
ANISOU 4765  CA  ARG B 220    13364  15031   7718   5064   3911  -2167       C  
ATOM   4766  C   ARG B 220     -15.623  23.376  30.639  1.00 97.50           C  
ANISOU 4766  C   ARG B 220    13626  15580   7840   4812   4177  -2081       C  
ATOM   4767  O   ARG B 220     -15.792  22.247  30.179  1.00 95.07           O  
ANISOU 4767  O   ARG B 220    12940  15487   7694   4488   4240  -1915       O  
ATOM   4768  CB  ARG B 220     -16.807  24.795  28.952  1.00 97.96           C  
ANISOU 4768  CB  ARG B 220    13197  15747   8275   5369   4097  -2159       C  
ATOM   4769  CG  ARG B 220     -18.007  25.175  29.840  1.00114.43           C  
ANISOU 4769  CG  ARG B 220    15199  18128  10152   5786   4515  -2288       C  
ATOM   4770  CD  ARG B 220     -17.913  26.610  30.335  1.00128.11           C  
ANISOU 4770  CD  ARG B 220    17456  19534  11686   6259   4492  -2483       C  
ATOM   4771  NE  ARG B 220     -19.084  27.023  31.116  1.00143.74           N  
ANISOU 4771  NE  ARG B 220    19343  21805  13467   6716   4898  -2613       N  
ATOM   4772  CZ  ARG B 220     -19.232  26.873  32.436  1.00163.19           C  
ANISOU 4772  CZ  ARG B 220    22062  24333  15608   6754   5190  -2700       C  
ATOM   4773  NH1 ARG B 220     -18.285  26.294  33.175  1.00149.35           N  
ANISOU 4773  NH1 ARG B 220    20689  22386  13669   6381   5107  -2666       N  
ATOM   4774  NH2 ARG B 220     -20.345  27.305  33.031  1.00155.58           N  
ANISOU 4774  NH2 ARG B 220    20974  23655  14484   7203   5573  -2822       N  
ATOM   4775  N   LYS B 221     -15.548  23.630  31.945  1.00 95.38           N  
ANISOU 4775  N   LYS B 221    13779  15251   7210   4963   4344  -2196       N  
ATOM   4776  CA  LYS B 221     -15.667  22.580  32.958  1.00 95.74           C  
ANISOU 4776  CA  LYS B 221    13891  15482   7001   4781   4631  -2107       C  
ATOM   4777  C   LYS B 221     -16.515  23.048  34.131  1.00104.60           C  
ANISOU 4777  C   LYS B 221    15188  16759   7795   5142   5033  -2247       C  
ATOM   4778  O   LYS B 221     -16.893  24.218  34.207  1.00106.52           O  
ANISOU 4778  O   LYS B 221    15549  16929   7995   5544   5050  -2431       O  
ATOM   4779  CB  LYS B 221     -14.282  22.152  33.458  1.00 95.29           C  
ANISOU 4779  CB  LYS B 221    14293  15160   6751   4521   4341  -2069       C  
ATOM   4780  CG  LYS B 221     -13.569  21.155  32.552  1.00101.67           C  
ANISOU 4780  CG  LYS B 221    14884  15928   7818   4105   4093  -1868       C  
ATOM   4781  CD  LYS B 221     -12.292  20.614  33.196  1.00107.11           C  
ANISOU 4781  CD  LYS B 221    15996  16440   8260   3913   3856  -1827       C  
ATOM   4782  CE  LYS B 221     -11.684  19.477  32.386  1.00109.69           C  
ANISOU 4782  CE  LYS B 221    16109  16758   8812   3538   3684  -1610       C  
ATOM   4783  NZ  LYS B 221     -11.119  19.941  31.095  1.00112.36           N  
ANISOU 4783  NZ  LYS B 221    16246  16935   9513   3425   3309  -1630       N  
ATOM   4784  N   ASN B1002     -16.811  22.118  35.037  1.00 55.46           N  
ANISOU 4784  N   ASN B1002     8509   8066   4497   1094  -1433  -1787       N  
ATOM   4785  CA  ASN B1002     -17.571  22.417  36.258  1.00 52.18           C  
ANISOU 4785  CA  ASN B1002     7935   7373   4517   1014  -1530  -1711       C  
ATOM   4786  C   ASN B1002     -17.029  21.711  37.510  1.00 52.54           C  
ANISOU 4786  C   ASN B1002     7875   7215   4874    988  -1366  -1810       C  
ATOM   4787  O   ASN B1002     -16.162  20.834  37.425  1.00 52.27           O  
ANISOU 4787  O   ASN B1002     7881   7196   4782   1055  -1229  -1973       O  
ATOM   4788  CB  ASN B1002     -19.067  22.102  36.062  1.00 54.42           C  
ANISOU 4788  CB  ASN B1002     8174   7614   4891    988  -1848  -1850       C  
ATOM   4789  CG  ASN B1002     -19.333  20.640  35.716  1.00 73.72           C  
ANISOU 4789  CG  ASN B1002    10669  10021   7321    968  -1952  -2224       C  
ATOM   4790  OD1 ASN B1002     -18.552  19.743  36.048  1.00 63.96           O  
ANISOU 4790  OD1 ASN B1002     9477   8669   6157    988  -1785  -2384       O  
ATOM   4791  ND2 ASN B1002     -20.456  20.397  35.053  1.00 68.26           N  
ANISOU 4791  ND2 ASN B1002     9963   9401   6571    935  -2265  -2378       N  
ATOM   4792  N   ILE B1003     -17.571  22.110  38.663  1.00 47.09           N  
ANISOU 4792  N   ILE B1003     7048   6353   4491    922  -1393  -1713       N  
ATOM   4793  CA  ILE B1003     -17.132  21.628  39.985  1.00 44.95           C  
ANISOU 4793  CA  ILE B1003     6687   5928   4463    896  -1259  -1731       C  
ATOM   4794  C   ILE B1003     -16.984  20.097  40.073  1.00 50.70           C  
ANISOU 4794  C   ILE B1003     7471   6534   5259    914  -1254  -1938       C  
ATOM   4795  O   ILE B1003     -16.042  19.596  40.693  1.00 49.43           O  
ANISOU 4795  O   ILE B1003     7306   6307   5168    976  -1122  -1939       O  
ATOM   4796  CB  ILE B1003     -18.100  22.137  41.099  1.00 46.31           C  
ANISOU 4796  CB  ILE B1003     6713   6000   4882    832  -1312  -1654       C  
ATOM   4797  CG1 ILE B1003     -17.573  21.806  42.490  1.00 45.02           C  
ANISOU 4797  CG1 ILE B1003     6486   5753   4865    815  -1170  -1626       C  
ATOM   4798  CG2 ILE B1003     -19.492  21.568  40.910  1.00 48.01           C  
ANISOU 4798  CG2 ILE B1003     6855   6185   5203    763  -1486  -1765       C  
ATOM   4799  CD1 ILE B1003     -16.258  22.468  42.801  1.00 52.39           C  
ANISOU 4799  CD1 ILE B1003     7421   6741   5745    858  -1046  -1540       C  
ATOM   4800  N   PHE B1004     -17.900  19.369  39.436  1.00 50.28           N  
ANISOU 4800  N   PHE B1004     7469   6427   5208    866  -1430  -2118       N  
ATOM   4801  CA  PHE B1004     -17.920  17.915  39.515  1.00 52.28           C  
ANISOU 4801  CA  PHE B1004     7801   6456   5606    849  -1472  -2329       C  
ATOM   4802  C   PHE B1004     -16.765  17.336  38.736  1.00 58.23           C  
ANISOU 4802  C   PHE B1004     8702   7261   6162   1036  -1383  -2521       C  
ATOM   4803  O   PHE B1004     -16.102  16.414  39.204  1.00 58.44           O  
ANISOU 4803  O   PHE B1004     8776   7085   6342   1126  -1311  -2601       O  
ATOM   4804  CB  PHE B1004     -19.231  17.356  38.984  1.00 56.78           C  
ANISOU 4804  CB  PHE B1004     8361   6948   6266    703  -1722  -2510       C  
ATOM   4805  CG  PHE B1004     -20.450  17.946  39.641  1.00 57.98           C  
ANISOU 4805  CG  PHE B1004     8291   7127   6613    544  -1797  -2350       C  
ATOM   4806  CD1 PHE B1004     -20.817  17.556  40.924  1.00 60.66           C  
ANISOU 4806  CD1 PHE B1004     8505   7299   7243    405  -1698  -2217       C  
ATOM   4807  CD2 PHE B1004     -21.238  18.885  38.974  1.00 60.91           C  
ANISOU 4807  CD2 PHE B1004     8568   7717   6860    558  -1964  -2323       C  
ATOM   4808  CE1 PHE B1004     -21.946  18.091  41.531  1.00 61.52           C  
ANISOU 4808  CE1 PHE B1004     8364   7502   7511    282  -1717  -2103       C  
ATOM   4809  CE2 PHE B1004     -22.363  19.421  39.571  1.00 63.66           C  
ANISOU 4809  CE2 PHE B1004     8662   8110   7416    470  -2028  -2217       C  
ATOM   4810  CZ  PHE B1004     -22.718  19.024  40.855  1.00 61.18           C  
ANISOU 4810  CZ  PHE B1004     8188   7670   7386    331  -1882  -2129       C  
ATOM   4811  N   GLU B1005     -16.510  17.884  37.554  1.00 56.60           N  
ANISOU 4811  N   GLU B1005     8563   7342   5601   1118  -1377  -2581       N  
ATOM   4812  CA  GLU B1005     -15.310  17.513  36.811  1.00 58.72           C  
ANISOU 4812  CA  GLU B1005     8918   7776   5618   1320  -1211  -2752       C  
ATOM   4813  C   GLU B1005     -14.044  17.955  37.571  1.00 60.71           C  
ANISOU 4813  C   GLU B1005     9028   8095   5944   1398   -955  -2544       C  
ATOM   4814  O   GLU B1005     -13.030  17.270  37.523  1.00 62.18           O  
ANISOU 4814  O   GLU B1005     9202   8293   6130   1586   -818  -2700       O  
ATOM   4815  CB  GLU B1005     -15.327  18.075  35.375  1.00 62.81           C  
ANISOU 4815  CB  GLU B1005     9538   8672   5655   1371  -1225  -2804       C  
ATOM   4816  CG  GLU B1005     -16.463  17.544  34.462  1.00 78.03           C  
ANISOU 4816  CG  GLU B1005    11607  10605   7435   1333  -1532  -3090       C  
ATOM   4817  CD  GLU B1005     -16.255  16.106  33.944  1.00109.75           C  
ANISOU 4817  CD  GLU B1005    15782  14485  11434   1467  -1597  -3589       C  
ATOM   4818  OE1 GLU B1005     -16.772  15.795  32.845  1.00112.63           O  
ANISOU 4818  OE1 GLU B1005    16294  15009  11491   1495  -1800  -3893       O  
ATOM   4819  OE2 GLU B1005     -15.594  15.277  34.618  1.00106.97           O  
ANISOU 4819  OE2 GLU B1005    15420  13850  11374   1563  -1478  -3699       O  
ATOM   4820  N   MET B1006     -14.115  19.074  38.289  1.00 54.33           N  
ANISOU 4820  N   MET B1006     8095   7321   5227   1268   -918  -2232       N  
ATOM   4821  CA  MET B1006     -12.974  19.571  39.066  1.00 52.95           C  
ANISOU 4821  CA  MET B1006     7761   7213   5146   1295   -734  -2060       C  
ATOM   4822  C   MET B1006     -12.598  18.635  40.207  1.00 56.54           C  
ANISOU 4822  C   MET B1006     8168   7438   5878   1381   -741  -2110       C  
ATOM   4823  O   MET B1006     -11.430  18.313  40.400  1.00 57.22           O  
ANISOU 4823  O   MET B1006     8152   7598   5989   1537   -619  -2147       O  
ATOM   4824  CB  MET B1006     -13.294  20.942  39.657  1.00 53.14           C  
ANISOU 4824  CB  MET B1006     7698   7243   5248   1127   -755  -1784       C  
ATOM   4825  CG  MET B1006     -12.092  21.694  40.199  1.00 56.49           C  
ANISOU 4825  CG  MET B1006     7955   7779   5732   1098   -598  -1630       C  
ATOM   4826  SD  MET B1006     -12.611  23.140  41.144  1.00 58.84           S  
ANISOU 4826  SD  MET B1006     8195   7947   6213    921   -688  -1417       S  
ATOM   4827  CE  MET B1006     -11.394  24.347  40.627  1.00 57.24           C  
ANISOU 4827  CE  MET B1006     7882   7921   5946    794   -526  -1216       C  
ATOM   4828  N   LEU B1007     -13.597  18.229  40.980  1.00 52.05           N  
ANISOU 4828  N   LEU B1007     7651   6615   5513   1280   -884  -2078       N  
ATOM   4829  CA  LEU B1007     -13.363  17.398  42.153  1.00 51.63           C  
ANISOU 4829  CA  LEU B1007     7590   6336   5692   1331   -903  -2025       C  
ATOM   4830  C   LEU B1007     -13.247  15.926  41.793  1.00 58.58           C  
ANISOU 4830  C   LEU B1007     8617   6957   6684   1475   -965  -2243       C  
ATOM   4831  O   LEU B1007     -12.734  15.152  42.594  1.00 59.77           O  
ANISOU 4831  O   LEU B1007     8785   6909   7015   1595   -978  -2184       O  
ATOM   4832  CB  LEU B1007     -14.461  17.596  43.202  1.00 50.03           C  
ANISOU 4832  CB  LEU B1007     7367   6010   5633   1140   -978  -1853       C  
ATOM   4833  CG  LEU B1007     -14.500  18.946  43.931  1.00 52.20           C  
ANISOU 4833  CG  LEU B1007     7507   6466   5862   1055   -930  -1682       C  
ATOM   4834  CD1 LEU B1007     -15.867  19.142  44.577  1.00 51.66           C  
ANISOU 4834  CD1 LEU B1007     7404   6339   5885    896   -983  -1605       C  
ATOM   4835  CD2 LEU B1007     -13.389  19.064  44.961  1.00 53.45           C  
ANISOU 4835  CD2 LEU B1007     7580   6693   6036   1147   -875  -1581       C  
ATOM   4836  N   ARG B1008     -13.722  15.524  40.614  1.00 56.06           N  
ANISOU 4836  N   ARG B1008     8423   6617   6263   1480  -1035  -2501       N  
ATOM   4837  CA  ARG B1008     -13.438  14.171  40.133  1.00 59.16           C  
ANISOU 4837  CA  ARG B1008     8973   6746   6758   1663  -1097  -2803       C  
ATOM   4838  C   ARG B1008     -11.933  14.011  39.957  1.00 63.55           C  
ANISOU 4838  C   ARG B1008     9446   7465   7236   1988   -929  -2902       C  
ATOM   4839  O   ARG B1008     -11.361  12.990  40.334  1.00 65.79           O  
ANISOU 4839  O   ARG B1008     9783   7473   7742   2209   -961  -2995       O  
ATOM   4840  CB  ARG B1008     -14.151  13.862  38.811  1.00 62.39           C  
ANISOU 4840  CB  ARG B1008     9530   7175   7001   1624  -1223  -3141       C  
ATOM   4841  CG  ARG B1008     -15.538  13.259  38.985  1.00 74.22           C  
ANISOU 4841  CG  ARG B1008    11117   8335   8750   1359  -1459  -3186       C  
ATOM   4842  CD  ARG B1008     -16.247  13.023  37.649  1.00 86.59           C  
ANISOU 4842  CD  ARG B1008    12803   9974  10124   1313  -1646  -3559       C  
ATOM   4843  NE  ARG B1008     -17.668  12.705  37.843  1.00 94.43           N  
ANISOU 4843  NE  ARG B1008    13774  10733  11372    991  -1885  -3560       N  
ATOM   4844  CZ  ARG B1008     -18.690  13.550  37.670  1.00106.98           C  
ANISOU 4844  CZ  ARG B1008    15216  12563  12867    789  -1993  -3438       C  
ATOM   4845  NH1 ARG B1008     -18.498  14.811  37.272  1.00 92.14           N  
ANISOU 4845  NH1 ARG B1008    13258  11112  10642    873  -1906  -3278       N  
ATOM   4846  NH2 ARG B1008     -19.931  13.123  37.891  1.00 94.72           N  
ANISOU 4846  NH2 ARG B1008    13580  10806  11605    498  -2199  -3463       N  
ATOM   4847  N   ILE B1009     -11.301  15.035  39.393  1.00 57.89           N  
ANISOU 4847  N   ILE B1009     8577   7191   6227   2012   -752  -2857       N  
ATOM   4848  CA  ILE B1009      -9.859  15.038  39.184  1.00 58.81           C  
ANISOU 4848  CA  ILE B1009     8514   7571   6260   2279   -547  -2932       C  
ATOM   4849  C   ILE B1009      -9.107  15.039  40.509  1.00 61.15           C  
ANISOU 4849  C   ILE B1009     8629   7791   6812   2352   -550  -2701       C  
ATOM   4850  O   ILE B1009      -8.162  14.274  40.687  1.00 63.28           O  
ANISOU 4850  O   ILE B1009     8815   8010   7217   2659   -522  -2823       O  
ATOM   4851  CB  ILE B1009      -9.424  16.270  38.372  1.00 61.40           C  
ANISOU 4851  CB  ILE B1009     8693   8398   6239   2185   -338  -2833       C  
ATOM   4852  CG1 ILE B1009      -9.973  16.186  36.946  1.00 64.12           C  
ANISOU 4852  CG1 ILE B1009     9226   8911   6224   2189   -333  -3072       C  
ATOM   4853  CG2 ILE B1009      -7.913  16.384  38.357  1.00 63.97           C  
ANISOU 4853  CG2 ILE B1009     8727   9039   6538   2390    -98  -2845       C  
ATOM   4854  CD1 ILE B1009      -9.895  17.487  36.172  1.00 70.60           C  
ANISOU 4854  CD1 ILE B1009     9983  10163   6677   2020   -179  -2848       C  
ATOM   4855  N   ASP B1010      -9.549  15.898  41.429  1.00 54.47           N  
ANISOU 4855  N   ASP B1010     7724   6952   6019   2098   -606  -2393       N  
ATOM   4856  CA  ASP B1010      -8.845  16.159  42.688  1.00 53.28           C  
ANISOU 4856  CA  ASP B1010     7392   6838   6013   2129   -630  -2174       C  
ATOM   4857  C   ASP B1010      -9.091  15.106  43.763  1.00 58.86           C  
ANISOU 4857  C   ASP B1010     8235   7172   6958   2226   -802  -2077       C  
ATOM   4858  O   ASP B1010      -8.259  14.931  44.649  1.00 59.24           O  
ANISOU 4858  O   ASP B1010     8154   7252   7104   2386   -853  -1956       O  
ATOM   4859  CB  ASP B1010      -9.221  17.547  43.237  1.00 51.52           C  
ANISOU 4859  CB  ASP B1010     7078   6776   5721   1837   -627  -1943       C  
ATOM   4860  CG  ASP B1010      -8.454  18.689  42.563  1.00 57.24           C  
ANISOU 4860  CG  ASP B1010     7594   7860   6295   1753   -459  -1919       C  
ATOM   4861  OD1 ASP B1010      -7.652  18.441  41.643  1.00 59.88           O  
ANISOU 4861  OD1 ASP B1010     7824   8403   6525   1904   -301  -2060       O  
ATOM   4862  OD2 ASP B1010      -8.649  19.853  42.964  1.00 59.75           O  
ANISOU 4862  OD2 ASP B1010     7848   8247   6608   1528   -473  -1756       O  
ATOM   4863  N   GLU B1011     -10.223  14.415  43.694  1.00 56.68           N  
ANISOU 4863  N   GLU B1011     8206   6554   6776   2112   -907  -2102       N  
ATOM   4864  CA  GLU B1011     -10.552  13.371  44.672  1.00 58.62           C  
ANISOU 4864  CA  GLU B1011     8614   6399   7259   2142  -1052  -1940       C  
ATOM   4865  C   GLU B1011     -10.445  11.951  44.102  1.00 68.72           C  
ANISOU 4865  C   GLU B1011    10095   7260   8756   2367  -1141  -2172       C  
ATOM   4866  O   GLU B1011     -10.136  11.014  44.835  1.00 71.15           O  
ANISOU 4866  O   GLU B1011    10509   7231   9293   2536  -1257  -2035       O  
ATOM   4867  CB  GLU B1011     -11.958  13.591  45.224  1.00 58.03           C  
ANISOU 4867  CB  GLU B1011     8638   6207   7205   1790  -1097  -1744       C  
ATOM   4868  CG  GLU B1011     -12.174  14.967  45.846  1.00 63.29           C  
ANISOU 4868  CG  GLU B1011     9135   7225   7685   1607  -1026  -1571       C  
ATOM   4869  CD  GLU B1011     -12.137  14.959  47.366  1.00 76.51           C  
ANISOU 4869  CD  GLU B1011    10799   8913   9358   1580  -1063  -1270       C  
ATOM   4870  OE1 GLU B1011     -12.623  13.970  47.955  1.00 72.65           O  
ANISOU 4870  OE1 GLU B1011    10471   8129   9006   1540  -1125  -1095       O  
ATOM   4871  OE2 GLU B1011     -11.652  15.949  47.971  1.00 63.96           O  
ANISOU 4871  OE2 GLU B1011     9055   7629   7620   1579  -1038  -1205       O  
ATOM   4872  N   GLY B1012     -10.710  11.783  42.809  1.00 68.02           N  
ANISOU 4872  N   GLY B1012    10083   7170   8589   2383  -1111  -2527       N  
ATOM   4873  CA  GLY B1012     -10.632  10.463  42.174  1.00 73.16           C  
ANISOU 4873  CA  GLY B1012    10949   7403   9447   2609  -1214  -2857       C  
ATOM   4874  C   GLY B1012     -11.782   9.544  42.558  1.00 80.47           C  
ANISOU 4874  C   GLY B1012    12135   7759  10679   2364  -1408  -2773       C  
ATOM   4875  O   GLY B1012     -12.641   9.911  43.368  1.00 77.98           O  
ANISOU 4875  O   GLY B1012    11803   7433  10394   2026  -1428  -2430       O  
ATOM   4876  N   LEU B1013     -11.794   8.346  41.976  1.00 82.68           N  
ANISOU 4876  N   LEU B1013    12643   7567  11204   2527  -1542  -3105       N  
ATOM   4877  CA  LEU B1013     -12.851   7.370  42.224  1.00 85.88           C  
ANISOU 4877  CA  LEU B1013    13301   7354  11975   2253  -1744  -3058       C  
ATOM   4878  C   LEU B1013     -12.265   6.056  42.742  1.00 97.19           C  
ANISOU 4878  C   LEU B1013    14956   8141  13832   2541  -1888  -3011       C  
ATOM   4879  O   LEU B1013     -11.268   5.562  42.200  1.00 99.96           O  
ANISOU 4879  O   LEU B1013    15340   8413  14227   3010  -1893  -3361       O  
ATOM   4880  CB  LEU B1013     -13.636   7.114  40.932  1.00 87.80           C  
ANISOU 4880  CB  LEU B1013    13664   7515  12179   2107  -1856  -3558       C  
ATOM   4881  CG  LEU B1013     -14.641   5.951  40.921  1.00 96.59           C  
ANISOU 4881  CG  LEU B1013    15033   7925  13742   1824  -2108  -3662       C  
ATOM   4882  CD1 LEU B1013     -15.825   6.244  41.843  1.00 94.42           C  
ANISOU 4882  CD1 LEU B1013    14661   7613  13601   1296  -2117  -3171       C  
ATOM   4883  CD2 LEU B1013     -15.110   5.655  39.499  1.00101.76           C  
ANISOU 4883  CD2 LEU B1013    15804   8553  14305   1799  -2262  -4301       C  
ATOM   4884  N   ARG B1014     -12.891   5.490  43.780  1.00 96.78           N  
ANISOU 4884  N   ARG B1014    15049   7634  14088   2273  -1995  -2565       N  
ATOM   4885  CA  ARG B1014     -12.519   4.160  44.305  1.00103.02           C  
ANISOU 4885  CA  ARG B1014    16121   7679  15342   2487  -2180  -2429       C  
ATOM   4886  C   ARG B1014     -13.766   3.322  44.678  1.00111.10           C  
ANISOU 4886  C   ARG B1014    17388   8049  16775   1989  -2332  -2192       C  
ATOM   4887  O   ARG B1014     -14.596   3.753  45.478  1.00108.25           O  
ANISOU 4887  O   ARG B1014    16931   7860  16338   1550  -2244  -1725       O  
ATOM   4888  CB  ARG B1014     -11.577   4.303  45.514  1.00103.51           C  
ANISOU 4888  CB  ARG B1014    16099   7885  15344   2769  -2148  -1929       C  
ATOM   4889  CG  ARG B1014     -10.388   5.268  45.299  1.00112.61           C  
ANISOU 4889  CG  ARG B1014    16919   9752  16117   3155  -1990  -2092       C  
ATOM   4890  CD  ARG B1014      -9.095   4.790  45.975  1.00129.16           C  
ANISOU 4890  CD  ARG B1014    18980  11746  18348   3687  -2090  -1915       C  
ATOM   4891  NE  ARG B1014      -8.546   3.576  45.352  1.00146.63           N  
ANISOU 4891  NE  ARG B1014    21395  13366  20951   4144  -2245  -2295       N  
ATOM   4892  CZ  ARG B1014      -7.907   3.532  44.179  1.00164.03           C  
ANISOU 4892  CZ  ARG B1014    23485  15738  23100   4510  -2159  -2920       C  
ATOM   4893  NH1 ARG B1014      -7.720   4.636  43.455  1.00147.22           N  
ANISOU 4893  NH1 ARG B1014    21050  14357  20531   4439  -1913  -3180       N  
ATOM   4894  NH2 ARG B1014      -7.454   2.368  43.719  1.00158.13           N  
ANISOU 4894  NH2 ARG B1014    22946  14398  22737   4959  -2313  -3286       N  
ATOM   4895  N   LEU B1015     -13.880   2.123  44.104  1.00114.72           N  
ANISOU 4895  N   LEU B1015    18145   7760  17683   2056  -2551  -2530       N  
ATOM   4896  CA  LEU B1015     -15.096   1.290  44.227  1.00119.28           C  
ANISOU 4896  CA  LEU B1015    18935   7668  18717   1518  -2719  -2407       C  
ATOM   4897  C   LEU B1015     -15.272   0.569  45.581  1.00127.42           C  
ANISOU 4897  C   LEU B1015    20161   8148  20104   1321  -2767  -1652       C  
ATOM   4898  O   LEU B1015     -16.389   0.491  46.109  1.00127.67           O  
ANISOU 4898  O   LEU B1015    20172   8057  20280    724  -2733  -1257       O  
ATOM   4899  CB  LEU B1015     -15.138   0.256  43.089  1.00125.59           C  
ANISOU 4899  CB  LEU B1015    20012   7807  19900   1647  -2975  -3104       C  
ATOM   4900  CG  LEU B1015     -15.136   0.808  41.658  1.00128.31           C  
ANISOU 4900  CG  LEU B1015    20226   8660  19866   1783  -2958  -3871       C  
ATOM   4901  CD1 LEU B1015     -15.064  -0.339  40.650  1.00136.02           C  
ANISOU 4901  CD1 LEU B1015    21528   8940  21214   1983  -3233  -4598       C  
ATOM   4902  CD2 LEU B1015     -16.358   1.695  41.401  1.00126.27           C  
ANISOU 4902  CD2 LEU B1015    19714   8928  19335   1214  -2900  -3830       C  
ATOM   4903  N   LYS B1016     -14.186   0.020  46.122  1.00127.53           N  
ANISOU 4903  N   LYS B1016    20351   7847  20256   1824  -2849  -1438       N  
ATOM   4904  CA  LYS B1016     -14.204  -0.542  47.476  1.00131.20           C  
ANISOU 4904  CA  LYS B1016    21009   7908  20932   1712  -2892   -629       C  
ATOM   4905  C   LYS B1016     -13.947   0.569  48.498  1.00130.07           C  
ANISOU 4905  C   LYS B1016    20584   8621  20216   1716  -2660   -113       C  
ATOM   4906  O   LYS B1016     -13.644   1.705  48.124  1.00123.50           O  
ANISOU 4906  O   LYS B1016    19427   8581  18918   1847  -2494   -410       O  
ATOM   4907  CB  LYS B1016     -13.157  -1.654  47.620  1.00140.45           C  
ANISOU 4907  CB  LYS B1016    22510   8329  22524   2301  -3145   -608       C  
ATOM   4908  CG  LYS B1016     -13.525  -2.954  46.902  1.00162.41           C  
ANISOU 4908  CG  LYS B1016    25674  10040  25996   2237  -3420   -993       C  
ATOM   4909  CD  LYS B1016     -12.527  -4.072  47.189  1.00179.29           C  
ANISOU 4909  CD  LYS B1016    28162  11351  28608   2850  -3690   -892       C  
ATOM   4910  CE  LYS B1016     -12.741  -4.691  48.562  1.00194.12           C  
ANISOU 4910  CE  LYS B1016    30316  12698  30741   2623  -3781    104       C  
ATOM   4911  NZ  LYS B1016     -11.653  -5.637  48.920  1.00210.34           N  
ANISOU 4911  NZ  LYS B1016    32680  14047  33193   3321  -4066    276       N  
ATOM   4912  N   ILE B1017     -14.073   0.239  49.782  1.00129.87           N  
ANISOU 4912  N   ILE B1017    20703   8425  20218   1563  -2658    658       N  
ATOM   4913  CA  ILE B1017     -13.816   1.199  50.862  1.00125.75           C  
ANISOU 4913  CA  ILE B1017    19962   8685  19133   1586  -2476   1139       C  
ATOM   4914  C   ILE B1017     -12.307   1.344  51.066  1.00129.65           C  
ANISOU 4914  C   ILE B1017    20404   9405  19452   2296  -2598   1082       C  
ATOM   4915  O   ILE B1017     -11.568   0.371  50.904  1.00134.73           O  
ANISOU 4915  O   ILE B1017    21284   9421  20485   2735  -2839   1025       O  
ATOM   4916  CB  ILE B1017     -14.463   0.750  52.196  1.00133.28           C  
ANISOU 4916  CB  ILE B1017    21106   9438  20095   1188  -2424   2008       C  
ATOM   4917  CG1 ILE B1017     -15.975   0.551  52.030  1.00135.21           C  
ANISOU 4917  CG1 ILE B1017    21330   9472  20572    445  -2284   2093       C  
ATOM   4918  CG2 ILE B1017     -14.187   1.775  53.295  1.00130.11           C  
ANISOU 4918  CG2 ILE B1017    20491   9909  19036   1247  -2249   2411       C  
ATOM   4919  CD1 ILE B1017     -16.670   0.052  53.283  1.00146.90           C  
ANISOU 4919  CD1 ILE B1017    22974  10767  22072     -9  -2172   2974       C  
ATOM   4920  N   TYR B1018     -11.857   2.550  51.417  1.00120.76           N  
ANISOU 4920  N   TYR B1018    18949   9153  17783   2411  -2450   1075       N  
ATOM   4921  CA  TYR B1018     -10.429   2.813  51.631  1.00120.51           C  
ANISOU 4921  CA  TYR B1018    18767   9447  17574   3029  -2566   1005       C  
ATOM   4922  C   TYR B1018     -10.178   3.833  52.743  1.00121.60           C  
ANISOU 4922  C   TYR B1018    18687  10362  17153   2992  -2479   1382       C  
ATOM   4923  O   TYR B1018     -11.095   4.534  53.172  1.00117.78           O  
ANISOU 4923  O   TYR B1018    18122  10265  16365   2524  -2273   1564       O  
ATOM   4924  CB  TYR B1018      -9.759   3.270  50.324  1.00118.63           C  
ANISOU 4924  CB  TYR B1018    18270   9473  17332   3349  -2512    239       C  
ATOM   4925  CG  TYR B1018     -10.097   4.684  49.888  1.00113.25           C  
ANISOU 4925  CG  TYR B1018    17242   9570  16216   3070  -2256    -52       C  
ATOM   4926  CD1 TYR B1018      -9.276   5.752  50.231  1.00111.48           C  
ANISOU 4926  CD1 TYR B1018    16688  10067  15603   3258  -2187    -64       C  
ATOM   4927  CD2 TYR B1018     -11.228   4.949  49.120  1.00111.61           C  
ANISOU 4927  CD2 TYR B1018    17036   9349  16022   2623  -2120   -317       C  
ATOM   4928  CE1 TYR B1018      -9.575   7.046  49.832  1.00106.61           C  
ANISOU 4928  CE1 TYR B1018    15793  10066  14646   3003  -1976   -304       C  
ATOM   4929  CE2 TYR B1018     -11.536   6.243  48.713  1.00106.56           C  
ANISOU 4929  CE2 TYR B1018    16105   9372  15012   2411  -1920   -545       C  
ATOM   4930  CZ  TYR B1018     -10.704   7.287  49.074  1.00110.96           C  
ANISOU 4930  CZ  TYR B1018    16380  10568  15212   2603  -1842   -525       C  
ATOM   4931  OH  TYR B1018     -11.003   8.574  48.682  1.00108.01           O  
ANISOU 4931  OH  TYR B1018    15755  10760  14524   2391  -1665   -722       O  
ATOM   4932  N   LYS B1019      -8.929   3.896  53.207  1.00120.28           N  
ANISOU 4932  N   LYS B1019    18407  10427  16865   3508  -2655   1461       N  
ATOM   4933  CA  LYS B1019      -8.508   4.883  54.205  1.00117.82           C  
ANISOU 4933  CA  LYS B1019    17868  10877  16022   3534  -2641   1706       C  
ATOM   4934  C   LYS B1019      -7.992   6.139  53.506  1.00116.36           C  
ANISOU 4934  C   LYS B1019    17246  11359  15606   3595  -2499   1137       C  
ATOM   4935  O   LYS B1019      -7.100   6.058  52.660  1.00115.94           O  
ANISOU 4935  O   LYS B1019    17011  11292  15751   3974  -2550    708       O  
ATOM   4936  CB  LYS B1019      -7.393   4.322  55.097  1.00125.69           C  
ANISOU 4936  CB  LYS B1019    18930  11818  17008   4054  -2966   2092       C  
ATOM   4937  CG  LYS B1019      -7.788   3.131  55.961  1.00149.95           C  
ANISOU 4937  CG  LYS B1019    22467  14256  20252   4020  -3139   2799       C  
ATOM   4938  CD  LYS B1019      -6.567   2.538  56.674  1.00167.22           C  
ANISOU 4938  CD  LYS B1019    24710  16350  22475   4648  -3527   3135       C  
ATOM   4939  CE  LYS B1019      -6.912   1.283  57.469  1.00185.41           C  
ANISOU 4939  CE  LYS B1019    27531  17923  24993   4647  -3728   3901       C  
ATOM   4940  NZ  LYS B1019      -5.698   0.661  58.067  1.00199.40           N  
ANISOU 4940  NZ  LYS B1019    29363  19552  26849   5336  -4160   4218       N  
ATOM   4941  N   ASP B1020      -8.534   7.298  53.866  1.00109.16           N  
ANISOU 4941  N   ASP B1020    16164  11025  14286   3232  -2311   1141       N  
ATOM   4942  CA  ASP B1020      -8.028   8.561  53.328  1.00104.53           C  
ANISOU 4942  CA  ASP B1020    15191  11036  13491   3254  -2197    687       C  
ATOM   4943  C   ASP B1020      -6.647   8.906  53.927  1.00110.62           C  
ANISOU 4943  C   ASP B1020    15703  12225  14103   3655  -2406    710       C  
ATOM   4944  O   ASP B1020      -6.053   8.088  54.638  1.00115.33           O  
ANISOU 4944  O   ASP B1020    16424  12629  14769   3988  -2662   1042       O  
ATOM   4945  CB  ASP B1020      -9.054   9.696  53.523  1.00101.85           C  
ANISOU 4945  CB  ASP B1020    14767  11103  12828   2775  -1965    659       C  
ATOM   4946  CG  ASP B1020      -9.304  10.038  54.991  1.00113.76           C  
ANISOU 4946  CG  ASP B1020    16337  12953  13934   2649  -1996   1088       C  
ATOM   4947  OD1 ASP B1020      -8.995   9.204  55.874  1.00119.32           O  
ANISOU 4947  OD1 ASP B1020    17245  13483  14607   2831  -2182   1529       O  
ATOM   4948  OD2 ASP B1020      -9.828  11.149  55.250  1.00116.21           O  
ANISOU 4948  OD2 ASP B1020    16505  13706  13942   2384  -1838    977       O  
ATOM   4949  N   THR B1021      -6.139  10.105  53.629  1.00103.75           N  
ANISOU 4949  N   THR B1021    14466  11906  13048   3615  -2320    372       N  
ATOM   4950  CA  THR B1021      -4.823  10.548  54.115  1.00105.22           C  
ANISOU 4950  CA  THR B1021    14317  12541  13120   3928  -2523    325       C  
ATOM   4951  C   THR B1021      -4.791  10.741  55.635  1.00111.85           C  
ANISOU 4951  C   THR B1021    15239  13676  13585   3908  -2735    731       C  
ATOM   4952  O   THR B1021      -3.718  10.720  56.246  1.00114.81           O  
ANISOU 4952  O   THR B1021    15415  14319  13887   4237  -3018    805       O  
ATOM   4953  CB  THR B1021      -4.387  11.878  53.457  1.00107.60           C  
ANISOU 4953  CB  THR B1021    14211  13338  13334   3774  -2365   -102       C  
ATOM   4954  OG1 THR B1021      -5.229  12.937  53.921  1.00102.62           O  
ANISOU 4954  OG1 THR B1021    13623  12975  12392   3347  -2244    -75       O  
ATOM   4955  CG2 THR B1021      -4.458  11.794  51.930  1.00104.06           C  
ANISOU 4955  CG2 THR B1021    13694  12707  13137   3768  -2125   -484       C  
ATOM   4956  N   GLU B1022      -5.969  10.947  56.227  1.00107.52           N  
ANISOU 4956  N   GLU B1022    14951  13129  12772   3532  -2595    971       N  
ATOM   4957  CA  GLU B1022      -6.128  11.099  57.678  1.00110.13           C  
ANISOU 4957  CA  GLU B1022    15419  13778  12649   3482  -2735   1364       C  
ATOM   4958  C   GLU B1022      -6.427   9.764  58.379  1.00119.75           C  
ANISOU 4958  C   GLU B1022    17039  14572  13889   3606  -2867   1963       C  
ATOM   4959  O   GLU B1022      -6.592   9.731  59.599  1.00122.63           O  
ANISOU 4959  O   GLU B1022    17573  15194  13825   3578  -2972   2378       O  
ATOM   4960  CB  GLU B1022      -7.258  12.097  57.987  1.00107.88           C  
ANISOU 4960  CB  GLU B1022    15167  13796  12028   3025  -2466   1287       C  
ATOM   4961  CG  GLU B1022      -7.158  13.455  57.264  1.00113.28           C  
ANISOU 4961  CG  GLU B1022    15525  14787  12731   2850  -2324    747       C  
ATOM   4962  CD  GLU B1022      -5.945  14.278  57.687  1.00135.21           C  
ANISOU 4962  CD  GLU B1022    17981  18042  15351   3022  -2568    528       C  
ATOM   4963  OE1 GLU B1022      -5.559  14.230  58.879  1.00134.43           O  
ANISOU 4963  OE1 GLU B1022    17928  18245  14905   3158  -2815    750       O  
ATOM   4964  OE2 GLU B1022      -5.380  14.983  56.824  1.00127.11           O  
ANISOU 4964  OE2 GLU B1022    16648  17109  14538   2998  -2520    142       O  
ATOM   4965  N   GLY B1023      -6.515   8.676  57.612  1.00118.17           N  
ANISOU 4965  N   GLY B1023    17014  13715  14172   3731  -2862   2009       N  
ATOM   4966  CA  GLY B1023      -6.663   7.325  58.174  1.00124.39           C  
ANISOU 4966  CA  GLY B1023    18200  13956  15106   3880  -3032   2589       C  
ATOM   4967  C   GLY B1023      -8.082   6.773  58.270  1.00129.14           C  
ANISOU 4967  C   GLY B1023    19157  14142  15770   3418  -2789   2936       C  
ATOM   4968  O   GLY B1023      -8.261   5.582  58.529  1.00134.34           O  
ANISOU 4968  O   GLY B1023    20165  14202  16677   3479  -2907   3404       O  
ATOM   4969  N   TYR B1024      -9.087   7.623  58.043  1.00120.78           N  
ANISOU 4969  N   TYR B1024    17990  13369  14532   2954  -2463   2715       N  
ATOM   4970  CA  TYR B1024     -10.499   7.252  58.249  1.00121.59           C  
ANISOU 4970  CA  TYR B1024    18323  13232  14644   2464  -2203   3042       C  
ATOM   4971  C   TYR B1024     -11.122   6.599  57.013  1.00124.13           C  
ANISOU 4971  C   TYR B1024    18721  12893  15550   2279  -2103   2791       C  
ATOM   4972  O   TYR B1024     -10.691   6.849  55.885  1.00120.39           O  
ANISOU 4972  O   TYR B1024    18065  12347  15332   2443  -2124   2231       O  
ATOM   4973  CB  TYR B1024     -11.331   8.485  58.625  1.00118.75           C  
ANISOU 4973  CB  TYR B1024    17765  13527  13828   2096  -1911   2893       C  
ATOM   4974  CG  TYR B1024     -10.668   9.429  59.613  1.00120.34           C  
ANISOU 4974  CG  TYR B1024    17822  14455  13448   2279  -2017   2878       C  
ATOM   4975  CD1 TYR B1024     -10.313   8.999  60.896  1.00128.04           C  
ANISOU 4975  CD1 TYR B1024    19007  15623  14019   2438  -2196   3429       C  
ATOM   4976  CD2 TYR B1024     -10.408  10.759  59.269  1.00115.83           C  
ANISOU 4976  CD2 TYR B1024    16921  14363  12724   2278  -1964   2316       C  
ATOM   4977  CE1 TYR B1024      -9.710   9.866  61.806  1.00129.23           C  
ANISOU 4977  CE1 TYR B1024    19028  16470  13603   2603  -2339   3354       C  
ATOM   4978  CE2 TYR B1024      -9.809  11.634  60.171  1.00117.15           C  
ANISOU 4978  CE2 TYR B1024    16960  15153  12399   2414  -2097   2239       C  
ATOM   4979  CZ  TYR B1024      -9.463  11.182  61.436  1.00130.31           C  
ANISOU 4979  CZ  TYR B1024    18825  17043  13645   2580  -2294   2726       C  
ATOM   4980  OH  TYR B1024      -8.872  12.046  62.327  1.00132.38           O  
ANISOU 4980  OH  TYR B1024    18962  17947  13389   2713  -2470   2591       O  
ATOM   4981  N   TYR B1025     -12.153   5.784  57.231  1.00123.86           N  
ANISOU 4981  N   TYR B1025    18947  12414  15701   1908  -1990   3201       N  
ATOM   4982  CA  TYR B1025     -12.836   5.093  56.134  1.00123.81           C  
ANISOU 4982  CA  TYR B1025    19031  11749  16263   1675  -1941   2964       C  
ATOM   4983  C   TYR B1025     -13.622   6.064  55.246  1.00120.55           C  
ANISOU 4983  C   TYR B1025    18314  11674  15814   1364  -1700   2414       C  
ATOM   4984  O   TYR B1025     -14.541   6.736  55.711  1.00118.37           O  
ANISOU 4984  O   TYR B1025    17899  11832  15245    997  -1455   2527       O  
ATOM   4985  CB  TYR B1025     -13.778   4.011  56.667  1.00131.47           C  
ANISOU 4985  CB  TYR B1025    20320  12163  17469   1275  -1886   3582       C  
ATOM   4986  CG  TYR B1025     -13.074   2.852  57.336  1.00140.78           C  
ANISOU 4986  CG  TYR B1025    21879  12786  18825   1582  -2169   4157       C  
ATOM   4987  CD1 TYR B1025     -12.876   2.837  58.716  1.00146.69           C  
ANISOU 4987  CD1 TYR B1025    22770  13872  19093   1634  -2193   4839       C  
ATOM   4988  CD2 TYR B1025     -12.610   1.763  56.593  1.00145.36           C  
ANISOU 4988  CD2 TYR B1025    22695  12498  20037   1850  -2433   4013       C  
ATOM   4989  CE1 TYR B1025     -12.231   1.768  59.341  1.00154.98           C  
ANISOU 4989  CE1 TYR B1025    24193  14399  20294   1945  -2494   5434       C  
ATOM   4990  CE2 TYR B1025     -11.961   0.691  57.208  1.00153.77           C  
ANISOU 4990  CE2 TYR B1025    24125  12984  21316   2183  -2728   4559       C  
ATOM   4991  CZ  TYR B1025     -11.776   0.701  58.581  1.00164.98           C  
ANISOU 4991  CZ  TYR B1025    25684  14744  22255   2227  -2767   5302       C  
ATOM   4992  OH  TYR B1025     -11.137  -0.351  59.196  1.00173.63           O  
ANISOU 4992  OH  TYR B1025    27160  15264  23547   2582  -3095   5901       O  
ATOM   4993  N   THR B1026     -13.236   6.118  53.971  1.00113.77           N  
ANISOU 4993  N   THR B1026    17357  10631  15239   1551  -1777   1826       N  
ATOM   4994  CA  THR B1026     -13.893   6.928  52.945  1.00108.11           C  
ANISOU 4994  CA  THR B1026    16398  10156  14523   1319  -1615   1304       C  
ATOM   4995  C   THR B1026     -14.291   5.982  51.809  1.00113.74           C  
ANISOU 4995  C   THR B1026    17266  10198  15754   1226  -1711   1011       C  
ATOM   4996  O   THR B1026     -13.870   4.826  51.804  1.00118.60           O  
ANISOU 4996  O   THR B1026    18157  10181  16725   1416  -1903   1142       O  
ATOM   4997  CB  THR B1026     -12.929   8.033  52.433  1.00110.35           C  
ANISOU 4997  CB  THR B1026    16407  10965  14556   1648  -1619    850       C  
ATOM   4998  OG1 THR B1026     -12.804   9.060  53.427  1.00107.74           O  
ANISOU 4998  OG1 THR B1026    15912  11261  13763   1626  -1531   1028       O  
ATOM   4999  CG2 THR B1026     -13.414   8.661  51.134  1.00104.51           C  
ANISOU 4999  CG2 THR B1026    15492  10340  13876   1502  -1516    318       C  
ATOM   5000  N   ILE B1027     -15.114   6.441  50.869  1.00106.68           N  
ANISOU 5000  N   ILE B1027    16212   9411  14909    951  -1614    609       N  
ATOM   5001  CA  ILE B1027     -15.446   5.637  49.685  1.00108.58           C  
ANISOU 5001  CA  ILE B1027    16584   9091  15579    885  -1746    212       C  
ATOM   5002  C   ILE B1027     -15.994   6.515  48.551  1.00107.58           C  
ANISOU 5002  C   ILE B1027    16217   9339  15320    744  -1672   -314       C  
ATOM   5003  O   ILE B1027     -16.521   7.598  48.802  1.00103.29           O  
ANISOU 5003  O   ILE B1027    15424   9352  14468    555  -1506   -262       O  
ATOM   5004  CB  ILE B1027     -16.464   4.508  50.041  1.00117.53           C  
ANISOU 5004  CB  ILE B1027    17938   9582  17136    440  -1795    564       C  
ATOM   5005  CG1 ILE B1027     -16.582   3.474  48.909  1.00121.93           C  
ANISOU 5005  CG1 ILE B1027    18708   9415  18205    442  -2019    122       C  
ATOM   5006  CG2 ILE B1027     -17.821   5.104  50.369  1.00116.84           C  
ANISOU 5006  CG2 ILE B1027    17608   9867  16920   -112  -1581    741       C  
ATOM   5007  CD1 ILE B1027     -17.396   2.239  49.273  1.00135.19           C  
ANISOU 5007  CD1 ILE B1027    20645  10315  20407     13  -2119    481       C  
ATOM   5008  N   GLY B1028     -15.845   6.048  47.310  1.00105.11           N  
ANISOU 5008  N   GLY B1028    15996   8722  15219    875  -1812   -827       N  
ATOM   5009  CA  GLY B1028     -16.428   6.707  46.136  1.00101.95           C  
ANISOU 5009  CA  GLY B1028    15427   8620  14690    739  -1798  -1308       C  
ATOM   5010  C   GLY B1028     -15.597   7.878  45.641  1.00100.52           C  
ANISOU 5010  C   GLY B1028    15047   9061  14085   1057  -1687  -1554       C  
ATOM   5011  O   GLY B1028     -14.407   7.709  45.336  1.00100.71           O  
ANISOU 5011  O   GLY B1028    15118   9082  14067   1485  -1708  -1738       O  
ATOM   5012  N   ILE B1029     -16.224   9.058  45.558  1.00 92.33           N  
ANISOU 5012  N   ILE B1029    13770   8541  12770    850  -1568  -1550       N  
ATOM   5013  CA  ILE B1029     -15.531  10.294  45.187  1.00 87.47           C  
ANISOU 5013  CA  ILE B1029    12966   8487  11780   1068  -1455  -1692       C  
ATOM   5014  C   ILE B1029     -15.204  11.050  46.465  1.00 88.66           C  
ANISOU 5014  C   ILE B1029    12986   8960  11742   1082  -1328  -1303       C  
ATOM   5015  O   ILE B1029     -15.674  12.171  46.694  1.00 85.08           O  
ANISOU 5015  O   ILE B1029    12347   8903  11077    935  -1226  -1239       O  
ATOM   5016  CB  ILE B1029     -16.362  11.185  44.236  1.00 88.05           C  
ANISOU 5016  CB  ILE B1029    12895   8886  11675    882  -1447  -1937       C  
ATOM   5017  CG1 ILE B1029     -16.807  10.389  43.008  1.00 91.72           C  
ANISOU 5017  CG1 ILE B1029    13502   9064  12284    837  -1621  -2349       C  
ATOM   5018  CG2 ILE B1029     -15.555  12.405  43.800  1.00 85.01           C  
ANISOU 5018  CG2 ILE B1029    12364   8995  10942   1094  -1332  -2032       C  
ATOM   5019  CD1 ILE B1029     -18.078   9.588  43.221  1.00102.08           C  
ANISOU 5019  CD1 ILE B1029    14856   9988  13943    444  -1755  -2287       C  
ATOM   5020  N   GLY B1030     -14.396  10.408  47.302  1.00 87.14           N  
ANISOU 5020  N   GLY B1030    12902   8578  11629   1287  -1367  -1064       N  
ATOM   5021  CA  GLY B1030     -13.958  10.995  48.553  1.00 85.51           C  
ANISOU 5021  CA  GLY B1030    12601   8683  11205   1343  -1301   -724       C  
ATOM   5022  C   GLY B1030     -15.102  11.392  49.464  1.00 88.43           C  
ANISOU 5022  C   GLY B1030    12912   9216  11471    990  -1191   -427       C  
ATOM   5023  O   GLY B1030     -15.152  12.532  49.944  1.00 85.18           O  
ANISOU 5023  O   GLY B1030    12325   9256  10782    957  -1089   -399       O  
ATOM   5024  N   HIS B1031     -16.026  10.458  49.681  1.00 87.87           N  
ANISOU 5024  N   HIS B1031    12972   8773  11641    721  -1202   -229       N  
ATOM   5025  CA  HIS B1031     -17.072  10.617  50.688  1.00 88.47           C  
ANISOU 5025  CA  HIS B1031    12976   9012  11628    387  -1052    124       C  
ATOM   5026  C   HIS B1031     -16.643   9.890  51.958  1.00 96.42           C  
ANISOU 5026  C   HIS B1031    14173   9882  12579    448  -1060    624       C  
ATOM   5027  O   HIS B1031     -16.383   8.686  51.928  1.00100.29           O  
ANISOU 5027  O   HIS B1031    14909   9830  13366    492  -1195    790       O  
ATOM   5028  CB  HIS B1031     -18.407  10.062  50.193  1.00 91.33           C  
ANISOU 5028  CB  HIS B1031    13305   9101  12297    -17  -1039     90       C  
ATOM   5029  CG  HIS B1031     -19.473  10.023  51.246  1.00 97.00           C  
ANISOU 5029  CG  HIS B1031    13912   9974  12969   -382   -843    495       C  
ATOM   5030  ND1 HIS B1031     -20.308  11.090  51.502  1.00 96.61           N  
ANISOU 5030  ND1 HIS B1031    13559  10445  12702   -527   -658    441       N  
ATOM   5031  CD2 HIS B1031     -19.836   9.046  52.111  1.00103.70           C  
ANISOU 5031  CD2 HIS B1031    14905  10542  13956   -623   -781    977       C  
ATOM   5032  CE1 HIS B1031     -21.142  10.771  52.477  1.00 99.55           C  
ANISOU 5032  CE1 HIS B1031    13858  10913  13056   -835   -460    837       C  
ATOM   5033  NE2 HIS B1031     -20.875   9.536  52.864  1.00104.35           N  
ANISOU 5033  NE2 HIS B1031    14741  11044  13863   -926   -523   1201       N  
ATOM   5034  N   LEU B1032     -16.582  10.624  53.066  1.00 92.33           N  
ANISOU 5034  N   LEU B1032    13564   9845  11674    465   -937    856       N  
ATOM   5035  CA  LEU B1032     -16.165  10.070  54.345  1.00 96.14           C  
ANISOU 5035  CA  LEU B1032    14230  10325  11975    543   -955   1360       C  
ATOM   5036  C   LEU B1032     -17.379   9.439  55.021  1.00104.47           C  
ANISOU 5036  C   LEU B1032    15342  11267  13084    118   -773   1806       C  
ATOM   5037  O   LEU B1032     -18.414  10.089  55.169  1.00102.91           O  
ANISOU 5037  O   LEU B1032    14915  11429  12759   -162   -546   1755       O  
ATOM   5038  CB  LEU B1032     -15.569  11.167  55.230  1.00 94.19           C  
ANISOU 5038  CB  LEU B1032    13860  10701  11229    743   -922   1356       C  
ATOM   5039  CG  LEU B1032     -14.554  10.750  56.298  1.00102.24           C  
ANISOU 5039  CG  LEU B1032    15056  11786  12003   1023  -1083   1724       C  
ATOM   5040  CD1 LEU B1032     -14.193  11.971  57.152  1.00100.64           C  
ANISOU 5040  CD1 LEU B1032    14696  12258  11283   1138  -1053   1622       C  
ATOM   5041  CD2 LEU B1032     -15.068   9.609  57.176  1.00110.61           C  
ANISOU 5041  CD2 LEU B1032    16382  12575  13071    839  -1040   2356       C  
ATOM   5042  N   LEU B1033     -17.245   8.177  55.421  1.00106.70           N  
ANISOU 5042  N   LEU B1033    15915  11044  13582     74   -868   2253       N  
ATOM   5043  CA  LEU B1033     -18.328   7.437  56.070  1.00112.01           C  
ANISOU 5043  CA  LEU B1033    16662  11540  14356   -384   -687   2772       C  
ATOM   5044  C   LEU B1033     -18.340   7.672  57.576  1.00119.30           C  
ANISOU 5044  C   LEU B1033    17631  12972  14726   -401   -509   3306       C  
ATOM   5045  O   LEU B1033     -19.345   8.103  58.139  1.00119.94           O  
ANISOU 5045  O   LEU B1033    17513  13497  14563   -724   -197   3456       O  
ATOM   5046  CB  LEU B1033     -18.181   5.940  55.798  1.00117.57           C  
ANISOU 5046  CB  LEU B1033    17706  11374  15591   -450   -890   3047       C  
ATOM   5047  CG  LEU B1033     -18.405   5.503  54.352  1.00121.28           C  
ANISOU 5047  CG  LEU B1033    18168  11294  16621   -521  -1053   2526       C  
ATOM   5048  CD1 LEU B1033     -17.774   4.147  54.106  1.00126.67           C  
ANISOU 5048  CD1 LEU B1033    19240  11109  17779   -350  -1336   2667       C  
ATOM   5049  CD2 LEU B1033     -19.893   5.476  54.029  1.00125.00           C  
ANISOU 5049  CD2 LEU B1033    18412  11756  17327  -1107   -872   2487       C  
ATOM   5050  N   THR B1034     -17.217   7.374  58.221  1.00118.12           N  
ANISOU 5050  N   THR B1034    17728  12791  14359    -26   -715   3576       N  
ATOM   5051  CA  THR B1034     -17.104   7.450  59.677  1.00122.02           C  
ANISOU 5051  CA  THR B1034    18339  13751  14270      4   -616   4125       C  
ATOM   5052  C   THR B1034     -15.652   7.723  60.085  1.00125.28           C  
ANISOU 5052  C   THR B1034    18856  14371  14374    554   -926   4071       C  
ATOM   5053  O   THR B1034     -14.721   7.443  59.322  1.00123.40           O  
ANISOU 5053  O   THR B1034    18662  13741  14483    889  -1215   3791       O  
ATOM   5054  CB  THR B1034     -17.622   6.136  60.348  1.00138.42           C  
ANISOU 5054  CB  THR B1034    20728  15371  16494   -314   -547   4928       C  
ATOM   5055  OG1 THR B1034     -17.484   6.217  61.773  1.00142.36           O  
ANISOU 5055  OG1 THR B1034    21368  16396  16326   -264   -446   5501       O  
ATOM   5056  CG2 THR B1034     -16.861   4.911  59.837  1.00140.12           C  
ANISOU 5056  CG2 THR B1034    21286  14681  17273    -95   -911   5084       C  
ATOM   5057  N   LYS B1035     -15.468   8.282  61.279  1.00123.39           N  
ANISOU 5057  N   LYS B1035    18621  14792  13470    650   -867   4302       N  
ATOM   5058  CA  LYS B1035     -14.132   8.434  61.867  1.00124.11           C  
ANISOU 5058  CA  LYS B1035    18809  15121  13225   1134  -1204   4345       C  
ATOM   5059  C   LYS B1035     -13.760   7.217  62.731  1.00135.99           C  
ANISOU 5059  C   LYS B1035    20710  16314  14644   1249  -1394   5140       C  
ATOM   5060  O   LYS B1035     -12.625   7.111  63.204  1.00137.62           O  
ANISOU 5060  O   LYS B1035    21018  16627  14642   1687  -1745   5260       O  
ATOM   5061  CB  LYS B1035     -14.047   9.729  62.688  1.00124.79           C  
ANISOU 5061  CB  LYS B1035    18705  16094  12615   1211  -1117   4095       C  
ATOM   5062  CG  LYS B1035     -14.127  10.990  61.837  1.00130.29           C  
ANISOU 5062  CG  LYS B1035    19046  17023  13435   1203  -1034   3314       C  
ATOM   5063  CD  LYS B1035     -13.789  12.256  62.619  1.00138.55           C  
ANISOU 5063  CD  LYS B1035    19940  18824  13878   1351  -1055   2995       C  
ATOM   5064  CE  LYS B1035     -13.700  13.457  61.680  1.00141.29           C  
ANISOU 5064  CE  LYS B1035    19975  19252  14455   1369  -1040   2263       C  
ATOM   5065  NZ  LYS B1035     -13.282  14.695  62.384  1.00148.89           N  
ANISOU 5065  NZ  LYS B1035    20807  20835  14930   1511  -1116   1896       N  
ATOM   5066  N   SER B1036     -14.718   6.303  62.917  1.00137.53           N  
ANISOU 5066  N   SER B1036    21113  16112  15030    847  -1181   5698       N  
ATOM   5067  CA  SER B1036     -14.543   5.108  63.753  1.00145.99           C  
ANISOU 5067  CA  SER B1036    22608  16814  16047    871  -1320   6571       C  
ATOM   5068  C   SER B1036     -13.466   4.155  63.199  1.00151.89           C  
ANISOU 5068  C   SER B1036    23585  16760  17365   1310  -1784   6616       C  
ATOM   5069  O   SER B1036     -13.286   4.073  61.978  1.00147.34           O  
ANISOU 5069  O   SER B1036    22880  15706  17399   1394  -1873   6049       O  
ATOM   5070  CB  SER B1036     -15.887   4.370  63.878  1.00154.27           C  
ANISOU 5070  CB  SER B1036    23773  17525  17316    245   -955   7105       C  
ATOM   5071  OG  SER B1036     -15.775   3.171  64.626  1.00171.67           O  
ANISOU 5071  OG  SER B1036    26423  19269  19536    208  -1076   8020       O  
ATOM   5072  N   PRO B1037     -12.748   3.431  64.091  1.00155.30           N  
ANISOU 5072  N   PRO B1037    24357  17068  17581   1625  -2085   7282       N  
ATOM   5073  CA  PRO B1037     -11.690   2.515  63.631  1.00157.84           C  
ANISOU 5073  CA  PRO B1037    24880  16634  18460   2128  -2548   7326       C  
ATOM   5074  C   PRO B1037     -12.184   1.162  63.100  1.00166.48           C  
ANISOU 5074  C   PRO B1037    26314  16607  20335   1905  -2574   7687       C  
ATOM   5075  O   PRO B1037     -11.425   0.453  62.429  1.00167.49           O  
ANISOU 5075  O   PRO B1037    26560  16018  21062   2318  -2915   7506       O  
ATOM   5076  CB  PRO B1037     -10.824   2.298  64.889  1.00166.09           C  
ANISOU 5076  CB  PRO B1037    26158  18022  18929   2550  -2885   7958       C  
ATOM   5077  CG  PRO B1037     -11.512   3.016  66.018  1.00171.67           C  
ANISOU 5077  CG  PRO B1037    26844  19641  18744   2212  -2567   8279       C  
ATOM   5078  CD  PRO B1037     -12.876   3.407  65.561  1.00163.25           C  
ANISOU 5078  CD  PRO B1037    25586  18642  17801   1570  -2026   8033       C  
ATOM   5079  N   SER B1038     -13.432   0.807  63.408  1.00166.12           N  
ANISOU 5079  N   SER B1038    26403  16414  20301   1262  -2219   8170       N  
ATOM   5080  CA  SER B1038     -14.010  -0.466  62.971  1.00171.60           C  
ANISOU 5080  CA  SER B1038    27418  16017  21763    935  -2237   8542       C  
ATOM   5081  C   SER B1038     -14.593  -0.336  61.561  1.00169.26           C  
ANISOU 5081  C   SER B1038    26861  15340  22108    664  -2105   7728       C  
ATOM   5082  O   SER B1038     -15.067   0.737  61.170  1.00161.36           O  
ANISOU 5082  O   SER B1038    25448  15008  20855    468  -1829   7141       O  
ATOM   5083  CB  SER B1038     -15.094  -0.923  63.955  1.00182.30           C  
ANISOU 5083  CB  SER B1038    28995  17412  22858    302  -1901   9476       C  
ATOM   5084  OG  SER B1038     -15.538  -2.234  63.657  1.00198.19           O  
ANISOU 5084  OG  SER B1038    31369  18287  25648    -19  -1981   9944       O  
ATOM   5085  N   LEU B1039     -14.546  -1.433  60.806  1.00169.54           N  
ANISOU 5085  N   LEU B1039    27160  14292  22965    679  -2334   7687       N  
ATOM   5086  CA  LEU B1039     -15.079  -1.472  59.441  1.00165.18           C  
ANISOU 5086  CA  LEU B1039    26425  13303  23031    438  -2277   6921       C  
ATOM   5087  C   LEU B1039     -16.596  -1.667  59.441  1.00170.53           C  
ANISOU 5087  C   LEU B1039    27037  13854  23903   -417  -1920   7173       C  
ATOM   5088  O   LEU B1039     -17.288  -1.155  58.557  1.00164.68           O  
ANISOU 5088  O   LEU B1039    25960  13283  23327   -719  -1749   6528       O  
ATOM   5089  CB  LEU B1039     -14.406  -2.592  58.635  1.00169.60           C  
ANISOU 5089  CB  LEU B1039    27304  12749  24388    828  -2688   6696       C  
ATOM   5090  CG  LEU B1039     -14.749  -2.697  57.143  1.00171.01           C  
ANISOU 5090  CG  LEU B1039    27341  12468  25168    711  -2712   5801       C  
ATOM   5091  CD1 LEU B1039     -14.263  -1.471  56.374  1.00161.35           C  
ANISOU 5091  CD1 LEU B1039    25662  12062  23581   1044  -2635   4920       C  
ATOM   5092  CD2 LEU B1039     -14.159  -3.972  56.556  1.00180.28           C  
ANISOU 5092  CD2 LEU B1039    28917  12457  27126   1081  -3114   5684       C  
ATOM   5093  N   ASN B1040     -17.104  -2.404  60.430  1.00175.02           N  
ANISOU 5093  N   ASN B1040    27904  14150  24446   -808  -1814   8133       N  
ATOM   5094  CA  ASN B1040     -18.546  -2.640  60.569  1.00178.17           C  
ANISOU 5094  CA  ASN B1040    28194  14476  25025  -1672  -1438   8488       C  
ATOM   5095  C   ASN B1040     -19.339  -1.358  60.863  1.00175.09           C  
ANISOU 5095  C   ASN B1040    27281  15277  23969  -1981   -967   8266       C  
ATOM   5096  O   ASN B1040     -20.545  -1.303  60.622  1.00175.21           O  
ANISOU 5096  O   ASN B1040    27017  15361  24193  -2630   -658   8224       O  
ATOM   5097  CB  ASN B1040     -18.816  -3.693  61.651  1.00190.40           C  
ANISOU 5097  CB  ASN B1040    30189  15526  26630  -2011  -1400   9669       C  
ATOM   5098  N   ALA B1041     -18.659  -0.341  61.389  1.00165.91           N  
ANISOU 5098  N   ALA B1041    25971  15029  22039  -1506   -937   8105       N  
ATOM   5099  CA  ALA B1041     -19.235   1.000  61.521  1.00158.92           C  
ANISOU 5099  CA  ALA B1041    24593  15224  20565  -1644   -564   7693       C  
ATOM   5100  C   ALA B1041     -19.289   1.706  60.162  1.00153.21           C  
ANISOU 5100  C   ALA B1041    23511  14536  20166  -1534   -634   6660       C  
ATOM   5101  O   ALA B1041     -20.253   2.412  59.860  1.00149.20           O  
ANISOU 5101  O   ALA B1041    22597  14495  19596  -1893   -335   6320       O  
ATOM   5102  CB  ALA B1041     -18.428   1.829  62.517  1.00157.79           C  
ANISOU 5102  CB  ALA B1041    24453  15962  19537  -1165   -572   7812       C  
ATOM   5103  N   ALA B1042     -18.245   1.515  59.357  1.00146.33           N  
ANISOU 5103  N   ALA B1042    22780  13205  19615  -1013  -1027   6184       N  
ATOM   5104  CA  ALA B1042     -18.174   2.081  58.009  1.00138.63           C  
ANISOU 5104  CA  ALA B1042    21530  12222  18921   -871  -1119   5252       C  
ATOM   5105  C   ALA B1042     -19.209   1.451  57.073  1.00143.94           C  
ANISOU 5105  C   ALA B1042    22148  12267  20275  -1395  -1095   5032       C  
ATOM   5106  O   ALA B1042     -19.916   2.164  56.356  1.00138.69           O  
ANISOU 5106  O   ALA B1042    21112  11954  19629  -1617   -952   4493       O  
ATOM   5107  CB  ALA B1042     -16.770   1.907  57.437  1.00137.37           C  
ANISOU 5107  CB  ALA B1042    21535  11740  18921   -187  -1508   4863       C  
ATOM   5108  N   LYS B1043     -19.287   0.119  57.085  1.00147.78           N  
ANISOU 5108  N   LYS B1043    23009  11805  21334  -1584  -1272   5447       N  
ATOM   5109  CA  LYS B1043     -20.260  -0.622  56.268  1.00151.02           C  
ANISOU 5109  CA  LYS B1043    23405  11515  22459  -2136  -1306   5267       C  
ATOM   5110  C   LYS B1043     -21.707  -0.281  56.636  1.00155.82           C  
ANISOU 5110  C   LYS B1043    23637  12595  22972  -2875   -900   5524       C  
ATOM   5111  O   LYS B1043     -22.562  -0.170  55.757  1.00154.11           O  
ANISOU 5111  O   LYS B1043    23127  12321  23109  -3247   -880   5035       O  
ATOM   5112  CB  LYS B1043     -20.047  -2.136  56.397  1.00162.85           C  
ANISOU 5112  CB  LYS B1043    25425  11844  24608  -2221  -1578   5760       C  
ATOM   5113  CG  LYS B1043     -18.810  -2.667  55.687  1.00175.68           C  
ANISOU 5113  CG  LYS B1043    27373  12803  26573  -1526  -2017   5311       C  
ATOM   5114  CD  LYS B1043     -18.755  -4.189  55.729  1.00194.74           C  
ANISOU 5114  CD  LYS B1043    30307  13939  29747  -1644  -2306   5735       C  
ATOM   5115  CE  LYS B1043     -17.552  -4.724  54.971  1.00204.92           C  
ANISOU 5115  CE  LYS B1043    31882  14569  31407   -893  -2733   5197       C  
ATOM   5116  NZ  LYS B1043     -17.484  -6.212  55.008  1.00222.26           N  
ANISOU 5116  NZ  LYS B1043    34566  15657  34225   -848  -2673   5450       N  
ATOM   5117  N   SER B1044     -21.971  -0.119  57.932  1.00155.08           N  
ANISOU 5117  N   SER B1044    23533  13011  22380  -3064   -583   6278       N  
ATOM   5118  CA  SER B1044     -23.308   0.225  58.420  1.00156.79           C  
ANISOU 5118  CA  SER B1044    23346  13792  22437  -3724   -129   6570       C  
ATOM   5119  C   SER B1044     -23.761   1.613  57.954  1.00151.83           C  
ANISOU 5119  C   SER B1044    22161  14081  21448  -3642     65   5855       C  
ATOM   5120  O   SER B1044     -24.939   1.818  57.658  1.00152.21           O  
ANISOU 5120  O   SER B1044    21783  14352  21697  -4153    287   5707       O  
ATOM   5121  CB  SER B1044     -23.346   0.152  59.948  1.00165.82           C  
ANISOU 5121  CB  SER B1044    24628  15389  22986  -3840    188   7512       C  
ATOM   5122  OG  SER B1044     -24.639   0.456  60.439  1.00177.47           O  
ANISOU 5122  OG  SER B1044    25676  17462  24293  -4467    682   7794       O  
ATOM   5123  N   GLU B1045     -22.827   2.559  57.899  1.00140.76           N  
ANISOU 5123  N   GLU B1045    20748  13188  19548  -3003    -35   5432       N  
ATOM   5124  CA  GLU B1045     -23.109   3.897  57.378  1.00132.64           C  
ANISOU 5124  CA  GLU B1045    19264  12908  18227  -2852     82   4740       C  
ATOM   5125  C   GLU B1045     -23.310   3.888  55.861  1.00132.46           C  
ANISOU 5125  C   GLU B1045    19102  12484  18743  -2870   -180   3993       C  
ATOM   5126  O   GLU B1045     -24.108   4.666  55.331  1.00128.63           O  
ANISOU 5126  O   GLU B1045    18187  12441  18244  -3031    -61   3560       O  
ATOM   5127  CB  GLU B1045     -21.981   4.866  57.747  1.00128.22           C  
ANISOU 5127  CB  GLU B1045    18763  12915  17040  -2204     15   4526       C  
ATOM   5128  CG  GLU B1045     -21.960   5.261  59.216  1.00140.95           C  
ANISOU 5128  CG  GLU B1045    20390  15217  17948  -2174    304   5077       C  
ATOM   5129  CD  GLU B1045     -23.106   6.185  59.585  1.00158.79           C  
ANISOU 5129  CD  GLU B1045    22174  18282  19878  -2473    736   4976       C  
ATOM   5130  OE1 GLU B1045     -23.100   7.354  59.138  1.00143.74           O  
ANISOU 5130  OE1 GLU B1045    19973  16857  17785  -2225    747   4345       O  
ATOM   5131  OE2 GLU B1045     -24.011   5.738  60.322  1.00159.29           O  
ANISOU 5131  OE2 GLU B1045    22148  18489  19885  -2950   1073   5540       O  
ATOM   5132  N   LEU B1046     -22.581   3.012  55.172  1.00129.96           N  
ANISOU 5132  N   LEU B1046    19154  11352  18874  -2667   -548   3834       N  
ATOM   5133  CA  LEU B1046     -22.678   2.882  53.715  1.00127.30           C  
ANISOU 5133  CA  LEU B1046    18760  10611  18998  -2646   -826   3108       C  
ATOM   5134  C   LEU B1046     -24.011   2.260  53.292  1.00135.66           C  
ANISOU 5134  C   LEU B1046    19620  11310  20615  -3345   -803   3109       C  
ATOM   5135  O   LEU B1046     -24.560   2.608  52.245  1.00132.45           O  
ANISOU 5135  O   LEU B1046    18939  10993  20393  -3455   -916   2501       O  
ATOM   5136  CB  LEU B1046     -21.516   2.034  53.187  1.00128.79           C  
ANISOU 5136  CB  LEU B1046    19406  10029  19499  -2205  -1200   2932       C  
ATOM   5137  CG  LEU B1046     -21.303   1.977  51.672  1.00131.00           C  
ANISOU 5137  CG  LEU B1046    19687   9992  20093  -2006  -1492   2100       C  
ATOM   5138  CD1 LEU B1046     -20.946   3.345  51.109  1.00122.64           C  
ANISOU 5138  CD1 LEU B1046    18332   9726  18539  -1631  -1431   1552       C  
ATOM   5139  CD2 LEU B1046     -20.219   0.959  51.335  1.00137.24           C  
ANISOU 5139  CD2 LEU B1046    20940   9971  21234  -1581  -1816   2000       C  
ATOM   5140  N   ASP B1047     -24.517   1.342  54.112  1.00139.91           N  
ANISOU 5140  N   ASP B1047    20291  11454  21414  -3829   -671   3817       N  
ATOM   5141  CA  ASP B1047     -25.811   0.695  53.874  1.00145.97           C  
ANISOU 5141  CA  ASP B1047    20828  11880  22754  -4594   -619   3925       C  
ATOM   5142  C   ASP B1047     -26.981   1.590  54.285  1.00148.90           C  
ANISOU 5142  C   ASP B1047    20577  13169  22830  -4979   -207   4007       C  
ATOM   5143  O   ASP B1047     -28.112   1.388  53.834  1.00151.86           O  
ANISOU 5143  O   ASP B1047    20574  13488  23637  -5547   -185   3865       O  
ATOM   5144  CB  ASP B1047     -25.892  -0.627  54.641  1.00157.43           C  
ANISOU 5144  CB  ASP B1047    22659  12537  24620  -5008   -607   4737       C  
ATOM   5145  CG  ASP B1047     -24.747  -1.568  54.311  1.00169.34           C  
ANISOU 5145  CG  ASP B1047    24791  13074  26476  -4578  -1027   4686       C  
ATOM   5146  OD1 ASP B1047     -23.941  -1.239  53.412  1.00164.02           O  
ANISOU 5146  OD1 ASP B1047    24209  12369  25742  -3997  -1306   3969       O  
ATOM   5147  OD2 ASP B1047     -24.647  -2.631  54.960  1.00183.35           O  
ANISOU 5147  OD2 ASP B1047    26958  14126  28580  -4804  -1068   5384       O  
ATOM   5148  N   LYS B1048     -26.706   2.560  55.156  1.00141.41           N  
ANISOU 5148  N   LYS B1048    19505  13062  21162  -4658    103   4210       N  
ATOM   5149  CA  LYS B1048     -27.703   3.548  55.566  1.00139.81           C  
ANISOU 5149  CA  LYS B1048    18712  13798  20612  -4870    505   4193       C  
ATOM   5150  C   LYS B1048     -27.867   4.601  54.463  1.00135.94           C  
ANISOU 5150  C   LYS B1048    17873  13701  20076  -4579    337   3340       C  
ATOM   5151  O   LYS B1048     -28.989   4.908  54.055  1.00136.59           O  
ANISOU 5151  O   LYS B1048    17442  14083  20374  -4932    421   3101       O  
ATOM   5152  CB  LYS B1048     -27.295   4.202  56.897  1.00141.37           C  
ANISOU 5152  CB  LYS B1048    18958  14724  20033  -4584    863   4648       C  
ATOM   5153  CG  LYS B1048     -28.416   4.964  57.610  1.00157.43           C  
ANISOU 5153  CG  LYS B1048    20419  17679  21720  -4875   1370   4794       C  
ATOM   5154  CD  LYS B1048     -27.987   5.477  58.991  1.00168.20           C  
ANISOU 5154  CD  LYS B1048    21903  19731  22274  -4601   1712   5246       C  
ATOM   5155  CE  LYS B1048     -26.987   6.645  58.911  1.00171.09           C  
ANISOU 5155  CE  LYS B1048    22375  20527  22105  -3861   1552   4714       C  
ATOM   5156  NZ  LYS B1048     -27.557   7.892  58.315  1.00174.60           N  
ANISOU 5156  NZ  LYS B1048    22314  21543  22482  -3699   1615   4017       N  
ATOM   5157  N   ALA B1049     -26.745   5.132  53.975  1.00125.54           N  
ANISOU 5157  N   ALA B1049    16822  12384  18492  -3943     90   2915       N  
ATOM   5158  CA  ALA B1049     -26.755   6.145  52.917  1.00118.62           C  
ANISOU 5158  CA  ALA B1049    15698  11848  17524  -3629    -81   2178       C  
ATOM   5159  C   ALA B1049     -27.412   5.628  51.632  1.00124.00           C  
ANISOU 5159  C   ALA B1049    16248  12077  18789  -3934   -395   1720       C  
ATOM   5160  O   ALA B1049     -28.232   6.324  51.029  1.00122.02           O  
ANISOU 5160  O   ALA B1049    15555  12243  18565  -4026   -413   1334       O  
ATOM   5161  CB  ALA B1049     -25.332   6.640  52.635  1.00113.14           C  
ANISOU 5161  CB  ALA B1049    15348  11153  16486  -2956   -279   1890       C  
ATOM   5162  N   ILE B1050     -27.059   4.411  51.223  1.00124.21           N  
ANISOU 5162  N   ILE B1050    16664  11250  19282  -4069   -672   1744       N  
ATOM   5163  CA  ILE B1050     -27.637   3.797  50.024  1.00126.81           C  
ANISOU 5163  CA  ILE B1050    16927  11083  20173  -4374  -1018   1265       C  
ATOM   5164  C   ILE B1050     -29.041   3.263  50.312  1.00137.49           C  
ANISOU 5164  C   ILE B1050    17877  12376  21986  -5155   -885   1555       C  
ATOM   5165  O   ILE B1050     -30.027   3.781  49.788  1.00136.62           O  
ANISOU 5165  O   ILE B1050    17253  12691  21967  -5385   -909   1225       O  
ATOM   5166  CB  ILE B1050     -26.745   2.643  49.487  1.00132.68           C  
ANISOU 5166  CB  ILE B1050    18250  10871  21293  -4217  -1377   1118       C  
ATOM   5167  CG1 ILE B1050     -25.414   3.192  48.955  1.00126.39           C  
ANISOU 5167  CG1 ILE B1050    17740  10196  20087  -3456  -1525    703       C  
ATOM   5168  CG2 ILE B1050     -27.475   1.852  48.402  1.00138.37           C  
ANISOU 5168  CG2 ILE B1050    18919  11016  22638  -4641  -1735    652       C  
ATOM   5169  CD1 ILE B1050     -25.554   4.092  47.742  1.00128.47           C  
ANISOU 5169  CD1 ILE B1050    17762  10908  20144  -3227  -1692    -10       C  
ATOM   5170  N   GLY B1051     -29.115   2.238  51.158  1.00140.90           N  
ANISOU 5170  N   GLY B1051    18529  12294  22712  -5557   -749   2205       N  
ATOM   5171  CA  GLY B1051     -30.374   1.560  51.469  1.00149.06           C  
ANISOU 5171  CA  GLY B1051    19210  13162  24262  -6385   -606   2569       C  
ATOM   5172  C   GLY B1051     -30.304   0.040  51.425  1.00161.43           C  
ANISOU 5172  C   GLY B1051    21204  13601  26529  -6829   -840   2853       C  
ATOM   5173  O   GLY B1051     -31.168  -0.631  51.998  1.00169.07           O  
ANISOU 5173  O   GLY B1051    21977  14358  27904  -7552   -643   3396       O  
ATOM   5174  N   ARG B1052     -29.279  -0.504  50.755  1.00157.01           N  
ANISOU 5174  N   ARG B1052    21217  12309  26132  -6399  -1246   2492       N  
ATOM   5175  CA  ARG B1052     -29.147  -1.956  50.538  1.00165.21           C  
ANISOU 5175  CA  ARG B1052    22717  12143  27910  -6728  -1560   2607       C  
ATOM   5176  C   ARG B1052     -27.958  -2.559  51.300  1.00170.71           C  
ANISOU 5176  C   ARG B1052    24069  12284  28508  -6316  -1553   3155       C  
ATOM   5177  O   ARG B1052     -27.144  -1.827  51.870  1.00164.18           O  
ANISOU 5177  O   ARG B1052    23336  12035  27012  -5731  -1360   3335       O  
ATOM   5178  CB  ARG B1052     -28.999  -2.253  49.038  1.00164.77           C  
ANISOU 5178  CB  ARG B1052    22798  11589  28218  -6562  -2097   1646       C  
ATOM   5179  CG  ARG B1052     -27.647  -1.847  48.439  1.00166.31           C  
ANISOU 5179  CG  ARG B1052    23386  11833  27973  -5644  -2296   1118       C  
ATOM   5180  CD  ARG B1052     -27.679  -1.799  46.918  1.00172.65           C  
ANISOU 5180  CD  ARG B1052    24171  12524  28905  -5470  -2727    116       C  
ATOM   5181  NE  ARG B1052     -26.368  -1.461  46.359  1.00173.73           N  
ANISOU 5181  NE  ARG B1052    24660  12730  28618  -4623  -2859   -344       N  
ATOM   5182  CZ  ARG B1052     -25.351  -2.315  46.230  1.00189.69           C  
ANISOU 5182  CZ  ARG B1052    27239  13964  30872  -4230  -3068   -441       C  
ATOM   5183  NH1 ARG B1052     -25.464  -3.581  46.624  1.00185.61           N  
ANISOU 5183  NH1 ARG B1052    27062  12431  31029  -4587  -3207    -93       N  
ATOM   5184  NH2 ARG B1052     -24.203  -1.898  45.705  1.00170.21           N  
ANISOU 5184  NH2 ARG B1052    24974  11716  27981  -3466  -3134   -878       N  
ATOM   5185  N   ASN B1053     -27.868  -3.892  51.291  1.00176.00           N  
ANISOU 5185  N   ASN B1053    25183  11810  29878  -6618  -1804   3398       N  
ATOM   5186  CA  ASN B1053     -26.755  -4.613  51.922  1.00178.71           C  
ANISOU 5186  CA  ASN B1053    26180  11471  30250  -6205  -1891   3908       C  
ATOM   5187  C   ASN B1053     -25.539  -4.686  50.994  1.00178.45           C  
ANISOU 5187  C   ASN B1053    26545  11058  30199  -5380  -2299   3149       C  
ATOM   5188  O   ASN B1053     -25.270  -5.732  50.393  1.00183.88           O  
ANISOU 5188  O   ASN B1053    27645  10680  31540  -5366  -2692   2856       O  
ATOM   5189  CB  ASN B1053     -27.195  -6.022  52.327  1.00191.59           C  
ANISOU 5189  CB  ASN B1053    28139  11960  32696  -6878  -1995   4540       C  
ATOM   5190  N   THR B1054     -24.803  -3.574  50.906  1.00165.53           N  
ANISOU 5190  N   THR B1054    24774  10294  27825  -4701  -2188   2835       N  
ATOM   5191  CA  THR B1054     -23.716  -3.398  49.925  1.00160.51           C  
ANISOU 5191  CA  THR B1054    24360   9569  27059  -3931  -2489   2042       C  
ATOM   5192  C   THR B1054     -22.529  -4.346  50.128  1.00169.09           C  
ANISOU 5192  C   THR B1054    26051   9779  28417  -3407  -2739   2213       C  
ATOM   5193  O   THR B1054     -22.006  -4.908  49.161  1.00170.59           O  
ANISOU 5193  O   THR B1054    26514   9338  28964  -3063  -3091   1543       O  
ATOM   5194  CB  THR B1054     -23.172  -1.933  49.915  1.00157.47           C  
ANISOU 5194  CB  THR B1054    23666  10342  25822  -3377  -2269   1790       C  
ATOM   5195  OG1 THR B1054     -22.613  -1.602  51.193  1.00155.40           O  
ANISOU 5195  OG1 THR B1054    23479  10475  25092  -3144  -2004   2520       O  
ATOM   5196  CG2 THR B1054     -24.276  -0.938  49.570  1.00151.52           C  
ANISOU 5196  CG2 THR B1054    22328  10420  24823  -3764  -2081   1517       C  
ATOM   5197  N   ASN B1055     -22.112  -4.512  51.383  1.00168.07           N  
ANISOU 5197  N   ASN B1055    26120   9647  28091  -3315  -2566   3092       N  
ATOM   5198  CA  ASN B1055     -20.936  -5.316  51.737  1.00172.22           C  
ANISOU 5198  CA  ASN B1055    27185   9443  28807  -2740  -2806   3368       C  
ATOM   5199  C   ASN B1055     -19.620  -4.661  51.294  1.00169.18           C  
ANISOU 5199  C   ASN B1055    26796   9533  27952  -1815  -2902   2805       C  
ATOM   5200  O   ASN B1055     -18.652  -5.356  50.981  1.00172.10           O  
ANISOU 5200  O   ASN B1055    27532   9231  28628  -1246  -3202   2580       O  
ATOM   5201  CB  ASN B1055     -21.052  -6.745  51.175  1.00182.77           C  
ANISOU 5201  CB  ASN B1055    28967   9387  31090  -2929  -3199   3197       C  
ATOM   5202  N   GLY B1056     -19.594  -3.326  51.273  1.00156.79           N  
ANISOU 5202  N   GLY B1056    24791   9106  25675  -1672  -2642   2580       N  
ATOM   5203  CA  GLY B1056     -18.388  -2.561  50.934  1.00149.83           C  
ANISOU 5203  CA  GLY B1056    23826   8793  24308   -889  -2673   2122       C  
ATOM   5204  C   GLY B1056     -18.297  -2.080  49.493  1.00148.91           C  
ANISOU 5204  C   GLY B1056    23513   8917  24149   -674  -2768   1118       C  
ATOM   5205  O   GLY B1056     -17.675  -1.048  49.219  1.00141.16           O  
ANISOU 5205  O   GLY B1056    22283   8722  22631   -259  -2656    785       O  
ATOM   5206  N   VAL B1057     -18.922  -2.818  48.575  1.00150.16           N  
ANISOU 5206  N   VAL B1057    23788   8407  24858   -978  -2984    646       N  
ATOM   5207  CA  VAL B1057     -18.805  -2.553  47.137  1.00147.20           C  
ANISOU 5207  CA  VAL B1057    23313   8171  24444   -744  -3130   -331       C  
ATOM   5208  C   VAL B1057     -19.967  -1.712  46.599  1.00146.86           C  
ANISOU 5208  C   VAL B1057    22847   8778  24175  -1262  -3007   -616       C  
ATOM   5209  O   VAL B1057     -21.115  -1.894  47.002  1.00149.13           O  
ANISOU 5209  O   VAL B1057    22997   8959  24709  -1943  -2942   -258       O  
ATOM   5210  CB  VAL B1057     -18.706  -3.876  46.326  1.00159.23           C  
ANISOU 5210  CB  VAL B1057    25247   8578  26676   -671  -3511   -837       C  
ATOM   5211  CG1 VAL B1057     -17.431  -4.628  46.683  1.00163.05           C  
ANISOU 5211  CG1 VAL B1057    26120   8457  27377      9  -3665   -692       C  
ATOM   5212  CG2 VAL B1057     -19.931  -4.762  46.551  1.00166.50           C  
ANISOU 5212  CG2 VAL B1057    26281   8731  28250  -1483  -3633   -537       C  
ATOM   5213  N   ILE B1058     -19.652  -0.787  45.693  1.00137.50           N  
ANISOU 5213  N   ILE B1058    21439   8281  22524   -928  -2974  -1231       N  
ATOM   5214  CA  ILE B1058     -20.662   0.047  45.029  1.00133.84           C  
ANISOU 5214  CA  ILE B1058    20592   8435  21826  -1302  -2924  -1567       C  
ATOM   5215  C   ILE B1058     -20.353   0.194  43.535  1.00136.93           C  
ANISOU 5215  C   ILE B1058    21013   8949  22066   -970  -3127  -2469       C  
ATOM   5216  O   ILE B1058     -19.318  -0.280  43.064  1.00138.23           O  
ANISOU 5216  O   ILE B1058    21457   8798  22267   -431  -3245  -2840       O  
ATOM   5217  CB  ILE B1058     -20.763   1.456  45.675  1.00129.31           C  
ANISOU 5217  CB  ILE B1058    19628   8868  20635  -1290  -2583  -1202       C  
ATOM   5218  CG1 ILE B1058     -19.430   2.211  45.588  1.00124.12           C  
ANISOU 5218  CG1 ILE B1058    18983   8707  19472   -604  -2478  -1344       C  
ATOM   5219  CG2 ILE B1058     -21.203   1.341  47.126  1.00131.81           C  
ANISOU 5219  CG2 ILE B1058    19893   9173  21014  -1652  -2357   -356       C  
ATOM   5220  CD1 ILE B1058     -19.576   3.705  45.780  1.00123.97           C  
ANISOU 5220  CD1 ILE B1058    18583   9644  18875   -585  -2227  -1255       C  
ATOM   5221  N   THR B1059     -21.256   0.842  42.797  1.00131.45           N  
ANISOU 5221  N   THR B1059    20020   8745  21182  -1269  -3168  -2816       N  
ATOM   5222  CA  THR B1059     -21.056   1.105  41.369  1.00130.62           C  
ANISOU 5222  CA  THR B1059    19927   8900  20801   -983  -3350  -3625       C  
ATOM   5223  C   THR B1059     -20.773   2.591  41.137  1.00126.47           C  
ANISOU 5223  C   THR B1059    19099   9387  19565   -712  -3116  -3628       C  
ATOM   5224  O   THR B1059     -20.798   3.392  42.076  1.00121.29           O  
ANISOU 5224  O   THR B1059    18219   9179  18687   -765  -2845  -3071       O  
ATOM   5225  CB  THR B1059     -22.283   0.670  40.522  1.00144.12           C  
ANISOU 5225  CB  THR B1059    21561  10377  22821  -1500  -3673  -4092       C  
ATOM   5226  OG1 THR B1059     -23.402   1.518  40.814  1.00140.49           O  
ANISOU 5226  OG1 THR B1059    20648  10509  22224  -1964  -3565  -3789       O  
ATOM   5227  CG2 THR B1059     -22.653  -0.785  40.803  1.00151.56           C  
ANISOU 5227  CG2 THR B1059    22791  10241  24553  -1875  -3916  -4051       C  
ATOM   5228  N   LYS B1060     -20.501   2.946  39.882  1.00122.26           N  
ANISOU 5228  N   LYS B1060    18583   9198  18673   -423  -3227  -4260       N  
ATOM   5229  CA  LYS B1060     -20.186   4.328  39.504  1.00115.45           C  
ANISOU 5229  CA  LYS B1060    17482   9228  17156   -167  -3033  -4276       C  
ATOM   5230  C   LYS B1060     -21.394   5.267  39.626  1.00115.96           C  
ANISOU 5230  C   LYS B1060    17169   9808  17083   -589  -3011  -4049       C  
ATOM   5231  O   LYS B1060     -21.223   6.447  39.925  1.00109.93           O  
ANISOU 5231  O   LYS B1060    16187   9658  15923   -464  -2785  -3768       O  
ATOM   5232  CB  LYS B1060     -19.616   4.377  38.076  1.00119.34           C  
ANISOU 5232  CB  LYS B1060    18118   9952  17272    227  -3151  -4981       C  
ATOM   5233  CG  LYS B1060     -19.028   5.737  37.667  1.00126.68           C  
ANISOU 5233  CG  LYS B1060    18864  11739  17531    540  -2915  -4939       C  
ATOM   5234  CD  LYS B1060     -18.253   5.647  36.347  1.00138.26           C  
ANISOU 5234  CD  LYS B1060    20507  13432  18595    976  -2953  -5573       C  
ATOM   5235  CE  LYS B1060     -17.614   6.983  35.962  1.00142.09           C  
ANISOU 5235  CE  LYS B1060    20813  14738  18438   1238  -2685  -5444       C  
ATOM   5236  NZ  LYS B1060     -18.619   8.005  35.535  1.00147.28           N  
ANISOU 5236  NZ  LYS B1060    21268  15906  18786    951  -2774  -5341       N  
ATOM   5237  N   ASP B1061     -22.600   4.744  39.398  1.00116.65           N  
ANISOU 5237  N   ASP B1061    17162   9628  17532  -1078  -3261  -4191       N  
ATOM   5238  CA  ASP B1061     -23.830   5.535  39.528  1.00114.79           C  
ANISOU 5238  CA  ASP B1061    16505   9864  17247  -1471  -3266  -3998       C  
ATOM   5239  C   ASP B1061     -24.105   5.880  40.987  1.00115.74           C  
ANISOU 5239  C   ASP B1061    16403  10081  17493  -1688  -2945  -3288       C  
ATOM   5240  O   ASP B1061     -24.443   7.026  41.314  1.00110.87           O  
ANISOU 5240  O   ASP B1061    15473  10077  16578  -1675  -2765  -3045       O  
ATOM   5241  CB  ASP B1061     -25.037   4.772  38.976  1.00123.25           C  
ANISOU 5241  CB  ASP B1061    17475  10605  18750  -1977  -3632  -4334       C  
ATOM   5242  CG  ASP B1061     -24.918   4.472  37.496  1.00138.51           C  
ANISOU 5242  CG  ASP B1061    19613  12522  20491  -1789  -3997  -5103       C  
ATOM   5243  OD1 ASP B1061     -24.274   3.460  37.141  1.00143.34           O  
ANISOU 5243  OD1 ASP B1061    20614  12547  21300  -1621  -4132  -5474       O  
ATOM   5244  OD2 ASP B1061     -25.489   5.238  36.690  1.00144.11           O  
ANISOU 5244  OD2 ASP B1061    20102  13809  20845  -1791  -4163  -5347       O  
ATOM   5245  N   GLU B1062     -23.969   4.873  41.851  1.00115.53           N  
ANISOU 5245  N   GLU B1062    16560   9437  17901  -1872  -2886  -2964       N  
ATOM   5246  CA  GLU B1062     -24.218   5.021  43.290  1.00114.14           C  
ANISOU 5246  CA  GLU B1062    16227   9328  17813  -2098  -2576  -2263       C  
ATOM   5247  C   GLU B1062     -23.311   6.074  43.932  1.00110.44           C  
ANISOU 5247  C   GLU B1062    15734   9397  16833  -1658  -2276  -1971       C  
ATOM   5248  O   GLU B1062     -23.771   6.886  44.738  1.00107.08           O  
ANISOU 5248  O   GLU B1062    15017   9445  16225  -1779  -2035  -1603       O  
ATOM   5249  CB  GLU B1062     -24.058   3.673  44.004  1.00121.41           C  
ANISOU 5249  CB  GLU B1062    17449   9429  19251  -2314  -2600  -1941       C  
ATOM   5250  CG  GLU B1062     -25.156   2.665  43.661  1.00138.87           C  
ANISOU 5250  CG  GLU B1062    19616  11075  22074  -2919  -2858  -2092       C  
ATOM   5251  CD  GLU B1062     -25.105   1.402  44.513  1.00163.11           C  
ANISOU 5251  CD  GLU B1062    22974  13302  25698  -3215  -2848  -1626       C  
ATOM   5252  OE1 GLU B1062     -24.071   1.167  45.177  1.00154.79           O  
ANISOU 5252  OE1 GLU B1062    22238  12026  24550  -2840  -2723  -1292       O  
ATOM   5253  OE2 GLU B1062     -26.100   0.641  44.520  1.00161.71           O  
ANISOU 5253  OE2 GLU B1062    22697  12675  26069  -3835  -2984  -1570       O  
ATOM   5254  N   ALA B1063     -22.030   6.058  43.574  1.00104.29           N  
ANISOU 5254  N   ALA B1063    15233   8553  15838  -1151  -2295  -2171       N  
ATOM   5255  CA  ALA B1063     -21.092   7.082  44.028  1.00 97.91           C  
ANISOU 5255  CA  ALA B1063    14376   8256  14568   -747  -2062  -1980       C  
ATOM   5256  C   ALA B1063     -21.438   8.452  43.426  1.00 96.25           C  
ANISOU 5256  C   ALA B1063    13882   8734  13955   -683  -2018  -2172       C  
ATOM   5257  O   ALA B1063     -21.362   9.484  44.101  1.00 91.42           O  
ANISOU 5257  O   ALA B1063    13083   8584  13070   -609  -1808  -1896       O  
ATOM   5258  CB  ALA B1063     -19.669   6.683  43.665  1.00 98.70           C  
ANISOU 5258  CB  ALA B1063    14773   8141  14588   -243  -2107  -2196       C  
ATOM   5259  N   GLU B1064     -21.835   8.435  42.155  1.00 93.94           N  
ANISOU 5259  N   GLU B1064    13581   8479  13632   -706  -2247  -2652       N  
ATOM   5260  CA  GLU B1064     -22.129   9.651  41.399  1.00 90.33           C  
ANISOU 5260  CA  GLU B1064    12915   8613  12792   -607  -2270  -2835       C  
ATOM   5261  C   GLU B1064     -23.320  10.419  41.977  1.00 92.60           C  
ANISOU 5261  C   GLU B1064    12819   9244  13118   -905  -2195  -2567       C  
ATOM   5262  O   GLU B1064     -23.308  11.651  41.992  1.00 88.21           O  
ANISOU 5262  O   GLU B1064    12094   9171  12252   -742  -2090  -2483       O  
ATOM   5263  CB  GLU B1064     -22.390   9.307  39.925  1.00 94.82           C  
ANISOU 5263  CB  GLU B1064    13586   9141  13300   -588  -2580  -3396       C  
ATOM   5264  CG  GLU B1064     -22.162  10.452  38.955  1.00103.13           C  
ANISOU 5264  CG  GLU B1064    14582  10767  13837   -320  -2601  -3583       C  
ATOM   5265  CD  GLU B1064     -22.444  10.078  37.498  1.00131.56           C  
ANISOU 5265  CD  GLU B1064    18309  14395  17284   -293  -2924  -4138       C  
ATOM   5266  OE1 GLU B1064     -22.959   8.964  37.228  1.00135.51           O  
ANISOU 5266  OE1 GLU B1064    18902  14458  18129   -522  -3172  -4438       O  
ATOM   5267  OE2 GLU B1064     -22.151  10.913  36.613  1.00126.66           O  
ANISOU 5267  OE2 GLU B1064    17707  14238  16182    -52  -2940  -4271       O  
ATOM   5268  N   LYS B1065     -24.341   9.694  42.445  1.00 92.66           N  
ANISOU 5268  N   LYS B1065    12678   8994  13533  -1340  -2243  -2438       N  
ATOM   5269  CA  LYS B1065     -25.528  10.323  43.044  1.00 92.09           C  
ANISOU 5269  CA  LYS B1065    12172   9279  13537  -1626  -2134  -2199       C  
ATOM   5270  C   LYS B1065     -25.240  10.824  44.462  1.00 92.86           C  
ANISOU 5270  C   LYS B1065    12198   9581  13505  -1564  -1765  -1715       C  
ATOM   5271  O   LYS B1065     -25.885  11.758  44.936  1.00 90.89           O  
ANISOU 5271  O   LYS B1065    11616   9780  13138  -1591  -1612  -1577       O  
ATOM   5272  CB  LYS B1065     -26.744   9.374  43.029  1.00100.39           C  
ANISOU 5272  CB  LYS B1065    13018  10041  15084  -2164  -2288  -2227       C  
ATOM   5273  CG  LYS B1065     -26.843   8.373  44.184  1.00116.73           C  
ANISOU 5273  CG  LYS B1065    15154  11679  17517  -2505  -2094  -1791       C  
ATOM   5274  CD  LYS B1065     -28.175   7.618  44.156  1.00131.87           C  
ANISOU 5274  CD  LYS B1065    16765  13391  19949  -3117  -2220  -1785       C  
ATOM   5275  CE  LYS B1065     -28.362   6.753  45.404  1.00144.37           C  
ANISOU 5275  CE  LYS B1065    18379  14615  21860  -3510  -1960  -1223       C  
ATOM   5276  NZ  LYS B1065     -29.585   5.897  45.338  1.00159.86           N  
ANISOU 5276  NZ  LYS B1065    20051  16291  24399  -4180  -2082  -1199       N  
ATOM   5277  N   LEU B1066     -24.273  10.197  45.130  1.00 89.19           N  
ANISOU 5277  N   LEU B1066    12044   8794  13049  -1448  -1646  -1488       N  
ATOM   5278  CA  LEU B1066     -23.846  10.622  46.463  1.00 86.84           C  
ANISOU 5278  CA  LEU B1066    11737   8710  12550  -1346  -1344  -1056       C  
ATOM   5279  C   LEU B1066     -22.940  11.841  46.362  1.00 84.71           C  
ANISOU 5279  C   LEU B1066    11494   8839  11854   -911  -1276  -1158       C  
ATOM   5280  O   LEU B1066     -22.983  12.737  47.206  1.00 82.14           O  
ANISOU 5280  O   LEU B1066    11011   8897  11303   -837  -1072   -964       O  
ATOM   5281  CB  LEU B1066     -23.119   9.474  47.173  1.00 89.76           C  
ANISOU 5281  CB  LEU B1066    12440   8581  13084  -1354  -1308   -755       C  
ATOM   5282  CG  LEU B1066     -22.539   9.695  48.580  1.00 93.67           C  
ANISOU 5282  CG  LEU B1066    13001   9258  13331  -1228  -1056   -284       C  
ATOM   5283  CD1 LEU B1066     -23.380  10.638  49.457  1.00 92.98           C  
ANISOU 5283  CD1 LEU B1066    12562   9746  13019  -1377   -785    -70       C  
ATOM   5284  CD2 LEU B1066     -22.341   8.336  49.266  1.00101.26           C  
ANISOU 5284  CD2 LEU B1066    14243   9655  14576  -1397  -1064    111       C  
ATOM   5285  N   PHE B1067     -22.122  11.856  45.316  1.00 79.09           N  
ANISOU 5285  N   PHE B1067    10980   8032  11040   -640  -1443  -1481       N  
ATOM   5286  CA  PHE B1067     -21.205  12.951  45.042  1.00 74.14           C  
ANISOU 5286  CA  PHE B1067    10376   7739  10055   -282  -1390  -1578       C  
ATOM   5287  C   PHE B1067     -21.937  14.282  44.827  1.00 74.23           C  
ANISOU 5287  C   PHE B1067    10111   8195   9899   -286  -1369  -1633       C  
ATOM   5288  O   PHE B1067     -21.405  15.345  45.140  1.00 70.49           O  
ANISOU 5288  O   PHE B1067     9598   7997   9186    -82  -1257  -1568       O  
ATOM   5289  CB  PHE B1067     -20.365  12.577  43.818  1.00 76.39           C  
ANISOU 5289  CB  PHE B1067    10886   7865  10275    -49  -1549  -1925       C  
ATOM   5290  CG  PHE B1067     -19.361  13.624  43.399  1.00 74.55           C  
ANISOU 5290  CG  PHE B1067    10663   7969   9694    270  -1476  -2005       C  
ATOM   5291  CD1 PHE B1067     -18.549  14.259  44.327  1.00 74.90           C  
ANISOU 5291  CD1 PHE B1067    10673   8192   9595    423  -1304  -1769       C  
ATOM   5292  CD2 PHE B1067     -19.200  13.936  42.051  1.00 76.90           C  
ANISOU 5292  CD2 PHE B1067    11010   8412   9797    396  -1588  -2315       C  
ATOM   5293  CE1 PHE B1067     -17.618  15.206  43.916  1.00 73.41           C  
ANISOU 5293  CE1 PHE B1067    10465   8279   9148    651  -1243  -1837       C  
ATOM   5294  CE2 PHE B1067     -18.270  14.880  41.642  1.00 77.37           C  
ANISOU 5294  CE2 PHE B1067    11071   8776   9551    634  -1488  -2330       C  
ATOM   5295  CZ  PHE B1067     -17.480  15.512  42.574  1.00 72.90           C  
ANISOU 5295  CZ  PHE B1067    10439   8340   8919    740  -1315  -2089       C  
ATOM   5296  N   ASN B1068     -23.155  14.215  44.295  1.00 72.16           N  
ANISOU 5296  N   ASN B1068     9646   7972   9798   -515  -1505  -1763       N  
ATOM   5297  CA  ASN B1068     -24.007  15.396  44.161  1.00 70.49           C  
ANISOU 5297  CA  ASN B1068     9134   8149   9499   -498  -1515  -1794       C  
ATOM   5298  C   ASN B1068     -24.396  15.915  45.537  1.00 72.99           C  
ANISOU 5298  C   ASN B1068     9234   8687   9811   -548  -1248  -1521       C  
ATOM   5299  O   ASN B1068     -24.246  17.099  45.826  1.00 70.07           O  
ANISOU 5299  O   ASN B1068     8782   8592   9251   -338  -1160  -1506       O  
ATOM   5300  CB  ASN B1068     -25.289  15.076  43.374  1.00 74.39           C  
ANISOU 5300  CB  ASN B1068     9395   8656  10212   -740  -1754  -1990       C  
ATOM   5301  CG  ASN B1068     -25.019  14.611  41.939  1.00 94.32           C  
ANISOU 5301  CG  ASN B1068    12137  11033  12669   -680  -2056  -2332       C  
ATOM   5302  OD1 ASN B1068     -23.916  14.772  41.411  1.00 84.62           O  
ANISOU 5302  OD1 ASN B1068    11190   9784  11177   -412  -2052  -2425       O  
ATOM   5303  ND2 ASN B1068     -26.040  14.033  41.305  1.00 89.91           N  
ANISOU 5303  ND2 ASN B1068    11419  10410  12333   -938  -2315  -2542       N  
ATOM   5304  N   GLN B1069     -24.887  15.011  46.382  1.00 71.87           N  
ANISOU 5304  N   GLN B1069     9019   8414   9874   -834  -1117  -1309       N  
ATOM   5305  CA  GLN B1069     -25.387  15.363  47.714  1.00 72.10           C  
ANISOU 5305  CA  GLN B1069     8824   8720   9851   -917   -826  -1046       C  
ATOM   5306  C   GLN B1069     -24.344  16.059  48.553  1.00 71.94           C  
ANISOU 5306  C   GLN B1069     8977   8852   9503   -628   -662   -932       C  
ATOM   5307  O   GLN B1069     -24.662  17.000  49.272  1.00 71.11           O  
ANISOU 5307  O   GLN B1069     8682   9099   9239   -525   -494   -912       O  
ATOM   5308  CB  GLN B1069     -25.840  14.119  48.471  1.00 77.77           C  
ANISOU 5308  CB  GLN B1069     9526   9227  10796  -1293   -691   -748       C  
ATOM   5309  CG  GLN B1069     -27.072  13.455  47.894  1.00 97.91           C  
ANISOU 5309  CG  GLN B1069    11799  11668  13734  -1684   -818   -834       C  
ATOM   5310  CD  GLN B1069     -27.241  12.020  48.366  1.00120.96           C  
ANISOU 5310  CD  GLN B1069    14835  14167  16958  -2090   -764   -544       C  
ATOM   5311  OE1 GLN B1069     -26.352  11.452  49.007  1.00116.24           O  
ANISOU 5311  OE1 GLN B1069    14584  13308  16274  -2022   -675   -278       O  
ATOM   5312  NE2 GLN B1069     -28.386  11.426  48.046  1.00116.63           N  
ANISOU 5312  NE2 GLN B1069    13987  13531  16797  -2520   -845   -579       N  
ATOM   5313  N   ASP B1070     -23.107  15.582  48.470  1.00 66.32           N  
ANISOU 5313  N   ASP B1070     8605   7885   8709   -485   -728   -894       N  
ATOM   5314  CA  ASP B1070     -22.013  16.119  49.281  1.00 63.78           C  
ANISOU 5314  CA  ASP B1070     8433   7700   8103   -235   -623   -791       C  
ATOM   5315  C   ASP B1070     -21.612  17.523  48.823  1.00 63.36           C  
ANISOU 5315  C   ASP B1070     8327   7869   7876     20   -678  -1021       C  
ATOM   5316  O   ASP B1070     -21.477  18.446  49.637  1.00 62.02           O  
ANISOU 5316  O   ASP B1070     8087   7959   7519    142   -562  -1008       O  
ATOM   5317  CB  ASP B1070     -20.792  15.198  49.209  1.00 65.94           C  
ANISOU 5317  CB  ASP B1070     9022   7644   8389   -124   -715   -709       C  
ATOM   5318  CG  ASP B1070     -21.064  13.800  49.760  1.00 81.67           C  
ANISOU 5318  CG  ASP B1070    11135   9314  10582   -354   -684   -418       C  
ATOM   5319  OD1 ASP B1070     -22.219  13.519  50.177  1.00 85.44           O  
ANISOU 5319  OD1 ASP B1070    11431   9844  11187   -664   -565   -259       O  
ATOM   5320  OD2 ASP B1070     -20.108  12.983  49.764  1.00 88.14           O  
ANISOU 5320  OD2 ASP B1070    12218   9815  11458   -223   -779   -337       O  
ATOM   5321  N   VAL B1071     -21.412  17.656  47.512  1.00 57.84           N  
ANISOU 5321  N   VAL B1071     7689   7053   7235     92   -861  -1230       N  
ATOM   5322  CA  VAL B1071     -21.116  18.936  46.872  1.00 54.79           C  
ANISOU 5322  CA  VAL B1071     7276   6820   6723    284   -931  -1388       C  
ATOM   5323  C   VAL B1071     -22.200  19.959  47.149  1.00 58.13           C  
ANISOU 5323  C   VAL B1071     7439   7475   7173    292   -895  -1435       C  
ATOM   5324  O   VAL B1071     -21.909  21.131  47.382  1.00 56.39           O  
ANISOU 5324  O   VAL B1071     7201   7375   6851    461   -873  -1485       O  
ATOM   5325  CB  VAL B1071     -21.005  18.776  45.353  1.00 58.49           C  
ANISOU 5325  CB  VAL B1071     7839   7177   7206    315  -1125  -1562       C  
ATOM   5326  CG1 VAL B1071     -21.246  20.116  44.654  1.00 57.30           C  
ANISOU 5326  CG1 VAL B1071     7611   7196   6964    442  -1214  -1644       C  
ATOM   5327  CG2 VAL B1071     -19.645  18.160  44.981  1.00 57.71           C  
ANISOU 5327  CG2 VAL B1071     7982   6924   7023    434  -1131  -1592       C  
ATOM   5328  N   ASP B1072     -23.449  19.512  47.100  1.00 56.38           N  
ANISOU 5328  N   ASP B1072     6995   7298   7128    111   -902  -1438       N  
ATOM   5329  CA  ASP B1072     -24.566  20.347  47.497  1.00 57.16           C  
ANISOU 5329  CA  ASP B1072     6772   7658   7288    144   -836  -1489       C  
ATOM   5330  C   ASP B1072     -24.480  20.683  48.987  1.00 60.45           C  
ANISOU 5330  C   ASP B1072     7128   8281   7558    192   -565  -1395       C  
ATOM   5331  O   ASP B1072     -24.746  21.817  49.384  1.00 60.40           O  
ANISOU 5331  O   ASP B1072     6990   8466   7493    387   -510  -1518       O  
ATOM   5332  CB  ASP B1072     -25.893  19.656  47.193  1.00 62.32           C  
ANISOU 5332  CB  ASP B1072     7129   8359   8191   -102   -887  -1505       C  
ATOM   5333  CG  ASP B1072     -27.063  20.593  47.314  1.00 74.60           C  
ANISOU 5333  CG  ASP B1072     8288  10212   9847      0   -872  -1612       C  
ATOM   5334  OD1 ASP B1072     -27.328  21.336  46.345  1.00 75.04           O  
ANISOU 5334  OD1 ASP B1072     8291  10277   9942    176  -1115  -1756       O  
ATOM   5335  OD2 ASP B1072     -27.701  20.594  48.384  1.00 82.76           O  
ANISOU 5335  OD2 ASP B1072     9060  11487  10900    -70   -611  -1543       O  
ATOM   5336  N   ALA B1073     -24.112  19.696  49.805  1.00 56.89           N  
ANISOU 5336  N   ALA B1073     6796   7785   7034     37   -416  -1185       N  
ATOM   5337  CA  ALA B1073     -23.886  19.914  51.238  1.00 57.00           C  
ANISOU 5337  CA  ALA B1073     6816   8039   6801     91   -177  -1070       C  
ATOM   5338  C   ALA B1073     -22.791  20.949  51.457  1.00 56.71           C  
ANISOU 5338  C   ALA B1073     6960   8031   6558    364   -241  -1212       C  
ATOM   5339  O   ALA B1073     -22.869  21.757  52.380  1.00 57.07           O  
ANISOU 5339  O   ALA B1073     6934   8331   6419    499   -115  -1308       O  
ATOM   5340  CB  ALA B1073     -23.519  18.613  51.927  1.00 59.52           C  
ANISOU 5340  CB  ALA B1073     7306   8247   7060   -105    -73   -751       C  
ATOM   5341  N   ALA B1074     -21.770  20.913  50.604  1.00 49.53           N  
ANISOU 5341  N   ALA B1074     6267   6869   5683    432   -432  -1248       N  
ATOM   5342  CA  ALA B1074     -20.721  21.921  50.617  1.00 46.58           C  
ANISOU 5342  CA  ALA B1074     6018   6490   5190    627   -515  -1377       C  
ATOM   5343  C   ALA B1074     -21.305  23.314  50.371  1.00 49.29           C  
ANISOU 5343  C   ALA B1074     6221   6902   5605    767   -557  -1592       C  
ATOM   5344  O   ALA B1074     -20.940  24.259  51.057  1.00 48.90           O  
ANISOU 5344  O   ALA B1074     6190   6937   5452    902   -537  -1726       O  
ATOM   5345  CB  ALA B1074     -19.659  21.592  49.585  1.00 45.31           C  
ANISOU 5345  CB  ALA B1074     6039   6096   5079    646   -668  -1364       C  
ATOM   5346  N   VAL B1075     -22.220  23.430  49.409  1.00 45.71           N  
ANISOU 5346  N   VAL B1075     5632   6394   5340    751   -648  -1638       N  
ATOM   5347  CA  VAL B1075     -22.892  24.705  49.100  1.00 46.00           C  
ANISOU 5347  CA  VAL B1075     5530   6455   5494    929   -730  -1807       C  
ATOM   5348  C   VAL B1075     -23.825  25.166  50.223  1.00 52.47           C  
ANISOU 5348  C   VAL B1075     6101   7538   6296   1030   -547  -1940       C  
ATOM   5349  O   VAL B1075     -23.758  26.312  50.662  1.00 52.84           O  
ANISOU 5349  O   VAL B1075     6147   7595   6335   1240   -553  -2133       O  
ATOM   5350  CB  VAL B1075     -23.716  24.613  47.793  1.00 50.15           C  
ANISOU 5350  CB  VAL B1075     5945   6909   6199    909   -917  -1802       C  
ATOM   5351  CG1 VAL B1075     -24.642  25.800  47.657  1.00 51.81           C  
ANISOU 5351  CG1 VAL B1075     5952   7170   6562   1132  -1004  -1943       C  
ATOM   5352  CG2 VAL B1075     -22.793  24.520  46.594  1.00 48.14           C  
ANISOU 5352  CG2 VAL B1075     5948   6450   5894    887  -1091  -1730       C  
ATOM   5353  N   ARG B1076     -24.697  24.274  50.680  1.00 50.73           N  
ANISOU 5353  N   ARG B1076     5665   7531   6081    873   -375  -1848       N  
ATOM   5354  CA  ARG B1076     -25.630  24.591  51.768  1.00 53.78           C  
ANISOU 5354  CA  ARG B1076     5763   8268   6402    953   -126  -1958       C  
ATOM   5355  C   ARG B1076     -24.900  25.128  53.000  1.00 57.06           C  
ANISOU 5355  C   ARG B1076     6338   8828   6514   1094     12  -2069       C  
ATOM   5356  O   ARG B1076     -25.388  26.036  53.674  1.00 58.97           O  
ANISOU 5356  O   ARG B1076     6428   9277   6699   1320    123  -2329       O  
ATOM   5357  CB  ARG B1076     -26.448  23.348  52.147  1.00 57.23           C  
ANISOU 5357  CB  ARG B1076     5974   8913   6855    661     85  -1742       C  
ATOM   5358  CG  ARG B1076     -27.395  22.892  51.053  1.00 68.92           C  
ANISOU 5358  CG  ARG B1076     7205  10317   8663    509    -68  -1717       C  
ATOM   5359  CD  ARG B1076     -28.216  21.687  51.467  1.00 82.99           C  
ANISOU 5359  CD  ARG B1076     8736  12267  10529    152    140  -1502       C  
ATOM   5360  NE  ARG B1076     -29.239  21.376  50.465  1.00 95.20           N  
ANISOU 5360  NE  ARG B1076     9964  13787  12420      4    -42  -1554       N  
ATOM   5361  CZ  ARG B1076     -30.364  22.073  50.268  1.00113.97           C  
ANISOU 5361  CZ  ARG B1076    11891  16426  14986    150    -64  -1743       C  
ATOM   5362  NH1 ARG B1076     -30.647  23.148  51.002  1.00103.20           N  
ANISOU 5362  NH1 ARG B1076    10351  15341  13518    477    112  -1926       N  
ATOM   5363  NH2 ARG B1076     -31.222  21.692  49.322  1.00103.35           N  
ANISOU 5363  NH2 ARG B1076    10256  15065  13947     -7   -291  -1784       N  
ATOM   5364  N   GLY B1077     -23.730  24.550  53.277  1.00 50.87           N  
ANISOU 5364  N   GLY B1077     5849   7942   5537    984    -18  -1906       N  
ATOM   5365  CA  GLY B1077     -22.900  24.938  54.410  1.00 50.73           C  
ANISOU 5365  CA  GLY B1077     5999   8076   5199   1092     42  -2001       C  
ATOM   5366  C   GLY B1077     -22.198  26.263  54.191  1.00 52.16           C  
ANISOU 5366  C   GLY B1077     6310   8054   5454   1295   -163  -2293       C  
ATOM   5367  O   GLY B1077     -22.147  27.098  55.087  1.00 54.30           O  
ANISOU 5367  O   GLY B1077     6586   8483   5564   1469   -117  -2570       O  
ATOM   5368  N   ILE B1078     -21.647  26.459  53.002  1.00 44.54           N  
ANISOU 5368  N   ILE B1078     5461   6738   4726   1260   -385  -2236       N  
ATOM   5369  CA  ILE B1078     -21.040  27.731  52.657  1.00 43.34           C  
ANISOU 5369  CA  ILE B1078     5423   6332   4713   1391   -576  -2440       C  
ATOM   5370  C   ILE B1078     -22.036  28.845  52.868  1.00 49.63           C  
ANISOU 5370  C   ILE B1078     6066   7139   5651   1630   -564  -2731       C  
ATOM   5371  O   ILE B1078     -21.696  29.882  53.430  1.00 51.27           O  
ANISOU 5371  O   ILE B1078     6354   7265   5861   1781   -629  -3017       O  
ATOM   5372  CB  ILE B1078     -20.593  27.768  51.199  1.00 43.79           C  
ANISOU 5372  CB  ILE B1078     5582   6068   4989   1308   -763  -2273       C  
ATOM   5373  CG1 ILE B1078     -19.308  26.964  51.021  1.00 42.05           C  
ANISOU 5373  CG1 ILE B1078     5519   5806   4650   1147   -794  -2086       C  
ATOM   5374  CG2 ILE B1078     -20.344  29.185  50.761  1.00 45.11           C  
ANISOU 5374  CG2 ILE B1078     5830   5946   5364   1427   -936  -2422       C  
ATOM   5375  CD1 ILE B1078     -18.990  26.662  49.589  1.00 47.72           C  
ANISOU 5375  CD1 ILE B1078     6308   6330   5492   1061   -897  -1912       C  
ATOM   5376  N   LEU B1079     -23.268  28.631  52.426  1.00 46.54           N  
ANISOU 5376  N   LEU B1079     5435   6840   5407   1678   -502  -2691       N  
ATOM   5377  CA  LEU B1079     -24.310  29.643  52.577  1.00 49.49           C  
ANISOU 5377  CA  LEU B1079     5600   7245   5960   1969   -495  -2975       C  
ATOM   5378  C   LEU B1079     -24.800  29.810  54.030  1.00 57.10           C  
ANISOU 5378  C   LEU B1079     6407   8612   6677   2124   -224  -3258       C  
ATOM   5379  O   LEU B1079     -25.178  30.915  54.431  1.00 59.83           O  
ANISOU 5379  O   LEU B1079     6691   8925   7116   2430   -240  -3626       O  
ATOM   5380  CB  LEU B1079     -25.492  29.341  51.645  1.00 50.16           C  
ANISOU 5380  CB  LEU B1079     5408   7365   6286   1985   -541  -2853       C  
ATOM   5381  CG  LEU B1079     -25.248  29.292  50.127  1.00 52.37           C  
ANISOU 5381  CG  LEU B1079     5821   7318   6758   1898   -826  -2621       C  
ATOM   5382  CD1 LEU B1079     -26.593  29.336  49.411  1.00 54.86           C  
ANISOU 5382  CD1 LEU B1079     5811   7723   7312   2022   -928  -2622       C  
ATOM   5383  CD2 LEU B1079     -24.328  30.406  49.616  1.00 53.52           C  
ANISOU 5383  CD2 LEU B1079     6271   7048   7015   1996  -1054  -2641       C  
ATOM   5384  N   ARG B1080     -24.790  28.722  54.807  1.00 53.75           N  
ANISOU 5384  N   ARG B1080     5937   8559   5927   1928     23  -3083       N  
ATOM   5385  CA  ARG B1080     -25.216  28.749  56.218  1.00 57.36           C  
ANISOU 5385  CA  ARG B1080     6263   9501   6029   2042    327  -3286       C  
ATOM   5386  C   ARG B1080     -24.160  29.328  57.164  1.00 61.81           C  
ANISOU 5386  C   ARG B1080     7114  10088   6282   2140    263  -3542       C  
ATOM   5387  O   ARG B1080     -24.464  29.601  58.319  1.00 65.67           O  
ANISOU 5387  O   ARG B1080     7537  10980   6434   2304    474  -3814       O  
ATOM   5388  CB  ARG B1080     -25.602  27.342  56.690  1.00 57.87           C  
ANISOU 5388  CB  ARG B1080     6198   9945   5844   1758    614  -2915       C  
ATOM   5389  N   ASN B1081     -22.932  29.506  56.672  1.00 54.75           N  
ANISOU 5389  N   ASN B1081     6511   8806   5486   2034    -24  -3472       N  
ATOM   5390  CA  ASN B1081     -21.811  30.053  57.455  1.00 55.19           C  
ANISOU 5390  CA  ASN B1081     6812   8845   5313   2075   -164  -3718       C  
ATOM   5391  C   ASN B1081     -21.671  31.568  57.255  1.00 60.25           C  
ANISOU 5391  C   ASN B1081     7532   9099   6261   2293   -391  -4157       C  
ATOM   5392  O   ASN B1081     -21.750  32.068  56.134  1.00 58.15           O  
ANISOU 5392  O   ASN B1081     7276   8389   6428   2298   -567  -4079       O  
ATOM   5393  CB  ASN B1081     -20.508  29.333  57.064  1.00 51.38           C  
ANISOU 5393  CB  ASN B1081     6533   8189   4798   1813   -341  -3382       C  
ATOM   5394  CG  ASN B1081     -19.279  29.863  57.802  1.00 69.57           C  
ANISOU 5394  CG  ASN B1081     9030  10492   6910   1820   -541  -3623       C  
ATOM   5395  OD1 ASN B1081     -18.715  30.899  57.440  1.00 61.17           O  
ANISOU 5395  OD1 ASN B1081     8054   9063   6124   1843   -775  -3865       O  
ATOM   5396  ND2 ASN B1081     -18.837  29.127  58.816  1.00 62.04           N  
ANISOU 5396  ND2 ASN B1081     8143   9935   5493   1777   -474  -3525       N  
ATOM   5397  N   ALA B1082     -21.437  32.280  58.353  1.00 60.58           N  
ANISOU 5397  N   ALA B1082     7657   9298   6063   2466   -403  -4612       N  
ATOM   5398  CA  ALA B1082     -21.438  33.745  58.364  1.00 63.72           C  
ANISOU 5398  CA  ALA B1082     8137   9307   6765   2705   -607  -5117       C  
ATOM   5399  C   ALA B1082     -20.229  34.381  57.672  1.00 66.17           C  
ANISOU 5399  C   ALA B1082     8680   9032   7428   2512   -969  -5078       C  
ATOM   5400  O   ALA B1082     -20.305  35.535  57.246  1.00 68.07           O  
ANISOU 5400  O   ALA B1082     9000   8768   8095   2642  -1167  -5322       O  
ATOM   5401  CB  ALA B1082     -21.529  34.248  59.801  1.00 69.94           C  
ANISOU 5401  CB  ALA B1082     8959  10471   7145   2945   -517  -5683       C  
ATOM   5402  N   LYS B1083     -19.127  33.637  57.565  1.00 59.36           N  
ANISOU 5402  N   LYS B1083     7910   8232   6412   2208  -1049  -4759       N  
ATOM   5403  CA  LYS B1083     -17.850  34.175  57.063  1.00 58.00           C  
ANISOU 5403  CA  LYS B1083     7894   7625   6520   1980  -1351  -4728       C  
ATOM   5404  C   LYS B1083     -17.596  33.859  55.593  1.00 57.06           C  
ANISOU 5404  C   LYS B1083     7768   7180   6733   1774  -1394  -4229       C  
ATOM   5405  O   LYS B1083     -16.941  34.641  54.901  1.00 56.95           O  
ANISOU 5405  O   LYS B1083     7851   6704   7082   1635  -1598  -4196       O  
ATOM   5406  CB  LYS B1083     -16.678  33.670  57.922  1.00 60.89           C  
ANISOU 5406  CB  LYS B1083     8316   8305   6514   1813  -1445  -4759       C  
ATOM   5407  CG  LYS B1083     -16.429  34.520  59.170  1.00 83.66           C  
ANISOU 5407  CG  LYS B1083    11293  11304   9192   1949  -1593  -5372       C  
ATOM   5408  CD  LYS B1083     -15.352  33.939  60.089  1.00 96.84           C  
ANISOU 5408  CD  LYS B1083    12995  13386  10413   1819  -1721  -5390       C  
ATOM   5409  CE  LYS B1083     -15.929  32.953  61.118  1.00110.66           C  
ANISOU 5409  CE  LYS B1083    14720  15824  11503   1978  -1460  -5307       C  
ATOM   5410  NZ  LYS B1083     -15.017  32.730  62.293  1.00124.52           N  
ANISOU 5410  NZ  LYS B1083    16556  18014  12741   1960  -1650  -5488       N  
ATOM   5411  N   LEU B1084     -18.121  32.726  55.126  1.00 50.10           N  
ANISOU 5411  N   LEU B1084     6778   6542   5717   1740  -1201  -3850       N  
ATOM   5412  CA  LEU B1084     -17.913  32.264  53.747  1.00 46.35           C  
ANISOU 5412  CA  LEU B1084     6304   5852   5454   1567  -1228  -3414       C  
ATOM   5413  C   LEU B1084     -19.009  32.714  52.772  1.00 50.76           C  
ANISOU 5413  C   LEU B1084     6811   6167   6309   1709  -1236  -3331       C  
ATOM   5414  O   LEU B1084     -18.744  32.850  51.580  1.00 48.81           O  
ANISOU 5414  O   LEU B1084     6630   5640   6277   1596  -1340  -3056       O  
ATOM   5415  CB  LEU B1084     -17.787  30.735  53.709  1.00 43.37           C  
ANISOU 5415  CB  LEU B1084     5865   5812   4799   1442  -1072  -3080       C  
ATOM   5416  CG  LEU B1084     -16.592  30.165  54.488  1.00 47.65           C  
ANISOU 5416  CG  LEU B1084     6459   6576   5072   1324  -1115  -3059       C  
ATOM   5417  CD1 LEU B1084     -16.770  28.675  54.730  1.00 46.05           C  
ANISOU 5417  CD1 LEU B1084     6218   6685   4593   1285   -950  -2764       C  
ATOM   5418  CD2 LEU B1084     -15.270  30.439  53.784  1.00 48.89           C  
ANISOU 5418  CD2 LEU B1084     6659   6486   5431   1134  -1290  -2951       C  
ATOM   5419  N   LYS B1085     -20.226  32.936  53.265  1.00 49.79           N  
ANISOU 5419  N   LYS B1085     6550   6195   6174   1969  -1128  -3560       N  
ATOM   5420  CA  LYS B1085     -21.332  33.384  52.408  1.00 50.63           C  
ANISOU 5420  CA  LYS B1085     6552   6110   6576   2160  -1178  -3507       C  
ATOM   5421  C   LYS B1085     -21.024  34.695  51.658  1.00 56.13           C  
ANISOU 5421  C   LYS B1085     7431   6221   7676   2220  -1447  -3525       C  
ATOM   5422  O   LYS B1085     -21.122  34.740  50.428  1.00 54.84           O  
ANISOU 5422  O   LYS B1085     7314   5833   7690   2165  -1565  -3191       O  
ATOM   5423  CB  LYS B1085     -22.640  33.529  53.206  1.00 56.48           C  
ANISOU 5423  CB  LYS B1085     7048   7148   7264   2472  -1006  -3822       C  
ATOM   5424  CG  LYS B1085     -23.884  33.652  52.331  1.00 71.26           C  
ANISOU 5424  CG  LYS B1085     8704   8966   9407   2665  -1046  -3718       C  
ATOM   5425  CD  LYS B1085     -24.983  34.480  52.983  1.00 86.51           C  
ANISOU 5425  CD  LYS B1085    10417  10977  11475   3086   -981  -4147       C  
ATOM   5426  CE  LYS B1085     -26.361  34.192  52.352  1.00 98.63           C  
ANISOU 5426  CE  LYS B1085    11585  12702  13188   3256   -950  -4032       C  
ATOM   5427  NZ  LYS B1085     -26.347  34.192  50.851  1.00105.54           N  
ANISOU 5427  NZ  LYS B1085    12548  13243  14309   3167  -1236  -3643       N  
ATOM   5428  N   PRO B1086     -20.640  35.760  52.383  1.00 55.40           N  
ANISOU 5428  N   PRO B1086     7465   5867   7719   2320  -1560  -3903       N  
ATOM   5429  CA  PRO B1086     -20.353  37.016  51.687  1.00 57.68           C  
ANISOU 5429  CA  PRO B1086     7953   5511   8452   2341  -1826  -3878       C  
ATOM   5430  C   PRO B1086     -19.311  36.867  50.569  1.00 58.59           C  
ANISOU 5430  C   PRO B1086     8218   5399   8644   1972  -1921  -3393       C  
ATOM   5431  O   PRO B1086     -19.452  37.473  49.499  1.00 59.26           O  
ANISOU 5431  O   PRO B1086     8418   5087   9010   1979  -2074  -3105       O  
ATOM   5432  CB  PRO B1086     -19.809  37.922  52.804  1.00 63.34           C  
ANISOU 5432  CB  PRO B1086     8795   6027   9246   2390  -1929  -4397       C  
ATOM   5433  CG  PRO B1086     -20.260  37.302  54.076  1.00 68.14           C  
ANISOU 5433  CG  PRO B1086     9236   7230   9426   2556  -1700  -4756       C  
ATOM   5434  CD  PRO B1086     -20.291  35.839  53.812  1.00 58.85           C  
ANISOU 5434  CD  PRO B1086     7910   6554   7896   2365  -1484  -4340       C  
ATOM   5435  N   VAL B1087     -18.282  36.062  50.834  1.00 51.99           N  
ANISOU 5435  N   VAL B1087     7368   4848   7537   1678  -1823  -3295       N  
ATOM   5436  CA  VAL B1087     -17.211  35.802  49.874  1.00 49.52           C  
ANISOU 5436  CA  VAL B1087     7130   4440   7244   1340  -1848  -2883       C  
ATOM   5437  C   VAL B1087     -17.766  35.103  48.638  1.00 50.70           C  
ANISOU 5437  C   VAL B1087     7247   4713   7304   1353  -1782  -2472       C  
ATOM   5438  O   VAL B1087     -17.594  35.592  47.522  1.00 51.47           O  
ANISOU 5438  O   VAL B1087     7467   4525   7565   1264  -1880  -2150       O  
ATOM   5439  CB  VAL B1087     -16.102  34.903  50.473  1.00 50.96           C  
ANISOU 5439  CB  VAL B1087     7235   4992   7136   1109  -1748  -2896       C  
ATOM   5440  CG1 VAL B1087     -14.862  34.952  49.590  1.00 50.28           C  
ANISOU 5440  CG1 VAL B1087     7183   4768   7153    777  -1780  -2567       C  
ATOM   5441  CG2 VAL B1087     -15.767  35.317  51.903  1.00 53.30           C  
ANISOU 5441  CG2 VAL B1087     7527   5354   7369   1154  -1818  -3369       C  
ATOM   5442  N   TYR B1088     -18.427  33.961  48.859  1.00 44.20           N  
ANISOU 5442  N   TYR B1088     6267   4318   6207   1446  -1627  -2481       N  
ATOM   5443  CA  TYR B1088     -19.055  33.143  47.804  1.00 41.54           C  
ANISOU 5443  CA  TYR B1088     5873   4146   5763   1457  -1589  -2187       C  
ATOM   5444  C   TYR B1088     -19.857  34.002  46.836  1.00 45.78           C  
ANISOU 5444  C   TYR B1088     6471   4384   6539   1629  -1773  -2040       C  
ATOM   5445  O   TYR B1088     -19.614  33.975  45.624  1.00 44.70           O  
ANISOU 5445  O   TYR B1088     6445   4164   6374   1523  -1846  -1697       O  
ATOM   5446  CB  TYR B1088     -19.978  32.097  48.461  1.00 41.80           C  
ANISOU 5446  CB  TYR B1088     5700   4583   5599   1565  -1431  -2320       C  
ATOM   5447  CG  TYR B1088     -20.603  31.055  47.538  1.00 42.38           C  
ANISOU 5447  CG  TYR B1088     5685   4849   5567   1523  -1407  -2091       C  
ATOM   5448  CD1 TYR B1088     -19.860  29.965  47.071  1.00 41.79           C  
ANISOU 5448  CD1 TYR B1088     5669   4912   5298   1313  -1334  -1902       C  
ATOM   5449  CD2 TYR B1088     -21.956  31.131  47.173  1.00 44.82           C  
ANISOU 5449  CD2 TYR B1088     5827   5213   5989   1710  -1475  -2115       C  
ATOM   5450  CE1 TYR B1088     -20.438  29.001  46.234  1.00 41.31           C  
ANISOU 5450  CE1 TYR B1088     5551   4990   5155   1272  -1345  -1768       C  
ATOM   5451  CE2 TYR B1088     -22.539  30.170  46.335  1.00 44.65           C  
ANISOU 5451  CE2 TYR B1088     5709   5370   5886   1639  -1502  -1955       C  
ATOM   5452  CZ  TYR B1088     -21.773  29.112  45.873  1.00 48.73           C  
ANISOU 5452  CZ  TYR B1088     6334   5977   6205   1411  -1440  -1798       C  
ATOM   5453  OH  TYR B1088     -22.336  28.162  45.055  1.00 49.37           O  
ANISOU 5453  OH  TYR B1088     6346   6195   6217   1338  -1496  -1711       O  
ATOM   5454  N   ASP B1089     -20.792  34.775  47.391  1.00 44.33           N  
ANISOU 5454  N   ASP B1089     6215   4062   6567   1923  -1850  -2306       N  
ATOM   5455  CA  ASP B1089     -21.638  35.672  46.606  1.00 47.33           C  
ANISOU 5455  CA  ASP B1089     6635   4126   7223   2173  -2071  -2193       C  
ATOM   5456  C   ASP B1089     -20.811  36.526  45.644  1.00 52.88           C  
ANISOU 5456  C   ASP B1089     7629   4372   8091   2009  -2242  -1841       C  
ATOM   5457  O   ASP B1089     -21.142  36.631  44.469  1.00 53.64           O  
ANISOU 5457  O   ASP B1089     7806   4391   8184   2047  -2383  -1484       O  
ATOM   5458  CB  ASP B1089     -22.458  36.597  47.524  1.00 53.05           C  
ANISOU 5458  CB  ASP B1089     7266   4673   8218   2541  -2130  -2612       C  
ATOM   5459  CG  ASP B1089     -23.668  35.903  48.174  1.00 62.15           C  
ANISOU 5459  CG  ASP B1089     8063   6308   9245   2772  -1964  -2873       C  
ATOM   5460  OD1 ASP B1089     -24.345  35.085  47.513  1.00 60.97           O  
ANISOU 5460  OD1 ASP B1089     7731   6451   8984   2756  -1953  -2668       O  
ATOM   5461  OD2 ASP B1089     -23.962  36.212  49.353  1.00 68.98           O  
ANISOU 5461  OD2 ASP B1089     8816   7271  10123   2964  -1845  -3300       O  
ATOM   5462  N   SER B1090     -19.726  37.113  46.148  1.00 50.17           N  
ANISOU 5462  N   SER B1090     7432   3759   7873   1801  -2232  -1927       N  
ATOM   5463  CA  SER B1090     -18.875  38.015  45.356  1.00 52.59           C  
ANISOU 5463  CA  SER B1090     7992   3596   8393   1575  -2363  -1579       C  
ATOM   5464  C   SER B1090     -18.134  37.347  44.189  1.00 55.26           C  
ANISOU 5464  C   SER B1090     8387   4165   8445   1271  -2259  -1098       C  
ATOM   5465  O   SER B1090     -17.690  38.032  43.268  1.00 57.84           O  
ANISOU 5465  O   SER B1090     8911   4185   8881   1113  -2344   -692       O  
ATOM   5466  CB  SER B1090     -17.851  38.726  46.261  1.00 57.30           C  
ANISOU 5466  CB  SER B1090     8668   3886   9219   1363  -2381  -1840       C  
ATOM   5467  OG  SER B1090     -16.760  37.883  46.606  1.00 61.07           O  
ANISOU 5467  OG  SER B1090     9037   4739   9427   1047  -2195  -1860       O  
ATOM   5468  N   LEU B1091     -18.006  36.022  44.225  1.00 48.07           N  
ANISOU 5468  N   LEU B1091     7314   3784   7166   1197  -2067  -1139       N  
ATOM   5469  CA  LEU B1091     -17.165  35.302  43.268  1.00 46.39           C  
ANISOU 5469  CA  LEU B1091     7133   3833   6662    936  -1929   -803       C  
ATOM   5470  C   LEU B1091     -17.928  34.860  42.023  1.00 51.63           C  
ANISOU 5470  C   LEU B1091     7845   4682   7090   1059  -1997   -523       C  
ATOM   5471  O   LEU B1091     -19.151  34.718  42.051  1.00 51.67           O  
ANISOU 5471  O   LEU B1091     7766   4748   7118   1333  -2124   -644       O  
ATOM   5472  CB  LEU B1091     -16.534  34.087  43.950  1.00 42.42           C  
ANISOU 5472  CB  LEU B1091     6457   3745   5917    820  -1720  -1018       C  
ATOM   5473  CG  LEU B1091     -15.634  34.377  45.153  1.00 46.80           C  
ANISOU 5473  CG  LEU B1091     6946   4227   6611    682  -1681  -1287       C  
ATOM   5474  CD1 LEU B1091     -15.171  33.080  45.797  1.00 43.49           C  
ANISOU 5474  CD1 LEU B1091     6365   4238   5922    644  -1519  -1446       C  
ATOM   5475  CD2 LEU B1091     -14.444  35.216  44.735  1.00 51.65           C  
ANISOU 5475  CD2 LEU B1091     7638   4579   7409    373  -1693  -1065       C  
ATOM   5476  N   ASP B1092     -17.186  34.652  40.933  1.00 49.24           N  
ANISOU 5476  N   ASP B1092     7651   4512   6544    854  -1912   -167       N  
ATOM   5477  CA  ASP B1092     -17.751  34.135  39.682  1.00 49.72           C  
ANISOU 5477  CA  ASP B1092     7784   4833   6275    946  -1978     72       C  
ATOM   5478  C   ASP B1092     -17.795  32.605  39.702  1.00 50.37           C  
ANISOU 5478  C   ASP B1092     7711   5379   6047    946  -1836   -160       C  
ATOM   5479  O   ASP B1092     -17.159  31.963  40.539  1.00 47.08           O  
ANISOU 5479  O   ASP B1092     7166   5081   5641    845  -1656   -393       O  
ATOM   5480  CB  ASP B1092     -16.959  34.621  38.462  1.00 54.75           C  
ANISOU 5480  CB  ASP B1092     8631   5454   6718    741  -1927    562       C  
ATOM   5481  CG  ASP B1092     -15.517  34.140  38.467  1.00 63.24           C  
ANISOU 5481  CG  ASP B1092     9630   6760   7639    432  -1616    589       C  
ATOM   5482  OD1 ASP B1092     -15.056  33.519  37.472  1.00 63.88           O  
ANISOU 5482  OD1 ASP B1092     9746   7213   7312    350  -1463    771       O  
ATOM   5483  OD2 ASP B1092     -14.848  34.388  39.486  1.00 68.36           O  
ANISOU 5483  OD2 ASP B1092    10161   7244   8567    295  -1537    394       O  
ATOM   5484  N   ALA B1093     -18.544  32.040  38.757  1.00 47.73           N  
ANISOU 5484  N   ALA B1093     7407   5280   5447   1065  -1954    -90       N  
ATOM   5485  CA  ALA B1093     -18.897  30.619  38.754  1.00 44.99           C  
ANISOU 5485  CA  ALA B1093     6928   5274   4892   1091  -1902   -351       C  
ATOM   5486  C   ALA B1093     -17.697  29.676  38.891  1.00 47.07           C  
ANISOU 5486  C   ALA B1093     7166   5739   4978    915  -1629   -449       C  
ATOM   5487  O   ALA B1093     -17.786  28.648  39.580  1.00 44.16           O  
ANISOU 5487  O   ALA B1093     6667   5478   4635    921  -1550   -720       O  
ATOM   5488  CB  ALA B1093     -19.685  30.291  37.492  1.00 48.03           C  
ANISOU 5488  CB  ALA B1093     7391   5874   4986   1199  -2111   -244       C  
ATOM   5489  N   VAL B1094     -16.586  30.029  38.238  1.00 45.43           N  
ANISOU 5489  N   VAL B1094     7070   5584   4608    767  -1481   -205       N  
ATOM   5490  CA  VAL B1094     -15.340  29.255  38.337  1.00 44.10           C  
ANISOU 5490  CA  VAL B1094     6824   5627   4305    638  -1214   -294       C  
ATOM   5491  C   VAL B1094     -14.727  29.337  39.732  1.00 45.45           C  
ANISOU 5491  C   VAL B1094     6836   5652   4781    564  -1123   -468       C  
ATOM   5492  O   VAL B1094     -14.579  28.322  40.398  1.00 43.09           O  
ANISOU 5492  O   VAL B1094     6424   5466   4482    610  -1054   -712       O  
ATOM   5493  CB  VAL B1094     -14.284  29.713  37.303  1.00 51.43           C  
ANISOU 5493  CB  VAL B1094     7842   6709   4992    479  -1036     29       C  
ATOM   5494  CG1 VAL B1094     -12.930  29.082  37.599  1.00 50.50           C  
ANISOU 5494  CG1 VAL B1094     7549   6799   4838    369   -753    -88       C  
ATOM   5495  CG2 VAL B1094     -14.732  29.356  35.898  1.00 53.85           C  
ANISOU 5495  CG2 VAL B1094     8318   7297   4847    572  -1092    151       C  
ATOM   5496  N   ARG B1095     -14.377  30.542  40.174  1.00 42.64           N  
ANISOU 5496  N   ARG B1095     6489   5028   4684    451  -1152   -342       N  
ATOM   5497  CA  ARG B1095     -13.767  30.720  41.492  1.00 40.76           C  
ANISOU 5497  CA  ARG B1095     6108   4676   4701    375  -1114   -543       C  
ATOM   5498  C   ARG B1095     -14.652  30.129  42.602  1.00 41.32           C  
ANISOU 5498  C   ARG B1095     6104   4751   4845    553  -1193   -856       C  
ATOM   5499  O   ARG B1095     -14.141  29.477  43.502  1.00 39.55           O  
ANISOU 5499  O   ARG B1095     5763   4648   4618    544  -1116  -1038       O  
ATOM   5500  CB  ARG B1095     -13.456  32.199  41.761  1.00 43.02           C  
ANISOU 5500  CB  ARG B1095     6450   4596   5298    225  -1200   -414       C  
ATOM   5501  CG  ARG B1095     -12.448  32.842  40.794  1.00 52.22           C  
ANISOU 5501  CG  ARG B1095     7660   5747   6437    -42  -1080    -40       C  
ATOM   5502  CD  ARG B1095     -12.180  34.317  41.164  1.00 61.80           C  
ANISOU 5502  CD  ARG B1095     8943   6482   8056   -234  -1202     77       C  
ATOM   5503  NE  ARG B1095     -11.040  34.908  40.452  1.00 69.82           N  
ANISOU 5503  NE  ARG B1095     9936   7482   9111   -588  -1047    446       N  
ATOM   5504  CZ  ARG B1095     -11.094  35.550  39.283  1.00 86.06           C  
ANISOU 5504  CZ  ARG B1095    12184   9438  11079   -705  -1020    923       C  
ATOM   5505  NH1 ARG B1095     -12.242  35.716  38.634  1.00 73.31           N  
ANISOU 5505  NH1 ARG B1095    10810   7717   9326   -462  -1189   1086       N  
ATOM   5506  NH2 ARG B1095      -9.976  36.032  38.751  1.00 76.81           N  
ANISOU 5506  NH2 ARG B1095    10940   8300   9944  -1079   -823   1267       N  
ATOM   5507  N   ARG B1096     -15.967  30.341  42.520  1.00 37.68           N  
ANISOU 5507  N   ARG B1096     5690   4191   4435    718  -1341   -890       N  
ATOM   5508  CA  ARG B1096     -16.929  29.696  43.433  1.00 35.95           C  
ANISOU 5508  CA  ARG B1096     5356   4052   4251    862  -1365  -1144       C  
ATOM   5509  C   ARG B1096     -16.761  28.176  43.499  1.00 39.21           C  
ANISOU 5509  C   ARG B1096     5706   4718   4473    842  -1250  -1229       C  
ATOM   5510  O   ARG B1096     -16.949  27.570  44.556  1.00 37.52           O  
ANISOU 5510  O   ARG B1096     5399   4574   4281    868  -1194  -1387       O  
ATOM   5511  CB  ARG B1096     -18.368  29.964  43.001  1.00 36.64           C  
ANISOU 5511  CB  ARG B1096     5434   4090   4399   1035  -1531  -1137       C  
ATOM   5512  CG  ARG B1096     -18.970  31.276  43.449  1.00 45.00           C  
ANISOU 5512  CG  ARG B1096     6495   4869   5733   1179  -1666  -1189       C  
ATOM   5513  CD  ARG B1096     -20.378  31.412  42.881  1.00 53.55           C  
ANISOU 5513  CD  ARG B1096     7510   5964   6870   1392  -1852  -1166       C  
ATOM   5514  NE  ARG B1096     -20.904  32.772  42.995  1.00 64.17           N  
ANISOU 5514  NE  ARG B1096     8896   6982   8504   1592  -2026  -1161       N  
ATOM   5515  CZ  ARG B1096     -21.999  33.218  42.376  1.00 79.39           C  
ANISOU 5515  CZ  ARG B1096    10782   8847  10535   1827  -2251  -1081       C  
ATOM   5516  NH1 ARG B1096     -22.700  32.417  41.581  1.00 67.49           N  
ANISOU 5516  NH1 ARG B1096     9179   7622   8844   1855  -2345  -1012       N  
ATOM   5517  NH2 ARG B1096     -22.395  34.475  42.544  1.00 66.43           N  
ANISOU 5517  NH2 ARG B1096     9192   6842   9205   2050  -2419  -1088       N  
ATOM   5518  N   ALA B1097     -16.454  27.552  42.364  1.00 36.84           N  
ANISOU 5518  N   ALA B1097     5477   4545   3975    808  -1221  -1123       N  
ATOM   5519  CA  ALA B1097     -16.078  26.140  42.368  1.00 35.65           C  
ANISOU 5519  CA  ALA B1097     5301   4554   3691    804  -1122  -1229       C  
ATOM   5520  C   ALA B1097     -14.854  25.977  43.262  1.00 39.66           C  
ANISOU 5520  C   ALA B1097     5733   5092   4244    758   -996  -1269       C  
ATOM   5521  O   ALA B1097     -14.913  25.272  44.262  1.00 38.62           O  
ANISOU 5521  O   ALA B1097     5543   4978   4153    792   -975  -1375       O  
ATOM   5522  CB  ALA B1097     -15.800  25.629  40.959  1.00 37.51           C  
ANISOU 5522  CB  ALA B1097     5639   4933   3681    809  -1103  -1173       C  
ATOM   5523  N   ALA B1098     -13.767  26.676  42.941  1.00 37.43           N  
ANISOU 5523  N   ALA B1098     5434   4829   3961    665   -927  -1157       N  
ATOM   5524  CA  ALA B1098     -12.530  26.548  43.706  1.00 37.40           C  
ANISOU 5524  CA  ALA B1098     5297   4900   4015    616   -845  -1207       C  
ATOM   5525  C   ALA B1098     -12.781  26.604  45.211  1.00 41.50           C  
ANISOU 5525  C   ALA B1098     5761   5359   4647    651   -923  -1352       C  
ATOM   5526  O   ALA B1098     -12.149  25.878  45.979  1.00 40.50           O  
ANISOU 5526  O   ALA B1098     5552   5343   4491    697   -903  -1422       O  
ATOM   5527  CB  ALA B1098     -11.544  27.615  43.298  1.00 40.20           C  
ANISOU 5527  CB  ALA B1098     5591   5244   4441    442   -790  -1059       C  
ATOM   5528  N   LEU B1099     -13.710  27.456  45.628  1.00 39.47           N  
ANISOU 5528  N   LEU B1099     5552   4949   4495    662  -1016  -1400       N  
ATOM   5529  CA  LEU B1099     -14.091  27.545  47.038  1.00 39.32           C  
ANISOU 5529  CA  LEU B1099     5492   4938   4509    723  -1060  -1573       C  
ATOM   5530  C   LEU B1099     -14.743  26.242  47.510  1.00 42.54           C  
ANISOU 5530  C   LEU B1099     5892   5478   4791    812  -1004  -1594       C  
ATOM   5531  O   LEU B1099     -14.254  25.602  48.444  1.00 42.28           O  
ANISOU 5531  O   LEU B1099     5827   5567   4672    837   -983  -1623       O  
ATOM   5532  CB  LEU B1099     -15.041  28.725  47.267  1.00 40.57           C  
ANISOU 5532  CB  LEU B1099     5690   4912   4814    773  -1149  -1665       C  
ATOM   5533  CG  LEU B1099     -15.499  28.982  48.705  1.00 46.02           C  
ANISOU 5533  CG  LEU B1099     6336   5658   5494    868  -1165  -1905       C  
ATOM   5534  CD1 LEU B1099     -14.306  29.091  49.622  1.00 46.71           C  
ANISOU 5534  CD1 LEU B1099     6385   5830   5531    793  -1201  -2017       C  
ATOM   5535  CD2 LEU B1099     -16.341  30.251  48.765  1.00 50.62           C  
ANISOU 5535  CD2 LEU B1099     6950   6016   6270    970  -1257  -2041       C  
ATOM   5536  N   ILE B1100     -15.829  25.847  46.849  1.00 38.63           N  
ANISOU 5536  N   ILE B1100     5425   4954   4298    842  -1004  -1556       N  
ATOM   5537  CA  ILE B1100     -16.504  24.580  47.147  1.00 38.04           C  
ANISOU 5537  CA  ILE B1100     5336   4948   4168    855   -955  -1547       C  
ATOM   5538  C   ILE B1100     -15.510  23.420  47.211  1.00 42.02           C  
ANISOU 5538  C   ILE B1100     5882   5483   4600    860   -913  -1490       C  
ATOM   5539  O   ILE B1100     -15.637  22.530  48.037  1.00 42.18           O  
ANISOU 5539  O   ILE B1100     5911   5532   4585    870   -878  -1449       O  
ATOM   5540  CB  ILE B1100     -17.528  24.224  46.068  1.00 41.32           C  
ANISOU 5540  CB  ILE B1100     5759   5319   4621    841  -1009  -1528       C  
ATOM   5541  CG1 ILE B1100     -18.653  25.254  46.013  1.00 42.43           C  
ANISOU 5541  CG1 ILE B1100     5817   5438   4866    895  -1083  -1576       C  
ATOM   5542  CG2 ILE B1100     -18.098  22.841  46.324  1.00 42.37           C  
ANISOU 5542  CG2 ILE B1100     5877   5461   4762    786   -972  -1517       C  
ATOM   5543  CD1 ILE B1100     -19.166  25.471  44.620  1.00 48.36           C  
ANISOU 5543  CD1 ILE B1100     6606   6146   5621    913  -1218  -1524       C  
ATOM   5544  N   ASN B1101     -14.536  23.432  46.310  1.00 38.68           N  
ANISOU 5544  N   ASN B1101     5481   5059   4156    867   -908  -1471       N  
ATOM   5545  CA  ASN B1101     -13.460  22.463  46.321  1.00 39.05           C  
ANISOU 5545  CA  ASN B1101     5524   5147   4166    938   -871  -1458       C  
ATOM   5546  C   ASN B1101     -12.765  22.474  47.665  1.00 43.09           C  
ANISOU 5546  C   ASN B1101     5966   5744   4663    976   -897  -1444       C  
ATOM   5547  O   ASN B1101     -12.617  21.433  48.302  1.00 42.71           O  
ANISOU 5547  O   ASN B1101     5953   5687   4589   1057   -910  -1387       O  
ATOM   5548  CB  ASN B1101     -12.465  22.781  45.200  1.00 41.45           C  
ANISOU 5548  CB  ASN B1101     5789   5528   4431    942   -814  -1458       C  
ATOM   5549  CG  ASN B1101     -11.265  21.842  45.178  1.00 63.24           C  
ANISOU 5549  CG  ASN B1101     8478   8370   7179   1073   -763  -1490       C  
ATOM   5550  OD1 ASN B1101     -10.486  21.771  46.139  1.00 57.75           O  
ANISOU 5550  OD1 ASN B1101     7673   7744   6526   1124   -798  -1476       O  
ATOM   5551  ND2 ASN B1101     -11.092  21.140  44.058  1.00 54.70           N  
ANISOU 5551  ND2 ASN B1101     7449   7306   6027   1161   -697  -1560       N  
ATOM   5552  N   MET B1102     -12.343  23.653  48.100  1.00 40.61           N  
ANISOU 5552  N   MET B1102     5570   5494   4366    915   -933  -1493       N  
ATOM   5553  CA  MET B1102     -11.597  23.759  49.356  1.00 41.62           C  
ANISOU 5553  CA  MET B1102     5620   5752   4441    949  -1009  -1530       C  
ATOM   5554  C   MET B1102     -12.412  23.235  50.529  1.00 46.29           C  
ANISOU 5554  C   MET B1102     6293   6396   4898   1002  -1015  -1500       C  
ATOM   5555  O   MET B1102     -11.923  22.438  51.334  1.00 46.77           O  
ANISOU 5555  O   MET B1102     6364   6555   4851   1092  -1062  -1414       O  
ATOM   5556  CB  MET B1102     -11.164  25.201  49.619  1.00 44.69           C  
ANISOU 5556  CB  MET B1102     5925   6150   4904    835  -1082  -1649       C  
ATOM   5557  CG  MET B1102      -9.895  25.581  48.897  1.00 49.41           C  
ANISOU 5557  CG  MET B1102     6369   6787   5618    745  -1076  -1625       C  
ATOM   5558  SD  MET B1102      -9.380  27.251  49.296  1.00 55.78           S  
ANISOU 5558  SD  MET B1102     7082   7516   6596    536  -1196  -1758       S  
ATOM   5559  CE  MET B1102      -8.939  27.121  51.029  1.00 53.98           C  
ANISOU 5559  CE  MET B1102     6786   7489   6235    616  -1388  -1951       C  
ATOM   5560  N   VAL B1103     -13.658  23.691  50.602  1.00 42.96           N  
ANISOU 5560  N   VAL B1103     5913   5932   4479    955   -961  -1547       N  
ATOM   5561  CA  VAL B1103     -14.621  23.209  51.587  1.00 43.82           C  
ANISOU 5561  CA  VAL B1103     6059   6141   4451    971   -892  -1497       C  
ATOM   5562  C   VAL B1103     -14.787  21.686  51.496  1.00 48.75           C  
ANISOU 5562  C   VAL B1103     6761   6690   5074    971   -847  -1283       C  
ATOM   5563  O   VAL B1103     -14.896  21.003  52.518  1.00 49.52           O  
ANISOU 5563  O   VAL B1103     6911   6887   5019    988   -817  -1134       O  
ATOM   5564  CB  VAL B1103     -15.982  23.925  51.403  1.00 47.41           C  
ANISOU 5564  CB  VAL B1103     6469   6571   4975    940   -822  -1600       C  
ATOM   5565  CG1 VAL B1103     -17.115  23.152  52.051  1.00 48.56           C  
ANISOU 5565  CG1 VAL B1103     6588   6831   5030    907   -686  -1495       C  
ATOM   5566  CG2 VAL B1103     -15.900  25.330  51.955  1.00 47.95           C  
ANISOU 5566  CG2 VAL B1103     6500   6686   5031    986   -876  -1831       C  
ATOM   5567  N   PHE B1104     -14.780  21.164  50.268  1.00 45.64           N  
ANISOU 5567  N   PHE B1104     6396   6108   4839    952   -852  -1268       N  
ATOM   5568  CA  PHE B1104     -14.954  19.728  50.027  1.00 46.54           C  
ANISOU 5568  CA  PHE B1104     6608   6049   5026    948   -843  -1130       C  
ATOM   5569  C   PHE B1104     -13.767  18.921  50.545  1.00 52.62           C  
ANISOU 5569  C   PHE B1104     7436   6800   5757   1096   -914  -1014       C  
ATOM   5570  O   PHE B1104     -13.900  17.737  50.828  1.00 54.13           O  
ANISOU 5570  O   PHE B1104     7745   6824   5999   1114   -925   -842       O  
ATOM   5571  CB  PHE B1104     -15.177  19.444  48.540  1.00 47.43           C  
ANISOU 5571  CB  PHE B1104     6751   5989   5282    923   -864  -1234       C  
ATOM   5572  CG  PHE B1104     -15.887  18.146  48.269  1.00 50.37           C  
ANISOU 5572  CG  PHE B1104     7221   6133   5786    846   -874  -1172       C  
ATOM   5573  CD1 PHE B1104     -17.272  18.115  48.127  1.00 53.83           C  
ANISOU 5573  CD1 PHE B1104     7602   6544   6308    668   -852  -1175       C  
ATOM   5574  CD2 PHE B1104     -15.178  16.955  48.149  1.00 53.75           C  
ANISOU 5574  CD2 PHE B1104     7775   6347   6300    951   -924  -1128       C  
ATOM   5575  CE1 PHE B1104     -17.939  16.915  47.872  1.00 56.54           C  
ANISOU 5575  CE1 PHE B1104     8012   6642   6828    531   -885  -1130       C  
ATOM   5576  CE2 PHE B1104     -15.837  15.754  47.897  1.00 58.45           C  
ANISOU 5576  CE2 PHE B1104     8490   6640   7079    852   -963  -1091       C  
ATOM   5577  CZ  PHE B1104     -17.219  15.734  47.760  1.00 56.98           C  
ANISOU 5577  CZ  PHE B1104     8244   6419   6985    609   -946  -1090       C  
ATOM   5578  N   GLN B1105     -12.612  19.565  50.671  1.00 49.17           N  
ANISOU 5578  N   GLN B1105     6903   6517   5264   1197   -981  -1098       N  
ATOM   5579  CA  GLN B1105     -11.449  18.932  51.273  1.00 50.69           C  
ANISOU 5579  CA  GLN B1105     7082   6762   5417   1375  -1089  -1002       C  
ATOM   5580  C   GLN B1105     -11.493  19.053  52.788  1.00 57.08           C  
ANISOU 5580  C   GLN B1105     7920   7776   5990   1390  -1152   -873       C  
ATOM   5581  O   GLN B1105     -11.426  18.050  53.490  1.00 59.04           O  
ANISOU 5581  O   GLN B1105     8289   7977   6166   1481  -1205   -634       O  
ATOM   5582  CB  GLN B1105     -10.162  19.569  50.747  1.00 51.42           C  
ANISOU 5582  CB  GLN B1105     6981   6990   5568   1452  -1140  -1157       C  
ATOM   5583  CG  GLN B1105      -8.892  18.894  51.248  1.00 55.34           C  
ANISOU 5583  CG  GLN B1105     7384   7573   6070   1681  -1279  -1088       C  
ATOM   5584  CD  GLN B1105      -7.642  19.437  50.595  1.00 64.91           C  
ANISOU 5584  CD  GLN B1105     8323   8953   7387   1730  -1287  -1244       C  
ATOM   5585  OE1 GLN B1105      -7.673  20.491  49.951  1.00 57.94           O  
ANISOU 5585  OE1 GLN B1105     7343   8133   6538   1547  -1196  -1365       O  
ATOM   5586  NE2 GLN B1105      -6.527  18.718  50.756  1.00 55.18           N  
ANISOU 5586  NE2 GLN B1105     6947   7796   6224   1982  -1394  -1217       N  
ATOM   5587  N   MET B1106     -11.626  20.288  53.273  1.00 53.84           N  
ANISOU 5587  N   MET B1106     7426   7583   5449   1308  -1155  -1035       N  
ATOM   5588  CA  MET B1106     -11.369  20.637  54.684  1.00 56.23           C  
ANISOU 5588  CA  MET B1106     7731   8174   5460   1357  -1255  -1027       C  
ATOM   5589  C   MET B1106     -12.596  20.901  55.569  1.00 60.90           C  
ANISOU 5589  C   MET B1106     8408   8921   5810   1273  -1120  -1005       C  
ATOM   5590  O   MET B1106     -12.440  21.257  56.743  1.00 63.13           O  
ANISOU 5590  O   MET B1106     8710   9500   5775   1326  -1187  -1045       O  
ATOM   5591  CB  MET B1106     -10.514  21.903  54.742  1.00 58.78           C  
ANISOU 5591  CB  MET B1106     7885   8648   5800   1334  -1387  -1308       C  
ATOM   5592  CG  MET B1106      -9.108  21.758  54.224  1.00 63.28           C  
ANISOU 5592  CG  MET B1106     8280   9223   6542   1414  -1523  -1332       C  
ATOM   5593  SD  MET B1106      -8.341  23.389  54.204  1.00 68.34           S  
ANISOU 5593  SD  MET B1106     8702   9980   7285   1255  -1644  -1652       S  
ATOM   5594  CE  MET B1106      -9.280  24.200  52.909  1.00 62.07           C  
ANISOU 5594  CE  MET B1106     7965   8899   6719   1072  -1432  -1724       C  
ATOM   5595  N   GLY B1107     -13.803  20.765  55.029  1.00 56.05           N  
ANISOU 5595  N   GLY B1107     7816   8161   5321   1152   -935   -972       N  
ATOM   5596  CA  GLY B1107     -15.007  21.098  55.791  1.00 57.25           C  
ANISOU 5596  CA  GLY B1107     7963   8514   5275   1081   -763   -988       C  
ATOM   5597  C   GLY B1107     -15.148  22.593  56.032  1.00 61.02           C  
ANISOU 5597  C   GLY B1107     8346   9146   5693   1112   -778  -1357       C  
ATOM   5598  O   GLY B1107     -14.165  23.346  56.000  1.00 59.93           O  
ANISOU 5598  O   GLY B1107     8176   9009   5587   1161   -956  -1559       O  
ATOM   5599  N   GLU B1108     -16.382  23.011  56.294  1.00 58.96           N  
ANISOU 5599  N   GLU B1108     8022   9003   5377   1083   -595  -1454       N  
ATOM   5600  CA  GLU B1108     -16.752  24.431  56.353  1.00 59.24           C  
ANISOU 5600  CA  GLU B1108     7972   9083   5453   1151   -601  -1837       C  
ATOM   5601  C   GLU B1108     -15.908  25.275  57.325  1.00 65.23           C  
ANISOU 5601  C   GLU B1108     8778  10039   5969   1252   -759  -2116       C  
ATOM   5602  O   GLU B1108     -15.301  26.264  56.912  1.00 64.06           O  
ANISOU 5602  O   GLU B1108     8609   9702   6028   1253   -931  -2370       O  
ATOM   5603  CB  GLU B1108     -18.249  24.578  56.692  1.00 62.53           C  
ANISOU 5603  CB  GLU B1108     8268   9683   5808   1162   -352  -1895       C  
ATOM   5604  CG  GLU B1108     -19.217  24.152  55.551  1.00 72.64           C  
ANISOU 5604  CG  GLU B1108     9430  10743   7428   1054   -265  -1757       C  
ATOM   5605  CD  GLU B1108     -19.718  22.695  55.635  1.00 95.67           C  
ANISOU 5605  CD  GLU B1108    12343  13693  10312    881   -116  -1376       C  
ATOM   5606  OE1 GLU B1108     -19.972  22.193  56.755  1.00 99.22           O  
ANISOU 5606  OE1 GLU B1108    12809  14443  10447    849     54  -1208       O  
ATOM   5607  OE2 GLU B1108     -19.887  22.064  54.566  1.00 84.88           O  
ANISOU 5607  OE2 GLU B1108    10971  12047   9234    765   -173  -1246       O  
ATOM   5608  N   THR B1109     -15.865  24.878  58.598  1.00 64.60           N  
ANISOU 5608  N   THR B1109     8764  10336   5443   1314   -715  -2057       N  
ATOM   5609  CA  THR B1109     -15.177  25.660  59.632  1.00 67.26           C  
ANISOU 5609  CA  THR B1109     9149  10933   5472   1419   -892  -2381       C  
ATOM   5610  C   THR B1109     -13.649  25.696  59.485  1.00 70.26           C  
ANISOU 5610  C   THR B1109     9536  11213   5945   1397  -1217  -2395       C  
ATOM   5611  O   THR B1109     -12.996  26.594  60.023  1.00 72.44           O  
ANISOU 5611  O   THR B1109     9803  11586   6133   1429  -1434  -2754       O  
ATOM   5612  CB  THR B1109     -15.524  25.171  61.068  1.00 80.84           C  
ANISOU 5612  CB  THR B1109    10958  13176   6580   1505   -764  -2284       C  
ATOM   5613  OG1 THR B1109     -15.274  23.767  61.176  1.00 80.88           O  
ANISOU 5613  OG1 THR B1109    11052  13221   6459   1449   -737  -1749       O  
ATOM   5614  CG2 THR B1109     -16.985  25.450  61.408  1.00 81.76           C  
ANISOU 5614  CG2 THR B1109    10992  13512   6561   1547   -420  -2403       C  
ATOM   5615  N   GLY B1110     -13.080  24.729  58.772  1.00 64.14           N  
ANISOU 5615  N   GLY B1110     8751  10254   5365   1347  -1258  -2045       N  
ATOM   5616  CA  GLY B1110     -11.632  24.700  58.538  1.00 63.68           C  
ANISOU 5616  CA  GLY B1110     8618  10137   5441   1346  -1533  -2050       C  
ATOM   5617  C   GLY B1110     -11.188  25.723  57.506  1.00 64.77           C  
ANISOU 5617  C   GLY B1110     8629   9970   6012   1224  -1610  -2290       C  
ATOM   5618  O   GLY B1110     -10.089  26.276  57.597  1.00 65.22           O  
ANISOU 5618  O   GLY B1110     8569  10051   6159   1175  -1842  -2466       O  
ATOM   5619  N   VAL B1111     -12.052  25.961  56.522  1.00 58.46           N  
ANISOU 5619  N   VAL B1111     7838   8895   5480   1158  -1424  -2266       N  
ATOM   5620  CA  VAL B1111     -11.803  26.939  55.468  1.00 56.59           C  
ANISOU 5620  CA  VAL B1111     7527   8347   5627   1036  -1465  -2406       C  
ATOM   5621  C   VAL B1111     -12.119  28.368  55.929  1.00 62.72           C  
ANISOU 5621  C   VAL B1111     8326   9047   6458   1022  -1549  -2797       C  
ATOM   5622  O   VAL B1111     -11.476  29.328  55.491  1.00 63.29           O  
ANISOU 5622  O   VAL B1111     8344   8889   6815    890  -1689  -2951       O  
ATOM   5623  CB  VAL B1111     -12.646  26.622  54.231  1.00 57.19           C  
ANISOU 5623  CB  VAL B1111     7628   8182   5919   1004  -1280  -2213       C  
ATOM   5624  CG1 VAL B1111     -12.360  27.621  53.131  1.00 56.09           C  
ANISOU 5624  CG1 VAL B1111     7448   7751   6114    883  -1325  -2277       C  
ATOM   5625  CG2 VAL B1111     -12.370  25.197  53.764  1.00 55.60           C  
ANISOU 5625  CG2 VAL B1111     7434   7998   5693   1031  -1215  -1901       C  
ATOM   5626  N   ALA B1112     -13.104  28.506  56.816  1.00 60.49           N  
ANISOU 5626  N   ALA B1112     8120   8948   5917   1155  -1452  -2962       N  
ATOM   5627  CA  ALA B1112     -13.506  29.815  57.328  1.00 63.00           C  
ANISOU 5627  CA  ALA B1112     8475   9189   6273   1216  -1521  -3407       C  
ATOM   5628  C   ALA B1112     -12.454  30.421  58.261  1.00 71.08           C  
ANISOU 5628  C   ALA B1112     9501  10344   7163   1181  -1802  -3744       C  
ATOM   5629  O   ALA B1112     -12.519  31.607  58.592  1.00 74.11           O  
ANISOU 5629  O   ALA B1112     9927  10563   7668   1194  -1935  -4176       O  
ATOM   5630  CB  ALA B1112     -14.845  29.716  58.031  1.00 65.18           C  
ANISOU 5630  CB  ALA B1112     8781   9712   6272   1403  -1296  -3516       C  
ATOM   5631  N   GLY B1113     -11.493  29.607  58.692  1.00 67.53           N  
ANISOU 5631  N   GLY B1113     9002  10173   6482   1152  -1926  -3571       N  
ATOM   5632  CA  GLY B1113     -10.326  30.110  59.402  1.00 70.51           C  
ANISOU 5632  CA  GLY B1113     9317  10684   6789   1083  -2258  -3859       C  
ATOM   5633  C   GLY B1113      -9.399  30.965  58.542  1.00 74.58           C  
ANISOU 5633  C   GLY B1113     9692  10812   7835    831  -2438  -3950       C  
ATOM   5634  O   GLY B1113      -8.531  31.662  59.074  1.00 77.69           O  
ANISOU 5634  O   GLY B1113    10005  11230   8283    712  -2737  -4278       O  
ATOM   5635  N   PHE B1114      -9.566  30.920  57.217  1.00 68.28           N  
ANISOU 5635  N   PHE B1114     8854   9676   7411    723  -2264  -3657       N  
ATOM   5636  CA  PHE B1114      -8.698  31.679  56.306  1.00 68.55           C  
ANISOU 5636  CA  PHE B1114     8751   9373   7923    448  -2369  -3640       C  
ATOM   5637  C   PHE B1114      -9.250  33.084  56.103  1.00 73.99           C  
ANISOU 5637  C   PHE B1114     9569   9607   8938    364  -2420  -3924       C  
ATOM   5638  O   PHE B1114      -9.662  33.425  54.999  1.00 72.06           O  
ANISOU 5638  O   PHE B1114     9372   9009   8997    292  -2284  -3706       O  
ATOM   5639  CB  PHE B1114      -8.539  30.951  54.951  1.00 66.70           C  
ANISOU 5639  CB  PHE B1114     8430   9047   7864    385  -2153  -3178       C  
ATOM   5640  CG  PHE B1114      -7.814  29.626  55.052  1.00 67.27           C  
ANISOU 5640  CG  PHE B1114     8361   9472   7726    481  -2140  -2933       C  
ATOM   5641  CD1 PHE B1114      -6.473  29.578  55.422  1.00 73.11           C  
ANISOU 5641  CD1 PHE B1114     8851  10422   8504    390  -2361  -3000       C  
ATOM   5642  CD2 PHE B1114      -8.471  28.431  54.785  1.00 66.53           C  
ANISOU 5642  CD2 PHE B1114     8366   9474   7438    669  -1936  -2649       C  
ATOM   5643  CE1 PHE B1114      -5.800  28.359  55.536  1.00 73.80           C  
ANISOU 5643  CE1 PHE B1114     8799  10812   8429    548  -2381  -2781       C  
ATOM   5644  CE2 PHE B1114      -7.808  27.213  54.893  1.00 69.28           C  
ANISOU 5644  CE2 PHE B1114     8620  10060   7645    793  -1952  -2432       C  
ATOM   5645  CZ  PHE B1114      -6.467  27.177  55.272  1.00 70.08           C  
ANISOU 5645  CZ  PHE B1114     8478  10371   7777    763  -2176  -2494       C  
ATOM   5646  N   THR B1115      -9.243  33.895  57.166  1.00 73.85           N  
ANISOU 5646  N   THR B1115     9622   9590   8848    396  -2641  -4417       N  
ATOM   5647  CA  THR B1115      -9.878  35.227  57.139  1.00 75.95           C  
ANISOU 5647  CA  THR B1115    10052   9379   9428    399  -2714  -4768       C  
ATOM   5648  C   THR B1115      -9.105  36.203  56.262  1.00 81.42           C  
ANISOU 5648  C   THR B1115    10685   9539  10711     38  -2859  -4700       C  
ATOM   5649  O   THR B1115      -9.693  36.899  55.426  1.00 80.77           O  
ANISOU 5649  O   THR B1115    10732   8969  10988     15  -2785  -4579       O  
ATOM   5650  CB  THR B1115     -10.011  35.853  58.552  1.00 85.64           C  
ANISOU 5650  CB  THR B1115    11384  10746  10408    546  -2933  -5409       C  
ATOM   5651  OG1 THR B1115     -10.563  34.897  59.464  1.00 81.30           O  
ANISOU 5651  OG1 THR B1115    10871  10791   9230    836  -2786  -5418       O  
ATOM   5652  CG2 THR B1115     -10.917  37.072  58.506  1.00 87.06           C  
ANISOU 5652  CG2 THR B1115    11757  10423  10898    674  -2954  -5783       C  
ATOM   5653  N   ASN B1116      -7.790  36.250  56.472  1.00 80.58           N  
ANISOU 5653  N   ASN B1116    10368   9544  10705   -248  -3074  -4753       N  
ATOM   5654  CA  ASN B1116      -6.908  37.136  55.713  1.00 83.28           C  
ANISOU 5654  CA  ASN B1116    10589   9440  11614   -676  -3197  -4656       C  
ATOM   5655  C   ASN B1116      -7.106  36.988  54.216  1.00 83.60           C  
ANISOU 5655  C   ASN B1116    10632   9246  11885   -780  -2909  -4075       C  
ATOM   5656  O   ASN B1116      -7.327  37.976  53.512  1.00 85.16           O  
ANISOU 5656  O   ASN B1116    10964   8883  12509   -952  -2919  -3978       O  
ATOM   5657  CB  ASN B1116      -5.433  36.894  56.077  1.00 87.12           C  
ANISOU 5657  CB  ASN B1116    10727  10248  12127   -960  -3414  -4709       C  
ATOM   5658  CG  ASN B1116      -4.969  37.751  57.243  1.00114.96           C  
ANISOU 5658  CG  ASN B1116    14248  13708  15723  -1083  -3833  -5344       C  
ATOM   5659  OD1 ASN B1116      -5.765  38.457  57.867  1.00109.97           O  
ANISOU 5659  OD1 ASN B1116    13900  12826  15059   -907  -3942  -5788       O  
ATOM   5660  ND2 ASN B1116      -3.670  37.700  57.536  1.00110.21           N  
ANISOU 5660  ND2 ASN B1116    13299  13350  15226  -1373  -4086  -5429       N  
ATOM   5661  N   SER B1117      -7.044  35.753  53.736  1.00 75.57           N  
ANISOU 5661  N   SER B1117     9495   8646  10573   -657  -2671  -3694       N  
ATOM   5662  CA  SER B1117      -7.226  35.488  52.315  1.00 72.59           C  
ANISOU 5662  CA  SER B1117     9126   8147  10309   -721  -2398  -3184       C  
ATOM   5663  C   SER B1117      -8.684  35.728  51.874  1.00 74.49           C  
ANISOU 5663  C   SER B1117     9666   8101  10535   -468  -2276  -3109       C  
ATOM   5664  O   SER B1117      -8.915  36.324  50.821  1.00 74.76           O  
ANISOU 5664  O   SER B1117     9804   7764  10838   -590  -2206  -2822       O  
ATOM   5665  CB  SER B1117      -6.745  34.075  51.973  1.00 72.48           C  
ANISOU 5665  CB  SER B1117     8909   8639   9991   -622  -2208  -2893       C  
ATOM   5666  OG  SER B1117      -5.394  33.895  52.380  1.00 83.89           O  
ANISOU 5666  OG  SER B1117    10025  10362  11487   -812  -2347  -2971       O  
ATOM   5667  N   LEU B1118      -9.658  35.306  52.686  1.00 69.20           N  
ANISOU 5667  N   LEU B1118     9114   7624   9554   -121  -2258  -3349       N  
ATOM   5668  CA  LEU B1118     -11.091  35.456  52.334  1.00 67.15           C  
ANISOU 5668  CA  LEU B1118     9052   7177   9285    149  -2144  -3308       C  
ATOM   5669  C   LEU B1118     -11.492  36.912  52.165  1.00 74.17           C  
ANISOU 5669  C   LEU B1118    10118   7462  10603    120  -2304  -3477       C  
ATOM   5670  O   LEU B1118     -12.391  37.230  51.381  1.00 73.23           O  
ANISOU 5670  O   LEU B1118    10129   7068  10628    257  -2244  -3281       O  
ATOM   5671  CB  LEU B1118     -12.017  34.794  53.371  1.00 65.79           C  
ANISOU 5671  CB  LEU B1118     8910   7374   8713    488  -2069  -3562       C  
ATOM   5672  CG  LEU B1118     -12.142  33.270  53.294  1.00 66.09           C  
ANISOU 5672  CG  LEU B1118     8858   7880   8374    586  -1867  -3278       C  
ATOM   5673  CD1 LEU B1118     -12.860  32.728  54.508  1.00 66.45           C  
ANISOU 5673  CD1 LEU B1118     8925   8297   8028    834  -1803  -3508       C  
ATOM   5674  CD2 LEU B1118     -12.857  32.872  52.036  1.00 65.37           C  
ANISOU 5674  CD2 LEU B1118     8800   7681   8357    627  -1697  -2911       C  
ATOM   5675  N   ARG B1119     -10.826  37.788  52.909  1.00 74.68           N  
ANISOU 5675  N   ARG B1119    10189   7300  10885    -45  -2544  -3854       N  
ATOM   5676  CA  ARG B1119     -11.049  39.220  52.777  1.00 79.26           C  
ANISOU 5676  CA  ARG B1119    10959   7195  11960   -109  -2742  -4037       C  
ATOM   5677  C   ARG B1119     -10.479  39.735  51.453  1.00 84.05           C  
ANISOU 5677  C   ARG B1119    11585   7381  12968   -473  -2724  -3514       C  
ATOM   5678  O   ARG B1119     -11.035  40.653  50.853  1.00 86.48           O  
ANISOU 5678  O   ARG B1119    12106   7114  13638   -440  -2797  -3386       O  
ATOM   5679  CB  ARG B1119     -10.422  39.963  53.951  1.00 85.00           C  
ANISOU 5679  CB  ARG B1119    11690   7788  12819   -226  -3035  -4633       C  
ATOM   5680  CG  ARG B1119     -10.963  41.368  54.150  1.00102.59           C  
ANISOU 5680  CG  ARG B1119    14170   9300  15508   -135  -3260  -5017       C  
ATOM   5681  CD  ARG B1119     -10.389  42.034  55.400  1.00120.70           C  
ANISOU 5681  CD  ARG B1119    16482  11502  17875   -222  -3577  -5722       C  
ATOM   5682  NE  ARG B1119      -8.922  41.984  55.440  1.00132.20           N  
ANISOU 5682  NE  ARG B1119    17716  13056  19458   -731  -3733  -5650       N  
ATOM   5683  CZ  ARG B1119      -8.192  41.064  56.080  1.00145.35           C  
ANISOU 5683  CZ  ARG B1119    19134  15408  20683   -787  -3740  -5719       C  
ATOM   5684  NH1 ARG B1119      -8.771  40.075  56.763  1.00128.96           N  
ANISOU 5684  NH1 ARG B1119    17046  13971  17982   -395  -3586  -5822       N  
ATOM   5685  NH2 ARG B1119      -6.861  41.133  56.036  1.00135.57           N  
ANISOU 5685  NH2 ARG B1119    17639  14219  19652  -1247  -3908  -5657       N  
ATOM   5686  N   MET B1120      -9.382  39.133  50.998  1.00 78.72           N  
ANISOU 5686  N   MET B1120    10682   7016  12213   -794  -2616  -3193       N  
ATOM   5687  CA  MET B1120      -8.752  39.519  49.735  1.00 79.85           C  
ANISOU 5687  CA  MET B1120    10798   6898  12645  -1169  -2525  -2657       C  
ATOM   5688  C   MET B1120      -9.521  38.991  48.528  1.00 79.10           C  
ANISOU 5688  C   MET B1120    10812   6903  12340   -981  -2286  -2159       C  
ATOM   5689  O   MET B1120      -9.621  39.680  47.518  1.00 81.24           O  
ANISOU 5689  O   MET B1120    11236   6775  12858  -1133  -2270  -1756       O  
ATOM   5690  CB  MET B1120      -7.296  39.037  49.674  1.00 82.69           C  
ANISOU 5690  CB  MET B1120    10804   7639  12975  -1548  -2460  -2526       C  
ATOM   5691  CG  MET B1120      -6.361  39.722  50.654  1.00 91.25           C  
ANISOU 5691  CG  MET B1120    11735   8578  14357  -1851  -2751  -2956       C  
ATOM   5692  SD  MET B1120      -4.802  38.832  50.765  1.00 95.36           S  
ANISOU 5692  SD  MET B1120    11740   9758  14735  -2138  -2684  -2871       S  
ATOM   5693  CE  MET B1120      -3.887  39.851  51.934  1.00 99.00           C  
ANISOU 5693  CE  MET B1120    12045   9964  15606  -2507  -3128  -3442       C  
ATOM   5694  N   LEU B1121     -10.051  37.774  48.620  1.00 69.94           N  
ANISOU 5694  N   LEU B1121     9586   6263  10725   -671  -2123  -2171       N  
ATOM   5695  CA  LEU B1121     -10.868  37.220  47.534  1.00 66.71           C  
ANISOU 5695  CA  LEU B1121     9275   5969  10101   -479  -1947  -1788       C  
ATOM   5696  C   LEU B1121     -12.104  38.090  47.328  1.00 72.46           C  
ANISOU 5696  C   LEU B1121    10262   6228  11042   -232  -2084  -1803       C  
ATOM   5697  O   LEU B1121     -12.463  38.424  46.192  1.00 72.97           O  
ANISOU 5697  O   LEU B1121    10471   6077  11177   -243  -2066  -1385       O  
ATOM   5698  CB  LEU B1121     -11.303  35.776  47.832  1.00 61.59           C  
ANISOU 5698  CB  LEU B1121     8518   5885   8999   -204  -1795  -1875       C  
ATOM   5699  CG  LEU B1121     -10.226  34.684  47.815  1.00 63.84           C  
ANISOU 5699  CG  LEU B1121     8564   6649   9044   -335  -1648  -1788       C  
ATOM   5700  CD1 LEU B1121     -10.712  33.405  48.488  1.00 60.16           C  
ANISOU 5700  CD1 LEU B1121     8044   6596   8218    -51  -1577  -1955       C  
ATOM   5701  CD2 LEU B1121      -9.777  34.394  46.402  1.00 65.58           C  
ANISOU 5701  CD2 LEU B1121     8750   6970   9196   -491  -1456  -1341       C  
ATOM   5702  N   GLN B1122     -12.736  38.459  48.443  1.00 69.83           N  
ANISOU 5702  N   GLN B1122     9975   5769  10788     18  -2228  -2294       N  
ATOM   5703  CA  GLN B1122     -13.900  39.352  48.447  1.00 72.14           C  
ANISOU 5703  CA  GLN B1122    10465   5608  11337    326  -2380  -2427       C  
ATOM   5704  C   GLN B1122     -13.543  40.776  47.988  1.00 81.87           C  
ANISOU 5704  C   GLN B1122    11908   6089  13108    109  -2588  -2275       C  
ATOM   5705  O   GLN B1122     -14.389  41.486  47.446  1.00 84.02           O  
ANISOU 5705  O   GLN B1122    12376   5923  13626    327  -2710  -2124       O  
ATOM   5706  CB  GLN B1122     -14.513  39.387  49.851  1.00 73.77           C  
ANISOU 5706  CB  GLN B1122    10633   5935  11460    641  -2440  -3057       C  
ATOM   5707  CG  GLN B1122     -15.899  40.014  49.952  1.00 84.10           C  
ANISOU 5707  CG  GLN B1122    12047   6963  12944   1086  -2528  -3269       C  
ATOM   5708  CD  GLN B1122     -16.334  40.179  51.398  1.00 99.48           C  
ANISOU 5708  CD  GLN B1122    13948   9055  14794   1369  -2555  -3946       C  
ATOM   5709  OE1 GLN B1122     -16.569  39.200  52.108  1.00 90.12           O  
ANISOU 5709  OE1 GLN B1122    12596   8479  13166   1483  -2371  -4110       O  
ATOM   5710  NE2 GLN B1122     -16.429  41.423  51.844  1.00 97.59           N  
ANISOU 5710  NE2 GLN B1122    13874   8248  14959   1483  -2781  -4339       N  
ATOM   5711  N   GLN B1123     -12.295  41.184  48.203  1.00 81.19           N  
ANISOU 5711  N   GLN B1123    11769   5843  13235   -325  -2648  -2295       N  
ATOM   5712  CA  GLN B1123     -11.792  42.461  47.680  1.00 87.29           C  
ANISOU 5712  CA  GLN B1123    12725   5885  14555   -658  -2819  -2052       C  
ATOM   5713  C   GLN B1123     -11.293  42.354  46.234  1.00 92.30           C  
ANISOU 5713  C   GLN B1123    13374   6550  15146   -979  -2643  -1290       C  
ATOM   5714  O   GLN B1123     -10.689  43.295  45.717  1.00 97.04           O  
ANISOU 5714  O   GLN B1123    14091   6622  16157  -1364  -2722   -961       O  
ATOM   5715  CB  GLN B1123     -10.665  43.008  48.573  1.00 92.30           C  
ANISOU 5715  CB  GLN B1123    13259   6322  15491  -1045  -2984  -2437       C  
ATOM   5716  CG  GLN B1123     -11.146  43.691  49.849  1.00107.96           C  
ANISOU 5716  CG  GLN B1123    15362   7975  17681   -776  -3254  -3187       C  
ATOM   5717  CD  GLN B1123     -10.020  43.961  50.830  1.00128.46           C  
ANISOU 5717  CD  GLN B1123    17808  10574  20427  -1134  -3436  -3650       C  
ATOM   5718  OE1 GLN B1123      -8.841  43.817  50.502  1.00123.65           O  
ANISOU 5718  OE1 GLN B1123    16985  10101  19895  -1631  -3388  -3374       O  
ATOM   5719  NE2 GLN B1123     -10.380  44.357  52.046  1.00123.96           N  
ANISOU 5719  NE2 GLN B1123    17320   9899  19879   -873  -3652  -4387       N  
ATOM   5720  N   LYS B1124     -11.529  41.212  45.589  1.00 84.72           N  
ANISOU 5720  N   LYS B1124    12301   6207  13683   -839  -2400  -1017       N  
ATOM   5721  CA  LYS B1124     -11.120  40.995  44.202  1.00 85.26           C  
ANISOU 5721  CA  LYS B1124    12384   6431  13579  -1078  -2201   -348       C  
ATOM   5722  C   LYS B1124      -9.589  41.025  44.017  1.00 92.35           C  
ANISOU 5722  C   LYS B1124    13057   7468  14566  -1637  -2044   -141       C  
ATOM   5723  O   LYS B1124      -9.101  41.164  42.894  1.00 94.38           O  
ANISOU 5723  O   LYS B1124    13334   7758  14769  -1923  -1869    435       O  
ATOM   5724  CB  LYS B1124     -11.804  42.018  43.275  1.00 92.27           C  
ANISOU 5724  CB  LYS B1124    13614   6718  14726  -1015  -2352    108       C  
ATOM   5725  CG  LYS B1124     -13.331  42.144  43.472  1.00104.69           C  
ANISOU 5725  CG  LYS B1124    15355   8113  16310   -436  -2551   -118       C  
ATOM   5726  CD  LYS B1124     -14.114  41.153  42.589  1.00109.30           C  
ANISOU 5726  CD  LYS B1124    15913   9242  16376   -151  -2425    149       C  
ATOM   5727  CE  LYS B1124     -15.351  40.568  43.286  1.00114.50           C  
ANISOU 5727  CE  LYS B1124    16467  10149  16887    357  -2492   -328       C  
ATOM   5728  NZ  LYS B1124     -15.035  39.336  44.091  1.00116.29           N  
ANISOU 5728  NZ  LYS B1124    16416  11000  16769    345  -2284   -713       N  
ATOM   5729  N   ARG B1125      -8.841  40.874  45.112  1.00 89.32           N  
ANISOU 5729  N   ARG B1125    12429   7224  14285  -1782  -2103   -606       N  
ATOM   5730  CA  ARG B1125      -7.377  40.902  45.081  1.00 92.06           C  
ANISOU 5730  CA  ARG B1125    12467   7741  14770  -2299  -1994   -492       C  
ATOM   5731  C   ARG B1125      -6.852  39.496  44.836  1.00 91.95           C  
ANISOU 5731  C   ARG B1125    12138   8547  14251  -2226  -1703   -433       C  
ATOM   5732  O   ARG B1125      -6.424  38.821  45.775  1.00 89.25           O  
ANISOU 5732  O   ARG B1125    11549   8579  13784  -2143  -1744   -845       O  
ATOM   5733  CB  ARG B1125      -6.816  41.423  46.411  1.00 95.20           C  
ANISOU 5733  CB  ARG B1125    12734   7916  15523  -2468  -2269  -1069       C  
ATOM   5734  CG  ARG B1125      -7.212  42.854  46.787  1.00112.82           C  
ANISOU 5734  CG  ARG B1125    15272   9265  18330  -2550  -2596  -1258       C  
ATOM   5735  CD  ARG B1125      -6.772  43.169  48.220  1.00126.06           C  
ANISOU 5735  CD  ARG B1125    16825  10849  20222  -2619  -2891  -1979       C  
ATOM   5736  NE  ARG B1125      -7.083  44.537  48.645  1.00141.38           N  
ANISOU 5736  NE  ARG B1125    19062  11908  22748  -2691  -3230  -2271       N  
ATOM   5737  CZ  ARG B1125      -6.293  45.601  48.470  1.00164.21           C  
ANISOU 5737  CZ  ARG B1125    21965  14174  26251  -3249  -3394  -2144       C  
ATOM   5738  NH1 ARG B1125      -5.116  45.495  47.852  1.00154.04           N  
ANISOU 5738  NH1 ARG B1125    20363  13101  25066  -3823  -3214  -1693       N  
ATOM   5739  NH2 ARG B1125      -6.688  46.792  48.913  1.00157.27           N  
ANISOU 5739  NH2 ARG B1125    21404  12432  25918  -3238  -3734  -2482       N  
ATOM   5740  N   TRP B1126      -6.873  39.062  43.577  1.00 88.49           N  
ANISOU 5740  N   TRP B1126    11726   8381  13516  -2234  -1429     71       N  
ATOM   5741  CA  TRP B1126      -6.569  37.660  43.233  1.00 84.45           C  
ANISOU 5741  CA  TRP B1126    10981   8600  12506  -2060  -1159     87       C  
ATOM   5742  C   TRP B1126      -5.081  37.308  43.451  1.00 89.91           C  
ANISOU 5742  C   TRP B1126    11210   9696  13257  -2382  -1009     38       C  
ATOM   5743  O   TRP B1126      -4.755  36.330  44.133  1.00 86.08           O  
ANISOU 5743  O   TRP B1126    10484   9640  12582  -2182  -1005   -297       O  
ATOM   5744  CB  TRP B1126      -6.973  37.332  41.781  1.00 83.33           C  
ANISOU 5744  CB  TRP B1126    11005   8662  11994  -1974   -921    583       C  
ATOM   5745  CG  TRP B1126      -8.276  37.937  41.307  1.00 84.96           C  
ANISOU 5745  CG  TRP B1126    11631   8439  12213  -1749  -1093    776       C  
ATOM   5746  CD1 TRP B1126      -8.456  38.745  40.215  1.00 92.35           C  
ANISOU 5746  CD1 TRP B1126    12814   9093  13182  -1909  -1066   1332       C  
ATOM   5747  CD2 TRP B1126      -9.570  37.782  41.904  1.00 81.46           C  
ANISOU 5747  CD2 TRP B1126    11376   7830  11746  -1309  -1322    440       C  
ATOM   5748  NE1 TRP B1126      -9.779  39.105  40.098  1.00 91.27           N  
ANISOU 5748  NE1 TRP B1126    13007   8607  13066  -1560  -1309   1346       N  
ATOM   5749  CE2 TRP B1126     -10.487  38.529  41.121  1.00 87.87           C  
ANISOU 5749  CE2 TRP B1126    12516   8256  12615  -1192  -1453    784       C  
ATOM   5750  CE3 TRP B1126     -10.046  37.090  43.027  1.00 78.39           C  
ANISOU 5750  CE3 TRP B1126    10894   7608  11283  -1004  -1419    -89       C  
ATOM   5751  CZ2 TRP B1126     -11.851  38.598  41.424  1.00 85.41           C  
ANISOU 5751  CZ2 TRP B1126    12382   7742  12327   -765  -1680    569       C  
ATOM   5752  CZ3 TRP B1126     -11.402  37.164  43.329  1.00 78.27           C  
ANISOU 5752  CZ3 TRP B1126    11066   7407  11267   -624  -1595   -279       C  
ATOM   5753  CH2 TRP B1126     -12.288  37.912  42.528  1.00 81.43           C  
ANISOU 5753  CH2 TRP B1126    11734   7443  11763   -499  -1725     25       C  
ATOM   5754  N   ASP B1127      -4.187  38.110  42.877  1.00 92.29           N  
ANISOU 5754  N   ASP B1127    11366   9859  13840  -2882   -893    397       N  
ATOM   5755  CA  ASP B1127      -2.747  37.851  42.981  1.00 94.86           C  
ANISOU 5755  CA  ASP B1127    11169  10606  14267  -3223   -731    384       C  
ATOM   5756  C   ASP B1127      -2.222  37.874  44.423  1.00 98.17           C  
ANISOU 5756  C   ASP B1127    11328  11011  14961  -3264  -1040   -173       C  
ATOM   5757  O   ASP B1127      -1.235  37.200  44.734  1.00 97.89           O  
ANISOU 5757  O   ASP B1127    10834  11488  14871  -3308   -966   -327       O  
ATOM   5758  CB  ASP B1127      -1.948  38.849  42.126  1.00104.09           C  
ANISOU 5758  CB  ASP B1127    12219  11583  15749  -3830   -544    913       C  
ATOM   5759  CG  ASP B1127      -1.853  38.436  40.658  1.00116.97           C  
ANISOU 5759  CG  ASP B1127    13860  13642  16943  -3840   -102   1467       C  
ATOM   5760  OD1 ASP B1127      -2.328  37.333  40.291  1.00113.01           O  
ANISOU 5760  OD1 ASP B1127    13430  13591  15919  -3376     41   1380       O  
ATOM   5761  OD2 ASP B1127      -1.284  39.224  39.870  1.00129.53           O  
ANISOU 5761  OD2 ASP B1127    15389  15120  18707  -4333    103   1990       O  
ATOM   5762  N   GLU B1128      -2.869  38.649  45.292  1.00 94.57           N  
ANISOU 5762  N   GLU B1128    11155   9997  14781  -3221  -1398   -492       N  
ATOM   5763  CA  GLU B1128      -2.440  38.760  46.688  1.00 94.79           C  
ANISOU 5763  CA  GLU B1128    10994  10015  15008  -3250  -1732  -1061       C  
ATOM   5764  C   GLU B1128      -2.851  37.549  47.514  1.00 91.96           C  
ANISOU 5764  C   GLU B1128    10619  10126  14194  -2718  -1792  -1442       C  
ATOM   5765  O   GLU B1128      -2.086  37.086  48.355  1.00 91.93           O  
ANISOU 5765  O   GLU B1128    10287  10487  14156  -2715  -1929  -1750       O  
ATOM   5766  CB  GLU B1128      -3.001  40.029  47.329  1.00 99.40           C  
ANISOU 5766  CB  GLU B1128    11911   9840  16017  -3358  -2087  -1332       C  
ATOM   5767  CG  GLU B1128      -2.403  41.314  46.783  1.00116.82           C  
ANISOU 5767  CG  GLU B1128    14106  11474  18808  -3973  -2121  -1015       C  
ATOM   5768  CD  GLU B1128      -2.788  42.527  47.607  1.00140.25           C  
ANISOU 5768  CD  GLU B1128    17363  13657  22269  -4074  -2540  -1423       C  
ATOM   5769  OE1 GLU B1128      -2.641  42.482  48.848  1.00132.11           O  
ANISOU 5769  OE1 GLU B1128    16236  12706  21254  -3969  -2842  -2060       O  
ATOM   5770  OE2 GLU B1128      -3.234  43.531  47.013  1.00139.64           O  
ANISOU 5770  OE2 GLU B1128    17626  12876  22553  -4239  -2582  -1114       O  
ATOM   5771  N   ALA B1129      -4.057  37.046  47.275  1.00 83.21           N  
ANISOU 5771  N   ALA B1129     9857   9007  12753  -2285  -1708  -1393       N  
ATOM   5772  CA  ALA B1129      -4.575  35.903  48.024  1.00 77.82           C  
ANISOU 5772  CA  ALA B1129     9202   8708  11657  -1815  -1741  -1684       C  
ATOM   5773  C   ALA B1129      -4.018  34.560  47.530  1.00 78.50           C  
ANISOU 5773  C   ALA B1129     9025   9388  11413  -1662  -1485  -1506       C  
ATOM   5774  O   ALA B1129      -4.095  33.560  48.242  1.00 75.00           O  
ANISOU 5774  O   ALA B1129     8525   9275  10697  -1347  -1539  -1721       O  
ATOM   5775  CB  ALA B1129      -6.093  35.897  47.983  1.00 75.31           C  
ANISOU 5775  CB  ALA B1129     9298   8148  11170  -1453  -1753  -1714       C  
ATOM   5776  N   ALA B1130      -3.471  34.530  46.317  1.00 76.49           N  
ANISOU 5776  N   ALA B1130     8626   9264  11172  -1866  -1203  -1113       N  
ATOM   5777  CA  ALA B1130      -2.807  33.325  45.798  1.00 75.03           C  
ANISOU 5777  CA  ALA B1130     8153   9641  10715  -1712   -947  -1004       C  
ATOM   5778  C   ALA B1130      -1.411  33.150  46.411  1.00 82.29           C  
ANISOU 5778  C   ALA B1130     8550  10906  11810  -1880  -1022  -1172       C  
ATOM   5779  O   ALA B1130      -0.949  32.025  46.629  1.00 80.36           O  
ANISOU 5779  O   ALA B1130     8070  11098  11365  -1597   -977  -1280       O  
ATOM   5780  CB  ALA B1130      -2.714  33.384  44.282  1.00 77.20           C  
ANISOU 5780  CB  ALA B1130     8448  10008  10877  -1848   -594   -562       C  
ATOM   5781  N   VAL B1131      -0.747  34.275  46.673  1.00 83.99           N  
ANISOU 5781  N   VAL B1131     8577  10898  12438  -2340  -1164  -1194       N  
ATOM   5782  CA  VAL B1131       0.552  34.290  47.337  1.00 87.89           C  
ANISOU 5782  CA  VAL B1131     8534  11692  13168  -2559  -1316  -1395       C  
ATOM   5783  C   VAL B1131       0.380  34.091  48.844  1.00 91.04           C  
ANISOU 5783  C   VAL B1131     8989  12100  13504  -2324  -1739  -1873       C  
ATOM   5784  O   VAL B1131       1.231  33.478  49.493  1.00 91.92           O  
ANISOU 5784  O   VAL B1131     8710  12637  13578  -2222  -1887  -2066       O  
ATOM   5785  CB  VAL B1131       1.299  35.616  47.063  1.00 98.30           C  
ANISOU 5785  CB  VAL B1131     9626  12724  14999  -3213  -1339  -1250       C  
ATOM   5786  CG1 VAL B1131       2.636  35.659  47.803  1.00102.93           C  
ANISOU 5786  CG1 VAL B1131     9595  13643  15873  -3473  -1551  -1505       C  
ATOM   5787  CG2 VAL B1131       1.505  35.805  45.563  1.00100.25           C  
ANISOU 5787  CG2 VAL B1131     9820  13033  15236  -3464   -881   -702       C  
ATOM   5788  N   ASN B1132      -0.720  34.607  49.392  1.00 86.22           N  
ANISOU 5788  N   ASN B1132     8851  11056  12854  -2211  -1931  -2059       N  
ATOM   5789  CA  ASN B1132      -1.020  34.465  50.823  1.00 85.69           C  
ANISOU 5789  CA  ASN B1132     8897  11031  12629  -1968  -2293  -2514       C  
ATOM   5790  C   ASN B1132      -1.435  33.030  51.192  1.00 85.81           C  
ANISOU 5790  C   ASN B1132     8993  11451  12159  -1440  -2233  -2526       C  
ATOM   5791  O   ASN B1132      -1.197  32.584  52.315  1.00 85.88           O  
ANISOU 5791  O   ASN B1132     8921  11729  11980  -1248  -2496  -2799       O  
ATOM   5792  CB  ASN B1132      -2.106  35.471  51.245  1.00 86.60           C  
ANISOU 5792  CB  ASN B1132     9473  10587  12843  -1975  -2463  -2731       C  
ATOM   5793  CG  ASN B1132      -2.101  35.765  52.746  1.00108.28           C  
ANISOU 5793  CG  ASN B1132    12260  13358  15525  -1894  -2871  -3279       C  
ATOM   5794  OD1 ASN B1132      -1.052  36.026  53.342  1.00106.12           O  
ANISOU 5794  OD1 ASN B1132    11646  13248  15426  -2140  -3138  -3516       O  
ATOM   5795  ND2 ASN B1132      -3.286  35.748  53.354  1.00 96.64           N  
ANISOU 5795  ND2 ASN B1132    11180  11756  13782  -1552  -2922  -3500       N  
ATOM   5796  N   LEU B1133      -2.042  32.316  50.243  1.00 79.25           N  
ANISOU 5796  N   LEU B1133     8334  10651  11127  -1224  -1910  -2221       N  
ATOM   5797  CA  LEU B1133      -2.440  30.915  50.443  1.00 75.52           C  
ANISOU 5797  CA  LEU B1133     7952  10474  10268   -771  -1834  -2189       C  
ATOM   5798  C   LEU B1133      -1.320  29.911  50.151  1.00 80.97           C  
ANISOU 5798  C   LEU B1133     8231  11611  10925   -651  -1739  -2085       C  
ATOM   5799  O   LEU B1133      -1.458  28.721  50.446  1.00 78.29           O  
ANISOU 5799  O   LEU B1133     7937  11481  10328   -273  -1739  -2077       O  
ATOM   5800  CB  LEU B1133      -3.654  30.571  49.572  1.00 71.55           C  
ANISOU 5800  CB  LEU B1133     7819   9777   9590   -592  -1578  -1973       C  
ATOM   5801  CG  LEU B1133      -5.032  31.019  50.058  1.00 74.15           C  
ANISOU 5801  CG  LEU B1133     8554   9788   9831   -479  -1669  -2104       C  
ATOM   5802  CD1 LEU B1133      -6.065  30.674  48.991  1.00 71.17           C  
ANISOU 5802  CD1 LEU B1133     8432   9275   9333   -346  -1430  -1859       C  
ATOM   5803  CD2 LEU B1133      -5.389  30.382  51.403  1.00 75.49           C  
ANISOU 5803  CD2 LEU B1133     8810  10150   9724   -201  -1850  -2343       C  
ATOM   5804  N   ALA B1134      -0.224  30.386  49.563  1.00 82.06           N  
ANISOU 5804  N   ALA B1134     7955  11878  11344   -968  -1647  -1995       N  
ATOM   5805  CA  ALA B1134       0.972  29.560  49.359  1.00 84.56           C  
ANISOU 5805  CA  ALA B1134     7771  12669  11688   -849  -1570  -1957       C  
ATOM   5806  C   ALA B1134       1.694  29.266  50.681  1.00 91.18           C  
ANISOU 5806  C   ALA B1134     8331  13783  12531   -719  -1973  -2225       C  
ATOM   5807  O   ALA B1134       2.537  28.368  50.750  1.00 92.13           O  
ANISOU 5807  O   ALA B1134     8082  14297  12628   -465  -1992  -2223       O  
ATOM   5808  CB  ALA B1134       1.926  30.240  48.378  1.00 89.69           C  
ANISOU 5808  CB  ALA B1134     8000  13436  12643  -1272  -1324  -1774       C  
ATOM   5809  N   LYS B1135       1.353  30.027  51.720  1.00 88.89           N  
ANISOU 5809  N   LYS B1135     8225  13297  12254   -858  -2310  -2473       N  
ATOM   5810  CA  LYS B1135       1.992  29.907  53.026  1.00 91.94           C  
ANISOU 5810  CA  LYS B1135     8388  13963  12584   -769  -2748  -2756       C  
ATOM   5811  C   LYS B1135       1.327  28.889  53.966  1.00 93.63           C  
ANISOU 5811  C   LYS B1135     8936  14299  12342   -274  -2909  -2797       C  
ATOM   5812  O   LYS B1135       1.989  28.367  54.862  1.00 96.11           O  
ANISOU 5812  O   LYS B1135     9028  14964  12524    -68  -3227  -2907       O  
ATOM   5813  CB  LYS B1135       2.032  31.281  53.714  1.00 97.71           C  
ANISOU 5813  CB  LYS B1135     9145  14447  13533  -1180  -3060  -3071       C  
ATOM   5814  CG  LYS B1135       2.740  32.376  52.909  1.00116.49           C  
ANISOU 5814  CG  LYS B1135    11194  16640  16429  -1754  -2950  -3002       C  
ATOM   5815  CD  LYS B1135       3.279  33.495  53.814  1.00133.39           C  
ANISOU 5815  CD  LYS B1135    13158  18660  18863  -2155  -3398  -3399       C  
ATOM   5816  CE  LYS B1135       4.132  34.498  53.037  1.00150.05           C  
ANISOU 5816  CE  LYS B1135    14863  20597  21553  -2790  -3296  -3280       C  
ATOM   5817  NZ  LYS B1135       4.839  35.461  53.933  1.00165.26           N  
ANISOU 5817  NZ  LYS B1135    16520  22443  23828  -3211  -3783  -3704       N  
ATOM   5818  N   SER B1136       0.043  28.596  53.762  1.00 85.70           N  
ANISOU 5818  N   SER B1136     8438  13026  11100    -96  -2701  -2677       N  
ATOM   5819  CA  SER B1136      -0.740  27.836  54.749  1.00 83.87           C  
ANISOU 5819  CA  SER B1136     8559  12864  10444    267  -2834  -2699       C  
ATOM   5820  C   SER B1136      -0.341  26.364  54.905  1.00 88.67           C  
ANISOU 5820  C   SER B1136     9073  13753  10866    683  -2857  -2497       C  
ATOM   5821  O   SER B1136       0.503  25.848  54.168  1.00 89.10           O  
ANISOU 5821  O   SER B1136     8784  13950  11121    757  -2744  -2375       O  
ATOM   5822  CB  SER B1136      -2.221  27.900  54.400  1.00 82.81           C  
ANISOU 5822  CB  SER B1136     8910  12386  10168    312  -2576  -2609       C  
ATOM   5823  OG  SER B1136      -2.508  27.021  53.328  1.00 87.59           O  
ANISOU 5823  OG  SER B1136     9576  12919  10784    465  -2259  -2323       O  
ATOM   5824  N   ARG B1137      -0.977  25.705  55.875  1.00 85.63           N  
ANISOU 5824  N   ARG B1137     9003  13433  10097    962  -2992  -2454       N  
ATOM   5825  CA  ARG B1137      -0.734  24.290  56.199  1.00 86.50           C  
ANISOU 5825  CA  ARG B1137     9127  13719  10019   1376  -3067  -2217       C  
ATOM   5826  C   ARG B1137      -1.316  23.362  55.139  1.00 87.51           C  
ANISOU 5826  C   ARG B1137     9441  13586  10222   1538  -2706  -1961       C  
ATOM   5827  O   ARG B1137      -0.713  22.352  54.780  1.00 88.36           O  
ANISOU 5827  O   ARG B1137     9391  13758  10422   1818  -2691  -1816       O  
ATOM   5828  CB  ARG B1137      -1.364  23.958  57.560  1.00 87.82           C  
ANISOU 5828  CB  ARG B1137     9636  14015   9717   1561  -3285  -2188       C  
ATOM   5829  CG  ARG B1137      -1.165  22.522  58.043  1.00100.63           C  
ANISOU 5829  CG  ARG B1137    11342  15764  11127   1978  -3408  -1871       C  
ATOM   5830  CD  ARG B1137       0.243  22.290  58.551  1.00117.70           C  
ANISOU 5830  CD  ARG B1137    13082  18301  13339   2162  -3807  -1916       C  
ATOM   5831  NE  ARG B1137       0.526  20.865  58.704  1.00129.45           N  
ANISOU 5831  NE  ARG B1137    14619  19803  14761   2607  -3900  -1573       N  
ATOM   5832  CZ  ARG B1137       1.660  20.364  59.194  1.00149.80           C  
ANISOU 5832  CZ  ARG B1137    16869  22690  17358   2905  -4274  -1523       C  
ATOM   5833  NH1 ARG B1137       2.644  21.168  59.597  1.00141.62           N  
ANISOU 5833  NH1 ARG B1137    15385  22030  16394   2771  -4603  -1813       N  
ATOM   5834  NH2 ARG B1137       1.811  19.046  59.287  1.00138.10           N  
ANISOU 5834  NH2 ARG B1137    15498  21118  15857   3343  -4351  -1183       N  
ATOM   5835  N   TRP B1138      -2.511  23.711  54.678  1.00 80.71           N  
ANISOU 5835  N   TRP B1138     8914  12429   9324   1383  -2450  -1941       N  
ATOM   5836  CA  TRP B1138      -3.205  23.023  53.582  1.00 77.51           C  
ANISOU 5836  CA  TRP B1138     8701  11759   8991   1460  -2128  -1765       C  
ATOM   5837  C   TRP B1138      -2.340  22.838  52.323  1.00 81.26           C  
ANISOU 5837  C   TRP B1138     8864  12271   9741   1469  -1947  -1753       C  
ATOM   5838  O   TRP B1138      -2.485  21.849  51.603  1.00 79.58           O  
ANISOU 5838  O   TRP B1138     8735  11947   9553   1684  -1780  -1642       O  
ATOM   5839  CB  TRP B1138      -4.483  23.813  53.278  1.00 73.40           C  
ANISOU 5839  CB  TRP B1138     8472  10983   8435   1230  -1947  -1814       C  
ATOM   5840  CG  TRP B1138      -5.135  23.589  51.954  1.00 71.83           C  
ANISOU 5840  CG  TRP B1138     8402  10542   8350   1192  -1653  -1713       C  
ATOM   5841  CD1 TRP B1138      -5.751  22.453  51.516  1.00 73.27           C  
ANISOU 5841  CD1 TRP B1138     8784  10578   8477   1376  -1522  -1564       C  
ATOM   5842  CD2 TRP B1138      -5.297  24.560  50.915  1.00 70.68           C  
ANISOU 5842  CD2 TRP B1138     8222  10261   8372    941  -1486  -1753       C  
ATOM   5843  NE1 TRP B1138      -6.264  22.649  50.254  1.00 70.86           N  
ANISOU 5843  NE1 TRP B1138     8552  10106   8265   1268  -1301  -1555       N  
ATOM   5844  CE2 TRP B1138      -5.999  23.936  49.864  1.00 72.49           C  
ANISOU 5844  CE2 TRP B1138     8627  10332   8585   1014  -1269  -1637       C  
ATOM   5845  CE3 TRP B1138      -4.902  25.896  50.765  1.00 73.24           C  
ANISOU 5845  CE3 TRP B1138     8399  10558   8870    649  -1520  -1859       C  
ATOM   5846  CZ2 TRP B1138      -6.315  24.603  48.678  1.00 70.89           C  
ANISOU 5846  CZ2 TRP B1138     8462  10009   8466    838  -1092  -1602       C  
ATOM   5847  CZ3 TRP B1138      -5.218  26.559  49.587  1.00 73.91           C  
ANISOU 5847  CZ3 TRP B1138     8535  10462   9084    457  -1323  -1776       C  
ATOM   5848  CH2 TRP B1138      -5.913  25.910  48.558  1.00 72.32           C  
ANISOU 5848  CH2 TRP B1138     8514  10170   8795    568  -1114  -1638       C  
ATOM   5849  N   TYR B1139      -1.440  23.787  52.077  1.00 79.85           N  
ANISOU 5849  N   TYR B1139     8319  12256   9765   1226  -1976  -1882       N  
ATOM   5850  CA  TYR B1139      -0.493  23.699  50.971  1.00 81.28           C  
ANISOU 5850  CA  TYR B1139     8121  12585  10175   1208  -1772  -1865       C  
ATOM   5851  C   TYR B1139       0.560  22.627  51.237  1.00 88.25           C  
ANISOU 5851  C   TYR B1139     8680  13742  11109   1590  -1907  -1857       C  
ATOM   5852  O   TYR B1139       0.772  21.758  50.402  1.00 88.35           O  
ANISOU 5852  O   TYR B1139     8635  13760  11174   1845  -1702  -1811       O  
ATOM   5853  CB  TYR B1139       0.181  25.056  50.727  1.00 84.78           C  
ANISOU 5853  CB  TYR B1139     8232  13126  10853    774  -1765  -1960       C  
ATOM   5854  CG  TYR B1139       0.985  25.123  49.444  1.00 88.70           C  
ANISOU 5854  CG  TYR B1139     8362  13798  11544    668  -1448  -1887       C  
ATOM   5855  CD1 TYR B1139       0.449  25.697  48.286  1.00 89.09           C  
ANISOU 5855  CD1 TYR B1139     8584  13668  11599    423  -1124  -1762       C  
ATOM   5856  CD2 TYR B1139       2.288  24.609  49.385  1.00 93.80           C  
ANISOU 5856  CD2 TYR B1139     8464  14835  12338    836  -1466  -1933       C  
ATOM   5857  CE1 TYR B1139       1.194  25.754  47.100  1.00 92.70           C  
ANISOU 5857  CE1 TYR B1139     8712  14361  12150    321   -792  -1666       C  
ATOM   5858  CE2 TYR B1139       3.038  24.659  48.207  1.00 97.37           C  
ANISOU 5858  CE2 TYR B1139     8535  15532  12931    750  -1115  -1878       C  
ATOM   5859  CZ  TYR B1139       2.491  25.232  47.073  1.00103.06           C  
ANISOU 5859  CZ  TYR B1139     9463  16098  13598    479   -763  -1736       C  
ATOM   5860  OH  TYR B1139       3.236  25.278  45.920  1.00107.29           O  
ANISOU 5860  OH  TYR B1139     9629  16943  14191    391   -383  -1655       O  
ATOM   5861  N   ASN B1140       1.209  22.674  52.395  1.00 87.50           N  
ANISOU 5861  N   ASN B1140     8379  13877  10990   1665  -2276  -1926       N  
ATOM   5862  CA  ASN B1140       2.285  21.717  52.701  1.00 91.32           C  
ANISOU 5862  CA  ASN B1140     8504  14641  11554   2067  -2469  -1908       C  
ATOM   5863  C   ASN B1140       1.852  20.243  52.810  1.00 94.05           C  
ANISOU 5863  C   ASN B1140     9179  14785  11772   2554  -2484  -1731       C  
ATOM   5864  O   ASN B1140       2.699  19.349  52.767  1.00 97.47           O  
ANISOU 5864  O   ASN B1140     9339  15361  12336   2954  -2581  -1709       O  
ATOM   5865  CB  ASN B1140       3.037  22.124  53.973  1.00 96.84           C  
ANISOU 5865  CB  ASN B1140     8922  15658  12215   2044  -2935  -2018       C  
ATOM   5866  CG  ASN B1140       3.983  23.286  53.740  1.00124.89           C  
ANISOU 5866  CG  ASN B1140    11927  19470  16057   1635  -2966  -2217       C  
ATOM   5867  OD1 ASN B1140       5.203  23.158  53.903  1.00123.55           O  
ANISOU 5867  OD1 ASN B1140    11176  19680  16086   1738  -3160  -2297       O  
ATOM   5868  ND2 ASN B1140       3.426  24.427  53.344  1.00115.69           N  
ANISOU 5868  ND2 ASN B1140    10921  18083  14953   1162  -2784  -2284       N  
ATOM   5869  N   GLN B1141       0.549  19.994  52.953  1.00 85.88           N  
ANISOU 5869  N   GLN B1141     8705  13403  10524   2518  -2396  -1605       N  
ATOM   5870  CA  GLN B1141       0.008  18.625  53.006  1.00 84.92           C  
ANISOU 5870  CA  GLN B1141     8940  12994  10331   2885  -2391  -1410       C  
ATOM   5871  C   GLN B1141      -0.437  18.129  51.630  1.00 85.80           C  
ANISOU 5871  C   GLN B1141     9190  12835  10577   2927  -2029  -1448       C  
ATOM   5872  O   GLN B1141      -0.242  16.960  51.295  1.00 87.32           O  
ANISOU 5872  O   GLN B1141     9437  12860  10882   3302  -2016  -1410       O  
ATOM   5873  CB  GLN B1141      -1.175  18.550  53.980  1.00 84.20           C  
ANISOU 5873  CB  GLN B1141     9343  12716   9935   2796  -2491  -1233       C  
ATOM   5874  CG  GLN B1141      -0.795  18.771  55.431  1.00100.46           C  
ANISOU 5874  CG  GLN B1141    11356  15067  11748   2852  -2874  -1179       C  
ATOM   5875  CD  GLN B1141       0.064  17.656  55.976  1.00121.79           C  
ANISOU 5875  CD  GLN B1141    13941  17861  14471   3318  -3174   -994       C  
ATOM   5876  OE1 GLN B1141       1.254  17.842  56.221  1.00120.12           O  
ANISOU 5876  OE1 GLN B1141    13278  17994  14367   3453  -3426  -1108       O  
ATOM   5877  NE2 GLN B1141      -0.531  16.482  56.150  1.00113.76           N  
ANISOU 5877  NE2 GLN B1141    13314  16516  13393   3565  -3166   -696       N  
ATOM   5878  N   THR B1142      -1.042  19.022  50.848  1.00 78.28           N  
ANISOU 5878  N   THR B1142     8312  11825   9605   2561  -1766  -1536       N  
ATOM   5879  CA  THR B1142      -1.533  18.702  49.507  1.00 75.82           C  
ANISOU 5879  CA  THR B1142     8148  11320   9340   2559  -1444  -1593       C  
ATOM   5880  C   THR B1142      -1.046  19.775  48.514  1.00 78.61           C  
ANISOU 5880  C   THR B1142     8193  11913   9761   2269  -1197  -1708       C  
ATOM   5881  O   THR B1142      -1.842  20.588  48.041  1.00 75.45           O  
ANISOU 5881  O   THR B1142     7989  11397   9282   1948  -1052  -1687       O  
ATOM   5882  CB  THR B1142      -3.084  18.605  49.502  1.00 78.50           C  
ANISOU 5882  CB  THR B1142     8996  11299   9532   2398  -1379  -1499       C  
ATOM   5883  OG1 THR B1142      -3.654  19.886  49.788  1.00 75.04           O  
ANISOU 5883  OG1 THR B1142     8609  10905   8997   2023  -1371  -1504       O  
ATOM   5884  CG2 THR B1142      -3.571  17.608  50.552  1.00 77.30           C  
ANISOU 5884  CG2 THR B1142     9134  10928   9308   2603  -1590  -1312       C  
ATOM   5885  N   PRO B1143       0.266  19.775  48.189  1.00 77.81           N  
ANISOU 5885  N   PRO B1143     7590  12158   9817   2386  -1145  -1801       N  
ATOM   5886  CA  PRO B1143       0.857  20.879  47.417  1.00 78.33           C  
ANISOU 5886  CA  PRO B1143     7301  12500   9959   2039   -913  -1840       C  
ATOM   5887  C   PRO B1143       0.488  20.894  45.937  1.00 80.32           C  
ANISOU 5887  C   PRO B1143     7677  12735  10106   1971   -521  -1851       C  
ATOM   5888  O   PRO B1143       0.584  21.942  45.298  1.00 80.11           O  
ANISOU 5888  O   PRO B1143     7533  12832  10075   1597   -322  -1781       O  
ATOM   5889  CB  PRO B1143       2.371  20.670  47.583  1.00 85.34           C  
ANISOU 5889  CB  PRO B1143     7559  13813  11055   2231   -972  -1932       C  
ATOM   5890  CG  PRO B1143       2.542  19.414  48.408  1.00 91.43           C  
ANISOU 5890  CG  PRO B1143     8398  14495  11846   2745  -1265  -1941       C  
ATOM   5891  CD  PRO B1143       1.241  18.693  48.408  1.00 83.33           C  
ANISOU 5891  CD  PRO B1143     8010  13000  10651   2864  -1265  -1859       C  
ATOM   5892  N   ASN B1144       0.089  19.743  45.403  1.00 75.72           N  
ANISOU 5892  N   ASN B1144     7342  11991   9435   2325   -434  -1933       N  
ATOM   5893  CA  ASN B1144      -0.378  19.652  44.025  1.00 74.72           C  
ANISOU 5893  CA  ASN B1144     7401  11859   9131   2299   -114  -1991       C  
ATOM   5894  C   ASN B1144      -1.822  20.112  43.895  1.00 72.76           C  
ANISOU 5894  C   ASN B1144     7651  11272   8724   2027   -149  -1881       C  
ATOM   5895  O   ASN B1144      -2.158  20.878  42.991  1.00 71.74           O  
ANISOU 5895  O   ASN B1144     7594  11213   8451   1764     51  -1809       O  
ATOM   5896  CB  ASN B1144      -0.229  18.224  43.514  1.00 78.13           C  
ANISOU 5896  CB  ASN B1144     7906  12225   9556   2797    -50  -2206       C  
ATOM   5897  CG  ASN B1144       1.214  17.828  43.349  1.00106.56           C  
ANISOU 5897  CG  ASN B1144    10954  16228  13305   3116     62  -2357       C  
ATOM   5898  OD1 ASN B1144       2.003  18.571  42.764  1.00102.54           O  
ANISOU 5898  OD1 ASN B1144    10023  16162  12777   2927    327  -2348       O  
ATOM   5899  ND2 ASN B1144       1.575  16.659  43.868  1.00101.60           N  
ANISOU 5899  ND2 ASN B1144    10304  15449  12850   3604   -136  -2474       N  
ATOM   5900  N   ARG B1145      -2.677  19.648  44.796  1.00 65.76           N  
ANISOU 5900  N   ARG B1145     7086  10041   7857   2096   -402  -1841       N  
ATOM   5901  CA  ARG B1145      -4.066  20.080  44.783  1.00 61.48           C  
ANISOU 5901  CA  ARG B1145     6939   9219   7202   1858   -445  -1752       C  
ATOM   5902  C   ARG B1145      -4.158  21.586  45.001  1.00 64.11           C  
ANISOU 5902  C   ARG B1145     7195   9617   7548   1469   -452  -1631       C  
ATOM   5903  O   ARG B1145      -4.867  22.282  44.272  1.00 62.20           O  
ANISOU 5903  O   ARG B1145     7124   9298   7209   1257   -349  -1562       O  
ATOM   5904  CB  ARG B1145      -4.878  19.352  45.857  1.00 58.96           C  
ANISOU 5904  CB  ARG B1145     6901   8589   6914   1968   -681  -1700       C  
ATOM   5905  CG  ARG B1145      -6.374  19.713  45.870  1.00 60.95           C  
ANISOU 5905  CG  ARG B1145     7493   8593   7073   1745   -707  -1630       C  
ATOM   5906  CD  ARG B1145      -7.163  18.690  46.669  1.00 63.70           C  
ANISOU 5906  CD  ARG B1145     8096   8660   7447   1865   -854  -1567       C  
ATOM   5907  NE  ARG B1145      -8.607  18.875  46.556  1.00 64.35           N  
ANISOU 5907  NE  ARG B1145     8430   8548   7471   1670   -849  -1528       N  
ATOM   5908  CZ  ARG B1145      -9.516  18.051  47.079  1.00 74.92           C  
ANISOU 5908  CZ  ARG B1145     9983   9642   8843   1679   -925  -1449       C  
ATOM   5909  NH1 ARG B1145      -9.139  16.973  47.762  1.00 61.89           N  
ANISOU 5909  NH1 ARG B1145     8390   7855   7272   1876  -1025  -1361       N  
ATOM   5910  NH2 ARG B1145     -10.811  18.304  46.920  1.00 58.57           N  
ANISOU 5910  NH2 ARG B1145     8050   7460   6744   1486   -907  -1431       N  
ATOM   5911  N   ALA B1146      -3.441  22.080  46.007  1.00 61.81           N  
ANISOU 5911  N   ALA B1146     6654   9443   7387   1392   -610  -1617       N  
ATOM   5912  CA  ALA B1146      -3.486  23.496  46.362  1.00 61.00           C  
ANISOU 5912  CA  ALA B1146     6493   9326   7359   1027   -674  -1560       C  
ATOM   5913  C   ALA B1146      -2.957  24.364  45.218  1.00 66.19           C  
ANISOU 5913  C   ALA B1146     6958  10135   8056    764   -426  -1471       C  
ATOM   5914  O   ALA B1146      -3.487  25.449  44.966  1.00 64.74           O  
ANISOU 5914  O   ALA B1146     6919   9784   7895    470   -410  -1364       O  
ATOM   5915  CB  ALA B1146      -2.711  23.753  47.646  1.00 63.36           C  
ANISOU 5915  CB  ALA B1146     6541   9756   7777   1010   -930  -1628       C  
ATOM   5916  N   LYS B1147      -1.928  23.876  44.524  1.00 65.48           N  
ANISOU 5916  N   LYS B1147     6544  10364   7971    886   -223  -1499       N  
ATOM   5917  CA  LYS B1147      -1.415  24.559  43.330  1.00 67.83           C  
ANISOU 5917  CA  LYS B1147     6653  10886   8233    644     89  -1368       C  
ATOM   5918  C   LYS B1147      -2.524  24.764  42.295  1.00 68.88           C  
ANISOU 5918  C   LYS B1147     7204  10847   8120    577    228  -1247       C  
ATOM   5919  O   LYS B1147      -2.629  25.832  41.688  1.00 69.43           O  
ANISOU 5919  O   LYS B1147     7315  10892   8174    249    343  -1031       O  
ATOM   5920  CB  LYS B1147      -0.244  23.786  42.697  1.00 74.36           C  
ANISOU 5920  CB  LYS B1147     7066  12149   9037    880    338  -1466       C  
ATOM   5921  CG  LYS B1147       1.148  24.234  43.143  1.00 93.67           C  
ANISOU 5921  CG  LYS B1147     8906  14931  11753    727    339  -1471       C  
ATOM   5922  CD  LYS B1147       2.225  23.331  42.532  1.00109.20           C  
ANISOU 5922  CD  LYS B1147    10432  17360  13701   1063    597  -1613       C  
ATOM   5923  CE  LYS B1147       3.647  23.848  42.793  1.00124.95           C  
ANISOU 5923  CE  LYS B1147    11714  19780  15981    866    649  -1601       C  
ATOM   5924  NZ  LYS B1147       4.693  23.023  42.113  1.00137.30           N  
ANISOU 5924  NZ  LYS B1147    12782  21857  17528   1220    955  -1755       N  
ATOM   5925  N   ARG B1148      -3.348  23.737  42.109  1.00 62.40           N  
ANISOU 5925  N   ARG B1148     6692   9890   7127    880    184  -1374       N  
ATOM   5926  CA  ARG B1148      -4.459  23.797  41.157  1.00 60.30           C  
ANISOU 5926  CA  ARG B1148     6804   9490   6616    854    248  -1308       C  
ATOM   5927  C   ARG B1148      -5.623  24.685  41.622  1.00 60.65           C  
ANISOU 5927  C   ARG B1148     7137   9179   6729    646     38  -1183       C  
ATOM   5928  O   ARG B1148      -6.239  25.390  40.818  1.00 60.22           O  
ANISOU 5928  O   ARG B1148     7274   9061   6547    490     88  -1014       O  
ATOM   5929  CB  ARG B1148      -4.977  22.391  40.864  1.00 58.38           C  
ANISOU 5929  CB  ARG B1148     6771   9181   6230   1211    222  -1533       C  
ATOM   5930  CG  ARG B1148      -4.031  21.548  40.052  1.00 68.57           C  
ANISOU 5930  CG  ARG B1148     7856  10805   7393   1474    464  -1709       C  
ATOM   5931  CD  ARG B1148      -4.754  20.343  39.484  1.00 72.19           C  
ANISOU 5931  CD  ARG B1148     8622  11119   7688   1768    426  -1955       C  
ATOM   5932  NE  ARG B1148      -5.148  19.392  40.519  1.00 71.66           N  
ANISOU 5932  NE  ARG B1148     8684  10694   7851   1965    166  -2069       N  
ATOM   5933  CZ  ARG B1148      -4.325  18.524  41.104  1.00 84.32           C  
ANISOU 5933  CZ  ARG B1148    10101  12294   9642   2262    120  -2198       C  
ATOM   5934  NH1 ARG B1148      -3.034  18.477  40.776  1.00 74.88           N  
ANISOU 5934  NH1 ARG B1148     8519  11471   8462   2421    320  -2283       N  
ATOM   5935  NH2 ARG B1148      -4.796  17.701  42.035  1.00 68.16           N  
ANISOU 5935  NH2 ARG B1148     8237   9883   7778   2404   -126  -2213       N  
ATOM   5936  N   VAL B1149      -5.929  24.642  42.913  1.00 54.77           N  
ANISOU 5936  N   VAL B1149     6420   8229   6161    676   -197  -1265       N  
ATOM   5937  CA  VAL B1149      -7.029  25.436  43.456  1.00 51.95           C  
ANISOU 5937  CA  VAL B1149     6295   7570   5872    540   -377  -1214       C  
ATOM   5938  C   VAL B1149      -6.671  26.932  43.470  1.00 57.85           C  
ANISOU 5938  C   VAL B1149     6954   8237   6788    218   -386  -1068       C  
ATOM   5939  O   VAL B1149      -7.508  27.778  43.142  1.00 56.94           O  
ANISOU 5939  O   VAL B1149     7053   7894   6690    100   -438   -948       O  
ATOM   5940  CB  VAL B1149      -7.418  24.962  44.868  1.00 53.27           C  
ANISOU 5940  CB  VAL B1149     6509   7614   6116    669   -583  -1351       C  
ATOM   5941  CG1 VAL B1149      -8.558  25.792  45.397  1.00 51.40           C  
ANISOU 5941  CG1 VAL B1149     6470   7131   5930    568   -719  -1347       C  
ATOM   5942  CG2 VAL B1149      -7.791  23.482  44.856  1.00 51.97           C  
ANISOU 5942  CG2 VAL B1149     6460   7438   5846    941   -583  -1436       C  
ATOM   5943  N   ILE B1150      -5.422  27.237  43.832  1.00 57.17           N  
ANISOU 5943  N   ILE B1150     6540   8319   6863     81   -359  -1079       N  
ATOM   5944  CA  ILE B1150      -4.912  28.615  43.886  1.00 59.70           C  
ANISOU 5944  CA  ILE B1150     6734   8529   7420   -287   -381   -953       C  
ATOM   5945  C   ILE B1150      -4.933  29.295  42.517  1.00 65.87           C  
ANISOU 5945  C   ILE B1150     7594   9307   8125   -500   -162   -642       C  
ATOM   5946  O   ILE B1150      -5.385  30.437  42.382  1.00 66.28           O  
ANISOU 5946  O   ILE B1150     7823   9040   8321   -728   -241   -473       O  
ATOM   5947  CB  ILE B1150      -3.462  28.654  44.446  1.00 65.85           C  
ANISOU 5947  CB  ILE B1150     7058   9565   8397   -413   -392  -1039       C  
ATOM   5948  CG1 ILE B1150      -3.466  28.380  45.952  1.00 65.00           C  
ANISOU 5948  CG1 ILE B1150     6915   9416   8367   -272   -696  -1303       C  
ATOM   5949  CG2 ILE B1150      -2.805  30.005  44.176  1.00 70.63           C  
ANISOU 5949  CG2 ILE B1150     7486  10074   9275   -873   -352   -863       C  
ATOM   5950  CD1 ILE B1150      -2.087  28.176  46.556  1.00 75.95           C  
ANISOU 5950  CD1 ILE B1150     7835  11117   9904   -302   -778  -1420       C  
ATOM   5951  N   THR B1151      -4.425  28.591  41.510  1.00 63.88           N  
ANISOU 5951  N   THR B1151     7223   9416   7633   -405    112   -566       N  
ATOM   5952  CA  THR B1151      -4.461  29.077  40.139  1.00 66.31           C  
ANISOU 5952  CA  THR B1151     7632   9828   7734   -566    353   -249       C  
ATOM   5953  C   THR B1151      -5.872  29.517  39.793  1.00 68.08           C  
ANISOU 5953  C   THR B1151     8305   9712   7852   -522    191   -126       C  
ATOM   5954  O   THR B1151      -6.086  30.653  39.366  1.00 69.80           O  
ANISOU 5954  O   THR B1151     8664   9704   8153   -775    175    180       O  
ATOM   5955  CB  THR B1151      -4.039  27.982  39.151  1.00 74.94           C  
ANISOU 5955  CB  THR B1151     8626  11385   8462   -328    644   -310       C  
ATOM   5956  OG1 THR B1151      -2.680  27.620  39.399  1.00 76.29           O  
ANISOU 5956  OG1 THR B1151     8318  11910   8758   -335    813   -417       O  
ATOM   5957  CG2 THR B1151      -4.182  28.461  37.714  1.00 77.24           C  
ANISOU 5957  CG2 THR B1151     9078  11852   8419   -469    890     24       C  
ATOM   5958  N   THR B1152      -6.831  28.620  40.011  1.00 61.03           N  
ANISOU 5958  N   THR B1152     7613   8761   6814   -204     52   -354       N  
ATOM   5959  CA  THR B1152      -8.226  28.857  39.630  1.00 59.36           C  
ANISOU 5959  CA  THR B1152     7756   8309   6489   -112   -111   -282       C  
ATOM   5960  C   THR B1152      -8.812  30.136  40.230  1.00 62.82           C  
ANISOU 5960  C   THR B1152     8322   8310   7236   -267   -331   -175       C  
ATOM   5961  O   THR B1152      -9.481  30.896  39.523  1.00 63.88           O  
ANISOU 5961  O   THR B1152     8682   8264   7325   -318   -397     79       O  
ATOM   5962  CB  THR B1152      -9.106  27.661  40.001  1.00 64.91           C  
ANISOU 5962  CB  THR B1152     8570   9004   7090    195   -239   -576       C  
ATOM   5963  OG1 THR B1152      -8.699  26.528  39.220  1.00 66.54           O  
ANISOU 5963  OG1 THR B1152     8736   9536   7011    364    -63   -689       O  
ATOM   5964  CG2 THR B1152     -10.578  27.974  39.741  1.00 62.35           C  
ANISOU 5964  CG2 THR B1152     8520   8451   6719    270   -440   -527       C  
ATOM   5965  N   PHE B1153      -8.563  30.371  41.521  1.00 57.92           N  
ANISOU 5965  N   PHE B1153     7572   7522   6912   -310   -466   -384       N  
ATOM   5966  CA  PHE B1153      -8.916  31.653  42.148  1.00 58.47           C  
ANISOU 5966  CA  PHE B1153     7739   7166   7310   -458   -666   -363       C  
ATOM   5967  C   PHE B1153      -8.210  32.786  41.411  1.00 67.07           C  
ANISOU 5967  C   PHE B1153     8814   8117   8551   -808   -575     -3       C  
ATOM   5968  O   PHE B1153      -8.813  33.806  41.107  1.00 68.84           O  
ANISOU 5968  O   PHE B1153     9268   7962   8927   -884   -700    203       O  
ATOM   5969  CB  PHE B1153      -8.514  31.715  43.628  1.00 59.14           C  
ANISOU 5969  CB  PHE B1153     7660   7182   7627   -474   -811   -686       C  
ATOM   5970  CG  PHE B1153      -9.340  30.842  44.541  1.00 56.81           C  
ANISOU 5970  CG  PHE B1153     7423   6951   7212   -172   -916   -978       C  
ATOM   5971  CD1 PHE B1153     -10.716  30.980  44.612  1.00 58.27           C  
ANISOU 5971  CD1 PHE B1153     7822   6944   7373      8  -1024  -1028       C  
ATOM   5972  CD2 PHE B1153      -8.728  29.912  45.369  1.00 57.42           C  
ANISOU 5972  CD2 PHE B1153     7317   7286   7214    -75   -912  -1174       C  
ATOM   5973  CE1 PHE B1153     -11.473  30.179  45.474  1.00 56.37           C  
ANISOU 5973  CE1 PHE B1153     7595   6797   7025    232  -1075  -1257       C  
ATOM   5974  CE2 PHE B1153      -9.470  29.121  46.227  1.00 57.51           C  
ANISOU 5974  CE2 PHE B1153     7400   7349   7102    161   -988  -1363       C  
ATOM   5975  CZ  PHE B1153     -10.846  29.251  46.280  1.00 54.16           C  
ANISOU 5975  CZ  PHE B1153     7174   6757   6647    289  -1046  -1399       C  
ATOM   5976  N   ARG B1154      -6.930  32.599  41.118  1.00 65.81           N  
ANISOU 5976  N   ARG B1154     8369   8263   8371  -1019   -354     93       N  
ATOM   5977  CA  ARG B1154      -6.141  33.657  40.497  1.00 70.94           C  
ANISOU 5977  CA  ARG B1154     8942   8811   9199  -1433   -226    469       C  
ATOM   5978  C   ARG B1154      -6.635  34.018  39.088  1.00 77.33           C  
ANISOU 5978  C   ARG B1154    10029   9619   9735  -1468    -97    929       C  
ATOM   5979  O   ARG B1154      -6.853  35.197  38.792  1.00 80.40           O  
ANISOU 5979  O   ARG B1154    10615   9591  10341  -1697   -189   1262       O  
ATOM   5980  CB  ARG B1154      -4.654  33.272  40.463  1.00 74.31           C  
ANISOU 5980  CB  ARG B1154     8912   9675   9646  -1640     25    462       C  
ATOM   5981  CG  ARG B1154      -3.693  34.436  40.157  1.00 91.51           C  
ANISOU 5981  CG  ARG B1154    10900  11724  12144  -2175    138    805       C  
ATOM   5982  CD  ARG B1154      -2.232  34.040  40.391  1.00107.32           C  
ANISOU 5982  CD  ARG B1154    12338  14187  14253  -2365    334    700       C  
ATOM   5983  NE  ARG B1154      -1.959  32.672  39.939  1.00118.63           N  
ANISOU 5983  NE  ARG B1154    13595  16213  15266  -2006    582    560       N  
ATOM   5984  CZ  ARG B1154      -1.787  32.299  38.667  1.00138.12           C  
ANISOU 5984  CZ  ARG B1154    16060  19084  17337  -1967    946    820       C  
ATOM   5985  NH1 ARG B1154      -1.846  33.187  37.671  1.00130.43           N  
ANISOU 5985  NH1 ARG B1154    15248  18032  16276  -2287   1128   1317       N  
ATOM   5986  NH2 ARG B1154      -1.549  31.020  38.384  1.00124.38           N  
ANISOU 5986  NH2 ARG B1154    14170  17822  15265  -1590   1125    580       N  
ATOM   5987  N   THR B1155      -6.827  33.006  38.238  1.00 72.67           N  
ANISOU 5987  N   THR B1155     9476   9471   8665  -1227     84    938       N  
ATOM   5988  CA  THR B1155      -7.091  33.225  36.804  1.00 75.85           C  
ANISOU 5988  CA  THR B1155    10104  10038   8678  -1261    241   1371       C  
ATOM   5989  C   THR B1155      -8.582  33.262  36.417  1.00 78.33           C  
ANISOU 5989  C   THR B1155    10814  10137   8809   -973    -25   1411       C  
ATOM   5990  O   THR B1155      -8.942  33.749  35.336  1.00 81.30           O  
ANISOU 5990  O   THR B1155    11438  10533   8918  -1013     -9   1829       O  
ATOM   5991  CB  THR B1155      -6.378  32.154  35.930  1.00 83.34           C  
ANISOU 5991  CB  THR B1155    10865  11659   9140  -1162    604   1334       C  
ATOM   5992  OG1 THR B1155      -6.860  30.846  36.262  1.00 77.26           O  
ANISOU 5992  OG1 THR B1155    10097  11057   8200   -760    516    864       O  
ATOM   5993  CG2 THR B1155      -4.874  32.199  36.138  1.00 84.54           C  
ANISOU 5993  CG2 THR B1155    10559  12096   9468  -1445    898   1355       C  
ATOM   5994  N   GLY B1156      -9.442  32.743  37.289  1.00 70.41           N  
ANISOU 5994  N   GLY B1156     9848   8971   7933   -687   -271   1001       N  
ATOM   5995  CA  GLY B1156     -10.854  32.588  36.958  1.00 68.90           C  
ANISOU 5995  CA  GLY B1156     9926   8673   7580   -397   -514    969       C  
ATOM   5996  C   GLY B1156     -11.112  31.607  35.817  1.00 73.68           C  
ANISOU 5996  C   GLY B1156    10620   9746   7629   -216   -410    971       C  
ATOM   5997  O   GLY B1156     -12.187  31.646  35.208  1.00 73.81           O  
ANISOU 5997  O   GLY B1156    10862   9734   7447    -37   -618   1055       O  
ATOM   5998  N   THR B1157     -10.137  30.726  35.541  1.00 70.74           N  
ANISOU 5998  N   THR B1157    10055   9809   7015   -234   -115    837       N  
ATOM   5999  CA  THR B1157     -10.210  29.746  34.438  1.00 71.71           C  
ANISOU 5999  CA  THR B1157    10256  10403   6585    -52     15    754       C  
ATOM   6000  C   THR B1157      -9.958  28.312  34.922  1.00 72.53           C  
ANISOU 6000  C   THR B1157    10185  10701   6672    165     83    247       C  
ATOM   6001  O   THR B1157      -9.496  28.091  36.048  1.00 69.55           O  
ANISOU 6001  O   THR B1157     9592  10178   6657    148     85     41       O  
ATOM   6002  CB  THR B1157      -9.199  30.072  33.312  1.00 82.66           C  
ANISOU 6002  CB  THR B1157    11610  12205   7593   -246    374   1119       C  
ATOM   6003  OG1 THR B1157      -7.872  30.120  33.848  1.00 80.55           O  
ANISOU 6003  OG1 THR B1157    10985  12045   7576   -451    655   1093       O  
ATOM   6004  CG2 THR B1157      -9.530  31.402  32.661  1.00 85.82           C  
ANISOU 6004  CG2 THR B1157    12260  12404   7943   -451    293   1705       C  
ATOM   6005  N   TRP B1158     -10.263  27.349  34.051  1.00 69.88           N  
ANISOU 6005  N   TRP B1158     9965  10679   5908    376    110     50       N  
ATOM   6006  CA  TRP B1158     -10.130  25.925  34.359  1.00 67.74           C  
ANISOU 6006  CA  TRP B1158     9596  10515   5626    610    136   -429       C  
ATOM   6007  C   TRP B1158      -8.824  25.359  33.818  1.00 75.09           C  
ANISOU 6007  C   TRP B1158    10329  11889   6312    665    511   -533       C  
ATOM   6008  O   TRP B1158      -8.675  24.144  33.699  1.00 74.89           O  
ANISOU 6008  O   TRP B1158    10279  12000   6176    915    553   -931       O  
ATOM   6009  CB  TRP B1158     -11.297  25.152  33.744  1.00 66.46           C  
ANISOU 6009  CB  TRP B1158     9677  10376   5198    811   -102   -670       C  
ATOM   6010  CG  TRP B1158     -12.640  25.585  34.245  1.00 65.03           C  
ANISOU 6010  CG  TRP B1158     9613   9830   5266    797   -461   -616       C  
ATOM   6011  CD1 TRP B1158     -13.535  26.413  33.613  1.00 69.74           C  
ANISOU 6011  CD1 TRP B1158    10397  10389   5714    772   -675   -346       C  
ATOM   6012  CD2 TRP B1158     -13.250  25.211  35.486  1.00 60.86           C  
ANISOU 6012  CD2 TRP B1158     8996   8961   5169    831   -638   -827       C  
ATOM   6013  NE1 TRP B1158     -14.662  26.575  34.391  1.00 66.48           N  
ANISOU 6013  NE1 TRP B1158     9972   9637   5651    811   -969   -420       N  
ATOM   6014  CE2 TRP B1158     -14.508  25.850  35.545  1.00 64.34           C  
ANISOU 6014  CE2 TRP B1158     9533   9199   5716    828   -924   -710       C  
ATOM   6015  CE3 TRP B1158     -12.855  24.399  36.553  1.00 59.41           C  
ANISOU 6015  CE3 TRP B1158     8657   8649   5269    878   -581  -1076       C  
ATOM   6016  CZ2 TRP B1158     -15.368  25.698  36.628  1.00 60.61           C  
ANISOU 6016  CZ2 TRP B1158     8972   8449   5609    854  -1099   -861       C  
ATOM   6017  CZ3 TRP B1158     -13.712  24.250  37.628  1.00 57.94           C  
ANISOU 6017  CZ3 TRP B1158     8434   8172   5407    883   -768  -1176       C  
ATOM   6018  CH2 TRP B1158     -14.950  24.895  37.658  1.00 58.26           C  
ANISOU 6018  CH2 TRP B1158     8541   8063   5534    862   -998  -1081       C  
ATOM   6019  N   ASP B1159      -7.874  26.238  33.508  1.00 74.97           N  
ANISOU 6019  N   ASP B1159    10154  12081   6251    430    785   -183       N  
ATOM   6020  CA  ASP B1159      -6.671  25.861  32.756  1.00 79.32           C  
ANISOU 6020  CA  ASP B1159    10480  13174   6483    465   1204   -218       C  
ATOM   6021  C   ASP B1159      -5.662  25.007  33.547  1.00 81.86           C  
ANISOU 6021  C   ASP B1159    10426  13575   7101    622   1342   -571       C  
ATOM   6022  O   ASP B1159      -4.842  24.295  32.955  1.00 84.99           O  
ANISOU 6022  O   ASP B1159    10637  14417   7239    812   1644   -784       O  
ATOM   6023  CB  ASP B1159      -5.994  27.116  32.171  1.00 85.88           C  
ANISOU 6023  CB  ASP B1159    11222  14213   7196    100   1478    337       C  
ATOM   6024  CG  ASP B1159      -6.686  27.629  30.897  1.00 99.97           C  
ANISOU 6024  CG  ASP B1159    13378  16180   8424     56   1468    685       C  
ATOM   6025  OD1 ASP B1159      -7.766  27.111  30.524  1.00 99.02           O  
ANISOU 6025  OD1 ASP B1159    13569  16005   8049    297   1190    476       O  
ATOM   6026  OD2 ASP B1159      -6.139  28.554  30.258  1.00110.83           O  
ANISOU 6026  OD2 ASP B1159    14726  17770   9615   -237   1727   1193       O  
ATOM   6027  N   ALA B1160      -5.730  25.062  34.874  1.00 73.68           N  
ANISOU 6027  N   ALA B1160     9281  12136   6580    582   1111   -647       N  
ATOM   6028  CA  ALA B1160      -4.914  24.183  35.709  1.00 72.26           C  
ANISOU 6028  CA  ALA B1160     8791  11989   6677    784   1144   -965       C  
ATOM   6029  C   ALA B1160      -5.465  22.762  35.693  1.00 73.74           C  
ANISOU 6029  C   ALA B1160     9165  12074   6777   1173   1003  -1394       C  
ATOM   6030  O   ALA B1160      -4.795  21.838  36.146  1.00 74.04           O  
ANISOU 6030  O   ALA B1160     9000  12154   6979   1429   1040  -1672       O  
ATOM   6031  CB  ALA B1160      -4.847  24.706  37.132  1.00 69.72           C  
ANISOU 6031  CB  ALA B1160     8333  11307   6852    621    914   -897       C  
ATOM   6032  N   TYR B1161      -6.687  22.601  35.184  1.00 67.93           N  
ANISOU 6032  N   TYR B1161     8807  11178   5826   1212    811  -1440       N  
ATOM   6033  CA  TYR B1161      -7.319  21.290  35.033  1.00 83.00           C  
ANISOU 6033  CA  TYR B1161    10922  12948   7664   1511    652  -1848       C  
ATOM   6034  C   TYR B1161      -7.563  20.882  33.571  1.00 93.96           C  
ANISOU 6034  C   TYR B1161    12521  14671   8511   1654    757  -2031       C  
ATOM   6035  O   TYR B1161      -7.869  19.721  33.299  1.00 66.11           O  
ANISOU 6035  O   TYR B1161     9139  11067   4912   1916    658  -2451       O  
ATOM   6036  CB  TYR B1161      -8.661  21.279  35.760  1.00 79.86           C  
ANISOU 6036  CB  TYR B1161    10755  12080   7507   1432    282  -1833       C  
ATOM   6037  CG  TYR B1161      -8.582  21.513  37.251  1.00 78.06           C  
ANISOU 6037  CG  TYR B1161    10380  11542   7735   1341    153  -1729       C  
ATOM   6038  CD1 TYR B1161      -8.895  20.496  38.149  1.00 78.19           C  
ANISOU 6038  CD1 TYR B1161    10436  11260   8012   1493    -20  -1934       C  
ATOM   6039  CD2 TYR B1161      -8.221  22.751  37.763  1.00 78.03           C  
ANISOU 6039  CD2 TYR B1161    10226  11534   7887   1094    188  -1423       C  
ATOM   6040  CE1 TYR B1161      -8.841  20.701  39.515  1.00 76.57           C  
ANISOU 6040  CE1 TYR B1161    10123  10842   8129   1424   -136  -1825       C  
ATOM   6041  CE2 TYR B1161      -8.166  22.971  39.131  1.00 76.35           C  
ANISOU 6041  CE2 TYR B1161     9900  11080   8028   1028     47  -1389       C  
ATOM   6042  CZ  TYR B1161      -8.476  21.940  40.006  1.00 82.42           C  
ANISOU 6042  CZ  TYR B1161    10710  11636   8969   1206   -107  -1584       C  
ATOM   6043  OH  TYR B1161      -8.422  22.153  41.371  1.00 81.14           O  
ANISOU 6043  OH  TYR B1161    10457  11307   9067   1153   -242  -1535       O  
ATOM   6044  N   GLY B 319      -7.444  21.824  32.636  1.00132.69           N  
ANISOU 6044  N   GLY B 319    28081  13487   8848    475   7255  -1809       N  
ATOM   6045  CA  GLY B 319      -7.791  21.564  31.241  1.00125.56           C  
ANISOU 6045  CA  GLY B 319    26321  12507   8880    534   7148  -1680       C  
ATOM   6046  C   GLY B 319      -6.767  20.710  30.522  1.00124.15           C  
ANISOU 6046  C   GLY B 319    25758  12804   8609    700   6435  -1391       C  
ATOM   6047  O   GLY B 319      -6.777  19.488  30.639  1.00124.02           O  
ANISOU 6047  O   GLY B 319    25844  12802   8477    940   6536  -1083       O  
ATOM   6048  N   VAL B 320      -5.896  21.368  29.761  1.00116.21           N  
ANISOU 6048  N   VAL B 320    24303  12147   7703    569   5768  -1493       N  
ATOM   6049  CA  VAL B 320      -4.827  20.709  29.009  1.00112.07           C  
ANISOU 6049  CA  VAL B 320    23374  12066   7141    692   5077  -1254       C  
ATOM   6050  C   VAL B 320      -3.609  21.640  29.053  1.00114.99           C  
ANISOU 6050  C   VAL B 320    23713  12854   7125    506   4400  -1457       C  
ATOM   6051  O   VAL B 320      -3.774  22.862  29.024  1.00114.86           O  
ANISOU 6051  O   VAL B 320    23653  12723   7267    265   4464  -1782       O  
ATOM   6052  CB  VAL B 320      -5.250  20.453  27.543  1.00109.89           C  
ANISOU 6052  CB  VAL B 320    22329  11675   7748    729   5050  -1153       C  
ATOM   6053  CG1 VAL B 320      -4.153  19.745  26.786  1.00106.60           C  
ANISOU 6053  CG1 VAL B 320    21541  11672   7291    847   4416   -916       C  
ATOM   6054  CG2 VAL B 320      -6.542  19.647  27.485  1.00109.49           C  
ANISOU 6054  CG2 VAL B 320    22250  11176   8176    865   5735  -1029       C  
ATOM   6055  N   PRO B 321      -2.385  21.084  29.139  1.00110.73           N  
ANISOU 6055  N   PRO B 321    23178  12774   6121    615   3774  -1275       N  
ATOM   6056  CA  PRO B 321      -1.241  21.996  29.273  1.00111.73           C  
ANISOU 6056  CA  PRO B 321    23272  13275   5905    418   3149  -1510       C  
ATOM   6057  C   PRO B 321      -1.053  22.892  28.052  1.00111.32           C  
ANISOU 6057  C   PRO B 321    22555  13213   6528    236   2924  -1684       C  
ATOM   6058  O   PRO B 321      -1.358  22.478  26.933  1.00106.23           O  
ANISOU 6058  O   PRO B 321    21395  12464   6504    331   2972  -1506       O  
ATOM   6059  CB  PRO B 321      -0.046  21.047  29.439  1.00114.57           C  
ANISOU 6059  CB  PRO B 321    23639  14089   5802    620   2543  -1210       C  
ATOM   6060  CG  PRO B 321      -0.636  19.732  29.831  1.00119.92           C  
ANISOU 6060  CG  PRO B 321    24616  14605   6342    917   2958   -848       C  
ATOM   6061  CD  PRO B 321      -1.964  19.672  29.165  1.00111.87           C  
ANISOU 6061  CD  PRO B 321    23347  13101   6057    910   3619   -866       C  
ATOM   6062  N   LEU B 322      -0.560  24.109  28.269  1.00109.86           N  
ANISOU 6062  N   LEU B 322    22405  13125   6210    -27   2700  -2036       N  
ATOM   6063  CA  LEU B 322      -0.360  25.057  27.171  1.00105.97           C  
ANISOU 6063  CA  LEU B 322    21334  12593   6338   -199   2537  -2203       C  
ATOM   6064  C   LEU B 322       0.697  24.534  26.204  1.00106.68           C  
ANISOU 6064  C   LEU B 322    20898  13014   6622    -95   1946  -1981       C  
ATOM   6065  O   LEU B 322       0.621  24.777  25.003  1.00101.92           O  
ANISOU 6065  O   LEU B 322    19768  12321   6636   -110   1920  -1937       O  
ATOM   6066  CB  LEU B 322       0.041  26.439  27.701  1.00109.40           C  
ANISOU 6066  CB  LEU B 322    21946  13054   6565   -511   2445  -2643       C  
ATOM   6067  CG  LEU B 322      -0.145  27.612  26.732  1.00111.04           C  
ANISOU 6067  CG  LEU B 322    21677  13047   7467   -697   2551  -2846       C  
ATOM   6068  CD1 LEU B 322      -1.618  27.814  26.408  1.00109.31           C  
ANISOU 6068  CD1 LEU B 322    21404  12332   7798   -659   3242  -2813       C  
ATOM   6069  CD2 LEU B 322       0.447  28.888  27.307  1.00117.69           C  
ANISOU 6069  CD2 LEU B 322    22695  13949   8075  -1013   2421  -3293       C  
ATOM   6070  N   ARG B 323       1.679  23.816  26.742  1.00105.74           N  
ANISOU 6070  N   ARG B 323    20940  13267   5970     19   1