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***  alt_ede1  ***

elNémo ID: 22101204534384325

Job options:

ID        	=	 22101204534384325
JOBID     	=	 alt_ede1
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 alt_ede1

HEADER    IMMUNE SYSTEM-VIRAL PROTEIN             17-JUN-16   5LBS              
TITLE     STRUCTURAL BASIS OF ZIKA AND DENGUE VIRUS POTENT ANTIBODY CROSS-      
TITLE    2 NEUTRALIZATION                                                       
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: ENVELOPE PROTEIN E;                                        
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 ENGINEERED: YES;                                                     
COMPND   5 MOL_ID: 2;                                                           
COMPND   6 MOLECULE: BROADLY NEUTRALIZING HUMAN ANTIBODY EDE1 C8;               
COMPND   7 CHAIN: H, I;                                                         
COMPND   8 ENGINEERED: YES;                                                     
COMPND   9 OTHER_DETAILS: SCFV FRAGMENT, HEAVY CHAIN;                           
COMPND  10 MOL_ID: 3;                                                           
COMPND  11 MOLECULE: BROADLY NEUTRALIZING HUMAN ANTIBODY EDE1 C8;               
COMPND  12 CHAIN: L, M;                                                         
COMPND  13 ENGINEERED: YES;                                                     
COMPND  14 OTHER_DETAILS: SCFV FRAGMENT, LIGHT CHAIN                            
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: ZIKA VIRUS;                                     
SOURCE   3 ORGANISM_COMMON: ZIKV;                                               
SOURCE   4 ORGANISM_TAXID: 64320;                                               
SOURCE   5 STRAIN: MR 766;                                                      
SOURCE   6 EXPRESSION_SYSTEM: DROSOPHILA MELANOGASTER;                          
SOURCE   7 EXPRESSION_SYSTEM_COMMON: FUIT FLY;                                  
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 7227;                                       
SOURCE   9 EXPRESSION_SYSTEM_CELL: SCHNEIDER 2;                                 
SOURCE  10 MOL_ID: 2;                                                           
SOURCE  11 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  12 ORGANISM_COMMON: HUMAN;                                              
SOURCE  13 ORGANISM_TAXID: 9606;                                                
SOURCE  14 EXPRESSION_SYSTEM: DROSOPHILA MELANOGASTER;                          
SOURCE  15 EXPRESSION_SYSTEM_COMMON: FUIT FLY;                                  
SOURCE  16 EXPRESSION_SYSTEM_TAXID: 7227;                                       
SOURCE  17 EXPRESSION_SYSTEM_CELL: SCHNEIDER 2;                                 
SOURCE  18 MOL_ID: 3;                                                           
SOURCE  19 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  20 ORGANISM_COMMON: HUMAN;                                              
SOURCE  21 ORGANISM_TAXID: 9606;                                                
SOURCE  22 EXPRESSION_SYSTEM: DROSOPHILA MELANOGASTER;                          
SOURCE  23 EXPRESSION_SYSTEM_COMMON: FRUIT FLY;                                 
SOURCE  24 EXPRESSION_SYSTEM_TAXID: 7227;                                       
SOURCE  25 EXPRESSION_SYSTEM_CELL: SCHNEIDER 2                                  
KEYWDS    IMMUNE SYSTEM-VIRAL PROTEIN COMPLEX, ZIKA VIRUS, BROADLY NEUTRALIZING 
KEYWDS   2 ANTIBODY, IMMUNE SYSTEM-VIRAL PROTEIN                                
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    M.C.VANEY,A.ROUVINSKI,G.BARBA-SPAETH,F.A.REY                          
REVDAT   5   12-JUN-19 5LBS    1       AUTHOR ATOM                              
REVDAT   4   17-AUG-16 5LBS    1       JRNL                                     
REVDAT   3   20-JUL-16 5LBS    1       JRNL                                     
REVDAT   2   13-JUL-16 5LBS    1       REMARK                                   
REVDAT   1   06-JUL-16 5LBS    0                                                
JRNL        AUTH   G.BARBA-SPAETH,W.DEJNIRATTISAI,A.ROUVINSKI,M.C.VANEY,        
JRNL        AUTH 2 I.MEDITS,A.SHARMA,E.SIMON-LORIERE,A.SAKUNTABHAI,             
JRNL        AUTH 3 V.M.CAO-LORMEAU,A.HAOUZ,P.ENGLAND,K.STIASNY,J.MONGKOLSAPAYA, 
JRNL        AUTH 4 F.X.HEINZ,G.R.SCREATON,F.A.REY                               
JRNL        TITL   STRUCTURAL BASIS OF POTENT ZIKA-DENGUE VIRUS ANTIBODY        
JRNL        TITL 2 CROSS-NEUTRALIZATION.                                        
JRNL        REF    NATURE                        V. 536    48 2016              
JRNL        REFN                   ESSN 1476-4687                               
JRNL        PMID   27338953                                                     
JRNL        DOI    10.1038/NATURE18938                                          
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   A.ROUVINSKI,P.GUARDADO-CALVO,G.BARBA-SPAETH,S.DUQUERROY,     
REMARK   1  AUTH 2 M.C.VANEY,C.M.KIKUTI,M.E.NAVARRO SANCHEZ,W.DEJNIRATTISAI,    
REMARK   1  AUTH 3 W.WONGWIWAT,A.HAOUZ,C.GIRARD-BLANC,S.PETRES,W.E.SHEPARD,     
REMARK   1  AUTH 4 P.DESPRES,F.ARENZANA-SEISDEDOS,P.DUSSART,J.MONGKOLSAPAYA,    
REMARK   1  AUTH 5 G.R.SCREATON,F.A.REY                                         
REMARK   1  TITL   RECOGNITION DETERMINANTS OF BROADLY NEUTRALIZING HUMAN       
REMARK   1  TITL 2 ANTIBODIES AGAINST DENGUE VIRUSES.                           
REMARK   1  REF    NATURE                        V. 520   109 2015              
REMARK   1  REFN                   ESSN 1476-4687                               
REMARK   1  PMID   25581790                                                     
REMARK   1  DOI    10.1038/NATURE14130                                          
REMARK   1 REFERENCE 2                                                          
REMARK   1  AUTH   W.DEJNIRATTISAI,W.WONGWIWAT,S.SUPASA,X.ZHANG,X.DAI,          
REMARK   1  AUTH 2 A.ROUVINSKI,A.ROUVINSKY,A.JUMNAINSONG,C.EDWARDS,N.T.QUYEN,   
REMARK   1  AUTH 3 T.DUANGCHINDA,J.M.GRIMES,W.Y.TSAI,C.Y.LAI,W.K.WANG,          
REMARK   1  AUTH 4 P.MALASIT,J.FARRAR,C.P.SIMMONS,Z.H.ZHOU,F.A.REY,             
REMARK   1  AUTH 5 J.MONGKOLSAPAYA,G.R.SCREATON                                 
REMARK   1  TITL   A NEW CLASS OF HIGHLY POTENT, BROADLY NEUTRALIZING           
REMARK   1  TITL 2 ANTIBODIES ISOLATED FROM VIREMIC PATIENTS INFECTED WITH      
REMARK   1  TITL 3 DENGUE VIRUS.                                                
REMARK   1  REF    NAT. IMMUNOL.                 V.  16   170 2015              
REMARK   1  REFN                   ESSN 1529-2916                               
REMARK   1  PMID   25501631                                                     
REMARK   1  DOI    10.1038/NI.3058                                              
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.41 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : BUSTER 2.10.2                                        
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) : 2.41                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 39.96                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 87.3                           
REMARK   3   NUMBER OF REFLECTIONS             : 65260                          
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)  : 0.195                          
REMARK   3   R VALUE            (WORKING SET)  : 0.194                          
REMARK   3   FREE R VALUE                      : 0.217                          
REMARK   3   FREE R VALUE TEST SET SIZE   (%)  : 4.910                          
REMARK   3   FREE R VALUE TEST SET COUNT       : 3203                           
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               : 20                       
REMARK   3   BIN RESOLUTION RANGE HIGH   (ANGSTROMS) : 2.41                     
REMARK   3   BIN RESOLUTION RANGE LOW    (ANGSTROMS) : 2.47                     
REMARK   3   BIN COMPLETENESS (WORKING+TEST)     (%) : 40.32                    
REMARK   3   REFLECTIONS IN BIN (WORKING + TEST SET) : 2191                     
REMARK   3   BIN R VALUE        (WORKING + TEST SET) : 0.2314                   
REMARK   3   REFLECTIONS IN BIN        (WORKING SET) : 2071                     
REMARK   3   BIN R VALUE               (WORKING SET) : 0.2300                   
REMARK   3   BIN FREE R VALUE                        : 0.2552                   
REMARK   3   BIN FREE R VALUE TEST SET SIZE      (%) : 5.48                     
REMARK   3   BIN FREE R VALUE TEST SET COUNT         : 120                      
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            : 9572                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 59                                      
REMARK   3   SOLVENT ATOMS            : 180                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 35.74                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 55.69                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 1.90830                                              
REMARK   3    B22 (A**2) : -1.67340                                             
REMARK   3    B33 (A**2) : -0.23490                                             
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) : 0.363               
REMARK   3   DPI (BLOW EQ-10) BASED ON R VALUE        (A) : 0.297               
REMARK   3   DPI (BLOW EQ-9) BASED ON FREE R VALUE    (A) : 0.209               
REMARK   3   DPI (CRUICKSHANK) BASED ON R VALUE       (A) : 0.299               
REMARK   3   DPI (CRUICKSHANK) BASED ON FREE R VALUE  (A) : 0.212               
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      : 0.916                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.901                         
REMARK   3                                                                      
REMARK   3   NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15                    
REMARK   3   TERM                          COUNT    WEIGHT   FUNCTION.          
REMARK   3    BOND LENGTHS              : 9862   ; 2.000  ; HARMONIC            
REMARK   3    BOND ANGLES               : 13363  ; 2.500  ; HARMONIC            
REMARK   3    TORSION ANGLES            : 3296   ; 2.000  ; SINUSOIDAL          
REMARK   3    TRIGONAL CARBON PLANES    : 205    ; 2.000  ; HARMONIC            
REMARK   3    GENERAL PLANES            : 1443   ; 5.000  ; HARMONIC            
REMARK   3    ISOTROPIC THERMAL FACTORS : 9862   ; 20.000 ; HARMONIC            
REMARK   3    BAD NON-BONDED CONTACTS   : NULL   ; NULL   ; NULL                
REMARK   3    IMPROPER TORSIONS         : NULL   ; NULL   ; NULL                
REMARK   3    PSEUDOROTATION ANGLES     : NULL   ; NULL   ; NULL                
REMARK   3    CHIRAL IMPROPER TORSION   : 1272   ; 5.000  ; SEMIHARMONIC        
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   : 10248  ; 4.000  ; SEMIHARMONIC        
REMARK   3                                                                      
REMARK   3   RMS DEVIATIONS FROM IDEAL VALUES.                                  
REMARK   3    BOND LENGTHS                       (A) : 0.008                    
REMARK   3    BOND ANGLES                  (DEGREES) : 0.91                     
REMARK   3    PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 2.76                     
REMARK   3    OTHER TORSION ANGLES         (DEGREES) : 18.41                    
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 12                                         
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: {A|1:46 138:194 287:302}                               
REMARK   3    ORIGIN FOR THE GROUP (A):   93.3839  166.9080   32.3725           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.2546 T22:    0.3828                                    
REMARK   3     T33:   -0.3240 T12:    0.2461                                    
REMARK   3     T13:   -0.0277 T23:    0.0707                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    4.8990 L22:    1.7930                                    
REMARK   3     L33:    7.1762 L12:   -0.4030                                    
REMARK   3     L13:   -2.2402 L23:   -0.5094                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:    0.2415 S12:    1.1510 S13:   -0.1502                     
REMARK   3     S21:   -0.2216 S22:   -0.7169 S23:   -0.3305                     
REMARK   3     S31:    0.3185 S32:    1.1811 S33:    0.4754                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: {B|1:46 138:194 287:302}                               
REMARK   3    ORIGIN FOR THE GROUP (A):   51.1889  133.2610   44.0424           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:    0.4520 T22:   -0.1506                                    
REMARK   3     T33:   -0.3609 T12:    0.0970                                    
REMARK   3     T13:    0.1065 T23:   -0.0819                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    6.1335 L22:    1.9004                                    
REMARK   3     L33:    5.7165 L12:   -1.7784                                    
REMARK   3     L13:    0.8336 L23:   -1.9266                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:   -0.0151 S12:    0.3412 S13:   -0.1271                     
REMARK   3     S21:    0.0172 S22:   -0.1476 S23:    0.1900                     
REMARK   3     S31:   -0.2886 S32:   -1.1760 S33:    0.1627                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: {A|47:137 195:286}                                     
REMARK   3    ORIGIN FOR THE GROUP (A):   70.3014  172.9110   -9.9790           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.2942 T22:    0.4515                                    
REMARK   3     T33:   -0.3223 T12:    0.2165                                    
REMARK   3     T13:   -0.0833 T23:    0.0141                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    3.6839 L22:    0.0000                                    
REMARK   3     L33:    9.9775 L12:   -0.1895                                    
REMARK   3     L13:    5.4490 L23:   -0.7746                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:    0.0370 S12:   -0.3319 S13:   -0.1139                     
REMARK   3     S21:   -0.0653 S22:   -0.0001 S23:    0.0198                     
REMARK   3     S31:    0.4334 S32:    1.0874 S33:   -0.0369                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: {B|47:137 195:286}                                     
REMARK   3    ORIGIN FOR THE GROUP (A):   47.2213  127.5200   -2.8105           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:    0.6272 T22:   -0.0465                                    
REMARK   3     T33:   -0.3946 T12:    0.0697                                    
REMARK   3     T13:    0.0270 T23:   -0.1121                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    0.0244 L22:    0.0000                                    
REMARK   3     L33:   15.5701 L12:    0.1043                                    
REMARK   3     L13:    1.7666 L23:    2.2184                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:   -0.0406 S12:   -0.4184 S13:    0.1373                     
REMARK   3     S21:    0.1260 S22:   -0.1272 S23:    0.0958                     
REMARK   3     S31:    0.1863 S32:   -0.5665 S33:    0.1678                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION: {A|303:403}                                            
REMARK   3    ORIGIN FOR THE GROUP (A):   84.7258  167.2240   54.4554           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.0543 T22:   -0.2232                                    
REMARK   3     T33:   -0.2415 T12:   -0.0049                                    
REMARK   3     T13:   -0.0465 T23:   -0.0089                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    6.0814 L22:    3.3500                                    
REMARK   3     L33:    5.6631 L12:   -1.6002                                    
REMARK   3     L13:    2.3369 L23:   -0.4559                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:   -0.1701 S12:   -0.0134 S13:   -0.1420                     
REMARK   3     S21:    0.4851 S22:    0.0726 S23:   -0.0311                     
REMARK   3     S31:    0.1822 S32:    0.1902 S33:    0.0975                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    SELECTION: {B|303:403}                                            
REMARK   3    ORIGIN FOR THE GROUP (A):   70.6722  132.5750   59.0076           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:    0.6121 T22:   -0.3911                                    
REMARK   3     T33:   -0.2667 T12:    0.0427                                    
REMARK   3     T13:   -0.0281 T23:   -0.0895                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    4.6777 L22:    4.0543                                    
REMARK   3     L33:    7.9185 L12:   -1.6563                                    
REMARK   3     L13:   -1.1879 L23:   -0.5799                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:   -0.4157 S12:   -0.5322 S13:    0.3732                     
REMARK   3     S21:    0.6565 S22:    0.2813 S23:   -0.3875                     
REMARK   3     S31:   -0.5593 S32:    0.4777 S33:    0.1345                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    SELECTION: {A|437:446}                                            
REMARK   3    ORIGIN FOR THE GROUP (A):   93.7633  162.9890   60.7542           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:    0.0876 T22:    0.0144                                    
REMARK   3     T33:   -0.0940 T12:    0.0827                                    
REMARK   3     T13:   -0.1961 T23:   -0.0180                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    0.0000 L22:    7.8765                                    
REMARK   3     L33:    0.7595 L12:    2.4626                                    
REMARK   3     L13:    4.1280 L23:   -0.1044                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:    0.1301 S12:    0.6138 S13:   -0.5038                     
REMARK   3     S21:   -0.0286 S22:   -0.3318 S23:   -0.4765                     
REMARK   3     S31:    0.4965 S32:    0.1007 S33:    0.2017                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 8                                                      
REMARK   3    SELECTION: {B|437:443}                                            
REMARK   3    ORIGIN FOR THE GROUP (A):   63.0963  136.5400   66.2415           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:    0.3655 T22:   -0.1680                                    
REMARK   3     T33:   -0.3630 T12:    0.1399                                    
REMARK   3     T13:   -0.0295 T23:   -0.0396                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    0.4315 L22:    1.2830                                    
REMARK   3     L33:    0.0000 L12:    4.1382                                    
REMARK   3     L13:    2.9015 L23:   -1.5442                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:    0.0555 S12:   -0.3491 S13:    0.6019                     
REMARK   3     S21:    0.2108 S22:    0.1008 S23:   -0.3035                     
REMARK   3     S31:   -0.2315 S32:    0.2077 S33:   -0.1563                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 9                                                      
REMARK   3    SELECTION: TLS_H_SCFV                                             
REMARK   3    ORIGIN FOR THE GROUP (A):   67.7341  195.8080   29.6810           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:    0.0698 T22:   -0.0577                                    
REMARK   3     T33:   -0.2599 T12:    0.0516                                    
REMARK   3     T13:   -0.0203 T23:    0.0607                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    2.6289 L22:    5.9146                                    
REMARK   3     L33:    5.2798 L12:   -0.3338                                    
REMARK   3     L13:    0.7318 L23:    1.1910                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:   -0.0295 S12:    0.3940 S13:    0.1545                     
REMARK   3     S21:   -0.6551 S22:   -0.0533 S23:    0.2274                     
REMARK   3     S31:   -0.9622 S32:   -0.3013 S33:    0.0827                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 10                                                     
REMARK   3    SELECTION: {L|1:110}                                              
REMARK   3    ORIGIN FOR THE GROUP (A):   72.8940  193.5280   51.1555           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:    0.0799 T22:   -0.0965                                    
REMARK   3     T33:   -0.0906 T12:    0.0056                                    
REMARK   3     T13:    0.0128 T23:    0.0253                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    1.2417 L22:    4.0436                                    
REMARK   3     L33:    3.6543 L12:    0.3941                                    
REMARK   3     L13:   -0.1255 L23:    1.6196                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:    0.1001 S12:   -0.1025 S13:    0.0585                     
REMARK   3     S21:    0.4136 S22:   -0.0567 S23:   -0.0223                     
REMARK   3     S31:   -0.2515 S32:   -0.0889 S33:   -0.0434                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 11                                                     
REMARK   3    SELECTION: {I|1:113}                                              
REMARK   3    ORIGIN FOR THE GROUP (A):   72.4990  104.3170   28.4725           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:    0.3722 T22:   -0.2997                                    
REMARK   3     T33:   -0.3207 T12:    0.0054                                    
REMARK   3     T13:   -0.0968 T23:   -0.0926                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    2.2923 L22:    5.8188                                    
REMARK   3     L33:    6.2594 L12:   -0.9905                                    
REMARK   3     L13:    0.7115 L23:   -0.3536                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:    0.1610 S12:    0.5067 S13:   -0.1384                     
REMARK   3     S21:   -1.0932 S22:   -0.1561 S23:    0.3157                     
REMARK   3     S31:    0.5306 S32:    0.0009 S33:   -0.0049                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 12                                                     
REMARK   3    SELECTION: {M|1:110}                                              
REMARK   3    ORIGIN FOR THE GROUP (A):   79.7077  106.7910   49.1974           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:    0.1875 T22:   -0.1692                                    
REMARK   3     T33:   -0.1346 T12:   -0.0759                                    
REMARK   3     T13:   -0.0264 T23:   -0.0456                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    1.3085 L22:    5.4783                                    
REMARK   3     L33:    3.6071 L12:   -0.4979                                    
REMARK   3     L13:    0.4823 L23:   -1.8477                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:    0.0160 S12:    0.0150 S13:    0.0020                     
REMARK   3     S21:    0.0685 S22:   -0.1636 S23:   -0.1980                     
REMARK   3     S31:   -0.2740 S32:    0.3299 S33:    0.1476                     
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: THE DEBYE AND STARANISO PROGAMS           
REMARK   3  DEVELOPPED BY GLOBAL PHASING LTD. WERE APPLIED TO THE AIMLESS       
REMARK   3  SCALED DATA WITHOUT TRUNCATION OF THE RESOLUTION. THESE             
REMARK   3  CORRECTED ANISOTROPIC AMPLITUDES WERE USED FOR FURTHER CYCLES OF    
REMARK   3  REFINEMENTS WITH BUSTER.                                            
REMARK   4                                                                      
REMARK   4 5LBS COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 17-JUN-16.                  
REMARK 100 THE DEPOSITION ID IS D_1200000369.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 18-MAR-16                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 9.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SOLEIL                             
REMARK 200  BEAMLINE                       : PROXIMA 1                          
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9786                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS 6M                 
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : AIMLESS                            
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 74842                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.410                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 40.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY                : 7.500                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 6.7000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.41                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.46                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 7.70                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : 1.400                              
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: 4UTA                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 48.30                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.38                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.26M (NH4)2SO4 0.1M CHES PH 9.5 0.2M    
REMARK 280  NACL, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 293K               
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 2 21                        
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y,-Z                                                 
REMARK 290       3555   X+1/2,-Y,-Z+1/2                                         
REMARK 290       4555   -X+1/2,-Y,Z+1/2                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   3  1.000000  0.000000  0.000000       30.39950            
REMARK 290   SMTRY2   3  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000      128.92750            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000       30.39950            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000      128.92750            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: HEXAMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, H, L                               
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 APPLY THE FOLLOWING TO CHAINS: A, H, L                               
REMARK 350   BIOMT1   2 -1.000000  0.000000  0.000000      121.59800            
REMARK 350   BIOMT2   2  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: HEXAMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, I, M                               
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 APPLY THE FOLLOWING TO CHAINS: B, I, M                               
REMARK 350   BIOMT1   2 -1.000000  0.000000  0.000000      121.59800            
REMARK 350   BIOMT2   2  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 375                                                                      
REMARK 375 SPECIAL POSITION                                                     
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS            
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL          
REMARK 375 POSITIONS.                                                           
REMARK 375                                                                      
REMARK 375 ATOM RES CSSEQI                                                      
REMARK 375      HOH A 942  LIES ON A SPECIAL POSITION.                          
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     SER A   149                                                      
REMARK 465     GLY A   150                                                      
REMARK 465     MET A   151                                                      
REMARK 465     ILE A   152                                                      
REMARK 465     VAL A   153                                                      
REMARK 465     ASN A   154                                                      
REMARK 465     ASP A   155                                                      
REMARK 465     THR A   156                                                      
REMARK 465     GLY A   157                                                      
REMARK 465     HIS A   158                                                      
REMARK 465     GLU A   159                                                      
REMARK 465     THR A   160                                                      
REMARK 465     ARG A   193                                                      
REMARK 465     THR A   194                                                      
REMARK 465     GLY A   195                                                      
REMARK 465     LEU A   196                                                      
REMARK 465     ASP A   197                                                      
REMARK 465     THR A   231                                                      
REMARK 465     GLY A   232                                                      
REMARK 465     GLY A   404                                                      
REMARK 465     SER A   405                                                      
REMARK 465     THR A   406                                                      
REMARK 465     ILE A   407                                                      
REMARK 465     GLY A   408                                                      
REMARK 465     GLY A   409                                                      
REMARK 465     PRO A   410                                                      
REMARK 465     PHE A   411                                                      
REMARK 465     GLU A   412                                                      
REMARK 465     ASP A   413                                                      
REMARK 465     ASP A   414                                                      
REMARK 465     ASP A   415                                                      
REMARK 465     ASP A   416                                                      
REMARK 465     LYS A   417                                                      
REMARK 465     ALA A   418                                                      
REMARK 465     GLY A   419                                                      
REMARK 465     TRP A   420                                                      
REMARK 465     SER A   421                                                      
REMARK 465     HIS A   422                                                      
REMARK 465     PRO A   423                                                      
REMARK 465     GLN A   424                                                      
REMARK 465     PHE A   425                                                      
REMARK 465     GLU A   426                                                      
REMARK 465     LYS A   427                                                      
REMARK 465     GLY A   428                                                      
REMARK 465     GLY A   429                                                      
REMARK 465     GLY A   430                                                      
REMARK 465     SER A   431                                                      
REMARK 465     GLY A   432                                                      
REMARK 465     GLY A   433                                                      
REMARK 465     GLY A   434                                                      
REMARK 465     SER A   435                                                      
REMARK 465     GLY A   436                                                      
REMARK 465     LYS A   447                                                      
REMARK 465     MET B    15                                                      
REMARK 465     SER B    16                                                      
REMARK 465     GLY B    17                                                      
REMARK 465     HIS B   148                                                      
REMARK 465     SER B   149                                                      
REMARK 465     GLY B   150                                                      
REMARK 465     MET B   151                                                      
REMARK 465     ILE B   152                                                      
REMARK 465     VAL B   153                                                      
REMARK 465     ASN B   154                                                      
REMARK 465     ASP B   155                                                      
REMARK 465     THR B   156                                                      
REMARK 465     GLY B   157                                                      
REMARK 465     HIS B   158                                                      
REMARK 465     GLU B   159                                                      
REMARK 465     THR B   160                                                      
REMARK 465     ASP B   161                                                      
REMARK 465     ALA B   227                                                      
REMARK 465     GLY B   228                                                      
REMARK 465     ALA B   229                                                      
REMARK 465     ASP B   230                                                      
REMARK 465     THR B   231                                                      
REMARK 465     GLY B   232                                                      
REMARK 465     THR B   233                                                      
REMARK 465     GLY B   404                                                      
REMARK 465     SER B   405                                                      
REMARK 465     THR B   406                                                      
REMARK 465     ILE B   407                                                      
REMARK 465     GLY B   408                                                      
REMARK 465     GLY B   409                                                      
REMARK 465     PRO B   410                                                      
REMARK 465     PHE B   411                                                      
REMARK 465     GLU B   412                                                      
REMARK 465     ASP B   413                                                      
REMARK 465     ASP B   414                                                      
REMARK 465     ASP B   415                                                      
REMARK 465     ASP B   416                                                      
REMARK 465     LYS B   417                                                      
REMARK 465     ALA B   418                                                      
REMARK 465     GLY B   419                                                      
REMARK 465     TRP B   420                                                      
REMARK 465     SER B   421                                                      
REMARK 465     HIS B   422                                                      
REMARK 465     PRO B   423                                                      
REMARK 465     GLN B   424                                                      
REMARK 465     PHE B   425                                                      
REMARK 465     GLU B   426                                                      
REMARK 465     LYS B   427                                                      
REMARK 465     GLY B   428                                                      
REMARK 465     GLY B   429                                                      
REMARK 465     GLY B   430                                                      
REMARK 465     SER B   431                                                      
REMARK 465     GLY B   432                                                      
REMARK 465     GLY B   433                                                      
REMARK 465     GLY B   434                                                      
REMARK 465     SER B   435                                                      
REMARK 465     GLY B   436                                                      
REMARK 465     GLN B   444                                                      
REMARK 465     PHE B   445                                                      
REMARK 465     GLU B   446                                                      
REMARK 465     LYS B   447                                                      
REMARK 465     SER H   113                                                      
REMARK 465     GLY H   114                                                      
REMARK 465     THR H   115                                                      
REMARK 465     GLY H   116                                                      
REMARK 465     GLY H   117                                                      
REMARK 465     SER H   118                                                      
REMARK 465     GLY H   119                                                      
REMARK 465     GLY H   120                                                      
REMARK 465     GLY H   121                                                      
REMARK 465     GLY H   122                                                      
REMARK 465     SER H   123                                                      
REMARK 465     GLY H   124                                                      
REMARK 465     GLY H   125                                                      
REMARK 465     GLY H   126                                                      
REMARK 465     GLY H   127                                                      
REMARK 465     SER H   128                                                      
REMARK 465     GLY H   129                                                      
REMARK 465     GLY H   130                                                      
REMARK 465     GLY H   131                                                      
REMARK 465     ALA H   132                                                      
REMARK 465     GLY I   114                                                      
REMARK 465     THR I   115                                                      
REMARK 465     GLY I   116                                                      
REMARK 465     GLY I   117                                                      
REMARK 465     SER I   118                                                      
REMARK 465     GLY I   119                                                      
REMARK 465     GLY I   120                                                      
REMARK 465     GLY I   121                                                      
REMARK 465     GLY I   122                                                      
REMARK 465     SER I   123                                                      
REMARK 465     GLY I   124                                                      
REMARK 465     GLY I   125                                                      
REMARK 465     GLY I   126                                                      
REMARK 465     GLY I   127                                                      
REMARK 465     SER I   128                                                      
REMARK 465     GLY I   129                                                      
REMARK 465     GLY I   130                                                      
REMARK 465     GLY I   131                                                      
REMARK 465     ALA I   132                                                      
REMARK 465     SER L     0                                                      
REMARK 465     ASP L   111                                                      
REMARK 465     ASP L   112                                                      
REMARK 465     ASP L   113                                                      
REMARK 465     ASP L   114                                                      
REMARK 465     LYS L   115                                                      
REMARK 465     ALA L   116                                                      
REMARK 465     GLY L   117                                                      
REMARK 465     TRP L   118                                                      
REMARK 465     SER L   119                                                      
REMARK 465     HIS L   120                                                      
REMARK 465     PRO L   121                                                      
REMARK 465     GLN L   122                                                      
REMARK 465     PHE L   123                                                      
REMARK 465     GLU L   124                                                      
REMARK 465     LYS L   125                                                      
REMARK 465     GLY L   126                                                      
REMARK 465     GLY L   127                                                      
REMARK 465     GLY L   128                                                      
REMARK 465     SER L   129                                                      
REMARK 465     GLY L   130                                                      
REMARK 465     GLY L   131                                                      
REMARK 465     GLY L   132                                                      
REMARK 465     SER L   133                                                      
REMARK 465     GLY L   134                                                      
REMARK 465     GLY L   135                                                      
REMARK 465     GLY L   136                                                      
REMARK 465     SER L   137                                                      
REMARK 465     TRP L   138                                                      
REMARK 465     SER L   139                                                      
REMARK 465     HIS L   140                                                      
REMARK 465     PRO L   141                                                      
REMARK 465     GLN L   142                                                      
REMARK 465     PHE L   143                                                      
REMARK 465     GLU L   144                                                      
REMARK 465     LYS L   145                                                      
REMARK 465     ASP M   111                                                      
REMARK 465     ASP M   112                                                      
REMARK 465     ASP M   113                                                      
REMARK 465     ASP M   114                                                      
REMARK 465     LYS M   115                                                      
REMARK 465     ALA M   116                                                      
REMARK 465     GLY M   117                                                      
REMARK 465     TRP M   118                                                      
REMARK 465     SER M   119                                                      
REMARK 465     HIS M   120                                                      
REMARK 465     PRO M   121                                                      
REMARK 465     GLN M   122                                                      
REMARK 465     PHE M   123                                                      
REMARK 465     GLU M   124                                                      
REMARK 465     LYS M   125                                                      
REMARK 465     GLY M   126                                                      
REMARK 465     GLY M   127                                                      
REMARK 465     GLY M   128                                                      
REMARK 465     SER M   129                                                      
REMARK 465     GLY M   130                                                      
REMARK 465     GLY M   131                                                      
REMARK 465     GLY M   132                                                      
REMARK 465     SER M   133                                                      
REMARK 465     GLY M   134                                                      
REMARK 465     GLY M   135                                                      
REMARK 465     GLY M   136                                                      
REMARK 465     SER M   137                                                      
REMARK 465     TRP M   138                                                      
REMARK 465     SER M   139                                                      
REMARK 465     HIS M   140                                                      
REMARK 465     PRO M   141                                                      
REMARK 465     GLN M   142                                                      
REMARK 465     PHE M   143                                                      
REMARK 465     GLU M   144                                                      
REMARK 465     LYS M   145                                                      
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     HIS A 148    CG   ND1  CD2  CE1  NE2                             
REMARK 470     PHE A 198    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     THR A 233    N    CB   OG1  CG2                                  
REMARK 470     GLU H   1    CG   CD   OE1  OE2                                  
REMARK 470     GLU I   1    CG   CD   OE1  OE2                                  
REMARK 470     ALA M 110    C    O    CB                                        
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    CYS A   3      -29.29     65.35                                   
REMARK 500    LEU A 269       42.23    -94.24                                   
REMARK 500    ASP A 278       23.52   -142.62                                   
REMARK 500    CYS B   3      -34.59     76.89                                   
REMARK 500    ASN B 207       72.27     44.71                                   
REMARK 500    LEU B 269       37.92    -94.95                                   
REMARK 500    ASP B 278       23.58   -142.30                                   
REMARK 500    TYR H 100     -109.05     43.15                                   
REMARK 500    THR H 100D     -73.72   -109.20                                   
REMARK 500    TYR I 100     -108.41     42.82                                   
REMARK 500    THR I 100D     -71.57   -104.04                                   
REMARK 500    SER L  30     -122.00     50.92                                   
REMARK 500    ALA L  51      -32.28     69.10                                   
REMARK 500    ASN L  93      -93.06     60.44                                   
REMARK 500    SER M  30     -121.75     50.96                                   
REMARK 500    ALA M  51      -32.47     69.09                                   
REMARK 500    ASN M  93      -98.09     59.62                                   
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 EDO A 801                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 802                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 803                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 804                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 501                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO H 201                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO H 202                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO I 201                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 I 202                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO L 201                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO L 202                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO L 203                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO M 801                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO M 802                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 4UTA   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4UTB   RELATED DB: PDB                                   
DBREF  5LBS H    1   132  PDB    5LBS     5LBS             1    132             
DBREF  5LBS I    1   132  PDB    5LBS     5LBS             1    132             
DBREF  5LBS L    0   145  PDB    5LBS     5LBS             0    145             
DBREF  5LBS M    0   145  PDB    5LBS     5LBS             0    145             
SEQADV 5LBS GLY A  409  UNP  A0A120IIH           EXPRESSION TAG                 
SEQADV 5LBS PRO A  410  UNP  A0A120IIH           EXPRESSION TAG                 
SEQADV 5LBS PHE A  411  UNP  A0A120IIH           EXPRESSION TAG                 
SEQADV 5LBS GLU A  412  UNP  A0A120IIH           EXPRESSION TAG                 
SEQADV 5LBS ASP A  413  UNP  A0A120IIH           EXPRESSION TAG                 
SEQADV 5LBS ASP A  414  UNP  A0A120IIH           EXPRESSION TAG                 
SEQADV 5LBS ASP A  415  UNP  A0A120IIH           EXPRESSION TAG                 
SEQADV 5LBS ASP A  416  UNP  A0A120IIH           EXPRESSION TAG                 
SEQADV 5LBS LYS A  417  UNP  A0A120IIH           EXPRESSION TAG                 
SEQADV 5LBS ALA A  418  UNP  A0A120IIH           EXPRESSION TAG                 
SEQADV 5LBS GLY A  419  UNP  A0A120IIH           EXPRESSION TAG                 
SEQADV 5LBS TRP A  420  UNP  A0A120IIH           EXPRESSION TAG                 
SEQADV 5LBS SER A  421  UNP  A0A120IIH           EXPRESSION TAG                 
SEQADV 5LBS HIS A  422  UNP  A0A120IIH           EXPRESSION TAG                 
SEQADV 5LBS PRO A  423  UNP  A0A120IIH           EXPRESSION TAG                 
SEQADV 5LBS GLN A  424  UNP  A0A120IIH           EXPRESSION TAG                 
SEQADV 5LBS PHE A  425  UNP  A0A120IIH           EXPRESSION TAG                 
SEQADV 5LBS GLU A  426  UNP  A0A120IIH           EXPRESSION TAG                 
SEQADV 5LBS LYS A  427  UNP  A0A120IIH           EXPRESSION TAG                 
SEQADV 5LBS GLY A  428  UNP  A0A120IIH           EXPRESSION TAG                 
SEQADV 5LBS GLY A  429  UNP  A0A120IIH           EXPRESSION TAG                 
SEQADV 5LBS GLY A  430  UNP  A0A120IIH           EXPRESSION TAG                 
SEQADV 5LBS SER A  431  UNP  A0A120IIH           EXPRESSION TAG                 
SEQADV 5LBS GLY A  432  UNP  A0A120IIH           EXPRESSION TAG                 
SEQADV 5LBS GLY A  433  UNP  A0A120IIH           EXPRESSION TAG                 
SEQADV 5LBS GLY A  434  UNP  A0A120IIH           EXPRESSION TAG                 
SEQADV 5LBS SER A  435  UNP  A0A120IIH           EXPRESSION TAG                 
SEQADV 5LBS GLY A  436  UNP  A0A120IIH           EXPRESSION TAG                 
SEQADV 5LBS GLY A  437  UNP  A0A120IIH           EXPRESSION TAG                 
SEQADV 5LBS GLY A  438  UNP  A0A120IIH           EXPRESSION TAG                 
SEQADV 5LBS SER A  439  UNP  A0A120IIH           EXPRESSION TAG                 
SEQADV 5LBS TRP A  440  UNP  A0A120IIH           EXPRESSION TAG                 
SEQADV 5LBS SER A  441  UNP  A0A120IIH           EXPRESSION TAG                 
SEQADV 5LBS HIS A  442  UNP  A0A120IIH           EXPRESSION TAG                 
SEQADV 5LBS PRO A  443  UNP  A0A120IIH           EXPRESSION TAG                 
SEQADV 5LBS GLN A  444  UNP  A0A120IIH           EXPRESSION TAG                 
SEQADV 5LBS PHE A  445  UNP  A0A120IIH           EXPRESSION TAG                 
SEQADV 5LBS GLU A  446  UNP  A0A120IIH           EXPRESSION TAG                 
SEQADV 5LBS LYS A  447  UNP  A0A120IIH           EXPRESSION TAG                 
SEQADV 5LBS GLY B  409  UNP  A0A120IIH           EXPRESSION TAG                 
SEQADV 5LBS PRO B  410  UNP  A0A120IIH           EXPRESSION TAG                 
SEQADV 5LBS PHE B  411  UNP  A0A120IIH           EXPRESSION TAG                 
SEQADV 5LBS GLU B  412  UNP  A0A120IIH           EXPRESSION TAG                 
SEQADV 5LBS ASP B  413  UNP  A0A120IIH           EXPRESSION TAG                 
SEQADV 5LBS ASP B  414  UNP  A0A120IIH           EXPRESSION TAG                 
SEQADV 5LBS ASP B  415  UNP  A0A120IIH           EXPRESSION TAG                 
SEQADV 5LBS ASP B  416  UNP  A0A120IIH           EXPRESSION TAG                 
SEQADV 5LBS LYS B  417  UNP  A0A120IIH           EXPRESSION TAG                 
SEQADV 5LBS ALA B  418  UNP  A0A120IIH           EXPRESSION TAG                 
SEQADV 5LBS GLY B  419  UNP  A0A120IIH           EXPRESSION TAG                 
SEQADV 5LBS TRP B  420  UNP  A0A120IIH           EXPRESSION TAG                 
SEQADV 5LBS SER B  421  UNP  A0A120IIH           EXPRESSION TAG                 
SEQADV 5LBS HIS B  422  UNP  A0A120IIH           EXPRESSION TAG                 
SEQADV 5LBS PRO B  423  UNP  A0A120IIH           EXPRESSION TAG                 
SEQADV 5LBS GLN B  424  UNP  A0A120IIH           EXPRESSION TAG                 
SEQADV 5LBS PHE B  425  UNP  A0A120IIH           EXPRESSION TAG                 
SEQADV 5LBS GLU B  426  UNP  A0A120IIH           EXPRESSION TAG                 
SEQADV 5LBS LYS B  427  UNP  A0A120IIH           EXPRESSION TAG                 
SEQADV 5LBS GLY B  428  UNP  A0A120IIH           EXPRESSION TAG                 
SEQADV 5LBS GLY B  429  UNP  A0A120IIH           EXPRESSION TAG                 
SEQADV 5LBS GLY B  430  UNP  A0A120IIH           EXPRESSION TAG                 
SEQADV 5LBS SER B  431  UNP  A0A120IIH           EXPRESSION TAG                 
SEQADV 5LBS GLY B  432  UNP  A0A120IIH           EXPRESSION TAG                 
SEQADV 5LBS GLY B  433  UNP  A0A120IIH           EXPRESSION TAG                 
SEQADV 5LBS GLY B  434  UNP  A0A120IIH           EXPRESSION TAG                 
SEQADV 5LBS SER B  435  UNP  A0A120IIH           EXPRESSION TAG                 
SEQADV 5LBS GLY B  436  UNP  A0A120IIH           EXPRESSION TAG                 
SEQADV 5LBS GLY B  437  UNP  A0A120IIH           EXPRESSION TAG                 
SEQADV 5LBS GLY B  438  UNP  A0A120IIH           EXPRESSION TAG                 
SEQADV 5LBS SER B  439  UNP  A0A120IIH           EXPRESSION TAG                 
SEQADV 5LBS TRP B  440  UNP  A0A120IIH           EXPRESSION TAG                 
SEQADV 5LBS SER B  441  UNP  A0A120IIH           EXPRESSION TAG                 
SEQADV 5LBS HIS B  442  UNP  A0A120IIH           EXPRESSION TAG                 
SEQADV 5LBS PRO B  443  UNP  A0A120IIH           EXPRESSION TAG                 
SEQADV 5LBS GLN B  444  UNP  A0A120IIH           EXPRESSION TAG                 
SEQADV 5LBS PHE B  445  UNP  A0A120IIH           EXPRESSION TAG                 
SEQADV 5LBS GLU B  446  UNP  A0A120IIH           EXPRESSION TAG                 
SEQADV 5LBS LYS B  447  UNP  A0A120IIH           EXPRESSION TAG                 
SEQRES   1 A  447  ILE ARG CYS ILE GLY VAL SER ASN ARG ASP PHE VAL GLU          
SEQRES   2 A  447  GLY MET SER GLY GLY THR TRP VAL ASP VAL VAL LEU GLU          
SEQRES   3 A  447  HIS GLY GLY CYS VAL THR VAL MET ALA GLN ASP LYS PRO          
SEQRES   4 A  447  THR VAL ASP ILE GLU LEU VAL THR THR THR VAL SER ASN          
SEQRES   5 A  447  MET ALA GLU VAL ARG SER TYR CYS TYR GLU ALA SER ILE          
SEQRES   6 A  447  SER ASP MET ALA SER ASP SER ARG CYS PRO THR GLN GLY          
SEQRES   7 A  447  GLU ALA TYR LEU ASP LYS GLN SER ASP THR GLN TYR VAL          
SEQRES   8 A  447  CYS LYS ARG THR LEU VAL ASP ARG GLY TRP GLY ASN GLY          
SEQRES   9 A  447  CYS GLY LEU PHE GLY LYS GLY SER LEU VAL THR CYS ALA          
SEQRES  10 A  447  LYS PHE ALA CYS SER LYS LYS MET THR GLY LYS SER ILE          
SEQRES  11 A  447  GLN PRO GLU ASN LEU GLU TYR ARG ILE MET LEU SER VAL          
SEQRES  12 A  447  HIS GLY SER GLN HIS SER GLY MET ILE VAL ASN ASP THR          
SEQRES  13 A  447  GLY HIS GLU THR ASP GLU ASN ARG ALA LYS VAL GLU ILE          
SEQRES  14 A  447  THR PRO ASN SER PRO ARG ALA GLU ALA THR LEU GLY GLY          
SEQRES  15 A  447  PHE GLY SER LEU GLY LEU ASP CYS GLU PRO ARG THR GLY          
SEQRES  16 A  447  LEU ASP PHE SER ASP LEU TYR TYR LEU THR MET ASN ASN          
SEQRES  17 A  447  LYS HIS TRP LEU VAL HIS LYS GLU TRP PHE HIS ASP ILE          
SEQRES  18 A  447  PRO LEU PRO TRP HIS ALA GLY ALA ASP THR GLY THR PRO          
SEQRES  19 A  447  HIS TRP ASN ASN LYS GLU ALA LEU VAL GLU PHE LYS ASP          
SEQRES  20 A  447  ALA HIS ALA LYS ARG GLN THR VAL VAL VAL LEU GLY SER          
SEQRES  21 A  447  GLN GLU GLY ALA VAL HIS THR ALA LEU ALA GLY ALA LEU          
SEQRES  22 A  447  GLU ALA GLU MET ASP GLY ALA LYS GLY ARG LEU SER SER          
SEQRES  23 A  447  GLY HIS LEU LYS CYS ARG LEU LYS MET ASP LYS LEU ARG          
SEQRES  24 A  447  LEU LYS GLY VAL SER TYR SER LEU CYS THR ALA ALA PHE          
SEQRES  25 A  447  THR PHE THR LYS ILE PRO ALA GLU THR LEU HIS GLY THR          
SEQRES  26 A  447  VAL THR VAL GLU VAL GLN TYR ALA GLY THR ASP GLY PRO          
SEQRES  27 A  447  CYS LYS VAL PRO ALA GLN MET ALA VAL ASP MET GLN THR          
SEQRES  28 A  447  LEU THR PRO VAL GLY ARG LEU ILE THR ALA ASN PRO VAL          
SEQRES  29 A  447  ILE THR GLU SER THR GLU ASN SER LYS MET MET LEU GLU          
SEQRES  30 A  447  LEU ASP PRO PRO PHE GLY ASP SER TYR ILE VAL ILE GLY          
SEQRES  31 A  447  VAL GLY GLU LYS LYS ILE THR HIS HIS TRP HIS ARG SER          
SEQRES  32 A  447  GLY SER THR ILE GLY GLY PRO PHE GLU ASP ASP ASP ASP          
SEQRES  33 A  447  LYS ALA GLY TRP SER HIS PRO GLN PHE GLU LYS GLY GLY          
SEQRES  34 A  447  GLY SER GLY GLY GLY SER GLY GLY GLY SER TRP SER HIS          
SEQRES  35 A  447  PRO GLN PHE GLU LYS                                          
SEQRES   1 B  447  ILE ARG CYS ILE GLY VAL SER ASN ARG ASP PHE VAL GLU          
SEQRES   2 B  447  GLY MET SER GLY GLY THR TRP VAL ASP VAL VAL LEU GLU          
SEQRES   3 B  447  HIS GLY GLY CYS VAL THR VAL MET ALA GLN ASP LYS PRO          
SEQRES   4 B  447  THR VAL ASP ILE GLU LEU VAL THR THR THR VAL SER ASN          
SEQRES   5 B  447  MET ALA GLU VAL ARG SER TYR CYS TYR GLU ALA SER ILE          
SEQRES   6 B  447  SER ASP MET ALA SER ASP SER ARG CYS PRO THR GLN GLY          
SEQRES   7 B  447  GLU ALA TYR LEU ASP LYS GLN SER ASP THR GLN TYR VAL          
SEQRES   8 B  447  CYS LYS ARG THR LEU VAL ASP ARG GLY TRP GLY ASN GLY          
SEQRES   9 B  447  CYS GLY LEU PHE GLY LYS GLY SER LEU VAL THR CYS ALA          
SEQRES  10 B  447  LYS PHE ALA CYS SER LYS LYS MET THR GLY LYS SER ILE          
SEQRES  11 B  447  GLN PRO GLU ASN LEU GLU TYR ARG ILE MET LEU SER VAL          
SEQRES  12 B  447  HIS GLY SER GLN HIS SER GLY MET ILE VAL ASN ASP THR          
SEQRES  13 B  447  GLY HIS GLU THR ASP GLU ASN ARG ALA LYS VAL GLU ILE          
SEQRES  14 B  447  THR PRO ASN SER PRO ARG ALA GLU ALA THR LEU GLY GLY          
SEQRES  15 B  447  PHE GLY SER LEU GLY LEU ASP CYS GLU PRO ARG THR GLY          
SEQRES  16 B  447  LEU ASP PHE SER ASP LEU TYR TYR LEU THR MET ASN ASN          
SEQRES  17 B  447  LYS HIS TRP LEU VAL HIS LYS GLU TRP PHE HIS ASP ILE          
SEQRES  18 B  447  PRO LEU PRO TRP HIS ALA GLY ALA ASP THR GLY THR PRO          
SEQRES  19 B  447  HIS TRP ASN ASN LYS GLU ALA LEU VAL GLU PHE LYS ASP          
SEQRES  20 B  447  ALA HIS ALA LYS ARG GLN THR VAL VAL VAL LEU GLY SER          
SEQRES  21 B  447  GLN GLU GLY ALA VAL HIS THR ALA LEU ALA GLY ALA LEU          
SEQRES  22 B  447  GLU ALA GLU MET ASP GLY ALA LYS GLY ARG LEU SER SER          
SEQRES  23 B  447  GLY HIS LEU LYS CYS ARG LEU LYS MET ASP LYS LEU ARG          
SEQRES  24 B  447  LEU LYS GLY VAL SER TYR SER LEU CYS THR ALA ALA PHE          
SEQRES  25 B  447  THR PHE THR LYS ILE PRO ALA GLU THR LEU HIS GLY THR          
SEQRES  26 B  447  VAL THR VAL GLU VAL GLN TYR ALA GLY THR ASP GLY PRO          
SEQRES  27 B  447  CYS LYS VAL PRO ALA GLN MET ALA VAL ASP MET GLN THR          
SEQRES  28 B  447  LEU THR PRO VAL GLY ARG LEU ILE THR ALA ASN PRO VAL          
SEQRES  29 B  447  ILE THR GLU SER THR GLU ASN SER LYS MET MET LEU GLU          
SEQRES  30 B  447  LEU ASP PRO PRO PHE GLY ASP SER TYR ILE VAL ILE GLY          
SEQRES  31 B  447  VAL GLY GLU LYS LYS ILE THR HIS HIS TRP HIS ARG SER          
SEQRES  32 B  447  GLY SER THR ILE GLY GLY PRO PHE GLU ASP ASP ASP ASP          
SEQRES  33 B  447  LYS ALA GLY TRP SER HIS PRO GLN PHE GLU LYS GLY GLY          
SEQRES  34 B  447  GLY SER GLY GLY GLY SER GLY GLY GLY SER TRP SER HIS          
SEQRES  35 B  447  PRO GLN PHE GLU LYS                                          
SEQRES   1 H  141  GLU VAL GLN LEU VAL GLU SER GLY GLY GLY LEU VAL GLN          
SEQRES   2 H  141  PRO GLY GLY SER LEU ARG LEU SER CYS SER ALA SER GLY          
SEQRES   3 H  141  PHE THR PHE SER THR TYR SER MET HIS TRP VAL ARG GLN          
SEQRES   4 H  141  ALA PRO GLY LYS GLY LEU GLU TYR VAL SER ALA ILE THR          
SEQRES   5 H  141  GLY GLU GLY ASP SER ALA PHE TYR ALA ASP SER VAL LYS          
SEQRES   6 H  141  GLY ARG PHE THR ILE SER ARG ASP ASN SER LYS ASN THR          
SEQRES   7 H  141  LEU TYR PHE GLU MET ASN SER LEU ARG PRO GLU ASP THR          
SEQRES   8 H  141  ALA VAL TYR TYR CYS VAL GLY GLY TYR SER ASN PHE TYR          
SEQRES   9 H  141  TYR TYR TYR THR MET ASP VAL TRP GLY GLN GLY THR THR          
SEQRES  10 H  141  VAL THR VAL SER SER GLY THR GLY GLY SER GLY GLY GLY          
SEQRES  11 H  141  GLY SER GLY GLY GLY GLY SER GLY GLY GLY ALA                  
SEQRES   1 I  141  GLU VAL GLN LEU VAL GLU SER GLY GLY GLY LEU VAL GLN          
SEQRES   2 I  141  PRO GLY GLY SER LEU ARG LEU SER CYS SER ALA SER GLY          
SEQRES   3 I  141  PHE THR PHE SER THR TYR SER MET HIS TRP VAL ARG GLN          
SEQRES   4 I  141  ALA PRO GLY LYS GLY LEU GLU TYR VAL SER ALA ILE THR          
SEQRES   5 I  141  GLY GLU GLY ASP SER ALA PHE TYR ALA ASP SER VAL LYS          
SEQRES   6 I  141  GLY ARG PHE THR ILE SER ARG ASP ASN SER LYS ASN THR          
SEQRES   7 I  141  LEU TYR PHE GLU MET ASN SER LEU ARG PRO GLU ASP THR          
SEQRES   8 I  141  ALA VAL TYR TYR CYS VAL GLY GLY TYR SER ASN PHE TYR          
SEQRES   9 I  141  TYR TYR TYR THR MET ASP VAL TRP GLY GLN GLY THR THR          
SEQRES  10 I  141  VAL THR VAL SER SER GLY THR GLY GLY SER GLY GLY GLY          
SEQRES  11 I  141  GLY SER GLY GLY GLY GLY SER GLY GLY GLY ALA                  
SEQRES   1 L  147  SER GLU ILE VAL LEU THR GLN SER PRO ALA THR LEU SER          
SEQRES   2 L  147  LEU SER PRO GLY GLU ARG ALA THR LEU SER CYS ARG ALA          
SEQRES   3 L  147  SER GLN SER ILE SER THR PHE LEU ALA TRP TYR GLN HIS          
SEQRES   4 L  147  LYS PRO GLY GLN ALA PRO ARG LEU LEU ILE TYR ASP ALA          
SEQRES   5 L  147  SER THR ARG ALA THR GLY VAL PRO ALA ARG PHE SER GLY          
SEQRES   6 L  147  SER ARG SER GLY THR ASP PHE THR LEU THR ILE SER THR          
SEQRES   7 L  147  LEU GLU PRO GLU ASP PHE ALA VAL TYR TYR CYS GLN GLN          
SEQRES   8 L  147  ARG TYR ASN TRP PRO PRO TYR THR PHE GLY GLN GLY THR          
SEQRES   9 L  147  LYS VAL GLU ILE LYS ALA ALA ALA ASP ASP ASP ASP LYS          
SEQRES  10 L  147  ALA GLY TRP SER HIS PRO GLN PHE GLU LYS GLY GLY GLY          
SEQRES  11 L  147  SER GLY GLY GLY SER GLY GLY GLY SER TRP SER HIS PRO          
SEQRES  12 L  147  GLN PHE GLU LYS                                              
SEQRES   1 M  147  SER GLU ILE VAL LEU THR GLN SER PRO ALA THR LEU SER          
SEQRES   2 M  147  LEU SER PRO GLY GLU ARG ALA THR LEU SER CYS ARG ALA          
SEQRES   3 M  147  SER GLN SER ILE SER THR PHE LEU ALA TRP TYR GLN HIS          
SEQRES   4 M  147  LYS PRO GLY GLN ALA PRO ARG LEU LEU ILE TYR ASP ALA          
SEQRES   5 M  147  SER THR ARG ALA THR GLY VAL PRO ALA ARG PHE SER GLY          
SEQRES   6 M  147  SER ARG SER GLY THR ASP PHE THR LEU THR ILE SER THR          
SEQRES   7 M  147  LEU GLU PRO GLU ASP PHE ALA VAL TYR TYR CYS GLN GLN          
SEQRES   8 M  147  ARG TYR ASN TRP PRO PRO TYR THR PHE GLY GLN GLY THR          
SEQRES   9 M  147  LYS VAL GLU ILE LYS ALA ALA ALA ASP ASP ASP ASP LYS          
SEQRES  10 M  147  ALA GLY TRP SER HIS PRO GLN PHE GLU LYS GLY GLY GLY          
SEQRES  11 M  147  SER GLY GLY GLY SER GLY GLY GLY SER TRP SER HIS PRO          
SEQRES  12 M  147  GLN PHE GLU LYS                                              
HET    EDO  A 801       4                                                       
HET    EDO  A 802       4                                                       
HET    EDO  A 803       4                                                       
HET    SO4  A 804       5                                                       
HET    SO4  B 501       5                                                       
HET    EDO  H 201       4                                                       
HET    EDO  H 202       4                                                       
HET    EDO  I 201       4                                                       
HET    SO4  I 202       5                                                       
HET    EDO  L 201       4                                                       
HET    EDO  L 202       4                                                       
HET    EDO  L 203       4                                                       
HET    EDO  M 801       4                                                       
HET    EDO  M 802       4                                                       
HETNAM     EDO 1,2-ETHANEDIOL                                                   
HETNAM     SO4 SULFATE ION                                                      
HETSYN     EDO ETHYLENE GLYCOL                                                  
FORMUL   7  EDO    11(C2 H6 O2)                                                 
FORMUL  10  SO4    3(O4 S 2-)                                                   
FORMUL  21  HOH   *180(H2 O)                                                    
HELIX    1   1 THR H   28  SER H   30  1                                   3
HELIX    2   2 ARG H   83  THR H   87  1                                   5
HELIX    3   3 GLU L   79  PHE L   83  1                                   5
SHEET    1   1 1 GLN H   3  SER H   7  0
SHEET    2   2 1 GLY H  10  VAL H  12  0
SHEET    3   3 1 LEU H  18  SER H  25  0
SHEET    4   4 1 TYR H  32  GLN H  39  0
SHEET    5   5 1 LEU H  45  ILE H  51  0
SHEET    6   6 1 ALA H  57  TYR H  59  0
SHEET    7   7 1 PHE H  67  ASP H  72  0
SHEET    8   8 1 THR H  77  MET H  82  0
SHEET    9   9 1 ALA H  88  TYR H  96  0
SHEET   10  10 1 VAL H 102  TRP H 103  0
SHEET   11  11 1 THR H 107  VAL H 111  0
SHEET   12  12 1 LEU L   4  SER L   7  0
SHEET   13  13 1 THR L  10  LEU L  13  0
SHEET   14  14 1 ALA L  19  ALA L  25  0
SHEET   15  15 1 LEU L  33  HIS L  38  0
SHEET   16  16 1 ARG L  45  TYR L  49  0
SHEET   17  17 1 THR L  53  ARG L  54  0
SHEET   18  18 1 PHE L  62  SER L  67  0
SHEET   19  19 1 ASP L  70  ILE L  75  0
SHEET   20  20 1 VAL L  85  GLN L  90  0
SHEET   21  21 1 THR L 102  ILE L 106  0
SSBOND   1 CYS A    3    CYS A   30                          1555   1555  2.04  
SSBOND   2 CYS A   60    CYS A  121                          1555   1555  2.05  
SSBOND   3 CYS A   74    CYS A  105                          1555   1555  2.05  
SSBOND   4 CYS A   92    CYS A  116                          1555   1555  2.05  
SSBOND   5 CYS A  190    CYS A  291                          1555   1555  2.04  
SSBOND   6 CYS A  308    CYS A  339                          1555   1555  2.05  
SSBOND   7 CYS B    3    CYS B   30                          1555   1555  2.03  
SSBOND   8 CYS B   60    CYS B  121                          1555   1555  2.05  
SSBOND   9 CYS B   74    CYS B  105                          1555   1555  2.04  
SSBOND  10 CYS B   92    CYS B  116                          1555   1555  2.04  
SSBOND  11 CYS B  190    CYS B  291                          1555   1555  2.04  
SSBOND  12 CYS B  308    CYS B  339                          1555   1555  2.04  
SSBOND  13 CYS H   22    CYS H   92                          1555   1555  2.06  
SSBOND  14 CYS I   22    CYS I   92                          1555   1555  2.05  
SSBOND  15 CYS L   23    CYS L   88                          1555   1555  2.08  
SSBOND  16 CYS M   23    CYS M   88                          1555   1555  2.06  
CISPEP   1 GLY B  337    PRO B  338          0         2.61                     
CISPEP   2 SER L    7    PRO L    8          0        -1.66                     
CISPEP   3 PRO L   95    PRO L   95A         0         5.56                     
CISPEP   4 SER M    7    PRO M    8          0        -1.51                     
CISPEP   5 PRO M   95    PRO M   95A         0         5.38                     
SITE     1 AC1  4 HIS A 323  ARG A 357  ASP A 379  ARG A 402                    
SITE     1 AC2  2 HIS A 398  HIS A 399                                          
SITE     1 AC3  2 ILE A   1  ARG A 164                                          
SITE     1 AC4  6 ARG A 299  LEU A 300  GLY A 302  VAL A 303                    
SITE     2 AC4  6 SER A 304  TYR A 305                                          
SITE     1 AC5  4 LYS B 340  TRP B 440  SER B 441  ARG M  18                    
SITE     1 AC6  4 SER A  66  ASP A  67  MET A  68  GLY H  54                    
SITE     1 AC7  3 TYR H  32  TYR H  96  MET H 100E                              
SITE     1 AC8  4 TYR I  32  GLY I  95  TYR I  96  MET I 100E                   
SITE     1 AC9  3 THR H 108  THR I 107  THR I 108                               
SITE     1 AD1  3 ILE A 317  ARG L  66  HOH L 305                               
SITE     1 AD2  4 ARG L  45  PRO L  59  ARG L  61  GLU L  81                    
SITE     1 AD3  6 LEU H  45  GLU H  46  TYR H  47  THR L  97                    
SITE     2 AD3  6 PHE L  98  HOH L 303                                          
SITE     1 AD4  3 SER M  67  THR M  69  ASP M  70                               
SITE     1 AD5  3 ILE B 317  SER M  30  ARG M  66                               
CRYST1   60.799  121.353  257.855  90.00  90.00  90.00 P 21 2 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      0.016448  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.008240  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.003878        0.00000                         
DBREF1 5LBS A    1   408  UNP                  A0A120IIH9_ZIKV                  
DBREF1 5LBS B    1   408  UNP                  A0A120IIH9_ZIKV                  
DBREF2 5LBS A     A0A120IIH9                          1         408             
DBREF2 5LBS B     A0A120IIH9                          1         408             
ATOM      1  N   GLU H   1      89.156 196.511  30.043  1.00 52.27           N
ANISOU    1  N   GLU H   1     4361   7960   7538  -3261   2153   -485       N
ATOM      2  CA  GLU H   1      88.177 196.475  31.127  1.00 47.47           C
ANISOU    2  CA  GLU H   1     4083   7128   6824  -2992   1687   -424       C
ATOM      3  C   GLU H   1      86.775 196.175  30.609  1.00 47.63           C
ANISOU    3  C   GLU H   1     4612   7040   6444  -2710   1707   -261       C
ATOM      4  O   GLU H   1      86.392 196.654  29.537  1.00 48.36           O
ANISOU    4  O   GLU H   1     5019   7087   6270  -2833   2010   -113       O
ATOM      5  CB  GLU H   1      88.179 197.799  31.907  1.00 49.70           C
ANISOU    5  CB  GLU H   1     4602   7138   7144  -3288   1487   -337       C
ATOM      6  N   VAL H   2      86.007 195.392  31.382  1.00 40.11           N
ANISOU    6  N   VAL H   2     3751   6042   5448  -2342   1373   -287       N
ATOM      7  CA  VAL H   2      84.629 195.013  31.056  1.00 35.77           C
ANISOU    7  CA  VAL H   2     3612   5402   4578  -2067   1331   -164       C
ATOM      8  C   VAL H   2      83.708 196.235  31.276  1.00 39.38           C
ANISOU    8  C   VAL H   2     4568   5582   4814  -2162   1243     31       C
ATOM      9  O   VAL H   2      83.683 196.801  32.375  1.00 37.72           O
ANISOU    9  O   VAL H   2     4424   5215   4692  -2205    986     29       O
ATOM     10  CB  VAL H   2      84.196 193.748  31.853  1.00 35.71           C
ANISOU   10  CB  VAL H   2     3500   5435   4632  -1694   1035   -261       C
ATOM     11  CG1 VAL H   2      82.692 193.519  31.779  1.00 32.04           C
ANISOU   11  CG1 VAL H   2     3441   4849   3883  -1465    942   -133       C
ATOM     12  CG2 VAL H   2      84.947 192.515  31.366  1.00 36.45           C
ANISOU   12  CG2 VAL H   2     3197   5765   4889  -1546   1151   -442       C
ATOM     13  N   GLN H   3      83.001 196.667  30.207  1.00 37.20           N
ANISOU   13  N   GLN H   3     4657   5237   4242  -2185   1448    187       N
ATOM     14  CA  GLN H   3      82.131 197.846  30.244  1.00 37.13           C
ANISOU   14  CA  GLN H   3     5140   4953   4015  -2238   1377    371       C
ATOM     15  C   GLN H   3      80.793 197.672  29.528  1.00 39.69           C
ANISOU   15  C   GLN H   3     5828   5230   4022  -1977   1363    490       C
ATOM     16  O   GLN H   3      80.694 196.934  28.543  1.00 39.30           O
ANISOU   16  O   GLN H   3     5740   5343   3848  -1881   1523    471       O
ATOM     17  CB  GLN H   3      82.847 199.050  29.632  1.00 42.61           C
ANISOU   17  CB  GLN H   3     5978   5529   4684  -2645   1631    473       C
ATOM     18  CG  GLN H   3      83.869 199.704  30.536  1.00 63.46           C
ANISOU   18  CG  GLN H   3     8402   8090   7620  -2945   1541    392       C
ATOM     19  CD  GLN H   3      84.462 200.890  29.841  1.00 87.83           C
ANISOU   19  CD  GLN H   3    11679  11026  10667  -3384   1816    515       C
ATOM     20  OE1 GLN H   3      83.882 201.979  29.831  1.00 85.02           O
ANISOU   20  OE1 GLN H   3    11817  10357  10131  -3467   1759    678       O
ATOM     21  NE2 GLN H   3      85.596 200.685  29.184  1.00 82.90           N
ANISOU   21  NE2 GLN H   3    10684  10615  10200  -3667   2143    444       N
ATOM     22  N   LEU H   4      79.779 198.422  30.004  1.00 34.92           N
ANISOU   22  N   LEU H   4     5582   4398   3289  -1863   1164    599       N
ATOM     23  CA  LEU H   4      78.441 198.515  29.425  1.00 32.66           C
ANISOU   23  CA  LEU H   4     5642   4036   2731  -1617   1094    712       C
ATOM     24  C   LEU H   4      78.084 199.992  29.347  1.00 37.31           C
ANISOU   24  C   LEU H   4     6682   4323   3170  -1713   1065    873       C
ATOM     25  O   LEU H   4      77.931 200.647  30.378  1.00 36.64           O
ANISOU   25  O   LEU H   4     6690   4057   3174  -1705    889    863       O
ATOM     26  CB  LEU H   4      77.390 197.760  30.263  1.00 29.05           C
ANISOU   26  CB  LEU H   4     5103   3623   2312  -1287    841    644       C
ATOM     27  CG  LEU H   4      77.392 196.238  30.213  1.00 31.80           C
ANISOU   27  CG  LEU H   4     5131   4209   2744  -1133    834    518       C
ATOM     28  CD1 LEU H   4      76.271 195.684  31.059  1.00 29.05           C
ANISOU   28  CD1 LEU H   4     4770   3856   2413   -869    614    489       C
ATOM     29  CD2 LEU H   4      77.242 195.720  28.793  1.00 35.41           C
ANISOU   29  CD2 LEU H   4     5647   4790   3017  -1100    999    533       C
ATOM     30  N   VAL H   5      78.025 200.531  28.134  1.00 36.28           N
ANISOU   30  N   VAL H   5     6868   4119   2799  -1812   1239   1017       N
ATOM     31  CA  VAL H   5      77.713 201.943  27.922  1.00 38.62           C
ANISOU   31  CA  VAL H   5     7665   4083   2924  -1900   1212   1193       C
ATOM     32  C   VAL H   5      76.334 202.034  27.290  1.00 44.00           C
ANISOU   32  C   VAL H   5     8692   4698   3329  -1555   1057   1295       C
ATOM     33  O   VAL H   5      76.150 201.626  26.142  1.00 45.96           O
ANISOU   33  O   VAL H   5     9040   5064   3360  -1506   1165   1348       O
ATOM     34  CB  VAL H   5      78.801 202.685  27.092  1.00 45.81           C
ANISOU   34  CB  VAL H   5     8741   4897   3768  -2333   1529   1309       C
ATOM     35  CG1 VAL H   5      78.475 204.169  26.963  1.00 48.33           C
ANISOU   35  CG1 VAL H   5     9639   4804   3922  -2436   1471   1501       C
ATOM     36  CG2 VAL H   5      80.188 202.496  27.702  1.00 46.43           C
ANISOU   36  CG2 VAL H   5     8357   5104   4179  -2670   1670   1168       C
ATOM     37  N   GLU H   6      75.364 202.551  28.039  1.00 39.02           N
ANISOU   37  N   GLU H   6     8228   3892   2706  -1299    794   1301       N
ATOM     38  CA  GLU H   6      74.003 202.659  27.536  1.00 38.78           C
ANISOU   38  CA  GLU H   6     8454   3813   2467   -935    603   1369       C
ATOM     39  C   GLU H   6      73.621 204.066  27.054  1.00 47.83           C
ANISOU   39  C   GLU H   6    10189   4592   3393   -903    526   1556       C
ATOM     40  O   GLU H   6      74.360 205.032  27.271  1.00 50.13           O
ANISOU   40  O   GLU H   6    10714   4620   3712  -1176    612   1631       O
ATOM     41  CB  GLU H   6      72.987 202.118  28.545  1.00 36.89           C
ANISOU   41  CB  GLU H   6     7955   3684   2378   -600    377   1232       C
ATOM     42  CG  GLU H   6      73.265 202.439  29.996  1.00 42.93           C
ANISOU   42  CG  GLU H   6     8604   4349   3359   -645    314   1138       C
ATOM     43  CD  GLU H   6      72.302 201.730  30.923  1.00 55.51           C
ANISOU   43  CD  GLU H   6     9935   6092   5066   -342    163   1009       C
ATOM     44  OE1 GLU H   6      71.104 201.638  30.570  1.00 54.99           O
ANISOU   44  OE1 GLU H   6     9921   6064   4909    -40     39   1022       O
ATOM     45  OE2 GLU H   6      72.746 201.246  31.989  1.00 36.10           O
ANISOU   45  OE2 GLU H   6     7216   3717   2784   -414    167    895       O
ATOM     46  N   SER H   7      72.483 204.151  26.334  1.00 45.53           N
ANISOU   46  N   SER H   7    10148   4272   2879   -575    348   1630       N
ATOM     47  CA  SER H   7      71.913 205.372  25.756  1.00 48.52           C
ANISOU   47  CA  SER H   7    11124   4300   3012   -436    206   1812       C
ATOM     48  C   SER H   7      70.474 205.091  25.291  1.00 51.19           C
ANISOU   48  C   SER H   7    11507   4725   3219     40    -89   1797       C
ATOM     49  O   SER H   7      69.998 203.956  25.392  1.00 48.28           O
ANISOU   49  O   SER H   7    10704   4682   2959    195   -148   1649       O
ATOM     50  CB  SER H   7      72.759 205.851  24.575  1.00 57.09           C
ANISOU   50  CB  SER H   7    12624   5240   3828   -770    442   2013       C
ATOM     51  OG  SER H   7      72.855 204.859  23.565  1.00 67.71           O
ANISOU   51  OG  SER H   7    13856   6875   4995   -777    559   2007       O
ATOM     52  N   GLY H   8      69.805 206.124  24.789  1.00 50.22           N
ANISOU   52  N   GLY H   8    11908   4296   2878    261   -288   1945       N
ATOM     53  CA  GLY H   8      68.444 206.016  24.283  1.00 50.51           C
ANISOU   53  CA  GLY H   8    12011   4389   2793    731   -617   1934       C
ATOM     54  C   GLY H   8      67.405 206.675  25.160  1.00 53.62           C
ANISOU   54  C   GLY H   8    12398   4631   3344   1135   -886   1853       C
ATOM     55  O   GLY H   8      66.258 206.853  24.734  1.00 54.14           O
ANISOU   55  O   GLY H   8    12559   4687   3323   1557  -1191   1850       O
ATOM     56  N   GLY H   9      67.804 207.016  26.387  1.00 48.64           N
ANISOU   56  N   GLY H   9    11639   3896   2945   1022   -781   1767       N
ATOM     57  CA  GLY H   9      66.941 207.675  27.356  1.00 48.71           C
ANISOU   57  CA  GLY H   9    11652   3753   3102   1386   -972   1662       C
ATOM     58  C   GLY H   9      66.498 209.049  26.899  1.00 57.46           C
ANISOU   58  C   GLY H   9    13407   4410   4016   1632  -1188   1811       C
ATOM     59  O   GLY H   9      67.162 209.685  26.073  1.00 59.40           O
ANISOU   59  O   GLY H   9    14171   4374   4024   1392  -1126   2023       O
ATOM     60  N   GLY H  10      65.361 209.490  27.414  1.00 55.09           N
ANISOU   60  N   GLY H  10    13085   4037   3811   2120  -1431   1701       N
ATOM     61  CA  GLY H  10      64.816 210.792  27.069  1.00 58.97           C
ANISOU   61  CA  GLY H  10    14183   4079   4145   2451  -1686   1813       C
ATOM     62  C   GLY H  10      63.416 211.040  27.577  1.00 63.22           C
ANISOU   62  C   GLY H  10    14542   4654   4826   3073  -1963   1641       C
ATOM     63  O   GLY H  10      62.823 210.188  28.248  1.00 59.50           O
ANISOU   63  O   GLY H  10    13445   4574   4588   3220  -1924   1429       O
ATOM     64  N   LEU H  11      62.893 212.235  27.264  1.00 64.35           N
ANISOU   64  N   LEU H  11    15247   4370   4833   3441  -2234   1731       N
ATOM     65  CA  LEU H  11      61.555 212.655  27.640  1.00 66.78           C
ANISOU   65  CA  LEU H  11    15438   4663   5271   4096  -2523   1566       C
ATOM     66  C   LEU H  11      60.576 212.195  26.561  1.00 73.84           C
ANISOU   66  C   LEU H  11    16182   5794   6080   4457  -2841   1588       C
ATOM     67  O   LEU H  11      60.822 212.407  25.369  1.00 76.38           O
ANISOU   67  O   LEU H  11    16985   5936   6101   4390  -2990   1816       O
ATOM     68  CB  LEU H  11      61.520 214.183  27.828  1.00 71.34           C
ANISOU   68  CB  LEU H  11    16728   4625   5753   4343  -2686   1636       C
ATOM     69  CG  LEU H  11      60.240 214.786  28.401  1.00 78.74           C
ANISOU   69  CG  LEU H  11    17577   5490   6853   5055  -2951   1429       C
ATOM     70  CD1 LEU H  11      60.133 214.539  29.890  1.00 75.64           C
ANISOU   70  CD1 LEU H  11    16708   5293   6738   5082  -2708   1148       C
ATOM     71  CD2 LEU H  11      60.164 216.279  28.103  1.00 87.16           C
ANISOU   71  CD2 LEU H  11    19494   5887   7736   5352  -3217   1566       C
ATOM     72  N   VAL H  12      59.494 211.519  26.979  1.00 69.98           N
ANISOU   72  N   VAL H  12    15016   5723   5850   4807  -2935   1348       N
ATOM     73  CA  VAL H  12      58.476 210.986  26.075  1.00 71.95           C
ANISOU   73  CA  VAL H  12    14989   6258   6089   5152  -3268   1309       C
ATOM     74  C   VAL H  12      57.047 211.231  26.619  1.00 79.56           C
ANISOU   74  C   VAL H  12    15541   7357   7332   5804  -3515   1060       C
ATOM     75  O   VAL H  12      56.872 211.511  27.809  1.00 79.02           O
ANISOU   75  O   VAL H  12    15261   7279   7483   5923  -3327    886       O
ATOM     76  CB  VAL H  12      58.770 209.496  25.734  1.00 71.51           C
ANISOU   76  CB  VAL H  12    14403   6692   6074   4751  -3094   1273       C
ATOM     77  CG1 VAL H  12      58.309 208.556  26.846  1.00 68.10           C
ANISOU   77  CG1 VAL H  12    13161   6699   6015   4744  -2888   1006       C
ATOM     78  CG2 VAL H  12      58.178 209.096  24.387  1.00 73.67           C
ANISOU   78  CG2 VAL H  12    14718   7111   6163   4929  -3453   1337       C
ATOM     79  N   GLN H  13      56.044 211.141  25.734  1.00 80.09           N
ANISOU   79  N   GLN H  13    15499   7554   7379   6229  -3937   1034       N
ATOM     80  CA  GLN H  13      54.626 211.339  26.035  1.00 83.93           C
ANISOU   80  CA  GLN H  13    15533   8212   8145   6881  -4227    790       C
ATOM     81  C   GLN H  13      53.949 210.009  26.425  1.00 85.72           C
ANISOU   81  C   GLN H  13    14792   9068   8708   6804  -4102    544       C
ATOM     82  O   GLN H  13      54.423 208.951  25.995  1.00 81.41           O
ANISOU   82  O   GLN H  13    14049   8784   8101   6348  -3976    601       O
ATOM     83  CB  GLN H  13      53.918 211.947  24.805  1.00 91.09           C
ANISOU   83  CB  GLN H  13    16834   8923   8855   7381  -4813    892       C
ATOM     84  CG  GLN H  13      54.108 213.452  24.666  1.00112.94           C
ANISOU   84  CG  GLN H  13    20479  11041  11394   7697  -5014   1061       C
ATOM     85  CD  GLN H  13      53.072 214.217  25.450  1.00141.19           C
ANISOU   85  CD  GLN H  13    23848  14537  15260   8377  -5183    817       C
ATOM     86  OE1 GLN H  13      51.970 214.491  24.963  1.00142.90           O
ANISOU   86  OE1 GLN H  13    23939  14797  15558   9001  -5659    718       O
ATOM     87  NE2 GLN H  13      53.398 214.573  26.684  1.00132.12           N
ANISOU   87  NE2 GLN H  13    22656  13274  14270   8292  -4808    698       N
ATOM     88  N   PRO H  14      52.828 210.024  27.201  1.00 85.18           N
ANISOU   88  N   PRO H  14    14117   9248   8999   7241  -4130    265       N
ATOM     89  CA  PRO H  14      52.151 208.755  27.532  1.00 83.44           C
ANISOU   89  CA  PRO H  14    12986   9614   9104   7124  -4001     46       C
ATOM     90  C   PRO H  14      51.548 208.102  26.289  1.00 89.25           C
ANISOU   90  C   PRO H  14    13495  10597   9818   7211  -4434     46       C
ATOM     91  O   PRO H  14      50.827 208.752  25.525  1.00 93.86           O
ANISOU   91  O   PRO H  14    14269  11050  10344   7724  -4932     47       O
ATOM     92  CB  PRO H  14      51.075 209.168  28.550  1.00 88.54           C
ANISOU   92  CB  PRO H  14    13133  10405  10102   7624  -3935   -238       C
ATOM     93  CG  PRO H  14      51.435 210.556  28.973  1.00 94.97           C
ANISOU   93  CG  PRO H  14    14630  10693  10760   7905  -3929   -173       C
ATOM     94  CD  PRO H  14      52.118 211.171  27.800  1.00 91.50           C
ANISOU   94  CD  PRO H  14    15021   9813   9931   7853  -4257    126       C
ATOM     95  N   GLY H  15      51.905 206.838  26.078  1.00 81.89           N
ANISOU   95  N   GLY H  15    12225   9983   8905   6710  -4266     49       N
ATOM     96  CA  GLY H  15      51.492 206.062  24.914  1.00 83.16           C
ANISOU   96  CA  GLY H  15    12204  10379   9013   6683  -4641     40       C
ATOM     97  C   GLY H  15      52.522 206.112  23.801  1.00 85.25           C
ANISOU   97  C   GLY H  15    13215  10373   8805   6385  -4736    318       C
ATOM     98  O   GLY H  15      52.323 205.515  22.737  1.00 85.90           O
ANISOU   98  O   GLY H  15    13289  10600   8748   6334  -5042    332       O
ATOM     99  N   GLY H  16      53.621 206.827  24.060  1.00 79.25           N
ANISOU   99  N   GLY H  16    13094   9220   7796   6176  -4461    528       N
ATOM    100  CA  GLY H  16      54.728 207.005  23.130  1.00 77.80           C
ANISOU  100  CA  GLY H  16    13649   8748   7163   5848  -4439    807       C
ATOM    101  C   GLY H  16      55.722 205.862  23.130  1.00 75.97           C
ANISOU  101  C   GLY H  16    13264   8720   6880   5214  -4047    844       C
ATOM    102  O   GLY H  16      55.624 204.934  23.942  1.00 71.67           O
ANISOU  102  O   GLY H  16    12086   8501   6643   5001  -3778    671       O
ATOM    103  N   SER H  17      56.693 205.930  22.208  1.00 72.36           N
ANISOU  103  N   SER H  17    13410   8061   6022   4917  -4002   1072       N
ATOM    104  CA  SER H  17      57.717 204.902  22.050  1.00 67.56           C
ANISOU  104  CA  SER H  17    12726   7619   5326   4354  -3648   1110       C
ATOM    105  C   SER H  17      59.130 205.440  22.236  1.00 68.61           C
ANISOU  105  C   SER H  17    13378   7438   5251   3959  -3257   1320       C
ATOM    106  O   SER H  17      59.380 206.629  22.031  1.00 70.86           O
ANISOU  106  O   SER H  17    14272   7323   5329   4082  -3327   1499       O
ATOM    107  CB  SER H  17      57.582 204.219  20.692  1.00 72.78           C
ANISOU  107  CB  SER H  17    13513   8427   5713   4315  -3915   1134       C
ATOM    108  OG  SER H  17      56.317 203.589  20.564  1.00 83.56           O
ANISOU  108  OG  SER H  17    14317  10115   7318   4609  -4280    908       O
ATOM    109  N   LEU H  18      60.055 204.549  22.621  1.00 60.66           N
ANISOU  109  N   LEU H  18    12123   6608   4318   3481  -2859   1292       N
ATOM    110  CA  LEU H  18      61.470 204.850  22.849  1.00 58.58           C
ANISOU  110  CA  LEU H  18    12198   6132   3928   3045  -2462   1447       C
ATOM    111  C   LEU H  18      62.289 203.562  22.704  1.00 57.65           C
ANISOU  111  C   LEU H  18    11781   6298   3825   2611  -2170   1393       C
ATOM    112  O   LEU H  18      61.776 202.477  22.979  1.00 54.90           O
ANISOU  112  O   LEU H  18    10876   6280   3702   2623  -2198   1206       O
ATOM    113  CB  LEU H  18      61.655 205.439  24.270  1.00 57.32           C
ANISOU  113  CB  LEU H  18    11910   5833   4035   3037  -2258   1391       C
ATOM    114  CG  LEU H  18      62.847 206.375  24.491  1.00 62.71           C
ANISOU  114  CG  LEU H  18    13114   6136   4575   2742  -2014   1570       C
ATOM    115  CD1 LEU H  18      62.627 207.733  23.801  1.00 68.29           C
ANISOU  115  CD1 LEU H  18    14537   6405   5003   2995  -2265   1765       C
ATOM    116  CD2 LEU H  18      63.074 206.608  25.961  1.00 62.64           C
ANISOU  116  CD2 LEU H  18    12873   6080   4848   2681  -1812   1454       C
ATOM    117  N   ARG H  19      63.554 203.676  22.280  1.00 53.33           N
ANISOU  117  N   ARG H  19    11594   5617   3053   2228  -1884   1548       N
ATOM    118  CA  ARG H  19      64.433 202.517  22.151  1.00 49.78           C
ANISOU  118  CA  ARG H  19    10876   5415   2624   1845  -1588   1484       C
ATOM    119  C   ARG H  19      65.737 202.746  22.899  1.00 51.85           C
ANISOU  119  C   ARG H  19    11148   5566   2987   1457  -1190   1537       C
ATOM    120  O   ARG H  19      66.458 203.703  22.609  1.00 54.06           O
ANISOU  120  O   ARG H  19    11911   5558   3071   1291  -1063   1720       O
ATOM    121  CB  ARG H  19      64.702 202.169  20.678  1.00 51.26           C
ANISOU  121  CB  ARG H  19    11409   5645   2422   1760  -1626   1570       C
ATOM    122  CG  ARG H  19      65.260 200.760  20.488  1.00 61.27           C
ANISOU  122  CG  ARG H  19    12310   7223   3747   1493  -1410   1428       C
ATOM    123  CD  ARG H  19      65.798 200.518  19.089  1.00 78.22           C
ANISOU  123  CD  ARG H  19    14869   9383   5467   1354  -1336   1514       C
ATOM    124  NE  ARG H  19      67.125 201.108  18.905  1.00 91.54           N
ANISOU  124  NE  ARG H  19    16910  10894   6978   1005   -935   1688       N
ATOM    125  CZ  ARG H  19      67.949 200.804  17.906  1.00109.24           C
ANISOU  125  CZ  ARG H  19    19430  13181   8895    773   -688   1749       C
ATOM    126  NH1 ARG H  19      67.599 199.898  17.000  1.00 97.53           N
ANISOU  126  NH1 ARG H  19    17957  11899   7201    869   -819   1641       N
ATOM    127  NH2 ARG H  19      69.133 201.393  17.813  1.00 98.95           N
ANISOU  127  NH2 ARG H  19    18388  11729   7480    431   -295   1901       N
ATOM    128  N   LEU H  20      66.042 201.865  23.853  1.00 44.56           N
ANISOU  128  N   LEU H  20     9703   4859   2369   1302  -1010   1379       N
ATOM    129  CA  LEU H  20      67.277 201.946  24.631  1.00 42.43           C
ANISOU  129  CA  LEU H  20     9366   4527   2230    949   -683   1393       C
ATOM    130  C   LEU H  20      68.337 201.058  24.014  1.00 47.07           C
ANISOU  130  C   LEU H  20     9863   5285   2737    619   -422   1383       C
ATOM    131  O   LEU H  20      68.023 199.990  23.485  1.00 45.92           O
ANISOU  131  O   LEU H  20     9507   5380   2562    670   -476   1282       O
ATOM    132  CB  LEU H  20      67.057 201.532  26.098  1.00 38.88           C
ANISOU  132  CB  LEU H  20     8449   4193   2130    986   -647   1232       C
ATOM    133  CG  LEU H  20      66.011 202.292  26.906  1.00 43.65           C
ANISOU  133  CG  LEU H  20     9055   4675   2855   1322   -840   1190       C
ATOM    134  CD1 LEU H  20      65.917 201.741  28.310  1.00 40.61           C
ANISOU  134  CD1 LEU H  20     8239   4432   2758   1303   -734   1036       C
ATOM    135  CD2 LEU H  20      66.306 203.783  26.950  1.00 48.29           C
ANISOU  135  CD2 LEU H  20    10164   4871   3312   1343   -863   1334       C
ATOM    136  N   SER H  21      69.593 201.498  24.093  1.00 44.86           N
ANISOU  136  N   SER H  21     9726   4880   2437    281   -140   1468       N
ATOM    137  CA  SER H  21      70.745 200.762  23.589  1.00 44.45           C
ANISOU  137  CA  SER H  21     9553   4991   2344    -38    161   1442       C
ATOM    138  C   SER H  21      71.711 200.547  24.728  1.00 46.32           C
ANISOU  138  C   SER H  21     9437   5270   2892   -283    358   1352       C
ATOM    139  O   SER H  21      71.703 201.315  25.686  1.00 44.80           O
ANISOU  139  O   SER H  21     9279   4897   2846   -284    302   1370       O
ATOM    140  CB  SER H  21      71.423 201.538  22.468  1.00 51.51           C
ANISOU  140  CB  SER H  21    10959   5713   2899   -245    342   1637       C
ATOM    141  OG  SER H  21      70.587 201.520  21.325  1.00 67.24           O
ANISOU  141  OG  SER H  21    13284   7704   4562     -7    138   1704       O
ATOM    142  N   CYS H  22      72.528 199.497  24.639  1.00 42.64           N
ANISOU  142  N   CYS H  22     8644   5035   2522   -462    560   1240       N
ATOM    143  CA  CYS H  22      73.545 199.195  25.633  1.00 41.36           C
ANISOU  143  CA  CYS H  22     8131   4935   2651   -683    719   1143       C
ATOM    144  C   CYS H  22      74.733 198.520  24.932  1.00 45.13           C
ANISOU  144  C   CYS H  22     8452   5591   3104   -928   1019   1091       C
ATOM    145  O   CYS H  22      74.677 197.332  24.619  1.00 44.39           O
ANISOU  145  O   CYS H  22     8126   5716   3022   -834   1032    963       O
ATOM    146  CB  CYS H  22      72.974 198.345  26.770  1.00 39.20           C
ANISOU  146  CB  CYS H  22     7468   4789   2637   -499    549    990       C
ATOM    147  SG  CYS H  22      74.212 197.750  27.951  1.00 42.06           S
ANISOU  147  SG  CYS H  22     7410   5244   3324   -716    675    858       S
ATOM    148  N   SER H  23      75.770 199.315  24.612  1.00 42.65           N
ANISOU  148  N   SER H  23     8291   5171   2742  -1244   1274   1187       N
ATOM    149  CA  SER H  23      76.985 198.848  23.946  1.00 43.47           C
ANISOU  149  CA  SER H  23     8230   5450   2836  -1504   1623   1136       C
ATOM    150  C   SER H  23      77.910 198.151  24.941  1.00 43.08           C
ANISOU  150  C   SER H  23     7635   5563   3172  -1609   1682    952       C
ATOM    151  O   SER H  23      78.110 198.648  26.049  1.00 41.55           O
ANISOU  151  O   SER H  23     7331   5251   3206  -1680   1562    941       O
ATOM    152  CB  SER H  23      77.708 200.014  23.280  1.00 52.57           C
ANISOU  152  CB  SER H  23     9743   6423   3809  -1836   1892   1318       C
ATOM    153  OG  SER H  23      78.714 199.546  22.395  1.00 66.57           O
ANISOU  153  OG  SER H  23    11402   8395   5496  -2056   2277   1275       O
ATOM    154  N   ALA H  24      78.465 196.998  24.546  1.00 38.35           N
ANISOU  154  N   ALA H  24     6720   5220   2632  -1594   1841    797       N
ATOM    155  CA  ALA H  24      79.339 196.178  25.391  1.00 36.44           C
ANISOU  155  CA  ALA H  24     5958   5141   2746  -1629   1862    607       C
ATOM    156  C   ALA H  24      80.769 196.101  24.865  1.00 43.40           C
ANISOU  156  C   ALA H  24     6591   6180   3718  -1906   2237    533       C
ATOM    157  O   ALA H  24      80.983 196.038  23.654  1.00 45.79           O
ANISOU  157  O   ALA H  24     7056   6571   3773  -1978   2521    561       O
ATOM    158  CB  ALA H  24      78.766 194.781  25.517  1.00 34.24           C
ANISOU  158  CB  ALA H  24     5476   5013   2520  -1330   1695    455       C
ATOM    159  N   SER H  25      81.747 196.075  25.787  1.00 39.72           N
ANISOU  159  N   SER H  25     5716   5768   3609  -2051   2236    422       N
ATOM    160  CA  SER H  25      83.176 195.993  25.461  1.00 41.92           C
ANISOU  160  CA  SER H  25     5629   6228   4069  -2316   2575    313       C
ATOM    161  C   SER H  25      83.971 195.337  26.594  1.00 42.54           C
ANISOU  161  C   SER H  25     5157   6431   4575  -2267   2411    108       C
ATOM    162  O   SER H  25      83.571 195.407  27.756  1.00 38.64           O
ANISOU  162  O   SER H  25     4653   5811   4218  -2154   2061    106       O
ATOM    163  CB  SER H  25      83.740 197.380  25.153  1.00 48.48           C
ANISOU  163  CB  SER H  25     6661   6911   4847  -2733   2811    474       C
ATOM    164  OG  SER H  25      83.509 198.293  26.216  1.00 56.71           O
ANISOU  164  OG  SER H  25     7820   7706   6023  -2822   2531    553       O
ATOM    165  N   GLY H  26      85.088 194.713  26.234  1.00 40.97           N
ANISOU  165  N   GLY H  26     4522   6479   4566  -2335   2667    -68       N
ATOM    166  CA  GLY H  26      85.990 194.063  27.178  1.00 40.83           C
ANISOU  166  CA  GLY H  26     3949   6600   4964  -2270   2514   -282       C
ATOM    167  C   GLY H  26      85.702 192.599  27.433  1.00 41.42           C
ANISOU  167  C   GLY H  26     3853   6777   5107  -1861   2314   -444       C
ATOM    168  O   GLY H  26      86.375 191.979  28.263  1.00 41.16           O
ANISOU  168  O   GLY H  26     3408   6832   5399  -1746   2131   -615       O
ATOM    169  N   PHE H  27      84.703 192.029  26.722  1.00 35.22           N
ANISOU  169  N   PHE H  27     3401   5963   4017  -1639   2321   -397       N
ATOM    170  CA  PHE H  27      84.309 190.626  26.874  1.00 33.21           C
ANISOU  170  CA  PHE H  27     3064   5755   3798  -1277   2134   -538       C
ATOM    171  C   PHE H  27      83.579 190.094  25.644  1.00 37.44           C
ANISOU  171  C   PHE H  27     3909   6322   3995  -1137   2287   -533       C
ATOM    172  O   PHE H  27      83.062 190.883  24.845  1.00 37.42           O
ANISOU  172  O   PHE H  27     4278   6259   3683  -1274   2431   -372       O
ATOM    173  CB  PHE H  27      83.428 190.443  28.133  1.00 31.53           C
ANISOU  173  CB  PHE H  27     2977   5357   3647  -1110   1695   -471       C
ATOM    174  CG  PHE H  27      82.081 191.137  28.090  1.00 30.67           C
ANISOU  174  CG  PHE H  27     3334   5065   3255  -1119   1580   -263       C
ATOM    175  CD1 PHE H  27      81.948 192.459  28.489  1.00 33.63           C
ANISOU  175  CD1 PHE H  27     3893   5296   3586  -1330   1550   -106       C
ATOM    176  CD2 PHE H  27      80.942 190.458  27.669  1.00 30.76           C
ANISOU  176  CD2 PHE H  27     3583   5039   3064   -906   1480   -244       C
ATOM    177  CE1 PHE H  27      80.701 193.091  28.464  1.00 32.59           C
ANISOU  177  CE1 PHE H  27     4170   4996   3215  -1283   1429     63       C
ATOM    178  CE2 PHE H  27      79.700 191.095  27.633  1.00 31.47           C
ANISOU  178  CE2 PHE H  27     4037   4988   2933   -888   1356    -77       C
ATOM    179  CZ  PHE H  27      79.584 192.399  28.050  1.00 29.50           C
ANISOU  179  CZ  PHE H  27     3957   4605   2648  -1052   1329     73       C
ATOM    180  N   THR H  28      83.494 188.746  25.522  1.00 33.73           N
ANISOU  180  N   THR H  28     3327   5916   3572   -850   2208   -710       N
ATOM    181  CA  THR H  28      82.747 188.073  24.461  1.00 33.20           C
ANISOU  181  CA  THR H  28     3553   5858   3203   -689   2272   -749       C
ATOM    182  C   THR H  28      81.268 188.235  24.837  1.00 34.06           C
ANISOU  182  C   THR H  28     4018   5772   3151   -619   1944   -583       C
ATOM    183  O   THR H  28      80.818 187.667  25.835  1.00 31.18           O
ANISOU  183  O   THR H  28     3581   5307   2958   -478   1640   -597       O
ATOM    184  CB  THR H  28      83.188 186.594  24.332  1.00 41.16           C
ANISOU  184  CB  THR H  28     4326   6953   4358   -412   2262  -1010       C
ATOM    185  OG1 THR H  28      84.613 186.525  24.241  1.00 44.03           O
ANISOU  185  OG1 THR H  28     4256   7510   4963   -453   2526  -1179       O
ATOM    186  CG2 THR H  28      82.566 185.897  23.127  1.00 38.50           C
ANISOU  186  CG2 THR H  28     4294   6633   3699   -268   2360  -1095       C
ATOM    187  N   PHE H  29      80.552 189.090  24.090  1.00 31.51           N
ANISOU  187  N   PHE H  29     4071   5395   2506   -726   2013   -418       N
ATOM    188  CA  PHE H  29      79.153 189.454  24.326  1.00 28.98           C
ANISOU  188  CA  PHE H  29     4062   4916   2033   -664   1731   -261       C
ATOM    189  C   PHE H  29      78.195 188.251  24.389  1.00 30.92           C
ANISOU  189  C   PHE H  29     4345   5126   2275   -428   1475   -360       C
ATOM    190  O   PHE H  29      77.375 188.177  25.305  1.00 27.82           O
ANISOU  190  O   PHE H  29     3950   4625   1994   -363   1206   -297       O
ATOM    191  CB  PHE H  29      78.690 190.493  23.281  1.00 32.72           C
ANISOU  191  CB  PHE H  29     4944   5349   2140   -778   1857    -94       C
ATOM    192  CG  PHE H  29      77.327 191.101  23.514  1.00 32.61           C
ANISOU  192  CG  PHE H  29     5221   5177   1993   -702   1568     69       C
ATOM    193  CD1 PHE H  29      77.054 191.815  24.678  1.00 33.84           C
ANISOU  193  CD1 PHE H  29     5326   5204   2329   -738   1392    175       C
ATOM    194  CD2 PHE H  29      76.332 191.005  22.549  1.00 35.55           C
ANISOU  194  CD2 PHE H  29     5919   5536   2053   -583   1465    100       C
ATOM    195  CE1 PHE H  29      75.795 192.389  24.887  1.00 33.82           C
ANISOU  195  CE1 PHE H  29     5559   5072   2218   -633   1149    301       C
ATOM    196  CE2 PHE H  29      75.072 191.579  22.758  1.00 37.43           C
ANISOU  196  CE2 PHE H  29     6368   5650   2205   -483   1182    228       C
ATOM    197  CZ  PHE H  29      74.812 192.266  23.925  1.00 33.93           C
ANISOU  197  CZ  PHE H  29     5840   5091   1963   -500   1044    325       C
ATOM    198  N   SER H  30      78.342 187.296  23.454  1.00 29.38           N
ANISOU  198  N   SER H  30     4184   5018   1961   -316   1575   -526       N
ATOM    199  CA  SER H  30      77.519 186.084  23.345  1.00 28.20           C
ANISOU  199  CA  SER H  30     4097   4818   1802   -128   1350   -647       C
ATOM    200  C   SER H  30      77.582 185.156  24.578  1.00 30.32           C
ANISOU  200  C   SER H  30     4111   5002   2407    -24   1143   -724       C
ATOM    201  O   SER H  30      76.688 184.329  24.755  1.00 29.89           O
ANISOU  201  O   SER H  30     4131   4852   2373     73    918   -765       O
ATOM    202  CB  SER H  30      77.896 185.311  22.086  1.00 34.55           C
ANISOU  202  CB  SER H  30     5004   5719   2405    -38   1533   -839       C
ATOM    203  OG  SER H  30      79.260 184.922  22.093  1.00 45.81           O
ANISOU  203  OG  SER H  30     6147   7257   3999    -14   1791   -997       O
ATOM    204  N   THR H  31      78.635 185.277  25.413  1.00 25.57           N
ANISOU  204  N   THR H  31     3226   4428   2062    -54   1207   -743       N
ATOM    205  CA  THR H  31      78.809 184.431  26.601  1.00 23.96           C
ANISOU  205  CA  THR H  31     2830   4130   2144     62    996   -801       C
ATOM    206  C   THR H  31      78.074 184.999  27.825  1.00 25.56           C
ANISOU  206  C   THR H  31     3078   4213   2421     -4    776   -619       C
ATOM    207  O   THR H  31      78.015 184.341  28.871  1.00 24.31           O
ANISOU  207  O   THR H  31     2846   3951   2440     77    584   -628       O
ATOM    208  CB  THR H  31      80.311 184.178  26.895  1.00 30.92           C
ANISOU  208  CB  THR H  31     3372   5106   3269    110   1118   -943       C
ATOM    209  OG1 THR H  31      80.951 185.399  27.284  1.00 30.55           O
ANISOU  209  OG1 THR H  31     3186   5128   3293    -81   1221   -838       O
ATOM    210  CG2 THR H  31      81.041 183.544  25.730  1.00 28.19           C
ANISOU  210  CG2 THR H  31     2955   4894   2861    210   1374  -1154       C
ATOM    211  N   TYR H  32      77.507 186.208  27.690  1.00 20.71           N
ANISOU  211  N   TYR H  32     2620   3598   1650   -136    807   -457       N
ATOM    212  CA  TYR H  32      76.814 186.897  28.770  1.00 18.14           C
ANISOU  212  CA  TYR H  32     2356   3172   1366   -183    642   -302       C
ATOM    213  C   TYR H  32      75.316 186.967  28.556  1.00 22.25           C
ANISOU  213  C   TYR H  32     3079   3639   1735   -146    516   -220       C
ATOM    214  O   TYR H  32      74.859 187.343  27.479  1.00 23.02           O
ANISOU  214  O   TYR H  32     3341   3781   1626   -155    572   -200       O
ATOM    215  CB  TYR H  32      77.345 188.338  28.895  1.00 19.19           C
ANISOU  215  CB  TYR H  32     2506   3315   1469   -346    756   -192       C
ATOM    216  CG  TYR H  32      78.608 188.520  29.711  1.00 21.09           C
ANISOU  216  CG  TYR H  32     2500   3575   1938   -418    772   -241       C
ATOM    217  CD1 TYR H  32      79.722 187.709  29.501  1.00 24.27           C
ANISOU  217  CD1 TYR H  32     2639   4081   2502   -365    857   -407       C
ATOM    218  CD2 TYR H  32      78.741 189.589  30.592  1.00 21.42           C
ANISOU  218  CD2 TYR H  32     2570   3539   2032   -537    703   -140       C
ATOM    219  CE1 TYR H  32      80.906 187.906  30.211  1.00 24.87           C
ANISOU  219  CE1 TYR H  32     2436   4197   2814   -423    839   -472       C
ATOM    220  CE2 TYR H  32      79.931 189.817  31.282  1.00 23.43           C
ANISOU  220  CE2 TYR H  32     2587   3817   2498   -626    684   -203       C
ATOM    221  CZ  TYR H  32      81.009 188.967  31.095  1.00 31.60           C
ANISOU  221  CZ  TYR H  32     3315   4974   3718   -569    741   -368       C
ATOM    222  OH  TYR H  32      82.180 189.180  31.785  1.00 34.94           O
ANISOU  222  OH  TYR H  32     3453   5440   4382   -642    680   -450       O
ATOM    223  N   SER H  33      74.549 186.686  29.608  1.00 18.93           N
ANISOU  223  N   SER H  33     2650   3131   1412   -109    348   -167       N
ATOM    224  CA  SER H  33      73.105 186.894  29.601  1.00 17.48           C
ANISOU  224  CA  SER H  33     2581   2921   1141    -85    237    -91       C
ATOM    225  C   SER H  33      72.949 188.382  29.942  1.00 20.58           C
ANISOU  225  C   SER H  33     3068   3291   1461   -128    261     44       C
ATOM    226  O   SER H  33      73.747 188.917  30.716  1.00 19.73           O
ANISOU  226  O   SER H  33     2918   3144   1435   -185    296     78       O
ATOM    227  CB  SER H  33      72.425 186.035  30.660  1.00 19.41           C
ANISOU  227  CB  SER H  33     2766   3087   1524    -57    110    -89       C
ATOM    228  OG  SER H  33      72.847 186.386  31.968  1.00 27.96           O
ANISOU  228  OG  SER H  33     3815   4107   2701    -74     95    -23       O
ATOM    229  N   MET H  34      72.000 189.060  29.303  1.00 17.58           N
ANISOU  229  N   MET H  34     2830   2923    927    -91    222    106       N
ATOM    230  CA  MET H  34      71.781 190.490  29.503  1.00 17.16           C
ANISOU  230  CA  MET H  34     2915   2803    801    -96    225    226       C
ATOM    231  C   MET H  34      70.411 190.719  30.123  1.00 20.18           C
ANISOU  231  C   MET H  34     3299   3168   1199     16     93    269       C
ATOM    232  O   MET H  34      69.449 190.023  29.792  1.00 20.58           O
ANISOU  232  O   MET H  34     3277   3280   1261     82     -3    219       O
ATOM    233  CB  MET H  34      71.934 191.264  28.186  1.00 21.16           C
ANISOU  233  CB  MET H  34     3645   3324   1072   -118    295    280       C
ATOM    234  CG  MET H  34      73.319 191.153  27.538  1.00 26.20           C
ANISOU  234  CG  MET H  34     4275   4008   1671   -255    502    241       C
ATOM    235  SD  MET H  34      74.716 191.777  28.515  1.00 30.54           S
ANISOU  235  SD  MET H  34     4695   4505   2403   -426    627    261       S
ATOM    236  CE  MET H  34      74.182 193.473  28.818  1.00 27.66           C
ANISOU  236  CE  MET H  34     4613   3968   1927   -456    574    431       C
ATOM    237  N   HIS H  35      70.336 191.671  31.051  1.00 16.31           N
ANISOU  237  N   HIS H  35     2816   2545    835     32     87    313       N
ATOM    238  CA  HIS H  35      69.143 191.964  31.839  1.00 15.87           C
ANISOU  238  CA  HIS H  35     2715   2462    854    152     21    322       C
ATOM    239  C   HIS H  35      68.877 193.466  31.928  1.00 20.70           C
ANISOU  239  C   HIS H  35     3602   3031   1233    237      0    442       C
ATOM    240  O   HIS H  35      69.809 194.271  31.826  1.00 21.39           O
ANISOU  240  O   HIS H  35     3855   3014   1260    142     56    493       O
ATOM    241  CB  HIS H  35      69.309 191.388  33.273  1.00 14.98           C
ANISOU  241  CB  HIS H  35     2486   2322    883    114     48    296       C
ATOM    242  CG  HIS H  35      69.983 190.044  33.320  1.00 16.20           C
ANISOU  242  CG  HIS H  35     2595   2577    982     24     64    279       C
ATOM    243  ND1 HIS H  35      69.259 188.882  33.484  1.00 17.26           N
ANISOU  243  ND1 HIS H  35     2610   2752   1196     26     35    238       N
ATOM    244  CD2 HIS H  35      71.293 189.727  33.208  1.00 16.52           C
ANISOU  244  CD2 HIS H  35     2613   2601   1061    -58     98    243       C
ATOM    245  CE1 HIS H  35      70.141 187.902  33.463  1.00 15.81           C
ANISOU  245  CE1 HIS H  35     2385   2544   1077    -33     35    185       C
ATOM    246  NE2 HIS H  35      71.379 188.362  33.299  1.00 15.93           N
ANISOU  246  NE2 HIS H  35     2432   2542   1078    -66     71    178       N
ATOM    247  N   TRP H  36      67.608 193.841  32.133  1.00 17.43           N
ANISOU  247  N   TRP H  36     3168   2634    822    414    -79    443       N
ATOM    248  CA  TRP H  36      67.244 195.234  32.349  1.00 18.75           C
ANISOU  248  CA  TRP H  36     3539   2672    914    552   -117    498       C
ATOM    249  C   TRP H  36      66.651 195.361  33.734  1.00 21.73           C
ANISOU  249  C   TRP H  36     3831   3045   1382    646    -75    458       C
ATOM    250  O   TRP H  36      65.772 194.579  34.112  1.00 20.26           O
ANISOU  250  O   TRP H  36     3409   2995   1295    699    -59    401       O
ATOM    251  CB  TRP H  36      66.287 195.774  31.271  1.00 19.39           C
ANISOU  251  CB  TRP H  36     3712   2763    895    745   -263    523       C
ATOM    252  CG  TRP H  36      66.933 196.041  29.943  1.00 21.13           C
ANISOU  252  CG  TRP H  36     4163   2929    935    665   -286    594       C
ATOM    253  CD1 TRP H  36      66.834 195.274  28.820  1.00 24.59           C
ANISOU  253  CD1 TRP H  36     4560   3487   1298    638   -342    565       C
ATOM    254  CD2 TRP H  36      67.717 197.188  29.577  1.00 22.27           C
ANISOU  254  CD2 TRP H  36     4654   2877    929    593   -241    705       C
ATOM    255  NE1 TRP H  36      67.531 195.851  27.784  1.00 25.48           N
ANISOU  255  NE1 TRP H  36     4979   3507   1195    564   -309    655       N
ATOM    256  CE2 TRP H  36      68.075 197.034  28.215  1.00 27.39           C
ANISOU  256  CE2 TRP H  36     5458   3553   1396    519   -238    753       C
ATOM    257  CE3 TRP H  36      68.137 198.349  30.261  1.00 23.99           C
ANISOU  257  CE3 TRP H  36     5096   2882   1137    569   -202    766       C
ATOM    258  CZ2 TRP H  36      68.852 197.980  27.530  1.00 27.96           C
ANISOU  258  CZ2 TRP H  36     5892   3455   1277    398   -158    881       C
ATOM    259  CZ3 TRP H  36      68.916 199.279  29.583  1.00 26.94           C
ANISOU  259  CZ3 TRP H  36     5816   3066   1352    437   -152    885       C
ATOM    260  CH2 TRP H  36      69.261 199.093  28.234  1.00 28.76           C
ANISOU  260  CH2 TRP H  36     6188   3337   1403    344   -114    952       C
ATOM    261  N   VAL H  37      67.209 196.292  34.523  1.00 18.95           N
ANISOU  261  N   VAL H  37     3680   2530    990    633    -38    480       N
ATOM    262  CA  VAL H  37      66.790 196.610  35.891  1.00 18.17           C
ANISOU  262  CA  VAL H  37     3596   2392    914    731     16    434       C
ATOM    263  C   VAL H  37      66.427 198.105  35.890  1.00 24.08           C
ANISOU  263  C   VAL H  37     4611   2960   1577    919    -42    448       C
ATOM    264  O   VAL H  37      67.146 198.903  35.289  1.00 24.52           O
ANISOU  264  O   VAL H  37     4916   2846   1556    840    -95    514       O
ATOM    265  CB  VAL H  37      67.911 196.274  36.922  1.00 20.45           C
ANISOU  265  CB  VAL H  37     3930   2623   1216    544     68    421       C
ATOM    266  CG1 VAL H  37      67.529 196.704  38.341  1.00 20.90           C
ANISOU  266  CG1 VAL H  37     4093   2618   1230    650    119    370       C
ATOM    267  CG2 VAL H  37      68.258 194.788  36.897  1.00 18.65           C
ANISOU  267  CG2 VAL H  37     3477   2536   1074    402     98    408       C
ATOM    268  N   ARG H  38      65.300 198.476  36.505  1.00 21.44           N
ANISOU  268  N   ARG H  38     4231   2654   1261   1168    -22    385       N
ATOM    269  CA  ARG H  38      64.893 199.880  36.562  1.00 22.58           C
ANISOU  269  CA  ARG H  38     4644   2602   1332   1403    -91    375       C
ATOM    270  C   ARG H  38      64.671 200.385  37.990  1.00 26.67           C
ANISOU  270  C   ARG H  38     5270   3042   1823   1523      8    282       C
ATOM    271  O   ARG H  38      64.403 199.595  38.891  1.00 24.38           O
ANISOU  271  O   ARG H  38     4786   2909   1568   1490    146    224       O
ATOM    272  CB  ARG H  38      63.668 200.148  35.664  1.00 23.28           C
ANISOU  272  CB  ARG H  38     4629   2766   1449   1692   -210    366       C
ATOM    273  CG  ARG H  38      62.349 199.583  36.174  1.00 26.26           C
ANISOU  273  CG  ARG H  38     4628   3390   1961   1888   -135    253       C
ATOM    274  CD  ARG H  38      61.228 199.882  35.205  1.00 27.17           C
ANISOU  274  CD  ARG H  38     4608   3586   2131   2174   -314    228       C
ATOM    275  NE  ARG H  38      59.938 199.442  35.723  1.00 30.00           N
ANISOU  275  NE  ARG H  38     4548   4193   2659   2359   -229     97       N
ATOM    276  CZ  ARG H  38      58.806 199.436  35.025  1.00 39.18           C
ANISOU  276  CZ  ARG H  38     5440   5508   3939   2605   -385     31       C
ATOM    277  NH1 ARG H  38      58.795 199.847  33.761  1.00 22.04           N
ANISOU  277  NH1 ARG H  38     3433   3248   1693   2722   -666     95       N
ATOM    278  NH2 ARG H  38      57.678 199.021  35.584  1.00 26.91           N
ANISOU  278  NH2 ARG H  38     3450   4202   2574   2732   -265   -101       N
ATOM    279  N   GLN H  39      64.786 201.708  38.187  1.00 26.03           N
ANISOU  279  N   GLN H  39     5542   2694   1655   1658    -60    268       N
ATOM    280  CA  GLN H  39      64.537 202.353  39.473  1.00 27.50           C
ANISOU  280  CA  GLN H  39     5902   2768   1779   1818     17    153       C
ATOM    281  C   GLN H  39      63.697 203.609  39.289  1.00 36.10           C
ANISOU  281  C   GLN H  39     7205   3675   2836   2188    -66    100       C
ATOM    282  O   GLN H  39      64.191 204.624  38.780  1.00 38.03           O
ANISOU  282  O   GLN H  39     7813   3621   3013   2183   -210    162       O
ATOM    283  CB  GLN H  39      65.837 202.666  40.224  1.00 28.03           C
ANISOU  283  CB  GLN H  39     6256   2633   1762   1560     -3    149       C
ATOM    284  CG  GLN H  39      65.581 203.265  41.610  1.00 36.06           C
ANISOU  284  CG  GLN H  39     7488   3542   2672   1726     69      8       C
ATOM    285  CD  GLN H  39      66.821 203.398  42.443  1.00 49.80           C
ANISOU  285  CD  GLN H  39     9471   5121   4329   1465      9    -20       C
ATOM    286  OE1 GLN H  39      67.840 203.919  41.993  1.00 49.87           O
ANISOU  286  OE1 GLN H  39     9495   5203   4250   1456     91   -100       O
ATOM    287  NE2 GLN H  39      66.785 202.895  43.657  1.00 39.08           N
ANISOU  287  NE2 GLN H  39     8322   3536   2989   1243   -139     41       N
ATOM    288  N   ALA H  40      62.419 203.534  39.690  1.00 34.62           N
ANISOU  288  N   ALA H  40     6786   3661   2708   2512     31    -16       N
ATOM    289  CA  ALA H  40      61.490 204.656  39.619  1.00 38.06           C
ANISOU  289  CA  ALA H  40     7363   3957   3143   2946    -43   -106       C
ATOM    290  C   ALA H  40      61.853 205.684  40.713  1.00 44.84           C
ANISOU  290  C   ALA H  40     8655   4519   3865   3039     -3   -211       C
ATOM    291  O   ALA H  40      62.410 205.281  41.742  1.00 43.44           O
ANISOU  291  O   ALA H  40     8524   4373   3610   2832    134   -256       O
ATOM    292  CB  ALA H  40      60.069 204.154  39.812  1.00 40.39           C
ANISOU  292  CB  ALA H  40     7187   4580   3579   3237     85   -228       C
ATOM    293  N   PRO H  41      61.581 207.006  40.534  1.00 45.42           N
ANISOU  293  N   PRO H  41     9094   4275   3890   3348   -147   -257       N
ATOM    294  CA  PRO H  41      61.927 207.964  41.604  1.00 47.68           C
ANISOU  294  CA  PRO H  41     9826   4252   4039   3431   -121   -385       C
ATOM    295  C   PRO H  41      61.270 207.605  42.938  1.00 53.65           C
ANISOU  295  C   PRO H  41    10404   5226   4753   3604    147   -578       C
ATOM    296  O   PRO H  41      60.070 207.303  42.979  1.00 55.05           O
ANISOU  296  O   PRO H  41    10202   5680   5033   3912    288   -671       O
ATOM    297  CB  PRO H  41      61.435 209.311  41.058  1.00 52.97           C
ANISOU  297  CB  PRO H  41    10851   4578   4696   3821   -318   -412       C
ATOM    298  CG  PRO H  41      61.343 209.118  39.582  1.00 56.56           C
ANISOU  298  CG  PRO H  41    11183   5078   5228   3785   -500   -226       C
ATOM    299  CD  PRO H  41      60.941 207.692  39.391  1.00 49.39           C
ANISOU  299  CD  PRO H  41     9666   4656   4442   3655   -363   -204       C
ATOM    300  N   GLY H  42      62.091 207.548  43.990  1.00 49.34           N
ANISOU  300  N   GLY H  42    10104   4585   4057   3369    219   -629       N
ATOM    301  CA  GLY H  42      61.666 207.220  45.349  1.00 49.79           C
ANISOU  301  CA  GLY H  42    10115   4809   3993   3477    482   -795       C
ATOM    302  C   GLY H  42      61.389 205.751  45.612  1.00 50.18           C
ANISOU  302  C   GLY H  42     9687   5287   4094   3292    712   -740       C
ATOM    303  O   GLY H  42      60.991 205.395  46.719  1.00 51.69           O
ANISOU  303  O   GLY H  42     9842   5634   4162   3362    971   -852       O
ATOM    304  N   LYS H  43      61.592 204.886  44.605  1.00 42.86           N
ANISOU  304  N   LYS H  43     8426   4533   3327   3051    630   -568       N
ATOM    305  CA  LYS H  43      61.359 203.444  44.721  1.00 39.93           C
ANISOU  305  CA  LYS H  43     7623   4521   3027   2845    814   -502       C
ATOM    306  C   LYS H  43      62.705 202.685  44.703  1.00 39.89           C
ANISOU  306  C   LYS H  43     7702   4476   2978   2399    705   -363       C
ATOM    307  O   LYS H  43      63.757 203.302  44.510  1.00 39.89           O
ANISOU  307  O   LYS H  43     8023   4208   2925   2249    497   -325       O
ATOM    308  CB  LYS H  43      60.425 202.949  43.586  1.00 42.21           C
ANISOU  308  CB  LYS H  43     7431   5055   3550   2949    796   -452       C
ATOM    309  CG  LYS H  43      59.105 203.720  43.440  1.00 58.08           C
ANISOU  309  CG  LYS H  43     9291   7120   5657   3427    841   -598       C
ATOM    310  CD  LYS H  43      58.017 203.254  44.407  1.00 70.11           C
ANISOU  310  CD  LYS H  43    10488   8945   7205   3587   1205   -746       C
ATOM    311  CE  LYS H  43      56.790 204.134  44.338  1.00 88.41           C
ANISOU  311  CE  LYS H  43    12648  11309   9633   4104   1248   -929       C
ATOM    312  NZ  LYS H  43      55.881 203.915  45.497  1.00100.30           N
ANISOU  312  NZ  LYS H  43    13926  13071  11114   4269   1667  -1104       N
ATOM    313  N   GLY H  44      62.661 201.373  44.930  1.00 32.94           N
ANISOU  313  N   GLY H  44     6534   3852   2132   2195    846   -299       N
ATOM    314  CA  GLY H  44      63.850 200.531  44.908  1.00 29.40           C
ANISOU  314  CA  GLY H  44     6113   3390   1667   1829    739   -182       C
ATOM    315  C   GLY H  44      64.171 199.995  43.521  1.00 31.79           C
ANISOU  315  C   GLY H  44     6163   3760   2156   1661    592    -56       C
ATOM    316  O   GLY H  44      63.599 200.451  42.523  1.00 32.48           O
ANISOU  316  O   GLY H  44     6136   3854   2350   1818    522    -47       O
ATOM    317  N   LEU H  45      65.105 199.029  43.443  1.00 24.66           N
ANISOU  317  N   LEU H  45     5196   2897   1276   1365    531     33       N
ATOM    318  CA  LEU H  45      65.483 198.411  42.177  1.00 21.35           C
ANISOU  318  CA  LEU H  45     4556   2551   1007   1203    421    132       C
ATOM    319  C   LEU H  45      64.433 197.388  41.764  1.00 24.15           C
ANISOU  319  C   LEU H  45     4530   3161   1485   1234    542    148       C
ATOM    320  O   LEU H  45      63.922 196.657  42.612  1.00 24.90           O
ANISOU  320  O   LEU H  45     4519   3385   1557   1216    720    129       O
ATOM    321  CB  LEU H  45      66.859 197.726  42.286  1.00 19.35           C
ANISOU  321  CB  LEU H  45     4346   2252    753    914    317    190       C
ATOM    322  CG  LEU H  45      68.076 198.610  42.568  1.00 23.29           C
ANISOU  322  CG  LEU H  45     5145   2519   1186    804    161    169       C
ATOM    323  CD1 LEU H  45      69.271 197.760  42.926  1.00 22.13           C
ANISOU  323  CD1 LEU H  45     4962   2386   1059    570     69    190       C
ATOM    324  CD2 LEU H  45      68.421 199.473  41.375  1.00 23.13           C
ANISOU  324  CD2 LEU H  45     5187   2371   1229    767     57    214       C
ATOM    325  N   GLU H  46      64.126 197.321  40.464  1.00 20.60           N
ANISOU  325  N   GLU H  46     3899   2776   1153   1258    441    185       N
ATOM    326  CA  GLU H  46      63.157 196.377  39.917  1.00 20.04           C
ANISOU  326  CA  GLU H  46     3456   2935   1223   1263    495    181       C
ATOM    327  C   GLU H  46      63.711 195.635  38.710  1.00 22.43           C
ANISOU  327  C   GLU H  46     3652   3272   1597   1081    356    249       C
ATOM    328  O   GLU H  46      64.086 196.255  37.719  1.00 22.93           O
ANISOU  328  O   GLU H  46     3834   3244   1633   1113    207    284       O
ATOM    329  CB  GLU H  46      61.818 197.061  39.579  1.00 23.50           C
ANISOU  329  CB  GLU H  46     3730   3462   1736   1568    499    103       C
ATOM    330  CG  GLU H  46      60.732 196.061  39.200  1.00 34.70           C
ANISOU  330  CG  GLU H  46     4708   5143   3332   1550    560     69       C
ATOM    331  CD  GLU H  46      59.504 196.553  38.451  1.00 56.66           C
ANISOU  331  CD  GLU H  46     7236   8047   6245   1832    458    -11       C
ATOM    332  OE1 GLU H  46      59.407 197.770  38.168  1.00 47.58           O
ANISOU  332  OE1 GLU H  46     6286   6757   5034   2099    331    -33       O
ATOM    333  OE2 GLU H  46      58.632 195.707  38.145  1.00 47.60           O
ANISOU  333  OE2 GLU H  46     5692   7124   5271   1785    484    -57       O
ATOM    334  N   TYR H  47      63.738 194.304  38.793  1.00 17.45           N
ANISOU  334  N   TYR H  47     2832   2759   1040    894    417    266       N
ATOM    335  CA  TYR H  47      64.166 193.416  37.720  1.00 15.07           C
ANISOU  335  CA  TYR H  47     2416   2502    807    736    309    298       C
ATOM    336  C   TYR H  47      62.982 193.313  36.750  1.00 21.58           C
ANISOU  336  C   TYR H  47     2989   3475   1736    851    235    253       C
ATOM    337  O   TYR H  47      61.890 192.915  37.177  1.00 23.90           O
ANISOU  337  O   TYR H  47     3033   3912   2136    891    337    200       O
ATOM    338  CB  TYR H  47      64.506 192.042  38.314  1.00 14.17           C
ANISOU  338  CB  TYR H  47     2226   2420    736    530    392    317       C
ATOM    339  CG  TYR H  47      65.148 191.089  37.335  1.00 12.77           C
ANISOU  339  CG  TYR H  47     1926   2191    735    384    258    300       C
ATOM    340  CD1 TYR H  47      66.529 191.046  37.180  1.00 13.09           C
ANISOU  340  CD1 TYR H  47     2085   2101    786    292    194    300       C
ATOM    341  CD2 TYR H  47      64.380 190.188  36.603  1.00 12.36           C
ANISOU  341  CD2 TYR H  47     1705   2313    678    331    252    291       C
ATOM    342  CE1 TYR H  47      67.128 190.149  36.302  1.00 12.42           C
ANISOU  342  CE1 TYR H  47     1880   1982    858    188    121    251       C
ATOM    343  CE2 TYR H  47      64.968 189.299  35.708  1.00 11.72           C
ANISOU  343  CE2 TYR H  47     1575   2191    686    216    147    262       C
ATOM    344  CZ  TYR H  47      66.343 189.274  35.573  1.00 15.61           C
ANISOU  344  CZ  TYR H  47     2257   2611   1061    154    125    297       C
ATOM    345  OH  TYR H  47      66.932 188.373  34.730  1.00 17.52           O
ANISOU  345  OH  TYR H  47     2474   2849   1334     70     61    257       O
ATOM    346  N   VAL H  48      63.173 193.707  35.464  1.00 17.70           N
ANISOU  346  N   VAL H  48     2564   2955   1207    904     59    269       N
ATOM    347  CA  VAL H  48      62.063 193.735  34.497  1.00 19.20           C
ANISOU  347  CA  VAL H  48     2555   3273   1468   1052    -84    218       C
ATOM    348  C   VAL H  48      62.230 192.803  33.286  1.00 24.60           C
ANISOU  348  C   VAL H  48     3161   4022   2163    918   -221    207       C
ATOM    349  O   VAL H  48      61.221 192.358  32.723  1.00 26.36           O
ANISOU  349  O   VAL H  48     3135   4390   2492    967   -335    134       O
ATOM    350  CB  VAL H  48      61.704 195.176  34.015  1.00 24.32           C
ANISOU  350  CB  VAL H  48     3380   3831   2030   1334   -221    229       C
ATOM    351  CG1 VAL H  48      61.106 196.014  35.146  1.00 25.95           C
ANISOU  351  CG1 VAL H  48     3583   4013   2264   1542   -102    182       C
ATOM    352  CG2 VAL H  48      62.891 195.885  33.361  1.00 22.65           C
ANISOU  352  CG2 VAL H  48     3554   3416   1637   1274   -291    329       C
ATOM    353  N   SER H  49      63.467 192.574  32.829  1.00 18.93           N
ANISOU  353  N   SER H  49     2650   3204   1338    767   -224    259       N
ATOM    354  CA  SER H  49      63.658 191.795  31.614  1.00 18.27           C
ANISOU  354  CA  SER H  49     2548   3172   1223    677   -341    230       C
ATOM    355  C   SER H  49      64.997 191.075  31.543  1.00 20.59           C
ANISOU  355  C   SER H  49     2946   3401   1479    476   -251    245       C
ATOM    356  O   SER H  49      65.945 191.461  32.224  1.00 20.04           O
ANISOU  356  O   SER H  49     3004   3232   1381    417   -141    296       O
ATOM    357  CB  SER H  49      63.482 192.690  30.390  1.00 22.49           C
ANISOU  357  CB  SER H  49     3272   3678   1597    834   -517    259       C
ATOM    358  OG  SER H  49      63.384 191.915  29.211  1.00 28.94           O
ANISOU  358  OG  SER H  49     4063   4571   2361    784   -655    202       O
ATOM    359  N   ALA H  50      65.078 190.031  30.695  1.00 16.08           N
ANISOU  359  N   ALA H  50     2313   2884    913    385   -317    178       N
ATOM    360  CA  ALA H  50      66.291 189.233  30.505  1.00 14.94           C
ANISOU  360  CA  ALA H  50     2234   2692    750    240   -241    157       C
ATOM    361  C   ALA H  50      66.324 188.560  29.134  1.00 20.62           C
ANISOU  361  C   ALA H  50     2993   3460   1381    221   -341     73       C
ATOM    362  O   ALA H  50      65.279 188.264  28.556  1.00 21.27           O
ANISOU  362  O   ALA H  50     2985   3618   1479    267   -498      9       O
ATOM    363  CB  ALA H  50      66.398 188.178  31.598  1.00 15.00           C
ANISOU  363  CB  ALA H  50     2109   2673    918    129   -162    135       C
ATOM    364  N   ILE H  51      67.532 188.311  28.625  1.00 17.07           N
ANISOU  364  N   ILE H  51     2666   2975    843    155   -252     56       N
ATOM    365  CA  ILE H  51      67.750 187.639  27.352  1.00 18.07           C
ANISOU  365  CA  ILE H  51     2877   3141    849    143   -300    -43       C
ATOM    366  C   ILE H  51      68.972 186.716  27.468  1.00 23.12           C
ANISOU  366  C   ILE H  51     3493   3744   1549     60   -166   -117       C
ATOM    367  O   ILE H  51      69.943 187.057  28.148  1.00 20.66           O
ANISOU  367  O   ILE H  51     3165   3392   1292     21    -32    -65       O
ATOM    368  CB  ILE H  51      67.824 188.655  26.154  1.00 22.67           C
ANISOU  368  CB  ILE H  51     3711   3744   1160    216   -327     10       C
ATOM    369  CG1 ILE H  51      67.697 187.943  24.790  1.00 24.10           C
ANISOU  369  CG1 ILE H  51     4013   3980   1166    234   -424   -109       C
ATOM    370  CG2 ILE H  51      69.072 189.567  26.219  1.00 23.18           C
ANISOU  370  CG2 ILE H  51     3925   3749   1132    154   -119    111       C
ATOM    371  CD1 ILE H  51      67.261 188.814  23.648  1.00 27.30           C
ANISOU  371  CD1 ILE H  51     4688   4404   1281    339   -545    -54       C
ATOM    372  N   THR H  52      68.907 185.531  26.835  1.00 23.02           N
ANISOU  372  N   THR H  52     3472   3735   1541     45   -228   -256       N
ATOM    373  CA  THR H  52      70.023 184.580  26.839  1.00 22.85           C
ANISOU  373  CA  THR H  52     3435   3668   1581     22   -123   -359       C
ATOM    374  C   THR H  52      71.138 185.112  25.920  1.00 28.10           C
ANISOU  374  C   THR H  52     4223   4394   2059     40     50   -378       C
ATOM    375  O   THR H  52      70.869 185.942  25.045  1.00 28.38           O
ANISOU  375  O   THR H  52     4425   4486   1873     58     53   -328       O
ATOM    376  CB  THR H  52      69.544 183.183  26.420  1.00 30.32           C
ANISOU  376  CB  THR H  52     4377   4563   2579     10   -252   -516       C
ATOM    377  OG1 THR H  52      69.110 183.227  25.068  1.00 34.47           O
ANISOU  377  OG1 THR H  52     5049   5157   2891     49   -344   -602       O
ATOM    378  CG2 THR H  52      68.431 182.651  27.304  1.00 28.18           C
ANISOU  378  CG2 THR H  52     3974   4230   2504    -66   -380   -487       C
ATOM    379  N   GLY H  52A     72.359 184.612  26.117  1.00 25.69           N
ANISOU  379  N   GLY H  52A    3838   4078   1846     40    194   -452       N
ATOM    380  CA  GLY H  52A     73.547 184.985  25.349  1.00 26.93           C
ANISOU  380  CA  GLY H  52A    4036   4317   1880     32    419   -495       C
ATOM    381  C   GLY H  52A     73.400 184.911  23.841  1.00 34.47           C
ANISOU  381  C   GLY H  52A    5209   5343   2545     64    471   -580       C
ATOM    382  O   GLY H  52A     73.904 185.782  23.126  1.00 36.22           O
ANISOU  382  O   GLY H  52A    5561   5636   2563     17    657   -521       O
ATOM    383  N   GLU H  53      72.704 183.873  23.344  1.00 31.70           N
ANISOU  383  N   GLU H  53     4931   4959   2155    128    306   -718       N
ATOM    384  CA  GLU H  53      72.456 183.696  21.913  1.00 33.81           C
ANISOU  384  CA  GLU H  53     5451   5282   2113    175    298   -826       C
ATOM    385  C   GLU H  53      71.266 184.529  21.425  1.00 37.32           C
ANISOU  385  C   GLU H  53     6078   5745   2356    175     97   -709       C
ATOM    386  O   GLU H  53      71.077 184.662  20.223  1.00 38.90           O
ANISOU  386  O   GLU H  53     6547   5995   2238    217     74   -756       O
ATOM    387  CB  GLU H  53      72.253 182.211  21.563  1.00 36.57           C
ANISOU  387  CB  GLU H  53     5826   5563   2508    243    173  -1057       C
ATOM    388  CG  GLU H  53      73.529 181.369  21.466  1.00 52.11           C
ANISOU  388  CG  GLU H  53     7723   7525   4552    323    387  -1234       C
ATOM    389  CD  GLU H  53      74.774 182.001  20.865  1.00 81.55           C
ANISOU  389  CD  GLU H  53    11465  11397   8121    332    741  -1245       C
ATOM    390  OE1 GLU H  53      75.838 181.952  21.522  1.00 80.77           O
ANISOU  390  OE1 GLU H  53    11122  11323   8244    346    915  -1261       O
ATOM    391  OE2 GLU H  53      74.712 182.434  19.690  1.00 78.26           O
ANISOU  391  OE2 GLU H  53    11311  11070   7355    329    845  -1261       O
ATOM    392  N   GLY H  54      70.485 185.074  22.356  1.00 32.34           N
ANISOU  392  N   GLY H  54     5312   5078   1899    151    -50   -568       N
ATOM    393  CA  GLY H  54      69.317 185.897  22.051  1.00 32.46           C
ANISOU  393  CA  GLY H  54     5436   5110   1786    196   -266   -466       C
ATOM    394  C   GLY H  54      68.115 185.125  21.554  1.00 37.14           C
ANISOU  394  C   GLY H  54     6032   5713   2368    239   -574   -600       C
ATOM    395  O   GLY H  54      67.190 185.711  20.987  1.00 37.38           O
ANISOU  395  O   GLY H  54     6179   5780   2241    314   -793   -562       O
ATOM    396  N   ASP H  55      68.111 183.807  21.783  1.00 34.77           N
ANISOU  396  N   ASP H  55     5601   5362   2247    191   -619   -761       N
ATOM    397  CA  ASP H  55      67.047 182.913  21.329  1.00 36.66           C
ANISOU  397  CA  ASP H  55     5827   5586   2517    177   -912   -919       C
ATOM    398  C   ASP H  55      65.911 182.746  22.346  1.00 38.48           C
ANISOU  398  C   ASP H  55     5757   5800   3065    100  -1080   -875       C
ATOM    399  O   ASP H  55      64.920 182.079  22.054  1.00 40.38           O
ANISOU  399  O   ASP H  55     5922   6038   3383     49  -1334  -1000       O
ATOM    400  CB  ASP H  55      67.626 181.547  20.899  1.00 40.10           C
ANISOU  400  CB  ASP H  55     6349   5937   2948    157   -878  -1139       C
ATOM    401  CG  ASP H  55      68.593 180.898  21.883  1.00 54.85           C
ANISOU  401  CG  ASP H  55     8074   7705   5061    124   -662  -1144       C
ATOM    402  OD1 ASP H  55      68.699 181.393  23.044  1.00 52.35           O
ANISOU  402  OD1 ASP H  55     7568   7381   4941     84   -566   -977       O
ATOM    403  OD2 ASP H  55      69.242 179.893  21.501  1.00 64.77           O
ANISOU  403  OD2 ASP H  55     9425   8881   6302    159   -610  -1325       O
ATOM    404  N   SER H  56      66.049 183.344  23.530  1.00 30.88           N
ANISOU  404  N   SER H  56     4622   4830   2282     78   -931   -711       N
ATOM    405  CA  SER H  56      65.025 183.278  24.570  1.00 29.23           C
ANISOU  405  CA  SER H  56     4136   4625   2346      7  -1013   -658       C
ATOM    406  C   SER H  56      65.013 184.569  25.373  1.00 30.36           C
ANISOU  406  C   SER H  56     4214   4810   2510     77   -897   -472       C
ATOM    407  O   SER H  56      66.080 185.090  25.718  1.00 27.80           O
ANISOU  407  O   SER H  56     3990   4447   2124     96   -693   -379       O
ATOM    408  CB  SER H  56      65.250 182.071  25.476  1.00 32.26           C
ANISOU  408  CB  SER H  56     4402   4881   2973   -136   -931   -702       C
ATOM    409  OG  SER H  56      64.184 181.881  26.391  1.00 42.17           O
ANISOU  409  OG  SER H  56     5409   6144   4469   -247   -980   -661       O
ATOM    410  N   ALA H  57      63.803 185.106  25.638  1.00 27.63           N
ANISOU  410  N   ALA H  57     3694   4545   2261    124  -1036   -437       N
ATOM    411  CA  ALA H  57      63.607 186.351  26.382  1.00 26.02           C
ANISOU  411  CA  ALA H  57     3440   4368   2078    228   -955   -290       C
ATOM    412  C   ALA H  57      62.612 186.206  27.543  1.00 29.08           C
ANISOU  412  C   ALA H  57     3513   4800   2735    179   -930   -277       C
ATOM    413  O   ALA H  57      61.671 185.418  27.466  1.00 30.85           O
ANISOU  413  O   ALA H  57     3518   5082   3122     89  -1058   -381       O
ATOM    414  CB  ALA H  57      63.156 187.447  25.443  1.00 28.49           C
ANISOU  414  CB  ALA H  57     3904   4737   2184    415  -1133   -255       C
ATOM    415  N   PHE H  58      62.846 186.958  28.626  1.00 22.94           N
ANISOU  415  N   PHE H  58     2722   3995   2000    220   -749   -158       N
ATOM    416  CA  PHE H  58      62.006 186.977  29.825  1.00 22.13           C
ANISOU  416  CA  PHE H  58     2367   3941   2102    192   -653   -135       C
ATOM    417  C   PHE H  58      61.492 188.387  30.064  1.00 25.59           C
ANISOU  417  C   PHE H  58     2791   4431   2500    411   -664    -74       C
ATOM    418  O   PHE H  58      62.239 189.351  29.888  1.00 23.87           O
ANISOU  418  O   PHE H  58     2829   4131   2108    519   -637      9       O
ATOM    419  CB  PHE H  58      62.783 186.477  31.070  1.00 21.60           C
ANISOU  419  CB  PHE H  58     2348   3765   2096     55   -420    -64       C
ATOM    420  CG  PHE H  58      62.131 186.861  32.380  1.00 22.55           C
ANISOU  420  CG  PHE H  58     2322   3923   2324     66   -260     -7       C
ATOM    421  CD1 PHE H  58      61.104 186.093  32.917  1.00 26.24           C
ANISOU  421  CD1 PHE H  58     2529   4460   2981    -70   -200    -48       C
ATOM    422  CD2 PHE H  58      62.481 188.042  33.032  1.00 22.76           C
ANISOU  422  CD2 PHE H  58     2475   3918   2254    208   -161     75       C
ATOM    423  CE1 PHE H  58      60.463 186.482  34.098  1.00 26.87           C
ANISOU  423  CE1 PHE H  58     2476   4600   3133    -53     -3     -4       C
ATOM    424  CE2 PHE H  58      61.815 188.444  34.188  1.00 25.23           C
ANISOU  424  CE2 PHE H  58     2677   4275   2632    251     -4    102       C
ATOM    425  CZ  PHE H  58      60.815 187.658  34.715  1.00 24.63           C
ANISOU  425  CZ  PHE H  58     2338   4293   2727    127     92     63       C
ATOM    426  N   TYR H  59      60.235 188.502  30.525  1.00 23.45           N
ANISOU  426  N   TYR H  59     2217   4286   2406    470   -683   -122       N
ATOM    427  CA  TYR H  59      59.612 189.785  30.834  1.00 23.91           C
ANISOU  427  CA  TYR H  59     2230   4393   2461    723   -694    -95       C
ATOM    428  C   TYR H  59      58.817 189.712  32.133  1.00 29.52           C
ANISOU  428  C   TYR H  59     2653   5195   3367    701   -481   -114       C
ATOM    429  O   TYR H  59      58.071 188.753  32.345  1.00 31.48           O
ANISOU  429  O   TYR H  59     2593   5553   3813    531   -443   -188       O
ATOM    430  CB  TYR H  59      58.697 190.238  29.685  1.00 26.98           C
ANISOU  430  CB  TYR H  59     2526   4887   2840    932  -1010   -173       C
ATOM    431  CG  TYR H  59      59.390 190.364  28.349  1.00 27.30           C
ANISOU  431  CG  TYR H  59     2904   4842   2628    966  -1210   -148       C
ATOM    432  CD1 TYR H  59      60.183 191.467  28.055  1.00 27.95           C
ANISOU  432  CD1 TYR H  59     3369   4782   2469   1101  -1196    -28       C
ATOM    433  CD2 TYR H  59      59.217 189.402  27.360  1.00 29.25           C
ANISOU  433  CD2 TYR H  59     3112   5142   2861    852  -1404   -251       C
ATOM    434  CE1 TYR H  59      60.801 191.604  26.811  1.00 27.74           C
ANISOU  434  CE1 TYR H  59     3676   4685   2180   1113  -1330      7       C
ATOM    435  CE2 TYR H  59      59.835 189.525  26.116  1.00 30.51           C
ANISOU  435  CE2 TYR H  59     3619   5234   2741    894  -1558   -237       C
ATOM    436  CZ  TYR H  59      60.630 190.625  25.848  1.00 36.52           C
ANISOU  436  CZ  TYR H  59     4754   5870   3251   1020  -1500   -100       C
ATOM    437  OH  TYR H  59      61.233 190.752  24.620  1.00 42.01           O
ANISOU  437  OH  TYR H  59     5811   6506   3644   1038  -1602    -74       O
ATOM    438  N   ALA H  60      58.973 190.724  33.002  1.00 25.59           N
ANISOU  438  N   ALA H  60     2273   4644   2805    859   -329    -54       N
ATOM    439  CA  ALA H  60      58.219 190.820  34.253  1.00 26.95           C
ANISOU  439  CA  ALA H  60     2219   4910   3110    885    -89    -80       C
ATOM    440  C   ALA H  60      56.797 191.255  33.900  1.00 36.26           C
ANISOU  440  C   ALA H  60     3021   6288   4468   1105   -214   -201       C
ATOM    441  O   ALA H  60      56.612 191.964  32.906  1.00 37.76           O
ANISOU  441  O   ALA H  60     3274   6474   4601   1333   -495   -226       O
ATOM    442  CB  ALA H  60      58.867 191.839  35.183  1.00 26.22           C
ANISOU  442  CB  ALA H  60     2423   4679   2859   1019     69     -7       C
ATOM    443  N   ASP H  61      55.793 190.822  34.690  1.00 35.84           N
ANISOU  443  N   ASP H  61     2575   6413   4629   1038     -9   -278       N
ATOM    444  CA  ASP H  61      54.376 191.139  34.455  1.00 40.37           C
ANISOU  444  CA  ASP H  61     2676   7223   5439   1236   -101   -425       C
ATOM    445  C   ASP H  61      54.097 192.648  34.287  1.00 45.34           C
ANISOU  445  C   ASP H  61     3397   7832   5998   1691   -239   -457       C
ATOM    446  O   ASP H  61      53.128 193.028  33.621  1.00 48.37           O
ANISOU  446  O   ASP H  61     3478   8366   6534   1938   -486   -575       O
ATOM    447  CB  ASP H  61      53.492 190.538  35.563  1.00 45.47           C
ANISOU  447  CB  ASP H  61     2913   8056   6306   1066    256   -487       C
ATOM    448  CG  ASP H  61      53.468 189.014  35.632  1.00 60.69           C
ANISOU  448  CG  ASP H  61     4690  10006   8364    615    354   -472       C
ATOM    449  OD1 ASP H  61      53.657 188.362  34.574  1.00 59.95           O
ANISOU  449  OD1 ASP H  61     4608   9872   8297    482     61   -497       O
ATOM    450  OD2 ASP H  61      53.197 188.474  36.732  1.00 71.62           O
ANISOU  450  OD2 ASP H  61     5958  11440   9815    398    724   -444       O
ATOM    451  N   SER H  62      54.970 193.494  34.870  1.00 39.05           N
ANISOU  451  N   SER H  62     3035   6829   4973   1804   -113   -357       N
ATOM    452  CA  SER H  62      54.885 194.953  34.816  1.00 39.65           C
ANISOU  452  CA  SER H  62     3320   6798   4946   2211   -222   -368       C
ATOM    453  C   SER H  62      55.155 195.526  33.416  1.00 43.50           C
ANISOU  453  C   SER H  62     4069   7158   5302   2383   -629   -321       C
ATOM    454  O   SER H  62      54.561 196.545  33.057  1.00 46.19           O
ANISOU  454  O   SER H  62     4426   7477   5649   2765   -830   -371       O
ATOM    455  CB  SER H  62      55.843 195.576  35.829  1.00 39.33           C
ANISOU  455  CB  SER H  62     3709   6540   4694   2203     14   -279       C
ATOM    456  OG  SER H  62      57.189 195.216  35.569  1.00 41.19           O
ANISOU  456  OG  SER H  62     4323   6585   4744   1936    -20   -142       O
ATOM    457  N   VAL H  63      56.058 194.889  32.642  1.00 36.68           N
ANISOU  457  N   VAL H  63     3441   6197   4298   2120   -739   -226       N
ATOM    458  CA  VAL H  63      56.451 195.359  31.304  1.00 36.74           C
ANISOU  458  CA  VAL H  63     3772   6073   4113   2231  -1069   -160       C
ATOM    459  C   VAL H  63      55.968 194.432  30.160  1.00 42.32           C
ANISOU  459  C   VAL H  63     4257   6934   4888   2134  -1344   -233       C
ATOM    460  O   VAL H  63      56.023 194.822  28.993  1.00 41.80           O
ANISOU  460  O   VAL H  63     4426   6801   4657   2279  -1654   -204       O
ATOM    461  CB  VAL H  63      57.981 195.631  31.220  1.00 37.05           C
ANISOU  461  CB  VAL H  63     4336   5856   3885   2054   -974     -1       C
ATOM    462  CG1 VAL H  63      58.434 196.602  32.307  1.00 36.17           C
ANISOU  462  CG1 VAL H  63     4462   5573   3707   2146   -766     49       C
ATOM    463  CG2 VAL H  63      58.791 194.336  31.271  1.00 33.76           C
ANISOU  463  CG2 VAL H  63     3890   5468   3470   1664   -829     24       C
ATOM    464  N   LYS H  64      55.501 193.217  30.517  1.00 40.86           N
ANISOU  464  N   LYS H  64     3663   6935   4928   1878  -1229   -326       N
ATOM    465  CA  LYS H  64      55.022 192.161  29.619  1.00 42.46           C
ANISOU  465  CA  LYS H  64     3618   7277   5238   1715  -1460   -428       C
ATOM    466  C   LYS H  64      54.039 192.697  28.579  1.00 51.40           C
ANISOU  466  C   LYS H  64     4606   8518   6407   2033  -1891   -529       C
ATOM    467  O   LYS H  64      53.056 193.354  28.935  1.00 54.67           O
ANISOU  467  O   LYS H  64     4707   9060   7006   2317  -1942   -616       O
ATOM    468  CB  LYS H  64      54.374 191.028  30.448  1.00 45.81           C
ANISOU  468  CB  LYS H  64     3561   7878   5966   1434  -1233   -523       C
ATOM    469  CG  LYS H  64      54.157 189.716  29.691  1.00 57.95           C
ANISOU  469  CG  LYS H  64     4918   9489   7611   1147  -1411   -617       C
ATOM    470  CD  LYS H  64      55.071 188.588  30.184  1.00 65.01           C
ANISOU  470  CD  LYS H  64     5988  10251   8462    763  -1155   -544       C
ATOM    471  CE  LYS H  64      54.460 187.765  31.298  1.00 76.03           C
ANISOU  471  CE  LYS H  64     7018  11745  10126    497   -853   -577       C
ATOM    472  NZ  LYS H  64      55.375 186.683  31.754  1.00 82.33           N
ANISOU  472  NZ  LYS H  64     8042  12373  10868    155   -666   -499       N
ATOM    473  N   GLY H  65      54.340 192.441  27.308  1.00 48.07           N
ANISOU  473  N   GLY H  65     4435   8039   5789   2010  -2201   -523       N
ATOM    474  CA  GLY H  65      53.495 192.854  26.195  1.00 51.77           C
ANISOU  474  CA  GLY H  65     4846   8591   6234   2303  -2679   -613       C
ATOM    475  C   GLY H  65      53.898 194.152  25.523  1.00 55.82           C
ANISOU  475  C   GLY H  65     5891   8901   6418   2641  -2881   -479       C
ATOM    476  O   GLY H  65      53.891 194.232  24.291  1.00 57.78           O
ANISOU  476  O   GLY H  65     6410   9107   6437   2748  -3245   -474       O
ATOM    477  N   ARG H  66      54.246 195.181  26.324  1.00 50.03           N
ANISOU  477  N   ARG H  66     5352   8019   5637   2805  -2651   -369       N
ATOM    478  CA  ARG H  66      54.628 196.510  25.826  1.00 50.28           C
ANISOU  478  CA  ARG H  66     5926   7803   5375   3109  -2807   -225       C
ATOM    479  C   ARG H  66      56.115 196.618  25.459  1.00 50.45           C
ANISOU  479  C   ARG H  66     6550   7577   5043   2867  -2628    -32       C
ATOM    480  O   ARG H  66      56.451 197.210  24.431  1.00 52.25           O
ANISOU  480  O   ARG H  66     7261   7637   4957   2992  -2845     82       O
ATOM    481  CB  ARG H  66      54.278 197.608  26.849  1.00 50.46           C
ANISOU  481  CB  ARG H  66     5899   7750   5522   3405  -2662   -221       C
ATOM    482  CG  ARG H  66      52.862 197.543  27.415  1.00 60.45           C
ANISOU  482  CG  ARG H  66     6508   9287   7172   3645  -2727   -428       C
ATOM    483  CD  ARG H  66      52.515 198.730  28.317  1.00 67.20           C
ANISOU  483  CD  ARG H  66     7381  10046   8105   4015  -2605   -444       C
ATOM    484  NE  ARG H  66      53.602 199.127  29.221  1.00 62.49           N
ANISOU  484  NE  ARG H  66     7176   9217   7352   3843  -2215   -310       N
ATOM    485  CZ  ARG H  66      53.909 198.502  30.352  1.00 73.04           C
ANISOU  485  CZ  ARG H  66     8306  10640   8806   3551  -1798   -334       C
ATOM    486  NH1 ARG H  66      53.231 197.424  30.729  1.00 60.55           N
ANISOU  486  NH1 ARG H  66     6154   9357   7495   3362  -1670   -466       N
ATOM    487  NH2 ARG H  66      54.911 198.935  31.104  1.00 57.89           N
ANISOU  487  NH2 ARG H  66     6773   8495   6725   3425  -1520   -222       N
ATOM    488  N   PHE H  67      57.002 196.096  26.318  1.00 42.26           N
ANISOU  488  N   PHE H  67     5488   6514   4054   2533  -2229      8       N
ATOM    489  CA  PHE H  67      58.448 196.197  26.122  1.00 38.97           C
ANISOU  489  CA  PHE H  67     5542   5894   3370   2295  -2020    165       C
ATOM    490  C   PHE H  67      59.031 194.965  25.433  1.00 42.16           C
ANISOU  490  C   PHE H  67     5952   6379   3690   1990  -1993    132       C
ATOM    491  O   PHE H  67      58.536 193.848  25.630  1.00 42.21           O
ANISOU  491  O   PHE H  67     5559   6568   3913   1848  -1994     -5       O
ATOM    492  CB  PHE H  67      59.172 196.474  27.462  1.00 37.57           C
ANISOU  492  CB  PHE H  67     5382   5613   3279   2159  -1645    223       C
ATOM    493  CG  PHE H  67      58.871 197.781  28.177  1.00 39.97           C
ANISOU  493  CG  PHE H  67     5810   5770   3606   2439  -1625    258       C
ATOM    494  CD1 PHE H  67      57.789 198.573  27.801  1.00 46.83           C
ANISOU  494  CD1 PHE H  67     6649   6642   4504   2841  -1919    213       C
ATOM    495  CD2 PHE H  67      59.653 198.201  29.244  1.00 39.07           C
ANISOU  495  CD2 PHE H  67     5842   5508   3492   2323  -1339    316       C
ATOM    496  CE1 PHE H  67      57.504 199.760  28.480  1.00 49.34           C
ANISOU  496  CE1 PHE H  67     7097   6802   4849   3133  -1899    222       C
ATOM    497  CE2 PHE H  67      59.363 199.384  29.926  1.00 43.19           C
ANISOU  497  CE2 PHE H  67     6509   5874   4028   2587  -1325    322       C
ATOM    498  CZ  PHE H  67      58.292 200.153  29.542  1.00 45.49           C
ANISOU  498  CZ  PHE H  67     6783   6155   4348   2996  -1591    273       C
ATOM    499  N   THR H  68      60.083 195.171  24.621  1.00 37.48           N
ANISOU  499  N   THR H  68     5822   5637   2780   1883  -1951    251       N
ATOM    500  CA  THR H  68      60.747 194.097  23.889  1.00 36.28           C
ANISOU  500  CA  THR H  68     5741   5542   2503   1633  -1901    209       C
ATOM    501  C   THR H  68      62.262 194.167  24.060  1.00 38.04           C
ANISOU  501  C   THR H  68     6237   5630   2587   1392  -1557    322       C
ATOM    502  O   THR H  68      62.874 195.194  23.762  1.00 38.02           O
ANISOU  502  O   THR H  68     6628   5455   2364   1424  -1493    472       O
ATOM    503  CB  THR H  68      60.328 194.108  22.407  1.00 46.30           C
ANISOU  503  CB  THR H  68     7265   6831   3496   1774  -2249    186       C
ATOM    504  OG1 THR H  68      58.904 194.114  22.323  1.00 48.62           O
ANISOU  504  OG1 THR H  68     7245   7262   3967   2017  -2607     64       O
ATOM    505  CG2 THR H  68      60.885 192.918  21.631  1.00 43.41           C
ANISOU  505  CG2 THR H  68     6962   6536   2997   1546  -2211     95       C
ATOM    506  N   ILE H  69      62.859 193.063  24.531  1.00 32.36           N
ANISOU  506  N   ILE H  69     5304   4982   2011   1146  -1347    246       N
ATOM    507  CA  ILE H  69      64.305 192.935  24.691  1.00 30.18           C
ANISOU  507  CA  ILE H  69     5189   4623   1657    922  -1043    309       C
ATOM    508  C   ILE H  69      64.861 192.195  23.473  1.00 35.29           C
ANISOU  508  C   ILE H  69     6014   5313   2082    821  -1044    253       C
ATOM    509  O   ILE H  69      64.200 191.298  22.944  1.00 36.70           O
ANISOU  509  O   ILE H  69     6064   5600   2281    844  -1235    117       O
ATOM    510  CB  ILE H  69      64.707 192.298  26.068  1.00 30.37           C
ANISOU  510  CB  ILE H  69     4908   4667   1963    765   -823    269       C
ATOM    511  CG1 ILE H  69      66.204 192.535  26.393  1.00 28.87           C
ANISOU  511  CG1 ILE H  69     4873   4375   1722    586   -552    345       C
ATOM    512  CG2 ILE H  69      64.314 190.815  26.170  1.00 31.04           C
ANISOU  512  CG2 ILE H  69     4692   4875   2226    663   -864    120       C
ATOM    513  CD1 ILE H  69      66.667 192.083  27.818  1.00 33.33           C
ANISOU  513  CD1 ILE H  69     5206   4931   2527    468   -385    322       C
ATOM    514  N   SER H  70      66.025 192.635  22.975  1.00 31.02           N
ANISOU  514  N   SER H  70     5786   4686   1315    712   -835    348       N
ATOM    515  CA  SER H  70      66.683 192.043  21.812  1.00 31.80           C
ANISOU  515  CA  SER H  70     6096   4828   1158    623   -761    294       C
ATOM    516  C   SER H  70      68.176 192.321  21.865  1.00 36.29           C
ANISOU  516  C   SER H  70     6794   5341   1655    427   -395    369       C
ATOM    517  O   SER H  70      68.610 193.170  22.642  1.00 34.99           O
ANISOU  517  O   SER H  70     6632   5075   1589    366   -263    486       O
ATOM    518  CB  SER H  70      66.075 192.568  20.508  1.00 37.50           C
ANISOU  518  CB  SER H  70     7196   5530   1523    784  -1005    340       C
ATOM    519  OG  SER H  70      66.106 193.984  20.415  1.00 43.75           O
ANISOU  519  OG  SER H  70     8315   6164   2143    863  -1006    539       O
ATOM    520  N   ARG H  71      68.970 191.598  21.050  1.00 34.80           N
ANISOU  520  N   ARG H  71     6693   5222   1305    326   -228    281       N
ATOM    521  CA  ARG H  71      70.423 191.769  21.013  1.00 34.03           C
ANISOU  521  CA  ARG H  71     6647   5117   1167    134    145    318       C
ATOM    522  C   ARG H  71      71.017 191.456  19.649  1.00 40.67           C
ANISOU  522  C   ARG H  71     7771   6023   1659     88    313    268       C
ATOM    523  O   ARG H  71      70.491 190.617  18.910  1.00 42.25           O
ANISOU  523  O   ARG H  71     8033   6298   1723    190    153    127       O
ATOM    524  CB  ARG H  71      71.121 190.959  22.134  1.00 29.28           C
ANISOU  524  CB  ARG H  71     5635   4560    930     35    289    212       C
ATOM    525  CG  ARG H  71      71.045 189.434  21.982  1.00 32.81           C
ANISOU  525  CG  ARG H  71     5884   5102   1480     75    232      1       C
ATOM    526  CD  ARG H  71      71.405 188.714  23.266  1.00 31.37           C
ANISOU  526  CD  ARG H  71     5343   4911   1663     30    270    -66       C
ATOM    527  NE  ARG H  71      72.839 188.767  23.558  1.00 32.75           N
ANISOU  527  NE  ARG H  71     5413   5105   1927    -87    552    -77       N
ATOM    528  CZ  ARG H  71      73.361 188.565  24.766  1.00 41.12           C
ANISOU  528  CZ  ARG H  71     6213   6136   3273   -131    585    -88       C
ATOM    529  NH1 ARG H  71      72.575 188.291  25.799  1.00 26.82           N
ANISOU  529  NH1 ARG H  71     4268   4270   1654    -80    396    -72       N
ATOM    530  NH2 ARG H  71      74.670 188.634  24.948  1.00 20.90           N
ANISOU  530  NH2 ARG H  71     3524   3612    805   -227    806   -118       N
ATOM    531  N   ASP H  72      72.120 192.137  19.324  1.00 37.53           N
ANISOU  531  N   ASP H  72     7548   5597   1114    -82    649    374       N
ATOM    532  CA  ASP H  72      72.867 191.947  18.093  1.00 40.07           C
ANISOU  532  CA  ASP H  72     8139   5994   1090   -162    921    338       C
ATOM    533  C   ASP H  72      74.297 191.623  18.495  1.00 44.57           C
ANISOU  533  C   ASP H  72     8408   6653   1872   -354   1324    260       C
ATOM    534  O   ASP H  72      75.049 192.518  18.899  1.00 44.96           O
ANISOU  534  O   ASP H  72     8443   6643   1998   -545   1549    396       O
ATOM    535  CB  ASP H  72      72.806 193.211  17.221  1.00 44.94           C
ANISOU  535  CB  ASP H  72     9296   6490   1291   -207    975    566       C
ATOM    536  CG  ASP H  72      73.308 193.032  15.799  1.00 60.57           C
ANISOU  536  CG  ASP H  72    11662   8545   2807   -260   1223    543       C
ATOM    537  OD1 ASP H  72      73.808 191.922  15.472  1.00 59.77           O
ANISOU  537  OD1 ASP H  72    11384   8605   2721   -256   1387    323       O
ATOM    538  OD2 ASP H  72      73.191 193.992  15.007  1.00 72.75           O
ANISOU  538  OD2 ASP H  72    13720   9972   3950   -290   1254    741       O
ATOM    539  N   ASN H  73      74.656 190.332  18.436  1.00 40.93           N
ANISOU  539  N   ASN H  73     7693   6322   1535   -296   1385     27       N
ATOM    540  CA  ASN H  73      75.972 189.856  18.854  1.00 41.20           C
ANISOU  540  CA  ASN H  73     7374   6461   1821   -409   1711    -95       C
ATOM    541  C   ASN H  73      77.103 190.291  17.918  1.00 49.56           C
ANISOU  541  C   ASN H  73     8592   7613   2626   -582   2175    -74       C
ATOM    542  O   ASN H  73      78.246 190.402  18.367  1.00 49.72           O
ANISOU  542  O   ASN H  73     8299   7707   2883   -737   2467   -109       O
ATOM    543  CB  ASN H  73      75.957 188.345  19.077  1.00 40.91           C
ANISOU  543  CB  ASN H  73     7063   6494   1988   -253   1606   -351       C
ATOM    544  CG  ASN H  73      75.134 187.919  20.282  1.00 51.09           C
ANISOU  544  CG  ASN H  73     8109   7693   3611   -161   1251   -357       C
ATOM    545  OD1 ASN H  73      74.542 188.737  21.003  1.00 40.71           O
ANISOU  545  OD1 ASN H  73     6794   6284   2390   -191   1085   -190       O
ATOM    546  ND2 ASN H  73      75.077 186.618  20.526  1.00 41.66           N
ANISOU  546  ND2 ASN H  73     6728   6509   2592    -48   1143   -554       N
ATOM    547  N   SER H  74      76.788 190.589  16.645  1.00 49.91           N
ANISOU  547  N   SER H  74     9120   7656   2187   -569   2242    -12       N
ATOM    548  CA  SER H  74      77.783 191.095  15.697  1.00 54.37           C
ANISOU  548  CA  SER H  74     9911   8303   2446   -765   2728     42       C
ATOM    549  C   SER H  74      78.092 192.583  15.975  1.00 58.71           C
ANISOU  549  C   SER H  74    10611   8712   2984  -1025   2869    328       C
ATOM    550  O   SER H  74      79.194 193.041  15.676  1.00 61.93           O
ANISOU  550  O   SER H  74    10991   9187   3351  -1284   3326    373       O
ATOM    551  CB  SER H  74      77.318 190.899  14.256  1.00 61.40           C
ANISOU  551  CB  SER H  74    11341   9220   2769   -657   2741     18       C
ATOM    552  OG  SER H  74      76.091 191.563  14.005  1.00 70.54           O
ANISOU  552  OG  SER H  74    12923  10208   3670   -553   2340    203       O
ATOM    553  N   LYS H  75      77.122 193.320  16.564  1.00 52.13           N
ANISOU  553  N   LYS H  75     9921   7680   2207   -960   2484    504       N
ATOM    554  CA  LYS H  75      77.253 194.740  16.917  1.00 52.26           C
ANISOU  554  CA  LYS H  75    10131   7499   2225  -1166   2533    766       C
ATOM    555  C   LYS H  75      77.591 194.948  18.409  1.00 52.77           C
ANISOU  555  C   LYS H  75     9721   7516   2813  -1253   2453    749       C
ATOM    556  O   LYS H  75      77.813 196.091  18.828  1.00 53.81           O
ANISOU  556  O   LYS H  75     9971   7473   3003  -1447   2499    931       O
ATOM    557  CB  LYS H  75      75.974 195.512  16.552  1.00 54.74           C
ANISOU  557  CB  LYS H  75    10963   7602   2235   -996   2157    962       C
ATOM    558  CG  LYS H  75      75.922 195.977  15.108  1.00 67.55           C
ANISOU  558  CG  LYS H  75    13225   9174   3267  -1032   2305   1105       C
ATOM    559  CD  LYS H  75      74.800 196.982  14.890  1.00 79.73           C
ANISOU  559  CD  LYS H  75    15285  10457   4554   -876   1921   1337       C
ATOM    560  CE  LYS H  75      74.795 197.550  13.488  1.00 97.52           C
ANISOU  560  CE  LYS H  75    18257  12616   6178   -917   2051   1518       C
ATOM    561  NZ  LYS H  75      73.767 198.614  13.328  1.00107.66           N
ANISOU  561  NZ  LYS H  75    20063  13610   7233   -744   1653   1758       N
ATOM    562  N   ASN H  76      77.629 193.846  19.207  1.00 44.32           N
ANISOU  562  N   ASN H  76     8163   6576   2101  -1110   2316    532       N
ATOM    563  CA  ASN H  76      77.927 193.848  20.645  1.00 40.79           C
ANISOU  563  CA  ASN H  76     7281   6099   2117  -1151   2201    488       C
ATOM    564  C   ASN H  76      76.997 194.798  21.432  1.00 42.77           C
ANISOU  564  C   ASN H  76     7704   6125   2421  -1098   1880    659       C
ATOM    565  O   ASN H  76      77.425 195.428  22.398  1.00 40.50           O
ANISOU  565  O   ASN H  76     7262   5743   2384  -1239   1879    708       O
ATOM    566  CB  ASN H  76      79.422 194.156  20.902  1.00 41.60           C
ANISOU  566  CB  ASN H  76     7088   6283   2435  -1447   2575    456       C
ATOM    567  CG  ASN H  76      80.291 192.936  21.102  1.00 64.00           C
ANISOU  567  CG  ASN H  76     9431   9344   5542  -1386   2709    198       C
ATOM    568  OD1 ASN H  76      80.142 191.908  20.438  1.00 56.27           O
ANISOU  568  OD1 ASN H  76     8451   8491   4438  -1201   2738     43       O
ATOM    569  ND2 ASN H  76      81.241 193.030  22.019  1.00 61.12           N
ANISOU  569  ND2 ASN H  76     8646   9021   5556  -1525   2769    133       N
ATOM    570  N   THR H  77      75.718 194.887  21.009  1.00 39.81           N
ANISOU  570  N   THR H  77     7640   5670   1814   -876   1594    726       N
ATOM    571  CA  THR H  77      74.736 195.793  21.603  1.00 38.48           C
ANISOU  571  CA  THR H  77     7656   5299   1664   -765   1296    870       C
ATOM    572  C   THR H  77      73.447 195.093  22.031  1.00 38.75           C
ANISOU  572  C   THR H  77     7546   5374   1803   -471    927    775       C
ATOM    573  O   THR H  77      72.965 194.189  21.349  1.00 39.12           O
ANISOU  573  O   THR H  77     7596   5543   1727   -334    830    665       O
ATOM    574  CB  THR H  77      74.442 196.965  20.634  1.00 53.92           C
ANISOU  574  CB  THR H  77    10189   7073   3224   -797   1312   1089       C
ATOM    575  OG1 THR H  77      75.641 197.336  19.953  1.00 57.02           O
ANISOU  575  OG1 THR H  77    10727   7479   3459  -1099   1726   1158       O
ATOM    576  CG2 THR H  77      73.863 198.186  21.344  1.00 54.90           C
ANISOU  576  CG2 THR H  77    10517   6934   3407   -748   1103   1249       C
ATOM    577  N   LEU H  78      72.880 195.559  23.150  1.00 32.44           N
ANISOU  577  N   LEU H  78     6637   4467   1223   -390    731    811       N
ATOM    578  CA  LEU H  78      71.615 195.114  23.737  1.00 29.20           C
ANISOU  578  CA  LEU H  78     6064   4084    948   -144    420    742       C
ATOM    579  C   LEU H  78      70.581 196.216  23.496  1.00 34.43           C
ANISOU  579  C   LEU H  78     7057   4585   1440     35    193    881       C
ATOM    580  O   LEU H  78      70.913 197.403  23.587  1.00 35.51           O
ANISOU  580  O   LEU H  78     7466   4527   1498    -45    259   1030       O
ATOM    581  CB  LEU H  78      71.797 194.864  25.252  1.00 25.67           C
ANISOU  581  CB  LEU H  78     5262   3638    853   -172    408    675       C
ATOM    582  CG  LEU H  78      70.525 194.572  26.070  1.00 27.61           C
ANISOU  582  CG  LEU H  78     5335   3900   1255     40    157    625       C
ATOM    583  CD1 LEU H  78      69.959 193.190  25.758  1.00 26.05           C
ANISOU  583  CD1 LEU H  78     4924   3865   1108    121     57    482       C
ATOM    584  CD2 LEU H  78      70.777 194.738  27.552  1.00 26.13           C
ANISOU  584  CD2 LEU H  78     4956   3656   1315     -3    180    611       C
ATOM    585  N   TYR H  79      69.341 195.832  23.179  1.00 30.95           N
ANISOU  585  N   TYR H  79     6591   4212    958    278    -90    825       N
ATOM    586  CA  TYR H  79      68.283 196.802  22.907  1.00 33.11           C
ANISOU  586  CA  TYR H  79     7137   4353   1091    514   -356    928       C
ATOM    587  C   TYR H  79      67.072 196.619  23.815  1.00 36.42           C
ANISOU  587  C   TYR H  79     7238   4827   1771    742   -598    836       C
ATOM    588  O   TYR H  79      66.840 195.523  24.325  1.00 33.62           O
ANISOU  588  O   TYR H  79     6498   4640   1636    721   -602    691       O
ATOM    589  CB  TYR H  79      67.849 196.743  21.431  1.00 37.25           C
ANISOU  589  CB  TYR H  79     7996   4902   1254    627   -513    958       C
ATOM    590  CG  TYR H  79      68.975 196.918  20.432  1.00 41.21           C
ANISOU  590  CG  TYR H  79     8857   5363   1439    405   -231   1053       C
ATOM    591  CD1 TYR H  79      69.433 198.185  20.083  1.00 45.99           C
ANISOU  591  CD1 TYR H  79     9924   5737   1814    318   -122   1268       C
ATOM    592  CD2 TYR H  79      69.528 195.821  19.775  1.00 41.99           C
ANISOU  592  CD2 TYR H  79     8864   5643   1448    288    -67    926       C
ATOM    593  CE1 TYR H  79      70.447 198.354  19.139  1.00 50.20           C
ANISOU  593  CE1 TYR H  79    10790   6243   2042     80    186   1365       C
ATOM    594  CE2 TYR H  79      70.548 195.977  18.838  1.00 45.33           C
ANISOU  594  CE2 TYR H  79     9601   6057   1567     90    243    998       C
ATOM    595  CZ  TYR H  79      71.002 197.246  18.520  1.00 57.33           C
ANISOU  595  CZ  TYR H  79    11554   7368   2862    -29    385   1225       C
ATOM    596  OH  TYR H  79      71.997 197.408  17.585  1.00 65.03           O
ANISOU  596  OH  TYR H  79    12839   8342   3526   -258    740   1306       O
ATOM    597  N   PHE H  80      66.286 197.695  23.995  1.00 35.12           N
ANISOU  597  N   PHE H  80     7251   4514   1579    965   -787    920       N
ATOM    598  CA  PHE H  80      65.051 197.667  24.772  1.00 34.50           C
ANISOU  598  CA  PHE H  80     6874   4501   1732   1217   -995    827       C
ATOM    599  C   PHE H  80      64.003 198.583  24.133  1.00 42.60           C
ANISOU  599  C   PHE H  80     8158   5424   2606   1549  -1315    889       C
ATOM    600  O   PHE H  80      64.004 199.792  24.367  1.00 43.69           O
ANISOU  600  O   PHE H  80     8592   5329   2682   1666  -1342   1002       O
ATOM    601  CB  PHE H  80      65.308 198.018  26.249  1.00 34.43           C
ANISOU  601  CB  PHE H  80     6693   4422   1967   1164   -832    814       C
ATOM    602  CG  PHE H  80      64.342 197.423  27.253  1.00 34.72           C
ANISOU  602  CG  PHE H  80     6285   4621   2285   1294   -888    673       C
ATOM    603  CD1 PHE H  80      63.892 196.112  27.121  1.00 37.03           C
ANISOU  603  CD1 PHE H  80     6228   5140   2700   1248   -932    547       C
ATOM    604  CD2 PHE H  80      63.938 198.148  28.365  1.00 36.74           C
ANISOU  604  CD2 PHE H  80     6490   4791   2679   1432   -862    661       C
ATOM    605  CE1 PHE H  80      63.021 195.555  28.061  1.00 37.29           C
ANISOU  605  CE1 PHE H  80     5860   5316   2993   1313   -936    433       C
ATOM    606  CE2 PHE H  80      63.079 197.584  29.313  1.00 39.05           C
ANISOU  606  CE2 PHE H  80     6380   5249   3209   1524   -848    536       C
ATOM    607  CZ  PHE H  80      62.626 196.291  29.154  1.00 36.50           C
ANISOU  607  CZ  PHE H  80     5704   5155   3011   1447   -873    433       C
ATOM    608  N   GLU H  81      63.155 198.005  23.260  1.00 41.82           N
ANISOU  608  N   GLU H  81     7984   5477   2431   1705  -1586    809       N
ATOM    609  CA  GLU H  81      62.075 198.721  22.583  1.00 45.64           C
ANISOU  609  CA  GLU H  81     8661   5897   2782   2064  -1969    837       C
ATOM    610  C   GLU H  81      60.931 198.885  23.567  1.00 48.60           C
ANISOU  610  C   GLU H  81     8614   6358   3495   2327  -2108    717       C
ATOM    611  O   GLU H  81      60.411 197.893  24.074  1.00 46.86           O
ANISOU  611  O   GLU H  81     7883   6374   3546   2273  -2088    553       O
ATOM    612  CB  GLU H  81      61.603 197.958  21.331  1.00 49.44           C
ANISOU  612  CB  GLU H  81     9173   6535   3076   2121  -2239    761       C
ATOM    613  CG  GLU H  81      62.511 198.123  20.123  1.00 67.30           C
ANISOU  613  CG  GLU H  81    11996   8680   4895   1974  -2159    900       C
ATOM    614  CD  GLU H  81      62.250 197.150  18.988  1.00 94.62           C
ANISOU  614  CD  GLU H  81    15484  12313   8155   1968  -2356    785       C
ATOM    615  OE1 GLU H  81      61.243 197.336  18.266  1.00103.55           O
ANISOU  615  OE1 GLU H  81    16715  13467   9161   2257  -2790    751       O
ATOM    616  OE2 GLU H  81      63.066 196.215  18.805  1.00 77.68           O
ANISOU  616  OE2 GLU H  81    13274  10270   5971   1692  -2096    717       O
ATOM    617  N   MET H  82      60.582 200.127  23.887  1.00 46.95           N
ANISOU  617  N   MET H  82     8624   5943   3273   2594  -2211    795       N
ATOM    618  CA  MET H  82      59.514 200.411  24.841  1.00 47.72           C
ANISOU  618  CA  MET H  82     8340   6115   3677   2884  -2303    668       C
ATOM    619  C   MET H  82      58.363 201.103  24.136  1.00 57.24           C
ANISOU  619  C   MET H  82     9646   7283   4820   3342  -2746    652       C
ATOM    620  O   MET H  82      58.538 202.202  23.611  1.00 60.03           O
ANISOU  620  O   MET H  82    10547   7343   4917   3518  -2891    809       O
ATOM    621  CB  MET H  82      60.032 201.263  26.014  1.00 48.57           C
ANISOU  621  CB  MET H  82     8577   6012   3867   2858  -2043    722       C
ATOM    622  CG  MET H  82      61.237 200.663  26.721  1.00 47.96           C
ANISOU  622  CG  MET H  82     8425   5954   3842   2428  -1656    739       C
ATOM    623  SD  MET H  82      61.921 201.730  28.013  1.00 51.25           S
ANISOU  623  SD  MET H  82     9067   6095   4311   2379  -1417    792       S
ATOM    624  CE  MET H  82      62.496 203.053  27.058  1.00 51.08           C
ANISOU  624  CE  MET H  82     9760   5687   3962   2409  -1529   1007       C
ATOM    625  N   ASN H  82A     57.200 200.439  24.077  1.00 55.58           N
ANISOU  625  N   ASN H  82A    8916   7359   4842   3522  -2981    463       N
ATOM    626  CA  ASN H  82A     55.985 200.970  23.447  1.00 60.42           C
ANISOU  626  CA  ASN H  82A    9496   7998   5465   3992  -3459    399       C
ATOM    627  C   ASN H  82A     54.889 201.126  24.506  1.00 65.93           C
ANISOU  627  C   ASN H  82A    9615   8863   6572   4278  -3461    211       C
ATOM    628  O   ASN H  82A     54.997 200.528  25.581  1.00 62.64           O
ANISOU  628  O   ASN H  82A    8789   8602   6409   4050  -3103    120       O
ATOM    629  CB  ASN H  82A     55.511 200.050  22.312  1.00 62.70           C
ANISOU  629  CB  ASN H  82A    9643   8505   5676   3965  -3793    308       C
ATOM    630  CG  ASN H  82A     56.529 199.833  21.212  1.00 89.08           C
ANISOU  630  CG  ASN H  82A   13555  11711   8581   3709  -3774    466       C
ATOM    631  OD1 ASN H  82A     57.039 200.779  20.596  1.00 85.63           O
ANISOU  631  OD1 ASN H  82A   13768  10983   7786   3801  -3837    668       O
ATOM    632  ND2 ASN H  82A     56.820 198.574  20.916  1.00 80.18           N
ANISOU  632  ND2 ASN H  82A   12214  10785   7466   3386  -3678    371       N
ATOM    633  N   SER H  82B     53.849 201.946  24.214  1.00 67.09           N
ANISOU  633  N   SER H  82B    9746   8974   6772   4793  -3853    152       N
ATOM    634  CA  SER H  82B     52.706 202.215  25.109  1.00 69.17           C
ANISOU  634  CA  SER H  82B    9446   9410   7426   5150  -3877    -52       C
ATOM    635  C   SER H  82B     53.168 202.613  26.531  1.00 68.58           C
ANISOU  635  C   SER H  82B    9356   9230   7472   5057  -3395    -48       C
ATOM    636  O   SER H  82B     52.663 202.084  27.526  1.00 66.55           O
ANISOU  636  O   SER H  82B    8517   9235   7536   4999  -3137   -217       O
ATOM    637  CB  SER H  82B     51.754 201.014  25.149  1.00 74.30           C
ANISOU  637  CB  SER H  82B    9302  10502   8426   5065  -3956   -286       C
ATOM    638  OG  SER H  82B     51.397 200.581  23.845  1.00 87.40           O
ANISOU  638  OG  SER H  82B   11001  12253   9956   5108  -4418   -308       O
ATOM    639  N   LEU H  82C     54.155 203.530  26.611  1.00 63.46           N
ANISOU  639  N   LEU H  82C    9376   8190   6545   5014  -3272    146       N
ATOM    640  CA  LEU H  82C     54.747 203.983  27.872  1.00 60.68           C
ANISOU  640  CA  LEU H  82C    9130   7682   6244   4903  -2866    159       C
ATOM    641  C   LEU H  82C     53.755 204.706  28.773  1.00 67.93           C
ANISOU  641  C   LEU H  82C    9773   8626   7410   5369  -2863    -21       C
ATOM    642  O   LEU H  82C     53.011 205.572  28.316  1.00 72.46           O
ANISOU  642  O   LEU H  82C   10479   9073   7979   5869  -3216    -52       O
ATOM    643  CB  LEU H  82C     56.010 204.829  27.627  1.00 59.35           C
ANISOU  643  CB  LEU H  82C    9739   7076   5735   4727  -2788    397       C
ATOM    644  CG  LEU H  82C     57.252 204.047  27.183  1.00 59.73           C
ANISOU  644  CG  LEU H  82C    9971   7132   5593   4170  -2579    541       C
ATOM    645  CD1 LEU H  82C     58.137 204.881  26.290  1.00 60.90           C
ANISOU  645  CD1 LEU H  82C   10866   6902   5372   4084  -2669    782       C
ATOM    646  CD2 LEU H  82C     58.041 203.540  28.374  1.00 57.17           C
ANISOU  646  CD2 LEU H  82C    9458   6870   5393   3795  -2139    505       C
ATOM    647  N   ARG H  83      53.721 204.304  30.046  1.00 62.45           N
ANISOU  647  N   ARG H  83     8695   8108   6925   5220  -2464   -147       N
ATOM    648  CA  ARG H  83      52.822 204.841  31.071  1.00 65.08           C
ANISOU  648  CA  ARG H  83     8711   8522   7494   5611  -2342   -349       C
ATOM    649  C   ARG H  83      53.623 205.710  32.070  1.00 66.38           C
ANISOU  649  C   ARG H  83     9359   8349   7514   5578  -2059   -299       C
ATOM    650  O   ARG H  83      54.839 205.528  32.160  1.00 62.18           O
ANISOU  650  O   ARG H  83     9192   7647   6787   5139  -1884   -140       O
ATOM    651  CB  ARG H  83      52.115 203.679  31.808  1.00 65.72           C
ANISOU  651  CB  ARG H  83     8004   9071   7895   5442  -2064   -538       C
ATOM    652  CG  ARG H  83      51.416 202.684  30.877  1.00 79.16           C
ANISOU  652  CG  ARG H  83     9211  11104   9763   5370  -2330   -601       C
ATOM    653  CD  ARG H  83      50.250 201.978  31.544  1.00 94.63           C
ANISOU  653  CD  ARG H  83    10341  13498  12117   5420  -2155   -842       C
ATOM    654  NE  ARG H  83      49.604 201.027  30.635  1.00106.23           N
ANISOU  654  NE  ARG H  83    11341  15260  13762   5313  -2445   -918       N
ATOM    655  CZ  ARG H  83      49.881 199.728  30.594  1.00114.07           C
ANISOU  655  CZ  ARG H  83    12093  16438  14810   4804  -2295   -899       C
ATOM    656  NH1 ARG H  83      50.782 199.208  31.419  1.00 91.17           N
ANISOU  656  NH1 ARG H  83     9362  13470  11808   4379  -1863   -798       N
ATOM    657  NH2 ARG H  83      49.263 198.938  29.724  1.00102.81           N
ANISOU  657  NH2 ARG H  83    10278  15246  13540   4728  -2606   -989       N
ATOM    658  N   PRO H  84      52.999 206.643  32.844  1.00 65.21           N
ANISOU  658  N   PRO H  84     9218   8098   7462   6030  -2011   -452       N
ATOM    659  CA  PRO H  84      53.796 207.437  33.806  1.00 63.71           C
ANISOU  659  CA  PRO H  84     9525   7568   7115   5970  -1763   -426       C
ATOM    660  C   PRO H  84      54.519 206.582  34.860  1.00 62.25           C
ANISOU  660  C   PRO H  84     9187   7539   6926   5472  -1317   -433       C
ATOM    661  O   PRO H  84      55.495 207.034  35.457  1.00 60.65           O
ANISOU  661  O   PRO H  84     9445   7049   6548   5273  -1162   -366       O
ATOM    662  CB  PRO H  84      52.761 208.373  34.444  1.00 70.58           C
ANISOU  662  CB  PRO H  84    10297   8389   8130   6594  -1787   -649       C
ATOM    663  CG  PRO H  84      51.444 207.716  34.207  1.00 77.65           C
ANISOU  663  CG  PRO H  84    10416   9750   9337   6856  -1873   -831       C
ATOM    664  CD  PRO H  84      51.571 207.024  32.892  1.00 71.75           C
ANISOU  664  CD  PRO H  84     9603   9110   8548   6624  -2187   -677       C
ATOM    665  N   GLU H  85      54.054 205.333  35.052  1.00 56.18           N
ANISOU  665  N   GLU H  85     7793   7206   6347   5261  -1142   -511       N
ATOM    666  CA  GLU H  85      54.606 204.350  35.987  1.00 52.09           C
ANISOU  666  CA  GLU H  85     7098   6862   5831   4805   -751   -509       C
ATOM    667  C   GLU H  85      55.939 203.779  35.472  1.00 51.62           C
ANISOU  667  C   GLU H  85     7349   6675   5589   4291   -773   -295       C
ATOM    668  O   GLU H  85      56.692 203.178  36.241  1.00 48.61           O
ANISOU  668  O   GLU H  85     7001   6317   5151   3929   -506   -262       O
ATOM    669  CB  GLU H  85      53.593 203.209  36.225  1.00 54.38           C
ANISOU  669  CB  GLU H  85     6642   7626   6395   4747   -584   -647       C
ATOM    670  CG  GLU H  85      52.320 203.632  36.952  1.00 72.32           C
ANISOU  670  CG  GLU H  85     8503  10097   8880   5197   -442   -888       C
ATOM    671  CD  GLU H  85      51.255 204.317  36.111  1.00101.33           C
ANISOU  671  CD  GLU H  85    11971  13809  12720   5734   -817   -998       C
ATOM    672  OE1 GLU H  85      50.947 203.809  35.008  1.00 97.26           O
ANISOU  672  OE1 GLU H  85    11223  13432  12297   5684  -1129   -953       O
ATOM    673  OE2 GLU H  85      50.706 205.346  36.570  1.00 97.09           O
ANISOU  673  OE2 GLU H  85    11508  13161  12218   6227   -815  -1144       O
ATOM    674  N   ASP H  86      56.222 203.966  34.169  1.00 47.53           N
ANISOU  674  N   ASP H  86     7063   6027   4969   4280  -1091   -157       N
ATOM    675  CA  ASP H  86      57.446 203.505  33.519  1.00 43.09           C
ANISOU  675  CA  ASP H  86     6787   5354   4232   3839  -1111     32       C
ATOM    676  C   ASP H  86      58.612 204.491  33.692  1.00 45.06           C
ANISOU  676  C   ASP H  86     7670   5189   4261   3718  -1085    159       C
ATOM    677  O   ASP H  86      59.736 204.160  33.314  1.00 41.63           O
ANISOU  677  O   ASP H  86     7447   4670   3701   3328  -1037    298       O
ATOM    678  CB  ASP H  86      57.189 203.220  32.027  1.00 46.04           C
ANISOU  678  CB  ASP H  86     7143   5790   4559   3874  -1434    111       C
ATOM    679  CG  ASP H  86      56.243 202.065  31.755  1.00 54.84           C
ANISOU  679  CG  ASP H  86     7633   7308   5894   3870  -1486    -11       C
ATOM    680  OD1 ASP H  86      56.385 201.009  32.422  1.00 51.84           O
ANISOU  680  OD1 ASP H  86     6911   7147   5637   3566  -1220    -63       O
ATOM    681  OD2 ASP H  86      55.407 202.187  30.829  1.00 62.11           O
ANISOU  681  OD2 ASP H  86     8435   8307   6856   4151  -1819    -49       O
ATOM    682  N   THR H  87      58.348 205.697  34.266  1.00 44.50           N
ANISOU  682  N   THR H  87     7893   4857   4160   4049  -1112     96       N
ATOM    683  CA  THR H  87      59.371 206.726  34.528  1.00 44.06           C
ANISOU  683  CA  THR H  87     8452   4369   3920   3934  -1101    190       C
ATOM    684  C   THR H  87      60.391 206.162  35.514  1.00 43.56           C
ANISOU  684  C   THR H  87     8363   4348   3840   3504   -819    183       C
ATOM    685  O   THR H  87      60.038 205.860  36.659  1.00 42.97           O
ANISOU  685  O   THR H  87     8046   4432   3849   3563   -613     34       O
ATOM    686  CB  THR H  87      58.731 208.025  35.052  1.00 53.90           C
ANISOU  686  CB  THR H  87     9977   5339   5162   4412  -1187     76       C
ATOM    687  OG1 THR H  87      57.730 208.464  34.135  1.00 57.60           O
ANISOU  687  OG1 THR H  87    10426   5792   5666   4854  -1492     74       O
ATOM    688  CG2 THR H  87      59.756 209.135  35.271  1.00 52.62           C
ANISOU  688  CG2 THR H  87    10491   4681   4819   4273  -1209    167       C
ATOM    689  N   ALA H  88      61.641 205.971  35.048  1.00 36.50           N
ANISOU  689  N   ALA H  88     7699   3334   2835   3077   -806    341       N
ATOM    690  CA  ALA H  88      62.708 205.381  35.850  1.00 32.85           C
ANISOU  690  CA  ALA H  88     7193   2917   2370   2667   -600    340       C
ATOM    691  C   ALA H  88      64.079 205.523  35.194  1.00 33.77           C
ANISOU  691  C   ALA H  88     7616   2836   2378   2265   -622    503       C
ATOM    692  O   ALA H  88      64.171 205.811  33.998  1.00 32.66           O
ANISOU  692  O   ALA H  88     7676   2588   2147   2254   -754    638       O
ATOM    693  CB  ALA H  88      62.416 203.893  36.054  1.00 31.26           C
ANISOU  693  CB  ALA H  88     6453   3129   2294   2529   -460    289       C
ATOM    694  N   VAL H  89      65.151 205.256  35.985  1.00 28.46           N
ANISOU  694  N   VAL H  89     6958   2142   1714   1926   -487    486       N
ATOM    695  CA  VAL H  89      66.526 205.131  35.496  1.00 26.48           C
ANISOU  695  CA  VAL H  89     6835   1803   1424   1495   -455    604       C
ATOM    696  C   VAL H  89      66.624 203.648  35.134  1.00 27.71           C
ANISOU  696  C   VAL H  89     6545   2325   1657   1333   -369    612       C
ATOM    697  O   VAL H  89      66.314 202.805  35.974  1.00 26.47           O
ANISOU  697  O   VAL H  89     6080   2388   1590   1354   -280    512       O
ATOM    698  CB  VAL H  89      67.600 205.533  36.546  1.00 29.54           C
ANISOU  698  CB  VAL H  89     7406   2002   1818   1236   -403    550       C
ATOM    699  CG1 VAL H  89      69.006 205.179  36.062  1.00 28.17           C
ANISOU  699  CG1 VAL H  89     7202   1833   1667    781   -347    642       C
ATOM    700  CG2 VAL H  89      67.515 207.012  36.880  1.00 32.35           C
ANISOU  700  CG2 VAL H  89     8252   1948   2092   1380   -505    528       C
ATOM    701  N   TYR H  90      66.964 203.338  33.873  1.00 24.22           N
ANISOU  701  N   TYR H  90     6106   1934   1161   1195   -394    728       N
ATOM    702  CA  TYR H  90      67.062 201.971  33.352  1.00 21.78           C
ANISOU  702  CA  TYR H  90     5432   1933    909   1059   -333    724       C
ATOM    703  C   TYR H  90      68.525 201.559  33.222  1.00 26.44           C
ANISOU  703  C   TYR H  90     6007   2529   1511    666   -213    768       C
ATOM    704  O   TYR H  90      69.319 202.281  32.617  1.00 27.28           O
ANISOU  704  O   TYR H  90     6396   2442   1529    481   -192    867       O
ATOM    705  CB  TYR H  90      66.341 201.850  31.995  1.00 23.41           C
ANISOU  705  CB  TYR H  90     5655   2217   1024   1219   -457    792       C
ATOM    706  CG  TYR H  90      64.828 201.845  32.088  1.00 25.99           C
ANISOU  706  CG  TYR H  90     5804   2658   1411   1606   -592    709       C
ATOM    707  CD1 TYR H  90      64.118 203.025  32.298  1.00 30.70           C
ANISOU  707  CD1 TYR H  90     6640   3048   1974   1926   -712    698       C
ATOM    708  CD2 TYR H  90      64.102 200.672  31.911  1.00 25.21           C
ANISOU  708  CD2 TYR H  90     5293   2866   1421   1657   -608    630       C
ATOM    709  CE1 TYR H  90      62.728 203.027  32.392  1.00 31.80           C
ANISOU  709  CE1 TYR H  90     6551   3324   2207   2308   -830    596       C
ATOM    710  CE2 TYR H  90      62.709 200.665  31.984  1.00 27.44           C
ANISOU  710  CE2 TYR H  90     5343   3281   1801   1987   -727    537       C
ATOM    711  CZ  TYR H  90      62.027 201.847  32.229  1.00 35.81           C
ANISOU  711  CZ  TYR H  90     6590   4171   2844   2324   -833    515       C
ATOM    712  OH  TYR H  90      60.657 201.855  32.311  1.00 37.60           O
ANISOU  712  OH  TYR H  90     6529   4556   3202   2675   -945    399       O
ATOM    713  N   TYR H  91      68.886 200.416  33.826  1.00 21.95           N
ANISOU  713  N   TYR H  91     5108   2170   1062    539   -131    689       N
ATOM    714  CA  TYR H  91      70.241 199.884  33.820  1.00 21.35           C
ANISOU  714  CA  TYR H  91     4928   2139   1044    220    -36    690       C
ATOM    715  C   TYR H  91      70.315 198.580  33.037  1.00 29.13           C
ANISOU  715  C   TYR H  91     5638   3369   2060    162     14    677       C
ATOM    716  O   TYR H  91      69.465 197.697  33.234  1.00 28.10           O
ANISOU  716  O   TYR H  91     5284   3406   1985    306    -14    618       O
ATOM    717  CB  TYR H  91      70.701 199.574  35.260  1.00 19.94           C
ANISOU  717  CB  TYR H  91     4633   1972    973    152    -27    594       C
ATOM    718  CG  TYR H  91      70.796 200.753  36.198  1.00 20.88           C
ANISOU  718  CG  TYR H  91     5032   1845   1058    178    -83    566       C
ATOM    719  CD1 TYR H  91      71.969 201.492  36.298  1.00 23.43           C
ANISOU  719  CD1 TYR H  91     5524   1979   1398    -82    -95    579       C
ATOM    720  CD2 TYR H  91      69.768 201.040  37.091  1.00 21.75           C
ANISOU  720  CD2 TYR H  91     5208   1924   1132    445   -113    499       C
ATOM    721  CE1 TYR H  91      72.082 202.551  37.195  1.00 25.44           C
ANISOU  721  CE1 TYR H  91     6063   1980   1621    -75   -175    530       C
ATOM    722  CE2 TYR H  91      69.877 202.086  38.009  1.00 23.77           C
ANISOU  722  CE2 TYR H  91     5752   1942   1337    487   -165    443       C
ATOM    723  CZ  TYR H  91      71.035 202.846  38.052  1.00 29.67           C
ANISOU  723  CZ  TYR H  91     6714   2468   2090    225   -215    457       C
ATOM    724  OH  TYR H  91      71.153 203.905  38.923  1.00 27.83           O
ANISOU  724  OH  TYR H  91     6804   1967   1803    251   -295    386       O
ATOM    725  N   CYS H  92      71.358 198.419  32.198  1.00 28.77           N
ANISOU  725  N   CYS H  92     5599   3343   1990    -65    108    716       N
ATOM    726  CA  CYS H  92      71.593 197.128  31.563  1.00 29.03           C
ANISOU  726  CA  CYS H  92     5381   3593   2057   -118    169    669       C
ATOM    727  C   CYS H  92      72.603 196.383  32.430  1.00 28.38           C
ANISOU  727  C   CYS H  92     5055   3580   2146   -268    218    582       C
ATOM    728  O   CYS H  92      73.576 196.977  32.918  1.00 28.71           O
ANISOU  728  O   CYS H  92     5141   3520   2249   -438    246    580       O
ATOM    729  CB  CYS H  92      72.044 197.238  30.105  1.00 32.60           C
ANISOU  729  CB  CYS H  92     5968   4062   2358   -229    265    735       C
ATOM    730  SG  CYS H  92      73.552 198.214  29.846  1.00 40.04           S
ANISOU  730  SG  CYS H  92     7083   4850   3278   -558    442    811       S
ATOM    731  N   VAL H  93      72.304 195.119  32.722  1.00 20.10           N
ANISOU  731  N   VAL H  93     3769   2684   1185   -196    193    506       N
ATOM    732  CA  VAL H  93      73.146 194.284  33.571  1.00 18.21           C
ANISOU  732  CA  VAL H  93     3326   2496   1097   -279    192    427       C
ATOM    733  C   VAL H  93      73.549 193.086  32.750  1.00 20.59           C
ANISOU  733  C   VAL H  93     3441   2941   1441   -307    250    366       C
ATOM    734  O   VAL H  93      72.713 192.508  32.065  1.00 19.43           O
ANISOU  734  O   VAL H  93     3281   2868   1234   -208    235    358       O
ATOM    735  CB  VAL H  93      72.425 193.848  34.878  1.00 20.12           C
ANISOU  735  CB  VAL H  93     3526   2730   1386   -158    107    400       C
ATOM    736  CG1 VAL H  93      73.389 193.165  35.846  1.00 19.74           C
ANISOU  736  CG1 VAL H  93     3360   2685   1455   -233     58    339       C
ATOM    737  CG2 VAL H  93      71.728 195.025  35.549  1.00 20.14           C
ANISOU  737  CG2 VAL H  93     3737   2606   1309    -61     72    438       C
ATOM    738  N   GLY H  94      74.820 192.721  32.837  1.00 16.15           N
ANISOU  738  N   GLY H  94     2727   2417    993   -429    300    302       N
ATOM    739  CA  GLY H  94      75.366 191.575  32.141  1.00 15.13           C
ANISOU  739  CA  GLY H  94     2415   2413    923   -429    366    212       C
ATOM    740  C   GLY H  94      76.149 190.704  33.086  1.00 17.88           C
ANISOU  740  C   GLY H  94     2561   2776   1458   -413    282    122       C
ATOM    741  O   GLY H  94      76.770 191.208  34.013  1.00 17.93           O
ANISOU  741  O   GLY H  94     2543   2722   1547   -477    209    120       O
ATOM    742  N   GLY H  95      76.125 189.404  32.842  1.00 13.06           N
ANISOU  742  N   GLY H  95     1834   2225    902   -319    264     41       N
ATOM    743  CA  GLY H  95      76.880 188.431  33.610  1.00 12.11           C
ANISOU  743  CA  GLY H  95     1551   2097    951   -259    159    -48       C
ATOM    744  C   GLY H  95      77.186 187.205  32.786  1.00 17.04           C
ANISOU  744  C   GLY H  95     2057   2789   1628   -173    208   -166       C
ATOM    745  O   GLY H  95      76.322 186.741  32.034  1.00 16.12           O
ANISOU  745  O   GLY H  95     2035   2683   1405   -130    243   -167       O
ATOM    746  N   TYR H  96      78.424 186.675  32.900  1.00 15.25           N
ANISOU  746  N   TYR H  96     1615   2606   1572   -134    195   -286       N
ATOM    747  CA  TYR H  96      78.801 185.451  32.192  1.00 15.75           C
ANISOU  747  CA  TYR H  96     1573   2713   1700     -5    235   -430       C
ATOM    748  C   TYR H  96      77.820 184.357  32.576  1.00 20.26           C
ANISOU  748  C   TYR H  96     2302   3151   2245    106     85   -410       C
ATOM    749  O   TYR H  96      77.552 184.138  33.763  1.00 19.64           O
ANISOU  749  O   TYR H  96     2300   2955   2208    136    -83   -337       O
ATOM    750  CB  TYR H  96      80.247 185.018  32.506  1.00 18.32           C
ANISOU  750  CB  TYR H  96     1612   3094   2255     75    197   -576       C
ATOM    751  CG  TYR H  96      80.578 183.658  31.932  1.00 20.30           C
ANISOU  751  CG  TYR H  96     1785   3347   2582    270    205   -742       C
ATOM    752  CD1 TYR H  96      80.812 183.491  30.569  1.00 23.36           C
ANISOU  752  CD1 TYR H  96     2121   3860   2896    278    448   -858       C
ATOM    753  CD2 TYR H  96      80.590 182.523  32.741  1.00 21.08           C
ANISOU  753  CD2 TYR H  96     1927   3293   2791    454    -32   -778       C
ATOM    754  CE1 TYR H  96      81.063 182.231  30.026  1.00 25.55           C
ANISOU  754  CE1 TYR H  96     2370   4116   3223    480    454  -1034       C
ATOM    755  CE2 TYR H  96      80.833 181.255  32.207  1.00 23.54           C
ANISOU  755  CE2 TYR H  96     2223   3555   3168    650    -43   -936       C
ATOM    756  CZ  TYR H  96      81.078 181.115  30.849  1.00 30.60           C
ANISOU  756  CZ  TYR H  96     3043   4580   4002    670    200  -1078       C
ATOM    757  OH  TYR H  96      81.345 179.874  30.321  1.00 31.40           O
ANISOU  757  OH  TYR H  96     3151   4617   4160    885    188  -1262       O
ATOM    758  N   SER H  97      77.269 183.693  31.570  1.00 17.99           N
ANISOU  758  N   SER H  97     2089   2874   1871    145    152   -473       N
ATOM    759  CA  SER H  97      76.262 182.666  31.761  1.00 17.13           C
ANISOU  759  CA  SER H  97     2129   2633   1748    194     29   -463       C
ATOM    760  C   SER H  97      76.515 181.479  30.851  1.00 22.70           C
ANISOU  760  C   SER H  97     2835   3313   2477    307     46   -637       C
ATOM    761  O   SER H  97      76.892 181.661  29.699  1.00 25.15           O
ANISOU  761  O   SER H  97     3107   3748   2702    317    203   -740       O
ATOM    762  CB  SER H  97      74.883 183.254  31.480  1.00 19.26           C
ANISOU  762  CB  SER H  97     2533   2922   1863     90     46   -352       C
ATOM    763  OG  SER H  97      73.869 182.281  31.643  1.00 31.65           O
ANISOU  763  OG  SER H  97     4199   4380   3447     89    -57   -351       O
ATOM    764  N   ASN H  98      76.299 180.265  31.360  1.00 19.01           N
ANISOU  764  N   ASN H  98     2454   2666   2104    391   -107   -672       N
ATOM    765  CA  ASN H  98      76.413 179.044  30.565  1.00 20.24           C
ANISOU  765  CA  ASN H  98     2672   2736   2284    508   -126   -849       C
ATOM    766  C   ASN H  98      75.107 178.240  30.660  1.00 22.09           C
ANISOU  766  C   ASN H  98     3111   2793   2488    420   -249   -805       C
ATOM    767  O   ASN H  98      75.034 177.113  30.175  1.00 23.32           O
ANISOU  767  O   ASN H  98     3378   2808   2673    490   -314   -943       O
ATOM    768  CB  ASN H  98      77.661 178.214  30.936  1.00 25.32           C
ANISOU  768  CB  ASN H  98     3217   3295   3110    725   -200   -983       C
ATOM    769  CG  ASN H  98      77.691 177.624  32.332  1.00 48.25           C
ANISOU  769  CG  ASN H  98     6216   5983   6135    784   -424   -882       C
ATOM    770  OD1 ASN H  98      76.681 177.535  33.042  1.00 39.52           O
ANISOU  770  OD1 ASN H  98     5294   4748   4973    652   -507   -720       O
ATOM    771  ND2 ASN H  98      78.863 177.158  32.734  1.00 43.99           N
ANISOU  771  ND2 ASN H  98     5558   5399   5757    998   -526   -985       N
ATOM    772  N   PHE H  99      74.079 178.842  31.291  1.00 16.12           N
ANISOU  772  N   PHE H  99     2395   2046   1684    260   -271   -627       N
ATOM    773  CA  PHE H  99      72.743 178.273  31.442  1.00 15.68           C
ANISOU  773  CA  PHE H  99     2461   1873   1624    123   -349   -572       C
ATOM    774  C   PHE H  99      71.710 179.386  31.454  1.00 20.48           C
ANISOU  774  C   PHE H  99     3009   2636   2138    -10   -292   -450       C
ATOM    775  O   PHE H  99      71.539 180.060  32.469  1.00 20.24           O
ANISOU  775  O   PHE H  99     2955   2626   2111    -52   -265   -304       O
ATOM    776  CB  PHE H  99      72.619 177.406  32.720  1.00 17.28           C
ANISOU  776  CB  PHE H  99     2795   1837   1933     97   -455   -474       C
ATOM    777  CG  PHE H  99      71.265 176.738  32.865  1.00 17.54           C
ANISOU  777  CG  PHE H  99     2933   1743   1988    -97   -495   -423       C
ATOM    778  CD1 PHE H  99      70.994 175.529  32.228  1.00 19.87           C
ANISOU  778  CD1 PHE H  99     3352   1859   2341   -126   -585   -555       C
ATOM    779  CD2 PHE H  99      70.253 177.334  33.612  1.00 16.62           C
ANISOU  779  CD2 PHE H  99     2777   1692   1847   -259   -430   -262       C
ATOM    780  CE1 PHE H  99      69.738 174.931  32.333  1.00 20.87           C
ANISOU  780  CE1 PHE H  99     3540   1870   2517   -356   -621   -519       C
ATOM    781  CE2 PHE H  99      68.988 176.744  33.695  1.00 19.74           C
ANISOU  781  CE2 PHE H  99     3198   2008   2296   -468   -435   -231       C
ATOM    782  CZ  PHE H  99      68.743 175.541  33.063  1.00 19.05           C
ANISOU  782  CZ  PHE H  99     3215   1738   2284   -536   -537   -355       C
ATOM    783  N   TYR H 100      71.021 179.561  30.320  1.00 18.45           N
ANISOU  783  N   TYR H 100     2746   2479   1787    -51   -294   -526       N
ATOM    784  CA  TYR H 100      69.945 180.525  30.086  1.00 17.46           C
ANISOU  784  CA  TYR H 100     2562   2496   1576   -129   -289   -447       C
ATOM    785  C   TYR H 100      70.214 181.930  30.653  1.00 20.63           C
ANISOU  785  C   TYR H 100     2910   3008   1922   -102   -194   -308       C
ATOM    786  O   TYR H 100      71.048 182.648  30.103  1.00 20.43           O
ANISOU  786  O   TYR H 100     2890   3069   1803    -41   -115   -325       O
ATOM    787  CB  TYR H 100      68.591 179.959  30.567  1.00 18.46           C
ANISOU  787  CB  TYR H 100     2656   2554   1803   -275   -369   -408       C
ATOM    788  CG  TYR H 100      68.091 178.834  29.685  1.00 20.81           C
ANISOU  788  CG  TYR H 100     3009   2765   2133   -340   -495   -565       C
ATOM    789  CD1 TYR H 100      67.306 179.095  28.565  1.00 23.63           C
ANISOU  789  CD1 TYR H 100     3331   3244   2402   -359   -595   -657       C
ATOM    790  CD2 TYR H 100      68.430 177.511  29.950  1.00 22.27           C
ANISOU  790  CD2 TYR H 100     3315   2723   2424   -369   -546   -634       C
ATOM    791  CE1 TYR H 100      66.858 178.065  27.737  1.00 25.84           C
ANISOU  791  CE1 TYR H 100     3682   3435   2700   -427   -746   -827       C
ATOM    792  CE2 TYR H 100      67.993 176.473  29.127  1.00 24.93           C
ANISOU  792  CE2 TYR H 100     3739   2943   2789   -437   -677   -799       C
ATOM    793  CZ  TYR H 100      67.201 176.755  28.023  1.00 31.44           C
ANISOU  793  CZ  TYR H 100     4514   3906   3526   -478   -778   -904       C
ATOM    794  OH  TYR H 100      66.765 175.749  27.195  1.00 31.31           O
ANISOU  794  OH  TYR H 100     4600   3770   3525   -554   -942  -1090       O
ATOM    795  N   TYR H 100A     69.498 182.323  31.724  1.00 17.83           N
ANISOU  795  N   TYR H 100A    2519   2640   1616   -160   -185   -181       N
ATOM    796  CA  TYR H 100A     69.599 183.658  32.323  1.00 16.88           C
ANISOU  796  CA  TYR H 100A    2385   2591   1436   -130   -115    -66       C
ATOM    797  C   TYR H 100A     70.423 183.689  33.620  1.00 19.39           C
ANISOU  797  C   TYR H 100A    2744   2821   1803   -118    -90      4       C
ATOM    798  O   TYR H 100A     70.584 184.762  34.198  1.00 18.83           O
ANISOU  798  O   TYR H 100A    2690   2783   1681    -99    -49     79       O
ATOM    799  CB  TYR H 100A     68.188 184.241  32.598  1.00 18.31           C
ANISOU  799  CB  TYR H 100A    2501   2844   1613   -160   -116      0       C
ATOM    800  CG  TYR H 100A     67.189 184.081  31.471  1.00 20.71           C
ANISOU  800  CG  TYR H 100A    2737   3234   1899   -168   -209    -78       C
ATOM    801  CD1 TYR H 100A     67.193 184.946  30.381  1.00 22.29           C
ANISOU  801  CD1 TYR H 100A    2984   3528   1956    -81   -251    -98       C
ATOM    802  CD2 TYR H 100A     66.201 183.103  31.524  1.00 22.91           C
ANISOU  802  CD2 TYR H 100A    2919   3490   2296   -277   -272   -128       C
ATOM    803  CE1 TYR H 100A     66.248 184.830  29.362  1.00 23.09           C
ANISOU  803  CE1 TYR H 100A    3049   3708   2017    -64   -392   -174       C
ATOM    804  CE2 TYR H 100A     65.252 182.977  30.510  1.00 24.96           C
ANISOU  804  CE2 TYR H 100A    3092   3837   2555   -290   -408   -222       C
ATOM    805  CZ  TYR H 100A     65.281 183.842  29.430  1.00 29.67           C
ANISOU  805  CZ  TYR H 100A    3746   4536   2992   -165   -486   -249       C
ATOM    806  OH  TYR H 100A     64.356 183.703  28.427  1.00 31.85           O
ANISOU  806  OH  TYR H 100A    3963   4895   3244   -155   -672   -348       O
ATOM    807  N   TYR H 100B     70.915 182.533  34.095  1.00 14.70           N
ANISOU  807  N   TYR H 100B    2196   2092   1295   -116   -144    -24       N
ATOM    808  CA  TYR H 100B     71.673 182.483  35.348  1.00 13.77           C
ANISOU  808  CA  TYR H 100B    2150   1878   1205    -81   -179     41       C
ATOM    809  C   TYR H 100B     73.058 183.125  35.249  1.00 20.14           C
ANISOU  809  C   TYR H 100B    2891   2738   2024     -1   -191     -6       C
ATOM    810  O   TYR H 100B     73.757 182.940  34.263  1.00 22.44           O
ANISOU  810  O   TYR H 100B    3094   3086   2347     44   -168   -118       O
ATOM    811  CB  TYR H 100B     71.770 181.039  35.882  1.00 14.59           C
ANISOU  811  CB  TYR H 100B    2369   1788   1386    -80   -267     37       C
ATOM    812  CG  TYR H 100B     72.376 180.956  37.262  1.00 13.96           C
ANISOU  812  CG  TYR H 100B    2423   1589   1292    -32   -343    126       C
ATOM    813  CD1 TYR H 100B     71.635 181.292  38.392  1.00 15.42           C
ANISOU  813  CD1 TYR H 100B    2733   1744   1382   -109   -287    264       C
ATOM    814  CD2 TYR H 100B     73.709 180.602  37.439  1.00 14.57           C
ANISOU  814  CD2 TYR H 100B    2499   1599   1439    109   -476     60       C
ATOM    815  CE1 TYR H 100B     72.209 181.279  39.662  1.00 14.09           C
ANISOU  815  CE1 TYR H 100B    2743   1465   1145    -55   -376    344       C
ATOM    816  CE2 TYR H 100B     74.287 180.572  38.704  1.00 15.44           C
ANISOU  816  CE2 TYR H 100B    2746   1601   1519    174   -604    134       C
ATOM    817  CZ  TYR H 100B     73.534 180.919  39.811  1.00 19.85           C
ANISOU  817  CZ  TYR H 100B    3486   2117   1940     88   -561    282       C
ATOM    818  OH  TYR H 100B     74.090 180.882  41.060  1.00 24.20           O
ANISOU  818  OH  TYR H 100B    4231   2554   2410    158   -705    353       O
ATOM    819  N   TYR H 100C     73.442 183.877  36.283  1.00 16.25           N
ANISOU  819  N   TYR H 100C    2439   2232   1505      3   -218     67       N
ATOM    820  CA  TYR H 100C     74.740 184.544  36.419  1.00 15.28           C
ANISOU  820  CA  TYR H 100C    2230   2151   1426     36   -257     23       C
ATOM    821  C   TYR H 100C     75.067 184.662  37.901  1.00 18.98           C
ANISOU  821  C   TYR H 100C    2814   2520   1876     62   -387     88       C
ATOM    822  O   TYR H 100C     74.154 184.613  38.724  1.00 17.54           O
ANISOU  822  O   TYR H 100C    2800   2269   1595     36   -375    187       O
ATOM    823  CB  TYR H 100C     74.727 185.940  35.749  1.00 15.47           C
ANISOU  823  CB  TYR H 100C    2206   2292   1380    -35   -140     36       C
ATOM    824  CG  TYR H 100C     73.734 186.938  36.321  1.00 16.02           C
ANISOU  824  CG  TYR H 100C    2404   2350   1333    -72   -106    143       C
ATOM    825  CD1 TYR H 100C     72.363 186.792  36.110  1.00 17.03           C
ANISOU  825  CD1 TYR H 100C    2573   2498   1401    -71    -51    186       C
ATOM    826  CD2 TYR H 100C     74.171 188.079  36.995  1.00 16.94           C
ANISOU  826  CD2 TYR H 100C    2582   2442   1413   -102   -130    176       C
ATOM    827  CE1 TYR H 100C     71.446 187.706  36.632  1.00 17.18           C
ANISOU  827  CE1 TYR H 100C    2672   2523   1334    -62     -7    258       C
ATOM    828  CE2 TYR H 100C     73.264 189.005  37.517  1.00 17.16           C
ANISOU  828  CE2 TYR H 100C    2749   2444   1329    -97    -93    248       C
ATOM    829  CZ  TYR H 100C     71.901 188.820  37.325  1.00 22.01           C
ANISOU  829  CZ  TYR H 100C    3380   3093   1891    -59    -20    287       C
ATOM    830  OH  TYR H 100C     71.000 189.748  37.799  1.00 19.39           O
ANISOU  830  OH  TYR H 100C    3147   2753   1469    -13     31    333       O
ATOM    831  N   THR H 100D     76.366 184.767  38.241  1.00 16.98           N
ANISOU  831  N   THR H 100D    2468   2266   1716    114   -512     21       N
ATOM    832  CA  THR H 100D     76.838 184.990  39.609  1.00 17.63           C
ANISOU  832  CA  THR H 100D    2670   2261   1765    148   -693     59       C
ATOM    833  C   THR H 100D     77.380 186.422  39.665  1.00 23.24           C
ANISOU  833  C   THR H 100D    3304   3051   2477     58   -685     34       C
ATOM    834  O   THR H 100D     76.689 187.311  40.147  1.00 23.20           O
ANISOU  834  O   THR H 100D    3461   3022   2331     -2   -634    109       O
ATOM    835  CB  THR H 100D     77.812 183.892  40.075  1.00 21.91           C
ANISOU  835  CB  THR H 100D    3192   2709   2423    298   -917     -3       C
ATOM    836  OG1 THR H 100D     78.997 183.922  39.287  1.00 20.22           O
ANISOU  836  OG1 THR H 100D    2669   2609   2405    344   -935   -155       O
ATOM    837  CG2 THR H 100D     77.194 182.503  40.034  1.00 19.55           C
ANISOU  837  CG2 THR H 100D    3047   2271   2110    364   -923     38       C
ATOM    838  N   MET H 100E     78.554 186.667  39.074  1.00 21.72           N
ANISOU  838  N   MET H 100E    2855   2950   2447     36   -704    -79       N
ATOM    839  CA  MET H 100E     79.127 188.004  38.993  1.00 22.36           C
ANISOU  839  CA  MET H 100E    2851   3089   2557   -106   -675   -106       C
ATOM    840  C   MET H 100E     78.511 188.781  37.835  1.00 21.40           C
ANISOU  840  C   MET H 100E    2738   3035   2359   -221   -420    -61       C
ATOM    841  O   MET H 100E     78.068 188.179  36.853  1.00 19.87           O
ANISOU  841  O   MET H 100E    2505   2897   2147   -183   -284    -65       O
ATOM    842  CB  MET H 100E     80.636 187.925  38.850  1.00 28.24           C
ANISOU  842  CB  MET H 100E    3280   3919   3533   -115   -775   -249       C
ATOM    843  CG  MET H 100E     81.332 187.800  40.169  1.00 36.13           C
ANISOU  843  CG  MET H 100E    4301   4843   4585    -48  -1095   -290       C
ATOM    844  SD  MET H 100E     83.026 187.199  40.000  1.00 46.10           S
ANISOU  844  SD  MET H 100E    5116   6223   6177     44  -1273   -491       S
ATOM    845  CE  MET H 100E     82.711 185.476  39.466  1.00 42.69           C
ANISOU  845  CE  MET H 100E    4700   5754   5766    303  -1242   -508       C
ATOM    846  N   ASP H 101      78.478 190.114  37.948  1.00 15.80           N
ANISOU  846  N   ASP H 101     2120   2295   1587   -352   -382    -21       N
ATOM    847  CA  ASP H 101      77.865 190.960  36.937  1.00 14.56           C
ANISOU  847  CA  ASP H 101     2046   2158   1326   -439   -181     44       C
ATOM    848  C   ASP H 101      78.604 192.264  36.648  1.00 20.75           C
ANISOU  848  C   ASP H 101     2817   2921   2145   -636   -121     40       C
ATOM    849  O   ASP H 101      79.541 192.633  37.356  1.00 23.70           O
ANISOU  849  O   ASP H 101     3104   3265   2637   -728   -252    -24       O
ATOM    850  CB  ASP H 101      76.391 191.254  37.307  1.00 15.31           C
ANISOU  850  CB  ASP H 101     2396   2179   1242   -354   -165    145       C
ATOM    851  CG  ASP H 101      76.143 192.048  38.598  1.00 24.96           C
ANISOU  851  CG  ASP H 101     3826   3278   2379   -345   -277    173       C
ATOM    852  OD1 ASP H 101      77.116 192.636  39.145  1.00 25.15           O
ANISOU  852  OD1 ASP H 101     3837   3249   2468   -440   -394    121       O
ATOM    853  OD2 ASP H 101      74.971 192.153  39.008  1.00 26.65           O
ANISOU  853  OD2 ASP H 101     4207   3456   2464   -249   -240    232       O
ATOM    854  N   VAL H 102      78.134 192.974  35.617  1.00 16.35           N
ANISOU  854  N   VAL H 102     2376   2361   1476   -708     57    113       N
ATOM    855  CA  VAL H 102      78.599 194.280  35.181  1.00 17.90           C
ANISOU  855  CA  VAL H 102     2657   2487   1656   -916    154    153       C
ATOM    856  C   VAL H 102      77.362 195.151  34.920  1.00 22.11           C
ANISOU  856  C   VAL H 102     3523   2897   1981   -853    191    275       C
ATOM    857  O   VAL H 102      76.390 194.686  34.319  1.00 20.38           O
ANISOU  857  O   VAL H 102     3361   2733   1651   -705    239    318       O
ATOM    858  CB  VAL H 102      79.591 194.223  33.980  1.00 23.77           C
ANISOU  858  CB  VAL H 102     3191   3359   2482  -1085    367    113       C
ATOM    859  CG1 VAL H 102      78.969 193.559  32.743  1.00 23.17           C
ANISOU  859  CG1 VAL H 102     3148   3387   2268   -975    530    140       C
ATOM    860  CG2 VAL H 102      80.132 195.609  33.642  1.00 25.76           C
ANISOU  860  CG2 VAL H 102     3558   3507   2724  -1360    482    172       C
ATOM    861  N   TRP H 103      77.369 196.379  35.434  1.00 19.87           N
ANISOU  861  N   TRP H 103     3457   2436   1658   -941    133    313       N
ATOM    862  CA  TRP H 103      76.240 197.273  35.252  1.00 19.38           C
ANISOU  862  CA  TRP H 103     3717   2231   1416   -836    141    412       C
ATOM    863  C   TRP H 103      76.574 198.437  34.332  1.00 27.44           C
ANISOU  863  C   TRP H 103     4944   3116   2367  -1025    256    501       C
ATOM    864  O   TRP H 103      77.722 198.897  34.287  1.00 29.30           O
ANISOU  864  O   TRP H 103     5114   3307   2711  -1293    306    478       O
ATOM    865  CB  TRP H 103      75.764 197.806  36.608  1.00 17.44           C
ANISOU  865  CB  TRP H 103     3652   1839   1135   -732    -16    383       C
ATOM    866  CG  TRP H 103      75.070 196.794  37.464  1.00 16.54           C
ANISOU  866  CG  TRP H 103     3449   1826   1011   -525    -87    341       C
ATOM    867  CD1 TRP H 103      75.622 195.682  38.030  1.00 19.27           C
ANISOU  867  CD1 TRP H 103     3582   2283   1457   -525   -156    275       C
ATOM    868  CD2 TRP H 103      73.721 196.860  37.942  1.00 15.59           C
ANISOU  868  CD2 TRP H 103     3459   1675    789   -300    -91    353       C
ATOM    869  NE1 TRP H 103      74.687 195.024  38.795  1.00 18.15           N
ANISOU  869  NE1 TRP H 103     3482   2172   1243   -343   -186    279       N
ATOM    870  CE2 TRP H 103      73.510 195.726  38.762  1.00 19.28           C
ANISOU  870  CE2 TRP H 103     3810   2255   1262   -215   -126    325       C
ATOM    871  CE3 TRP H 103      72.657 197.749  37.733  1.00 16.83           C
ANISOU  871  CE3 TRP H 103     3838   1743    813   -150    -63    409       C
ATOM    872  CZ2 TRP H 103      72.280 195.468  39.385  1.00 17.84           C
ANISOU  872  CZ2 TRP H 103     3688   2100    990    -31    -88    334       C
ATOM    873  CZ3 TRP H 103      71.437 197.483  38.330  1.00 18.05           C
ANISOU  873  CZ3 TRP H 103     4000   1949    907     72    -45    393       C
ATOM    874  CH2 TRP H 103      71.263 196.367  39.168  1.00 17.91           C
ANISOU  874  CH2 TRP H 103     3839   2052    914    108    -36    356       C
ATOM    875  N   GLY H 104      75.559 198.921  33.622  1.00 24.41           N
ANISOU  875  N   GLY H 104     4815   2656   1804   -889    286    604       N
ATOM    876  CA  GLY H 104      75.678 200.119  32.803  1.00 26.81           C
ANISOU  876  CA  GLY H 104     5434   2766   1984  -1028    368    723       C
ATOM    877  C   GLY H 104      75.579 201.336  33.710  1.00 31.97           C
ANISOU  877  C   GLY H 104     6372   3139   2636  -1047    243    728       C
ATOM    878  O   GLY H 104      75.174 201.207  34.870  1.00 30.04           O
ANISOU  878  O   GLY H 104     6093   2882   2438   -893    105    639       O
ATOM    879  N   GLN H 105      75.946 202.523  33.207  1.00 30.81           N
ANISOU  879  N   GLN H 105     6545   2745   2415  -1240    297    829       N
ATOM    880  CA  GLN H 105      75.894 203.756  34.005  1.00 31.83           C
ANISOU  880  CA  GLN H 105     7006   2551   2537  -1273    169    824       C
ATOM    881  C   GLN H 105      74.455 204.195  34.353  1.00 34.15           C
ANISOU  881  C   GLN H 105     7572   2713   2691   -873     27    834       C
ATOM    882  O   GLN H 105      74.255 204.892  35.345  1.00 35.10           O
ANISOU  882  O   GLN H 105     7894   2626   2817   -797    -98    764       O
ATOM    883  CB  GLN H 105      76.697 204.894  33.328  1.00 36.81           C
ANISOU  883  CB  GLN H 105     7935   2916   3137  -1629    277    940       C
ATOM    884  CG  GLN H 105      76.029 205.533  32.091  1.00 53.69           C
ANISOU  884  CG  GLN H 105    10479   4889   5031  -1540    348   1132       C
ATOM    885  CD  GLN H 105      76.194 204.767  30.797  1.00 69.13           C
ANISOU  885  CD  GLN H 105    12288   7090   6888  -1599    549   1215       C
ATOM    886  OE1 GLN H 105      76.659 203.619  30.752  1.00 62.15           O
ANISOU  886  OE1 GLN H 105    10965   6529   6120  -1640    642   1118       O
ATOM    887  NE2 GLN H 105      75.809 205.404  29.704  1.00 61.91           N
ANISOU  887  NE2 GLN H 105    11786   6005   5733  -1585    608   1395       N
ATOM    888  N   GLY H 106      73.489 203.752  33.551  1.00 29.65           N
ANISOU  888  N   GLY H 106     6982   2277   2006   -616     44    898       N
ATOM    889  CA  GLY H 106      72.075 204.070  33.703  1.00 29.29           C
ANISOU  889  CA  GLY H 106     7099   2168   1860   -215    -81    896       C
ATOM    890  C   GLY H 106      71.624 205.168  32.760  1.00 35.27           C
ANISOU  890  C   GLY H 106     8306   2653   2444   -121   -130   1041       C
ATOM    891  O   GLY H 106      72.352 206.140  32.549  1.00 38.74           O
ANISOU  891  O   GLY H 106     9080   2798   2841   -361   -105   1123       O
ATOM    892  N   THR H 107      70.428 205.023  32.179  1.00 29.27           N
ANISOU  892  N   THR H 107     7566   1975   1583    220   -219   1075       N
ATOM    893  CA  THR H 107      69.847 206.033  31.300  1.00 31.28           C
ANISOU  893  CA  THR H 107     8270   1965   1651    395   -330   1212       C
ATOM    894  C   THR H 107      68.428 206.382  31.809  1.00 34.67           C
ANISOU  894  C   THR H 107     8730   2353   2090    887   -518   1126       C
ATOM    895  O   THR H 107      67.690 205.490  32.220  1.00 30.36           O
ANISOU  895  O   THR H 107     7783   2105   1647   1090   -531   1006       O
ATOM    896  CB  THR H 107      69.975 205.629  29.802  1.00 38.24           C
ANISOU  896  CB  THR H 107     9208   2958   2363    305   -275   1353       C
ATOM    897  OG1 THR H 107      69.776 206.772  28.969  1.00 43.79           O
ANISOU  897  OG1 THR H 107    10469   3321   2846    368   -364   1527       O
ATOM    898  CG2 THR H 107      69.041 204.500  29.389  1.00 33.50           C
ANISOU  898  CG2 THR H 107     8258   2703   1768    567   -354   1283       C
ATOM    899  N   THR H 108      68.072 207.683  31.829  1.00 36.27           N
ANISOU  899  N   THR H 108     9404   2177   2201   1071   -649   1177       N
ATOM    900  CA  THR H 108      66.773 208.122  32.351  1.00 37.33           C
ANISOU  900  CA  THR H 108     9563   2257   2362   1571   -815   1069       C
ATOM    901  C   THR H 108      65.697 208.215  31.266  1.00 42.97           C
ANISOU  901  C   THR H 108    10361   3000   2967   1940  -1011   1144       C
ATOM    902  O   THR H 108      65.909 208.827  30.222  1.00 45.66           O
ANISOU  902  O   THR H 108    11131   3100   3118   1895  -1097   1325       O
ATOM    903  CB  THR H 108      66.908 209.421  33.160  1.00 44.41           C
ANISOU  903  CB  THR H 108    10896   2731   3248   1639   -874   1025       C
ATOM    904  OG1 THR H 108      67.955 209.262  34.123  1.00 39.46           O
ANISOU  904  OG1 THR H 108    10172   2103   2718   1274   -733    942       O
ATOM    905  CG2 THR H 108      65.612 209.806  33.876  1.00 44.00           C
ANISOU  905  CG2 THR H 108    10810   2661   3248   2180   -995    863       C
ATOM    906  N   VAL H 109      64.535 207.599  31.547  1.00 38.56           N
ANISOU  906  N   VAL H 109     9387   2737   2527   2299  -1086   1001       N
ATOM    907  CA  VAL H 109      63.340 207.589  30.708  1.00 40.35           C
ANISOU  907  CA  VAL H 109     9561   3057   2714   2711  -1322   1008       C
ATOM    908  C   VAL H 109      62.248 208.326  31.486  1.00 48.70           C
ANISOU  908  C   VAL H 109    10616   4011   3876   3209  -1446    856       C
ATOM    909  O   VAL H 109      61.970 207.977  32.641  1.00 46.79           O
ANISOU  909  O   VAL H 109    10038   3942   3800   3264  -1295    680       O
ATOM    910  CB  VAL H 109      62.915 206.148  30.340  1.00 41.35           C
ANISOU  910  CB  VAL H 109     9121   3652   2937   2670  -1298    939       C
ATOM    911  CG1 VAL H 109      61.631 206.141  29.515  1.00 43.75           C
ANISOU  911  CG1 VAL H 109     9327   4070   3228   3096  -1591    915       C
ATOM    912  CG2 VAL H 109      64.032 205.423  29.597  1.00 39.08           C
ANISOU  912  CG2 VAL H 109     8849   3457   2543   2212  -1155   1059       C
ATOM    913  N   THR H 110      61.654 209.371  30.869  1.00 50.64           N
ANISOU  913  N   THR H 110    11271   3959   4009   3583  -1712    923       N
ATOM    914  CA  THR H 110      60.622 210.170  31.527  1.00 53.81           C
ANISOU  914  CA  THR H 110    11703   4231   4511   4116  -1845    765       C
ATOM    915  C   THR H 110      59.317 210.178  30.742  1.00 60.16           C
ANISOU  915  C   THR H 110    12337   5171   5350   4630  -2159    727       C
ATOM    916  O   THR H 110      59.320 210.454  29.545  1.00 63.17           O
ANISOU  916  O   THR H 110    13062   5396   5542   4684  -2402    902       O
ATOM    917  CB  THR H 110      61.132 211.591  31.851  1.00 66.28           C
ANISOU  917  CB  THR H 110    13973   5244   5968   4149  -1891    828       C
ATOM    918  OG1 THR H 110      62.525 211.562  32.176  1.00 67.80           O
ANISOU  918  OG1 THR H 110    14366   5296   6097   3572  -1666    919       O
ATOM    919  CG2 THR H 110      60.356 212.241  32.989  1.00 65.49           C
ANISOU  919  CG2 THR H 110    13844   5043   5999   4595  -1894    596       C
ATOM    920  N   VAL H 111      58.201 209.865  31.427  1.00 56.42           N
ANISOU  920  N   VAL H 111    11325   4998   5114   5002  -2151    492       N
ATOM    921  CA  VAL H 111      56.844 209.858  30.867  1.00 59.56           C
ANISOU  921  CA  VAL H 111    11424   5580   5627   5532  -2457    392       C
ATOM    922  C   VAL H 111      56.013 210.875  31.667  1.00 67.78           C
ANISOU  922  C   VAL H 111    12526   6439   6789   6096  -2520    205       C
ATOM    923  O   VAL H 111      55.929 210.758  32.896  1.00 66.83           O
ANISOU  923  O   VAL H 111    12143   6438   6809   6093  -2226     24       O
ATOM    924  CB  VAL H 111      56.192 208.445  30.884  1.00 60.96           C
ANISOU  924  CB  VAL H 111    10799   6336   6029   5448  -2375    253       C
ATOM    925  CG1 VAL H 111      54.881 208.442  30.109  1.00 64.91           C
ANISOU  925  CG1 VAL H 111    10996   7019   6648   5946  -2757    159       C
ATOM    926  CG2 VAL H 111      57.138 207.384  30.333  1.00 56.25           C
ANISOU  926  CG2 VAL H 111    10149   5899   5323   4869  -2243    398       C
ATOM    927  N   SER H 112      55.417 211.874  30.980  1.00 68.78           N
ANISOU  927  N   SER H 112    13033   6261   6839   6596  -2904    245       N
ATOM    928  CA  SER H 112      54.649 212.927  31.647  1.00 98.15           C
ANISOU  928  CA  SER H 112    16872   9754  10665   7191  -2995     59       C
ATOM    929  C   SER H 112      53.161 212.922  31.301  1.00136.03           C
ANISOU  929  C   SER H 112    21182  14817  15688   7845  -3301   -129       C
ATOM    930  O   SER H 112      52.748 213.385  30.239  1.00107.21           O
ANISOU  930  O   SER H 112    17804  10988  11943   8189  -3743    -28       O
ATOM    931  CB  SER H 112      55.269 214.293  31.375  1.00104.60           C
ANISOU  931  CB  SER H 112    18622   9891  11230   7273  -3172    232       C
ATOM    932  OG  SER H 112      55.321 214.555  29.982  1.00116.63           O
ANISOU  932  OG  SER H 112    20576  11201  12536   7321  -3542    477       O
TER     933      SER H 112
ATOM    934  N   GLU L   1      56.185 183.064  43.168  1.00 39.64           N
ANISOU  934  N   GLU L   1     3322   6138   5602   -552    465  -1119       N
ATOM    935  CA  GLU L   1      56.792 184.394  43.207  1.00 38.49           C
ANISOU  935  CA  GLU L   1     3299   5931   5396   -272    361   -996       C
ATOM    936  C   GLU L   1      57.573 184.645  44.529  1.00 39.18           C
ANISOU  936  C   GLU L   1     3634   5863   5389   -319    560   -867       C
ATOM    937  O   GLU L   1      56.958 184.844  45.592  1.00 40.38           O
ANISOU  937  O   GLU L   1     3693   6059   5590   -387    761   -954       O
ATOM    938  CB  GLU L   1      55.726 185.485  42.934  1.00 42.59           C
ANISOU  938  CB  GLU L   1     3515   6623   6045    -36    243  -1145       C
ATOM    939  CG  GLU L   1      56.248 186.921  42.931  1.00 59.20           C
ANISOU  939  CG  GLU L   1     5762   8644   8086    257    137  -1031       C
ATOM    940  CD  GLU L   1      57.407 187.252  41.999  1.00 85.64           C
ANISOU  940  CD  GLU L   1     9404  11852  11285    387    -57   -843       C
ATOM    941  OE1 GLU L   1      57.497 186.649  40.904  1.00 78.33           O
ANISOU  941  OE1 GLU L   1     8498  10942  10321    350   -206   -835       O
ATOM    942  OE2 GLU L   1      58.208 188.147  42.356  1.00 81.47           O
ANISOU  942  OE2 GLU L   1     9085  11196  10674    518    -51   -716       O
ATOM    943  N   ILE L   2      58.934 184.640  44.448  1.00 30.67           N
ANISOU  943  N   ILE L   2     2868   4610   4176   -283    501   -673       N
ATOM    944  CA  ILE L   2      59.804 184.808  45.621  1.00 27.54           C
ANISOU  944  CA  ILE L   2     2724   4062   3678   -323    634   -548       C
ATOM    945  C   ILE L   2      59.900 186.269  46.013  1.00 27.81           C
ANISOU  945  C   ILE L   2     2771   4091   3703   -113    612   -524       C
ATOM    946  O   ILE L   2      60.207 187.113  45.171  1.00 26.56           O
ANISOU  946  O   ILE L   2     2627   3928   3536     86    435   -477       O
ATOM    947  CB  ILE L   2      61.199 184.130  45.465  1.00 27.81           C
ANISOU  947  CB  ILE L   2     3043   3925   3600   -375    578   -386       C
ATOM    948  CG1 ILE L   2      61.051 182.641  45.100  1.00 28.07           C
ANISOU  948  CG1 ILE L   2     3087   3935   3641   -577    609   -421       C
ATOM    949  CG2 ILE L   2      62.040 184.303  46.751  1.00 26.52           C
ANISOU  949  CG2 ILE L   2     3123   3618   3336   -406    682   -276       C
ATOM    950  CD1 ILE L   2      62.256 182.025  44.445  1.00 36.13           C
ANISOU  950  CD1 ILE L   2     4308   4826   4594   -564    500   -306       C
ATOM    951  N   VAL L   3      59.621 186.557  47.296  1.00 22.35           N
ANISOU  951  N   VAL L   3     2107   3385   2999   -170    804   -559       N
ATOM    952  CA  VAL L   3      59.635 187.899  47.879  1.00 20.73           C
ANISOU  952  CA  VAL L   3     1935   3161   2782      4    824   -557       C
ATOM    953  C   VAL L   3      60.768 188.012  48.906  1.00 20.76           C
ANISOU  953  C   VAL L   3     2255   2994   2639    -55    893   -418       C
ATOM    954  O   VAL L   3      60.870 187.174  49.803  1.00 21.69           O
ANISOU  954  O   VAL L   3     2500   3054   2686   -252   1042   -402       O
ATOM    955  CB  VAL L   3      58.248 188.235  48.509  1.00 26.41           C
ANISOU  955  CB  VAL L   3     2396   4022   3617      4    995   -753       C
ATOM    956  CG1 VAL L   3      58.272 189.563  49.264  1.00 25.77           C
ANISOU  956  CG1 VAL L   3     2384   3894   3511    172   1052   -762       C
ATOM    957  CG2 VAL L   3      57.149 188.234  47.449  1.00 27.90           C
ANISOU  957  CG2 VAL L   3     2235   4396   3971    104    873   -910       C
ATOM    958  N   LEU L   4      61.602 189.050  48.780  1.00 14.09           N
ANISOU  958  N   LEU L   4     1552   2063   1741    108    777   -325       N
ATOM    959  CA  LEU L   4      62.676 189.324  49.732  1.00 12.69           C
ANISOU  959  CA  LEU L   4     1646   1740   1437     70    809   -216       C
ATOM    960  C   LEU L   4      62.275 190.497  50.605  1.00 17.54           C
ANISOU  960  C   LEU L   4     2284   2345   2036    162    911   -279       C
ATOM    961  O   LEU L   4      61.891 191.547  50.087  1.00 17.45           O
ANISOU  961  O   LEU L   4     2175   2366   2089    352    842   -325       O
ATOM    962  CB  LEU L   4      64.012 189.641  49.026  1.00 10.64           C
ANISOU  962  CB  LEU L   4     1529   1382   1130    149    630    -87       C
ATOM    963  CG  LEU L   4      64.574 188.614  48.077  1.00 12.40           C
ANISOU  963  CG  LEU L   4     1750   1598   1364     88    528    -29       C
ATOM    964  CD1 LEU L   4      65.837 189.128  47.453  1.00 11.71           C
ANISOU  964  CD1 LEU L   4     1785   1425   1239    162    398     67       C
ATOM    965  CD2 LEU L   4      64.822 187.300  48.764  1.00 11.74           C
ANISOU  965  CD2 LEU L   4     1761   1464   1235    -94    605     -4       C
ATOM    966  N   THR L   5      62.361 190.325  51.928  1.00 15.63           N
ANISOU  966  N   THR L   5     2201   2044   1695     33   1070   -281       N
ATOM    967  CA  THR L   5      61.994 191.371  52.873  1.00 16.66           C
ANISOU  967  CA  THR L   5     2384   2154   1790     98   1196   -353       C
ATOM    968  C   THR L   5      63.214 191.837  53.640  1.00 20.71           C
ANISOU  968  C   THR L   5     3202   2514   2152     81   1146   -245       C
ATOM    969  O   THR L   5      63.757 191.096  54.459  1.00 20.94           O
ANISOU  969  O   THR L   5     3431   2470   2056    -77   1187   -184       O
ATOM    970  CB  THR L   5      60.813 190.929  53.757  1.00 22.31           C
ANISOU  970  CB  THR L   5     3000   2956   2522    -34   1459   -498       C
ATOM    971  OG1 THR L   5      59.790 190.392  52.917  1.00 21.26           O
ANISOU  971  OG1 THR L   5     2549   2978   2550    -36   1470   -608       O
ATOM    972  CG2 THR L   5      60.239 192.075  54.575  1.00 21.09           C
ANISOU  972  CG2 THR L   5     2847   2803   2362     65   1607   -613       C
ATOM    973  N   GLN L   6      63.647 193.072  53.362  1.00 16.69           N
ANISOU  973  N   GLN L   6     2744   1948   1650    242   1045   -226       N
ATOM    974  CA  GLN L   6      64.802 193.677  54.010  1.00 14.88           C
ANISOU  974  CA  GLN L   6     2775   1583   1297    226    982   -149       C
ATOM    975  C   GLN L   6      64.413 194.405  55.268  1.00 21.41           C
ANISOU  975  C   GLN L   6     3733   2366   2036    220   1142   -231       C
ATOM    976  O   GLN L   6      63.295 194.924  55.367  1.00 23.08           O
ANISOU  976  O   GLN L   6     3807   2642   2320    312   1277   -357       O
ATOM    977  CB  GLN L   6      65.529 194.618  53.052  1.00 14.46           C
ANISOU  977  CB  GLN L   6     2739   1471   1284    361    814    -91       C
ATOM    978  CG  GLN L   6      66.329 193.875  52.004  1.00 12.20           C
ANISOU  978  CG  GLN L   6     2410   1192   1032    322    664      5       C
ATOM    979  CD  GLN L   6      67.183 194.787  51.177  1.00 30.88           C
ANISOU  979  CD  GLN L   6     4842   3484   3408    404    537     60       C
ATOM    980  OE1 GLN L   6      66.906 195.039  49.999  1.00 30.51           O
ANISOU  980  OE1 GLN L   6     4703   3465   3426    508    471     66       O
ATOM    981  NE2 GLN L   6      68.268 195.264  51.760  1.00 15.65           N
ANISOU  981  NE2 GLN L   6     3087   1455   1406    343    498     97       N
ATOM    982  N   SER L   7      65.334 194.437  56.246  1.00 17.78           N
ANISOU  982  N   SER L   7     3537   1798   1420    117   1123   -176       N
ATOM    983  CA  SER L   7      65.133 195.132  57.505  1.00 19.09           C
ANISOU  983  CA  SER L   7     3892   1900   1460     91   1263   -249       C
ATOM    984  C   SER L   7      66.470 195.555  58.122  1.00 25.01           C
ANISOU  984  C   SER L   7     4913   2520   2069     40   1121   -175       C
ATOM    985  O   SER L   7      67.459 194.819  58.021  1.00 24.01           O
ANISOU  985  O   SER L   7     4852   2366   1903    -39    963    -74       O
ATOM    986  CB  SER L   7      64.309 194.295  58.488  1.00 22.57           C
ANISOU  986  CB  SER L   7     4381   2382   1811    -60   1487   -313       C
ATOM    987  OG  SER L   7      65.008 193.146  58.927  1.00 29.58           O
ANISOU  987  OG  SER L   7     5447   3220   2574   -223   1421   -207       O
ATOM    988  N   PRO L   8      66.526 196.749  58.757  1.00 23.17           N
ANISOU  988  N   PRO L   8     4832   2205   1765     88   1168   -240       N
ATOM    989  CA  PRO L   8      65.445 197.736  58.907  1.00 24.45           C
ANISOU  989  CA  PRO L   8     4934   2375   1979    216   1344   -373       C
ATOM    990  C   PRO L   8      65.290 198.600  57.647  1.00 29.12           C
ANISOU  990  C   PRO L   8     5360   2966   2738    414   1246   -376       C
ATOM    991  O   PRO L   8      65.988 198.369  56.663  1.00 27.41           O
ANISOU  991  O   PRO L   8     5080   2751   2584    422   1071   -275       O
ATOM    992  CB  PRO L   8      65.886 198.517  60.145  1.00 26.81           C
ANISOU  992  CB  PRO L   8     5538   2551   2097    160   1391   -418       C
ATOM    993  CG  PRO L   8      67.377 198.525  60.055  1.00 29.61           C
ANISOU  993  CG  PRO L   8     6037   2826   2390     85   1148   -307       C
ATOM    994  CD  PRO L   8      67.774 197.224  59.389  1.00 24.01           C
ANISOU  994  CD  PRO L   8     5189   2195   1740     22   1027   -197       C
ATOM    995  N   ALA L   9      64.365 199.572  57.660  1.00 28.08           N
ANISOU  995  N   ALA L   9     5173   2823   2672    581   1360   -496       N
ATOM    996  CA  ALA L   9      64.174 200.491  56.531  1.00 27.23           C
ANISOU  996  CA  ALA L   9     4975   2677   2694    795   1253   -497       C
ATOM    997  C   ALA L   9      65.353 201.479  56.488  1.00 29.80           C
ANISOU  997  C   ALA L   9     5560   2825   2937    783   1125   -427       C
ATOM    998  O   ALA L   9      65.945 201.689  55.431  1.00 27.81           O
ANISOU  998  O   ALA L   9     5300   2533   2733    818    970   -336       O
ATOM    999  CB  ALA L   9      62.853 201.236  56.677  1.00 30.00           C
ANISOU  999  CB  ALA L   9     5208   3052   3139   1000   1400   -660       C
ATOM   1000  N   THR L  10      65.723 202.031  57.661  1.00 27.60           N
ANISOU 1000  N   THR L  10     5522   2442   2521    702   1201   -477       N
ATOM   1001  CA  THR L  10      66.842 202.959  57.826  1.00 27.61           C
ANISOU 1001  CA  THR L  10     5778   2277   2435    644   1099   -442       C
ATOM   1002  C   THR L  10      67.674 202.558  59.045  1.00 31.30           C
ANISOU 1002  C   THR L  10     6438   2722   2731    429   1091   -436       C
ATOM   1003  O   THR L  10      67.130 202.252  60.108  1.00 32.28           O
ANISOU 1003  O   THR L  10     6631   2878   2756    379   1238   -510       O
ATOM   1004  CB  THR L  10      66.357 204.435  57.906  1.00 36.59           C
ANISOU 1004  CB  THR L  10     7060   3262   3582    820   1170   -540       C
ATOM   1005  OG1 THR L  10      65.452 204.707  56.833  1.00 40.28           O
ANISOU 1005  OG1 THR L  10     7348   3755   4201   1054   1153   -551       O
ATOM   1006  CG2 THR L  10      67.507 205.434  57.848  1.00 31.58           C
ANISOU 1006  CG2 THR L  10     6687   2438   2874    743   1065   -503       C
ATOM   1007  N   LEU L  11      68.994 202.589  58.876  1.00 26.35           N
ANISOU 1007  N   LEU L  11     5903   2040   2068    303    918   -359       N
ATOM   1008  CA  LEU L  11      69.988 202.256  59.877  1.00 26.09           C
ANISOU 1008  CA  LEU L  11     6042   1984   1886    117    831   -349       C
ATOM   1009  C   LEU L  11      70.880 203.493  60.034  1.00 31.51           C
ANISOU 1009  C   LEU L  11     6930   2516   2525     61    753   -388       C
ATOM   1010  O   LEU L  11      71.656 203.798  59.130  1.00 31.94           O
ANISOU 1010  O   LEU L  11     6929   2539   2670     34    639   -338       O
ATOM   1011  CB  LEU L  11      70.787 201.047  59.341  1.00 24.64           C
ANISOU 1011  CB  LEU L  11     5706   1901   1753     28    668   -239       C
ATOM   1012  CG  LEU L  11      71.587 200.185  60.314  1.00 29.63           C
ANISOU 1012  CG  LEU L  11     6457   2553   2249   -121    550   -213       C
ATOM   1013  CD1 LEU L  11      70.691 199.493  61.331  1.00 30.93           C
ANISOU 1013  CD1 LEU L  11     6727   2750   2276   -146    698   -240       C
ATOM   1014  CD2 LEU L  11      72.382 199.140  59.559  1.00 28.99           C
ANISOU 1014  CD2 LEU L  11     6199   2554   2264   -157    383   -118       C
ATOM   1015  N   SER L  12      70.690 204.268  61.126  1.00 28.92           N
ANISOU 1015  N   SER L  12     6844   2084   2059     40    843   -492       N
ATOM   1016  CA  SER L  12      71.455 205.493  61.400  1.00 29.33           C
ANISOU 1016  CA  SER L  12     7121   1973   2051    -31    789   -553       C
ATOM   1017  C   SER L  12      72.640 205.183  62.316  1.00 34.37           C
ANISOU 1017  C   SER L  12     7896   2612   2550   -239    622   -564       C
ATOM   1018  O   SER L  12      72.454 204.900  63.501  1.00 34.59           O
ANISOU 1018  O   SER L  12     8093   2645   2405   -295    657   -614       O
ATOM   1019  CB  SER L  12      70.566 206.572  62.017  1.00 33.53           C
ANISOU 1019  CB  SER L  12     7851   2374   2516     80    976   -677       C
ATOM   1020  OG  SER L  12      69.472 206.896  61.176  1.00 41.04           O
ANISOU 1020  OG  SER L  12     8661   3320   3611    305   1091   -681       O
ATOM   1021  N   LEU L  13      73.859 205.198  61.755  1.00 30.84           N
ANISOU 1021  N   LEU L  13     7373   2169   2177   -354    438   -526       N
ATOM   1022  CA  LEU L  13      75.061 204.848  62.511  1.00 31.12           C
ANISOU 1022  CA  LEU L  13     7475   2230   2120   -531    231   -549       C
ATOM   1023  C   LEU L  13      76.208 205.836  62.330  1.00 34.54           C
ANISOU 1023  C   LEU L  13     7970   2565   2589   -678    121   -619       C
ATOM   1024  O   LEU L  13      76.218 206.632  61.389  1.00 32.71           O
ANISOU 1024  O   LEU L  13     7710   2248   2471   -660    199   -615       O
ATOM   1025  CB  LEU L  13      75.541 203.438  62.116  1.00 29.95           C
ANISOU 1025  CB  LEU L  13     7092   2239   2049   -542     80   -450       C
ATOM   1026  CG  LEU L  13      74.564 202.282  62.293  1.00 33.65           C
ANISOU 1026  CG  LEU L  13     7498   2804   2482   -444    171   -378       C
ATOM   1027  CD1 LEU L  13      74.913 201.172  61.387  1.00 32.22           C
ANISOU 1027  CD1 LEU L  13     7056   2740   2447   -420     71   -280       C
ATOM   1028  CD2 LEU L  13      74.520 201.797  63.731  1.00 34.79           C
ANISOU 1028  CD2 LEU L  13     7880   2942   2398   -509    132   -404       C
ATOM   1029  N   SER L  14      77.195 205.758  63.232  1.00 32.10           N
ANISOU 1029  N   SER L  14     7753   2265   2177   -835    -71   -686       N
ATOM   1030  CA  SER L  14      78.395 206.583  63.194  1.00 32.69           C
ANISOU 1030  CA  SER L  14     7855   2274   2290  -1019   -198   -781       C
ATOM   1031  C   SER L  14      79.523 205.772  62.538  1.00 35.44           C
ANISOU 1031  C   SER L  14     7898   2767   2801  -1096   -394   -750       C
ATOM   1032  O   SER L  14      79.458 204.537  62.564  1.00 33.54           O
ANISOU 1032  O   SER L  14     7514   2658   2573  -1013   -485   -670       O
ATOM   1033  CB  SER L  14      78.798 206.981  64.610  1.00 37.81           C
ANISOU 1033  CB  SER L  14     8774   2860   2732  -1141   -314   -902       C
ATOM   1034  OG  SER L  14      77.789 207.760  65.229  1.00 48.28           O
ANISOU 1034  OG  SER L  14    10389   4046   3909  -1073   -110   -953       O
ATOM   1035  N   PRO L  15      80.572 206.411  61.952  1.00 32.66           N
ANISOU 1035  N   PRO L  15     7442   2389   2577  -1261   -450   -824       N
ATOM   1036  CA  PRO L  15      81.674 205.615  61.382  1.00 32.04           C
ANISOU 1036  CA  PRO L  15     7042   2464   2668  -1333   -623   -827       C
ATOM   1037  C   PRO L  15      82.408 204.860  62.493  1.00 35.81           C
ANISOU 1037  C   PRO L  15     7498   3045   3063  -1366   -914   -886       C
ATOM   1038  O   PRO L  15      82.532 205.358  63.607  1.00 36.39           O
ANISOU 1038  O   PRO L  15     7810   3052   2964  -1439  -1005   -975       O
ATOM   1039  CB  PRO L  15      82.578 206.666  60.717  1.00 34.92           C
ANISOU 1039  CB  PRO L  15     7357   2755   3156  -1545   -578   -933       C
ATOM   1040  CG  PRO L  15      81.759 207.905  60.645  1.00 39.29           C
ANISOU 1040  CG  PRO L  15     8211   3099   3619  -1533   -355   -931       C
ATOM   1041  CD  PRO L  15      80.840 207.856  61.815  1.00 35.07           C
ANISOU 1041  CD  PRO L  15     7924   2520   2881  -1406   -349   -924       C
ATOM   1042  N   GLY L  16      82.832 203.647  62.186  1.00 31.70           N
ANISOU 1042  N   GLY L  16     6722   2674   2650  -1293  -1062   -834       N
ATOM   1043  CA  GLY L  16      83.501 202.778  63.138  1.00 32.80           C
ANISOU 1043  CA  GLY L  16     6842   2904   2716  -1274  -1371   -869       C
ATOM   1044  C   GLY L  16      82.570 201.744  63.731  1.00 36.31           C
ANISOU 1044  C   GLY L  16     7451   3355   2991  -1099  -1372   -736       C
ATOM   1045  O   GLY L  16      83.028 200.715  64.231  1.00 37.09           O
ANISOU 1045  O   GLY L  16     7516   3525   3050  -1033  -1616   -715       O
ATOM   1046  N   GLU L  17      81.252 202.012  63.678  1.00 31.60           N
ANISOU 1046  N   GLU L  17     7035   2675   2295  -1024  -1096   -655       N
ATOM   1047  CA  GLU L  17      80.220 201.123  64.218  1.00 30.60           C
ANISOU 1047  CA  GLU L  17     7071   2546   2008   -895  -1024   -545       C
ATOM   1048  C   GLU L  17      79.921 199.965  63.278  1.00 32.33           C
ANISOU 1048  C   GLU L  17     7052   2859   2374   -774   -982   -423       C
ATOM   1049  O   GLU L  17      80.261 200.020  62.098  1.00 32.63           O
ANISOU 1049  O   GLU L  17     6823   2947   2628   -771   -936   -415       O
ATOM   1050  CB  GLU L  17      78.932 201.903  64.559  1.00 31.65           C
ANISOU 1050  CB  GLU L  17     7450   2572   2004   -868   -735   -545       C
ATOM   1051  CG  GLU L  17      79.031 202.704  65.849  1.00 42.84           C
ANISOU 1051  CG  GLU L  17     9201   3887   3192   -965   -777   -655       C
ATOM   1052  CD  GLU L  17      77.911 203.688  66.149  1.00 69.80           C
ANISOU 1052  CD  GLU L  17    12842   7180   6499   -939   -486   -698       C
ATOM   1053  OE1 GLU L  17      78.144 204.607  66.968  1.00 74.07           O
ANISOU 1053  OE1 GLU L  17    13634   7617   6891  -1037   -507   -813       O
ATOM   1054  OE2 GLU L  17      76.798 203.530  65.597  1.00 65.02           O
ANISOU 1054  OE2 GLU L  17    12162   6584   5959   -815   -246   -631       O
ATOM   1055  N   ARG L  18      79.303 198.909  63.811  1.00 27.95           N
ANISOU 1055  N   ARG L  18     6619   2314   1687   -690   -989   -333       N
ATOM   1056  CA  ARG L  18      78.927 197.716  63.066  1.00 26.46           C
ANISOU 1056  CA  ARG L  18     6257   2193   1603   -586   -947   -221       C
ATOM   1057  C   ARG L  18      77.520 197.874  62.478  1.00 29.84           C
ANISOU 1057  C   ARG L  18     6669   2611   2057   -528   -624   -166       C
ATOM   1058  O   ARG L  18      76.576 198.229  63.192  1.00 30.38           O
ANISOU 1058  O   ARG L  18     6957   2620   1964   -532   -454   -180       O
ATOM   1059  CB  ARG L  18      79.000 196.481  63.973  1.00 26.91           C
ANISOU 1059  CB  ARG L  18     6494   2240   1490   -543  -1118   -156       C
ATOM   1060  CG  ARG L  18      78.458 195.192  63.337  1.00 40.05           C
ANISOU 1060  CG  ARG L  18     8049   3942   3227   -450  -1045    -39       C
ATOM   1061  CD  ARG L  18      78.521 194.005  64.289  1.00 55.95           C
ANISOU 1061  CD  ARG L  18    10315   5902   5042   -417  -1208     32       C
ATOM   1062  NE  ARG L  18      79.854 193.873  64.889  1.00 73.47           N
ANISOU 1062  NE  ARG L  18    12571   8117   7227   -402  -1581    -18       N
ATOM   1063  CZ  ARG L  18      80.907 193.338  64.277  1.00 89.63           C
ANISOU 1063  CZ  ARG L  18    14349  10229   9475   -326  -1813    -37       C
ATOM   1064  NH1 ARG L  18      80.793 192.851  63.048  1.00 73.20           N
ANISOU 1064  NH1 ARG L  18    11980   8213   7622   -269  -1698      2       N
ATOM   1065  NH2 ARG L  18      82.082 193.280  64.892  1.00 81.48           N
ANISOU 1065  NH2 ARG L  18    13332   9205   8421   -301  -2166   -110       N
ATOM   1066  N   ALA L  19      77.386 197.595  61.176  1.00 24.79           N
ANISOU 1066  N   ALA L  19     5763   2036   1622   -470   -546   -118       N
ATOM   1067  CA  ALA L  19      76.104 197.646  60.487  1.00 23.14           C
ANISOU 1067  CA  ALA L  19     5490   1838   1465   -396   -291    -74       C
ATOM   1068  C   ALA L  19      75.663 196.219  60.178  1.00 25.75           C
ANISOU 1068  C   ALA L  19     5730   2232   1822   -338   -279     16       C
ATOM   1069  O   ALA L  19      76.395 195.482  59.521  1.00 25.92           O
ANISOU 1069  O   ALA L  19     5577   2305   1967   -318   -413     51       O
ATOM   1070  CB  ALA L  19      76.221 198.464  59.201  1.00 22.44           C
ANISOU 1070  CB  ALA L  19     5214   1754   1557   -379   -216    -89       C
ATOM   1071  N   THR L  20      74.508 195.810  60.713  1.00 21.32           N
ANISOU 1071  N   THR L  20     5296   1660   1143   -324   -113     40       N
ATOM   1072  CA  THR L  20      73.937 194.489  60.467  1.00 20.73           C
ANISOU 1072  CA  THR L  20     5164   1629   1082   -301    -64    115       C
ATOM   1073  C   THR L  20      72.614 194.672  59.728  1.00 23.19           C
ANISOU 1073  C   THR L  20     5328   1994   1488   -249    183    104       C
ATOM   1074  O   THR L  20      71.649 195.215  60.279  1.00 23.58           O
ANISOU 1074  O   THR L  20     5475   2027   1456   -252    373     48       O
ATOM   1075  CB  THR L  20      73.849 193.646  61.772  1.00 33.47           C
ANISOU 1075  CB  THR L  20     7069   3181   2467   -362   -104    147       C
ATOM   1076  OG1 THR L  20      75.171 193.321  62.211  1.00 37.75           O
ANISOU 1076  OG1 THR L  20     7692   3688   2964   -366   -402    162       O
ATOM   1077  CG2 THR L  20      73.068 192.351  61.580  1.00 30.07           C
ANISOU 1077  CG2 THR L  20     6628   2768   2031   -369      5    217       C
ATOM   1078  N   LEU L  21      72.596 194.256  58.465  1.00 18.54           N
ANISOU 1078  N   LEU L  21     4496   1472   1074   -195    171    142       N
ATOM   1079  CA  LEU L  21      71.442 194.364  57.581  1.00 17.70           C
ANISOU 1079  CA  LEU L  21     4215   1432   1079   -128    345    128       C
ATOM   1080  C   LEU L  21      70.854 192.975  57.363  1.00 19.63           C
ANISOU 1080  C   LEU L  21     4387   1729   1342   -154    394    172       C
ATOM   1081  O   LEU L  21      71.599 192.012  57.201  1.00 17.43           O
ANISOU 1081  O   LEU L  21     4106   1441   1076   -178    254    232       O
ATOM   1082  CB  LEU L  21      71.868 194.978  56.243  1.00 17.17           C
ANISOU 1082  CB  LEU L  21     3965   1388   1172    -59    288    134       C
ATOM   1083  CG  LEU L  21      72.231 196.469  56.236  1.00 23.43           C
ANISOU 1083  CG  LEU L  21     4830   2110   1963    -38    289     84       C
ATOM   1084  CD1 LEU L  21      73.628 196.720  56.796  1.00 24.43           C
ANISOU 1084  CD1 LEU L  21     5066   2179   2037   -130    128     72       C
ATOM   1085  CD2 LEU L  21      72.217 196.987  54.839  1.00 25.32           C
ANISOU 1085  CD2 LEU L  21     4926   2361   2334     32    290    100       C
ATOM   1086  N   SER L  22      69.523 192.869  57.401  1.00 17.45           N
ANISOU 1086  N   SER L  22     4052   1504   1073   -152    595    128       N
ATOM   1087  CA  SER L  22      68.818 191.604  57.232  1.00 17.62           C
ANISOU 1087  CA  SER L  22     4008   1574   1113   -211    680    147       C
ATOM   1088  C   SER L  22      67.992 191.544  55.946  1.00 23.25           C
ANISOU 1088  C   SER L  22     4437   2395   2003   -139    739    115       C
ATOM   1089  O   SER L  22      67.592 192.576  55.405  1.00 22.57           O
ANISOU 1089  O   SER L  22     4230   2345   2000    -31    769     62       O
ATOM   1090  CB  SER L  22      67.937 191.328  58.444  1.00 22.71           C
ANISOU 1090  CB  SER L  22     4826   2198   1607   -319    882    100       C
ATOM   1091  OG  SER L  22      68.749 191.125  59.591  1.00 32.38           O
ANISOU 1091  OG  SER L  22     6359   3310   2633   -392    792    147       O
ATOM   1092  N   CYS L  23      67.755 190.323  55.456  1.00 21.64           N
ANISOU 1092  N   CYS L  23     4149   2228   1847   -195    739    145       N
ATOM   1093  CA  CYS L  23      66.966 190.040  54.264  1.00 22.23           C
ANISOU 1093  CA  CYS L  23     3968   2408   2071   -151    775    109       C
ATOM   1094  C   CYS L  23      66.336 188.649  54.460  1.00 26.15           C
ANISOU 1094  C   CYS L  23     4468   2921   2547   -292    879    103       C
ATOM   1095  O   CYS L  23      67.065 187.674  54.660  1.00 26.59           O
ANISOU 1095  O   CYS L  23     4671   2893   2538   -363    797    181       O
ATOM   1096  CB  CYS L  23      67.839 190.107  53.005  1.00 21.49           C
ANISOU 1096  CB  CYS L  23     3771   2320   2075    -66    596    165       C
ATOM   1097  SG  CYS L  23      66.957 189.769  51.459  1.00 25.47           S
ANISOU 1097  SG  CYS L  23     4004   2946   2729     -6    598    123       S
ATOM   1098  N   ARG L  24      64.990 188.572  54.509  1.00 20.65           N
ANISOU 1098  N   ARG L  24     3627   2319   1901   -339   1069     -2       N
ATOM   1099  CA  ARG L  24      64.296 187.293  54.654  1.00 19.53           C
ANISOU 1099  CA  ARG L  24     3478   2195   1749   -510   1202    -30       C
ATOM   1100  C   ARG L  24      63.634 186.896  53.345  1.00 21.96           C
ANISOU 1100  C   ARG L  24     3491   2624   2227   -485   1175    -89       C
ATOM   1101  O   ARG L  24      62.869 187.682  52.784  1.00 22.65           O
ANISOU 1101  O   ARG L  24     3339   2833   2434   -375   1196   -186       O
ATOM   1102  CB  ARG L  24      63.262 187.328  55.789  1.00 19.11           C
ANISOU 1102  CB  ARG L  24     3485   2161   1617   -642   1474   -131       C
ATOM   1103  CG  ARG L  24      62.605 185.973  56.014  1.00 29.57           C
ANISOU 1103  CG  ARG L  24     4821   3489   2924   -862   1646   -169       C
ATOM   1104  CD  ARG L  24      61.799 185.842  57.272  1.00 51.63           C
ANISOU 1104  CD  ARG L  24     7781   6254   5581  -1052   1935   -242       C
ATOM   1105  NE  ARG L  24      61.505 184.427  57.473  1.00 75.79           N
ANISOU 1105  NE  ARG L  24    10985   9241   8571  -1286   2046   -218       N
ATOM   1106  CZ  ARG L  24      61.845 183.720  58.549  1.00101.97           C
ANISOU 1106  CZ  ARG L  24    14706  12382  11655  -1451   2126   -134       C
ATOM   1107  NH1 ARG L  24      62.449 184.307  59.575  1.00 95.33           N
ANISOU 1107  NH1 ARG L  24    14152  11443  10625  -1417   2114    -80       N
ATOM   1108  NH2 ARG L  24      61.551 182.427  58.621  1.00 92.88           N
ANISOU 1108  NH2 ARG L  24    13703  11142  10445  -1659   2220   -108       N
ATOM   1109  N   ALA L  25      63.917 185.682  52.854  1.00 17.45           N
ANISOU 1109  N   ALA L  25     2953   2014   1663   -575   1114    -36       N
ATOM   1110  CA  ALA L  25      63.284 185.167  51.644  1.00 17.66           C
ANISOU 1110  CA  ALA L  25     2733   2147   1829   -582   1086   -100       C
ATOM   1111  C   ALA L  25      61.932 184.541  52.015  1.00 25.33           C
ANISOU 1111  C   ALA L  25     3587   3201   2836   -767   1314   -231       C
ATOM   1112  O   ALA L  25      61.818 183.933  53.077  1.00 25.06           O
ANISOU 1112  O   ALA L  25     3762   3078   2683   -946   1478   -219       O
ATOM   1113  CB  ALA L  25      64.181 184.136  50.983  1.00 17.23           C
ANISOU 1113  CB  ALA L  25     2780   2003   1764   -608    943     -6       C
ATOM   1114  N   SER L  26      60.904 184.704  51.148  1.00 24.15           N
ANISOU 1114  N   SER L  26     3110   3222   2846   -732   1324   -365       N
ATOM   1115  CA  SER L  26      59.547 184.166  51.379  1.00 26.30           C
ANISOU 1115  CA  SER L  26     3185   3610   3196   -915   1542   -534       C
ATOM   1116  C   SER L  26      59.500 182.624  51.349  1.00 31.06           C
ANISOU 1116  C   SER L  26     3904   4137   3760  -1168   1617   -520       C
ATOM   1117  O   SER L  26      58.535 182.024  51.830  1.00 33.58           O
ANISOU 1117  O   SER L  26     4158   4502   4098  -1395   1850   -642       O
ATOM   1118  CB  SER L  26      58.568 184.743  50.363  1.00 29.67           C
ANISOU 1118  CB  SER L  26     3213   4244   3817   -779   1467   -688       C
ATOM   1119  OG  SER L  26      58.980 184.451  49.039  1.00 35.81           O
ANISOU 1119  OG  SER L  26     3928   5036   4642   -691   1232   -638       O
ATOM   1120  N   GLN L  27      60.535 181.997  50.767  1.00 25.52           N
ANISOU 1120  N   GLN L  27     3376   3312   3007  -1134   1433   -383       N
ATOM   1121  CA  GLN L  27      60.699 180.544  50.657  1.00 25.67           C
ANISOU 1121  CA  GLN L  27     3561   3213   2979  -1331   1463   -348       C
ATOM   1122  C   GLN L  27      62.193 180.194  50.576  1.00 27.48           C
ANISOU 1122  C   GLN L  27     4081   3255   3105  -1225   1273   -168       C
ATOM   1123  O   GLN L  27      63.015 181.082  50.365  1.00 24.22           O
ANISOU 1123  O   GLN L  27     3665   2846   2693  -1015   1113    -95       O
ATOM   1124  CB  GLN L  27      59.928 179.991  49.437  1.00 27.78           C
ANISOU 1124  CB  GLN L  27     3547   3613   3396  -1391   1420   -474       C
ATOM   1125  CG  GLN L  27      60.453 180.466  48.088  1.00 44.88           C
ANISOU 1125  CG  GLN L  27     5577   5842   5634  -1160   1154   -439       C
ATOM   1126  CD  GLN L  27      59.855 179.689  46.949  1.00 71.35           C
ANISOU 1126  CD  GLN L  27     8745   9280   9084  -1247   1094   -546       C
ATOM   1127  OE1 GLN L  27      58.775 180.013  46.449  1.00 71.60           O
ANISOU 1127  OE1 GLN L  27     8461   9504   9241  -1245   1093   -703       O
ATOM   1128  NE2 GLN L  27      60.553 178.648  46.505  1.00 62.97           N
ANISOU 1128  NE2 GLN L  27     7878   8078   7971  -1315   1030   -473       N
ATOM   1129  N   SER L  28      62.542 178.909  50.735  1.00 27.00           N
ANISOU 1129  N   SER L  28     4266   3027   2967  -1370   1293   -109       N
ATOM   1130  CA  SER L  28      63.935 178.456  50.660  1.00 26.28           C
ANISOU 1130  CA  SER L  28     4426   2757   2803  -1254   1106     37       C
ATOM   1131  C   SER L  28      64.531 178.717  49.277  1.00 26.69           C
ANISOU 1131  C   SER L  28     4288   2882   2970  -1072    903     39       C
ATOM   1132  O   SER L  28      63.935 178.337  48.269  1.00 27.77           O
ANISOU 1132  O   SER L  28     4240   3109   3202  -1122    900    -50       O
ATOM   1133  CB  SER L  28      64.050 176.980  51.032  1.00 33.07           C
ANISOU 1133  CB  SER L  28     5593   3409   3565  -1432   1167     84       C
ATOM   1134  OG  SER L  28      65.407 176.562  51.027  1.00 44.36           O
ANISOU 1134  OG  SER L  28     7257   4662   4934  -1282    971    212       O
ATOM   1135  N   ILE L  29      65.671 179.429  49.238  1.00 18.69           N
ANISOU 1135  N   ILE L  29     3319   1839   1943   -873    744    126       N
ATOM   1136  CA  ILE L  29      66.383 179.782  48.005  1.00 15.61           C
ANISOU 1136  CA  ILE L  29     2789   1504   1638   -709    579    133       C
ATOM   1137  C   ILE L  29      67.854 179.325  48.093  1.00 19.02           C
ANISOU 1137  C   ILE L  29     3411   1780   2037   -609    440    228       C
ATOM   1138  O   ILE L  29      68.718 179.873  47.396  1.00 16.74           O
ANISOU 1138  O   ILE L  29     3035   1524   1800   -464    323    243       O
ATOM   1139  CB  ILE L  29      66.254 181.312  47.670  1.00 16.71           C
ANISOU 1139  CB  ILE L  29     2733   1790   1825   -567    538    110       C
ATOM   1140  CG1 ILE L  29      66.760 182.218  48.831  1.00 15.56           C
ANISOU 1140  CG1 ILE L  29     2710   1600   1604   -505    543    171       C
ATOM   1141  CG2 ILE L  29      64.830 181.672  47.236  1.00 17.77           C
ANISOU 1141  CG2 ILE L  29     2628   2091   2031   -613    622     -9       C
ATOM   1142  CD1 ILE L  29      67.282 183.585  48.401  1.00 16.51           C
ANISOU 1142  CD1 ILE L  29     2737   1780   1757   -340    446    187       C
ATOM   1143  N   SER L  30      68.129 178.316  48.961  1.00 17.48           N
ANISOU 1143  N   SER L  30     3479   1410   1753   -686    457    283       N
ATOM   1144  CA  SER L  30      69.475 177.784  49.238  1.00 17.36           C
ANISOU 1144  CA  SER L  30     3657   1232   1707   -570    305    362       C
ATOM   1145  C   SER L  30      70.418 178.966  49.573  1.00 20.20           C
ANISOU 1145  C   SER L  30     3961   1640   2072   -413    187    398       C
ATOM   1146  O   SER L  30      70.088 179.765  50.461  1.00 20.24           O
ANISOU 1146  O   SER L  30     4005   1680   2004   -440    239    413       O
ATOM   1147  CB  SER L  30      69.987 176.936  48.064  1.00 20.41           C
ANISOU 1147  CB  SER L  30     3996   1575   2184   -515    229    331       C
ATOM   1148  OG  SER L  30      71.201 176.262  48.357  1.00 25.07           O
ANISOU 1148  OG  SER L  30     4757   2001   2766   -389     85    384       O
ATOM   1149  N   THR L  31      71.517 179.134  48.812  1.00 14.94           N
ANISOU 1149  N   THR L  31     3190    989   1499   -268     54    391       N
ATOM   1150  CA  THR L  31      72.468 180.229  49.014  1.00 13.46           C
ANISOU 1150  CA  THR L  31     2928    851   1336   -149    -47    402       C
ATOM   1151  C   THR L  31      72.455 181.225  47.855  1.00 14.79           C
ANISOU 1151  C   THR L  31     2856   1169   1594   -108    -20    351       C
ATOM   1152  O   THR L  31      73.329 182.074  47.797  1.00 14.03           O
ANISOU 1152  O   THR L  31     2692   1107   1533    -30    -87    348       O
ATOM   1153  CB  THR L  31      73.892 179.677  49.257  1.00 20.48           C
ANISOU 1153  CB  THR L  31     3898   1626   2257    -21   -223    421       C
ATOM   1154  OG1 THR L  31      74.307 178.919  48.120  1.00 21.48           O
ANISOU 1154  OG1 THR L  31     3933   1739   2490     29   -241    374       O
ATOM   1155  CG2 THR L  31      74.002 178.843  50.528  1.00 12.66           C
ANISOU 1155  CG2 THR L  31     3106    593   1110    -40   -290    367       C
ATOM   1156  N   PHE L  32      71.462 181.144  46.945  1.00 11.71           N
ANISOU 1156  N   PHE L  32     2356    863   1232   -168     72    308       N
ATOM   1157  CA  PHE L  32      71.392 182.012  45.754  1.00 11.18           C
ANISOU 1157  CA  PHE L  32     2114    914   1218   -121     80    268       C
ATOM   1158  C   PHE L  32      70.839 183.418  46.079  1.00 15.64           C
ANISOU 1158  C   PHE L  32     2623   1564   1754   -103    118    271       C
ATOM   1159  O   PHE L  32      69.729 183.796  45.673  1.00 15.63           O
ANISOU 1159  O   PHE L  32     2531   1654   1755   -122    174    234       O
ATOM   1160  CB  PHE L  32      70.643 181.313  44.597  1.00 12.89           C
ANISOU 1160  CB  PHE L  32     2257   1177   1463   -172    117    213       C
ATOM   1161  CG  PHE L  32      71.180 179.928  44.342  1.00 15.31           C
ANISOU 1161  CG  PHE L  32     2650   1374   1794   -187     91    202       C
ATOM   1162  CD1 PHE L  32      72.394 179.745  43.694  1.00 19.60           C
ANISOU 1162  CD1 PHE L  32     3176   1879   2392    -97     32    186       C
ATOM   1163  CD2 PHE L  32      70.514 178.807  44.822  1.00 18.56           C
ANISOU 1163  CD2 PHE L  32     3176   1703   2175   -294    137    200       C
ATOM   1164  CE1 PHE L  32      72.929 178.461  43.522  1.00 21.98           C
ANISOU 1164  CE1 PHE L  32     3563   2062   2725    -80      3    165       C
ATOM   1165  CE2 PHE L  32      71.046 177.525  44.641  1.00 22.36           C
ANISOU 1165  CE2 PHE L  32     3780   2046   2672   -293    105    194       C
ATOM   1166  CZ  PHE L  32      72.249 177.360  43.996  1.00 20.69           C
ANISOU 1166  CZ  PHE L  32     3541   1796   2523   -169     30    176       C
ATOM   1167  N   LEU L  33      71.661 184.188  46.806  1.00 11.54           N
ANISOU 1167  N   LEU L  33     2156   1012   1216    -56     73    303       N
ATOM   1168  CA  LEU L  33      71.361 185.526  47.289  1.00 11.05           C
ANISOU 1168  CA  LEU L  33     2088    990   1119    -33    102    306       C
ATOM   1169  C   LEU L  33      72.631 186.372  47.158  1.00 15.68           C
ANISOU 1169  C   LEU L  33     2672   1556   1729     20     34    314       C
ATOM   1170  O   LEU L  33      73.732 185.933  47.545  1.00 15.80           O
ANISOU 1170  O   LEU L  33     2722   1514   1767     30    -48    320       O
ATOM   1171  CB  LEU L  33      70.911 185.442  48.767  1.00 11.69           C
ANISOU 1171  CB  LEU L  33     2298   1027   1117    -87    147    325       C
ATOM   1172  CG  LEU L  33      70.133 186.617  49.444  1.00 16.05           C
ANISOU 1172  CG  LEU L  33     2857   1620   1621    -80    228    304       C
ATOM   1173  CD1 LEU L  33      71.042 187.748  49.892  1.00 14.80           C
ANISOU 1173  CD1 LEU L  33     2761   1425   1437    -30    165    320       C
ATOM   1174  CD2 LEU L  33      68.902 187.043  48.668  1.00 19.58           C
ANISOU 1174  CD2 LEU L  33     3149   2171   2117    -53    303    248       C
ATOM   1175  N   ALA L  34      72.461 187.582  46.588  1.00 10.27           N
ANISOU 1175  N   ALA L  34     1946    912   1043     53     63    303       N
ATOM   1176  CA  ALA L  34      73.506 188.549  46.353  1.00  9.11           C
ANISOU 1176  CA  ALA L  34     1794    753    913     65     37    284       C
ATOM   1177  C   ALA L  34      73.192 189.861  47.074  1.00 12.60           C
ANISOU 1177  C   ALA L  34     2320   1167   1299     78     63    303       C
ATOM   1178  O   ALA L  34      72.031 190.167  47.330  1.00 10.97           O
ANISOU 1178  O   ALA L  34     2126    985   1057    108    114    301       O
ATOM   1179  CB  ALA L  34      73.652 188.795  44.851  1.00  9.77           C
ANISOU 1179  CB  ALA L  34     1836    857   1021     79     64    284       C
ATOM   1180  N   TRP L  35      74.235 190.623  47.424  1.00 10.52           N
ANISOU 1180  N   TRP L  35     2097    860   1040     52     31    292       N
ATOM   1181  CA  TRP L  35      74.104 191.906  48.104  1.00 10.47           C
ANISOU 1181  CA  TRP L  35     2188    812    978     52     55    287       C
ATOM   1182  C   TRP L  35      74.716 192.997  47.245  1.00 14.90           C
ANISOU 1182  C   TRP L  35     2770   1338   1552     31     84    275       C
ATOM   1183  O   TRP L  35      75.798 192.806  46.683  1.00 15.08           O
ANISOU 1183  O   TRP L  35     2731   1365   1633    -26     71    250       O
ATOM   1184  CB  TRP L  35      74.773 191.869  49.484  1.00  9.28           C
ANISOU 1184  CB  TRP L  35     2086    644    794      7    -15    240       C
ATOM   1185  CG  TRP L  35      74.007 191.104  50.528  1.00  9.73           C
ANISOU 1185  CG  TRP L  35     2233    680    782     12    -11    288       C
ATOM   1186  CD1 TRP L  35      74.253 189.833  50.959  1.00 12.63           C
ANISOU 1186  CD1 TRP L  35     2621   1034   1143     -2    -78    314       C
ATOM   1187  CD2 TRP L  35      72.941 191.609  51.350  1.00  9.70           C
ANISOU 1187  CD2 TRP L  35     2312    673    699     20     76    263       C
ATOM   1188  NE1 TRP L  35      73.387 189.502  51.981  1.00 12.11           N
ANISOU 1188  NE1 TRP L  35     2679    946    975    -26    -25    331       N
ATOM   1189  CE2 TRP L  35      72.563 190.571  52.232  1.00 13.44           C
ANISOU 1189  CE2 TRP L  35     2877   1127   1101    -18     82    305       C
ATOM   1190  CE3 TRP L  35      72.268 192.844  51.427  1.00 10.72           C
ANISOU 1190  CE3 TRP L  35     2500    782    793     60    160    260       C
ATOM   1191  CZ2 TRP L  35      71.531 190.721  53.168  1.00 13.20           C
ANISOU 1191  CZ2 TRP L  35     2946   1092    978    -42    197    287       C
ATOM   1192  CZ3 TRP L  35      71.250 192.994  52.355  1.00 12.62           C
ANISOU 1192  CZ3 TRP L  35     2811   1022    961     66    257    233       C
ATOM   1193  CH2 TRP L  35      70.900 191.946  53.223  1.00 13.94           C
ANISOU 1193  CH2 TRP L  35     3038   1195   1063      3    288    242       C
ATOM   1194  N   TYR L  36      74.016 194.134  47.137  1.00 11.38           N
ANISOU 1194  N   TYR L  36     2422    850   1052     77    134    283       N
ATOM   1195  CA  TYR L  36      74.441 195.293  46.343  1.00 11.78           C
ANISOU 1195  CA  TYR L  36     2567    827   1080     55    175    285       C
ATOM   1196  C   TYR L  36      74.556 196.547  47.174  1.00 14.14           C
ANISOU 1196  C   TYR L  36     3010   1032   1330     36    194    266       C
ATOM   1197  O   TYR L  36      73.796 196.734  48.122  1.00 12.75           O
ANISOU 1197  O   TYR L  36     2876    850   1117     96    195    257       O
ATOM   1198  CB  TYR L  36      73.455 195.559  45.194  1.00 12.70           C
ANISOU 1198  CB  TYR L  36     2722    943   1159    158    195    319       C
ATOM   1199  CG  TYR L  36      73.515 194.503  44.127  1.00 13.71           C
ANISOU 1199  CG  TYR L  36     2748   1143   1317    150    184    327       C
ATOM   1200  CD1 TYR L  36      72.787 193.318  44.247  1.00 14.52           C
ANISOU 1200  CD1 TYR L  36     2723   1338   1455    190    150    323       C
ATOM   1201  CD2 TYR L  36      74.324 194.664  43.003  1.00 14.13           C
ANISOU 1201  CD2 TYR L  36     2849   1165   1356     81    226    330       C
ATOM   1202  CE1 TYR L  36      72.884 192.312  43.293  1.00 12.99           C
ANISOU 1202  CE1 TYR L  36     2452   1199   1286    173    140    319       C
ATOM   1203  CE2 TYR L  36      74.434 193.661  42.048  1.00 14.22           C
ANISOU 1203  CE2 TYR L  36     2779   1238   1384     68    228    324       C
ATOM   1204  CZ  TYR L  36      73.709 192.485  42.198  1.00 21.24           C
ANISOU 1204  CZ  TYR L  36     3544   2214   2313    121    176    318       C
ATOM   1205  OH  TYR L  36      73.786 191.491  41.260  1.00 23.46           O
ANISOU 1205  OH  TYR L  36     3765   2543   2607    106    178    303       O
ATOM   1206  N   GLN L  37      75.490 197.419  46.788  1.00 11.28           N
ANISOU 1206  N   GLN L  37     2735    590    963    -63    229    248       N
ATOM   1207  CA  GLN L  37      75.688 198.740  47.373  1.00 11.98           C
ANISOU 1207  CA  GLN L  37     2996    558    998   -105    260    223       C
ATOM   1208  C   GLN L  37      75.274 199.727  46.303  1.00 18.49           C
ANISOU 1208  C   GLN L  37     3996   1271   1758    -57    323    264       C
ATOM   1209  O   GLN L  37      75.704 199.608  45.154  1.00 18.63           O
ANISOU 1209  O   GLN L  37     4020   1284   1775   -111    362    285       O
ATOM   1210  CB  GLN L  37      77.156 198.966  47.761  1.00 13.48           C
ANISOU 1210  CB  GLN L  37     3157    732   1234   -289    251    155       C
ATOM   1211  CG  GLN L  37      77.418 200.330  48.389  1.00 18.02           C
ANISOU 1211  CG  GLN L  37     3923   1173   1751   -365    283    114       C
ATOM   1212  CD  GLN L  37      78.888 200.564  48.607  1.00 40.00           C
ANISOU 1212  CD  GLN L  37     6646   3956   4598   -572    276     25       C
ATOM   1213  OE1 GLN L  37      79.658 200.746  47.659  1.00 40.45           O
ANISOU 1213  OE1 GLN L  37     6675   3997   4697   -695    358      1       O
ATOM   1214  NE2 GLN L  37      79.315 200.556  49.861  1.00 26.07           N
ANISOU 1214  NE2 GLN L  37     4856   2213   2838   -624    180    -40       N
ATOM   1215  N   HIS L  38      74.408 200.665  46.652  1.00 16.16           N
ANISOU 1215  N   HIS L  38     3862    878   1400     58    333    273       N
ATOM   1216  CA  HIS L  38      73.959 201.666  45.704  1.00 17.02           C
ANISOU 1216  CA  HIS L  38     4186    849   1433    141    362    318       C
ATOM   1217  C   HIS L  38      74.103 203.058  46.260  1.00 21.12           C
ANISOU 1217  C   HIS L  38     4952   1183   1889    117    406    294       C
ATOM   1218  O   HIS L  38      73.435 203.412  47.231  1.00 19.51           O
ANISOU 1218  O   HIS L  38     4778    956   1679    221    395    259       O
ATOM   1219  CB  HIS L  38      72.523 201.389  45.247  1.00 18.35           C
ANISOU 1219  CB  HIS L  38     4309   1071   1593    375    301    351       C
ATOM   1220  CG  HIS L  38      72.138 202.154  44.024  1.00 23.48           C
ANISOU 1220  CG  HIS L  38     5173   1594   2156    480    282    409       C
ATOM   1221  ND1 HIS L  38      70.845 202.581  43.825  1.00 26.71           N
ANISOU 1221  ND1 HIS L  38     5635   1972   2542    728    206    417       N
ATOM   1222  CD2 HIS L  38      72.896 202.551  42.976  1.00 25.96           C
ANISOU 1222  CD2 HIS L  38     5673   1801   2391    367    328    454       C
ATOM   1223  CE1 HIS L  38      70.852 203.211  42.663  1.00 27.35           C
ANISOU 1223  CE1 HIS L  38     5954   1918   2519    778    177    481       C
ATOM   1224  NE2 HIS L  38      72.066 203.223  42.121  1.00 27.38           N
ANISOU 1224  NE2 HIS L  38     6066   1864   2473    551    265    510       N
ATOM   1225  N   LYS L  39      75.006 203.843  45.655  1.00 20.81           N
ANISOU 1225  N   LYS L  39     5102   1004   1801    -40    478    301       N
ATOM   1226  CA  LYS L  39      75.291 205.241  46.023  1.00 21.72           C
ANISOU 1226  CA  LYS L  39     5502    903   1846   -108    538    276       C
ATOM   1227  C   LYS L  39      74.619 206.163  45.007  1.00 25.95           C
ANISOU 1227  C   LYS L  39     6346   1245   2269     34    550    353       C
ATOM   1228  O   LYS L  39      74.485 205.763  43.849  1.00 24.26           O
ANISOU 1228  O   LYS L  39     6141   1057   2019     66    539    417       O
ATOM   1229  CB  LYS L  39      76.808 205.500  46.028  1.00 23.66           C
ANISOU 1229  CB  LYS L  39     5763   1113   2115   -418    624    216       C
ATOM   1230  CG  LYS L  39      77.574 204.691  47.056  1.00 25.39           C
ANISOU 1230  CG  LYS L  39     5701   1503   2441   -542    572    129       C
ATOM   1231  CD  LYS L  39      78.909 205.335  47.344  1.00 32.57           C
ANISOU 1231  CD  LYS L  39     6655   2344   3376   -824    636     33       C
ATOM   1232  CE  LYS L  39      79.906 204.357  47.878  1.00 37.83           C
ANISOU 1232  CE  LYS L  39     7002   3203   4170   -953    566    -56       C
ATOM   1233  NZ  LYS L  39      81.167 205.033  48.253  1.00 45.77           N
ANISOU 1233  NZ  LYS L  39     8015   4158   5218  -1226    608   -180       N
ATOM   1234  N   PRO L  40      74.224 207.409  45.387  1.00 26.12           N
ANISOU 1234  N   PRO L  40     6653   1053   2219    121    564    346       N
ATOM   1235  CA  PRO L  40      73.586 208.303  44.404  1.00 27.53           C
ANISOU 1235  CA  PRO L  40     7167   1016   2277    287    545    426       C
ATOM   1236  C   PRO L  40      74.503 208.675  43.240  1.00 34.35           C
ANISOU 1236  C   PRO L  40     8275   1738   3037     72    643    483       C
ATOM   1237  O   PRO L  40      75.715 208.813  43.430  1.00 34.83           O
ANISOU 1237  O   PRO L  40     8338   1780   3117   -234    766    430       O
ATOM   1238  CB  PRO L  40      73.193 209.529  45.237  1.00 30.27           C
ANISOU 1238  CB  PRO L  40     7768   1149   2583    387    559    383       C
ATOM   1239  CG  PRO L  40      73.274 209.103  46.649  1.00 32.85           C
ANISOU 1239  CG  PRO L  40     7842   1632   3010    345    563    284       C
ATOM   1240  CD  PRO L  40      74.320 208.063  46.713  1.00 27.42           C
ANISOU 1240  CD  PRO L  40     6878   1145   2394     90    587    262       C
ATOM   1241  N   GLY L  41      73.920 208.768  42.043  1.00 32.00           N
ANISOU 1241  N   GLY L  41     8164   1363   2632    227    586    579       N
ATOM   1242  CA  GLY L  41      74.637 209.121  40.822  1.00 34.11           C
ANISOU 1242  CA  GLY L  41     8724   1477   2758     41    690    646       C
ATOM   1243  C   GLY L  41      75.538 208.031  40.277  1.00 39.11           C
ANISOU 1243  C   GLY L  41     9098   2316   3448   -193    779    623       C
ATOM   1244  O   GLY L  41      76.300 208.264  39.330  1.00 41.57           O
ANISOU 1244  O   GLY L  41     9620   2522   3653   -410    919    650       O
ATOM   1245  N   GLN L  42      75.437 206.833  40.853  1.00 32.40           N
ANISOU 1245  N   GLN L  42     7809   1745   2756   -149    710    569       N
ATOM   1246  CA  GLN L  42      76.233 205.674  40.482  1.00 30.64           C
ANISOU 1246  CA  GLN L  42     7297   1729   2616   -326    773    530       C
ATOM   1247  C   GLN L  42      75.313 204.488  40.306  1.00 32.10           C
ANISOU 1247  C   GLN L  42     7212   2123   2859   -106    628    553       C
ATOM   1248  O   GLN L  42      74.229 204.457  40.891  1.00 32.00           O
ANISOU 1248  O   GLN L  42     7124   2152   2882    132    497    559       O
ATOM   1249  CB  GLN L  42      77.243 205.353  41.606  1.00 31.38           C
ANISOU 1249  CB  GLN L  42     7114   1942   2867   -537    832    414       C
ATOM   1250  CG  GLN L  42      78.450 206.274  41.654  1.00 44.40           C
ANISOU 1250  CG  GLN L  42     8940   3437   4493   -843   1001    352       C
ATOM   1251  CD  GLN L  42      79.381 205.882  42.768  1.00 58.12           C
ANISOU 1251  CD  GLN L  42    10368   5319   6395  -1015   1004    222       C
ATOM   1252  OE1 GLN L  42      79.294 206.387  43.883  1.00 57.69           O
ANISOU 1252  OE1 GLN L  42    10333   5220   6365   -999    948    179       O
ATOM   1253  NE2 GLN L  42      80.299 204.971  42.496  1.00 51.58           N
ANISOU 1253  NE2 GLN L  42     9253   4665   5680  -1172   1057    149       N
ATOM   1254  N   ALA L  43      75.756 203.493  39.541  1.00 25.88           N
ANISOU 1254  N   ALA L  43     6269   1473   2093   -198    666    547       N
ATOM   1255  CA  ALA L  43      75.006 202.264  39.357  1.00 23.08           C
ANISOU 1255  CA  ALA L  43     5653   1318   1800    -37    545    553       C
ATOM   1256  C   ALA L  43      75.231 201.359  40.578  1.00 25.07           C
ANISOU 1256  C   ALA L  43     5539   1754   2231    -66    516    476       C
ATOM   1257  O   ALA L  43      76.273 201.481  41.235  1.00 24.73           O
ANISOU 1257  O   ALA L  43     5421   1714   2262   -252    597    411       O
ATOM   1258  CB  ALA L  43      75.496 201.557  38.108  1.00 23.76           C
ANISOU 1258  CB  ALA L  43     5739   1456   1830   -145    614    562       C
ATOM   1259  N   PRO L  44      74.315 200.404  40.879  1.00 19.26           N
ANISOU 1259  N   PRO L  44     4581   1173   1564    100    399    475       N
ATOM   1260  CA  PRO L  44      74.576 199.470  41.984  1.00 16.92           C
ANISOU 1260  CA  PRO L  44     3996   1026   1406     58    378    414       C
ATOM   1261  C   PRO L  44      75.851 198.646  41.746  1.00 20.55           C
ANISOU 1261  C   PRO L  44     4297   1569   1943   -130    448    365       C
ATOM   1262  O   PRO L  44      76.181 198.326  40.601  1.00 21.53           O
ANISOU 1262  O   PRO L  44     4452   1700   2028   -185    504    374       O
ATOM   1263  CB  PRO L  44      73.328 198.584  41.995  1.00 17.56           C
ANISOU 1263  CB  PRO L  44     3919   1234   1518    239    272    426       C
ATOM   1264  CG  PRO L  44      72.288 199.382  41.299  1.00 23.20           C
ANISOU 1264  CG  PRO L  44     4820   1860   2134    417    209    473       C
ATOM   1265  CD  PRO L  44      73.017 200.117  40.242  1.00 20.40           C
ANISOU 1265  CD  PRO L  44     4731   1360   1661    319    277    517       C
ATOM   1266  N   ARG L  45      76.592 198.371  42.823  1.00 16.02           N
ANISOU 1266  N   ARG L  45     3569   1048   1470   -223    443    302       N
ATOM   1267  CA  ARG L  45      77.845 197.622  42.828  1.00 15.74           C
ANISOU 1267  CA  ARG L  45     3342   1097   1542   -369    478    228       C
ATOM   1268  C   ARG L  45      77.647 196.328  43.638  1.00 17.95           C
ANISOU 1268  C   ARG L  45     3400   1506   1913   -288    367    211       C
ATOM   1269  O   ARG L  45      77.186 196.375  44.785  1.00 16.15           O
ANISOU 1269  O   ARG L  45     3169   1283   1685   -227    292    218       O
ATOM   1270  CB  ARG L  45      78.970 198.507  43.425  1.00 19.77           C
ANISOU 1270  CB  ARG L  45     3881   1542   2089   -549    536    153       C
ATOM   1271  CG  ARG L  45      80.298 197.811  43.769  1.00 33.35           C
ANISOU 1271  CG  ARG L  45     5346   3368   3959   -676    528     41       C
ATOM   1272  CD  ARG L  45      80.816 198.321  45.115  1.00 48.20           C
ANISOU 1272  CD  ARG L  45     7199   5233   5881   -744    451    -24       C
ATOM   1273  NE  ARG L  45      82.185 197.887  45.417  1.00 53.59           N
ANISOU 1273  NE  ARG L  45     7640   6006   6713   -872    424   -155       N
ATOM   1274  CZ  ARG L  45      82.849 198.209  46.527  1.00 60.33           C
ANISOU 1274  CZ  ARG L  45     8430   6871   7620   -946    326   -240       C
ATOM   1275  NH1 ARG L  45      82.279 198.965  47.457  1.00 36.05           N
ANISOU 1275  NH1 ARG L  45     5539   3712   4447   -918    269   -203       N
ATOM   1276  NH2 ARG L  45      84.088 197.776  46.714  1.00 50.17           N
ANISOU 1276  NH2 ARG L  45     6890   5684   6489  -1041    276   -376       N
ATOM   1277  N   LEU L  46      77.967 195.177  43.025  1.00 13.87           N
ANISOU 1277  N   LEU L  46     2733   1078   1460   -289    368    190       N
ATOM   1278  CA  LEU L  46      77.842 193.875  43.673  1.00 12.44           C
ANISOU 1278  CA  LEU L  46     2384    988   1355   -219    270    179       C
ATOM   1279  C   LEU L  46      78.890 193.718  44.763  1.00 16.75           C
ANISOU 1279  C   LEU L  46     2818   1555   1993   -279    201    110       C
ATOM   1280  O   LEU L  46      80.078 193.907  44.497  1.00 18.74           O
ANISOU 1280  O   LEU L  46     2981   1817   2324   -389    244     28       O
ATOM   1281  CB  LEU L  46      77.948 192.736  42.625  1.00 12.02           C
ANISOU 1281  CB  LEU L  46     2232    996   1340   -204    296    164       C
ATOM   1282  CG  LEU L  46      77.971 191.284  43.158  1.00 15.30           C
ANISOU 1282  CG  LEU L  46     2501   1475   1837   -140    205    148       C
ATOM   1283  CD1 LEU L  46      76.622 190.874  43.730  1.00 14.27           C
ANISOU 1283  CD1 LEU L  46     2418   1355   1649    -46    139    213       C
ATOM   1284  CD2 LEU L  46      78.396 190.325  42.079  1.00 15.88           C
ANISOU 1284  CD2 LEU L  46     2490   1586   1958   -147    255    105       C
ATOM   1285  N   LEU L  47      78.450 193.393  45.993  1.00 11.29           N
ANISOU 1285  N   LEU L  47     2134    870   1285   -214     94    133       N
ATOM   1286  CA  LEU L  47      79.345 193.179  47.125  1.00 10.58           C
ANISOU 1286  CA  LEU L  47     1973    793   1253   -246    -19     75       C
ATOM   1287  C   LEU L  47      79.571 191.700  47.387  1.00 13.47           C
ANISOU 1287  C   LEU L  47     2224   1209   1685   -171   -125     68       C
ATOM   1288  O   LEU L  47      80.709 191.273  47.583  1.00 13.03           O
ANISOU 1288  O   LEU L  47     2031   1184   1736   -185   -208    -11       O
ATOM   1289  CB  LEU L  47      78.786 193.810  48.410  1.00 10.86           C
ANISOU 1289  CB  LEU L  47     2153    780   1193   -231    -73    101       C
ATOM   1290  CG  LEU L  47      78.539 195.310  48.460  1.00 15.03           C
ANISOU 1290  CG  LEU L  47     2833   1228   1651   -288      9     99       C
ATOM   1291  CD1 LEU L  47      77.787 195.649  49.723  1.00 14.35           C
ANISOU 1291  CD1 LEU L  47     2887   1101   1465   -241    -29    121       C
ATOM   1292  CD2 LEU L  47      79.846 196.096  48.401  1.00 18.00           C
ANISOU 1292  CD2 LEU L  47     3168   1582   2088   -437     18      7       C
ATOM   1293  N   ILE L  48      78.474 190.923  47.455  1.00 10.45           N
ANISOU 1293  N   ILE L  48     1901    827   1242    -89   -129    141       N
ATOM   1294  CA  ILE L  48      78.503 189.499  47.808  1.00 10.01           C
ANISOU 1294  CA  ILE L  48     1807    779   1218    -21   -223    152       C
ATOM   1295  C   ILE L  48      77.557 188.684  46.940  1.00 14.40           C
ANISOU 1295  C   ILE L  48     2361   1351   1759     16   -149    194       C
ATOM   1296  O   ILE L  48      76.466 189.143  46.636  1.00 15.16           O
ANISOU 1296  O   ILE L  48     2519   1456   1786     17    -69    235       O
ATOM   1297  CB  ILE L  48      78.187 189.361  49.346  1.00 12.90           C
ANISOU 1297  CB  ILE L  48     2309   1101   1492      0   -327    188       C
ATOM   1298  CG1 ILE L  48      79.476 189.524  50.186  1.00 14.01           C
ANISOU 1298  CG1 ILE L  48     2413   1233   1677    -10   -485    123       C
ATOM   1299  CG2 ILE L  48      77.466 188.060  49.694  1.00 11.76           C
ANISOU 1299  CG2 ILE L  48     2239    928   1301     50   -355    244       C
ATOM   1300  CD1 ILE L  48      79.317 190.257  51.373  1.00 19.27           C
ANISOU 1300  CD1 ILE L  48     3227   1861   2234    -41   -538    133       C
ATOM   1301  N   TYR L  49      77.982 187.489  46.524  1.00  9.92           N
ANISOU 1301  N   TYR L  49     1718    786   1264     55   -186    170       N
ATOM   1302  CA  TYR L  49      77.151 186.549  45.775  1.00  8.54           C
ANISOU 1302  CA  TYR L  49     1552    617   1076     76   -134    196       C
ATOM   1303  C   TYR L  49      77.298 185.174  46.428  1.00 11.70           C
ANISOU 1303  C   TYR L  49     1992    959   1493    127   -231    206       C
ATOM   1304  O   TYR L  49      78.237 184.973  47.202  1.00 10.18           O
ANISOU 1304  O   TYR L  49     1795    732   1341    169   -353    183       O
ATOM   1305  CB  TYR L  49      77.486 186.530  44.266  1.00  9.27           C
ANISOU 1305  CB  TYR L  49     1556    748   1220     60    -44    148       C
ATOM   1306  CG  TYR L  49      78.878 186.047  43.934  1.00 11.64           C
ANISOU 1306  CG  TYR L  49     1729   1050   1643     77    -66     59       C
ATOM   1307  CD1 TYR L  49      79.959 186.922  43.932  1.00 14.69           C
ANISOU 1307  CD1 TYR L  49     2024   1461   2095     28    -48     -8       C
ATOM   1308  CD2 TYR L  49      79.110 184.723  43.577  1.00 12.41           C
ANISOU 1308  CD2 TYR L  49     1786   1124   1803    136    -92     25       C
ATOM   1309  CE1 TYR L  49      81.244 186.482  43.621  1.00 17.25           C
ANISOU 1309  CE1 TYR L  49     2182   1809   2563     43    -55   -122       C
ATOM   1310  CE2 TYR L  49      80.387 184.274  43.258  1.00 14.81           C
ANISOU 1310  CE2 TYR L  49     1948   1435   2244    177   -107    -80       C
ATOM   1311  CZ  TYR L  49      81.452 185.159  43.268  1.00 26.14           C
ANISOU 1311  CZ  TYR L  49     3254   2918   3760    131    -86   -161       C
ATOM   1312  OH  TYR L  49      82.715 184.703  42.960  1.00 31.20           O
ANISOU 1312  OH  TYR L  49     3705   3585   4563    172    -91   -295       O
ATOM   1313  N   ASP L  50      76.360 184.247  46.152  1.00  9.07           N
ANISOU 1313  N   ASP L  50     1714    607   1124    121   -191    235       N
ATOM   1314  CA  ASP L  50      76.330 182.906  46.751  1.00 11.12           C
ANISOU 1314  CA  ASP L  50     2076    777   1374    150   -262    257       C
ATOM   1315  C   ASP L  50      76.269 183.017  48.292  1.00 18.35           C
ANISOU 1315  C   ASP L  50     3145   1629   2198    148   -345    310       C
ATOM   1316  O   ASP L  50      76.838 182.196  49.012  1.00 18.99           O
ANISOU 1316  O   ASP L  50     3331   1615   2272    207   -472    324       O
ATOM   1317  CB  ASP L  50      77.489 182.004  46.247  1.00 15.12           C
ANISOU 1317  CB  ASP L  50     2509   1239   1995    236   -337    196       C
ATOM   1318  CG  ASP L  50      77.497 181.707  44.738  1.00 35.24           C
ANISOU 1318  CG  ASP L  50     4949   3832   4607    227   -235    135       C
ATOM   1319  OD1 ASP L  50      76.442 181.926  44.071  1.00 36.59           O
ANISOU 1319  OD1 ASP L  50     5133   4052   4717    156   -134    154       O
ATOM   1320  OD2 ASP L  50      78.545 181.235  44.229  1.00 43.59           O
ANISOU 1320  OD2 ASP L  50     5911   4876   5775    296   -262     57       O
ATOM   1321  N   ALA L  51      75.570 184.085  48.769  1.00 14.80           N
ANISOU 1321  N   ALA L  51     2728   1225   1669     91   -276    334       N
ATOM   1322  CA  ALA L  51      75.283 184.459  50.154  1.00 15.06           C
ANISOU 1322  CA  ALA L  51     2921   1215   1585     62   -303    374       C
ATOM   1323  C   ALA L  51      76.496 184.926  50.968  1.00 18.45           C
ANISOU 1323  C   ALA L  51     3379   1615   2015    110   -462    358       C
ATOM   1324  O   ALA L  51      76.323 185.799  51.822  1.00 18.51           O
ANISOU 1324  O   ALA L  51     3474   1624   1934     75   -459    367       O
ATOM   1325  CB  ALA L  51      74.544 183.342  50.886  1.00 16.49           C
ANISOU 1325  CB  ALA L  51     3295   1305   1665     16   -280    424       C
ATOM   1326  N   SER L  52      77.710 184.387  50.698  1.00 13.53           N
ANISOU 1326  N   SER L  52     2669    972   1498    193   -601    317       N
ATOM   1327  CA  SER L  52      78.900 184.743  51.476  1.00 14.18           C
ANISOU 1327  CA  SER L  52     2743   1041   1602    246   -786    277       C
ATOM   1328  C   SER L  52      80.190 184.958  50.662  1.00 19.84           C
ANISOU 1328  C   SER L  52     3203   1828   2506    293   -844    170       C
ATOM   1329  O   SER L  52      81.231 185.214  51.261  1.00 20.73           O
ANISOU 1329  O   SER L  52     3259   1950   2668    335  -1011    108       O
ATOM   1330  CB  SER L  52      79.141 183.721  52.586  1.00 16.47           C
ANISOU 1330  CB  SER L  52     3248   1207   1801    320   -968    324       C
ATOM   1331  OG  SER L  52      79.086 182.386  52.118  1.00 21.97           O
ANISOU 1331  OG  SER L  52     3980   1830   2540    384   -979    343       O
ATOM   1332  N   THR L  53      80.133 184.891  49.322  1.00 17.56           N
ANISOU 1332  N   THR L  53     2759   1596   2317    275   -703    133       N
ATOM   1333  CA  THR L  53      81.336 185.111  48.504  1.00 18.11           C
ANISOU 1333  CA  THR L  53     2587   1735   2558    291   -704     15       C
ATOM   1334  C   THR L  53      81.502 186.591  48.176  1.00 22.01           C
ANISOU 1334  C   THR L  53     3003   2301   3058    172   -593    -24       C
ATOM   1335  O   THR L  53      80.635 187.177  47.537  1.00 19.39           O
ANISOU 1335  O   THR L  53     2727   1984   2656    102   -432     25       O
ATOM   1336  CB  THR L  53      81.347 184.213  47.234  1.00 18.02           C
ANISOU 1336  CB  THR L  53     2481   1730   2636    328   -604    -21       C
ATOM   1337  OG1 THR L  53      81.191 182.845  47.614  1.00 21.32           O
ANISOU 1337  OG1 THR L  53     3012   2050   3040    435   -711     16       O
ATOM   1338  CG2 THR L  53      82.627 184.361  46.425  1.00 10.36           C
ANISOU 1338  CG2 THR L  53     1260    831   1845    339   -576   -164       C
ATOM   1339  N   ARG L  54      82.622 187.190  48.603  1.00 21.51           N
ANISOU 1339  N   ARG L  54     2817   2276   3081    151   -688   -119       N
ATOM   1340  CA  ARG L  54      82.921 188.589  48.292  1.00 21.31           C
ANISOU 1340  CA  ARG L  54     2732   2297   3068     13   -574   -171       C
ATOM   1341  C   ARG L  54      83.298 188.708  46.822  1.00 27.26           C
ANISOU 1341  C   ARG L  54     3337   3101   3920    -51   -385   -240       C
ATOM   1342  O   ARG L  54      84.081 187.901  46.313  1.00 28.98           O
ANISOU 1342  O   ARG L  54     3379   3355   4277      5   -399   -331       O
ATOM   1343  CB  ARG L  54      84.074 189.111  49.158  1.00 20.74           C
ANISOU 1343  CB  ARG L  54     2552   2257   3074    -17   -733   -280       C
ATOM   1344  CG  ARG L  54      83.638 189.703  50.478  1.00 26.98           C
ANISOU 1344  CG  ARG L  54     3545   2995   3712    -36   -845   -219       C
ATOM   1345  CD  ARG L  54      84.781 190.416  51.172  1.00 34.35           C
ANISOU 1345  CD  ARG L  54     4367   3969   4717   -103   -988   -345       C
ATOM   1346  NE  ARG L  54      85.731 189.485  51.777  1.00 47.12           N
ANISOU 1346  NE  ARG L  54     5855   5611   6437     28  -1252   -425       N
ATOM   1347  CZ  ARG L  54      87.027 189.437  51.482  1.00 69.02           C
ANISOU 1347  CZ  ARG L  54     8326   8475   9422     27  -1328   -597       C
ATOM   1348  NH1 ARG L  54      87.543 190.271  50.588  1.00 60.07           N
ANISOU 1348  NH1 ARG L  54     7005   7412   8407   -136  -1128   -705       N
ATOM   1349  NH2 ARG L  54      87.819 188.562  52.086  1.00 60.37           N
ANISOU 1349  NH2 ARG L  54     7121   7397   8421    188  -1605   -671       N
ATOM   1350  N   ALA L  55      82.746 189.712  46.139  1.00 23.93           N
ANISOU 1350  N   ALA L  55     3007   2670   3415   -161   -209   -200       N
ATOM   1351  CA  ALA L  55      83.043 189.979  44.735  1.00 23.74           C
ANISOU 1351  CA  ALA L  55     2917   2673   3432   -248    -12   -251       C
ATOM   1352  C   ALA L  55      84.440 190.629  44.608  1.00 31.17           C
ANISOU 1352  C   ALA L  55     3669   3663   4510   -375     38   -407       C
ATOM   1353  O   ALA L  55      85.039 190.997  45.620  1.00 31.65           O
ANISOU 1353  O   ALA L  55     3661   3739   4624   -396    -97   -466       O
ATOM   1354  CB  ALA L  55      81.975 190.890  44.151  1.00 23.16           C
ANISOU 1354  CB  ALA L  55     3050   2548   3200   -305    122   -150       C
ATOM   1355  N   THR L  56      84.958 190.748  43.372  1.00 29.91           N
ANISOU 1355  N   THR L  56     3428   3533   4405   -474    236   -487       N
ATOM   1356  CA  THR L  56      86.279 191.321  43.083  1.00 32.09           C
ANISOU 1356  CA  THR L  56     3502   3866   4825   -633    345   -661       C
ATOM   1357  C   THR L  56      86.410 192.751  43.625  1.00 35.11           C
ANISOU 1357  C   THR L  56     3985   4207   5150   -798    371   -664       C
ATOM   1358  O   THR L  56      85.553 193.607  43.359  1.00 33.96           O
ANISOU 1358  O   THR L  56     4105   3968   4831   -854    465   -544       O
ATOM   1359  CB  THR L  56      86.589 191.233  41.565  1.00 43.09           C
ANISOU 1359  CB  THR L  56     4864   5277   6233   -732    607   -728       C
ATOM   1360  OG1 THR L  56      86.396 189.886  41.115  1.00 44.10           O
ANISOU 1360  OG1 THR L  56     4925   5428   6402   -570    572   -726       O
ATOM   1361  CG2 THR L  56      87.999 191.703  41.223  1.00 43.26           C
ANISOU 1361  CG2 THR L  56     4642   5371   6424   -917    762   -939       C
ATOM   1362  N   GLY L  57      87.462 192.969  44.413  1.00 31.42           N
ANISOU 1362  N   GLY L  57     3306   3801   4829   -857    263   -809       N
ATOM   1363  CA  GLY L  57      87.778 194.259  45.011  1.00 31.06           C
ANISOU 1363  CA  GLY L  57     3325   3721   4756  -1034    272   -851       C
ATOM   1364  C   GLY L  57      86.915 194.684  46.187  1.00 31.41           C
ANISOU 1364  C   GLY L  57     3597   3687   4650   -956     95   -721       C
ATOM   1365  O   GLY L  57      87.063 195.811  46.669  1.00 32.71           O
ANISOU 1365  O   GLY L  57     3860   3799   4767  -1100    109   -749       O
ATOM   1366  N   VAL L  58      86.004 193.808  46.662  1.00 22.66           N
ANISOU 1366  N   VAL L  58     2588   2562   3459   -747    -52   -590       N
ATOM   1367  CA  VAL L  58      85.148 194.140  47.802  1.00 20.35           C
ANISOU 1367  CA  VAL L  58     2515   2200   3017   -679   -188   -480       C
ATOM   1368  C   VAL L  58      85.960 193.967  49.097  1.00 24.86           C
ANISOU 1368  C   VAL L  58     2969   2817   3659   -654   -438   -576       C
ATOM   1369  O   VAL L  58      86.502 192.885  49.316  1.00 26.09           O
ANISOU 1369  O   VAL L  58     2948   3038   3926   -530   -597   -629       O
ATOM   1370  CB  VAL L  58      83.804 193.362  47.803  1.00 20.76           C
ANISOU 1370  CB  VAL L  58     2732   2213   2942   -507   -209   -316       C
ATOM   1371  CG1 VAL L  58      82.958 193.717  49.021  1.00 19.62           C
ANISOU 1371  CG1 VAL L  58     2801   2004   2648   -457   -311   -229       C
ATOM   1372  CG2 VAL L  58      83.023 193.640  46.528  1.00 19.24           C
ANISOU 1372  CG2 VAL L  58     2652   1983   2676   -529      0   -238       C
ATOM   1373  N   PRO L  59      86.115 195.034  49.925  1.00 21.16           N
ANISOU 1373  N   PRO L  59     2604   2308   3129   -768   -488   -612       N
ATOM   1374  CA  PRO L  59      86.949 194.911  51.142  1.00 23.09           C
ANISOU 1374  CA  PRO L  59     2744   2600   3427   -753   -755   -719       C
ATOM   1375  C   PRO L  59      86.433 193.922  52.199  1.00 26.10           C
ANISOU 1375  C   PRO L  59     3252   2961   3705   -549   -992   -622       C
ATOM   1376  O   PRO L  59      85.239 193.629  52.252  1.00 23.06           O
ANISOU 1376  O   PRO L  59     3086   2506   3169   -461   -925   -465       O
ATOM   1377  CB  PRO L  59      87.041 196.343  51.673  1.00 25.61           C
ANISOU 1377  CB  PRO L  59     3205   2857   3668   -941   -716   -768       C
ATOM   1378  CG  PRO L  59      85.914 197.053  51.069  1.00 28.31           C
ANISOU 1378  CG  PRO L  59     3809   3086   3863   -972   -482   -632       C
ATOM   1379  CD  PRO L  59      85.591 196.404  49.767  1.00 22.38           C
ANISOU 1379  CD  PRO L  59     2985   2359   3159   -911   -318   -569       C
ATOM   1380  N   ALA L  60      87.366 193.405  53.034  1.00 25.34           N
ANISOU 1380  N   ALA L  60     3015   2922   3690   -480  -1272   -726       N
ATOM   1381  CA  ALA L  60      87.135 192.382  54.066  1.00 25.67           C
ANISOU 1381  CA  ALA L  60     3191   2930   3632   -287  -1535   -651       C
ATOM   1382  C   ALA L  60      86.058 192.721  55.109  1.00 29.06           C
ANISOU 1382  C   ALA L  60     3994   3252   3796   -284  -1553   -515       C
ATOM   1383  O   ALA L  60      85.429 191.802  55.645  1.00 29.17           O
ANISOU 1383  O   ALA L  60     4194   3206   3683   -147  -1637   -398       O
ATOM   1384  CB  ALA L  60      88.440 192.038  54.760  1.00 29.32           C
ANISOU 1384  CB  ALA L  60     3444   3469   4227   -225  -1857   -812       C
ATOM   1385  N   ARG L  61      85.829 194.024  55.382  1.00 23.83           N
ANISOU 1385  N   ARG L  61     3456   2553   3046   -443  -1452   -538       N
ATOM   1386  CA  ARG L  61      84.823 194.480  56.346  1.00 22.17           C
ANISOU 1386  CA  ARG L  61     3589   2243   2592   -450  -1431   -439       C
ATOM   1387  C   ARG L  61      83.377 194.099  55.958  1.00 22.93           C
ANISOU 1387  C   ARG L  61     3856   2281   2576   -374  -1221   -276       C
ATOM   1388  O   ARG L  61      82.498 194.131  56.810  1.00 20.88           O
ANISOU 1388  O   ARG L  61     3857   1950   2125   -348  -1209   -198       O
ATOM   1389  CB  ARG L  61      84.960 195.984  56.618  1.00 22.77           C
ANISOU 1389  CB  ARG L  61     3749   2280   2622   -631  -1351   -520       C
ATOM   1390  CG  ARG L  61      84.711 196.862  55.405  1.00 26.65           C
ANISOU 1390  CG  ARG L  61     4183   2752   3191   -745  -1062   -520       C
ATOM   1391  CD  ARG L  61      84.921 198.309  55.757  1.00 30.44           C
ANISOU 1391  CD  ARG L  61     4786   3162   3618   -925  -1003   -604       C
ATOM   1392  NE  ARG L  61      84.576 199.187  54.645  1.00 31.53           N
ANISOU 1392  NE  ARG L  61     4957   3238   3787  -1023   -729   -582       N
ATOM   1393  CZ  ARG L  61      85.438 199.621  53.735  1.00 41.13           C
ANISOU 1393  CZ  ARG L  61     5989   4484   5155  -1176   -626   -680       C
ATOM   1394  NH1 ARG L  61      86.709 199.245  53.781  1.00 31.41           N
ANISOU 1394  NH1 ARG L  61     4469   3372   4095  -1245   -765   -828       N
ATOM   1395  NH2 ARG L  61      85.035 200.428  52.768  1.00 28.47           N
ANISOU 1395  NH2 ARG L  61     4496   2789   3531  -1259   -381   -638       N
ATOM   1396  N   PHE L  62      83.150 193.723  54.678  1.00 19.85           N
ANISOU 1396  N   PHE L  62     3310   1926   2305   -347  -1057   -242       N
ATOM   1397  CA  PHE L  62      81.857 193.266  54.151  1.00 17.36           C
ANISOU 1397  CA  PHE L  62     3095   1580   1920   -276   -882   -112       C
ATOM   1398  C   PHE L  62      81.797 191.747  54.217  1.00 23.13           C
ANISOU 1398  C   PHE L  62     3801   2321   2668   -145   -993    -58       C
ATOM   1399  O   PHE L  62      82.648 191.069  53.640  1.00 23.00           O
ANISOU 1399  O   PHE L  62     3577   2357   2807    -97  -1074   -116       O
ATOM   1400  CB  PHE L  62      81.668 193.713  52.687  1.00 16.96           C
ANISOU 1400  CB  PHE L  62     2923   1553   1970   -323   -665   -111       C
ATOM   1401  CG  PHE L  62      81.495 195.197  52.523  1.00 17.81           C
ANISOU 1401  CG  PHE L  62     3127   1607   2032   -438   -527   -135       C
ATOM   1402  CD1 PHE L  62      80.241 195.785  52.644  1.00 18.94           C
ANISOU 1402  CD1 PHE L  62     3469   1683   2045   -406   -399    -57       C
ATOM   1403  CD2 PHE L  62      82.590 196.017  52.266  1.00 21.18           C
ANISOU 1403  CD2 PHE L  62     3450   2044   2554   -580   -522   -250       C
ATOM   1404  CE1 PHE L  62      80.089 197.169  52.531  1.00 20.05           C
ANISOU 1404  CE1 PHE L  62     3733   1745   2141   -486   -286    -80       C
ATOM   1405  CE2 PHE L  62      82.436 197.401  52.152  1.00 23.99           C
ANISOU 1405  CE2 PHE L  62     3946   2316   2852   -697   -391   -269       C
ATOM   1406  CZ  PHE L  62      81.186 197.966  52.278  1.00 20.72           C
ANISOU 1406  CZ  PHE L  62     3759   1814   2300   -635   -282   -177       C
ATOM   1407  N   SER L  63      80.798 191.212  54.919  1.00 21.15           N
ANISOU 1407  N   SER L  63     3769   2010   2257    -93   -980     42       N
ATOM   1408  CA  SER L  63      80.617 189.771  55.014  1.00 21.26           C
ANISOU 1408  CA  SER L  63     3825   1996   2256     11  -1060    106       C
ATOM   1409  C   SER L  63      79.149 189.380  54.951  1.00 23.77           C
ANISOU 1409  C   SER L  63     4297   2275   2458      8   -875    208       C
ATOM   1410  O   SER L  63      78.290 190.064  55.505  1.00 23.18           O
ANISOU 1410  O   SER L  63     4380   2176   2253    -47   -762    232       O
ATOM   1411  CB  SER L  63      81.280 189.212  56.268  1.00 26.33           C
ANISOU 1411  CB  SER L  63     4609   2584   2810     74  -1332     98       C
ATOM   1412  OG  SER L  63      80.645 189.686  57.438  1.00 39.89           O
ANISOU 1412  OG  SER L  63     6609   4237   4310     19  -1326    138       O
ATOM   1413  N   GLY L  64      78.882 188.288  54.259  1.00 19.33           N
ANISOU 1413  N   GLY L  64     3675   1713   1958     62   -839    249       N
ATOM   1414  CA  GLY L  64      77.543 187.746  54.129  1.00 17.85           C
ANISOU 1414  CA  GLY L  64     3593   1501   1687     44   -674    323       C
ATOM   1415  C   GLY L  64      77.383 186.480  54.930  1.00 21.20           C
ANISOU 1415  C   GLY L  64     4224   1828   2002     75   -765    385       C
ATOM   1416  O   GLY L  64      78.330 185.703  55.054  1.00 22.35           O
ANISOU 1416  O   GLY L  64     4367   1930   2196    161   -959    378       O
ATOM   1417  N   SER L  65      76.207 186.287  55.528  1.00 17.20           N
ANISOU 1417  N   SER L  65     3914   1277   1345      6   -625    439       N
ATOM   1418  CA  SER L  65      75.905 185.077  56.304  1.00 18.11           C
ANISOU 1418  CA  SER L  65     4289   1271   1319     -4   -665    508       C
ATOM   1419  C   SER L  65      74.457 184.652  56.115  1.00 20.80           C
ANISOU 1419  C   SER L  65     4681   1614   1610   -106   -415    535       C
ATOM   1420  O   SER L  65      73.641 185.422  55.596  1.00 18.55           O
ANISOU 1420  O   SER L  65     4242   1429   1377   -151   -236    495       O
ATOM   1421  CB  SER L  65      76.268 185.235  57.782  1.00 22.17           C
ANISOU 1421  CB  SER L  65     5097   1692   1633    -12   -805    532       C
ATOM   1422  OG  SER L  65      75.434 186.173  58.433  1.00 36.10           O
ANISOU 1422  OG  SER L  65     6971   3479   3268   -113   -632    518       O
ATOM   1423  N   ARG L  66      74.143 183.417  56.505  1.00 18.88           N
ANISOU 1423  N   ARG L  66     4648   1255   1271   -142   -409    593       N
ATOM   1424  CA  ARG L  66      72.819 182.872  56.276  1.00 18.18           C
ANISOU 1424  CA  ARG L  66     4583   1171   1155   -268   -168    598       C
ATOM   1425  C   ARG L  66      72.408 181.856  57.317  1.00 24.64           C
ANISOU 1425  C   ARG L  66     5770   1825   1768   -368   -124    664       C
ATOM   1426  O   ARG L  66      73.223 181.039  57.743  1.00 26.81           O
ANISOU 1426  O   ARG L  66     6264   1953   1970   -296   -322    726       O
ATOM   1427  CB  ARG L  66      72.804 182.233  54.885  1.00 13.79           C
ANISOU 1427  CB  ARG L  66     3671    746    824   -226   -160    392       C
ATOM   1428  CG  ARG L  66      71.541 181.523  54.523  1.00 11.21           C
ANISOU 1428  CG  ARG L  66     3178    540    540   -311      8    137       C
ATOM   1429  CD  ARG L  66      71.858 180.512  53.479  1.00 15.13           C
ANISOU 1429  CD  ARG L  66     3817    858   1076   -313    -13    481       C
ATOM   1430  NE  ARG L  66      70.843 179.477  53.448  1.00 25.34           N
ANISOU 1430  NE  ARG L  66     5274   2040   2314   -475    155    561       N
ATOM   1431  CZ  ARG L  66      71.104 178.184  53.499  1.00 39.76           C
ANISOU 1431  CZ  ARG L  66     7307   3699   4100   -490    101    604       C
ATOM   1432  NH1 ARG L  66      72.355 177.758  53.585  1.00 26.14           N
ANISOU 1432  NH1 ARG L  66     5683   1862   2388   -328   -127    648       N
ATOM   1433  NH2 ARG L  66      70.121 177.304  53.460  1.00 36.74           N
ANISOU 1433  NH2 ARG L  66     7028   3258   3673   -666    273    592       N
ATOM   1434  N   SER L  67      71.118 181.884  57.685  1.00 21.30           N
ANISOU 1434  N   SER L  67     5416   1421   1255   -535    143    641       N
ATOM   1435  CA  SER L  67      70.482 180.926  58.584  1.00 23.15           C
ANISOU 1435  CA  SER L  67     6006   1502   1286   -694    274    690       C
ATOM   1436  C   SER L  67      69.101 180.630  57.982  1.00 26.07           C
ANISOU 1436  C   SER L  67     6201   1964   1741   -859    569    618       C
ATOM   1437  O   SER L  67      68.187 181.449  58.106  1.00 25.35           O
ANISOU 1437  O   SER L  67     5962   2003   1668   -935    774    536       O
ATOM   1438  CB  SER L  67      70.370 181.493  59.997  1.00 27.64           C
ANISOU 1438  CB  SER L  67     6878   2009   1614   -762    323    706       C
ATOM   1439  OG  SER L  67      69.571 180.656  60.818  1.00 42.86           O
ANISOU 1439  OG  SER L  67     9164   3794   3329   -956    514    743       O
ATOM   1440  N   GLY L  68      69.001 179.510  57.260  1.00 22.17           N
ANISOU 1440  N   GLY L  68     5691   1412   1323   -896    568    633       N
ATOM   1441  CA  GLY L  68      67.781 179.102  56.568  1.00 22.15           C
ANISOU 1441  CA  GLY L  68     5497   1498   1421  -1057    807    549       C
ATOM   1442  C   GLY L  68      67.396 180.089  55.482  1.00 24.87           C
ANISOU 1442  C   GLY L  68     5390   2076   1981   -971    829    451       C
ATOM   1443  O   GLY L  68      68.162 180.299  54.537  1.00 21.81           O
ANISOU 1443  O   GLY L  68     4817   1738   1730   -809    645    460       O
ATOM   1444  N   THR L  69      66.231 180.749  55.647  1.00 22.91           N
ANISOU 1444  N   THR L  69     4979   1967   1758  -1071   1053    351       N
ATOM   1445  CA  THR L  69      65.731 181.772  54.714  1.00 21.62           C
ANISOU 1445  CA  THR L  69     4421   2014   1781   -971   1067    254       C
ATOM   1446  C   THR L  69      66.119 183.195  55.158  1.00 25.55           C
ANISOU 1446  C   THR L  69     4889   2564   2256   -832   1011    253       C
ATOM   1447  O   THR L  69      65.703 184.161  54.522  1.00 25.50           O
ANISOU 1447  O   THR L  69     4613   2700   2377   -735   1021    181       O
ATOM   1448  CB  THR L  69      64.199 181.653  54.531  1.00 30.71           C
ANISOU 1448  CB  THR L  69     5363   3297   3009  -1130   1320    116       C
ATOM   1449  OG1 THR L  69      63.553 181.760  55.797  1.00 33.10           O
ANISOU 1449  OG1 THR L  69     5848   3561   3167  -1289   1552     80       O
ATOM   1450  CG2 THR L  69      63.783 180.381  53.839  1.00 27.30           C
ANISOU 1450  CG2 THR L  69     4883   2847   2643  -1266   1358     88       C
ATOM   1451  N   ASP L  70      66.892 183.325  56.257  1.00 23.22           N
ANISOU 1451  N   ASP L  70     4893   2141   1790   -822    942    329       N
ATOM   1452  CA  ASP L  70      67.324 184.617  56.790  1.00 22.80           C
ANISOU 1452  CA  ASP L  70     4860   2111   1692   -718    886    322       C
ATOM   1453  C   ASP L  70      68.772 184.895  56.404  1.00 24.80           C
ANISOU 1453  C   ASP L  70     5113   2324   1987   -559    604    393       C
ATOM   1454  O   ASP L  70      69.675 184.123  56.736  1.00 26.14           O
ANISOU 1454  O   ASP L  70     5482   2369   2081   -544    444    471       O
ATOM   1455  CB  ASP L  70      67.133 184.698  58.326  1.00 27.86           C
ANISOU 1455  CB  ASP L  70     5833   2652   2099   -832   1009    331       C
ATOM   1456  CG  ASP L  70      65.747 184.330  58.848  1.00 53.09           C
ANISOU 1456  CG  ASP L  70     9058   5877   5237  -1030   1333    246       C
ATOM   1457  OD1 ASP L  70      64.764 184.487  58.090  1.00 54.90           O
ANISOU 1457  OD1 ASP L  70     8963   6258   5639  -1042   1475    138       O
ATOM   1458  OD2 ASP L  70      65.647 183.895  60.026  1.00 66.88           O
ANISOU 1458  OD2 ASP L  70    11158   7495   6758  -1176   1446    278       O
ATOM   1459  N   PHE L  71      68.987 186.001  55.700  1.00 18.00           N
ANISOU 1459  N   PHE L  71     4027   1562   1250   -440    547    354       N
ATOM   1460  CA  PHE L  71      70.291 186.421  55.203  1.00 14.84           C
ANISOU 1460  CA  PHE L  71     3570   1150    919   -317    326    389       C
ATOM   1461  C   PHE L  71      70.753 187.697  55.897  1.00 18.90           C
ANISOU 1461  C   PHE L  71     4157   1654   1368   -276    283    370       C
ATOM   1462  O   PHE L  71      69.943 188.583  56.181  1.00 18.75           O
ANISOU 1462  O   PHE L  71     4113   1682   1330   -285    429    312       O
ATOM   1463  CB  PHE L  71      70.231 186.616  53.681  1.00 13.44           C
ANISOU 1463  CB  PHE L  71     3109   1074    924   -243    307    361       C
ATOM   1464  CG  PHE L  71      69.903 185.348  52.919  1.00 13.53           C
ANISOU 1464  CG  PHE L  71     3053   1089    999   -284    324    370       C
ATOM   1465  CD1 PHE L  71      68.583 184.937  52.752  1.00 14.78           C
ANISOU 1465  CD1 PHE L  71     3137   1306   1173   -376    495    319       C
ATOM   1466  CD2 PHE L  71      70.914 184.582  52.340  1.00 13.44           C
ANISOU 1466  CD2 PHE L  71     3037   1025   1044   -234    174    408       C
ATOM   1467  CE1 PHE L  71      68.284 183.778  52.034  1.00 14.71           C
ANISOU 1467  CE1 PHE L  71     3076   1293   1220   -435    509    315       C
ATOM   1468  CE2 PHE L  71      70.611 183.430  51.615  1.00 14.92           C
ANISOU 1468  CE2 PHE L  71     3184   1201   1286   -272    196    406       C
ATOM   1469  CZ  PHE L  71      69.299 183.033  51.472  1.00 13.23           C
ANISOU 1469  CZ  PHE L  71     2920   1035   1071   -381    359    363       C
ATOM   1470  N   THR L  72      72.058 187.793  56.154  1.00 14.89           N
ANISOU 1470  N   THR L  72     3727   1089    842   -226     77    402       N
ATOM   1471  CA  THR L  72      72.649 188.927  56.842  1.00 14.49           C
ANISOU 1471  CA  THR L  72     3762   1018    726   -209      6    374       C
ATOM   1472  C   THR L  72      73.881 189.462  56.106  1.00 17.64           C
ANISOU 1472  C   THR L  72     3999   1445   1259   -139   -163    357       C
ATOM   1473  O   THR L  72      74.742 188.686  55.690  1.00 17.25           O
ANISOU 1473  O   THR L  72     3884   1386   1286   -100   -310    378       O
ATOM   1474  CB  THR L  72      72.989 188.514  58.299  1.00 24.10           C
ANISOU 1474  CB  THR L  72     5298   2125   1732   -260    -79    407       C
ATOM   1475  OG1 THR L  72      71.785 188.168  58.993  1.00 27.80           O
ANISOU 1475  OG1 THR L  72     5933   2566   2062   -360    137    408       O
ATOM   1476  CG2 THR L  72      73.727 189.592  59.073  1.00 22.88           C
ANISOU 1476  CG2 THR L  72     5252   1944   1497   -252   -194    369       C
ATOM   1477  N   LEU L  73      73.974 190.794  55.996  1.00 13.46           N
ANISOU 1477  N   LEU L  73     3421    940    755   -131   -129    307       N
ATOM   1478  CA  LEU L  73      75.141 191.497  55.501  1.00 12.89           C
ANISOU 1478  CA  LEU L  73     3238    879    781   -114   -253    272       C
ATOM   1479  C   LEU L  73      75.708 192.278  56.691  1.00 20.03           C
ANISOU 1479  C   LEU L  73     4317   1726   1566   -157   -345    233       C
ATOM   1480  O   LEU L  73      74.989 193.067  57.315  1.00 20.31           O
ANISOU 1480  O   LEU L  73     4487   1732   1497   -182   -226    208       O
ATOM   1481  CB  LEU L  73      74.779 192.462  54.360  1.00 11.45           C
ANISOU 1481  CB  LEU L  73     2908    740    704    -90   -134    248       C
ATOM   1482  CG  LEU L  73      75.897 193.389  53.847  1.00 14.23           C
ANISOU 1482  CG  LEU L  73     3183   1085   1138   -115   -203    202       C
ATOM   1483  CD1 LEU L  73      76.918 192.630  53.004  1.00 12.98           C
ANISOU 1483  CD1 LEU L  73     2853    969   1111   -112   -305    197       C
ATOM   1484  CD2 LEU L  73      75.326 194.506  53.048  1.00 15.07           C
ANISOU 1484  CD2 LEU L  73     3265   1183   1276    -95    -71    192       C
ATOM   1485  N   THR L  74      76.974 192.028  57.030  1.00 17.71           N
ANISOU 1485  N   THR L  74     4019   1420   1290   -159   -562    212       N
ATOM   1486  CA  THR L  74      77.622 192.748  58.114  1.00 18.67           C
ANISOU 1486  CA  THR L  74     4294   1497   1305   -207   -691    158       C
ATOM   1487  C   THR L  74      78.752 193.601  57.561  1.00 23.49           C
ANISOU 1487  C   THR L  74     4725   2143   2058   -245   -778     73       C
ATOM   1488  O   THR L  74      79.521 193.145  56.713  1.00 23.25           O
ANISOU 1488  O   THR L  74     4475   2168   2192   -220   -851     54       O
ATOM   1489  CB  THR L  74      78.091 191.800  59.244  1.00 23.58           C
ANISOU 1489  CB  THR L  74     5110   2063   1786   -186   -901    187       C
ATOM   1490  OG1 THR L  74      77.055 190.874  59.568  1.00 22.27           O
ANISOU 1490  OG1 THR L  74     5111   1854   1498   -179   -782    269       O
ATOM   1491  CG2 THR L  74      78.492 192.551  60.503  1.00 21.35           C
ANISOU 1491  CG2 THR L  74     5048   1729   1336   -242  -1024    132       C
ATOM   1492  N   ILE L  75      78.790 194.866  57.988  1.00 20.44           N
ANISOU 1492  N   ILE L  75     4436   1720   1612   -319   -737     12       N
ATOM   1493  CA  ILE L  75      79.861 195.809  57.706  1.00 20.73           C
ANISOU 1493  CA  ILE L  75     4361   1767   1750   -404   -808    -87       C
ATOM   1494  C   ILE L  75      80.433 196.039  59.093  1.00 27.58           C
ANISOU 1494  C   ILE L  75     5408   2596   2476   -453  -1003   -147       C
ATOM   1495  O   ILE L  75      79.859 196.800  59.877  1.00 27.55           O
ANISOU 1495  O   ILE L  75     5635   2520   2313   -494   -927   -162       O
ATOM   1496  CB  ILE L  75      79.410 197.119  56.998  1.00 22.71           C
ANISOU 1496  CB  ILE L  75     4620   1974   2035   -458   -601   -109       C
ATOM   1497  CG1 ILE L  75      78.418 196.831  55.834  1.00 21.04           C
ANISOU 1497  CG1 ILE L  75     4316   1786   1894   -375   -415    -29       C
ATOM   1498  CG2 ILE L  75      80.640 197.893  56.503  1.00 23.45           C
ANISOU 1498  CG2 ILE L  75     4581   2076   2254   -582   -656   -213       C
ATOM   1499  CD1 ILE L  75      77.552 198.066  55.362  1.00 18.13           C
ANISOU 1499  CD1 ILE L  75     4036   1345   1507   -369   -223    -28       C
ATOM   1500  N   SER L  76      81.471 195.246  59.440  1.00 26.49           N
ANISOU 1500  N   SER L  76     5184   2501   2381   -422  -1266   -180       N
ATOM   1501  CA  SER L  76      82.116 195.175  60.761  1.00 28.67           C
ANISOU 1501  CA  SER L  76     5630   2749   2515   -435  -1532   -233       C
ATOM   1502  C   SER L  76      82.478 196.519  61.369  1.00 35.73           C
ANISOU 1502  C   SER L  76     6628   3607   3340   -571  -1554   -345       C
ATOM   1503  O   SER L  76      82.263 196.723  62.570  1.00 38.72           O
ANISOU 1503  O   SER L  76     7297   3919   3496   -594  -1635   -353       O
ATOM   1504  CB  SER L  76      83.342 194.269  60.711  1.00 32.93           C
ANISOU 1504  CB  SER L  76     5964   3358   3190   -359  -1829   -284       C
ATOM   1505  OG  SER L  76      84.346 194.791  59.855  1.00 40.68           O
ANISOU 1505  OG  SER L  76     6617   4428   4412   -434  -1843   -410       O
ATOM   1506  N   THR L  77      83.061 197.419  60.557  1.00 31.08           N
ANISOU 1506  N   THR L  77     5829   3052   2928   -676  -1478   -438       N
ATOM   1507  CA  THR L  77      83.483 198.756  60.965  1.00 31.98           C
ANISOU 1507  CA  THR L  77     6024   3120   3007   -835  -1478   -559       C
ATOM   1508  C   THR L  77      83.162 199.672  59.802  1.00 33.12           C
ANISOU 1508  C   THR L  77     6081   3232   3273   -910  -1197   -560       C
ATOM   1509  O   THR L  77      83.808 199.562  58.761  1.00 32.49           O
ANISOU 1509  O   THR L  77     5730   3220   3393   -948  -1166   -594       O
ATOM   1510  CB  THR L  77      84.995 198.754  61.306  1.00 46.07           C
ANISOU 1510  CB  THR L  77     7621   4986   4900   -914  -1782   -716       C
ATOM   1511  OG1 THR L  77      85.256 197.794  62.329  1.00 49.20           O
ANISOU 1511  OG1 THR L  77     8123   5399   5172   -798  -2078   -696       O
ATOM   1512  CG2 THR L  77      85.506 200.117  61.747  1.00 47.34           C
ANISOU 1512  CG2 THR L  77     7864   5097   5025  -1111  -1797   -863       C
ATOM   1513  N   LEU L  78      82.139 200.538  59.953  1.00 28.32           N
ANISOU 1513  N   LEU L  78     5713   2511   2535   -918   -987   -522       N
ATOM   1514  CA  LEU L  78      81.724 201.467  58.903  1.00 27.25           C
ANISOU 1514  CA  LEU L  78     5567   2308   2478   -958   -739   -508       C
ATOM   1515  C   LEU L  78      82.790 202.479  58.574  1.00 32.30           C
ANISOU 1515  C   LEU L  78     6137   2916   3220  -1157   -746   -638       C
ATOM   1516  O   LEU L  78      83.292 203.164  59.466  1.00 34.40           O
ANISOU 1516  O   LEU L  78     6531   3131   3406  -1280   -848   -749       O
ATOM   1517  CB  LEU L  78      80.449 202.231  59.294  1.00 27.24           C
ANISOU 1517  CB  LEU L  78     5851   2181   2318   -897   -550   -468       C
ATOM   1518  CG  LEU L  78      79.115 201.551  59.057  1.00 30.19           C
ANISOU 1518  CG  LEU L  78     6246   2575   2651   -720   -410   -346       C
ATOM   1519  CD1 LEU L  78      78.044 202.234  59.848  1.00 31.04           C
ANISOU 1519  CD1 LEU L  78     6620   2580   2595   -670   -271   -359       C
ATOM   1520  CD2 LEU L  78      78.733 201.558  57.579  1.00 28.37           C
ANISOU 1520  CD2 LEU L  78     5856   2359   2565   -657   -262   -277       C
ATOM   1521  N   GLU L  79      83.111 202.600  57.285  1.00 27.98           N
ANISOU 1521  N   GLU L  79     5410   2389   2834  -1207   -620   -632       N
ATOM   1522  CA  GLU L  79      84.029 203.610  56.782  1.00 29.44           C
ANISOU 1522  CA  GLU L  79     5545   2526   3116  -1429   -554   -751       C
ATOM   1523  C   GLU L  79      83.178 204.732  56.152  1.00 33.33           C
ANISOU 1523  C   GLU L  79     6290   2837   3536  -1438   -300   -689       C
ATOM   1524  O   GLU L  79      82.016 204.472  55.821  1.00 31.92           O
ANISOU 1524  O   GLU L  79     6203   2629   3297  -1249   -197   -558       O
ATOM   1525  CB  GLU L  79      85.011 203.007  55.765  1.00 31.03           C
ANISOU 1525  CB  GLU L  79     5403   2857   3530  -1499   -560   -800       C
ATOM   1526  CG  GLU L  79      86.061 202.091  56.379  1.00 44.75           C
ANISOU 1526  CG  GLU L  79     6875   4756   5370  -1497   -836   -906       C
ATOM   1527  CD  GLU L  79      86.896 202.668  57.507  1.00 82.09           C
ANISOU 1527  CD  GLU L  79    11637   9487  10069  -1646  -1038  -1069       C
ATOM   1528  OE1 GLU L  79      87.514 203.739  57.309  1.00 86.96           O
ANISOU 1528  OE1 GLU L  79    12253  10048  10740  -1882   -949  -1197       O
ATOM   1529  OE2 GLU L  79      86.946 202.032  58.586  1.00 82.33           O
ANISOU 1529  OE2 GLU L  79    11711   9565  10007  -1537  -1289  -1072       O
ATOM   1530  N   PRO L  80      83.690 205.986  56.004  1.00 31.54           N
ANISOU 1530  N   PRO L  80     6194   2479   3311  -1647   -206   -785       N
ATOM   1531  CA  PRO L  80      82.862 207.060  55.413  1.00 31.58           C
ANISOU 1531  CA  PRO L  80     6490   2277   3233  -1625     13   -718       C
ATOM   1532  C   PRO L  80      82.220 206.741  54.049  1.00 35.75           C
ANISOU 1532  C   PRO L  80     6982   2800   3803  -1490    164   -579       C
ATOM   1533  O   PRO L  80      81.111 207.200  53.765  1.00 35.67           O
ANISOU 1533  O   PRO L  80     7188   2662   3701  -1329    272   -484       O
ATOM   1534  CB  PRO L  80      83.846 208.227  55.308  1.00 35.49           C
ANISOU 1534  CB  PRO L  80     7075   2650   3759  -1923     80   -856       C
ATOM   1535  CG  PRO L  80      84.836 207.972  56.371  1.00 40.60           C
ANISOU 1535  CG  PRO L  80     7562   3420   4445  -2062   -139  -1010       C
ATOM   1536  CD  PRO L  80      85.030 206.497  56.365  1.00 34.87           C
ANISOU 1536  CD  PRO L  80     6515   2922   3812  -1916   -300   -969       C
ATOM   1537  N   GLU L  81      82.908 205.935  53.222  1.00 31.60           N
ANISOU 1537  N   GLU L  81     6177   2416   3415  -1543    157   -580       N
ATOM   1538  CA  GLU L  81      82.452 205.511  51.894  1.00 29.86           C
ANISOU 1538  CA  GLU L  81     5905   2212   3229  -1441    280   -465       C
ATOM   1539  C   GLU L  81      81.363 204.423  51.939  1.00 29.99           C
ANISOU 1539  C   GLU L  81     5845   2331   3218  -1165    216   -343       C
ATOM   1540  O   GLU L  81      80.827 204.069  50.898  1.00 27.33           O
ANISOU 1540  O   GLU L  81     5488   2005   2892  -1059    298   -248       O
ATOM   1541  CB  GLU L  81      83.650 205.053  51.018  1.00 32.05           C
ANISOU 1541  CB  GLU L  81     5911   2603   3662  -1619    319   -539       C
ATOM   1542  CG  GLU L  81      84.525 203.952  51.625  1.00 44.83           C
ANISOU 1542  CG  GLU L  81     7185   4434   5414  -1628    125   -635       C
ATOM   1543  CD  GLU L  81      85.705 204.384  52.490  1.00 75.19           C
ANISOU 1543  CD  GLU L  81    10927   8314   9329  -1842      6   -820       C
ATOM   1544  OE1 GLU L  81      85.674 205.505  53.051  1.00 58.01           O
ANISOU 1544  OE1 GLU L  81     8988   5993   7062  -1968     39   -870       O
ATOM   1545  OE2 GLU L  81      86.648 203.573  52.636  1.00 79.15           O
ANISOU 1545  OE2 GLU L  81    11107   8989   9979  -1871   -138   -924       O
ATOM   1546  N   ASP L  82      81.036 203.896  53.130  1.00 26.54           N
ANISOU 1546  N   ASP L  82     5386   1963   2735  -1068     76   -351       N
ATOM   1547  CA  ASP L  82      80.045 202.821  53.251  1.00 24.80           C
ANISOU 1547  CA  ASP L  82     5097   1838   2488   -850     36   -251       C
ATOM   1548  C   ASP L  82      78.599 203.299  53.444  1.00 28.73           C
ANISOU 1548  C   ASP L  82     5805   2237   2872   -677    130   -183       C
ATOM   1549  O   ASP L  82      77.681 202.485  53.407  1.00 27.45           O
ANISOU 1549  O   ASP L  82     5576   2153   2701   -515    133   -112       O
ATOM   1550  CB  ASP L  82      80.448 201.840  54.354  1.00 26.35           C
ANISOU 1550  CB  ASP L  82     5176   2154   2681   -836   -151   -288       C
ATOM   1551  CG  ASP L  82      81.799 201.192  54.150  1.00 33.35           C
ANISOU 1551  CG  ASP L  82     5804   3159   3709   -944   -278   -365       C
ATOM   1552  OD1 ASP L  82      82.270 201.141  52.983  1.00 33.59           O
ANISOU 1552  OD1 ASP L  82     5687   3219   3856  -1004   -188   -372       O
ATOM   1553  OD2 ASP L  82      82.378 200.718  55.143  1.00 36.48           O
ANISOU 1553  OD2 ASP L  82     6147   3619   4097   -959   -469   -426       O
ATOM   1554  N   PHE L  83      78.388 204.598  53.648  1.00 26.82           N
ANISOU 1554  N   PHE L  83     5808   1827   2557   -710    211   -218       N
ATOM   1555  CA  PHE L  83      77.034 205.128  53.803  1.00 26.22           C
ANISOU 1555  CA  PHE L  83     5913   1653   2396   -520    301   -178       C
ATOM   1556  C   PHE L  83      76.358 205.191  52.424  1.00 29.32           C
ANISOU 1556  C   PHE L  83     6300   2015   2826   -386    381    -86       C
ATOM   1557  O   PHE L  83      76.757 205.984  51.559  1.00 30.12           O
ANISOU 1557  O   PHE L  83     6529   1988   2926   -462    444    -74       O
ATOM   1558  CB  PHE L  83      77.050 206.488  54.524  1.00 29.32           C
ANISOU 1558  CB  PHE L  83     6590   1855   2694   -579    351   -257       C
ATOM   1559  CG  PHE L  83      77.550 206.389  55.945  1.00 31.02           C
ANISOU 1559  CG  PHE L  83     6839   2106   2843   -689    255   -351       C
ATOM   1560  CD1 PHE L  83      76.696 206.020  56.976  1.00 34.37           C
ANISOU 1560  CD1 PHE L  83     7314   2571   3174   -566    253   -359       C
ATOM   1561  CD2 PHE L  83      78.884 206.632  56.248  1.00 33.99           C
ANISOU 1561  CD2 PHE L  83     7193   2480   3242   -925    164   -443       C
ATOM   1562  CE1 PHE L  83      77.163 205.922  58.291  1.00 36.50           C
ANISOU 1562  CE1 PHE L  83     7666   2860   3344   -670    153   -440       C
ATOM   1563  CE2 PHE L  83      79.351 206.526  57.559  1.00 37.82           C
ANISOU 1563  CE2 PHE L  83     7722   2999   3649  -1015     34   -533       C
ATOM   1564  CZ  PHE L  83      78.491 206.163  58.572  1.00 36.25           C
ANISOU 1564  CZ  PHE L  83     7623   2824   3327   -883     24   -522       C
ATOM   1565  N   ALA L  84      75.404 204.266  52.198  1.00 23.05           N
ANISOU 1565  N   ALA L  84     5357   1344   2057   -210    371    -24       N
ATOM   1566  CA  ALA L  84      74.672 204.095  50.939  1.00 20.66           C
ANISOU 1566  CA  ALA L  84     5011   1053   1786    -63    403     56       C
ATOM   1567  C   ALA L  84      73.391 203.279  51.164  1.00 21.82           C
ANISOU 1567  C   ALA L  84     5017   1323   1949    130    396     76       C
ATOM   1568  O   ALA L  84      73.063 202.945  52.309  1.00 21.84           O
ANISOU 1568  O   ALA L  84     4995   1380   1924    138    399     32       O
ATOM   1569  CB  ALA L  84      75.560 203.380  49.937  1.00 20.27           C
ANISOU 1569  CB  ALA L  84     4806   1088   1806   -181    380     92       C
ATOM   1570  N   VAL L  85      72.664 202.960  50.073  1.00 15.83           N
ANISOU 1570  N   VAL L  85     4178    609   1228    269    393    135       N
ATOM   1571  CA  VAL L  85      71.473 202.097  50.121  1.00 13.49           C
ANISOU 1571  CA  VAL L  85     3699    458    968    422    388    136       C
ATOM   1572  C   VAL L  85      71.923 200.683  49.746  1.00 15.17           C
ANISOU 1572  C   VAL L  85     3703    819   1240    332    339    175       C
ATOM   1573  O   VAL L  85      72.699 200.520  48.812  1.00 13.55           O
ANISOU 1573  O   VAL L  85     3480    611   1056    252    313    214       O
ATOM   1574  CB  VAL L  85      70.288 202.602  49.253  1.00 15.93           C
ANISOU 1574  CB  VAL L  85     4035    724   1293    651    383    152       C
ATOM   1575  CG1 VAL L  85      69.086 201.675  49.372  1.00 15.28           C
ANISOU 1575  CG1 VAL L  85     3721    809   1276    778    385    121       C
ATOM   1576  CG2 VAL L  85      69.893 204.022  49.637  1.00 16.50           C
ANISOU 1576  CG2 VAL L  85     4342    614   1316    767    424    109       C
ATOM   1577  N   TYR L  86      71.497 199.680  50.516  1.00 12.33           N
ANISOU 1577  N   TYR L  86     3211    579    895    330    341    156       N
ATOM   1578  CA  TYR L  86      71.877 198.285  50.290  1.00 11.20           C
ANISOU 1578  CA  TYR L  86     2899    556    799    256    292    188       C
ATOM   1579  C   TYR L  86      70.678 197.435  49.911  1.00 14.85           C
ANISOU 1579  C   TYR L  86     3208   1130   1304    357    313    192       C
ATOM   1580  O   TYR L  86      69.635 197.512  50.567  1.00 13.88           O
ANISOU 1580  O   TYR L  86     3067   1035   1171    431    380    145       O
ATOM   1581  CB  TYR L  86      72.591 197.710  51.532  1.00 12.19           C
ANISOU 1581  CB  TYR L  86     3041    701    889    136    256    169       C
ATOM   1582  CG  TYR L  86      73.948 198.337  51.774  1.00 13.25           C
ANISOU 1582  CG  TYR L  86     3264    761   1011     12    199    146       C
ATOM   1583  CD1 TYR L  86      74.069 199.551  52.446  1.00 15.41           C
ANISOU 1583  CD1 TYR L  86     3715    923   1218    -14    228     98       C
ATOM   1584  CD2 TYR L  86      75.102 197.749  51.283  1.00 13.46           C
ANISOU 1584  CD2 TYR L  86     3183    828   1105    -83    123    152       C
ATOM   1585  CE1 TYR L  86      75.313 200.152  52.634  1.00 15.18           C
ANISOU 1585  CE1 TYR L  86     3752    829   1187   -155    177     58       C
ATOM   1586  CE2 TYR L  86      76.347 198.343  51.459  1.00 14.95           C
ANISOU 1586  CE2 TYR L  86     3405    967   1309   -211     77    103       C
ATOM   1587  CZ  TYR L  86      76.449 199.543  52.133  1.00 20.87           C
ANISOU 1587  CZ  TYR L  86     4328   1611   1990   -259    101     55       C
ATOM   1588  OH  TYR L  86      77.690 200.108  52.279  1.00 22.22           O
ANISOU 1588  OH  TYR L  86     4515   1741   2187   -413     57    -12       O
ATOM   1589  N   TYR L  87      70.830 196.623  48.840  1.00 11.40           N
ANISOU 1589  N   TYR L  87     2654    760    918    349    268    231       N
ATOM   1590  CA  TYR L  87      69.786 195.730  48.340  1.00 11.08           C
ANISOU 1590  CA  TYR L  87     2456    831    924    416    271    225       C
ATOM   1591  C   TYR L  87      70.229 194.285  48.345  1.00 15.98           C
ANISOU 1591  C   TYR L  87     2976   1521   1573    312    245    245       C
ATOM   1592  O   TYR L  87      71.396 193.995  48.083  1.00 13.98           O
ANISOU 1592  O   TYR L  87     2740   1243   1330    232    198    273       O
ATOM   1593  CB  TYR L  87      69.411 196.095  46.898  1.00 11.49           C
ANISOU 1593  CB  TYR L  87     2492    883    992    521    223    246       C
ATOM   1594  CG  TYR L  87      68.785 197.458  46.740  1.00 13.20           C
ANISOU 1594  CG  TYR L  87     2824   1013   1180    671    222    229       C
ATOM   1595  CD1 TYR L  87      67.409 197.628  46.834  1.00 15.92           C
ANISOU 1595  CD1 TYR L  87     3070   1416   1565    831    225    167       C
ATOM   1596  CD2 TYR L  87      69.563 198.574  46.446  1.00 13.92           C
ANISOU 1596  CD2 TYR L  87     3121    955   1211    657    218    264       C
ATOM   1597  CE1 TYR L  87      66.824 198.889  46.703  1.00 18.09           C
ANISOU 1597  CE1 TYR L  87     3454   1596   1823   1009    206    142       C
ATOM   1598  CE2 TYR L  87      68.990 199.834  46.287  1.00 16.50           C
ANISOU 1598  CE2 TYR L  87     3600   1167   1501    810    209    254       C
ATOM   1599  CZ  TYR L  87      67.620 199.991  46.440  1.00 23.24           C
ANISOU 1599  CZ  TYR L  87     4358   2073   2398   1005    193    195       C
ATOM   1600  OH  TYR L  87      67.049 201.228  46.275  1.00 21.36           O
ANISOU 1600  OH  TYR L  87     4272   1709   2134   1194    165    177       O
ATOM   1601  N   CYS L  88      69.286 193.367  48.583  1.00 15.63           N
ANISOU 1601  N   CYS L  88     2824   1563   1553    314    283    219       N
ATOM   1602  CA  CYS L  88      69.559 191.950  48.422  1.00 15.99           C
ANISOU 1602  CA  CYS L  88     2798   1654   1623    228    259    240       C
ATOM   1603  C   CYS L  88      68.860 191.511  47.119  1.00 17.55           C
ANISOU 1603  C   CYS L  88     2863   1929   1875    279    235    227       C
ATOM   1604  O   CYS L  88      67.863 192.120  46.725  1.00 16.53           O
ANISOU 1604  O   CYS L  88     2675   1843   1765    381    242    187       O
ATOM   1605  CB  CYS L  88      69.132 191.117  49.633  1.00 17.81           C
ANISOU 1605  CB  CYS L  88     3053   1895   1817    149    326    223       C
ATOM   1606  SG  CYS L  88      67.391 191.288  50.101  1.00 24.27           S
ANISOU 1606  SG  CYS L  88     3777   2796   2650    182    467    135       S
ATOM   1607  N   GLN L  89      69.453 190.558  46.394  1.00 11.48           N
ANISOU 1607  N   GLN L  89     2060   1172   1131    226    189    251       N
ATOM   1608  CA  GLN L  89      68.880 190.042  45.163  1.00 10.49           C
ANISOU 1608  CA  GLN L  89     1835   1115   1038    254    156    233       C
ATOM   1609  C   GLN L  89      68.937 188.528  45.154  1.00 14.15           C
ANISOU 1609  C   GLN L  89     2247   1600   1528    159    162    225       C
ATOM   1610  O   GLN L  89      69.996 187.932  45.346  1.00 12.64           O
ANISOU 1610  O   GLN L  89     2112   1350   1339    105    143    256       O
ATOM   1611  CB  GLN L  89      69.561 190.619  43.921  1.00 11.08           C
ANISOU 1611  CB  GLN L  89     1965   1155   1089    295    103    262       C
ATOM   1612  CG  GLN L  89      68.787 190.317  42.643  1.00  6.49           C
ANISOU 1612  CG  GLN L  89     1182    699    587    279     97     44       C
ATOM   1613  CD  GLN L  89      69.622 190.378  41.400  1.00 20.06           C
ANISOU 1613  CD  GLN L  89     3123   2321   2177    335     20    267       C
ATOM   1614  OE1 GLN L  89      70.857 190.399  41.433  1.00 19.49           O
ANISOU 1614  OE1 GLN L  89     3112   2188   2104    265     61    290       O
ATOM   1615  NE2 GLN L  89      68.959 190.370  40.263  1.00 11.30           N
ANISOU 1615  NE2 GLN L  89     2013   1253   1028    396    -48    252       N
ATOM   1616  N   GLN L  90      67.789 187.920  44.917  1.00 11.15           N
ANISOU 1616  N   GLN L  90     1758   1300   1179    142    183    172       N
ATOM   1617  CA  GLN L  90      67.596 186.485  44.860  1.00 10.65           C
ANISOU 1617  CA  GLN L  90     1661   1249   1139     36    204    151       C
ATOM   1618  C   GLN L  90      67.916 186.016  43.414  1.00 15.17           C
ANISOU 1618  C   GLN L  90     2206   1836   1722     49    130    145       C
ATOM   1619  O   GLN L  90      67.520 186.667  42.458  1.00 13.30           O
ANISOU 1619  O   GLN L  90     1928   1652   1475    130     73    127       O
ATOM   1620  CB  GLN L  90      66.138 186.190  45.295  1.00 12.78           C
ANISOU 1620  CB  GLN L  90     1810   1606   1441    -16    284     69       C
ATOM   1621  CG  GLN L  90      65.520 184.894  44.810  1.00 22.05           C
ANISOU 1621  CG  GLN L  90     2904   2823   2652   -129    301     12       C
ATOM   1622  CD  GLN L  90      64.821 185.068  43.501  1.00 28.92           C
ANISOU 1622  CD  GLN L  90     3626   3800   3562    -64    210    -54       C
ATOM   1623  OE1 GLN L  90      65.148 184.408  42.526  1.00 34.60           O
ANISOU 1623  OE1 GLN L  90     4362   4511   4275    -89    146    -55       O
ATOM   1624  NE2 GLN L  90      63.861 185.972  43.437  1.00 11.74           N
ANISOU 1624  NE2 GLN L  90     1316   1723   1423     37    190   -118       N
ATOM   1625  N   ARG L  91      68.692 184.937  43.272  1.00 13.46           N
ANISOU 1625  N   ARG L  91     2043   1558   1513    -17    126    160       N
ATOM   1626  CA  ARG L  91      69.078 184.398  41.964  1.00 13.41           C
ANISOU 1626  CA  ARG L  91     2032   1554   1509    -15     83    141       C
ATOM   1627  C   ARG L  91      68.738 182.912  41.900  1.00 16.23           C
ANISOU 1627  C   ARG L  91     2385   1891   1891   -115    103    101       C
ATOM   1628  O   ARG L  91      69.366 182.158  41.159  1.00 15.63           O
ANISOU 1628  O   ARG L  91     2347   1770   1820   -128     86     87       O
ATOM   1629  CB  ARG L  91      70.580 184.616  41.684  1.00 15.81           C
ANISOU 1629  CB  ARG L  91     2408   1787   1812     18     72    177       C
ATOM   1630  CG  ARG L  91      71.084 186.006  42.016  1.00 24.16           C
ANISOU 1630  CG  ARG L  91     3501   2832   2848     73     73    216       C
ATOM   1631  CD  ARG L  91      71.189 186.878  40.787  1.00 19.78           C
ANISOU 1631  CD  ARG L  91     2980   2294   2244    117     62    216       C
ATOM   1632  NE  ARG L  91      72.144 187.967  41.012  1.00 16.43           N
ANISOU 1632  NE  ARG L  91     2621   1815   1806    126     89    246       N
ATOM   1633  CZ  ARG L  91      73.459 187.838  40.864  1.00 33.10           C
ANISOU 1633  CZ  ARG L  91     4738   3885   3952     82    123    233       C
ATOM   1634  NH1 ARG L  91      73.982 186.677  40.499  1.00 23.70           N
ANISOU 1634  NH1 ARG L  91     3500   2693   2810     55    131    194       N
ATOM   1635  NH2 ARG L  91      74.258 188.866  41.088  1.00 22.44           N
ANISOU 1635  NH2 ARG L  91     3434   2495   2599     62    154    242       N
ATOM   1636  N   TYR L  92      67.735 182.501  42.678  1.00 12.73           N
ANISOU 1636  N   TYR L  92     1905   1472   1459   -197    158     71       N
ATOM   1637  CA  TYR L  92      67.296 181.127  42.744  1.00 12.68           C
ANISOU 1637  CA  TYR L  92     1922   1429   1468   -326    200     30       C
ATOM   1638  C   TYR L  92      66.534 180.702  41.495  1.00 19.66           C
ANISOU 1638  C   TYR L  92     2702   2399   2370   -363    160    -58       C
ATOM   1639  O   TYR L  92      65.564 181.356  41.091  1.00 19.36           O
ANISOU 1639  O   TYR L  92     2521   2490   2347   -331    125   -115       O
ATOM   1640  CB  TYR L  92      66.464 180.892  44.007  1.00 13.64           C
ANISOU 1640  CB  TYR L  92     2054   1546   1583   -436    307     16       C
ATOM   1641  CG  TYR L  92      65.917 179.485  44.120  1.00 16.94           C
ANISOU 1641  CG  TYR L  92     2524   1907   2004   -609    380    -32       C
ATOM   1642  CD1 TYR L  92      66.728 178.429  44.531  1.00 18.51           C
ANISOU 1642  CD1 TYR L  92     2935   1931   2167   -653    385     25       C
ATOM   1643  CD2 TYR L  92      64.585 179.207  43.818  1.00 19.28           C
ANISOU 1643  CD2 TYR L  92     2664   2317   2346   -730    438   -145       C
ATOM   1644  CE1 TYR L  92      66.227 177.132  44.639  1.00 20.60           C
ANISOU 1644  CE1 TYR L  92     3297   2109   2421   -823    461    -14       C
ATOM   1645  CE2 TYR L  92      64.078 177.912  43.908  1.00 21.79           C
ANISOU 1645  CE2 TYR L  92     3040   2572   2666   -926    524   -200       C
ATOM   1646  CZ  TYR L  92      64.901 176.877  44.321  1.00 31.58           C
ANISOU 1646  CZ  TYR L  92     4537   3611   3851   -978    543   -127       C
ATOM   1647  OH  TYR L  92      64.402 175.595  44.392  1.00 37.96           O
ANISOU 1647  OH  TYR L  92     5448   4325   4649  -1180    634   -179       O
ATOM   1648  N   ASN L  93      66.988 179.585  40.898  1.00 18.46           N
ANISOU 1648  N   ASN L  93     2631   2168   2215   -419    151    -77       N
ATOM   1649  CA  ASN L  93      66.412 178.891  39.752  1.00 19.78           C
ANISOU 1649  CA  ASN L  93     2749   2384   2384   -485    113   -169       C
ATOM   1650  C   ASN L  93      66.326 179.731  38.446  1.00 24.73           C
ANISOU 1650  C   ASN L  93     3311   3115   2971   -378      8   -194       C
ATOM   1651  O   ASN L  93      67.273 179.732  37.648  1.00 26.68           O
ANISOU 1651  O   ASN L  93     3652   3309   3175   -318    -15   -171       O
ATOM   1652  CB  ASN L  93      65.037 178.286  40.130  1.00 21.35           C
ANISOU 1652  CB  ASN L  93     2843   2647   2621   -648    169   -261       C
ATOM   1653  CG  ASN L  93      64.327 177.569  39.012  1.00 34.32           C
ANISOU 1653  CG  ASN L  93     4415   4355   4272   -741    115   -379       C
ATOM   1654  OD1 ASN L  93      64.946 177.014  38.100  1.00 35.51           O
ANISOU 1654  OD1 ASN L  93     4667   4439   4385   -730     70   -390       O
ATOM   1655  ND2 ASN L  93      63.007 177.602  39.039  1.00 19.69           N
ANISOU 1655  ND2 ASN L  93     2369   2641   2470   -830    115   -489       N
ATOM   1656  N   TRP L  94      65.171 180.393  38.222  1.00 18.22           N
ANISOU 1656  N   TRP L  94     2335   2432   2157   -356    -53   -252       N
ATOM   1657  CA  TRP L  94      64.797 181.100  37.007  1.00 15.86           C
ANISOU 1657  CA  TRP L  94     1994   2229   1802   -256   -188   -287       C
ATOM   1658  C   TRP L  94      64.330 182.532  37.332  1.00 17.54           C
ANISOU 1658  C   TRP L  94     2125   2518   2020   -112   -240   -258       C
ATOM   1659  O   TRP L  94      63.741 182.722  38.395  1.00 16.67           O
ANISOU 1659  O   TRP L  94     1904   2445   1984   -133   -173   -275       O
ATOM   1660  CB  TRP L  94      63.619 180.320  36.392  1.00 15.20           C
ANISOU 1660  CB  TRP L  94     1782   2249   1745   -362   -257   -424       C
ATOM   1661  CG  TRP L  94      63.467 180.442  34.907  1.00 16.58           C
ANISOU 1661  CG  TRP L  94     1995   2478   1827   -305   -412   -473       C
ATOM   1662  CD1 TRP L  94      62.558 181.200  34.235  1.00 20.54           C
ANISOU 1662  CD1 TRP L  94     2392   3111   2303   -199   -585   -532       C
ATOM   1663  CD2 TRP L  94      64.241 179.765  33.910  1.00 16.24           C
ANISOU 1663  CD2 TRP L  94     2126   2351   1692   -344   -417   -477       C
ATOM   1664  NE1 TRP L  94      62.738 181.065  32.883  1.00 20.66           N
ANISOU 1664  NE1 TRP L  94     2536   3124   2189   -175   -708   -557       N
ATOM   1665  CE2 TRP L  94      63.750 180.172  32.653  1.00 21.11           C
ANISOU 1665  CE2 TRP L  94     2762   3053   2204   -276   -590   -531       C
ATOM   1666  CE3 TRP L  94      65.308 178.852  33.957  1.00 16.34           C
ANISOU 1666  CE3 TRP L  94     2287   2221   1699   -416   -297   -450       C
ATOM   1667  CZ2 TRP L  94      64.268 179.683  31.456  1.00 20.87           C
ANISOU 1667  CZ2 TRP L  94     2911   2972   2048   -305   -622   -559       C
ATOM   1668  CZ3 TRP L  94      65.821 178.371  32.768  1.00 17.91           C
ANISOU 1668  CZ3 TRP L  94     2630   2373   1800   -431   -319   -490       C
ATOM   1669  CH2 TRP L  94      65.284 178.761  31.538  1.00 19.79           C
ANISOU 1669  CH2 TRP L  94     2899   2701   1920   -391   -469   -546       C
ATOM   1670  N   PRO L  95      64.480 183.551  36.435  1.00 12.88           N
ANISOU 1670  N   PRO L  95     1602   1945   1345     34   -355   -225       N
ATOM   1671  CA  PRO L  95      63.965 184.921  36.589  1.00 13.34           C
ANISOU 1671  CA  PRO L  95     1617   2054   1399    196   -431   -205       C
ATOM   1672  C   PRO L  95      62.441 184.906  36.833  1.00 20.52           C
ANISOU 1672  C   PRO L  95     2274   3116   2409    215   -501   -331       C
ATOM   1673  O   PRO L  95      61.790 183.917  36.487  1.00 20.44           O
ANISOU 1673  O   PRO L  95     2144   3182   2439     99   -530   -437       O
ATOM   1674  CB  PRO L  95      64.379 185.605  35.271  1.00 14.91           C
ANISOU 1674  CB  PRO L  95     1996   2215   1453    307   -552   -159       C
ATOM   1675  CG  PRO L  95      64.587 184.498  34.314  1.00 19.35           C
ANISOU 1675  CG  PRO L  95     2616   2777   1960    199   -574   -208       C
ATOM   1676  CD  PRO L  95      65.153 183.389  35.135  1.00 13.79           C
ANISOU 1676  CD  PRO L  95     1880   2015   1344     45   -412   -211       C
ATOM   1677  N   PRO L  95A     61.844 185.917  37.510  1.00 18.83           N
ANISOU 1677  N   PRO L  95A    1956   2948   2253    341   -508   -342       N
ATOM   1678  CA  PRO L  95A     62.449 187.173  37.997  1.00 17.86           C
ANISOU 1678  CA  PRO L  95A    1967   2730   2087    475   -476   -237       C
ATOM   1679  C   PRO L  95A     63.433 186.992  39.139  1.00 19.72           C
ANISOU 1679  C   PRO L  95A    2302   2859   2333    368   -291   -154       C
ATOM   1680  O   PRO L  95A     63.154 186.273  40.094  1.00 19.46           O
ANISOU 1680  O   PRO L  95A    2173   2848   2373    241   -169   -195       O
ATOM   1681  CB  PRO L  95A     61.228 188.007  38.399  1.00 21.37           C
ANISOU 1681  CB  PRO L  95A    2218   3280   2623    626   -538   -328       C
ATOM   1682  CG  PRO L  95A     60.181 186.992  38.759  1.00 26.67           C
ANISOU 1682  CG  PRO L  95A    2615   4096   3423    488   -487   -478       C
ATOM   1683  CD  PRO L  95A     60.394 185.870  37.791  1.00 21.87           C
ANISOU 1683  CD  PRO L  95A    2050   3495   2764    357   -550   -496       C
ATOM   1684  N   TYR L  96      64.616 187.594  38.995  1.00 15.03           N
ANISOU 1684  N   TYR L  96     1912   2143   1655    404   -274    -44       N
ATOM   1685  CA  TYR L  96      65.662 187.600  40.012  1.00 12.47           C
ANISOU 1685  CA  TYR L  96     1685   1719   1335    333   -144     29       C
ATOM   1686  C   TYR L  96      65.427 188.885  40.818  1.00 17.67           C
ANISOU 1686  C   TYR L  96     2358   2356   2001    443   -123     48       C
ATOM   1687  O   TYR L  96      66.082 189.913  40.608  1.00 16.76           O
ANISOU 1687  O   TYR L  96     2393   2154   1822    520   -143    114       O
ATOM   1688  CB  TYR L  96      67.043 187.558  39.349  1.00 11.66           C
ANISOU 1688  CB  TYR L  96     1752   1517   1161    301   -134    101       C
ATOM   1689  CG  TYR L  96      67.333 186.258  38.627  1.00 12.34           C
ANISOU 1689  CG  TYR L  96     1834   1609   1244    200   -134     69       C
ATOM   1690  CD1 TYR L  96      67.004 185.032  39.197  1.00 14.39           C
ANISOU 1690  CD1 TYR L  96     2007   1888   1572     89    -84     24       C
ATOM   1691  CD2 TYR L  96      68.013 186.248  37.417  1.00 12.51           C
ANISOU 1691  CD2 TYR L  96     1973   1597   1185    203   -161     83       C
ATOM   1692  CE1 TYR L  96      67.322 183.832  38.568  1.00 14.08           C
ANISOU 1692  CE1 TYR L  96     1993   1825   1530      1    -78     -9       C
ATOM   1693  CE2 TYR L  96      68.321 185.054  36.771  1.00 13.30           C
ANISOU 1693  CE2 TYR L  96     2083   1690   1282    116   -145     40       C
ATOM   1694  CZ  TYR L  96      67.980 183.846  37.356  1.00 19.82           C
ANISOU 1694  CZ  TYR L  96     2818   2527   2187     23   -111     -6       C
ATOM   1695  OH  TYR L  96      68.287 182.652  36.738  1.00 24.08           O
ANISOU 1695  OH  TYR L  96     3390   3035   2724    -57    -94    -54       O
ATOM   1696  N   THR L  97      64.407 188.823  41.688  1.00 14.69           N
ANISOU 1696  N   THR L  97     1825   2056   1701    442    -72    -28       N
ATOM   1697  CA  THR L  97      63.863 189.934  42.451  1.00 14.57           C
ANISOU 1697  CA  THR L  97     1780   2044   1711    558    -43    -53       C
ATOM   1698  C   THR L  97      64.802 190.507  43.499  1.00 16.21           C
ANISOU 1698  C   THR L  97     2149   2135   1876    528     54     21       C
ATOM   1699  O   THR L  97      65.645 189.800  44.061  1.00 14.80           O
ANISOU 1699  O   THR L  97     2044   1902   1677    393    121     68       O
ATOM   1700  CB  THR L  97      62.514 189.554  43.075  1.00 21.36           C
ANISOU 1700  CB  THR L  97     2404   3037   2677    535     23   -186       C
ATOM   1701  OG1 THR L  97      62.723 188.585  44.091  1.00 22.99           O
ANISOU 1701  OG1 THR L  97     2618   3225   2891    342    180   -186       O
ATOM   1702  CG2 THR L  97      61.512 189.047  42.056  1.00 18.89           C
ANISOU 1702  CG2 THR L  97     1893   2859   2424    561    -95   -289       C
ATOM   1703  N   PHE L  98      64.591 191.803  43.793  1.00 11.88           N
ANISOU 1703  N   PHE L  98     1656   1544   1316    667     47     20       N
ATOM   1704  CA  PHE L  98      65.331 192.578  44.780  1.00  9.68           C
ANISOU 1704  CA  PHE L  98     1531   1154    992    653    124     68       C
ATOM   1705  C   PHE L  98      64.488 192.803  46.033  1.00 13.67           C
ANISOU 1705  C   PHE L  98     1957   1699   1539    665    241    -14       C
ATOM   1706  O   PHE L  98      63.255 192.712  45.994  1.00 13.99           O
ANISOU 1706  O   PHE L  98     1807   1850   1659    734    254   -119       O
ATOM   1707  CB  PHE L  98      65.723 193.950  44.202  1.00 10.67           C
ANISOU 1707  CB  PHE L  98     1827   1171   1056    789     51    119       C
ATOM   1708  CG  PHE L  98      66.730 193.913  43.087  1.00 10.44           C
ANISOU 1708  CG  PHE L  98     1931   1076    958    747    -14    199       C
ATOM   1709  CD1 PHE L  98      68.093 193.978  43.356  1.00 11.47           C
ANISOU 1709  CD1 PHE L  98     2193   1115   1050    624     40    259       C
ATOM   1710  CD2 PHE L  98      66.318 193.843  41.758  1.00 11.11           C
ANISOU 1710  CD2 PHE L  98     2013   1194   1015    829   -128    201       C
ATOM   1711  CE1 PHE L  98      69.027 193.961  42.315  1.00 11.33           C
ANISOU 1711  CE1 PHE L  98     2279   1045    979    569     18    309       C
ATOM   1712  CE2 PHE L  98      67.255 193.799  40.716  1.00 12.27           C
ANISOU 1712  CE2 PHE L  98     2309   1275   1078    771   -154    266       C
ATOM   1713  CZ  PHE L  98      68.601 193.861  41.000  1.00  9.79           C
ANISOU 1713  CZ  PHE L  98     2084    890    744    620    -49    279       C
ATOM   1714  N   GLY L  99      65.171 193.128  47.118  1.00  9.65           N
ANISOU 1714  N   GLY L  99     1589   1102    975    596    325     20       N
ATOM   1715  CA  GLY L  99      64.551 193.552  48.358  1.00 10.71           C
ANISOU 1715  CA  GLY L  99     1718   1241   1111    604    454    -53       C
ATOM   1716  C   GLY L  99      64.257 195.029  48.213  1.00 15.83           C
ANISOU 1716  C   GLY L  99     2427   1828   1762    797    420    -79       C
ATOM   1717  O   GLY L  99      64.727 195.661  47.255  1.00 15.47           O
ANISOU 1717  O   GLY L  99     2477   1709   1689    887    300    -16       O
ATOM   1718  N   GLN L 100      63.479 195.595  49.140  1.00 12.58           N
ANISOU 1718  N   GLN L 100     1982   1427   1371    860    535   -176       N
ATOM   1719  CA  GLN L 100      63.076 197.007  49.081  1.00 13.93           C
ANISOU 1719  CA  GLN L 100     2214   1523   1555   1072    510   -221       C
ATOM   1720  C   GLN L 100      64.224 198.004  49.381  1.00 17.20           C
ANISOU 1720  C   GLN L 100     2923   1751   1861   1059    491   -136       C
ATOM   1721  O   GLN L 100      64.091 199.187  49.086  1.00 17.51           O
ANISOU 1721  O   GLN L 100     3076   1684   1892   1228    442   -144       O
ATOM   1722  CB  GLN L 100      61.855 197.266  49.987  1.00 17.77           C
ANISOU 1722  CB  GLN L 100     2553   2086   2114   1148    664   -380       C
ATOM   1723  CG  GLN L 100      62.076 196.902  51.486  1.00 38.25           C
ANISOU 1723  CG  GLN L 100     5244   4661   4627    956    863   -405       C
ATOM   1724  CD  GLN L 100      61.631 195.492  51.837  1.00 51.24           C
ANISOU 1724  CD  GLN L 100     6736   6438   6296    763    977   -444       C
ATOM   1725  OE1 GLN L 100      62.177 194.483  51.353  1.00 36.42           O
ANISOU 1725  OE1 GLN L 100     4860   4580   4400    633    902   -353       O
ATOM   1726  NE2 GLN L 100      60.656 195.395  52.726  1.00 49.53           N
ANISOU 1726  NE2 GLN L 100     6405   6300   6115    728   1182   -586       N
ATOM   1727  N   GLY L 101      65.317 197.512  49.974  1.00 13.06           N
ANISOU 1727  N   GLY L 101     2520   1183   1258    860    521    -66       N
ATOM   1728  CA  GLY L 101      66.482 198.321  50.321  1.00 12.06           C
ANISOU 1728  CA  GLY L 101     2636    903   1043    802    500     -8       C
ATOM   1729  C   GLY L 101      66.549 198.778  51.768  1.00 17.56           C
ANISOU 1729  C   GLY L 101     3465   1539   1670    748    613    -64       C
ATOM   1730  O   GLY L 101      65.519 198.964  52.423  1.00 18.36           O
ANISOU 1730  O   GLY L 101     3504   1681   1792    823    728   -164       O
ATOM   1731  N   THR L 102      67.781 198.955  52.276  1.00 13.76           N
ANISOU 1731  N   THR L 102     3159    964   1104    611    581    -15       N
ATOM   1732  CA  THR L 102      68.071 199.481  53.610  1.00 14.30           C
ANISOU 1732  CA  THR L 102     3407    952   1075    542    651    -63       C
ATOM   1733  C   THR L 102      69.011 200.653  53.423  1.00 19.38           C
ANISOU 1733  C   THR L 102     4245   1441   1677    528    589    -42       C
ATOM   1734  O   THR L 102      70.051 200.505  52.782  1.00 18.39           O
ANISOU 1734  O   THR L 102     4128   1296   1564    436    493     24       O
ATOM   1735  CB  THR L 102      68.671 198.398  54.536  1.00 19.17           C
ANISOU 1735  CB  THR L 102     4054   1614   1616    363    645    -38       C
ATOM   1736  OG1 THR L 102      67.694 197.382  54.755  1.00 19.87           O
ANISOU 1736  OG1 THR L 102     4003   1818   1727    354    739    -64       O
ATOM   1737  CG2 THR L 102      69.133 198.958  55.891  1.00 16.12           C
ANISOU 1737  CG2 THR L 102     3896   1135   1096    278    678    -81       C
ATOM   1738  N   LYS L 103      68.638 201.820  53.955  1.00 18.29           N
ANISOU 1738  N   LYS L 103     4264   1189   1498    612    659   -112       N
ATOM   1739  CA  LYS L 103      69.461 203.019  53.872  1.00 19.38           C
ANISOU 1739  CA  LYS L 103     4624   1152   1586    579    623   -107       C
ATOM   1740  C   LYS L 103      70.386 203.056  55.086  1.00 25.63           C
ANISOU 1740  C   LYS L 103     5561   1902   2275    391    615   -138       C
ATOM   1741  O   LYS L 103      69.904 203.024  56.224  1.00 26.22           O
ANISOU 1741  O   LYS L 103     5699   1988   2276    386    699   -208       O
ATOM   1742  CB  LYS L 103      68.583 204.293  53.828  1.00 24.14           C
ANISOU 1742  CB  LYS L 103     5358   1623   2192    780    691   -174       C
ATOM   1743  CG  LYS L 103      67.429 204.250  52.826  1.00 39.23           C
ANISOU 1743  CG  LYS L 103     7110   3591   4205   1015    675   -174       C
ATOM   1744  CD  LYS L 103      66.436 205.376  53.074  1.00 54.86           C
ANISOU 1744  CD  LYS L 103     9185   5461   6200   1249    743   -274       C
ATOM   1745  CE  LYS L 103      65.172 205.224  52.259  1.00 64.48           C
ANISOU 1745  CE  LYS L 103    10192   6771   7537   1505    704   -306       C
ATOM   1746  NZ  LYS L 103      64.208 206.322  52.533  1.00 75.37           N
ANISOU 1746  NZ  LYS L 103    11649   8037   8952   1770    752   -421       N
ATOM   1747  N   VAL L 104      71.706 203.050  54.853  1.00 22.74           N
ANISOU 1747  N   VAL L 104     5236   1502   1903    231    513    -98       N
ATOM   1748  CA  VAL L 104      72.689 203.152  55.938  1.00 23.76           C
ANISOU 1748  CA  VAL L 104     5490   1594   1943     56    458   -142       C
ATOM   1749  C   VAL L 104      73.109 204.616  55.941  1.00 29.76           C
ANISOU 1749  C   VAL L 104     6473   2168   2666     18    481   -193       C
ATOM   1750  O   VAL L 104      73.775 205.073  55.012  1.00 29.03           O
ANISOU 1750  O   VAL L 104     6395   2010   2625    -41    451   -161       O
ATOM   1751  CB  VAL L 104      73.879 202.155  55.802  1.00 26.75           C
ANISOU 1751  CB  VAL L 104     5732   2073   2359    -92    318    -99       C
ATOM   1752  CG1 VAL L 104      74.913 202.373  56.904  1.00 27.38           C
ANISOU 1752  CG1 VAL L 104     5937   2115   2353   -252    219   -163       C
ATOM   1753  CG2 VAL L 104      73.384 200.711  55.813  1.00 25.39           C
ANISOU 1753  CG2 VAL L 104     5388   2048   2212    -45    306    -47       C
ATOM   1754  N   GLU L 105      72.612 205.372  56.929  1.00 28.70           N
ANISOU 1754  N   GLU L 105     6532   1936   2436     56    561   -277       N
ATOM   1755  CA  GLU L 105      72.795 206.823  57.017  1.00 30.06           C
ANISOU 1755  CA  GLU L 105     6960   1899   2561     45    606   -339       C
ATOM   1756  C   GLU L 105      73.678 207.247  58.175  1.00 34.34           C
ANISOU 1756  C   GLU L 105     7684   2374   2990   -148    559   -426       C
ATOM   1757  O   GLU L 105      73.737 206.557  59.191  1.00 34.93           O
ANISOU 1757  O   GLU L 105     7745   2544   2983   -206    523   -455       O
ATOM   1758  CB  GLU L 105      71.429 207.520  57.165  1.00 32.86           C
ANISOU 1758  CB  GLU L 105     7412   2168   2906    281    742   -392       C
ATOM   1759  CG  GLU L 105      70.442 207.241  56.044  1.00 45.88           C
ANISOU 1759  CG  GLU L 105     8877   3887   4669    502    763   -332       C
ATOM   1760  CD  GLU L 105      69.199 208.114  56.034  1.00 76.40           C
ANISOU 1760  CD  GLU L 105    12821   7651   8555    766    865   -404       C
ATOM   1761  OE1 GLU L 105      68.812 208.623  57.113  1.00 70.61           O
ANISOU 1761  OE1 GLU L 105    12224   6852   7752    795    970   -515       O
ATOM   1762  OE2 GLU L 105      68.598 208.268  54.945  1.00 74.14           O
ANISOU 1762  OE2 GLU L 105    12459   7355   8355    956    832   -357       O
ATOM   1763  N   ILE L 106      74.315 208.423  58.048  1.00 30.36           N
ANISOU 1763  N   ILE L 106     7384   1687   2463   -251    562   -475       N
ATOM   1764  CA  ILE L 106      75.143 208.988  59.110  1.00 30.54           C
ANISOU 1764  CA  ILE L 106     7598   1627   2378   -446    510   -581       C
ATOM   1765  C   ILE L 106      74.213 209.437  60.258  1.00 32.93           C
ANISOU 1765  C   ILE L 106     8110   1854   2549   -337    620   -671       C
ATOM   1766  O   ILE L 106      73.178 210.057  60.009  1.00 33.13           O
ANISOU 1766  O   ILE L 106     8223   1776   2589   -136    757   -685       O
ATOM   1767  CB  ILE L 106      76.086 210.155  58.659  1.00 34.84           C
ANISOU 1767  CB  ILE L 106     8316   1985   2937   -623    505   -627       C
ATOM   1768  CG1 ILE L 106      76.603 210.053  57.191  1.00 34.62           C
ANISOU 1768  CG1 ILE L 106     8147   1969   3039   -673    500   -537       C
ATOM   1769  CG2 ILE L 106      77.248 210.363  59.645  1.00 36.14           C
ANISOU 1769  CG2 ILE L 106     8561   2144   3029   -884    387   -743       C
ATOM   1770  CD1 ILE L 106      75.754 210.782  56.153  1.00 45.57           C
ANISOU 1770  CD1 ILE L 106     9671   3196   4448   -480    618   -467       C
ATOM   1771  N   LYS L 107      74.567 209.069  61.495  1.00 28.19           N
ANISOU 1771  N   LYS L 107     7583   1310   1817   -457    554   -737       N
ATOM   1772  CA  LYS L 107      73.814 209.404  62.704  1.00 28.90           C
ANISOU 1772  CA  LYS L 107     7895   1337   1750   -397    670   -837       C
ATOM   1773  C   LYS L 107      74.031 210.872  63.046  1.00 34.68           C
ANISOU 1773  C   LYS L 107     8938   1829   2409   -454    726   -953       C
ATOM   1774  O   LYS L 107      75.169 211.342  63.032  1.00 34.97           O
ANISOU 1774  O   LYS L 107     9053   1795   2438   -662    605   -990       O
ATOM   1775  CB  LYS L 107      74.291 208.520  63.869  1.00 30.84           C
ANISOU 1775  CB  LYS L 107     8173   1701   1844   -536    550   -859       C
ATOM   1776  CG  LYS L 107      73.360 208.479  65.084  1.00 40.82           C
ANISOU 1776  CG  LYS L 107     9635   2950   2924   -473    703   -939       C
ATOM   1777  CD  LYS L 107      74.069 207.942  66.337  1.00 55.23           C
ANISOU 1777  CD  LYS L 107    11627   4821   4538   -649    549   -976       C
ATOM   1778  CE  LYS L 107      74.252 206.441  66.341  1.00 75.10           C
ANISOU 1778  CE  LYS L 107    13959   7519   7055   -665    423   -862       C
ATOM   1779  NZ  LYS L 107      74.987 205.977  67.548  1.00 90.65           N
ANISOU 1779  NZ  LYS L 107    16137   9506   8800   -813    234   -893       N
ATOM   1780  N   ALA L 108      72.950 211.593  63.359  1.00 32.18           N
ANISOU 1780  N   ALA L 108     8792   1386   2050   -273    913  -1027       N
ATOM   1781  CA  ALA L 108      73.035 212.994  63.761  1.00 34.58           C
ANISOU 1781  CA  ALA L 108     9433   1433   2271   -301    987  -1150       C
ATOM   1782  C   ALA L 108      73.550 213.094  65.192  1.00 42.02           C
ANISOU 1782  C   ALA L 108    10605   2355   3005   -492    943  -1273       C
ATOM   1783  O   ALA L 108      73.426 212.136  65.959  1.00 41.56           O
ANISOU 1783  O   ALA L 108    10483   2461   2846   -520    916  -1267       O
ATOM   1784  CB  ALA L 108      71.668 213.651  63.662  1.00 36.41           C
ANISOU 1784  CB  ALA L 108     9752   1546   2537     -6   1195  -1204       C
ATOM   1785  N   ALA L 109      74.121 214.246  65.555  1.00 41.85           N
ANISOU 1785  N   ALA L 109    10879   2119   2901   -631    932  -1386       N
ATOM   1786  CA  ALA L 109      74.620 214.509  66.901  1.00 44.61           C
ANISOU 1786  CA  ALA L 109    11492   2423   3034   -819    875  -1524       C
ATOM   1787  C   ALA L 109      73.441 214.699  67.877  1.00 52.40           C
ANISOU 1787  C   ALA L 109    12682   3357   3871   -653   1094  -1629       C
ATOM   1788  O   ALA L 109      72.339 215.055  67.442  1.00 53.10           O
ANISOU 1788  O   ALA L 109    12747   3375   4053   -397   1294  -1634       O
ATOM   1789  CB  ALA L 109      75.494 215.753  66.888  1.00 47.40           C
ANISOU 1789  CB  ALA L 109    12101   2548   3362  -1020    822  -1628       C
ATOM   1790  N   ALA L 110      73.674 214.461  69.188  1.00 50.31           N
ANISOU 1790  N   ALA L 110    12616   3126   3372   -795   1053  -1722       N
ATOM   1791  CA  ALA L 110      72.654 214.589  70.235  1.00 73.72           C
ANISOU 1791  CA  ALA L 110    15803   6049   6157   -687   1281  -1841       C
ATOM   1792  C   ALA L 110      72.194 216.038  70.479  1.00106.95           C
ANISOU 1792  C   ALA L 110    20334   9980  10324   -603   1470  -2006       C
ATOM   1793  O   ALA L 110      72.867 216.995  70.096  1.00 69.41           O
ANISOU 1793  O   ALA L 110    15716   5037   5621   -693   1391  -2040       O
ATOM   1794  CB  ALA L 110      73.158 213.972  71.529  1.00 75.52           C
ANISOU 1794  CB  ALA L 110    16215   6367   6111   -886   1161  -1888       C
TER    1795      ALA L 110
HETATM 1796  C1  EDO H 201      62.437 186.099  19.332  1.00 61.86           C
HETATM 1797  O1  EDO H 201      61.366 186.778  18.675  1.00 61.78           O
HETATM 1798  C2  EDO H 201      62.372 186.323  20.874  1.00 60.84           C
HETATM 1799  O2  EDO H 201      63.536 185.800  21.502  1.00 59.15           O
HETATM 1800  C1  EDO H 202      80.368 189.046  34.698  1.00 37.23           C
HETATM 1801  O1  EDO H 202      80.888 187.722  34.755  1.00 38.19           O
HETATM 1802  C2  EDO H 202      81.390 190.082  35.226  1.00 36.48           C
HETATM 1803  O2  EDO H 202      82.380 190.337  34.243  1.00 36.86           O
HETATM 1804  C1  EDO L 201      69.058 174.637  54.619  1.00 25.42           C
HETATM 1805  O1  EDO L 201      69.452 175.206  55.864  1.00 27.11           O
HETATM 1806  C2  EDO L 201      70.305 174.112  53.880  1.00 24.36           C
HETATM 1807  O2  EDO L 201      70.101 174.239  52.493  1.00 25.91           O
HETATM 1808  C1  EDO L 202      85.356 200.625  49.348  1.00 66.00           C
HETATM 1809  O1  EDO L 202      86.353 201.015  50.279  1.00 65.17           O
HETATM 1810  C2  EDO L 202      86.039 200.249  48.020  1.00 67.68           C
HETATM 1811  O2  EDO L 202      86.956 199.188  48.246  1.00 68.51           O
HETATM 1812  C1  EDO L 203      62.356 193.709  42.248  1.00 21.08           C
HETATM 1813  O1  EDO L 203      63.032 192.937  41.305  1.00 12.44           O
HETATM 1814  C2  EDO L 203      60.865 193.657  41.933  1.00 29.65           C
HETATM 1815  O2  EDO L 203      60.473 192.311  41.764  1.00 34.59           O
HETATM 1816  O   HOH H 301      76.051 179.113  41.245  1.00 24.17           O
HETATM 1817  O   HOH H 302      78.074 185.323  36.122  1.00 16.74           O
HETATM 1818  O   HOH H 303      68.871 205.118  39.679  1.00 19.18           O
HETATM 1819  O   HOH H 304      61.759 183.146  28.966  1.00 17.16           O
HETATM 1820  O   HOH H 305      61.709 200.969  40.650  1.00 16.11           O
HETATM 1821  O   HOH H 306      72.238 191.819  39.041  1.00 16.48           O
HETATM 1822  O   HOH H 307      59.164 185.975  26.523  1.00 47.62           O
HETATM 1823  O   HOH H 308      81.183 182.523  40.177  1.00 29.39           O
HETATM 1824  O   HOH H 309      79.643 197.081  36.890  1.00 36.94           O
HETATM 1825  O   HOH H 310      72.795 182.078  27.975  1.00 18.46           O
HETATM 1826  O   HOH H 311      60.468 199.706  45.692  1.00 39.94           O
HETATM 1827  O   HOH H 312      72.181 188.387  18.080  1.00 27.01           O
HETATM 1828  O   HOH H 313      67.839 181.049  33.781  1.00 22.31           O
HETATM 1829  O   HOH H 314      75.664 180.052  34.289  1.00 36.65           O
HETATM 1830  O   HOH H 315      60.506 188.567  22.710  1.00 36.00           O
HETATM 1831  O   HOH H 316      73.050 206.058  38.070  1.00 32.11           O
HETATM 1832  O   HOH H 317      72.222 181.222  24.740  1.00 29.92           O
HETATM 1833  O   HOH H 318      76.602 184.563  18.584  1.00 44.43           O
HETATM 1834  O   HOH H 319      80.553 199.020  33.109  1.00 22.14           O
HETATM 1835  O   HOH H 320      71.425 177.845  27.758  1.00 30.08           O
HETATM 1836  O   HOH H 321      65.118 207.274  43.248  1.00 32.50           O
HETATM 1837  O   HOH H 322      58.402 185.797  30.183  1.00 28.02           O
HETATM 1838  O   HOH H 323      77.545 181.477  35.723  1.00 23.88           O
HETATM 1839  O   HOH H 324      79.941 188.539  20.785  1.00 39.08           O
HETATM 1840  O   HOH H 325      81.115 184.720  36.477  1.00 24.76           O
HETATM 1841  O   HOH L 301      75.428 179.550  45.814  1.00 22.37           O
HETATM 1842  O   HOH L 302      59.877 187.788  52.332  1.00 21.34           O
HETATM 1843  O   HOH L 303      60.305 191.876  39.134  1.00 20.27           O
HETATM 1844  O   HOH L 304      84.772 186.309  43.533  1.00 28.53           O
HETATM 1845  O   HOH L 305      70.895 174.049  49.931  1.00 22.25           O
HETATM 1846  O   HOH L 306      64.792 201.942  53.010  1.00 30.59           O
HETATM 1847  O   HOH L 307      77.010 180.673  52.314  1.00 23.09           O
HETATM 1848  O   HOH L 308      74.000 178.555  57.023  1.00 21.47           O
HETATM 1849  O   HOH L 309      77.675 208.774  45.301  1.00 30.52           O
HETATM 1850  O   HOH L 310      59.228 183.231  35.930  1.00 36.18           O
HETATM 1851  O   HOH L 311      63.822 197.256  45.259  1.00 19.27           O
HETATM 1852  O   HOH L 312      68.708 194.881  54.499  1.00 24.60           O
HETATM 1853  O   HOH L 313      70.490 209.685  60.194  1.00 44.63           O
HETATM 1854  O   HOH L 314      69.597 193.433  60.759  1.00 34.81           O
HETATM 1855  O   HOH L 315      81.472 192.000  58.614  1.00 32.80           O
HETATM 1856  O   HOH L 316      63.146 183.189  41.135  1.00 14.27           O
HETATM 1857  O   HOH L 317      61.471 190.613  46.148  1.00 30.78           O
HETATM 1858  O   HOH L 318      84.491 188.735  54.141  1.00 34.62           O
HETATM 1859  O   HOH L 319      76.635 202.511  43.807  1.00 13.51           O
HETATM 1860  O   HOH L 320      63.942 190.947  57.562  1.00 28.60           O
HETATM 1861  O   HOH L 321      82.065 201.056  50.158  1.00 21.14           O
HETATM 1862  O   HOH L 322      77.561 188.426  58.217  1.00 24.49           O
HETATM 1863  O   HOH L 323      73.807 186.602  53.013  1.00  9.01           O
HETATM 1864  O   HOH L 324      68.837 203.494  45.625  1.00 21.91           O
HETATM 1865  O   HOH L 325      71.488 185.331  58.993  1.00 22.63           O
HETATM 1866  O   HOH L 326      81.612 186.935  53.514  1.00 14.48           O
HETATM 1867  O   HOH L 327      84.060 196.968  43.450  1.00 39.09           O
HETATM 1868  O   HOH L 328      69.614 203.313  63.612  1.00 24.09           O
HETATM 1869  O   HOH L 329      67.249 179.814  51.629  1.00 19.72           O
HETATM 1870  O   HOH L 330      66.240 173.379  44.692  1.00 17.36           O
HETATM 1871  O   HOH L 331      84.818 185.852  49.934  1.00 32.70           O
HETATM 1872  O   HOH L 332      78.079 210.169  63.579  1.00 31.81           O
HETATM 1873  O   HOH L 333      60.640 181.914  38.322  1.00 26.93           O
HETATM 1874  O   HOH L 334      78.743 194.995  40.173  1.00 19.50           O
HETATM 1875  O   HOH L 335      83.960 191.062  58.153  1.00 13.06           O
HETATM 1876  O   HOH L 336      70.377 196.223  62.818  1.00 30.55           O
HETATM 1877  O   HOH L 337      71.316 205.445  46.554  1.00 33.01           O
HETATM 1878  O   HOH L 338      79.007 201.680  44.833  1.00 29.90           O
HETATM 1879  O   HOH L 339      73.453 197.530  63.077  1.00 27.01           O
HETATM 1880  O   HOH L 340      74.205 184.148  43.596  1.00 35.54           O
HETATM 1881  O   HOH L 341      61.800 175.674  41.279  1.00 24.28           O
HETATM 1882  O   HOH L 342      82.104 194.328  42.060  1.00 30.90           O
HETATM 1883  O   HOH L 343      71.487 177.497  56.959  1.00 17.09           O
HETATM 1884  O   HOH L 344      76.899 181.632  56.446  1.00 31.89           O
HETATM 1885  O   HOH L 345      64.420 179.836  58.317  1.00 28.78           O
HETATM 1886  O   HOH L 346      63.464 182.098  61.791  1.00 34.94           O
HETATM 1887  O   HOH L 347      60.597 184.377  41.583  1.00 29.68           O
HETATM 1888  O   HOH L 348      88.236 196.352  55.265  1.00 24.96           O
HETATM 1889  O   HOH L 349      88.478 189.846  45.278  1.00 38.22           O
HETATM 1890  O   HOH L 350      68.092 187.562  58.896  1.00 33.80           O
HETATM 1891  O   HOH L 351      81.801 202.664  44.564  1.00 41.13           O
HETATM 1892  O   HOH L 352      73.168 207.302  50.078  1.00 19.74           O
CONECT  147  146  730
CONECT  730  147  729
CONECT 1097 1096 1606
CONECT 1606 1097 1605
CONECT 1796 1798 1797
CONECT 1798 1796 1799
CONECT 1797 1796
CONECT 1799 1798
CONECT 1800 1802 1801
CONECT 1802 1803 1800
CONECT 1801 1800
CONECT 1803 1802
CONECT 1804 1805 1806
CONECT 1806 1807 1804
CONECT 1805 1804
CONECT 1807 1806
CONECT 1808 1809 1810
CONECT 1810 1811 1808
CONECT 1809 1808
CONECT 1811 1810
CONECT 1812 1813 1814
CONECT 1814 1815 1812
CONECT 1813 1812
CONECT 1815 1814
END



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