CNRS Nantes University UFIP UFIP
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***  7j  ***

elNémo ID: 21031504272780815

Job options:

ID        	=	 21031504272780815
JOBID     	=	 7j
USERID    	=	 valcarcel
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 7j

HEADER    VIRAL PROTEIN                           18-AUG-20   7JTL              
TITLE     STRUCTURE OF SARS-COV-2 ORF8 ACCESSORY PROTEIN                        
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: ORF8 PROTEIN;                                              
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 SYNONYM: ORF8, NON-STRUCTURAL PROTEIN 8, NS8;                        
COMPND   5 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: SEVERE ACUTE RESPIRATORY SYNDROME CORONAVIRUS   
SOURCE   3 2;                                                                   
SOURCE   4 ORGANISM_COMMON: 2019-NCOV;                                          
SOURCE   5 ORGANISM_TAXID: 2697049;                                             
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    SARS-COV-2, SARS2, COVID-19, CORONAVIRUS, ACCESSORY PROTEIN, HOST-    
KEYWDS   2 FACTOR RESTRICTION, RNA VIRUS, IMMUNE EVASION, MHC-I, OPEN READING   
KEYWDS   3 FRAME 8, VIRAL PROTEIN                                               
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    T.G.FLOWER,C.Z.BUFFALO,R.M.HOOY,M.ALLAIRE,X.REN,J.H.HURLEY            
REVDAT   4   10-FEB-21 7JTL    1       COMPND JRNL   REMARK HET                 
REVDAT   4 2                   1       HETNAM FORMUL SHEET  SSBOND              
REVDAT   4 3                   1       LINK   ATOM                              
REVDAT   3   16-SEP-20 7JTL    1       JRNL                                     
REVDAT   2   09-SEP-20 7JTL    1       COMPND SOURCE JRNL   DBREF               
REVDAT   2 2                   1       SEQADV                                   
REVDAT   1   26-AUG-20 7JTL    0                                                
JRNL        AUTH   T.G.FLOWER,C.Z.BUFFALO,R.M.HOOY,M.ALLAIRE,X.REN,J.H.HURLEY   
JRNL        TITL   STRUCTURE OF SARS-COV-2 ORF8, A RAPIDLY EVOLVING IMMUNE      
JRNL        TITL 2 EVASION PROTEIN.                                             
JRNL        REF    PROC.NATL.ACAD.SCI.USA        V. 118       2021              
JRNL        REFN                   ESSN 1091-6490                               
JRNL        PMID   33361333                                                     
JRNL        DOI    10.1073/PNAS.2021785118                                      
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   T.G.FLOWER,C.Z.BUFFALO,R.M.HOOY,M.ALLAIRE,X.REN,J.H.HURLEY   
REMARK   1  TITL   STRUCTURE OF SARS-COV-2 ORF8, A RAPIDLY EVOLVING CORONAVIRUS 
REMARK   1  TITL 2 PROTEIN IMPLICATED IN IMMUNE EVASION.                        
REMARK   1  REF    BIORXIV                                    2020              
REMARK   1  REFN                                                                
REMARK   1  PMID   32869027                                                     
REMARK   1  DOI    10.1101/2020.08.27.270637                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.04 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX 1.18.2_3874                                   
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : GEOSTD + MONOMER LIBRARY + CDL V1.2           
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.04                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 43.65                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 95.1                           
REMARK   3   NUMBER OF REFLECTIONS             : 17005                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.221                           
REMARK   3   R VALUE            (WORKING SET) : 0.217                           
REMARK   3   FREE R VALUE                     : 0.257                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 10.000                          
REMARK   3   FREE R VALUE TEST SET COUNT      : 1700                            
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        
REMARK   3     1 43.6500 -  4.6700    1.00     1520   166  0.2096 0.2274        
REMARK   3     2  4.6700 -  3.7100    1.00     1380   153  0.1621 0.2242        
REMARK   3     3  3.7100 -  3.2400    1.00     1377   154  0.2023 0.2415        
REMARK   3     4  3.2400 -  2.9400    1.00     1329   145  0.2165 0.2120        
REMARK   3     5  2.9400 -  2.7300    1.00     1337   149  0.2220 0.3016        
REMARK   3     6  2.7300 -  2.5700    0.99     1322   148  0.2510 0.3079        
REMARK   3     7  2.5700 -  2.4400    0.98     1284   142  0.2608 0.2999        
REMARK   3     8  2.4400 -  2.3400    0.96     1243   136  0.2654 0.3287        
REMARK   3     9  2.3400 -  2.2500    0.92     1199   136  0.2662 0.3124        
REMARK   3    10  2.2500 -  2.1700    0.89     1173   131  0.3091 0.3531        
REMARK   3    11  2.1700 -  2.1000    0.86     1100   122  0.3140 0.3445        
REMARK   3    12  2.1000 -  2.0400    0.79     1041   118  0.3599 0.3850        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.259            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 26.000           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 36.25                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 46.47                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.008           1666                                  
REMARK   3   ANGLE     :  0.991           2272                                  
REMARK   3   CHIRALITY :  0.061            254                                  
REMARK   3   PLANARITY :  0.007            290                                  
REMARK   3   DIHEDRAL  : 15.114            596                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 9                                          
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 18 THROUGH 32 )                   
REMARK   3    ORIGIN FOR THE GROUP (A):  50.5066  38.7414 111.8821              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2173 T22:   0.4823                                     
REMARK   3      T33:   0.3447 T12:  -0.0175                                     
REMARK   3      T13:  -0.0004 T23:   0.0268                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.9016 L22:   0.5503                                     
REMARK   3      L33:   0.8301 L12:  -0.3241                                     
REMARK   3      L13:   0.7770 L23:  -0.2548                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1723 S12:   0.1935 S13:   0.3931                       
REMARK   3      S21:   0.2825 S22:   0.1117 S23:  -0.1514                       
REMARK   3      S31:  -0.0399 S32:  -0.1833 S33:  -0.0013                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 33 THROUGH 64 )                   
REMARK   3    ORIGIN FOR THE GROUP (A):  49.0822  24.3404 116.8811              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2969 T22:   0.3879                                     
REMARK   3      T33:   0.4494 T12:   0.0121                                     
REMARK   3      T13:   0.0095 T23:   0.0799                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.8272 L22:   0.5271                                     
REMARK   3      L33:   0.8120 L12:   0.5105                                     
REMARK   3      L13:  -0.7893 L23:  -0.3600                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1737 S12:  -0.4268 S13:  -0.4456                       
REMARK   3      S21:   0.0449 S22:  -0.0542 S23:  -0.0595                       
REMARK   3      S31:   0.0453 S32:  -0.1111 S33:  -0.0027                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 67 THROUGH 76 )                   
REMARK   3    ORIGIN FOR THE GROUP (A):  51.0986  16.2759 102.0040              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4110 T22:   0.5710                                     
REMARK   3      T33:   0.1974 T12:  -0.0197                                     
REMARK   3      T13:   0.0689 T23:   0.0018                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.4269 L22:   4.4737                                     
REMARK   3      L33:   0.4313 L12:   1.9386                                     
REMARK   3      L13:   0.3182 L23:  -0.3762                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1716 S12:  -0.3786 S13:   0.4137                       
REMARK   3      S21:   0.4594 S22:  -0.5035 S23:   0.6831                       
REMARK   3      S31:   0.0400 S32:   0.4548 S33:  -0.1023                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 77 THROUGH 121 )                  
REMARK   3    ORIGIN FOR THE GROUP (A):  49.9656  28.2630 115.4266              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2614 T22:   0.3950                                     
REMARK   3      T33:   0.2867 T12:  -0.0072                                     
REMARK   3      T13:   0.0057 T23:   0.0192                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.1017 L22:   1.8004                                     
REMARK   3      L33:   1.1902 L12:   0.3269                                     
REMARK   3      L13:  -0.3679 L23:   0.6340                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0691 S12:   0.1497 S13:   0.0174                       
REMARK   3      S21:   0.0505 S22:  -0.0809 S23:  -0.0993                       
REMARK   3      S31:   0.1019 S32:   0.0764 S33:  -0.0003                       
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 18 THROUGH 32 )                   
REMARK   3    ORIGIN FOR THE GROUP (A):  30.8035  33.1377 113.4943              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2175 T22:   0.4343                                     
REMARK   3      T33:   0.4322 T12:  -0.0186                                     
REMARK   3      T13:   0.0179 T23:   0.0225                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.0202 L22:   3.0923                                     
REMARK   3      L33:   3.1037 L12:  -2.3275                                     
REMARK   3      L13:  -1.0760 L23:  -1.0679                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0217 S12:   0.0032 S13:  -0.0675                       
REMARK   3      S21:   0.2985 S22:  -0.0186 S23:  -0.4732                       
REMARK   3      S31:  -0.0958 S32:   0.0636 S33:   0.0001                       
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 33 THROUGH 64 )                   
REMARK   3    ORIGIN FOR THE GROUP (A):  31.5156  47.5338 112.4522              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3278 T22:   0.3599                                     
REMARK   3      T33:   0.3545 T12:   0.0913                                     
REMARK   3      T13:  -0.1025 T23:   0.0162                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.1297 L22:   0.9338                                     
REMARK   3      L33:   1.2118 L12:  -1.0217                                     
REMARK   3      L13:  -0.1596 L23:   0.3138                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1628 S12:   0.0552 S13:   0.3801                       
REMARK   3      S21:   0.2762 S22:   0.0790 S23:   0.0140                       
REMARK   3      S31:  -0.2596 S32:  -0.0854 S33:   0.0009                       
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 65 THROUGH 77 )                   
REMARK   3    ORIGIN FOR THE GROUP (A):  26.1819  50.1437 100.3417              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4784 T22:   0.5203                                     
REMARK   3      T33:   0.7210 T12:   0.0644                                     
REMARK   3      T13:  -0.0895 T23:   0.0352                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.1549 L22:   0.1812                                     
REMARK   3      L33:   0.3001 L12:   0.0788                                     
REMARK   3      L13:  -0.2195 L23:  -0.1473                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.3842 S12:   0.6980 S13:   0.5445                       
REMARK   3      S21:   0.2496 S22:  -0.5896 S23:   0.2165                       
REMARK   3      S31:  -0.1180 S32:  -0.3146 S33:  -0.0003                       
REMARK   3   TLS GROUP : 8                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 78 THROUGH 95 )                   
REMARK   3    ORIGIN FOR THE GROUP (A):  26.6891  37.7976 106.6155              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2862 T22:   0.4551                                     
REMARK   3      T33:   0.3692 T12:  -0.0022                                     
REMARK   3      T13:   0.0275 T23:   0.0491                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.8112 L22:   0.6878                                     
REMARK   3      L33:   0.7148 L12:   0.7496                                     
REMARK   3      L13:   0.3734 L23:   0.2465                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.3727 S12:   0.2971 S13:  -0.1121                       
REMARK   3      S21:   0.0092 S22:   0.2501 S23:   0.0392                       
REMARK   3      S31:   0.0834 S32:  -0.1515 S33:  -0.0004                       
REMARK   3   TLS GROUP : 9                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 96 THROUGH 121 )                  
REMARK   3    ORIGIN FOR THE GROUP (A):  33.2028  46.7680 116.5354              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3426 T22:   0.2902                                     
REMARK   3      T33:   0.2820 T12:   0.0701                                     
REMARK   3      T13:  -0.1461 T23:  -0.0037                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.3470 L22:   0.5476                                     
REMARK   3      L33:   1.2162 L12:   0.4002                                     
REMARK   3      L13:   0.2002 L23:   0.8312                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.3423 S12:  -0.0800 S13:   0.0970                       
REMARK   3      S21:   0.1924 S22:   0.0946 S23:  -0.0839                       
REMARK   3      S31:  -0.2533 S32:  -0.1337 S33:  -0.1906                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : 1                                           
REMARK   3   NCS GROUP : 1                                                      
REMARK   3    NCS OPERATOR : 1                                                  
REMARK   3     REFERENCE SELECTION: chain "A" and (resid 18 through 63 or       
REMARK   3                          (resid 64 and (name N or name CA or name    
REMARK   3                          C or name O or name CB )) or resid 69       
REMARK   3                          through 121))                               
REMARK   3     SELECTION          : (chain "B" and ((resid 18 through 19 and    
REMARK   3                          (name N or name CA or name C or name O or   
REMARK   3                          name CB )) or resid 20 through 64 or        
REMARK   3                          resid 69 through 120 or (resid 121 and      
REMARK   3                          (name N or name CA or name C or name O or   
REMARK   3                          name CB ))))                                
REMARK   3     ATOM PAIRS NUMBER  : NULL                                        
REMARK   3     RMSD               : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 7JTL COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 18-AUG-20.                  
REMARK 100 THE DEPOSITION ID IS D_1000251370.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 29-MAY-20                          
REMARK 200  TEMPERATURE           (KELVIN) : 80                                 
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ALS                                
REMARK 200  BEAMLINE                       : 5.0.2                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.000001                           
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS3 S 6M              
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : AIMLESS                            
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 17510                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.040                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 43.650                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 95.1                               
REMARK 200  DATA REDUNDANCY                : 10.00                              
REMARK 200  R MERGE                    (I) : 0.10090                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 14.9200                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.04                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.11                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : 1.59200                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : 1.200                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD                          
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 53.50                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.65                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 100 MM SODIUM DIHYDROGEN PHOSPHATE PH    
REMARK 280  6.5, 12 % (W/V) PEG8000, VAPOR DIFFUSION, HANGING DROP,             
REMARK 280  TEMPERATURE 298K                                                    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 41 21 2                        
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z+1/2                                             
REMARK 290       3555   -Y+1/2,X+1/2,Z+1/4                                      
REMARK 290       4555   Y+1/2,-X+1/2,Z+3/4                                      
REMARK 290       5555   -X+1/2,Y+1/2,-Z+1/4                                     
REMARK 290       6555   X+1/2,-Y+1/2,-Z+3/4                                     
REMARK 290       7555   Y,X,-Z                                                  
REMARK 290       8555   -Y,-X,-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      132.05550            
REMARK 290   SMTRY1   3  0.000000 -1.000000  0.000000       22.12900            
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000       22.12900            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       66.02775            
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000       22.12900            
REMARK 290   SMTRY2   4 -1.000000  0.000000  0.000000       22.12900            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000      198.08325            
REMARK 290   SMTRY1   5 -1.000000  0.000000  0.000000       22.12900            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       22.12900            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000       66.02775            
REMARK 290   SMTRY1   6  1.000000  0.000000  0.000000       22.12900            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       22.12900            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000      198.08325            
REMARK 290   SMTRY1   7  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   7  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   8  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   8 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000      132.05550            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 1620 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 12190 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -16.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 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    15                                                      
REMARK 465     ASN A    16                                                      
REMARK 465     ALA A    17                                                      
REMARK 465     ALA A    65                                                      
REMARK 465     GLY A    66                                                      
REMARK 465     SER B    15                                                      
REMARK 465     ASN B    16                                                      
REMARK 465     ALA B    17                                                      
REMARK 465     GLY B    66                                                      
REMARK 465     SER B    67                                                      
REMARK 465     LYS B    68                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     GLN A  18    CG   CD   OE1  NE2                                  
REMARK 470     GLU A  19    CG   CD   OE1  OE2                                  
REMARK 470     ASP A  63    CG   OD1  OD2                                       
REMARK 470     SER A  67    OG                                                  
REMARK 470     LYS A  68    CG   CD   CE   NZ                                   
REMARK 470     ILE A 121    CG1  CG2  CD1                                       
REMARK 470     ASP B  63    CG   OD1  OD2                                       
REMARK 470     GLU B  64    CG   CD   OE1  OE2                                  
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   O    HOH A   351     O    HOH A   379              1.86            
REMARK 500   O    HOH A   370     O    HOH A   392              1.88            
REMARK 500   O    HOH B   221     O    HOH B   291              1.92            
REMARK 500   O    HOH A   364     O    HOH A   384              1.93            
REMARK 500   O    HOH B   253     O    HOH B   287              1.95            
REMARK 500   OH   TYR A   105     O    HOH A   301              1.95            
REMARK 500   O    HOH A   353     O    HOH A   372              1.97            
REMARK 500   O    HOH A   334     O    HOH A   374              1.98            
REMARK 500   O    HOH B   231     O    HOH B   266              2.00            
REMARK 500   O    HOH B   231     O    HOH B   257              2.01            
REMARK 500   O    HOH B   271     O    HOH B   292              2.04            
REMARK 500   O    HOH B   208     O    HOH B   277              2.05            
REMARK 500   O    HOH A   387     O    HOH B   282              2.05            
REMARK 500   O    HOH B   234     O    HOH B   284              2.07            
REMARK 500   O    HOH B   258     O    HOH B   260              2.11            
REMARK 500   O    HOH A   367     O    HOH A   388              2.13            
REMARK 500   O    HOH A   311     O    HOH A   366              2.13            
REMARK 500   OD2  ASP B   107     O    HOH B   201              2.13            
REMARK 500   O    GLU A    64     O    HOH A   302              2.14            
REMARK 500   OG   SER B    69     O    HOH B   202              2.14            
REMARK 500   O    HOH B   254     O    HOH B   268              2.14            
REMARK 500   O    HOH B   271     O    HOH B   280              2.19            
REMARK 500   O    HOH A   338     O    HOH A   370              2.19            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   O    HOH A   317     O    HOH A   352     1545     2.04            
REMARK 500   O    HOH A   389     O    HOH B   281     6565     2.18            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ASP A  63       51.47   -140.96                                   
REMARK 500    SER A  69      140.86    177.25                                   
REMARK 500    CYS A  90       98.36    -65.03                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH A 407        DISTANCE =  5.93 ANGSTROMS                       
REMARK 525    HOH B 294        DISTANCE =  5.93 ANGSTROMS                       
REMARK 525    HOH B 295        DISTANCE =  6.98 ANGSTROMS                       
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              NA A 201  NA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH A 307   O                                                      
REMARK 620 2 HOH B 287   O   130.5                                              
REMARK 620 N                    1                                               
DBREF  7JTL A   18   121  UNP    P0DTC8   NS8_SARS2       18    121             
DBREF  7JTL B   18   121  UNP    P0DTC8   NS8_SARS2       18    121             
SEQADV 7JTL SER A   15  UNP  P0DTC8              EXPRESSION TAG                 
SEQADV 7JTL ASN A   16  UNP  P0DTC8              EXPRESSION TAG                 
SEQADV 7JTL ALA A   17  UNP  P0DTC8              EXPRESSION TAG                 
SEQADV 7JTL SER B   15  UNP  P0DTC8              EXPRESSION TAG                 
SEQADV 7JTL ASN B   16  UNP  P0DTC8              EXPRESSION TAG                 
SEQADV 7JTL ALA B   17  UNP  P0DTC8              EXPRESSION TAG                 
SEQRES   1 A  107  SER ASN ALA GLN GLU CYS SER LEU GLN SER CYS THR GLN          
SEQRES   2 A  107  HIS GLN PRO TYR VAL VAL ASP ASP PRO CYS PRO ILE HIS          
SEQRES   3 A  107  PHE TYR SER LYS TRP TYR ILE ARG VAL GLY ALA ARG LYS          
SEQRES   4 A  107  SER ALA PRO LEU ILE GLU LEU CYS VAL ASP GLU ALA GLY          
SEQRES   5 A  107  SER LYS SER PRO ILE GLN TYR ILE ASP ILE GLY ASN TYR          
SEQRES   6 A  107  THR VAL SER CYS LEU PRO PHE THR ILE ASN CYS GLN GLU          
SEQRES   7 A  107  PRO LYS LEU GLY SER LEU VAL VAL ARG CYS SER PHE TYR          
SEQRES   8 A  107  GLU ASP PHE LEU GLU TYR HIS ASP VAL ARG VAL VAL LEU          
SEQRES   9 A  107  ASP PHE ILE                                                  
SEQRES   1 B  107  SER ASN ALA GLN GLU CYS SER LEU GLN SER CYS THR GLN          
SEQRES   2 B  107  HIS GLN PRO TYR VAL VAL ASP ASP PRO CYS PRO ILE HIS          
SEQRES   3 B  107  PHE TYR SER LYS TRP TYR ILE ARG VAL GLY ALA ARG LYS          
SEQRES   4 B  107  SER ALA PRO LEU ILE GLU LEU CYS VAL ASP GLU ALA GLY          
SEQRES   5 B  107  SER LYS SER PRO ILE GLN TYR ILE ASP ILE GLY ASN TYR          
SEQRES   6 B  107  THR VAL SER CYS LEU PRO PHE THR ILE ASN CYS GLN GLU          
SEQRES   7 B  107  PRO LYS LEU GLY SER LEU VAL VAL ARG CYS SER PHE TYR          
SEQRES   8 B  107  GLU ASP PHE LEU GLU TYR HIS ASP VAL ARG VAL VAL LEU          
SEQRES   9 B  107  ASP PHE ILE                                                  
HET     NA  A 201       1                                                       
HETNAM      NA SODIUM ION                                                       
FORMUL   3   NA    NA 1+                                                        
FORMUL   4  HOH   *202(H2 O)                                                    
SHEET    1 AA1 5 CYS A  20  CYS A  25  0                                        
SHEET    2 AA1 5 TYR A 111  PHE A 120  1  O  ASP A 119   N  GLN A  23           
SHEET    3 AA1 5 GLY A  96  SER A 103 -1  N  VAL A 100   O  VAL A 114           
SHEET    4 AA1 5 TYR A  42  VAL A  49 -1  N  TYR A  42   O  SER A 103           
SHEET    5 AA1 5 LEU A  57  GLU A  59 -1  O  ILE A  58   N  ILE A  47           
SHEET    1 AA2 3 PRO A  30  VAL A  32  0                                        
SHEET    2 AA2 3 THR A  87  ASN A  89 -1  O  ILE A  88   N  TYR A  31           
SHEET    3 AA2 3 THR A  80  SER A  82 -1  N  SER A  82   O  THR A  87           
SHEET    1 AA3 5 GLU B  19  CYS B  25  0                                        
SHEET    2 AA3 5 HIS B 112  PHE B 120  1  O  ASP B 119   N  GLN B  23           
SHEET    3 AA3 5 GLY B  96  SER B 103 -1  N  CYS B 102   O  HIS B 112           
SHEET    4 AA3 5 TYR B  42  VAL B  49 -1  N  TYR B  42   O  SER B 103           
SHEET    5 AA3 5 LEU B  57  GLU B  59 -1  O  ILE B  58   N  ILE B  47           
SHEET    1 AA4 3 PRO B  30  VAL B  32  0                                        
SHEET    2 AA4 3 THR B  87  ASN B  89 -1  O  ILE B  88   N  TYR B  31           
SHEET    3 AA4 3 THR B  80  SER B  82 -1  N  SER B  82   O  THR B  87           
SSBOND   1 CYS A   20    CYS B   20                          1555   1555  2.06  
SSBOND   2 CYS A   25    CYS A   90                          1555   1555  2.02  
SSBOND   3 CYS A   37    CYS A  102                          1555   1555  2.04  
SSBOND   4 CYS A   61    CYS A   83                          1555   1555  2.07  
SSBOND   5 CYS B   25    CYS B   90                          1555   1555  2.02  
SSBOND   6 CYS B   37    CYS B  102                          1555   1555  2.01  
SSBOND   7 CYS B   61    CYS B   83                          1555   1555  2.08  
LINK        NA    NA A 201                 O   HOH A 307     1555   1555  2.38  
LINK        NA    NA A 201                 O   HOH B 287     1555   1555  2.80  
CISPEP   1 LEU A   84    PRO A   85          0        -6.82                     
CISPEP   2 LEU B   84    PRO B   85          0        -5.54                     
CRYST1   44.258   44.258  264.111  90.00  90.00  90.00 P 41 21 2    16          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.022595  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.022595  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.003786        0.00000                         
MTRIX1   1 -0.999049  0.030579  0.031078       75.72260    1                    
MTRIX2   1 -0.018405 -0.941971  0.335190       32.30323    1                    
MTRIX3   1  0.039524  0.334300  0.941638       -7.30091    1                    
ATOM      1  N   GLN A  18      40.917  33.173 126.601  1.00 73.92           N  
ANISOU    1  N   GLN A  18     9116  11193   7776    437    509   -283       N  
ATOM      2  CA  GLN A  18      42.025  33.162 125.645  1.00 73.89           C  
ANISOU    2  CA  GLN A  18     9103  11065   7907    364    439   -296       C  
ATOM      3  C   GLN A  18      41.754  32.204 124.493  1.00 67.88           C  
ANISOU    3  C   GLN A  18     8268  10380   7143    204    481   -210       C  
ATOM      4  O   GLN A  18      42.414  31.177 124.374  1.00 66.48           O  
ANISOU    4  O   GLN A  18     8146  10157   6957    112    453   -218       O  
ATOM      5  CB  GLN A  18      43.339  32.782 126.337  1.00 73.82           C  
ANISOU    5  CB  GLN A  18     9225  10902   7922    375    352   -382       C  
ATOM      6  N   GLU A  19      40.764  32.527 123.665  1.00 60.90           N  
ANISOU    6  N   GLU A  19     7263   9614   6263    177    544   -133       N  
ATOM      7  CA  GLU A  19      40.434  31.695 122.517  1.00 50.80           C  
ANISOU    7  CA  GLU A  19     5910   8411   4982     35    579    -52       C  
ATOM      8  C   GLU A  19      40.928  32.273 121.201  1.00 50.81           C  
ANISOU    8  C   GLU A  19     5827   8367   5112      2    547    -34       C  
ATOM      9  O   GLU A  19      41.122  31.517 120.240  1.00 47.32           O  
ANISOU    9  O   GLU A  19     5351   7944   4684   -111    547      6       O  
ATOM     10  CB  GLU A  19      38.918  31.467 122.431  1.00 55.27           C  
ANISOU   10  CB  GLU A  19     6392   9155   5453      6    675     36       C  
ATOM     11  N   CYS A  20      41.101  33.590 121.115  1.00 51.03           N  
ANISOU   11  N   CYS A  20     5818   8340   5230    100    518    -56       N  
ATOM     12  CA  CYS A  20      41.551  34.244 119.893  1.00 41.77           C  
ANISOU   12  CA  CYS A  20     4558   7129   4182     72    486    -27       C  
ATOM     13  C   CYS A  20      42.699  35.209 120.189  1.00 40.41           C  
ANISOU   13  C   CYS A  20     4430   6798   4126    157    392    -95       C  
ATOM     14  O   CYS A  20      42.709  35.887 121.221  1.00 46.45           O  
ANISOU   14  O   CYS A  20     5256   7505   4888    274    362   -155       O  
ATOM     15  CB  CYS A  20      40.393  34.986 119.225  1.00 46.48           C  
ANISOU   15  CB  CYS A  20     5034   7839   4789     88    542     45       C  
ATOM     16  SG  CYS A  20      40.867  35.722 117.656  1.00 56.21           S  
ANISOU   16  SG  CYS A  20     6153   9040   6163     43    508     99       S  
ATOM     17  N   SER A  21      43.669  35.254 119.283  1.00 38.94           N  
ANISOU   17  N   SER A  21     4211   6543   4040    100    343    -84       N  
ATOM     18  CA  SER A  21      44.851  36.104 119.410  1.00 35.69           C  
ANISOU   18  CA  SER A  21     3826   5980   3754    157    246   -131       C  
ATOM     19  C   SER A  21      44.916  36.902 118.118  1.00 35.79           C  
ANISOU   19  C   SER A  21     3715   6007   3878    126    236    -58       C  
ATOM     20  O   SER A  21      45.172  36.333 117.051  1.00 32.57           O  
ANISOU   20  O   SER A  21     3247   5648   3481     27    255     -7       O  
ATOM     21  CB  SER A  21      46.118  35.269 119.634  1.00 33.65           C  
ANISOU   21  CB  SER A  21     3651   5628   3507    112    192   -184       C  
ATOM     22  OG  SER A  21      47.328  36.023 119.512  1.00 33.95           O  
ANISOU   22  OG  SER A  21     3690   5529   3679    143     99   -210       O  
ATOM     23  N   LEU A  22      44.643  38.202 118.205  1.00 36.94           N  
ANISOU   23  N   LEU A  22     3822   6114   4098    214    203    -52       N  
ATOM     24  CA  LEU A  22      44.631  39.082 117.041  1.00 35.49           C  
ANISOU   24  CA  LEU A  22     3521   5941   4024    191    186     25       C  
ATOM     25  C   LEU A  22      45.993  39.763 116.942  1.00 34.55           C  
ANISOU   25  C   LEU A  22     3410   5670   4047    207     78      8       C  
ATOM     26  O   LEU A  22      46.412  40.451 117.875  1.00 37.54           O  
ANISOU   26  O   LEU A  22     3860   5927   4477    301      0    -57       O  
ATOM     27  CB  LEU A  22      43.520  40.122 117.155  1.00 38.67           C  
ANISOU   27  CB  LEU A  22     3873   6386   4434    277    203     46       C  
ATOM     28  CG  LEU A  22      43.475  41.147 116.024  1.00 41.31           C  
ANISOU   28  CG  LEU A  22     4090   6719   4887    262    174    127       C  
ATOM     29  CD1 LEU A  22      43.308  40.438 114.693  1.00 37.10           C  
ANISOU   29  CD1 LEU A  22     3462   6302   4330    134    240    214       C  
ATOM     30  CD2 LEU A  22      42.386  42.162 116.241  1.00 46.10           C  
ANISOU   30  CD2 LEU A  22     4659   7359   5499    358    181    136       C  
ATOM     31  N   GLN A  23      46.676  39.584 115.820  1.00 32.31           N  
ANISOU   31  N   GLN A  23     3052   5399   3827    117     70     70       N  
ATOM     32  CA  GLN A  23      48.026  40.101 115.679  1.00 35.96           C  
ANISOU   32  CA  GLN A  23     3512   5733   4420    116    -28     67       C  
ATOM     33  C   GLN A  23      48.129  40.869 114.379  1.00 36.92           C  
ANISOU   33  C   GLN A  23     3499   5886   4645     69    -41    173       C  
ATOM     34  O   GLN A  23      47.308  40.706 113.477  1.00 34.85           O  
ANISOU   34  O   GLN A  23     3152   5752   4338     19     33    242       O  
ATOM     35  CB  GLN A  23      49.080  38.978 115.752  1.00 33.22           C  
ANISOU   35  CB  GLN A  23     3219   5360   4042     56    -37     26       C  
ATOM     36  CG  GLN A  23      49.081  38.307 117.122  1.00 36.84           C  
ANISOU   36  CG  GLN A  23     3818   5768   4409    106    -40    -77       C  
ATOM     37  CD  GLN A  23      50.113  37.220 117.258  1.00 37.90           C  
ANISOU   37  CD  GLN A  23     4016   5867   4518     54    -59   -123       C  
ATOM     38  OE1 GLN A  23      51.178  37.277 116.645  1.00 33.05           O  
ANISOU   38  OE1 GLN A  23     3358   5210   3989     15   -106   -101       O  
ATOM     39  NE2 GLN A  23      49.808  36.219 118.072  1.00 35.01           N  
ANISOU   39  NE2 GLN A  23     3749   5521   4031     55    -24   -184       N  
ATOM     40  N   SER A  24      49.141  41.729 114.310  1.00 33.69           N  
ANISOU   40  N   SER A  24     3069   5354   4376     86   -142    189       N  
ATOM     41  CA  SER A  24      49.355  42.636 113.187  1.00 36.00           C  
ANISOU   41  CA  SER A  24     3236   5655   4787     48   -175    298       C  
ATOM     42  C   SER A  24      50.733  42.408 112.590  1.00 38.21           C  
ANISOU   42  C   SER A  24     3474   5903   5142    -20   -218    336       C  
ATOM     43  O   SER A  24      51.714  42.271 113.320  1.00 33.70           O  
ANISOU   43  O   SER A  24     2976   5218   4609      2   -286    273       O  
ATOM     44  CB  SER A  24      49.242  44.119 113.611  1.00 38.78           C  
ANISOU   44  CB  SER A  24     3586   5885   5262    135   -274    304       C  
ATOM     45  OG  SER A  24      47.976  44.409 114.168  1.00 44.24           O  
ANISOU   45  OG  SER A  24     4311   6612   5886    214   -238    266       O  
ATOM     46  N   CYS A  25      50.799  42.381 111.261  1.00 37.57           N  
ANISOU   46  N   CYS A  25     3271   5926   5079    -99   -180    440       N  
ATOM     47  CA  CYS A  25      52.067  42.290 110.554  1.00 33.80           C  
ANISOU   47  CA  CYS A  25     2727   5442   4674   -160   -216    495       C  
ATOM     48  C   CYS A  25      51.886  42.883 109.167  1.00 38.31           C  
ANISOU   48  C   CYS A  25     3149   6108   5298   -218   -196    631       C  
ATOM     49  O   CYS A  25      50.774  43.217 108.752  1.00 37.87           O  
ANISOU   49  O   CYS A  25     3050   6126   5211   -215   -149    673       O  
ATOM     50  CB  CYS A  25      52.561  40.843 110.471  1.00 33.18           C  
ANISOU   50  CB  CYS A  25     2689   5432   4488   -206   -159    442       C  
ATOM     51  SG  CYS A  25      51.337  39.589 109.939  1.00 34.65           S  
ANISOU   51  SG  CYS A  25     2877   5799   4490   -251    -26    430       S  
ATOM     52  N   THR A  26      52.999  43.022 108.458  1.00 37.28           N  
ANISOU   52  N   THR A  26     2936   5981   5246   -269   -233    704       N  
ATOM     53  CA  THR A  26      52.990  43.479 107.076  1.00 39.85           C  
ANISOU   53  CA  THR A  26     3115   6414   5613   -331   -212    842       C  
ATOM     54  C   THR A  26      52.792  42.275 106.164  1.00 40.66           C  
ANISOU   54  C   THR A  26     3179   6693   5577   -387   -103    850       C  
ATOM     55  O   THR A  26      53.510  41.278 106.279  1.00 37.48           O  
ANISOU   55  O   THR A  26     2816   6311   5115   -402    -86    792       O  
ATOM     56  CB  THR A  26      54.291  44.212 106.741  1.00 43.03           C  
ANISOU   56  CB  THR A  26     3437   6748   6164   -359   -304    928       C  
ATOM     57  OG1 THR A  26      54.380  45.394 107.539  1.00 45.38           O  
ANISOU   57  OG1 THR A  26     3771   6873   6598   -307   -419    924       O  
ATOM     58  CG2 THR A  26      54.323  44.609 105.287  1.00 47.35           C  
ANISOU   58  CG2 THR A  26     3827   7423   6740   -427   -275   1080       C  
ATOM     59  N   GLN A  27      51.791  42.355 105.296  1.00 39.07           N  
ANISOU   59  N   GLN A  27     2908   6614   5324   -414    -37    916       N  
ATOM     60  CA  GLN A  27      51.447  41.228 104.442  1.00 40.47           C  
ANISOU   60  CA  GLN A  27     3057   6956   5365   -461     59    918       C  
ATOM     61  C   GLN A  27      52.587  40.888 103.489  1.00 41.74           C  
ANISOU   61  C   GLN A  27     3214   7126   5519   -488     57    945       C  
ATOM     62  O   GLN A  27      53.234  41.774 102.934  1.00 43.01           O  
ANISOU   62  O   GLN A  27     3329   7238   5775   -496     12   1025       O  
ATOM     63  CB  GLN A  27      50.170  41.542 103.657  1.00 39.82           C  
ANISOU   63  CB  GLN A  27     2980   6920   5231   -462    111    959       C  
ATOM     64  CG  GLN A  27      49.340  40.334 103.259  1.00 41.91           C  
ANISOU   64  CG  GLN A  27     3322   7267   5336   -476    193    901       C  
ATOM     65  CD  GLN A  27      47.966  40.738 102.716  1.00 41.41           C  
ANISOU   65  CD  GLN A  27     3265   7231   5238   -469    228    935       C  
ATOM     66  OE1 GLN A  27      47.728  41.907 102.403  1.00 43.00           O  
ANISOU   66  OE1 GLN A  27     3413   7399   5525   -458    197   1008       O  
ATOM     67  NE2 GLN A  27      47.060  39.773 102.619  1.00 46.57           N  
ANISOU   67  NE2 GLN A  27     3984   7941   5770   -477    283    885       N  
ATOM     68  N   HIS A  28      52.809  39.585 103.295  1.00 40.41           N  
ANISOU   68  N   HIS A  28     3099   7022   5232   -499    105    875       N  
ATOM     69  CA  HIS A  28      53.733  38.995 102.329  1.00 39.47           C  
ANISOU   69  CA  HIS A  28     2988   6940   5068   -510    118    882       C  
ATOM     70  C   HIS A  28      55.189  39.134 102.752  1.00 43.47           C  
ANISOU   70  C   HIS A  28     3455   7398   5665   -510     58    885       C  
ATOM     71  O   HIS A  28      56.099  38.850 101.955  1.00 42.90           O  
ANISOU   71  O   HIS A  28     3370   7355   5575   -513     62    905       O  
ATOM     72  CB  HIS A  28      53.507  39.591 100.935  1.00 43.74           C  
ANISOU   72  CB  HIS A  28     3513   7503   5604   -516    134    969       C  
ATOM     73  CG  HIS A  28      52.112  39.381 100.428  1.00 43.95           C  
ANISOU   73  CG  HIS A  28     3581   7577   5542   -516    182    965       C  
ATOM     74  ND1 HIS A  28      51.423  40.331  99.703  1.00 48.58           N  
ANISOU   74  ND1 HIS A  28     4143   8158   6159   -517    182   1042       N  
ATOM     75  CD2 HIS A  28      51.266  38.332 100.571  1.00 42.25           C  
ANISOU   75  CD2 HIS A  28     3428   7413   5212   -517    226    893       C  
ATOM     76  CE1 HIS A  28      50.221  39.870  99.404  1.00 47.26           C  
ANISOU   76  CE1 HIS A  28     4021   8035   5901   -515    223   1016       C  
ATOM     77  NE2 HIS A  28      50.099  38.658  99.919  1.00 47.94           N  
ANISOU   77  NE2 HIS A  28     4160   8154   5900   -516    249    929       N  
ATOM     78  N   GLN A  29      55.428  39.497 104.007  1.00 37.96           N  
ANISOU   78  N   GLN A  29     2735   6632   5058   -501     -3    860       N  
ATOM     79  CA  GLN A  29      56.725  39.619 104.629  1.00 38.42           C  
ANISOU   79  CA  GLN A  29     2784   6605   5208   -492    -79    844       C  
ATOM     80  C   GLN A  29      56.769  38.722 105.857  1.00 35.70           C  
ANISOU   80  C   GLN A  29     2599   6166   4800   -452    -89    692       C  
ATOM     81  O   GLN A  29      55.724  38.434 106.452  1.00 34.82           O  
ANISOU   81  O   GLN A  29     2580   6034   4618   -432    -58    624       O  
ATOM     82  CB  GLN A  29      56.987  41.073 105.027  1.00 40.77           C  
ANISOU   82  CB  GLN A  29     3048   6767   5675   -481   -171    915       C  
ATOM     83  CG  GLN A  29      57.029  41.982 103.824  1.00 45.36           C  
ANISOU   83  CG  GLN A  29     3549   7377   6307   -509   -166   1043       C  
ATOM     84  CD  GLN A  29      57.565  43.369 104.134  1.00 56.53           C  
ANISOU   84  CD  GLN A  29     4910   8664   7904   -510   -276   1127       C  
ATOM     85  OE1 GLN A  29      58.086  43.628 105.226  1.00 59.38           O  
ANISOU   85  OE1 GLN A  29     5285   8910   8369   -490   -369   1093       O  
ATOM     86  NE2 GLN A  29      57.435  44.274 103.170  1.00 64.25           N  
ANISOU   86  NE2 GLN A  29     5857   9638   8915   -528   -274   1228       N  
ATOM     87  N   PRO A  30      57.943  38.231 106.237  1.00 34.34           N  
ANISOU   87  N   PRO A  30     2457   5944   4645   -443   -131    639       N  
ATOM     88  CA  PRO A  30      58.009  37.306 107.372  1.00 33.03           C  
ANISOU   88  CA  PRO A  30     2444   5693   4412   -408   -142    496       C  
ATOM     89  C   PRO A  30      57.578  37.960 108.676  1.00 34.58           C  
ANISOU   89  C   PRO A  30     2746   5727   4666   -361   -198    440       C  
ATOM     90  O   PRO A  30      57.801  39.149 108.927  1.00 32.35           O  
ANISOU   90  O   PRO A  30     2431   5347   4515   -345   -267    492       O  
ATOM     91  CB  PRO A  30      59.485  36.881 107.400  1.00 32.98           C  
ANISOU   91  CB  PRO A  30     2424   5664   4442   -406   -188    472       C  
ATOM     92  CG  PRO A  30      59.947  37.098 105.995  1.00 36.59           C  
ANISOU   92  CG  PRO A  30     2719   6269   4916   -446   -158    593       C  
ATOM     93  CD  PRO A  30      59.234  38.327 105.532  1.00 37.38           C  
ANISOU   93  CD  PRO A  30     2733   6379   5092   -466   -157    710       C  
ATOM     94  N   TYR A  31      56.955  37.153 109.524  1.00 29.97           N  
ANISOU   94  N   TYR A  31     2293   5115   3980   -336   -171    331       N  
ATOM     95  CA  TYR A  31      56.445  37.647 110.788  1.00 27.88           C  
ANISOU   95  CA  TYR A  31     2135   4719   3739   -280   -211    268       C  
ATOM     96  C   TYR A  31      56.704  36.585 111.831  1.00 30.48           C  
ANISOU   96  C   TYR A  31     2607   4986   3987   -256   -220    141       C  
ATOM     97  O   TYR A  31      56.250  35.442 111.673  1.00 26.85           O  
ANISOU   97  O   TYR A  31     2190   4613   3400   -281   -157     99       O  
ATOM     98  CB  TYR A  31      54.957  37.984 110.692  1.00 27.25           C  
ANISOU   98  CB  TYR A  31     2050   4697   3606   -273   -152    294       C  
ATOM     99  CG  TYR A  31      54.316  38.284 112.033  1.00 28.70           C  
ANISOU   99  CG  TYR A  31     2353   4774   3778   -205   -177    215       C  
ATOM    100  CD1 TYR A  31      54.724  39.376 112.803  1.00 30.26           C  
ANISOU  100  CD1 TYR A  31     2579   4823   4096   -146   -272    203       C  
ATOM    101  CD2 TYR A  31      53.299  37.484 112.525  1.00 30.32           C  
ANISOU  101  CD2 TYR A  31     2639   5030   3850   -197   -111    154       C  
ATOM    102  CE1 TYR A  31      54.138  39.646 114.024  1.00 32.38           C  
ANISOU  102  CE1 TYR A  31     2958   5004   4342    -71   -296    124       C  
ATOM    103  CE2 TYR A  31      52.698  37.747 113.748  1.00 29.72           C  
ANISOU  103  CE2 TYR A  31     2665   4876   3750   -128   -126     86       C  
ATOM    104  CZ  TYR A  31      53.122  38.823 114.491  1.00 32.12           C  
ANISOU  104  CZ  TYR A  31     2999   5039   4165    -60   -217     67       C  
ATOM    105  OH  TYR A  31      52.530  39.072 115.700  1.00 35.30           O  
ANISOU  105  OH  TYR A  31     3505   5374   4533     20   -233     -8       O  
ATOM    106  N   VAL A  32      57.451  36.953 112.870  1.00 28.69           N  
ANISOU  106  N   VAL A  32     2456   4608   3838   -209   -307     84       N  
ATOM    107  CA  VAL A  32      57.655  36.073 114.011  1.00 32.08           C  
ANISOU  107  CA  VAL A  32     3033   4962   4196   -177   -326    -37       C  
ATOM    108  C   VAL A  32      56.385  36.107 114.850  1.00 30.44           C  
ANISOU  108  C   VAL A  32     2915   4742   3909   -138   -291    -83       C  
ATOM    109  O   VAL A  32      56.067  37.126 115.465  1.00 31.60           O  
ANISOU  109  O   VAL A  32     3083   4804   4121    -82   -334    -83       O  
ATOM    110  CB  VAL A  32      58.871  36.495 114.833  1.00 30.01           C  
ANISOU  110  CB  VAL A  32     2818   4541   4044   -138   -435    -82       C  
ATOM    111  CG1 VAL A  32      59.035  35.582 116.050  1.00 33.80           C  
ANISOU  111  CG1 VAL A  32     3457   4942   4443   -103   -455   -207       C  
ATOM    112  CG2 VAL A  32      60.104  36.493 113.959  1.00 31.42           C  
ANISOU  112  CG2 VAL A  32     2889   4748   4301   -179   -464    -23       C  
ATOM    113  N   VAL A  33      55.673  34.980 114.898  1.00 32.30           N  
ANISOU  113  N   VAL A  33     3932   4305   4036    224   -498     89       N  
ATOM    114  CA  VAL A  33      54.365  34.968 115.536  1.00 31.37           C  
ANISOU  114  CA  VAL A  33     3788   4269   3862    242   -478     84       C  
ATOM    115  C   VAL A  33      54.522  35.061 117.041  1.00 34.03           C  
ANISOU  115  C   VAL A  33     4082   4761   4088    226   -487    170       C  
ATOM    116  O   VAL A  33      55.210  34.244 117.658  1.00 35.38           O  
ANISOU  116  O   VAL A  33     4180   4969   4295    203   -482    307       O  
ATOM    117  CB  VAL A  33      53.582  33.703 115.162  1.00 31.06           C  
ANISOU  117  CB  VAL A  33     3680   4168   3953    241   -427    139       C  
ATOM    118  CG1 VAL A  33      52.226  33.729 115.851  1.00 29.40           C  
ANISOU  118  CG1 VAL A  33     3439   4051   3682    259   -408    134       C  
ATOM    119  CG2 VAL A  33      53.448  33.572 113.650  1.00 28.69           C  
ANISOU  119  CG2 VAL A  33     3423   3722   3757    239   -416     52       C  
ATOM    120  N   ASP A  34      53.853  36.037 117.646  1.00 33.34           N  
ANISOU  120  N   ASP A  34     4038   4766   3865    237   -494     96       N  
ATOM    121  CA  ASP A  34      53.847  36.112 119.101  1.00 38.04           C  
ANISOU  121  CA  ASP A  34     4596   5514   4343    213   -495    170       C  
ATOM    122  C   ASP A  34      53.085  34.909 119.650  1.00 38.52           C  
ANISOU  122  C   ASP A  34     4558   5608   4469    216   -456    284       C  
ATOM    123  O   ASP A  34      51.918  34.697 119.309  1.00 33.88           O  
ANISOU  123  O   ASP A  34     3963   4988   3924    245   -425    242       O  
ATOM    124  CB  ASP A  34      53.215  37.422 119.564  1.00 38.94           C  
ANISOU  124  CB  ASP A  34     4787   5703   4307    222   -493     54       C  
ATOM    125  CG  ASP A  34      53.428  37.675 121.030  1.00 48.63           C  
ANISOU  125  CG  ASP A  34     5996   7089   5393    178   -496    113       C  
ATOM    126  OD1 ASP A  34      54.156  36.885 121.671  1.00 52.82           O  
ANISOU  126  OD1 ASP A  34     6452   7681   5936    140   -511    249       O  
ATOM    127  OD2 ASP A  34      52.855  38.643 121.564  1.00 55.44           O  
ANISOU  127  OD2 ASP A  34     6917   8018   6131    178   -477     28       O  
ATOM    128  N   ASP A  35      53.751  34.101 120.453  1.00 37.97           N  
ANISOU  128  N   ASP A  35     4411   5604   4414    187   -457    432       N  
ATOM    129  CA  ASP A  35      53.118  32.915 120.997  1.00 39.79           C  
ANISOU  129  CA  ASP A  35     4547   5860   4710    190   -414    551       C  
ATOM    130  C   ASP A  35      52.142  33.323 122.088  1.00 41.28           C  
ANISOU  130  C   ASP A  35     4732   6181   4771    188   -402    537       C  
ATOM    131  O   ASP A  35      52.565  33.878 123.106  1.00 42.24           O  
ANISOU  131  O   ASP A  35     4861   6431   4756    154   -426    562       O  
ATOM    132  CB  ASP A  35      54.169  31.957 121.554  1.00 42.69           C  
ANISOU  132  CB  ASP A  35     4828   6260   5132    165   -413    728       C  
ATOM    133  CG  ASP A  35      53.578  30.616 122.003  1.00 48.82           C  
ANISOU  133  CG  ASP A  35     5506   7040   6002    172   -357    861       C  
ATOM    134  OD1 ASP A  35      52.381  30.555 122.367  1.00 45.04           O  
ANISOU  134  OD1 ASP A  35     5020   6602   5492    183   -329    830       O  
ATOM    135  OD2 ASP A  35      54.318  29.608 121.978  1.00 47.86           O  
ANISOU  135  OD2 ASP A  35     5315   6877   5992    168   -333    999       O  
ATOM    136  N   PRO A  36      50.836  33.079 121.924  1.00 41.68           N  
ANISOU  136  N   PRO A  36     4771   6210   4855    216   -363    496       N  
ATOM    137  CA  PRO A  36      49.855  33.477 122.942  1.00 42.07           C  
ANISOU  137  CA  PRO A  36     4817   6378   4789    218   -343    480       C  
ATOM    138  C   PRO A  36      49.641  32.471 124.064  1.00 45.20           C  
ANISOU  138  C   PRO A  36     5119   6868   5186    197   -316    628       C  
ATOM    139  O   PRO A  36      48.705  32.656 124.845  1.00 49.16           O  
ANISOU  139  O   PRO A  36     5613   7458   5609    199   -290    617       O  
ATOM    140  CB  PRO A  36      48.572  33.623 122.113  1.00 39.61           C  
ANISOU  140  CB  PRO A  36     4526   5993   4530    262   -314    375       C  
ATOM    141  CG  PRO A  36      48.702  32.562 121.092  1.00 38.64           C  
ANISOU  141  CG  PRO A  36     4363   5744   4574    264   -300    414       C  
ATOM    142  CD  PRO A  36      50.188  32.448 120.767  1.00 37.74           C  
ANISOU  142  CD  PRO A  36     4262   5580   4500    242   -332    459       C  
ATOM    143  N   CYS A  37      50.427  31.400 124.140  1.00 43.90           N  
ANISOU  143  N   CYS A  37     4883   6683   5114    181   -312    769       N  
ATOM    144  CA  CYS A  37      50.279  30.476 125.246  1.00 48.63           C  
ANISOU  144  CA  CYS A  37     5391   7376   5709    163   -285    922       C  
ATOM    145  C   CYS A  37      50.800  31.129 126.522  1.00 51.31           C  
ANISOU  145  C   CYS A  37     5736   7885   5874    118   -321    964       C  
ATOM    146  O   CYS A  37      51.737  31.926 126.475  1.00 53.09           O  
ANISOU  146  O   CYS A  37     6011   8138   6025     94   -369    927       O  
ATOM    147  CB  CYS A  37      51.052  29.187 124.974  1.00 48.95           C  
ANISOU  147  CB  CYS A  37     5353   7343   5901    162   -263   1072       C  
ATOM    148  SG  CYS A  37      50.405  28.245 123.560  1.00 49.59           S  
ANISOU  148  SG  CYS A  37     5426   7229   6187    192   -201   1030       S  
ATOM    149  N   PRO A  38      50.223  30.793 127.676  1.00 55.23           N  
ANISOU  149  N   PRO A  38     6183   8502   6302    100   -298   1042       N  
ATOM    150  CA  PRO A  38      50.739  31.322 128.942  1.00 57.99           C  
ANISOU  150  CA  PRO A  38     6531   9024   6478     42   -329   1093       C  
ATOM    151  C   PRO A  38      52.182  30.900 129.152  1.00 60.19           C  
ANISOU  151  C   PRO A  38     6755   9344   6771      9   -371   1236       C  
ATOM    152  O   PRO A  38      52.677  29.954 128.537  1.00 61.66           O  
ANISOU  152  O   PRO A  38     6882   9431   7113     37   -360   1330       O  
ATOM    153  CB  PRO A  38      49.815  30.707 129.998  1.00 56.56           C  
ANISOU  153  CB  PRO A  38     6288   8939   6262     34   -287   1175       C  
ATOM    154  CG  PRO A  38      48.579  30.313 129.251  1.00 57.71           C  
ANISOU  154  CG  PRO A  38     6435   8968   6525     90   -234   1103       C  
ATOM    155  CD  PRO A  38      49.042  29.934 127.876  1.00 56.31           C  
ANISOU  155  CD  PRO A  38     6263   8624   6506    124   -239   1081       C  
ATOM    156  N   ILE A  39      52.882  31.653 129.998  1.00 62.48           N  
ANISOU  156  N   ILE A  39     7065   9782   6894    -55   -416   1247       N  
ATOM    157  CA  ILE A  39      54.288  31.353 130.215  1.00 67.08           C  
ANISOU  157  CA  ILE A  39     7590  10422   7476    -91   -464   1384       C  
ATOM    158  C   ILE A  39      54.419  29.983 130.886  1.00 67.27           C  
ANISOU  158  C   ILE A  39     7483  10499   7576    -87   -442   1607       C  
ATOM    159  O   ILE A  39      53.553  29.558 131.658  1.00 67.78           O  
ANISOU  159  O   ILE A  39     7512  10630   7610    -89   -406   1654       O  
ATOM    160  CB  ILE A  39      54.974  32.465 131.028  1.00 68.97           C  
ANISOU  160  CB  ILE A  39     7877  10826   7504   -177   -517   1347       C  
ATOM    161  CG1 ILE A  39      56.492  32.313 130.929  1.00 72.96           C  
ANISOU  161  CG1 ILE A  39     8333  11368   8023   -209   -573   1461       C  
ATOM    162  CG2 ILE A  39      54.481  32.483 132.469  1.00 70.10           C  
ANISOU  162  CG2 ILE A  39     7991  11154   7491   -237   -507   1408       C  
ATOM    163  CD1 ILE A  39      56.981  32.163 129.495  1.00 75.75           C  
ANISOU  163  CD1 ILE A  39     8708  11527   8545   -148   -574   1413       C  
ATOM    164  N   HIS A  40      55.502  29.277 130.555  1.00 68.12           N  
ANISOU  164  N   HIS A  40     7521  10568   7795    -75   -456   1746       N  
ATOM    165  CA  HIS A  40      55.837  27.912 130.962  1.00 69.48           C  
ANISOU  165  CA  HIS A  40     7565  10755   8081    -56   -425   1974       C  
ATOM    166  C   HIS A  40      54.973  26.854 130.293  1.00 66.31           C  
ANISOU  166  C   HIS A  40     7137  10186   7870     12   -342   1986       C  
ATOM    167  O   HIS A  40      55.119  25.669 130.611  1.00 69.51           O  
ANISOU  167  O   HIS A  40     7442  10585   8383     33   -298   2169       O  
ATOM    168  CB  HIS A  40      55.756  27.694 132.482  1.00 72.93           C  
ANISOU  168  CB  HIS A  40     7930  11404   8377   -110   -438   2116       C  
ATOM    169  CG  HIS A  40      56.555  28.673 133.286  1.00 75.39           C  
ANISOU  169  CG  HIS A  40     8260  11906   8480   -198   -514   2115       C  
ATOM    170  ND1 HIS A  40      55.968  29.631 134.085  1.00 77.13           N  
ANISOU  170  ND1 HIS A  40     8549  12257   8498   -262   -530   2002       N  
ATOM    171  CD2 HIS A  40      57.893  28.841 133.415  1.00 80.28           C  
ANISOU  171  CD2 HIS A  40     8837  12609   9057   -239   -574   2212       C  
ATOM    172  CE1 HIS A  40      56.910  30.346 134.675  1.00 77.74           C  
ANISOU  172  CE1 HIS A  40     8633  12492   8413   -348   -595   2023       C  
ATOM    173  NE2 HIS A  40      58.087  29.888 134.284  1.00 81.83           N  
ANISOU  173  NE2 HIS A  40     9080  12991   9022   -336   -628   2152       N  
ATOM    174  N   PHE A  41      54.077  27.229 129.392  1.00 60.49           N  
ANISOU  174  N   PHE A  41     6484   9319   7178     43   -317   1802       N  
ATOM    175  CA  PHE A  41      53.342  26.259 128.596  1.00 62.07           C  
ANISOU  175  CA  PHE A  41     6667   9355   7563     94   -240   1798       C  
ATOM    176  C   PHE A  41      54.123  25.883 127.342  1.00 59.54           C  
ANISOU  176  C   PHE A  41     6353   8861   7409    123   -224   1796       C  
ATOM    177  O   PHE A  41      54.781  26.725 126.725  1.00 55.99           O  
ANISOU  177  O   PHE A  41     5967   8378   6926    115   -274   1699       O  
ATOM    178  CB  PHE A  41      51.975  26.818 128.190  1.00 57.77           C  
ANISOU  178  CB  PHE A  41     6200   8762   6986    108   -221   1609       C  
ATOM    179  CG  PHE A  41      50.907  26.641 129.233  1.00 58.70           C  
ANISOU  179  CG  PHE A  41     6290   8992   7023     97   -193   1635       C  
ATOM    180  CD1 PHE A  41      51.096  27.105 130.520  1.00 61.23           C  
ANISOU  180  CD1 PHE A  41     6595   9499   7170     51   -230   1692       C  
ATOM    181  CD2 PHE A  41      49.718  26.005 128.923  1.00 56.73           C  
ANISOU  181  CD2 PHE A  41     6028   8663   6865    125   -127   1602       C  
ATOM    182  CE1 PHE A  41      50.118  26.946 131.475  1.00 63.44           C  
ANISOU  182  CE1 PHE A  41     6852   9878   7374     38   -199   1714       C  
ATOM    183  CE2 PHE A  41      48.735  25.841 129.880  1.00 59.55           C  
ANISOU  183  CE2 PHE A  41     6357   9121   7149    115    -99   1626       C  
ATOM    184  CZ  PHE A  41      48.936  26.313 131.154  1.00 61.84           C  
ANISOU  184  CZ  PHE A  41     6636   9590   7271     74   -134   1682       C  
ATOM    185  N   TYR A  42      53.989  24.623 126.933  1.00 59.53           N  
ANISOU  185  N   TYR A  42     6292   8738   7588    154   -144   1894       N  
ATOM    186  CA  TYR A  42      54.482  24.182 125.635  1.00 57.82           C  
ANISOU  186  CA  TYR A  42     6093   8330   7545    178   -104   1869       C  
ATOM    187  C   TYR A  42      53.480  24.515 124.535  1.00 55.35           C  
ANISOU  187  C   TYR A  42     5868   7890   7272    186    -84   1666       C  
ATOM    188  O   TYR A  42      52.263  24.520 124.753  1.00 53.31           O  
ANISOU  188  O   TYR A  42     5621   7658   6976    185    -63   1600       O  
ATOM    189  CB  TYR A  42      54.764  22.683 125.639  1.00 58.00           C  
ANISOU  189  CB  TYR A  42     6022   8266   7749    201    -10   2056       C  
ATOM    190  CG  TYR A  42      55.805  22.266 126.646  1.00 66.46           C  
ANISOU  190  CG  TYR A  42     6992   9458   8801    201    -25   2280       C  
ATOM    191  CD1 TYR A  42      57.158  22.395 126.355  1.00 69.42           C  
ANISOU  191  CD1 TYR A  42     7347   9817   9213    204    -56   2353       C  
ATOM    192  CD2 TYR A  42      55.446  21.738 127.878  1.00 70.23           C  
ANISOU  192  CD2 TYR A  42     7389  10070   9223    195     -9   2427       C  
ATOM    193  CE1 TYR A  42      58.121  22.020 127.260  1.00 75.15           C  
ANISOU  193  CE1 TYR A  42     7968  10665   9919    203    -73   2571       C  
ATOM    194  CE2 TYR A  42      56.408  21.351 128.794  1.00 74.72           C  
ANISOU  194  CE2 TYR A  42     7858  10762   9771    193    -27   2646       C  
ATOM    195  CZ  TYR A  42      57.743  21.496 128.479  1.00 78.64           C  
ANISOU  195  CZ  TYR A  42     8329  11247  10303    197    -60   2720       C  
ATOM    196  OH  TYR A  42      58.714  21.119 129.379  1.00 83.02           O  
ANISOU  196  OH  TYR A  42     8772  11937  10835    194    -82   2950       O  
ATOM    197  N   SER A  43      54.007  24.798 123.337  1.00 53.98           N  
ANISOU  197  N   SER A  43     5753   7583   7174    191    -91   1573       N  
ATOM    198  CA  SER A  43      53.192  25.193 122.194  1.00 48.54           C  
ANISOU  198  CA  SER A  43     5147   6780   6516    194    -82   1384       C  
ATOM    199  C   SER A  43      53.503  24.348 120.967  1.00 46.86           C  
ANISOU  199  C   SER A  43     4939   6372   6495    196    -12   1383       C  
ATOM    200  O   SER A  43      54.666  24.054 120.685  1.00 47.13           O  
ANISOU  200  O   SER A  43     4954   6343   6609    200     -2   1465       O  
ATOM    201  CB  SER A  43      53.428  26.655 121.840  1.00 47.41           C  
ANISOU  201  CB  SER A  43     5098   6670   6246    189   -168   1228       C  
ATOM    202  OG  SER A  43      53.182  27.493 122.954  1.00 53.51           O  
ANISOU  202  OG  SER A  43     5878   7616   6838    179   -222   1216       O  
ATOM    203  N   LYS A  44      52.451  23.972 120.240  1.00 44.21           N  
ANISOU  203  N   LYS A  44     4627   5943   6228    187     41   1290       N  
ATOM    204  CA  LYS A  44      52.548  23.354 118.925  1.00 43.97           C  
ANISOU  204  CA  LYS A  44     4626   5727   6356    171    107   1240       C  
ATOM    205  C   LYS A  44      51.622  24.091 117.972  1.00 39.82           C  
ANISOU  205  C   LYS A  44     4180   5163   5787    156     77   1041       C  
ATOM    206  O   LYS A  44      50.492  24.433 118.331  1.00 38.12           O  
ANISOU  206  O   LYS A  44     3966   5032   5484    158     59    979       O  
ATOM    207  CB  LYS A  44      52.177  21.872 118.931  1.00 46.52           C  
ANISOU  207  CB  LYS A  44     4884   5962   6830    158    227   1346       C  
ATOM    208  CG  LYS A  44      53.215  20.940 119.474  1.00 48.98           C  
ANISOU  208  CG  LYS A  44     5117   6249   7243    176    286   1549       C  
ATOM    209  CD  LYS A  44      52.615  19.550 119.603  1.00 54.83           C  
ANISOU  209  CD  LYS A  44     5801   6916   8116    164    413   1644       C  
ATOM    210  CE  LYS A  44      53.643  18.535 120.071  1.00 60.33           C  
ANISOU  210  CE  LYS A  44     6415   7569   8938    189    491   1860       C  
ATOM    211  NZ  LYS A  44      53.015  17.233 120.437  1.00 66.39           N  
ANISOU  211  NZ  LYS A  44     7122   8288   9816    183    615   1968       N  
ATOM    212  N   TRP A  45      52.103  24.332 116.761  1.00 35.55           N  
ANISOU  212  N   TRP A  45     3701   4498   5307    143     74    949       N  
ATOM    213  CA  TRP A  45      51.377  25.110 115.772  1.00 36.65           C  
ANISOU  213  CA  TRP A  45     3918   4605   5404    130     37    768       C  
ATOM    214  C   TRP A  45      50.703  24.193 114.768  1.00 35.36           C  
ANISOU  214  C   TRP A  45     3756   4312   5366     84    121    723       C  
ATOM    215  O   TRP A  45      51.279  23.180 114.366  1.00 38.77           O  
ANISOU  215  O   TRP A  45     4169   4621   5941     59    204    794       O  
ATOM    216  CB  TRP A  45      52.332  26.065 115.076  1.00 34.41           C  
ANISOU  216  CB  TRP A  45     3708   4278   5089    138    -27    687       C  
ATOM    217  CG  TRP A  45      52.849  27.055 116.032  1.00 34.61           C  
ANISOU  217  CG  TRP A  45     3740   4440   4972    168   -108    708       C  
ATOM    218  CD1 TRP A  45      53.989  26.958 116.792  1.00 38.16           C  
ANISOU  218  CD1 TRP A  45     4149   4939   5411    178   -124    834       C  
ATOM    219  CD2 TRP A  45      52.239  28.297 116.370  1.00 33.69           C  
ANISOU  219  CD2 TRP A  45     3670   4434   4698    188   -179    604       C  
ATOM    220  NE1 TRP A  45      54.124  28.082 117.574  1.00 38.71           N  
ANISOU  220  NE1 TRP A  45     4243   5148   5315    191   -203    804       N  
ATOM    221  CE2 TRP A  45      53.063  28.919 117.337  1.00 35.10           C  
ANISOU  221  CE2 TRP A  45     3844   4724   4770    198   -231    661       C  
ATOM    222  CE3 TRP A  45      51.072  28.944 115.955  1.00 31.76           C  
ANISOU  222  CE3 TRP A  45     3468   4208   4392    195   -197    472       C  
ATOM    223  CZ2 TRP A  45      52.757  30.158 117.891  1.00 37.45           C  
ANISOU  223  CZ2 TRP A  45     4189   5138   4904    211   -291    580       C  
ATOM    224  CZ3 TRP A  45      50.771  30.192 116.500  1.00 34.15           C  
ANISOU  224  CZ3 TRP A  45     3812   4622   4541    221   -256    401       C  
ATOM    225  CH2 TRP A  45      51.612  30.779 117.461  1.00 35.51           C  
ANISOU  225  CH2 TRP A  45     3989   4892   4610    227   -297    450       C  
ATOM    226  N   TYR A  46      49.475  24.547 114.382  1.00 34.60           N  
ANISOU  226  N   TYR A  46     3682   4249   5217     69    104    608       N  
ATOM    227  CA  TYR A  46      48.658  23.714 113.511  1.00 35.07           C  
ANISOU  227  CA  TYR A  46     3737   4216   5370     10    179    559       C  
ATOM    228  C   TYR A  46      47.861  24.578 112.544  1.00 31.59           C  
ANISOU  228  C   TYR A  46     3354   3785   4864     -6    123    397       C  
ATOM    229  O   TYR A  46      47.615  25.759 112.791  1.00 30.28           O  
ANISOU  229  O   TYR A  46     3216   3717   4573     38     38    334       O  
ATOM    230  CB  TYR A  46      47.641  22.855 114.269  1.00 37.45           C  
ANISOU  230  CB  TYR A  46     3966   4576   5687     -3    240    629       C  
ATOM    231  CG  TYR A  46      48.181  21.815 115.220  1.00 39.50           C  
ANISOU  231  CG  TYR A  46     4158   4828   6024      9    313    801       C  
ATOM    232  CD1 TYR A  46      48.447  22.135 116.555  1.00 40.47           C  
ANISOU  232  CD1 TYR A  46     4238   5082   6058     61    269    902       C  
ATOM    233  CD2 TYR A  46      48.362  20.491 114.808  1.00 38.46           C  
ANISOU  233  CD2 TYR A  46     4001   4560   6051    -37    434    865       C  
ATOM    234  CE1 TYR A  46      48.921  21.173 117.441  1.00 41.09           C  
ANISOU  234  CE1 TYR A  46     4246   5165   6204     73    333   1074       C  
ATOM    235  CE2 TYR A  46      48.826  19.523 115.691  1.00 44.27           C  
ANISOU  235  CE2 TYR A  46     4670   5287   6864    -18    510   1036       C  
ATOM    236  CZ  TYR A  46      49.100  19.872 117.004  1.00 46.72           C  
ANISOU  236  CZ  TYR A  46     4932   5738   7082     39    454   1144       C  
ATOM    237  OH  TYR A  46      49.569  18.934 117.889  1.00 52.04           O  
ANISOU  237  OH  TYR A  46     5532   6415   7827     59    523   1325       O  
ATOM    238  N   ILE A  47      47.436  23.959 111.443  1.00 29.86           N  
ANISOU  238  N   ILE A  47     3150   3465   4730    -75    179    334       N  
ATOM    239  CA  ILE A  47      46.329  24.450 110.623  1.00 27.94           C  
ANISOU  239  CA  ILE A  47     2931   3253   4433   -106    145    206       C  
ATOM    240  C   ILE A  47      45.132  23.550 110.870  1.00 31.41           C  
ANISOU  240  C   ILE A  47     3306   3729   4901   -152    211    230       C  
ATOM    241  O   ILE A  47      45.234  22.322 110.730  1.00 31.22           O  
ANISOU  241  O   ILE A  47     3258   3612   4994   -210    313    285       O  
ATOM    242  CB  ILE A  47      46.663  24.453 109.124  1.00 27.66           C  
ANISOU  242  CB  ILE A  47     2960   3093   4456   -169    155    107       C  
ATOM    243  CG1 ILE A  47      47.908  25.283 108.823  1.00 29.99           C  
ANISOU  243  CG1 ILE A  47     3321   3340   4735   -128     98     82       C  
ATOM    244  CG2 ILE A  47      45.445  24.966 108.326  1.00 27.36           C  
ANISOU  244  CG2 ILE A  47     2932   3112   4351   -203    114    -10       C  
ATOM    245  CD1 ILE A  47      47.713  26.728 108.960  1.00 29.57           C  
ANISOU  245  CD1 ILE A  47     3303   3389   4544    -64     -9     12       C  
ATOM    246  N   ARG A  48      43.998  24.152 111.237  1.00 29.18           N  
ANISOU  246  N   ARG A  48     2996   3576   4516   -126    161    192       N  
ATOM    247  CA  ARG A  48      42.728  23.440 111.295  1.00 34.50           C  
ANISOU  247  CA  ARG A  48     3610   4294   5203   -177    212    192       C  
ATOM    248  C   ARG A  48      42.078  23.573 109.924  1.00 32.74           C  
ANISOU  248  C   ARG A  48     3414   4043   4983   -249    201     74       C  
ATOM    249  O   ARG A  48      41.707  24.676 109.511  1.00 28.72           O  
ANISOU  249  O   ARG A  48     2930   3599   4384   -216    118     -6       O  
ATOM    250  CB  ARG A  48      41.828  23.990 112.401  1.00 33.26           C  
ANISOU  250  CB  ARG A  48     3404   4294   4939   -113    170    218       C  
ATOM    251  CG  ARG A  48      40.425  23.358 112.391  1.00 40.38           C  
ANISOU  251  CG  ARG A  48     4242   5252   5847   -166    216    208       C  
ATOM    252  CD  ARG A  48      40.484  21.920 112.940  1.00 42.42           C  
ANISOU  252  CD  ARG A  48     4453   5457   6208   -212    324    309       C  
ATOM    253  NE  ARG A  48      40.554  21.901 114.404  1.00 43.90           N  
ANISOU  253  NE  ARG A  48     4598   5729   6355   -144    325    416       N  
ATOM    254  CZ  ARG A  48      40.587  20.795 115.142  1.00 43.96           C  
ANISOU  254  CZ  ARG A  48     4556   5715   6432   -161    411    524       C  
ATOM    255  NH1 ARG A  48      40.554  19.598 114.557  1.00 46.38           N  
ANISOU  255  NH1 ARG A  48     4853   5909   6860   -243    513    537       N  
ATOM    256  NH2 ARG A  48      40.648  20.882 116.467  1.00 45.96           N  
ANISOU  256  NH2 ARG A  48     4772   6059   6633   -101    401    619       N  
ATOM    257  N   VAL A  49      41.958  22.454 109.211  1.00 32.63           N  
ANISOU  257  N   VAL A  49     3395   3931   5070   -351    291     64       N  
ATOM    258  CA  VAL A  49      41.526  22.507 107.821  1.00 33.88           C  
ANISOU  258  CA  VAL A  49     3587   4053   5234   -440    285    -47       C  
ATOM    259  C   VAL A  49      40.162  23.179 107.730  1.00 35.41           C  
ANISOU  259  C   VAL A  49     3738   4394   5321   -434    218   -103       C  
ATOM    260  O   VAL A  49      39.216  22.817 108.446  1.00 32.66           O  
ANISOU  260  O   VAL A  49     3320   4136   4953   -432    242    -62       O  
ATOM    261  CB  VAL A  49      41.513  21.093 107.217  1.00 36.21           C  
ANISOU  261  CB  VAL A  49     3881   4228   5651   -565    412    -45       C  
ATOM    262  CG1 VAL A  49      41.005  21.145 105.786  1.00 38.50           C  
ANISOU  262  CG1 VAL A  49     4202   4497   5930   -675    405   -164       C  
ATOM    263  CG2 VAL A  49      42.906  20.452 107.288  1.00 37.77           C  
ANISOU  263  CG2 VAL A  49     4116   4270   5965   -560    488     21       C  
ATOM    264  N   GLY A  50      40.068  24.192 106.869  1.00 34.39           N  
ANISOU  264  N   GLY A  50     3648   4293   5126   -423    136   -190       N  
ATOM    265  CA  GLY A  50      38.816  24.890 106.655  1.00 33.35           C  
ANISOU  265  CA  GLY A  50     3472   4298   4899   -413     72   -236       C  
ATOM    266  C   GLY A  50      38.237  25.576 107.879  1.00 34.04           C  
ANISOU  266  C   GLY A  50     3512   4517   4906   -301     31   -186       C  
ATOM    267  O   GLY A  50      37.072  25.978 107.863  1.00 36.47           O  
ANISOU  267  O   GLY A  50     3766   4943   5149   -291     -1   -204       O  
ATOM    268  N   ALA A  51      39.011  25.675 108.961  1.00 30.67           N  
ANISOU  268  N   ALA A  51     3099   4075   4480   -224     37   -118       N  
ATOM    269  CA  ALA A  51      38.531  26.206 110.236  1.00 32.20           C  
ANISOU  269  CA  ALA A  51     3252   4386   4598   -132     14    -66       C  
ATOM    270  C   ALA A  51      37.321  25.437 110.764  1.00 36.75           C  
ANISOU  270  C   ALA A  51     3741   5042   5181   -167     65    -26       C  
ATOM    271  O   ALA A  51      36.517  25.967 111.545  1.00 41.59           O  
ANISOU  271  O   ALA A  51     4310   5772   5721   -104     42     -7       O  
ATOM    272  CB  ALA A  51      38.223  27.701 110.117  1.00 33.46           C  
ANISOU  272  CB  ALA A  51     3436   4626   4652    -47    -71   -123       C  
ATOM    273  N   ARG A  52      37.168  24.197 110.316  1.00 38.90           N  
ANISOU  273  N   ARG A  52     3990   5249   5542   -272    140    -16       N  
ATOM    274  CA  ARG A  52      36.092  23.316 110.737  1.00 42.26           C  
ANISOU  274  CA  ARG A  52     4337   5734   5987   -324    202     19       C  
ATOM    275  C   ARG A  52      36.552  22.517 111.955  1.00 40.98           C  
ANISOU  275  C   ARG A  52     4153   5543   5873   -300    270    126       C  
ATOM    276  O   ARG A  52      37.556  21.800 111.894  1.00 39.61           O  
ANISOU  276  O   ARG A  52     4013   5249   5787   -328    326    166       O  
ATOM    277  CB  ARG A  52      35.721  22.413 109.568  1.00 44.21           C  
ANISOU  277  CB  ARG A  52     4578   5921   6300   -462    256    -34       C  
ATOM    278  CG  ARG A  52      34.483  21.566 109.708  1.00 51.42           C  
ANISOU  278  CG  ARG A  52     5411   6902   7224   -540    315    -22       C  
ATOM    279  CD  ARG A  52      34.067  21.008 108.336  1.00 54.09           C  
ANISOU  279  CD  ARG A  52     5753   7204   7593   -687    345   -102       C  
ATOM    280  NE  ARG A  52      35.187  20.904 107.384  1.00 58.92           N  
ANISOU  280  NE  ARG A  52     6452   7674   8263   -735    358   -148       N  
ATOM    281  CZ  ARG A  52      35.474  21.811 106.442  1.00 61.99           C  
ANISOU  281  CZ  ARG A  52     6888   8061   8606   -727    278   -220       C  
ATOM    282  NH1 ARG A  52      34.720  22.903 106.329  1.00 60.33           N  
ANISOU  282  NH1 ARG A  52     6645   7984   8293   -667    180   -248       N  
ATOM    283  NH2 ARG A  52      36.518  21.638 105.630  1.00 52.19           N  
ANISOU  283  NH2 ARG A  52     5725   6681   7422   -774    300   -259       N  
ATOM    284  N   LYS A  53      35.831  22.654 113.061  1.00 40.43           N  
ANISOU  284  N   LYS A  53     4027   5585   5748   -245    268    177       N  
ATOM    285  CA  LYS A  53      36.238  22.008 114.304  1.00 43.63           C  
ANISOU  285  CA  LYS A  53     4411   5984   6184   -214    322    285       C  
ATOM    286  C   LYS A  53      36.328  20.493 114.152  1.00 45.46           C  
ANISOU  286  C   LYS A  53     4621   6117   6536   -308    435    334       C  
ATOM    287  O   LYS A  53      37.135  19.849 114.827  1.00 50.23           O  
ANISOU  287  O   LYS A  53     5226   6659   7199   -292    489    428       O  
ATOM    288  CB  LYS A  53      35.247  22.387 115.403  1.00 50.68           C  
ANISOU  288  CB  LYS A  53     5244   7020   6991   -156    307    318       C  
ATOM    289  CG  LYS A  53      35.229  23.869 115.684  1.00 49.18           C  
ANISOU  289  CG  LYS A  53     5083   6916   6689    -60    216    278       C  
ATOM    290  CD  LYS A  53      34.050  24.287 116.529  1.00 50.69           C  
ANISOU  290  CD  LYS A  53     5215   7244   6801    -14    211    290       C  
ATOM    291  CE  LYS A  53      34.261  24.224 118.022  1.00 57.72           C  
ANISOU  291  CE  LYS A  53     6090   8188   7652     38    232    378       C  
ATOM    292  NZ  LYS A  53      33.060  24.919 118.621  1.00 61.98           N  
ANISOU  292  NZ  LYS A  53     6586   8859   8104     88    219    360       N  
ATOM    293  N   SER A  54      35.561  19.913 113.240  1.00 47.14           N  
ANISOU  293  N   SER A  54     4814   6310   6786   -409    476    273       N  
ATOM    294  CA  SER A  54      35.616  18.476 113.009  1.00 52.51           C  
ANISOU  294  CA  SER A  54     5483   6884   7582   -510    599    305       C  
ATOM    295  C   SER A  54      36.670  18.070 111.985  1.00 52.24           C  
ANISOU  295  C   SER A  54     5519   6689   7641   -571    642    273       C  
ATOM    296  O   SER A  54      36.810  16.875 111.700  1.00 57.05           O  
ANISOU  296  O   SER A  54     6131   7188   8357   -660    760    294       O  
ATOM    297  CB  SER A  54      34.244  17.974 112.559  1.00 57.97           C  
ANISOU  297  CB  SER A  54     6121   7639   8267   -609    636    251       C  
ATOM    298  OG  SER A  54      33.793  18.697 111.430  1.00 59.47           O  
ANISOU  298  OG  SER A  54     6325   7871   8400   -648    563    144       O  
ATOM    299  N   ALA A  55      37.422  19.013 111.446  1.00 47.36           N  
ANISOU  299  N   ALA A  55     4960   6047   6988   -526    559    224       N  
ATOM    300  CA  ALA A  55      38.336  18.726 110.354  1.00 47.60           C  
ANISOU  300  CA  ALA A  55     5058   5930   7098   -589    594    179       C  
ATOM    301  C   ALA A  55      39.734  18.441 110.894  1.00 46.46           C  
ANISOU  301  C   ALA A  55     4944   5680   7029   -530    632    274       C  
ATOM    302  O   ALA A  55      40.006  18.623 112.089  1.00 44.58           O  
ANISOU  302  O   ALA A  55     4675   5500   6761   -439    611    370       O  
ATOM    303  CB  ALA A  55      38.310  19.892 109.371  1.00 43.80           C  
ANISOU  303  CB  ALA A  55     4622   5483   6537   -582    486     70       C  
ATOM    304  N   PRO A  56      40.649  17.965 110.035  1.00 48.09           N  
ANISOU  304  N   PRO A  56     5208   5731   7334   -586    693    255       N  
ATOM    305  CA  PRO A  56      41.989  17.599 110.512  1.00 48.32           C  
ANISOU  305  CA  PRO A  56     5254   5656   7449   -533    740    359       C  
ATOM    306  C   PRO A  56      42.778  18.781 111.036  1.00 42.50           C  
ANISOU  306  C   PRO A  56     4536   4982   6629   -417    622    383       C  
ATOM    307  O   PRO A  56      42.645  19.911 110.563  1.00 39.21           O  
ANISOU  307  O   PRO A  56     4154   4626   6117   -392    515    290       O  
ATOM    308  CB  PRO A  56      42.666  17.020 109.264  1.00 51.44           C  
ANISOU  308  CB  PRO A  56     5714   5876   7956   -624    823    304       C  
ATOM    309  CG  PRO A  56      41.558  16.534 108.436  1.00 55.48           C  
ANISOU  309  CG  PRO A  56     6223   6390   8467   -750    871    207       C  
ATOM    310  CD  PRO A  56      40.424  17.485 108.658  1.00 51.87           C  
ANISOU  310  CD  PRO A  56     5727   6117   7865   -717    750    152       C  
ATOM    311  N   LEU A  57      43.619  18.496 112.019  1.00 43.03           N  
ANISOU  311  N   LEU A  57     4579   5036   6734   -350    646    513       N  
ATOM    312  CA  LEU A  57      44.648  19.420 112.479  1.00 42.70           C  
ANISOU  312  CA  LEU A  57     4560   5029   6636   -259    557    550       C  
ATOM    313  C   LEU A  57      45.965  19.060 111.810  1.00 40.99           C  
ANISOU  313  C   LEU A  57     4388   4654   6531   -274    607    573       C  
ATOM    314  O   LEU A  57      46.510  17.983 112.053  1.00 45.97           O  
ANISOU  314  O   LEU A  57     4993   5188   7286   -287    718    680       O  
ATOM    315  CB  LEU A  57      44.792  19.361 114.000  1.00 46.22           C  
ANISOU  315  CB  LEU A  57     4944   5577   7041   -183    546    687       C  
ATOM    316  CG  LEU A  57      44.010  20.401 114.804  1.00 45.47           C  
ANISOU  316  CG  LEU A  57     4829   5658   6787   -126    443    657       C  
ATOM    317  CD1 LEU A  57      44.437  20.364 116.264  1.00 48.00           C  
ANISOU  317  CD1 LEU A  57     5101   6068   7067    -61    433    796       C  
ATOM    318  CD2 LEU A  57      44.205  21.800 114.244  1.00 38.63           C  
ANISOU  318  CD2 LEU A  57     4026   4829   5820    -93    330    542       C  
ATOM    319  N   ILE A  58      46.486  19.952 110.983  1.00 38.61           N  
ANISOU  319  N   ILE A  58     4153   4325   6194   -269    533    478       N  
ATOM    320  CA  ILE A  58      47.745  19.692 110.296  1.00 39.69           C  
ANISOU  320  CA  ILE A  58     4336   4312   6434   -283    578    491       C  
ATOM    321  C   ILE A  58      48.857  20.361 111.086  1.00 37.45           C  
ANISOU  321  C   ILE A  58     4045   4076   6106   -190    506    576       C  
ATOM    322  O   ILE A  58      48.878  21.589 111.222  1.00 36.93           O  
ANISOU  322  O   ILE A  58     4008   4109   5915   -142    388    515       O  
ATOM    323  CB  ILE A  58      47.719  20.189 108.843  1.00 39.57           C  
ANISOU  323  CB  ILE A  58     4399   4225   6412   -344    549    338       C  
ATOM    324  CG1 ILE A  58      46.485  19.635 108.125  1.00 41.16           C  
ANISOU  324  CG1 ILE A  58     4597   4417   6624   -447    603    250       C  
ATOM    325  CG2 ILE A  58      49.014  19.781 108.130  1.00 44.51           C  
ANISOU  325  CG2 ILE A  58     5072   4680   7160   -367    616    354       C  
ATOM    326  CD1 ILE A  58      46.272  18.150 108.312  1.00 47.16           C  
ANISOU  326  CD1 ILE A  58     5319   5089   7512   -511    756    326       C  
ATOM    327  N   GLU A  59      49.784  19.569 111.609  1.00 41.78           N  
ANISOU  327  N   GLU A  59     4557   4559   6759   -167    582    719       N  
ATOM    328  CA  GLU A  59      50.848  20.140 112.422  1.00 44.73           C  
ANISOU  328  CA  GLU A  59     4913   4996   7088    -88    514    814       C  
ATOM    329  C   GLU A  59      51.921  20.775 111.547  1.00 40.02           C  
ANISOU  329  C   GLU A  59     4384   4315   6507    -85    473    751       C  
ATOM    330  O   GLU A  59      52.400  20.177 110.579  1.00 44.09           O  
ANISOU  330  O   GLU A  59     4934   4671   7148   -132    557    729       O  
ATOM    331  CB  GLU A  59      51.465  19.095 113.353  1.00 46.30           C  
ANISOU  331  CB  GLU A  59     5033   5174   7385    -59    602   1009       C  
ATOM    332  CG  GLU A  59      52.422  19.711 114.375  1.00 47.67           C  
ANISOU  332  CG  GLU A  59     5170   5458   7483     15    519   1121       C  
ATOM    333  CD  GLU A  59      52.772  18.774 115.516  1.00 57.26           C  
ANISOU  333  CD  GLU A  59     6291   6706   8760     49    587   1327       C  
ATOM    334  OE1 GLU A  59      52.354  17.596 115.469  1.00 65.14           O  
ANISOU  334  OE1 GLU A  59     7256   7617   9878     20    712   1386       O  
ATOM    335  OE2 GLU A  59      53.470  19.215 116.457  1.00 58.75           O  
ANISOU  335  OE2 GLU A  59     6439   7009   8875    100    518   1431       O  
ATOM    336  N   LEU A  60      52.299  21.985 111.914  1.00 37.75           N  
ANISOU  336  N   LEU A  60     4118   4135   6092    -33    352    722       N  
ATOM    337  CA  LEU A  60      53.346  22.740 111.267  1.00 39.06           C  
ANISOU  337  CA  LEU A  60     4344   4247   6250    -21    298    668       C  
ATOM    338  C   LEU A  60      54.642  22.466 112.008  1.00 48.06           C  
ANISOU  338  C   LEU A  60     5434   5388   7437     24    311    827       C  
ATOM    339  O   LEU A  60      54.637  22.076 113.176  1.00 55.71           O  
ANISOU  339  O   LEU A  60     6326   6450   8390     56    321    964       O  
ATOM    340  CB  LEU A  60      53.026  24.231 111.296  1.00 36.82           C  
ANISOU  340  CB  LEU A  60     4112   4082   5797      9    166    549       C  
ATOM    341  CG  LEU A  60      51.697  24.595 110.641  1.00 35.05           C  
ANISOU  341  CG  LEU A  60     3922   3880   5514    -24    144    408       C  
ATOM    342  CD1 LEU A  60      51.428  26.085 110.844  1.00 31.06           C  
ANISOU  342  CD1 LEU A  60     3460   3496   4846     22     26    316       C  
ATOM    343  CD2 LEU A  60      51.733  24.239 109.158  1.00 32.05           C  
ANISOU  343  CD2 LEU A  60     3600   3347   5230    -92    196    311       C  
ATOM    344  N   CYS A  61      55.747  22.653 111.312  1.00 44.66           N  
ANISOU  344  N   CYS A  61     5045   4858   7068     23    312    814       N  
ATOM    345  CA  CYS A  61      57.068  22.470 111.906  1.00 49.24           C  
ANISOU  345  CA  CYS A  61     5574   5441   7693     64    318    965       C  
ATOM    346  C   CYS A  61      57.245  21.038 112.380  1.00 56.16           C  
ANISOU  346  C   CYS A  61     6365   6253   8718     68    447   1140       C  
ATOM    347  O   CYS A  61      57.823  20.771 113.440  1.00 63.56           O  
ANISOU  347  O   CYS A  61     7222   7274   9656    112    444   1309       O  
ATOM    348  CB  CYS A  61      57.296  23.474 113.028  1.00 49.46           C  
ANISOU  348  CB  CYS A  61     5578   5660   7554    110    197   1002       C  
ATOM    349  SG  CYS A  61      57.527  25.082 112.290  1.00 49.03           S  
ANISOU  349  SG  CYS A  61     5632   5629   7369    109     76    814       S  
ATOM    350  N   VAL A  62      56.691  20.136 111.577  1.00 57.32           N  
ANISOU  350  N   VAL A  62     6534   6258   8988     15    562   1096       N  
ATOM    351  CA  VAL A  62      56.911  18.706 111.616  1.00 66.36           C  
ANISOU  351  CA  VAL A  62     7626   7276  10312      4    720   1229       C  
ATOM    352  C   VAL A  62      57.034  18.334 110.155  1.00 77.99           C  
ANISOU  352  C   VAL A  62     9179   8551  11904    -63    811   1114       C  
ATOM    353  O   VAL A  62      56.094  18.535 109.384  1.00 82.16           O  
ANISOU  353  O   VAL A  62     9770   9058  12391   -126    802    954       O  
ATOM    354  CB  VAL A  62      55.753  17.954 112.291  1.00 62.17           C  
ANISOU  354  CB  VAL A  62     7044   6799   9780    -10    777   1276       C  
ATOM    355  CG1 VAL A  62      55.929  16.450 112.132  1.00 76.29           C  
ANISOU  355  CG1 VAL A  62     8795   8425  11768    -33    963   1391       C  
ATOM    356  CG2 VAL A  62      55.652  18.327 113.752  1.00 65.51           C  
ANISOU  356  CG2 VAL A  62     7391   7420  10079     51    690   1390       C  
ATOM    357  N   ASP A  63      58.186  17.834 109.760  1.00 80.85           N  
ANISOU  357  N   ASP A  63     9537   8774  12408    -54    896   1194       N  
ATOM    358  CA  ASP A  63      58.437  17.577 108.346  1.00 88.06           C  
ANISOU  358  CA  ASP A  63    10534   9495  13428   -122    981   1078       C  
ATOM    359  C   ASP A  63      59.213  16.278 108.170  1.00 96.23           C  
ANISOU  359  C   ASP A  63    11536  10366  14663   -120   1160   1205       C  
ATOM    360  O   ASP A  63      60.235  16.218 107.485  1.00 99.99           O  
ANISOU  360  O   ASP A  63    12041  10803  15149   -101   1172   1158       O  
ATOM    361  CB  ASP A  63      59.153  18.769 107.711  1.00 87.05           C  
ANISOU  361  CB  ASP A  63    10475   9378  13223   -112    865    971       C  
ATOM    362  N   GLU A  64      58.704  15.215 108.787  1.00 97.08           N  
ANISOU  362  N   GLU A  64    11581  10482  14822   -113   1258   1300       N  
ATOM    363  CA  GLU A  64      59.336  13.901 108.722  1.00101.24           C  
ANISOU  363  CA  GLU A  64    12072  10962  15434    -73   1387   1356       C  
ATOM    364  C   GLU A  64      58.800  13.137 107.515  1.00109.27           C  
ANISOU  364  C   GLU A  64    13172  11888  16457   -148   1482   1177       C  
ATOM    365  O   GLU A  64      59.308  12.071 107.169  1.00113.01           O  
ANISOU  365  O   GLU A  64    13639  12302  16997   -127   1595   1184       O  
ATOM    366  CB  GLU A  64      59.080  13.119 110.004  1.00101.38           C  
ANISOU  366  CB  GLU A  64    11983  11036  15500    -20   1444   1549       C  
ATOM    367  CG  GLU A  64      58.704  13.986 111.193  1.00104.84           C  
ANISOU  367  CG  GLU A  64    12360  11599  15876      0   1336   1687       C  
ATOM    368  CD  GLU A  64      59.899  14.659 111.820  1.00102.69           C  
ANISOU  368  CD  GLU A  64    12031  11405  15581     75   1245   1830       C  
ATOM    369  OE1 GLU A  64      60.705  13.944 112.453  1.00 97.55           O  
ANISOU  369  OE1 GLU A  64    11292  10788  14986    148   1293   1984       O  
ATOM    370  OE2 GLU A  64      60.038  15.893 111.671  1.00100.19           O  
ANISOU  370  OE2 GLU A  64    11759  11190  15118     79   1088   1717       O  
ATOM    371  N   SER A  67      56.043  11.522 105.642  1.00104.96           N  
ANISOU  371  N   SER A  67    13970  15152  10756   -188    410    695       N  
ATOM    372  CA  SER A  67      56.403  10.382 104.805  1.00102.26           C  
ANISOU  372  CA  SER A  67    13559  14790  10505    -50    353    787       C  
ATOM    373  C   SER A  67      55.173   9.796 104.112  1.00 97.86           C  
ANISOU  373  C   SER A  67    13005  14156  10022     28    449    694       C  
ATOM    374  O   SER A  67      54.174  10.496 103.907  1.00 92.75           O  
ANISOU  374  O   SER A  67    12355  13491   9394      7    538    575       O  
ATOM    375  CB  SER A  67      57.106   9.304 105.635  1.00104.62           C  
ANISOU  375  CB  SER A  67    13930  15091  10731    -71    293    898       C  
ATOM    376  N   LYS A  68      55.264   8.510 103.767  1.00 97.40           N  
ANISOU  376  N   LYS A  68    12934  14065  10007    118    428    754       N  
ATOM    377  CA  LYS A  68      54.230   7.844 102.984  1.00 90.67           C  
ANISOU  377  CA  LYS A  68    12065  13150   9236    213    488    692       C  
ATOM    378  C   LYS A  68      52.869   7.984 103.648  1.00 85.57           C  
ANISOU  378  C   LYS A  68    11524  12444   8544    122    632    549       C  
ATOM    379  O   LYS A  68      52.728   7.771 104.856  1.00 90.24           O  
ANISOU  379  O   LYS A  68    12255  13002   9029      7    702    519       O  
ATOM    380  CB  LYS A  68      54.576   6.366 102.807  1.00 93.87           C  
ANISOU  380  CB  LYS A  68    12458  13538   9670    303    453    777       C  
ATOM    381  N   SER A  69      51.865   8.333 102.839  1.00 76.97           N  
ANISOU  381  N   SER A  69    10373  11337   7536    191    690    464       N  
ATOM    382  CA  SER A  69      50.504   8.634 103.271  1.00 71.17           C  
ANISOU  382  CA  SER A  69     9677  10562   6800    132    866    303       C  
ATOM    383  C   SER A  69      49.679   9.055 102.060  1.00 62.65           C  
ANISOU  383  C   SER A  69     8487   9490   5829    273    871    256       C  
ATOM    384  O   SER A  69      50.181   9.784 101.197  1.00 62.51           O  
ANISOU  384  O   SER A  69     8394   9525   5833    336    758    319       O  
ATOM    385  CB  SER A  69      50.500   9.737 104.333  1.00 73.35           C  
ANISOU  385  CB  SER A  69    10012  10860   6998    -22    971    210       C  
ATOM    386  OG  SER A  69      49.189  10.006 104.796  1.00 69.89           O  
ANISOU  386  OG  SER A  69     9572  10376   6607    -76   1190     21       O  
ATOM    387  N   PRO A  70      48.412   8.645 101.958  1.00 58.05           N  
ANISOU  387  N   PRO A  70     7902   8841   5313    339   1004    150       N  
ATOM    388  CA  PRO A  70      47.659   8.974 100.737  1.00 58.46           C  
ANISOU  388  CA  PRO A  70     7870   8759   5584    469    933    114       C  
ATOM    389  C   PRO A  70      47.379  10.462 100.602  1.00 58.54           C  
ANISOU  389  C   PRO A  70     7768   8662   5813    365    903     -7       C  
ATOM    390  O   PRO A  70      47.377  10.981  99.477  1.00 57.02           O  
ANISOU  390  O   PRO A  70     7514   8394   5756    433    736     40       O  
ATOM    391  CB  PRO A  70      46.364   8.161 100.887  1.00 60.28           C  
ANISOU  391  CB  PRO A  70     8112   8778   6012    490   1036     -1       C  
ATOM    392  CG  PRO A  70      46.621   7.183 101.995  1.00 55.34           C  
ANISOU  392  CG  PRO A  70     7604   8283   5140    441   1175     29       C  
ATOM    393  CD  PRO A  70      47.626   7.823 102.889  1.00 58.86           C  
ANISOU  393  CD  PRO A  70     8082   8864   5417    263   1169     51       C  
ATOM    394  N   ILE A  71      47.125  11.162 101.710  1.00 58.91           N  
ANISOU  394  N   ILE A  71     7800   8686   5899    188   1060   -164       N  
ATOM    395  CA  ILE A  71      46.930  12.611 101.705  1.00 57.27           C  
ANISOU  395  CA  ILE A  71     7483   8377   5901     79   1049   -289       C  
ATOM    396  C   ILE A  71      48.144  13.233 102.375  1.00 56.32           C  
ANISOU  396  C   ILE A  71     7417   8497   5486    -33   1044   -222       C  
ATOM    397  O   ILE A  71      48.445  12.927 103.536  1.00 57.97           O  
ANISOU  397  O   ILE A  71     7740   8821   5465   -156   1182   -243       O  
ATOM    398  CB  ILE A  71      45.645  13.014 102.446  1.00 58.92           C  
ANISOU  398  CB  ILE A  71     7624   8332   6430    -52   1264   -550       C  
ATOM    399  CG1 ILE A  71      44.411  12.452 101.732  1.00 59.30           C  
ANISOU  399  CG1 ILE A  71     7587   8112   6832     56   1238   -603       C  
ATOM    400  CG2 ILE A  71      45.553  14.537 102.557  1.00 52.25           C  
ANISOU  400  CG2 ILE A  71     6665   7386   5800   -175   1270   -685       C  
ATOM    401  CD1 ILE A  71      43.109  12.749 102.441  1.00 65.15           C  
ANISOU  401  CD1 ILE A  71     8231   8577   7948    -60   1475   -859       C  
ATOM    402  N   GLN A  72      48.836  14.112 101.664  1.00 51.36           N  
ANISOU  402  N   GLN A  72     6720   7936   4858     -9    874   -133       N  
ATOM    403  CA  GLN A  72      49.977  14.800 102.243  1.00 53.65           C  
ANISOU  403  CA  GLN A  72     7042   8436   4906   -119    846    -62       C  
ATOM    404  C   GLN A  72      49.875  16.305 101.984  1.00 50.88           C  
ANISOU  404  C   GLN A  72     6579   7988   4764   -206    784   -159       C  
ATOM    405  O   GLN A  72      49.293  16.737 100.982  1.00 47.66           O  
ANISOU  405  O   GLN A  72     6065   7405   4638   -134    672   -186       O  
ATOM    406  CB  GLN A  72      51.261  14.157 101.740  1.00 55.42           C  
ANISOU  406  CB  GLN A  72     7304   8900   4852      4    704    198       C  
ATOM    407  CG  GLN A  72      52.519  14.684 102.354  1.00 65.64           C  
ANISOU  407  CG  GLN A  72     8631  10255   6054    -94    617    289       C  
ATOM    408  CD  GLN A  72      53.641  13.687 102.220  1.00 73.78           C  
ANISOU  408  CD  GLN A  72     9704  11241   7090      0    499    460       C  
ATOM    409  OE1 GLN A  72      53.653  12.864 101.302  1.00 69.48           O  
ANISOU  409  OE1 GLN A  72     9135  10647   6615    138    451    526       O  
ATOM    410  NE2 GLN A  72      54.565  13.714 103.176  1.00 79.16           N  
ANISOU  410  NE2 GLN A  72    10442  11941   7695    -88    464    516       N  
ATOM    411  N   TYR A  73      50.357  17.102 102.943  1.00 50.48           N  
ANISOU  411  N   TYR A  73     6566   8024   4590   -382    852   -220       N  
ATOM    412  CA  TYR A  73      50.231  18.562 102.924  1.00 49.80           C  
ANISOU  412  CA  TYR A  73     6384   7835   4702   -493    825   -341       C  
ATOM    413  C   TYR A  73      51.582  19.214 102.619  1.00 50.45           C  
ANISOU  413  C   TYR A  73     6456   8137   4574   -502    638   -155       C  
ATOM    414  O   TYR A  73      52.578  18.940 103.297  1.00 54.89           O  
ANISOU  414  O   TYR A  73     7119   8920   4818   -565    633    -33       O  
ATOM    415  CB  TYR A  73      49.661  19.064 104.253  1.00 54.69           C  
ANISOU  415  CB  TYR A  73     7064   8348   5367   -708   1073   -586       C  
ATOM    416  CG  TYR A  73      48.269  18.524 104.482  1.00 54.45           C  
ANISOU  416  CG  TYR A  73     7009   8069   5609   -702   1279   -785       C  
ATOM    417  CD1 TYR A  73      48.076  17.274 105.075  1.00 56.99           C  
ANISOU  417  CD1 TYR A  73     7464   8446   5742   -698   1417   -771       C  
ATOM    418  CD2 TYR A  73      47.152  19.228 104.060  1.00 54.63           C  
ANISOU  418  CD2 TYR A  73     6861   7789   6108   -696   1320   -969       C  
ATOM    419  CE1 TYR A  73      46.809  16.751 105.259  1.00 57.11           C  
ANISOU  419  CE1 TYR A  73     7449   8232   6017   -691   1609   -944       C  
ATOM    420  CE2 TYR A  73      45.870  18.713 104.247  1.00 56.17           C  
ANISOU  420  CE2 TYR A  73     7004   7736   6601   -686   1509  -1142       C  
ATOM    421  CZ  TYR A  73      45.712  17.475 104.848  1.00 54.85           C  
ANISOU  421  CZ  TYR A  73     6979   7643   6219   -684   1662  -1131       C  
ATOM    422  OH  TYR A  73      44.454  16.971 105.032  1.00 55.62           O  
ANISOU  422  OH  TYR A  73     7020   7495   6620   -679   1855  -1298       O  
ATOM    423  N   ILE A  74      51.608  20.054 101.584  1.00 46.52           N  
ANISOU  423  N   ILE A  74     5838   7568   4272   -449    470   -119       N  
ATOM    424  CA  ILE A  74      52.798  20.774 101.134  1.00 46.82           C  
ANISOU  424  CA  ILE A  74     5844   7782   4163   -457    292     50       C  
ATOM    425  C   ILE A  74      52.620  22.280 101.315  1.00 47.66           C  
ANISOU  425  C   ILE A  74     5868   7776   4466   -600    261    -84       C  
ATOM    426  O   ILE A  74      51.511  22.811 101.420  1.00 47.00           O  
ANISOU  426  O   ILE A  74     5712   7435   4710   -654    340   -294       O  
ATOM    427  CB  ILE A  74      53.131  20.465  99.664  1.00 42.20           C  
ANISOU  427  CB  ILE A  74     5216   7226   3591   -288    110    234       C  
ATOM    428  CG1 ILE A  74      51.986  20.972  98.781  1.00 41.58           C  
ANISOU  428  CG1 ILE A  74     5051   6864   3885   -262     26    124       C  
ATOM    429  CG2 ILE A  74      53.387  18.975  99.493  1.00 45.39           C  
ANISOU  429  CG2 ILE A  74     5703   7740   3802   -145    155    362       C  
ATOM    430  CD1 ILE A  74      52.260  20.947  97.289  1.00 37.61           C  
ANISOU  430  CD1 ILE A  74     4543   6353   3394   -158   -180    289       C  
ATOM    431  N   ASP A  75      53.750  22.969 101.417  1.00 37.14           N  
ANISOU  431  N   ASP A  75     4536   6626   2948   -669    154     38       N  
ATOM    432  CA  ASP A  75      53.787  24.414 101.605  1.00 36.59           C  
ANISOU  432  CA  ASP A  75     4400   6482   3022   -809    104    -62       C  
ATOM    433  C   ASP A  75      54.432  25.078 100.383  1.00 34.86           C  
ANISOU  433  C   ASP A  75     4086   6315   2846   -744   -137    111       C  
ATOM    434  O   ASP A  75      55.631  25.391 100.387  1.00 35.94           O  
ANISOU  434  O   ASP A  75     4232   6665   2760   -774   -237    278       O  
ATOM    435  CB  ASP A  75      54.491  24.709 102.890  1.00 35.69           C  
ANISOU  435  CB  ASP A  75     4394   6517   2650   -986    188    -83       C  
ATOM    436  CG  ASP A  75      54.469  26.153 103.221  1.00 39.83           C  
ANISOU  436  CG  ASP A  75     4873   6949   3312  -1147    170   -214       C  
ATOM    437  OD1 ASP A  75      53.679  26.882 102.555  1.00 35.69           O  
ANISOU  437  OD1 ASP A  75     4216   6200   3146  -1120    126   -329       O  
ATOM    438  OD2 ASP A  75      55.191  26.528 104.179  1.00 36.73           O  
ANISOU  438  OD2 ASP A  75     4585   6688   2684  -1311    194   -204       O  
ATOM    439  N   ILE A  76      53.615  25.352  99.358  1.00 32.58           N  
ANISOU  439  N   ILE A  76     3708   5811   2859   -676   -239     70       N  
ATOM    440  CA  ILE A  76      54.145  25.855  98.095  1.00 32.06           C  
ANISOU  440  CA  ILE A  76     3592   5778   2811   -627   -471    243       C  
ATOM    441  C   ILE A  76      54.662  27.272  98.244  1.00 35.38           C  
ANISOU  441  C   ILE A  76     3944   6216   3282   -762   -576    236       C  
ATOM    442  O   ILE A  76      55.712  27.620  97.687  1.00 35.23           O  
ANISOU  442  O   ILE A  76     3922   6371   3095   -761   -716    423       O  
ATOM    443  CB  ILE A  76      53.068  25.779  97.006  1.00 32.22           C  
ANISOU  443  CB  ILE A  76     3566   5535   3141   -556   -586    209       C  
ATOM    444  CG1 ILE A  76      52.832  24.334  96.571  1.00 31.52           C  
ANISOU  444  CG1 ILE A  76     3567   5471   2936   -409   -532    282       C  
ATOM    445  CG2 ILE A  76      53.507  26.607  95.792  1.00 34.16           C  
ANISOU  445  CG2 ILE A  76     3780   5768   3432   -574   -841    356       C  
ATOM    446  CD1 ILE A  76      51.579  24.172  95.645  1.00 32.26           C  
ANISOU  446  CD1 ILE A  76     3633   5263   3364   -361   -648    229       C  
ATOM    447  N   GLY A  77      53.967  28.098  99.025  1.00 38.96           N  
ANISOU  447  N   GLY A  77     4524   6456   3822   -360    674    295       N  
ATOM    448  CA  GLY A  77      54.267  29.504  99.179  1.00 40.65           C  
ANISOU  448  CA  GLY A  77     4748   6644   4053   -373    629    404       C  
ATOM    449  C   GLY A  77      55.211  29.821 100.318  1.00 45.80           C  
ANISOU  449  C   GLY A  77     5306   7231   4864   -352    643    428       C  
ATOM    450  O   GLY A  77      55.401  30.999 100.644  1.00 45.94           O  
ANISOU  450  O   GLY A  77     5325   7215   4917   -363    598    510       O  
ATOM    451  N   ASN A  78      55.829  28.800 100.917  1.00 41.02           N  
ANISOU  451  N   ASN A  78     4624   6604   4356   -322    702    358       N  
ATOM    452  CA  ASN A  78      56.707  28.982 102.068  1.00 38.95           C  
ANISOU  452  CA  ASN A  78     4268   6288   4244   -293    696    373       C  
ATOM    453  C   ASN A  78      55.986  29.733 103.182  1.00 41.40           C  
ANISOU  453  C   ASN A  78     4576   6551   4604   -263    566    418       C  
ATOM    454  O   ASN A  78      56.540  30.666 103.778  1.00 39.87           O  
ANISOU  454  O   ASN A  78     4343   6322   4482   -272    538    472       O  
ATOM    455  CB  ASN A  78      58.012  29.680 101.691  1.00 42.75           C  
ANISOU  455  CB  ASN A  78     4707   6772   4763   -340    781    413       C  
ATOM    456  CG  ASN A  78      59.141  29.321 102.634  1.00 47.21           C  
ANISOU  456  CG  ASN A  78     5151   7301   5484   -306    808    384       C  
ATOM    457  OD1 ASN A  78      59.075  28.295 103.309  1.00 45.25           O  
ANISOU  457  OD1 ASN A  78     4865   7032   5297   -246    791    328       O  
ATOM    458  ND2 ASN A  78      60.173  30.162 102.698  1.00 44.34           N  
ANISOU  458  ND2 ASN A  78     4729   6930   5190   -345    845    421       N  
ATOM    459  N   TYR A  79      54.711  29.368 103.404  1.00 34.86           N  
ANISOU  459  N   TYR A  79     3790   5723   3734   -236    493    388       N  
ATOM    460  CA  TYR A  79      53.929  29.956 104.485  1.00 34.80           C  
ANISOU  460  CA  TYR A  79     3778   5668   3776   -208    383    411       C  
ATOM    461  C   TYR A  79      54.686  29.887 105.801  1.00 36.78           C  
ANISOU  461  C   TYR A  79     3960   5864   4152   -180    372    410       C  
ATOM    462  O   TYR A  79      54.736  30.869 106.551  1.00 33.29           O  
ANISOU  462  O   TYR A  79     3502   5384   3763   -183    310    457       O  
ATOM    463  CB  TYR A  79      52.595  29.234 104.624  1.00 36.70           C  
ANISOU  463  CB  TYR A  79     4050   5916   3978   -185    335    347       C  
ATOM    464  CG  TYR A  79      51.843  29.630 105.874  1.00 38.11           C  
ANISOU  464  CG  TYR A  79     4217   6041   4224   -158    246    349       C  
ATOM    465  CD1 TYR A  79      51.277  30.898 106.006  1.00 36.01           C  
ANISOU  465  CD1 TYR A  79     3966   5758   3959   -162    166    406       C  
ATOM    466  CD2 TYR A  79      51.710  28.735 106.930  1.00 34.24           C  
ANISOU  466  CD2 TYR A  79     3707   5508   3794   -129    250    293       C  
ATOM    467  CE1 TYR A  79      50.588  31.258 107.159  1.00 34.73           C  
ANISOU  467  CE1 TYR A  79     3790   5544   3861   -141     98    396       C  
ATOM    468  CE2 TYR A  79      51.034  29.084 108.086  1.00 36.34           C  
ANISOU  468  CE2 TYR A  79     3972   5725   4112   -114    183    288       C  
ATOM    469  CZ  TYR A  79      50.464  30.344 108.194  1.00 33.10           C  
ANISOU  469  CZ  TYR A  79     3567   5304   3705   -122    110    334       C  
ATOM    470  OH  TYR A  79      49.783  30.697 109.335  1.00 33.97           O  
ANISOU  470  OH  TYR A  79     3675   5363   3869   -112     56    318       O  
ATOM    471  N   THR A  80      55.279  28.727 106.100  1.00 32.98           N  
ANISOU  471  N   THR A  80     3439   5374   3716   -151    427    355       N  
ATOM    472  CA  THR A  80      56.142  28.599 107.268  1.00 38.26           C  
ANISOU  472  CA  THR A  80     4042   5998   4497   -118    409    358       C  
ATOM    473  C   THR A  80      57.509  29.106 106.847  1.00 37.35           C  
ANISOU  473  C   THR A  80     3861   5902   4430   -145    468    387       C  
ATOM    474  O   THR A  80      58.203  28.454 106.058  1.00 40.93           O  
ANISOU  474  O   THR A  80     4288   6384   4881   -149    564    354       O  
ATOM    475  CB  THR A  80      56.227  27.150 107.743  1.00 36.67           C  
ANISOU  475  CB  THR A  80     3832   5770   4330    -66    438    294       C  
ATOM    476  OG1 THR A  80      54.924  26.665 108.057  1.00 40.86           O  
ANISOU  476  OG1 THR A  80     4428   6283   4815    -57    402    258       O  
ATOM    477  CG2 THR A  80      57.075  27.044 108.994  1.00 40.53           C  
ANISOU  477  CG2 THR A  80     4263   6213   4923    -23    396    307       C  
ATOM    478  N   VAL A  81      57.916  30.259 107.378  1.00 35.38           N  
ANISOU  478  N   VAL A  81     3580   5633   4230   -168    420    440       N  
ATOM    479  CA  VAL A  81      59.252  30.746 107.046  1.00 32.81           C  
ANISOU  479  CA  VAL A  81     3178   5322   3965   -203    483    457       C  
ATOM    480  C   VAL A  81      60.300  30.058 107.908  1.00 35.31           C  
ANISOU  480  C   VAL A  81     3394   5624   4399   -155    480    420       C  
ATOM    481  O   VAL A  81      61.329  29.608 107.401  1.00 35.57           O  
ANISOU  481  O   VAL A  81     3354   5680   4481   -155    566    389       O  
ATOM    482  CB  VAL A  81      59.323  32.277 107.184  1.00 34.78           C  
ANISOU  482  CB  VAL A  81     3435   5554   4226   -258    445    523       C  
ATOM    483  CG1 VAL A  81      60.765  32.741 107.175  1.00 34.85           C  
ANISOU  483  CG1 VAL A  81     3346   5569   4328   -297    502    526       C  
ATOM    484  CG2 VAL A  81      58.539  32.975 106.064  1.00 36.09           C  
ANISOU  484  CG2 VAL A  81     3699   5735   4276   -302    463    570       C  
ATOM    485  N   SER A  82      60.054  29.926 109.208  1.00 31.59           N  
ANISOU  485  N   SER A  82     2918   5114   3972   -111    382    418       N  
ATOM    486  CA  SER A  82      61.028  29.286 110.075  1.00 36.68           C  
ANISOU  486  CA  SER A  82     3475   5742   4720    -56    356    392       C  
ATOM    487  C   SER A  82      60.318  28.637 111.243  1.00 35.62           C  
ANISOU  487  C   SER A  82     3397   5562   4576      2    268    383       C  
ATOM    488  O   SER A  82      59.255  29.087 111.671  1.00 37.49           O  
ANISOU  488  O   SER A  82     3712   5778   4756    -16    213    400       O  
ATOM    489  CB  SER A  82      62.080  30.268 110.615  1.00 37.87           C  
ANISOU  489  CB  SER A  82     3529   5896   4962    -86    319    412       C  
ATOM    490  OG  SER A  82      62.830  29.653 111.655  1.00 42.83           O  
ANISOU  490  OG  SER A  82     4084   6510   5680    -21    254    388       O  
ATOM    491  N   CYS A  83      60.936  27.590 111.778  1.00 40.38           N  
ANISOU  491  N   CYS A  83     3958   6144   5239     73    258    356       N  
ATOM    492  CA  CYS A  83      60.410  26.888 112.935  1.00 40.57           C  
ANISOU  492  CA  CYS A  83     4046   6116   5254    129    182    353       C  
ATOM    493  C   CYS A  83      61.108  27.265 114.229  1.00 40.84           C  
ANISOU  493  C   CYS A  83     4033   6133   5352    154     72    374       C  
ATOM    494  O   CYS A  83      60.785  26.713 115.281  1.00 44.97           O  
ANISOU  494  O   CYS A  83     4617   6610   5859    199      3    379       O  
ATOM    495  CB  CYS A  83      60.505  25.385 112.705  1.00 41.59           C  
ANISOU  495  CB  CYS A  83     4190   6218   5394    198    238    315       C  
ATOM    496  SG  CYS A  83      59.385  24.853 111.406  1.00 52.78           S  
ANISOU  496  SG  CYS A  83     5692   7652   6712    161    347    276       S  
ATOM    497  N   LEU A  84      62.045  28.226 114.187  1.00 39.83           N  
ANISOU  497  N   LEU A  84     3804   6040   5290    117     55    386       N  
ATOM    498  CA  LEU A  84      62.803  28.604 115.370  1.00 42.03           C  
ANISOU  498  CA  LEU A  84     4023   6313   5632    134    -55    395       C  
ATOM    499  C   LEU A  84      63.271  30.052 115.230  1.00 42.37           C  
ANISOU  499  C   LEU A  84     3998   6390   5712     50    -61    406       C  
ATOM    500  O   LEU A  84      64.333  30.324 114.660  1.00 42.44           O  
ANISOU  500  O   LEU A  84     3888   6435   5801     30    -14    390       O  
ATOM    501  CB  LEU A  84      64.004  27.680 115.577  1.00 44.92           C  
ANISOU  501  CB  LEU A  84     4286   6683   6096    219    -74    374       C  
ATOM    502  CG  LEU A  84      64.693  27.884 116.917  1.00 53.21           C  
ANISOU  502  CG  LEU A  84     5290   7729   7198    253   -215    383       C  
ATOM    503  CD1 LEU A  84      64.020  26.975 117.928  1.00 50.43           C  
ANISOU  503  CD1 LEU A  84     5064   7317   6779    321   -290    402       C  
ATOM    504  CD2 LEU A  84      66.212  27.638 116.841  1.00 53.72           C  
ANISOU  504  CD2 LEU A  84     5182   7829   7400    302   -232    354       C  
ATOM    505  N   PRO A  85      62.483  31.014 115.734  1.00 38.98           N  
ANISOU  505  N   PRO A  85     3641   5940   5229     -5   -109    428       N  
ATOM    506  CA  PRO A  85      61.134  30.869 116.300  1.00 35.09           C  
ANISOU  506  CA  PRO A  85     3282   5404   4645      0   -143    437       C  
ATOM    507  C   PRO A  85      60.112  30.662 115.193  1.00 34.79           C  
ANISOU  507  C   PRO A  85     3315   5368   4536    -16    -54    438       C  
ATOM    508  O   PRO A  85      60.418  30.933 114.025  1.00 33.19           O  
ANISOU  508  O   PRO A  85     3072   5199   4340    -46     26    444       O  
ATOM    509  CB  PRO A  85      60.911  32.200 117.014  1.00 38.31           C  
ANISOU  509  CB  PRO A  85     3705   5798   5051    -65   -206    448       C  
ATOM    510  CG  PRO A  85      61.709  33.178 116.172  1.00 38.21           C  
ANISOU  510  CG  PRO A  85     3601   5818   5099   -127   -153    457       C  
ATOM    511  CD  PRO A  85      62.923  32.424 115.699  1.00 36.75           C  
ANISOU  511  CD  PRO A  85     3303   5672   4987    -88   -116    438       C  
ATOM    512  N   PHE A  86      58.924  30.181 115.548  1.00 33.42           N  
ANISOU  512  N   PHE A  86     3245   5161   4293      1    -66    429       N  
ATOM    513  CA  PHE A  86      57.883  30.002 114.549  1.00 32.87           C  
ANISOU  513  CA  PHE A  86     3235   5099   4156    -15      3    421       C  
ATOM    514  C   PHE A  86      57.595  31.321 113.857  1.00 32.46           C  
ANISOU  514  C   PHE A  86     3179   5064   4090    -79     17    450       C  
ATOM    515  O   PHE A  86      57.177  32.285 114.502  1.00 33.39           O  
ANISOU  515  O   PHE A  86     3320   5155   4211   -110    -37    464       O  
ATOM    516  CB  PHE A  86      56.611  29.450 115.180  1.00 32.76           C  
ANISOU  516  CB  PHE A  86     3321   5044   4083     -1    -17    397       C  
ATOM    517  CG  PHE A  86      55.523  29.212 114.191  1.00 34.52           C  
ANISOU  517  CG  PHE A  86     3591   5281   4244    -16     41    377       C  
ATOM    518  CD1 PHE A  86      55.704  28.307 113.157  1.00 34.27           C  
ANISOU  518  CD1 PHE A  86     3549   5278   4195      3    116    355       C  
ATOM    519  CD2 PHE A  86      54.311  29.872 114.304  1.00 37.50           C  
ANISOU  519  CD2 PHE A  86     4019   5645   4585    -48     18    370       C  
ATOM    520  CE1 PHE A  86      54.713  28.078 112.240  1.00 37.74           C  
ANISOU  520  CE1 PHE A  86     4031   5738   4570    -16    160    329       C  
ATOM    521  CE2 PHE A  86      53.303  29.655 113.392  1.00 32.32           C  
ANISOU  521  CE2 PHE A  86     3395   5010   3875    -58     55    346       C  
ATOM    522  CZ  PHE A  86      53.493  28.751 112.359  1.00 35.89           C  
ANISOU  522  CZ  PHE A  86     3840   5497   4298    -44    122    325       C  
ATOM    523  N   THR A  87      57.825  31.351 112.550  1.00 27.79           N  
ANISOU  523  N   THR A  87     2568   4511   3481    -98     92    460       N  
ATOM    524  CA  THR A  87      57.815  32.564 111.748  1.00 29.14           C  
ANISOU  524  CA  THR A  87     2739   4696   3639   -156    116    500       C  
ATOM    525  C   THR A  87      57.057  32.224 110.480  1.00 32.84           C  
ANISOU  525  C   THR A  87     3263   5194   4020   -161    174    499       C  
ATOM    526  O   THR A  87      57.324  31.184 109.865  1.00 31.16           O  
ANISOU  526  O   THR A  87     3041   5011   3789   -138    236    467       O  
ATOM    527  CB  THR A  87      59.247  33.048 111.414  1.00 30.55           C  
ANISOU  527  CB  THR A  87     2825   4896   3885   -190    159    515       C  
ATOM    528  OG1 THR A  87      59.955  33.324 112.625  1.00 30.24           O  
ANISOU  528  OG1 THR A  87     2724   4838   3926   -186     90    506       O  
ATOM    529  CG2 THR A  87      59.246  34.298 110.544  1.00 31.03           C  
ANISOU  529  CG2 THR A  87     2906   4960   3925   -259    197    564       C  
ATOM    530  N   ILE A  88      56.096  33.069 110.116  1.00 29.42           N  
ANISOU  530  N   ILE A  88     2889   4752   3536   -185    147    529       N  
ATOM    531  CA  ILE A  88      55.254  32.796 108.966  1.00 31.47           C  
ANISOU  531  CA  ILE A  88     3207   5046   3705   -187    177    527       C  
ATOM    532  C   ILE A  88      55.442  33.899 107.946  1.00 33.21           C  
ANISOU  532  C   ILE A  88     3453   5278   3887   -234    201    591       C  
ATOM    533  O   ILE A  88      55.910  34.996 108.251  1.00 36.38           O  
ANISOU  533  O   ILE A  88     3839   5646   4338   -266    186    636       O  
ATOM    534  CB  ILE A  88      53.758  32.679 109.326  1.00 32.64           C  
ANISOU  534  CB  ILE A  88     3408   5175   3817   -163    115    500       C  
ATOM    535  CG1 ILE A  88      53.234  34.020 109.847  1.00 33.47           C  
ANISOU  535  CG1 ILE A  88     3530   5235   3952   -178     46    539       C  
ATOM    536  CG2 ILE A  88      53.541  31.593 110.342  1.00 31.49           C  
ANISOU  536  CG2 ILE A  88     3257   5008   3699   -127    105    440       C  
ATOM    537  CD1 ILE A  88      51.713  34.073 110.099  1.00 27.51           C  
ANISOU  537  CD1 ILE A  88     2813   4463   3176   -156    -10    508       C  
ATOM    538  N   ASN A  89      55.074  33.578 106.719  1.00 31.78           N  
ANISOU  538  N   ASN A  89     3320   5143   3612   -242    242    594       N  
ATOM    539  CA  ASN A  89      54.749  34.591 105.742  1.00 36.20           C  
ANISOU  539  CA  ASN A  89     3945   5708   4102   -275    237    662       C  
ATOM    540  C   ASN A  89      53.437  35.231 106.171  1.00 38.22           C  
ANISOU  540  C   ASN A  89     4240   5928   4353   -247    134    677       C  
ATOM    541  O   ASN A  89      52.443  34.526 106.372  1.00 38.87           O  
ANISOU  541  O   ASN A  89     4330   6024   4414   -211     93    622       O  
ATOM    542  CB  ASN A  89      54.609  33.967 104.361  1.00 39.99           C  
ANISOU  542  CB  ASN A  89     4476   6253   4465   -289    296    652       C  
ATOM    543  CG  ASN A  89      54.755  34.982 103.259  1.00 51.78           C  
ANISOU  543  CG  ASN A  89     6043   7754   5879   -336    320    734       C  
ATOM    544  OD1 ASN A  89      54.500  36.169 103.469  1.00 52.12           O  
ANISOU  544  OD1 ASN A  89     6115   7747   5942   -343    265    802       O  
ATOM    545  ND2 ASN A  89      55.171  34.531 102.073  1.00 53.54           N  
ANISOU  545  ND2 ASN A  89     6304   8033   6006   -372    408    729       N  
ATOM    546  N   CYS A  90      53.462  36.531 106.437  1.00 34.36           N  
ANISOU  546  N   CYS A  90     3766   5385   3905   -264     97    739       N  
ATOM    547  CA  CYS A  90      52.322  37.205 107.050  1.00 38.09           C  
ANISOU  547  CA  CYS A  90     4258   5808   4406   -233      4    744       C  
ATOM    548  C   CYS A  90      51.152  37.146 106.069  1.00 36.42           C  
ANISOU  548  C   CYS A  90     4107   5631   4101   -204    -44    754       C  
ATOM    549  O   CYS A  90      51.077  37.929 105.121  1.00 37.77           O  
ANISOU  549  O   CYS A  90     4340   5800   4210   -215    -55    830       O  
ATOM    550  CB  CYS A  90      52.688  38.637 107.413  1.00 34.99           C  
ANISOU  550  CB  CYS A  90     3875   5343   4078   -261    -13    809       C  
ATOM    551  SG  CYS A  90      51.300  39.713 107.922  1.00 38.97           S  
ANISOU  551  SG  CYS A  90     4411   5772   4623   -220   -117    826       S  
ATOM    552  N   GLN A  91      50.257  36.189 106.281  1.00 35.45           N  
ANISOU  552  N   GLN A  91     3966   5540   3962   -169    -73    677       N  
ATOM    553  CA  GLN A  91      49.131  35.916 105.395  1.00 39.44           C  
ANISOU  553  CA  GLN A  91     4510   6095   4382   -143   -123    661       C  
ATOM    554  C   GLN A  91      48.183  34.993 106.142  1.00 37.83           C  
ANISOU  554  C   GLN A  91     4262   5898   4213   -115   -149    558       C  
ATOM    555  O   GLN A  91      48.601  34.251 107.040  1.00 31.55           O  
ANISOU  555  O   GLN A  91     3430   5088   3471   -121   -103    505       O  
ATOM    556  CB  GLN A  91      49.568  35.250 104.080  1.00 36.36           C  
ANISOU  556  CB  GLN A  91     4161   5782   3873   -170    -64    667       C  
ATOM    557  CG  GLN A  91      49.869  33.739 104.243  1.00 42.56           C  
ANISOU  557  CG  GLN A  91     4908   6610   4654   -176      8    573       C  
ATOM    558  CD  GLN A  91      50.562  33.076 103.028  1.00 47.63           C  
ANISOU  558  CD  GLN A  91     5585   7318   5195   -211     95    569       C  
ATOM    559  OE1 GLN A  91      51.696  33.411 102.658  1.00 51.87           O  
ANISOU  559  OE1 GLN A  91     6130   7852   5726   -247    169    618       O  
ATOM    560  NE2 GLN A  91      49.878  32.100 102.431  1.00 44.45           N  
ANISOU  560  NE2 GLN A  91     5198   6974   4716   -207     96    498       N  
ATOM    561  N   GLU A  92      46.910  35.029 105.759  1.00 36.82           N  
ANISOU  561  N   GLU A  92     4141   5794   4056    -84   -223    530       N  
ATOM    562  CA  GLU A  92      45.968  34.016 106.234  1.00 38.14           C  
ANISOU  562  CA  GLU A  92     4268   5981   4242    -72   -230    418       C  
ATOM    563  C   GLU A  92      46.151  32.768 105.371  1.00 36.53           C  
ANISOU  563  C   GLU A  92     4081   5854   3946    -93   -173    368       C  
ATOM    564  O   GLU A  92      46.042  32.867 104.146  1.00 38.82           O  
ANISOU  564  O   GLU A  92     4412   6203   4136    -98   -194    398       O  
ATOM    565  CB  GLU A  92      44.531  34.531 106.117  1.00 36.49           C  
ANISOU  565  CB  GLU A  92     4041   5774   4050    -33   -331    393       C  
ATOM    566  CG  GLU A  92      44.140  35.664 107.109  1.00 39.61           C  
ANISOU  566  CG  GLU A  92     4410   6084   4557     -7   -379    414       C  
ATOM    567  CD  GLU A  92      44.148  35.280 108.618  1.00 42.40           C  
ANISOU  567  CD  GLU A  92     4724   6381   5004    -23   -330    342       C  
ATOM    568  OE1 GLU A  92      44.379  34.089 108.947  1.00 46.68           O  
ANISOU  568  OE1 GLU A  92     5261   6945   5529    -47   -265    278       O  
ATOM    569  OE2 GLU A  92      43.900  36.165 109.484  1.00 40.55           O  
ANISOU  569  OE2 GLU A  92     4474   6077   4857    -12   -356    348       O  
ATOM    570  N   PRO A  93      46.414  31.591 105.949  1.00 34.66           N  
ANISOU  570  N   PRO A  93     3822   5613   3734   -106   -101    293       N  
ATOM    571  CA  PRO A  93      46.569  30.390 105.110  1.00 35.46           C  
ANISOU  571  CA  PRO A  93     3942   5777   3756   -127    -38    237       C  
ATOM    572  C   PRO A  93      45.224  30.000 104.533  1.00 37.40           C  
ANISOU  572  C   PRO A  93     4183   6076   3951   -124    -93    160       C  
ATOM    573  O   PRO A  93      44.243  29.884 105.263  1.00 33.38           O  
ANISOU  573  O   PRO A  93     3635   5543   3504   -113   -129     95       O  
ATOM    574  CB  PRO A  93      47.098  29.328 106.078  1.00 37.20           C  
ANISOU  574  CB  PRO A  93     4142   5955   4039   -131     42    181       C  
ATOM    575  CG  PRO A  93      46.633  29.760 107.398  1.00 36.21           C  
ANISOU  575  CG  PRO A  93     3992   5763   4004   -116      3    173       C  
ATOM    576  CD  PRO A  93      46.556  31.272 107.382  1.00 36.68           C  
ANISOU  576  CD  PRO A  93     4049   5804   4085   -104    -73    256       C  
ATOM    577  N   LYS A  94      45.197  29.731 103.230  1.00 36.08           N  
ANISOU  577  N   LYS A  94     4052   5986   3670   -142    -94    158       N  
ATOM    578  CA  LYS A  94      43.923  29.442 102.600  1.00 37.02           C  
ANISOU  578  CA  LYS A  94     4162   6169   3735   -140   -165     84       C  
ATOM    579  C   LYS A  94      43.352  28.112 103.071  1.00 37.46           C  
ANISOU  579  C   LYS A  94     4182   6225   3826   -162   -109    -51       C  
ATOM    580  O   LYS A  94      42.135  28.000 103.242  1.00 37.00           O  
ANISOU  580  O   LYS A  94     4080   6183   3797   -157   -169   -130       O  
ATOM    581  CB  LYS A  94      44.094  29.444 101.086  1.00 40.99           C  
ANISOU  581  CB  LYS A  94     4728   6758   4089   -161   -178    112       C  
ATOM    582  CG  LYS A  94      42.944  28.781 100.336  1.00 41.21           C  
ANISOU  582  CG  LYS A  94     4747   6869   4043   -173   -235      9       C  
ATOM    583  CD  LYS A  94      43.081  29.027  98.841  1.00 47.08           C  
ANISOU  583  CD  LYS A  94     5569   7699   4621   -191   -272     56       C  
ATOM    584  CE  LYS A  94      42.197  28.100  98.011  1.00 54.48           C  
ANISOU  584  CE  LYS A  94     6503   8731   5464   -221   -303    -65       C  
ATOM    585  NZ  LYS A  94      42.434  28.329  96.542  1.00 52.87           N  
ANISOU  585  NZ  LYS A  94     6397   8616   5077   -245   -334    -15       N  
ATOM    586  N   LEU A  95      44.222  27.130 103.351  1.00 38.71           N  
ANISOU  586  N   LEU A  95     4355   6355   3996   -184      8    -80       N  
ATOM    587  CA  LEU A  95      43.781  25.794 103.736  1.00 35.41           C  
ANISOU  587  CA  LEU A  95     3924   5924   3607   -209     77   -202       C  
ATOM    588  C   LEU A  95      42.898  25.814 104.987  1.00 36.50           C  
ANISOU  588  C   LEU A  95     4019   6001   3849   -201     55   -253       C  
ATOM    589  O   LEU A  95      42.001  24.966 105.121  1.00 34.19           O  
ANISOU  589  O   LEU A  95     3707   5714   3571   -229     79   -368       O  
ATOM    590  CB  LEU A  95      44.990  24.888 103.962  1.00 36.01           C  
ANISOU  590  CB  LEU A  95     4027   5958   3698   -217    200   -201       C  
ATOM    591  CG  LEU A  95      44.655  23.447 104.373  1.00 40.68           C  
ANISOU  591  CG  LEU A  95     4623   6514   4320   -240    286   -317       C  
ATOM    592  CD1 LEU A  95      43.820  22.743 103.292  1.00 42.49           C  
ANISOU  592  CD1 LEU A  95     4858   6821   4465   -284    290   -424       C  
ATOM    593  CD2 LEU A  95      45.888  22.624 104.750  1.00 44.22           C  
ANISOU  593  CD2 LEU A  95     5096   6902   4806   -228    395   -304       C  
ATOM    594  N   GLY A  96      43.140  26.751 105.904  1.00 33.96           N  
ANISOU  594  N   GLY A  96     3684   5619   3599   -172     21   -178       N  
ATOM    595  CA  GLY A  96      42.366  26.811 107.130  1.00 31.78           C  
ANISOU  595  CA  GLY A  96     3377   5282   3416   -171     13   -228       C  
ATOM    596  C   GLY A  96      42.939  27.823 108.107  1.00 28.69           C  
ANISOU  596  C   GLY A  96     2986   4823   3090   -145    -10   -139       C  
ATOM    597  O   GLY A  96      43.693  28.718 107.729  1.00 29.87           O  
ANISOU  597  O   GLY A  96     3147   4981   3221   -125    -45    -38       O  
ATOM    598  N   SER A  97      42.584  27.650 109.371  1.00 27.02           N  
ANISOU  598  N   SER A  97     2770   4544   2952   -154     18   -181       N  
ATOM    599  CA  SER A  97      42.950  28.601 110.407  1.00 29.86           C  
ANISOU  599  CA  SER A  97     3131   4840   3374   -138     -6   -118       C  
ATOM    600  C   SER A  97      44.240  28.209 111.118  1.00 28.74           C  
ANISOU  600  C   SER A  97     3032   4650   3239   -137     50    -67       C  
ATOM    601  O   SER A  97      44.525  27.025 111.329  1.00 29.40           O  
ANISOU  601  O   SER A  97     3146   4715   3308   -148    121   -106       O  
ATOM    602  CB  SER A  97      41.823  28.696 111.430  1.00 30.90           C  
ANISOU  602  CB  SER A  97     3240   4926   3576   -153     -5   -198       C  
ATOM    603  OG  SER A  97      41.531  27.387 111.891  1.00 35.52           O  
ANISOU  603  OG  SER A  97     3851   5486   4157   -188     81   -286       O  
ATOM    604  N   LEU A  98      44.990  29.220 111.539  1.00 27.77           N  
ANISOU  604  N   LEU A  98     2907   4500   3144   -122     14     18       N  
ATOM    605  CA  LEU A  98      46.214  29.006 112.291  1.00 27.55           C  
ANISOU  605  CA  LEU A  98     2903   4431   3133   -117     45     66       C  
ATOM    606  C   LEU A  98      45.857  28.851 113.760  1.00 27.87           C  
ANISOU  606  C   LEU A  98     2972   4402   3216   -129     57     27       C  
ATOM    607  O   LEU A  98      45.221  29.727 114.343  1.00 27.93           O  
ANISOU  607  O   LEU A  98     2968   4383   3262   -138     21     17       O  
ATOM    608  CB  LEU A  98      47.181  30.171 112.097  1.00 28.34           C  
ANISOU  608  CB  LEU A  98     2984   4535   3247   -107      3    162       C  
ATOM    609  CG  LEU A  98      48.491  29.995 112.855  1.00 28.75           C  
ANISOU  609  CG  LEU A  98     3042   4555   3325   -101     22    203       C  
ATOM    610  CD1 LEU A  98      49.271  28.766 112.323  1.00 29.48           C  
ANISOU  610  CD1 LEU A  98     3140   4672   3390    -87     84    194       C  
ATOM    611  CD2 LEU A  98      49.326  31.258 112.783  1.00 29.96           C  
ANISOU  611  CD2 LEU A  98     3170   4708   3507   -106    -17    282       C  
ATOM    612  N   VAL A  99      46.230  27.728 114.347  1.00 26.26           N  
ANISOU  612  N   VAL A  99     2813   4164   3002   -131    112      4       N  
ATOM    613  CA  VAL A  99      45.875  27.423 115.727  1.00 29.20           C  
ANISOU  613  CA  VAL A  99     3237   4467   3392   -149    134    -32       C  
ATOM    614  C   VAL A  99      47.136  27.017 116.466  1.00 31.80           C  
ANISOU  614  C   VAL A  99     3606   4760   3717   -126    135     24       C  
ATOM    615  O   VAL A  99      47.921  26.211 115.963  1.00 30.61           O  
ANISOU  615  O   VAL A  99     3457   4621   3552    -99    162     44       O  
ATOM    616  CB  VAL A  99      44.830  26.285 115.805  1.00 29.93           C  
ANISOU  616  CB  VAL A  99     3363   4540   3470   -178    206   -129       C  
ATOM    617  CG1 VAL A  99      44.532  25.955 117.253  1.00 35.79           C  
ANISOU  617  CG1 VAL A  99     4179   5203   4217   -205    242   -159       C  
ATOM    618  CG2 VAL A  99      43.556  26.668 115.078  1.00 28.71           C  
ANISOU  618  CG2 VAL A  99     3151   4430   3328   -198    192   -197       C  
ATOM    619  N   VAL A 100      47.314  27.531 117.670  1.00 30.87           N  
ANISOU  619  N   VAL A 100     3520   4597   3613   -136    105     43       N  
ATOM    620  CA  VAL A 100      48.387  27.078 118.538  1.00 32.87           C  
ANISOU  620  CA  VAL A 100     3820   4813   3857   -113     91     89       C  
ATOM    621  C   VAL A 100      47.753  26.284 119.671  1.00 33.01           C  
ANISOU  621  C   VAL A 100     3938   4760   3843   -136    135     43       C  
ATOM    622  O   VAL A 100      46.765  26.723 120.273  1.00 32.66           O  
ANISOU  622  O   VAL A 100     3918   4691   3799   -182    150     -7       O  
ATOM    623  CB  VAL A 100      49.248  28.245 119.057  1.00 32.47           C  
ANISOU  623  CB  VAL A 100     3737   4768   3832   -110     16    148       C  
ATOM    624  CG1 VAL A 100      48.424  29.239 119.869  1.00 36.05           C  
ANISOU  624  CG1 VAL A 100     4209   5193   4296   -154     -3    118       C  
ATOM    625  CG2 VAL A 100      50.429  27.716 119.880  1.00 38.05           C  
ANISOU  625  CG2 VAL A 100     4478   5449   4530    -78    -17    193       C  
ATOM    626  N   ARG A 101      48.301  25.108 119.938  1.00 32.97           N  
ANISOU  626  N   ARG A 101     3995   4718   3815   -107    163     58       N  
ATOM    627  CA  ARG A 101      47.846  24.264 121.032  1.00 34.92           C  
ANISOU  627  CA  ARG A 101     4362   4886   4021   -128    209     31       C  
ATOM    628  C   ARG A 101      48.797  24.497 122.191  1.00 41.08           C  
ANISOU  628  C   ARG A 101     5195   5634   4778   -105    137     96       C  
ATOM    629  O   ARG A 101      50.012  24.337 122.038  1.00 42.88           O  
ANISOU  629  O   ARG A 101     5391   5878   5022    -46     82    159       O  
ATOM    630  CB  ARG A 101      47.825  22.795 120.618  1.00 36.28           C  
ANISOU  630  CB  ARG A 101     4584   5022   4180   -107    284     10       C  
ATOM    631  CG  ARG A 101      47.386  21.817 121.703  1.00 39.43           C  
ANISOU  631  CG  ARG A 101     5127   5324   4532   -131    345    -11       C  
ATOM    632  CD  ARG A 101      46.846  20.550 121.038  1.00 42.34           C  
ANISOU  632  CD  ARG A 101     5527   5660   4902   -140    449    -70       C  
ATOM    633  NE  ARG A 101      45.496  20.770 120.520  1.00 43.25           N  
ANISOU  633  NE  ARG A 101     5596   5806   5031   -211    510   -170       N  
ATOM    634  CZ  ARG A 101      44.750  19.841 119.928  1.00 45.63           C  
ANISOU  634  CZ  ARG A 101     5909   6091   5336   -244    603   -250       C  
ATOM    635  NH1 ARG A 101      45.218  18.609 119.742  1.00 39.41           N  
ANISOU  635  NH1 ARG A 101     5186   5248   4541   -214    658   -240       N  
ATOM    636  NH2 ARG A 101      43.531  20.152 119.510  1.00 42.83           N  
ANISOU  636  NH2 ARG A 101     5495   5775   5002   -306    639   -345       N  
ATOM    637  N   CYS A 102      48.250  24.908 123.325  1.00 38.08           N  
ANISOU  637  N   CYS A 102     4891   5215   4364   -154    136     75       N  
ATOM    638  CA  CYS A 102      49.025  25.206 124.517  1.00 40.66           C  
ANISOU  638  CA  CYS A 102     5282   5516   4651   -145     60    127       C  
ATOM    639  C   CYS A 102      48.835  24.065 125.501  1.00 46.65           C  
ANISOU  639  C   CYS A 102     6200   6189   5335   -150    103    129       C  
ATOM    640  O   CYS A 102      47.700  23.642 125.746  1.00 44.05           O  
ANISOU  640  O   CYS A 102     5945   5813   4979   -208    200     64       O  
ATOM    641  CB  CYS A 102      48.574  26.516 125.158  1.00 43.50           C  
ANISOU  641  CB  CYS A 102     5631   5886   5012   -204     33     98       C  
ATOM    642  SG  CYS A 102      48.449  27.913 124.022  1.00 42.71           S  
ANISOU  642  SG  CYS A 102     5368   5861   4998   -210      5     88       S  
ATOM    643  N   SER A 103      49.933  23.546 126.035  1.00 44.12           N  
ANISOU  643  N   SER A 103     5933   5845   4985    -89     32    203       N  
ATOM    644  CA  SER A 103      49.833  22.500 127.035  1.00 51.00           C  
ANISOU  644  CA  SER A 103     6978   6626   5775    -87     58    223       C  
ATOM    645  C   SER A 103      50.854  22.736 128.129  1.00 53.46           C  
ANISOU  645  C   SER A 103     7351   6929   6031    -51    -66    296       C  
ATOM    646  O   SER A 103      51.985  23.140 127.861  1.00 53.75           O  
ANISOU  646  O   SER A 103     7283   7023   6116     10   -172    344       O  
ATOM    647  CB  SER A 103      50.044  21.111 126.442  1.00 55.52           C  
ANISOU  647  CB  SER A 103     7581   7149   6363    -27    112    241       C  
ATOM    648  OG  SER A 103      49.977  20.130 127.468  1.00 58.77           O  
ANISOU  648  OG  SER A 103     8180   7459   6692    -22    135    272       O  
ATOM    649  N   PHE A 104      50.431  22.495 129.363  1.00 54.67           N  
ANISOU  649  N   PHE A 104     7675   7016   6081    -97    -51    297       N  
ATOM    650  CA  PHE A 104      51.349  22.572 130.489  1.00 59.38           C  
ANISOU  650  CA  PHE A 104     8360   7600   6601    -64   -177    367       C  
ATOM    651  C   PHE A 104      52.318  21.399 130.482  1.00 65.24           C  
ANISOU  651  C   PHE A 104     9148   8298   7340     47   -237    452       C  
ATOM    652  O   PHE A 104      53.504  21.559 130.794  1.00 65.96           O  
ANISOU  652  O   PHE A 104     9202   8424   7438    120   -380    515       O  
ATOM    653  CB  PHE A 104      50.548  22.597 131.783  1.00 64.32           C  
ANISOU  653  CB  PHE A 104     9176   8162   7100   -152   -129    342       C  
ATOM    654  CG  PHE A 104      51.378  22.477 133.006  1.00 69.80           C  
ANISOU  654  CG  PHE A 104    10003   8833   7685   -122   -254    416       C  
ATOM    655  CD1 PHE A 104      52.069  23.563 133.493  1.00 70.38           C  
ANISOU  655  CD1 PHE A 104    10016   8977   7749   -130   -382    425       C  
ATOM    656  CD2 PHE A 104      51.464  21.270 133.681  1.00 71.97           C  
ANISOU  656  CD2 PHE A 104    10471   9012   7862    -88   -247    478       C  
ATOM    657  CE1 PHE A 104      52.837  23.451 134.635  1.00 72.74           C  
ANISOU  657  CE1 PHE A 104    10437   9264   7937   -104   -512    488       C  
ATOM    658  CE2 PHE A 104      52.229  21.151 134.823  1.00 76.49           C  
ANISOU  658  CE2 PHE A 104    11177   9565   8321    -54   -379    554       C  
ATOM    659  CZ  PHE A 104      52.919  22.241 135.298  1.00 74.75           C  
ANISOU  659  CZ  PHE A 104    10887   9428   8087    -62   -517    557       C  
ATOM    660  N   TYR A 105      51.839  20.223 130.103  1.00 65.67           N  
ANISOU  660  N   TYR A 105     9277   8278   7397     63   -131    446       N  
ATOM    661  CA  TYR A 105      52.639  19.013 130.102  1.00 67.66           C  
ANISOU  661  CA  TYR A 105     9590   8464   7652    171   -169    522       C  
ATOM    662  C   TYR A 105      53.213  18.762 128.717  1.00 69.51           C  
ANISOU  662  C   TYR A 105     9646   8746   8020    246   -159    516       C  
ATOM    663  O   TYR A 105      52.614  19.124 127.701  1.00 65.85           O  
ANISOU  663  O   TYR A 105     9066   8332   7620    198    -72    445       O  
ATOM    664  CB  TYR A 105      51.789  17.816 130.536  1.00 73.15           C  
ANISOU  664  CB  TYR A 105    10491   9031   8272    140    -44    519       C  
ATOM    665  CG  TYR A 105      51.318  17.937 131.959  1.00 74.93           C  
ANISOU  665  CG  TYR A 105    10920   9199   8350     68    -46    534       C  
ATOM    666  CD1 TYR A 105      52.196  17.753 133.012  1.00 76.66           C  
ANISOU  666  CD1 TYR A 105    11261   9388   8479    131   -186    630       C  
ATOM    667  CD2 TYR A 105      50.002  18.270 132.247  1.00 75.15           C  
ANISOU  667  CD2 TYR A 105    11015   9209   8330    -64     88    447       C  
ATOM    668  CE1 TYR A 105      51.778  17.877 134.316  1.00 83.12           C  
ANISOU  668  CE1 TYR A 105    12282  10157   9144     58   -187    644       C  
ATOM    669  CE2 TYR A 105      49.572  18.399 133.549  1.00 75.24           C  
ANISOU  669  CE2 TYR A 105    11217   9168   8202   -140    102    452       C  
ATOM    670  CZ  TYR A 105      50.466  18.202 134.582  1.00 84.51           C  
ANISOU  670  CZ  TYR A 105    12529  10312   9270    -81    -35    553       C  
ATOM    671  OH  TYR A 105      50.056  18.325 135.892  1.00 94.07           O  
ANISOU  671  OH  TYR A 105    13948  11472  10323   -163    -22    559       O  
ATOM    672  N   GLU A 106      54.379  18.118 128.681  1.00 70.52           N  
ANISOU  672  N   GLU A 106     9753   8855   8188    365   -249    587       N  
ATOM    673  CA  GLU A 106      55.000  17.831 127.395  1.00 73.57           C  
ANISOU  673  CA  GLU A 106     9972   9280   8701    436   -230    575       C  
ATOM    674  C   GLU A 106      54.201  16.818 126.582  1.00 71.53           C  
ANISOU  674  C   GLU A 106     9755   8956   8466    419    -69    525       C  
ATOM    675  O   GLU A 106      54.334  16.788 125.354  1.00 72.98           O  
ANISOU  675  O   GLU A 106     9799   9189   8740    433    -15    483       O  
ATOM    676  CB  GLU A 106      56.433  17.342 127.594  1.00 80.10           C  
ANISOU  676  CB  GLU A 106    10758  10096   9579    573   -359    653       C  
ATOM    677  CG  GLU A 106      57.483  18.338 127.104  1.00 81.36           C  
ANISOU  677  CG  GLU A 106    10703  10377   9834    604   -462    651       C  
ATOM    678  CD  GLU A 106      58.907  17.813 127.207  1.00 86.38           C  
ANISOU  678  CD  GLU A 106    11267  11006  10546    744   -584    712       C  
ATOM    679  OE1 GLU A 106      59.095  16.667 127.676  1.00 90.15           O  
ANISOU  679  OE1 GLU A 106    11871  11379  11002    829   -600    766       O  
ATOM    680  OE2 GLU A 106      59.838  18.554 126.817  1.00 85.53           O  
ANISOU  680  OE2 GLU A 106    10975  10994  10527    769   -662    704       O  
ATOM    681  N   ASP A 107      53.378  15.995 127.237  1.00 70.57           N  
ANISOU  681  N   ASP A 107     9827   8723   8262    381     14    524       N  
ATOM    682  CA  ASP A 107      52.551  15.014 126.545  1.00 70.99           C  
ANISOU  682  CA  ASP A 107     9930   8707   8336    349    175    465       C  
ATOM    683  C   ASP A 107      51.337  15.625 125.859  1.00 68.24           C  
ANISOU  683  C   ASP A 107     9509   8423   7996    229    284    358       C  
ATOM    684  O   ASP A 107      50.697  14.934 125.061  1.00 69.89           O  
ANISOU  684  O   ASP A 107     9714   8603   8238    199    408    292       O  
ATOM    685  CB  ASP A 107      52.081  13.926 127.520  1.00 74.60           C  
ANISOU  685  CB  ASP A 107    10629   9014   8703    340    236    499       C  
ATOM    686  CG  ASP A 107      51.386  14.492 128.752  1.00 76.05           C  
ANISOU  686  CG  ASP A 107    10952   9180   8762    245    229    502       C  
ATOM    687  OD1 ASP A 107      50.429  15.285 128.608  1.00 72.63           O  
ANISOU  687  OD1 ASP A 107    10469   8808   8320    134    295    418       O  
ATOM    688  OD2 ASP A 107      51.795  14.133 129.878  1.00 78.96           O  
ANISOU  688  OD2 ASP A 107    11486   9473   9042    284    157    587       O  
ATOM    689  N   PHE A 108      50.993  16.880 126.164  1.00 64.91           N  
ANISOU  689  N   PHE A 108     9032   8082   7548    161    238    336       N  
ATOM    690  CA  PHE A 108      49.880  17.578 125.513  1.00 63.03           C  
ANISOU  690  CA  PHE A 108     8709   7909   7330     62    319    239       C  
ATOM    691  C   PHE A 108      48.555  16.847 125.717  1.00 64.36           C  
ANISOU  691  C   PHE A 108     9000   7997   7457    -27    468    164       C  
ATOM    692  O   PHE A 108      47.685  16.862 124.846  1.00 65.87           O  
ANISOU  692  O   PHE A 108     9115   8222   7689    -84    557     74       O  
ATOM    693  CB  PHE A 108      50.147  17.783 124.018  1.00 60.46           C  
ANISOU  693  CB  PHE A 108     8203   7672   7097     90    329    205       C  
ATOM    694  CG  PHE A 108      50.997  18.987 123.706  1.00 59.02           C  
ANISOU  694  CG  PHE A 108     7871   7595   6957    122    214    241       C  
ATOM    695  CD1 PHE A 108      52.361  18.968 123.950  1.00 58.29           C  
ANISOU  695  CD1 PHE A 108     7744   7511   6892    213    107    320       C  
ATOM    696  CD2 PHE A 108      50.436  20.127 123.155  1.00 50.47           C  
ANISOU  696  CD2 PHE A 108     6680   6599   5896     60    215    194       C  
ATOM    697  CE1 PHE A 108      53.147  20.068 123.662  1.00 54.52           C  
ANISOU  697  CE1 PHE A 108     7127   7128   6461    230     14    344       C  
ATOM    698  CE2 PHE A 108      51.220  21.233 122.864  1.00 49.69           C  
ANISOU  698  CE2 PHE A 108     6457   6584   5837     82    121    228       C  
ATOM    699  CZ  PHE A 108      52.577  21.204 123.119  1.00 51.09           C  
ANISOU  699  CZ  PHE A 108     6600   6771   6041    160     27    300       C  
ATOM    700  N   LEU A 109      48.400  16.182 126.862  1.00 68.48           N  
ANISOU  700  N   LEU A 109     9715   8408   7895    -41    496    198       N  
ATOM    701  CA  LEU A 109      47.146  15.503 127.162  1.00 68.97           C  
ANISOU  701  CA  LEU A 109     9905   8385   7917   -140    651    123       C  
ATOM    702  C   LEU A 109      46.095  16.466 127.690  1.00 69.51           C  
ANISOU  702  C   LEU A 109     9969   8490   7951   -254    691     49       C  
ATOM    703  O   LEU A 109      44.900  16.269 127.452  1.00 70.75           O  
ANISOU  703  O   LEU A 109    10127   8631   8124   -348    821    -56       O  
ATOM    704  CB  LEU A 109      47.394  14.372 128.159  1.00 72.24           C  
ANISOU  704  CB  LEU A 109    10546   8652   8248   -115    680    195       C  
ATOM    705  CG  LEU A 109      48.126  13.169 127.548  1.00 77.06           C  
ANISOU  705  CG  LEU A 109    11174   9194   8911    -14    690    241       C  
ATOM    706  CD1 LEU A 109      48.203  12.013 128.538  1.00 79.58           C  
ANISOU  706  CD1 LEU A 109    11740   9348   9148      5    733    311       C  
ATOM    707  CD2 LEU A 109      47.468  12.733 126.242  1.00 78.56           C  
ANISOU  707  CD2 LEU A 109    11256   9408   9187    -53    812    134       C  
ATOM    708  N   GLU A 110      46.516  17.506 128.394  1.00 66.73           N  
ANISOU  708  N   GLU A 110     9605   8187   7562   -249    582     92       N  
ATOM    709  CA  GLU A 110      45.640  18.589 128.808  1.00 62.21           C  
ANISOU  709  CA  GLU A 110     9001   7660   6978   -345    608     18       C  
ATOM    710  C   GLU A 110      46.077  19.830 128.047  1.00 56.98           C  
ANISOU  710  C   GLU A 110     8135   7122   6394   -308    502     19       C  
ATOM    711  O   GLU A 110      47.245  20.231 128.119  1.00 55.40           O  
ANISOU  711  O   GLU A 110     7892   6962   6195   -232    371    103       O  
ATOM    712  CB  GLU A 110      45.735  18.840 130.311  1.00 62.56           C  
ANISOU  712  CB  GLU A 110     9215   7652   6905   -382    579     59       C  
ATOM    713  CG  GLU A 110      44.991  17.871 131.190  1.00 69.81           C  
ANISOU  713  CG  GLU A 110    10351   8444   7729   -457    713     38       C  
ATOM    714  CD  GLU A 110      45.068  18.286 132.644  1.00 74.07           C  
ANISOU  714  CD  GLU A 110    11057   8947   8139   -505    681     73       C  
ATOM    715  OE1 GLU A 110      45.669  19.351 132.915  1.00 74.41           O  
ANISOU  715  OE1 GLU A 110    11028   9068   8178   -480    553    103       O  
ATOM    716  OE2 GLU A 110      44.548  17.555 133.518  1.00 82.20           O  
ANISOU  716  OE2 GLU A 110    12296   9869   9068   -572    786     70       O  
ATOM    717  N   TYR A 111      45.153  20.438 127.319  1.00 52.95           N  
ANISOU  717  N   TYR A 111     7498   6670   5950   -362    556    -74       N  
ATOM    718  CA  TYR A 111      45.566  21.537 126.472  1.00 48.75           C  
ANISOU  718  CA  TYR A 111     6787   6245   5492   -323    462    -64       C  
ATOM    719  C   TYR A 111      44.398  22.482 126.250  1.00 47.23           C  
ANISOU  719  C   TYR A 111     6504   6095   5346   -396    508   -162       C  
ATOM    720  O   TYR A 111      43.249  22.191 126.586  1.00 47.06           O  
ANISOU  720  O   TYR A 111     6534   6030   5317   -474    619   -251       O  
ATOM    721  CB  TYR A 111      46.111  21.021 125.135  1.00 44.76           C  
ANISOU  721  CB  TYR A 111     6177   5782   5047   -253    448    -43       C  
ATOM    722  CG  TYR A 111      45.091  20.271 124.319  1.00 49.27           C  
ANISOU  722  CG  TYR A 111     6728   6343   5650   -295    566   -134       C  
ATOM    723  CD1 TYR A 111      44.211  20.954 123.491  1.00 45.93           C  
ANISOU  723  CD1 TYR A 111     6176   5992   5283   -335    585   -215       C  
ATOM    724  CD2 TYR A 111      45.001  18.879 124.373  1.00 54.62           C  
ANISOU  724  CD2 TYR A 111     7515   6936   6303   -294    654   -143       C  
ATOM    725  CE1 TYR A 111      43.273  20.286 122.745  1.00 46.18           C  
ANISOU  725  CE1 TYR A 111     6179   6024   5342   -376    680   -307       C  
ATOM    726  CE2 TYR A 111      44.059  18.192 123.621  1.00 49.44           C  
ANISOU  726  CE2 TYR A 111     6834   6271   5678   -344    764   -239       C  
ATOM    727  CZ  TYR A 111      43.198  18.904 122.807  1.00 51.32           C  
ANISOU  727  CZ  TYR A 111     6935   6596   5970   -386    773   -325       C  
ATOM    728  OH  TYR A 111      42.249  18.258 122.052  1.00 58.53           O  
ANISOU  728  OH  TYR A 111     7812   7513   6914   -438    869   -430       O  
ATOM    729  N   HIS A 112      44.715  23.625 125.661  1.00 43.51           N  
ANISOU  729  N   HIS A 112     5895   5706   4932   -368    422   -146       N  
ATOM    730  CA  HIS A 112      43.704  24.502 125.108  1.00 42.32           C  
ANISOU  730  CA  HIS A 112     5629   5603   4848   -408    446   -228       C  
ATOM    731  C   HIS A 112      44.288  25.108 123.845  1.00 41.22           C  
ANISOU  731  C   HIS A 112     5344   5549   4769   -347    364   -186       C  
ATOM    732  O   HIS A 112      45.495  25.356 123.756  1.00 40.11           O  
ANISOU  732  O   HIS A 112     5185   5434   4623   -291    278    -98       O  
ATOM    733  CB  HIS A 112      43.269  25.580 126.108  1.00 41.12           C  
ANISOU  733  CB  HIS A 112     5498   5436   4691   -462    440   -262       C  
ATOM    734  CG  HIS A 112      44.371  26.502 126.525  1.00 41.60           C  
ANISOU  734  CG  HIS A 112     5546   5521   4738   -428    325   -181       C  
ATOM    735  ND1 HIS A 112      44.467  27.798 126.067  1.00 43.68           N  
ANISOU  735  ND1 HIS A 112     5691   5839   5068   -415    260   -177       N  
ATOM    736  CD2 HIS A 112      45.426  26.315 127.353  1.00 44.34           C  
ANISOU  736  CD2 HIS A 112     5986   5845   5015   -404    260   -104       C  
ATOM    737  CE1 HIS A 112      45.530  28.373 126.602  1.00 45.74           C  
ANISOU  737  CE1 HIS A 112     5968   6108   5304   -395    171   -109       C  
ATOM    738  NE2 HIS A 112      46.131  27.494 127.386  1.00 46.86           N  
ANISOU  738  NE2 HIS A 112     6231   6210   5364   -386    162    -65       N  
ATOM    739  N   ASP A 113      43.430  25.322 122.863  1.00 38.11           N  
ANISOU  739  N   ASP A 113     4850   5200   4430   -359    390   -250       N  
ATOM    740  CA  ASP A 113      43.862  25.831 121.576  1.00 33.95           C  
ANISOU  740  CA  ASP A 113     4203   4752   3944   -308    324   -212       C  
ATOM    741  C   ASP A 113      43.535  27.308 121.487  1.00 37.80           C  
ANISOU  741  C   ASP A 113     4608   5274   4482   -314    266   -216       C  
ATOM    742  O   ASP A 113      42.510  27.752 122.009  1.00 35.29           O  
ANISOU  742  O   ASP A 113     4286   4931   4191   -360    302   -291       O  
ATOM    743  CB  ASP A 113      43.196  25.064 120.438  1.00 33.87           C  
ANISOU  743  CB  ASP A 113     4146   4775   3949   -311    376   -272       C  
ATOM    744  CG  ASP A 113      43.646  23.615 120.370  1.00 39.82           C  
ANISOU  744  CG  ASP A 113     4977   5490   4663   -298    434   -263       C  
ATOM    745  OD1 ASP A 113      44.713  23.284 120.942  1.00 36.86           O  
ANISOU  745  OD1 ASP A 113     4670   5079   4257   -261    408   -186       O  
ATOM    746  OD2 ASP A 113      42.954  22.814 119.701  1.00 42.60           O  
ANISOU  746  OD2 ASP A 113     5317   5849   5021   -322    502   -335       O  
ATOM    747  N   VAL A 114      44.427  28.069 120.852  1.00 31.95           N  
ANISOU  747  N   VAL A 114     3800   4580   3759   -269    185   -139       N  
ATOM    748  CA  VAL A 114      44.226  29.497 120.600  1.00 34.19           C  
ANISOU  748  CA  VAL A 114     4007   4888   4094   -267    128   -129       C  
ATOM    749  C   VAL A 114      44.344  29.720 119.100  1.00 32.94           C  
ANISOU  749  C   VAL A 114     3764   4798   3955   -229     93    -98       C  
ATOM    750  O   VAL A 114      45.361  29.355 118.488  1.00 29.09           O  
ANISOU  750  O   VAL A 114     3269   4342   3442   -197     75    -35       O  
ATOM    751  CB  VAL A 114      45.243  30.372 121.354  1.00 35.94           C  
ANISOU  751  CB  VAL A 114     4246   5093   4316   -264     67    -63       C  
ATOM    752  CG1 VAL A 114      44.981  31.860 121.087  1.00 33.27           C  
ANISOU  752  CG1 VAL A 114     3838   4764   4040   -265     20    -56       C  
ATOM    753  CG2 VAL A 114      45.229  30.066 122.859  1.00 37.44           C  
ANISOU  753  CG2 VAL A 114     4542   5221   4463   -303     95    -88       C  
ATOM    754  N   ARG A 115      43.314  30.307 118.508  1.00 28.63           N  
ANISOU  754  N   ARG A 115     3155   4275   3450   -231     81   -144       N  
ATOM    755  CA  ARG A 115      43.384  30.678 117.103  1.00 29.21           C  
ANISOU  755  CA  ARG A 115     3161   4411   3525   -196     34   -105       C  
ATOM    756  C   ARG A 115      44.111  32.009 116.939  1.00 28.94           C  
ANISOU  756  C   ARG A 115     3099   4378   3517   -176    -33    -20       C  
ATOM    757  O   ARG A 115      43.894  32.950 117.703  1.00 28.38           O  
ANISOU  757  O   ARG A 115     3028   4263   3492   -188    -52    -26       O  
ATOM    758  CB  ARG A 115      41.979  30.767 116.521  1.00 31.89           C  
ANISOU  758  CB  ARG A 115     3443   4776   3897   -198     32   -186       C  
ATOM    759  CG  ARG A 115      41.967  31.100 115.052  1.00 30.06           C  
ANISOU  759  CG  ARG A 115     3158   4614   3648   -162    -27   -146       C  
ATOM    760  CD  ARG A 115      40.629  30.861 114.441  1.00 35.07           C  
ANISOU  760  CD  ARG A 115     3736   5286   4302   -163    -35   -237       C  
ATOM    761  NE  ARG A 115      40.573  31.416 113.097  1.00 36.06           N  
ANISOU  761  NE  ARG A 115     3821   5475   4404   -124   -114   -188       N  
ATOM    762  CZ  ARG A 115      39.532  31.293 112.286  1.00 36.06           C  
ANISOU  762  CZ  ARG A 115     3766   5529   4407   -113   -152   -250       C  
ATOM    763  NH1 ARG A 115      38.445  30.643 112.685  1.00 36.70           N  
ANISOU  763  NH1 ARG A 115     3811   5607   4528   -143   -111   -374       N  
ATOM    764  NH2 ARG A 115      39.576  31.832 111.077  1.00 34.45           N  
ANISOU  764  NH2 ARG A 115     3544   5381   4162    -75   -233   -190       N  
ATOM    765  N   VAL A 116      44.974  32.096 115.936  1.00 26.87           N  
ANISOU  765  N   VAL A 116     2820   4162   3228   -151    -59     54       N  
ATOM    766  CA  VAL A 116      45.704  33.322 115.664  1.00 26.70           C  
ANISOU  766  CA  VAL A 116     2777   4138   3230   -141   -109    136       C  
ATOM    767  C   VAL A 116      45.169  33.909 114.374  1.00 28.11           C  
ANISOU  767  C   VAL A 116     2920   4357   3404   -117   -148    161       C  
ATOM    768  O   VAL A 116      45.091  33.216 113.351  1.00 25.25           O  
ANISOU  768  O   VAL A 116     2553   4052   2990   -106   -138    157       O  
ATOM    769  CB  VAL A 116      47.222  33.093 115.581  1.00 29.02           C  
ANISOU  769  CB  VAL A 116     3078   4447   3500   -139   -102    205       C  
ATOM    770  CG1 VAL A 116      47.904  34.350 115.060  1.00 28.59           C  
ANISOU  770  CG1 VAL A 116     2998   4395   3469   -140   -140    284       C  
ATOM    771  CG2 VAL A 116      47.775  32.729 116.953  1.00 32.92           C  
ANISOU  771  CG2 VAL A 116     3609   4898   4000   -155    -92    192       C  
ATOM    772  N   VAL A 117      44.839  35.200 114.423  1.00 28.68           N  
ANISOU  772  N   VAL A 117     2975   4395   3528   -108   -195    188       N  
ATOM    773  CA  VAL A 117      44.237  35.948 113.334  1.00 30.72           C  
ANISOU  773  CA  VAL A 117     3210   4674   3788    -76   -250    220       C  
ATOM    774  C   VAL A 117      45.127  37.148 113.062  1.00 31.38           C  
ANISOU  774  C   VAL A 117     3309   4729   3887    -76   -277    322       C  
ATOM    775  O   VAL A 117      45.689  37.725 113.999  1.00 28.99           O  
ANISOU  775  O   VAL A 117     3013   4371   3632   -100   -267    333       O  
ATOM    776  CB  VAL A 117      42.826  36.419 113.735  1.00 34.36           C  
ANISOU  776  CB  VAL A 117     3635   5100   4319    -57   -280    148       C  
ATOM    777  CG1 VAL A 117      42.154  37.141 112.609  1.00 32.61           C  
ANISOU  777  CG1 VAL A 117     3388   4901   4102    -10   -356    184       C  
ATOM    778  CG2 VAL A 117      42.011  35.259 114.231  1.00 32.28           C  
ANISOU  778  CG2 VAL A 117     3358   4853   4053    -76   -233     36       C  
ATOM    779  N   LEU A 118      45.255  37.532 111.796  1.00 30.20           N  
ANISOU  779  N   LEU A 118     3169   4613   3693    -56   -308    392       N  
ATOM    780  CA  LEU A 118      46.128  38.633 111.407  1.00 34.23           C  
ANISOU  780  CA  LEU A 118     3705   5092   4210    -66   -318    492       C  
ATOM    781  C   LEU A 118      45.318  39.826 110.923  1.00 34.03           C  
ANISOU  781  C   LEU A 118     3688   5022   4218    -26   -387    535       C  
ATOM    782  O   LEU A 118      44.537  39.709 109.977  1.00 35.52           O  
ANISOU  782  O   LEU A 118     3880   5253   4364     13   -436    541       O  
ATOM    783  CB  LEU A 118      47.121  38.217 110.304  1.00 32.05           C  
ANISOU  783  CB  LEU A 118     3454   4877   3848    -83   -284    555       C  
ATOM    784  CG  LEU A 118      47.994  36.993 110.530  1.00 31.27           C  
ANISOU  784  CG  LEU A 118     3343   4823   3717   -108   -218    521       C  
ATOM    785  CD1 LEU A 118      48.982  36.804 109.374  1.00 34.78           C  
ANISOU  785  CD1 LEU A 118     3807   5318   4091   -128   -174    581       C  
ATOM    786  CD2 LEU A 118      48.726  37.106 111.862  1.00 32.16           C  
ANISOU  786  CD2 LEU A 118     3437   4887   3896   -134   -197    504       C  
ATOM    787  N   ASP A 119      45.556  40.980 111.532  1.00 34.18           N  
ANISOU  787  N   ASP A 119     3714   4957   4314    -35   -393    567       N  
ATOM    788  CA  ASP A 119      45.325  42.251 110.868  1.00 36.34           C  
ANISOU  788  CA  ASP A 119     4021   5176   4611     -5   -444    651       C  
ATOM    789  C   ASP A 119      46.611  42.605 110.129  1.00 40.55           C  
ANISOU  789  C   ASP A 119     4605   5714   5088    -46   -406    753       C  
ATOM    790  O   ASP A 119      47.709  42.355 110.630  1.00 41.08           O  
ANISOU  790  O   ASP A 119     4662   5788   5160   -101   -344    748       O  
ATOM    791  CB  ASP A 119      44.975  43.353 111.874  1.00 43.68           C  
ANISOU  791  CB  ASP A 119     4938   5998   5659      0   -455    630       C  
ATOM    792  CG  ASP A 119      43.528  43.276 112.363  1.00 44.56           C  
ANISOU  792  CG  ASP A 119     4999   6092   5839     50   -495    537       C  
ATOM    793  OD1 ASP A 119      42.744  42.443 111.837  1.00 41.33           O  
ANISOU  793  OD1 ASP A 119     4562   5755   5388     83   -524    493       O  
ATOM    794  OD2 ASP A 119      43.184  44.056 113.277  1.00 44.32           O  
ANISOU  794  OD2 ASP A 119     4954   5976   5910     51   -491    498       O  
ATOM    795  N   PHE A 120      46.481  43.195 108.948  1.00 39.01           N  
ANISOU  795  N   PHE A 120     4466   5517   4841    -21   -442    844       N  
ATOM    796  CA  PHE A 120      47.643  43.547 108.148  1.00 41.61           C  
ANISOU  796  CA  PHE A 120     4853   5848   5108    -69   -391    940       C  
ATOM    797  C   PHE A 120      47.929  45.030 108.278  1.00 45.49           C  
ANISOU  797  C   PHE A 120     5390   6225   5669    -82   -392   1017       C  
ATOM    798  O   PHE A 120      47.008  45.848 108.309  1.00 47.47           O  
ANISOU  798  O   PHE A 120     5658   6405   5974    -25   -460   1037       O  
ATOM    799  CB  PHE A 120      47.433  43.177 106.681  1.00 43.86           C  
ANISOU  799  CB  PHE A 120     5195   6206   5264    -48   -414    996       C  
ATOM    800  CG  PHE A 120      47.105  41.734 106.480  1.00 43.61           C  
ANISOU  800  CG  PHE A 120     5124   6281   5165    -40   -409    914       C  
ATOM    801  CD1 PHE A 120      48.056  40.754 106.759  1.00 42.67           C  
ANISOU  801  CD1 PHE A 120     4971   6214   5027    -90   -323    868       C  
ATOM    802  CD2 PHE A 120      45.858  41.347 106.038  1.00 41.70           C  
ANISOU  802  CD2 PHE A 120     4871   6084   4888     19   -490    876       C  
ATOM    803  CE1 PHE A 120      47.760  39.421 106.586  1.00 40.50           C  
ANISOU  803  CE1 PHE A 120     4668   6023   4699    -82   -310    791       C  
ATOM    804  CE2 PHE A 120      45.553  40.018 105.863  1.00 43.50           C  
ANISOU  804  CE2 PHE A 120     5063   6404   5059     17   -476    791       C  
ATOM    805  CZ  PHE A 120      46.498  39.054 106.133  1.00 41.75           C  
ANISOU  805  CZ  PHE A 120     4822   6222   4817    -34   -382    750       C  
ATOM    806  N   ILE A 121      49.210  45.361 108.398  1.00 46.60           N  
ANISOU  806  N   ILE A 121     5542   6343   5821   -156   -314   1052       N  
ATOM    807  CA  ILE A 121      49.644  46.744 108.502  1.00 50.83           C  
ANISOU  807  CA  ILE A 121     6125   6765   6422   -188   -295   1122       C  
ATOM    808  C   ILE A 121      49.575  47.381 107.117  1.00 55.85           C  
ANISOU  808  C   ILE A 121     6868   7377   6976   -174   -307   1246       C  
ATOM    809  O   ILE A 121      48.785  48.296 106.891  1.00 59.29           O  
ANISOU  809  O   ILE A 121     7357   7728   7441   -118   -372   1302       O  
ATOM    810  CB  ILE A 121      51.056  46.850 109.098  1.00 51.28           C  
ANISOU  810  CB  ILE A 121     6147   6813   6524   -282   -207   1104       C  
TER     811      ILE A 121                                                      
ATOM    812  N   GLN B  18      42.440  46.092 120.773  1.00 62.84           N  
ANISOU  812  N   GLN B  18     6066   6916  10896  -2210  -2379  -1172       N  
ATOM    813  CA  GLN B  18      42.754  44.971 119.879  1.00 60.32           C  
ANISOU  813  CA  GLN B  18     5436   6827  10656  -2106  -2175   -896       C  
ATOM    814  C   GLN B  18      42.068  43.694 120.379  1.00 57.35           C  
ANISOU  814  C   GLN B  18     5219   6730   9841  -1819  -2198   -853       C  
ATOM    815  O   GLN B  18      42.737  42.742 120.806  1.00 57.86           O  
ANISOU  815  O   GLN B  18     5091   7010   9882  -1762  -2395   -828       O  
ATOM    816  CB  GLN B  18      44.277  44.783 119.759  1.00 63.34           C  
ANISOU  816  CB  GLN B  18     5344   7266  11456  -2303  -2368   -852       C  
ATOM    817  CG  GLN B  18      44.694  43.776 118.672  1.00 61.22           C  
ANISOU  817  CG  GLN B  18     4777   7197  11286  -2178  -2085   -540       C  
ATOM    818  CD  GLN B  18      46.089  44.024 118.098  1.00 64.35           C  
ANISOU  818  CD  GLN B  18     4857   7603  11990  -2294  -1996   -402       C  
ATOM    819  OE1 GLN B  18      46.954  44.641 118.736  1.00 68.44           O  
ANISOU  819  OE1 GLN B  18     5294   8067  12645  -2474  -2236   -544       O  
ATOM    820  NE2 GLN B  18      46.314  43.530 116.880  1.00 62.71           N  
ANISOU  820  NE2 GLN B  18     4475   7471  11880  -2178  -1654   -129       N  
ATOM    821  N   GLU B  19      40.739  43.682 120.318  1.00 83.49           N  
ANISOU  821  N   GLU B  19     8867  10032  12823  -1634  -1982   -827       N  
ATOM    822  CA  GLU B  19      39.967  42.548 120.789  1.00 74.33           C  
ANISOU  822  CA  GLU B  19     7870   9094  11277  -1375  -1966   -774       C  
ATOM    823  C   GLU B  19      39.470  41.690 119.636  1.00 68.86           C  
ANISOU  823  C   GLU B  19     7075   8520  10569  -1248  -1618   -534       C  
ATOM    824  O   GLU B  19      39.178  42.165 118.535  1.00 63.58           O  
ANISOU  824  O   GLU B  19     6368   7756  10034  -1283  -1334   -425       O  
ATOM    825  CB  GLU B  19      38.786  42.999 121.644  1.00 51.57           C  
ANISOU  825  CB  GLU B  19     5422   6151   8019  -1234  -1987   -903       C  
ATOM    826  CG  GLU B  19      38.998  42.711 123.120  1.00 53.68           C  
ANISOU  826  CG  GLU B  19     5838   6519   8038  -1140  -2352  -1080       C  
ATOM    827  CD  GLU B  19      38.038  43.480 124.001  1.00 54.44           C  
ANISOU  827  CD  GLU B  19     6374   6501   7812  -1024  -2400  -1239       C  
ATOM    828  OE1 GLU B  19      36.960  43.870 123.481  1.00 52.34           O  
ANISOU  828  OE1 GLU B  19     6301   6148   7440   -947  -2096  -1150       O  
ATOM    829  OE2 GLU B  19      38.353  43.701 125.197  1.00 57.34           O  
ANISOU  829  OE2 GLU B  19     6897   6876   8015   -987  -2738  -1450       O  
ATOM    830  N   CYS B  20      39.359  40.413 119.926  1.00 67.09           N  
ANISOU  830  N   CYS B  20     6825   8501  10164  -1082  -1645   -458       N  
ATOM    831  CA  CYS B  20      38.946  39.419 118.962  1.00 60.91           C  
ANISOU  831  CA  CYS B  20     5956   7834   9354   -959  -1369   -268       C  
ATOM    832  C   CYS B  20      37.781  38.621 119.520  1.00 54.86           C  
ANISOU  832  C   CYS B  20     5439   7172   8234   -755  -1314   -251       C  
ATOM    833  O   CYS B  20      37.723  38.343 120.722  1.00 59.50           O  
ANISOU  833  O   CYS B  20     6165   7819   8623   -666  -1522   -331       O  
ATOM    834  CB  CYS B  20      40.095  38.487 118.626  1.00 61.84           C  
ANISOU  834  CB  CYS B  20     5747   8076   9673   -965  -1417   -159       C  
ATOM    835  SG  CYS B  20      39.598  37.322 117.392  1.00 67.95           S  
ANISOU  835  SG  CYS B  20     6458   8952  10410   -812  -1084     35       S  
ATOM    836  N   SER B  21      36.842  38.280 118.643  1.00 47.19           N  
ANISOU  836  N   SER B  21     4517   6225   7187   -674  -1033   -142       N  
ATOM    837  CA  SER B  21      35.660  37.532 119.035  1.00 43.83           C  
ANISOU  837  CA  SER B  21     4288   5885   6482   -506   -945   -102       C  
ATOM    838  C   SER B  21      35.548  36.321 118.128  1.00 41.27           C  
ANISOU  838  C   SER B  21     3817   5656   6208   -444   -764     26       C  
ATOM    839  O   SER B  21      35.265  36.458 116.935  1.00 39.42           O  
ANISOU  839  O   SER B  21     3511   5412   6056   -465   -561     82       O  
ATOM    840  CB  SER B  21      34.406  38.394 118.958  1.00 39.90           C  
ANISOU  840  CB  SER B  21     4026   5320   5814   -468   -797   -122       C  
ATOM    841  OG  SER B  21      33.257  37.584 119.135  1.00 41.78           O  
ANISOU  841  OG  SER B  21     4384   5654   5838   -321   -674    -44       O  
ATOM    842  N   LEU B  22      35.795  35.148 118.691  1.00 40.81           N  
ANISOU  842  N   LEU B  22     3727   5685   6096   -350   -839     69       N  
ATOM    843  CA  LEU B  22      35.718  33.888 117.969  1.00 41.00           C  
ANISOU  843  CA  LEU B  22     3646   5768   6165   -283   -684    171       C  
ATOM    844  C   LEU B  22      34.354  33.263 118.227  1.00 37.15           C  
ANISOU  844  C   LEU B  22     3336   5300   5479   -182   -560    205       C  
ATOM    845  O   LEU B  22      33.979  33.034 119.380  1.00 37.17           O  
ANISOU  845  O   LEU B  22     3485   5321   5317    -89   -643    210       O  
ATOM    846  CB  LEU B  22      36.835  32.936 118.393  1.00 44.11           C  
ANISOU  846  CB  LEU B  22     3893   6224   6643   -230   -808    221       C  
ATOM    847  CG  LEU B  22      36.784  31.542 117.767  1.00 44.25           C  
ANISOU  847  CG  LEU B  22     3845   6271   6698   -139   -645    320       C  
ATOM    848  CD1 LEU B  22      36.772  31.638 116.254  1.00 42.51           C  
ANISOU  848  CD1 LEU B  22     3516   6025   6610   -190   -455    339       C  
ATOM    849  CD2 LEU B  22      37.995  30.738 118.235  1.00 49.32           C  
ANISOU  849  CD2 LEU B  22     4342   6977   7422    -64   -763    387       C  
ATOM    850  N   GLN B  23      33.624  32.987 117.157  1.00 33.11           N  
ANISOU  850  N   GLN B  23     2800   4793   4986   -190   -363    235       N  
ATOM    851  CA  GLN B  23      32.265  32.480 117.243  1.00 32.68           C  
ANISOU  851  CA  GLN B  23     2867   4760   4792   -130   -239    267       C  
ATOM    852  C   GLN B  23      32.150  31.287 116.318  1.00 34.55           C  
ANISOU  852  C   GLN B  23     3002   5006   5122   -123   -112    296       C  
ATOM    853  O   GLN B  23      32.960  31.122 115.407  1.00 32.99           O  
ANISOU  853  O   GLN B  23     2669   4808   5059   -147    -84    288       O  
ATOM    854  CB  GLN B  23      31.268  33.567 116.863  1.00 32.59           C  
ANISOU  854  CB  GLN B  23     2946   4754   4682   -153   -146    242       C  
ATOM    855  CG  GLN B  23      31.340  34.753 117.790  1.00 35.35           C  
ANISOU  855  CG  GLN B  23     3441   5058   4932   -151   -262    196       C  
ATOM    856  CD  GLN B  23      30.357  35.834 117.417  1.00 35.16           C  
ANISOU  856  CD  GLN B  23     3525   5030   4805   -144   -141    191       C  
ATOM    857  OE1 GLN B  23      29.289  35.538 116.892  1.00 32.84           O  
ANISOU  857  OE1 GLN B  23     3230   4804   4442   -105      9    243       O  
ATOM    858  NE2 GLN B  23      30.715  37.102 117.678  1.00 37.66           N  
ANISOU  858  NE2 GLN B  23     3930   5260   5118   -184   -206    127       N  
ATOM    859  N   SER B  24      31.138  30.459 116.550  1.00 38.56           N  
ANISOU  859  N   SER B  24     3577   5511   5565    -85    -27    332       N  
ATOM    860  CA  SER B  24      30.963  29.205 115.824  1.00 34.48           C  
ANISOU  860  CA  SER B  24     2993   4966   5143    -88     76    334       C  
ATOM    861  C   SER B  24      29.617  29.179 115.120  1.00 36.88           C  
ANISOU  861  C   SER B  24     3306   5303   5406   -132    190    301       C  
ATOM    862  O   SER B  24      28.596  29.563 115.699  1.00 36.82           O  
ANISOU  862  O   SER B  24     3375   5325   5291   -123    215    340       O  
ATOM    863  CB  SER B  24      31.024  27.984 116.753  1.00 41.45           C  
ANISOU  863  CB  SER B  24     3920   5784   6044    -17     80    414       C  
ATOM    864  OG  SER B  24      32.245  27.906 117.460  1.00 52.58           O  
ANISOU  864  OG  SER B  24     5310   7197   7472     52    -38    454       O  
ATOM    865  N   CYS B  25      29.607  28.707 113.880  1.00 38.23           N  
ANISOU  865  N   CYS B  25     3396   5481   5650   -161    254    230       N  
ATOM    866  CA  CYS B  25      28.339  28.500 113.200  1.00 35.24           C  
ANISOU  866  CA  CYS B  25     3000   5150   5239   -206    329    177       C  
ATOM    867  C   CYS B  25      28.507  27.435 112.129  1.00 37.64           C  
ANISOU  867  C   CYS B  25     3248   5411   5641   -221    366     80       C  
ATOM    868  O   CYS B  25      29.614  26.965 111.842  1.00 39.23           O  
ANISOU  868  O   CYS B  25     3432   5553   5922   -176    361     72       O  
ATOM    869  CB  CYS B  25      27.794  29.797 112.599  1.00 31.18           C  
ANISOU  869  CB  CYS B  25     2476   4762   4608   -200    353    154       C  
ATOM    870  SG  CYS B  25      28.944  30.807 111.652  1.00 37.56           S  
ANISOU  870  SG  CYS B  25     3234   5608   5431   -158    359    130       S  
ATOM    871  N   THR B  26      27.383  27.064 111.542  1.00 35.43           N  
ANISOU  871  N   THR B  26     2940   5168   5353   -278    399      3       N  
ATOM    872  CA  THR B  26      27.349  26.102 110.457  1.00 40.93           C  
ANISOU  872  CA  THR B  26     3607   5826   6119   -297    413   -136       C  
ATOM    873  C   THR B  26      27.586  26.819 109.136  1.00 40.30           C  
ANISOU  873  C   THR B  26     3489   5885   5936   -225    417   -224       C  
ATOM    874  O   THR B  26      26.877  27.775 108.811  1.00 37.11           O  
ANISOU  874  O   THR B  26     3054   5634   5412   -214    422   -224       O  
ATOM    875  CB  THR B  26      25.997  25.391 110.427  1.00 41.96           C  
ANISOU  875  CB  THR B  26     3703   5937   6304   -409    418   -199       C  
ATOM    876  OG1 THR B  26      25.811  24.701 111.669  1.00 41.90           O  
ANISOU  876  OG1 THR B  26     3731   5784   6406   -451    455    -78       O  
ATOM    877  CG2 THR B  26      25.966  24.390 109.268  1.00 44.87           C  
ANISOU  877  CG2 THR B  26     4062   6247   6740   -439    401   -390       C  
ATOM    878  N   GLN B  27      28.563  26.342 108.369  1.00 38.56           N  
ANISOU  878  N   GLN B  27     3278   5618   5754   -146    437   -281       N  
ATOM    879  CA  GLN B  27      28.910  27.028 107.133  1.00 41.96           C  
ANISOU  879  CA  GLN B  27     3682   6180   6081    -31    473   -328       C  
ATOM    880  C   GLN B  27      27.717  27.048 106.179  1.00 42.87           C  
ANISOU  880  C   GLN B  27     3776   6436   6075    -33    450   -474       C  
ATOM    881  O   GLN B  27      26.944  26.090 106.102  1.00 45.43           O  
ANISOU  881  O   GLN B  27     4106   6710   6447   -124    397   -599       O  
ATOM    882  CB  GLN B  27      30.127  26.365 106.474  1.00 42.74           C  
ANISOU  882  CB  GLN B  27     3801   6202   6238     85    519   -348       C  
ATOM    883  CG  GLN B  27      30.933  27.331 105.631  1.00 43.57           C  
ANISOU  883  CG  GLN B  27     3860   6417   6279    231    596   -281       C  
ATOM    884  CD  GLN B  27      32.293  26.766 105.176  1.00 47.27           C  
ANISOU  884  CD  GLN B  27     4324   6810   6826    365    666   -234       C  
ATOM    885  OE1 GLN B  27      32.553  25.562 105.253  1.00 51.39           O  
ANISOU  885  OE1 GLN B  27     4908   7206   7414    376    660   -290       O  
ATOM    886  NE2 GLN B  27      33.165  27.654 104.721  1.00 52.86           N  
ANISOU  886  NE2 GLN B  27     4956   7587   7542    475    752   -110       N  
ATOM    887  N   HIS B  28      27.533  28.187 105.505  1.00 39.14           N  
ANISOU  887  N   HIS B  28     3271   6142   5457     65    489   -448       N  
ATOM    888  CA  HIS B  28      26.554  28.376 104.431  1.00 44.97           C  
ANISOU  888  CA  HIS B  28     3977   7074   6034    126    468   -574       C  
ATOM    889  C   HIS B  28      25.106  28.390 104.929  1.00 43.64           C  
ANISOU  889  C   HIS B  28     3749   6985   5846     -5    401   -597       C  
ATOM    890  O   HIS B  28      24.175  28.267 104.132  1.00 49.20           O  
ANISOU  890  O   HIS B  28     4397   7849   6445     10    342   -728       O  
ATOM    891  CB  HIS B  28      26.731  27.331 103.323  1.00 47.81           C  
ANISOU  891  CB  HIS B  28     4377   7423   6366    200    431   -770       C  
ATOM    892  CG  HIS B  28      28.071  27.385 102.660  1.00 49.34           C  
ANISOU  892  CG  HIS B  28     4620   7581   6545    383    528   -724       C  
ATOM    893  ND1 HIS B  28      28.577  28.544 102.105  1.00 51.41           N  
ANISOU  893  ND1 HIS B  28     4855   7972   6706    551    642   -596       N  
ATOM    894  CD2 HIS B  28      29.009  26.428 102.457  1.00 52.10           C  
ANISOU  894  CD2 HIS B  28     5037   7778   6980    439    552   -764       C  
ATOM    895  CE1 HIS B  28      29.770  28.299 101.594  1.00 53.92           C  
ANISOU  895  CE1 HIS B  28     5202   8226   7060    697    732   -551       C  
ATOM    896  NE2 HIS B  28      30.054  27.023 101.792  1.00 53.46           N  
ANISOU  896  NE2 HIS B  28     5205   8007   7100    641    676   -652       N  
ATOM    897  N   GLN B  29      24.892  28.537 106.231  1.00 41.36           N  
ANISOU  897  N   GLN B  29     3465   6603   5649   -117    407   -466       N  
ATOM    898  CA  GLN B  29      23.573  28.663 106.836  1.00 40.52           C  
ANISOU  898  CA  GLN B  29     3295   6571   5531   -214    382   -427       C  
ATOM    899  C   GLN B  29      23.497  29.980 107.603  1.00 36.34           C  
ANISOU  899  C   GLN B  29     2800   6096   4913   -160    453   -244       C  
ATOM    900  O   GLN B  29      24.530  30.507 108.030  1.00 33.88           O  
ANISOU  900  O   GLN B  29     2564   5687   4621   -116    490   -159       O  
ATOM    901  CB  GLN B  29      23.250  27.501 107.791  1.00 43.97           C  
ANISOU  901  CB  GLN B  29     3727   6822   6159   -374    351   -421       C  
ATOM    902  CG  GLN B  29      23.117  26.135 107.126  1.00 48.90           C  
ANISOU  902  CG  GLN B  29     4328   7348   6903   -462    284   -616       C  
ATOM    903  CD  GLN B  29      21.845  26.027 106.297  1.00 56.05           C  
ANISOU  903  CD  GLN B  29     5108   8432   7755   -519    198   -764       C  
ATOM    904  OE1 GLN B  29      21.858  26.244 105.081  1.00 59.86           O  
ANISOU  904  OE1 GLN B  29     5580   9074   8090   -417    146   -911       O  
ATOM    905  NE2 GLN B  29      20.732  25.703 106.957  1.00 60.39           N  
ANISOU  905  NE2 GLN B  29     5549   8974   8421   -668    185   -713       N  
ATOM    906  N   PRO B  30      22.302  30.551 107.766  1.00 34.75           N  
ANISOU  906  N   PRO B  30     2542   6047   4614   -157    471   -186       N  
ATOM    907  CA  PRO B  30      22.190  31.829 108.480  1.00 33.09           C  
ANISOU  907  CA  PRO B  30     2401   5870   4301    -82    552    -20       C  
ATOM    908  C   PRO B  30      22.709  31.723 109.901  1.00 32.30           C  
ANISOU  908  C   PRO B  30     2405   5574   4293   -138    551     82       C  
ATOM    909  O   PRO B  30      22.630  30.677 110.550  1.00 33.91           O  
ANISOU  909  O   PRO B  30     2598   5660   4625   -232    514     81       O  
ATOM    910  CB  PRO B  30      20.682  32.118 108.466  1.00 36.12           C  
ANISOU  910  CB  PRO B  30     2689   6450   4585    -71    572     29       C  
ATOM    911  CG  PRO B  30      20.193  31.409 107.257  1.00 41.21           C  
ANISOU  911  CG  PRO B  30     3198   7236   5223    -94    490   -141       C  
ATOM    912  CD  PRO B  30      21.013  30.148 107.177  1.00 40.34           C  
ANISOU  912  CD  PRO B  30     3114   6926   5288   -202    416   -274       C  
ATOM    913  N   TYR B  31      23.304  32.812 110.364  1.00 30.12           N  
ANISOU  913  N   TYR B  31     2236   5254   3954    -68    591    167       N  
ATOM    914  CA  TYR B  31      23.856  32.852 111.706  1.00 29.04           C  
ANISOU  914  CA  TYR B  31     2212   4957   3863    -92    561    243       C  
ATOM    915  C   TYR B  31      23.651  34.255 112.238  1.00 27.36           C  
ANISOU  915  C   TYR B  31     2120   4763   3514     -8    616    333       C  
ATOM    916  O   TYR B  31      24.151  35.215 111.654  1.00 28.06           O  
ANISOU  916  O   TYR B  31     2234   4861   3568     43    658    324       O  
ATOM    917  CB  TYR B  31      25.343  32.461 111.712  1.00 30.16           C  
ANISOU  917  CB  TYR B  31     2369   4959   4133   -123    497    194       C  
ATOM    918  CG  TYR B  31      26.024  32.667 113.044  1.00 29.84           C  
ANISOU  918  CG  TYR B  31     2437   4789   4112   -125    435    256       C  
ATOM    919  CD1 TYR B  31      25.612  31.954 114.172  1.00 28.99           C  
ANISOU  919  CD1 TYR B  31     2381   4626   4008   -132    412    318       C  
ATOM    920  CD2 TYR B  31      27.058  33.596 113.194  1.00 30.69           C  
ANISOU  920  CD2 TYR B  31     2593   4833   4234   -113    398    256       C  
ATOM    921  CE1 TYR B  31      26.225  32.130 115.393  1.00 31.92           C  
ANISOU  921  CE1 TYR B  31     2864   4908   4355    -95    340    367       C  
ATOM    922  CE2 TYR B  31      27.673  33.782 114.432  1.00 29.82           C  
ANISOU  922  CE2 TYR B  31     2580   4624   4127   -114    299    282       C  
ATOM    923  CZ  TYR B  31      27.244  33.038 115.521  1.00 31.06           C  
ANISOU  923  CZ  TYR B  31     2803   4755   4243    -90    265    332       C  
ATOM    924  OH  TYR B  31      27.818  33.196 116.756  1.00 31.38           O  
ANISOU  924  OH  TYR B  31     2953   4726   4243    -51    157    352       O  
ATOM    925  N   VAL B  32      22.941  34.366 113.349  1.00 29.50           N  
ANISOU  925  N   VAL B  32     2474   5021   3713     21    633    429       N  
ATOM    926  CA  VAL B  32      22.805  35.639 114.046  1.00 32.37           C  
ANISOU  926  CA  VAL B  32     3004   5361   3935    117    679    504       C  
ATOM    927  C   VAL B  32      24.116  35.901 114.789  1.00 31.18           C  
ANISOU  927  C   VAL B  32     2972   5033   3840     89    574    458       C  
ATOM    928  O   VAL B  32      24.444  35.194 115.747  1.00 28.25           O  
ANISOU  928  O   VAL B  32     2645   4583   3505     73    492    469       O  
ATOM    929  CB  VAL B  32      21.614  35.622 115.008  1.00 31.48           C  
ANISOU  929  CB  VAL B  32     2954   5299   3707    194    742    633       C  
ATOM    930  CG1 VAL B  32      21.542  36.921 115.784  1.00 31.99           C  
ANISOU  930  CG1 VAL B  32     3239   5313   3603    320    788    694       C  
ATOM    931  CG2 VAL B  32      20.323  35.377 114.239  1.00 28.37           C  
ANISOU  931  CG2 VAL B  32     2391   5102   3286    205    828    681       C  
ATOM    932  N   VAL B  33      24.853  36.932 114.360  1.00 32.23           N  
ANISOU  932  N   VAL B  33     3709   4669   3868    886    -22    -40       N  
ATOM    933  CA  VAL B  33      26.165  37.202 114.931  1.00 30.11           C  
ANISOU  933  CA  VAL B  33     3569   4352   3521    921    -95    -32       C  
ATOM    934  C   VAL B  33      26.004  37.729 116.350  1.00 34.72           C  
ANISOU  934  C   VAL B  33     4269   4864   4058   1027    -50    -53       C  
ATOM    935  O   VAL B  33      25.251  38.679 116.605  1.00 37.03           O  
ANISOU  935  O   VAL B  33     4543   5143   4386   1082    -53    -61       O  
ATOM    936  CB  VAL B  33      26.954  38.184 114.053  1.00 32.08           C  
ANISOU  936  CB  VAL B  33     3780   4619   3789    899   -249     -5       C  
ATOM    937  CG1 VAL B  33      28.320  38.480 114.682  1.00 28.13           C  
ANISOU  937  CG1 VAL B  33     3398   4070   3221    929   -326     -8       C  
ATOM    938  CG2 VAL B  33      27.148  37.601 112.650  1.00 27.09           C  
ANISOU  938  CG2 VAL B  33     3038   4068   3185    811   -289     19       C  
ATOM    939  N   ASP B  34      26.701  37.098 117.287  1.00 36.74           N  
ANISOU  939  N   ASP B  34     4652   5081   4226   1069     -8    -64       N  
ATOM    940  CA  ASP B  34      26.713  37.567 118.661  1.00 39.21           C  
ANISOU  940  CA  ASP B  34     5091   5334   4474   1189     22    -90       C  
ATOM    941  C   ASP B  34      27.451  38.899 118.728  1.00 38.16           C  
ANISOU  941  C   ASP B  34     4990   5170   4340   1228   -132   -108       C  
ATOM    942  O   ASP B  34      28.636  38.970 118.397  1.00 39.10           O  
ANISOU  942  O   ASP B  34     5129   5291   4437   1194   -237   -109       O  
ATOM    943  CB  ASP B  34      27.395  36.519 119.522  1.00 40.68           C  
ANISOU  943  CB  ASP B  34     5404   5496   4556   1232     92    -97       C  
ATOM    944  CG  ASP B  34      27.171  36.735 120.989  1.00 51.92           C  
ANISOU  944  CG  ASP B  34     6958   6870   5902   1372    164   -120       C  
ATOM    945  OD1 ASP B  34      26.388  37.645 121.353  1.00 56.81           O  
ANISOU  945  OD1 ASP B  34     7562   7473   6552   1432    169   -133       O  
ATOM    946  OD2 ASP B  34      27.782  35.974 121.782  1.00 57.68           O  
ANISOU  946  OD2 ASP B  34     7808   7578   6528   1434    216   -126       O  
ATOM    947  N   ASP B  35      26.764  39.950 119.150  1.00 40.82           N  
ANISOU  947  N   ASP B  35     5330   5474   4704   1299   -143   -125       N  
ATOM    948  CA  ASP B  35      27.358  41.287 119.198  1.00 42.69           C  
ANISOU  948  CA  ASP B  35     5595   5665   4960   1332   -285   -146       C  
ATOM    949  C   ASP B  35      28.323  41.367 120.374  1.00 40.50           C  
ANISOU  949  C   ASP B  35     5461   5336   4591   1422   -326   -198       C  
ATOM    950  O   ASP B  35      27.891  41.284 121.530  1.00 42.52           O  
ANISOU  950  O   ASP B  35     5808   5567   4781   1536   -249   -230       O  
ATOM    951  CB  ASP B  35      26.246  42.345 119.322  1.00 45.22           C  
ANISOU  951  CB  ASP B  35     5883   5964   5335   1393   -278   -153       C  
ATOM    952  CG  ASP B  35      26.765  43.774 119.169  1.00 50.46           C  
ANISOU  952  CG  ASP B  35     6563   6568   6042   1412   -425   -168       C  
ATOM    953  OD1 ASP B  35      27.953  44.037 119.502  1.00 50.35           O  
ANISOU  953  OD1 ASP B  35     6621   6509   6000   1416   -520   -198       O  
ATOM    954  OD2 ASP B  35      25.983  44.613 118.692  1.00 50.57           O  
ANISOU  954  OD2 ASP B  35     6513   6578   6123   1421   -443   -152       O  
ATOM    955  N   PRO B  36      29.634  41.532 120.146  1.00 39.94           N  
ANISOU  955  N   PRO B  36     5411   5255   4508   1385   -444   -213       N  
ATOM    956  CA  PRO B  36      30.568  41.547 121.266  1.00 38.80           C  
ANISOU  956  CA  PRO B  36     5395   5076   4272   1477   -490   -278       C  
ATOM    957  C   PRO B  36      30.735  42.905 121.921  1.00 44.86           C  
ANISOU  957  C   PRO B  36     6216   5770   5060   1559   -594   -340       C  
ATOM    958  O   PRO B  36      31.601  43.033 122.793  1.00 44.47           O  
ANISOU  958  O   PRO B  36     6262   5693   4942   1636   -659   -410       O  
ATOM    959  CB  PRO B  36      31.873  41.126 120.586  1.00 38.70           C  
ANISOU  959  CB  PRO B  36     5354   5095   4253   1387   -575   -268       C  
ATOM    960  CG  PRO B  36      31.782  41.773 119.254  1.00 38.91           C  
ANISOU  960  CG  PRO B  36     5254   5134   4397   1272   -642   -215       C  
ATOM    961  CD  PRO B  36      30.319  41.758 118.864  1.00 40.54           C  
ANISOU  961  CD  PRO B  36     5392   5358   4654   1265   -544   -174       C  
ATOM    962  N   CYS B  37      29.975  43.914 121.496  1.00 47.24           N  
ANISOU  962  N   CYS B  37     6459   6040   5452   1547   -620   -323       N  
ATOM    963  CA  CYS B  37      30.041  45.215 122.134  1.00 48.44           C  
ANISOU  963  CA  CYS B  37     6668   6110   5628   1630   -714   -386       C  
ATOM    964  C   CYS B  37      29.412  45.130 123.517  1.00 50.89           C  
ANISOU  964  C   CYS B  37     7089   6405   5841   1792   -637   -440       C  
ATOM    965  O   CYS B  37      28.504  44.324 123.741  1.00 50.73           O  
ANISOU  965  O   CYS B  37     7066   6431   5776   1824   -491   -404       O  
ATOM    966  CB  CYS B  37      29.306  46.277 121.319  1.00 50.98           C  
ANISOU  966  CB  CYS B  37     6907   6401   6063   1590   -749   -347       C  
ATOM    967  SG  CYS B  37      30.023  46.684 119.705  1.00 51.72           S  
ANISOU  967  SG  CYS B  37     6881   6498   6272   1426   -848   -277       S  
ATOM    968  N   PRO B  38      29.854  45.967 124.455  1.00 55.56           N  
ANISOU  968  N   PRO B  38     7774   6930   6404   1900   -730   -528       N  
ATOM    969  CA  PRO B  38      29.221  45.974 125.776  1.00 58.33           C  
ANISOU  969  CA  PRO B  38     8236   7272   6655   2076   -659   -579       C  
ATOM    970  C   PRO B  38      27.742  46.285 125.643  1.00 59.14           C  
ANISOU  970  C   PRO B  38     8292   7383   6796   2106   -559   -533       C  
ATOM    971  O   PRO B  38      27.297  46.891 124.666  1.00 58.10           O  
ANISOU  971  O   PRO B  38     8061   7241   6772   2019   -591   -489       O  
ATOM    972  CB  PRO B  38      29.953  47.094 126.521  1.00 61.34           C  
ANISOU  972  CB  PRO B  38     8699   7572   7035   2166   -814   -690       C  
ATOM    973  CG  PRO B  38      31.227  47.297 125.768  1.00 59.27           C  
ANISOU  973  CG  PRO B  38     8383   7289   6847   2034   -948   -702       C  
ATOM    974  CD  PRO B  38      30.905  46.994 124.340  1.00 55.54           C  
ANISOU  974  CD  PRO B  38     7779   6857   6469   1869   -902   -588       C  
ATOM    975  N   ILE B  39      26.970  45.844 126.631  1.00 63.93           N  
ANISOU  975  N   ILE B  39     8968   8015   7308   2240   -432   -540       N  
ATOM    976  CA  ILE B  39      25.539  46.083 126.566  1.00 68.02           C  
ANISOU  976  CA  ILE B  39     9434   8554   7858   2275   -327   -499       C  
ATOM    977  C   ILE B  39      25.304  47.586 126.637  1.00 69.46           C  
ANISOU  977  C   ILE B  39     9628   8667   8097   2337   -446   -549       C  
ATOM    978  O   ILE B  39      26.095  48.332 127.238  1.00 68.81           O  
ANISOU  978  O   ILE B  39     9635   8516   7994   2408   -575   -633       O  
ATOM    979  CB  ILE B  39      24.803  45.329 127.690  1.00 71.26           C  
ANISOU  979  CB  ILE B  39     9921   9002   8153   2414   -158   -492       C  
ATOM    980  CG1 ILE B  39      23.293  45.273 127.409  1.00 72.13           C  
ANISOU  980  CG1 ILE B  39     9937   9158   8313   2410    -20   -434       C  
ATOM    981  CG2 ILE B  39      25.108  45.953 129.050  1.00 73.09           C  
ANISOU  981  CG2 ILE B  39    10301   9190   8278   2611   -213   -583       C  
ATOM    982  CD1 ILE B  39      22.923  44.774 126.002  1.00 70.60           C  
ANISOU  982  CD1 ILE B  39     9582   9011   8231   2224     15   -362       C  
ATOM    983  N   HIS B  40      24.263  48.050 125.945  1.00 67.34           N  
ANISOU  983  N   HIS B  40     9264   8414   7909   2302   -412   -502       N  
ATOM    984  CA  HIS B  40      23.890  49.457 125.858  1.00 69.39           C  
ANISOU  984  CA  HIS B  40     9527   8608   8231   2356   -510   -534       C  
ATOM    985  C   HIS B  40      24.887  50.282 125.059  1.00 66.03           C  
ANISOU  985  C   HIS B  40     9081   8106   7904   2251   -677   -546       C  
ATOM    986  O   HIS B  40      24.753  51.508 125.008  1.00 72.62           O  
ANISOU  986  O   HIS B  40     9934   8861   8796   2293   -772   -577       O  
ATOM    987  CB  HIS B  40      23.674  50.082 127.242  1.00 73.53           C  
ANISOU  987  CB  HIS B  40    10182   9087   8667   2556   -524   -619       C  
ATOM    988  CG  HIS B  40      22.736  49.290 128.101  1.00 77.08           C  
ANISOU  988  CG  HIS B  40    10661   9612   9014   2672   -347   -600       C  
ATOM    989  ND1 HIS B  40      23.147  48.607 129.225  1.00 77.40           N  
ANISOU  989  ND1 HIS B  40    10814   9667   8927   2782   -292   -635       N  
ATOM    990  CD2 HIS B  40      21.415  49.024 127.962  1.00 77.31           C  
ANISOU  990  CD2 HIS B  40    10613   9710   9053   2691   -204   -543       C  
ATOM    991  CE1 HIS B  40      22.115  47.978 129.759  1.00 77.49           C  
ANISOU  991  CE1 HIS B  40    10825   9744   8876   2864   -114   -592       C  
ATOM    992  NE2 HIS B  40      21.052  48.213 129.011  1.00 79.72           N  
ANISOU  992  NE2 HIS B  40    10986  10061   9245   2804    -58   -540       N  
ATOM    993  N   PHE B  41      25.891  49.660 124.452  1.00 60.45           N  
ANISOU  993  N   PHE B  41     8337   7414   7217   2121   -713   -521       N  
ATOM    994  CA  PHE B  41      26.723  50.346 123.481  1.00 61.84           C  
ANISOU  994  CA  PHE B  41     8463   7532   7501   2000   -844   -504       C  
ATOM    995  C   PHE B  41      26.037  50.316 122.124  1.00 59.67           C  
ANISOU  995  C   PHE B  41     8057   7308   7308   1894   -801   -407       C  
ATOM    996  O   PHE B  41      25.302  49.383 121.799  1.00 58.49           O  
ANISOU  996  O   PHE B  41     7837   7253   7133   1867   -680   -356       O  
ATOM    997  CB  PHE B  41      28.092  49.681 123.372  1.00 58.98           C  
ANISOU  997  CB  PHE B  41     8109   7180   7122   1912   -898   -517       C  
ATOM    998  CG  PHE B  41      29.084  50.169 124.367  1.00 61.00           C  
ANISOU  998  CG  PHE B  41     8472   7361   7344   1988  -1010   -626       C  
ATOM    999  CD1 PHE B  41      28.774  50.200 125.713  1.00 64.82           C  
ANISOU  999  CD1 PHE B  41     9069   7834   7724   2159   -986   -707       C  
ATOM   1000  CD2 PHE B  41      30.350  50.548 123.966  1.00 59.19           C  
ANISOU 1000  CD2 PHE B  41     8226   7080   7184   1892  -1140   -651       C  
ATOM   1001  CE1 PHE B  41      29.699  50.636 126.640  1.00 64.25           C  
ANISOU 1001  CE1 PHE B  41     9094   7703   7616   2242  -1101   -823       C  
ATOM   1002  CE2 PHE B  41      31.286  50.982 124.890  1.00 59.81           C  
ANISOU 1002  CE2 PHE B  41     8392   7096   7239   1960  -1252   -769       C  
ATOM   1003  CZ  PHE B  41      30.961  51.025 126.229  1.00 65.00           C  
ANISOU 1003  CZ  PHE B  41     9164   7745   7790   2139  -1239   -860       C  
ATOM   1004  N   TYR B  42      26.262  51.360 121.338  1.00 59.42           N  
ANISOU 1004  N   TYR B  42     7991   7209   7378   1842   -900   -384       N  
ATOM   1005  CA  TYR B  42      25.845  51.327 119.947  1.00 57.63           C  
ANISOU 1005  CA  TYR B  42     7642   7033   7222   1742   -878   -290       C  
ATOM   1006  C   TYR B  42      26.915  50.590 119.152  1.00 53.63           C  
ANISOU 1006  C   TYR B  42     7079   6565   6733   1602   -904   -245       C  
ATOM   1007  O   TYR B  42      28.107  50.684 119.463  1.00 53.37           O  
ANISOU 1007  O   TYR B  42     7097   6478   6704   1569   -986   -284       O  
ATOM   1008  CB  TYR B  42      25.650  52.745 119.405  1.00 60.04           C  
ANISOU 1008  CB  TYR B  42     7944   7248   7620   1756   -963   -270       C  
ATOM   1009  CG  TYR B  42      24.654  53.587 120.181  1.00 64.10           C  
ANISOU 1009  CG  TYR B  42     8522   7717   8117   1906   -953   -319       C  
ATOM   1010  CD1 TYR B  42      23.284  53.490 119.948  1.00 68.45           C  
ANISOU 1010  CD1 TYR B  42     9011   8348   8650   1966   -860   -288       C  
ATOM   1011  CD2 TYR B  42      25.088  54.490 121.143  1.00 66.49           C  
ANISOU 1011  CD2 TYR B  42     8942   7899   8423   1992  -1042   -405       C  
ATOM   1012  CE1 TYR B  42      22.378  54.269 120.658  1.00 69.28           C  
ANISOU 1012  CE1 TYR B  42     9171   8419   8732   2112   -850   -332       C  
ATOM   1013  CE2 TYR B  42      24.194  55.267 121.855  1.00 71.64           C  
ANISOU 1013  CE2 TYR B  42     9658   8511   9052   2140  -1038   -453       C  
ATOM   1014  CZ  TYR B  42      22.842  55.155 121.608  1.00 75.00           C  
ANISOU 1014  CZ  TYR B  42    10022   9021   9452   2201   -939   -412       C  
ATOM   1015  OH  TYR B  42      21.959  55.931 122.324  1.00 81.79           O  
ANISOU 1015  OH  TYR B  42    10944   9849  10283   2357   -934   -460       O  
ATOM   1016  N   SER B  43      26.487  49.830 118.142  1.00 50.84           N  
ANISOU 1016  N   SER B  43     6617   6312   6388   1525   -836   -172       N  
ATOM   1017  CA  SER B  43      27.399  49.030 117.337  1.00 47.27           C  
ANISOU 1017  CA  SER B  43     6107   5913   5941   1402   -850   -127       C  
ATOM   1018  C   SER B  43      27.143  49.247 115.852  1.00 46.65           C  
ANISOU 1018  C   SER B  43     5913   5879   5931   1327   -862    -39       C  
ATOM   1019  O   SER B  43      25.993  49.311 115.411  1.00 43.16           O  
ANISOU 1019  O   SER B  43     5408   5491   5501   1360   -806    -14       O  
ATOM   1020  CB  SER B  43      27.274  47.539 117.684  1.00 45.25           C  
ANISOU 1020  CB  SER B  43     5845   5748   5601   1390   -745   -137       C  
ATOM   1021  OG  SER B  43      25.938  47.076 117.562  1.00 48.12           O  
ANISOU 1021  OG  SER B  43     6147   6182   5955   1420   -634   -121       O  
ATOM   1022  N   LYS B  44      28.223  49.336 115.077  1.00 42.56           N  
ANISOU 1022  N   LYS B  44     5366   5350   5454   1232   -932      5       N  
ATOM   1023  CA  LYS B  44      28.140  49.380 113.626  1.00 40.46           C  
ANISOU 1023  CA  LYS B  44     4994   5143   5235   1165   -939     96       C  
ATOM   1024  C   LYS B  44      29.033  48.293 113.069  1.00 39.76           C  
ANISOU 1024  C   LYS B  44     4858   5133   5115   1069   -935    124       C  
ATOM   1025  O   LYS B  44      30.183  48.128 113.507  1.00 37.25           O  
ANISOU 1025  O   LYS B  44     4589   4779   4784   1031   -983     97       O  
ATOM   1026  CB  LYS B  44      28.589  50.721 113.045  1.00 43.41           C  
ANISOU 1026  CB  LYS B  44     5374   5421   5699   1151  -1025    146       C  
ATOM   1027  CG  LYS B  44      27.626  51.881 113.200  1.00 45.86           C  
ANISOU 1027  CG  LYS B  44     5715   5661   6049   1245  -1032    142       C  
ATOM   1028  CD  LYS B  44      28.312  53.169 112.813  1.00 50.78           C  
ANISOU 1028  CD  LYS B  44     6370   6157   6767   1222  -1118    185       C  
ATOM   1029  CE  LYS B  44      27.370  54.326 112.925  1.00 54.65           C  
ANISOU 1029  CE  LYS B  44     6900   6572   7295   1323  -1126    185       C  
ATOM   1030  NZ  LYS B  44      28.082  55.625 112.796  1.00 60.16           N  
ANISOU 1030  NZ  LYS B  44     7655   7111   8094   1304  -1207    210       N  
ATOM   1031  N   TRP B  45      28.514  47.585 112.076  1.00 34.50           N  
ANISOU 1031  N   TRP B  45     4094   4577   4438   1036   -887    173       N  
ATOM   1032  CA  TRP B  45      29.200  46.450 111.486  1.00 34.55           C  
ANISOU 1032  CA  TRP B  45     4051   4671   4407    956   -876    196       C  
ATOM   1033  C   TRP B  45      29.902  46.894 110.212  1.00 32.15           C  
ANISOU 1033  C   TRP B  45     3682   4385   4147    896   -939    284       C  
ATOM   1034  O   TRP B  45      29.348  47.668 109.432  1.00 32.74           O  
ANISOU 1034  O   TRP B  45     3710   4461   4270    922   -952    338       O  
ATOM   1035  CB  TRP B  45      28.217  45.318 111.191  1.00 34.00           C  
ANISOU 1035  CB  TRP B  45     3911   4709   4298    957   -785    185       C  
ATOM   1036  CG  TRP B  45      27.642  44.718 112.423  1.00 35.48           C  
ANISOU 1036  CG  TRP B  45     4160   4882   4439   1005   -704    113       C  
ATOM   1037  CD1 TRP B  45      26.471  45.049 113.042  1.00 36.10           C  
ANISOU 1037  CD1 TRP B  45     4249   4943   4524   1082   -646     78       C  
ATOM   1038  CD2 TRP B  45      28.239  43.684 113.217  1.00 32.94           C  
ANISOU 1038  CD2 TRP B  45     3905   4561   4050    991   -664     73       C  
ATOM   1039  NE1 TRP B  45      26.289  44.265 114.158  1.00 37.52           N  
ANISOU 1039  NE1 TRP B  45     4495   5114   4648   1113   -564     25       N  
ATOM   1040  CE2 TRP B  45      27.367  43.431 114.297  1.00 36.69           C  
ANISOU 1040  CE2 TRP B  45     4431   5016   4494   1062   -575     21       C  
ATOM   1041  CE3 TRP B  45      29.428  42.958 113.123  1.00 34.49           C  
ANISOU 1041  CE3 TRP B  45     4124   4776   4203    934   -693     77       C  
ATOM   1042  CZ2 TRP B  45      27.640  42.463 115.267  1.00 35.19           C  
ANISOU 1042  CZ2 TRP B  45     4321   4818   4231   1080   -507    -18       C  
ATOM   1043  CZ3 TRP B  45      29.705  42.000 114.096  1.00 36.01           C  
ANISOU 1043  CZ3 TRP B  45     4397   4964   4321    955   -635     30       C  
ATOM   1044  CH2 TRP B  45      28.810  41.768 115.155  1.00 32.04           C  
ANISOU 1044  CH2 TRP B  45     3951   4434   3787   1029   -540    -14       C  
ATOM   1045  N   TYR B  46      31.129  46.411 110.013  1.00 32.78           N  
ANISOU 1045  N   TYR B  46     3762   4484   4210    827   -975    300       N  
ATOM   1046  CA  TYR B  46      31.945  46.865 108.894  1.00 30.85           C  
ANISOU 1046  CA  TYR B  46     3462   4252   4008    771  -1029    388       C  
ATOM   1047  C   TYR B  46      32.695  45.695 108.298  1.00 31.51           C  
ANISOU 1047  C   TYR B  46     3496   4441   4035    710  -1024    409       C  
ATOM   1048  O   TYR B  46      33.022  44.737 108.991  1.00 26.77           O  
ANISOU 1048  O   TYR B  46     2935   3865   3373    700  -1002    348       O  
ATOM   1049  CB  TYR B  46      33.012  47.887 109.301  1.00 32.28           C  
ANISOU 1049  CB  TYR B  46     3698   4313   4255    742  -1103    391       C  
ATOM   1050  CG  TYR B  46      32.526  49.199 109.863  1.00 35.95           C  
ANISOU 1050  CG  TYR B  46     4222   4648   4789    797  -1128    371       C  
ATOM   1051  CD1 TYR B  46      32.286  49.340 111.223  1.00 35.34           C  
ANISOU 1051  CD1 TYR B  46     4236   4498   4695    853  -1131    270       C  
ATOM   1052  CD2 TYR B  46      32.351  50.313 109.042  1.00 39.27           C  
ANISOU 1052  CD2 TYR B  46     4616   5015   5288    802  -1150    455       C  
ATOM   1053  CE1 TYR B  46      31.858  50.541 111.753  1.00 39.18           C  
ANISOU 1053  CE1 TYR B  46     4783   4865   5241    911  -1160    245       C  
ATOM   1054  CE2 TYR B  46      31.922  51.525 109.566  1.00 40.42           C  
ANISOU 1054  CE2 TYR B  46     4827   5032   5499    857  -1175    434       C  
ATOM   1055  CZ  TYR B  46      31.685  51.631 110.922  1.00 41.05           C  
ANISOU 1055  CZ  TYR B  46     4994   5043   5561    909  -1185    325       C  
ATOM   1056  OH  TYR B  46      31.256  52.820 111.450  1.00 46.18           O  
ANISOU 1056  OH  TYR B  46     5711   5564   6270    972  -1215    297       O  
ATOM   1057  N   ILE B  47      33.063  45.844 107.028  1.00 31.79           N  
ANISOU 1057  N   ILE B  47     3454   4535   4089    677  -1046    500       N  
ATOM   1058  CA  ILE B  47      34.144  45.068 106.436  1.00 28.03           C  
ANISOU 1058  CA  ILE B  47     2940   4139   3573    617  -1065    534       C  
ATOM   1059  C   ILE B  47      35.367  45.972 106.365  1.00 29.35           C  
ANISOU 1059  C   ILE B  47     3116   4232   3802    569  -1126    582       C  
ATOM   1060  O   ILE B  47      35.322  47.053 105.765  1.00 29.83           O  
ANISOU 1060  O   ILE B  47     3156   4241   3937    571  -1144    659       O  
ATOM   1061  CB  ILE B  47      33.787  44.540 105.036  1.00 26.72           C  
ANISOU 1061  CB  ILE B  47     2675   4102   3376    622  -1048    601       C  
ATOM   1062  CG1 ILE B  47      32.553  43.649 105.096  1.00 24.93           C  
ANISOU 1062  CG1 ILE B  47     2423   3944   3106    660   -990    539       C  
ATOM   1063  CG2 ILE B  47      34.980  43.760 104.478  1.00 24.37           C  
ANISOU 1063  CG2 ILE B  47     2343   3886   3029    568  -1070    634       C  
ATOM   1064  CD1 ILE B  47      32.832  42.337 105.774  1.00 25.66           C  
ANISOU 1064  CD1 ILE B  47     2551   4067   3132    633   -958    465       C  
ATOM   1065  N   ARG B  48      36.468  45.537 106.955  1.00 29.56           N  
ANISOU 1065  N   ARG B  48     3174   4253   3805    526  -1156    539       N  
ATOM   1066  CA  ARG B  48      37.734  46.218 106.747  1.00 28.79           C  
ANISOU 1066  CA  ARG B  48     3059   4109   3770    465  -1212    584       C  
ATOM   1067  C   ARG B  48      38.404  45.578 105.539  1.00 28.81           C  
ANISOU 1067  C   ARG B  48     2976   4238   3733    426  -1208    670       C  
ATOM   1068  O   ARG B  48      38.861  44.432 105.611  1.00 28.85           O  
ANISOU 1068  O   ARG B  48     2975   4333   3652    416  -1203    634       O  
ATOM   1069  CB  ARG B  48      38.612  46.131 107.984  1.00 31.43           C  
ANISOU 1069  CB  ARG B  48     3459   4384   4099    447  -1256    484       C  
ATOM   1070  CG  ARG B  48      40.050  46.626 107.732  1.00 35.69           C  
ANISOU 1070  CG  ARG B  48     3957   4900   4702    371  -1315    518       C  
ATOM   1071  CD  ARG B  48      40.120  48.147 107.681  1.00 34.71           C  
ANISOU 1071  CD  ARG B  48     3835   4636   4718    344  -1347    556       C  
ATOM   1072  NE  ARG B  48      40.121  48.679 109.042  1.00 44.82           N  
ANISOU 1072  NE  ARG B  48     5200   5795   6033    370  -1392    435       N  
ATOM   1073  CZ  ARG B  48      40.204  49.972 109.346  1.00 44.20           C  
ANISOU 1073  CZ  ARG B  48     5147   5569   6077    354  -1433    426       C  
ATOM   1074  NH1 ARG B  48      40.294  50.882 108.377  1.00 42.05           N  
ANISOU 1074  NH1 ARG B  48     4825   5244   5908    309  -1425    542       N  
ATOM   1075  NH2 ARG B  48      40.189  50.353 110.622  1.00 41.83           N  
ANISOU 1075  NH2 ARG B  48     4929   5172   5793    392  -1481    301       N  
ATOM   1076  N   VAL B  49      38.510  46.342 104.451  1.00 27.04           N  
ANISOU 1076  N   VAL B  49     2691   4015   3568    412  -1209    785       N  
ATOM   1077  CA  VAL B  49      39.025  45.815 103.193  1.00 28.22           C  
ANISOU 1077  CA  VAL B  49     2757   4292   3674    396  -1199    879       C  
ATOM   1078  C   VAL B  49      40.400  45.204 103.388  1.00 32.72           C  
ANISOU 1078  C   VAL B  49     3311   4910   4212    338  -1230    860       C  
ATOM   1079  O   VAL B  49      41.290  45.801 104.015  1.00 35.33           O  
ANISOU 1079  O   VAL B  49     3659   5154   4610    286  -1268    836       O  
ATOM   1080  CB  VAL B  49      39.037  46.925 102.132  1.00 34.34           C  
ANISOU 1080  CB  VAL B  49     3485   5038   4525    399  -1190   1015       C  
ATOM   1081  CG1 VAL B  49      39.718  46.452 100.844  1.00 31.95           C  
ANISOU 1081  CG1 VAL B  49     3096   4870   4173    390  -1179   1121       C  
ATOM   1082  CG2 VAL B  49      37.626  47.317 101.845  1.00 33.50           C  
ANISOU 1082  CG2 VAL B  49     3388   4920   4421    477  -1161   1027       C  
ATOM   1083  N   GLY B  50      40.561  43.975 102.885  1.00 29.51           N  
ANISOU 1083  N   GLY B  50     2871   4642   3700    351  -1216    859       N  
ATOM   1084  CA  GLY B  50      41.799  43.218 102.960  1.00 32.20           C  
ANISOU 1084  CA  GLY B  50     3208   5039   3986    312  -1226    824       C  
ATOM   1085  C   GLY B  50      42.254  42.892 104.360  1.00 31.26           C  
ANISOU 1085  C   GLY B  50     3150   4880   3846    302  -1270    718       C  
ATOM   1086  O   GLY B  50      43.350  42.363 104.557  1.00 30.41           O  
ANISOU 1086  O   GLY B  50     3039   4818   3697    277  -1292    684       O  
ATOM   1087  N   ALA B  51      41.407  43.167 105.347  1.00 27.66           N  
ANISOU 1087  N   ALA B  51     2772   4328   3412    334  -1260    638       N  
ATOM   1088  CA  ALA B  51      41.817  43.090 106.745  1.00 26.08           C  
ANISOU 1088  CA  ALA B  51     2652   4058   3199    341  -1291    522       C  
ATOM   1089  C   ALA B  51      43.034  43.970 107.013  1.00 31.59           C  
ANISOU 1089  C   ALA B  51     3327   4694   3984    283  -1356    519       C  
ATOM   1090  O   ALA B  51      43.757  43.762 107.990  1.00 31.62           O  
ANISOU 1090  O   ALA B  51     3373   4678   3962    286  -1398    423       O  
ATOM   1091  CB  ALA B  51      42.090  41.641 107.172  1.00 29.12           C  
ANISOU 1091  CB  ALA B  51     3076   4533   3454    371  -1275    454       C  
ATOM   1092  N   ARG B  52      43.280  44.950 106.151  1.00 31.36           N  
ANISOU 1092  N   ARG B  52     3227   4630   4056    232  -1362    622       N  
ATOM   1093  CA  ARG B  52      44.388  45.888 106.314  1.00 36.76           C  
ANISOU 1093  CA  ARG B  52     3876   5239   4853    161  -1416    626       C  
ATOM   1094  C   ARG B  52      43.923  47.112 107.100  1.00 35.77           C  
ANISOU 1094  C   ARG B  52     3809   4942   4841    162  -1442    577       C  
ATOM   1095  O   ARG B  52      43.024  47.825 106.655  1.00 38.93           O  
ANISOU 1095  O   ARG B  52     4216   5278   5296    180  -1409    644       O  
ATOM   1096  CB  ARG B  52      44.940  46.296 104.947  1.00 38.92           C  
ANISOU 1096  CB  ARG B  52     4045   5559   5184    105  -1395    776       C  
ATOM   1097  CG  ARG B  52      46.239  47.097 105.044  1.00 42.08           C  
ANISOU 1097  CG  ARG B  52     4387   5898   5704     15  -1440    785       C  
ATOM   1098  CD  ARG B  52      46.952  47.214 103.689  1.00 46.75           C  
ANISOU 1098  CD  ARG B  52     4868   6570   6324    -35  -1406    938       C  
ATOM   1099  NE  ARG B  52      48.361  47.609 103.826  1.00 51.61           N  
ANISOU 1099  NE  ARG B  52     5410   7169   7031   -125  -1445    931       N  
ATOM   1100  CZ  ARG B  52      49.118  48.046 102.820  1.00 54.89           C  
ANISOU 1100  CZ  ARG B  52     5724   7612   7519   -188  -1413   1064       C  
ATOM   1101  NH1 ARG B  52      48.604  48.162 101.599  1.00 52.64           N  
ANISOU 1101  NH1 ARG B  52     5411   7375   7216   -157  -1344   1218       N  
ATOM   1102  NH2 ARG B  52      50.381  48.384 103.030  1.00 59.02           N  
ANISOU 1102  NH2 ARG B  52     6172   8119   8134   -276  -1448   1043       N  
ATOM   1103  N   LYS B  53      44.545  47.374 108.257  1.00 35.94           N  
ANISOU 1103  N   LYS B  53     3872   4890   4894    153  -1506    456       N  
ATOM   1104  CA  LYS B  53      44.066  48.463 109.105  1.00 41.24           C  
ANISOU 1104  CA  LYS B  53     4611   5399   5661    170  -1538    388       C  
ATOM   1105  C   LYS B  53      44.140  49.835 108.436  1.00 43.98           C  
ANISOU 1105  C   LYS B  53     4913   5625   6171    105  -1540    484       C  
ATOM   1106  O   LYS B  53      43.376  50.729 108.812  1.00 44.67           O  
ANISOU 1106  O   LYS B  53     5060   5584   6328    135  -1543    465       O  
ATOM   1107  CB  LYS B  53      44.794  48.497 110.451  1.00 41.49           C  
ANISOU 1107  CB  LYS B  53     4691   5381   5692    182  -1618    229       C  
ATOM   1108  CG  LYS B  53      44.524  47.279 111.308  1.00 43.82           C  
ANISOU 1108  CG  LYS B  53     5064   5764   5824    273  -1606    131       C  
ATOM   1109  CD  LYS B  53      45.256  47.315 112.652  1.00 48.20           C  
ANISOU 1109  CD  LYS B  53     5672   6280   6361    309  -1688    -30       C  
ATOM   1110  CE  LYS B  53      46.755  47.100 112.552  1.00 45.79           C  
ANISOU 1110  CE  LYS B  53     5288   6040   6071    246  -1752    -60       C  
ATOM   1111  NZ  LYS B  53      47.320  46.931 113.926  1.00 54.74           N  
ANISOU 1111  NZ  LYS B  53     6486   7163   7151    315  -1830   -233       N  
ATOM   1112  N   SER B  54      45.025  50.023 107.460  1.00 45.47           N  
ANISOU 1112  N   SER B  54     5004   5850   6422     22  -1530    590       N  
ATOM   1113  CA  SER B  54      45.121  51.282 106.730  1.00 44.99           C  
ANISOU 1113  CA  SER B  54     4902   5674   6518    -40  -1513    703       C  
ATOM   1114  C   SER B  54      44.167  51.343 105.548  1.00 48.13           C  
ANISOU 1114  C   SER B  54     5288   6115   6884      5  -1433    853       C  
ATOM   1115  O   SER B  54      44.167  52.336 104.815  1.00 51.87           O  
ANISOU 1115  O   SER B  54     5736   6504   7470    -28  -1402    969       O  
ATOM   1116  CB  SER B  54      46.559  51.505 106.250  1.00 53.19           C  
ANISOU 1116  CB  SER B  54     5835   6728   7648   -149  -1530    753       C  
ATOM   1117  OG  SER B  54      47.014  50.409 105.468  1.00 48.08           O  
ANISOU 1117  OG  SER B  54     5118   6266   6884   -148  -1496    820       O  
ATOM   1118  N   ALA B  55      43.358  50.313 105.350  1.00 44.39           N  
ANISOU 1118  N   ALA B  55     4832   5770   6264     83  -1398    849       N  
ATOM   1119  CA  ALA B  55      42.439  50.224 104.224  1.00 42.67           C  
ANISOU 1119  CA  ALA B  55     4593   5621   5998    138  -1332    970       C  
ATOM   1120  C   ALA B  55      41.061  50.726 104.628  1.00 41.22           C  
ANISOU 1120  C   ALA B  55     4487   5354   5820    216  -1318    936       C  
ATOM   1121  O   ALA B  55      40.792  50.985 105.799  1.00 42.38           O  
ANISOU 1121  O   ALA B  55     4709   5406   5988    235  -1354    817       O  
ATOM   1122  CB  ALA B  55      42.383  48.781 103.730  1.00 41.82           C  
ANISOU 1122  CB  ALA B  55     4448   5703   5737    172  -1307    974       C  
ATOM   1123  N   PRO B  56      40.158  50.913 103.668  1.00 41.23           N  
ANISOU 1123  N   PRO B  56     4471   5393   5800    275  -1267   1037       N  
ATOM   1124  CA  PRO B  56      38.822  51.425 104.008  1.00 43.52           C  
ANISOU 1124  CA  PRO B  56     4827   5615   6095    357  -1254   1006       C  
ATOM   1125  C   PRO B  56      38.000  50.477 104.877  1.00 39.89           C  
ANISOU 1125  C   PRO B  56     4411   5215   5530    415  -1252    878       C  
ATOM   1126  O   PRO B  56      38.087  49.249 104.773  1.00 36.15           O  
ANISOU 1126  O   PRO B  56     3907   4874   4953    417  -1238    849       O  
ATOM   1127  CB  PRO B  56      38.157  51.615 102.636  1.00 44.30           C  
ANISOU 1127  CB  PRO B  56     4877   5785   6169    415  -1201   1143       C  
ATOM   1128  CG  PRO B  56      39.046  50.882 101.652  1.00 45.17           C  
ANISOU 1128  CG  PRO B  56     4902   6034   6228    376  -1186   1228       C  
ATOM   1129  CD  PRO B  56      40.410  51.012 102.221  1.00 42.92           C  
ANISOU 1129  CD  PRO B  56     4609   5686   6013    272  -1224   1196       C  
ATOM   1130  N   LEU B  57      37.193  51.085 105.744  1.00 38.69           N  
ANISOU 1130  N   LEU B  57     4334   4957   5410    466  -1260    805       N  
ATOM   1131  CA  LEU B  57      36.134  50.422 106.492  1.00 37.05           C  
ANISOU 1131  CA  LEU B  57     4169   4790   5117    538  -1238    707       C  
ATOM   1132  C   LEU B  57      34.817  50.620 105.758  1.00 37.49           C  
ANISOU 1132  C   LEU B  57     4202   4890   5153    618  -1192    763       C  
ATOM   1133  O   LEU B  57      34.295  51.733 105.722  1.00 41.87           O  
ANISOU 1133  O   LEU B  57     4790   5344   5776    659  -1196    793       O  
ATOM   1134  CB  LEU B  57      36.000  51.011 107.893  1.00 40.31           C  
ANISOU 1134  CB  LEU B  57     4678   5069   5570    564  -1274    593       C  
ATOM   1135  CG  LEU B  57      36.635  50.443 109.146  1.00 42.65           C  
ANISOU 1135  CG  LEU B  57     5028   5352   5826    552  -1309    467       C  
ATOM   1136  CD1 LEU B  57      36.046  51.183 110.334  1.00 44.35           C  
ANISOU 1136  CD1 LEU B  57     5337   5443   6070    620  -1332    370       C  
ATOM   1137  CD2 LEU B  57      36.382  48.954 109.264  1.00 39.71           C  
ANISOU 1137  CD2 LEU B  57     4642   5120   5324    572  -1263    429       C  
ATOM   1138  N   ILE B  58      34.241  49.538 105.259  1.00 34.05           N  
ANISOU 1138  N   ILE B  58     3714   4601   4624    645  -1153    761       N  
ATOM   1139  CA  ILE B  58      32.993  49.580 104.503  1.00 38.41           C  
ANISOU 1139  CA  ILE B  58     4224   5222   5149    723  -1115    799       C  
ATOM   1140  C   ILE B  58      31.838  49.261 105.448  1.00 36.73           C  
ANISOU 1140  C   ILE B  58     4048   5006   4902    783  -1086    691       C  
ATOM   1141  O   ILE B  58      31.763  48.151 105.987  1.00 34.61           O  
ANISOU 1141  O   ILE B  58     3780   4800   4570    768  -1062    615       O  
ATOM   1142  CB  ILE B  58      33.032  48.595 103.324  1.00 38.81           C  
ANISOU 1142  CB  ILE B  58     4182   5439   5127    720  -1095    852       C  
ATOM   1143  CG1 ILE B  58      34.265  48.843 102.449  1.00 40.11           C  
ANISOU 1143  CG1 ILE B  58     4309   5616   5316    664  -1116    962       C  
ATOM   1144  CG2 ILE B  58      31.750  48.680 102.501  1.00 41.14           C  
ANISOU 1144  CG2 ILE B  58     4422   5814   5394    810  -1067    879       C  
ATOM   1145  CD1 ILE B  58      34.464  50.298 102.054  1.00 40.08           C  
ANISOU 1145  CD1 ILE B  58     4326   5495   5408    673  -1124   1062       C  
ATOM   1146  N   GLU B  59      30.917  50.205 105.638  1.00 35.77           N  
ANISOU 1146  N   GLU B  59     3958   4814   4819    855  -1081    689       N  
ATOM   1147  CA  GLU B  59      29.830  49.982 106.587  1.00 35.18           C  
ANISOU 1147  CA  GLU B  59     3916   4735   4715    917  -1048    591       C  
ATOM   1148  C   GLU B  59      28.766  49.075 105.991  1.00 37.53           C  
ANISOU 1148  C   GLU B  59     4127   5180   4952    955   -998    577       C  
ATOM   1149  O   GLU B  59      28.323  49.281 104.861  1.00 35.78           O  
ANISOU 1149  O   GLU B  59     3837   5031   4729    993   -997    642       O  
ATOM   1150  CB  GLU B  59      29.169  51.287 107.004  1.00 40.37           C  
ANISOU 1150  CB  GLU B  59     4634   5275   5430    992  -1062    587       C  
ATOM   1151  CG  GLU B  59      28.179  51.077 108.126  1.00 39.40           C  
ANISOU 1151  CG  GLU B  59     4553   5143   5274   1057  -1026    483       C  
ATOM   1152  CD  GLU B  59      27.694  52.373 108.753  1.00 47.88           C  
ANISOU 1152  CD  GLU B  59     5706   6086   6399   1135  -1049    463       C  
ATOM   1153  OE1 GLU B  59      28.026  53.464 108.239  1.00 52.59           O  
ANISOU 1153  OE1 GLU B  59     6325   6593   7064   1139  -1090    534       O  
ATOM   1154  OE2 GLU B  59      26.974  52.295 109.770  1.00 51.07           O  
ANISOU 1154  OE2 GLU B  59     6155   6474   6776   1196  -1022    378       O  
ATOM   1155  N   LEU B  60      28.343  48.080 106.756  1.00 35.53           N  
ANISOU 1155  N   LEU B  60     3878   4970   4652    950   -953    488       N  
ATOM   1156  CA  LEU B  60      27.302  47.160 106.324  1.00 37.08           C  
ANISOU 1156  CA  LEU B  60     3988   5294   4808    974   -900    455       C  
ATOM   1157  C   LEU B  60      25.964  47.613 106.893  1.00 39.01           C  
ANISOU 1157  C   LEU B  60     4237   5520   5066   1058   -862    403       C  
ATOM   1158  O   LEU B  60      25.918  48.336 107.893  1.00 38.59           O  
ANISOU 1158  O   LEU B  60     4271   5357   5033   1094   -866    372       O  
ATOM   1159  CB  LEU B  60      27.599  45.719 106.786  1.00 33.88           C  
ANISOU 1159  CB  LEU B  60     3580   4942   4352    914   -859    394       C  
ATOM   1160  CG  LEU B  60      28.947  45.079 106.408  1.00 33.54           C  
ANISOU 1160  CG  LEU B  60     3539   4925   4279    836   -892    428       C  
ATOM   1161  CD1 LEU B  60      29.100  43.660 106.975  1.00 29.52           C  
ANISOU 1161  CD1 LEU B  60     3044   4459   3714    795   -843    361       C  
ATOM   1162  CD2 LEU B  60      29.193  45.123 104.901  1.00 31.70           C  
ANISOU 1162  CD2 LEU B  60     3217   4783   4043    828   -927    512       C  
ATOM   1163  N   CYS B  61      24.876  47.220 106.224  1.00 39.46           N  
ANISOU 1163  N   CYS B  61     4193   5690   5111   1098   -829    388       N  
ATOM   1164  CA  CYS B  61      23.519  47.475 106.720  1.00 41.86           C  
ANISOU 1164  CA  CYS B  61     4476   6005   5425   1177   -782    330       C  
ATOM   1165  C   CYS B  61      23.202  48.962 106.856  1.00 48.80           C  
ANISOU 1165  C   CYS B  61     5411   6794   6336   1264   -818    362       C  
ATOM   1166  O   CYS B  61      22.648  49.411 107.859  1.00 52.12           O  
ANISOU 1166  O   CYS B  61     5889   7149   6764   1319   -793    313       O  
ATOM   1167  CB  CYS B  61      23.291  46.753 108.045  1.00 41.89           C  
ANISOU 1167  CB  CYS B  61     4529   5976   5411   1158   -714    247       C  
ATOM   1168  SG  CYS B  61      23.138  44.992 107.768  1.00 47.60           S  
ANISOU 1168  SG  CYS B  61     5163   6815   6106   1078   -649    200       S  
ATOM   1169  N   VAL B  62      23.568  49.736 105.845  1.00 47.65           N  
ANISOU 1169  N   VAL B  62     5255   6642   6208   1285   -872    449       N  
ATOM   1170  CA  VAL B  62      23.132  51.127 105.771  1.00 52.12           C  
ANISOU 1170  CA  VAL B  62     5866   7131   6805   1380   -899    488       C  
ATOM   1171  C   VAL B  62      21.706  51.164 105.224  1.00 58.03           C  
ANISOU 1171  C   VAL B  62     6520   7996   7534   1481   -874    463       C  
ATOM   1172  O   VAL B  62      21.441  50.672 104.121  1.00 59.86           O  
ANISOU 1172  O   VAL B  62     6647   8359   7740   1490   -878    483       O  
ATOM   1173  CB  VAL B  62      24.093  51.964 104.913  1.00 52.11           C  
ANISOU 1173  CB  VAL B  62     5898   7066   6836   1365   -954    602       C  
ATOM   1174  CG1 VAL B  62      23.515  53.354 104.668  1.00 60.99           C  
ANISOU 1174  CG1 VAL B  62     7064   8118   7990   1476   -974    651       C  
ATOM   1175  CG2 VAL B  62      25.422  52.082 105.604  1.00 45.90           C  
ANISOU 1175  CG2 VAL B  62     5201   6153   6084   1271   -982    610       C  
ATOM   1176  N   ASP B  63      20.783  51.725 106.016  1.00 64.49           N  
ANISOU 1176  N   ASP B  63     7370   8776   8360   1564   -851    410       N  
ATOM   1177  CA  ASP B  63      19.364  51.745 105.652  1.00 64.59           C  
ANISOU 1177  CA  ASP B  63     7284   8905   8354   1665   -824    368       C  
ATOM   1178  C   ASP B  63      19.114  52.588 104.406  1.00 69.28           C  
ANISOU 1178  C   ASP B  63     7845   9540   8940   1759   -870    447       C  
ATOM   1179  O   ASP B  63      18.429  52.149 103.476  1.00 65.71           O  
ANISOU 1179  O   ASP B  63     7270   9238   8458   1802   -868    433       O  
ATOM   1180  CB  ASP B  63      18.531  52.267 106.826  1.00 67.15           C  
ANISOU 1180  CB  ASP B  63     7661   9169   8683   1742   -790    303       C  
ATOM   1181  N   GLU B  64      19.652  53.805 104.377  1.00 67.52           N  
ANISOU 1181  N   GLU B  64     7731   9181   8744   1797   -910    526       N  
ATOM   1182  CA  GLU B  64      19.477  54.721 103.254  1.00 71.83           C  
ANISOU 1182  CA  GLU B  64     8272   9740   9280   1898   -944    618       C  
ATOM   1183  C   GLU B  64      20.567  55.787 103.326  1.00 70.05           C  
ANISOU 1183  C   GLU B  64     8180   9329   9108   1872   -978    715       C  
ATOM   1184  O   GLU B  64      21.482  55.707 104.153  1.00 69.50           O  
ANISOU 1184  O   GLU B  64     8185   9142   9078   1769   -986    700       O  
ATOM   1185  CB  GLU B  64      18.074  55.339 103.262  1.00 72.23           C  
ANISOU 1185  CB  GLU B  64     8292   9845   9307   2054   -935    576       C  
ATOM   1186  N   ALA B  65      20.457  56.795 102.463  1.00 83.91           N  
ANISOU 1186  N   ALA B  65     9395   9428  13061    796   -301    197       N  
ATOM   1187  CA  ALA B  65      21.424  57.893 102.374  1.00 83.10           C  
ANISOU 1187  CA  ALA B  65     9312   9200  13061    848   -303    468       C  
ATOM   1188  C   ALA B  65      22.816  57.361 102.076  1.00 77.64           C  
ANISOU 1188  C   ALA B  65     8684   8546  12270    830   -406    613       C  
ATOM   1189  O   ALA B  65      23.048  56.780 101.015  1.00 81.07           O  
ANISOU 1189  O   ALA B  65     8996   9226  12580    975   -485    677       O  
ATOM   1190  CB  ALA B  65      21.433  58.720 103.654  1.00 80.94           C  
ANISOU 1190  CB  ALA B  65     9205   8603  12946    672   -213    443       C  
ATOM   1191  N   SER B  69      27.015  55.771 106.756  1.00 67.95           N  
ANISOU 1191  N   SER B  69     8443   6361  11015   -195   -489    525       N  
ATOM   1192  CA  SER B  69      25.908  56.728 106.780  1.00 68.74           C  
ANISOU 1192  CA  SER B  69     8456   6421  11243   -119   -394    485       C  
ATOM   1193  C   SER B  69      25.721  57.413 105.417  1.00 70.74           C  
ANISOU 1193  C   SER B  69     8481   6886  11513    163   -409    676       C  
ATOM   1194  O   SER B  69      24.655  57.276 104.813  1.00 72.96           O  
ANISOU 1194  O   SER B  69     8610   7341  11769    294   -387    576       O  
ATOM   1195  CB  SER B  69      26.111  57.770 107.903  1.00 70.29           C  
ANISOU 1195  CB  SER B  69     8802   6304  11602   -272   -315    526       C  
ATOM   1196  OG  SER B  69      25.030  58.689 107.962  1.00 76.15           O  
ANISOU 1196  OG  SER B  69     9465   6998  12469   -203   -217    483       O  
ATOM   1197  N   PRO B  70      26.736  58.141 104.922  1.00 73.72           N  
ANISOU 1197  N   PRO B  70     8828   7253  11929    258   -448    948       N  
ATOM   1198  CA  PRO B  70      26.529  58.864 103.654  1.00 72.54           C  
ANISOU 1198  CA  PRO B  70     8462   7294  11805    527   -457   1132       C  
ATOM   1199  C   PRO B  70      26.485  57.961 102.433  1.00 72.50           C  
ANISOU 1199  C   PRO B  70     8302   7604  11641    697   -542   1138       C  
ATOM   1200  O   PRO B  70      25.732  58.242 101.495  1.00 73.25           O  
ANISOU 1200  O   PRO B  70     8206   7891  11735    899   -531   1164       O  
ATOM   1201  CB  PRO B  70      27.715  59.835 103.611  1.00 66.91           C  
ANISOU 1201  CB  PRO B  70     7790   6455  11177    549   -475   1412       C  
ATOM   1202  CG  PRO B  70      28.787  59.115 104.305  1.00 70.36           C  
ANISOU 1202  CG  PRO B  70     8410   6777  11546    356   -533   1403       C  
ATOM   1203  CD  PRO B  70      28.144  58.238 105.358  1.00 66.85           C  
ANISOU 1203  CD  PRO B  70     8104   6233  11065    143   -498   1108       C  
ATOM   1204  N   ILE B  71      27.274  56.888 102.404  1.00 70.98           N  
ANISOU 1204  N   ILE B  71     8184   7473  11314    623   -625   1118       N  
ATOM   1205  CA  ILE B  71      27.276  55.934 101.297  1.00 67.47           C  
ANISOU 1205  CA  ILE B  71     7609   7320  10708    767   -706   1112       C  
ATOM   1206  C   ILE B  71      26.619  54.636 101.742  1.00 65.20           C  
ANISOU 1206  C   ILE B  71     7383   7083  10306    637   -707    823       C  
ATOM   1207  O   ILE B  71      26.956  54.085 102.799  1.00 58.99           O  
ANISOU 1207  O   ILE B  71     6785   6124   9505    415   -703    700       O  
ATOM   1208  CB  ILE B  71      28.696  55.665 100.768  1.00 63.08           C  
ANISOU 1208  CB  ILE B  71     7070   6822  10073    808   -802   1325       C  
ATOM   1209  CG1 ILE B  71      29.270  56.918 100.113  1.00 70.13           C  
ANISOU 1209  CG1 ILE B  71     7868   7713  11066    974   -806   1618       C  
ATOM   1210  CG2 ILE B  71      28.687  54.529  99.769  1.00 62.27           C  
ANISOU 1210  CG2 ILE B  71     6862   7004   9794    923   -881   1284       C  
ATOM   1211  CD1 ILE B  71      30.683  56.742  99.608  1.00 65.72           C  
ANISOU 1211  CD1 ILE B  71     7327   7202  10441   1016   -897   1841       C  
ATOM   1212  N   GLN B  72      25.693  54.139 100.929  1.00 64.69           N  
ANISOU 1212  N   GLN B  72     7162   7259  10160    774   -715    715       N  
ATOM   1213  CA  GLN B  72      25.067  52.847 101.165  1.00 60.89           C  
ANISOU 1213  CA  GLN B  72     6716   6865   9554    677   -724    450       C  
ATOM   1214  C   GLN B  72      25.783  51.792 100.333  1.00 55.07           C  
ANISOU 1214  C   GLN B  72     5942   6338   8644    745   -824    499       C  
ATOM   1215  O   GLN B  72      25.907  51.931  99.111  1.00 57.84           O  
ANISOU 1215  O   GLN B  72     6125   6907   8945    958   -872    650       O  
ATOM   1216  CB  GLN B  72      23.580  52.871 100.793  1.00 59.00           C  
ANISOU 1216  CB  GLN B  72     6329   6769   9321    777   -670    287       C  
ATOM   1217  CG  GLN B  72      22.923  51.526 100.976  1.00 58.69           C  
ANISOU 1217  CG  GLN B  72     6318   6833   9148    683   -681     15       C  
ATOM   1218  CD  GLN B  72      21.420  51.584 100.942  1.00 64.98           C  
ANISOU 1218  CD  GLN B  72     7009   7708   9972    726   -614   -177       C  
ATOM   1219  OE1 GLN B  72      20.840  52.466 100.324  1.00 70.66           O  
ANISOU 1219  OE1 GLN B  72     7572   8509  10768    896   -582    -84       O  
ATOM   1220  NE2 GLN B  72      20.774  50.633 101.619  1.00 63.69           N  
ANISOU 1220  NE2 GLN B  72     6933   7520   9745    570   -591   -447       N  
ATOM   1221  N   TYR B  73      26.203  50.720 100.987  1.00 50.94           N  
ANISOU 1221  N   TYR B  73     5574   5753   8027    565   -853    364       N  
ATOM   1222  CA  TYR B  73      26.982  49.677 100.336  1.00 51.95           C  
ANISOU 1222  CA  TYR B  73     5696   6049   7993    603   -945    407       C  
ATOM   1223  C   TYR B  73      26.098  48.461 100.211  1.00 51.21           C  
ANISOU 1223  C   TYR B  73     5576   6114   7768    575   -947    147       C  
ATOM   1224  O   TYR B  73      25.587  47.963 101.219  1.00 49.87           O  
ANISOU 1224  O   TYR B  73     5533   5814   7602    388   -902    -80       O  
ATOM   1225  CB  TYR B  73      28.261  49.332 101.105  1.00 46.09           C  
ANISOU 1225  CB  TYR B  73     5150   5128   7235    428   -982    473       C  
ATOM   1226  CG  TYR B  73      29.259  50.446 101.144  1.00 50.05           C  
ANISOU 1226  CG  TYR B  73     5676   5491   7849    458   -991    743       C  
ATOM   1227  CD1 TYR B  73      30.134  50.647 100.083  1.00 53.24           C  
ANISOU 1227  CD1 TYR B  73     5978   6041   8210    633  -1062    992       C  
ATOM   1228  CD2 TYR B  73      29.345  51.293 102.239  1.00 49.10           C  
ANISOU 1228  CD2 TYR B  73     5684   5095   7876    311   -929    753       C  
ATOM   1229  CE1 TYR B  73      31.072  51.674 100.099  1.00 53.09           C  
ANISOU 1229  CE1 TYR B  73     5980   5898   8294    662  -1071   1246       C  
ATOM   1230  CE2 TYR B  73      30.283  52.322 102.271  1.00 54.31           C  
ANISOU 1230  CE2 TYR B  73     6369   5628   8638    336   -937   1004       C  
ATOM   1231  CZ  TYR B  73      31.142  52.507 101.194  1.00 55.13           C  
ANISOU 1231  CZ  TYR B  73     6366   5883   8698    513  -1009   1250       C  
ATOM   1232  OH  TYR B  73      32.072  53.525 101.214  1.00 57.49           O  
ANISOU 1232  OH  TYR B  73     6688   6058   9098    537  -1017   1500       O  
ATOM   1233  N   ILE B  74      25.922  47.983  98.987  1.00 53.17           N  
ANISOU 1233  N   ILE B  74     5662   6641   7899    758   -999    180       N  
ATOM   1234  CA  ILE B  74      25.125  46.793  98.734  1.00 51.89           C  
ANISOU 1234  CA  ILE B  74     5463   6656   7598    747  -1008    -54       C  
ATOM   1235  C   ILE B  74      26.052  45.705  98.224  1.00 48.19           C  
ANISOU 1235  C   ILE B  74     5027   6317   6966    755  -1093    -10       C  
ATOM   1236  O   ILE B  74      26.914  45.958  97.376  1.00 48.77           O  
ANISOU 1236  O   ILE B  74     5028   6490   7012    896  -1152    221       O  
ATOM   1237  CB  ILE B  74      23.987  47.085  97.733  1.00 53.37           C  
ANISOU 1237  CB  ILE B  74     5428   7073   7776    949   -992    -82       C  
ATOM   1238  CG1 ILE B  74      23.128  48.252  98.247  1.00 56.96           C  
ANISOU 1238  CG1 ILE B  74     5851   7386   8404    947   -903   -103       C  
ATOM   1239  CG2 ILE B  74      23.144  45.839  97.488  1.00 51.99           C  
ANISOU 1239  CG2 ILE B  74     5216   7081   7455    929  -1000   -331       C  
ATOM   1240  CD1 ILE B  74      21.919  48.593  97.368  1.00 62.22           C  
ANISOU 1240  CD1 ILE B  74     6302   8264   9075   1135   -877   -141       C  
ATOM   1241  N   ASP B  75      25.760  44.475  98.623  1.00 49.02           N  
ANISOU 1241  N   ASP B  75     5219   6450   6957    624  -1096   -240       N  
ATOM   1242  CA  ASP B  75      26.599  43.325  98.349  1.00 42.45           C  
ANISOU 1242  CA  ASP B  75     4451   5708   5970    593  -1165   -236       C  
ATOM   1243  C   ASP B  75      26.010  42.547  97.191  1.00 42.31           C  
ANISOU 1243  C   ASP B  75     4276   5995   5806    746  -1200   -310       C  
ATOM   1244  O   ASP B  75      24.793  42.385  97.094  1.00 47.31           O  
ANISOU 1244  O   ASP B  75     4827   6722   6427    767  -1160   -495       O  
ATOM   1245  CB  ASP B  75      26.669  42.398  99.562  1.00 41.23           C  
ANISOU 1245  CB  ASP B  75     4503   5385   5777    341  -1144   -450       C  
ATOM   1246  CG  ASP B  75      27.696  41.270  99.390  1.00 41.26           C  
ANISOU 1246  CG  ASP B  75     4595   5449   5634    294  -1213   -423       C  
ATOM   1247  OD1 ASP B  75      28.643  41.420  98.575  1.00 41.40           O  
ANISOU 1247  OD1 ASP B  75     4553   5562   5613    425  -1275   -193       O  
ATOM   1248  OD2 ASP B  75      27.498  40.190 100.004  1.00 40.16           O  
ANISOU 1248  OD2 ASP B  75     4574   5277   5408    138  -1203   -638       O  
ATOM   1249  N   ILE B  76      26.881  42.133  96.280  1.00 42.07           N  
ANISOU 1249  N   ILE B  76     4197   6120   5668    861  -1274   -153       N  
ATOM   1250  CA  ILE B  76      26.475  41.312  95.147  1.00 43.73           C  
ANISOU 1250  CA  ILE B  76     4270   6622   5722   1002  -1315   -210       C  
ATOM   1251  C   ILE B  76      26.079  39.921  95.633  1.00 41.58           C  
ANISOU 1251  C   ILE B  76     4103   6373   5324    846  -1307   -484       C  
ATOM   1252  O   ILE B  76      25.180  39.278  95.078  1.00 44.18           O  
ANISOU 1252  O   ILE B  76     4335   6899   5554    905  -1305   -643       O  
ATOM   1253  CB  ILE B  76      27.615  41.254  94.108  1.00 46.08           C  
ANISOU 1253  CB  ILE B  76     4506   7060   5944   1155  -1394     41       C  
ATOM   1254  CG1 ILE B  76      27.644  42.510  93.232  1.00 45.39           C  
ANISOU 1254  CG1 ILE B  76     4246   7053   5949   1369  -1403    281       C  
ATOM   1255  CG2 ILE B  76      27.522  40.004  93.240  1.00 50.72           C  
ANISOU 1255  CG2 ILE B  76     5034   7900   6338   1223  -1441    -49       C  
ATOM   1256  CD1 ILE B  76      28.133  43.758  93.886  1.00 51.54           C  
ANISOU 1256  CD1 ILE B  76     5083   7595   6903   1330  -1374    446       C  
ATOM   1257  N   GLY B  77      26.757  39.428  96.663  1.00 41.79           N  
ANISOU 1257  N   GLY B  77     4330   6201   5348    646  -1304   -539       N  
ATOM   1258  CA  GLY B  77      26.564  38.080  97.150  1.00 40.93           C  
ANISOU 1258  CA  GLY B  77     4338   6098   5115    493  -1300   -777       C  
ATOM   1259  C   GLY B  77      25.570  38.000  98.282  1.00 39.62           C  
ANISOU 1259  C   GLY B  77     4264   5776   5014    315  -1225  -1033       C  
ATOM   1260  O   GLY B  77      24.821  38.940  98.559  1.00 43.40           O  
ANISOU 1260  O   GLY B  77     4688   6180   5622    331  -1172  -1051       O  
ATOM   1261  N   ASN B  78      25.610  36.874  98.989  1.00 41.90           N  
ANISOU 1261  N   ASN B  78     4202   6750   4967  -1012    303    319       N  
ATOM   1262  CA  ASN B  78      24.640  36.561 100.029  1.00 44.01           C  
ANISOU 1262  CA  ASN B  78     4481   6949   5291   -886    331    354       C  
ATOM   1263  C   ASN B  78      25.233  36.624 101.432  1.00 43.64           C  
ANISOU 1263  C   ASN B  78     4488   6777   5316   -690    341    363       C  
ATOM   1264  O   ASN B  78      24.781  35.906 102.327  1.00 46.07           O  
ANISOU 1264  O   ASN B  78     4819   7012   5674   -600    412    351       O  
ATOM   1265  CB  ASN B  78      24.114  35.153  99.794  1.00 42.40           C  
ANISOU 1265  CB  ASN B  78     4268   6748   5096   -958    462    276       C  
ATOM   1266  CG  ASN B  78      25.209  34.097  99.998  1.00 48.07           C  
ANISOU 1266  CG  ASN B  78     5019   7391   5856   -937    576    168       C  
ATOM   1267  OD1 ASN B  78      26.406  34.414 100.004  1.00 50.91           O  
ANISOU 1267  OD1 ASN B  78     5394   7726   6224   -909    558    142       O  
ATOM   1268  ND2 ASN B  78      24.806  32.850 100.184  1.00 50.20           N  
ANISOU 1268  ND2 ASN B  78     5297   7619   6156   -949    688    107       N  
ATOM   1269  N   TYR B  79      26.229  37.474 101.658  1.00 41.87           N  
ANISOU 1269  N   TYR B  79     4288   6527   5094   -629    269    388       N  
ATOM   1270  CA  TYR B  79      26.861  37.486 102.970  1.00 38.57           C  
ANISOU 1270  CA  TYR B  79     3924   5992   4740   -453    280    395       C  
ATOM   1271  C   TYR B  79      25.862  37.837 104.067  1.00 38.34           C  
ANISOU 1271  C   TYR B  79     3908   5913   4745   -323    251    466       C  
ATOM   1272  O   TYR B  79      25.750  37.126 105.072  1.00 34.27           O  
ANISOU 1272  O   TYR B  79     3429   5312   4279   -226    323    447       O  
ATOM   1273  CB  TYR B  79      28.043  38.454 102.971  1.00 35.36           C  
ANISOU 1273  CB  TYR B  79     3537   5578   4322   -420    196    417       C  
ATOM   1274  CG  TYR B  79      28.742  38.505 104.292  1.00 33.57           C  
ANISOU 1274  CG  TYR B  79     3365   5232   4156   -247    201    428       C  
ATOM   1275  CD1 TYR B  79      29.509  37.420 104.711  1.00 32.83           C  
ANISOU 1275  CD1 TYR B  79     3298   5061   4114   -207    302    350       C  
ATOM   1276  CD2 TYR B  79      28.640  39.620 105.130  1.00 33.88           C  
ANISOU 1276  CD2 TYR B  79     3433   5234   4206   -125    103    514       C  
ATOM   1277  CE1 TYR B  79      30.157  37.430 105.925  1.00 33.60           C  
ANISOU 1277  CE1 TYR B  79     3450   5050   4269    -56    301    364       C  
ATOM   1278  CE2 TYR B  79      29.303  39.649 106.358  1.00 33.35           C  
ANISOU 1278  CE2 TYR B  79     3421   5060   4189     25    109    523       C  
ATOM   1279  CZ  TYR B  79      30.063  38.547 106.745  1.00 32.38           C  
ANISOU 1279  CZ  TYR B  79     3325   4866   4114     56    206    452       C  
ATOM   1280  OH  TYR B  79      30.735  38.524 107.959  1.00 35.22           O  
ANISOU 1280  OH  TYR B  79     3741   5117   4523    197    207    466       O  
ATOM   1281  N   THR B  80      25.100  38.911 103.862  1.00 35.37           N  
ANISOU 1281  N   THR B  80     3502   5592   4345   -329    144    543       N  
ATOM   1282  CA  THR B  80      24.128  39.405 104.827  1.00 37.15           C  
ANISOU 1282  CA  THR B  80     3728   5784   4604   -209    106    604       C  
ATOM   1283  C   THR B  80      22.772  38.724 104.655  1.00 40.51           C  
ANISOU 1283  C   THR B  80     4110   6255   5029   -265    164    594       C  
ATOM   1284  O   THR B  80      22.146  38.842 103.597  1.00 40.77           O  
ANISOU 1284  O   THR B  80     4089   6381   5022   -392    130    605       O  
ATOM   1285  CB  THR B  80      23.977  40.914 104.664  1.00 36.83           C  
ANISOU 1285  CB  THR B  80     3669   5775   4551   -184    -46    686       C  
ATOM   1286  OG1 THR B  80      25.260  41.526 104.787  1.00 39.44           O  
ANISOU 1286  OG1 THR B  80     4042   6069   4876   -145    -98    695       O  
ATOM   1287  CG2 THR B  80      23.067  41.478 105.740  1.00 41.77           C  
ANISOU 1287  CG2 THR B  80     4291   6359   5222    -47    -83    735       C  
ATOM   1288  N   VAL B  81      22.324  37.994 105.679  1.00 37.09           N  
ANISOU 1288  N   VAL B  81     3701   5758   4634   -179    249    574       N  
ATOM   1289  CA  VAL B  81      20.957  37.465 105.639  1.00 37.08           C  
ANISOU 1289  CA  VAL B  81     3656   5802   4630   -222    296    571       C  
ATOM   1290  C   VAL B  81      19.954  38.519 106.100  1.00 38.83           C  
ANISOU 1290  C   VAL B  81     3837   6046   4869   -145    207    637       C  
ATOM   1291  O   VAL B  81      18.877  38.678 105.507  1.00 41.64           O  
ANISOU 1291  O   VAL B  81     4126   6482   5213   -215    177    657       O  
ATOM   1292  CB  VAL B  81      20.833  36.185 106.480  1.00 36.95           C  
ANISOU 1292  CB  VAL B  81     3684   5717   4640   -184    426    521       C  
ATOM   1293  CG1 VAL B  81      19.326  35.835 106.711  1.00 35.77           C  
ANISOU 1293  CG1 VAL B  81     3490   5611   4488   -203    464    529       C  
ATOM   1294  CG2 VAL B  81      21.568  35.038 105.800  1.00 36.45           C  
ANISOU 1294  CG2 VAL B  81     3642   5642   4566   -285    514    446       C  
ATOM   1295  N   SER B  82      20.273  39.241 107.174  1.00 39.35           N  
ANISOU 1295  N   SER B  82     3939   6043   4970      1    164    667       N  
ATOM   1296  CA  SER B  82      19.374  40.252 107.709  1.00 36.77           C  
ANISOU 1296  CA  SER B  82     3572   5727   4671     89     84    716       C  
ATOM   1297  C   SER B  82      20.184  41.307 108.435  1.00 36.31           C  
ANISOU 1297  C   SER B  82     3558   5601   4635    214      3    752       C  
ATOM   1298  O   SER B  82      21.294  41.047 108.892  1.00 33.00           O  
ANISOU 1298  O   SER B  82     3209   5115   4217    258     36    736       O  
ATOM   1299  CB  SER B  82      18.325  39.632 108.656  1.00 38.99           C  
ANISOU 1299  CB  SER B  82     3841   5998   4975    142    173    693       C  
ATOM   1300  OG  SER B  82      17.666  40.631 109.408  1.00 38.91           O  
ANISOU 1300  OG  SER B  82     3800   5982   5002    253    106    726       O  
ATOM   1301  N   CYS B  83      19.631  42.507 108.508  1.00 38.36           N  
ANISOU 1301  N   CYS B  83     3777   5879   4919    270   -110    801       N  
ATOM   1302  CA  CYS B  83      20.234  43.609 109.242  1.00 41.95           C  
ANISOU 1302  CA  CYS B  83     4271   6270   5399    394   -195    836       C  
ATOM   1303  C   CYS B  83      19.595  43.842 110.603  1.00 44.92           C  
ANISOU 1303  C   CYS B  83     4650   6599   5818    531   -168    829       C  
ATOM   1304  O   CYS B  83      19.954  44.809 111.279  1.00 46.26           O  
ANISOU 1304  O   CYS B  83     4847   6717   6012    639   -240    855       O  
ATOM   1305  CB  CYS B  83      20.158  44.890 108.420  1.00 42.90           C  
ANISOU 1305  CB  CYS B  83     4350   6428   5520    366   -354    896       C  
ATOM   1306  SG  CYS B  83      21.218  44.865 106.986  1.00 49.32           S  
ANISOU 1306  SG  CYS B  83     5180   7289   6270    211   -400    908       S  
ATOM   1307  N   LEU B  84      18.639  43.007 111.008  1.00 43.00           N  
ANISOU 1307  N   LEU B  84     4379   6379   5582    523    -69    792       N  
ATOM   1308  CA  LEU B  84      17.951  43.172 112.282  1.00 42.73           C  
ANISOU 1308  CA  LEU B  84     4340   6315   5579    635    -32    775       C  
ATOM   1309  C   LEU B  84      17.381  41.837 112.744  1.00 44.51           C  
ANISOU 1309  C   LEU B  84     4573   6550   5787    597    112    728       C  
ATOM   1310  O   LEU B  84      16.294  41.445 112.299  1.00 44.83           O  
ANISOU 1310  O   LEU B  84     4543   6663   5827    529    143    712       O  
ATOM   1311  CB  LEU B  84      16.829  44.206 112.185  1.00 46.62           C  
ANISOU 1311  CB  LEU B  84     4742   6855   6117    675   -123    793       C  
ATOM   1312  CG  LEU B  84      16.265  44.519 113.579  1.00 54.00           C  
ANISOU 1312  CG  LEU B  84     5674   7756   7086    802    -87    764       C  
ATOM   1313  CD1 LEU B  84      17.042  45.676 114.215  1.00 56.89           C  
ANISOU 1313  CD1 LEU B  84     6089   8050   7477    919   -176    791       C  
ATOM   1314  CD2 LEU B  84      14.765  44.798 113.576  1.00 52.61           C  
ANISOU 1314  CD2 LEU B  84     5387   7649   6953    810    -97    743       C  
ATOM   1315  N   PRO B  85      18.089  41.091 113.591  1.00 40.36           N  
ANISOU 1315  N   PRO B  85     4134   5954   5246    630    196    708       N  
ATOM   1316  CA  PRO B  85      19.447  41.398 114.038  1.00 37.46           C  
ANISOU 1316  CA  PRO B  85     3852   5503   4878    696    165    726       C  
ATOM   1317  C   PRO B  85      20.438  41.128 112.929  1.00 39.52           C  
ANISOU 1317  C   PRO B  85     4129   5767   5119    610    143    731       C  
ATOM   1318  O   PRO B  85      20.115  40.361 112.011  1.00 35.66           O  
ANISOU 1318  O   PRO B  85     3606   5332   4612    496    186    708       O  
ATOM   1319  CB  PRO B  85      19.671  40.413 115.177  1.00 37.88           C  
ANISOU 1319  CB  PRO B  85     3980   5490   4921    729    274    699       C  
ATOM   1320  CG  PRO B  85      18.861  39.208 114.763  1.00 35.81           C  
ANISOU 1320  CG  PRO B  85     3688   5277   4643    625    371    665       C  
ATOM   1321  CD  PRO B  85      17.636  39.769 114.066  1.00 40.45           C  
ANISOU 1321  CD  PRO B  85     4168   5962   5238    586    327    668       C  
ATOM   1322  N   PHE B  86      21.632  41.712 113.034  1.00 34.63           N  
ANISOU 1322  N   PHE B  86     3562   5095   4501    659     82    754       N  
ATOM   1323  CA  PHE B  86      22.670  41.447 112.049  1.00 36.00           C  
ANISOU 1323  CA  PHE B  86     3751   5274   4654    577     68    748       C  
ATOM   1324  C   PHE B  86      22.911  39.951 111.940  1.00 32.61           C  
ANISOU 1324  C   PHE B  86     3348   4824   4217    510    188    696       C  
ATOM   1325  O   PHE B  86      23.277  39.297 112.917  1.00 32.09           O  
ANISOU 1325  O   PHE B  86     3345   4682   4166    568    254    680       O  
ATOM   1326  CB  PHE B  86      23.970  42.143 112.434  1.00 35.20           C  
ANISOU 1326  CB  PHE B  86     3709   5107   4556    651      4    773       C  
ATOM   1327  CG  PHE B  86      25.057  41.945 111.438  1.00 35.23           C  
ANISOU 1327  CG  PHE B  86     3721   5125   4539    567    -11    759       C  
ATOM   1328  CD1 PHE B  86      24.925  42.451 110.164  1.00 36.11           C  
ANISOU 1328  CD1 PHE B  86     3778   5319   4623    464    -80    774       C  
ATOM   1329  CD2 PHE B  86      26.194  41.240 111.765  1.00 34.02           C  
ANISOU 1329  CD2 PHE B  86     3626   4907   4394    583     44    729       C  
ATOM   1330  CE1 PHE B  86      25.905  42.294 109.244  1.00 38.30           C  
ANISOU 1330  CE1 PHE B  86     4059   5621   4873    375    -89    754       C  
ATOM   1331  CE2 PHE B  86      27.192  41.055 110.845  1.00 34.84           C  
ANISOU 1331  CE2 PHE B  86     3726   5030   4482    504     38    704       C  
ATOM   1332  CZ  PHE B  86      27.058  41.591 109.578  1.00 37.29           C  
ANISOU 1332  CZ  PHE B  86     3982   5431   4755    396    -25    713       C  
ATOM   1333  N   THR B  87      22.683  39.420 110.744  1.00 32.33           N  
ANISOU 1333  N   THR B  87     3267   4856   4160    382    211    671       N  
ATOM   1334  CA  THR B  87      22.672  37.986 110.492  1.00 32.00           C  
ANISOU 1334  CA  THR B  87     3237   4806   4115    302    325    615       C  
ATOM   1335  C   THR B  87      23.425  37.760 109.198  1.00 33.20           C  
ANISOU 1335  C   THR B  87     3370   4999   4244    188    319    585       C  
ATOM   1336  O   THR B  87      23.167  38.447 108.203  1.00 32.40           O  
ANISOU 1336  O   THR B  87     3216   4981   4115    113    247    606       O  
ATOM   1337  CB  THR B  87      21.235  37.422 110.374  1.00 35.06           C  
ANISOU 1337  CB  THR B  87     3575   5253   4493    244    383    603       C  
ATOM   1338  OG1 THR B  87      20.498  37.683 111.578  1.00 31.95           O  
ANISOU 1338  OG1 THR B  87     3190   4834   4115    343    392    623       O  
ATOM   1339  CG2 THR B  87      21.278  35.883 110.122  1.00 34.47           C  
ANISOU 1339  CG2 THR B  87     3523   5160   4414    157    501    543       C  
ATOM   1340  N   ILE B  88      24.358  36.811 109.215  1.00 29.85           N  
ANISOU 1340  N   ILE B  88     2990   4517   3836    173    389    533       N  
ATOM   1341  CA  ILE B  88      25.190  36.551 108.049  1.00 35.10           C  
ANISOU 1341  CA  ILE B  88     3635   5217   4483     67    395    487       C  
ATOM   1342  C   ILE B  88      24.933  35.140 107.562  1.00 33.54           C  
ANISOU 1342  C   ILE B  88     3430   5025   4290    -31    507    416       C  
ATOM   1343  O   ILE B  88      24.443  34.276 108.294  1.00 33.34           O  
ANISOU 1343  O   ILE B  88     3434   4944   4288      1    581    402       O  
ATOM   1344  CB  ILE B  88      26.683  36.736 108.343  1.00 29.88           C  
ANISOU 1344  CB  ILE B  88     3020   4489   3846    129    373    474       C  
ATOM   1345  CG1 ILE B  88      27.133  35.705 109.374  1.00 29.52           C  
ANISOU 1345  CG1 ILE B  88     3036   4328   3854    208    453    442       C  
ATOM   1346  CG2 ILE B  88      26.919  38.131 108.859  1.00 32.41           C  
ANISOU 1346  CG2 ILE B  88     3354   4802   4160    224    262    546       C  
ATOM   1347  CD1 ILE B  88      28.675  35.743 109.621  1.00 32.56           C  
ANISOU 1347  CD1 ILE B  88     3458   4641   4272    265    435    420       C  
ATOM   1348  N   ASN B  89      25.251  34.918 106.298  1.00 33.39           N  
ANISOU 1348  N   ASN B  89     3373   5074   4241   -161    519    369       N  
ATOM   1349  CA  ASN B  89      25.406  33.559 105.812  1.00 36.21           C  
ANISOU 1349  CA  ASN B  89     3731   5417   4611   -249    627    282       C  
ATOM   1350  C   ASN B  89      26.772  33.075 106.293  1.00 37.96           C  
ANISOU 1350  C   ASN B  89     4001   5535   4888   -178    659    233       C  
ATOM   1351  O   ASN B  89      27.806  33.574 105.833  1.00 36.85           O  
ANISOU 1351  O   ASN B  89     3849   5410   4742   -191    618    215       O  
ATOM   1352  CB  ASN B  89      25.270  33.540 104.297  1.00 38.94           C  
ANISOU 1352  CB  ASN B  89     4016   5877   4901   -419    629    244       C  
ATOM   1353  CG  ASN B  89      24.759  32.234 103.794  1.00 46.04           C  
ANISOU 1353  CG  ASN B  89     4904   6789   5800   -524    737    173       C  
ATOM   1354  OD1 ASN B  89      25.489  31.455 103.177  1.00 51.60           O  
ANISOU 1354  OD1 ASN B  89     5606   7484   6515   -597    803     84       O  
ATOM   1355  ND2 ASN B  89      23.480  31.964 104.075  1.00 47.43           N  
ANISOU 1355  ND2 ASN B  89     5071   6985   5966   -532    759    205       N  
ATOM   1356  N   CYS B  90      26.784  32.075 107.173  1.00 35.35           N  
ANISOU 1356  N   CYS B  90     3720   5101   4611   -114    728    210       N  
ATOM   1357  CA  CYS B  90      27.966  31.770 107.968  1.00 37.44           C  
ANISOU 1357  CA  CYS B  90     4038   5248   4940    -11    734    190       C  
ATOM   1358  C   CYS B  90      29.165  31.405 107.102  1.00 35.19           C  
ANISOU 1358  C   CYS B  90     3728   4965   4679    -71    759    101       C  
ATOM   1359  O   CYS B  90      29.252  30.291 106.583  1.00 38.44           O  
ANISOU 1359  O   CYS B  90     4129   5359   5118   -145    842     16       O  
ATOM   1360  CB  CYS B  90      27.654  30.649 108.948  1.00 38.86           C  
ANISOU 1360  CB  CYS B  90     4276   5318   5169     42    801    182       C  
ATOM   1361  SG  CYS B  90      29.061  29.940 109.832  1.00 42.21           S  
ANISOU 1361  SG  CYS B  90     4766   5583   5688    148    814    148       S  
ATOM   1362  N   GLN B  91      30.079  32.358 106.938  1.00 32.71           N  
ANISOU 1362  N   GLN B  91     3402   4674   4354    -43    688    117       N  
ATOM   1363  CA  GLN B  91      31.221  32.228 106.054  1.00 36.00           C  
ANISOU 1363  CA  GLN B  91     3782   5116   4779   -108    704     32       C  
ATOM   1364  C   GLN B  91      32.209  33.328 106.418  1.00 36.68           C  
ANISOU 1364  C   GLN B  91     3879   5193   4863    -28    614     76       C  
ATOM   1365  O   GLN B  91      31.830  34.353 106.988  1.00 34.26           O  
ANISOU 1365  O   GLN B  91     3595   4897   4526     40    533    173       O  
ATOM   1366  CB  GLN B  91      30.793  32.326 104.580  1.00 34.61           C  
ANISOU 1366  CB  GLN B  91     3540   5078   4530   -282    720     -9       C  
ATOM   1367  CG  GLN B  91      30.544  33.728 104.092  1.00 35.73           C  
ANISOU 1367  CG  GLN B  91     3656   5328   4592   -324    617     68       C  
ATOM   1368  CD  GLN B  91      29.713  33.773 102.816  1.00 40.70           C  
ANISOU 1368  CD  GLN B  91     4231   6088   5145   -495    623     56       C  
ATOM   1369  OE1 GLN B  91      28.531  33.408 102.811  1.00 40.86           O  
ANISOU 1369  OE1 GLN B  91     4246   6128   5152   -526    650     78       O  
ATOM   1370  NE2 GLN B  91      30.326  34.201 101.728  1.00 40.65           N  
ANISOU 1370  NE2 GLN B  91     4185   6176   5085   -615    600     19       N  
ATOM   1371  N   GLU B  92      33.484  33.097 106.109  1.00 34.42           N  
ANISOU 1371  N   GLU B  92     3576   4886   4614    -33    630      1       N  
ATOM   1372  CA  GLU B  92      34.424  34.196 106.251  1.00 37.26           C  
ANISOU 1372  CA  GLU B  92     3938   5262   4957     15    545     38       C  
ATOM   1373  C   GLU B  92      34.335  35.127 105.049  1.00 36.51           C  
ANISOU 1373  C   GLU B  92     3792   5312   4768   -117    494     47       C  
ATOM   1374  O   GLU B  92      34.355  34.662 103.908  1.00 38.84           O  
ANISOU 1374  O   GLU B  92     4036   5686   5034   -258    549    -35       O  
ATOM   1375  CB  GLU B  92      35.865  33.719 106.425  1.00 38.86           C  
ANISOU 1375  CB  GLU B  92     4136   5393   5235     64    570    -40       C  
ATOM   1376  CG  GLU B  92      36.215  33.241 107.835  1.00 43.34           C  
ANISOU 1376  CG  GLU B  92     4768   5808   5893    222    569    -11       C  
ATOM   1377  CD  GLU B  92      36.118  34.331 108.943  1.00 37.55           C  
ANISOU 1377  CD  GLU B  92     4092   5040   5136    343    473    113       C  
ATOM   1378  OE1 GLU B  92      36.357  34.002 110.121  1.00 36.11           O  
ANISOU 1378  OE1 GLU B  92     3967   4739   5014    461    466    146       O  
ATOM   1379  OE2 GLU B  92      35.830  35.514 108.658  1.00 46.51           O  
ANISOU 1379  OE2 GLU B  92     5217   6260   6195    317    400    176       O  
ATOM   1380  N   PRO B  93      34.213  36.434 105.270  1.00 35.10           N  
ANISOU 1380  N   PRO B  93     3629   5169   4539    -82    387    144       N  
ATOM   1381  CA  PRO B  93      34.197  37.381 104.145  1.00 34.90           C  
ANISOU 1381  CA  PRO B  93     3563   5274   4423   -212    321    163       C  
ATOM   1382  C   PRO B  93      35.560  37.463 103.466  1.00 36.18           C  
ANISOU 1382  C   PRO B  93     3692   5479   4574   -280    327     85       C  
ATOM   1383  O   PRO B  93      36.604  37.511 104.126  1.00 35.87           O  
ANISOU 1383  O   PRO B  93     3674   5370   4587   -182    318     71       O  
ATOM   1384  CB  PRO B  93      33.812  38.711 104.803  1.00 33.44           C  
ANISOU 1384  CB  PRO B  93     3413   5082   4209   -124    199    288       C  
ATOM   1385  CG  PRO B  93      34.218  38.565 106.251  1.00 32.19           C  
ANISOU 1385  CG  PRO B  93     3312   4792   4125     53    203    314       C  
ATOM   1386  CD  PRO B  93      34.085  37.091 106.583  1.00 36.05           C  
ANISOU 1386  CD  PRO B  93     3808   5206   4682     75    320    241       C  
ATOM   1387  N   LYS B  94      35.547  37.393 102.131  1.00 35.07           N  
ANISOU 1387  N   LYS B  94     3499   5458   4368   -457    350     27       N  
ATOM   1388  CA  LYS B  94      36.769  37.499 101.332  1.00 34.30           C  
ANISOU 1388  CA  LYS B  94     3361   5427   4243   -553    361    -58       C  
ATOM   1389  C   LYS B  94      37.226  38.943 101.128  1.00 32.42           C  
ANISOU 1389  C   LYS B  94     3133   5256   3930   -580    236     22       C  
ATOM   1390  O   LYS B  94      38.422  39.191 100.970  1.00 35.34           O  
ANISOU 1390  O   LYS B  94     3486   5644   4295   -595    228    -25       O  
ATOM   1391  CB  LYS B  94      36.565  36.833  99.972  1.00 36.96           C  
ANISOU 1391  CB  LYS B  94     3640   5874   4531   -748    441   -159       C  
ATOM   1392  CG  LYS B  94      36.982  35.400  99.886  1.00 39.82           C  
ANISOU 1392  CG  LYS B  94     3973   6184   4974   -750    577   -300       C  
ATOM   1393  CD  LYS B  94      36.012  34.455 100.521  1.00 47.17           C  
ANISOU 1393  CD  LYS B  94     4932   7020   5968   -674    637   -290       C  
ATOM   1394  CE  LYS B  94      36.490  33.005 100.309  1.00 47.17           C  
ANISOU 1394  CE  LYS B  94     4903   6968   6051   -692    768   -441       C  
ATOM   1395  NZ  LYS B  94      35.352  32.107  99.902  1.00 54.28           N  
ANISOU 1395  NZ  LYS B  94     5800   7881   6944   -772    842   -468       N  
ATOM   1396  N   LEU B  95      36.301  39.897 101.041  1.00 30.50           N  
ANISOU 1396  N   LEU B  95     2909   5054   3624   -601    136    137       N  
ATOM   1397  CA  LEU B  95      36.705  41.274 100.782  1.00 31.72           C  
ANISOU 1397  CA  LEU B  95     3078   5268   3707   -639      7    215       C  
ATOM   1398  C   LEU B  95      37.643  41.794 101.857  1.00 30.23           C  
ANISOU 1398  C   LEU B  95     2931   4990   3566   -482    -40    249       C  
ATOM   1399  O   LEU B  95      38.528  42.606 101.571  1.00 31.71           O  
ANISOU 1399  O   LEU B  95     3119   5224   3706   -525   -108    261       O  
ATOM   1400  CB  LEU B  95      35.468  42.165 100.677  1.00 33.29           C  
ANISOU 1400  CB  LEU B  95     3293   5498   3857   -657   -100    336       C  
ATOM   1401  CG  LEU B  95      35.662  43.666 100.447  1.00 33.66           C  
ANISOU 1401  CG  LEU B  95     3363   5593   3835   -691   -255    437       C  
ATOM   1402  CD1 LEU B  95      36.464  43.918  99.166  1.00 30.48           C  
ANISOU 1402  CD1 LEU B  95     2927   5317   3339   -891   -270    387       C  
ATOM   1403  CD2 LEU B  95      34.285  44.316 100.353  1.00 34.10           C  
ANISOU 1403  CD2 LEU B  95     3424   5664   3868   -699   -348    542       C  
ATOM   1404  N   GLY B  96      37.474  41.331 103.088  1.00 27.58           N  
ANISOU 1404  N   GLY B  96     2609   4283   3586   -876   -740   -272       N  
ATOM   1405  CA  GLY B  96      38.267  41.813 104.200  1.00 27.63           C  
ANISOU 1405  CA  GLY B  96     2743   4128   3628   -793   -840   -217       C  
ATOM   1406  C   GLY B  96      37.715  41.219 105.477  1.00 28.09           C  
ANISOU 1406  C   GLY B  96     2867   4059   3746   -617   -803   -218       C  
ATOM   1407  O   GLY B  96      36.977  40.240 105.439  1.00 28.22           O  
ANISOU 1407  O   GLY B  96     2809   4108   3807   -585   -683   -277       O  
ATOM   1408  N   SER B  97      38.046  41.842 106.600  1.00 26.39           N  
ANISOU 1408  N   SER B  97     2790   3710   3526   -510   -906   -153       N  
ATOM   1409  CA  SER B  97      37.649  41.294 107.886  1.00 29.62           C  
ANISOU 1409  CA  SER B  97     3263   4014   3978   -353   -878   -146       C  
ATOM   1410  C   SER B  97      36.314  41.867 108.352  1.00 28.66           C  
ANISOU 1410  C   SER B  97     3242   3874   3771   -240   -903    -99       C  
ATOM   1411  O   SER B  97      35.927  42.991 108.002  1.00 27.44           O  
ANISOU 1411  O   SER B  97     3154   3736   3535   -248   -995    -51       O  
ATOM   1412  CB  SER B  97      38.704  41.588 108.933  1.00 29.34           C  
ANISOU 1412  CB  SER B  97     3310   3864   3973   -290   -972   -116       C  
ATOM   1413  OG  SER B  97      38.933  42.967 108.954  1.00 30.43           O  
ANISOU 1413  OG  SER B  97     3551   3975   4037   -301  -1107    -58       O  
ATOM   1414  N   LEU B  98      35.592  41.064 109.127  1.00 29.52           N  
ANISOU 1414  N   LEU B  98     3356   3952   3906   -138   -819   -115       N  
ATOM   1415  CA  LEU B  98      34.355  41.521 109.736  1.00 25.32           C  
ANISOU 1415  CA  LEU B  98     2912   3411   3298    -23   -835    -90       C  
ATOM   1416  C   LEU B  98      34.689  42.209 111.047  1.00 26.33           C  
ANISOU 1416  C   LEU B  98     3175   3432   3398     93   -947    -39       C  
ATOM   1417  O   LEU B  98      35.262  41.598 111.952  1.00 27.88           O  
ANISOU 1417  O   LEU B  98     3386   3566   3641    144   -929    -31       O  
ATOM   1418  CB  LEU B  98      33.390  40.368 109.960  1.00 26.36           C  
ANISOU 1418  CB  LEU B  98     2984   3574   3459     16   -686   -135       C  
ATOM   1419  CG  LEU B  98      32.118  40.865 110.642  1.00 28.53           C  
ANISOU 1419  CG  LEU B  98     3341   3854   3645    133   -704   -124       C  
ATOM   1420  CD1 LEU B  98      31.385  41.884 109.763  1.00 27.10           C  
ANISOU 1420  CD1 LEU B  98     3164   3750   3383    113   -770   -127       C  
ATOM   1421  CD2 LEU B  98      31.225  39.679 110.968  1.00 23.57           C  
ANISOU 1421  CD2 LEU B  98     2655   3253   3046    160   -548   -167       C  
ATOM   1422  N   VAL B  99      34.346  43.472 111.151  1.00 25.76           N  
ANISOU 1422  N   VAL B  99     3194   3340   3253    137  -1065     -9       N  
ATOM   1423  CA  VAL B  99      34.698  44.259 112.321  1.00 30.94           C  
ANISOU 1423  CA  VAL B  99     3967   3904   3884    238  -1181     18       C  
ATOM   1424  C   VAL B  99      33.446  44.946 112.830  1.00 31.16           C  
ANISOU 1424  C   VAL B  99     4065   3934   3838    352  -1221      8       C  
ATOM   1425  O   VAL B  99      32.660  45.464 112.035  1.00 30.42           O  
ANISOU 1425  O   VAL B  99     3961   3886   3713    334  -1239      4       O  
ATOM   1426  CB  VAL B  99      35.796  45.290 111.987  1.00 30.57           C  
ANISOU 1426  CB  VAL B  99     3963   3805   3847    168  -1312     48       C  
ATOM   1427  CG1 VAL B  99      36.067  46.161 113.178  1.00 36.67           C  
ANISOU 1427  CG1 VAL B  99     4848   4488   4595    274  -1432     57       C  
ATOM   1428  CG2 VAL B  99      37.073  44.552 111.585  1.00 34.54           C  
ANISOU 1428  CG2 VAL B  99     4384   4319   4422     61  -1270     36       C  
ATOM   1429  N   VAL B 100      33.263  44.953 114.150  1.00 31.02           N  
ANISOU 1429  N   VAL B 100     4113   3880   3792    470  -1238     -1       N  
ATOM   1430  CA  VAL B 100      32.196  45.706 114.789  1.00 34.51           C  
ANISOU 1430  CA  VAL B 100     4619   4327   4166    585  -1291    -33       C  
ATOM   1431  C   VAL B 100      32.834  46.862 115.546  1.00 37.56           C  
ANISOU 1431  C   VAL B 100     5100   4627   4542    644  -1445    -31       C  
ATOM   1432  O   VAL B 100      33.862  46.689 116.218  1.00 34.69           O  
ANISOU 1432  O   VAL B 100     4759   4225   4198    645  -1470    -15       O  
ATOM   1433  CB  VAL B 100      31.336  44.830 115.720  1.00 34.03           C  
ANISOU 1433  CB  VAL B 100     4546   4321   4063    667  -1181    -62       C  
ATOM   1434  CG1 VAL B 100      32.154  44.302 116.885  1.00 34.73           C  
ANISOU 1434  CG1 VAL B 100     4668   4374   4154    705  -1175    -32       C  
ATOM   1435  CG2 VAL B 100      30.124  45.627 116.210  1.00 38.90           C  
ANISOU 1435  CG2 VAL B 100     5204   4968   4606    775  -1228   -121       C  
ATOM   1436  N   ARG B 101      32.264  48.052 115.377  1.00 37.91           N  
ANISOU 1436  N   ARG B 101     5195   4641   4569    689  -1552    -52       N  
ATOM   1437  CA  ARG B 101      32.693  49.248 116.089  1.00 41.14           C  
ANISOU 1437  CA  ARG B 101     5689   4960   4981    752  -1701    -71       C  
ATOM   1438  C   ARG B 101      31.713  49.489 117.229  1.00 42.69           C  
ANISOU 1438  C   ARG B 101     5915   5186   5118    896  -1712   -150       C  
ATOM   1439  O   ARG B 101      30.503  49.612 116.995  1.00 44.01           O  
ANISOU 1439  O   ARG B 101     6063   5401   5257    948  -1691   -191       O  
ATOM   1440  CB  ARG B 101      32.740  50.453 115.150  1.00 40.25           C  
ANISOU 1440  CB  ARG B 101     5614   4773   4908    704  -1825    -42       C  
ATOM   1441  CG  ARG B 101      33.212  51.751 115.812  1.00 42.41           C  
ANISOU 1441  CG  ARG B 101     5970   4930   5215    750  -1960    -70       C  
ATOM   1442  CD  ARG B 101      33.779  52.701 114.768  1.00 46.44           C  
ANISOU 1442  CD  ARG B 101     6509   5350   5785    638  -2043     -5       C  
ATOM   1443  NE  ARG B 101      35.114  52.292 114.324  1.00 50.04           N  
ANISOU 1443  NE  ARG B 101     6946   5805   6263    509  -2045     52       N  
ATOM   1444  CZ  ARG B 101      35.874  52.998 113.492  1.00 52.73           C  
ANISOU 1444  CZ  ARG B 101     7309   6080   6645    386  -2118    114       C  
ATOM   1445  NH1 ARG B 101      35.432  54.152 113.008  1.00 54.19           N  
ANISOU 1445  NH1 ARG B 101     7547   6180   6861    381  -2198    144       N  
ATOM   1446  NH2 ARG B 101      37.074  52.556 113.146  1.00 51.04           N  
ANISOU 1446  NH2 ARG B 101     7060   5887   6447    264  -2103    143       N  
ATOM   1447  N   CYS B 102      32.236  49.543 118.448  1.00 41.87           N  
ANISOU 1447  N   CYS B 102     5848   5071   4989    958  -1744   -178       N  
ATOM   1448  CA  CYS B 102      31.458  49.721 119.666  1.00 44.65           C  
ANISOU 1448  CA  CYS B 102     6219   5478   5269   1085  -1750   -262       C  
ATOM   1449  C   CYS B 102      31.662  51.125 120.207  1.00 50.23           C  
ANISOU 1449  C   CYS B 102     6981   6102   6001   1140  -1885   -333       C  
ATOM   1450  O   CYS B 102      32.799  51.535 120.444  1.00 50.05           O  
ANISOU 1450  O   CYS B 102     6986   6010   6019   1096  -1936   -318       O  
ATOM   1451  CB  CYS B 102      31.895  48.711 120.723  1.00 47.95           C  
ANISOU 1451  CB  CYS B 102     6626   5963   5629   1102  -1668   -241       C  
ATOM   1452  SG  CYS B 102      31.963  47.059 120.076  1.00 45.06           S  
ANISOU 1452  SG  CYS B 102     6193   5646   5284   1008  -1494   -151       S  
ATOM   1453  N   SER B 103      30.565  51.841 120.441  1.00 51.27           N  
ANISOU 1453  N   SER B 103     7118   6244   6119   1228  -1920   -424       N  
ATOM   1454  CA  SER B 103      30.645  53.181 120.997  1.00 58.01           C  
ANISOU 1454  CA  SER B 103     8013   7010   7017   1282  -2029   -514       C  
ATOM   1455  C   SER B 103      29.499  53.387 121.971  1.00 59.37           C  
ANISOU 1455  C   SER B 103     8167   7272   7120   1416  -2035   -648       C  
ATOM   1456  O   SER B 103      28.370  52.969 121.708  1.00 56.76           O  
ANISOU 1456  O   SER B 103     7796   7026   6743   1460  -1984   -675       O  
ATOM   1457  CB  SER B 103      30.599  54.245 119.894  1.00 58.16           C  
ANISOU 1457  CB  SER B 103     8062   6894   7141   1235  -2113   -488       C  
ATOM   1458  OG  SER B 103      30.660  55.546 120.438  1.00 54.94           O  
ANISOU 1458  OG  SER B 103     7699   6383   6794   1297  -2234   -582       O  
ATOM   1459  N   PHE B 104      29.797  54.027 123.100  1.00 60.63           N  
ANISOU 1459  N   PHE B 104     8345   7427   7265   1482  -2100   -747       N  
ATOM   1460  CA  PHE B 104      28.736  54.344 124.045  1.00 63.75           C  
ANISOU 1460  CA  PHE B 104     8710   7918   7593   1610  -2118   -899       C  
ATOM   1461  C   PHE B 104      27.869  55.497 123.551  1.00 65.91           C  
ANISOU 1461  C   PHE B 104     8988   8098   7958   1674  -2211   -993       C  
ATOM   1462  O   PHE B 104      26.651  55.481 123.742  1.00 68.15           O  
ANISOU 1462  O   PHE B 104     9225   8473   8196   1763  -2196  -1094       O  
ATOM   1463  CB  PHE B 104      29.324  54.665 125.414  1.00 68.52           C  
ANISOU 1463  CB  PHE B 104     9319   8568   8146   1660  -2159   -988       C  
ATOM   1464  CG  PHE B 104      28.309  55.160 126.389  1.00 70.01           C  
ANISOU 1464  CG  PHE B 104     9467   8861   8273   1785  -2189  -1171       C  
ATOM   1465  CD1 PHE B 104      27.456  54.280 127.020  1.00 70.93           C  
ANISOU 1465  CD1 PHE B 104     9533   9175   8241   1825  -2092  -1207       C  
ATOM   1466  CD2 PHE B 104      28.189  56.514 126.658  1.00 72.70           C  
ANISOU 1466  CD2 PHE B 104     9814   9103   8706   1859  -2317  -1316       C  
ATOM   1467  CE1 PHE B 104      26.510  54.744 127.918  1.00 76.35           C  
ANISOU 1467  CE1 PHE B 104    10166   9978   8863   1928  -2108  -1391       C  
ATOM   1468  CE2 PHE B 104      27.242  56.981 127.551  1.00 77.96           C  
ANISOU 1468  CE2 PHE B 104    10424   9873   9324   1977  -2344  -1507       C  
ATOM   1469  CZ  PHE B 104      26.404  56.096 128.180  1.00 75.72           C  
ANISOU 1469  CZ  PHE B 104    10081   9804   8884   2006  -2232  -1546       C  
ATOM   1470  N   TYR B 105      28.469  56.502 122.917  1.00 66.93           N  
ANISOU 1470  N   TYR B 105     9168   8046   8216   1632  -2314   -963       N  
ATOM   1471  CA  TYR B 105      27.735  57.662 122.425  1.00 69.74           C  
ANISOU 1471  CA  TYR B 105     9538   8284   8675   1691  -2421  -1036       C  
ATOM   1472  C   TYR B 105      27.363  57.482 120.956  1.00 70.11           C  
ANISOU 1472  C   TYR B 105     9587   8288   8763   1614  -2390   -908       C  
ATOM   1473  O   TYR B 105      28.052  56.792 120.203  1.00 66.61           O  
ANISOU 1473  O   TYR B 105     9151   7848   8310   1493  -2322   -760       O  
ATOM   1474  CB  TYR B 105      28.536  58.962 122.597  1.00 76.81           C  
ANISOU 1474  CB  TYR B 105    10493   8998   9694   1692  -2571  -1080       C  
ATOM   1475  CG  TYR B 105      28.719  59.410 124.031  1.00 76.59           C  
ANISOU 1475  CG  TYR B 105    10448   9010   9642   1793  -2632  -1251       C  
ATOM   1476  CD1 TYR B 105      27.657  59.955 124.743  1.00 78.37           C  
ANISOU 1476  CD1 TYR B 105    10628   9285   9864   1937  -2685  -1443       C  
ATOM   1477  CD2 TYR B 105      29.949  59.313 124.665  1.00 75.16           C  
ANISOU 1477  CD2 TYR B 105    10285   8830   9442   1745  -2639  -1234       C  
ATOM   1478  CE1 TYR B 105      27.808  60.373 126.053  1.00 82.50           C  
ANISOU 1478  CE1 TYR B 105    11118   9869  10359   2026  -2736  -1614       C  
ATOM   1479  CE2 TYR B 105      30.109  59.732 125.978  1.00 79.39           C  
ANISOU 1479  CE2 TYR B 105    10793   9426   9946   1834  -2690  -1396       C  
ATOM   1480  CZ  TYR B 105      29.034  60.262 126.665  1.00 81.34           C  
ANISOU 1480  CZ  TYR B 105    10990   9731  10186   1971  -2735  -1586       C  
ATOM   1481  OH  TYR B 105      29.171  60.680 127.967  1.00 85.92           O  
ANISOU 1481  OH  TYR B 105    11524  10394  10729   2051  -2773  -1759       O  
ATOM   1482  N   GLU B 106      26.257  58.117 120.556  1.00 72.10           N  
ANISOU 1482  N   GLU B 106     9825   8509   9060   1689  -2443   -975       N  
ATOM   1483  CA  GLU B 106      25.774  57.972 119.189  1.00 73.11           C  
ANISOU 1483  CA  GLU B 106     9944   8623   9212   1628  -2416   -863       C  
ATOM   1484  C   GLU B 106      26.692  58.624 118.161  1.00 73.72           C  
ANISOU 1484  C   GLU B 106    10085   8538   9387   1506  -2486   -719       C  
ATOM   1485  O   GLU B 106      26.659  58.232 116.991  1.00 72.78           O  
ANISOU 1485  O   GLU B 106     9954   8440   9259   1416  -2440   -588       O  
ATOM   1486  CB  GLU B 106      24.363  58.542 119.065  1.00 75.90           C  
ANISOU 1486  CB  GLU B 106    10262   8989   9589   1747  -2466   -979       C  
ATOM   1487  CG  GLU B 106      23.526  57.911 117.929  1.00 78.93           C  
ANISOU 1487  CG  GLU B 106    10594   9464   9933   1716  -2390   -901       C  
ATOM   1488  CD  GLU B 106      22.146  58.550 117.743  1.00 87.33           C  
ANISOU 1488  CD  GLU B 106    11619  10535  11026   1836  -2450  -1017       C  
ATOM   1489  OE1 GLU B 106      21.606  59.125 118.717  1.00 96.27           O  
ANISOU 1489  OE1 GLU B 106    12737  11667  12175   1962  -2512  -1196       O  
ATOM   1490  OE2 GLU B 106      21.608  58.475 116.614  1.00 87.08           O  
ANISOU 1490  OE2 GLU B 106    11565  10520  11000   1804  -2439   -936       O  
ATOM   1491  N   ASP B 107      27.503  59.608 118.552  1.00 75.20           N  
ANISOU 1491  N   ASP B 107    10335   8575   9663   1499  -2602   -743       N  
ATOM   1492  CA  ASP B 107      28.395  60.241 117.585  1.00 72.89           C  
ANISOU 1492  CA  ASP B 107    10104   8133   9458   1375  -2674   -604       C  
ATOM   1493  C   ASP B 107      29.620  59.396 117.249  1.00 72.87           C  
ANISOU 1493  C   ASP B 107    10104   8173   9411   1234  -2593   -477       C  
ATOM   1494  O   ASP B 107      30.331  59.732 116.299  1.00 74.85           O  
ANISOU 1494  O   ASP B 107    10392   8336   9712   1112  -2634   -350       O  
ATOM   1495  CB  ASP B 107      28.861  61.605 118.088  1.00 76.96           C  
ANISOU 1495  CB  ASP B 107    10684   8462  10096   1410  -2837   -680       C  
ATOM   1496  CG  ASP B 107      29.507  61.520 119.450  1.00 79.10           C  
ANISOU 1496  CG  ASP B 107    10953   8758  10344   1463  -2848   -802       C  
ATOM   1497  OD1 ASP B 107      30.432  60.700 119.608  1.00 74.82           O  
ANISOU 1497  OD1 ASP B 107    10403   8288   9736   1384  -2767   -737       O  
ATOM   1498  OD2 ASP B 107      29.101  62.264 120.365  1.00 83.23           O  
ANISOU 1498  OD2 ASP B 107    11473   9238  10912   1587  -2940   -971       O  
ATOM   1499  N   PHE B 108      29.912  58.352 118.027  1.00 67.74           N  
ANISOU 1499  N   PHE B 108     9415   7653   8670   1245  -2490   -511       N  
ATOM   1500  CA  PHE B 108      30.997  57.418 117.728  1.00 66.74           C  
ANISOU 1500  CA  PHE B 108     9276   7581   8501   1123  -2408   -403       C  
ATOM   1501  C   PHE B 108      32.355  58.103 117.652  1.00 67.29           C  
ANISOU 1501  C   PHE B 108     9403   7519   8646   1032  -2499   -359       C  
ATOM   1502  O   PHE B 108      33.217  57.688 116.874  1.00 68.77           O  
ANISOU 1502  O   PHE B 108     9587   7710   8832    901  -2469   -246       O  
ATOM   1503  CB  PHE B 108      30.742  56.652 116.423  1.00 64.60           C  
ANISOU 1503  CB  PHE B 108     8964   7384   8198   1030  -2325   -280       C  
ATOM   1504  CG  PHE B 108      29.885  55.428 116.579  1.00 60.31           C  
ANISOU 1504  CG  PHE B 108     8348   7007   7559   1079  -2200   -307       C  
ATOM   1505  CD1 PHE B 108      28.518  55.535 116.755  1.00 59.87           C  
ANISOU 1505  CD1 PHE B 108     8264   7006   7477   1192  -2194   -392       C  
ATOM   1506  CD2 PHE B 108      30.451  54.160 116.520  1.00 53.64           C  
ANISOU 1506  CD2 PHE B 108     7462   6261   6658   1012  -2096   -252       C  
ATOM   1507  CE1 PHE B 108      27.726  54.402 116.887  1.00 53.46           C  
ANISOU 1507  CE1 PHE B 108     7385   6350   6576   1233  -2084   -421       C  
ATOM   1508  CE2 PHE B 108      29.664  53.018 116.656  1.00 54.00           C  
ANISOU 1508  CE2 PHE B 108     7446   6447   6624   1056  -1993   -275       C  
ATOM   1509  CZ  PHE B 108      28.299  53.140 116.836  1.00 50.60           C  
ANISOU 1509  CZ  PHE B 108     6990   6076   6160   1163  -1985   -358       C  
ATOM   1510  N   LEU B 109      32.583  59.157 118.436  1.00 70.21           N  
ANISOU 1510  N   LEU B 109     9820   7774   9084   1097  -2619   -457       N  
ATOM   1511  CA  LEU B 109      33.918  59.752 118.411  1.00 71.88           C  
ANISOU 1511  CA  LEU B 109    10081   7866   9365   1008  -2711   -423       C  
ATOM   1512  C   LEU B 109      34.909  58.962 119.257  1.00 67.97           C  
ANISOU 1512  C   LEU B 109     9557   7463   8805    991  -2649   -450       C  
ATOM   1513  O   LEU B 109      36.089  58.890 118.903  1.00 70.09           O  
ANISOU 1513  O   LEU B 109     9838   7697   9096    877  -2666   -381       O  
ATOM   1514  CB  LEU B 109      33.889  61.215 118.882  1.00 71.43           C  
ANISOU 1514  CB  LEU B 109    10082   7633   9425   1076  -2883   -521       C  
ATOM   1515  CG  LEU B 109      33.340  62.348 117.989  1.00 78.35           C  
ANISOU 1515  CG  LEU B 109    11010   8347  10412   1063  -2998   -474       C  
ATOM   1516  CD1 LEU B 109      33.577  63.706 118.638  1.00 80.96           C  
ANISOU 1516  CD1 LEU B 109    11393   8493  10876   1124  -3176   -586       C  
ATOM   1517  CD2 LEU B 109      33.972  62.326 116.607  1.00 74.17           C  
ANISOU 1517  CD2 LEU B 109    10510   7770   9902    890  -2998   -284       C  
ATOM   1518  N   GLU B 110      34.464  58.363 120.360  1.00 66.98           N  
ANISOU 1518  N   GLU B 110     9391   7464   8596   1099  -2580   -546       N  
ATOM   1519  CA  GLU B 110      35.289  57.451 121.145  1.00 64.65           C  
ANISOU 1519  CA  GLU B 110     9062   7281   8222   1087  -2504   -551       C  
ATOM   1520  C   GLU B 110      34.671  56.062 121.077  1.00 61.35           C  
ANISOU 1520  C   GLU B 110     8587   7020   7702   1096  -2353   -499       C  
ATOM   1521  O   GLU B 110      33.488  55.888 121.384  1.00 64.54           O  
ANISOU 1521  O   GLU B 110     8970   7494   8057   1188  -2316   -554       O  
ATOM   1522  CB  GLU B 110      35.446  57.922 122.590  1.00 65.36           C  
ANISOU 1522  CB  GLU B 110     9152   7393   8291   1194  -2563   -696       C  
ATOM   1523  CG  GLU B 110      36.494  59.025 122.753  1.00 76.45           C  
ANISOU 1523  CG  GLU B 110    10599   8656   9793   1161  -2705   -744       C  
ATOM   1524  CD  GLU B 110      36.769  59.371 124.212  1.00 86.28           C  
ANISOU 1524  CD  GLU B 110    11825   9955  11004   1260  -2751   -898       C  
ATOM   1525  OE1 GLU B 110      36.164  58.733 125.103  1.00 92.60           O  
ANISOU 1525  OE1 GLU B 110    12580  10911  11693   1348  -2670   -954       O  
ATOM   1526  OE2 GLU B 110      37.600  60.270 124.471  1.00 93.32           O  
ANISOU 1526  OE2 GLU B 110    12740  10743  11975   1242  -2868   -963       O  
ATOM   1527  N   TYR B 111      35.467  55.084 120.656  1.00 57.49           N  
ANISOU 1527  N   TYR B 111     8071   6583   7190   1002  -2277   -402       N  
ATOM   1528  CA  TYR B 111      34.949  53.759 120.343  1.00 56.51           C  
ANISOU 1528  CA  TYR B 111     7896   6579   6999    993  -2150   -340       C  
ATOM   1529  C   TYR B 111      36.067  52.735 120.475  1.00 50.71           C  
ANISOU 1529  C   TYR B 111     7130   5896   6241    930  -2094   -279       C  
ATOM   1530  O   TYR B 111      37.232  53.075 120.700  1.00 53.21           O  
ANISOU 1530  O   TYR B 111     7460   6165   6592    886  -2149   -285       O  
ATOM   1531  CB  TYR B 111      34.356  53.744 118.935  1.00 49.95           C  
ANISOU 1531  CB  TYR B 111     7054   5724   6202    927  -2132   -266       C  
ATOM   1532  CG  TYR B 111      35.387  54.091 117.892  1.00 52.32           C  
ANISOU 1532  CG  TYR B 111     7369   5941   6571    789  -2182   -183       C  
ATOM   1533  CD1 TYR B 111      36.221  53.116 117.357  1.00 50.23           C  
ANISOU 1533  CD1 TYR B 111     7059   5728   6296    689  -2124   -112       C  
ATOM   1534  CD2 TYR B 111      35.558  55.406 117.469  1.00 57.04           C  
ANISOU 1534  CD2 TYR B 111     8023   6405   7244    756  -2300   -180       C  
ATOM   1535  CE1 TYR B 111      37.177  53.437 116.414  1.00 51.27           C  
ANISOU 1535  CE1 TYR B 111     7195   5805   6480    553  -2175    -47       C  
ATOM   1536  CE2 TYR B 111      36.511  55.735 116.516  1.00 55.94           C  
ANISOU 1536  CE2 TYR B 111     7900   6198   7157    616  -2353    -96       C  
ATOM   1537  CZ  TYR B 111      37.319  54.746 115.995  1.00 56.95           C  
ANISOU 1537  CZ  TYR B 111     7976   6403   7260    511  -2286    -34       C  
ATOM   1538  OH  TYR B 111      38.266  55.064 115.051  1.00 61.77           O  
ANISOU 1538  OH  TYR B 111     8592   6967   7909    360  -2340     39       O  
ATOM   1539  N   HIS B 112      35.695  51.466 120.324  1.00 45.85           N  
ANISOU 1539  N   HIS B 112     6469   5375   5575    932  -1992   -228       N  
ATOM   1540  CA  HIS B 112      36.663  50.401 120.142  1.00 48.96           C  
ANISOU 1540  CA  HIS B 112     6825   5802   5974    867  -1945   -160       C  
ATOM   1541  C   HIS B 112      36.116  49.387 119.145  1.00 46.85           C  
ANISOU 1541  C   HIS B 112     6508   5582   5712    819  -1856    -96       C  
ATOM   1542  O   HIS B 112      34.902  49.182 119.031  1.00 44.51           O  
ANISOU 1542  O   HIS B 112     6199   5332   5379    864  -1796   -110       O  
ATOM   1543  CB  HIS B 112      37.033  49.718 121.469  1.00 51.17           C  
ANISOU 1543  CB  HIS B 112     7099   6155   6190    942  -1914   -173       C  
ATOM   1544  CG  HIS B 112      35.877  49.077 122.175  1.00 50.69           C  
ANISOU 1544  CG  HIS B 112     7033   6190   6038   1040  -1848   -183       C  
ATOM   1545  ND1 HIS B 112      35.665  47.714 122.175  1.00 50.68           N  
ANISOU 1545  ND1 HIS B 112     6994   6252   6011   1035  -1735   -115       N  
ATOM   1546  CD2 HIS B 112      34.898  49.609 122.943  1.00 50.68           C  
ANISOU 1546  CD2 HIS B 112     7051   6234   5970   1133  -1860   -262       C  
ATOM   1547  CE1 HIS B 112      34.593  47.438 122.897  1.00 50.35           C  
ANISOU 1547  CE1 HIS B 112     6955   6294   5882   1112  -1677   -141       C  
ATOM   1548  NE2 HIS B 112      34.112  48.571 123.376  1.00 54.18           N  
ANISOU 1548  NE2 HIS B 112     7474   6781   6330   1185  -1771   -236       N  
ATOM   1549  N   ASP B 113      37.031  48.797 118.387  1.00 44.46           N  
ANISOU 1549  N   ASP B 113     6159   5272   5463    707  -1816    -45       N  
ATOM   1550  CA  ASP B 113      36.701  47.840 117.344  1.00 41.84           C  
ANISOU 1550  CA  ASP B 113     5755   4986   5157    626  -1696     -4       C  
ATOM   1551  C   ASP B 113      36.979  46.430 117.820  1.00 40.69           C  
ANISOU 1551  C   ASP B 113     5557   4888   5016    639  -1584     19       C  
ATOM   1552  O   ASP B 113      37.961  46.189 118.522  1.00 42.37           O  
ANISOU 1552  O   ASP B 113     5773   5086   5238    657  -1615     25       O  
ATOM   1553  CB  ASP B 113      37.515  48.093 116.078  1.00 40.34           C  
ANISOU 1553  CB  ASP B 113     5531   4768   5029    480  -1720     26       C  
ATOM   1554  CG  ASP B 113      37.144  49.372 115.403  1.00 45.11           C  
ANISOU 1554  CG  ASP B 113     6184   5319   5634    448  -1819     34       C  
ATOM   1555  OD1 ASP B 113      36.030  49.863 115.679  1.00 47.01           O  
ANISOU 1555  OD1 ASP B 113     6466   5556   5841    542  -1845     11       O  
ATOM   1556  OD2 ASP B 113      37.945  49.863 114.574  1.00 47.72           O  
ANISOU 1556  OD2 ASP B 113     6510   5617   6003    328  -1871     64       O  
ATOM   1557  N   VAL B 114      36.117  45.501 117.431  1.00 37.18           N  
ANISOU 1557  N   VAL B 114     5060   4497   4570    629  -1458     31       N  
ATOM   1558  CA  VAL B 114      36.322  44.083 117.695  1.00 36.13           C  
ANISOU 1558  CA  VAL B 114     4871   4389   4468    625  -1342     61       C  
ATOM   1559  C   VAL B 114      36.213  43.347 116.371  1.00 33.09           C  
ANISOU 1559  C   VAL B 114     4391   4029   4154    513  -1239     60       C  
ATOM   1560  O   VAL B 114      35.224  43.517 115.652  1.00 30.66           O  
ANISOU 1560  O   VAL B 114     4062   3762   3824    489  -1198     40       O  
ATOM   1561  CB  VAL B 114      35.301  43.527 118.708  1.00 37.49           C  
ANISOU 1561  CB  VAL B 114     5067   4608   4570    725  -1269     68       C  
ATOM   1562  CG1 VAL B 114      35.621  42.072 119.030  1.00 38.02           C  
ANISOU 1562  CG1 VAL B 114     5087   4674   4684    717  -1162    120       C  
ATOM   1563  CG2 VAL B 114      35.262  44.384 119.968  1.00 36.05           C  
ANISOU 1563  CG2 VAL B 114     4968   4432   4299    833  -1373     46       C  
ATOM   1564  N   ARG B 115      37.225  42.551 116.035  1.00 33.61           N  
ANISOU 1564  N   ARG B 115     4389   4078   4305    445  -1202     69       N  
ATOM   1565  CA  ARG B 115      37.133  41.691 114.866  1.00 32.17           C  
ANISOU 1565  CA  ARG B 115     4097   3931   4197    340  -1091     47       C  
ATOM   1566  C   ARG B 115      36.376  40.416 115.219  1.00 31.67           C  
ANISOU 1566  C   ARG B 115     3994   3879   4160    379   -953     56       C  
ATOM   1567  O   ARG B 115      36.538  39.859 116.310  1.00 31.55           O  
ANISOU 1567  O   ARG B 115     4015   3827   4145    459   -943     98       O  
ATOM   1568  CB  ARG B 115      38.520  41.344 114.325  1.00 33.31           C  
ANISOU 1568  CB  ARG B 115     4166   4057   4432    249  -1105     29       C  
ATOM   1569  CG  ARG B 115      38.458  40.494 113.075  1.00 30.33           C  
ANISOU 1569  CG  ARG B 115     3658   3733   4133    133   -991    -18       C  
ATOM   1570  CD  ARG B 115      39.782  40.463 112.368  1.00 32.33           C  
ANISOU 1570  CD  ARG B 115     3832   3996   4457     24  -1023    -59       C  
ATOM   1571  NE  ARG B 115      39.827  39.465 111.308  1.00 29.87           N  
ANISOU 1571  NE  ARG B 115     3374   3741   4234    -80   -906   -125       N  
ATOM   1572  CZ  ARG B 115      40.885  39.301 110.526  1.00 32.63           C  
ANISOU 1572  CZ  ARG B 115     3621   4127   4648   -192   -910   -187       C  
ATOM   1573  NH1 ARG B 115      41.956  40.062 110.717  1.00 35.10           N  
ANISOU 1573  NH1 ARG B 115     3971   4421   4944   -215  -1023   -182       N  
ATOM   1574  NH2 ARG B 115      40.898  38.363 109.590  1.00 28.48           N  
ANISOU 1574  NH2 ARG B 115     2949   3664   4208   -284   -799   -268       N  
ATOM   1575  N   VAL B 116      35.533  39.954 114.302  1.00 28.38           N  
ANISOU 1575  N   VAL B 116     3502   3517   3762    317   -846     20       N  
ATOM   1576  CA  VAL B 116      34.760  38.735 114.510  1.00 29.17           C  
ANISOU 1576  CA  VAL B 116     3556   3627   3902    333   -702     17       C  
ATOM   1577  C   VAL B 116      35.233  37.667 113.549  1.00 26.44           C  
ANISOU 1577  C   VAL B 116     3077   3281   3687    230   -602    -29       C  
ATOM   1578  O   VAL B 116      35.264  37.890 112.336  1.00 22.44           O  
ANISOU 1578  O   VAL B 116     2492   2841   3195    129   -589    -86       O  
ATOM   1579  CB  VAL B 116      33.261  39.001 114.339  1.00 28.70           C  
ANISOU 1579  CB  VAL B 116     3505   3640   3759    355   -648    -12       C  
ATOM   1580  CG1 VAL B 116      32.489  37.689 114.308  1.00 28.72           C  
ANISOU 1580  CG1 VAL B 116     3437   3660   3818    337   -481    -32       C  
ATOM   1581  CG2 VAL B 116      32.804  39.863 115.481  1.00 30.04           C  
ANISOU 1581  CG2 VAL B 116     3793   3805   3815    471   -735     16       C  
ATOM   1582  N   VAL B 117      35.543  36.490 114.076  1.00 24.58           N  
ANISOU 1582  N   VAL B 117     2811   2980   3549    253   -530     -6       N  
ATOM   1583  CA  VAL B 117      36.081  35.405 113.277  1.00 32.86           C  
ANISOU 1583  CA  VAL B 117     3725   4008   4750    167   -441    -64       C  
ATOM   1584  C   VAL B 117      35.289  34.135 113.568  1.00 31.00           C  
ANISOU 1584  C   VAL B 117     3452   3734   4592    182   -295    -58       C  
ATOM   1585  O   VAL B 117      34.843  33.910 114.697  1.00 29.23           O  
ANISOU 1585  O   VAL B 117     3317   3464   4324    269   -285     25       O  
ATOM   1586  CB  VAL B 117      37.598  35.246 113.555  1.00 32.62           C  
ANISOU 1586  CB  VAL B 117     3682   3906   4805    175   -524    -50       C  
ATOM   1587  CG1 VAL B 117      37.858  35.108 115.038  1.00 35.30           C  
ANISOU 1587  CG1 VAL B 117     4130   4164   5119    300   -582     54       C  
ATOM   1588  CG2 VAL B 117      38.133  34.055 112.855  1.00 36.01           C  
ANISOU 1588  CG2 VAL B 117     3968   4306   5411    104   -434   -122       C  
ATOM   1589  N   LEU B 118      35.129  33.289 112.549  1.00 28.60           N  
ANISOU 1589  N   LEU B 118     3010   3453   4405     87   -177   -149       N  
ATOM   1590  CA  LEU B 118      34.276  32.108 112.628  1.00 31.82           C  
ANISOU 1590  CA  LEU B 118     3365   3826   4898     77    -24   -165       C  
ATOM   1591  C   LEU B 118      35.075  30.808 112.644  1.00 33.20           C  
ANISOU 1591  C   LEU B 118     3454   3881   5280     60     34   -178       C  
ATOM   1592  O   LEU B 118      35.956  30.597 111.800  1.00 32.24           O  
ANISOU 1592  O   LEU B 118     3218   3766   5265     -8     24   -267       O  
ATOM   1593  CB  LEU B 118      33.297  32.084 111.452  1.00 30.83           C  
ANISOU 1593  CB  LEU B 118     3135   3825   4755    -16     79   -279       C  
ATOM   1594  CG  LEU B 118      32.448  33.346 111.251  1.00 33.72           C  
ANISOU 1594  CG  LEU B 118     3566   4313   4934      0     20   -278       C  
ATOM   1595  CD1 LEU B 118      31.458  33.089 110.099  1.00 27.86           C  
ANISOU 1595  CD1 LEU B 118     2701   3697   4190    -89    135   -393       C  
ATOM   1596  CD2 LEU B 118      31.689  33.728 112.525  1.00 32.17           C  
ANISOU 1596  CD2 LEU B 118     3511   4091   4621    112     -9   -188       C  
ATOM   1597  N   ASP B 119      34.779  29.949 113.619  1.00 34.97           N  
ANISOU 1597  N   ASP B 119     3730   3995   5561    122     89    -90       N  
ATOM   1598  CA  ASP B 119      35.005  28.510 113.506  1.00 35.42           C  
ANISOU 1598  CA  ASP B 119     3691   3930   5836     95    193   -113       C  
ATOM   1599  C   ASP B 119      33.737  27.894 112.931  1.00 42.08           C  
ANISOU 1599  C   ASP B 119     4457   4817   6713     20    361   -194       C  
ATOM   1600  O   ASP B 119      32.626  28.342 113.238  1.00 39.40           O  
ANISOU 1600  O   ASP B 119     4188   4557   6226     34    395   -166       O  
ATOM   1601  CB  ASP B 119      35.281  27.858 114.865  1.00 39.98           C  
ANISOU 1601  CB  ASP B 119     4371   4358   6460    193    168     46       C  
ATOM   1602  CG  ASP B 119      36.696  28.059 115.371  1.00 47.67           C  
ANISOU 1602  CG  ASP B 119     5381   5264   7469    264     20    106       C  
ATOM   1603  OD1 ASP B 119      37.569  28.591 114.652  1.00 45.29           O  
ANISOU 1603  OD1 ASP B 119     5012   5014   7183    230    -55     14       O  
ATOM   1604  OD2 ASP B 119      36.931  27.663 116.529  1.00 51.25           O  
ANISOU 1604  OD2 ASP B 119     5927   5618   7928    354    -22    250       O  
ATOM   1605  N   PHE B 120      33.890  26.878 112.096  1.00 42.02           N  
ANISOU 1605  N   PHE B 120     4296   4767   6904    -60    466   -311       N  
ATOM   1606  CA  PHE B 120      32.738  26.207 111.516  1.00 38.61           C  
ANISOU 1606  CA  PHE B 120     3771   4375   6524   -139    634   -407       C  
ATOM   1607  C   PHE B 120      32.545  24.861 112.193  1.00 48.51           C  
ANISOU 1607  C   PHE B 120     5027   5446   7958   -124    736   -344       C  
ATOM   1608  O   PHE B 120      33.519  24.168 112.514  1.00 46.77           O  
ANISOU 1608  O   PHE B 120     4793   5068   7910    -88    698   -301       O  
ATOM   1609  CB  PHE B 120      32.877  26.052 109.997  1.00 41.07           C  
ANISOU 1609  CB  PHE B 120     3889   4796   6919   -256    696   -608       C  
ATOM   1610  CG  PHE B 120      33.121  27.356 109.300  1.00 39.83           C  
ANISOU 1610  CG  PHE B 120     3733   4814   6588   -283    591   -648       C  
ATOM   1611  CD1 PHE B 120      32.139  28.338 109.280  1.00 38.13           C  
ANISOU 1611  CD1 PHE B 120     3593   4734   6162   -271    571   -623       C  
ATOM   1612  CD2 PHE B 120      34.334  27.617 108.696  1.00 38.02           C  
ANISOU 1612  CD2 PHE B 120     3432   4609   6406   -320    507   -707       C  
ATOM   1613  CE1 PHE B 120      32.367  29.559 108.662  1.00 38.24           C  
ANISOU 1613  CE1 PHE B 120     3618   4886   6024   -294    464   -640       C  
ATOM   1614  CE2 PHE B 120      34.568  28.835 108.073  1.00 40.92           C  
ANISOU 1614  CE2 PHE B 120     3809   5128   6609   -357    410   -726       C  
ATOM   1615  CZ  PHE B 120      33.591  29.805 108.056  1.00 36.88           C  
ANISOU 1615  CZ  PHE B 120     3382   4732   5898   -343    386   -683       C  
ATOM   1616  N   ILE B 121      31.282  24.525 112.442  1.00 46.22           N  
ANISOU 1616  N   ILE B 121     4760   5176   7625   -149    858   -333       N  
ATOM   1617  CA  ILE B 121      30.907  23.275 113.081  1.00 55.65           C  
ANISOU 1617  CA  ILE B 121     5966   6202   8975   -154    972   -263       C  
ATOM   1618  C   ILE B 121      31.020  22.094 112.116  1.00 61.28           C  
ANISOU 1618  C   ILE B 121     6492   6833   9958   -248   1100   -423       C  
ATOM   1619  O   ILE B 121      30.784  22.228 110.913  1.00 62.29           O  
ANISOU 1619  O   ILE B 121     6473   7098  10098   -334   1158   -613       O  
ATOM   1620  CB  ILE B 121      29.490  23.377 113.651  1.00 52.43           C  
ANISOU 1620  CB  ILE B 121     5638   5866   8417   -165   1065   -212       C  
ATOM   1621  CG1 ILE B 121      29.498  24.228 114.932  1.00 55.10           C  
ANISOU 1621  CG1 ILE B 121     6167   6229   8538    -59    944    -29       C  
ATOM   1622  CG2 ILE B 121      28.896  21.986 113.853  1.00 59.87           C  
ANISOU 1622  CG2 ILE B 121     6536   6664   9547   -226   1232   -204       C  
ATOM   1623  CD1 ILE B 121      28.152  24.899 115.250  1.00 53.75           C  
ANISOU 1623  CD1 ILE B 121     6059   6220   8144    -62    991    -35       C  
TER    1624      ILE B 121                                                      
HETATM 1625 NA    NA A 201      42.456  37.696 105.896  1.00 28.61          NA  
HETATM 1626  O   HOH A 301      49.281  17.444 137.451  1.00 46.55           O  
HETATM 1627  O   HOH A 302      60.178  12.550 105.277  1.00 45.31           O  
HETATM 1628  O   HOH A 303      50.744  30.796 100.813  1.00 45.37           O  
HETATM 1629  O   HOH A 304      55.997  18.055 107.184  1.00 46.71           O  
HETATM 1630  O   HOH A 305      50.807  16.735 116.937  1.00 45.18           O  
HETATM 1631  O   HOH A 306      59.277  26.710 104.990  1.00 45.31           O  
HETATM 1632  O   HOH A 307      43.189  37.996 108.143  1.00 33.95           O  
HETATM 1633  O   HOH A 308      35.674  25.808 105.940  1.00 45.31           O  
HETATM 1634  O   HOH A 309      44.719  16.912 135.903  1.00 45.31           O  
HETATM 1635  O   HOH A 310      40.889  44.698 114.009  1.00 51.03           O  
HETATM 1636  O   HOH A 311      52.258  17.609 105.384  1.00 45.31           O  
HETATM 1637  O   HOH A 312      44.111  14.901 106.398  1.00 47.71           O  
HETATM 1638  O   HOH A 313      47.533  22.122 129.757  1.00 53.48           O  
HETATM 1639  O   HOH A 314      44.856  44.969 114.939  1.00 48.72           O  
HETATM 1640  O   HOH A 315      64.747  28.503 110.469  1.00 40.91           O  
HETATM 1641  O   HOH A 316      36.205  23.776 104.302  1.00 46.55           O  
HETATM 1642  O   HOH A 317      53.462   5.550 105.896  1.00 46.71           O  
HETATM 1643  O   HOH A 318      57.195  32.720 117.095  1.00 34.76           O  
HETATM 1644  O   HOH A 319      48.549  33.111 109.363  1.00 33.59           O  
HETATM 1645  O   HOH A 320      51.848  28.148 101.209  1.00 45.18           O  
HETATM 1646  O   HOH A 321      56.623  25.731 120.304  1.00 45.31           O  
HETATM 1647  O   HOH A 322      46.121  33.688 110.859  1.00 28.63           O  
HETATM 1648  O   HOH A 323      39.460  31.678 128.202  1.00 45.18           O  
HETATM 1649  O   HOH A 324      40.282  24.142 103.275  1.00 36.85           O  
HETATM 1650  O   HOH A 325      58.165  43.017 107.811  1.00 48.25           O  
HETATM 1651  O   HOH A 326      54.326  14.962 130.157  1.00 45.37           O  
HETATM 1652  O   HOH A 327      46.684  21.578 131.819  1.00 65.70           O  
HETATM 1653  O   HOH A 328      57.243  37.767  99.766  1.00 45.18           O  
HETATM 1654  O   HOH A 329      62.014  29.106 104.841  1.00 38.10           O  
HETATM 1655  O   HOH A 330      55.196  40.829 108.337  1.00 36.82           O  
HETATM 1656  O   HOH A 331      43.294  31.797 111.920  1.00 34.00           O  
HETATM 1657  O   HOH A 332      47.412  31.444 101.509  1.00 40.58           O  
HETATM 1658  O   HOH A 333      48.961  16.806 112.032  1.00 44.60           O  
HETATM 1659  O   HOH A 334      56.623  39.516 116.679  1.00 45.31           O  
HETATM 1660  O   HOH A 335      37.904  22.284 103.351  1.00 46.71           O  
HETATM 1661  O   HOH A 336      66.342  32.176 114.915  1.00 37.76           O  
HETATM 1662  O   HOH A 337      62.923  25.981 110.762  1.00 38.35           O  
HETATM 1663  O   HOH A 338      58.736  28.888 117.994  1.00 28.61           O  
HETATM 1664  O   HOH A 339      44.931  41.968 102.267  1.00 45.18           O  
HETATM 1665  O   HOH A 340      57.607  25.186 104.642  1.00 46.55           O  
HETATM 1666  O   HOH A 341      39.881  26.815 114.087  1.00 41.53           O  
HETATM 1667  O   HOH A 342      62.424  34.342 111.746  1.00 29.84           O  
HETATM 1668  O   HOH A 343      40.737  24.751 123.436  1.00 41.29           O  
HETATM 1669  O   HOH A 344      64.310  32.087 112.462  1.00 35.22           O  
HETATM 1670  O   HOH A 345      46.472  36.765 103.566  1.00 38.53           O  
HETATM 1671  O   HOH A 346      43.121  16.955 118.726  1.00 50.55           O  
HETATM 1672  O   HOH A 347      58.301  25.726 101.355  1.00 44.08           O  
HETATM 1673  O   HOH A 348      56.265  21.586 101.686  1.00 39.81           O  
HETATM 1674  O   HOH A 349      41.793  33.976 110.215  1.00 45.31           O  
HETATM 1675  O   HOH A 350      57.746  33.322 102.620  1.00 42.69           O  
HETATM 1676  O   HOH A 351      44.058  39.266 120.864  1.00 41.30           O  
HETATM 1677  O   HOH A 352      54.407  48.209 106.748  1.00 59.19           O  
HETATM 1678  O   HOH A 353      40.505  16.961 115.847  1.00 45.37           O  
HETATM 1679  O   HOH A 354      58.242  39.782 113.155  1.00 35.54           O  
HETATM 1680  O   HOH A 355      55.536  23.798 108.412  1.00 45.13           O  
HETATM 1681  O   HOH A 356      41.560  36.051 126.281  1.00 46.55           O  
HETATM 1682  O   HOH A 357      54.424  24.162 106.527  1.00 45.18           O  
HETATM 1683  O   HOH A 358      40.222  28.376 120.166  1.00 42.23           O  
HETATM 1684  O   HOH A 359      44.034  15.711 113.106  1.00 46.60           O  
HETATM 1685  O   HOH A 360      57.576  41.641 110.630  1.00 40.38           O  
HETATM 1686  O   HOH A 361      54.340  43.728 113.852  1.00 44.87           O  
HETATM 1687  O   HOH A 362      55.006  36.566  99.765  1.00 47.85           O  
HETATM 1688  O   HOH A 363      42.066  18.296 103.562  1.00 47.58           O  
HETATM 1689  O   HOH A 364      47.585  16.415 114.509  1.00 45.37           O  
HETATM 1690  O   HOH A 365      57.094  25.045 123.070  1.00 47.48           O  
HETATM 1691  O   HOH A 366      51.842  15.522 105.272  1.00 45.31           O  
HETATM 1692  O   HOH A 367      56.799  34.721 121.180  1.00 46.55           O  
HETATM 1693  O   HOH A 368      39.804  28.308 105.410  1.00 46.55           O  
HETATM 1694  O   HOH A 369      57.707  35.271 103.897  1.00 48.75           O  
HETATM 1695  O   HOH A 370      57.138  27.501 118.572  1.00 46.55           O  
HETATM 1696  O   HOH A 371      42.435  22.632 129.690  1.00 50.64           O  
HETATM 1697  O   HOH A 372      40.910  17.804 117.580  1.00 45.31           O  
HETATM 1698  O   HOH A 373      55.174  43.337 110.911  1.00 45.37           O  
HETATM 1699  O   HOH A 374      55.036  40.504 117.342  1.00 46.55           O  
HETATM 1700  O   HOH A 375      40.721  20.270 125.547  1.00 45.18           O  
HETATM 1701  O   HOH A 376      54.020  19.198 106.352  1.00 45.31           O  
HETATM 1702  O   HOH A 377      52.205  18.332 107.729  1.00 45.31           O  
HETATM 1703  O   HOH A 378      50.761  42.207 117.298  1.00 62.24           O  
HETATM 1704  O   HOH A 379      42.485  39.251 121.866  1.00 45.18           O  
HETATM 1705  O   HOH A 380      49.464  38.853 120.915  1.00 46.71           O  
HETATM 1706  O   HOH A 381      55.907  38.770 118.736  1.00 45.18           O  
HETATM 1707  O   HOH A 382      61.790  26.682 105.303  1.00 46.55           O  
HETATM 1708  O   HOH A 383      40.482  25.738 100.833  1.00 45.18           O  
HETATM 1709  O   HOH A 384      48.486  15.843 116.111  1.00 45.18           O  
HETATM 1710  O   HOH A 385      48.477  15.112 136.959  1.00 45.18           O  
HETATM 1711  O   HOH A 386      61.224  25.193 103.330  1.00 46.71           O  
HETATM 1712  O   HOH A 387      38.253  35.165 124.680  1.00 46.55           O  
HETATM 1713  O   HOH A 388      57.603  36.187 119.863  1.00 46.71           O  
HETATM 1714  O   HOH A 389      52.545  35.623  99.545  1.00 45.31           O  
HETATM 1715  O   HOH A 390      41.862  18.501 126.691  1.00 45.18           O  
HETATM 1716  O   HOH A 391      47.335  36.151 101.171  1.00 45.37           O  
HETATM 1717  O   HOH A 392      57.329  25.828 117.730  1.00 45.31           O  
HETATM 1718  O   HOH A 393      50.089  41.026 119.282  1.00 63.22           O  
HETATM 1719  O   HOH A 394      40.418  31.507  95.209  1.00 45.31           O  
HETATM 1720  O   HOH A 395      39.743  22.561 124.509  1.00 45.18           O  
HETATM 1721  O   HOH A 396      63.197  30.472 119.785  1.00 45.18           O  
HETATM 1722  O   HOH A 397      61.134  25.539 100.961  1.00 46.55           O  
HETATM 1723  O   HOH A 398      59.208  35.988 102.225  1.00 46.55           O  
HETATM 1724  O   HOH A 399      58.735  38.292 118.644  1.00 45.31           O  
HETATM 1725  O   HOH A 400      64.960  31.826 119.180  1.00 45.31           O  
HETATM 1726  O   HOH A 401      41.339  13.881 105.400  1.00 46.55           O  
HETATM 1727  O   HOH A 402      56.904  16.500 100.419  1.00 45.18           O  
HETATM 1728  O   HOH A 403      37.759  30.409 106.748  1.00 40.75           O  
HETATM 1729  O   HOH A 404      45.985  13.917 136.080  1.00 45.18           O  
HETATM 1730  O   HOH A 405      57.349  18.968 100.512  1.00 45.18           O  
HETATM 1731  O   HOH A 406      41.092  19.878 101.549  1.00 45.37           O  
HETATM 1732  O   HOH A 407      39.454  21.299 100.483  1.00 45.18           O  
HETATM 1733  O   HOH B 201      27.185  61.342 120.513  1.00 45.31           O  
HETATM 1734  O   HOH B 202      24.987  60.819 107.765  1.00 45.37           O  
HETATM 1735  O   HOH B 203      41.245  47.722 121.688  1.00 46.71           O  
HETATM 1736  O   HOH B 204      35.845  31.838  97.622  1.00 46.71           O  
HETATM 1737  O   HOH B 205      29.658  54.400 106.798  1.00 46.71           O  
HETATM 1738  O   HOH B 206      24.199  25.154 113.370  1.00 45.37           O  
HETATM 1739  O   HOH B 207      52.555  48.305 104.104  1.00 45.31           O  
HETATM 1740  O   HOH B 208      24.766  54.441 124.896  1.00 45.31           O  
HETATM 1741  O   HOH B 209      25.069  36.709 123.186  1.00 45.37           O  
HETATM 1742  O   HOH B 210      29.950  23.885 109.318  1.00 43.07           O  
HETATM 1743  O   HOH B 211      31.801  36.550 108.961  1.00 30.34           O  
HETATM 1744  O   HOH B 212      25.110  40.396 101.840  1.00 38.90           O  
HETATM 1745  O   HOH B 213      40.426  43.932 110.750  1.00 45.37           O  
HETATM 1746  O   HOH B 214      37.275  31.182 109.710  1.00 39.42           O  
HETATM 1747  O   HOH B 215      29.472  34.393 120.679  1.00 46.55           O  
HETATM 1748  O   HOH B 216      23.351  40.035 115.527  1.00 31.36           O  
HETATM 1749  O   HOH B 217      32.182  59.637 121.178  1.00 58.37           O  
HETATM 1750  O   HOH B 218      21.995  47.716 124.753  1.00 46.55           O  
HETATM 1751  O   HOH B 219      32.747  35.202 101.730  1.00 34.45           O  
HETATM 1752  O   HOH B 220      34.126  36.645 110.299  1.00 31.52           O  
HETATM 1753  O   HOH B 221      18.455  25.880 108.297  1.00 46.55           O  
HETATM 1754  O   HOH B 222      38.072  36.937 108.519  1.00 38.54           O  
HETATM 1755  O   HOH B 223      31.488  57.056 122.697  1.00 57.79           O  
HETATM 1756  O   HOH B 224      32.659  54.595 103.619  1.00 58.18           O  
HETATM 1757  O   HOH B 225      28.755  37.851  99.498  1.00 39.19           O  
HETATM 1758  O   HOH B 226      36.163  41.300 123.212  1.00 46.71           O  
HETATM 1759  O   HOH B 227      27.928  64.540 119.483  1.00 46.71           O  
HETATM 1760  O   HOH B 228      15.457  41.231 107.933  1.00 41.30           O  
HETATM 1761  O   HOH B 229      22.159  35.157 102.155  1.00 46.71           O  
HETATM 1762  O   HOH B 230      40.460  46.863 111.082  1.00 44.58           O  
HETATM 1763  O   HOH B 231      25.080  40.324 121.295  1.00 46.71           O  
HETATM 1764  O   HOH B 232      18.087  37.360 103.211  1.00 41.11           O  
HETATM 1765  O   HOH B 233      22.754  40.599  97.754  1.00 42.66           O  
HETATM 1766  O   HOH B 234      17.361  43.052 107.015  1.00 45.18           O  
HETATM 1767  O   HOH B 235      39.678  49.621 118.740  1.00 45.51           O  
HETATM 1768  O   HOH B 236      25.782  49.301 103.664  1.00 41.60           O  
HETATM 1769  O   HOH B 237      17.896  36.812 111.042  1.00 35.64           O  
HETATM 1770  O   HOH B 238      40.058  42.124  99.263  1.00 45.31           O  
HETATM 1771  O   HOH B 239      37.056  38.983 110.367  1.00 33.41           O  
HETATM 1772  O   HOH B 240      20.068  28.077 103.839  1.00 45.37           O  
HETATM 1773  O   HOH B 241      23.074  50.991 110.200  1.00 45.37           O  
HETATM 1774  O   HOH B 242      34.024  30.740 104.573  1.00 38.03           O  
HETATM 1775  O   HOH B 243      26.240  48.840 110.830  1.00 36.30           O  
HETATM 1776  O   HOH B 244      29.630  33.148  99.135  1.00 45.18           O  
HETATM 1777  O   HOH B 245      26.772  55.389 109.990  1.00 45.37           O  
HETATM 1778  O   HOH B 246      25.149  60.164 122.294  1.00 45.31           O  
HETATM 1779  O   HOH B 247      36.173  34.882 121.582  1.00 45.31           O  
HETATM 1780  O   HOH B 248      29.150  55.340 104.285  1.00 45.18           O  
HETATM 1781  O   HOH B 249      22.084  43.778 115.070  1.00 44.15           O  
HETATM 1782  O   HOH B 250      38.704  37.808 106.176  1.00 46.71           O  
HETATM 1783  O   HOH B 251      34.094  44.530 123.736  1.00 45.31           O  
HETATM 1784  O   HOH B 252      25.022  28.992 110.954  1.00 37.27           O  
HETATM 1785  O   HOH B 253      40.606  40.127 102.728  1.00 45.37           O  
HETATM 1786  O   HOH B 254      39.202  53.513 109.228  1.00 45.31           O  
HETATM 1787  O   HOH B 255      29.552  31.259 118.937  1.00 40.63           O  
HETATM 1788  O   HOH B 256      15.950  38.587 110.742  1.00 36.30           O  
HETATM 1789  O   HOH B 257      25.386  39.766 123.207  1.00 46.55           O  
HETATM 1790  O   HOH B 258      24.086  35.886 120.613  1.00 46.71           O  
HETATM 1791  O   HOH B 259      23.363  43.624 119.744  1.00 46.55           O  
HETATM 1792  O   HOH B 260      23.554  35.709 118.580  1.00 45.18           O  
HETATM 1793  O   HOH B 261      39.614  48.041 112.834  1.00 45.50           O  
HETATM 1794  O   HOH B 262      40.036  44.716 116.878  1.00 45.48           O  
HETATM 1795  O   HOH B 263      25.784  28.668 116.460  1.00 52.37           O  
HETATM 1796  O   HOH B 264      30.821  20.677 108.250  1.00 45.18           O  
HETATM 1797  O   HOH B 265      23.522  43.333 117.286  1.00 46.71           O  
HETATM 1798  O   HOH B 266      23.779  39.595 119.956  1.00 45.31           O  
HETATM 1799  O   HOH B 267      22.650  28.970 113.161  1.00 46.55           O  
HETATM 1800  O   HOH B 268      39.502  53.334 111.341  1.00 45.31           O  
HETATM 1801  O   HOH B 269      31.621  53.307 105.310  1.00 48.57           O  
HETATM 1802  O   HOH B 270      25.704  43.213 122.694  1.00 46.55           O  
HETATM 1803  O   HOH B 271      24.403  44.460 101.536  1.00 45.37           O  
HETATM 1804  O   HOH B 272      39.970  27.327 117.551  1.00 52.06           O  
HETATM 1805  O   HOH B 273      37.694  54.963 110.805  1.00 45.18           O  
HETATM 1806  O   HOH B 274      23.294  50.099 117.324  1.00 45.18           O  
HETATM 1807  O   HOH B 275      39.401  34.814 109.087  1.00 45.37           O  
HETATM 1808  O   HOH B 276      23.166  51.062 115.199  1.00 45.18           O  
HETATM 1809  O   HOH B 277      23.211  55.663 125.418  1.00 45.37           O  
HETATM 1810  O   HOH B 278      22.828  42.733  99.807  1.00 45.31           O  
HETATM 1811  O   HOH B 279      25.107  27.933 113.900  1.00 39.49           O  
HETATM 1812  O   HOH B 280      25.120  45.207 103.464  1.00 45.37           O  
HETATM 1813  O   HOH B 281      31.988  31.448  99.880  1.00 45.31           O  
HETATM 1814  O   HOH B 282      38.474  35.573 122.683  1.00 45.31           O  
HETATM 1815  O   HOH B 283      33.123  30.517 102.044  1.00 45.31           O  
HETATM 1816  O   HOH B 284      18.452  43.382 105.288  1.00 46.71           O  
HETATM 1817  O   HOH B 285      36.680  36.786 123.836  1.00 45.31           O  
HETATM 1818  O   HOH B 286      21.883  39.674 118.319  1.00 45.31           O  
HETATM 1819  O   HOH B 287      40.576  39.118 104.393  1.00 49.98           O  
HETATM 1820  O   HOH B 288      13.844  41.102 115.344  1.00 45.37           O  
HETATM 1821  O   HOH B 289      22.083  26.915 111.545  1.00 45.37           O  
HETATM 1822  O   HOH B 290      36.742  29.361 104.509  1.00 47.86           O  
HETATM 1823  O   HOH B 291      16.780  25.353 107.521  1.00 46.55           O  
HETATM 1824  O   HOH B 292      22.955  44.441 102.976  1.00 45.31           O  
HETATM 1825  O   HOH B 293      14.474  43.183 116.289  1.00 46.55           O  
HETATM 1826  O   HOH B 294      19.561  38.798 118.857  1.00 45.31           O  
HETATM 1827  O   HOH B 295      19.455  38.445 121.643  1.00 46.55           O  
CONECT   16  835                                                                
CONECT   51  551                                                                
CONECT  148  642                                                                
CONECT  349  496                                                                
CONECT  496  349                                                                
CONECT  551   51                                                                
CONECT  642  148                                                                
CONECT  835   16                                                                
CONECT  870 1361                                                                
CONECT  967 1452                                                                
CONECT 1168 1306                                                                
CONECT 1306 1168                                                                
CONECT 1361  870                                                                
CONECT 1452  967                                                                
CONECT 1625 1632 1819                                                           
CONECT 1632 1625                                                                
CONECT 1819 1625                                                                
MASTER      508    0    1    0   16    0    0    9 1825    2   17   18          
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.